data_2ZKY
# 
_entry.id   2ZKY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.351 
_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   2ZKY         pdb_00002zky 10.2210/pdb2zky/pdb 
RCSB  RCSB028102   ?            ?                   
WWPDB D_1000028102 ?            ?                   
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2012-04-04 
_pdbx_database_PDB_obs_spr.pdb_id           2ZKY 
_pdbx_database_PDB_obs_spr.replace_pdb_id   2YQX 
_pdbx_database_PDB_obs_spr.details          ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB      2ZKW           'human Cu-Zn superoxide dismutase mutant G85R in space group P21'     unspecified 
PDB      2ZKX           'human Cu-Zn superoxide dismutase mutant G85R in space group I212121' unspecified 
TargetDB ar_001000133.1 .                                                                     unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2ZKY 
_pdbx_database_status.recvd_initial_deposition_date   2008-03-31 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Yoshikawa, S.'                                          1 
'Kukimoto-Niino, M.'                                     2 
'Ito, K.'                                                3 
'Shirouzu, M.'                                           4 
'Urushitani, M.'                                         5 
'Takahashi, R.'                                          6 
'Yokoyama, S.'                                           7 
'RIKEN Structural Genomics/Proteomics Initiative (RSGI)' 8 
# 
_citation.id                        primary 
_citation.title                     'Crystal structure of human Cu-Zn superoxide dismutase mutant G93A' 
_citation.journal_abbrev            'To be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yoshikawa, S.'      1 ? 
primary 'Kukimoto-Niino, M.' 2 ? 
primary 'Ito, K.'            3 ? 
primary 'Shirouzu, M.'       4 ? 
primary 'Urushitani, M.'     5 ? 
primary 'Takahashi, R.'      6 ? 
primary 'Yokoyama, S.'       7 ? 
# 
_cell.entry_id           2ZKY 
_cell.length_a           165.238 
_cell.length_b           204.509 
_cell.length_c           144.819 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              80 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2ZKY 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
# 
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]' 16384.232 10  1.15.1.1 G93A ? ? 
2 non-polymer syn 'ZINC ION'                     65.409    10  ?        ?    ? ? 
3 water       nat water                          18.015    479 ?        ?    ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GPLGSMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGP
KDEERHVGDLGNVTADKDAVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GPLGSMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGP
KDEERHVGDLGNVTADKDAVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F,G,H,I,J 
_entity_poly.pdbx_target_identifier         ar_001000133.1 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   PRO n 
1 3   LEU n 
1 4   GLY n 
1 5   SER n 
1 6   MET n 
1 7   ALA n 
1 8   THR n 
1 9   LYS n 
1 10  ALA n 
1 11  VAL n 
1 12  CYS n 
1 13  VAL n 
1 14  LEU n 
1 15  LYS n 
1 16  GLY n 
1 17  ASP n 
1 18  GLY n 
1 19  PRO n 
1 20  VAL n 
1 21  GLN n 
1 22  GLY n 
1 23  ILE n 
1 24  ILE n 
1 25  ASN n 
1 26  PHE n 
1 27  GLU n 
1 28  GLN n 
1 29  LYS n 
1 30  GLU n 
1 31  SER n 
1 32  ASN n 
1 33  GLY n 
1 34  PRO n 
1 35  VAL n 
1 36  LYS n 
1 37  VAL n 
1 38  TRP n 
1 39  GLY n 
1 40  SER n 
1 41  ILE n 
1 42  LYS n 
1 43  GLY n 
1 44  LEU n 
1 45  THR n 
1 46  GLU n 
1 47  GLY n 
1 48  LEU n 
1 49  HIS n 
1 50  GLY n 
1 51  PHE n 
1 52  HIS n 
1 53  VAL n 
1 54  HIS n 
1 55  GLU n 
1 56  PHE n 
1 57  GLY n 
1 58  ASP n 
1 59  ASN n 
1 60  THR n 
1 61  ALA n 
1 62  GLY n 
1 63  CYS n 
1 64  THR n 
1 65  SER n 
1 66  ALA n 
1 67  GLY n 
1 68  PRO n 
1 69  HIS n 
1 70  PHE n 
1 71  ASN n 
1 72  PRO n 
1 73  LEU n 
1 74  SER n 
1 75  ARG n 
1 76  LYS n 
1 77  HIS n 
1 78  GLY n 
1 79  GLY n 
1 80  PRO n 
1 81  LYS n 
1 82  ASP n 
1 83  GLU n 
1 84  GLU n 
1 85  ARG n 
1 86  HIS n 
1 87  VAL n 
1 88  GLY n 
1 89  ASP n 
1 90  LEU n 
1 91  GLY n 
1 92  ASN n 
1 93  VAL n 
1 94  THR n 
1 95  ALA n 
1 96  ASP n 
1 97  LYS n 
1 98  ASP n 
1 99  ALA n 
1 100 VAL n 
1 101 ALA n 
1 102 ASP n 
1 103 VAL n 
1 104 SER n 
1 105 ILE n 
1 106 GLU n 
1 107 ASP n 
1 108 SER n 
1 109 VAL n 
1 110 ILE n 
1 111 SER n 
1 112 LEU n 
1 113 SER n 
1 114 GLY n 
1 115 ASP n 
1 116 HIS n 
1 117 CYS n 
1 118 ILE n 
1 119 ILE n 
1 120 GLY n 
1 121 ARG n 
1 122 THR n 
1 123 LEU n 
1 124 VAL n 
1 125 VAL n 
1 126 HIS n 
1 127 GLU n 
1 128 LYS n 
1 129 ALA n 
1 130 ASP n 
1 131 ASP n 
1 132 LEU n 
1 133 GLY n 
1 134 LYS n 
1 135 GLY n 
1 136 GLY n 
1 137 ASN n 
1 138 GLU n 
1 139 GLU n 
1 140 SER n 
1 141 THR n 
1 142 LYS n 
1 143 THR n 
1 144 GLY n 
1 145 ASN n 
1 146 ALA n 
1 147 GLY n 
1 148 SER n 
1 149 ARG n 
1 150 LEU n 
1 151 ALA n 
1 152 CYS n 
1 153 GLY n 
1 154 VAL n 
1 155 ILE n 
1 156 GLY n 
1 157 ILE n 
1 158 ALA n 
1 159 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_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               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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               'BL21(DE3)' 
_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          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pGEX6P 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
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 2ZKY A 6 ? 159 ? P00441 1 ? 154 ? 0 153 
2  1 2ZKY B 6 ? 159 ? P00441 1 ? 154 ? 0 153 
3  1 2ZKY C 6 ? 159 ? P00441 1 ? 154 ? 0 153 
4  1 2ZKY D 6 ? 159 ? P00441 1 ? 154 ? 0 153 
5  1 2ZKY E 6 ? 159 ? P00441 1 ? 154 ? 0 153 
6  1 2ZKY F 6 ? 159 ? P00441 1 ? 154 ? 0 153 
7  1 2ZKY G 6 ? 159 ? P00441 1 ? 154 ? 0 153 
8  1 2ZKY H 6 ? 159 ? P00441 1 ? 154 ? 0 153 
9  1 2ZKY I 6 ? 159 ? P00441 1 ? 154 ? 0 153 
10 1 2ZKY J 6 ? 159 ? 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 
1  2ZKY GLY A 1  ? UNP P00441 ?   ?  'expression tag'      -5 1  
1  2ZKY PRO A 2  ? UNP P00441 ?   ?  'expression tag'      -4 2  
1  2ZKY LEU A 3  ? UNP P00441 ?   ?  'expression tag'      -3 3  
1  2ZKY GLY A 4  ? UNP P00441 ?   ?  'expression tag'      -2 4  
1  2ZKY SER A 5  ? UNP P00441 ?   ?  'expression tag'      -1 5  
1  2ZKY ALA A 99 ? UNP P00441 GLY 94 'engineered mutation' 93 6  
2  2ZKY GLY B 1  ? UNP P00441 ?   ?  'expression tag'      -5 7  
2  2ZKY PRO B 2  ? UNP P00441 ?   ?  'expression tag'      -4 8  
2  2ZKY LEU B 3  ? UNP P00441 ?   ?  'expression tag'      -3 9  
2  2ZKY GLY B 4  ? UNP P00441 ?   ?  'expression tag'      -2 10 
2  2ZKY SER B 5  ? UNP P00441 ?   ?  'expression tag'      -1 11 
2  2ZKY ALA B 99 ? UNP P00441 GLY 94 'engineered mutation' 93 12 
3  2ZKY GLY C 1  ? UNP P00441 ?   ?  'expression tag'      -5 13 
3  2ZKY PRO C 2  ? UNP P00441 ?   ?  'expression tag'      -4 14 
3  2ZKY LEU C 3  ? UNP P00441 ?   ?  'expression tag'      -3 15 
3  2ZKY GLY C 4  ? UNP P00441 ?   ?  'expression tag'      -2 16 
3  2ZKY SER C 5  ? UNP P00441 ?   ?  'expression tag'      -1 17 
3  2ZKY ALA C 99 ? UNP P00441 GLY 94 'engineered mutation' 93 18 
4  2ZKY GLY D 1  ? UNP P00441 ?   ?  'expression tag'      -5 19 
4  2ZKY PRO D 2  ? UNP P00441 ?   ?  'expression tag'      -4 20 
4  2ZKY LEU D 3  ? UNP P00441 ?   ?  'expression tag'      -3 21 
4  2ZKY GLY D 4  ? UNP P00441 ?   ?  'expression tag'      -2 22 
4  2ZKY SER D 5  ? UNP P00441 ?   ?  'expression tag'      -1 23 
4  2ZKY ALA D 99 ? UNP P00441 GLY 94 'engineered mutation' 93 24 
5  2ZKY GLY E 1  ? UNP P00441 ?   ?  'expression tag'      -5 25 
5  2ZKY PRO E 2  ? UNP P00441 ?   ?  'expression tag'      -4 26 
5  2ZKY LEU E 3  ? UNP P00441 ?   ?  'expression tag'      -3 27 
5  2ZKY GLY E 4  ? UNP P00441 ?   ?  'expression tag'      -2 28 
5  2ZKY SER E 5  ? UNP P00441 ?   ?  'expression tag'      -1 29 
5  2ZKY ALA E 99 ? UNP P00441 GLY 94 'engineered mutation' 93 30 
6  2ZKY GLY F 1  ? UNP P00441 ?   ?  'expression tag'      -5 31 
6  2ZKY PRO F 2  ? UNP P00441 ?   ?  'expression tag'      -4 32 
6  2ZKY LEU F 3  ? UNP P00441 ?   ?  'expression tag'      -3 33 
6  2ZKY GLY F 4  ? UNP P00441 ?   ?  'expression tag'      -2 34 
6  2ZKY SER F 5  ? UNP P00441 ?   ?  'expression tag'      -1 35 
6  2ZKY ALA F 99 ? UNP P00441 GLY 94 'engineered mutation' 93 36 
7  2ZKY GLY G 1  ? UNP P00441 ?   ?  'expression tag'      -5 37 
7  2ZKY PRO G 2  ? UNP P00441 ?   ?  'expression tag'      -4 38 
7  2ZKY LEU G 3  ? UNP P00441 ?   ?  'expression tag'      -3 39 
7  2ZKY GLY G 4  ? UNP P00441 ?   ?  'expression tag'      -2 40 
7  2ZKY SER G 5  ? UNP P00441 ?   ?  'expression tag'      -1 41 
7  2ZKY ALA G 99 ? UNP P00441 GLY 94 'engineered mutation' 93 42 
8  2ZKY GLY H 1  ? UNP P00441 ?   ?  'expression tag'      -5 43 
8  2ZKY PRO H 2  ? UNP P00441 ?   ?  'expression tag'      -4 44 
8  2ZKY LEU H 3  ? UNP P00441 ?   ?  'expression tag'      -3 45 
8  2ZKY GLY H 4  ? UNP P00441 ?   ?  'expression tag'      -2 46 
8  2ZKY SER H 5  ? UNP P00441 ?   ?  'expression tag'      -1 47 
8  2ZKY ALA H 99 ? UNP P00441 GLY 94 'engineered mutation' 93 48 
9  2ZKY GLY I 1  ? UNP P00441 ?   ?  'expression tag'      -5 49 
9  2ZKY PRO I 2  ? UNP P00441 ?   ?  'expression tag'      -4 50 
9  2ZKY LEU I 3  ? UNP P00441 ?   ?  'expression tag'      -3 51 
9  2ZKY GLY I 4  ? UNP P00441 ?   ?  'expression tag'      -2 52 
9  2ZKY SER I 5  ? UNP P00441 ?   ?  'expression tag'      -1 53 
9  2ZKY ALA I 99 ? UNP P00441 GLY 94 'engineered mutation' 93 54 
10 2ZKY GLY J 1  ? UNP P00441 ?   ?  'expression tag'      -5 55 
10 2ZKY PRO J 2  ? UNP P00441 ?   ?  'expression tag'      -4 56 
10 2ZKY LEU J 3  ? UNP P00441 ?   ?  'expression tag'      -3 57 
10 2ZKY GLY J 4  ? UNP P00441 ?   ?  'expression tag'      -2 58 
10 2ZKY SER J 5  ? UNP P00441 ?   ?  'expression tag'      -1 59 
10 2ZKY ALA J 99 ? UNP P00441 GLY 94 'engineered mutation' 93 60 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
_exptl.entry_id          2ZKY 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.73 
_exptl_crystal.density_percent_sol   67.06 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pdbx_details    
'0.1M Cacodylate(pH 6.5), 0.2M NaCl, 2.0M Ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315' 
_diffrn_detector.pdbx_collection_date   2007-02-15 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PHOTON FACTORY BEAMLINE BL-5A' 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
_diffrn_source.pdbx_synchrotron_beamline   BL-5A 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
# 
_reflns.entry_id                     2ZKY 
_reflns.observed_criterion_sigma_I   -3 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.00 
_reflns.d_resolution_high            2.40 
_reflns.number_obs                   94985 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.4 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.121 
_reflns.pdbx_netI_over_sigmaI        15.138 
_reflns.B_iso_Wilson_estimate        24.3 
_reflns.pdbx_redundancy              6.157 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.40 
_reflns_shell.d_res_low              2.49 
_reflns_shell.percent_possible_all   96.8 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.898 
_reflns_shell.meanI_over_sigI_obs    1.459 
_reflns_shell.pdbx_redundancy        4.7 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      9150 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2ZKY 
_refine.ls_number_reflns_obs                     88403 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               44635.65 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             49.93 
_refine.ls_d_res_high                            2.40 
_refine.ls_percent_reflns_obs                    92.4 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.189 
_refine.ls_R_factor_R_free                       0.235 
_refine.ls_R_factor_R_free_error                 0.002 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 10.0 
_refine.ls_number_reflns_R_free                  8837 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               39.7 
_refine.aniso_B[1][1]                            1.95 
_refine.aniso_B[2][2]                            -3.76 
_refine.aniso_B[3][3]                            1.80 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.367897 
_refine.solvent_model_param_bsol                 36.8559 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 1PU0' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        2ZKY 
_refine_analyze.Luzzati_coordinate_error_obs    0.26 
_refine_analyze.Luzzati_sigma_a_obs             0.36 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.33 
_refine_analyze.Luzzati_sigma_a_free            0.38 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11100 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_refine_hist.number_atoms_solvent             479 
_refine_hist.number_atoms_total               11589 
_refine_hist.d_res_high                       2.40 
_refine_hist.d_res_low                        49.93 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d                0.008 ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             1.5   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      25.3  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      0.79  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             4.00  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            5.48  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             6.69  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            8.79  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       2.40 
_refine_ls_shell.d_res_low                        2.55 
_refine_ls_shell.number_reflns_R_work             11584 
_refine_ls_shell.R_factor_R_work                  0.282 
_refine_ls_shell.percent_reflns_obs               81.5 
_refine_ls_shell.R_factor_R_free                  0.333 
_refine_ls_shell.R_factor_R_free_error            0.009 
_refine_ls_shell.percent_reflns_R_free            10.0 
_refine_ls_shell.number_reflns_R_free             1288 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                12872 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 protein_rep.param protein.top 'X-RAY DIFFRACTION' 
2 ion.param         water.top   'X-RAY DIFFRACTION' 
3 water_rep.param   ion.top     'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2ZKY 
_struct.title                     'Crystal structure of human Cu-Zn superoxide dismutase mutant G93A' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2ZKY 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
;oxidoreductase, human Cu-Zn superoxide dismutase, ALS, FALS, metal-binding, disease mutation, E.C.1.15.1.1, Amyotrophic lateral sclerosis, Antioxidant, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI
;
# 
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 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 1 ? 
H  N N 1 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 2 ? 
L  N N 2 ? 
M  N N 2 ? 
N  N N 2 ? 
O  N N 2 ? 
P  N N 2 ? 
Q  N N 2 ? 
R  N N 2 ? 
S  N N 2 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 3 ? 
W  N N 3 ? 
X  N N 3 ? 
Y  N N 3 ? 
Z  N N 3 ? 
AA N N 3 ? 
BA N N 3 ? 
CA N N 3 ? 
DA N N 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  ALA A 61  ? GLY A 67  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  2  SER A 113 ? CYS A 117 ? SER A 107 CYS A 111 5 ? 5 
HELX_P HELX_P3  3  GLU A 139 ? GLY A 144 ? GLU A 133 GLY A 138 1 ? 6 
HELX_P HELX_P4  4  ALA B 61  ? GLY B 67  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P5  5  SER B 113 ? CYS B 117 ? SER B 107 CYS B 111 5 ? 5 
HELX_P HELX_P6  6  GLU B 139 ? GLY B 144 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P7  7  ALA C 61  ? GLY C 67  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P8  8  GLU C 139 ? GLY C 144 ? GLU C 133 GLY C 138 1 ? 6 
HELX_P HELX_P9  9  ALA D 61  ? GLY D 67  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P10 10 SER D 113 ? CYS D 117 ? SER D 107 CYS D 111 5 ? 5 
HELX_P HELX_P11 11 GLU D 139 ? GLY D 144 ? GLU D 133 GLY D 138 1 ? 6 
HELX_P HELX_P12 12 ALA E 61  ? GLY E 67  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P13 13 SER E 113 ? CYS E 117 ? SER E 107 CYS E 111 5 ? 5 
HELX_P HELX_P14 14 ASN E 137 ? THR E 143 ? ASN E 131 THR E 137 1 ? 7 
HELX_P HELX_P15 15 ALA F 61  ? GLY F 67  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P16 16 ASN F 137 ? GLY F 144 ? ASN F 131 GLY F 138 1 ? 8 
HELX_P HELX_P17 17 ALA G 61  ? GLY G 67  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P18 18 CYS H 63  ? GLY H 67  ? CYS H 57  GLY H 61  5 ? 5 
HELX_P HELX_P19 19 SER H 113 ? CYS H 117 ? SER H 107 CYS H 111 5 ? 5 
HELX_P HELX_P20 20 ALA I 61  ? GLY I 67  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P21 21 ALA J 61  ? GLY J 67  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P22 22 SER J 113 ? CYS J 117 ? SER J 107 CYS J 111 5 ? 5 
HELX_P HELX_P23 23 ASN J 137 ? THR J 141 ? ASN J 131 THR J 135 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 63 SG  ? ? ? 1_555 A CYS 152 SG ? ? A CYS 57 A CYS 146 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
disulf2  disulf ? ? B CYS 63 SG  ? ? ? 1_555 B CYS 152 SG ? ? B CYS 57 B CYS 146 1_555 ? ? ? ? ? ? ? 2.081 ? ? 
disulf3  disulf ? ? C CYS 63 SG  ? ? ? 1_555 C CYS 152 SG ? ? C CYS 57 C CYS 146 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
disulf4  disulf ? ? D CYS 63 SG  ? ? ? 1_555 D CYS 152 SG ? ? D CYS 57 D CYS 146 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
disulf5  disulf ? ? E CYS 63 SG  ? ? ? 1_555 E CYS 152 SG ? ? E CYS 57 E CYS 146 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
disulf6  disulf ? ? F CYS 63 SG  ? ? ? 1_555 F CYS 152 SG ? ? F CYS 57 F CYS 146 1_555 ? ? ? ? ? ? ? 2.073 ? ? 
disulf7  disulf ? ? G CYS 63 SG  ? ? ? 1_555 G CYS 152 SG ? ? G CYS 57 G CYS 146 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
disulf8  disulf ? ? H CYS 63 SG  ? ? ? 1_555 H CYS 152 SG ? ? H CYS 57 H CYS 146 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
disulf9  disulf ? ? I CYS 63 SG  ? ? ? 1_555 I CYS 152 SG ? ? I CYS 57 I CYS 146 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
disulf10 disulf ? ? J CYS 63 SG  ? ? ? 1_555 J CYS 152 SG ? ? J CYS 57 J CYS 146 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc1  metalc ? ? A HIS 69 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? A HIS 63 A ZN  601 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
metalc2  metalc ? ? A HIS 77 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? A HIS 71 A ZN  601 1_555 ? ? ? ? ? ? ? 2.170 ? ? 
metalc3  metalc ? ? A HIS 86 ND1 ? ? ? 1_555 K ZN  .   ZN ? ? A HIS 80 A ZN  601 1_555 ? ? ? ? ? ? ? 2.208 ? ? 
metalc4  metalc ? ? A ASP 89 OD1 ? ? ? 1_555 K ZN  .   ZN ? ? A ASP 83 A ZN  601 1_555 ? ? ? ? ? ? ? 1.968 ? ? 
metalc5  metalc ? ? B HIS 69 ND1 ? ? ? 1_555 L ZN  .   ZN ? ? B HIS 63 B ZN  602 1_555 ? ? ? ? ? ? ? 1.950 ? ? 
metalc6  metalc ? ? B HIS 77 ND1 ? ? ? 1_555 L ZN  .   ZN ? ? B HIS 71 B ZN  602 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc7  metalc ? ? B HIS 86 ND1 ? ? ? 1_555 L ZN  .   ZN ? ? B HIS 80 B ZN  602 1_555 ? ? ? ? ? ? ? 1.984 ? ? 
metalc8  metalc ? ? B ASP 89 OD1 ? ? ? 1_555 L ZN  .   ZN ? ? B ASP 83 B ZN  602 1_555 ? ? ? ? ? ? ? 1.925 ? ? 
metalc9  metalc ? ? C HIS 69 ND1 ? ? ? 1_555 M ZN  .   ZN ? ? C HIS 63 C ZN  603 1_555 ? ? ? ? ? ? ? 2.224 ? ? 
metalc10 metalc ? ? C HIS 77 ND1 ? ? ? 1_555 M ZN  .   ZN ? ? C HIS 71 C ZN  603 1_555 ? ? ? ? ? ? ? 2.154 ? ? 
metalc11 metalc ? ? C HIS 86 ND1 ? ? ? 1_555 M ZN  .   ZN ? ? C HIS 80 C ZN  603 1_555 ? ? ? ? ? ? ? 1.869 ? ? 
metalc12 metalc ? ? C ASP 89 OD1 ? ? ? 1_555 M ZN  .   ZN ? ? C ASP 83 C ZN  603 1_555 ? ? ? ? ? ? ? 1.884 ? ? 
metalc13 metalc ? ? D HIS 69 ND1 ? ? ? 1_555 N ZN  .   ZN ? ? D HIS 63 D ZN  604 1_555 ? ? ? ? ? ? ? 1.945 ? ? 
metalc14 metalc ? ? D HIS 77 ND1 ? ? ? 1_555 N ZN  .   ZN ? ? D HIS 71 D ZN  604 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
metalc15 metalc ? ? D HIS 86 ND1 ? ? ? 1_555 N ZN  .   ZN ? ? D HIS 80 D ZN  604 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc16 metalc ? ? D ASP 89 OD1 ? ? ? 1_555 N ZN  .   ZN ? ? D ASP 83 D ZN  604 1_555 ? ? ? ? ? ? ? 1.937 ? ? 
metalc17 metalc ? ? E HIS 69 ND1 ? ? ? 1_555 O ZN  .   ZN ? ? E HIS 63 E ZN  605 1_555 ? ? ? ? ? ? ? 2.010 ? ? 
metalc18 metalc ? ? E HIS 77 ND1 ? ? ? 1_555 O ZN  .   ZN ? ? E HIS 71 E ZN  605 1_555 ? ? ? ? ? ? ? 2.146 ? ? 
metalc19 metalc ? ? E HIS 86 ND1 ? ? ? 1_555 O ZN  .   ZN ? ? E HIS 80 E ZN  605 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc20 metalc ? ? E ASP 89 OD1 ? ? ? 1_555 O ZN  .   ZN ? ? E ASP 83 E ZN  605 1_555 ? ? ? ? ? ? ? 1.919 ? ? 
metalc21 metalc ? ? F HIS 69 ND1 ? ? ? 1_555 P ZN  .   ZN ? ? F HIS 63 F ZN  606 1_555 ? ? ? ? ? ? ? 1.932 ? ? 
metalc22 metalc ? ? F HIS 77 ND1 ? ? ? 1_555 P ZN  .   ZN ? ? F HIS 71 F ZN  606 1_555 ? ? ? ? ? ? ? 2.133 ? ? 
metalc23 metalc ? ? F HIS 86 ND1 ? ? ? 1_555 P ZN  .   ZN ? ? F HIS 80 F ZN  606 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc24 metalc ? ? F ASP 89 OD1 ? ? ? 1_555 P ZN  .   ZN ? ? F ASP 83 F ZN  606 1_555 ? ? ? ? ? ? ? 1.856 ? ? 
metalc25 metalc ? ? G HIS 69 ND1 ? ? ? 1_555 Q ZN  .   ZN ? ? G HIS 63 G ZN  607 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc26 metalc ? ? G HIS 77 ND1 ? ? ? 1_555 Q ZN  .   ZN ? ? G HIS 71 G ZN  607 1_555 ? ? ? ? ? ? ? 2.174 ? ? 
metalc27 metalc ? ? G HIS 86 ND1 ? ? ? 1_555 Q ZN  .   ZN ? ? G HIS 80 G ZN  607 1_555 ? ? ? ? ? ? ? 2.193 ? ? 
metalc28 metalc ? ? G ASP 89 OD1 ? ? ? 1_555 Q ZN  .   ZN ? ? G ASP 83 G ZN  607 1_555 ? ? ? ? ? ? ? 1.937 ? ? 
metalc29 metalc ? ? H HIS 69 ND1 ? ? ? 1_555 R ZN  .   ZN ? ? H HIS 63 H ZN  608 1_555 ? ? ? ? ? ? ? 2.115 ? ? 
metalc30 metalc ? ? H HIS 77 ND1 ? ? ? 1_555 R ZN  .   ZN ? ? H HIS 71 H ZN  608 1_555 ? ? ? ? ? ? ? 1.975 ? ? 
metalc31 metalc ? ? H HIS 86 ND1 ? ? ? 1_555 R ZN  .   ZN ? ? H HIS 80 H ZN  608 1_555 ? ? ? ? ? ? ? 1.923 ? ? 
metalc32 metalc ? ? H ASP 89 OD1 ? ? ? 1_555 R ZN  .   ZN ? ? H ASP 83 H ZN  608 1_555 ? ? ? ? ? ? ? 1.873 ? ? 
metalc33 metalc ? ? I HIS 69 ND1 ? ? ? 1_555 S ZN  .   ZN ? ? I HIS 63 I ZN  609 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
metalc34 metalc ? ? I HIS 77 ND1 ? ? ? 1_555 S ZN  .   ZN ? ? I HIS 71 I ZN  609 1_555 ? ? ? ? ? ? ? 2.235 ? ? 
metalc35 metalc ? ? I HIS 86 ND1 ? ? ? 1_555 S ZN  .   ZN ? ? I HIS 80 I ZN  609 1_555 ? ? ? ? ? ? ? 2.124 ? ? 
metalc36 metalc ? ? I ASP 89 OD1 ? ? ? 1_555 S ZN  .   ZN ? ? I ASP 83 I ZN  609 1_555 ? ? ? ? ? ? ? 1.995 ? ? 
metalc37 metalc ? ? I ASP 89 OD2 ? ? ? 1_555 S ZN  .   ZN ? ? I ASP 83 I ZN  609 1_555 ? ? ? ? ? ? ? 2.694 ? ? 
metalc38 metalc ? ? J HIS 69 ND1 ? ? ? 1_555 T ZN  .   ZN ? ? J HIS 63 J ZN  610 1_555 ? ? ? ? ? ? ? 2.175 ? ? 
metalc39 metalc ? ? J HIS 77 ND1 ? ? ? 1_555 T ZN  .   ZN ? ? J HIS 71 J ZN  610 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc40 metalc ? ? J HIS 86 ND1 ? ? ? 1_555 T ZN  .   ZN ? ? J HIS 80 J ZN  610 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc41 metalc ? ? J ASP 89 OD1 ? ? ? 1_555 T ZN  .   ZN ? ? J ASP 83 J ZN  610 1_555 ? ? ? ? ? ? ? 1.912 ? ? 
# 
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 
A ? 5 ? 
B ? 4 ? 
C ? 5 ? 
D ? 4 ? 
E ? 5 ? 
F ? 4 ? 
G ? 5 ? 
H ? 4 ? 
I ? 5 ? 
J ? 4 ? 
K ? 5 ? 
L ? 4 ? 
M ? 5 ? 
N ? 4 ? 
O ? 9 ? 
P ? 5 ? 
Q ? 4 ? 
R ? 5 ? 
S ? 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 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
G 3 4 ? anti-parallel 
G 4 5 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
I 4 5 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
K 1 2 ? anti-parallel 
K 2 3 ? anti-parallel 
K 3 4 ? anti-parallel 
K 4 5 ? anti-parallel 
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
M 1 2 ? anti-parallel 
M 2 3 ? anti-parallel 
M 3 4 ? anti-parallel 
M 4 5 ? anti-parallel 
N 1 2 ? anti-parallel 
N 2 3 ? anti-parallel 
N 3 4 ? anti-parallel 
O 1 2 ? anti-parallel 
O 2 3 ? anti-parallel 
O 3 4 ? anti-parallel 
O 4 5 ? anti-parallel 
O 5 6 ? anti-parallel 
O 6 7 ? anti-parallel 
O 7 8 ? anti-parallel 
O 8 9 ? anti-parallel 
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? anti-parallel 
P 4 5 ? anti-parallel 
Q 1 2 ? anti-parallel 
Q 2 3 ? anti-parallel 
Q 3 4 ? anti-parallel 
R 1 2 ? anti-parallel 
R 2 3 ? anti-parallel 
R 3 4 ? anti-parallel 
R 4 5 ? anti-parallel 
S 1 2 ? anti-parallel 
S 2 3 ? anti-parallel 
S 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 
A 1 VAL A 100 ? ASP A 107 ? VAL A 94  ASP A 101 
A 2 VAL A 35  ? LYS A 42  ? VAL A 29  LYS A 36  
A 3 GLN A 21  ? GLU A 27  ? GLN A 15  GLU A 21  
A 4 LYS A 9   ? LYS A 15  ? LYS A 3   LYS A 9   
A 5 GLY A 156 ? ALA A 158 ? GLY A 150 ALA A 152 
B 1 ASP A 89  ? ALA A 95  ? ASP A 83  ALA A 89  
B 2 GLY A 47  ? HIS A 54  ? GLY A 41  HIS A 48  
B 3 THR A 122 ? HIS A 126 ? THR A 116 HIS A 120 
B 4 ARG A 149 ? VAL A 154 ? ARG A 143 VAL A 148 
C 1 VAL B 100 ? ASP B 107 ? VAL B 94  ASP B 101 
C 2 VAL B 35  ? LYS B 42  ? VAL B 29  LYS B 36  
C 3 GLN B 21  ? GLU B 27  ? GLN B 15  GLU B 21  
C 4 LYS B 9   ? LEU B 14  ? LYS B 3   LEU B 8   
C 5 GLY B 156 ? ALA B 158 ? GLY B 150 ALA B 152 
D 1 ASP B 89  ? ALA B 95  ? ASP B 83  ALA B 89  
D 2 GLY B 47  ? HIS B 54  ? GLY B 41  HIS B 48  
D 3 THR B 122 ? HIS B 126 ? THR B 116 HIS B 120 
D 4 ARG B 149 ? VAL B 154 ? ARG B 143 VAL B 148 
E 1 VAL C 100 ? ASP C 107 ? VAL C 94  ASP C 101 
E 2 VAL C 35  ? LYS C 42  ? VAL C 29  LYS C 36  
E 3 GLN C 21  ? GLN C 28  ? GLN C 15  GLN C 22  
E 4 THR C 8   ? LEU C 14  ? THR C 2   LEU C 8   
E 5 GLY C 156 ? ALA C 158 ? GLY C 150 ALA C 152 
F 1 ASP C 89  ? ALA C 95  ? ASP C 83  ALA C 89  
F 2 GLY C 47  ? HIS C 54  ? GLY C 41  HIS C 48  
F 3 THR C 122 ? HIS C 126 ? THR C 116 HIS C 120 
F 4 ARG C 149 ? VAL C 154 ? ARG C 143 VAL C 148 
G 1 VAL D 100 ? ASP D 107 ? VAL D 94  ASP D 101 
G 2 VAL D 35  ? LYS D 42  ? VAL D 29  LYS D 36  
G 3 GLN D 21  ? GLU D 27  ? GLN D 15  GLU D 21  
G 4 LYS D 9   ? LYS D 15  ? LYS D 3   LYS D 9   
G 5 GLY D 156 ? ILE D 157 ? GLY D 150 ILE D 151 
H 1 ASP D 89  ? ALA D 95  ? ASP D 83  ALA D 89  
H 2 GLY D 47  ? HIS D 54  ? GLY D 41  HIS D 48  
H 3 THR D 122 ? HIS D 126 ? THR D 116 HIS D 120 
H 4 ARG D 149 ? VAL D 154 ? ARG D 143 VAL D 148 
I 1 VAL E 100 ? ASP E 107 ? VAL E 94  ASP E 101 
I 2 VAL E 35  ? LYS E 42  ? VAL E 29  LYS E 36  
I 3 GLN E 21  ? GLU E 27  ? GLN E 15  GLU E 21  
I 4 LYS E 9   ? LEU E 14  ? LYS E 3   LEU E 8   
I 5 GLY E 156 ? ILE E 157 ? GLY E 150 ILE E 151 
J 1 ASP E 89  ? ALA E 95  ? ASP E 83  ALA E 89  
J 2 GLY E 47  ? HIS E 54  ? GLY E 41  HIS E 48  
J 3 THR E 122 ? HIS E 126 ? THR E 116 HIS E 120 
J 4 ARG E 149 ? VAL E 154 ? ARG E 143 VAL E 148 
K 1 VAL F 100 ? ASP F 107 ? VAL F 94  ASP F 101 
K 2 VAL F 35  ? LYS F 42  ? VAL F 29  LYS F 36  
K 3 GLN F 21  ? GLU F 27  ? GLN F 15  GLU F 21  
K 4 LYS F 9   ? LYS F 15  ? LYS F 3   LYS F 9   
K 5 GLY F 156 ? ALA F 158 ? GLY F 150 ALA F 152 
L 1 ASP F 89  ? ALA F 95  ? ASP F 83  ALA F 89  
L 2 GLY F 47  ? HIS F 54  ? GLY F 41  HIS F 48  
L 3 THR F 122 ? HIS F 126 ? THR F 116 HIS F 120 
L 4 ARG F 149 ? VAL F 154 ? ARG F 143 VAL F 148 
M 1 VAL G 100 ? ASP G 107 ? VAL G 94  ASP G 101 
M 2 VAL G 35  ? LYS G 42  ? VAL G 29  LYS G 36  
M 3 GLN G 21  ? GLU G 27  ? GLN G 15  GLU G 21  
M 4 LYS G 9   ? LYS G 15  ? LYS G 3   LYS G 9   
M 5 GLY G 156 ? ALA G 158 ? GLY G 150 ALA G 152 
N 1 ASP G 89  ? ALA G 95  ? ASP G 83  ALA G 89  
N 2 GLY G 47  ? HIS G 54  ? GLY G 41  HIS G 48  
N 3 THR G 122 ? HIS G 126 ? THR G 116 HIS G 120 
N 4 ARG G 149 ? VAL G 154 ? ARG G 143 VAL G 148 
O 1 LYS H 9   ? LYS H 15  ? LYS H 3   LYS H 9   
O 2 GLN H 21  ? GLN H 28  ? GLN H 15  GLN H 22  
O 3 VAL H 35  ? LYS H 42  ? VAL H 29  LYS H 36  
O 4 ALA H 101 ? ASP H 107 ? ALA H 95  ASP H 101 
O 5 ASP H 89  ? ALA H 95  ? ASP H 83  ALA H 89  
O 6 GLY H 47  ? HIS H 54  ? GLY H 41  HIS H 48  
O 7 THR H 122 ? HIS H 126 ? THR H 116 HIS H 120 
O 8 ARG H 149 ? ILE H 157 ? ARG H 143 ILE H 151 
O 9 LYS H 9   ? LYS H 15  ? LYS H 3   LYS H 9   
P 1 ALA I 101 ? ASP I 107 ? ALA I 95  ASP I 101 
P 2 VAL I 35  ? LYS I 42  ? VAL I 29  LYS I 36  
P 3 GLN I 21  ? GLN I 28  ? GLN I 15  GLN I 22  
P 4 THR I 8   ? LEU I 14  ? THR I 2   LEU I 8   
P 5 GLY I 156 ? ALA I 158 ? GLY I 150 ALA I 152 
Q 1 ASP I 89  ? ALA I 95  ? ASP I 83  ALA I 89  
Q 2 GLY I 47  ? HIS I 54  ? GLY I 41  HIS I 48  
Q 3 THR I 122 ? HIS I 126 ? THR I 116 HIS I 120 
Q 4 ARG I 149 ? VAL I 154 ? ARG I 143 VAL I 148 
R 1 VAL J 100 ? ASP J 107 ? VAL J 94  ASP J 101 
R 2 VAL J 35  ? LYS J 42  ? VAL J 29  LYS J 36  
R 3 GLN J 21  ? GLN J 28  ? GLN J 15  GLN J 22  
R 4 THR J 8   ? LYS J 15  ? THR J 2   LYS J 9   
R 5 GLY J 156 ? ALA J 158 ? GLY J 150 ALA J 152 
S 1 ASP J 89  ? ALA J 95  ? ASP J 83  ALA J 89  
S 2 GLY J 47  ? HIS J 54  ? GLY J 41  HIS J 48  
S 3 THR J 122 ? HIS J 126 ? THR J 116 HIS J 120 
S 4 ARG J 149 ? VAL J 154 ? 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 
A 1 2 O ASP A 107 ? O ASP A 101 N VAL A 35  ? N VAL A 29  
A 2 3 O TRP A 38  ? O TRP A 32  N ASN A 25  ? N ASN A 19  
A 3 4 O GLY A 22  ? O GLY A 16  N LEU A 14  ? N LEU A 8   
A 4 5 N VAL A 11  ? N VAL A 5   O GLY A 156 ? O GLY A 150 
B 1 2 O ALA A 95  ? O ALA A 89  N GLY A 47  ? N GLY A 41  
B 2 3 N HIS A 54  ? N HIS A 48  O THR A 122 ? O THR A 116 
B 3 4 N VAL A 125 ? N VAL A 119 O ALA A 151 ? O ALA A 145 
C 1 2 O ILE B 105 ? O ILE B 99  N VAL B 37  ? N VAL B 31  
C 2 3 O TRP B 38  ? O TRP B 32  N ASN B 25  ? N ASN B 19  
C 3 4 O GLY B 22  ? O GLY B 16  N LEU B 14  ? N LEU B 8   
C 4 5 N LYS B 9   ? N LYS B 3   O ALA B 158 ? O ALA B 152 
D 1 2 O GLY B 91  ? O GLY B 85  N PHE B 51  ? N PHE B 45  
D 2 3 N HIS B 54  ? N HIS B 48  O THR B 122 ? O THR B 116 
D 3 4 N VAL B 125 ? N VAL B 119 O ALA B 151 ? O ALA B 145 
E 1 2 O ASP C 107 ? O ASP C 101 N VAL C 35  ? N VAL C 29  
E 2 3 O TRP C 38  ? O TRP C 32  N ASN C 25  ? N ASN C 19  
E 3 4 O GLY C 22  ? O GLY C 16  N LEU C 14  ? N LEU C 8   
E 4 5 N VAL C 11  ? N VAL C 5   O GLY C 156 ? O GLY C 150 
F 1 2 O ALA C 95  ? O ALA C 89  N GLY C 47  ? N GLY C 41  
F 2 3 N HIS C 54  ? N HIS C 48  O THR C 122 ? O THR C 116 
F 3 4 N LEU C 123 ? N LEU C 117 O GLY C 153 ? O GLY C 147 
G 1 2 O ILE D 105 ? O ILE D 99  N VAL D 37  ? N VAL D 31  
G 2 3 O TRP D 38  ? O TRP D 32  N ASN D 25  ? N ASN D 19  
G 3 4 O GLY D 22  ? O GLY D 16  N LEU D 14  ? N LEU D 8   
G 4 5 N VAL D 11  ? N VAL D 5   O GLY D 156 ? O GLY D 150 
H 1 2 O ALA D 95  ? O ALA D 89  N GLY D 47  ? N GLY D 41  
H 2 3 N HIS D 54  ? N HIS D 48  O THR D 122 ? O THR D 116 
H 3 4 N VAL D 125 ? N VAL D 119 O ALA D 151 ? O ALA D 145 
I 1 2 O ILE E 105 ? O ILE E 99  N VAL E 37  ? N VAL E 31  
I 2 3 O TRP E 38  ? O TRP E 32  N ASN E 25  ? N ASN E 19  
I 3 4 O GLY E 22  ? O GLY E 16  N LEU E 14  ? N LEU E 8   
I 4 5 N VAL E 11  ? N VAL E 5   O GLY E 156 ? O GLY E 150 
J 1 2 O ALA E 95  ? O ALA E 89  N GLY E 47  ? N GLY E 41  
J 2 3 N HIS E 54  ? N HIS E 48  O THR E 122 ? O THR E 116 
J 3 4 N VAL E 125 ? N VAL E 119 O ALA E 151 ? O ALA E 145 
K 1 2 O ILE F 105 ? O ILE F 99  N VAL F 37  ? N VAL F 31  
K 2 3 O TRP F 38  ? O TRP F 32  N ASN F 25  ? N ASN F 19  
K 3 4 O ILE F 24  ? O ILE F 18  N CYS F 12  ? N CYS F 6   
K 4 5 N VAL F 11  ? N VAL F 5   O GLY F 156 ? O GLY F 150 
L 1 2 O GLY F 91  ? O GLY F 85  N PHE F 51  ? N PHE F 45  
L 2 3 N HIS F 54  ? N HIS F 48  O THR F 122 ? O THR F 116 
L 3 4 N LEU F 123 ? N LEU F 117 O GLY F 153 ? O GLY F 147 
M 1 2 O ILE G 105 ? O ILE G 99  N VAL G 37  ? N VAL G 31  
M 2 3 O TRP G 38  ? O TRP G 32  N ASN G 25  ? N ASN G 19  
M 3 4 O GLY G 22  ? O GLY G 16  N LEU G 14  ? N LEU G 8   
M 4 5 N VAL G 11  ? N VAL G 5   O GLY G 156 ? O GLY G 150 
N 1 2 O ALA G 95  ? O ALA G 89  N GLY G 47  ? N GLY G 41  
N 2 3 N HIS G 54  ? N HIS G 48  O THR G 122 ? O THR G 116 
N 3 4 N LEU G 123 ? N LEU G 117 O GLY G 153 ? O GLY G 147 
O 1 2 N LEU H 14  ? N LEU H 8   O GLY H 22  ? O GLY H 16  
O 2 3 N ASN H 25  ? N ASN H 19  O TRP H 38  ? O TRP H 32  
O 3 4 N ILE H 41  ? N ILE H 35  O ALA H 101 ? O ALA H 95  
O 4 5 O ASP H 102 ? O ASP H 96  N THR H 94  ? N THR H 88  
O 5 6 O ALA H 95  ? O ALA H 89  N GLY H 47  ? N GLY H 41  
O 6 7 N GLY H 50  ? N GLY H 44  O HIS H 126 ? O HIS H 120 
O 7 8 N LEU H 123 ? N LEU H 117 O GLY H 153 ? O GLY H 147 
O 8 9 O GLY H 156 ? O GLY H 150 N VAL H 11  ? N VAL H 5   
P 1 2 O ASP I 107 ? O ASP I 101 N VAL I 35  ? N VAL I 29  
P 2 3 O TRP I 38  ? O TRP I 32  N ASN I 25  ? N ASN I 19  
P 3 4 O GLY I 22  ? O GLY I 16  N LEU I 14  ? N LEU I 8   
P 4 5 N LYS I 9   ? N LYS I 3   O ALA I 158 ? O ALA I 152 
Q 1 2 O ALA I 95  ? O ALA I 89  N GLY I 47  ? N GLY I 41  
Q 2 3 N HIS I 54  ? N HIS I 48  O THR I 122 ? O THR I 116 
Q 3 4 N LEU I 123 ? N LEU I 117 O GLY I 153 ? O GLY I 147 
R 1 2 O ASP J 107 ? O ASP J 101 N VAL J 35  ? N VAL J 29  
R 2 3 O TRP J 38  ? O TRP J 32  N ASN J 25  ? N ASN J 19  
R 3 4 O GLY J 22  ? O GLY J 16  N LEU J 14  ? N LEU J 8   
R 4 5 N LYS J 9   ? N LYS J 3   O ALA J 158 ? O ALA J 152 
S 1 2 O GLY J 91  ? O GLY J 85  N PHE J 51  ? N PHE J 45  
S 2 3 N HIS J 54  ? N HIS J 48  O THR J 122 ? O THR J 116 
S 3 4 N LEU J 123 ? N LEU J 117 O GLY J 153 ? O GLY J 147 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN 601 ? 4 'BINDING SITE FOR RESIDUE ZN A 601' 
AC2 Software B ZN 602 ? 4 'BINDING SITE FOR RESIDUE ZN B 602' 
AC3 Software C ZN 603 ? 4 'BINDING SITE FOR RESIDUE ZN C 603' 
AC4 Software D ZN 604 ? 4 'BINDING SITE FOR RESIDUE ZN D 604' 
AC5 Software E ZN 605 ? 5 'BINDING SITE FOR RESIDUE ZN E 605' 
AC6 Software F ZN 606 ? 4 'BINDING SITE FOR RESIDUE ZN F 606' 
AC7 Software G ZN 607 ? 5 'BINDING SITE FOR RESIDUE ZN G 607' 
AC8 Software H ZN 608 ? 4 'BINDING SITE FOR RESIDUE ZN H 608' 
AC9 Software I ZN 609 ? 4 'BINDING SITE FOR RESIDUE ZN I 609' 
BC1 Software J ZN 610 ? 4 'BINDING SITE FOR RESIDUE ZN J 610' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 HIS A 69  ? HIS A 63  . ? 1_555 ? 
2  AC1 4 HIS A 77  ? HIS A 71  . ? 1_555 ? 
3  AC1 4 HIS A 86  ? HIS A 80  . ? 1_555 ? 
4  AC1 4 ASP A 89  ? ASP A 83  . ? 1_555 ? 
5  AC2 4 HIS B 69  ? HIS B 63  . ? 1_555 ? 
6  AC2 4 HIS B 77  ? HIS B 71  . ? 1_555 ? 
7  AC2 4 HIS B 86  ? HIS B 80  . ? 1_555 ? 
8  AC2 4 ASP B 89  ? ASP B 83  . ? 1_555 ? 
9  AC3 4 HIS C 69  ? HIS C 63  . ? 1_555 ? 
10 AC3 4 HIS C 77  ? HIS C 71  . ? 1_555 ? 
11 AC3 4 HIS C 86  ? HIS C 80  . ? 1_555 ? 
12 AC3 4 ASP C 89  ? ASP C 83  . ? 1_555 ? 
13 AC4 4 HIS D 69  ? HIS D 63  . ? 1_555 ? 
14 AC4 4 HIS D 77  ? HIS D 71  . ? 1_555 ? 
15 AC4 4 HIS D 86  ? HIS D 80  . ? 1_555 ? 
16 AC4 4 ASP D 89  ? ASP D 83  . ? 1_555 ? 
17 AC5 5 HIS E 69  ? HIS E 63  . ? 1_555 ? 
18 AC5 5 HIS E 77  ? HIS E 71  . ? 1_555 ? 
19 AC5 5 HIS E 86  ? HIS E 80  . ? 1_555 ? 
20 AC5 5 ASP E 89  ? ASP E 83  . ? 1_555 ? 
21 AC5 5 LYS E 142 ? LYS E 136 . ? 1_555 ? 
22 AC6 4 HIS F 69  ? HIS F 63  . ? 1_555 ? 
23 AC6 4 HIS F 77  ? HIS F 71  . ? 1_555 ? 
24 AC6 4 HIS F 86  ? HIS F 80  . ? 1_555 ? 
25 AC6 4 ASP F 89  ? ASP F 83  . ? 1_555 ? 
26 AC7 5 HIS G 69  ? HIS G 63  . ? 1_555 ? 
27 AC7 5 HIS G 77  ? HIS G 71  . ? 1_555 ? 
28 AC7 5 HIS G 86  ? HIS G 80  . ? 1_555 ? 
29 AC7 5 ASP G 89  ? ASP G 83  . ? 1_555 ? 
30 AC7 5 LYS G 142 ? LYS G 136 . ? 1_555 ? 
31 AC8 4 HIS H 69  ? HIS H 63  . ? 1_555 ? 
32 AC8 4 HIS H 77  ? HIS H 71  . ? 1_555 ? 
33 AC8 4 HIS H 86  ? HIS H 80  . ? 1_555 ? 
34 AC8 4 ASP H 89  ? ASP H 83  . ? 1_555 ? 
35 AC9 4 HIS I 69  ? HIS I 63  . ? 1_555 ? 
36 AC9 4 HIS I 77  ? HIS I 71  . ? 1_555 ? 
37 AC9 4 HIS I 86  ? HIS I 80  . ? 1_555 ? 
38 AC9 4 ASP I 89  ? ASP I 83  . ? 1_555 ? 
39 BC1 4 HIS J 69  ? HIS J 63  . ? 1_555 ? 
40 BC1 4 HIS J 77  ? HIS J 71  . ? 1_555 ? 
41 BC1 4 HIS J 86  ? HIS J 80  . ? 1_555 ? 
42 BC1 4 ASP J 89  ? ASP J 83  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2ZKY 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    2ZKY 
_atom_sites.fract_transf_matrix[1][1]   0.006052 
_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]   0.004890 
_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]   0.006905 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
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   . THR A  1 8   ? 53.196  48.678  44.528 1.00 30.64  ? 2   THR A N   1 
ATOM   2     C  CA  . THR A  1 8   ? 53.133  50.058  45.111 1.00 36.84  ? 2   THR A CA  1 
ATOM   3     C  C   . THR A  1 8   ? 52.287  50.059  46.388 1.00 32.31  ? 2   THR A C   1 
ATOM   4     O  O   . THR A  1 8   ? 51.189  49.497  46.446 1.00 34.63  ? 2   THR A O   1 
ATOM   5     C  CB  . THR A  1 8   ? 52.590  51.093  44.062 1.00 33.61  ? 2   THR A CB  1 
ATOM   6     O  OG1 . THR A  1 8   ? 53.287  52.336  44.206 1.00 42.16  ? 2   THR A OG1 1 
ATOM   7     C  CG2 . THR A  1 8   ? 51.121  51.350  44.246 1.00 48.47  ? 2   THR A CG2 1 
ATOM   8     N  N   . LYS A  1 9   ? 52.832  50.664  47.430 1.00 32.24  ? 3   LYS A N   1 
ATOM   9     C  CA  . LYS A  1 9   ? 52.161  50.720  48.716 1.00 29.85  ? 3   LYS A CA  1 
ATOM   10    C  C   . LYS A  1 9   ? 52.213  52.113  49.323 1.00 28.41  ? 3   LYS A C   1 
ATOM   11    O  O   . LYS A  1 9   ? 53.058  52.941  48.969 1.00 30.37  ? 3   LYS A O   1 
ATOM   12    C  CB  . LYS A  1 9   ? 52.819  49.772  49.720 1.00 40.97  ? 3   LYS A CB  1 
ATOM   13    C  CG  . LYS A  1 9   ? 52.838  48.299  49.387 1.00 44.01  ? 3   LYS A CG  1 
ATOM   14    C  CD  . LYS A  1 9   ? 53.174  47.535  50.666 1.00 58.16  ? 3   LYS A CD  1 
ATOM   15    C  CE  . LYS A  1 9   ? 53.252  46.036  50.450 1.00 68.20  ? 3   LYS A CE  1 
ATOM   16    N  NZ  . LYS A  1 9   ? 54.407  45.666  49.581 1.00 70.71  ? 3   LYS A NZ  1 
ATOM   17    N  N   . ALA A  1 10  ? 51.303  52.350  50.255 1.00 16.86  ? 4   ALA A N   1 
ATOM   18    C  CA  . ALA A  1 10  ? 51.222  53.604  50.971 1.00 18.86  ? 4   ALA A CA  1 
ATOM   19    C  C   . ALA A  1 10  ? 50.712  53.280  52.374 1.00 28.35  ? 4   ALA A C   1 
ATOM   20    O  O   . ALA A  1 10  ? 50.208  52.176  52.637 1.00 27.01  ? 4   ALA A O   1 
ATOM   21    C  CB  . ALA A  1 10  ? 50.280  54.539  50.277 1.00 22.93  ? 4   ALA A CB  1 
ATOM   22    N  N   . VAL A  1 11  ? 50.861  54.227  53.286 1.00 24.27  ? 5   VAL A N   1 
ATOM   23    C  CA  . VAL A  1 11  ? 50.396  54.008  54.636 1.00 25.60  ? 5   VAL A CA  1 
ATOM   24    C  C   . VAL A  1 11  ? 49.971  55.337  55.203 1.00 26.29  ? 5   VAL A C   1 
ATOM   25    O  O   . VAL A  1 11  ? 50.348  56.384  54.693 1.00 32.61  ? 5   VAL A O   1 
ATOM   26    C  CB  . VAL A  1 11  ? 51.485  53.386  55.521 1.00 27.46  ? 5   VAL A CB  1 
ATOM   27    C  CG1 . VAL A  1 11  ? 52.639  54.366  55.702 1.00 25.39  ? 5   VAL A CG1 1 
ATOM   28    C  CG2 . VAL A  1 11  ? 50.890  52.978  56.863 1.00 18.95  ? 5   VAL A CG2 1 
ATOM   29    N  N   . CYS A  1 12  ? 49.169  55.292  56.253 1.00 25.97  ? 6   CYS A N   1 
ATOM   30    C  CA  . CYS A  1 12  ? 48.697  56.505  56.878 1.00 25.06  ? 6   CYS A CA  1 
ATOM   31    C  C   . CYS A  1 12  ? 48.468  56.316  58.369 1.00 30.67  ? 6   CYS A C   1 
ATOM   32    O  O   . CYS A  1 12  ? 47.834  55.344  58.801 1.00 28.34  ? 6   CYS A O   1 
ATOM   33    C  CB  . CYS A  1 12  ? 47.394  56.946  56.228 1.00 30.97  ? 6   CYS A CB  1 
ATOM   34    S  SG  . CYS A  1 12  ? 46.710  58.442  56.929 1.00 27.15  ? 6   CYS A SG  1 
ATOM   35    N  N   . VAL A  1 13  ? 49.015  57.237  59.152 1.00 23.90  ? 7   VAL A N   1 
ATOM   36    C  CA  . VAL A  1 13  ? 48.834  57.208  60.579 1.00 23.57  ? 7   VAL A CA  1 
ATOM   37    C  C   . VAL A  1 13  ? 47.797  58.282  60.900 1.00 25.70  ? 7   VAL A C   1 
ATOM   38    O  O   . VAL A  1 13  ? 48.014  59.470  60.652 1.00 23.55  ? 7   VAL A O   1 
ATOM   39    C  CB  . VAL A  1 13  ? 50.139  57.504  61.300 1.00 27.48  ? 7   VAL A CB  1 
ATOM   40    C  CG1 . VAL A  1 13  ? 49.887  57.581  62.804 1.00 25.72  ? 7   VAL A CG1 1 
ATOM   41    C  CG2 . VAL A  1 13  ? 51.152  56.407  60.982 1.00 18.54  ? 7   VAL A CG2 1 
ATOM   42    N  N   . LEU A  1 14  ? 46.652  57.859  61.423 1.00 25.96  ? 8   LEU A N   1 
ATOM   43    C  CA  . LEU A  1 14  ? 45.592  58.798  61.757 1.00 22.14  ? 8   LEU A CA  1 
ATOM   44    C  C   . LEU A  1 14  ? 45.658  59.204  63.216 1.00 24.19  ? 8   LEU A C   1 
ATOM   45    O  O   . LEU A  1 14  ? 45.738  58.350  64.111 1.00 24.50  ? 8   LEU A O   1 
ATOM   46    C  CB  . LEU A  1 14  ? 44.221  58.180  61.461 1.00 26.33  ? 8   LEU A CB  1 
ATOM   47    C  CG  . LEU A  1 14  ? 43.926  57.799  60.007 1.00 29.50  ? 8   LEU A CG  1 
ATOM   48    C  CD1 . LEU A  1 14  ? 42.671  56.951  59.913 1.00 29.62  ? 8   LEU A CD1 1 
ATOM   49    C  CD2 . LEU A  1 14  ? 43.756  59.058  59.193 1.00 42.05  ? 8   LEU A CD2 1 
ATOM   50    N  N   . LYS A  1 15  ? 45.622  60.515  63.445 1.00 29.03  ? 9   LYS A N   1 
ATOM   51    C  CA  . LYS A  1 15  ? 45.658  61.084  64.787 1.00 26.77  ? 9   LYS A CA  1 
ATOM   52    C  C   . LYS A  1 15  ? 44.730  62.283  64.834 1.00 31.26  ? 9   LYS A C   1 
ATOM   53    O  O   . LYS A  1 15  ? 44.415  62.875  63.801 1.00 30.51  ? 9   LYS A O   1 
ATOM   54    C  CB  . LYS A  1 15  ? 47.077  61.506  65.149 1.00 30.87  ? 9   LYS A CB  1 
ATOM   55    C  CG  . LYS A  1 15  ? 47.940  60.326  65.510 1.00 50.47  ? 9   LYS A CG  1 
ATOM   56    C  CD  . LYS A  1 15  ? 49.402  60.690  65.722 1.00 61.29  ? 9   LYS A CD  1 
ATOM   57    C  CE  . LYS A  1 15  ? 50.179  59.455  66.199 1.00 65.90  ? 9   LYS A CE  1 
ATOM   58    N  NZ  . LYS A  1 15  ? 51.655  59.611  66.106 1.00 66.41  ? 9   LYS A NZ  1 
ATOM   59    N  N   . GLY A  1 16  ? 44.280  62.630  66.035 1.00 35.60  ? 10  GLY A N   1 
ATOM   60    C  CA  . GLY A  1 16  ? 43.385  63.762  66.195 1.00 35.14  ? 10  GLY A CA  1 
ATOM   61    C  C   . GLY A  1 16  ? 43.535  64.391  67.563 1.00 34.35  ? 10  GLY A C   1 
ATOM   62    O  O   . GLY A  1 16  ? 44.461  64.057  68.295 1.00 34.52  ? 10  GLY A O   1 
ATOM   63    N  N   . ASP A  1 17  ? 42.633  65.302  67.907 1.00 36.71  ? 11  ASP A N   1 
ATOM   64    C  CA  . ASP A  1 17  ? 42.680  65.958  69.206 1.00 40.63  ? 11  ASP A CA  1 
ATOM   65    C  C   . ASP A  1 17  ? 42.122  65.049  70.271 1.00 44.04  ? 11  ASP A C   1 
ATOM   66    O  O   . ASP A  1 17  ? 42.441  65.197  71.448 1.00 45.85  ? 11  ASP A O   1 
ATOM   67    C  CB  . ASP A  1 17  ? 41.872  67.248  69.186 1.00 40.15  ? 11  ASP A CB  1 
ATOM   68    C  CG  . ASP A  1 17  ? 42.552  68.335  68.395 1.00 54.39  ? 11  ASP A CG  1 
ATOM   69    O  OD1 . ASP A  1 17  ? 41.880  69.328  68.042 1.00 52.90  ? 11  ASP A OD1 1 
ATOM   70    O  OD2 . ASP A  1 17  ? 43.771  68.193  68.137 1.00 59.30  ? 11  ASP A OD2 1 
ATOM   71    N  N   . GLY A  1 18  ? 41.287  64.105  69.847 1.00 45.03  ? 12  GLY A N   1 
ATOM   72    C  CA  . GLY A  1 18  ? 40.670  63.192  70.783 1.00 38.02  ? 12  GLY A CA  1 
ATOM   73    C  C   . GLY A  1 18  ? 41.416  61.886  70.920 1.00 38.14  ? 12  GLY A C   1 
ATOM   74    O  O   . GLY A  1 18  ? 42.631  61.826  70.703 1.00 32.14  ? 12  GLY A O   1 
ATOM   75    N  N   . PRO A  1 19  ? 40.696  60.810  71.274 1.00 33.00  ? 13  PRO A N   1 
ATOM   76    C  CA  . PRO A  1 19  ? 41.247  59.464  71.459 1.00 31.19  ? 13  PRO A CA  1 
ATOM   77    C  C   . PRO A  1 19  ? 41.423  58.680  70.151 1.00 29.24  ? 13  PRO A C   1 
ATOM   78    O  O   . PRO A  1 19  ? 42.126  57.669  70.128 1.00 28.74  ? 13  PRO A O   1 
ATOM   79    C  CB  . PRO A  1 19  ? 40.223  58.809  72.379 1.00 18.81  ? 13  PRO A CB  1 
ATOM   80    C  CG  . PRO A  1 19  ? 38.917  59.371  71.853 1.00 25.44  ? 13  PRO A CG  1 
ATOM   81    C  CD  . PRO A  1 19  ? 39.233  60.823  71.493 1.00 23.50  ? 13  PRO A CD  1 
ATOM   82    N  N   . VAL A  1 20  ? 40.793  59.149  69.071 1.00 20.79  ? 14  VAL A N   1 
ATOM   83    C  CA  . VAL A  1 20  ? 40.871  58.450  67.791 1.00 25.71  ? 14  VAL A CA  1 
ATOM   84    C  C   . VAL A  1 20  ? 42.279  58.344  67.224 1.00 25.67  ? 14  VAL A C   1 
ATOM   85    O  O   . VAL A  1 20  ? 42.983  59.340  67.070 1.00 33.08  ? 14  VAL A O   1 
ATOM   86    C  CB  . VAL A  1 20  ? 39.971  59.109  66.727 1.00 29.76  ? 14  VAL A CB  1 
ATOM   87    C  CG1 . VAL A  1 20  ? 40.038  58.310  65.448 1.00 25.77  ? 14  VAL A CG1 1 
ATOM   88    C  CG2 . VAL A  1 20  ? 38.518  59.182  67.228 1.00 28.43  ? 14  VAL A CG2 1 
ATOM   89    N  N   . GLN A  1 21  ? 42.695  57.121  66.938 1.00 21.91  ? 15  GLN A N   1 
ATOM   90    C  CA  . GLN A  1 21  ? 44.004  56.893  66.372 1.00 30.93  ? 15  GLN A CA  1 
ATOM   91    C  C   . GLN A  1 21  ? 44.051  55.545  65.680 1.00 31.99  ? 15  GLN A C   1 
ATOM   92    O  O   . GLN A  1 21  ? 43.391  54.600  66.102 1.00 31.91  ? 15  GLN A O   1 
ATOM   93    C  CB  . GLN A  1 21  ? 45.098  56.994  67.444 1.00 30.55  ? 15  GLN A CB  1 
ATOM   94    C  CG  . GLN A  1 21  ? 44.821  56.303  68.748 1.00 39.71  ? 15  GLN A CG  1 
ATOM   95    C  CD  . GLN A  1 21  ? 45.932  56.540  69.783 1.00 48.36  ? 15  GLN A CD  1 
ATOM   96    O  OE1 . GLN A  1 21  ? 46.850  55.726  69.931 1.00 41.33  ? 15  GLN A OE1 1 
ATOM   97    N  NE2 . GLN A  1 21  ? 45.852  57.667  70.493 1.00 46.24  ? 15  GLN A NE2 1 
ATOM   98    N  N   . GLY A  1 22  ? 44.819  55.478  64.597 1.00 29.61  ? 16  GLY A N   1 
ATOM   99    C  CA  . GLY A  1 22  ? 44.937  54.243  63.853 1.00 30.55  ? 16  GLY A CA  1 
ATOM   100   C  C   . GLY A  1 22  ? 45.935  54.280  62.705 1.00 31.37  ? 16  GLY A C   1 
ATOM   101   O  O   . GLY A  1 22  ? 46.558  55.305  62.420 1.00 29.23  ? 16  GLY A O   1 
ATOM   102   N  N   . ILE A  1 23  ? 46.060  53.141  62.034 1.00 27.50  ? 17  ILE A N   1 
ATOM   103   C  CA  . ILE A  1 23  ? 46.974  52.971  60.925 1.00 24.04  ? 17  ILE A CA  1 
ATOM   104   C  C   . ILE A  1 23  ? 46.251  52.327  59.757 1.00 32.67  ? 17  ILE A C   1 
ATOM   105   O  O   . ILE A  1 23  ? 45.680  51.246  59.897 1.00 31.69  ? 17  ILE A O   1 
ATOM   106   C  CB  . ILE A  1 23  ? 48.137  52.069  61.339 1.00 21.19  ? 17  ILE A CB  1 
ATOM   107   C  CG1 . ILE A  1 23  ? 48.920  52.753  62.458 1.00 27.01  ? 17  ILE A CG1 1 
ATOM   108   C  CG2 . ILE A  1 23  ? 49.003  51.740  60.129 1.00 13.68  ? 17  ILE A CG2 1 
ATOM   109   C  CD1 . ILE A  1 23  ? 50.096  51.965  62.967 1.00 31.75  ? 17  ILE A CD1 1 
ATOM   110   N  N   . ILE A  1 24  ? 46.280  52.991  58.606 1.00 28.97  ? 18  ILE A N   1 
ATOM   111   C  CA  . ILE A  1 24  ? 45.627  52.467  57.425 1.00 25.35  ? 18  ILE A CA  1 
ATOM   112   C  C   . ILE A  1 24  ? 46.643  52.197  56.341 1.00 26.34  ? 18  ILE A C   1 
ATOM   113   O  O   . ILE A  1 24  ? 47.483  53.052  56.045 1.00 32.04  ? 18  ILE A O   1 
ATOM   114   C  CB  . ILE A  1 24  ? 44.589  53.450  56.901 1.00 27.08  ? 18  ILE A CB  1 
ATOM   115   C  CG1 . ILE A  1 24  ? 43.566  53.726  57.996 1.00 27.64  ? 18  ILE A CG1 1 
ATOM   116   C  CG2 . ILE A  1 24  ? 43.912  52.885  55.657 1.00 25.62  ? 18  ILE A CG2 1 
ATOM   117   C  CD1 . ILE A  1 24  ? 42.748  52.511  58.376 1.00 33.77  ? 18  ILE A CD1 1 
ATOM   118   N  N   . ASN A  1 25  ? 46.558  51.004  55.754 1.00 26.00  ? 19  ASN A N   1 
ATOM   119   C  CA  . ASN A  1 25  ? 47.456  50.555  54.684 1.00 24.48  ? 19  ASN A CA  1 
ATOM   120   C  C   . ASN A  1 25  ? 46.804  50.625  53.310 1.00 26.04  ? 19  ASN A C   1 
ATOM   121   O  O   . ASN A  1 25  ? 45.583  50.579  53.186 1.00 30.65  ? 19  ASN A O   1 
ATOM   122   C  CB  . ASN A  1 25  ? 47.897  49.116  54.943 1.00 25.52  ? 19  ASN A CB  1 
ATOM   123   C  CG  . ASN A  1 25  ? 48.638  48.965  56.256 1.00 38.12  ? 19  ASN A CG  1 
ATOM   124   O  OD1 . ASN A  1 25  ? 49.776  49.420  56.393 1.00 28.50  ? 19  ASN A OD1 1 
ATOM   125   N  ND2 . ASN A  1 25  ? 47.990  48.332  57.237 1.00 27.12  ? 19  ASN A ND2 1 
ATOM   126   N  N   . PHE A  1 26  ? 47.624  50.734  52.272 1.00 28.22  ? 20  PHE A N   1 
ATOM   127   C  CA  . PHE A  1 26  ? 47.104  50.809  50.911 1.00 27.14  ? 20  PHE A CA  1 
ATOM   128   C  C   . PHE A  1 26  ? 48.013  49.986  50.028 1.00 32.72  ? 20  PHE A C   1 
ATOM   129   O  O   . PHE A  1 26  ? 49.240  50.076  50.133 1.00 29.75  ? 20  PHE A O   1 
ATOM   130   C  CB  . PHE A  1 26  ? 47.116  52.243  50.381 1.00 18.80  ? 20  PHE A CB  1 
ATOM   131   C  CG  . PHE A  1 26  ? 46.270  53.205  51.157 1.00 25.21  ? 20  PHE A CG  1 
ATOM   132   C  CD1 . PHE A  1 26  ? 45.006  53.572  50.694 1.00 24.86  ? 20  PHE A CD1 1 
ATOM   133   C  CD2 . PHE A  1 26  ? 46.780  53.836  52.297 1.00 30.24  ? 20  PHE A CD2 1 
ATOM   134   C  CE1 . PHE A  1 26  ? 44.262  54.565  51.345 1.00 23.86  ? 20  PHE A CE1 1 
ATOM   135   C  CE2 . PHE A  1 26  ? 46.047  54.829  52.958 1.00 22.74  ? 20  PHE A CE2 1 
ATOM   136   C  CZ  . PHE A  1 26  ? 44.785  55.197  52.475 1.00 28.55  ? 20  PHE A CZ  1 
ATOM   137   N  N   . GLU A  1 27  ? 47.413  49.184  49.155 1.00 35.12  ? 21  GLU A N   1 
ATOM   138   C  CA  . GLU A  1 27  ? 48.196  48.358  48.251 1.00 38.68  ? 21  GLU A CA  1 
ATOM   139   C  C   . GLU A  1 27  ? 47.570  48.315  46.868 1.00 36.29  ? 21  GLU A C   1 
ATOM   140   O  O   . GLU A  1 27  ? 46.340  48.246  46.721 1.00 32.56  ? 21  GLU A O   1 
ATOM   141   C  CB  . GLU A  1 27  ? 48.340  46.949  48.809 1.00 33.77  ? 21  GLU A CB  1 
ATOM   142   C  CG  . GLU A  1 27  ? 49.172  46.049  47.939 1.00 56.03  ? 21  GLU A CG  1 
ATOM   143   C  CD  . GLU A  1 27  ? 49.446  44.715  48.594 1.00 64.62  ? 21  GLU A CD  1 
ATOM   144   O  OE1 . GLU A  1 27  ? 50.214  44.689  49.577 1.00 69.38  ? 21  GLU A OE1 1 
ATOM   145   O  OE2 . GLU A  1 27  ? 48.884  43.699  48.131 1.00 70.74  ? 21  GLU A OE2 1 
ATOM   146   N  N   . GLN A  1 28  ? 48.426  48.377  45.853 1.00 31.93  ? 22  GLN A N   1 
ATOM   147   C  CA  . GLN A  1 28  ? 47.971  48.354  44.473 1.00 30.32  ? 22  GLN A CA  1 
ATOM   148   C  C   . GLN A  1 28  ? 49.036  47.662  43.638 1.00 33.03  ? 22  GLN A C   1 
ATOM   149   O  O   . GLN A  1 28  ? 50.054  48.261  43.280 1.00 30.80  ? 22  GLN A O   1 
ATOM   150   C  CB  . GLN A  1 28  ? 47.723  49.784  43.986 1.00 28.07  ? 22  GLN A CB  1 
ATOM   151   C  CG  . GLN A  1 28  ? 47.381  49.907  42.504 1.00 32.51  ? 22  GLN A CG  1 
ATOM   152   C  CD  . GLN A  1 28  ? 46.947  51.312  42.124 1.00 28.76  ? 22  GLN A CD  1 
ATOM   153   O  OE1 . GLN A  1 28  ? 47.569  52.293  42.520 1.00 31.74  ? 22  GLN A OE1 1 
ATOM   154   N  NE2 . GLN A  1 28  ? 45.879  51.413  41.352 1.00 36.30  ? 22  GLN A NE2 1 
ATOM   155   N  N   . LYS A  1 29  ? 48.795  46.390  43.336 1.00 34.60  ? 23  LYS A N   1 
ATOM   156   C  CA  . LYS A  1 29  ? 49.738  45.590  42.561 1.00 37.98  ? 23  LYS A CA  1 
ATOM   157   C  C   . LYS A  1 29  ? 49.868  46.058  41.114 1.00 34.14  ? 23  LYS A C   1 
ATOM   158   O  O   . LYS A  1 29  ? 50.940  45.967  40.533 1.00 35.93  ? 23  LYS A O   1 
ATOM   159   C  CB  . LYS A  1 29  ? 49.314  44.121  42.595 1.00 43.33  ? 23  LYS A CB  1 
ATOM   160   C  CG  . LYS A  1 29  ? 49.005  43.609  43.990 1.00 61.09  ? 23  LYS A CG  1 
ATOM   161   C  CD  . LYS A  1 29  ? 48.514  42.167  43.968 1.00 73.26  ? 23  LYS A CD  1 
ATOM   162   C  CE  . LYS A  1 29  ? 48.265  41.643  45.378 1.00 76.60  ? 23  LYS A CE  1 
ATOM   163   N  NZ  . LYS A  1 29  ? 48.009  40.176  45.388 1.00 79.73  ? 23  LYS A NZ  1 
ATOM   164   N  N   . GLU A  1 30  ? 48.784  46.575  40.538 1.00 35.68  ? 24  GLU A N   1 
ATOM   165   C  CA  . GLU A  1 30  ? 48.798  47.035  39.146 1.00 41.15  ? 24  GLU A CA  1 
ATOM   166   C  C   . GLU A  1 30  ? 48.408  48.496  39.050 1.00 37.13  ? 24  GLU A C   1 
ATOM   167   O  O   . GLU A  1 30  ? 47.428  48.925  39.657 1.00 38.97  ? 24  GLU A O   1 
ATOM   168   C  CB  . GLU A  1 30  ? 47.814  46.225  38.293 1.00 44.37  ? 24  GLU A CB  1 
ATOM   169   C  CG  . GLU A  1 30  ? 48.038  44.728  38.303 1.00 65.06  ? 24  GLU A CG  1 
ATOM   170   C  CD  . GLU A  1 30  ? 49.075  44.288  37.298 1.00 80.35  ? 24  GLU A CD  1 
ATOM   171   O  OE1 . GLU A  1 30  ? 50.186  44.858  37.298 1.00 88.34  ? 24  GLU A OE1 1 
ATOM   172   O  OE2 . GLU A  1 30  ? 48.778  43.367  36.510 1.00 90.26  ? 24  GLU A OE2 1 
ATOM   173   N  N   . SER A  1 31  ? 49.161  49.253  38.263 1.00 31.78  ? 25  SER A N   1 
ATOM   174   C  CA  . SER A  1 31  ? 48.875  50.670  38.094 1.00 26.60  ? 25  SER A CA  1 
ATOM   175   C  C   . SER A  1 31  ? 47.443  50.896  37.603 1.00 33.03  ? 25  SER A C   1 
ATOM   176   O  O   . SER A  1 31  ? 46.835  51.935  37.888 1.00 30.33  ? 25  SER A O   1 
ATOM   177   C  CB  . SER A  1 31  ? 49.863  51.284  37.099 1.00 20.45  ? 25  SER A CB  1 
ATOM   178   O  OG  . SER A  1 31  ? 49.763  50.690  35.812 1.00 28.91  ? 25  SER A OG  1 
ATOM   179   N  N   . ASN A  1 32  ? 46.907  49.934  36.853 1.00 28.07  ? 26  ASN A N   1 
ATOM   180   C  CA  . ASN A  1 32  ? 45.553  50.069  36.330 1.00 30.51  ? 26  ASN A CA  1 
ATOM   181   C  C   . ASN A  1 32  ? 44.559  49.169  37.049 1.00 36.25  ? 26  ASN A C   1 
ATOM   182   O  O   . ASN A  1 32  ? 43.415  49.004  36.605 1.00 32.59  ? 26  ASN A O   1 
ATOM   183   C  CB  . ASN A  1 32  ? 45.533  49.815  34.815 1.00 32.41  ? 26  ASN A CB  1 
ATOM   184   C  CG  . ASN A  1 32  ? 45.881  48.386  34.433 1.00 37.00  ? 26  ASN A CG  1 
ATOM   185   O  OD1 . ASN A  1 32  ? 46.663  47.709  35.106 1.00 44.76  ? 26  ASN A OD1 1 
ATOM   186   N  ND2 . ASN A  1 32  ? 45.318  47.931  33.315 1.00 29.14  ? 26  ASN A ND2 1 
ATOM   187   N  N   . GLY A  1 33  ? 45.009  48.617  38.179 1.00 37.53  ? 27  GLY A N   1 
ATOM   188   C  CA  . GLY A  1 33  ? 44.178  47.747  38.992 1.00 30.42  ? 27  GLY A CA  1 
ATOM   189   C  C   . GLY A  1 33  ? 43.576  48.461  40.191 1.00 41.11  ? 27  GLY A C   1 
ATOM   190   O  O   . GLY A  1 33  ? 43.724  49.675  40.350 1.00 33.26  ? 27  GLY A O   1 
ATOM   191   N  N   . PRO A  1 34  ? 42.872  47.728  41.061 1.00 43.28  ? 28  PRO A N   1 
ATOM   192   C  CA  . PRO A  1 34  ? 42.263  48.355  42.235 1.00 40.24  ? 28  PRO A CA  1 
ATOM   193   C  C   . PRO A  1 34  ? 43.224  48.505  43.405 1.00 33.67  ? 28  PRO A C   1 
ATOM   194   O  O   . PRO A  1 34  ? 44.315  47.931  43.414 1.00 29.77  ? 28  PRO A O   1 
ATOM   195   C  CB  . PRO A  1 34  ? 41.095  47.424  42.545 1.00 41.49  ? 28  PRO A CB  1 
ATOM   196   C  CG  . PRO A  1 34  ? 41.659  46.090  42.203 1.00 47.11  ? 28  PRO A CG  1 
ATOM   197   C  CD  . PRO A  1 34  ? 42.386  46.347  40.892 1.00 44.98  ? 28  PRO A CD  1 
ATOM   198   N  N   . VAL A  1 35  ? 42.795  49.277  44.397 1.00 32.71  ? 29  VAL A N   1 
ATOM   199   C  CA  . VAL A  1 35  ? 43.593  49.550  45.594 1.00 31.55  ? 29  VAL A CA  1 
ATOM   200   C  C   . VAL A  1 35  ? 42.963  48.879  46.813 1.00 32.02  ? 29  VAL A C   1 
ATOM   201   O  O   . VAL A  1 35  ? 41.774  49.083  47.081 1.00 30.78  ? 29  VAL A O   1 
ATOM   202   C  CB  . VAL A  1 35  ? 43.675  51.098  45.854 1.00 30.86  ? 29  VAL A CB  1 
ATOM   203   C  CG1 . VAL A  1 35  ? 44.433  51.396  47.138 1.00 26.62  ? 29  VAL A CG1 1 
ATOM   204   C  CG2 . VAL A  1 35  ? 44.348  51.786  44.684 1.00 27.25  ? 29  VAL A CG2 1 
ATOM   205   N  N   . LYS A  1 36  ? 43.743  48.056  47.515 1.00 28.61  ? 30  LYS A N   1 
ATOM   206   C  CA  . LYS A  1 36  ? 43.271  47.400  48.737 1.00 37.21  ? 30  LYS A CA  1 
ATOM   207   C  C   . LYS A  1 36  ? 43.584  48.387  49.869 1.00 36.47  ? 30  LYS A C   1 
ATOM   208   O  O   . LYS A  1 36  ? 44.681  48.960  49.925 1.00 30.03  ? 30  LYS A O   1 
ATOM   209   C  CB  . LYS A  1 36  ? 44.022  46.092  49.011 1.00 42.61  ? 30  LYS A CB  1 
ATOM   210   C  CG  . LYS A  1 36  ? 43.767  44.951  48.037 1.00 63.43  ? 30  LYS A CG  1 
ATOM   211   C  CD  . LYS A  1 36  ? 44.651  43.734  48.385 1.00 72.14  ? 30  LYS A CD  1 
ATOM   212   C  CE  . LYS A  1 36  ? 44.640  42.656  47.297 1.00 74.93  ? 30  LYS A CE  1 
ATOM   213   N  NZ  . LYS A  1 36  ? 43.278  42.106  47.055 1.00 76.17  ? 30  LYS A NZ  1 
ATOM   214   N  N   . VAL A  1 37  ? 42.625  48.579  50.766 1.00 29.21  ? 31  VAL A N   1 
ATOM   215   C  CA  . VAL A  1 37  ? 42.777  49.504  51.881 1.00 31.07  ? 31  VAL A CA  1 
ATOM   216   C  C   . VAL A  1 37  ? 42.421  48.788  53.176 1.00 35.27  ? 31  VAL A C   1 
ATOM   217   O  O   . VAL A  1 37  ? 41.292  48.318  53.323 1.00 37.95  ? 31  VAL A O   1 
ATOM   218   C  CB  . VAL A  1 37  ? 41.838  50.718  51.693 1.00 32.49  ? 31  VAL A CB  1 
ATOM   219   C  CG1 . VAL A  1 37  ? 42.016  51.722  52.836 1.00 35.48  ? 31  VAL A CG1 1 
ATOM   220   C  CG2 . VAL A  1 37  ? 42.116  51.377  50.344 1.00 27.48  ? 31  VAL A CG2 1 
ATOM   221   N  N   . TRP A  1 38  ? 43.359  48.690  54.116 1.00 32.50  ? 32  TRP A N   1 
ATOM   222   C  CA  . TRP A  1 38  ? 43.040  47.995  55.359 1.00 31.43  ? 32  TRP A CA  1 
ATOM   223   C  C   . TRP A  1 38  ? 43.797  48.452  56.589 1.00 30.53  ? 32  TRP A C   1 
ATOM   224   O  O   . TRP A  1 38  ? 44.860  49.058  56.488 1.00 34.34  ? 32  TRP A O   1 
ATOM   225   C  CB  . TRP A  1 38  ? 43.268  46.504  55.179 1.00 25.86  ? 32  TRP A CB  1 
ATOM   226   C  CG  . TRP A  1 38  ? 44.691  46.103  55.318 1.00 36.85  ? 32  TRP A CG  1 
ATOM   227   C  CD1 . TRP A  1 38  ? 45.312  45.642  56.453 1.00 33.77  ? 32  TRP A CD1 1 
ATOM   228   C  CD2 . TRP A  1 38  ? 45.684  46.114  54.291 1.00 34.30  ? 32  TRP A CD2 1 
ATOM   229   N  NE1 . TRP A  1 38  ? 46.630  45.360  56.186 1.00 34.87  ? 32  TRP A NE1 1 
ATOM   230   C  CE2 . TRP A  1 38  ? 46.885  45.640  54.866 1.00 34.76  ? 32  TRP A CE2 1 
ATOM   231   C  CE3 . TRP A  1 38  ? 45.678  46.482  52.940 1.00 41.48  ? 32  TRP A CE3 1 
ATOM   232   C  CZ2 . TRP A  1 38  ? 48.071  45.520  54.131 1.00 32.34  ? 32  TRP A CZ2 1 
ATOM   233   C  CZ3 . TRP A  1 38  ? 46.865  46.365  52.207 1.00 45.55  ? 32  TRP A CZ3 1 
ATOM   234   C  CH2 . TRP A  1 38  ? 48.041  45.887  52.808 1.00 42.30  ? 32  TRP A CH2 1 
ATOM   235   N  N   . GLY A  1 39  ? 43.236  48.131  57.752 1.00 28.12  ? 33  GLY A N   1 
ATOM   236   C  CA  . GLY A  1 39  ? 43.839  48.483  59.031 1.00 24.13  ? 33  GLY A CA  1 
ATOM   237   C  C   . GLY A  1 39  ? 42.761  48.669  60.088 1.00 28.01  ? 33  GLY A C   1 
ATOM   238   O  O   . GLY A  1 39  ? 41.662  48.141  59.954 1.00 30.58  ? 33  GLY A O   1 
ATOM   239   N  N   . SER A  1 40  ? 43.050  49.412  61.147 1.00 25.53  ? 34  SER A N   1 
ATOM   240   C  CA  . SER A  1 40  ? 42.031  49.628  62.160 1.00 33.67  ? 34  SER A CA  1 
ATOM   241   C  C   . SER A  1 40  ? 42.130  50.995  62.797 1.00 32.96  ? 34  SER A C   1 
ATOM   242   O  O   . SER A  1 40  ? 43.183  51.624  62.783 1.00 41.89  ? 34  SER A O   1 
ATOM   243   C  CB  . SER A  1 40  ? 42.110  48.547  63.235 1.00 40.69  ? 34  SER A CB  1 
ATOM   244   O  OG  . SER A  1 40  ? 43.439  48.373  63.676 1.00 30.78  ? 34  SER A OG  1 
ATOM   245   N  N   . ILE A  1 41  ? 41.021  51.461  63.345 1.00 28.66  ? 35  ILE A N   1 
ATOM   246   C  CA  . ILE A  1 41  ? 40.993  52.761  63.991 1.00 32.67  ? 35  ILE A CA  1 
ATOM   247   C  C   . ILE A  1 41  ? 40.283  52.591  65.322 1.00 34.68  ? 35  ILE A C   1 
ATOM   248   O  O   . ILE A  1 41  ? 39.197  52.018  65.368 1.00 43.40  ? 35  ILE A O   1 
ATOM   249   C  CB  . ILE A  1 41  ? 40.200  53.770  63.161 1.00 27.48  ? 35  ILE A CB  1 
ATOM   250   C  CG1 . ILE A  1 41  ? 40.628  53.687  61.692 1.00 27.11  ? 35  ILE A CG1 1 
ATOM   251   C  CG2 . ILE A  1 41  ? 40.392  55.155  63.742 1.00 24.21  ? 35  ILE A CG2 1 
ATOM   252   C  CD1 . ILE A  1 41  ? 39.870  54.629  60.772 1.00 23.83  ? 35  ILE A CD1 1 
ATOM   253   N  N   . LYS A  1 42  ? 40.885  53.063  66.407 1.00 31.65  ? 36  LYS A N   1 
ATOM   254   C  CA  . LYS A  1 42  ? 40.238  52.928  67.702 1.00 28.76  ? 36  LYS A CA  1 
ATOM   255   C  C   . LYS A  1 42  ? 39.804  54.274  68.260 1.00 29.13  ? 36  LYS A C   1 
ATOM   256   O  O   . LYS A  1 42  ? 40.220  55.331  67.775 1.00 29.15  ? 36  LYS A O   1 
ATOM   257   C  CB  . LYS A  1 42  ? 41.141  52.186  68.692 1.00 30.33  ? 36  LYS A CB  1 
ATOM   258   C  CG  . LYS A  1 42  ? 42.361  52.921  69.188 1.00 38.29  ? 36  LYS A CG  1 
ATOM   259   C  CD  . LYS A  1 42  ? 43.001  52.129  70.349 1.00 46.45  ? 36  LYS A CD  1 
ATOM   260   C  CE  . LYS A  1 42  ? 44.284  52.773  70.873 1.00 44.39  ? 36  LYS A CE  1 
ATOM   261   N  NZ  . LYS A  1 42  ? 44.059  54.217  71.129 1.00 40.73  ? 36  LYS A NZ  1 
ATOM   262   N  N   . GLY A  1 43  ? 38.932  54.235  69.257 1.00 28.28  ? 37  GLY A N   1 
ATOM   263   C  CA  . GLY A  1 43  ? 38.443  55.465  69.849 1.00 24.44  ? 37  GLY A CA  1 
ATOM   264   C  C   . GLY A  1 43  ? 37.202  55.995  69.163 1.00 23.65  ? 37  GLY A C   1 
ATOM   265   O  O   . GLY A  1 43  ? 36.775  57.139  69.404 1.00 28.51  ? 37  GLY A O   1 
ATOM   266   N  N   . LEU A  1 44  ? 36.611  55.177  68.301 1.00 24.49  ? 38  LEU A N   1 
ATOM   267   C  CA  . LEU A  1 44  ? 35.402  55.599  67.589 1.00 31.54  ? 38  LEU A CA  1 
ATOM   268   C  C   . LEU A  1 44  ? 34.141  55.103  68.282 1.00 30.86  ? 38  LEU A C   1 
ATOM   269   O  O   . LEU A  1 44  ? 34.070  53.950  68.719 1.00 30.40  ? 38  LEU A O   1 
ATOM   270   C  CB  . LEU A  1 44  ? 35.416  55.079  66.146 1.00 30.50  ? 38  LEU A CB  1 
ATOM   271   C  CG  . LEU A  1 44  ? 36.491  55.613  65.198 1.00 30.80  ? 38  LEU A CG  1 
ATOM   272   C  CD1 . LEU A  1 44  ? 36.662  54.671  64.017 1.00 30.80  ? 38  LEU A CD1 1 
ATOM   273   C  CD2 . LEU A  1 44  ? 36.096  57.001  64.737 1.00 27.92  ? 38  LEU A CD2 1 
ATOM   274   N  N   . THR A  1 45  ? 33.147  55.975  68.392 1.00 32.05  ? 39  THR A N   1 
ATOM   275   C  CA  . THR A  1 45  ? 31.902  55.576  69.013 1.00 42.78  ? 39  THR A CA  1 
ATOM   276   C  C   . THR A  1 45  ? 31.317  54.510  68.097 1.00 45.94  ? 39  THR A C   1 
ATOM   277   O  O   . THR A  1 45  ? 31.438  54.605  66.875 1.00 44.84  ? 39  THR A O   1 
ATOM   278   C  CB  . THR A  1 45  ? 30.926  56.750  69.124 1.00 44.22  ? 39  THR A CB  1 
ATOM   279   O  OG1 . THR A  1 45  ? 30.727  57.331  67.829 1.00 50.78  ? 39  THR A OG1 1 
ATOM   280   C  CG2 . THR A  1 45  ? 31.473  57.793  70.081 1.00 39.46  ? 39  THR A CG2 1 
ATOM   281   N  N   . GLU A  1 46  ? 30.706  53.490  68.690 1.00 49.60  ? 40  GLU A N   1 
ATOM   282   C  CA  . GLU A  1 46  ? 30.121  52.396  67.924 1.00 48.17  ? 40  GLU A CA  1 
ATOM   283   C  C   . GLU A  1 46  ? 29.244  52.957  66.817 1.00 41.99  ? 40  GLU A C   1 
ATOM   284   O  O   . GLU A  1 46  ? 28.447  53.858  67.052 1.00 37.24  ? 40  GLU A O   1 
ATOM   285   C  CB  . GLU A  1 46  ? 29.306  51.501  68.852 1.00 52.99  ? 40  GLU A CB  1 
ATOM   286   C  CG  . GLU A  1 46  ? 28.806  50.225  68.219 1.00 54.36  ? 40  GLU A CG  1 
ATOM   287   C  CD  . GLU A  1 46  ? 28.134  49.317  69.225 1.00 55.03  ? 40  GLU A CD  1 
ATOM   288   O  OE1 . GLU A  1 46  ? 27.630  48.256  68.811 1.00 53.03  ? 40  GLU A OE1 1 
ATOM   289   O  OE2 . GLU A  1 46  ? 28.114  49.662  70.428 1.00 57.21  ? 40  GLU A OE2 1 
ATOM   290   N  N   . GLY A  1 47  ? 29.409  52.448  65.603 1.00 38.09  ? 41  GLY A N   1 
ATOM   291   C  CA  . GLY A  1 47  ? 28.601  52.955  64.508 1.00 37.58  ? 41  GLY A CA  1 
ATOM   292   C  C   . GLY A  1 47  ? 29.357  53.196  63.213 1.00 41.39  ? 41  GLY A C   1 
ATOM   293   O  O   . GLY A  1 47  ? 30.497  52.744  63.044 1.00 38.32  ? 41  GLY A O   1 
ATOM   294   N  N   . LEU A  1 48  ? 28.700  53.907  62.299 1.00 35.03  ? 42  LEU A N   1 
ATOM   295   C  CA  . LEU A  1 48  ? 29.261  54.233  60.999 1.00 35.46  ? 42  LEU A CA  1 
ATOM   296   C  C   . LEU A  1 48  ? 30.021  55.570  61.025 1.00 38.35  ? 42  LEU A C   1 
ATOM   297   O  O   . LEU A  1 48  ? 29.592  56.542  61.659 1.00 30.19  ? 42  LEU A O   1 
ATOM   298   C  CB  . LEU A  1 48  ? 28.146  54.297  59.935 1.00 33.64  ? 42  LEU A CB  1 
ATOM   299   C  CG  . LEU A  1 48  ? 27.337  53.038  59.566 1.00 31.49  ? 42  LEU A CG  1 
ATOM   300   C  CD1 . LEU A  1 48  ? 26.471  53.314  58.334 1.00 25.35  ? 42  LEU A CD1 1 
ATOM   301   C  CD2 . LEU A  1 48  ? 28.271  51.886  59.276 1.00 34.91  ? 42  LEU A CD2 1 
ATOM   302   N  N   . HIS A  1 49  ? 31.150  55.615  60.321 1.00 35.08  ? 43  HIS A N   1 
ATOM   303   C  CA  . HIS A  1 49  ? 31.946  56.833  60.267 1.00 36.28  ? 43  HIS A CA  1 
ATOM   304   C  C   . HIS A  1 49  ? 32.420  57.175  58.856 1.00 33.28  ? 43  HIS A C   1 
ATOM   305   O  O   . HIS A  1 49  ? 32.941  56.314  58.133 1.00 30.30  ? 43  HIS A O   1 
ATOM   306   C  CB  . HIS A  1 49  ? 33.142  56.713  61.219 1.00 36.87  ? 43  HIS A CB  1 
ATOM   307   C  CG  . HIS A  1 49  ? 32.762  56.724  62.672 1.00 42.63  ? 43  HIS A CG  1 
ATOM   308   N  ND1 . HIS A  1 49  ? 32.266  57.844  63.307 1.00 42.25  ? 43  HIS A ND1 1 
ATOM   309   C  CD2 . HIS A  1 49  ? 32.826  55.756  63.618 1.00 38.29  ? 43  HIS A CD2 1 
ATOM   310   C  CE1 . HIS A  1 49  ? 32.047  57.568  64.581 1.00 37.58  ? 43  HIS A CE1 1 
ATOM   311   N  NE2 . HIS A  1 49  ? 32.378  56.308  64.796 1.00 35.25  ? 43  HIS A NE2 1 
ATOM   312   N  N   . GLY A  1 50  ? 32.204  58.432  58.463 1.00 29.53  ? 44  GLY A N   1 
ATOM   313   C  CA  . GLY A  1 50  ? 32.645  58.898  57.156 1.00 27.67  ? 44  GLY A CA  1 
ATOM   314   C  C   . GLY A  1 50  ? 34.143  58.665  57.008 1.00 32.03  ? 44  GLY A C   1 
ATOM   315   O  O   . GLY A  1 50  ? 34.935  58.949  57.918 1.00 29.13  ? 44  GLY A O   1 
ATOM   316   N  N   . PHE A  1 51  ? 34.540  58.156  55.855 1.00 24.65  ? 45  PHE A N   1 
ATOM   317   C  CA  . PHE A  1 51  ? 35.933  57.833  55.613 1.00 30.13  ? 45  PHE A CA  1 
ATOM   318   C  C   . PHE A  1 51  ? 36.311  58.399  54.237 1.00 33.81  ? 45  PHE A C   1 
ATOM   319   O  O   . PHE A  1 51  ? 35.890  57.870  53.202 1.00 32.22  ? 45  PHE A O   1 
ATOM   320   C  CB  . PHE A  1 51  ? 36.060  56.306  55.647 1.00 25.04  ? 45  PHE A CB  1 
ATOM   321   C  CG  . PHE A  1 51  ? 37.465  55.791  55.710 1.00 23.04  ? 45  PHE A CG  1 
ATOM   322   C  CD1 . PHE A  1 51  ? 38.295  56.102  56.783 1.00 22.97  ? 45  PHE A CD1 1 
ATOM   323   C  CD2 . PHE A  1 51  ? 37.933  54.917  54.741 1.00 17.77  ? 45  PHE A CD2 1 
ATOM   324   C  CE1 . PHE A  1 51  ? 39.586  55.533  56.892 1.00 27.06  ? 45  PHE A CE1 1 
ATOM   325   C  CE2 . PHE A  1 51  ? 39.209  54.341  54.840 1.00 24.51  ? 45  PHE A CE2 1 
ATOM   326   C  CZ  . PHE A  1 51  ? 40.040  54.648  55.917 1.00 16.59  ? 45  PHE A CZ  1 
ATOM   327   N  N   . HIS A  1 52  ? 37.091  59.477  54.209 1.00 29.65  ? 46  HIS A N   1 
ATOM   328   C  CA  . HIS A  1 52  ? 37.448  60.050  52.918 1.00 31.42  ? 46  HIS A CA  1 
ATOM   329   C  C   . HIS A  1 52  ? 38.881  60.543  52.750 1.00 34.28  ? 46  HIS A C   1 
ATOM   330   O  O   . HIS A  1 52  ? 39.627  60.767  53.718 1.00 27.75  ? 46  HIS A O   1 
ATOM   331   C  CB  . HIS A  1 52  ? 36.519  61.223  52.577 1.00 30.86  ? 46  HIS A CB  1 
ATOM   332   C  CG  . HIS A  1 52  ? 35.123  61.084  53.108 1.00 41.78  ? 46  HIS A CG  1 
ATOM   333   N  ND1 . HIS A  1 52  ? 34.654  61.829  54.169 1.00 36.56  ? 46  HIS A ND1 1 
ATOM   334   C  CD2 . HIS A  1 52  ? 34.088  60.307  52.709 1.00 43.12  ? 46  HIS A CD2 1 
ATOM   335   C  CE1 . HIS A  1 52  ? 33.391  61.520  54.396 1.00 36.73  ? 46  HIS A CE1 1 
ATOM   336   N  NE2 . HIS A  1 52  ? 33.023  60.600  53.526 1.00 38.19  ? 46  HIS A NE2 1 
ATOM   337   N  N   . VAL A  1 53  ? 39.266  60.689  51.488 1.00 26.69  ? 47  VAL A N   1 
ATOM   338   C  CA  . VAL A  1 53  ? 40.558  61.237  51.180 1.00 26.07  ? 47  VAL A CA  1 
ATOM   339   C  C   . VAL A  1 53  ? 40.238  62.688  50.836 1.00 26.63  ? 47  VAL A C   1 
ATOM   340   O  O   . VAL A  1 53  ? 39.474  62.951  49.902 1.00 27.24  ? 47  VAL A O   1 
ATOM   341   C  CB  . VAL A  1 53  ? 41.192  60.552  49.980 1.00 28.13  ? 47  VAL A CB  1 
ATOM   342   C  CG1 . VAL A  1 53  ? 42.470  61.275  49.615 1.00 21.92  ? 47  VAL A CG1 1 
ATOM   343   C  CG2 . VAL A  1 53  ? 41.477  59.091  50.307 1.00 25.96  ? 47  VAL A CG2 1 
ATOM   344   N  N   . HIS A  1 54  ? 40.762  63.628  51.621 1.00 27.04  ? 48  HIS A N   1 
ATOM   345   C  CA  . HIS A  1 54  ? 40.516  65.044  51.352 1.00 25.53  ? 48  HIS A CA  1 
ATOM   346   C  C   . HIS A  1 54  ? 41.659  65.559  50.488 1.00 24.84  ? 48  HIS A C   1 
ATOM   347   O  O   . HIS A  1 54  ? 42.746  64.982  50.479 1.00 26.59  ? 48  HIS A O   1 
ATOM   348   C  CB  . HIS A  1 54  ? 40.380  65.840  52.656 1.00 28.23  ? 48  HIS A CB  1 
ATOM   349   C  CG  . HIS A  1 54  ? 39.103  65.572  53.393 1.00 30.45  ? 48  HIS A CG  1 
ATOM   350   N  ND1 . HIS A  1 54  ? 38.235  66.577  53.767 1.00 31.99  ? 48  HIS A ND1 1 
ATOM   351   C  CD2 . HIS A  1 54  ? 38.551  64.412  53.835 1.00 32.38  ? 48  HIS A CD2 1 
ATOM   352   C  CE1 . HIS A  1 54  ? 37.205  66.049  54.409 1.00 42.41  ? 48  HIS A CE1 1 
ATOM   353   N  NE2 . HIS A  1 54  ? 37.371  64.737  54.464 1.00 41.64  ? 48  HIS A NE2 1 
ATOM   354   N  N   . GLU A  1 55  ? 41.409  66.646  49.769 1.00 28.64  ? 49  GLU A N   1 
ATOM   355   C  CA  . GLU A  1 55  ? 42.374  67.188  48.826 1.00 30.00  ? 49  GLU A CA  1 
ATOM   356   C  C   . GLU A  1 55  ? 43.809  67.469  49.225 1.00 31.95  ? 49  GLU A C   1 
ATOM   357   O  O   . GLU A  1 55  ? 44.730  66.979  48.571 1.00 27.90  ? 49  GLU A O   1 
ATOM   358   C  CB  . GLU A  1 55  ? 41.828  68.446  48.164 1.00 30.17  ? 49  GLU A CB  1 
ATOM   359   C  CG  . GLU A  1 55  ? 42.655  68.833  46.955 1.00 32.25  ? 49  GLU A CG  1 
ATOM   360   C  CD  . GLU A  1 55  ? 42.025  69.925  46.111 1.00 36.18  ? 49  GLU A CD  1 
ATOM   361   O  OE1 . GLU A  1 55  ? 42.589  70.223  45.035 1.00 39.83  ? 49  GLU A OE1 1 
ATOM   362   O  OE2 . GLU A  1 55  ? 40.984  70.494  46.513 1.00 35.07  ? 49  GLU A OE2 1 
ATOM   363   N  N   . PHE A  1 56  ? 44.003  68.232  50.294 1.00 25.24  ? 50  PHE A N   1 
ATOM   364   C  CA  . PHE A  1 56  ? 45.341  68.614  50.694 1.00 21.04  ? 50  PHE A CA  1 
ATOM   365   C  C   . PHE A  1 56  ? 45.985  67.847  51.833 1.00 26.17  ? 50  PHE A C   1 
ATOM   366   O  O   . PHE A  1 56  ? 45.355  67.577  52.863 1.00 28.63  ? 50  PHE A O   1 
ATOM   367   C  CB  . PHE A  1 56  ? 45.333  70.106  51.012 1.00 24.57  ? 50  PHE A CB  1 
ATOM   368   C  CG  . PHE A  1 56  ? 44.748  70.944  49.913 1.00 26.30  ? 50  PHE A CG  1 
ATOM   369   C  CD1 . PHE A  1 56  ? 45.365  70.999  48.661 1.00 25.62  ? 50  PHE A CD1 1 
ATOM   370   C  CD2 . PHE A  1 56  ? 43.552  71.639  50.109 1.00 24.51  ? 50  PHE A CD2 1 
ATOM   371   C  CE1 . PHE A  1 56  ? 44.794  71.734  47.609 1.00 32.64  ? 50  PHE A CE1 1 
ATOM   372   C  CE2 . PHE A  1 56  ? 42.967  72.382  49.070 1.00 22.06  ? 50  PHE A CE2 1 
ATOM   373   C  CZ  . PHE A  1 56  ? 43.588  72.429  47.809 1.00 19.05  ? 50  PHE A CZ  1 
ATOM   374   N  N   . GLY A  1 57  ? 47.252  67.491  51.638 1.00 20.28  ? 51  GLY A N   1 
ATOM   375   C  CA  . GLY A  1 57  ? 47.985  66.794  52.680 1.00 20.18  ? 51  GLY A CA  1 
ATOM   376   C  C   . GLY A  1 57  ? 48.591  67.837  53.606 1.00 22.00  ? 51  GLY A C   1 
ATOM   377   O  O   . GLY A  1 57  ? 49.762  67.768  53.968 1.00 23.33  ? 51  GLY A O   1 
ATOM   378   N  N   . ASP A  1 58  ? 47.779  68.818  53.977 1.00 14.92  ? 52  ASP A N   1 
ATOM   379   C  CA  . ASP A  1 58  ? 48.210  69.911  54.835 1.00 19.19  ? 52  ASP A CA  1 
ATOM   380   C  C   . ASP A  1 58  ? 47.602  69.777  56.229 1.00 23.20  ? 52  ASP A C   1 
ATOM   381   O  O   . ASP A  1 58  ? 46.406  70.000  56.405 1.00 16.21  ? 52  ASP A O   1 
ATOM   382   C  CB  . ASP A  1 58  ? 47.787  71.238  54.178 1.00 17.91  ? 52  ASP A CB  1 
ATOM   383   C  CG  . ASP A  1 58  ? 48.115  72.455  55.019 1.00 27.50  ? 52  ASP A CG  1 
ATOM   384   O  OD1 . ASP A  1 58  ? 48.020  73.574  54.476 1.00 33.80  ? 52  ASP A OD1 1 
ATOM   385   O  OD2 . ASP A  1 58  ? 48.453  72.312  56.215 1.00 25.84  ? 52  ASP A OD2 1 
ATOM   386   N  N   . ASN A  1 59  ? 48.416  69.404  57.214 1.00 18.64  ? 53  ASN A N   1 
ATOM   387   C  CA  . ASN A  1 59  ? 47.905  69.270  58.567 1.00 24.74  ? 53  ASN A CA  1 
ATOM   388   C  C   . ASN A  1 59  ? 48.377  70.373  59.498 1.00 26.67  ? 53  ASN A C   1 
ATOM   389   O  O   . ASN A  1 59  ? 48.439  70.181  60.714 1.00 27.76  ? 53  ASN A O   1 
ATOM   390   C  CB  . ASN A  1 59  ? 48.263  67.901  59.156 1.00 33.97  ? 53  ASN A CB  1 
ATOM   391   C  CG  . ASN A  1 59  ? 47.416  66.757  58.562 1.00 52.80  ? 53  ASN A CG  1 
ATOM   392   O  OD1 . ASN A  1 59  ? 47.561  65.606  58.978 1.00 56.65  ? 53  ASN A OD1 1 
ATOM   393   N  ND2 . ASN A  1 59  ? 46.534  67.071  57.587 1.00 41.02  ? 53  ASN A ND2 1 
ATOM   394   N  N   . THR A  1 60  ? 48.682  71.535  58.928 1.00 22.12  ? 54  THR A N   1 
ATOM   395   C  CA  . THR A  1 60  ? 49.153  72.672  59.713 1.00 26.00  ? 54  THR A CA  1 
ATOM   396   C  C   . THR A  1 60  ? 48.088  73.161  60.669 1.00 28.80  ? 54  THR A C   1 
ATOM   397   O  O   . THR A  1 60  ? 48.406  73.796  61.676 1.00 30.26  ? 54  THR A O   1 
ATOM   398   C  CB  . THR A  1 60  ? 49.562  73.854  58.831 1.00 24.53  ? 54  THR A CB  1 
ATOM   399   O  OG1 . THR A  1 60  ? 48.448  74.246  58.027 1.00 19.01  ? 54  THR A OG1 1 
ATOM   400   C  CG2 . THR A  1 60  ? 50.730  73.465  57.925 1.00 21.00  ? 54  THR A CG2 1 
ATOM   401   N  N   . ALA A  1 61  ? 46.826  72.877  60.357 1.00 27.44  ? 55  ALA A N   1 
ATOM   402   C  CA  . ALA A  1 61  ? 45.723  73.290  61.233 1.00 33.82  ? 55  ALA A CA  1 
ATOM   403   C  C   . ALA A  1 61  ? 44.960  72.039  61.619 1.00 31.21  ? 55  ALA A C   1 
ATOM   404   O  O   . ALA A  1 61  ? 43.734  72.047  61.710 1.00 30.97  ? 55  ALA A O   1 
ATOM   405   C  CB  . ALA A  1 61  ? 44.801  74.262  60.510 1.00 29.60  ? 55  ALA A CB  1 
ATOM   406   N  N   . GLY A  1 62  ? 45.700  70.961  61.858 1.00 28.07  ? 56  GLY A N   1 
ATOM   407   C  CA  . GLY A  1 62  ? 45.053  69.712  62.184 1.00 26.99  ? 56  GLY A CA  1 
ATOM   408   C  C   . GLY A  1 62  ? 44.364  69.216  60.922 1.00 34.38  ? 56  GLY A C   1 
ATOM   409   O  O   . GLY A  1 62  ? 44.856  69.440  59.813 1.00 30.96  ? 56  GLY A O   1 
ATOM   410   N  N   . CYS A  1 63  ? 43.215  68.567  61.075 1.00 31.24  ? 57  CYS A N   1 
ATOM   411   C  CA  . CYS A  1 63  ? 42.494  68.026  59.928 1.00 28.90  ? 57  CYS A CA  1 
ATOM   412   C  C   . CYS A  1 63  ? 41.768  69.097  59.157 1.00 26.54  ? 57  CYS A C   1 
ATOM   413   O  O   . CYS A  1 63  ? 41.419  68.903  58.002 1.00 28.37  ? 57  CYS A O   1 
ATOM   414   C  CB  . CYS A  1 63  ? 41.500  66.965  60.397 1.00 27.75  ? 57  CYS A CB  1 
ATOM   415   S  SG  . CYS A  1 63  ? 42.328  65.654  61.340 1.00 33.72  ? 57  CYS A SG  1 
ATOM   416   N  N   . THR A  1 64  ? 41.563  70.232  59.815 1.00 28.80  ? 58  THR A N   1 
ATOM   417   C  CA  . THR A  1 64  ? 40.861  71.378  59.247 1.00 28.18  ? 58  THR A CA  1 
ATOM   418   C  C   . THR A  1 64  ? 41.488  71.895  57.963 1.00 33.77  ? 58  THR A C   1 
ATOM   419   O  O   . THR A  1 64  ? 40.772  72.302  57.052 1.00 37.04  ? 58  THR A O   1 
ATOM   420   C  CB  . THR A  1 64  ? 40.831  72.560  60.241 1.00 27.39  ? 58  THR A CB  1 
ATOM   421   O  OG1 . THR A  1 64  ? 40.460  72.094  61.544 1.00 25.64  ? 58  THR A OG1 1 
ATOM   422   C  CG2 . THR A  1 64  ? 39.843  73.603  59.778 1.00 25.01  ? 58  THR A CG2 1 
ATOM   423   N  N   . SER A  1 65  ? 42.820  71.897  57.896 1.00 29.27  ? 59  SER A N   1 
ATOM   424   C  CA  . SER A  1 65  ? 43.510  72.398  56.710 1.00 34.15  ? 59  SER A CA  1 
ATOM   425   C  C   . SER A  1 65  ? 43.530  71.433  55.518 1.00 31.81  ? 59  SER A C   1 
ATOM   426   O  O   . SER A  1 65  ? 44.079  71.753  54.468 1.00 33.10  ? 59  SER A O   1 
ATOM   427   C  CB  . SER A  1 65  ? 44.944  72.798  57.077 1.00 31.79  ? 59  SER A CB  1 
ATOM   428   O  OG  . SER A  1 65  ? 45.558  71.830  57.918 1.00 32.03  ? 59  SER A OG  1 
ATOM   429   N  N   . ALA A  1 66  ? 42.924  70.263  55.682 1.00 26.93  ? 60  ALA A N   1 
ATOM   430   C  CA  . ALA A  1 66  ? 42.905  69.250  54.623 1.00 26.87  ? 60  ALA A CA  1 
ATOM   431   C  C   . ALA A  1 66  ? 42.064  69.611  53.409 1.00 28.35  ? 60  ALA A C   1 
ATOM   432   O  O   . ALA A  1 66  ? 42.246  69.032  52.336 1.00 29.17  ? 60  ALA A O   1 
ATOM   433   C  CB  . ALA A  1 66  ? 42.423  67.923  55.190 1.00 23.23  ? 60  ALA A CB  1 
ATOM   434   N  N   . GLY A  1 67  ? 41.141  70.559  53.574 1.00 32.55  ? 61  GLY A N   1 
ATOM   435   C  CA  . GLY A  1 67  ? 40.288  70.951  52.465 1.00 26.47  ? 61  GLY A CA  1 
ATOM   436   C  C   . GLY A  1 67  ? 39.104  70.015  52.266 1.00 26.81  ? 61  GLY A C   1 
ATOM   437   O  O   . GLY A  1 67  ? 38.803  69.161  53.112 1.00 26.13  ? 61  GLY A O   1 
ATOM   438   N  N   . PRO A  1 68  ? 38.408  70.137  51.140 1.00 24.38  ? 62  PRO A N   1 
ATOM   439   C  CA  . PRO A  1 68  ? 37.263  69.242  50.944 1.00 28.39  ? 62  PRO A CA  1 
ATOM   440   C  C   . PRO A  1 68  ? 37.710  67.886  50.450 1.00 31.80  ? 62  PRO A C   1 
ATOM   441   O  O   . PRO A  1 68  ? 38.909  67.603  50.369 1.00 27.84  ? 62  PRO A O   1 
ATOM   442   C  CB  . PRO A  1 68  ? 36.420  69.972  49.910 1.00 23.05  ? 62  PRO A CB  1 
ATOM   443   C  CG  . PRO A  1 68  ? 37.510  70.560  49.000 1.00 41.73  ? 62  PRO A CG  1 
ATOM   444   C  CD  . PRO A  1 68  ? 38.588  71.051  49.997 1.00 31.07  ? 62  PRO A CD  1 
ATOM   445   N  N   . HIS A  1 69  ? 36.728  67.050  50.140 1.00 29.86  ? 63  HIS A N   1 
ATOM   446   C  CA  . HIS A  1 69  ? 36.971  65.719  49.636 1.00 30.64  ? 63  HIS A CA  1 
ATOM   447   C  C   . HIS A  1 69  ? 37.718  65.848  48.312 1.00 26.36  ? 63  HIS A C   1 
ATOM   448   O  O   . HIS A  1 69  ? 37.405  66.717  47.504 1.00 32.14  ? 63  HIS A O   1 
ATOM   449   C  CB  . HIS A  1 69  ? 35.631  64.985  49.420 1.00 26.57  ? 63  HIS A CB  1 
ATOM   450   C  CG  . HIS A  1 69  ? 34.868  64.715  50.683 1.00 36.14  ? 63  HIS A CG  1 
ATOM   451   N  ND1 . HIS A  1 69  ? 33.631  64.107  50.691 1.00 35.42  ? 63  HIS A ND1 1 
ATOM   452   C  CD2 . HIS A  1 69  ? 35.159  64.986  51.980 1.00 41.00  ? 63  HIS A CD2 1 
ATOM   453   C  CE1 . HIS A  1 69  ? 33.191  64.018  51.936 1.00 30.39  ? 63  HIS A CE1 1 
ATOM   454   N  NE2 . HIS A  1 69  ? 34.100  64.544  52.737 1.00 39.72  ? 63  HIS A NE2 1 
ATOM   455   N  N   . PHE A  1 70  ? 38.712  64.993  48.105 1.00 22.59  ? 64  PHE A N   1 
ATOM   456   C  CA  . PHE A  1 70  ? 39.484  65.003  46.872 1.00 26.18  ? 64  PHE A CA  1 
ATOM   457   C  C   . PHE A  1 70  ? 38.488  64.811  45.727 1.00 34.53  ? 64  PHE A C   1 
ATOM   458   O  O   . PHE A  1 70  ? 37.878  63.743  45.594 1.00 32.64  ? 64  PHE A O   1 
ATOM   459   C  CB  . PHE A  1 70  ? 40.486  63.859  46.888 1.00 18.98  ? 64  PHE A CB  1 
ATOM   460   C  CG  . PHE A  1 70  ? 41.375  63.819  45.694 1.00 24.60  ? 64  PHE A CG  1 
ATOM   461   C  CD1 . PHE A  1 70  ? 41.822  62.599  45.186 1.00 31.69  ? 64  PHE A CD1 1 
ATOM   462   C  CD2 . PHE A  1 70  ? 41.795  64.997  45.077 1.00 29.78  ? 64  PHE A CD2 1 
ATOM   463   C  CE1 . PHE A  1 70  ? 42.678  62.551  44.073 1.00 27.16  ? 64  PHE A CE1 1 
ATOM   464   C  CE2 . PHE A  1 70  ? 42.648  64.959  43.967 1.00 25.62  ? 64  PHE A CE2 1 
ATOM   465   C  CZ  . PHE A  1 70  ? 43.087  63.735  43.468 1.00 27.47  ? 64  PHE A CZ  1 
ATOM   466   N  N   . ASN A  1 71  ? 38.334  65.836  44.894 1.00 36.67  ? 65  ASN A N   1 
ATOM   467   C  CA  . ASN A  1 71  ? 37.375  65.776  43.806 1.00 36.55  ? 65  ASN A CA  1 
ATOM   468   C  C   . ASN A  1 71  ? 37.926  66.337  42.499 1.00 38.33  ? 65  ASN A C   1 
ATOM   469   O  O   . ASN A  1 71  ? 37.420  67.332  41.973 1.00 36.88  ? 65  ASN A O   1 
ATOM   470   C  CB  . ASN A  1 71  ? 36.124  66.543  44.242 1.00 33.74  ? 65  ASN A CB  1 
ATOM   471   C  CG  . ASN A  1 71  ? 35.021  66.512  43.207 1.00 35.85  ? 65  ASN A CG  1 
ATOM   472   O  OD1 . ASN A  1 71  ? 34.878  65.546  42.450 1.00 31.89  ? 65  ASN A OD1 1 
ATOM   473   N  ND2 . ASN A  1 71  ? 34.217  67.564  43.187 1.00 27.29  ? 65  ASN A ND2 1 
ATOM   474   N  N   . PRO A  1 72  ? 38.951  65.683  41.934 1.00 36.13  ? 66  PRO A N   1 
ATOM   475   C  CA  . PRO A  1 72  ? 39.551  66.156  40.685 1.00 34.00  ? 66  PRO A CA  1 
ATOM   476   C  C   . PRO A  1 72  ? 38.612  66.217  39.485 1.00 39.76  ? 66  PRO A C   1 
ATOM   477   O  O   . PRO A  1 72  ? 38.843  66.994  38.561 1.00 41.43  ? 66  PRO A O   1 
ATOM   478   C  CB  . PRO A  1 72  ? 40.722  65.190  40.480 1.00 31.63  ? 66  PRO A CB  1 
ATOM   479   C  CG  . PRO A  1 72  ? 40.196  63.916  41.051 1.00 32.43  ? 66  PRO A CG  1 
ATOM   480   C  CD  . PRO A  1 72  ? 39.535  64.393  42.338 1.00 35.80  ? 66  PRO A CD  1 
ATOM   481   N  N   . LEU A  1 73  ? 37.547  65.421  39.485 1.00 39.86  ? 67  LEU A N   1 
ATOM   482   C  CA  . LEU A  1 73  ? 36.629  65.445  38.347 1.00 43.67  ? 67  LEU A CA  1 
ATOM   483   C  C   . LEU A  1 73  ? 35.432  66.377  38.541 1.00 41.78  ? 67  LEU A C   1 
ATOM   484   O  O   . LEU A  1 73  ? 34.541  66.445  37.697 1.00 38.31  ? 67  LEU A O   1 
ATOM   485   C  CB  . LEU A  1 73  ? 36.155  64.024  38.011 1.00 36.46  ? 67  LEU A CB  1 
ATOM   486   C  CG  . LEU A  1 73  ? 37.257  63.082  37.519 1.00 38.19  ? 67  LEU A CG  1 
ATOM   487   C  CD1 . LEU A  1 73  ? 36.649  61.757  37.104 1.00 38.13  ? 67  LEU A CD1 1 
ATOM   488   C  CD2 . LEU A  1 73  ? 37.986  63.701  36.338 1.00 35.11  ? 67  LEU A CD2 1 
ATOM   489   N  N   . SER A  1 74  ? 35.421  67.097  39.656 1.00 45.32  ? 68  SER A N   1 
ATOM   490   C  CA  . SER A  1 74  ? 34.345  68.038  39.956 1.00 49.24  ? 68  SER A CA  1 
ATOM   491   C  C   . SER A  1 74  ? 32.957  67.412  39.963 1.00 48.73  ? 68  SER A C   1 
ATOM   492   O  O   . SER A  1 74  ? 32.025  67.968  39.392 1.00 49.67  ? 68  SER A O   1 
ATOM   493   C  CB  . SER A  1 74  ? 34.360  69.193  38.952 1.00 43.22  ? 68  SER A CB  1 
ATOM   494   O  OG  . SER A  1 74  ? 35.607  69.859  38.968 1.00 50.60  ? 68  SER A OG  1 
ATOM   495   N  N   . ARG A  1 75  ? 32.813  66.260  40.603 1.00 47.71  ? 69  ARG A N   1 
ATOM   496   C  CA  . ARG A  1 75  ? 31.518  65.611  40.664 1.00 46.61  ? 69  ARG A CA  1 
ATOM   497   C  C   . ARG A  1 75  ? 30.886  65.740  42.045 1.00 46.57  ? 69  ARG A C   1 
ATOM   498   O  O   . ARG A  1 75  ? 31.540  66.187  42.982 1.00 49.30  ? 69  ARG A O   1 
ATOM   499   C  CB  . ARG A  1 75  ? 31.651  64.148  40.253 1.00 51.30  ? 69  ARG A CB  1 
ATOM   500   C  CG  . ARG A  1 75  ? 31.240  63.954  38.813 1.00 59.79  ? 69  ARG A CG  1 
ATOM   501   C  CD  . ARG A  1 75  ? 32.377  63.549  37.919 1.00 62.02  ? 69  ARG A CD  1 
ATOM   502   N  NE  . ARG A  1 75  ? 32.470  62.099  37.834 1.00 70.46  ? 69  ARG A NE  1 
ATOM   503   C  CZ  . ARG A  1 75  ? 32.910  61.447  36.765 1.00 70.58  ? 69  ARG A CZ  1 
ATOM   504   N  NH1 . ARG A  1 75  ? 33.296  62.122  35.690 1.00 71.47  ? 69  ARG A NH1 1 
ATOM   505   N  NH2 . ARG A  1 75  ? 32.960  60.124  36.771 1.00 72.07  ? 69  ARG A NH2 1 
ATOM   506   N  N   . LYS A  1 76  ? 29.612  65.375  42.167 1.00 45.18  ? 70  LYS A N   1 
ATOM   507   C  CA  . LYS A  1 76  ? 28.915  65.466  43.447 1.00 45.19  ? 70  LYS A CA  1 
ATOM   508   C  C   . LYS A  1 76  ? 29.359  64.360  44.398 1.00 40.92  ? 70  LYS A C   1 
ATOM   509   O  O   . LYS A  1 76  ? 29.856  63.310  43.972 1.00 36.36  ? 70  LYS A O   1 
ATOM   510   C  CB  . LYS A  1 76  ? 27.401  65.363  43.249 1.00 55.48  ? 70  LYS A CB  1 
ATOM   511   C  CG  . LYS A  1 76  ? 26.731  66.555  42.582 1.00 65.80  ? 70  LYS A CG  1 
ATOM   512   C  CD  . LYS A  1 76  ? 25.323  66.165  42.108 1.00 76.31  ? 70  LYS A CD  1 
ATOM   513   C  CE  . LYS A  1 76  ? 24.543  67.342  41.524 1.00 80.00  ? 70  LYS A CE  1 
ATOM   514   N  NZ  . LYS A  1 76  ? 24.036  68.270  42.578 1.00 83.48  ? 70  LYS A NZ  1 
ATOM   515   N  N   . HIS A  1 77  ? 29.179  64.598  45.691 1.00 37.45  ? 71  HIS A N   1 
ATOM   516   C  CA  . HIS A  1 77  ? 29.551  63.606  46.691 1.00 39.49  ? 71  HIS A CA  1 
ATOM   517   C  C   . HIS A  1 77  ? 28.711  62.342  46.488 1.00 32.17  ? 71  HIS A C   1 
ATOM   518   O  O   . HIS A  1 77  ? 27.560  62.413  46.088 1.00 36.61  ? 71  HIS A O   1 
ATOM   519   C  CB  . HIS A  1 77  ? 29.317  64.158  48.102 1.00 34.60  ? 71  HIS A CB  1 
ATOM   520   C  CG  . HIS A  1 77  ? 29.562  63.155  49.184 1.00 48.48  ? 71  HIS A CG  1 
ATOM   521   N  ND1 . HIS A  1 77  ? 30.828  62.816  49.612 1.00 46.37  ? 71  HIS A ND1 1 
ATOM   522   C  CD2 . HIS A  1 77  ? 28.707  62.362  49.873 1.00 46.69  ? 71  HIS A CD2 1 
ATOM   523   C  CE1 . HIS A  1 77  ? 30.742  61.855  50.515 1.00 39.56  ? 71  HIS A CE1 1 
ATOM   524   N  NE2 . HIS A  1 77  ? 29.466  61.561  50.690 1.00 46.37  ? 71  HIS A NE2 1 
ATOM   525   N  N   . GLY A  1 78  ? 29.287  61.187  46.773 1.00 33.51  ? 72  GLY A N   1 
ATOM   526   C  CA  . GLY A  1 78  ? 28.544  59.957  46.615 1.00 35.18  ? 72  GLY A CA  1 
ATOM   527   C  C   . GLY A  1 78  ? 29.155  58.839  47.433 1.00 41.34  ? 72  GLY A C   1 
ATOM   528   O  O   . GLY A  1 78  ? 30.093  59.059  48.208 1.00 41.84  ? 72  GLY A O   1 
ATOM   529   N  N   . GLY A  1 79  ? 28.607  57.639  47.276 1.00 40.39  ? 73  GLY A N   1 
ATOM   530   C  CA  . GLY A  1 79  ? 29.130  56.490  47.983 1.00 35.75  ? 73  GLY A CA  1 
ATOM   531   C  C   . GLY A  1 79  ? 30.209  55.909  47.100 1.00 36.63  ? 73  GLY A C   1 
ATOM   532   O  O   . GLY A  1 79  ? 30.197  56.132  45.879 1.00 31.67  ? 73  GLY A O   1 
ATOM   533   N  N   . PRO A  1 80  ? 31.156  55.154  47.676 1.00 40.24  ? 74  PRO A N   1 
ATOM   534   C  CA  . PRO A  1 80  ? 32.246  54.556  46.902 1.00 42.52  ? 74  PRO A CA  1 
ATOM   535   C  C   . PRO A  1 80  ? 31.831  53.780  45.666 1.00 44.81  ? 74  PRO A C   1 
ATOM   536   O  O   . PRO A  1 80  ? 32.562  53.740  44.678 1.00 44.75  ? 74  PRO A O   1 
ATOM   537   C  CB  . PRO A  1 80  ? 32.970  53.684  47.930 1.00 39.28  ? 74  PRO A CB  1 
ATOM   538   C  CG  . PRO A  1 80  ? 31.916  53.390  48.959 1.00 41.97  ? 74  PRO A CG  1 
ATOM   539   C  CD  . PRO A  1 80  ? 31.215  54.716  49.080 1.00 44.51  ? 74  PRO A CD  1 
ATOM   540   N  N   . LYS A  1 81  ? 30.658  53.168  45.699 1.00 46.86  ? 75  LYS A N   1 
ATOM   541   C  CA  . LYS A  1 81  ? 30.231  52.402  44.542 1.00 48.50  ? 75  LYS A CA  1 
ATOM   542   C  C   . LYS A  1 81  ? 29.364  53.198  43.568 1.00 46.15  ? 75  LYS A C   1 
ATOM   543   O  O   . LYS A  1 81  ? 28.901  52.662  42.569 1.00 44.82  ? 75  LYS A O   1 
ATOM   544   C  CB  . LYS A  1 81  ? 29.521  51.126  45.001 1.00 48.63  ? 75  LYS A CB  1 
ATOM   545   C  CG  . LYS A  1 81  ? 30.412  50.213  45.855 1.00 54.91  ? 75  LYS A CG  1 
ATOM   546   C  CD  . LYS A  1 81  ? 31.681  49.782  45.112 1.00 51.71  ? 75  LYS A CD  1 
ATOM   547   C  CE  . LYS A  1 81  ? 32.576  48.914  45.999 1.00 61.12  ? 75  LYS A CE  1 
ATOM   548   N  NZ  . LYS A  1 81  ? 33.819  48.424  45.312 1.00 56.99  ? 75  LYS A NZ  1 
ATOM   549   N  N   . ASP A  1 82  ? 29.159  54.481  43.846 1.00 45.55  ? 76  ASP A N   1 
ATOM   550   C  CA  . ASP A  1 82  ? 28.367  55.313  42.952 1.00 48.06  ? 76  ASP A CA  1 
ATOM   551   C  C   . ASP A  1 82  ? 29.219  55.815  41.798 1.00 51.92  ? 76  ASP A C   1 
ATOM   552   O  O   . ASP A  1 82  ? 30.400  56.130  41.967 1.00 51.98  ? 76  ASP A O   1 
ATOM   553   C  CB  . ASP A  1 82  ? 27.794  56.528  43.681 1.00 53.18  ? 76  ASP A CB  1 
ATOM   554   C  CG  . ASP A  1 82  ? 26.829  56.151  44.778 1.00 62.32  ? 76  ASP A CG  1 
ATOM   555   O  OD1 . ASP A  1 82  ? 26.226  57.070  45.377 1.00 58.06  ? 76  ASP A OD1 1 
ATOM   556   O  OD2 . ASP A  1 82  ? 26.679  54.937  45.045 1.00 76.26  ? 76  ASP A OD2 1 
ATOM   557   N  N   . GLU A  1 83  ? 28.614  55.900  40.622 1.00 55.37  ? 77  GLU A N   1 
ATOM   558   C  CA  . GLU A  1 83  ? 29.319  56.397  39.456 1.00 61.24  ? 77  GLU A CA  1 
ATOM   559   C  C   . GLU A  1 83  ? 29.571  57.883  39.721 1.00 56.88  ? 77  GLU A C   1 
ATOM   560   O  O   . GLU A  1 83  ? 30.653  58.401  39.455 1.00 61.90  ? 77  GLU A O   1 
ATOM   561   C  CB  . GLU A  1 83  ? 28.462  56.197  38.202 1.00 75.04  ? 77  GLU A CB  1 
ATOM   562   C  CG  . GLU A  1 83  ? 29.254  56.119  36.907 1.00 88.17  ? 77  GLU A CG  1 
ATOM   563   C  CD  . GLU A  1 83  ? 30.045  57.384  36.639 1.00 99.11  ? 77  GLU A CD  1 
ATOM   564   O  OE1 . GLU A  1 83  ? 29.419  58.466  36.533 1.00 102.73 ? 77  GLU A OE1 1 
ATOM   565   O  OE2 . GLU A  1 83  ? 31.290  57.294  36.537 1.00 100.19 ? 77  GLU A OE2 1 
ATOM   566   N  N   . GLU A  1 84  ? 28.570  58.558  40.273 1.00 54.93  ? 78  GLU A N   1 
ATOM   567   C  CA  . GLU A  1 84  ? 28.689  59.974  40.595 1.00 52.30  ? 78  GLU A CA  1 
ATOM   568   C  C   . GLU A  1 84  ? 29.262  60.146  42.000 1.00 51.01  ? 78  GLU A C   1 
ATOM   569   O  O   . GLU A  1 84  ? 28.511  60.227  42.978 1.00 52.21  ? 78  GLU A O   1 
ATOM   570   C  CB  . GLU A  1 84  ? 27.323  60.657  40.521 1.00 49.34  ? 78  GLU A CB  1 
ATOM   571   C  CG  . GLU A  1 84  ? 27.377  62.156  40.763 1.00 56.77  ? 78  GLU A CG  1 
ATOM   572   C  CD  . GLU A  1 84  ? 28.118  62.901  39.660 1.00 64.49  ? 78  GLU A CD  1 
ATOM   573   O  OE1 . GLU A  1 84  ? 28.406  64.107  39.852 1.00 57.40  ? 78  GLU A OE1 1 
ATOM   574   O  OE2 . GLU A  1 84  ? 28.405  62.285  38.603 1.00 64.25  ? 78  GLU A OE2 1 
ATOM   575   N  N   . ARG A  1 85  ? 30.587  60.209  42.094 1.00 42.38  ? 79  ARG A N   1 
ATOM   576   C  CA  . ARG A  1 85  ? 31.261  60.369  43.384 1.00 41.38  ? 79  ARG A CA  1 
ATOM   577   C  C   . ARG A  1 85  ? 32.540  61.201  43.297 1.00 41.79  ? 79  ARG A C   1 
ATOM   578   O  O   . ARG A  1 85  ? 33.040  61.523  42.208 1.00 37.60  ? 79  ARG A O   1 
ATOM   579   C  CB  . ARG A  1 85  ? 31.656  59.007  43.948 1.00 28.89  ? 79  ARG A CB  1 
ATOM   580   C  CG  . ARG A  1 85  ? 32.638  58.282  43.027 1.00 28.67  ? 79  ARG A CG  1 
ATOM   581   C  CD  . ARG A  1 85  ? 33.222  57.006  43.632 1.00 34.40  ? 79  ARG A CD  1 
ATOM   582   N  NE  . ARG A  1 85  ? 34.418  57.250  44.439 1.00 23.18  ? 79  ARG A NE  1 
ATOM   583   C  CZ  . ARG A  1 85  ? 35.240  56.290  44.851 1.00 28.03  ? 79  ARG A CZ  1 
ATOM   584   N  NH1 . ARG A  1 85  ? 36.308  56.590  45.576 1.00 39.33  ? 79  ARG A NH1 1 
ATOM   585   N  NH2 . ARG A  1 85  ? 35.005  55.025  44.535 1.00 27.10  ? 79  ARG A NH2 1 
ATOM   586   N  N   . HIS A  1 86  ? 33.056  61.535  44.474 1.00 37.03  ? 80  HIS A N   1 
ATOM   587   C  CA  . HIS A  1 86  ? 34.311  62.258  44.611 1.00 39.02  ? 80  HIS A CA  1 
ATOM   588   C  C   . HIS A  1 86  ? 35.345  61.143  44.627 1.00 35.42  ? 80  HIS A C   1 
ATOM   589   O  O   . HIS A  1 86  ? 35.097  60.085  45.204 1.00 37.85  ? 80  HIS A O   1 
ATOM   590   C  CB  . HIS A  1 86  ? 34.331  63.012  45.937 1.00 31.66  ? 80  HIS A CB  1 
ATOM   591   C  CG  . HIS A  1 86  ? 33.404  64.179  45.967 1.00 32.36  ? 80  HIS A CG  1 
ATOM   592   N  ND1 . HIS A  1 86  ? 32.918  64.719  47.138 1.00 27.81  ? 80  HIS A ND1 1 
ATOM   593   C  CD2 . HIS A  1 86  ? 32.933  64.961  44.967 1.00 28.67  ? 80  HIS A CD2 1 
ATOM   594   C  CE1 . HIS A  1 86  ? 32.196  65.788  46.860 1.00 28.48  ? 80  HIS A CE1 1 
ATOM   595   N  NE2 . HIS A  1 86  ? 32.190  65.958  45.549 1.00 35.82  ? 80  HIS A NE2 1 
ATOM   596   N  N   . VAL A  1 87  ? 36.491  61.344  43.988 1.00 34.57  ? 81  VAL A N   1 
ATOM   597   C  CA  . VAL A  1 87  ? 37.486  60.286  43.990 1.00 32.59  ? 81  VAL A CA  1 
ATOM   598   C  C   . VAL A  1 87  ? 37.858  59.884  45.414 1.00 29.42  ? 81  VAL A C   1 
ATOM   599   O  O   . VAL A  1 87  ? 38.091  58.716  45.682 1.00 27.00  ? 81  VAL A O   1 
ATOM   600   C  CB  . VAL A  1 87  ? 38.756  60.695  43.212 1.00 39.71  ? 81  VAL A CB  1 
ATOM   601   C  CG1 . VAL A  1 87  ? 39.870  59.658  43.454 1.00 30.40  ? 81  VAL A CG1 1 
ATOM   602   C  CG2 . VAL A  1 87  ? 38.428  60.796  41.705 1.00 23.93  ? 81  VAL A CG2 1 
ATOM   603   N  N   . GLY A  1 88  ? 37.891  60.849  46.331 1.00 28.03  ? 82  GLY A N   1 
ATOM   604   C  CA  . GLY A  1 88  ? 38.232  60.536  47.708 1.00 28.81  ? 82  GLY A CA  1 
ATOM   605   C  C   . GLY A  1 88  ? 37.085  59.973  48.544 1.00 33.35  ? 82  GLY A C   1 
ATOM   606   O  O   . GLY A  1 88  ? 37.215  59.866  49.764 1.00 31.26  ? 82  GLY A O   1 
ATOM   607   N  N   . ASP A  1 89  ? 35.971  59.605  47.904 1.00 28.98  ? 83  ASP A N   1 
ATOM   608   C  CA  . ASP A  1 89  ? 34.803  59.073  48.622 1.00 26.64  ? 83  ASP A CA  1 
ATOM   609   C  C   . ASP A  1 89  ? 34.893  57.579  48.901 1.00 26.72  ? 83  ASP A C   1 
ATOM   610   O  O   . ASP A  1 89  ? 34.591  56.763  48.033 1.00 22.78  ? 83  ASP A O   1 
ATOM   611   C  CB  . ASP A  1 89  ? 33.506  59.342  47.846 1.00 18.36  ? 83  ASP A CB  1 
ATOM   612   C  CG  . ASP A  1 89  ? 33.129  60.814  47.818 1.00 32.43  ? 83  ASP A CG  1 
ATOM   613   O  OD1 . ASP A  1 89  ? 33.617  61.588  48.688 1.00 26.07  ? 83  ASP A OD1 1 
ATOM   614   O  OD2 . ASP A  1 89  ? 32.323  61.198  46.935 1.00 27.52  ? 83  ASP A OD2 1 
ATOM   615   N  N   . LEU A  1 90  ? 35.285  57.214  50.119 1.00 29.12  ? 84  LEU A N   1 
ATOM   616   C  CA  . LEU A  1 90  ? 35.398  55.798  50.459 1.00 34.56  ? 84  LEU A CA  1 
ATOM   617   C  C   . LEU A  1 90  ? 34.263  55.269  51.346 1.00 33.37  ? 84  LEU A C   1 
ATOM   618   O  O   . LEU A  1 90  ? 34.370  54.192  51.930 1.00 38.29  ? 84  LEU A O   1 
ATOM   619   C  CB  . LEU A  1 90  ? 36.763  55.527  51.105 1.00 32.14  ? 84  LEU A CB  1 
ATOM   620   C  CG  . LEU A  1 90  ? 37.917  55.855  50.151 1.00 33.46  ? 84  LEU A CG  1 
ATOM   621   C  CD1 . LEU A  1 90  ? 39.244  55.505  50.794 1.00 20.58  ? 84  LEU A CD1 1 
ATOM   622   C  CD2 . LEU A  1 90  ? 37.736  55.078  48.846 1.00 29.79  ? 84  LEU A CD2 1 
ATOM   623   N  N   . GLY A  1 91  ? 33.172  56.018  51.439 1.00 30.33  ? 85  GLY A N   1 
ATOM   624   C  CA  . GLY A  1 91  ? 32.051  55.566  52.242 1.00 37.06  ? 85  GLY A CA  1 
ATOM   625   C  C   . GLY A  1 91  ? 32.222  55.609  53.755 1.00 36.36  ? 85  GLY A C   1 
ATOM   626   O  O   . GLY A  1 91  ? 32.738  56.575  54.307 1.00 32.49  ? 85  GLY A O   1 
ATOM   627   N  N   . ASN A  1 92  ? 31.786  54.550  54.430 1.00 31.75  ? 86  ASN A N   1 
ATOM   628   C  CA  . ASN A  1 92  ? 31.856  54.502  55.888 1.00 31.44  ? 86  ASN A CA  1 
ATOM   629   C  C   . ASN A  1 92  ? 32.664  53.310  56.347 1.00 28.73  ? 86  ASN A C   1 
ATOM   630   O  O   . ASN A  1 92  ? 32.879  52.362  55.599 1.00 28.09  ? 86  ASN A O   1 
ATOM   631   C  CB  . ASN A  1 92  ? 30.452  54.357  56.499 1.00 30.48  ? 86  ASN A CB  1 
ATOM   632   C  CG  . ASN A  1 92  ? 29.587  55.600  56.340 1.00 28.99  ? 86  ASN A CG  1 
ATOM   633   O  OD1 . ASN A  1 92  ? 29.857  56.626  56.943 1.00 31.51  ? 86  ASN A OD1 1 
ATOM   634   N  ND2 . ASN A  1 92  ? 28.520  55.499  55.538 1.00 26.22  ? 86  ASN A ND2 1 
ATOM   635   N  N   . VAL A  1 93  ? 33.134  53.390  57.580 1.00 23.49  ? 87  VAL A N   1 
ATOM   636   C  CA  . VAL A  1 93  ? 33.840  52.290  58.208 1.00 29.53  ? 87  VAL A CA  1 
ATOM   637   C  C   . VAL A  1 93  ? 32.945  52.033  59.424 1.00 31.13  ? 87  VAL A C   1 
ATOM   638   O  O   . VAL A  1 93  ? 32.155  52.902  59.828 1.00 20.62  ? 87  VAL A O   1 
ATOM   639   C  CB  . VAL A  1 93  ? 35.287  52.664  58.684 1.00 34.54  ? 87  VAL A CB  1 
ATOM   640   C  CG1 . VAL A  1 93  ? 36.206  52.836  57.489 1.00 33.72  ? 87  VAL A CG1 1 
ATOM   641   C  CG2 . VAL A  1 93  ? 35.260  53.929  59.536 1.00 33.19  ? 87  VAL A CG2 1 
ATOM   642   N  N   . THR A  1 94  ? 33.072  50.862  60.022 1.00 30.92  ? 88  THR A N   1 
ATOM   643   C  CA  . THR A  1 94  ? 32.225  50.541  61.148 1.00 29.52  ? 88  THR A CA  1 
ATOM   644   C  C   . THR A  1 94  ? 32.965  50.245  62.438 1.00 30.07  ? 88  THR A C   1 
ATOM   645   O  O   . THR A  1 94  ? 33.758  49.301  62.522 1.00 26.46  ? 88  THR A O   1 
ATOM   646   C  CB  . THR A  1 94  ? 31.315  49.331  60.800 1.00 36.49  ? 88  THR A CB  1 
ATOM   647   O  OG1 . THR A  1 94  ? 30.415  49.699  59.742 1.00 31.45  ? 88  THR A OG1 1 
ATOM   648   C  CG2 . THR A  1 94  ? 30.506  48.897  62.025 1.00 37.04  ? 88  THR A CG2 1 
ATOM   649   N  N   . ALA A  1 95  ? 32.692  51.050  63.457 1.00 34.32  ? 89  ALA A N   1 
ATOM   650   C  CA  . ALA A  1 95  ? 33.317  50.825  64.757 1.00 41.57  ? 89  ALA A CA  1 
ATOM   651   C  C   . ALA A  1 95  ? 32.409  49.878  65.550 1.00 38.45  ? 89  ALA A C   1 
ATOM   652   O  O   . ALA A  1 95  ? 31.204  50.109  65.669 1.00 35.15  ? 89  ALA A O   1 
ATOM   653   C  CB  . ALA A  1 95  ? 33.489  52.149  65.503 1.00 41.18  ? 89  ALA A CB  1 
ATOM   654   N  N   . ASP A  1 96  ? 32.991  48.811  66.080 1.00 37.34  ? 90  ASP A N   1 
ATOM   655   C  CA  . ASP A  1 96  ? 32.232  47.842  66.858 1.00 44.78  ? 90  ASP A CA  1 
ATOM   656   C  C   . ASP A  1 96  ? 31.978  48.335  68.296 1.00 46.83  ? 90  ASP A C   1 
ATOM   657   O  O   . ASP A  1 96  ? 32.237  49.490  68.624 1.00 46.86  ? 90  ASP A O   1 
ATOM   658   C  CB  . ASP A  1 96  ? 32.963  46.490  66.840 1.00 36.54  ? 90  ASP A CB  1 
ATOM   659   C  CG  . ASP A  1 96  ? 34.346  46.554  67.469 1.00 45.21  ? 90  ASP A CG  1 
ATOM   660   O  OD1 . ASP A  1 96  ? 35.229  45.786  67.025 1.00 47.45  ? 90  ASP A OD1 1 
ATOM   661   O  OD2 . ASP A  1 96  ? 34.553  47.351  68.412 1.00 35.08  ? 90  ASP A OD2 1 
ATOM   662   N  N   . LYS A  1 97  ? 31.466  47.470  69.156 1.00 47.92  ? 91  LYS A N   1 
ATOM   663   C  CA  . LYS A  1 97  ? 31.167  47.883  70.522 1.00 52.17  ? 91  LYS A CA  1 
ATOM   664   C  C   . LYS A  1 97  ? 32.423  48.228  71.322 1.00 48.19  ? 91  LYS A C   1 
ATOM   665   O  O   . LYS A  1 97  ? 32.360  48.945  72.316 1.00 44.70  ? 91  LYS A O   1 
ATOM   666   C  CB  . LYS A  1 97  ? 30.357  46.785  71.232 1.00 56.74  ? 91  LYS A CB  1 
ATOM   667   C  CG  . LYS A  1 97  ? 30.947  45.379  71.097 1.00 71.85  ? 91  LYS A CG  1 
ATOM   668   C  CD  . LYS A  1 97  ? 30.081  44.328  71.787 1.00 78.49  ? 91  LYS A CD  1 
ATOM   669   C  CE  . LYS A  1 97  ? 30.577  42.911  71.514 1.00 83.92  ? 91  LYS A CE  1 
ATOM   670   N  NZ  . LYS A  1 97  ? 31.942  42.677  72.052 1.00 84.09  ? 91  LYS A NZ  1 
ATOM   671   N  N   . ASP A  1 98  ? 33.567  47.725  70.879 1.00 50.18  ? 92  ASP A N   1 
ATOM   672   C  CA  . ASP A  1 98  ? 34.824  47.987  71.563 1.00 48.23  ? 92  ASP A CA  1 
ATOM   673   C  C   . ASP A  1 98  ? 35.492  49.269  71.051 1.00 46.84  ? 92  ASP A C   1 
ATOM   674   O  O   . ASP A  1 98  ? 36.680  49.503  71.284 1.00 47.07  ? 92  ASP A O   1 
ATOM   675   C  CB  . ASP A  1 98  ? 35.752  46.784  71.394 1.00 55.84  ? 92  ASP A CB  1 
ATOM   676   C  CG  . ASP A  1 98  ? 35.261  45.558  72.164 1.00 70.54  ? 92  ASP A CG  1 
ATOM   677   O  OD1 . ASP A  1 98  ? 35.294  44.435  71.609 1.00 79.63  ? 92  ASP A OD1 1 
ATOM   678   O  OD2 . ASP A  1 98  ? 34.844  45.715  73.333 1.00 72.57  ? 92  ASP A OD2 1 
ATOM   679   N  N   . ALA A  1 99  ? 34.707  50.094  70.362 1.00 38.41  ? 93  ALA A N   1 
ATOM   680   C  CA  . ALA A  1 99  ? 35.165  51.364  69.807 1.00 44.45  ? 93  ALA A CA  1 
ATOM   681   C  C   . ALA A  1 99  ? 36.281  51.210  68.765 1.00 43.53  ? 93  ALA A C   1 
ATOM   682   O  O   . ALA A  1 99  ? 37.083  52.122  68.556 1.00 47.65  ? 93  ALA A O   1 
ATOM   683   C  CB  . ALA A  1 99  ? 35.613  52.295  70.936 1.00 42.83  ? 93  ALA A CB  1 
ATOM   684   N  N   . VAL A  1 100 ? 36.306  50.059  68.102 1.00 34.83  ? 94  VAL A N   1 
ATOM   685   C  CA  . VAL A  1 100 ? 37.306  49.758  67.087 1.00 35.73  ? 94  VAL A CA  1 
ATOM   686   C  C   . VAL A  1 100 ? 36.727  49.442  65.699 1.00 36.94  ? 94  VAL A C   1 
ATOM   687   O  O   . VAL A  1 100 ? 35.807  48.638  65.562 1.00 32.29  ? 94  VAL A O   1 
ATOM   688   C  CB  . VAL A  1 100 ? 38.162  48.568  67.513 1.00 33.15  ? 94  VAL A CB  1 
ATOM   689   C  CG1 . VAL A  1 100 ? 39.108  48.189  66.396 1.00 35.39  ? 94  VAL A CG1 1 
ATOM   690   C  CG2 . VAL A  1 100 ? 38.920  48.913  68.770 1.00 29.65  ? 94  VAL A CG2 1 
ATOM   691   N  N   . ALA A  1 101 ? 37.282  50.073  64.670 1.00 34.79  ? 95  ALA A N   1 
ATOM   692   C  CA  . ALA A  1 101 ? 36.832  49.839  63.302 1.00 34.05  ? 95  ALA A CA  1 
ATOM   693   C  C   . ALA A  1 101 ? 37.912  49.100  62.529 1.00 37.79  ? 95  ALA A C   1 
ATOM   694   O  O   . ALA A  1 101 ? 39.028  49.603  62.350 1.00 34.32  ? 95  ALA A O   1 
ATOM   695   C  CB  . ALA A  1 101 ? 36.520  51.145  62.613 1.00 25.08  ? 95  ALA A CB  1 
ATOM   696   N  N   . ASP A  1 102 ? 37.590  47.889  62.095 1.00 41.30  ? 96  ASP A N   1 
ATOM   697   C  CA  . ASP A  1 102 ? 38.531  47.116  61.308 1.00 47.47  ? 96  ASP A CA  1 
ATOM   698   C  C   . ASP A  1 102 ? 38.162  47.401  59.864 1.00 42.68  ? 96  ASP A C   1 
ATOM   699   O  O   . ASP A  1 102 ? 37.082  47.055  59.397 1.00 42.79  ? 96  ASP A O   1 
ATOM   700   C  CB  . ASP A  1 102 ? 38.428  45.645  61.680 1.00 46.45  ? 96  ASP A CB  1 
ATOM   701   C  CG  . ASP A  1 102 ? 38.848  45.407  63.120 1.00 62.19  ? 96  ASP A CG  1 
ATOM   702   O  OD1 . ASP A  1 102 ? 40.042  45.622  63.429 1.00 62.29  ? 96  ASP A OD1 1 
ATOM   703   O  OD2 . ASP A  1 102 ? 37.990  45.037  63.950 1.00 71.12  ? 96  ASP A OD2 1 
ATOM   704   N  N   . VAL A  1 103 ? 39.070  48.089  59.182 1.00 37.71  ? 97  VAL A N   1 
ATOM   705   C  CA  . VAL A  1 103 ? 38.866  48.504  57.810 1.00 35.27  ? 97  VAL A CA  1 
ATOM   706   C  C   . VAL A  1 103 ? 39.396  47.523  56.783 1.00 30.80  ? 97  VAL A C   1 
ATOM   707   O  O   . VAL A  1 103 ? 40.529  47.049  56.871 1.00 27.94  ? 97  VAL A O   1 
ATOM   708   C  CB  . VAL A  1 103 ? 39.519  49.910  57.568 1.00 36.82  ? 97  VAL A CB  1 
ATOM   709   C  CG1 . VAL A  1 103 ? 39.324  50.372  56.120 1.00 27.97  ? 97  VAL A CG1 1 
ATOM   710   C  CG2 . VAL A  1 103 ? 38.911  50.922  58.510 1.00 30.09  ? 97  VAL A CG2 1 
ATOM   711   N  N   . SER A  1 104 ? 38.548  47.209  55.815 1.00 29.19  ? 98  SER A N   1 
ATOM   712   C  CA  . SER A  1 104 ? 38.938  46.331  54.722 1.00 34.79  ? 98  SER A CA  1 
ATOM   713   C  C   . SER A  1 104 ? 38.133  46.806  53.533 1.00 36.43  ? 98  SER A C   1 
ATOM   714   O  O   . SER A  1 104 ? 36.930  46.585  53.455 1.00 41.89  ? 98  SER A O   1 
ATOM   715   C  CB  . SER A  1 104 ? 38.628  44.876  55.030 1.00 30.83  ? 98  SER A CB  1 
ATOM   716   O  OG  . SER A  1 104 ? 39.317  44.034  54.122 1.00 33.29  ? 98  SER A OG  1 
ATOM   717   N  N   . ILE A  1 105 ? 38.807  47.481  52.616 1.00 36.18  ? 99  ILE A N   1 
ATOM   718   C  CA  . ILE A  1 105 ? 38.150  48.032  51.453 1.00 38.69  ? 99  ILE A CA  1 
ATOM   719   C  C   . ILE A  1 105 ? 38.920  47.773  50.175 1.00 37.45  ? 99  ILE A C   1 
ATOM   720   O  O   . ILE A  1 105 ? 40.128  47.581  50.184 1.00 34.31  ? 99  ILE A O   1 
ATOM   721   C  CB  . ILE A  1 105 ? 37.972  49.564  51.634 1.00 39.37  ? 99  ILE A CB  1 
ATOM   722   C  CG1 . ILE A  1 105 ? 36.862  49.823  52.649 1.00 41.14  ? 99  ILE A CG1 1 
ATOM   723   C  CG2 . ILE A  1 105 ? 37.683  50.245  50.303 1.00 31.47  ? 99  ILE A CG2 1 
ATOM   724   C  CD1 . ILE A  1 105 ? 36.796  51.250  53.140 1.00 38.50  ? 99  ILE A CD1 1 
ATOM   725   N  N   . GLU A  1 106 ? 38.193  47.732  49.071 1.00 37.49  ? 100 GLU A N   1 
ATOM   726   C  CA  . GLU A  1 106 ? 38.813  47.567  47.779 1.00 40.19  ? 100 GLU A CA  1 
ATOM   727   C  C   . GLU A  1 106 ? 38.079  48.596  46.939 1.00 37.87  ? 100 GLU A C   1 
ATOM   728   O  O   . GLU A  1 106 ? 36.839  48.613  46.898 1.00 32.36  ? 100 GLU A O   1 
ATOM   729   C  CB  . GLU A  1 106 ? 38.622  46.159  47.233 1.00 39.04  ? 100 GLU A CB  1 
ATOM   730   C  CG  . GLU A  1 106 ? 39.404  45.952  45.944 1.00 60.17  ? 100 GLU A CG  1 
ATOM   731   C  CD  . GLU A  1 106 ? 39.405  44.515  45.448 1.00 63.41  ? 100 GLU A CD  1 
ATOM   732   O  OE1 . GLU A  1 106 ? 40.000  43.649  46.127 1.00 62.60  ? 100 GLU A OE1 1 
ATOM   733   O  OE2 . GLU A  1 106 ? 38.812  44.260  44.375 1.00 67.18  ? 100 GLU A OE2 1 
ATOM   734   N  N   . ASP A  1 107 ? 38.842  49.493  46.324 1.00 30.65  ? 101 ASP A N   1 
ATOM   735   C  CA  . ASP A  1 107 ? 38.257  50.554  45.514 1.00 29.41  ? 101 ASP A CA  1 
ATOM   736   C  C   . ASP A  1 107 ? 39.007  50.597  44.195 1.00 32.18  ? 101 ASP A C   1 
ATOM   737   O  O   . ASP A  1 107 ? 40.184  50.220  44.124 1.00 27.62  ? 101 ASP A O   1 
ATOM   738   C  CB  . ASP A  1 107 ? 38.370  51.886  46.262 1.00 33.73  ? 101 ASP A CB  1 
ATOM   739   C  CG  . ASP A  1 107 ? 37.535  52.995  45.639 1.00 39.33  ? 101 ASP A CG  1 
ATOM   740   O  OD1 . ASP A  1 107 ? 38.071  53.752  44.806 1.00 46.26  ? 101 ASP A OD1 1 
ATOM   741   O  OD2 . ASP A  1 107 ? 36.342  53.118  45.981 1.00 37.38  ? 101 ASP A OD2 1 
ATOM   742   N  N   . SER A  1 108 ? 38.337  51.036  43.138 1.00 29.50  ? 102 SER A N   1 
ATOM   743   C  CA  . SER A  1 108 ? 39.006  51.069  41.848 1.00 33.67  ? 102 SER A CA  1 
ATOM   744   C  C   . SER A  1 108 ? 38.940  52.453  41.213 1.00 36.93  ? 102 SER A C   1 
ATOM   745   O  O   . SER A  1 108 ? 39.168  52.623  40.009 1.00 36.23  ? 102 SER A O   1 
ATOM   746   C  CB  . SER A  1 108 ? 38.411  50.004  40.919 1.00 28.01  ? 102 SER A CB  1 
ATOM   747   O  OG  . SER A  1 108 ? 37.051  50.284  40.662 1.00 37.07  ? 102 SER A OG  1 
ATOM   748   N  N   . VAL A  1 109 ? 38.618  53.444  42.033 1.00 26.36  ? 103 VAL A N   1 
ATOM   749   C  CA  . VAL A  1 109 ? 38.570  54.814  41.568 1.00 34.26  ? 103 VAL A CA  1 
ATOM   750   C  C   . VAL A  1 109 ? 39.872  55.478  42.037 1.00 36.36  ? 103 VAL A C   1 
ATOM   751   O  O   . VAL A  1 109 ? 40.615  56.036  41.232 1.00 39.59  ? 103 VAL A O   1 
ATOM   752   C  CB  . VAL A  1 109 ? 37.342  55.519  42.131 1.00 36.11  ? 103 VAL A CB  1 
ATOM   753   C  CG1 . VAL A  1 109 ? 37.349  56.976  41.752 1.00 29.01  ? 103 VAL A CG1 1 
ATOM   754   C  CG2 . VAL A  1 109 ? 36.099  54.842  41.587 1.00 34.97  ? 103 VAL A CG2 1 
ATOM   755   N  N   . ILE A  1 110 ? 40.154  55.391  43.335 1.00 34.84  ? 104 ILE A N   1 
ATOM   756   C  CA  . ILE A  1 110 ? 41.387  55.938  43.889 1.00 29.70  ? 104 ILE A CA  1 
ATOM   757   C  C   . ILE A  1 110 ? 42.569  55.135  43.325 1.00 28.45  ? 104 ILE A C   1 
ATOM   758   O  O   . ILE A  1 110 ? 42.417  53.983  42.928 1.00 30.61  ? 104 ILE A O   1 
ATOM   759   C  CB  . ILE A  1 110 ? 41.448  55.808  45.439 1.00 26.98  ? 104 ILE A CB  1 
ATOM   760   C  CG1 . ILE A  1 110 ? 41.322  54.338  45.847 1.00 31.24  ? 104 ILE A CG1 1 
ATOM   761   C  CG2 . ILE A  1 110 ? 40.359  56.644  46.096 1.00 23.04  ? 104 ILE A CG2 1 
ATOM   762   C  CD1 . ILE A  1 110 ? 41.743  54.071  47.283 1.00 25.71  ? 104 ILE A CD1 1 
ATOM   763   N  N   . SER A  1 111 ? 43.745  55.747  43.290 1.00 30.16  ? 105 SER A N   1 
ATOM   764   C  CA  . SER A  1 111 ? 44.945  55.070  42.804 1.00 27.25  ? 105 SER A CA  1 
ATOM   765   C  C   . SER A  1 111 ? 46.145  55.563  43.609 1.00 24.73  ? 105 SER A C   1 
ATOM   766   O  O   . SER A  1 111 ? 46.083  56.627  44.240 1.00 27.14  ? 105 SER A O   1 
ATOM   767   C  CB  . SER A  1 111 ? 45.169  55.362  41.310 1.00 21.65  ? 105 SER A CB  1 
ATOM   768   O  OG  . SER A  1 111 ? 46.223  54.563  40.783 1.00 19.36  ? 105 SER A OG  1 
ATOM   769   N  N   . LEU A  1 112 ? 47.222  54.785  43.609 1.00 24.80  ? 106 LEU A N   1 
ATOM   770   C  CA  . LEU A  1 112 ? 48.434  55.190  44.306 1.00 26.78  ? 106 LEU A CA  1 
ATOM   771   C  C   . LEU A  1 112 ? 49.403  55.818  43.297 1.00 25.15  ? 106 LEU A C   1 
ATOM   772   O  O   . LEU A  1 112 ? 50.588  55.979  43.579 1.00 33.20  ? 106 LEU A O   1 
ATOM   773   C  CB  . LEU A  1 112 ? 49.084  53.992  45.001 1.00 19.11  ? 106 LEU A CB  1 
ATOM   774   C  CG  . LEU A  1 112 ? 48.192  53.310  46.035 1.00 23.44  ? 106 LEU A CG  1 
ATOM   775   C  CD1 . LEU A  1 112 ? 49.020  52.279  46.795 1.00 21.91  ? 106 LEU A CD1 1 
ATOM   776   C  CD2 . LEU A  1 112 ? 47.589  54.349  46.990 1.00 17.27  ? 106 LEU A CD2 1 
ATOM   777   N  N   . SER A  1 113 ? 48.881  56.171  42.124 1.00 28.32  ? 107 SER A N   1 
ATOM   778   C  CA  . SER A  1 113 ? 49.655  56.807  41.048 1.00 29.29  ? 107 SER A CA  1 
ATOM   779   C  C   . SER A  1 113 ? 48.710  57.383  39.970 1.00 31.56  ? 107 SER A C   1 
ATOM   780   O  O   . SER A  1 113 ? 47.505  57.100  39.959 1.00 29.48  ? 107 SER A O   1 
ATOM   781   C  CB  . SER A  1 113 ? 50.603  55.793  40.404 1.00 25.85  ? 107 SER A CB  1 
ATOM   782   O  OG  . SER A  1 113 ? 49.875  54.892  39.585 1.00 33.44  ? 107 SER A OG  1 
ATOM   783   N  N   . GLY A  1 114 ? 49.252  58.185  39.059 1.00 28.89  ? 108 GLY A N   1 
ATOM   784   C  CA  . GLY A  1 114 ? 48.415  58.769  38.032 1.00 29.84  ? 108 GLY A CA  1 
ATOM   785   C  C   . GLY A  1 114 ? 47.654  59.963  38.576 1.00 41.62  ? 108 GLY A C   1 
ATOM   786   O  O   . GLY A  1 114 ? 47.993  60.477  39.635 1.00 44.16  ? 108 GLY A O   1 
ATOM   787   N  N   . ASP A  1 115 ? 46.612  60.392  37.871 1.00 48.24  ? 109 ASP A N   1 
ATOM   788   C  CA  . ASP A  1 115 ? 45.835  61.563  38.275 1.00 53.51  ? 109 ASP A CA  1 
ATOM   789   C  C   . ASP A  1 115 ? 44.865  61.366  39.423 1.00 50.44  ? 109 ASP A C   1 
ATOM   790   O  O   . ASP A  1 115 ? 44.348  62.336  39.972 1.00 48.96  ? 109 ASP A O   1 
ATOM   791   C  CB  . ASP A  1 115 ? 45.096  62.139  37.060 1.00 64.96  ? 109 ASP A CB  1 
ATOM   792   C  CG  . ASP A  1 115 ? 45.996  63.023  36.197 1.00 76.53  ? 109 ASP A CG  1 
ATOM   793   O  OD1 . ASP A  1 115 ? 47.169  62.647  35.962 1.00 81.86  ? 109 ASP A OD1 1 
ATOM   794   O  OD2 . ASP A  1 115 ? 45.531  64.093  35.749 1.00 79.41  ? 109 ASP A OD2 1 
ATOM   795   N  N   . HIS A  1 116 ? 44.598  60.118  39.775 1.00 48.05  ? 110 HIS A N   1 
ATOM   796   C  CA  . HIS A  1 116 ? 43.704  59.837  40.892 1.00 50.03  ? 110 HIS A CA  1 
ATOM   797   C  C   . HIS A  1 116 ? 44.563  59.488  42.106 1.00 45.57  ? 110 HIS A C   1 
ATOM   798   O  O   . HIS A  1 116 ? 44.050  58.933  43.092 1.00 35.17  ? 110 HIS A O   1 
ATOM   799   C  CB  . HIS A  1 116 ? 42.776  58.647  40.583 1.00 54.13  ? 110 HIS A CB  1 
ATOM   800   C  CG  . HIS A  1 116 ? 41.602  58.987  39.716 1.00 60.63  ? 110 HIS A CG  1 
ATOM   801   N  ND1 . HIS A  1 116 ? 41.172  60.281  39.511 1.00 57.29  ? 110 HIS A ND1 1 
ATOM   802   C  CD2 . HIS A  1 116 ? 40.744  58.194  39.031 1.00 61.61  ? 110 HIS A CD2 1 
ATOM   803   C  CE1 . HIS A  1 116 ? 40.102  60.270  38.737 1.00 55.76  ? 110 HIS A CE1 1 
ATOM   804   N  NE2 . HIS A  1 116 ? 39.822  59.016  38.433 1.00 55.34  ? 110 HIS A NE2 1 
ATOM   805   N  N   . CYS A  1 117 ? 45.863  59.796  42.009 1.00 38.82  ? 111 CYS A N   1 
ATOM   806   C  CA  . CYS A  1 117 ? 46.847  59.505  43.061 1.00 36.31  ? 111 CYS A CA  1 
ATOM   807   C  C   . CYS A  1 117 ? 46.437  60.191  44.360 1.00 31.09  ? 111 CYS A C   1 
ATOM   808   O  O   . CYS A  1 117 ? 46.184  61.399  44.382 1.00 32.48  ? 111 CYS A O   1 
ATOM   809   C  CB  . CYS A  1 117 ? 48.230  59.995  42.616 1.00 41.35  ? 111 CYS A CB  1 
ATOM   810   S  SG  . CYS A  1 117 ? 49.688  59.510  43.598 1.00 45.77  ? 111 CYS A SG  1 
ATOM   811   N  N   . ILE A  1 118 ? 46.353  59.416  45.436 1.00 20.71  ? 112 ILE A N   1 
ATOM   812   C  CA  . ILE A  1 118 ? 45.964  59.959  46.731 1.00 25.03  ? 112 ILE A CA  1 
ATOM   813   C  C   . ILE A  1 118 ? 47.169  60.089  47.653 1.00 27.16  ? 112 ILE A C   1 
ATOM   814   O  O   . ILE A  1 118 ? 47.041  60.547  48.788 1.00 25.66  ? 112 ILE A O   1 
ATOM   815   C  CB  . ILE A  1 118 ? 44.924  59.073  47.423 1.00 23.70  ? 112 ILE A CB  1 
ATOM   816   C  CG1 . ILE A  1 118 ? 45.506  57.675  47.626 1.00 21.00  ? 112 ILE A CG1 1 
ATOM   817   C  CG2 . ILE A  1 118 ? 43.629  59.051  46.601 1.00 14.15  ? 112 ILE A CG2 1 
ATOM   818   C  CD1 . ILE A  1 118 ? 44.680  56.805  48.557 1.00 27.55  ? 112 ILE A CD1 1 
ATOM   819   N  N   . ILE A  1 119 ? 48.334  59.665  47.172 1.00 22.07  ? 113 ILE A N   1 
ATOM   820   C  CA  . ILE A  1 119 ? 49.539  59.783  47.970 1.00 26.50  ? 113 ILE A CA  1 
ATOM   821   C  C   . ILE A  1 119 ? 49.800  61.265  48.163 1.00 23.92  ? 113 ILE A C   1 
ATOM   822   O  O   . ILE A  1 119 ? 49.670  62.055  47.230 1.00 27.73  ? 113 ILE A O   1 
ATOM   823   C  CB  . ILE A  1 119 ? 50.741  59.130  47.277 1.00 25.09  ? 113 ILE A CB  1 
ATOM   824   C  CG1 . ILE A  1 119 ? 50.624  57.609  47.400 1.00 24.10  ? 113 ILE A CG1 1 
ATOM   825   C  CG2 . ILE A  1 119 ? 52.031  59.613  47.924 1.00 25.57  ? 113 ILE A CG2 1 
ATOM   826   C  CD1 . ILE A  1 119 ? 51.663  56.843  46.658 1.00 20.06  ? 113 ILE A CD1 1 
ATOM   827   N  N   . GLY A  1 120 ? 50.134  61.654  49.383 1.00 18.99  ? 114 GLY A N   1 
ATOM   828   C  CA  . GLY A  1 120 ? 50.384  63.057  49.631 1.00 18.28  ? 114 GLY A CA  1 
ATOM   829   C  C   . GLY A  1 120 ? 49.133  63.855  49.965 1.00 23.30  ? 114 GLY A C   1 
ATOM   830   O  O   . GLY A  1 120 ? 49.201  65.074  50.150 1.00 20.19  ? 114 GLY A O   1 
ATOM   831   N  N   . ARG A  1 121 ? 47.986  63.185  50.026 1.00 16.95  ? 115 ARG A N   1 
ATOM   832   C  CA  . ARG A  1 121 ? 46.751  63.863  50.382 1.00 19.27  ? 115 ARG A CA  1 
ATOM   833   C  C   . ARG A  1 121 ? 46.342  63.379  51.784 1.00 24.67  ? 115 ARG A C   1 
ATOM   834   O  O   . ARG A  1 121 ? 47.062  62.558  52.389 1.00 23.56  ? 115 ARG A O   1 
ATOM   835   C  CB  . ARG A  1 121 ? 45.693  63.584  49.317 1.00 20.58  ? 115 ARG A CB  1 
ATOM   836   C  CG  . ARG A  1 121 ? 46.120  64.120  47.945 1.00 14.66  ? 115 ARG A CG  1 
ATOM   837   C  CD  . ARG A  1 121 ? 45.088  63.827  46.883 1.00 28.41  ? 115 ARG A CD  1 
ATOM   838   N  NE  . ARG A  1 121 ? 45.502  64.241  45.544 1.00 20.02  ? 115 ARG A NE  1 
ATOM   839   C  CZ  . ARG A  1 121 ? 45.591  65.504  45.135 1.00 24.04  ? 115 ARG A CZ  1 
ATOM   840   N  NH1 . ARG A  1 121 ? 45.969  65.766  43.898 1.00 22.63  ? 115 ARG A NH1 1 
ATOM   841   N  NH2 . ARG A  1 121 ? 45.312  66.505  45.954 1.00 19.78  ? 115 ARG A NH2 1 
ATOM   842   N  N   . THR A  1 122 ? 45.231  63.881  52.324 1.00 20.38  ? 116 THR A N   1 
ATOM   843   C  CA  . THR A  1 122 ? 44.847  63.468  53.681 1.00 27.17  ? 116 THR A CA  1 
ATOM   844   C  C   . THR A  1 122 ? 43.656  62.521  53.849 1.00 28.69  ? 116 THR A C   1 
ATOM   845   O  O   . THR A  1 122 ? 42.571  62.753  53.309 1.00 28.14  ? 116 THR A O   1 
ATOM   846   C  CB  . THR A  1 122 ? 44.568  64.689  54.578 1.00 30.38  ? 116 THR A CB  1 
ATOM   847   O  OG1 . THR A  1 122 ? 45.741  65.503  54.658 1.00 28.81  ? 116 THR A OG1 1 
ATOM   848   C  CG2 . THR A  1 122 ? 44.153  64.237  55.998 1.00 29.07  ? 116 THR A CG2 1 
ATOM   849   N  N   . LEU A  1 123 ? 43.867  61.457  54.616 1.00 24.80  ? 117 LEU A N   1 
ATOM   850   C  CA  . LEU A  1 123 ? 42.798  60.513  54.902 1.00 23.44  ? 117 LEU A CA  1 
ATOM   851   C  C   . LEU A  1 123 ? 42.161  61.026  56.196 1.00 25.63  ? 117 LEU A C   1 
ATOM   852   O  O   . LEU A  1 123 ? 42.867  61.356  57.154 1.00 27.99  ? 117 LEU A O   1 
ATOM   853   C  CB  . LEU A  1 123 ? 43.352  59.114  55.114 1.00 18.84  ? 117 LEU A CB  1 
ATOM   854   C  CG  . LEU A  1 123 ? 42.286  58.058  55.435 1.00 27.61  ? 117 LEU A CG  1 
ATOM   855   C  CD1 . LEU A  1 123 ? 41.364  57.862  54.253 1.00 22.87  ? 117 LEU A CD1 1 
ATOM   856   C  CD2 . LEU A  1 123 ? 42.950  56.763  55.795 1.00 17.23  ? 117 LEU A CD2 1 
ATOM   857   N  N   . VAL A  1 124 ? 40.835  61.100  56.214 1.00 22.43  ? 118 VAL A N   1 
ATOM   858   C  CA  . VAL A  1 124 ? 40.095  61.601  57.370 1.00 26.02  ? 118 VAL A CA  1 
ATOM   859   C  C   . VAL A  1 124 ? 38.966  60.659  57.819 1.00 31.40  ? 118 VAL A C   1 
ATOM   860   O  O   . VAL A  1 124 ? 38.188  60.150  57.001 1.00 29.30  ? 118 VAL A O   1 
ATOM   861   C  CB  . VAL A  1 124 ? 39.460  62.980  57.046 1.00 25.02  ? 118 VAL A CB  1 
ATOM   862   C  CG1 . VAL A  1 124 ? 38.640  63.479  58.218 1.00 20.61  ? 118 VAL A CG1 1 
ATOM   863   C  CG2 . VAL A  1 124 ? 40.545  63.983  56.688 1.00 29.54  ? 118 VAL A CG2 1 
ATOM   864   N  N   . VAL A  1 125 ? 38.875  60.423  59.121 1.00 28.08  ? 119 VAL A N   1 
ATOM   865   C  CA  . VAL A  1 125 ? 37.807  59.585  59.647 1.00 24.01  ? 119 VAL A CA  1 
ATOM   866   C  C   . VAL A  1 125 ? 36.869  60.607  60.283 1.00 27.15  ? 119 VAL A C   1 
ATOM   867   O  O   . VAL A  1 125 ? 37.309  61.478  61.051 1.00 21.70  ? 119 VAL A O   1 
ATOM   868   C  CB  . VAL A  1 125 ? 38.344  58.557  60.674 1.00 30.17  ? 119 VAL A CB  1 
ATOM   869   C  CG1 . VAL A  1 125 ? 38.930  59.266  61.886 1.00 36.05  ? 119 VAL A CG1 1 
ATOM   870   C  CG2 . VAL A  1 125 ? 37.237  57.614  61.080 1.00 35.85  ? 119 VAL A CG2 1 
ATOM   871   N  N   . HIS A  1 126 ? 35.584  60.532  59.939 1.00 26.92  ? 120 HIS A N   1 
ATOM   872   C  CA  . HIS A  1 126 ? 34.627  61.519  60.435 1.00 30.66  ? 120 HIS A CA  1 
ATOM   873   C  C   . HIS A  1 126 ? 33.837  61.138  61.692 1.00 34.34  ? 120 HIS A C   1 
ATOM   874   O  O   . HIS A  1 126 ? 33.923  60.013  62.178 1.00 32.21  ? 120 HIS A O   1 
ATOM   875   C  CB  . HIS A  1 126 ? 33.693  61.927  59.292 1.00 25.47  ? 120 HIS A CB  1 
ATOM   876   C  CG  . HIS A  1 126 ? 34.353  62.781  58.242 1.00 37.08  ? 120 HIS A CG  1 
ATOM   877   N  ND1 . HIS A  1 126 ? 34.279  64.159  58.245 1.00 33.50  ? 120 HIS A ND1 1 
ATOM   878   C  CD2 . HIS A  1 126 ? 35.104  62.451  57.161 1.00 39.14  ? 120 HIS A CD2 1 
ATOM   879   C  CE1 . HIS A  1 126 ? 34.951  64.639  57.211 1.00 39.14  ? 120 HIS A CE1 1 
ATOM   880   N  NE2 . HIS A  1 126 ? 35.461  63.624  56.535 1.00 36.09  ? 120 HIS A NE2 1 
ATOM   881   N  N   . GLU A  1 127 ? 33.096  62.105  62.225 1.00 39.43  ? 121 GLU A N   1 
ATOM   882   C  CA  . GLU A  1 127 ? 32.300  61.940  63.447 1.00 40.85  ? 121 GLU A CA  1 
ATOM   883   C  C   . GLU A  1 127 ? 31.039  61.119  63.247 1.00 43.93  ? 121 GLU A C   1 
ATOM   884   O  O   . GLU A  1 127 ? 30.780  60.158  63.977 1.00 39.78  ? 121 GLU A O   1 
ATOM   885   C  CB  . GLU A  1 127 ? 31.892  63.307  63.967 1.00 43.45  ? 121 GLU A CB  1 
ATOM   886   C  CG  . GLU A  1 127 ? 31.066  63.287  65.224 1.00 55.57  ? 121 GLU A CG  1 
ATOM   887   C  CD  . GLU A  1 127 ? 30.574  64.680  65.590 1.00 67.31  ? 121 GLU A CD  1 
ATOM   888   O  OE1 . GLU A  1 127 ? 30.571  65.005  66.800 1.00 71.87  ? 121 GLU A OE1 1 
ATOM   889   O  OE2 . GLU A  1 127 ? 30.186  65.444  64.666 1.00 59.09  ? 121 GLU A OE2 1 
ATOM   890   N  N   . LYS A  1 128 ? 30.253  61.527  62.256 1.00 40.94  ? 122 LYS A N   1 
ATOM   891   C  CA  . LYS A  1 128 ? 28.999  60.864  61.932 1.00 43.72  ? 122 LYS A CA  1 
ATOM   892   C  C   . LYS A  1 128 ? 29.108  60.014  60.671 1.00 45.43  ? 122 LYS A C   1 
ATOM   893   O  O   . LYS A  1 128 ? 30.116  60.044  59.953 1.00 45.31  ? 122 LYS A O   1 
ATOM   894   C  CB  . LYS A  1 128 ? 27.886  61.902  61.754 1.00 38.06  ? 122 LYS A CB  1 
ATOM   895   C  CG  . LYS A  1 128 ? 27.653  62.765  62.987 1.00 41.23  ? 122 LYS A CG  1 
ATOM   896   C  CD  . LYS A  1 128 ? 26.526  63.770  62.780 1.00 55.89  ? 122 LYS A CD  1 
ATOM   897   C  CE  . LYS A  1 128 ? 26.798  64.717  61.618 1.00 63.09  ? 122 LYS A CE  1 
ATOM   898   N  NZ  . LYS A  1 128 ? 25.620  65.588  61.312 1.00 67.73  ? 122 LYS A NZ  1 
ATOM   899   N  N   . ALA A  1 129 ? 28.060  59.243  60.419 1.00 43.35  ? 123 ALA A N   1 
ATOM   900   C  CA  . ALA A  1 129 ? 28.006  58.386  59.254 1.00 41.06  ? 123 ALA A CA  1 
ATOM   901   C  C   . ALA A  1 129 ? 27.820  59.226  58.005 1.00 39.56  ? 123 ALA A C   1 
ATOM   902   O  O   . ALA A  1 129 ? 27.184  60.289  58.033 1.00 37.41  ? 123 ALA A O   1 
ATOM   903   C  CB  . ALA A  1 129 ? 26.861  57.412  59.387 1.00 37.42  ? 123 ALA A CB  1 
ATOM   904   N  N   . ASP A  1 130 ? 28.399  58.753  56.911 1.00 35.81  ? 124 ASP A N   1 
ATOM   905   C  CA  . ASP A  1 130 ? 28.278  59.430  55.633 1.00 36.75  ? 124 ASP A CA  1 
ATOM   906   C  C   . ASP A  1 130 ? 26.991  58.900  55.001 1.00 38.12  ? 124 ASP A C   1 
ATOM   907   O  O   . ASP A  1 130 ? 26.837  57.689  54.804 1.00 33.74  ? 124 ASP A O   1 
ATOM   908   C  CB  . ASP A  1 130 ? 29.487  59.085  54.754 1.00 39.82  ? 124 ASP A CB  1 
ATOM   909   C  CG  . ASP A  1 130 ? 29.408  59.694  53.354 1.00 38.00  ? 124 ASP A CG  1 
ATOM   910   O  OD1 . ASP A  1 130 ? 30.355  59.467  52.573 1.00 32.86  ? 124 ASP A OD1 1 
ATOM   911   O  OD2 . ASP A  1 130 ? 28.416  60.389  53.031 1.00 40.68  ? 124 ASP A OD2 1 
ATOM   912   N  N   . ASP A  1 131 ? 26.065  59.801  54.700 1.00 37.59  ? 125 ASP A N   1 
ATOM   913   C  CA  . ASP A  1 131 ? 24.804  59.404  54.085 1.00 40.95  ? 125 ASP A CA  1 
ATOM   914   C  C   . ASP A  1 131 ? 24.998  59.206  52.582 1.00 45.90  ? 125 ASP A C   1 
ATOM   915   O  O   . ASP A  1 131 ? 24.074  59.385  51.793 1.00 46.54  ? 125 ASP A O   1 
ATOM   916   C  CB  . ASP A  1 131 ? 23.742  60.473  54.334 1.00 38.30  ? 125 ASP A CB  1 
ATOM   917   C  CG  . ASP A  1 131 ? 24.036  61.770  53.603 1.00 42.99  ? 125 ASP A CG  1 
ATOM   918   O  OD1 . ASP A  1 131 ? 23.483  62.809  54.021 1.00 42.43  ? 125 ASP A OD1 1 
ATOM   919   O  OD2 . ASP A  1 131 ? 24.805  61.749  52.609 1.00 32.94  ? 125 ASP A OD2 1 
ATOM   920   N  N   . LEU A  1 132 ? 26.217  58.850  52.198 1.00 47.89  ? 126 LEU A N   1 
ATOM   921   C  CA  . LEU A  1 132 ? 26.571  58.620  50.807 1.00 48.04  ? 126 LEU A CA  1 
ATOM   922   C  C   . LEU A  1 132 ? 25.905  59.534  49.773 1.00 48.70  ? 126 LEU A C   1 
ATOM   923   O  O   . LEU A  1 132 ? 25.712  59.149  48.619 1.00 48.14  ? 126 LEU A O   1 
ATOM   924   C  CB  . LEU A  1 132 ? 26.332  57.153  50.458 1.00 48.89  ? 126 LEU A CB  1 
ATOM   925   C  CG  . LEU A  1 132 ? 26.924  56.189  51.497 1.00 50.13  ? 126 LEU A CG  1 
ATOM   926   C  CD1 . LEU A  1 132 ? 26.775  54.769  50.985 1.00 54.65  ? 126 LEU A CD1 1 
ATOM   927   C  CD2 . LEU A  1 132 ? 28.398  56.499  51.764 1.00 49.60  ? 126 LEU A CD2 1 
ATOM   928   N  N   . GLY A  1 133 ? 25.573  60.752  50.190 1.00 48.38  ? 127 GLY A N   1 
ATOM   929   C  CA  . GLY A  1 133 ? 24.992  61.717  49.275 1.00 58.10  ? 127 GLY A CA  1 
ATOM   930   C  C   . GLY A  1 133 ? 23.534  61.547  48.899 1.00 66.24  ? 127 GLY A C   1 
ATOM   931   O  O   . GLY A  1 133 ? 23.097  62.072  47.872 1.00 60.20  ? 127 GLY A O   1 
ATOM   932   N  N   . LYS A  1 134 ? 22.779  60.827  49.725 1.00 72.81  ? 128 LYS A N   1 
ATOM   933   C  CA  . LYS A  1 134 ? 21.360  60.608  49.470 1.00 77.25  ? 128 LYS A CA  1 
ATOM   934   C  C   . LYS A  1 134 ? 20.539  61.235  50.593 1.00 78.74  ? 128 LYS A C   1 
ATOM   935   O  O   . LYS A  1 134 ? 19.369  60.902  50.773 1.00 80.33  ? 128 LYS A O   1 
ATOM   936   C  CB  . LYS A  1 134 ? 21.055  59.110  49.399 1.00 76.55  ? 128 LYS A CB  1 
ATOM   937   C  CG  . LYS A  1 134 ? 22.024  58.290  48.552 1.00 77.33  ? 128 LYS A CG  1 
ATOM   938   C  CD  . LYS A  1 134 ? 22.215  58.861  47.152 1.00 79.14  ? 128 LYS A CD  1 
ATOM   939   C  CE  . LYS A  1 134 ? 22.945  57.866  46.247 1.00 80.70  ? 128 LYS A CE  1 
ATOM   940   N  NZ  . LYS A  1 134 ? 24.156  57.262  46.884 1.00 72.37  ? 128 LYS A NZ  1 
ATOM   941   N  N   . GLY A  1 135 ? 21.162  62.157  51.325 1.00 79.52  ? 129 GLY A N   1 
ATOM   942   C  CA  . GLY A  1 135 ? 20.524  62.814  52.456 1.00 78.92  ? 129 GLY A CA  1 
ATOM   943   C  C   . GLY A  1 135 ? 19.447  63.865  52.240 1.00 79.55  ? 129 GLY A C   1 
ATOM   944   O  O   . GLY A  1 135 ? 18.825  64.307  53.209 1.00 77.32  ? 129 GLY A O   1 
ATOM   945   N  N   . GLY A  1 136 ? 19.227  64.292  51.001 1.00 79.08  ? 130 GLY A N   1 
ATOM   946   C  CA  . GLY A  1 136 ? 18.185  65.276  50.755 1.00 83.62  ? 130 GLY A CA  1 
ATOM   947   C  C   . GLY A  1 136 ? 18.557  66.751  50.739 1.00 87.20  ? 130 GLY A C   1 
ATOM   948   O  O   . GLY A  1 136 ? 17.923  67.538  50.034 1.00 91.24  ? 130 GLY A O   1 
ATOM   949   N  N   . ASN A  1 137 ? 19.565  67.144  51.511 1.00 89.07  ? 131 ASN A N   1 
ATOM   950   C  CA  . ASN A  1 137 ? 19.983  68.545  51.545 1.00 86.25  ? 131 ASN A CA  1 
ATOM   951   C  C   . ASN A  1 137 ? 21.289  68.761  50.780 1.00 85.52  ? 131 ASN A C   1 
ATOM   952   O  O   . ASN A  1 137 ? 21.961  67.802  50.406 1.00 83.88  ? 131 ASN A O   1 
ATOM   953   C  CB  . ASN A  1 137 ? 20.131  69.007  52.996 1.00 86.74  ? 131 ASN A CB  1 
ATOM   954   C  CG  . ASN A  1 137 ? 21.032  68.103  53.803 1.00 84.82  ? 131 ASN A CG  1 
ATOM   955   O  OD1 . ASN A  1 137 ? 22.248  68.103  53.629 1.00 87.61  ? 131 ASN A OD1 1 
ATOM   956   N  ND2 . ASN A  1 137 ? 20.437  67.317  54.690 1.00 84.93  ? 131 ASN A ND2 1 
ATOM   957   N  N   . GLU A  1 138 ? 21.643  70.021  50.542 1.00 87.05  ? 132 GLU A N   1 
ATOM   958   C  CA  . GLU A  1 138 ? 22.863  70.349  49.808 1.00 86.94  ? 132 GLU A CA  1 
ATOM   959   C  C   . GLU A  1 138 ? 24.113  69.751  50.438 1.00 83.13  ? 132 GLU A C   1 
ATOM   960   O  O   . GLU A  1 138 ? 24.946  69.164  49.747 1.00 83.37  ? 132 GLU A O   1 
ATOM   961   C  CB  . GLU A  1 138 ? 23.038  71.865  49.710 1.00 90.47  ? 132 GLU A CB  1 
ATOM   962   C  CG  . GLU A  1 138 ? 21.959  72.567  48.920 1.00 100.91 ? 132 GLU A CG  1 
ATOM   963   C  CD  . GLU A  1 138 ? 22.240  74.045  48.753 1.00 107.68 ? 132 GLU A CD  1 
ATOM   964   O  OE1 . GLU A  1 138 ? 22.364  74.750  49.780 1.00 110.05 ? 132 GLU A OE1 1 
ATOM   965   O  OE2 . GLU A  1 138 ? 22.340  74.501  47.594 1.00 109.90 ? 132 GLU A OE2 1 
ATOM   966   N  N   . GLU A  1 139 ? 24.237  69.907  51.751 1.00 76.73  ? 133 GLU A N   1 
ATOM   967   C  CA  . GLU A  1 139 ? 25.389  69.405  52.480 1.00 72.16  ? 133 GLU A CA  1 
ATOM   968   C  C   . GLU A  1 139 ? 25.661  67.925  52.206 1.00 69.46  ? 133 GLU A C   1 
ATOM   969   O  O   . GLU A  1 139 ? 26.773  67.439  52.411 1.00 73.61  ? 133 GLU A O   1 
ATOM   970   C  CB  . GLU A  1 139 ? 25.196  69.629  53.984 1.00 73.59  ? 133 GLU A CB  1 
ATOM   971   C  CG  . GLU A  1 139 ? 26.454  69.398  54.805 1.00 77.19  ? 133 GLU A CG  1 
ATOM   972   C  CD  . GLU A  1 139 ? 27.572  70.366  54.444 1.00 83.26  ? 133 GLU A CD  1 
ATOM   973   O  OE1 . GLU A  1 139 ? 28.720  70.136  54.875 1.00 87.31  ? 133 GLU A OE1 1 
ATOM   974   O  OE2 . GLU A  1 139 ? 27.305  71.361  53.735 1.00 81.80  ? 133 GLU A OE2 1 
ATOM   975   N  N   . SER A  1 140 ? 24.652  67.208  51.735 1.00 62.84  ? 134 SER A N   1 
ATOM   976   C  CA  . SER A  1 140 ? 24.818  65.790  51.454 1.00 60.07  ? 134 SER A CA  1 
ATOM   977   C  C   . SER A  1 140 ? 25.656  65.539  50.197 1.00 59.56  ? 134 SER A C   1 
ATOM   978   O  O   . SER A  1 140 ? 26.552  64.696  50.198 1.00 57.26  ? 134 SER A O   1 
ATOM   979   C  CB  . SER A  1 140 ? 23.450  65.121  51.311 1.00 56.08  ? 134 SER A CB  1 
ATOM   980   O  OG  . SER A  1 140 ? 23.596  63.737  51.066 1.00 53.08  ? 134 SER A OG  1 
ATOM   981   N  N   . THR A  1 141 ? 25.362  66.266  49.126 1.00 56.67  ? 135 THR A N   1 
ATOM   982   C  CA  . THR A  1 141 ? 26.103  66.094  47.888 1.00 61.91  ? 135 THR A CA  1 
ATOM   983   C  C   . THR A  1 141 ? 27.451  66.798  47.927 1.00 64.66  ? 135 THR A C   1 
ATOM   984   O  O   . THR A  1 141 ? 28.152  66.861  46.917 1.00 60.46  ? 135 THR A O   1 
ATOM   985   C  CB  . THR A  1 141 ? 25.314  66.609  46.693 1.00 61.61  ? 135 THR A CB  1 
ATOM   986   O  OG1 . THR A  1 141 ? 24.648  67.823  47.055 1.00 60.80  ? 135 THR A OG1 1 
ATOM   987   C  CG2 . THR A  1 141 ? 24.307  65.571  46.242 1.00 57.84  ? 135 THR A CG2 1 
ATOM   988   N  N   . LYS A  1 142 ? 27.808  67.319  49.100 1.00 64.97  ? 136 LYS A N   1 
ATOM   989   C  CA  . LYS A  1 142 ? 29.088  67.993  49.281 1.00 64.09  ? 136 LYS A CA  1 
ATOM   990   C  C   . LYS A  1 142 ? 29.958  67.188  50.264 1.00 59.04  ? 136 LYS A C   1 
ATOM   991   O  O   . LYS A  1 142 ? 31.065  66.767  49.924 1.00 57.34  ? 136 LYS A O   1 
ATOM   992   C  CB  . LYS A  1 142 ? 28.873  69.423  49.803 1.00 68.06  ? 136 LYS A CB  1 
ATOM   993   C  CG  . LYS A  1 142 ? 30.035  70.370  49.509 1.00 77.44  ? 136 LYS A CG  1 
ATOM   994   C  CD  . LYS A  1 142 ? 29.854  71.758  50.138 1.00 84.89  ? 136 LYS A CD  1 
ATOM   995   C  CE  . LYS A  1 142 ? 30.053  71.727  51.656 1.00 87.89  ? 136 LYS A CE  1 
ATOM   996   N  NZ  . LYS A  1 142 ? 30.046  73.085  52.281 1.00 84.14  ? 136 LYS A NZ  1 
ATOM   997   N  N   . THR A  1 143 ? 29.435  66.941  51.464 1.00 53.50  ? 137 THR A N   1 
ATOM   998   C  CA  . THR A  1 143 ? 30.173  66.209  52.493 1.00 50.35  ? 137 THR A CA  1 
ATOM   999   C  C   . THR A  1 143 ? 29.513  64.931  52.999 1.00 46.33  ? 137 THR A C   1 
ATOM   1000  O  O   . THR A  1 143 ? 30.108  64.203  53.795 1.00 43.33  ? 137 THR A O   1 
ATOM   1001  C  CB  . THR A  1 143 ? 30.397  67.075  53.731 1.00 52.78  ? 137 THR A CB  1 
ATOM   1002  O  OG1 . THR A  1 143 ? 29.152  67.234  54.422 1.00 55.21  ? 137 THR A OG1 1 
ATOM   1003  C  CG2 . THR A  1 143 ? 30.925  68.440  53.337 1.00 54.82  ? 137 THR A CG2 1 
ATOM   1004  N  N   . GLY A  1 144 ? 28.287  64.663  52.561 1.00 45.11  ? 138 GLY A N   1 
ATOM   1005  C  CA  . GLY A  1 144 ? 27.589  63.475  53.026 1.00 36.05  ? 138 GLY A CA  1 
ATOM   1006  C  C   . GLY A  1 144 ? 27.154  63.594  54.487 1.00 35.47  ? 138 GLY A C   1 
ATOM   1007  O  O   . GLY A  1 144 ? 26.779  62.597  55.109 1.00 30.43  ? 138 GLY A O   1 
ATOM   1008  N  N   . ASN A  1 145 ? 27.202  64.812  55.028 1.00 35.34  ? 139 ASN A N   1 
ATOM   1009  C  CA  . ASN A  1 145 ? 26.828  65.069  56.421 1.00 43.11  ? 139 ASN A CA  1 
ATOM   1010  C  C   . ASN A  1 145 ? 27.602  64.172  57.385 1.00 46.33  ? 139 ASN A C   1 
ATOM   1011  O  O   . ASN A  1 145 ? 27.024  63.654  58.343 1.00 41.77  ? 139 ASN A O   1 
ATOM   1012  C  CB  . ASN A  1 145 ? 25.322  64.830  56.627 1.00 39.19  ? 139 ASN A CB  1 
ATOM   1013  C  CG  . ASN A  1 145 ? 24.459  65.819  55.866 1.00 42.82  ? 139 ASN A CG  1 
ATOM   1014  O  OD1 . ASN A  1 145 ? 24.472  67.021  56.150 1.00 47.48  ? 139 ASN A OD1 1 
ATOM   1015  N  ND2 . ASN A  1 145 ? 23.705  65.321  54.889 1.00 31.92  ? 139 ASN A ND2 1 
ATOM   1016  N  N   . ALA A  1 146 ? 28.902  63.985  57.150 1.00 43.44  ? 140 ALA A N   1 
ATOM   1017  C  CA  . ALA A  1 146 ? 29.677  63.103  58.021 1.00 35.08  ? 140 ALA A CA  1 
ATOM   1018  C  C   . ALA A  1 146 ? 30.191  63.797  59.284 1.00 34.38  ? 140 ALA A C   1 
ATOM   1019  O  O   . ALA A  1 146 ? 30.979  63.228  60.052 1.00 31.83  ? 140 ALA A O   1 
ATOM   1020  C  CB  . ALA A  1 146 ? 30.833  62.474  57.234 1.00 40.19  ? 140 ALA A CB  1 
ATOM   1021  N  N   . GLY A  1 147 ? 29.738  65.024  59.510 1.00 34.90  ? 141 GLY A N   1 
ATOM   1022  C  CA  . GLY A  1 147 ? 30.166  65.744  60.696 1.00 36.27  ? 141 GLY A CA  1 
ATOM   1023  C  C   . GLY A  1 147 ? 31.645  66.104  60.697 1.00 42.49  ? 141 GLY A C   1 
ATOM   1024  O  O   . GLY A  1 147 ? 32.323  66.093  59.658 1.00 39.64  ? 141 GLY A O   1 
ATOM   1025  N  N   . SER A  1 148 ? 32.155  66.409  61.880 1.00 37.08  ? 142 SER A N   1 
ATOM   1026  C  CA  . SER A  1 148 ? 33.540  66.813  62.035 1.00 42.51  ? 142 SER A CA  1 
ATOM   1027  C  C   . SER A  1 148 ? 34.597  65.741  61.743 1.00 40.46  ? 142 SER A C   1 
ATOM   1028  O  O   . SER A  1 148 ? 34.286  64.564  61.543 1.00 36.50  ? 142 SER A O   1 
ATOM   1029  C  CB  . SER A  1 148 ? 33.741  67.376  63.440 1.00 41.70  ? 142 SER A CB  1 
ATOM   1030  O  OG  . SER A  1 148 ? 33.482  66.388  64.412 1.00 46.37  ? 142 SER A OG  1 
ATOM   1031  N  N   . ARG A  1 149 ? 35.853  66.178  61.717 1.00 35.00  ? 143 ARG A N   1 
ATOM   1032  C  CA  . ARG A  1 149 ? 36.987  65.305  61.441 1.00 34.45  ? 143 ARG A CA  1 
ATOM   1033  C  C   . ARG A  1 149 ? 37.630  64.934  62.776 1.00 31.31  ? 143 ARG A C   1 
ATOM   1034  O  O   . ARG A  1 149 ? 38.164  65.792  63.470 1.00 26.85  ? 143 ARG A O   1 
ATOM   1035  C  CB  . ARG A  1 149 ? 37.960  66.054  60.533 1.00 29.85  ? 143 ARG A CB  1 
ATOM   1036  C  CG  . ARG A  1 149 ? 37.224  66.782  59.405 1.00 31.98  ? 143 ARG A CG  1 
ATOM   1037  C  CD  . ARG A  1 149 ? 38.098  67.702  58.572 1.00 29.97  ? 143 ARG A CD  1 
ATOM   1038  N  NE  . ARG A  1 149 ? 37.314  68.256  57.473 1.00 37.80  ? 143 ARG A NE  1 
ATOM   1039  C  CZ  . ARG A  1 149 ? 37.807  68.978  56.471 1.00 34.49  ? 143 ARG A CZ  1 
ATOM   1040  N  NH1 . ARG A  1 149 ? 36.995  69.425  55.526 1.00 21.38  ? 143 ARG A NH1 1 
ATOM   1041  N  NH2 . ARG A  1 149 ? 39.105  69.250  56.403 1.00 34.98  ? 143 ARG A NH2 1 
ATOM   1042  N  N   . LEU A  1 150 ? 37.565  63.660  63.139 1.00 28.68  ? 144 LEU A N   1 
ATOM   1043  C  CA  . LEU A  1 150 ? 38.106  63.223  64.420 1.00 32.60  ? 144 LEU A CA  1 
ATOM   1044  C  C   . LEU A  1 150 ? 39.569  62.903  64.352 1.00 35.11  ? 144 LEU A C   1 
ATOM   1045  O  O   . LEU A  1 150 ? 40.273  63.028  65.348 1.00 43.95  ? 144 LEU A O   1 
ATOM   1046  C  CB  . LEU A  1 150 ? 37.352  61.996  64.927 1.00 38.81  ? 144 LEU A CB  1 
ATOM   1047  C  CG  . LEU A  1 150 ? 35.831  62.146  64.946 1.00 45.76  ? 144 LEU A CG  1 
ATOM   1048  C  CD1 . LEU A  1 150 ? 35.215  60.862  65.486 1.00 47.93  ? 144 LEU A CD1 1 
ATOM   1049  C  CD2 . LEU A  1 150 ? 35.435  63.364  65.794 1.00 35.35  ? 144 LEU A CD2 1 
ATOM   1050  N  N   . ALA A  1 151 ? 40.026  62.471  63.183 1.00 28.28  ? 145 ALA A N   1 
ATOM   1051  C  CA  . ALA A  1 151 ? 41.427  62.138  63.008 1.00 29.54  ? 145 ALA A CA  1 
ATOM   1052  C  C   . ALA A  1 151 ? 41.770  62.045  61.532 1.00 30.94  ? 145 ALA A C   1 
ATOM   1053  O  O   . ALA A  1 151 ? 40.919  61.720  60.684 1.00 27.35  ? 145 ALA A O   1 
ATOM   1054  C  CB  . ALA A  1 151 ? 41.765  60.823  63.723 1.00 23.23  ? 145 ALA A CB  1 
ATOM   1055  N  N   . CYS A  1 152 ? 43.033  62.322  61.235 1.00 26.39  ? 146 CYS A N   1 
ATOM   1056  C  CA  . CYS A  1 152 ? 43.516  62.305  59.868 1.00 27.05  ? 146 CYS A CA  1 
ATOM   1057  C  C   . CYS A  1 152 ? 45.022  62.111  59.837 1.00 30.26  ? 146 CYS A C   1 
ATOM   1058  O  O   . CYS A  1 152 ? 45.686  62.061  60.877 1.00 25.71  ? 146 CYS A O   1 
ATOM   1059  C  CB  . CYS A  1 152 ? 43.174  63.626  59.198 1.00 28.09  ? 146 CYS A CB  1 
ATOM   1060  S  SG  . CYS A  1 152 ? 43.868  65.034  60.116 1.00 30.51  ? 146 CYS A SG  1 
ATOM   1061  N  N   . GLY A  1 153 ? 45.547  62.009  58.624 1.00 27.87  ? 147 GLY A N   1 
ATOM   1062  C  CA  . GLY A  1 153 ? 46.972  61.821  58.432 1.00 28.89  ? 147 GLY A CA  1 
ATOM   1063  C  C   . GLY A  1 153 ? 47.281  61.944  56.949 1.00 31.48  ? 147 GLY A C   1 
ATOM   1064  O  O   . GLY A  1 153 ? 46.406  61.711  56.095 1.00 26.87  ? 147 GLY A O   1 
ATOM   1065  N  N   . VAL A  1 154 ? 48.515  62.322  56.634 1.00 27.59  ? 148 VAL A N   1 
ATOM   1066  C  CA  . VAL A  1 154 ? 48.909  62.461  55.244 1.00 24.13  ? 148 VAL A CA  1 
ATOM   1067  C  C   . VAL A  1 154 ? 49.321  61.099  54.736 1.00 26.88  ? 148 VAL A C   1 
ATOM   1068  O  O   . VAL A  1 154 ? 50.068  60.385  55.401 1.00 28.89  ? 148 VAL A O   1 
ATOM   1069  C  CB  . VAL A  1 154 ? 50.074  63.439  55.087 1.00 25.45  ? 148 VAL A CB  1 
ATOM   1070  C  CG1 . VAL A  1 154 ? 50.416  63.607  53.588 1.00 14.98  ? 148 VAL A CG1 1 
ATOM   1071  C  CG2 . VAL A  1 154 ? 49.686  64.782  55.695 1.00 11.21  ? 148 VAL A CG2 1 
ATOM   1072  N  N   . ILE A  1 155 ? 48.824  60.734  53.559 1.00 27.43  ? 149 ILE A N   1 
ATOM   1073  C  CA  . ILE A  1 155 ? 49.135  59.431  52.986 1.00 23.10  ? 149 ILE A CA  1 
ATOM   1074  C  C   . ILE A  1 155 ? 50.526  59.422  52.378 1.00 24.48  ? 149 ILE A C   1 
ATOM   1075  O  O   . ILE A  1 155 ? 50.823  60.235  51.507 1.00 19.84  ? 149 ILE A O   1 
ATOM   1076  C  CB  . ILE A  1 155 ? 48.128  59.084  51.916 1.00 26.33  ? 149 ILE A CB  1 
ATOM   1077  C  CG1 . ILE A  1 155 ? 46.714  59.226  52.499 1.00 18.75  ? 149 ILE A CG1 1 
ATOM   1078  C  CG2 . ILE A  1 155 ? 48.403  57.686  51.400 1.00 18.14  ? 149 ILE A CG2 1 
ATOM   1079  C  CD1 . ILE A  1 155 ? 45.610  59.277  51.466 1.00 16.86  ? 149 ILE A CD1 1 
ATOM   1080  N  N   . GLY A  1 156 ? 51.372  58.502  52.837 1.00 24.58  ? 150 GLY A N   1 
ATOM   1081  C  CA  . GLY A  1 156 ? 52.729  58.428  52.326 1.00 18.72  ? 150 GLY A CA  1 
ATOM   1082  C  C   . GLY A  1 156 ? 53.159  57.126  51.669 1.00 25.24  ? 150 GLY A C   1 
ATOM   1083  O  O   . GLY A  1 156 ? 52.610  56.056  51.947 1.00 25.74  ? 150 GLY A O   1 
ATOM   1084  N  N   . ILE A  1 157 ? 54.149  57.223  50.786 1.00 19.17  ? 151 ILE A N   1 
ATOM   1085  C  CA  . ILE A  1 157 ? 54.668  56.061  50.096 1.00 20.40  ? 151 ILE A CA  1 
ATOM   1086  C  C   . ILE A  1 157 ? 55.253  55.137  51.148 1.00 24.84  ? 151 ILE A C   1 
ATOM   1087  O  O   . ILE A  1 157 ? 55.936  55.588  52.064 1.00 24.50  ? 151 ILE A O   1 
ATOM   1088  C  CB  . ILE A  1 157 ? 55.778  56.459  49.103 1.00 33.35  ? 151 ILE A CB  1 
ATOM   1089  C  CG1 . ILE A  1 157 ? 55.228  57.475  48.099 1.00 38.55  ? 151 ILE A CG1 1 
ATOM   1090  C  CG2 . ILE A  1 157 ? 56.285  55.231  48.356 1.00 25.95  ? 151 ILE A CG2 1 
ATOM   1091  C  CD1 . ILE A  1 157 ? 56.276  58.042  47.177 1.00 51.40  ? 151 ILE A CD1 1 
ATOM   1092  N  N   . ALA A  1 158 ? 54.979  53.845  51.024 1.00 23.56  ? 152 ALA A N   1 
ATOM   1093  C  CA  . ALA A  1 158 ? 55.494  52.877  51.979 1.00 29.27  ? 152 ALA A CA  1 
ATOM   1094  C  C   . ALA A  1 158 ? 56.333  51.814  51.292 1.00 31.43  ? 152 ALA A C   1 
ATOM   1095  O  O   . ALA A  1 158 ? 56.222  51.591  50.080 1.00 28.11  ? 152 ALA A O   1 
ATOM   1096  C  CB  . ALA A  1 158 ? 54.346  52.223  52.723 1.00 26.52  ? 152 ALA A CB  1 
ATOM   1097  N  N   . GLN A  1 159 ? 57.179  51.162  52.074 1.00 34.36  ? 153 GLN A N   1 
ATOM   1098  C  CA  . GLN A  1 159 ? 58.018  50.110  51.529 1.00 40.02  ? 153 GLN A CA  1 
ATOM   1099  C  C   . GLN A  1 159 ? 57.210  48.832  51.476 1.00 44.73  ? 153 GLN A C   1 
ATOM   1100  O  O   . GLN A  1 159 ? 56.562  48.512  52.502 1.00 40.93  ? 153 GLN A O   1 
ATOM   1101  C  CB  . GLN A  1 159 ? 59.242  49.876  52.402 1.00 31.13  ? 153 GLN A CB  1 
ATOM   1102  C  CG  . GLN A  1 159 ? 60.168  48.829  51.834 1.00 31.92  ? 153 GLN A CG  1 
ATOM   1103  C  CD  . GLN A  1 159 ? 61.343  48.546  52.750 1.00 53.23  ? 153 GLN A CD  1 
ATOM   1104  O  OE1 . GLN A  1 159 ? 62.498  48.595  52.323 1.00 51.88  ? 153 GLN A OE1 1 
ATOM   1105  N  NE2 . GLN A  1 159 ? 61.054  48.248  54.023 1.00 51.18  ? 153 GLN A NE2 1 
ATOM   1106  O  OXT . GLN A  1 159 ? 57.256  48.172  50.417 1.00 51.69  ? 153 GLN A OXT 1 
ATOM   1107  N  N   . THR B  1 8   ? 52.353  74.914  42.071 1.00 18.59  ? 2   THR B N   1 
ATOM   1108  C  CA  . THR B  1 8   ? 52.592  73.661  42.869 1.00 32.62  ? 2   THR B CA  1 
ATOM   1109  C  C   . THR B  1 8   ? 53.192  73.980  44.272 1.00 32.64  ? 2   THR B C   1 
ATOM   1110  O  O   . THR B  1 8   ? 54.148  74.769  44.417 1.00 23.78  ? 2   THR B O   1 
ATOM   1111  C  CB  . THR B  1 8   ? 53.519  72.712  42.093 1.00 38.50  ? 2   THR B CB  1 
ATOM   1112  O  OG1 . THR B  1 8   ? 52.959  71.395  42.056 1.00 32.68  ? 2   THR B OG1 1 
ATOM   1113  C  CG2 . THR B  1 8   ? 54.880  72.657  42.749 1.00 53.11  ? 2   THR B CG2 1 
ATOM   1114  N  N   . LYS B  1 9   ? 52.623  73.351  45.295 1.00 24.08  ? 3   LYS B N   1 
ATOM   1115  C  CA  . LYS B  1 9   ? 53.017  73.589  46.677 1.00 22.25  ? 3   LYS B CA  1 
ATOM   1116  C  C   . LYS B  1 9   ? 52.829  72.361  47.541 1.00 25.40  ? 3   LYS B C   1 
ATOM   1117  O  O   . LYS B  1 9   ? 51.899  71.570  47.346 1.00 29.89  ? 3   LYS B O   1 
ATOM   1118  C  CB  . LYS B  1 9   ? 52.165  74.712  47.287 1.00 23.85  ? 3   LYS B CB  1 
ATOM   1119  C  CG  . LYS B  1 9   ? 52.251  76.049  46.568 1.00 36.80  ? 3   LYS B CG  1 
ATOM   1120  C  CD  . LYS B  1 9   ? 51.237  77.085  47.098 1.00 42.30  ? 3   LYS B CD  1 
ATOM   1121  C  CE  . LYS B  1 9   ? 51.565  77.565  48.510 1.00 42.42  ? 3   LYS B CE  1 
ATOM   1122  N  NZ  . LYS B  1 9   ? 50.663  78.649  49.002 1.00 42.95  ? 3   LYS B NZ  1 
ATOM   1123  N  N   . ALA B  1 10  ? 53.709  72.218  48.521 1.00 22.97  ? 4   ALA B N   1 
ATOM   1124  C  CA  . ALA B  1 10  ? 53.636  71.109  49.444 1.00 20.48  ? 4   ALA B CA  1 
ATOM   1125  C  C   . ALA B  1 10  ? 53.889  71.709  50.802 1.00 25.38  ? 4   ALA B C   1 
ATOM   1126  O  O   . ALA B  1 10  ? 54.311  72.859  50.906 1.00 17.95  ? 4   ALA B O   1 
ATOM   1127  C  CB  . ALA B  1 10  ? 54.696  70.070  49.129 1.00 13.62  ? 4   ALA B CB  1 
ATOM   1128  N  N   . VAL B  1 11  ? 53.649  70.921  51.843 1.00 22.49  ? 5   VAL B N   1 
ATOM   1129  C  CA  . VAL B  1 11  ? 53.860  71.386  53.191 1.00 15.82  ? 5   VAL B CA  1 
ATOM   1130  C  C   . VAL B  1 11  ? 54.097  70.183  54.098 1.00 23.26  ? 5   VAL B C   1 
ATOM   1131  O  O   . VAL B  1 11  ? 53.696  69.048  53.800 1.00 17.57  ? 5   VAL B O   1 
ATOM   1132  C  CB  . VAL B  1 11  ? 52.650  72.198  53.690 1.00 15.05  ? 5   VAL B CB  1 
ATOM   1133  C  CG1 . VAL B  1 11  ? 51.451  71.278  53.891 1.00 8.57   ? 5   VAL B CG1 1 
ATOM   1134  C  CG2 . VAL B  1 11  ? 53.005  72.910  54.967 1.00 14.61  ? 5   VAL B CG2 1 
ATOM   1135  N  N   . CYS B  1 12  ? 54.713  70.444  55.236 1.00 17.42  ? 6   CYS B N   1 
ATOM   1136  C  CA  . CYS B  1 12  ? 55.053  69.375  56.133 1.00 19.20  ? 6   CYS B CA  1 
ATOM   1137  C  C   . CYS B  1 12  ? 55.099  69.858  57.575 1.00 21.31  ? 6   CYS B C   1 
ATOM   1138  O  O   . CYS B  1 12  ? 55.668  70.913  57.883 1.00 19.43  ? 6   CYS B O   1 
ATOM   1139  C  CB  . CYS B  1 12  ? 56.409  68.833  55.689 1.00 18.07  ? 6   CYS B CB  1 
ATOM   1140  S  SG  . CYS B  1 12  ? 57.177  67.680  56.760 1.00 25.91  ? 6   CYS B SG  1 
ATOM   1141  N  N   . VAL B  1 13  ? 54.482  69.084  58.457 1.00 19.67  ? 7   VAL B N   1 
ATOM   1142  C  CA  . VAL B  1 13  ? 54.464  69.427  59.867 1.00 16.40  ? 7   VAL B CA  1 
ATOM   1143  C  C   . VAL B  1 13  ? 55.496  68.517  60.507 1.00 18.09  ? 7   VAL B C   1 
ATOM   1144  O  O   . VAL B  1 13  ? 55.383  67.305  60.415 1.00 12.93  ? 7   VAL B O   1 
ATOM   1145  C  CB  . VAL B  1 13  ? 53.078  69.159  60.467 1.00 18.89  ? 7   VAL B CB  1 
ATOM   1146  C  CG1 . VAL B  1 13  ? 53.038  69.588  61.921 1.00 16.23  ? 7   VAL B CG1 1 
ATOM   1147  C  CG2 . VAL B  1 13  ? 52.024  69.890  59.670 1.00 14.00  ? 7   VAL B CG2 1 
ATOM   1148  N  N   . LEU B  1 14  ? 56.523  69.097  61.126 1.00 25.84  ? 8   LEU B N   1 
ATOM   1149  C  CA  . LEU B  1 14  ? 57.585  68.301  61.765 1.00 27.37  ? 8   LEU B CA  1 
ATOM   1150  C  C   . LEU B  1 14  ? 57.292  68.039  63.242 1.00 24.47  ? 8   LEU B C   1 
ATOM   1151  O  O   . LEU B  1 14  ? 57.081  68.982  64.015 1.00 23.11  ? 8   LEU B O   1 
ATOM   1152  C  CB  . LEU B  1 14  ? 58.945  69.023  61.634 1.00 19.80  ? 8   LEU B CB  1 
ATOM   1153  C  CG  . LEU B  1 14  ? 59.525  69.174  60.218 1.00 23.83  ? 8   LEU B CG  1 
ATOM   1154  C  CD1 . LEU B  1 14  ? 60.708  70.116  60.214 1.00 34.00  ? 8   LEU B CD1 1 
ATOM   1155  C  CD2 . LEU B  1 14  ? 59.962  67.842  59.714 1.00 24.49  ? 8   LEU B CD2 1 
ATOM   1156  N  N   . LYS B  1 15  ? 57.287  66.765  63.626 1.00 21.74  ? 9   LYS B N   1 
ATOM   1157  C  CA  . LYS B  1 15  ? 57.038  66.358  65.017 1.00 26.15  ? 9   LYS B CA  1 
ATOM   1158  C  C   . LYS B  1 15  ? 57.986  65.223  65.392 1.00 25.85  ? 9   LYS B C   1 
ATOM   1159  O  O   . LYS B  1 15  ? 58.409  64.449  64.535 1.00 27.81  ? 9   LYS B O   1 
ATOM   1160  C  CB  . LYS B  1 15  ? 55.587  65.872  65.209 1.00 30.25  ? 9   LYS B CB  1 
ATOM   1161  C  CG  . LYS B  1 15  ? 54.509  66.943  65.071 1.00 51.15  ? 9   LYS B CG  1 
ATOM   1162  C  CD  . LYS B  1 15  ? 53.115  66.394  65.415 1.00 64.20  ? 9   LYS B CD  1 
ATOM   1163  C  CE  . LYS B  1 15  ? 52.002  67.400  65.100 1.00 69.42  ? 9   LYS B CE  1 
ATOM   1164  N  NZ  . LYS B  1 15  ? 52.163  68.681  65.845 1.00 73.53  ? 9   LYS B NZ  1 
ATOM   1165  N  N   . GLY B  1 16  ? 58.320  65.128  66.675 1.00 32.01  ? 10  GLY B N   1 
ATOM   1166  C  CA  . GLY B  1 16  ? 59.215  64.082  67.136 1.00 33.88  ? 10  GLY B CA  1 
ATOM   1167  C  C   . GLY B  1 16  ? 58.896  63.663  68.560 1.00 39.92  ? 10  GLY B C   1 
ATOM   1168  O  O   . GLY B  1 16  ? 57.875  64.071  69.116 1.00 31.96  ? 10  GLY B O   1 
ATOM   1169  N  N   . ASP B  1 17  ? 59.753  62.835  69.153 1.00 43.43  ? 11  ASP B N   1 
ATOM   1170  C  CA  . ASP B  1 17  ? 59.537  62.398  70.531 1.00 51.66  ? 11  ASP B CA  1 
ATOM   1171  C  C   . ASP B  1 17  ? 59.898  63.551  71.456 1.00 49.06  ? 11  ASP B C   1 
ATOM   1172  O  O   . ASP B  1 17  ? 59.263  63.758  72.487 1.00 49.68  ? 11  ASP B O   1 
ATOM   1173  C  CB  . ASP B  1 17  ? 60.407  61.188  70.862 1.00 58.00  ? 11  ASP B CB  1 
ATOM   1174  C  CG  . ASP B  1 17  ? 59.932  59.929  70.182 1.00 64.05  ? 11  ASP B CG  1 
ATOM   1175  O  OD1 . ASP B  1 17  ? 60.580  58.878  70.364 1.00 75.50  ? 11  ASP B OD1 1 
ATOM   1176  O  OD2 . ASP B  1 17  ? 58.911  59.987  69.468 1.00 75.76  ? 11  ASP B OD2 1 
ATOM   1177  N  N   . GLY B  1 18  ? 60.924  64.302  71.065 1.00 45.93  ? 12  GLY B N   1 
ATOM   1178  C  CA  . GLY B  1 18  ? 61.357  65.436  71.854 1.00 34.68  ? 12  GLY B CA  1 
ATOM   1179  C  C   . GLY B  1 18  ? 60.524  66.674  71.576 1.00 33.34  ? 12  GLY B C   1 
ATOM   1180  O  O   . GLY B  1 18  ? 59.382  66.581  71.126 1.00 33.76  ? 12  GLY B O   1 
ATOM   1181  N  N   . PRO B  1 19  ? 61.088  67.861  71.831 1.00 30.52  ? 13  PRO B N   1 
ATOM   1182  C  CA  . PRO B  1 19  ? 60.456  69.165  71.636 1.00 27.80  ? 13  PRO B CA  1 
ATOM   1183  C  C   . PRO B  1 19  ? 60.598  69.775  70.245 1.00 26.86  ? 13  PRO B C   1 
ATOM   1184  O  O   . PRO B  1 19  ? 60.068  70.852  69.987 1.00 25.76  ? 13  PRO B O   1 
ATOM   1185  C  CB  . PRO B  1 19  ? 61.160  70.028  72.670 1.00 33.88  ? 13  PRO B CB  1 
ATOM   1186  C  CG  . PRO B  1 19  ? 62.572  69.528  72.558 1.00 26.54  ? 13  PRO B CG  1 
ATOM   1187  C  CD  . PRO B  1 19  ? 62.377  68.011  72.537 1.00 24.72  ? 13  PRO B CD  1 
ATOM   1188  N  N   . VAL B  1 20  ? 61.324  69.123  69.350 1.00 29.04  ? 14  VAL B N   1 
ATOM   1189  C  CA  . VAL B  1 20  ? 61.490  69.709  68.035 1.00 23.70  ? 14  VAL B CA  1 
ATOM   1190  C  C   . VAL B  1 20  ? 60.196  69.638  67.240 1.00 28.55  ? 14  VAL B C   1 
ATOM   1191  O  O   . VAL B  1 20  ? 59.563  68.579  67.149 1.00 26.62  ? 14  VAL B O   1 
ATOM   1192  C  CB  . VAL B  1 20  ? 62.609  69.011  67.253 1.00 25.79  ? 14  VAL B CB  1 
ATOM   1193  C  CG1 . VAL B  1 20  ? 62.744  69.643  65.876 1.00 19.90  ? 14  VAL B CG1 1 
ATOM   1194  C  CG2 . VAL B  1 20  ? 63.915  69.115  68.023 1.00 17.71  ? 14  VAL B CG2 1 
ATOM   1195  N  N   . GLN B  1 21  ? 59.799  70.773  66.674 1.00 19.96  ? 15  GLN B N   1 
ATOM   1196  C  CA  . GLN B  1 21  ? 58.588  70.820  65.871 1.00 25.52  ? 15  GLN B CA  1 
ATOM   1197  C  C   . GLN B  1 21  ? 58.606  72.059  64.988 1.00 25.41  ? 15  GLN B C   1 
ATOM   1198  O  O   . GLN B  1 21  ? 59.231  73.071  65.316 1.00 29.06  ? 15  GLN B O   1 
ATOM   1199  C  CB  . GLN B  1 21  ? 57.351  70.851  66.766 1.00 21.59  ? 15  GLN B CB  1 
ATOM   1200  C  CG  . GLN B  1 21  ? 57.143  72.164  67.479 1.00 34.12  ? 15  GLN B CG  1 
ATOM   1201  C  CD  . GLN B  1 21  ? 56.031  72.102  68.511 1.00 44.60  ? 15  GLN B CD  1 
ATOM   1202  O  OE1 . GLN B  1 21  ? 55.524  73.129  68.944 1.00 57.82  ? 15  GLN B OE1 1 
ATOM   1203  N  NE2 . GLN B  1 21  ? 55.656  70.894  68.916 1.00 46.40  ? 15  GLN B NE2 1 
ATOM   1204  N  N   . GLY B  1 22  ? 57.913  71.985  63.867 1.00 19.73  ? 16  GLY B N   1 
ATOM   1205  C  CA  . GLY B  1 22  ? 57.888  73.119  62.974 1.00 16.03  ? 16  GLY B CA  1 
ATOM   1206  C  C   . GLY B  1 22  ? 57.085  72.830  61.732 1.00 17.06  ? 16  GLY B C   1 
ATOM   1207  O  O   . GLY B  1 22  ? 56.576  71.729  61.546 1.00 30.49  ? 16  GLY B O   1 
ATOM   1208  N  N   . ILE B  1 23  ? 56.967  73.837  60.884 1.00 21.06  ? 17  ILE B N   1 
ATOM   1209  C  CA  . ILE B  1 23  ? 56.227  73.727  59.648 1.00 19.46  ? 17  ILE B CA  1 
ATOM   1210  C  C   . ILE B  1 23  ? 57.168  74.156  58.552 1.00 20.51  ? 17  ILE B C   1 
ATOM   1211  O  O   . ILE B  1 23  ? 57.756  75.242  58.615 1.00 22.48  ? 17  ILE B O   1 
ATOM   1212  C  CB  . ILE B  1 23  ? 55.005  74.668  59.647 1.00 20.77  ? 17  ILE B CB  1 
ATOM   1213  C  CG1 . ILE B  1 23  ? 53.949  74.139  60.619 1.00 26.58  ? 17  ILE B CG1 1 
ATOM   1214  C  CG2 . ILE B  1 23  ? 54.404  74.760  58.254 1.00 17.90  ? 17  ILE B CG2 1 
ATOM   1215  C  CD1 . ILE B  1 23  ? 52.886  75.176  60.973 1.00 19.65  ? 17  ILE B CD1 1 
ATOM   1216  N  N   . ILE B  1 24  ? 57.332  73.297  57.559 1.00 15.68  ? 18  ILE B N   1 
ATOM   1217  C  CA  . ILE B  1 24  ? 58.189  73.620  56.435 1.00 17.61  ? 18  ILE B CA  1 
ATOM   1218  C  C   . ILE B  1 24  ? 57.330  73.635  55.185 1.00 21.20  ? 18  ILE B C   1 
ATOM   1219  O  O   . ILE B  1 24  ? 56.588  72.682  54.918 1.00 17.68  ? 18  ILE B O   1 
ATOM   1220  C  CB  . ILE B  1 24  ? 59.328  72.590  56.266 1.00 13.46  ? 18  ILE B CB  1 
ATOM   1221  C  CG1 . ILE B  1 24  ? 60.325  72.724  57.415 1.00 15.26  ? 18  ILE B CG1 1 
ATOM   1222  C  CG2 . ILE B  1 24  ? 60.032  72.804  54.937 1.00 11.63  ? 18  ILE B CG2 1 
ATOM   1223  C  CD1 . ILE B  1 24  ? 60.970  74.082  57.503 1.00 9.60   ? 18  ILE B CD1 1 
ATOM   1224  N  N   . ASN B  1 25  ? 57.438  74.726  54.437 1.00 17.61  ? 19  ASN B N   1 
ATOM   1225  C  CA  . ASN B  1 25  ? 56.694  74.942  53.188 1.00 21.90  ? 19  ASN B CA  1 
ATOM   1226  C  C   . ASN B  1 25  ? 57.559  74.682  51.970 1.00 20.11  ? 19  ASN B C   1 
ATOM   1227  O  O   . ASN B  1 25  ? 58.762  74.938  51.996 1.00 17.94  ? 19  ASN B O   1 
ATOM   1228  C  CB  . ASN B  1 25  ? 56.209  76.388  53.122 1.00 18.73  ? 19  ASN B CB  1 
ATOM   1229  C  CG  . ASN B  1 25  ? 55.339  76.743  54.291 1.00 24.47  ? 19  ASN B CG  1 
ATOM   1230  O  OD1 . ASN B  1 25  ? 54.223  76.257  54.396 1.00 29.89  ? 19  ASN B OD1 1 
ATOM   1231  N  ND2 . ASN B  1 25  ? 55.850  77.576  55.194 1.00 16.31  ? 19  ASN B ND2 1 
ATOM   1232  N  N   . PHE B  1 26  ? 56.941  74.178  50.906 1.00 20.64  ? 20  PHE B N   1 
ATOM   1233  C  CA  . PHE B  1 26  ? 57.656  73.905  49.658 1.00 17.13  ? 20  PHE B CA  1 
ATOM   1234  C  C   . PHE B  1 26  ? 56.907  74.581  48.526 1.00 22.39  ? 20  PHE B C   1 
ATOM   1235  O  O   . PHE B  1 26  ? 55.676  74.523  48.449 1.00 21.33  ? 20  PHE B O   1 
ATOM   1236  C  CB  . PHE B  1 26  ? 57.698  72.417  49.348 1.00 17.02  ? 20  PHE B CB  1 
ATOM   1237  C  CG  . PHE B  1 26  ? 58.488  71.603  50.329 1.00 22.08  ? 20  PHE B CG  1 
ATOM   1238  C  CD1 . PHE B  1 26  ? 59.799  71.232  50.050 1.00 21.09  ? 20  PHE B CD1 1 
ATOM   1239  C  CD2 . PHE B  1 26  ? 57.908  71.174  51.517 1.00 21.86  ? 20  PHE B CD2 1 
ATOM   1240  C  CE1 . PHE B  1 26  ? 60.519  70.444  50.931 1.00 16.91  ? 20  PHE B CE1 1 
ATOM   1241  C  CE2 . PHE B  1 26  ? 58.620  70.379  52.414 1.00 20.60  ? 20  PHE B CE2 1 
ATOM   1242  C  CZ  . PHE B  1 26  ? 59.932  70.013  52.115 1.00 28.32  ? 20  PHE B CZ  1 
ATOM   1243  N  N   . GLU B  1 27  ? 57.647  75.197  47.619 1.00 23.70  ? 21  GLU B N   1 
ATOM   1244  C  CA  . GLU B  1 27  ? 57.017  75.866  46.505 1.00 23.25  ? 21  GLU B CA  1 
ATOM   1245  C  C   . GLU B  1 27  ? 57.832  75.679  45.242 1.00 20.79  ? 21  GLU B C   1 
ATOM   1246  O  O   . GLU B  1 27  ? 59.053  75.800  45.253 1.00 26.40  ? 21  GLU B O   1 
ATOM   1247  C  CB  . GLU B  1 27  ? 56.865  77.347  46.827 1.00 28.74  ? 21  GLU B CB  1 
ATOM   1248  C  CG  . GLU B  1 27  ? 55.972  78.099  45.856 1.00 59.55  ? 21  GLU B CG  1 
ATOM   1249  C  CD  . GLU B  1 27  ? 55.761  79.545  46.264 1.00 67.94  ? 21  GLU B CD  1 
ATOM   1250  O  OE1 . GLU B  1 27  ? 55.065  80.279  45.523 1.00 75.22  ? 21  GLU B OE1 1 
ATOM   1251  O  OE2 . GLU B  1 27  ? 56.294  79.939  47.328 1.00 71.23  ? 21  GLU B OE2 1 
ATOM   1252  N  N   . GLN B  1 28  ? 57.155  75.367  44.149 1.00 21.25  ? 22  GLN B N   1 
ATOM   1253  C  CA  . GLN B  1 28  ? 57.835  75.187  42.878 1.00 26.25  ? 22  GLN B CA  1 
ATOM   1254  C  C   . GLN B  1 28  ? 56.973  75.808  41.770 1.00 26.22  ? 22  GLN B C   1 
ATOM   1255  O  O   . GLN B  1 28  ? 56.005  75.209  41.303 1.00 27.78  ? 22  GLN B O   1 
ATOM   1256  C  CB  . GLN B  1 28  ? 58.085  73.691  42.650 1.00 28.36  ? 22  GLN B CB  1 
ATOM   1257  C  CG  . GLN B  1 28  ? 58.699  73.327  41.311 1.00 25.16  ? 22  GLN B CG  1 
ATOM   1258  C  CD  . GLN B  1 28  ? 59.024  71.841  41.202 1.00 33.03  ? 22  GLN B CD  1 
ATOM   1259  O  OE1 . GLN B  1 28  ? 58.255  70.985  41.659 1.00 30.73  ? 22  GLN B OE1 1 
ATOM   1260  N  NE2 . GLN B  1 28  ? 60.161  71.526  40.580 1.00 22.34  ? 22  GLN B NE2 1 
ATOM   1261  N  N   . LYS B  1 29  ? 57.319  77.032  41.383 1.00 36.44  ? 23  LYS B N   1 
ATOM   1262  C  CA  . LYS B  1 29  ? 56.578  77.765  40.352 1.00 44.00  ? 23  LYS B CA  1 
ATOM   1263  C  C   . LYS B  1 29  ? 56.581  77.049  39.009 1.00 40.30  ? 23  LYS B C   1 
ATOM   1264  O  O   . LYS B  1 29  ? 55.536  76.877  38.398 1.00 35.88  ? 23  LYS B O   1 
ATOM   1265  C  CB  . LYS B  1 29  ? 57.147  79.188  40.183 1.00 46.90  ? 23  LYS B CB  1 
ATOM   1266  C  CG  . LYS B  1 29  ? 56.956  80.092  41.410 1.00 66.16  ? 23  LYS B CG  1 
ATOM   1267  C  CD  . LYS B  1 29  ? 57.695  81.439  41.293 1.00 73.76  ? 23  LYS B CD  1 
ATOM   1268  C  CE  . LYS B  1 29  ? 57.594  82.248  42.599 1.00 79.28  ? 23  LYS B CE  1 
ATOM   1269  N  NZ  . LYS B  1 29  ? 58.279  83.581  42.549 1.00 74.75  ? 23  LYS B NZ  1 
ATOM   1270  N  N   . GLU B  1 30  ? 57.756  76.630  38.554 1.00 44.08  ? 24  GLU B N   1 
ATOM   1271  C  CA  . GLU B  1 30  ? 57.888  75.940  37.277 1.00 46.97  ? 24  GLU B CA  1 
ATOM   1272  C  C   . GLU B  1 30  ? 58.115  74.451  37.475 1.00 48.28  ? 24  GLU B C   1 
ATOM   1273  O  O   . GLU B  1 30  ? 58.882  74.041  38.346 1.00 48.09  ? 24  GLU B O   1 
ATOM   1274  C  CB  . GLU B  1 30  ? 59.055  76.535  36.488 1.00 57.06  ? 24  GLU B CB  1 
ATOM   1275  C  CG  . GLU B  1 30  ? 58.851  77.970  36.083 1.00 68.06  ? 24  GLU B CG  1 
ATOM   1276  C  CD  . GLU B  1 30  ? 57.571  78.138  35.300 1.00 82.58  ? 24  GLU B CD  1 
ATOM   1277  O  OE1 . GLU B  1 30  ? 57.416  77.443  34.271 1.00 84.54  ? 24  GLU B OE1 1 
ATOM   1278  O  OE2 . GLU B  1 30  ? 56.719  78.956  35.716 1.00 90.44  ? 24  GLU B OE2 1 
ATOM   1279  N  N   . SER B  1 31  ? 57.463  73.644  36.649 1.00 48.19  ? 25  SER B N   1 
ATOM   1280  C  CA  . SER B  1 31  ? 57.576  72.190  36.732 1.00 54.81  ? 25  SER B CA  1 
ATOM   1281  C  C   . SER B  1 31  ? 59.022  71.679  36.791 1.00 54.22  ? 25  SER B C   1 
ATOM   1282  O  O   . SER B  1 31  ? 59.310  70.624  37.361 1.00 50.70  ? 25  SER B O   1 
ATOM   1283  C  CB  . SER B  1 31  ? 56.855  71.559  35.536 1.00 61.40  ? 25  SER B CB  1 
ATOM   1284  O  OG  . SER B  1 31  ? 56.901  70.141  35.592 1.00 73.28  ? 25  SER B OG  1 
ATOM   1285  N  N   . ASN B  1 32  ? 59.934  72.429  36.200 1.00 54.43  ? 26  ASN B N   1 
ATOM   1286  C  CA  . ASN B  1 32  ? 61.321  72.015  36.190 1.00 57.85  ? 26  ASN B CA  1 
ATOM   1287  C  C   . ASN B  1 32  ? 62.180  73.050  36.878 1.00 50.16  ? 26  ASN B C   1 
ATOM   1288  O  O   . ASN B  1 32  ? 63.402  73.046  36.753 1.00 47.25  ? 26  ASN B O   1 
ATOM   1289  C  CB  . ASN B  1 32  ? 61.763  71.824  34.750 1.00 71.88  ? 26  ASN B CB  1 
ATOM   1290  C  CG  . ASN B  1 32  ? 60.865  70.863  34.008 1.00 82.66  ? 26  ASN B CG  1 
ATOM   1291  O  OD1 . ASN B  1 32  ? 60.828  69.669  34.322 1.00 86.58  ? 26  ASN B OD1 1 
ATOM   1292  N  ND2 . ASN B  1 32  ? 60.118  71.376  33.032 1.00 82.14  ? 26  ASN B ND2 1 
ATOM   1293  N  N   . GLY B  1 33  ? 61.524  73.937  37.612 1.00 40.81  ? 27  GLY B N   1 
ATOM   1294  C  CA  . GLY B  1 33  ? 62.240  74.976  38.313 1.00 34.22  ? 27  GLY B CA  1 
ATOM   1295  C  C   . GLY B  1 33  ? 62.667  74.534  39.698 1.00 34.18  ? 27  GLY B C   1 
ATOM   1296  O  O   . GLY B  1 33  ? 62.294  73.455  40.182 1.00 21.73  ? 27  GLY B O   1 
ATOM   1297  N  N   . PRO B  1 34  ? 63.485  75.354  40.360 1.00 29.38  ? 28  PRO B N   1 
ATOM   1298  C  CA  . PRO B  1 34  ? 63.929  74.996  41.702 1.00 25.15  ? 28  PRO B CA  1 
ATOM   1299  C  C   . PRO B  1 34  ? 62.765  75.049  42.670 1.00 21.28  ? 28  PRO B C   1 
ATOM   1300  O  O   . PRO B  1 34  ? 61.759  75.696  42.400 1.00 18.48  ? 28  PRO B O   1 
ATOM   1301  C  CB  . PRO B  1 34  ? 64.983  76.054  42.008 1.00 26.21  ? 28  PRO B CB  1 
ATOM   1302  C  CG  . PRO B  1 34  ? 64.541  77.227  41.193 1.00 22.55  ? 28  PRO B CG  1 
ATOM   1303  C  CD  . PRO B  1 34  ? 64.136  76.589  39.894 1.00 20.54  ? 28  PRO B CD  1 
ATOM   1304  N  N   . VAL B  1 35  ? 62.906  74.348  43.787 1.00 19.79  ? 29  VAL B N   1 
ATOM   1305  C  CA  . VAL B  1 35  ? 61.892  74.323  44.824 1.00 18.97  ? 29  VAL B CA  1 
ATOM   1306  C  C   . VAL B  1 35  ? 62.345  75.237  45.947 1.00 22.92  ? 29  VAL B C   1 
ATOM   1307  O  O   . VAL B  1 35  ? 63.478  75.138  46.412 1.00 24.21  ? 29  VAL B O   1 
ATOM   1308  C  CB  . VAL B  1 35  ? 61.739  72.927  45.471 1.00 21.97  ? 29  VAL B CB  1 
ATOM   1309  C  CG1 . VAL B  1 35  ? 60.688  73.010  46.595 1.00 17.15  ? 29  VAL B CG1 1 
ATOM   1310  C  CG2 . VAL B  1 35  ? 61.371  71.882  44.430 1.00 11.46  ? 29  VAL B CG2 1 
ATOM   1311  N  N   . LYS B  1 36  ? 61.476  76.131  46.385 1.00 23.21  ? 30  LYS B N   1 
ATOM   1312  C  CA  . LYS B  1 36  ? 61.835  76.996  47.491 1.00 28.50  ? 30  LYS B CA  1 
ATOM   1313  C  C   . LYS B  1 36  ? 61.398  76.189  48.710 1.00 27.89  ? 30  LYS B C   1 
ATOM   1314  O  O   . LYS B  1 36  ? 60.311  75.615  48.721 1.00 26.84  ? 30  LYS B O   1 
ATOM   1315  C  CB  . LYS B  1 36  ? 61.069  78.329  47.430 1.00 37.05  ? 30  LYS B CB  1 
ATOM   1316  C  CG  . LYS B  1 36  ? 61.323  79.178  46.161 1.00 62.34  ? 30  LYS B CG  1 
ATOM   1317  C  CD  . LYS B  1 36  ? 60.588  80.541  46.209 1.00 72.17  ? 30  LYS B CD  1 
ATOM   1318  C  CE  . LYS B  1 36  ? 60.778  81.372  44.927 1.00 72.03  ? 30  LYS B CE  1 
ATOM   1319  N  NZ  . LYS B  1 36  ? 60.066  82.700  44.961 1.00 67.49  ? 30  LYS B NZ  1 
ATOM   1320  N  N   . VAL B  1 37  ? 62.255  76.105  49.717 1.00 21.99  ? 31  VAL B N   1 
ATOM   1321  C  CA  . VAL B  1 37  ? 61.913  75.374  50.927 1.00 15.82  ? 31  VAL B CA  1 
ATOM   1322  C  C   . VAL B  1 37  ? 62.107  76.338  52.061 1.00 13.73  ? 31  VAL B C   1 
ATOM   1323  O  O   . VAL B  1 37  ? 63.215  76.763  52.333 1.00 25.54  ? 31  VAL B O   1 
ATOM   1324  C  CB  . VAL B  1 37  ? 62.819  74.175  51.135 1.00 11.39  ? 31  VAL B CB  1 
ATOM   1325  C  CG1 . VAL B  1 37  ? 62.379  73.406  52.361 1.00 7.16   ? 31  VAL B CG1 1 
ATOM   1326  C  CG2 . VAL B  1 37  ? 62.783  73.279  49.908 1.00 12.09  ? 31  VAL B CG2 1 
ATOM   1327  N  N   . TRP B  1 38  ? 61.028  76.691  52.736 1.00 20.49  ? 32  TRP B N   1 
ATOM   1328  C  CA  . TRP B  1 38  ? 61.149  77.654  53.802 1.00 24.74  ? 32  TRP B CA  1 
ATOM   1329  C  C   . TRP B  1 38  ? 60.179  77.365  54.935 1.00 25.76  ? 32  TRP B C   1 
ATOM   1330  O  O   . TRP B  1 38  ? 59.141  76.748  54.738 1.00 20.82  ? 32  TRP B O   1 
ATOM   1331  C  CB  . TRP B  1 38  ? 60.906  79.060  53.245 1.00 17.29  ? 32  TRP B CB  1 
ATOM   1332  C  CG  . TRP B  1 38  ? 59.484  79.286  52.813 1.00 28.52  ? 32  TRP B CG  1 
ATOM   1333  C  CD1 . TRP B  1 38  ? 58.894  78.894  51.631 1.00 23.32  ? 32  TRP B CD1 1 
ATOM   1334  C  CD2 . TRP B  1 38  ? 58.460  79.919  53.583 1.00 24.46  ? 32  TRP B CD2 1 
ATOM   1335  N  NE1 . TRP B  1 38  ? 57.562  79.252  51.630 1.00 39.75  ? 32  TRP B NE1 1 
ATOM   1336  C  CE2 . TRP B  1 38  ? 57.272  79.882  52.815 1.00 30.60  ? 32  TRP B CE2 1 
ATOM   1337  C  CE3 . TRP B  1 38  ? 58.432  80.512  54.855 1.00 29.50  ? 32  TRP B CE3 1 
ATOM   1338  C  CZ2 . TRP B  1 38  ? 56.066  80.419  53.275 1.00 33.62  ? 32  TRP B CZ2 1 
ATOM   1339  C  CZ3 . TRP B  1 38  ? 57.230  81.047  55.317 1.00 40.01  ? 32  TRP B CZ3 1 
ATOM   1340  C  CH2 . TRP B  1 38  ? 56.062  80.995  54.523 1.00 40.83  ? 32  TRP B CH2 1 
ATOM   1341  N  N   . GLY B  1 39  ? 60.530  77.833  56.125 1.00 23.25  ? 33  GLY B N   1 
ATOM   1342  C  CA  . GLY B  1 39  ? 59.692  77.611  57.279 1.00 17.19  ? 33  GLY B CA  1 
ATOM   1343  C  C   . GLY B  1 39  ? 60.475  77.782  58.562 1.00 21.43  ? 33  GLY B C   1 
ATOM   1344  O  O   . GLY B  1 39  ? 61.639  78.168  58.564 1.00 30.90  ? 33  GLY B O   1 
ATOM   1345  N  N   . SER B  1 40  ? 59.845  77.429  59.661 1.00 21.89  ? 34  SER B N   1 
ATOM   1346  C  CA  . SER B  1 40  ? 60.447  77.598  60.953 1.00 24.47  ? 34  SER B CA  1 
ATOM   1347  C  C   . SER B  1 40  ? 60.401  76.328  61.790 1.00 29.36  ? 34  SER B C   1 
ATOM   1348  O  O   . SER B  1 40  ? 59.380  75.640  61.833 1.00 30.90  ? 34  SER B O   1 
ATOM   1349  C  CB  . SER B  1 40  ? 59.716  78.731  61.670 1.00 18.54  ? 34  SER B CB  1 
ATOM   1350  O  OG  . SER B  1 40  ? 60.145  78.824  63.006 1.00 49.85  ? 34  SER B OG  1 
ATOM   1351  N  N   . ILE B  1 41  ? 61.516  76.019  62.448 1.00 23.18  ? 35  ILE B N   1 
ATOM   1352  C  CA  . ILE B  1 41  ? 61.600  74.849  63.307 1.00 23.93  ? 35  ILE B CA  1 
ATOM   1353  C  C   . ILE B  1 41  ? 62.103  75.326  64.671 1.00 27.03  ? 35  ILE B C   1 
ATOM   1354  O  O   . ILE B  1 41  ? 63.121  76.030  64.755 1.00 30.76  ? 35  ILE B O   1 
ATOM   1355  C  CB  . ILE B  1 41  ? 62.593  73.802  62.755 1.00 29.05  ? 35  ILE B CB  1 
ATOM   1356  C  CG1 . ILE B  1 41  ? 62.340  73.574  61.260 1.00 24.37  ? 35  ILE B CG1 1 
ATOM   1357  C  CG2 . ILE B  1 41  ? 62.456  72.491  63.547 1.00 25.06  ? 35  ILE B CG2 1 
ATOM   1358  C  CD1 . ILE B  1 41  ? 63.202  72.478  60.657 1.00 28.65  ? 35  ILE B CD1 1 
ATOM   1359  N  N   . LYS B  1 42  ? 61.394  74.948  65.733 1.00 22.07  ? 36  LYS B N   1 
ATOM   1360  C  CA  . LYS B  1 42  ? 61.773  75.357  67.076 1.00 23.64  ? 36  LYS B CA  1 
ATOM   1361  C  C   . LYS B  1 42  ? 62.186  74.179  67.952 1.00 24.54  ? 36  LYS B C   1 
ATOM   1362  O  O   . LYS B  1 42  ? 61.946  73.018  67.593 1.00 26.11  ? 36  LYS B O   1 
ATOM   1363  C  CB  . LYS B  1 42  ? 60.627  76.130  67.727 1.00 29.72  ? 36  LYS B CB  1 
ATOM   1364  C  CG  . LYS B  1 42  ? 59.401  75.314  68.066 1.00 42.94  ? 36  LYS B CG  1 
ATOM   1365  C  CD  . LYS B  1 42  ? 58.394  76.186  68.808 1.00 53.28  ? 36  LYS B CD  1 
ATOM   1366  C  CE  . LYS B  1 42  ? 57.182  75.400  69.268 1.00 59.42  ? 36  LYS B CE  1 
ATOM   1367  N  NZ  . LYS B  1 42  ? 56.225  76.260  70.018 1.00 66.95  ? 36  LYS B NZ  1 
ATOM   1368  N  N   . GLY B  1 43  ? 62.821  74.482  69.091 1.00 25.49  ? 37  GLY B N   1 
ATOM   1369  C  CA  . GLY B  1 43  ? 63.286  73.444  70.004 1.00 17.89  ? 37  GLY B CA  1 
ATOM   1370  C  C   . GLY B  1 43  ? 64.593  72.759  69.603 1.00 26.99  ? 37  GLY B C   1 
ATOM   1371  O  O   . GLY B  1 43  ? 64.921  71.696  70.142 1.00 25.24  ? 37  GLY B O   1 
ATOM   1372  N  N   . LEU B  1 44  ? 65.328  73.340  68.650 1.00 26.78  ? 38  LEU B N   1 
ATOM   1373  C  CA  . LEU B  1 44  ? 66.608  72.780  68.199 1.00 30.51  ? 38  LEU B CA  1 
ATOM   1374  C  C   . LEU B  1 44  ? 67.771  73.411  68.951 1.00 33.14  ? 38  LEU B C   1 
ATOM   1375  O  O   . LEU B  1 44  ? 67.711  74.572  69.339 1.00 35.67  ? 38  LEU B O   1 
ATOM   1376  C  CB  . LEU B  1 44  ? 66.831  73.047  66.714 1.00 26.40  ? 38  LEU B CB  1 
ATOM   1377  C  CG  . LEU B  1 44  ? 66.037  72.251  65.691 1.00 29.71  ? 38  LEU B CG  1 
ATOM   1378  C  CD1 . LEU B  1 44  ? 66.169  72.919  64.317 1.00 27.02  ? 38  LEU B CD1 1 
ATOM   1379  C  CD2 . LEU B  1 44  ? 66.559  70.813  65.658 1.00 22.74  ? 38  LEU B CD2 1 
ATOM   1380  N  N   . THR B  1 45  ? 68.832  72.643  69.154 1.00 31.26  ? 39  THR B N   1 
ATOM   1381  C  CA  . THR B  1 45  ? 70.018  73.163  69.823 1.00 28.38  ? 39  THR B CA  1 
ATOM   1382  C  C   . THR B  1 45  ? 70.730  74.107  68.840 1.00 23.77  ? 39  THR B C   1 
ATOM   1383  O  O   . THR B  1 45  ? 70.754  73.884  67.621 1.00 23.79  ? 39  THR B O   1 
ATOM   1384  C  CB  . THR B  1 45  ? 70.972  72.020  70.228 1.00 29.69  ? 39  THR B CB  1 
ATOM   1385  O  OG1 . THR B  1 45  ? 71.465  71.350  69.056 1.00 36.11  ? 39  THR B OG1 1 
ATOM   1386  C  CG2 . THR B  1 45  ? 70.237  71.019  71.074 1.00 28.67  ? 39  THR B CG2 1 
ATOM   1387  N  N   . GLU B  1 46  ? 71.290  75.179  69.363 1.00 22.18  ? 40  GLU B N   1 
ATOM   1388  C  CA  . GLU B  1 46  ? 71.976  76.131  68.508 1.00 28.80  ? 40  GLU B CA  1 
ATOM   1389  C  C   . GLU B  1 46  ? 73.019  75.399  67.677 1.00 23.52  ? 40  GLU B C   1 
ATOM   1390  O  O   . GLU B  1 46  ? 73.753  74.574  68.194 1.00 26.87  ? 40  GLU B O   1 
ATOM   1391  C  CB  . GLU B  1 46  ? 72.653  77.209  69.357 1.00 22.11  ? 40  GLU B CB  1 
ATOM   1392  C  CG  . GLU B  1 46  ? 73.376  78.266  68.556 1.00 25.97  ? 40  GLU B CG  1 
ATOM   1393  C  CD  . GLU B  1 46  ? 73.876  79.384  69.426 1.00 32.04  ? 40  GLU B CD  1 
ATOM   1394  O  OE1 . GLU B  1 46  ? 74.408  80.370  68.879 1.00 35.96  ? 40  GLU B OE1 1 
ATOM   1395  O  OE2 . GLU B  1 46  ? 73.736  79.270  70.665 1.00 42.66  ? 40  GLU B OE2 1 
ATOM   1396  N  N   . GLY B  1 47  ? 73.083  75.704  66.391 1.00 24.19  ? 41  GLY B N   1 
ATOM   1397  C  CA  . GLY B  1 47  ? 74.057  75.049  65.541 1.00 24.39  ? 41  GLY B CA  1 
ATOM   1398  C  C   . GLY B  1 47  ? 73.435  74.425  64.308 1.00 28.77  ? 41  GLY B C   1 
ATOM   1399  O  O   . GLY B  1 47  ? 72.269  74.673  63.998 1.00 27.92  ? 41  GLY B O   1 
ATOM   1400  N  N   . LEU B  1 48  ? 74.225  73.605  63.622 1.00 27.59  ? 42  LEU B N   1 
ATOM   1401  C  CA  . LEU B  1 48  ? 73.814  72.935  62.404 1.00 23.52  ? 42  LEU B CA  1 
ATOM   1402  C  C   . LEU B  1 48  ? 73.097  71.609  62.615 1.00 25.76  ? 42  LEU B C   1 
ATOM   1403  O  O   . LEU B  1 48  ? 73.468  70.838  63.487 1.00 29.93  ? 42  LEU B O   1 
ATOM   1404  C  CB  . LEU B  1 48  ? 75.039  72.686  61.542 1.00 24.03  ? 42  LEU B CB  1 
ATOM   1405  C  CG  . LEU B  1 48  ? 75.767  73.921  61.026 1.00 29.09  ? 42  LEU B CG  1 
ATOM   1406  C  CD1 . LEU B  1 48  ? 77.042  73.476  60.322 1.00 31.60  ? 42  LEU B CD1 1 
ATOM   1407  C  CD2 . LEU B  1 48  ? 74.881  74.698  60.062 1.00 36.03  ? 42  LEU B CD2 1 
ATOM   1408  N  N   . HIS B  1 49  ? 72.079  71.351  61.793 1.00 21.59  ? 43  HIS B N   1 
ATOM   1409  C  CA  . HIS B  1 49  ? 71.303  70.109  61.840 1.00 18.36  ? 43  HIS B CA  1 
ATOM   1410  C  C   . HIS B  1 49  ? 71.044  69.558  60.434 1.00 20.56  ? 43  HIS B C   1 
ATOM   1411  O  O   . HIS B  1 49  ? 70.602  70.285  59.546 1.00 20.15  ? 43  HIS B O   1 
ATOM   1412  C  CB  . HIS B  1 49  ? 69.972  70.353  62.528 1.00 14.30  ? 43  HIS B CB  1 
ATOM   1413  C  CG  . HIS B  1 49  ? 70.104  70.712  63.974 1.00 23.73  ? 43  HIS B CG  1 
ATOM   1414  N  ND1 . HIS B  1 49  ? 70.213  69.764  64.972 1.00 22.97  ? 43  HIS B ND1 1 
ATOM   1415  C  CD2 . HIS B  1 49  ? 70.155  71.915  64.589 1.00 19.88  ? 43  HIS B CD2 1 
ATOM   1416  C  CE1 . HIS B  1 49  ? 70.322  70.370  66.141 1.00 19.93  ? 43  HIS B CE1 1 
ATOM   1417  N  NE2 . HIS B  1 49  ? 70.291  71.675  65.936 1.00 30.18  ? 43  HIS B NE2 1 
ATOM   1418  N  N   . GLY B  1 50  ? 71.351  68.279  60.232 1.00 22.09  ? 44  GLY B N   1 
ATOM   1419  C  CA  . GLY B  1 50  ? 71.111  67.652  58.946 1.00 21.60  ? 44  GLY B CA  1 
ATOM   1420  C  C   . GLY B  1 50  ? 69.642  67.826  58.601 1.00 20.29  ? 44  GLY B C   1 
ATOM   1421  O  O   . GLY B  1 50  ? 68.780  67.723  59.465 1.00 23.27  ? 44  GLY B O   1 
ATOM   1422  N  N   . PHE B  1 51  ? 69.357  68.061  57.329 1.00 17.15  ? 45  PHE B N   1 
ATOM   1423  C  CA  . PHE B  1 51  ? 67.993  68.299  56.860 1.00 23.99  ? 45  PHE B CA  1 
ATOM   1424  C  C   . PHE B  1 51  ? 67.835  67.452  55.591 1.00 22.93  ? 45  PHE B C   1 
ATOM   1425  O  O   . PHE B  1 51  ? 68.437  67.757  54.565 1.00 24.65  ? 45  PHE B O   1 
ATOM   1426  C  CB  . PHE B  1 51  ? 67.875  69.793  56.552 1.00 15.20  ? 45  PHE B CB  1 
ATOM   1427  C  CG  . PHE B  1 51  ? 66.480  70.292  56.344 1.00 17.20  ? 45  PHE B CG  1 
ATOM   1428  C  CD1 . PHE B  1 51  ? 65.546  70.257  57.377 1.00 17.85  ? 45  PHE B CD1 1 
ATOM   1429  C  CD2 . PHE B  1 51  ? 66.131  70.913  55.147 1.00 15.77  ? 45  PHE B CD2 1 
ATOM   1430  C  CE1 . PHE B  1 51  ? 64.292  70.839  57.222 1.00 16.70  ? 45  PHE B CE1 1 
ATOM   1431  C  CE2 . PHE B  1 51  ? 64.867  71.504  54.979 1.00 21.06  ? 45  PHE B CE2 1 
ATOM   1432  C  CZ  . PHE B  1 51  ? 63.952  71.467  56.013 1.00 15.02  ? 45  PHE B CZ  1 
ATOM   1433  N  N   . HIS B  1 52  ? 67.037  66.390  55.650 1.00 19.21  ? 46  HIS B N   1 
ATOM   1434  C  CA  . HIS B  1 52  ? 66.889  65.544  54.468 1.00 22.53  ? 46  HIS B CA  1 
ATOM   1435  C  C   . HIS B  1 52  ? 65.492  65.033  54.179 1.00 22.73  ? 46  HIS B C   1 
ATOM   1436  O  O   . HIS B  1 52  ? 64.645  64.941  55.074 1.00 17.21  ? 46  HIS B O   1 
ATOM   1437  C  CB  . HIS B  1 52  ? 67.789  64.305  54.571 1.00 19.43  ? 46  HIS B CB  1 
ATOM   1438  C  CG  . HIS B  1 52  ? 69.124  64.565  55.203 1.00 28.19  ? 46  HIS B CG  1 
ATOM   1439  N  ND1 . HIS B  1 52  ? 69.406  64.222  56.507 1.00 29.80  ? 46  HIS B ND1 1 
ATOM   1440  C  CD2 . HIS B  1 52  ? 70.255  65.125  54.707 1.00 17.80  ? 46  HIS B CD2 1 
ATOM   1441  C  CE1 . HIS B  1 52  ? 70.654  64.557  56.788 1.00 22.92  ? 46  HIS B CE1 1 
ATOM   1442  N  NE2 . HIS B  1 52  ? 71.191  65.106  55.712 1.00 26.03  ? 46  HIS B NE2 1 
ATOM   1443  N  N   . VAL B  1 53  ? 65.265  64.700  52.908 1.00 15.18  ? 47  VAL B N   1 
ATOM   1444  C  CA  . VAL B  1 53  ? 64.013  64.097  52.520 1.00 13.49  ? 47  VAL B CA  1 
ATOM   1445  C  C   . VAL B  1 53  ? 64.388  62.611  52.545 1.00 18.52  ? 47  VAL B C   1 
ATOM   1446  O  O   . VAL B  1 53  ? 65.352  62.199  51.903 1.00 16.86  ? 47  VAL B O   1 
ATOM   1447  C  CB  . VAL B  1 53  ? 63.578  64.494  51.101 1.00 22.16  ? 47  VAL B CB  1 
ATOM   1448  C  CG1 . VAL B  1 53  ? 62.295  63.745  50.726 1.00 8.29   ? 47  VAL B CG1 1 
ATOM   1449  C  CG2 . VAL B  1 53  ? 63.329  65.976  51.036 1.00 10.50  ? 47  VAL B CG2 1 
ATOM   1450  N  N   . HIS B  1 54  ? 63.666  61.814  53.322 1.00 15.17  ? 48  HIS B N   1 
ATOM   1451  C  CA  . HIS B  1 54  ? 63.963  60.396  53.397 1.00 19.96  ? 48  HIS B CA  1 
ATOM   1452  C  C   . HIS B  1 54  ? 62.962  59.695  52.490 1.00 25.91  ? 48  HIS B C   1 
ATOM   1453  O  O   . HIS B  1 54  ? 61.913  60.253  52.165 1.00 20.39  ? 48  HIS B O   1 
ATOM   1454  C  CB  . HIS B  1 54  ? 63.878  59.891  54.852 1.00 19.54  ? 48  HIS B CB  1 
ATOM   1455  C  CG  . HIS B  1 54  ? 65.038  60.309  55.709 1.00 18.42  ? 48  HIS B CG  1 
ATOM   1456  N  ND1 . HIS B  1 54  ? 65.835  59.403  56.376 1.00 23.74  ? 48  HIS B ND1 1 
ATOM   1457  C  CD2 . HIS B  1 54  ? 65.506  61.536  56.047 1.00 25.00  ? 48  HIS B CD2 1 
ATOM   1458  C  CE1 . HIS B  1 54  ? 66.739  60.052  57.091 1.00 25.07  ? 48  HIS B CE1 1 
ATOM   1459  N  NE2 . HIS B  1 54  ? 66.561  61.349  56.913 1.00 19.02  ? 48  HIS B NE2 1 
ATOM   1460  N  N   . GLU B  1 55  ? 63.286  58.463  52.110 1.00 23.30  ? 49  GLU B N   1 
ATOM   1461  C  CA  . GLU B  1 55  ? 62.485  57.696  51.187 1.00 23.17  ? 49  GLU B CA  1 
ATOM   1462  C  C   . GLU B  1 55  ? 61.005  57.425  51.382 1.00 23.52  ? 49  GLU B C   1 
ATOM   1463  O  O   . GLU B  1 55  ? 60.248  57.605  50.440 1.00 19.83  ? 49  GLU B O   1 
ATOM   1464  C  CB  . GLU B  1 55  ? 63.167  56.354  50.902 1.00 28.26  ? 49  GLU B CB  1 
ATOM   1465  C  CG  . GLU B  1 55  ? 62.609  55.709  49.640 1.00 29.56  ? 49  GLU B CG  1 
ATOM   1466  C  CD  . GLU B  1 55  ? 63.230  54.379  49.308 1.00 33.50  ? 49  GLU B CD  1 
ATOM   1467  O  OE1 . GLU B  1 55  ? 62.880  53.824  48.240 1.00 32.67  ? 49  GLU B OE1 1 
ATOM   1468  O  OE2 . GLU B  1 55  ? 64.053  53.885  50.109 1.00 31.52  ? 49  GLU B OE2 1 
ATOM   1469  N  N   . PHE B  1 56  ? 60.583  56.981  52.565 1.00 24.87  ? 50  PHE B N   1 
ATOM   1470  C  CA  . PHE B  1 56  ? 59.168  56.636  52.780 1.00 20.12  ? 50  PHE B CA  1 
ATOM   1471  C  C   . PHE B  1 56  ? 58.357  57.581  53.646 1.00 23.85  ? 50  PHE B C   1 
ATOM   1472  O  O   . PHE B  1 56  ? 58.849  58.114  54.641 1.00 25.65  ? 50  PHE B O   1 
ATOM   1473  C  CB  . PHE B  1 56  ? 59.048  55.223  53.395 1.00 22.70  ? 50  PHE B CB  1 
ATOM   1474  C  CG  . PHE B  1 56  ? 59.776  54.154  52.619 1.00 26.01  ? 50  PHE B CG  1 
ATOM   1475  C  CD1 . PHE B  1 56  ? 59.364  53.803  51.337 1.00 17.56  ? 50  PHE B CD1 1 
ATOM   1476  C  CD2 . PHE B  1 56  ? 60.923  53.552  53.146 1.00 27.93  ? 50  PHE B CD2 1 
ATOM   1477  C  CE1 . PHE B  1 56  ? 60.092  52.863  50.568 1.00 23.61  ? 50  PHE B CE1 1 
ATOM   1478  C  CE2 . PHE B  1 56  ? 61.658  52.619  52.401 1.00 32.76  ? 50  PHE B CE2 1 
ATOM   1479  C  CZ  . PHE B  1 56  ? 61.243  52.272  51.101 1.00 26.27  ? 50  PHE B CZ  1 
ATOM   1480  N  N   . GLY B  1 57  ? 57.099  57.770  53.264 1.00 22.50  ? 51  GLY B N   1 
ATOM   1481  C  CA  . GLY B  1 57  ? 56.212  58.611  54.043 1.00 25.24  ? 51  GLY B CA  1 
ATOM   1482  C  C   . GLY B  1 57  ? 55.555  57.715  55.078 1.00 24.62  ? 51  GLY B C   1 
ATOM   1483  O  O   . GLY B  1 57  ? 54.340  57.734  55.247 1.00 22.45  ? 51  GLY B O   1 
ATOM   1484  N  N   . ASP B  1 58  ? 56.373  56.924  55.767 1.00 21.38  ? 52  ASP B N   1 
ATOM   1485  C  CA  . ASP B  1 58  ? 55.883  55.973  56.764 1.00 23.70  ? 52  ASP B CA  1 
ATOM   1486  C  C   . ASP B  1 58  ? 56.266  56.373  58.185 1.00 20.38  ? 52  ASP B C   1 
ATOM   1487  O  O   . ASP B  1 58  ? 57.434  56.291  58.578 1.00 20.30  ? 52  ASP B O   1 
ATOM   1488  C  CB  . ASP B  1 58  ? 56.431  54.571  56.439 1.00 19.78  ? 52  ASP B CB  1 
ATOM   1489  C  CG  . ASP B  1 58  ? 55.860  53.479  57.346 1.00 29.79  ? 52  ASP B CG  1 
ATOM   1490  O  OD1 . ASP B  1 58  ? 55.934  52.308  56.930 1.00 33.98  ? 52  ASP B OD1 1 
ATOM   1491  O  OD2 . ASP B  1 58  ? 55.352  53.769  58.461 1.00 27.81  ? 52  ASP B OD2 1 
ATOM   1492  N  N   . ASN B  1 59  ? 55.265  56.781  58.952 1.00 21.81  ? 53  ASN B N   1 
ATOM   1493  C  CA  . ASN B  1 59  ? 55.476  57.214  60.326 1.00 31.95  ? 53  ASN B CA  1 
ATOM   1494  C  C   . ASN B  1 59  ? 54.962  56.193  61.341 1.00 33.20  ? 53  ASN B C   1 
ATOM   1495  O  O   . ASN B  1 59  ? 54.773  56.533  62.502 1.00 26.18  ? 53  ASN B O   1 
ATOM   1496  C  CB  . ASN B  1 59  ? 54.767  58.552  60.557 1.00 38.21  ? 53  ASN B CB  1 
ATOM   1497  C  CG  . ASN B  1 59  ? 55.060  59.146  61.932 1.00 58.13  ? 53  ASN B CG  1 
ATOM   1498  O  OD1 . ASN B  1 59  ? 54.136  59.488  62.686 1.00 62.66  ? 53  ASN B OD1 1 
ATOM   1499  N  ND2 . ASN B  1 59  ? 56.346  59.279  62.262 1.00 56.46  ? 53  ASN B ND2 1 
ATOM   1500  N  N   . THR B  1 60  ? 54.733  54.950  60.919 1.00 26.52  ? 54  THR B N   1 
ATOM   1501  C  CA  . THR B  1 60  ? 54.225  53.948  61.848 1.00 27.49  ? 54  THR B CA  1 
ATOM   1502  C  C   . THR B  1 60  ? 55.128  53.694  63.052 1.00 30.00  ? 54  THR B C   1 
ATOM   1503  O  O   . THR B  1 60  ? 54.641  53.392  64.140 1.00 36.21  ? 54  THR B O   1 
ATOM   1504  C  CB  . THR B  1 60  ? 53.948  52.631  61.132 1.00 29.51  ? 54  THR B CB  1 
ATOM   1505  O  OG1 . THR B  1 60  ? 55.140  52.174  60.482 1.00 25.92  ? 54  THR B OG1 1 
ATOM   1506  C  CG2 . THR B  1 60  ? 52.831  52.834  60.105 1.00 17.06  ? 54  THR B CG2 1 
ATOM   1507  N  N   . ALA B  1 61  ? 56.437  53.816  62.864 1.00 25.76  ? 55  ALA B N   1 
ATOM   1508  C  CA  . ALA B  1 61  ? 57.390  53.627  63.956 1.00 27.31  ? 55  ALA B CA  1 
ATOM   1509  C  C   . ALA B  1 61  ? 58.139  54.939  64.123 1.00 27.53  ? 55  ALA B C   1 
ATOM   1510  O  O   . ALA B  1 61  ? 59.369  54.960  64.251 1.00 34.32  ? 55  ALA B O   1 
ATOM   1511  C  CB  . ALA B  1 61  ? 58.381  52.492  63.626 1.00 15.69  ? 55  ALA B CB  1 
ATOM   1512  N  N   . GLY B  1 62  ? 57.397  56.037  64.098 1.00 27.62  ? 56  GLY B N   1 
ATOM   1513  C  CA  . GLY B  1 62  ? 58.025  57.338  64.228 1.00 27.67  ? 56  GLY B CA  1 
ATOM   1514  C  C   . GLY B  1 62  ? 58.913  57.602  63.029 1.00 31.83  ? 56  GLY B C   1 
ATOM   1515  O  O   . GLY B  1 62  ? 58.679  57.052  61.944 1.00 35.19  ? 56  GLY B O   1 
ATOM   1516  N  N   . CYS B  1 63  ? 59.940  58.421  63.226 1.00 22.14  ? 57  CYS B N   1 
ATOM   1517  C  CA  . CYS B  1 63  ? 60.854  58.780  62.151 1.00 27.27  ? 57  CYS B CA  1 
ATOM   1518  C  C   . CYS B  1 63  ? 61.711  57.629  61.643 1.00 27.87  ? 57  CYS B C   1 
ATOM   1519  O  O   . CYS B  1 63  ? 62.254  57.694  60.538 1.00 24.21  ? 57  CYS B O   1 
ATOM   1520  C  CB  . CYS B  1 63  ? 61.754  59.944  62.590 1.00 23.57  ? 57  CYS B CB  1 
ATOM   1521  S  SG  . CYS B  1 63  ? 60.813  61.403  63.139 1.00 28.42  ? 57  CYS B SG  1 
ATOM   1522  N  N   . THR B  1 64  ? 61.814  56.573  62.437 1.00 26.96  ? 58  THR B N   1 
ATOM   1523  C  CA  . THR B  1 64  ? 62.618  55.413  62.064 1.00 25.83  ? 58  THR B CA  1 
ATOM   1524  C  C   . THR B  1 64  ? 62.082  54.709  60.815 1.00 28.02  ? 58  THR B C   1 
ATOM   1525  O  O   . THR B  1 64  ? 62.850  54.242  59.979 1.00 27.88  ? 58  THR B O   1 
ATOM   1526  C  CB  . THR B  1 64  ? 62.660  54.385  63.227 1.00 29.91  ? 58  THR B CB  1 
ATOM   1527  O  OG1 . THR B  1 64  ? 63.007  55.053  64.443 1.00 40.39  ? 58  THR B OG1 1 
ATOM   1528  C  CG2 . THR B  1 64  ? 63.689  53.322  62.967 1.00 28.14  ? 58  THR B CG2 1 
ATOM   1529  N  N   . SER B  1 65  ? 60.761  54.646  60.675 1.00 28.75  ? 59  SER B N   1 
ATOM   1530  C  CA  . SER B  1 65  ? 60.164  53.958  59.532 1.00 28.55  ? 59  SER B CA  1 
ATOM   1531  C  C   . SER B  1 65  ? 60.207  54.724  58.223 1.00 28.85  ? 59  SER B C   1 
ATOM   1532  O  O   . SER B  1 65  ? 59.675  54.260  57.206 1.00 28.28  ? 59  SER B O   1 
ATOM   1533  C  CB  . SER B  1 65  ? 58.720  53.560  59.857 1.00 23.20  ? 59  SER B CB  1 
ATOM   1534  O  OG  . SER B  1 65  ? 58.097  54.528  60.678 1.00 34.09  ? 59  SER B OG  1 
ATOM   1535  N  N   . ALA B  1 66  ? 60.851  55.889  58.249 1.00 26.65  ? 60  ALA B N   1 
ATOM   1536  C  CA  . ALA B  1 66  ? 60.979  56.736  57.065 1.00 17.63  ? 60  ALA B CA  1 
ATOM   1537  C  C   . ALA B  1 66  ? 62.023  56.186  56.095 1.00 18.78  ? 60  ALA B C   1 
ATOM   1538  O  O   . ALA B  1 66  ? 62.097  56.605  54.936 1.00 12.55  ? 60  ALA B O   1 
ATOM   1539  C  CB  . ALA B  1 66  ? 61.360  58.124  57.477 1.00 12.14  ? 60  ALA B CB  1 
ATOM   1540  N  N   . GLY B  1 67  ? 62.826  55.242  56.568 1.00 20.54  ? 61  GLY B N   1 
ATOM   1541  C  CA  . GLY B  1 67  ? 63.860  54.683  55.715 1.00 24.10  ? 61  GLY B CA  1 
ATOM   1542  C  C   . GLY B  1 67  ? 65.044  55.623  55.552 1.00 26.74  ? 61  GLY B C   1 
ATOM   1543  O  O   . GLY B  1 67  ? 65.199  56.591  56.312 1.00 29.13  ? 61  GLY B O   1 
ATOM   1544  N  N   . PRO B  1 68  ? 65.902  55.374  54.555 1.00 24.23  ? 62  PRO B N   1 
ATOM   1545  C  CA  . PRO B  1 68  ? 67.075  56.218  54.323 1.00 20.79  ? 62  PRO B CA  1 
ATOM   1546  C  C   . PRO B  1 68  ? 66.770  57.461  53.509 1.00 24.14  ? 62  PRO B C   1 
ATOM   1547  O  O   . PRO B  1 68  ? 65.606  57.741  53.206 1.00 20.56  ? 62  PRO B O   1 
ATOM   1548  C  CB  . PRO B  1 68  ? 68.011  55.286  53.579 1.00 17.94  ? 62  PRO B CB  1 
ATOM   1549  C  CG  . PRO B  1 68  ? 67.071  54.569  52.682 1.00 25.33  ? 62  PRO B CG  1 
ATOM   1550  C  CD  . PRO B  1 68  ? 65.913  54.218  53.641 1.00 25.27  ? 62  PRO B CD  1 
ATOM   1551  N  N   . HIS B  1 69  ? 67.825  58.210  53.185 1.00 18.06  ? 63  HIS B N   1 
ATOM   1552  C  CA  . HIS B  1 69  ? 67.692  59.407  52.371 1.00 25.08  ? 63  HIS B CA  1 
ATOM   1553  C  C   . HIS B  1 69  ? 67.110  58.956  51.034 1.00 27.10  ? 63  HIS B C   1 
ATOM   1554  O  O   . HIS B  1 69  ? 67.512  57.914  50.492 1.00 20.55  ? 63  HIS B O   1 
ATOM   1555  C  CB  . HIS B  1 69  ? 69.070  60.055  52.126 1.00 19.03  ? 63  HIS B CB  1 
ATOM   1556  C  CG  . HIS B  1 69  ? 69.727  60.575  53.369 1.00 25.75  ? 63  HIS B CG  1 
ATOM   1557  N  ND1 . HIS B  1 69  ? 70.985  61.139  53.369 1.00 21.68  ? 63  HIS B ND1 1 
ATOM   1558  C  CD2 . HIS B  1 69  ? 69.299  60.617  54.654 1.00 17.10  ? 63  HIS B CD2 1 
ATOM   1559  C  CE1 . HIS B  1 69  ? 71.304  61.506  54.598 1.00 9.88   ? 63  HIS B CE1 1 
ATOM   1560  N  NE2 . HIS B  1 69  ? 70.298  61.202  55.396 1.00 17.77  ? 63  HIS B NE2 1 
ATOM   1561  N  N   . PHE B  1 70  ? 66.147  59.719  50.526 1.00 21.88  ? 64  PHE B N   1 
ATOM   1562  C  CA  . PHE B  1 70  ? 65.531  59.425  49.237 1.00 22.50  ? 64  PHE B CA  1 
ATOM   1563  C  C   . PHE B  1 70  ? 66.697  59.398  48.243 1.00 22.46  ? 64  PHE B C   1 
ATOM   1564  O  O   . PHE B  1 70  ? 67.362  60.413  48.038 1.00 20.98  ? 64  PHE B O   1 
ATOM   1565  C  CB  . PHE B  1 70  ? 64.566  60.551  48.889 1.00 23.40  ? 64  PHE B CB  1 
ATOM   1566  C  CG  . PHE B  1 70  ? 63.868  60.368  47.582 1.00 25.22  ? 64  PHE B CG  1 
ATOM   1567  C  CD1 . PHE B  1 70  ? 63.503  61.475  46.819 1.00 18.90  ? 64  PHE B CD1 1 
ATOM   1568  C  CD2 . PHE B  1 70  ? 63.566  59.093  47.108 1.00 23.71  ? 64  PHE B CD2 1 
ATOM   1569  C  CE1 . PHE B  1 70  ? 62.844  61.314  45.586 1.00 21.45  ? 64  PHE B CE1 1 
ATOM   1570  C  CE2 . PHE B  1 70  ? 62.914  58.927  45.882 1.00 25.00  ? 64  PHE B CE2 1 
ATOM   1571  C  CZ  . PHE B  1 70  ? 62.554  60.042  45.122 1.00 17.34  ? 64  PHE B CZ  1 
ATOM   1572  N  N   . ASN B  1 71  ? 66.944  58.253  47.620 1.00 25.79  ? 65  ASN B N   1 
ATOM   1573  C  CA  . ASN B  1 71  ? 68.086  58.122  46.713 1.00 24.93  ? 65  ASN B CA  1 
ATOM   1574  C  C   . ASN B  1 71  ? 67.742  57.403  45.392 1.00 28.32  ? 65  ASN B C   1 
ATOM   1575  O  O   . ASN B  1 71  ? 68.341  56.391  45.043 1.00 27.10  ? 65  ASN B O   1 
ATOM   1576  C  CB  . ASN B  1 71  ? 69.174  57.367  47.477 1.00 24.57  ? 65  ASN B CB  1 
ATOM   1577  C  CG  . ASN B  1 71  ? 70.486  57.279  46.718 1.00 30.80  ? 65  ASN B CG  1 
ATOM   1578  O  OD1 . ASN B  1 71  ? 70.784  58.107  45.855 1.00 27.96  ? 65  ASN B OD1 1 
ATOM   1579  N  ND2 . ASN B  1 71  ? 71.286  56.280  47.056 1.00 24.83  ? 65  ASN B ND2 1 
ATOM   1580  N  N   . PRO B  1 72  ? 66.796  57.945  44.620 1.00 24.39  ? 66  PRO B N   1 
ATOM   1581  C  CA  . PRO B  1 72  ? 66.432  57.278  43.368 1.00 25.00  ? 66  PRO B CA  1 
ATOM   1582  C  C   . PRO B  1 72  ? 67.517  56.969  42.346 1.00 29.00  ? 66  PRO B C   1 
ATOM   1583  O  O   . PRO B  1 72  ? 67.316  56.106  41.514 1.00 26.44  ? 66  PRO B O   1 
ATOM   1584  C  CB  . PRO B  1 72  ? 65.347  58.175  42.801 1.00 22.39  ? 66  PRO B CB  1 
ATOM   1585  C  CG  . PRO B  1 72  ? 65.722  59.527  43.310 1.00 29.41  ? 66  PRO B CG  1 
ATOM   1586  C  CD  . PRO B  1 72  ? 66.122  59.248  44.743 1.00 17.97  ? 66  PRO B CD  1 
ATOM   1587  N  N   . LEU B  1 73  ? 68.661  57.645  42.402 1.00 30.12  ? 67  LEU B N   1 
ATOM   1588  C  CA  . LEU B  1 73  ? 69.722  57.388  41.421 1.00 23.24  ? 67  LEU B CA  1 
ATOM   1589  C  C   . LEU B  1 73  ? 70.873  56.619  42.025 1.00 29.16  ? 67  LEU B C   1 
ATOM   1590  O  O   . LEU B  1 73  ? 71.969  56.595  41.473 1.00 26.85  ? 67  LEU B O   1 
ATOM   1591  C  CB  . LEU B  1 73  ? 70.232  58.704  40.836 1.00 19.51  ? 67  LEU B CB  1 
ATOM   1592  C  CG  . LEU B  1 73  ? 69.113  59.376  40.042 1.00 36.34  ? 67  LEU B CG  1 
ATOM   1593  C  CD1 . LEU B  1 73  ? 69.437  60.823  39.781 1.00 22.36  ? 67  LEU B CD1 1 
ATOM   1594  C  CD2 . LEU B  1 73  ? 68.885  58.582  38.740 1.00 32.89  ? 67  LEU B CD2 1 
ATOM   1595  N  N   . SER B  1 74  ? 70.624  56.017  43.183 1.00 31.93  ? 68  SER B N   1 
ATOM   1596  C  CA  . SER B  1 74  ? 71.633  55.229  43.867 1.00 35.36  ? 68  SER B CA  1 
ATOM   1597  C  C   . SER B  1 74  ? 73.006  55.886  43.876 1.00 33.98  ? 68  SER B C   1 
ATOM   1598  O  O   . SER B  1 74  ? 73.976  55.304  43.410 1.00 31.59  ? 68  SER B O   1 
ATOM   1599  C  CB  . SER B  1 74  ? 71.738  53.855  43.206 1.00 37.46  ? 68  SER B CB  1 
ATOM   1600  O  OG  . SER B  1 74  ? 70.523  53.146  43.338 1.00 46.04  ? 68  SER B OG  1 
ATOM   1601  N  N   . ARG B  1 75  ? 73.093  57.103  44.388 1.00 31.23  ? 69  ARG B N   1 
ATOM   1602  C  CA  . ARG B  1 75  ? 74.376  57.774  44.452 1.00 29.94  ? 69  ARG B CA  1 
ATOM   1603  C  C   . ARG B  1 75  ? 74.816  57.872  45.906 1.00 29.15  ? 69  ARG B C   1 
ATOM   1604  O  O   . ARG B  1 75  ? 74.072  57.482  46.811 1.00 28.21  ? 69  ARG B O   1 
ATOM   1605  C  CB  . ARG B  1 75  ? 74.273  59.145  43.794 1.00 30.77  ? 69  ARG B CB  1 
ATOM   1606  C  CG  . ARG B  1 75  ? 74.262  59.052  42.268 1.00 40.81  ? 69  ARG B CG  1 
ATOM   1607  C  CD  . ARG B  1 75  ? 74.107  60.415  41.650 1.00 58.92  ? 69  ARG B CD  1 
ATOM   1608  N  NE  . ARG B  1 75  ? 74.033  60.349  40.197 1.00 70.17  ? 69  ARG B NE  1 
ATOM   1609  C  CZ  . ARG B  1 75  ? 73.532  61.316  39.433 1.00 73.77  ? 69  ARG B CZ  1 
ATOM   1610  N  NH1 . ARG B  1 75  ? 73.059  62.426  39.986 1.00 76.68  ? 69  ARG B NH1 1 
ATOM   1611  N  NH2 . ARG B  1 75  ? 73.499  61.173  38.115 1.00 74.39  ? 69  ARG B NH2 1 
ATOM   1612  N  N   . LYS B  1 76  ? 76.031  58.356  46.137 1.00 31.65  ? 70  LYS B N   1 
ATOM   1613  C  CA  . LYS B  1 76  ? 76.539  58.484  47.501 1.00 29.61  ? 70  LYS B CA  1 
ATOM   1614  C  C   . LYS B  1 76  ? 76.045  59.773  48.116 1.00 28.38  ? 70  LYS B C   1 
ATOM   1615  O  O   . LYS B  1 76  ? 75.740  60.738  47.403 1.00 26.20  ? 70  LYS B O   1 
ATOM   1616  C  CB  . LYS B  1 76  ? 78.067  58.484  47.528 1.00 35.92  ? 70  LYS B CB  1 
ATOM   1617  C  CG  . LYS B  1 76  ? 78.729  57.120  47.344 1.00 49.85  ? 70  LYS B CG  1 
ATOM   1618  C  CD  . LYS B  1 76  ? 80.252  57.259  47.453 1.00 61.34  ? 70  LYS B CD  1 
ATOM   1619  C  CE  . LYS B  1 76  ? 80.978  55.922  47.325 1.00 74.97  ? 70  LYS B CE  1 
ATOM   1620  N  NZ  . LYS B  1 76  ? 82.455  56.066  47.578 1.00 83.91  ? 70  LYS B NZ  1 
ATOM   1621  N  N   . HIS B  1 77  ? 75.972  59.791  49.445 1.00 21.21  ? 71  HIS B N   1 
ATOM   1622  C  CA  . HIS B  1 77  ? 75.523  60.973  50.159 1.00 19.26  ? 71  HIS B CA  1 
ATOM   1623  C  C   . HIS B  1 77  ? 76.446  62.174  49.907 1.00 22.01  ? 71  HIS B C   1 
ATOM   1624  O  O   . HIS B  1 77  ? 77.665  62.027  49.894 1.00 24.44  ? 71  HIS B O   1 
ATOM   1625  C  CB  . HIS B  1 77  ? 75.476  60.694  51.656 1.00 17.17  ? 71  HIS B CB  1 
ATOM   1626  C  CG  . HIS B  1 77  ? 75.061  61.884  52.466 1.00 31.03  ? 71  HIS B CG  1 
ATOM   1627  N  ND1 . HIS B  1 77  ? 73.747  62.290  52.576 1.00 21.00  ? 71  HIS B ND1 1 
ATOM   1628  C  CD2 . HIS B  1 77  ? 75.795  62.797  53.145 1.00 19.40  ? 71  HIS B CD2 1 
ATOM   1629  C  CE1 . HIS B  1 77  ? 73.692  63.400  53.286 1.00 18.43  ? 71  HIS B CE1 1 
ATOM   1630  N  NE2 . HIS B  1 77  ? 74.921  63.730  53.641 1.00 24.16  ? 71  HIS B NE2 1 
ATOM   1631  N  N   . GLY B  1 78  ? 75.859  63.353  49.703 1.00 21.50  ? 72  GLY B N   1 
ATOM   1632  C  CA  . GLY B  1 78  ? 76.642  64.566  49.501 1.00 17.22  ? 72  GLY B CA  1 
ATOM   1633  C  C   . GLY B  1 78  ? 75.927  65.801  50.065 1.00 28.04  ? 72  GLY B C   1 
ATOM   1634  O  O   . GLY B  1 78  ? 74.890  65.689  50.748 1.00 16.89  ? 72  GLY B O   1 
ATOM   1635  N  N   . GLY B  1 79  ? 76.496  66.978  49.813 1.00 18.48  ? 73  GLY B N   1 
ATOM   1636  C  CA  . GLY B  1 79  ? 75.868  68.211  50.242 1.00 24.08  ? 73  GLY B CA  1 
ATOM   1637  C  C   . GLY B  1 79  ? 75.019  68.654  49.052 1.00 28.20  ? 73  GLY B C   1 
ATOM   1638  O  O   . GLY B  1 79  ? 75.257  68.195  47.931 1.00 23.68  ? 73  GLY B O   1 
ATOM   1639  N  N   . PRO B  1 80  ? 74.038  69.549  49.242 1.00 23.96  ? 74  PRO B N   1 
ATOM   1640  C  CA  . PRO B  1 80  ? 73.187  70.004  48.134 1.00 22.58  ? 74  PRO B CA  1 
ATOM   1641  C  C   . PRO B  1 80  ? 73.888  70.530  46.877 1.00 26.35  ? 74  PRO B C   1 
ATOM   1642  O  O   . PRO B  1 80  ? 73.427  70.281  45.760 1.00 19.85  ? 74  PRO B O   1 
ATOM   1643  C  CB  . PRO B  1 80  ? 72.280  71.051  48.791 1.00 13.70  ? 74  PRO B CB  1 
ATOM   1644  C  CG  . PRO B  1 80  ? 73.003  71.438  50.059 1.00 20.17  ? 74  PRO B CG  1 
ATOM   1645  C  CD  . PRO B  1 80  ? 73.617  70.151  50.516 1.00 25.32  ? 74  PRO B CD  1 
ATOM   1646  N  N   . LYS B  1 81  ? 74.994  71.252  47.050 1.00 25.24  ? 75  LYS B N   1 
ATOM   1647  C  CA  . LYS B  1 81  ? 75.731  71.793  45.909 1.00 24.45  ? 75  LYS B CA  1 
ATOM   1648  C  C   . LYS B  1 81  ? 76.479  70.739  45.066 1.00 23.63  ? 75  LYS B C   1 
ATOM   1649  O  O   . LYS B  1 81  ? 76.755  70.988  43.910 1.00 29.55  ? 75  LYS B O   1 
ATOM   1650  C  CB  . LYS B  1 81  ? 76.718  72.860  46.387 1.00 27.09  ? 75  LYS B CB  1 
ATOM   1651  C  CG  . LYS B  1 81  ? 76.066  74.072  47.040 1.00 35.42  ? 75  LYS B CG  1 
ATOM   1652  C  CD  . LYS B  1 81  ? 77.013  74.792  47.995 1.00 45.58  ? 75  LYS B CD  1 
ATOM   1653  C  CE  . LYS B  1 81  ? 78.209  75.430  47.293 1.00 46.56  ? 75  LYS B CE  1 
ATOM   1654  N  NZ  . LYS B  1 81  ? 79.328  75.629  48.261 1.00 50.15  ? 75  LYS B NZ  1 
ATOM   1655  N  N   . ASP B  1 82  ? 76.785  69.578  45.650 1.00 22.71  ? 76  ASP B N   1 
ATOM   1656  C  CA  . ASP B  1 82  ? 77.506  68.466  44.992 1.00 29.07  ? 76  ASP B CA  1 
ATOM   1657  C  C   . ASP B  1 82  ? 76.764  67.768  43.850 1.00 30.35  ? 76  ASP B C   1 
ATOM   1658  O  O   . ASP B  1 82  ? 75.546  67.644  43.886 1.00 34.15  ? 76  ASP B O   1 
ATOM   1659  C  CB  . ASP B  1 82  ? 77.841  67.372  46.020 1.00 20.86  ? 76  ASP B CB  1 
ATOM   1660  C  CG  . ASP B  1 82  ? 78.887  67.800  47.037 1.00 29.76  ? 76  ASP B CG  1 
ATOM   1661  O  OD1 . ASP B  1 82  ? 78.922  67.200  48.137 1.00 31.13  ? 76  ASP B OD1 1 
ATOM   1662  O  OD2 . ASP B  1 82  ? 79.683  68.719  46.743 1.00 33.52  ? 76  ASP B OD2 1 
ATOM   1663  N  N   . GLU B  1 83  ? 77.495  67.289  42.843 1.00 38.94  ? 77  GLU B N   1 
ATOM   1664  C  CA  . GLU B  1 83  ? 76.846  66.564  41.751 1.00 36.87  ? 77  GLU B CA  1 
ATOM   1665  C  C   . GLU B  1 83  ? 76.532  65.168  42.274 1.00 33.27  ? 77  GLU B C   1 
ATOM   1666  O  O   . GLU B  1 83  ? 75.506  64.574  41.929 1.00 29.27  ? 77  GLU B O   1 
ATOM   1667  C  CB  . GLU B  1 83  ? 77.748  66.474  40.524 1.00 48.45  ? 77  GLU B CB  1 
ATOM   1668  C  CG  . GLU B  1 83  ? 77.286  65.437  39.497 1.00 67.94  ? 77  GLU B CG  1 
ATOM   1669  C  CD  . GLU B  1 83  ? 78.021  65.549  38.163 1.00 82.56  ? 77  GLU B CD  1 
ATOM   1670  O  OE1 . GLU B  1 83  ? 79.230  65.873  38.163 1.00 84.63  ? 77  GLU B OE1 1 
ATOM   1671  O  OE2 . GLU B  1 83  ? 77.391  65.300  37.111 1.00 89.69  ? 77  GLU B OE2 1 
ATOM   1672  N  N   . GLU B  1 84  ? 77.420  64.641  43.114 1.00 28.37  ? 78  GLU B N   1 
ATOM   1673  C  CA  . GLU B  1 84  ? 77.194  63.324  43.702 1.00 26.15  ? 78  GLU B CA  1 
ATOM   1674  C  C   . GLU B  1 84  ? 76.448  63.528  45.024 1.00 24.97  ? 78  GLU B C   1 
ATOM   1675  O  O   . GLU B  1 84  ? 77.020  63.966  46.022 1.00 19.25  ? 78  GLU B O   1 
ATOM   1676  C  CB  . GLU B  1 84  ? 78.527  62.604  43.958 1.00 23.97  ? 78  GLU B CB  1 
ATOM   1677  C  CG  . GLU B  1 84  ? 78.393  61.177  44.503 1.00 29.01  ? 78  GLU B CG  1 
ATOM   1678  C  CD  . GLU B  1 84  ? 77.860  60.188  43.457 1.00 42.93  ? 78  GLU B CD  1 
ATOM   1679  O  OE1 . GLU B  1 84  ? 77.713  58.976  43.779 1.00 27.65  ? 78  GLU B OE1 1 
ATOM   1680  O  OE2 . GLU B  1 84  ? 77.595  60.625  42.307 1.00 47.66  ? 78  GLU B OE2 1 
ATOM   1681  N  N   . ARG B  1 85  ? 75.163  63.220  45.027 1.00 26.05  ? 79  ARG B N   1 
ATOM   1682  C  CA  . ARG B  1 85  ? 74.373  63.368  46.233 1.00 24.86  ? 79  ARG B CA  1 
ATOM   1683  C  C   . ARG B  1 85  ? 73.035  62.675  46.059 1.00 26.11  ? 79  ARG B C   1 
ATOM   1684  O  O   . ARG B  1 85  ? 72.618  62.365  44.944 1.00 24.82  ? 79  ARG B O   1 
ATOM   1685  C  CB  . ARG B  1 85  ? 74.157  64.848  46.533 1.00 18.10  ? 79  ARG B CB  1 
ATOM   1686  C  CG  . ARG B  1 85  ? 73.522  65.596  45.370 1.00 21.41  ? 79  ARG B CG  1 
ATOM   1687  C  CD  . ARG B  1 85  ? 72.085  65.927  45.688 1.00 28.78  ? 79  ARG B CD  1 
ATOM   1688  N  NE  . ARG B  1 85  ? 71.858  67.362  45.628 1.00 27.65  ? 79  ARG B NE  1 
ATOM   1689  C  CZ  . ARG B  1 85  ? 70.744  67.979  46.012 1.00 22.88  ? 79  ARG B CZ  1 
ATOM   1690  N  NH1 . ARG B  1 85  ? 69.712  67.304  46.513 1.00 7.29   ? 79  ARG B NH1 1 
ATOM   1691  N  NH2 . ARG B  1 85  ? 70.663  69.291  45.855 1.00 16.92  ? 79  ARG B NH2 1 
ATOM   1692  N  N   . HIS B  1 86  ? 72.379  62.411  47.178 1.00 20.74  ? 80  HIS B N   1 
ATOM   1693  C  CA  . HIS B  1 86  ? 71.078  61.778  47.166 1.00 14.55  ? 80  HIS B CA  1 
ATOM   1694  C  C   . HIS B  1 86  ? 70.131  62.894  46.762 1.00 15.61  ? 80  HIS B C   1 
ATOM   1695  O  O   . HIS B  1 86  ? 70.422  64.072  47.006 1.00 15.06  ? 80  HIS B O   1 
ATOM   1696  C  CB  . HIS B  1 86  ? 70.730  61.311  48.579 1.00 9.29   ? 80  HIS B CB  1 
ATOM   1697  C  CG  . HIS B  1 86  ? 71.679  60.301  49.132 1.00 22.31  ? 80  HIS B CG  1 
ATOM   1698  N  ND1 . HIS B  1 86  ? 71.925  60.177  50.484 1.00 19.97  ? 80  HIS B ND1 1 
ATOM   1699  C  CD2 . HIS B  1 86  ? 72.363  59.296  48.530 1.00 21.04  ? 80  HIS B CD2 1 
ATOM   1700  C  CE1 . HIS B  1 86  ? 72.709  59.136  50.692 1.00 20.61  ? 80  HIS B CE1 1 
ATOM   1701  N  NE2 . HIS B  1 86  ? 72.988  58.582  49.523 1.00 23.89  ? 80  HIS B NE2 1 
ATOM   1702  N  N   . VAL B  1 87  ? 69.008  62.545  46.143 1.00 18.00  ? 81  VAL B N   1 
ATOM   1703  C  CA  . VAL B  1 87  ? 68.042  63.565  45.772 1.00 15.90  ? 81  VAL B CA  1 
ATOM   1704  C  C   . VAL B  1 87  ? 67.580  64.282  47.055 1.00 16.49  ? 81  VAL B C   1 
ATOM   1705  O  O   . VAL B  1 87  ? 67.392  65.482  47.063 1.00 15.25  ? 81  VAL B O   1 
ATOM   1706  C  CB  . VAL B  1 87  ? 66.831  62.934  45.044 1.00 18.60  ? 81  VAL B CB  1 
ATOM   1707  C  CG1 . VAL B  1 87  ? 65.652  63.917  45.001 1.00 12.71  ? 81  VAL B CG1 1 
ATOM   1708  C  CG2 . VAL B  1 87  ? 67.230  62.552  43.624 1.00 6.21   ? 81  VAL B CG2 1 
ATOM   1709  N  N   . GLY B  1 88  ? 67.433  63.548  48.151 1.00 14.67  ? 82  GLY B N   1 
ATOM   1710  C  CA  . GLY B  1 88  ? 66.980  64.184  49.377 1.00 23.54  ? 82  GLY B CA  1 
ATOM   1711  C  C   . GLY B  1 88  ? 67.992  64.934  50.227 1.00 20.91  ? 82  GLY B C   1 
ATOM   1712  O  O   . GLY B  1 88  ? 67.664  65.354  51.335 1.00 24.02  ? 82  GLY B O   1 
ATOM   1713  N  N   . ASP B  1 89  ? 69.206  65.118  49.729 1.00 19.78  ? 83  ASP B N   1 
ATOM   1714  C  CA  . ASP B  1 89  ? 70.250  65.806  50.497 1.00 18.09  ? 83  ASP B CA  1 
ATOM   1715  C  C   . ASP B  1 89  ? 70.150  67.326  50.423 1.00 18.85  ? 83  ASP B C   1 
ATOM   1716  O  O   . ASP B  1 89  ? 70.698  67.949  49.516 1.00 13.04  ? 83  ASP B O   1 
ATOM   1717  C  CB  . ASP B  1 89  ? 71.647  65.383  50.010 1.00 25.24  ? 83  ASP B CB  1 
ATOM   1718  C  CG  . ASP B  1 89  ? 71.964  63.923  50.306 1.00 28.05  ? 83  ASP B CG  1 
ATOM   1719  O  OD1 . ASP B  1 89  ? 71.253  63.315  51.129 1.00 28.99  ? 83  ASP B OD1 1 
ATOM   1720  O  OD2 . ASP B  1 89  ? 72.937  63.391  49.730 1.00 31.04  ? 83  ASP B OD2 1 
ATOM   1721  N  N   . LEU B  1 90  ? 69.469  67.924  51.396 1.00 17.72  ? 84  LEU B N   1 
ATOM   1722  C  CA  . LEU B  1 90  ? 69.309  69.368  51.430 1.00 16.99  ? 84  LEU B CA  1 
ATOM   1723  C  C   . LEU B  1 90  ? 70.332  70.058  52.352 1.00 23.62  ? 84  LEU B C   1 
ATOM   1724  O  O   . LEU B  1 90  ? 70.253  71.262  52.582 1.00 22.36  ? 84  LEU B O   1 
ATOM   1725  C  CB  . LEU B  1 90  ? 67.877  69.709  51.842 1.00 18.93  ? 84  LEU B CB  1 
ATOM   1726  C  CG  . LEU B  1 90  ? 66.814  69.139  50.892 1.00 16.97  ? 84  LEU B CG  1 
ATOM   1727  C  CD1 . LEU B  1 90  ? 65.432  69.538  51.364 1.00 14.41  ? 84  LEU B CD1 1 
ATOM   1728  C  CD2 . LEU B  1 90  ? 67.060  69.652  49.472 1.00 10.99  ? 84  LEU B CD2 1 
ATOM   1729  N  N   . GLY B  1 91  ? 71.302  69.298  52.858 1.00 21.26  ? 85  GLY B N   1 
ATOM   1730  C  CA  . GLY B  1 91  ? 72.329  69.865  53.725 1.00 21.44  ? 85  GLY B CA  1 
ATOM   1731  C  C   . GLY B  1 91  ? 71.930  70.102  55.175 1.00 23.46  ? 85  GLY B C   1 
ATOM   1732  O  O   . GLY B  1 91  ? 71.272  69.278  55.801 1.00 17.55  ? 85  GLY B O   1 
ATOM   1733  N  N   . ASN B  1 92  ? 72.336  71.247  55.708 1.00 21.57  ? 86  ASN B N   1 
ATOM   1734  C  CA  . ASN B  1 92  ? 72.038  71.620  57.077 1.00 17.22  ? 86  ASN B CA  1 
ATOM   1735  C  C   . ASN B  1 92  ? 71.111  72.823  57.152 1.00 23.66  ? 86  ASN B C   1 
ATOM   1736  O  O   . ASN B  1 92  ? 70.986  73.590  56.195 1.00 16.00  ? 86  ASN B O   1 
ATOM   1737  C  CB  . ASN B  1 92  ? 73.325  72.019  57.799 1.00 11.39  ? 86  ASN B CB  1 
ATOM   1738  C  CG  . ASN B  1 92  ? 74.276  70.874  57.959 1.00 23.81  ? 86  ASN B CG  1 
ATOM   1739  O  OD1 . ASN B  1 92  ? 73.955  69.887  58.619 1.00 19.34  ? 86  ASN B OD1 1 
ATOM   1740  N  ND2 . ASN B  1 92  ? 75.459  70.985  57.346 1.00 8.18   ? 86  ASN B ND2 1 
ATOM   1741  N  N   . VAL B  1 93  ? 70.470  72.976  58.307 1.00 15.41  ? 87  VAL B N   1 
ATOM   1742  C  CA  . VAL B  1 93  ? 69.658  74.144  58.591 1.00 17.24  ? 87  VAL B CA  1 
ATOM   1743  C  C   . VAL B  1 93  ? 70.350  74.641  59.870 1.00 23.75  ? 87  VAL B C   1 
ATOM   1744  O  O   . VAL B  1 93  ? 70.981  73.854  60.575 1.00 22.88  ? 87  VAL B O   1 
ATOM   1745  C  CB  . VAL B  1 93  ? 68.176  73.801  58.884 1.00 25.03  ? 87  VAL B CB  1 
ATOM   1746  C  CG1 . VAL B  1 93  ? 67.502  73.302  57.622 1.00 23.54  ? 87  VAL B CG1 1 
ATOM   1747  C  CG2 . VAL B  1 93  ? 68.071  72.779  60.018 1.00 20.93  ? 87  VAL B CG2 1 
ATOM   1748  N  N   . THR B  1 94  ? 70.252  75.930  60.172 1.00 24.65  ? 88  THR B N   1 
ATOM   1749  C  CA  . THR B  1 94  ? 70.902  76.471  61.356 1.00 16.76  ? 88  THR B CA  1 
ATOM   1750  C  C   . THR B  1 94  ? 69.921  77.015  62.394 1.00 21.69  ? 88  THR B C   1 
ATOM   1751  O  O   . THR B  1 94  ? 69.056  77.828  62.080 1.00 21.21  ? 88  THR B O   1 
ATOM   1752  C  CB  . THR B  1 94  ? 71.900  77.601  60.942 1.00 24.14  ? 88  THR B CB  1 
ATOM   1753  O  OG1 . THR B  1 94  ? 72.965  77.033  60.180 1.00 21.26  ? 88  THR B OG1 1 
ATOM   1754  C  CG2 . THR B  1 94  ? 72.505  78.296  62.161 1.00 21.15  ? 88  THR B CG2 1 
ATOM   1755  N  N   . ALA B  1 95  ? 70.043  76.554  63.633 1.00 20.73  ? 89  ALA B N   1 
ATOM   1756  C  CA  . ALA B  1 95  ? 69.185  77.059  64.710 1.00 17.74  ? 89  ALA B CA  1 
ATOM   1757  C  C   . ALA B  1 95  ? 69.962  78.171  65.423 1.00 20.72  ? 89  ALA B C   1 
ATOM   1758  O  O   . ALA B  1 95  ? 71.184  78.054  65.626 1.00 16.17  ? 89  ALA B O   1 
ATOM   1759  C  CB  . ALA B  1 95  ? 68.846  75.953  65.698 1.00 14.30  ? 89  ALA B CB  1 
ATOM   1760  N  N   . ASP B  1 96  ? 69.255  79.236  65.796 1.00 20.60  ? 90  ASP B N   1 
ATOM   1761  C  CA  . ASP B  1 96  ? 69.856  80.386  66.477 1.00 22.54  ? 90  ASP B CA  1 
ATOM   1762  C  C   . ASP B  1 96  ? 69.942  80.128  67.986 1.00 28.25  ? 90  ASP B C   1 
ATOM   1763  O  O   . ASP B  1 96  ? 69.515  79.071  68.456 1.00 31.04  ? 90  ASP B O   1 
ATOM   1764  C  CB  . ASP B  1 96  ? 69.031  81.655  66.165 1.00 19.63  ? 90  ASP B CB  1 
ATOM   1765  C  CG  . ASP B  1 96  ? 67.587  81.608  66.729 1.00 34.16  ? 90  ASP B CG  1 
ATOM   1766  O  OD1 . ASP B  1 96  ? 66.741  82.407  66.255 1.00 34.35  ? 90  ASP B OD1 1 
ATOM   1767  O  OD2 . ASP B  1 96  ? 67.290  80.804  67.651 1.00 29.78  ? 90  ASP B OD2 1 
ATOM   1768  N  N   . LYS B  1 97  ? 70.483  81.075  68.752 1.00 33.73  ? 91  LYS B N   1 
ATOM   1769  C  CA  . LYS B  1 97  ? 70.614  80.873  70.197 1.00 40.79  ? 91  LYS B CA  1 
ATOM   1770  C  C   . LYS B  1 97  ? 69.277  80.664  70.914 1.00 37.02  ? 91  LYS B C   1 
ATOM   1771  O  O   . LYS B  1 97  ? 69.245  80.213  72.054 1.00 28.78  ? 91  LYS B O   1 
ATOM   1772  C  CB  . LYS B  1 97  ? 71.371  82.033  70.846 1.00 47.50  ? 91  LYS B CB  1 
ATOM   1773  C  CG  . LYS B  1 97  ? 70.764  83.404  70.609 1.00 67.06  ? 91  LYS B CG  1 
ATOM   1774  C  CD  . LYS B  1 97  ? 71.594  84.492  71.290 1.00 76.27  ? 91  LYS B CD  1 
ATOM   1775  C  CE  . LYS B  1 97  ? 71.151  85.885  70.868 1.00 81.89  ? 91  LYS B CE  1 
ATOM   1776  N  NZ  . LYS B  1 97  ? 69.708  86.130  71.157 1.00 89.56  ? 91  LYS B NZ  1 
ATOM   1777  N  N   . ASP B  1 98  ? 68.183  80.986  70.239 1.00 28.84  ? 92  ASP B N   1 
ATOM   1778  C  CA  . ASP B  1 98  ? 66.855  80.813  70.808 1.00 30.81  ? 92  ASP B CA  1 
ATOM   1779  C  C   . ASP B  1 98  ? 66.246  79.467  70.431 1.00 30.76  ? 92  ASP B C   1 
ATOM   1780  O  O   . ASP B  1 98  ? 65.058  79.247  70.647 1.00 28.13  ? 92  ASP B O   1 
ATOM   1781  C  CB  . ASP B  1 98  ? 65.936  81.928  70.326 1.00 36.23  ? 92  ASP B CB  1 
ATOM   1782  C  CG  . ASP B  1 98  ? 66.306  83.284  70.910 1.00 50.96  ? 92  ASP B CG  1 
ATOM   1783  O  OD1 . ASP B  1 98  ? 66.065  84.302  70.225 1.00 54.43  ? 92  ASP B OD1 1 
ATOM   1784  O  OD2 . ASP B  1 98  ? 66.822  83.341  72.053 1.00 43.99  ? 92  ASP B OD2 1 
ATOM   1785  N  N   . ALA B  1 99  ? 67.053  78.579  69.852 1.00 23.15  ? 93  ALA B N   1 
ATOM   1786  C  CA  . ALA B  1 99  ? 66.580  77.258  69.449 1.00 20.73  ? 93  ALA B CA  1 
ATOM   1787  C  C   . ALA B  1 99  ? 65.613  77.253  68.240 1.00 21.09  ? 93  ALA B C   1 
ATOM   1788  O  O   . ALA B  1 99  ? 64.822  76.316  68.047 1.00 21.15  ? 93  ALA B O   1 
ATOM   1789  C  CB  . ALA B  1 99  ? 65.937  76.546  70.651 1.00 11.15  ? 93  ALA B CB  1 
ATOM   1790  N  N   . VAL B  1 100 ? 65.692  78.292  67.422 1.00 16.68  ? 94  VAL B N   1 
ATOM   1791  C  CA  . VAL B  1 100 ? 64.854  78.395  66.238 1.00 19.36  ? 94  VAL B CA  1 
ATOM   1792  C  C   . VAL B  1 100 ? 65.679  78.444  64.945 1.00 26.44  ? 94  VAL B C   1 
ATOM   1793  O  O   . VAL B  1 100 ? 66.648  79.231  64.839 1.00 16.83  ? 94  VAL B O   1 
ATOM   1794  C  CB  . VAL B  1 100 ? 64.013  79.686  66.224 1.00 18.61  ? 94  VAL B CB  1 
ATOM   1795  C  CG1 . VAL B  1 100 ? 63.245  79.781  64.878 1.00 19.92  ? 94  VAL B CG1 1 
ATOM   1796  C  CG2 . VAL B  1 100 ? 63.069  79.716  67.409 1.00 10.62  ? 94  VAL B CG2 1 
ATOM   1797  N  N   . ALA B  1 101 ? 65.287  77.620  63.972 1.00 15.55  ? 95  ALA B N   1 
ATOM   1798  C  CA  . ALA B  1 101 ? 65.935  77.627  62.674 1.00 20.81  ? 95  ALA B CA  1 
ATOM   1799  C  C   . ALA B  1 101 ? 64.939  78.197  61.684 1.00 26.00  ? 95  ALA B C   1 
ATOM   1800  O  O   . ALA B  1 101 ? 63.892  77.592  61.415 1.00 25.79  ? 95  ALA B O   1 
ATOM   1801  C  CB  . ALA B  1 101 ? 66.329  76.233  62.241 1.00 17.33  ? 95  ALA B CB  1 
ATOM   1802  N  N   . ASP B  1 102 ? 65.266  79.368  61.155 1.00 18.95  ? 96  ASP B N   1 
ATOM   1803  C  CA  . ASP B  1 102 ? 64.431  80.016  60.154 1.00 22.53  ? 96  ASP B CA  1 
ATOM   1804  C  C   . ASP B  1 102 ? 64.912  79.487  58.811 1.00 22.23  ? 96  ASP B C   1 
ATOM   1805  O  O   . ASP B  1 102 ? 65.700  80.120  58.123 1.00 34.93  ? 96  ASP B O   1 
ATOM   1806  C  CB  . ASP B  1 102 ? 64.606  81.535  60.232 1.00 20.51  ? 96  ASP B CB  1 
ATOM   1807  C  CG  . ASP B  1 102 ? 63.929  82.127  61.460 1.00 30.32  ? 96  ASP B CG  1 
ATOM   1808  O  OD1 . ASP B  1 102 ? 64.487  83.065  62.073 1.00 42.68  ? 96  ASP B OD1 1 
ATOM   1809  O  OD2 . ASP B  1 102 ? 62.829  81.648  61.805 1.00 32.73  ? 96  ASP B OD2 1 
ATOM   1810  N  N   . VAL B  1 103 ? 64.422  78.318  58.446 1.00 19.22  ? 97  VAL B N   1 
ATOM   1811  C  CA  . VAL B  1 103 ? 64.816  77.684  57.215 1.00 17.34  ? 97  VAL B CA  1 
ATOM   1812  C  C   . VAL B  1 103 ? 64.523  78.476  55.936 1.00 25.15  ? 97  VAL B C   1 
ATOM   1813  O  O   . VAL B  1 103 ? 63.457  79.071  55.776 1.00 17.91  ? 97  VAL B O   1 
ATOM   1814  C  CB  . VAL B  1 103 ? 64.146  76.291  57.098 1.00 15.32  ? 97  VAL B CB  1 
ATOM   1815  C  CG1 . VAL B  1 103 ? 64.535  75.629  55.760 1.00 3.87   ? 97  VAL B CG1 1 
ATOM   1816  C  CG2 . VAL B  1 103 ? 64.566  75.396  58.290 1.00 6.70   ? 97  VAL B CG2 1 
ATOM   1817  N  N   . SER B  1 104 ? 65.483  78.473  55.021 1.00 19.87  ? 98  SER B N   1 
ATOM   1818  C  CA  . SER B  1 104 ? 65.290  79.134  53.739 1.00 26.08  ? 98  SER B CA  1 
ATOM   1819  C  C   . SER B  1 104 ? 66.269  78.535  52.758 1.00 22.98  ? 98  SER B C   1 
ATOM   1820  O  O   . SER B  1 104 ? 67.409  78.986  52.641 1.00 24.99  ? 98  SER B O   1 
ATOM   1821  C  CB  . SER B  1 104 ? 65.529  80.634  53.826 1.00 29.14  ? 98  SER B CB  1 
ATOM   1822  O  OG  . SER B  1 104 ? 65.300  81.226  52.558 1.00 31.62  ? 98  SER B OG  1 
ATOM   1823  N  N   . ILE B  1 105 ? 65.795  77.522  52.046 1.00 18.91  ? 99  ILE B N   1 
ATOM   1824  C  CA  . ILE B  1 105 ? 66.593  76.801  51.084 1.00 21.91  ? 99  ILE B CA  1 
ATOM   1825  C  C   . ILE B  1 105 ? 65.962  76.824  49.696 1.00 25.51  ? 99  ILE B C   1 
ATOM   1826  O  O   . ILE B  1 105 ? 64.742  76.911  49.548 1.00 25.76  ? 99  ILE B O   1 
ATOM   1827  C  CB  . ILE B  1 105 ? 66.752  75.339  51.556 1.00 24.12  ? 99  ILE B CB  1 
ATOM   1828  C  CG1 . ILE B  1 105 ? 67.671  75.302  52.775 1.00 30.23  ? 99  ILE B CG1 1 
ATOM   1829  C  CG2 . ILE B  1 105 ? 67.302  74.454  50.438 1.00 26.82  ? 99  ILE B CG2 1 
ATOM   1830  C  CD1 . ILE B  1 105 ? 67.627  73.980  53.530 1.00 27.54  ? 99  ILE B CD1 1 
ATOM   1831  N  N   . GLU B  1 106 ? 66.799  76.760  48.672 1.00 19.78  ? 100 GLU B N   1 
ATOM   1832  C  CA  . GLU B  1 106 ? 66.293  76.704  47.310 1.00 28.42  ? 100 GLU B CA  1 
ATOM   1833  C  C   . GLU B  1 106 ? 67.092  75.557  46.704 1.00 20.27  ? 100 GLU B C   1 
ATOM   1834  O  O   . GLU B  1 106 ? 68.303  75.585  46.735 1.00 19.36  ? 100 GLU B O   1 
ATOM   1835  C  CB  . GLU B  1 106 ? 66.545  78.030  46.591 1.00 27.57  ? 100 GLU B CB  1 
ATOM   1836  C  CG  . GLU B  1 106 ? 65.993  78.105  45.178 1.00 47.38  ? 100 GLU B CG  1 
ATOM   1837  C  CD  . GLU B  1 106 ? 65.777  79.543  44.703 1.00 60.90  ? 100 GLU B CD  1 
ATOM   1838  O  OE1 . GLU B  1 106 ? 65.645  79.749  43.474 1.00 58.65  ? 100 GLU B OE1 1 
ATOM   1839  O  OE2 . GLU B  1 106 ? 65.723  80.461  45.557 1.00 62.58  ? 100 GLU B OE2 1 
ATOM   1840  N  N   . ASP B  1 107 ? 66.411  74.535  46.195 1.00 16.24  ? 101 ASP B N   1 
ATOM   1841  C  CA  . ASP B  1 107 ? 67.084  73.363  45.623 1.00 15.64  ? 101 ASP B CA  1 
ATOM   1842  C  C   . ASP B  1 107 ? 66.533  72.993  44.254 1.00 19.77  ? 101 ASP B C   1 
ATOM   1843  O  O   . ASP B  1 107 ? 65.327  73.082  44.036 1.00 17.48  ? 101 ASP B O   1 
ATOM   1844  C  CB  . ASP B  1 107 ? 66.925  72.160  46.550 1.00 15.14  ? 101 ASP B CB  1 
ATOM   1845  C  CG  . ASP B  1 107 ? 67.752  70.979  46.097 1.00 26.36  ? 101 ASP B CG  1 
ATOM   1846  O  OD1 . ASP B  1 107 ? 67.217  70.093  45.389 1.00 30.04  ? 101 ASP B OD1 1 
ATOM   1847  O  OD2 . ASP B  1 107 ? 68.954  70.956  46.438 1.00 24.95  ? 101 ASP B OD2 1 
ATOM   1848  N  N   . SER B  1 108 ? 67.397  72.545  43.345 1.00 11.82  ? 102 SER B N   1 
ATOM   1849  C  CA  . SER B  1 108 ? 66.942  72.209  41.996 1.00 23.21  ? 102 SER B CA  1 
ATOM   1850  C  C   . SER B  1 108 ? 66.975  70.723  41.679 1.00 27.38  ? 102 SER B C   1 
ATOM   1851  O  O   . SER B  1 108 ? 66.704  70.321  40.539 1.00 24.07  ? 102 SER B O   1 
ATOM   1852  C  CB  . SER B  1 108 ? 67.789  72.950  40.966 1.00 19.72  ? 102 SER B CB  1 
ATOM   1853  O  OG  . SER B  1 108 ? 67.845  74.315  41.296 1.00 40.41  ? 102 SER B OG  1 
ATOM   1854  N  N   . VAL B  1 109 ? 67.324  69.915  42.677 1.00 23.45  ? 103 VAL B N   1 
ATOM   1855  C  CA  . VAL B  1 109 ? 67.392  68.482  42.490 1.00 14.59  ? 103 VAL B CA  1 
ATOM   1856  C  C   . VAL B  1 109 ? 66.103  67.845  43.019 1.00 21.20  ? 103 VAL B C   1 
ATOM   1857  O  O   . VAL B  1 109 ? 65.562  66.938  42.401 1.00 19.79  ? 103 VAL B O   1 
ATOM   1858  C  CB  . VAL B  1 109 ? 68.688  67.911  43.158 1.00 20.47  ? 103 VAL B CB  1 
ATOM   1859  C  CG1 . VAL B  1 109 ? 68.655  66.399  43.227 1.00 10.90  ? 103 VAL B CG1 1 
ATOM   1860  C  CG2 . VAL B  1 109 ? 69.905  68.334  42.325 1.00 12.93  ? 103 VAL B CG2 1 
ATOM   1861  N  N   . ILE B  1 110 ? 65.600  68.301  44.162 1.00 23.99  ? 104 ILE B N   1 
ATOM   1862  C  CA  . ILE B  1 110 ? 64.337  67.754  44.638 1.00 20.34  ? 104 ILE B CA  1 
ATOM   1863  C  C   . ILE B  1 110 ? 63.260  68.383  43.734 1.00 23.27  ? 104 ILE B C   1 
ATOM   1864  O  O   . ILE B  1 110 ? 63.499  69.404  43.084 1.00 23.50  ? 104 ILE B O   1 
ATOM   1865  C  CB  . ILE B  1 110 ? 64.037  68.160  46.097 1.00 18.94  ? 104 ILE B CB  1 
ATOM   1866  C  CG1 . ILE B  1 110 ? 64.204  69.668  46.267 1.00 19.74  ? 104 ILE B CG1 1 
ATOM   1867  C  CG2 . ILE B  1 110 ? 64.918  67.384  47.062 1.00 9.85   ? 104 ILE B CG2 1 
ATOM   1868  C  CD1 . ILE B  1 110 ? 63.450  70.241  47.503 1.00 12.33  ? 104 ILE B CD1 1 
ATOM   1869  N  N   . SER B  1 111 ? 62.082  67.784  43.678 1.00 17.66  ? 105 SER B N   1 
ATOM   1870  C  CA  . SER B  1 111 ? 61.010  68.349  42.867 1.00 21.37  ? 105 SER B CA  1 
ATOM   1871  C  C   . SER B  1 111 ? 59.649  68.041  43.472 1.00 22.04  ? 105 SER B C   1 
ATOM   1872  O  O   . SER B  1 111 ? 59.537  67.207  44.372 1.00 16.87  ? 105 SER B O   1 
ATOM   1873  C  CB  . SER B  1 111 ? 61.062  67.799  41.438 1.00 19.71  ? 105 SER B CB  1 
ATOM   1874  O  OG  . SER B  1 111 ? 60.096  68.434  40.609 1.00 23.68  ? 105 SER B OG  1 
ATOM   1875  N  N   . LEU B  1 112 ? 58.615  68.727  42.989 1.00 21.16  ? 106 LEU B N   1 
ATOM   1876  C  CA  . LEU B  1 112 ? 57.269  68.462  43.478 1.00 23.97  ? 106 LEU B CA  1 
ATOM   1877  C  C   . LEU B  1 112 ? 56.483  67.693  42.409 1.00 21.83  ? 106 LEU B C   1 
ATOM   1878  O  O   . LEU B  1 112 ? 55.268  67.646  42.448 1.00 20.95  ? 106 LEU B O   1 
ATOM   1879  C  CB  . LEU B  1 112 ? 56.548  69.766  43.858 1.00 12.63  ? 106 LEU B CB  1 
ATOM   1880  C  CG  . LEU B  1 112 ? 57.204  70.577  44.985 1.00 18.94  ? 106 LEU B CG  1 
ATOM   1881  C  CD1 . LEU B  1 112 ? 56.228  71.643  45.481 1.00 13.63  ? 106 LEU B CD1 1 
ATOM   1882  C  CD2 . LEU B  1 112 ? 57.599  69.661  46.154 1.00 15.35  ? 106 LEU B CD2 1 
ATOM   1883  N  N   . SER B  1 113 ? 57.197  67.099  41.458 1.00 17.02  ? 107 SER B N   1 
ATOM   1884  C  CA  . SER B  1 113 ? 56.584  66.301  40.391 1.00 26.76  ? 107 SER B CA  1 
ATOM   1885  C  C   . SER B  1 113 ? 57.674  65.479  39.704 1.00 24.79  ? 107 SER B C   1 
ATOM   1886  O  O   . SER B  1 113 ? 58.852  65.803  39.805 1.00 29.68  ? 107 SER B O   1 
ATOM   1887  C  CB  . SER B  1 113 ? 55.902  67.189  39.347 1.00 17.03  ? 107 SER B CB  1 
ATOM   1888  O  OG  . SER B  1 113 ? 56.867  67.971  38.684 1.00 31.67  ? 107 SER B OG  1 
ATOM   1889  N  N   . GLY B  1 114 ? 57.272  64.409  39.026 1.00 27.84  ? 108 GLY B N   1 
ATOM   1890  C  CA  . GLY B  1 114 ? 58.220  63.568  38.314 1.00 18.70  ? 108 GLY B CA  1 
ATOM   1891  C  C   . GLY B  1 114 ? 59.031  62.634  39.183 1.00 23.00  ? 108 GLY B C   1 
ATOM   1892  O  O   . GLY B  1 114 ? 58.788  62.511  40.387 1.00 26.18  ? 108 GLY B O   1 
ATOM   1893  N  N   . ASP B  1 115 ? 59.992  61.970  38.548 1.00 22.92  ? 109 ASP B N   1 
ATOM   1894  C  CA  . ASP B  1 115 ? 60.903  61.019  39.191 1.00 27.95  ? 109 ASP B CA  1 
ATOM   1895  C  C   . ASP B  1 115 ? 61.490  61.475  40.523 1.00 30.43  ? 109 ASP B C   1 
ATOM   1896  O  O   . ASP B  1 115 ? 61.761  60.652  41.397 1.00 31.11  ? 109 ASP B O   1 
ATOM   1897  C  CB  . ASP B  1 115 ? 62.076  60.698  38.250 1.00 26.87  ? 109 ASP B CB  1 
ATOM   1898  C  CG  . ASP B  1 115 ? 61.771  59.568  37.295 1.00 34.71  ? 109 ASP B CG  1 
ATOM   1899  O  OD1 . ASP B  1 115 ? 60.799  58.834  37.554 1.00 41.22  ? 109 ASP B OD1 1 
ATOM   1900  O  OD2 . ASP B  1 115 ? 62.513  59.402  36.298 1.00 33.83  ? 109 ASP B OD2 1 
ATOM   1901  N  N   . HIS B  1 116 ? 61.720  62.778  40.667 1.00 31.71  ? 110 HIS B N   1 
ATOM   1902  C  CA  . HIS B  1 116 ? 62.312  63.308  41.891 1.00 30.70  ? 110 HIS B CA  1 
ATOM   1903  C  C   . HIS B  1 116 ? 61.308  63.888  42.877 1.00 25.27  ? 110 HIS B C   1 
ATOM   1904  O  O   . HIS B  1 116 ? 61.718  64.516  43.850 1.00 27.43  ? 110 HIS B O   1 
ATOM   1905  C  CB  . HIS B  1 116 ? 63.366  64.383  41.562 1.00 23.10  ? 110 HIS B CB  1 
ATOM   1906  C  CG  . HIS B  1 116 ? 64.593  63.852  40.881 1.00 35.92  ? 110 HIS B CG  1 
ATOM   1907  N  ND1 . HIS B  1 116 ? 65.665  64.655  40.542 1.00 27.89  ? 110 HIS B ND1 1 
ATOM   1908  C  CD2 . HIS B  1 116 ? 64.922  62.600  40.480 1.00 36.16  ? 110 HIS B CD2 1 
ATOM   1909  C  CE1 . HIS B  1 116 ? 66.597  63.920  39.966 1.00 28.84  ? 110 HIS B CE1 1 
ATOM   1910  N  NE2 . HIS B  1 116 ? 66.172  62.670  39.916 1.00 30.30  ? 110 HIS B NE2 1 
ATOM   1911  N  N   . CYS B  1 117 ? 60.012  63.692  42.631 1.00 21.34  ? 111 CYS B N   1 
ATOM   1912  C  CA  . CYS B  1 117 ? 58.969  64.205  43.531 1.00 24.40  ? 111 CYS B CA  1 
ATOM   1913  C  C   . CYS B  1 117 ? 59.223  63.740  44.969 1.00 26.74  ? 111 CYS B C   1 
ATOM   1914  O  O   . CYS B  1 117 ? 59.581  62.583  45.199 1.00 25.10  ? 111 CYS B O   1 
ATOM   1915  C  CB  . CYS B  1 117 ? 57.581  63.716  43.103 1.00 23.02  ? 111 CYS B CB  1 
ATOM   1916  S  SG  . CYS B  1 117 ? 56.143  64.619  43.810 1.00 31.73  ? 111 CYS B SG  1 
ATOM   1917  N  N   . ILE B  1 118 ? 59.032  64.646  45.929 1.00 24.04  ? 112 ILE B N   1 
ATOM   1918  C  CA  . ILE B  1 118 ? 59.229  64.328  47.335 1.00 25.35  ? 112 ILE B CA  1 
ATOM   1919  C  C   . ILE B  1 118 ? 57.903  64.307  48.073 1.00 26.19  ? 112 ILE B C   1 
ATOM   1920  O  O   . ILE B  1 118 ? 57.857  64.079  49.279 1.00 20.65  ? 112 ILE B O   1 
ATOM   1921  C  CB  . ILE B  1 118 ? 60.140  65.344  48.003 1.00 21.65  ? 112 ILE B CB  1 
ATOM   1922  C  CG1 . ILE B  1 118 ? 59.590  66.749  47.746 1.00 17.29  ? 112 ILE B CG1 1 
ATOM   1923  C  CG2 . ILE B  1 118 ? 61.564  65.183  47.465 1.00 16.69  ? 112 ILE B CG2 1 
ATOM   1924  C  CD1 . ILE B  1 118 ? 60.165  67.797  48.655 1.00 21.64  ? 112 ILE B CD1 1 
ATOM   1925  N  N   . ILE B  1 119 ? 56.818  64.554  47.347 1.00 26.60  ? 113 ILE B N   1 
ATOM   1926  C  CA  . ILE B  1 119 ? 55.502  64.520  47.964 1.00 24.14  ? 113 ILE B CA  1 
ATOM   1927  C  C   . ILE B  1 119 ? 55.230  63.060  48.320 1.00 25.66  ? 113 ILE B C   1 
ATOM   1928  O  O   . ILE B  1 119 ? 55.508  62.160  47.529 1.00 24.83  ? 113 ILE B O   1 
ATOM   1929  C  CB  . ILE B  1 119 ? 54.432  65.045  47.000 1.00 22.18  ? 113 ILE B CB  1 
ATOM   1930  C  CG1 . ILE B  1 119 ? 54.563  66.574  46.905 1.00 25.05  ? 113 ILE B CG1 1 
ATOM   1931  C  CG2 . ILE B  1 119 ? 53.051  64.631  47.475 1.00 18.47  ? 113 ILE B CG2 1 
ATOM   1932  C  CD1 . ILE B  1 119 ? 53.642  67.223  45.918 1.00 23.72  ? 113 ILE B CD1 1 
ATOM   1933  N  N   . GLY B  1 120 ? 54.715  62.828  49.522 1.00 25.08  ? 114 GLY B N   1 
ATOM   1934  C  CA  . GLY B  1 120 ? 54.442  61.472  49.956 1.00 20.08  ? 114 GLY B CA  1 
ATOM   1935  C  C   . GLY B  1 120 ? 55.647  60.860  50.657 1.00 22.92  ? 114 GLY B C   1 
ATOM   1936  O  O   . GLY B  1 120 ? 55.620  59.702  51.064 1.00 17.42  ? 114 GLY B O   1 
ATOM   1937  N  N   . ARG B  1 121 ? 56.716  61.634  50.794 1.00 17.02  ? 115 ARG B N   1 
ATOM   1938  C  CA  . ARG B  1 121 ? 57.902  61.143  51.476 1.00 24.16  ? 115 ARG B CA  1 
ATOM   1939  C  C   . ARG B  1 121 ? 58.064  61.890  52.800 1.00 24.19  ? 115 ARG B C   1 
ATOM   1940  O  O   . ARG B  1 121 ? 57.185  62.677  53.182 1.00 22.59  ? 115 ARG B O   1 
ATOM   1941  C  CB  . ARG B  1 121 ? 59.127  61.295  50.567 1.00 18.32  ? 115 ARG B CB  1 
ATOM   1942  C  CG  . ARG B  1 121 ? 58.936  60.514  49.280 1.00 24.93  ? 115 ARG B CG  1 
ATOM   1943  C  CD  . ARG B  1 121 ? 60.207  60.358  48.501 1.00 34.04  ? 115 ARG B CD  1 
ATOM   1944  N  NE  . ARG B  1 121 ? 59.944  59.825  47.171 1.00 28.74  ? 115 ARG B NE  1 
ATOM   1945  C  CZ  . ARG B  1 121 ? 59.870  58.537  46.864 1.00 30.05  ? 115 ARG B CZ  1 
ATOM   1946  N  NH1 . ARG B  1 121 ? 59.617  58.187  45.610 1.00 19.22  ? 115 ARG B NH1 1 
ATOM   1947  N  NH2 . ARG B  1 121 ? 60.063  57.603  47.791 1.00 24.53  ? 115 ARG B NH2 1 
ATOM   1948  N  N   . THR B  1 122 ? 59.176  61.668  53.493 1.00 18.19  ? 116 THR B N   1 
ATOM   1949  C  CA  . THR B  1 122 ? 59.350  62.286  54.797 1.00 19.18  ? 116 THR B CA  1 
ATOM   1950  C  C   . THR B  1 122 ? 60.504  63.260  54.947 1.00 17.74  ? 116 THR B C   1 
ATOM   1951  O  O   . THR B  1 122 ? 61.649  62.952  54.626 1.00 20.09  ? 116 THR B O   1 
ATOM   1952  C  CB  . THR B  1 122 ? 59.502  61.187  55.905 1.00 19.58  ? 116 THR B CB  1 
ATOM   1953  O  OG1 . THR B  1 122 ? 58.324  60.380  55.936 1.00 19.76  ? 116 THR B OG1 1 
ATOM   1954  C  CG2 . THR B  1 122 ? 59.719  61.818  57.293 1.00 11.49  ? 116 THR B CG2 1 
ATOM   1955  N  N   . LEU B  1 123 ? 60.191  64.444  55.452 1.00 17.69  ? 117 LEU B N   1 
ATOM   1956  C  CA  . LEU B  1 123 ? 61.224  65.431  55.708 1.00 15.17  ? 117 LEU B CA  1 
ATOM   1957  C  C   . LEU B  1 123 ? 61.696  65.111  57.133 1.00 19.33  ? 117 LEU B C   1 
ATOM   1958  O  O   . LEU B  1 123 ? 60.885  64.868  58.033 1.00 16.41  ? 117 LEU B O   1 
ATOM   1959  C  CB  . LEU B  1 123 ? 60.647  66.837  55.664 1.00 12.38  ? 117 LEU B CB  1 
ATOM   1960  C  CG  . LEU B  1 123 ? 61.672  67.950  55.881 1.00 22.72  ? 117 LEU B CG  1 
ATOM   1961  C  CD1 . LEU B  1 123 ? 62.676  67.948  54.723 1.00 22.54  ? 117 LEU B CD1 1 
ATOM   1962  C  CD2 . LEU B  1 123 ? 60.960  69.298  55.978 1.00 19.66  ? 117 LEU B CD2 1 
ATOM   1963  N  N   . VAL B  1 124 ? 63.006  65.094  57.326 1.00 19.36  ? 118 VAL B N   1 
ATOM   1964  C  CA  . VAL B  1 124 ? 63.583  64.807  58.628 1.00 18.55  ? 118 VAL B CA  1 
ATOM   1965  C  C   . VAL B  1 124 ? 64.683  65.796  59.011 1.00 22.30  ? 118 VAL B C   1 
ATOM   1966  O  O   . VAL B  1 124 ? 65.597  66.077  58.213 1.00 19.25  ? 118 VAL B O   1 
ATOM   1967  C  CB  . VAL B  1 124 ? 64.231  63.408  58.665 1.00 19.18  ? 118 VAL B CB  1 
ATOM   1968  C  CG1 . VAL B  1 124 ? 64.741  63.133  60.070 1.00 14.28  ? 118 VAL B CG1 1 
ATOM   1969  C  CG2 . VAL B  1 124 ? 63.233  62.339  58.193 1.00 14.68  ? 118 VAL B CG2 1 
ATOM   1970  N  N   . VAL B  1 125 ? 64.591  66.328  60.224 1.00 15.99  ? 119 VAL B N   1 
ATOM   1971  C  CA  . VAL B  1 125 ? 65.620  67.221  60.716 1.00 22.13  ? 119 VAL B CA  1 
ATOM   1972  C  C   . VAL B  1 125 ? 66.387  66.362  61.730 1.00 23.13  ? 119 VAL B C   1 
ATOM   1973  O  O   . VAL B  1 125 ? 65.794  65.749  62.622 1.00 18.37  ? 119 VAL B O   1 
ATOM   1974  C  CB  . VAL B  1 125 ? 65.030  68.498  61.354 1.00 24.20  ? 119 VAL B CB  1 
ATOM   1975  C  CG1 . VAL B  1 125 ? 64.206  68.169  62.599 1.00 28.58  ? 119 VAL B CG1 1 
ATOM   1976  C  CG2 . VAL B  1 125 ? 66.164  69.454  61.685 1.00 30.20  ? 119 VAL B CG2 1 
ATOM   1977  N  N   . HIS B  1 126 ? 67.705  66.303  61.561 1.00 21.26  ? 120 HIS B N   1 
ATOM   1978  C  CA  . HIS B  1 126 ? 68.568  65.471  62.391 1.00 22.55  ? 120 HIS B CA  1 
ATOM   1979  C  C   . HIS B  1 126 ? 69.222  66.115  63.596 1.00 24.13  ? 120 HIS B C   1 
ATOM   1980  O  O   . HIS B  1 126 ? 69.270  67.340  63.748 1.00 25.36  ? 120 HIS B O   1 
ATOM   1981  C  CB  . HIS B  1 126 ? 69.662  64.828  61.517 1.00 22.86  ? 120 HIS B CB  1 
ATOM   1982  C  CG  . HIS B  1 126 ? 69.148  63.773  60.587 1.00 22.10  ? 120 HIS B CG  1 
ATOM   1983  N  ND1 . HIS B  1 126 ? 69.116  62.435  60.920 1.00 21.80  ? 120 HIS B ND1 1 
ATOM   1984  C  CD2 . HIS B  1 126 ? 68.624  63.864  59.342 1.00 18.23  ? 120 HIS B CD2 1 
ATOM   1985  C  CE1 . HIS B  1 126 ? 68.597  61.749  59.917 1.00 26.74  ? 120 HIS B CE1 1 
ATOM   1986  N  NE2 . HIS B  1 126 ? 68.291  62.592  58.945 1.00 28.00  ? 120 HIS B NE2 1 
ATOM   1987  N  N   . GLU B  1 127 ? 69.763  65.237  64.428 1.00 26.92  ? 121 GLU B N   1 
ATOM   1988  C  CA  . GLU B  1 127 ? 70.443  65.577  65.666 1.00 30.84  ? 121 GLU B CA  1 
ATOM   1989  C  C   . GLU B  1 127 ? 71.703  66.442  65.522 1.00 29.44  ? 121 GLU B C   1 
ATOM   1990  O  O   . GLU B  1 127 ? 71.888  67.403  66.269 1.00 22.96  ? 121 GLU B O   1 
ATOM   1991  C  CB  . GLU B  1 127 ? 70.815  64.283  66.375 1.00 27.78  ? 121 GLU B CB  1 
ATOM   1992  C  CG  . GLU B  1 127 ? 71.386  64.475  67.752 1.00 38.44  ? 121 GLU B CG  1 
ATOM   1993  C  CD  . GLU B  1 127 ? 72.095  63.233  68.262 1.00 46.63  ? 121 GLU B CD  1 
ATOM   1994  O  OE1 . GLU B  1 127 ? 72.372  63.199  69.480 1.00 46.95  ? 121 GLU B OE1 1 
ATOM   1995  O  OE2 . GLU B  1 127 ? 72.383  62.310  67.451 1.00 34.47  ? 121 GLU B OE2 1 
ATOM   1996  N  N   . LYS B  1 128 ? 72.558  66.106  64.560 1.00 26.63  ? 122 LYS B N   1 
ATOM   1997  C  CA  . LYS B  1 128 ? 73.813  66.832  64.372 1.00 26.59  ? 122 LYS B CA  1 
ATOM   1998  C  C   . LYS B  1 128 ? 73.987  67.389  62.977 1.00 25.59  ? 122 LYS B C   1 
ATOM   1999  O  O   . LYS B  1 128 ? 73.135  67.245  62.106 1.00 19.56  ? 122 LYS B O   1 
ATOM   2000  C  CB  . LYS B  1 128 ? 75.016  65.910  64.658 1.00 31.08  ? 122 LYS B CB  1 
ATOM   2001  C  CG  . LYS B  1 128 ? 74.784  64.899  65.776 1.00 35.17  ? 122 LYS B CG  1 
ATOM   2002  C  CD  . LYS B  1 128 ? 76.051  64.190  66.241 1.00 35.51  ? 122 LYS B CD  1 
ATOM   2003  C  CE  . LYS B  1 128 ? 76.523  63.138  65.261 1.00 49.06  ? 122 LYS B CE  1 
ATOM   2004  N  NZ  . LYS B  1 128 ? 77.612  62.294  65.850 1.00 56.54  ? 122 LYS B NZ  1 
ATOM   2005  N  N   . ALA B  1 129 ? 75.139  68.011  62.777 1.00 21.32  ? 123 ALA B N   1 
ATOM   2006  C  CA  . ALA B  1 129 ? 75.494  68.597  61.498 1.00 22.51  ? 123 ALA B CA  1 
ATOM   2007  C  C   . ALA B  1 129 ? 75.736  67.513  60.452 1.00 22.50  ? 123 ALA B C   1 
ATOM   2008  O  O   . ALA B  1 129 ? 76.237  66.436  60.752 1.00 21.79  ? 123 ALA B O   1 
ATOM   2009  C  CB  . ALA B  1 129 ? 76.743  69.443  61.649 1.00 9.54   ? 123 ALA B CB  1 
ATOM   2010  N  N   . ASP B  1 130 ? 75.344  67.812  59.227 1.00 18.04  ? 124 ASP B N   1 
ATOM   2011  C  CA  . ASP B  1 130 ? 75.538  66.921  58.111 1.00 17.17  ? 124 ASP B CA  1 
ATOM   2012  C  C   . ASP B  1 130 ? 76.964  67.273  57.682 1.00 20.05  ? 124 ASP B C   1 
ATOM   2013  O  O   . ASP B  1 130 ? 77.265  68.456  57.482 1.00 15.12  ? 124 ASP B O   1 
ATOM   2014  C  CB  . ASP B  1 130 ? 74.534  67.284  57.010 1.00 14.71  ? 124 ASP B CB  1 
ATOM   2015  C  CG  . ASP B  1 130 ? 74.616  66.358  55.812 1.00 22.06  ? 124 ASP B CG  1 
ATOM   2016  O  OD1 . ASP B  1 130 ? 73.605  66.237  55.083 1.00 22.54  ? 124 ASP B OD1 1 
ATOM   2017  O  OD2 . ASP B  1 130 ? 75.684  65.758  55.594 1.00 14.02  ? 124 ASP B OD2 1 
ATOM   2018  N  N   . ASP B  1 131 ? 77.855  66.282  57.582 1.00 18.05  ? 125 ASP B N   1 
ATOM   2019  C  CA  . ASP B  1 131 ? 79.226  66.591  57.169 1.00 18.43  ? 125 ASP B CA  1 
ATOM   2020  C  C   . ASP B  1 131 ? 79.324  66.672  55.643 1.00 18.11  ? 125 ASP B C   1 
ATOM   2021  O  O   . ASP B  1 131 ? 80.411  66.787  55.065 1.00 24.58  ? 125 ASP B O   1 
ATOM   2022  C  CB  . ASP B  1 131 ? 80.245  65.586  57.778 1.00 13.79  ? 125 ASP B CB  1 
ATOM   2023  C  CG  . ASP B  1 131 ? 80.161  64.173  57.191 1.00 23.17  ? 125 ASP B CG  1 
ATOM   2024  O  OD1 . ASP B  1 131 ? 80.727  63.258  57.843 1.00 23.01  ? 125 ASP B OD1 1 
ATOM   2025  O  OD2 . ASP B  1 131 ? 79.561  63.962  56.104 1.00 17.83  ? 125 ASP B OD2 1 
ATOM   2026  N  N   . LEU B  1 132 ? 78.164  66.632  54.996 1.00 18.72  ? 126 LEU B N   1 
ATOM   2027  C  CA  . LEU B  1 132 ? 78.074  66.738  53.544 1.00 22.88  ? 126 LEU B CA  1 
ATOM   2028  C  C   . LEU B  1 132 ? 78.926  65.729  52.798 1.00 22.91  ? 126 LEU B C   1 
ATOM   2029  O  O   . LEU B  1 132 ? 79.345  65.978  51.661 1.00 25.52  ? 126 LEU B O   1 
ATOM   2030  C  CB  . LEU B  1 132 ? 78.460  68.157  53.106 1.00 22.65  ? 126 LEU B CB  1 
ATOM   2031  C  CG  . LEU B  1 132 ? 77.816  69.241  53.977 1.00 31.15  ? 126 LEU B CG  1 
ATOM   2032  C  CD1 . LEU B  1 132 ? 78.262  70.647  53.501 1.00 19.69  ? 126 LEU B CD1 1 
ATOM   2033  C  CD2 . LEU B  1 132 ? 76.285  69.072  53.960 1.00 25.31  ? 126 LEU B CD2 1 
ATOM   2034  N  N   . GLY B  1 133 ? 79.184  64.596  53.440 1.00 24.54  ? 127 GLY B N   1 
ATOM   2035  C  CA  . GLY B  1 133 ? 79.968  63.543  52.811 1.00 28.46  ? 127 GLY B CA  1 
ATOM   2036  C  C   . GLY B  1 133 ? 81.470  63.765  52.803 1.00 28.00  ? 127 GLY B C   1 
ATOM   2037  O  O   . GLY B  1 133 ? 82.178  63.159  52.019 1.00 29.60  ? 127 GLY B O   1 
ATOM   2038  N  N   . LYS B  1 134 ? 81.970  64.622  53.680 1.00 29.83  ? 128 LYS B N   1 
ATOM   2039  C  CA  . LYS B  1 134 ? 83.401  64.889  53.714 1.00 29.56  ? 128 LYS B CA  1 
ATOM   2040  C  C   . LYS B  1 134 ? 84.059  64.400  55.007 1.00 24.20  ? 128 LYS B C   1 
ATOM   2041  O  O   . LYS B  1 134 ? 85.153  64.842  55.353 1.00 28.59  ? 128 LYS B O   1 
ATOM   2042  C  CB  . LYS B  1 134 ? 83.626  66.390  53.510 1.00 21.10  ? 128 LYS B CB  1 
ATOM   2043  C  CG  . LYS B  1 134 ? 82.970  66.882  52.219 1.00 27.39  ? 128 LYS B CG  1 
ATOM   2044  C  CD  . LYS B  1 134 ? 82.802  68.389  52.164 1.00 23.46  ? 128 LYS B CD  1 
ATOM   2045  C  CE  . LYS B  1 134 ? 84.114  69.105  51.965 1.00 35.88  ? 128 LYS B CE  1 
ATOM   2046  N  NZ  . LYS B  1 134 ? 83.914  70.570  51.778 1.00 39.99  ? 128 LYS B NZ  1 
ATOM   2047  N  N   . GLY B  1 135 ? 83.395  63.472  55.695 1.00 23.61  ? 129 GLY B N   1 
ATOM   2048  C  CA  . GLY B  1 135 ? 83.905  62.937  56.954 1.00 23.26  ? 129 GLY B CA  1 
ATOM   2049  C  C   . GLY B  1 135 ? 84.910  61.794  56.867 1.00 26.82  ? 129 GLY B C   1 
ATOM   2050  O  O   . GLY B  1 135 ? 85.457  61.343  57.895 1.00 21.10  ? 129 GLY B O   1 
ATOM   2051  N  N   . GLY B  1 136 ? 85.147  61.301  55.652 1.00 21.14  ? 130 GLY B N   1 
ATOM   2052  C  CA  . GLY B  1 136 ? 86.118  60.236  55.482 1.00 26.66  ? 130 GLY B CA  1 
ATOM   2053  C  C   . GLY B  1 136 ? 85.725  58.792  55.767 1.00 29.28  ? 130 GLY B C   1 
ATOM   2054  O  O   . GLY B  1 136 ? 86.588  57.917  55.817 1.00 33.15  ? 130 GLY B O   1 
ATOM   2055  N  N   . ASN B  1 137 ? 84.451  58.514  55.982 1.00 27.39  ? 131 ASN B N   1 
ATOM   2056  C  CA  . ASN B  1 137 ? 84.076  57.133  56.194 1.00 28.56  ? 131 ASN B CA  1 
ATOM   2057  C  C   . ASN B  1 137 ? 82.788  56.764  55.477 1.00 32.44  ? 131 ASN B C   1 
ATOM   2058  O  O   . ASN B  1 137 ? 82.189  57.590  54.772 1.00 32.08  ? 131 ASN B O   1 
ATOM   2059  C  CB  . ASN B  1 137 ? 83.996  56.788  57.681 1.00 17.82  ? 131 ASN B CB  1 
ATOM   2060  C  CG  . ASN B  1 137 ? 83.124  57.733  58.471 1.00 31.59  ? 131 ASN B CG  1 
ATOM   2061  O  OD1 . ASN B  1 137 ? 82.130  58.270  57.969 1.00 24.44  ? 131 ASN B OD1 1 
ATOM   2062  N  ND2 . ASN B  1 137 ? 83.474  57.916  59.743 1.00 21.54  ? 131 ASN B ND2 1 
ATOM   2063  N  N   . GLU B  1 138 ? 82.391  55.507  55.632 1.00 35.38  ? 132 GLU B N   1 
ATOM   2064  C  CA  . GLU B  1 138 ? 81.198  54.984  54.994 1.00 37.23  ? 132 GLU B CA  1 
ATOM   2065  C  C   . GLU B  1 138 ? 79.961  55.701  55.487 1.00 36.48  ? 132 GLU B C   1 
ATOM   2066  O  O   . GLU B  1 138 ? 79.039  55.970  54.707 1.00 35.49  ? 132 GLU B O   1 
ATOM   2067  C  CB  . GLU B  1 138 ? 81.057  53.497  55.286 1.00 46.67  ? 132 GLU B CB  1 
ATOM   2068  C  CG  . GLU B  1 138 ? 81.925  52.595  54.438 1.00 66.44  ? 132 GLU B CG  1 
ATOM   2069  C  CD  . GLU B  1 138 ? 81.736  51.127  54.802 1.00 79.59  ? 132 GLU B CD  1 
ATOM   2070  O  OE1 . GLU B  1 138 ? 82.142  50.732  55.920 1.00 77.20  ? 132 GLU B OE1 1 
ATOM   2071  O  OE2 . GLU B  1 138 ? 81.172  50.371  53.975 1.00 86.05  ? 132 GLU B OE2 1 
ATOM   2072  N  N   . GLU B  1 139 ? 79.944  56.001  56.783 1.00 24.46  ? 133 GLU B N   1 
ATOM   2073  C  CA  . GLU B  1 139 ? 78.819  56.687  57.383 1.00 24.23  ? 133 GLU B CA  1 
ATOM   2074  C  C   . GLU B  1 139 ? 78.639  58.041  56.684 1.00 29.15  ? 133 GLU B C   1 
ATOM   2075  O  O   . GLU B  1 139 ? 77.535  58.415  56.293 1.00 23.55  ? 133 GLU B O   1 
ATOM   2076  C  CB  . GLU B  1 139 ? 79.069  56.895  58.879 1.00 22.65  ? 133 GLU B CB  1 
ATOM   2077  C  CG  . GLU B  1 139 ? 77.818  57.279  59.669 1.00 24.69  ? 133 GLU B CG  1 
ATOM   2078  C  CD  . GLU B  1 139 ? 76.725  56.223  59.560 1.00 33.91  ? 133 GLU B CD  1 
ATOM   2079  O  OE1 . GLU B  1 139 ? 75.673  56.499  58.952 1.00 38.50  ? 133 GLU B OE1 1 
ATOM   2080  O  OE2 . GLU B  1 139 ? 76.920  55.104  60.075 1.00 44.94  ? 133 GLU B OE2 1 
ATOM   2081  N  N   . SER B  1 140 ? 79.739  58.761  56.511 1.00 24.03  ? 134 SER B N   1 
ATOM   2082  C  CA  . SER B  1 140 ? 79.688  60.068  55.879 1.00 27.37  ? 134 SER B CA  1 
ATOM   2083  C  C   . SER B  1 140 ? 79.007  60.030  54.516 1.00 28.41  ? 134 SER B C   1 
ATOM   2084  O  O   . SER B  1 140 ? 78.178  60.891  54.211 1.00 27.17  ? 134 SER B O   1 
ATOM   2085  C  CB  . SER B  1 140 ? 81.106  60.645  55.727 1.00 25.59  ? 134 SER B CB  1 
ATOM   2086  O  OG  . SER B  1 140 ? 81.100  61.928  55.106 1.00 22.46  ? 134 SER B OG  1 
ATOM   2087  N  N   . THR B  1 141 ? 79.350  59.039  53.699 1.00 23.83  ? 135 THR B N   1 
ATOM   2088  C  CA  . THR B  1 141 ? 78.769  58.949  52.366 1.00 28.85  ? 135 THR B CA  1 
ATOM   2089  C  C   . THR B  1 141 ? 77.467  58.201  52.333 1.00 23.12  ? 135 THR B C   1 
ATOM   2090  O  O   . THR B  1 141 ? 76.943  57.876  51.266 1.00 24.19  ? 135 THR B O   1 
ATOM   2091  C  CB  . THR B  1 141 ? 79.752  58.327  51.337 1.00 32.80  ? 135 THR B CB  1 
ATOM   2092  O  OG1 . THR B  1 141 ? 80.308  57.108  51.849 1.00 32.85  ? 135 THR B OG1 1 
ATOM   2093  C  CG2 . THR B  1 141 ? 80.863  59.314  51.032 1.00 28.82  ? 135 THR B CG2 1 
ATOM   2094  N  N   . LYS B  1 142 ? 76.928  57.946  53.511 1.00 25.54  ? 136 LYS B N   1 
ATOM   2095  C  CA  . LYS B  1 142 ? 75.659  57.262  53.600 1.00 27.53  ? 136 LYS B CA  1 
ATOM   2096  C  C   . LYS B  1 142 ? 74.649  58.250  54.213 1.00 29.02  ? 136 LYS B C   1 
ATOM   2097  O  O   . LYS B  1 142 ? 73.637  58.590  53.593 1.00 29.72  ? 136 LYS B O   1 
ATOM   2098  C  CB  . LYS B  1 142 ? 75.809  56.016  54.472 1.00 31.02  ? 136 LYS B CB  1 
ATOM   2099  C  CG  . LYS B  1 142 ? 74.616  55.084  54.437 1.00 55.83  ? 136 LYS B CG  1 
ATOM   2100  C  CD  . LYS B  1 142 ? 74.647  54.065  55.591 1.00 70.39  ? 136 LYS B CD  1 
ATOM   2101  C  CE  . LYS B  1 142 ? 74.358  54.734  56.944 1.00 79.12  ? 136 LYS B CE  1 
ATOM   2102  N  NZ  . LYS B  1 142 ? 74.296  53.817  58.123 1.00 68.67  ? 136 LYS B NZ  1 
ATOM   2103  N  N   . THR B  1 143 ? 74.961  58.751  55.405 1.00 19.55  ? 137 THR B N   1 
ATOM   2104  C  CA  . THR B  1 143 ? 74.080  59.665  56.120 1.00 22.49  ? 137 THR B CA  1 
ATOM   2105  C  C   . THR B  1 143 ? 74.696  61.031  56.450 1.00 24.39  ? 137 THR B C   1 
ATOM   2106  O  O   . THR B  1 143 ? 74.012  61.911  56.992 1.00 26.51  ? 137 THR B O   1 
ATOM   2107  C  CB  . THR B  1 143 ? 73.631  59.053  57.480 1.00 21.20  ? 137 THR B CB  1 
ATOM   2108  O  OG1 . THR B  1 143 ? 74.765  58.958  58.349 1.00 20.57  ? 137 THR B OG1 1 
ATOM   2109  C  CG2 . THR B  1 143 ? 73.048  57.669  57.308 1.00 12.29  ? 137 THR B CG2 1 
ATOM   2110  N  N   . GLY B  1 144 ? 75.977  61.207  56.150 1.00 23.58  ? 138 GLY B N   1 
ATOM   2111  C  CA  . GLY B  1 144 ? 76.651  62.456  56.484 1.00 17.62  ? 138 GLY B CA  1 
ATOM   2112  C  C   . GLY B  1 144 ? 76.935  62.546  57.988 1.00 16.92  ? 138 GLY B C   1 
ATOM   2113  O  O   . GLY B  1 144 ? 77.309  63.601  58.493 1.00 18.88  ? 138 GLY B O   1 
ATOM   2114  N  N   . ASN B  1 145 ? 76.759  61.444  58.712 1.00 19.68  ? 139 ASN B N   1 
ATOM   2115  C  CA  . ASN B  1 145 ? 76.983  61.431  60.162 1.00 27.13  ? 139 ASN B CA  1 
ATOM   2116  C  C   . ASN B  1 145 ? 76.081  62.421  60.871 1.00 26.12  ? 139 ASN B C   1 
ATOM   2117  O  O   . ASN B  1 145 ? 76.464  62.946  61.904 1.00 27.88  ? 139 ASN B O   1 
ATOM   2118  C  CB  . ASN B  1 145 ? 78.436  61.796  60.531 1.00 22.43  ? 139 ASN B CB  1 
ATOM   2119  C  CG  . ASN B  1 145 ? 79.429  60.677  60.233 1.00 22.71  ? 139 ASN B CG  1 
ATOM   2120  O  OD1 . ASN B  1 145 ? 79.389  59.622  60.843 1.00 31.77  ? 139 ASN B OD1 1 
ATOM   2121  N  ND2 . ASN B  1 145 ? 80.329  60.918  59.293 1.00 29.15  ? 139 ASN B ND2 1 
ATOM   2122  N  N   . ALA B  1 146 ? 74.886  62.674  60.353 1.00 23.13  ? 140 ALA B N   1 
ATOM   2123  C  CA  . ALA B  1 146 ? 74.007  63.654  61.009 1.00 24.01  ? 140 ALA B CA  1 
ATOM   2124  C  C   . ALA B  1 146 ? 73.304  63.178  62.286 1.00 23.80  ? 140 ALA B C   1 
ATOM   2125  O  O   . ALA B  1 146 ? 72.595  63.951  62.941 1.00 29.46  ? 140 ALA B O   1 
ATOM   2126  C  CB  . ALA B  1 146 ? 72.976  64.171  60.021 1.00 10.79  ? 140 ALA B CB  1 
ATOM   2127  N  N   . GLY B  1 147 ? 73.471  61.907  62.627 1.00 24.79  ? 141 GLY B N   1 
ATOM   2128  C  CA  . GLY B  1 147 ? 72.868  61.402  63.847 1.00 22.18  ? 141 GLY B CA  1 
ATOM   2129  C  C   . GLY B  1 147 ? 71.386  61.070  63.815 1.00 27.77  ? 141 GLY B C   1 
ATOM   2130  O  O   . GLY B  1 147 ? 70.767  60.961  62.745 1.00 28.38  ? 141 GLY B O   1 
ATOM   2131  N  N   . SER B  1 148 ? 70.817  60.942  65.012 1.00 23.00  ? 142 SER B N   1 
ATOM   2132  C  CA  . SER B  1 148 ? 69.413  60.580  65.192 1.00 28.92  ? 142 SER B CA  1 
ATOM   2133  C  C   . SER B  1 148 ? 68.393  61.534  64.567 1.00 25.58  ? 142 SER B C   1 
ATOM   2134  O  O   . SER B  1 148 ? 68.706  62.670  64.223 1.00 26.36  ? 142 SER B O   1 
ATOM   2135  C  CB  . SER B  1 148 ? 69.124  60.400  66.684 1.00 15.32  ? 142 SER B CB  1 
ATOM   2136  O  OG  . SER B  1 148 ? 69.141  61.640  67.351 1.00 31.74  ? 142 SER B OG  1 
ATOM   2137  N  N   . ARG B  1 149 ? 67.170  61.048  64.406 1.00 24.97  ? 143 ARG B N   1 
ATOM   2138  C  CA  . ARG B  1 149 ? 66.105  61.846  63.803 1.00 24.46  ? 143 ARG B CA  1 
ATOM   2139  C  C   . ARG B  1 149 ? 65.310  62.529  64.896 1.00 21.67  ? 143 ARG B C   1 
ATOM   2140  O  O   . ARG B  1 149 ? 64.609  61.880  65.648 1.00 26.39  ? 143 ARG B O   1 
ATOM   2141  C  CB  . ARG B  1 149 ? 65.220  60.927  62.971 1.00 12.58  ? 143 ARG B CB  1 
ATOM   2142  C  CG  . ARG B  1 149 ? 66.080  60.075  62.064 1.00 20.04  ? 143 ARG B CG  1 
ATOM   2143  C  CD  . ARG B  1 149 ? 65.347  58.956  61.336 1.00 22.07  ? 143 ARG B CD  1 
ATOM   2144  N  NE  . ARG B  1 149 ? 66.306  58.196  60.533 1.00 15.97  ? 143 ARG B NE  1 
ATOM   2145  C  CZ  . ARG B  1 149 ? 65.995  57.390  59.524 1.00 18.74  ? 143 ARG B CZ  1 
ATOM   2146  N  NH1 . ARG B  1 149 ? 66.967  56.759  58.878 1.00 18.13  ? 143 ARG B NH1 1 
ATOM   2147  N  NH2 . ARG B  1 149 ? 64.729  57.215  59.148 1.00 15.83  ? 143 ARG B NH2 1 
ATOM   2148  N  N   . LEU B  1 150 ? 65.427  63.846  64.987 1.00 22.32  ? 144 LEU B N   1 
ATOM   2149  C  CA  . LEU B  1 150 ? 64.733  64.596  66.022 1.00 23.64  ? 144 LEU B CA  1 
ATOM   2150  C  C   . LEU B  1 150 ? 63.258  64.851  65.733 1.00 22.03  ? 144 LEU B C   1 
ATOM   2151  O  O   . LEU B  1 150 ? 62.449  64.899  66.645 1.00 21.23  ? 144 LEU B O   1 
ATOM   2152  C  CB  . LEU B  1 150 ? 65.435  65.936  66.261 1.00 27.81  ? 144 LEU B CB  1 
ATOM   2153  C  CG  . LEU B  1 150 ? 66.910  65.918  66.645 1.00 32.25  ? 144 LEU B CG  1 
ATOM   2154  C  CD1 . LEU B  1 150 ? 67.369  67.336  66.878 1.00 32.21  ? 144 LEU B CD1 1 
ATOM   2155  C  CD2 . LEU B  1 150 ? 67.118  65.086  67.899 1.00 26.76  ? 144 LEU B CD2 1 
ATOM   2156  N  N   . ALA B  1 151 ? 62.906  65.055  64.472 1.00 22.70  ? 145 ALA B N   1 
ATOM   2157  C  CA  . ALA B  1 151 ? 61.503  65.287  64.124 1.00 23.51  ? 145 ALA B CA  1 
ATOM   2158  C  C   . ALA B  1 151 ? 61.337  65.055  62.636 1.00 21.90  ? 145 ALA B C   1 
ATOM   2159  O  O   . ALA B  1 151 ? 62.280  65.219  61.855 1.00 21.74  ? 145 ALA B O   1 
ATOM   2160  C  CB  . ALA B  1 151 ? 61.064  66.720  64.507 1.00 13.82  ? 145 ALA B CB  1 
ATOM   2161  N  N   . CYS B  1 152 ? 60.129  64.680  62.250 1.00 20.02  ? 146 CYS B N   1 
ATOM   2162  C  CA  . CYS B  1 152 ? 59.823  64.381  60.863 1.00 16.50  ? 146 CYS B CA  1 
ATOM   2163  C  C   . CYS B  1 152 ? 58.359  64.627  60.588 1.00 22.35  ? 146 CYS B C   1 
ATOM   2164  O  O   . CYS B  1 152 ? 57.580  64.965  61.490 1.00 22.38  ? 146 CYS B O   1 
ATOM   2165  C  CB  . CYS B  1 152 ? 60.136  62.913  60.552 1.00 16.76  ? 146 CYS B CB  1 
ATOM   2166  S  SG  . CYS B  1 152 ? 59.353  61.717  61.690 1.00 25.44  ? 146 CYS B SG  1 
ATOM   2167  N  N   . GLY B  1 153 ? 58.002  64.452  59.324 1.00 22.95  ? 147 GLY B N   1 
ATOM   2168  C  CA  . GLY B  1 153 ? 56.632  64.621  58.897 1.00 18.85  ? 147 GLY B CA  1 
ATOM   2169  C  C   . GLY B  1 153 ? 56.541  64.186  57.447 1.00 25.64  ? 147 GLY B C   1 
ATOM   2170  O  O   . GLY B  1 153 ? 57.555  64.163  56.720 1.00 22.56  ? 147 GLY B O   1 
ATOM   2171  N  N   . VAL B  1 154 ? 55.338  63.807  57.026 1.00 17.32  ? 148 VAL B N   1 
ATOM   2172  C  CA  . VAL B  1 154 ? 55.144  63.406  55.652 1.00 19.87  ? 148 VAL B CA  1 
ATOM   2173  C  C   . VAL B  1 154 ? 54.836  64.649  54.838 1.00 20.34  ? 148 VAL B C   1 
ATOM   2174  O  O   . VAL B  1 154 ? 54.046  65.504  55.253 1.00 15.66  ? 148 VAL B O   1 
ATOM   2175  C  CB  . VAL B  1 154 ? 53.999  62.419  55.504 1.00 22.92  ? 148 VAL B CB  1 
ATOM   2176  C  CG1 . VAL B  1 154 ? 53.904  61.983  54.054 1.00 24.33  ? 148 VAL B CG1 1 
ATOM   2177  C  CG2 . VAL B  1 154 ? 54.244  61.202  56.376 1.00 11.64  ? 148 VAL B CG2 1 
ATOM   2178  N  N   . ILE B  1 155 ? 55.460  64.745  53.673 1.00 20.85  ? 149 ILE B N   1 
ATOM   2179  C  CA  . ILE B  1 155 ? 55.274  65.903  52.806 1.00 20.89  ? 149 ILE B CA  1 
ATOM   2180  C  C   . ILE B  1 155 ? 53.970  65.771  52.029 1.00 23.62  ? 149 ILE B C   1 
ATOM   2181  O  O   . ILE B  1 155 ? 53.786  64.803  51.285 1.00 22.99  ? 149 ILE B O   1 
ATOM   2182  C  CB  . ILE B  1 155 ? 56.476  66.023  51.863 1.00 18.50  ? 149 ILE B CB  1 
ATOM   2183  C  CG1 . ILE B  1 155 ? 57.763  66.078  52.700 1.00 23.90  ? 149 ILE B CG1 1 
ATOM   2184  C  CG2 . ILE B  1 155 ? 56.335  67.246  50.984 1.00 19.45  ? 149 ILE B CG2 1 
ATOM   2185  C  CD1 . ILE B  1 155 ? 59.067  65.928  51.896 1.00 24.96  ? 149 ILE B CD1 1 
ATOM   2186  N  N   . GLY B  1 156 ? 53.070  66.744  52.202 1.00 25.00  ? 150 GLY B N   1 
ATOM   2187  C  CA  . GLY B  1 156 ? 51.770  66.710  51.530 1.00 13.73  ? 150 GLY B CA  1 
ATOM   2188  C  C   . GLY B  1 156 ? 51.470  67.818  50.531 1.00 23.29  ? 150 GLY B C   1 
ATOM   2189  O  O   . GLY B  1 156 ? 52.091  68.880  50.559 1.00 33.13  ? 150 GLY B O   1 
ATOM   2190  N  N   . ILE B  1 157 ? 50.512  67.578  49.638 1.00 24.13  ? 151 ILE B N   1 
ATOM   2191  C  CA  . ILE B  1 157 ? 50.139  68.568  48.641 1.00 26.07  ? 151 ILE B CA  1 
ATOM   2192  C  C   . ILE B  1 157 ? 49.496  69.736  49.361 1.00 26.01  ? 151 ILE B C   1 
ATOM   2193  O  O   . ILE B  1 157 ? 48.741  69.522  50.303 1.00 25.74  ? 151 ILE B O   1 
ATOM   2194  C  CB  . ILE B  1 157 ? 49.118  68.002  47.634 1.00 29.24  ? 151 ILE B CB  1 
ATOM   2195  C  CG1 . ILE B  1 157 ? 49.660  66.720  47.010 1.00 44.63  ? 151 ILE B CG1 1 
ATOM   2196  C  CG2 . ILE B  1 157 ? 48.894  68.992  46.514 1.00 30.28  ? 151 ILE B CG2 1 
ATOM   2197  C  CD1 . ILE B  1 157 ? 48.726  66.083  45.988 1.00 51.68  ? 151 ILE B CD1 1 
ATOM   2198  N  N   . ALA B  1 158 ? 49.789  70.965  48.938 1.00 19.96  ? 152 ALA B N   1 
ATOM   2199  C  CA  . ALA B  1 158 ? 49.170  72.131  49.586 1.00 25.72  ? 152 ALA B CA  1 
ATOM   2200  C  C   . ALA B  1 158 ? 48.620  73.083  48.534 1.00 25.56  ? 152 ALA B C   1 
ATOM   2201  O  O   . ALA B  1 158 ? 48.863  72.885  47.350 1.00 26.53  ? 152 ALA B O   1 
ATOM   2202  C  CB  . ALA B  1 158 ? 50.181  72.857  50.475 1.00 21.35  ? 152 ALA B CB  1 
ATOM   2203  N  N   . GLN B  1 159 ? 47.874  74.097  48.976 1.00 32.95  ? 153 GLN B N   1 
ATOM   2204  C  CA  . GLN B  1 159 ? 47.292  75.122  48.093 1.00 41.57  ? 153 GLN B CA  1 
ATOM   2205  C  C   . GLN B  1 159 ? 47.759  76.541  48.477 1.00 47.05  ? 153 GLN B C   1 
ATOM   2206  O  O   . GLN B  1 159 ? 48.353  76.726  49.571 1.00 43.54  ? 153 GLN B O   1 
ATOM   2207  C  CB  . GLN B  1 159 ? 45.751  75.088  48.144 1.00 45.79  ? 153 GLN B CB  1 
ATOM   2208  C  CG  . GLN B  1 159 ? 45.115  75.835  49.322 1.00 40.97  ? 153 GLN B CG  1 
ATOM   2209  C  CD  . GLN B  1 159 ? 43.593  75.725  49.345 1.00 52.53  ? 153 GLN B CD  1 
ATOM   2210  O  OE1 . GLN B  1 159 ? 42.895  76.214  48.445 1.00 51.95  ? 153 GLN B OE1 1 
ATOM   2211  N  NE2 . GLN B  1 159 ? 43.070  75.078  50.381 1.00 49.95  ? 153 GLN B NE2 1 
ATOM   2212  O  OXT . GLN B  1 159 ? 47.501  77.467  47.675 1.00 56.13  ? 153 GLN B OXT 1 
ATOM   2213  N  N   . ALA C  1 7   ? 72.417  110.745 43.414 1.00 75.88  ? 1   ALA C N   1 
ATOM   2214  C  CA  . ALA C  1 7   ? 73.511  111.637 43.922 1.00 76.49  ? 1   ALA C CA  1 
ATOM   2215  C  C   . ALA C  1 7   ? 74.614  110.877 44.693 1.00 70.25  ? 1   ALA C C   1 
ATOM   2216  O  O   . ALA C  1 7   ? 74.321  110.209 45.687 1.00 68.00  ? 1   ALA C O   1 
ATOM   2217  C  CB  . ALA C  1 7   ? 72.897  112.719 44.818 1.00 75.23  ? 1   ALA C CB  1 
ATOM   2218  N  N   . THR C  1 8   ? 75.870  110.974 44.248 1.00 58.07  ? 2   THR C N   1 
ATOM   2219  C  CA  . THR C  1 8   ? 76.945  110.288 44.963 1.00 51.40  ? 2   THR C CA  1 
ATOM   2220  C  C   . THR C  1 8   ? 77.135  111.000 46.300 1.00 49.88  ? 2   THR C C   1 
ATOM   2221  O  O   . THR C  1 8   ? 77.048  112.227 46.384 1.00 43.88  ? 2   THR C O   1 
ATOM   2222  C  CB  . THR C  1 8   ? 78.304  110.314 44.216 1.00 47.54  ? 2   THR C CB  1 
ATOM   2223  O  OG1 . THR C  1 8   ? 78.116  110.007 42.835 1.00 52.77  ? 2   THR C OG1 1 
ATOM   2224  C  CG2 . THR C  1 8   ? 79.227  109.266 44.787 1.00 45.76  ? 2   THR C CG2 1 
ATOM   2225  N  N   . LYS C  1 9   ? 77.389  110.222 47.345 1.00 42.95  ? 3   LYS C N   1 
ATOM   2226  C  CA  . LYS C  1 9   ? 77.581  110.774 48.670 1.00 41.62  ? 3   LYS C CA  1 
ATOM   2227  C  C   . LYS C  1 9   ? 78.751  110.109 49.376 1.00 35.69  ? 3   LYS C C   1 
ATOM   2228  O  O   . LYS C  1 9   ? 79.004  108.925 49.191 1.00 45.61  ? 3   LYS C O   1 
ATOM   2229  C  CB  . LYS C  1 9   ? 76.306  110.599 49.494 1.00 44.54  ? 3   LYS C CB  1 
ATOM   2230  C  CG  . LYS C  1 9   ? 75.095  111.254 48.861 1.00 59.28  ? 3   LYS C CG  1 
ATOM   2231  C  CD  . LYS C  1 9   ? 73.835  111.059 49.689 1.00 66.88  ? 3   LYS C CD  1 
ATOM   2232  C  CE  . LYS C  1 9   ? 72.620  111.631 48.963 1.00 75.98  ? 3   LYS C CE  1 
ATOM   2233  N  NZ  . LYS C  1 9   ? 71.348  111.441 49.721 1.00 80.29  ? 3   LYS C NZ  1 
ATOM   2234  N  N   . ALA C  1 10  ? 79.483  110.885 50.165 1.00 34.55  ? 4   ALA C N   1 
ATOM   2235  C  CA  . ALA C  1 10  ? 80.615  110.355 50.923 1.00 36.41  ? 4   ALA C CA  1 
ATOM   2236  C  C   . ALA C  1 10  ? 80.524  110.887 52.339 1.00 33.27  ? 4   ALA C C   1 
ATOM   2237  O  O   . ALA C  1 10  ? 79.764  111.825 52.615 1.00 26.33  ? 4   ALA C O   1 
ATOM   2238  C  CB  . ALA C  1 10  ? 81.937  110.768 50.293 1.00 23.28  ? 4   ALA C CB  1 
ATOM   2239  N  N   . VAL C  1 11  ? 81.285  110.278 53.241 1.00 27.26  ? 5   VAL C N   1 
ATOM   2240  C  CA  . VAL C  1 11  ? 81.284  110.712 54.626 1.00 23.17  ? 5   VAL C CA  1 
ATOM   2241  C  C   . VAL C  1 11  ? 82.670  110.439 55.206 1.00 28.44  ? 5   VAL C C   1 
ATOM   2242  O  O   . VAL C  1 11  ? 83.424  109.621 54.679 1.00 30.60  ? 5   VAL C O   1 
ATOM   2243  C  CB  . VAL C  1 11  ? 80.182  109.972 55.420 1.00 26.87  ? 5   VAL C CB  1 
ATOM   2244  C  CG1 . VAL C  1 11  ? 80.510  108.495 55.494 1.00 22.07  ? 5   VAL C CG1 1 
ATOM   2245  C  CG2 . VAL C  1 11  ? 80.013  110.595 56.811 1.00 15.74  ? 5   VAL C CG2 1 
ATOM   2246  N  N   . CYS C  1 12  ? 83.015  111.149 56.273 1.00 29.75  ? 6   CYS C N   1 
ATOM   2247  C  CA  . CYS C  1 12  ? 84.314  110.995 56.907 1.00 23.49  ? 6   CYS C CA  1 
ATOM   2248  C  C   . CYS C  1 12  ? 84.217  111.264 58.399 1.00 26.03  ? 6   CYS C C   1 
ATOM   2249  O  O   . CYS C  1 12  ? 83.598  112.238 58.826 1.00 26.51  ? 6   CYS C O   1 
ATOM   2250  C  CB  . CYS C  1 12  ? 85.302  111.966 56.272 1.00 30.10  ? 6   CYS C CB  1 
ATOM   2251  S  SG  . CYS C  1 12  ? 86.987  111.928 56.940 1.00 28.74  ? 6   CYS C SG  1 
ATOM   2252  N  N   . VAL C  1 13  ? 84.797  110.379 59.197 1.00 25.05  ? 7   VAL C N   1 
ATOM   2253  C  CA  . VAL C  1 13  ? 84.790  110.560 60.637 1.00 22.73  ? 7   VAL C CA  1 
ATOM   2254  C  C   . VAL C  1 13  ? 86.199  111.031 60.968 1.00 29.18  ? 7   VAL C C   1 
ATOM   2255  O  O   . VAL C  1 13  ? 87.176  110.338 60.688 1.00 34.91  ? 7   VAL C O   1 
ATOM   2256  C  CB  . VAL C  1 13  ? 84.470  109.228 61.390 1.00 27.73  ? 7   VAL C CB  1 
ATOM   2257  C  CG1 . VAL C  1 13  ? 84.638  109.418 62.911 1.00 18.30  ? 7   VAL C CG1 1 
ATOM   2258  C  CG2 . VAL C  1 13  ? 83.039  108.771 61.079 1.00 18.44  ? 7   VAL C CG2 1 
ATOM   2259  N  N   . LEU C  1 14  ? 86.312  112.228 61.527 1.00 30.55  ? 8   LEU C N   1 
ATOM   2260  C  CA  . LEU C  1 14  ? 87.619  112.765 61.873 1.00 29.36  ? 8   LEU C CA  1 
ATOM   2261  C  C   . LEU C  1 14  ? 87.957  112.389 63.299 1.00 28.25  ? 8   LEU C C   1 
ATOM   2262  O  O   . LEU C  1 14  ? 87.163  112.617 64.210 1.00 23.72  ? 8   LEU C O   1 
ATOM   2263  C  CB  . LEU C  1 14  ? 87.617  114.286 61.759 1.00 34.07  ? 8   LEU C CB  1 
ATOM   2264  C  CG  . LEU C  1 14  ? 87.315  114.917 60.400 1.00 38.69  ? 8   LEU C CG  1 
ATOM   2265  C  CD1 . LEU C  1 14  ? 87.052  116.387 60.619 1.00 34.47  ? 8   LEU C CD1 1 
ATOM   2266  C  CD2 . LEU C  1 14  ? 88.472  114.723 59.429 1.00 35.88  ? 8   LEU C CD2 1 
ATOM   2267  N  N   . LYS C  1 15  ? 89.129  111.803 63.496 1.00 24.52  ? 9   LYS C N   1 
ATOM   2268  C  CA  . LYS C  1 15  ? 89.551  111.446 64.842 1.00 28.70  ? 9   LYS C CA  1 
ATOM   2269  C  C   . LYS C  1 15  ? 91.030  111.723 64.969 1.00 29.48  ? 9   LYS C C   1 
ATOM   2270  O  O   . LYS C  1 15  ? 91.721  111.864 63.960 1.00 28.22  ? 9   LYS C O   1 
ATOM   2271  C  CB  . LYS C  1 15  ? 89.256  109.975 65.137 1.00 21.58  ? 9   LYS C CB  1 
ATOM   2272  C  CG  . LYS C  1 15  ? 87.794  109.713 65.419 1.00 41.09  ? 9   LYS C CG  1 
ATOM   2273  C  CD  . LYS C  1 15  ? 87.527  108.251 65.735 1.00 41.69  ? 9   LYS C CD  1 
ATOM   2274  C  CE  . LYS C  1 15  ? 86.083  108.051 66.155 1.00 46.22  ? 9   LYS C CE  1 
ATOM   2275  N  NZ  . LYS C  1 15  ? 85.803  106.638 66.508 1.00 53.32  ? 9   LYS C NZ  1 
ATOM   2276  N  N   . GLY C  1 16  ? 91.504  111.826 66.207 1.00 26.97  ? 10  GLY C N   1 
ATOM   2277  C  CA  . GLY C  1 16  ? 92.912  112.069 66.445 1.00 31.65  ? 10  GLY C CA  1 
ATOM   2278  C  C   . GLY C  1 16  ? 93.364  111.639 67.834 1.00 35.96  ? 10  GLY C C   1 
ATOM   2279  O  O   . GLY C  1 16  ? 92.653  110.913 68.542 1.00 32.89  ? 10  GLY C O   1 
ATOM   2280  N  N   . ASP C  1 17  ? 94.557  112.083 68.215 1.00 35.37  ? 11  ASP C N   1 
ATOM   2281  C  CA  . ASP C  1 17  ? 95.123  111.774 69.519 1.00 44.97  ? 11  ASP C CA  1 
ATOM   2282  C  C   . ASP C  1 17  ? 94.519  112.736 70.514 1.00 42.70  ? 11  ASP C C   1 
ATOM   2283  O  O   . ASP C  1 17  ? 94.288  112.392 71.671 1.00 49.61  ? 11  ASP C O   1 
ATOM   2284  C  CB  . ASP C  1 17  ? 96.638  111.959 69.499 1.00 52.63  ? 11  ASP C CB  1 
ATOM   2285  C  CG  . ASP C  1 17  ? 97.329  110.989 68.566 1.00 67.36  ? 11  ASP C CG  1 
ATOM   2286  O  OD1 . ASP C  1 17  ? 98.507  111.236 68.223 1.00 70.56  ? 11  ASP C OD1 1 
ATOM   2287  O  OD2 . ASP C  1 17  ? 96.701  109.974 68.182 1.00 70.15  ? 11  ASP C OD2 1 
ATOM   2288  N  N   . GLY C  1 18  ? 94.279  113.953 70.045 1.00 39.65  ? 12  GLY C N   1 
ATOM   2289  C  CA  . GLY C  1 18  ? 93.700  114.976 70.886 1.00 33.52  ? 12  GLY C CA  1 
ATOM   2290  C  C   . GLY C  1 18  ? 92.193  114.895 70.939 1.00 34.37  ? 12  GLY C C   1 
ATOM   2291  O  O   . GLY C  1 18  ? 91.608  113.887 70.561 1.00 37.91  ? 12  GLY C O   1 
ATOM   2292  N  N   . PRO C  1 19  ? 91.528  115.964 71.382 1.00 34.27  ? 13  PRO C N   1 
ATOM   2293  C  CA  . PRO C  1 19  ? 90.069  115.985 71.482 1.00 30.91  ? 13  PRO C CA  1 
ATOM   2294  C  C   . PRO C  1 19  ? 89.318  116.332 70.210 1.00 27.67  ? 13  PRO C C   1 
ATOM   2295  O  O   . PRO C  1 19  ? 88.097  116.230 70.190 1.00 33.18  ? 13  PRO C O   1 
ATOM   2296  C  CB  . PRO C  1 19  ? 89.832  117.029 72.556 1.00 31.88  ? 13  PRO C CB  1 
ATOM   2297  C  CG  . PRO C  1 19  ? 90.862  118.069 72.182 1.00 29.85  ? 13  PRO C CG  1 
ATOM   2298  C  CD  . PRO C  1 19  ? 92.106  117.223 71.890 1.00 32.28  ? 13  PRO C CD  1 
ATOM   2299  N  N   . VAL C  1 20  ? 90.025  116.755 69.165 1.00 20.99  ? 14  VAL C N   1 
ATOM   2300  C  CA  . VAL C  1 20  ? 89.357  117.130 67.910 1.00 27.14  ? 14  VAL C CA  1 
ATOM   2301  C  C   . VAL C  1 20  ? 88.673  115.966 67.197 1.00 23.27  ? 14  VAL C C   1 
ATOM   2302  O  O   . VAL C  1 20  ? 89.298  114.959 66.895 1.00 26.65  ? 14  VAL C O   1 
ATOM   2303  C  CB  . VAL C  1 20  ? 90.337  117.792 66.912 1.00 30.43  ? 14  VAL C CB  1 
ATOM   2304  C  CG1 . VAL C  1 20  ? 89.603  118.152 65.626 1.00 31.77  ? 14  VAL C CG1 1 
ATOM   2305  C  CG2 . VAL C  1 20  ? 90.930  119.050 67.523 1.00 30.06  ? 14  VAL C CG2 1 
ATOM   2306  N  N   . GLN C  1 21  ? 87.387  116.121 66.902 1.00 29.73  ? 15  GLN C N   1 
ATOM   2307  C  CA  . GLN C  1 21  ? 86.630  115.065 66.238 1.00 31.96  ? 15  GLN C CA  1 
ATOM   2308  C  C   . GLN C  1 21  ? 85.343  115.599 65.621 1.00 32.72  ? 15  GLN C C   1 
ATOM   2309  O  O   . GLN C  1 21  ? 84.773  116.586 66.082 1.00 35.62  ? 15  GLN C O   1 
ATOM   2310  C  CB  . GLN C  1 21  ? 86.306  113.937 67.239 1.00 30.66  ? 15  GLN C CB  1 
ATOM   2311  C  CG  . GLN C  1 21  ? 85.406  114.331 68.403 1.00 39.39  ? 15  GLN C CG  1 
ATOM   2312  C  CD  . GLN C  1 21  ? 85.546  113.403 69.617 1.00 49.61  ? 15  GLN C CD  1 
ATOM   2313  O  OE1 . GLN C  1 21  ? 85.507  112.174 69.489 1.00 54.23  ? 15  GLN C OE1 1 
ATOM   2314  N  NE2 . GLN C  1 21  ? 85.702  113.995 70.801 1.00 47.74  ? 15  GLN C NE2 1 
ATOM   2315  N  N   . GLY C  1 22  ? 84.888  114.947 64.562 1.00 35.75  ? 16  GLY C N   1 
ATOM   2316  C  CA  . GLY C  1 22  ? 83.671  115.394 63.915 1.00 33.42  ? 16  GLY C CA  1 
ATOM   2317  C  C   . GLY C  1 22  ? 83.259  114.533 62.743 1.00 30.93  ? 16  GLY C C   1 
ATOM   2318  O  O   . GLY C  1 22  ? 83.955  113.599 62.353 1.00 35.64  ? 16  GLY C O   1 
ATOM   2319  N  N   . ILE C  1 23  ? 82.110  114.847 62.175 1.00 32.84  ? 17  ILE C N   1 
ATOM   2320  C  CA  . ILE C  1 23  ? 81.617  114.097 61.044 1.00 31.37  ? 17  ILE C CA  1 
ATOM   2321  C  C   . ILE C  1 23  ? 81.432  115.047 59.880 1.00 32.38  ? 17  ILE C C   1 
ATOM   2322  O  O   . ILE C  1 23  ? 80.743  116.057 59.998 1.00 34.22  ? 17  ILE C O   1 
ATOM   2323  C  CB  . ILE C  1 23  ? 80.284  113.426 61.390 1.00 30.57  ? 17  ILE C CB  1 
ATOM   2324  C  CG1 . ILE C  1 23  ? 80.514  112.400 62.502 1.00 26.22  ? 17  ILE C CG1 1 
ATOM   2325  C  CG2 . ILE C  1 23  ? 79.672  112.790 60.140 1.00 20.49  ? 17  ILE C CG2 1 
ATOM   2326  C  CD1 . ILE C  1 23  ? 79.252  111.772 63.015 1.00 27.89  ? 17  ILE C CD1 1 
ATOM   2327  N  N   . ILE C  1 24  ? 82.058  114.733 58.758 1.00 28.45  ? 18  ILE C N   1 
ATOM   2328  C  CA  . ILE C  1 24  ? 81.928  115.577 57.586 1.00 28.53  ? 18  ILE C CA  1 
ATOM   2329  C  C   . ILE C  1 24  ? 81.242  114.833 56.441 1.00 31.18  ? 18  ILE C C   1 
ATOM   2330  O  O   . ILE C  1 24  ? 81.710  113.782 55.987 1.00 26.05  ? 18  ILE C O   1 
ATOM   2331  C  CB  . ILE C  1 24  ? 83.300  116.053 57.093 1.00 29.79  ? 18  ILE C CB  1 
ATOM   2332  C  CG1 . ILE C  1 24  ? 83.972  116.923 58.169 1.00 26.72  ? 18  ILE C CG1 1 
ATOM   2333  C  CG2 . ILE C  1 24  ? 83.148  116.749 55.740 1.00 23.25  ? 18  ILE C CG2 1 
ATOM   2334  C  CD1 . ILE C  1 24  ? 83.276  118.229 58.487 1.00 27.16  ? 18  ILE C CD1 1 
ATOM   2335  N  N   . ASN C  1 25  ? 80.134  115.394 55.972 1.00 29.23  ? 19  ASN C N   1 
ATOM   2336  C  CA  . ASN C  1 25  ? 79.385  114.821 54.862 1.00 26.78  ? 19  ASN C CA  1 
ATOM   2337  C  C   . ASN C  1 25  ? 79.782  115.455 53.531 1.00 26.65  ? 19  ASN C C   1 
ATOM   2338  O  O   . ASN C  1 25  ? 80.214  116.598 53.494 1.00 31.24  ? 19  ASN C O   1 
ATOM   2339  C  CB  . ASN C  1 25  ? 77.898  115.024 55.102 1.00 25.77  ? 19  ASN C CB  1 
ATOM   2340  C  CG  . ASN C  1 25  ? 77.426  114.345 56.360 1.00 30.53  ? 19  ASN C CG  1 
ATOM   2341  O  OD1 . ASN C  1 25  ? 77.390  113.114 56.441 1.00 39.71  ? 19  ASN C OD1 1 
ATOM   2342  N  ND2 . ASN C  1 25  ? 77.072  115.138 57.363 1.00 27.03  ? 19  ASN C ND2 1 
ATOM   2343  N  N   . PHE C  1 26  ? 79.656  114.694 52.447 1.00 32.31  ? 20  PHE C N   1 
ATOM   2344  C  CA  . PHE C  1 26  ? 79.953  115.174 51.095 1.00 33.66  ? 20  PHE C CA  1 
ATOM   2345  C  C   . PHE C  1 26  ? 78.748  114.802 50.241 1.00 40.69  ? 20  PHE C C   1 
ATOM   2346  O  O   . PHE C  1 26  ? 78.051  113.833 50.546 1.00 36.77  ? 20  PHE C O   1 
ATOM   2347  C  CB  . PHE C  1 26  ? 81.175  114.485 50.494 1.00 31.19  ? 20  PHE C CB  1 
ATOM   2348  C  CG  . PHE C  1 26  ? 82.449  114.762 51.213 1.00 40.21  ? 20  PHE C CG  1 
ATOM   2349  C  CD1 . PHE C  1 26  ? 83.439  115.531 50.620 1.00 43.58  ? 20  PHE C CD1 1 
ATOM   2350  C  CD2 . PHE C  1 26  ? 82.681  114.223 52.475 1.00 42.82  ? 20  PHE C CD2 1 
ATOM   2351  C  CE1 . PHE C  1 26  ? 84.653  115.758 51.272 1.00 50.52  ? 20  PHE C CE1 1 
ATOM   2352  C  CE2 . PHE C  1 26  ? 83.888  114.442 53.136 1.00 44.21  ? 20  PHE C CE2 1 
ATOM   2353  C  CZ  . PHE C  1 26  ? 84.876  115.210 52.534 1.00 48.81  ? 20  PHE C CZ  1 
ATOM   2354  N  N   . GLU C  1 27  ? 78.495  115.569 49.186 1.00 40.53  ? 21  GLU C N   1 
ATOM   2355  C  CA  . GLU C  1 27  ? 77.384  115.278 48.291 1.00 44.19  ? 21  GLU C CA  1 
ATOM   2356  C  C   . GLU C  1 27  ? 77.601  115.924 46.939 1.00 42.89  ? 21  GLU C C   1 
ATOM   2357  O  O   . GLU C  1 27  ? 77.877  117.114 46.849 1.00 43.70  ? 21  GLU C O   1 
ATOM   2358  C  CB  . GLU C  1 27  ? 76.066  115.755 48.880 1.00 45.77  ? 21  GLU C CB  1 
ATOM   2359  C  CG  . GLU C  1 27  ? 74.883  115.420 47.989 1.00 67.39  ? 21  GLU C CG  1 
ATOM   2360  C  CD  . GLU C  1 27  ? 73.547  115.522 48.703 1.00 72.66  ? 21  GLU C CD  1 
ATOM   2361  O  OE1 . GLU C  1 27  ? 72.504  115.404 48.028 1.00 77.62  ? 21  GLU C OE1 1 
ATOM   2362  O  OE2 . GLU C  1 27  ? 73.539  115.711 49.938 1.00 77.40  ? 21  GLU C OE2 1 
ATOM   2363  N  N   . GLN C  1 28  ? 77.500  115.131 45.883 1.00 42.31  ? 22  GLN C N   1 
ATOM   2364  C  CA  . GLN C  1 28  ? 77.694  115.651 44.538 1.00 47.84  ? 22  GLN C CA  1 
ATOM   2365  C  C   . GLN C  1 28  ? 76.630  115.083 43.596 1.00 53.69  ? 22  GLN C C   1 
ATOM   2366  O  O   . GLN C  1 28  ? 76.787  113.997 43.027 1.00 54.57  ? 22  GLN C O   1 
ATOM   2367  C  CB  . GLN C  1 28  ? 79.100  115.303 44.052 1.00 42.95  ? 22  GLN C CB  1 
ATOM   2368  C  CG  . GLN C  1 28  ? 79.404  115.735 42.639 1.00 29.29  ? 22  GLN C CG  1 
ATOM   2369  C  CD  . GLN C  1 28  ? 80.739  115.218 42.175 1.00 31.61  ? 22  GLN C CD  1 
ATOM   2370  O  OE1 . GLN C  1 28  ? 81.190  114.151 42.603 1.00 37.67  ? 22  GLN C OE1 1 
ATOM   2371  N  NE2 . GLN C  1 28  ? 81.380  115.955 41.286 1.00 30.78  ? 22  GLN C NE2 1 
ATOM   2372  N  N   . LYS C  1 29  ? 75.544  115.839 43.451 1.00 56.37  ? 23  LYS C N   1 
ATOM   2373  C  CA  . LYS C  1 29  ? 74.411  115.463 42.614 1.00 55.63  ? 23  LYS C CA  1 
ATOM   2374  C  C   . LYS C  1 29  ? 74.776  115.185 41.163 1.00 55.74  ? 23  LYS C C   1 
ATOM   2375  O  O   . LYS C  1 29  ? 74.162  114.337 40.531 1.00 52.96  ? 23  LYS C O   1 
ATOM   2376  C  CB  . LYS C  1 29  ? 73.354  116.571 42.635 1.00 59.99  ? 23  LYS C CB  1 
ATOM   2377  C  CG  . LYS C  1 29  ? 72.881  117.001 44.019 1.00 73.64  ? 23  LYS C CG  1 
ATOM   2378  C  CD  . LYS C  1 29  ? 72.066  118.299 43.935 1.00 81.19  ? 23  LYS C CD  1 
ATOM   2379  C  CE  . LYS C  1 29  ? 71.667  118.829 45.314 1.00 82.44  ? 23  LYS C CE  1 
ATOM   2380  N  NZ  . LYS C  1 29  ? 71.038  120.181 45.235 1.00 80.96  ? 23  LYS C NZ  1 
ATOM   2381  N  N   . GLU C  1 30  ? 75.775  115.889 40.639 1.00 57.89  ? 24  GLU C N   1 
ATOM   2382  C  CA  . GLU C  1 30  ? 76.150  115.730 39.239 1.00 58.95  ? 24  GLU C CA  1 
ATOM   2383  C  C   . GLU C  1 30  ? 77.616  115.385 39.000 1.00 53.54  ? 24  GLU C C   1 
ATOM   2384  O  O   . GLU C  1 30  ? 78.511  116.084 39.444 1.00 52.76  ? 24  GLU C O   1 
ATOM   2385  C  CB  . GLU C  1 30  ? 75.801  117.018 38.480 1.00 71.11  ? 24  GLU C CB  1 
ATOM   2386  C  CG  . GLU C  1 30  ? 75.362  116.831 37.030 1.00 83.49  ? 24  GLU C CG  1 
ATOM   2387  C  CD  . GLU C  1 30  ? 73.980  116.202 36.906 1.00 93.17  ? 24  GLU C CD  1 
ATOM   2388  O  OE1 . GLU C  1 30  ? 73.012  116.760 37.466 1.00 92.73  ? 24  GLU C OE1 1 
ATOM   2389  O  OE2 . GLU C  1 30  ? 73.861  115.148 36.245 1.00 97.26  ? 24  GLU C OE2 1 
ATOM   2390  N  N   . SER C  1 31  ? 77.832  114.302 38.267 1.00 57.36  ? 25  SER C N   1 
ATOM   2391  C  CA  . SER C  1 31  ? 79.155  113.794 37.912 1.00 58.08  ? 25  SER C CA  1 
ATOM   2392  C  C   . SER C  1 31  ? 80.202  114.858 37.605 1.00 57.96  ? 25  SER C C   1 
ATOM   2393  O  O   . SER C  1 31  ? 81.327  114.787 38.099 1.00 59.78  ? 25  SER C O   1 
ATOM   2394  C  CB  . SER C  1 31  ? 79.023  112.854 36.707 1.00 59.92  ? 25  SER C CB  1 
ATOM   2395  O  OG  . SER C  1 31  ? 80.261  112.692 36.034 1.00 64.79  ? 25  SER C OG  1 
ATOM   2396  N  N   . ASN C  1 32  ? 79.844  115.823 36.763 1.00 58.78  ? 26  ASN C N   1 
ATOM   2397  C  CA  . ASN C  1 32  ? 80.768  116.891 36.398 1.00 59.79  ? 26  ASN C CA  1 
ATOM   2398  C  C   . ASN C  1 32  ? 80.378  118.184 37.121 1.00 59.09  ? 26  ASN C C   1 
ATOM   2399  O  O   . ASN C  1 32  ? 80.876  119.268 36.811 1.00 57.49  ? 26  ASN C O   1 
ATOM   2400  C  CB  . ASN C  1 32  ? 80.820  117.065 34.855 1.00 60.27  ? 26  ASN C CB  1 
ATOM   2401  C  CG  . ASN C  1 32  ? 79.480  117.504 34.235 1.00 58.99  ? 26  ASN C CG  1 
ATOM   2402  O  OD1 . ASN C  1 32  ? 78.395  117.157 34.717 1.00 53.16  ? 26  ASN C OD1 1 
ATOM   2403  N  ND2 . ASN C  1 32  ? 79.565  118.254 33.135 1.00 45.70  ? 26  ASN C ND2 1 
ATOM   2404  N  N   . GLY C  1 33  ? 79.502  118.033 38.115 1.00 54.22  ? 27  GLY C N   1 
ATOM   2405  C  CA  . GLY C  1 33  ? 79.039  119.156 38.913 1.00 53.91  ? 27  GLY C CA  1 
ATOM   2406  C  C   . GLY C  1 33  ? 79.871  119.405 40.162 1.00 50.73  ? 27  GLY C C   1 
ATOM   2407  O  O   . GLY C  1 33  ? 80.883  118.746 40.379 1.00 52.16  ? 27  GLY C O   1 
ATOM   2408  N  N   . PRO C  1 34  ? 79.453  120.344 41.018 1.00 49.18  ? 28  PRO C N   1 
ATOM   2409  C  CA  . PRO C  1 34  ? 80.173  120.680 42.247 1.00 49.72  ? 28  PRO C CA  1 
ATOM   2410  C  C   . PRO C  1 34  ? 79.890  119.737 43.404 1.00 46.95  ? 28  PRO C C   1 
ATOM   2411  O  O   . PRO C  1 34  ? 78.885  119.030 43.397 1.00 48.73  ? 28  PRO C O   1 
ATOM   2412  C  CB  . PRO C  1 34  ? 79.676  122.088 42.537 1.00 49.44  ? 28  PRO C CB  1 
ATOM   2413  C  CG  . PRO C  1 34  ? 78.208  121.964 42.197 1.00 39.14  ? 28  PRO C CG  1 
ATOM   2414  C  CD  . PRO C  1 34  ? 78.256  121.196 40.870 1.00 48.48  ? 28  PRO C CD  1 
ATOM   2415  N  N   . VAL C  1 35  ? 80.779  119.752 44.400 1.00 48.81  ? 29  VAL C N   1 
ATOM   2416  C  CA  . VAL C  1 35  ? 80.646  118.924 45.604 1.00 41.02  ? 29  VAL C CA  1 
ATOM   2417  C  C   . VAL C  1 35  ? 80.296  119.792 46.810 1.00 35.04  ? 29  VAL C C   1 
ATOM   2418  O  O   . VAL C  1 35  ? 80.932  120.813 47.044 1.00 34.46  ? 29  VAL C O   1 
ATOM   2419  C  CB  . VAL C  1 35  ? 81.956  118.181 45.942 1.00 37.42  ? 29  VAL C CB  1 
ATOM   2420  C  CG1 . VAL C  1 35  ? 81.732  117.257 47.131 1.00 43.31  ? 29  VAL C CG1 1 
ATOM   2421  C  CG2 . VAL C  1 35  ? 82.435  117.387 44.753 1.00 35.79  ? 29  VAL C CG2 1 
ATOM   2422  N  N   . LYS C  1 36  ? 79.289  119.373 47.572 1.00 32.90  ? 30  LYS C N   1 
ATOM   2423  C  CA  . LYS C  1 36  ? 78.851  120.084 48.774 1.00 35.89  ? 30  LYS C CA  1 
ATOM   2424  C  C   . LYS C  1 36  ? 79.472  119.408 49.999 1.00 38.36  ? 30  LYS C C   1 
ATOM   2425  O  O   . LYS C  1 36  ? 79.266  118.223 50.220 1.00 43.57  ? 30  LYS C O   1 
ATOM   2426  C  CB  . LYS C  1 36  ? 77.320  120.036 48.887 1.00 39.43  ? 30  LYS C CB  1 
ATOM   2427  C  CG  . LYS C  1 36  ? 76.727  120.706 50.137 1.00 50.73  ? 30  LYS C CG  1 
ATOM   2428  C  CD  . LYS C  1 36  ? 76.700  122.235 50.011 1.00 67.33  ? 30  LYS C CD  1 
ATOM   2429  C  CE  . LYS C  1 36  ? 76.001  122.915 51.196 1.00 68.44  ? 30  LYS C CE  1 
ATOM   2430  N  NZ  . LYS C  1 36  ? 76.833  122.951 52.438 1.00 63.99  ? 30  LYS C NZ  1 
ATOM   2431  N  N   . VAL C  1 37  ? 80.214  120.165 50.801 1.00 37.96  ? 31  VAL C N   1 
ATOM   2432  C  CA  . VAL C  1 37  ? 80.870  119.622 51.987 1.00 31.11  ? 31  VAL C CA  1 
ATOM   2433  C  C   . VAL C  1 37  ? 80.351  120.252 53.260 1.00 37.23  ? 31  VAL C C   1 
ATOM   2434  O  O   . VAL C  1 37  ? 80.522  121.451 53.467 1.00 36.42  ? 31  VAL C O   1 
ATOM   2435  C  CB  . VAL C  1 37  ? 82.372  119.882 51.946 1.00 27.60  ? 31  VAL C CB  1 
ATOM   2436  C  CG1 . VAL C  1 37  ? 83.047  119.065 53.018 1.00 34.26  ? 31  VAL C CG1 1 
ATOM   2437  C  CG2 . VAL C  1 37  ? 82.931  119.570 50.540 1.00 21.12  ? 31  VAL C CG2 1 
ATOM   2438  N  N   . TRP C  1 38  ? 79.752  119.459 54.141 1.00 35.09  ? 32  TRP C N   1 
ATOM   2439  C  CA  . TRP C  1 38  ? 79.230  120.050 55.362 1.00 36.70  ? 32  TRP C CA  1 
ATOM   2440  C  C   . TRP C  1 38  ? 79.323  119.162 56.578 1.00 38.20  ? 32  TRP C C   1 
ATOM   2441  O  O   . TRP C  1 38  ? 79.329  117.939 56.469 1.00 41.34  ? 32  TRP C O   1 
ATOM   2442  C  CB  . TRP C  1 38  ? 77.771  120.469 55.158 1.00 39.52  ? 32  TRP C CB  1 
ATOM   2443  C  CG  . TRP C  1 38  ? 76.774  119.348 55.186 1.00 34.73  ? 32  TRP C CG  1 
ATOM   2444  C  CD1 . TRP C  1 38  ? 75.949  119.008 56.225 1.00 40.54  ? 32  TRP C CD1 1 
ATOM   2445  C  CD2 . TRP C  1 38  ? 76.460  118.452 54.117 1.00 37.61  ? 32  TRP C CD2 1 
ATOM   2446  N  NE1 . TRP C  1 38  ? 75.130  117.958 55.863 1.00 37.10  ? 32  TRP C NE1 1 
ATOM   2447  C  CE2 . TRP C  1 38  ? 75.423  117.597 54.573 1.00 44.04  ? 32  TRP C CE2 1 
ATOM   2448  C  CE3 . TRP C  1 38  ? 76.950  118.285 52.815 1.00 42.10  ? 32  TRP C CE3 1 
ATOM   2449  C  CZ2 . TRP C  1 38  ? 74.865  116.592 53.767 1.00 45.00  ? 32  TRP C CZ2 1 
ATOM   2450  C  CZ3 . TRP C  1 38  ? 76.392  117.279 52.010 1.00 51.98  ? 32  TRP C CZ3 1 
ATOM   2451  C  CH2 . TRP C  1 38  ? 75.360  116.449 52.492 1.00 45.53  ? 32  TRP C CH2 1 
ATOM   2452  N  N   . GLY C  1 39  ? 79.384  119.794 57.746 1.00 35.39  ? 33  GLY C N   1 
ATOM   2453  C  CA  . GLY C  1 39  ? 79.464  119.037 58.976 1.00 36.89  ? 33  GLY C CA  1 
ATOM   2454  C  C   . GLY C  1 39  ? 79.726  119.854 60.222 1.00 35.73  ? 33  GLY C C   1 
ATOM   2455  O  O   . GLY C  1 39  ? 79.309  120.992 60.367 1.00 40.84  ? 33  GLY C O   1 
ATOM   2456  N  N   . SER C  1 40  ? 80.445  119.257 61.144 1.00 36.31  ? 34  SER C N   1 
ATOM   2457  C  CA  . SER C  1 40  ? 80.741  119.932 62.379 1.00 37.60  ? 34  SER C CA  1 
ATOM   2458  C  C   . SER C  1 40  ? 81.943  119.232 62.988 1.00 35.85  ? 34  SER C C   1 
ATOM   2459  O  O   . SER C  1 40  ? 82.038  118.008 62.953 1.00 34.80  ? 34  SER C O   1 
ATOM   2460  C  CB  . SER C  1 40  ? 79.523  119.832 63.296 1.00 28.54  ? 34  SER C CB  1 
ATOM   2461  O  OG  . SER C  1 40  ? 79.713  120.568 64.472 1.00 51.43  ? 34  SER C OG  1 
ATOM   2462  N  N   . ILE C  1 41  ? 82.873  120.015 63.515 1.00 36.03  ? 35  ILE C N   1 
ATOM   2463  C  CA  . ILE C  1 41  ? 84.069  119.474 64.145 1.00 34.70  ? 35  ILE C CA  1 
ATOM   2464  C  C   . ILE C  1 41  ? 84.142  120.109 65.522 1.00 37.28  ? 35  ILE C C   1 
ATOM   2465  O  O   . ILE C  1 41  ? 83.962  121.324 65.646 1.00 46.29  ? 35  ILE C O   1 
ATOM   2466  C  CB  . ILE C  1 41  ? 85.331  119.850 63.347 1.00 26.51  ? 35  ILE C CB  1 
ATOM   2467  C  CG1 . ILE C  1 41  ? 85.177  119.388 61.902 1.00 27.02  ? 35  ILE C CG1 1 
ATOM   2468  C  CG2 . ILE C  1 41  ? 86.562  119.192 63.957 1.00 20.94  ? 35  ILE C CG2 1 
ATOM   2469  C  CD1 . ILE C  1 41  ? 86.354  119.758 61.013 1.00 27.41  ? 35  ILE C CD1 1 
ATOM   2470  N  N   . LYS C  1 42  ? 84.378  119.313 66.559 1.00 33.38  ? 36  LYS C N   1 
ATOM   2471  C  CA  . LYS C  1 42  ? 84.476  119.886 67.900 1.00 32.11  ? 36  LYS C CA  1 
ATOM   2472  C  C   . LYS C  1 42  ? 85.885  119.715 68.457 1.00 32.00  ? 36  LYS C C   1 
ATOM   2473  O  O   . LYS C  1 42  ? 86.715  119.042 67.841 1.00 38.34  ? 36  LYS C O   1 
ATOM   2474  C  CB  . LYS C  1 42  ? 83.439  119.251 68.829 1.00 35.88  ? 36  LYS C CB  1 
ATOM   2475  C  CG  . LYS C  1 42  ? 83.658  117.794 69.131 1.00 48.73  ? 36  LYS C CG  1 
ATOM   2476  C  CD  . LYS C  1 42  ? 82.441  117.222 69.843 1.00 59.09  ? 36  LYS C CD  1 
ATOM   2477  C  CE  . LYS C  1 42  ? 82.559  115.720 70.064 1.00 60.00  ? 36  LYS C CE  1 
ATOM   2478  N  NZ  . LYS C  1 42  ? 81.297  115.157 70.616 1.00 61.50  ? 36  LYS C NZ  1 
ATOM   2479  N  N   . GLY C  1 43  ? 86.162  120.349 69.599 1.00 29.32  ? 37  GLY C N   1 
ATOM   2480  C  CA  . GLY C  1 43  ? 87.478  120.260 70.224 1.00 27.03  ? 37  GLY C CA  1 
ATOM   2481  C  C   . GLY C  1 43  ? 88.570  121.130 69.614 1.00 28.45  ? 37  GLY C C   1 
ATOM   2482  O  O   . GLY C  1 43  ? 89.768  120.940 69.863 1.00 35.36  ? 37  GLY C O   1 
ATOM   2483  N  N   . LEU C  1 44  ? 88.168  122.102 68.814 1.00 26.45  ? 38  LEU C N   1 
ATOM   2484  C  CA  . LEU C  1 44  ? 89.136  122.980 68.180 1.00 28.96  ? 38  LEU C CA  1 
ATOM   2485  C  C   . LEU C  1 44  ? 89.357  124.272 68.955 1.00 29.96  ? 38  LEU C C   1 
ATOM   2486  O  O   . LEU C  1 44  ? 88.446  124.796 69.599 1.00 27.41  ? 38  LEU C O   1 
ATOM   2487  C  CB  . LEU C  1 44  ? 88.670  123.324 66.770 1.00 26.73  ? 38  LEU C CB  1 
ATOM   2488  C  CG  . LEU C  1 44  ? 88.748  122.254 65.683 1.00 28.69  ? 38  LEU C CG  1 
ATOM   2489  C  CD1 . LEU C  1 44  ? 87.797  122.630 64.545 1.00 18.56  ? 38  LEU C CD1 1 
ATOM   2490  C  CD2 . LEU C  1 44  ? 90.202  122.107 65.189 1.00 16.86  ? 38  LEU C CD2 1 
ATOM   2491  N  N   . THR C  1 45  ? 90.578  124.784 68.899 1.00 31.12  ? 39  THR C N   1 
ATOM   2492  C  CA  . THR C  1 45  ? 90.877  126.042 69.560 1.00 29.30  ? 39  THR C CA  1 
ATOM   2493  C  C   . THR C  1 45  ? 90.182  127.105 68.715 1.00 34.10  ? 39  THR C C   1 
ATOM   2494  O  O   . THR C  1 45  ? 90.129  126.990 67.486 1.00 31.74  ? 39  THR C O   1 
ATOM   2495  C  CB  . THR C  1 45  ? 92.386  126.304 69.587 1.00 35.39  ? 39  THR C CB  1 
ATOM   2496  O  OG1 . THR C  1 45  ? 92.904  126.300 68.243 1.00 28.33  ? 39  THR C OG1 1 
ATOM   2497  C  CG2 . THR C  1 45  ? 93.078  125.232 70.427 1.00 26.70  ? 39  THR C CG2 1 
ATOM   2498  N  N   . GLU C  1 46  ? 89.639  128.127 69.367 1.00 35.64  ? 40  GLU C N   1 
ATOM   2499  C  CA  . GLU C  1 46  ? 88.927  129.185 68.657 1.00 41.05  ? 40  GLU C CA  1 
ATOM   2500  C  C   . GLU C  1 46  ? 89.782  129.751 67.538 1.00 35.09  ? 40  GLU C C   1 
ATOM   2501  O  O   . GLU C  1 46  ? 90.968  129.987 67.720 1.00 36.64  ? 40  GLU C O   1 
ATOM   2502  C  CB  . GLU C  1 46  ? 88.548  130.307 69.622 1.00 39.96  ? 40  GLU C CB  1 
ATOM   2503  C  CG  . GLU C  1 46  ? 87.495  131.254 69.086 1.00 48.08  ? 40  GLU C CG  1 
ATOM   2504  C  CD  . GLU C  1 46  ? 87.150  132.361 70.073 1.00 50.89  ? 40  GLU C CD  1 
ATOM   2505  O  OE1 . GLU C  1 46  ? 87.232  132.123 71.290 1.00 57.18  ? 40  GLU C OE1 1 
ATOM   2506  O  OE2 . GLU C  1 46  ? 86.780  133.465 69.636 1.00 56.37  ? 40  GLU C OE2 1 
ATOM   2507  N  N   . GLY C  1 47  ? 89.187  129.960 66.374 1.00 36.36  ? 41  GLY C N   1 
ATOM   2508  C  CA  . GLY C  1 47  ? 89.963  130.512 65.282 1.00 34.14  ? 41  GLY C CA  1 
ATOM   2509  C  C   . GLY C  1 47  ? 89.990  129.639 64.049 1.00 37.15  ? 41  GLY C C   1 
ATOM   2510  O  O   . GLY C  1 47  ? 89.215  128.687 63.929 1.00 36.64  ? 41  GLY C O   1 
ATOM   2511  N  N   . LEU C  1 48  ? 90.907  129.970 63.144 1.00 33.07  ? 42  LEU C N   1 
ATOM   2512  C  CA  . LEU C  1 48  ? 91.067  129.272 61.884 1.00 34.64  ? 42  LEU C CA  1 
ATOM   2513  C  C   . LEU C  1 48  ? 91.855  127.973 61.934 1.00 38.61  ? 42  LEU C C   1 
ATOM   2514  O  O   . LEU C  1 48  ? 92.820  127.831 62.687 1.00 42.04  ? 42  LEU C O   1 
ATOM   2515  C  CB  . LEU C  1 48  ? 91.712  130.205 60.858 1.00 37.20  ? 42  LEU C CB  1 
ATOM   2516  C  CG  . LEU C  1 48  ? 90.975  131.522 60.586 1.00 39.51  ? 42  LEU C CG  1 
ATOM   2517  C  CD1 . LEU C  1 48  ? 91.467  132.120 59.254 1.00 27.81  ? 42  LEU C CD1 1 
ATOM   2518  C  CD2 . LEU C  1 48  ? 89.482  131.273 60.540 1.00 39.34  ? 42  LEU C CD2 1 
ATOM   2519  N  N   . HIS C  1 49  ? 91.443  127.027 61.098 1.00 38.65  ? 43  HIS C N   1 
ATOM   2520  C  CA  . HIS C  1 49  ? 92.101  125.733 61.032 1.00 35.53  ? 43  HIS C CA  1 
ATOM   2521  C  C   . HIS C  1 49  ? 92.154  125.244 59.594 1.00 33.55  ? 43  HIS C C   1 
ATOM   2522  O  O   . HIS C  1 49  ? 91.121  125.196 58.910 1.00 34.68  ? 43  HIS C O   1 
ATOM   2523  C  CB  . HIS C  1 49  ? 91.347  124.739 61.912 1.00 35.68  ? 43  HIS C CB  1 
ATOM   2524  C  CG  . HIS C  1 49  ? 91.468  125.025 63.376 1.00 28.54  ? 43  HIS C CG  1 
ATOM   2525  N  ND1 . HIS C  1 49  ? 92.575  124.665 64.113 1.00 25.66  ? 43  HIS C ND1 1 
ATOM   2526  C  CD2 . HIS C  1 49  ? 90.631  125.655 64.235 1.00 32.96  ? 43  HIS C CD2 1 
ATOM   2527  C  CE1 . HIS C  1 49  ? 92.413  125.058 65.366 1.00 29.05  ? 43  HIS C CE1 1 
ATOM   2528  N  NE2 . HIS C  1 49  ? 91.242  125.662 65.467 1.00 34.48  ? 43  HIS C NE2 1 
ATOM   2529  N  N   . GLY C  1 50  ? 93.363  124.921 59.135 1.00 27.05  ? 44  GLY C N   1 
ATOM   2530  C  CA  . GLY C  1 50  ? 93.550  124.427 57.779 1.00 28.66  ? 44  GLY C CA  1 
ATOM   2531  C  C   . GLY C  1 50  ? 92.700  123.186 57.554 1.00 32.99  ? 44  GLY C C   1 
ATOM   2532  O  O   . GLY C  1 50  ? 92.603  122.329 58.438 1.00 30.43  ? 44  GLY C O   1 
ATOM   2533  N  N   . PHE C  1 51  ? 92.119  123.065 56.363 1.00 32.15  ? 45  PHE C N   1 
ATOM   2534  C  CA  . PHE C  1 51  ? 91.202  121.965 56.050 1.00 33.59  ? 45  PHE C CA  1 
ATOM   2535  C  C   . PHE C  1 51  ? 91.499  121.423 54.659 1.00 29.71  ? 45  PHE C C   1 
ATOM   2536  O  O   . PHE C  1 51  ? 91.124  122.040 53.675 1.00 25.89  ? 45  PHE C O   1 
ATOM   2537  C  CB  . PHE C  1 51  ? 89.785  122.538 56.126 1.00 29.08  ? 45  PHE C CB  1 
ATOM   2538  C  CG  . PHE C  1 51  ? 88.693  121.524 56.137 1.00 37.51  ? 45  PHE C CG  1 
ATOM   2539  C  CD1 . PHE C  1 51  ? 88.585  120.606 57.171 1.00 40.29  ? 45  PHE C CD1 1 
ATOM   2540  C  CD2 . PHE C  1 51  ? 87.696  121.556 55.163 1.00 31.79  ? 45  PHE C CD2 1 
ATOM   2541  C  CE1 . PHE C  1 51  ? 87.490  119.739 57.243 1.00 36.43  ? 45  PHE C CE1 1 
ATOM   2542  C  CE2 . PHE C  1 51  ? 86.603  120.696 55.229 1.00 36.94  ? 45  PHE C CE2 1 
ATOM   2543  C  CZ  . PHE C  1 51  ? 86.499  119.788 56.274 1.00 36.58  ? 45  PHE C CZ  1 
ATOM   2544  N  N   . HIS C  1 52  ? 92.154  120.260 54.586 1.00 34.21  ? 46  HIS C N   1 
ATOM   2545  C  CA  . HIS C  1 52  ? 92.543  119.663 53.305 1.00 31.62  ? 46  HIS C CA  1 
ATOM   2546  C  C   . HIS C  1 52  ? 92.319  118.158 53.113 1.00 36.20  ? 46  HIS C C   1 
ATOM   2547  O  O   . HIS C  1 52  ? 92.172  117.396 54.075 1.00 28.39  ? 46  HIS C O   1 
ATOM   2548  C  CB  . HIS C  1 52  ? 94.032  119.903 53.057 1.00 33.84  ? 46  HIS C CB  1 
ATOM   2549  C  CG  . HIS C  1 52  ? 94.556  121.161 53.669 1.00 46.21  ? 46  HIS C CG  1 
ATOM   2550  N  ND1 . HIS C  1 52  ? 95.516  121.159 54.660 1.00 51.52  ? 46  HIS C ND1 1 
ATOM   2551  C  CD2 . HIS C  1 52  ? 94.253  122.460 53.437 1.00 45.20  ? 46  HIS C CD2 1 
ATOM   2552  C  CE1 . HIS C  1 52  ? 95.777  122.406 55.013 1.00 51.39  ? 46  HIS C CE1 1 
ATOM   2553  N  NE2 . HIS C  1 52  ? 95.026  123.213 54.286 1.00 49.90  ? 46  HIS C NE2 1 
ATOM   2554  N  N   . VAL C  1 53  ? 92.297  117.740 51.846 1.00 33.26  ? 47  VAL C N   1 
ATOM   2555  C  CA  . VAL C  1 53  ? 92.198  116.322 51.526 1.00 30.28  ? 47  VAL C CA  1 
ATOM   2556  C  C   . VAL C  1 53  ? 93.643  115.947 51.220 1.00 28.64  ? 47  VAL C C   1 
ATOM   2557  O  O   . VAL C  1 53  ? 94.284  116.573 50.382 1.00 30.64  ? 47  VAL C O   1 
ATOM   2558  C  CB  . VAL C  1 53  ? 91.350  116.033 50.274 1.00 30.06  ? 47  VAL C CB  1 
ATOM   2559  C  CG1 . VAL C  1 53  ? 91.420  114.541 49.948 1.00 17.34  ? 47  VAL C CG1 1 
ATOM   2560  C  CG2 . VAL C  1 53  ? 89.902  116.442 50.510 1.00 22.07  ? 47  VAL C CG2 1 
ATOM   2561  N  N   . HIS C  1 54  ? 94.175  114.964 51.931 1.00 27.44  ? 48  HIS C N   1 
ATOM   2562  C  CA  . HIS C  1 54  ? 95.545  114.546 51.702 1.00 28.18  ? 48  HIS C CA  1 
ATOM   2563  C  C   . HIS C  1 54  ? 95.523  113.370 50.749 1.00 30.95  ? 48  HIS C C   1 
ATOM   2564  O  O   . HIS C  1 54  ? 94.473  112.765 50.535 1.00 32.06  ? 48  HIS C O   1 
ATOM   2565  C  CB  . HIS C  1 54  ? 96.227  114.210 53.029 1.00 27.55  ? 48  HIS C CB  1 
ATOM   2566  C  CG  . HIS C  1 54  ? 96.628  115.425 53.823 1.00 38.94  ? 48  HIS C CG  1 
ATOM   2567  N  ND1 . HIS C  1 54  ? 97.942  115.714 54.135 1.00 31.56  ? 48  HIS C ND1 1 
ATOM   2568  C  CD2 . HIS C  1 54  ? 95.886  116.429 54.356 1.00 32.65  ? 48  HIS C CD2 1 
ATOM   2569  C  CE1 . HIS C  1 54  ? 97.989  116.839 54.829 1.00 40.48  ? 48  HIS C CE1 1 
ATOM   2570  N  NE2 . HIS C  1 54  ? 96.756  117.293 54.977 1.00 35.10  ? 48  HIS C NE2 1 
ATOM   2571  N  N   . GLU C  1 55  ? 96.676  113.039 50.183 1.00 33.81  ? 49  GLU C N   1 
ATOM   2572  C  CA  . GLU C  1 55  ? 96.754  111.980 49.183 1.00 36.82  ? 49  GLU C CA  1 
ATOM   2573  C  C   . GLU C  1 55  ? 96.312  110.554 49.509 1.00 40.09  ? 49  GLU C C   1 
ATOM   2574  O  O   . GLU C  1 55  ? 95.554  109.946 48.743 1.00 40.64  ? 49  GLU C O   1 
ATOM   2575  C  CB  . GLU C  1 55  ? 98.160  111.913 48.607 1.00 27.79  ? 49  GLU C CB  1 
ATOM   2576  C  CG  . GLU C  1 55  ? 98.217  111.031 47.381 1.00 44.03  ? 49  GLU C CG  1 
ATOM   2577  C  CD  . GLU C  1 55  ? 99.582  110.981 46.747 1.00 44.98  ? 49  GLU C CD  1 
ATOM   2578  O  OE1 . GLU C  1 55  ? 99.736  110.269 45.733 1.00 52.18  ? 49  GLU C OE1 1 
ATOM   2579  O  OE2 . GLU C  1 55  ? 100.504 111.646 47.261 1.00 53.35  ? 49  GLU C OE2 1 
ATOM   2580  N  N   . PHE C  1 56  ? 96.773  110.012 50.627 1.00 37.54  ? 50  PHE C N   1 
ATOM   2581  C  CA  . PHE C  1 56  ? 96.443  108.634 50.958 1.00 32.69  ? 50  PHE C CA  1 
ATOM   2582  C  C   . PHE C  1 56  ? 95.450  108.391 52.085 1.00 35.77  ? 50  PHE C C   1 
ATOM   2583  O  O   . PHE C  1 56  ? 95.430  109.103 53.091 1.00 35.43  ? 50  PHE C O   1 
ATOM   2584  C  CB  . PHE C  1 56  ? 97.728  107.885 51.270 1.00 29.25  ? 50  PHE C CB  1 
ATOM   2585  C  CG  . PHE C  1 56  ? 98.793  108.072 50.238 1.00 33.88  ? 50  PHE C CG  1 
ATOM   2586  C  CD1 . PHE C  1 56  ? 98.653  107.528 48.975 1.00 35.11  ? 50  PHE C CD1 1 
ATOM   2587  C  CD2 . PHE C  1 56  ? 99.940  108.798 50.532 1.00 39.60  ? 50  PHE C CD2 1 
ATOM   2588  C  CE1 . PHE C  1 56  ? 99.642  107.699 48.012 1.00 41.68  ? 50  PHE C CE1 1 
ATOM   2589  C  CE2 . PHE C  1 56  ? 100.932 108.975 49.576 1.00 37.78  ? 50  PHE C CE2 1 
ATOM   2590  C  CZ  . PHE C  1 56  ? 100.780 108.421 48.311 1.00 37.50  ? 50  PHE C CZ  1 
ATOM   2591  N  N   . GLY C  1 57  ? 94.626  107.366 51.899 1.00 28.84  ? 51  GLY C N   1 
ATOM   2592  C  CA  . GLY C  1 57  ? 93.673  106.993 52.922 1.00 28.85  ? 51  GLY C CA  1 
ATOM   2593  C  C   . GLY C  1 57  ? 94.376  105.975 53.805 1.00 29.87  ? 51  GLY C C   1 
ATOM   2594  O  O   . GLY C  1 57  ? 93.842  104.896 54.077 1.00 30.47  ? 51  GLY C O   1 
ATOM   2595  N  N   . ASP C  1 58  ? 95.586  106.325 54.244 1.00 23.92  ? 52  ASP C N   1 
ATOM   2596  C  CA  . ASP C  1 58  ? 96.403  105.451 55.079 1.00 26.23  ? 52  ASP C CA  1 
ATOM   2597  C  C   . ASP C  1 58  ? 96.571  106.024 56.495 1.00 30.66  ? 52  ASP C C   1 
ATOM   2598  O  O   . ASP C  1 58  ? 97.362  106.944 56.705 1.00 33.48  ? 52  ASP C O   1 
ATOM   2599  C  CB  . ASP C  1 58  ? 97.754  105.263 54.385 1.00 18.55  ? 52  ASP C CB  1 
ATOM   2600  C  CG  . ASP C  1 58  ? 98.725  104.407 55.185 1.00 30.74  ? 52  ASP C CG  1 
ATOM   2601  O  OD1 . ASP C  1 58  ? 99.702  103.902 54.585 1.00 30.58  ? 52  ASP C OD1 1 
ATOM   2602  O  OD2 . ASP C  1 58  ? 98.533  104.241 56.405 1.00 25.58  ? 52  ASP C OD2 1 
ATOM   2603  N  N   . ASN C  1 59  ? 95.821  105.488 57.461 1.00 32.29  ? 53  ASN C N   1 
ATOM   2604  C  CA  . ASN C  1 59  ? 95.885  105.959 58.850 1.00 32.64  ? 53  ASN C CA  1 
ATOM   2605  C  C   . ASN C  1 59  ? 96.748  105.002 59.660 1.00 31.08  ? 53  ASN C C   1 
ATOM   2606  O  O   . ASN C  1 59  ? 96.717  104.963 60.894 1.00 26.67  ? 53  ASN C O   1 
ATOM   2607  C  CB  . ASN C  1 59  ? 94.475  106.040 59.441 1.00 45.87  ? 53  ASN C CB  1 
ATOM   2608  C  CG  . ASN C  1 59  ? 94.467  106.468 60.918 1.00 59.83  ? 53  ASN C CG  1 
ATOM   2609  O  OD1 . ASN C  1 59  ? 94.345  105.637 61.834 1.00 58.65  ? 53  ASN C OD1 1 
ATOM   2610  N  ND2 . ASN C  1 59  ? 94.603  107.770 61.150 1.00 62.47  ? 53  ASN C ND2 1 
ATOM   2611  N  N   . THR C  1 60  ? 97.527  104.225 58.935 1.00 25.09  ? 54  THR C N   1 
ATOM   2612  C  CA  . THR C  1 60  ? 98.406  103.244 59.526 1.00 26.80  ? 54  THR C CA  1 
ATOM   2613  C  C   . THR C  1 60  ? 99.288  103.820 60.630 1.00 28.23  ? 54  THR C C   1 
ATOM   2614  O  O   . THR C  1 60  ? 99.550  103.162 61.629 1.00 28.51  ? 54  THR C O   1 
ATOM   2615  C  CB  . THR C  1 60  ? 99.221  102.599 58.407 1.00 30.62  ? 54  THR C CB  1 
ATOM   2616  O  OG1 . THR C  1 60  ? 98.886  101.207 58.351 1.00 41.82  ? 54  THR C OG1 1 
ATOM   2617  C  CG2 . THR C  1 60  ? 100.709 102.829 58.578 1.00 21.37  ? 54  THR C CG2 1 
ATOM   2618  N  N   . ALA C  1 61  ? 99.742  105.055 60.458 1.00 31.75  ? 55  ALA C N   1 
ATOM   2619  C  CA  . ALA C  1 61  ? 100.560 105.715 61.473 1.00 33.12  ? 55  ALA C CA  1 
ATOM   2620  C  C   . ALA C  1 61  ? 99.878  107.032 61.853 1.00 31.46  ? 55  ALA C C   1 
ATOM   2621  O  O   . ALA C  1 61  ? 100.510 108.090 61.880 1.00 35.21  ? 55  ALA C O   1 
ATOM   2622  C  CB  . ALA C  1 61  ? 101.947 105.986 60.938 1.00 28.29  ? 55  ALA C CB  1 
ATOM   2623  N  N   . GLY C  1 62  ? 98.586  106.966 62.153 1.00 32.75  ? 56  GLY C N   1 
ATOM   2624  C  CA  . GLY C  1 62  ? 97.870  108.179 62.496 1.00 34.58  ? 56  GLY C CA  1 
ATOM   2625  C  C   . GLY C  1 62  ? 97.792  109.036 61.247 1.00 38.93  ? 56  GLY C C   1 
ATOM   2626  O  O   . GLY C  1 62  ? 98.035  108.534 60.143 1.00 44.18  ? 56  GLY C O   1 
ATOM   2627  N  N   . CYS C  1 63  ? 97.488  110.321 61.414 1.00 34.49  ? 57  CYS C N   1 
ATOM   2628  C  CA  . CYS C  1 63  ? 97.340  111.240 60.286 1.00 33.40  ? 57  CYS C CA  1 
ATOM   2629  C  C   . CYS C  1 63  ? 98.649  111.523 59.566 1.00 34.06  ? 57  CYS C C   1 
ATOM   2630  O  O   . CYS C  1 63  ? 98.662  112.116 58.493 1.00 31.99  ? 57  CYS C O   1 
ATOM   2631  C  CB  . CYS C  1 63  ? 96.702  112.551 60.763 1.00 20.80  ? 57  CYS C CB  1 
ATOM   2632  S  SG  . CYS C  1 63  ? 95.134  112.299 61.655 1.00 35.31  ? 57  CYS C SG  1 
ATOM   2633  N  N   . THR C  1 64  ? 99.746  111.072 60.153 1.00 35.85  ? 58  THR C N   1 
ATOM   2634  C  CA  . THR C  1 64  ? 101.064 111.273 59.575 1.00 36.59  ? 58  THR C CA  1 
ATOM   2635  C  C   . THR C  1 64  ? 101.241 110.515 58.266 1.00 37.10  ? 58  THR C C   1 
ATOM   2636  O  O   . THR C  1 64  ? 101.877 110.998 57.327 1.00 33.06  ? 58  THR C O   1 
ATOM   2637  C  CB  . THR C  1 64  ? 102.164 110.780 60.534 1.00 38.03  ? 58  THR C CB  1 
ATOM   2638  O  OG1 . THR C  1 64  ? 102.064 111.479 61.777 1.00 40.10  ? 58  THR C OG1 1 
ATOM   2639  C  CG2 . THR C  1 64  ? 103.542 111.000 59.923 1.00 34.37  ? 58  THR C CG2 1 
ATOM   2640  N  N   . SER C  1 65  ? 100.681 109.319 58.199 1.00 30.98  ? 59  SER C N   1 
ATOM   2641  C  CA  . SER C  1 65  ? 100.860 108.518 57.002 1.00 33.49  ? 59  SER C CA  1 
ATOM   2642  C  C   . SER C  1 65  ? 99.969  108.891 55.813 1.00 28.70  ? 59  SER C C   1 
ATOM   2643  O  O   . SER C  1 65  ? 100.076 108.290 54.740 1.00 33.17  ? 59  SER C O   1 
ATOM   2644  C  CB  . SER C  1 65  ? 100.720 107.031 57.365 1.00 25.55  ? 59  SER C CB  1 
ATOM   2645  O  OG  . SER C  1 65  ? 99.604  106.818 58.219 1.00 36.12  ? 59  SER C OG  1 
ATOM   2646  N  N   . ALA C  1 66  ? 99.114  109.897 55.979 1.00 26.80  ? 60  ALA C N   1 
ATOM   2647  C  CA  . ALA C  1 66  ? 98.229  110.313 54.887 1.00 27.44  ? 60  ALA C CA  1 
ATOM   2648  C  C   . ALA C  1 66  ? 98.949  111.049 53.758 1.00 32.38  ? 60  ALA C C   1 
ATOM   2649  O  O   . ALA C  1 66  ? 98.315  111.452 52.782 1.00 33.15  ? 60  ALA C O   1 
ATOM   2650  C  CB  . ALA C  1 66  ? 97.120  111.182 55.426 1.00 22.36  ? 60  ALA C CB  1 
ATOM   2651  N  N   . GLY C  1 67  ? 100.263 111.237 53.895 1.00 37.73  ? 61  GLY C N   1 
ATOM   2652  C  CA  . GLY C  1 67  ? 101.036 111.923 52.867 1.00 34.22  ? 61  GLY C CA  1 
ATOM   2653  C  C   . GLY C  1 67  ? 100.752 113.411 52.734 1.00 35.15  ? 61  GLY C C   1 
ATOM   2654  O  O   . GLY C  1 67  ? 100.213 114.041 53.651 1.00 37.30  ? 61  GLY C O   1 
ATOM   2655  N  N   . PRO C  1 68  ? 101.103 114.010 51.590 1.00 35.61  ? 62  PRO C N   1 
ATOM   2656  C  CA  . PRO C  1 68  ? 100.873 115.442 51.360 1.00 33.29  ? 62  PRO C CA  1 
ATOM   2657  C  C   . PRO C  1 68  ? 99.446  115.728 50.926 1.00 31.28  ? 62  PRO C C   1 
ATOM   2658  O  O   . PRO C  1 68  ? 98.634  114.816 50.805 1.00 34.39  ? 62  PRO C O   1 
ATOM   2659  C  CB  . PRO C  1 68  ? 101.860 115.767 50.257 1.00 29.65  ? 62  PRO C CB  1 
ATOM   2660  C  CG  . PRO C  1 68  ? 101.798 114.538 49.427 1.00 36.70  ? 62  PRO C CG  1 
ATOM   2661  C  CD  . PRO C  1 68  ? 101.854 113.421 50.468 1.00 36.13  ? 62  PRO C CD  1 
ATOM   2662  N  N   . HIS C  1 69  ? 99.150  117.004 50.707 1.00 30.46  ? 63  HIS C N   1 
ATOM   2663  C  CA  . HIS C  1 69  ? 97.832  117.430 50.250 1.00 35.64  ? 63  HIS C CA  1 
ATOM   2664  C  C   . HIS C  1 69  ? 97.591  116.722 48.901 1.00 37.69  ? 63  HIS C C   1 
ATOM   2665  O  O   . HIS C  1 69  ? 98.532  116.542 48.121 1.00 34.60  ? 63  HIS C O   1 
ATOM   2666  C  CB  . HIS C  1 69  ? 97.808  118.962 50.047 1.00 37.23  ? 63  HIS C CB  1 
ATOM   2667  C  CG  . HIS C  1 69  ? 97.855  119.771 51.317 1.00 39.84  ? 63  HIS C CG  1 
ATOM   2668  N  ND1 . HIS C  1 69  ? 97.848  121.152 51.316 1.00 49.39  ? 63  HIS C ND1 1 
ATOM   2669  C  CD2 . HIS C  1 69  ? 97.873  119.403 52.621 1.00 49.06  ? 63  HIS C CD2 1 
ATOM   2670  C  CE1 . HIS C  1 69  ? 97.856  121.598 52.561 1.00 36.28  ? 63  HIS C CE1 1 
ATOM   2671  N  NE2 . HIS C  1 69  ? 97.870  120.556 53.372 1.00 45.96  ? 63  HIS C NE2 1 
ATOM   2672  N  N   . PHE C  1 70  ? 96.355  116.297 48.633 1.00 35.10  ? 64  PHE C N   1 
ATOM   2673  C  CA  . PHE C  1 70  ? 96.046  115.630 47.357 1.00 38.76  ? 64  PHE C CA  1 
ATOM   2674  C  C   . PHE C  1 70  ? 96.388  116.587 46.190 1.00 40.53  ? 64  PHE C C   1 
ATOM   2675  O  O   . PHE C  1 70  ? 95.764  117.645 46.035 1.00 31.30  ? 64  PHE C O   1 
ATOM   2676  C  CB  . PHE C  1 70  ? 94.561  115.249 47.294 1.00 34.85  ? 64  PHE C CB  1 
ATOM   2677  C  CG  . PHE C  1 70  ? 94.177  114.515 46.035 1.00 30.80  ? 64  PHE C CG  1 
ATOM   2678  C  CD1 . PHE C  1 70  ? 92.899  114.641 45.505 1.00 25.17  ? 64  PHE C CD1 1 
ATOM   2679  C  CD2 . PHE C  1 70  ? 95.094  113.684 45.390 1.00 31.86  ? 64  PHE C CD2 1 
ATOM   2680  C  CE1 . PHE C  1 70  ? 92.538  113.951 44.352 1.00 29.13  ? 64  PHE C CE1 1 
ATOM   2681  C  CE2 . PHE C  1 70  ? 94.741  112.989 44.236 1.00 31.78  ? 64  PHE C CE2 1 
ATOM   2682  C  CZ  . PHE C  1 70  ? 93.460  113.125 43.718 1.00 27.00  ? 64  PHE C CZ  1 
ATOM   2683  N  N   . ASN C  1 71  ? 97.348  116.203 45.354 1.00 33.16  ? 65  ASN C N   1 
ATOM   2684  C  CA  . ASN C  1 71  ? 97.774  117.098 44.293 1.00 36.58  ? 65  ASN C CA  1 
ATOM   2685  C  C   . ASN C  1 71  ? 98.038  116.391 42.959 1.00 37.89  ? 65  ASN C C   1 
ATOM   2686  O  O   . ASN C  1 71  ? 99.159  116.371 42.456 1.00 32.57  ? 65  ASN C O   1 
ATOM   2687  C  CB  . ASN C  1 71  ? 99.026  117.822 44.791 1.00 35.47  ? 65  ASN C CB  1 
ATOM   2688  C  CG  . ASN C  1 71  ? 99.424  119.003 43.923 1.00 39.76  ? 65  ASN C CG  1 
ATOM   2689  O  OD1 . ASN C  1 71  ? 98.649  119.473 43.088 1.00 38.86  ? 65  ASN C OD1 1 
ATOM   2690  N  ND2 . ASN C  1 71  ? 100.645 119.503 44.137 1.00 28.18  ? 65  ASN C ND2 1 
ATOM   2691  N  N   . PRO C  1 72  ? 96.990  115.818 42.357 1.00 43.58  ? 66  PRO C N   1 
ATOM   2692  C  CA  . PRO C  1 72  ? 97.122  115.109 41.080 1.00 45.74  ? 66  PRO C CA  1 
ATOM   2693  C  C   . PRO C  1 72  ? 97.630  115.957 39.895 1.00 51.33  ? 66  PRO C C   1 
ATOM   2694  O  O   . PRO C  1 72  ? 98.254  115.429 38.974 1.00 50.48  ? 66  PRO C O   1 
ATOM   2695  C  CB  . PRO C  1 72  ? 95.713  114.568 40.854 1.00 47.20  ? 66  PRO C CB  1 
ATOM   2696  C  CG  . PRO C  1 72  ? 94.850  115.620 41.494 1.00 40.82  ? 66  PRO C CG  1 
ATOM   2697  C  CD  . PRO C  1 72  ? 95.577  115.914 42.770 1.00 38.50  ? 66  PRO C CD  1 
ATOM   2698  N  N   . LEU C  1 73  ? 97.379  117.264 39.924 1.00 49.45  ? 67  LEU C N   1 
ATOM   2699  C  CA  . LEU C  1 73  ? 97.814  118.130 38.836 1.00 54.05  ? 67  LEU C CA  1 
ATOM   2700  C  C   . LEU C  1 73  ? 99.177  118.783 39.068 1.00 57.31  ? 67  LEU C C   1 
ATOM   2701  O  O   . LEU C  1 73  ? 99.584  119.648 38.301 1.00 62.97  ? 67  LEU C O   1 
ATOM   2702  C  CB  . LEU C  1 73  ? 96.760  119.209 38.565 1.00 48.70  ? 67  LEU C CB  1 
ATOM   2703  C  CG  . LEU C  1 73  ? 95.363  118.679 38.228 1.00 55.19  ? 67  LEU C CG  1 
ATOM   2704  C  CD1 . LEU C  1 73  ? 94.430  119.841 37.905 1.00 54.01  ? 67  LEU C CD1 1 
ATOM   2705  C  CD2 . LEU C  1 73  ? 95.443  117.708 37.054 1.00 54.06  ? 67  LEU C CD2 1 
ATOM   2706  N  N   . SER C  1 74  ? 99.878  118.364 40.119 1.00 61.42  ? 68  SER C N   1 
ATOM   2707  C  CA  . SER C  1 74  ? 101.206 118.894 40.451 1.00 59.90  ? 68  SER C CA  1 
ATOM   2708  C  C   . SER C  1 74  ? 101.282 120.421 40.463 1.00 60.48  ? 68  SER C C   1 
ATOM   2709  O  O   . SER C  1 74  ? 102.031 121.025 39.694 1.00 62.08  ? 68  SER C O   1 
ATOM   2710  C  CB  . SER C  1 74  ? 102.247 118.346 39.470 1.00 56.54  ? 68  SER C CB  1 
ATOM   2711  O  OG  . SER C  1 74  ? 102.162 116.937 39.378 1.00 59.90  ? 68  SER C OG  1 
ATOM   2712  N  N   . ARG C  1 75  ? 100.511 121.045 41.345 1.00 59.98  ? 69  ARG C N   1 
ATOM   2713  C  CA  . ARG C  1 75  ? 100.506 122.497 41.439 1.00 58.25  ? 69  ARG C CA  1 
ATOM   2714  C  C   . ARG C  1 75  ? 100.967 123.003 42.795 1.00 52.94  ? 69  ARG C C   1 
ATOM   2715  O  O   . ARG C  1 75  ? 101.402 122.231 43.642 1.00 52.43  ? 69  ARG C O   1 
ATOM   2716  C  CB  . ARG C  1 75  ? 99.113  123.029 41.141 1.00 61.16  ? 69  ARG C CB  1 
ATOM   2717  C  CG  . ARG C  1 75  ? 98.686  122.801 39.711 1.00 67.28  ? 69  ARG C CG  1 
ATOM   2718  C  CD  . ARG C  1 75  ? 97.328  123.397 39.497 1.00 75.98  ? 69  ARG C CD  1 
ATOM   2719  N  NE  . ARG C  1 75  ? 96.858  123.226 38.133 1.00 80.26  ? 69  ARG C NE  1 
ATOM   2720  C  CZ  . ARG C  1 75  ? 95.646  123.578 37.729 1.00 82.01  ? 69  ARG C CZ  1 
ATOM   2721  N  NH1 . ARG C  1 75  ? 94.788  124.118 38.588 1.00 77.67  ? 69  ARG C NH1 1 
ATOM   2722  N  NH2 . ARG C  1 75  ? 95.294  123.390 36.467 1.00 87.41  ? 69  ARG C NH2 1 
ATOM   2723  N  N   . LYS C  1 76  ? 100.887 124.312 42.982 1.00 52.17  ? 70  LYS C N   1 
ATOM   2724  C  CA  . LYS C  1 76  ? 101.285 124.929 44.237 1.00 51.37  ? 70  LYS C CA  1 
ATOM   2725  C  C   . LYS C  1 76  ? 100.060 125.124 45.131 1.00 49.23  ? 70  LYS C C   1 
ATOM   2726  O  O   . LYS C  1 76  ? 98.942  125.355 44.644 1.00 44.45  ? 70  LYS C O   1 
ATOM   2727  C  CB  . LYS C  1 76  ? 101.956 126.285 43.980 1.00 55.42  ? 70  LYS C CB  1 
ATOM   2728  C  CG  . LYS C  1 76  ? 103.340 126.207 43.347 1.00 66.62  ? 70  LYS C CG  1 
ATOM   2729  C  CD  . LYS C  1 76  ? 104.338 125.509 44.264 1.00 72.50  ? 70  LYS C CD  1 
ATOM   2730  C  CE  . LYS C  1 76  ? 105.756 125.550 43.691 1.00 76.27  ? 70  LYS C CE  1 
ATOM   2731  N  NZ  . LYS C  1 76  ? 106.757 124.910 44.607 1.00 75.17  ? 70  LYS C NZ  1 
ATOM   2732  N  N   . HIS C  1 77  ? 100.281 125.024 46.440 1.00 41.96  ? 71  HIS C N   1 
ATOM   2733  C  CA  . HIS C  1 77  ? 99.219  125.200 47.414 1.00 37.96  ? 71  HIS C CA  1 
ATOM   2734  C  C   . HIS C  1 77  ? 98.568  126.581 47.264 1.00 39.68  ? 71  HIS C C   1 
ATOM   2735  O  O   . HIS C  1 77  ? 99.244  127.585 47.028 1.00 41.12  ? 71  HIS C O   1 
ATOM   2736  C  CB  . HIS C  1 77  ? 99.778  125.053 48.845 1.00 32.78  ? 71  HIS C CB  1 
ATOM   2737  C  CG  . HIS C  1 77  ? 98.757  125.282 49.918 1.00 29.68  ? 71  HIS C CG  1 
ATOM   2738  N  ND1 . HIS C  1 77  ? 97.829  124.327 50.286 1.00 33.54  ? 71  HIS C ND1 1 
ATOM   2739  C  CD2 . HIS C  1 77  ? 98.474  126.381 50.657 1.00 30.44  ? 71  HIS C CD2 1 
ATOM   2740  C  CE1 . HIS C  1 77  ? 97.021  124.829 51.203 1.00 40.05  ? 71  HIS C CE1 1 
ATOM   2741  N  NE2 . HIS C  1 77  ? 97.392  126.074 51.446 1.00 37.99  ? 71  HIS C NE2 1 
ATOM   2742  N  N   . GLY C  1 78  ? 97.251  126.625 47.415 1.00 42.08  ? 72  GLY C N   1 
ATOM   2743  C  CA  . GLY C  1 78  ? 96.535  127.886 47.327 1.00 36.42  ? 72  GLY C CA  1 
ATOM   2744  C  C   . GLY C  1 78  ? 95.293  127.772 48.181 1.00 36.41  ? 72  GLY C C   1 
ATOM   2745  O  O   . GLY C  1 78  ? 95.185  126.859 49.006 1.00 37.50  ? 72  GLY C O   1 
ATOM   2746  N  N   . GLY C  1 79  ? 94.361  128.696 48.004 1.00 35.71  ? 73  GLY C N   1 
ATOM   2747  C  CA  . GLY C  1 79  ? 93.117  128.640 48.748 1.00 34.70  ? 73  GLY C CA  1 
ATOM   2748  C  C   . GLY C  1 79  ? 92.094  127.945 47.861 1.00 41.67  ? 73  GLY C C   1 
ATOM   2749  O  O   . GLY C  1 79  ? 92.367  127.709 46.679 1.00 38.50  ? 73  GLY C O   1 
ATOM   2750  N  N   . PRO C  1 80  ? 90.918  127.581 48.387 1.00 42.06  ? 74  PRO C N   1 
ATOM   2751  C  CA  . PRO C  1 80  ? 89.964  126.921 47.492 1.00 46.81  ? 74  PRO C CA  1 
ATOM   2752  C  C   . PRO C  1 80  ? 89.573  127.828 46.316 1.00 48.83  ? 74  PRO C C   1 
ATOM   2753  O  O   . PRO C  1 80  ? 89.418  127.357 45.189 1.00 45.53  ? 74  PRO C O   1 
ATOM   2754  C  CB  . PRO C  1 80  ? 88.782  126.615 48.413 1.00 44.93  ? 74  PRO C CB  1 
ATOM   2755  C  CG  . PRO C  1 80  ? 88.865  127.708 49.450 1.00 40.44  ? 74  PRO C CG  1 
ATOM   2756  C  CD  . PRO C  1 80  ? 90.346  127.770 49.730 1.00 39.86  ? 74  PRO C CD  1 
ATOM   2757  N  N   . LYS C  1 81  ? 89.430  129.127 46.588 1.00 48.67  ? 75  LYS C N   1 
ATOM   2758  C  CA  . LYS C  1 81  ? 89.056  130.107 45.567 1.00 50.42  ? 75  LYS C CA  1 
ATOM   2759  C  C   . LYS C  1 81  ? 90.070  130.236 44.427 1.00 48.53  ? 75  LYS C C   1 
ATOM   2760  O  O   . LYS C  1 81  ? 89.693  130.535 43.302 1.00 45.94  ? 75  LYS C O   1 
ATOM   2761  C  CB  . LYS C  1 81  ? 88.879  131.501 46.187 1.00 54.66  ? 75  LYS C CB  1 
ATOM   2762  C  CG  . LYS C  1 81  ? 87.688  131.685 47.112 1.00 57.11  ? 75  LYS C CG  1 
ATOM   2763  C  CD  . LYS C  1 81  ? 87.606  133.137 47.592 1.00 58.13  ? 75  LYS C CD  1 
ATOM   2764  C  CE  . LYS C  1 81  ? 86.407  133.376 48.512 1.00 62.81  ? 75  LYS C CE  1 
ATOM   2765  N  NZ  . LYS C  1 81  ? 86.376  134.751 49.099 1.00 56.07  ? 75  LYS C NZ  1 
ATOM   2766  N  N   . ASP C  1 82  ? 91.348  130.016 44.724 1.00 47.94  ? 76  ASP C N   1 
ATOM   2767  C  CA  . ASP C  1 82  ? 92.422  130.154 43.739 1.00 48.51  ? 76  ASP C CA  1 
ATOM   2768  C  C   . ASP C  1 82  ? 92.420  129.183 42.576 1.00 54.83  ? 76  ASP C C   1 
ATOM   2769  O  O   . ASP C  1 82  ? 91.859  128.092 42.657 1.00 58.83  ? 76  ASP C O   1 
ATOM   2770  C  CB  . ASP C  1 82  ? 93.776  130.063 44.435 1.00 50.05  ? 76  ASP C CB  1 
ATOM   2771  C  CG  . ASP C  1 82  ? 93.989  131.182 45.448 1.00 58.79  ? 76  ASP C CG  1 
ATOM   2772  O  OD1 . ASP C  1 82  ? 94.915  131.066 46.280 1.00 57.75  ? 76  ASP C OD1 1 
ATOM   2773  O  OD2 . ASP C  1 82  ? 93.237  132.181 45.409 1.00 58.91  ? 76  ASP C OD2 1 
ATOM   2774  N  N   . GLU C  1 83  ? 93.059  129.608 41.489 1.00 56.99  ? 77  GLU C N   1 
ATOM   2775  C  CA  . GLU C  1 83  ? 93.199  128.806 40.283 1.00 57.97  ? 77  GLU C CA  1 
ATOM   2776  C  C   . GLU C  1 83  ? 94.435  127.954 40.531 1.00 54.70  ? 77  GLU C C   1 
ATOM   2777  O  O   . GLU C  1 83  ? 94.480  126.765 40.214 1.00 53.72  ? 77  GLU C O   1 
ATOM   2778  C  CB  . GLU C  1 83  ? 93.400  129.721 39.069 1.00 70.38  ? 77  GLU C CB  1 
ATOM   2779  C  CG  . GLU C  1 83  ? 94.066  129.083 37.835 1.00 88.42  ? 77  GLU C CG  1 
ATOM   2780  C  CD  . GLU C  1 83  ? 93.263  127.943 37.219 1.00 99.18  ? 77  GLU C CD  1 
ATOM   2781  O  OE1 . GLU C  1 83  ? 92.038  128.106 37.019 1.00 104.95 ? 77  GLU C OE1 1 
ATOM   2782  O  OE2 . GLU C  1 83  ? 93.865  126.886 36.920 1.00 103.14 ? 77  GLU C OE2 1 
ATOM   2783  N  N   . GLU C  1 84  ? 95.445  128.577 41.111 1.00 50.80  ? 78  GLU C N   1 
ATOM   2784  C  CA  . GLU C  1 84  ? 96.657  127.861 41.435 1.00 52.60  ? 78  GLU C CA  1 
ATOM   2785  C  C   . GLU C  1 84  ? 96.449  127.220 42.806 1.00 52.04  ? 78  GLU C C   1 
ATOM   2786  O  O   . GLU C  1 84  ? 96.522  127.894 43.840 1.00 40.06  ? 78  GLU C O   1 
ATOM   2787  C  CB  . GLU C  1 84  ? 97.841  128.821 41.469 1.00 56.83  ? 78  GLU C CB  1 
ATOM   2788  C  CG  . GLU C  1 84  ? 98.792  128.590 40.332 1.00 62.78  ? 78  GLU C CG  1 
ATOM   2789  C  CD  . GLU C  1 84  ? 99.278  127.162 40.301 1.00 58.57  ? 78  GLU C CD  1 
ATOM   2790  O  OE1 . GLU C  1 84  ? 100.110 126.800 41.160 1.00 52.67  ? 78  GLU C OE1 1 
ATOM   2791  O  OE2 . GLU C  1 84  ? 98.814  126.402 39.426 1.00 60.80  ? 78  GLU C OE2 1 
ATOM   2792  N  N   . ARG C  1 85  ? 96.175  125.918 42.807 1.00 52.88  ? 79  ARG C N   1 
ATOM   2793  C  CA  . ARG C  1 85  ? 95.945  125.202 44.053 1.00 55.33  ? 79  ARG C CA  1 
ATOM   2794  C  C   . ARG C  1 85  ? 95.944  123.678 43.928 1.00 52.48  ? 79  ARG C C   1 
ATOM   2795  O  O   . ARG C  1 85  ? 95.821  123.130 42.837 1.00 55.71  ? 79  ARG C O   1 
ATOM   2796  C  CB  . ARG C  1 85  ? 94.622  125.677 44.680 1.00 54.02  ? 79  ARG C CB  1 
ATOM   2797  C  CG  . ARG C  1 85  ? 93.392  125.510 43.801 1.00 52.74  ? 79  ARG C CG  1 
ATOM   2798  C  CD  . ARG C  1 85  ? 92.682  124.216 44.107 1.00 52.02  ? 79  ARG C CD  1 
ATOM   2799  N  NE  . ARG C  1 85  ? 91.342  124.423 44.656 1.00 54.46  ? 79  ARG C NE  1 
ATOM   2800  C  CZ  . ARG C  1 85  ? 90.636  123.470 45.262 1.00 51.81  ? 79  ARG C CZ  1 
ATOM   2801  N  NH1 . ARG C  1 85  ? 91.147  122.258 45.402 1.00 56.15  ? 79  ARG C NH1 1 
ATOM   2802  N  NH2 . ARG C  1 85  ? 89.414  123.713 45.709 1.00 41.46  ? 79  ARG C NH2 1 
ATOM   2803  N  N   . HIS C  1 86  ? 96.108  123.012 45.070 1.00 48.38  ? 80  HIS C N   1 
ATOM   2804  C  CA  . HIS C  1 86  ? 96.090  121.555 45.171 1.00 39.55  ? 80  HIS C CA  1 
ATOM   2805  C  C   . HIS C  1 86  ? 94.615  121.137 45.058 1.00 35.98  ? 80  HIS C C   1 
ATOM   2806  O  O   . HIS C  1 86  ? 93.734  121.861 45.526 1.00 34.44  ? 80  HIS C O   1 
ATOM   2807  C  CB  . HIS C  1 86  ? 96.594  121.132 46.551 1.00 34.86  ? 80  HIS C CB  1 
ATOM   2808  C  CG  . HIS C  1 86  ? 98.030  121.448 46.808 1.00 35.64  ? 80  HIS C CG  1 
ATOM   2809  N  ND1 . HIS C  1 86  ? 98.545  121.567 48.085 1.00 22.87  ? 80  HIS C ND1 1 
ATOM   2810  C  CD2 . HIS C  1 86  ? 99.079  121.571 45.964 1.00 29.12  ? 80  HIS C CD2 1 
ATOM   2811  C  CE1 . HIS C  1 86  ? 99.850  121.740 48.013 1.00 28.58  ? 80  HIS C CE1 1 
ATOM   2812  N  NE2 . HIS C  1 86  ? 100.198 121.746 46.738 1.00 35.80  ? 80  HIS C NE2 1 
ATOM   2813  N  N   . VAL C  1 87  ? 94.318  119.987 44.465 1.00 32.13  ? 81  VAL C N   1 
ATOM   2814  C  CA  . VAL C  1 87  ? 92.911  119.601 44.394 1.00 34.21  ? 81  VAL C CA  1 
ATOM   2815  C  C   . VAL C  1 87  ? 92.338  119.475 45.802 1.00 36.53  ? 81  VAL C C   1 
ATOM   2816  O  O   . VAL C  1 87  ? 91.150  119.707 46.014 1.00 33.10  ? 81  VAL C O   1 
ATOM   2817  C  CB  . VAL C  1 87  ? 92.681  118.253 43.651 1.00 35.53  ? 81  VAL C CB  1 
ATOM   2818  C  CG1 . VAL C  1 87  ? 91.213  117.817 43.817 1.00 33.67  ? 81  VAL C CG1 1 
ATOM   2819  C  CG2 . VAL C  1 87  ? 92.989  118.415 42.160 1.00 29.33  ? 81  VAL C CG2 1 
ATOM   2820  N  N   . GLY C  1 88  ? 93.183  119.120 46.767 1.00 33.23  ? 82  GLY C N   1 
ATOM   2821  C  CA  . GLY C  1 88  ? 92.705  118.966 48.132 1.00 37.29  ? 82  GLY C CA  1 
ATOM   2822  C  C   . GLY C  1 88  ? 92.653  120.216 49.005 1.00 40.36  ? 82  GLY C C   1 
ATOM   2823  O  O   . GLY C  1 88  ? 92.332  120.114 50.190 1.00 39.38  ? 82  GLY C O   1 
ATOM   2824  N  N   . ASP C  1 89  ? 92.951  121.388 48.442 1.00 36.25  ? 83  ASP C N   1 
ATOM   2825  C  CA  . ASP C  1 89  ? 92.937  122.628 49.215 1.00 34.41  ? 83  ASP C CA  1 
ATOM   2826  C  C   . ASP C  1 89  ? 91.538  123.192 49.485 1.00 37.16  ? 83  ASP C C   1 
ATOM   2827  O  O   . ASP C  1 89  ? 90.956  123.872 48.634 1.00 38.36  ? 83  ASP C O   1 
ATOM   2828  C  CB  . ASP C  1 89  ? 93.775  123.700 48.518 1.00 31.37  ? 83  ASP C CB  1 
ATOM   2829  C  CG  . ASP C  1 89  ? 95.259  123.386 48.534 1.00 46.63  ? 83  ASP C CG  1 
ATOM   2830  O  OD1 . ASP C  1 89  ? 95.710  122.701 49.486 1.00 39.16  ? 83  ASP C OD1 1 
ATOM   2831  O  OD2 . ASP C  1 89  ? 95.978  123.844 47.607 1.00 38.26  ? 83  ASP C OD2 1 
ATOM   2832  N  N   . LEU C  1 90  ? 91.009  122.949 50.680 1.00 30.41  ? 84  LEU C N   1 
ATOM   2833  C  CA  . LEU C  1 90  ? 89.683  123.449 51.005 1.00 28.42  ? 84  LEU C CA  1 
ATOM   2834  C  C   . LEU C  1 90  ? 89.707  124.651 51.942 1.00 33.22  ? 84  LEU C C   1 
ATOM   2835  O  O   . LEU C  1 90  ? 88.691  124.996 52.550 1.00 35.51  ? 84  LEU C O   1 
ATOM   2836  C  CB  . LEU C  1 90  ? 88.828  122.322 51.590 1.00 33.85  ? 84  LEU C CB  1 
ATOM   2837  C  CG  . LEU C  1 90  ? 88.664  121.134 50.630 1.00 32.32  ? 84  LEU C CG  1 
ATOM   2838  C  CD1 . LEU C  1 90  ? 87.860  120.044 51.302 1.00 24.36  ? 84  LEU C CD1 1 
ATOM   2839  C  CD2 . LEU C  1 90  ? 87.986  121.595 49.343 1.00 26.52  ? 84  LEU C CD2 1 
ATOM   2840  N  N   . GLY C  1 91  ? 90.871  125.288 52.055 1.00 36.73  ? 85  GLY C N   1 
ATOM   2841  C  CA  . GLY C  1 91  ? 91.000  126.480 52.884 1.00 30.45  ? 85  GLY C CA  1 
ATOM   2842  C  C   . GLY C  1 91  ? 90.922  126.386 54.400 1.00 32.85  ? 85  GLY C C   1 
ATOM   2843  O  O   . GLY C  1 91  ? 91.643  125.621 55.039 1.00 36.04  ? 85  GLY C O   1 
ATOM   2844  N  N   . ASN C  1 92  ? 90.023  127.159 54.987 1.00 26.63  ? 86  ASN C N   1 
ATOM   2845  C  CA  . ASN C  1 92  ? 89.922  127.198 56.433 1.00 33.50  ? 86  ASN C CA  1 
ATOM   2846  C  C   . ASN C  1 92  ? 88.518  127.039 56.961 1.00 35.14  ? 86  ASN C C   1 
ATOM   2847  O  O   . ASN C  1 92  ? 87.552  127.464 56.331 1.00 31.50  ? 86  ASN C O   1 
ATOM   2848  C  CB  . ASN C  1 92  ? 90.465  128.535 56.956 1.00 32.67  ? 86  ASN C CB  1 
ATOM   2849  C  CG  . ASN C  1 92  ? 91.977  128.658 56.828 1.00 38.82  ? 86  ASN C CG  1 
ATOM   2850  O  OD1 . ASN C  1 92  ? 92.722  128.237 57.716 1.00 41.65  ? 86  ASN C OD1 1 
ATOM   2851  N  ND2 . ASN C  1 92  ? 92.438  129.236 55.720 1.00 36.65  ? 86  ASN C ND2 1 
ATOM   2852  N  N   . VAL C  1 93  ? 88.412  126.412 58.126 1.00 29.97  ? 87  VAL C N   1 
ATOM   2853  C  CA  . VAL C  1 93  ? 87.127  126.269 58.771 1.00 29.55  ? 87  VAL C CA  1 
ATOM   2854  C  C   . VAL C  1 93  ? 87.312  127.107 60.038 1.00 35.60  ? 87  VAL C C   1 
ATOM   2855  O  O   . VAL C  1 93  ? 88.440  127.332 60.489 1.00 35.83  ? 87  VAL C O   1 
ATOM   2856  C  CB  . VAL C  1 93  ? 86.783  124.785 59.062 1.00 31.83  ? 87  VAL C CB  1 
ATOM   2857  C  CG1 . VAL C  1 93  ? 86.755  124.026 57.750 1.00 31.52  ? 87  VAL C CG1 1 
ATOM   2858  C  CG2 . VAL C  1 93  ? 87.785  124.154 60.032 1.00 26.30  ? 87  VAL C CG2 1 
ATOM   2859  N  N   . THR C  1 94  ? 86.219  127.579 60.607 1.00 34.79  ? 88  THR C N   1 
ATOM   2860  C  CA  . THR C  1 94  ? 86.317  128.441 61.758 1.00 37.14  ? 88  THR C CA  1 
ATOM   2861  C  C   . THR C  1 94  ? 85.710  127.863 63.013 1.00 36.35  ? 88  THR C C   1 
ATOM   2862  O  O   . THR C  1 94  ? 84.538  127.500 63.035 1.00 37.95  ? 88  THR C O   1 
ATOM   2863  C  CB  . THR C  1 94  ? 85.626  129.793 61.448 1.00 47.59  ? 88  THR C CB  1 
ATOM   2864  O  OG1 . THR C  1 94  ? 86.236  130.387 60.290 1.00 48.51  ? 88  THR C OG1 1 
ATOM   2865  C  CG2 . THR C  1 94  ? 85.726  130.741 62.636 1.00 45.85  ? 88  THR C CG2 1 
ATOM   2866  N  N   . ALA C  1 95  ? 86.507  127.793 64.069 1.00 34.05  ? 89  ALA C N   1 
ATOM   2867  C  CA  . ALA C  1 95  ? 86.007  127.294 65.334 1.00 35.50  ? 89  ALA C CA  1 
ATOM   2868  C  C   . ALA C  1 95  ? 85.561  128.484 66.188 1.00 38.26  ? 89  ALA C C   1 
ATOM   2869  O  O   . ALA C  1 95  ? 86.183  129.553 66.149 1.00 40.00  ? 89  ALA C O   1 
ATOM   2870  C  CB  . ALA C  1 95  ? 87.080  126.513 66.039 1.00 37.94  ? 89  ALA C CB  1 
ATOM   2871  N  N   . ASP C  1 96  ? 84.481  128.296 66.946 1.00 38.06  ? 90  ASP C N   1 
ATOM   2872  C  CA  . ASP C  1 96  ? 83.937  129.343 67.815 1.00 39.23  ? 90  ASP C CA  1 
ATOM   2873  C  C   . ASP C  1 96  ? 84.453  129.238 69.251 1.00 41.49  ? 90  ASP C C   1 
ATOM   2874  O  O   . ASP C  1 96  ? 85.267  128.372 69.574 1.00 43.93  ? 90  ASP C O   1 
ATOM   2875  C  CB  . ASP C  1 96  ? 82.393  129.303 67.802 1.00 37.98  ? 90  ASP C CB  1 
ATOM   2876  C  CG  . ASP C  1 96  ? 81.811  128.034 68.446 1.00 46.70  ? 90  ASP C CG  1 
ATOM   2877  O  OD1 . ASP C  1 96  ? 80.633  127.698 68.163 1.00 46.15  ? 90  ASP C OD1 1 
ATOM   2878  O  OD2 . ASP C  1 96  ? 82.517  127.374 69.241 1.00 40.23  ? 90  ASP C OD2 1 
ATOM   2879  N  N   . LYS C  1 97  ? 83.979  130.133 70.107 1.00 48.65  ? 91  LYS C N   1 
ATOM   2880  C  CA  . LYS C  1 97  ? 84.380  130.153 71.508 1.00 50.96  ? 91  LYS C CA  1 
ATOM   2881  C  C   . LYS C  1 97  ? 84.055  128.835 72.216 1.00 48.28  ? 91  LYS C C   1 
ATOM   2882  O  O   . LYS C  1 97  ? 84.533  128.579 73.317 1.00 44.54  ? 91  LYS C O   1 
ATOM   2883  C  CB  . LYS C  1 97  ? 83.693  131.324 72.214 1.00 59.81  ? 91  LYS C CB  1 
ATOM   2884  C  CG  . LYS C  1 97  ? 84.081  132.666 71.606 1.00 79.58  ? 91  LYS C CG  1 
ATOM   2885  C  CD  . LYS C  1 97  ? 83.348  133.843 72.229 1.00 86.89  ? 91  LYS C CD  1 
ATOM   2886  C  CE  . LYS C  1 97  ? 83.810  135.152 71.594 1.00 86.86  ? 91  LYS C CE  1 
ATOM   2887  N  NZ  . LYS C  1 97  ? 83.034  136.321 72.087 1.00 86.85  ? 91  LYS C NZ  1 
ATOM   2888  N  N   . ASP C  1 98  ? 83.249  127.997 71.575 1.00 43.52  ? 92  ASP C N   1 
ATOM   2889  C  CA  . ASP C  1 98  ? 82.871  126.714 72.153 1.00 47.05  ? 92  ASP C CA  1 
ATOM   2890  C  C   . ASP C  1 98  ? 83.625  125.541 71.524 1.00 43.23  ? 92  ASP C C   1 
ATOM   2891  O  O   . ASP C  1 98  ? 83.241  124.383 71.701 1.00 41.57  ? 92  ASP C O   1 
ATOM   2892  C  CB  . ASP C  1 98  ? 81.358  126.500 72.008 1.00 59.75  ? 92  ASP C CB  1 
ATOM   2893  C  CG  . ASP C  1 98  ? 80.537  127.481 72.850 1.00 69.90  ? 92  ASP C CG  1 
ATOM   2894  O  OD1 . ASP C  1 98  ? 79.297  127.522 72.676 1.00 76.04  ? 92  ASP C OD1 1 
ATOM   2895  O  OD2 . ASP C  1 98  ? 81.128  128.205 73.686 1.00 70.03  ? 92  ASP C OD2 1 
ATOM   2896  N  N   . ALA C  1 99  ? 84.697  125.853 70.796 1.00 38.28  ? 93  ALA C N   1 
ATOM   2897  C  CA  . ALA C  1 99  ? 85.537  124.853 70.129 1.00 39.64  ? 93  ALA C CA  1 
ATOM   2898  C  C   . ALA C  1 99  ? 84.794  124.068 69.057 1.00 38.56  ? 93  ALA C C   1 
ATOM   2899  O  O   . ALA C  1 99  ? 85.142  122.922 68.773 1.00 36.07  ? 93  ALA C O   1 
ATOM   2900  C  CB  . ALA C  1 99  ? 86.127  123.889 71.152 1.00 28.43  ? 93  ALA C CB  1 
ATOM   2901  N  N   . VAL C  1 100 ? 83.771  124.685 68.474 1.00 34.20  ? 94  VAL C N   1 
ATOM   2902  C  CA  . VAL C  1 100 ? 82.982  124.043 67.433 1.00 35.98  ? 94  VAL C CA  1 
ATOM   2903  C  C   . VAL C  1 100 ? 83.116  124.774 66.104 1.00 38.82  ? 94  VAL C C   1 
ATOM   2904  O  O   . VAL C  1 100 ? 82.962  125.998 66.019 1.00 33.77  ? 94  VAL C O   1 
ATOM   2905  C  CB  . VAL C  1 100 ? 81.480  123.986 67.818 1.00 38.21  ? 94  VAL C CB  1 
ATOM   2906  C  CG1 . VAL C  1 100 ? 80.657  123.382 66.678 1.00 30.85  ? 94  VAL C CG1 1 
ATOM   2907  C  CG2 . VAL C  1 100 ? 81.301  123.149 69.083 1.00 41.32  ? 94  VAL C CG2 1 
ATOM   2908  N  N   . ALA C  1 101 ? 83.422  124.016 65.063 1.00 36.60  ? 95  ALA C N   1 
ATOM   2909  C  CA  . ALA C  1 101 ? 83.548  124.591 63.740 1.00 38.28  ? 95  ALA C CA  1 
ATOM   2910  C  C   . ALA C  1 101 ? 82.420  124.016 62.893 1.00 41.14  ? 95  ALA C C   1 
ATOM   2911  O  O   . ALA C  1 101 ? 82.360  122.808 62.672 1.00 44.26  ? 95  ALA C O   1 
ATOM   2912  C  CB  . ALA C  1 101 ? 84.898  124.235 63.131 1.00 30.07  ? 95  ALA C CB  1 
ATOM   2913  N  N   . ASP C  1 102 ? 81.512  124.877 62.447 1.00 40.99  ? 96  ASP C N   1 
ATOM   2914  C  CA  . ASP C  1 102 ? 80.408  124.442 61.605 1.00 38.64  ? 96  ASP C CA  1 
ATOM   2915  C  C   . ASP C  1 102 ? 80.890  124.621 60.184 1.00 41.01  ? 96  ASP C C   1 
ATOM   2916  O  O   . ASP C  1 102 ? 81.155  125.741 59.735 1.00 40.68  ? 96  ASP C O   1 
ATOM   2917  C  CB  . ASP C  1 102 ? 79.154  125.284 61.872 1.00 50.04  ? 96  ASP C CB  1 
ATOM   2918  C  CG  . ASP C  1 102 ? 78.530  124.987 63.236 1.00 63.93  ? 96  ASP C CG  1 
ATOM   2919  O  OD1 . ASP C  1 102 ? 78.341  125.938 64.031 1.00 69.28  ? 96  ASP C OD1 1 
ATOM   2920  O  OD2 . ASP C  1 102 ? 78.228  123.799 63.514 1.00 65.84  ? 96  ASP C OD2 1 
ATOM   2921  N  N   . VAL C  1 103 ? 81.026  123.502 59.483 1.00 41.59  ? 97  VAL C N   1 
ATOM   2922  C  CA  . VAL C  1 103 ? 81.508  123.507 58.112 1.00 32.23  ? 97  VAL C CA  1 
ATOM   2923  C  C   . VAL C  1 103 ? 80.392  123.532 57.082 1.00 34.84  ? 97  VAL C C   1 
ATOM   2924  O  O   . VAL C  1 103 ? 79.375  122.850 57.209 1.00 35.63  ? 97  VAL C O   1 
ATOM   2925  C  CB  . VAL C  1 103 ? 82.398  122.268 57.842 1.00 37.20  ? 97  VAL C CB  1 
ATOM   2926  C  CG1 . VAL C  1 103 ? 82.959  122.312 56.409 1.00 29.08  ? 97  VAL C CG1 1 
ATOM   2927  C  CG2 . VAL C  1 103 ? 83.527  122.215 58.862 1.00 29.71  ? 97  VAL C CG2 1 
ATOM   2928  N  N   . SER C  1 104 ? 80.597  124.332 56.050 1.00 40.37  ? 98  SER C N   1 
ATOM   2929  C  CA  . SER C  1 104 ? 79.637  124.447 54.970 1.00 43.47  ? 98  SER C CA  1 
ATOM   2930  C  C   . SER C  1 104 ? 80.452  124.991 53.818 1.00 41.20  ? 98  SER C C   1 
ATOM   2931  O  O   . SER C  1 104 ? 80.844  126.153 53.795 1.00 37.57  ? 98  SER C O   1 
ATOM   2932  C  CB  . SER C  1 104 ? 78.502  125.397 55.345 1.00 44.44  ? 98  SER C CB  1 
ATOM   2933  O  OG  . SER C  1 104 ? 77.360  125.151 54.537 1.00 50.29  ? 98  SER C OG  1 
ATOM   2934  N  N   . ILE C  1 105 ? 80.724  124.115 52.869 1.00 40.85  ? 99  ILE C N   1 
ATOM   2935  C  CA  . ILE C  1 105 ? 81.538  124.461 51.731 1.00 41.20  ? 99  ILE C CA  1 
ATOM   2936  C  C   . ILE C  1 105 ? 80.965  123.885 50.457 1.00 41.08  ? 99  ILE C C   1 
ATOM   2937  O  O   . ILE C  1 105 ? 80.195  122.931 50.469 1.00 45.23  ? 99  ILE C O   1 
ATOM   2938  C  CB  . ILE C  1 105 ? 82.971  123.911 51.931 1.00 40.66  ? 99  ILE C CB  1 
ATOM   2939  C  CG1 . ILE C  1 105 ? 83.609  124.614 53.115 1.00 49.81  ? 99  ILE C CG1 1 
ATOM   2940  C  CG2 . ILE C  1 105 ? 83.822  124.088 50.677 1.00 36.67  ? 99  ILE C CG2 1 
ATOM   2941  C  CD1 . ILE C  1 105 ? 85.030  124.177 53.365 1.00 66.56  ? 99  ILE C CD1 1 
ATOM   2942  N  N   . GLU C  1 106 ? 81.345  124.497 49.352 1.00 42.66  ? 100 GLU C N   1 
ATOM   2943  C  CA  . GLU C  1 106 ? 80.940  124.051 48.040 1.00 43.18  ? 100 GLU C CA  1 
ATOM   2944  C  C   . GLU C  1 106 ? 82.216  124.243 47.277 1.00 38.21  ? 100 GLU C C   1 
ATOM   2945  O  O   . GLU C  1 106 ? 82.834  125.296 47.350 1.00 35.78  ? 100 GLU C O   1 
ATOM   2946  C  CB  . GLU C  1 106 ? 79.820  124.924 47.469 1.00 48.15  ? 100 GLU C CB  1 
ATOM   2947  C  CG  . GLU C  1 106 ? 78.429  124.470 47.899 1.00 70.89  ? 100 GLU C CG  1 
ATOM   2948  C  CD  . GLU C  1 106 ? 77.311  125.131 47.103 1.00 83.38  ? 100 GLU C CD  1 
ATOM   2949  O  OE1 . GLU C  1 106 ? 77.462  125.270 45.865 1.00 85.44  ? 100 GLU C OE1 1 
ATOM   2950  O  OE2 . GLU C  1 106 ? 76.277  125.493 47.716 1.00 86.30  ? 100 GLU C OE2 1 
ATOM   2951  N  N   . ASP C  1 107 ? 82.644  123.205 46.588 1.00 32.92  ? 101 ASP C N   1 
ATOM   2952  C  CA  . ASP C  1 107 ? 83.863  123.285 45.830 1.00 35.48  ? 101 ASP C CA  1 
ATOM   2953  C  C   . ASP C  1 107 ? 83.596  122.564 44.528 1.00 43.40  ? 101 ASP C C   1 
ATOM   2954  O  O   . ASP C  1 107 ? 82.733  121.692 44.469 1.00 48.26  ? 101 ASP C O   1 
ATOM   2955  C  CB  . ASP C  1 107 ? 84.993  122.616 46.605 1.00 38.27  ? 101 ASP C CB  1 
ATOM   2956  C  CG  . ASP C  1 107 ? 86.335  122.774 45.928 1.00 33.82  ? 101 ASP C CG  1 
ATOM   2957  O  OD1 . ASP C  1 107 ? 86.763  121.823 45.248 1.00 33.92  ? 101 ASP C OD1 1 
ATOM   2958  O  OD2 . ASP C  1 107 ? 86.954  123.858 46.076 1.00 42.14  ? 101 ASP C OD2 1 
ATOM   2959  N  N   . SER C  1 108 ? 84.330  122.929 43.486 1.00 45.22  ? 102 SER C N   1 
ATOM   2960  C  CA  . SER C  1 108 ? 84.130  122.312 42.192 1.00 47.35  ? 102 SER C CA  1 
ATOM   2961  C  C   . SER C  1 108 ? 85.427  121.757 41.635 1.00 46.43  ? 102 SER C C   1 
ATOM   2962  O  O   . SER C  1 108 ? 85.509  121.473 40.444 1.00 44.99  ? 102 SER C O   1 
ATOM   2963  C  CB  . SER C  1 108 ? 83.573  123.327 41.207 1.00 42.80  ? 102 SER C CB  1 
ATOM   2964  O  OG  . SER C  1 108 ? 84.644  124.068 40.657 1.00 40.60  ? 102 SER C OG  1 
ATOM   2965  N  N   . VAL C  1 109 ? 86.447  121.623 42.475 1.00 44.20  ? 103 VAL C N   1 
ATOM   2966  C  CA  . VAL C  1 109 ? 87.704  121.063 42.001 1.00 45.23  ? 103 VAL C CA  1 
ATOM   2967  C  C   . VAL C  1 109 ? 87.800  119.595 42.414 1.00 49.46  ? 103 VAL C C   1 
ATOM   2968  O  O   . VAL C  1 109 ? 88.289  118.757 41.653 1.00 54.55  ? 103 VAL C O   1 
ATOM   2969  C  CB  . VAL C  1 109 ? 88.904  121.845 42.541 1.00 45.75  ? 103 VAL C CB  1 
ATOM   2970  C  CG1 . VAL C  1 109 ? 90.214  121.181 42.087 1.00 42.50  ? 103 VAL C CG1 1 
ATOM   2971  C  CG2 . VAL C  1 109 ? 88.841  123.271 42.029 1.00 35.84  ? 103 VAL C CG2 1 
ATOM   2972  N  N   . ILE C  1 110 ? 87.324  119.292 43.618 1.00 46.90  ? 104 ILE C N   1 
ATOM   2973  C  CA  . ILE C  1 110 ? 87.317  117.927 44.136 1.00 46.59  ? 104 ILE C CA  1 
ATOM   2974  C  C   . ILE C  1 110 ? 86.066  117.248 43.594 1.00 50.02  ? 104 ILE C C   1 
ATOM   2975  O  O   . ILE C  1 110 ? 85.020  117.881 43.458 1.00 50.00  ? 104 ILE C O   1 
ATOM   2976  C  CB  . ILE C  1 110 ? 87.196  117.886 45.680 1.00 36.39  ? 104 ILE C CB  1 
ATOM   2977  C  CG1 . ILE C  1 110 ? 85.915  118.607 46.110 1.00 26.75  ? 104 ILE C CG1 1 
ATOM   2978  C  CG2 . ILE C  1 110 ? 88.413  118.500 46.326 1.00 38.00  ? 104 ILE C CG2 1 
ATOM   2979  C  CD1 . ILE C  1 110 ? 85.752  118.759 47.602 1.00 31.23  ? 104 ILE C CD1 1 
ATOM   2980  N  N   . SER C  1 111 ? 86.160  115.965 43.282 1.00 49.90  ? 105 SER C N   1 
ATOM   2981  C  CA  . SER C  1 111 ? 84.980  115.261 42.811 1.00 47.23  ? 105 SER C CA  1 
ATOM   2982  C  C   . SER C  1 111 ? 84.831  113.957 43.589 1.00 48.22  ? 105 SER C C   1 
ATOM   2983  O  O   . SER C  1 111 ? 85.810  113.421 44.116 1.00 42.82  ? 105 SER C O   1 
ATOM   2984  C  CB  . SER C  1 111 ? 85.074  114.966 41.308 1.00 43.53  ? 105 SER C CB  1 
ATOM   2985  O  OG  . SER C  1 111 ? 83.811  114.532 40.818 1.00 40.66  ? 105 SER C OG  1 
ATOM   2986  N  N   . LEU C  1 112 ? 83.602  113.458 43.671 1.00 45.02  ? 106 LEU C N   1 
ATOM   2987  C  CA  . LEU C  1 112 ? 83.351  112.209 44.363 1.00 42.51  ? 106 LEU C CA  1 
ATOM   2988  C  C   . LEU C  1 112 ? 83.410  111.077 43.355 1.00 44.55  ? 106 LEU C C   1 
ATOM   2989  O  O   . LEU C  1 112 ? 82.983  109.959 43.639 1.00 49.26  ? 106 LEU C O   1 
ATOM   2990  C  CB  . LEU C  1 112 ? 81.981  112.236 45.031 1.00 34.90  ? 106 LEU C CB  1 
ATOM   2991  C  CG  . LEU C  1 112 ? 81.872  113.270 46.151 1.00 31.62  ? 106 LEU C CG  1 
ATOM   2992  C  CD1 . LEU C  1 112 ? 80.527  113.120 46.854 1.00 25.67  ? 106 LEU C CD1 1 
ATOM   2993  C  CD2 . LEU C  1 112 ? 83.027  113.064 47.146 1.00 28.32  ? 106 LEU C CD2 1 
ATOM   2994  N  N   . SER C  1 113 ? 83.949  111.368 42.175 1.00 41.55  ? 107 SER C N   1 
ATOM   2995  C  CA  . SER C  1 113 ? 84.030  110.364 41.129 1.00 45.32  ? 107 SER C CA  1 
ATOM   2996  C  C   . SER C  1 113 ? 84.950  110.770 40.011 1.00 46.80  ? 107 SER C C   1 
ATOM   2997  O  O   . SER C  1 113 ? 85.200  111.949 39.788 1.00 42.62  ? 107 SER C O   1 
ATOM   2998  C  CB  . SER C  1 113 ? 82.639  110.097 40.532 1.00 48.42  ? 107 SER C CB  1 
ATOM   2999  O  OG  . SER C  1 113 ? 82.038  111.294 40.050 1.00 45.54  ? 107 SER C OG  1 
ATOM   3000  N  N   . GLY C  1 114 ? 85.433  109.765 39.298 1.00 50.73  ? 108 GLY C N   1 
ATOM   3001  C  CA  . GLY C  1 114 ? 86.309  110.011 38.180 1.00 63.66  ? 108 GLY C CA  1 
ATOM   3002  C  C   . GLY C  1 114 ? 87.733  110.311 38.566 1.00 70.08  ? 108 GLY C C   1 
ATOM   3003  O  O   . GLY C  1 114 ? 87.985  110.921 39.595 1.00 74.18  ? 108 GLY C O   1 
ATOM   3004  N  N   . ASP C  1 115 ? 88.649  109.863 37.714 1.00 78.71  ? 109 ASP C N   1 
ATOM   3005  C  CA  . ASP C  1 115 ? 90.088  110.045 37.865 1.00 84.86  ? 109 ASP C CA  1 
ATOM   3006  C  C   . ASP C  1 115 ? 90.598  110.636 39.174 1.00 84.12  ? 109 ASP C C   1 
ATOM   3007  O  O   . ASP C  1 115 ? 91.453  110.040 39.829 1.00 86.10  ? 109 ASP C O   1 
ATOM   3008  C  CB  . ASP C  1 115 ? 90.640  110.884 36.694 1.00 91.47  ? 109 ASP C CB  1 
ATOM   3009  C  CG  . ASP C  1 115 ? 89.824  112.156 36.429 1.00 94.25  ? 109 ASP C CG  1 
ATOM   3010  O  OD1 . ASP C  1 115 ? 89.356  112.799 37.397 1.00 96.93  ? 109 ASP C OD1 1 
ATOM   3011  O  OD2 . ASP C  1 115 ? 89.665  112.516 35.241 1.00 86.34  ? 109 ASP C OD2 1 
ATOM   3012  N  N   . HIS C  1 116 ? 90.086  111.804 39.553 1.00 79.14  ? 110 HIS C N   1 
ATOM   3013  C  CA  . HIS C  1 116 ? 90.545  112.461 40.763 1.00 76.07  ? 110 HIS C CA  1 
ATOM   3014  C  C   . HIS C  1 116 ? 89.523  112.662 41.883 1.00 69.79  ? 110 HIS C C   1 
ATOM   3015  O  O   . HIS C  1 116 ? 89.399  113.761 42.443 1.00 67.08  ? 110 HIS C O   1 
ATOM   3016  C  CB  . HIS C  1 116 ? 91.175  113.786 40.361 1.00 84.42  ? 110 HIS C CB  1 
ATOM   3017  C  CG  . HIS C  1 116 ? 92.335  113.626 39.429 1.00 97.65  ? 110 HIS C CG  1 
ATOM   3018  N  ND1 . HIS C  1 116 ? 92.851  114.668 38.688 1.00 106.27 ? 110 HIS C ND1 1 
ATOM   3019  C  CD2 . HIS C  1 116 ? 93.076  112.536 39.111 1.00 99.77  ? 110 HIS C CD2 1 
ATOM   3020  C  CE1 . HIS C  1 116 ? 93.858  114.228 37.953 1.00 108.93 ? 110 HIS C CE1 1 
ATOM   3021  N  NE2 . HIS C  1 116 ? 94.015  112.937 38.192 1.00 107.15 ? 110 HIS C NE2 1 
ATOM   3022  N  N   . CYS C  1 117 ? 88.788  111.606 42.221 1.00 58.59  ? 111 CYS C N   1 
ATOM   3023  C  CA  . CYS C  1 117 ? 87.827  111.745 43.294 1.00 50.53  ? 111 CYS C CA  1 
ATOM   3024  C  C   . CYS C  1 117 ? 88.616  111.637 44.587 1.00 42.87  ? 111 CYS C C   1 
ATOM   3025  O  O   . CYS C  1 117 ? 89.749  111.156 44.593 1.00 43.32  ? 111 CYS C O   1 
ATOM   3026  C  CB  . CYS C  1 117 ? 86.706  110.682 43.217 1.00 54.34  ? 111 CYS C CB  1 
ATOM   3027  S  SG  . CYS C  1 117 ? 87.075  108.935 43.558 1.00 48.63  ? 111 CYS C SG  1 
ATOM   3028  N  N   . ILE C  1 118 ? 88.027  112.115 45.672 1.00 32.75  ? 112 ILE C N   1 
ATOM   3029  C  CA  . ILE C  1 118 ? 88.680  112.086 46.969 1.00 33.53  ? 112 ILE C CA  1 
ATOM   3030  C  C   . ILE C  1 118 ? 88.270  110.866 47.794 1.00 39.57  ? 112 ILE C C   1 
ATOM   3031  O  O   . ILE C  1 118 ? 88.818  110.637 48.877 1.00 39.62  ? 112 ILE C O   1 
ATOM   3032  C  CB  . ILE C  1 118 ? 88.358  113.366 47.757 1.00 26.85  ? 112 ILE C CB  1 
ATOM   3033  C  CG1 . ILE C  1 118 ? 86.844  113.488 47.959 1.00 26.12  ? 112 ILE C CG1 1 
ATOM   3034  C  CG2 . ILE C  1 118 ? 88.863  114.573 46.986 1.00 23.78  ? 112 ILE C CG2 1 
ATOM   3035  C  CD1 . ILE C  1 118 ? 86.402  114.752 48.689 1.00 18.17  ? 112 ILE C CD1 1 
ATOM   3036  N  N   . ILE C  1 119 ? 87.303  110.094 47.293 1.00 35.49  ? 113 ILE C N   1 
ATOM   3037  C  CA  . ILE C  1 119 ? 86.866  108.902 48.001 1.00 33.16  ? 113 ILE C CA  1 
ATOM   3038  C  C   . ILE C  1 119 ? 88.069  107.997 48.197 1.00 32.41  ? 113 ILE C C   1 
ATOM   3039  O  O   . ILE C  1 119 ? 88.831  107.777 47.269 1.00 20.35  ? 113 ILE C O   1 
ATOM   3040  C  CB  . ILE C  1 119 ? 85.763  108.149 47.233 1.00 33.62  ? 113 ILE C CB  1 
ATOM   3041  C  CG1 . ILE C  1 119 ? 84.465  108.953 47.320 1.00 27.70  ? 113 ILE C CG1 1 
ATOM   3042  C  CG2 . ILE C  1 119 ? 85.530  106.741 47.860 1.00 22.02  ? 113 ILE C CG2 1 
ATOM   3043  C  CD1 . ILE C  1 119 ? 83.386  108.478 46.385 1.00 28.45  ? 113 ILE C CD1 1 
ATOM   3044  N  N   . GLY C  1 120 ? 88.247  107.496 49.419 1.00 27.95  ? 114 GLY C N   1 
ATOM   3045  C  CA  . GLY C  1 120 ? 89.391  106.640 49.687 1.00 29.69  ? 114 GLY C CA  1 
ATOM   3046  C  C   . GLY C  1 120 ? 90.674  107.368 50.075 1.00 26.15  ? 114 GLY C C   1 
ATOM   3047  O  O   . GLY C  1 120 ? 91.703  106.727 50.286 1.00 29.38  ? 114 GLY C O   1 
ATOM   3048  N  N   . ARG C  1 121 ? 90.627  108.696 50.156 1.00 25.67  ? 115 ARG C N   1 
ATOM   3049  C  CA  . ARG C  1 121 ? 91.789  109.494 50.542 1.00 32.45  ? 115 ARG C CA  1 
ATOM   3050  C  C   . ARG C  1 121 ? 91.480  110.037 51.942 1.00 32.10  ? 115 ARG C C   1 
ATOM   3051  O  O   . ARG C  1 121 ? 90.390  109.778 52.471 1.00 31.66  ? 115 ARG C O   1 
ATOM   3052  C  CB  . ARG C  1 121 ? 92.025  110.631 49.530 1.00 29.92  ? 115 ARG C CB  1 
ATOM   3053  C  CG  . ARG C  1 121 ? 91.609  110.256 48.101 1.00 47.11  ? 115 ARG C CG  1 
ATOM   3054  C  CD  . ARG C  1 121 ? 92.291  111.088 47.013 1.00 40.58  ? 115 ARG C CD  1 
ATOM   3055  N  NE  . ARG C  1 121 ? 93.645  110.604 46.777 1.00 40.02  ? 115 ARG C NE  1 
ATOM   3056  C  CZ  . ARG C  1 121 ? 94.042  109.972 45.682 1.00 28.53  ? 115 ARG C CZ  1 
ATOM   3057  N  NH1 . ARG C  1 121 ? 93.188  109.744 44.700 1.00 28.91  ? 115 ARG C NH1 1 
ATOM   3058  N  NH2 . ARG C  1 121 ? 95.297  109.555 45.581 1.00 32.71  ? 115 ARG C NH2 1 
ATOM   3059  N  N   . THR C  1 122 ? 92.414  110.779 52.544 1.00 32.59  ? 116 THR C N   1 
ATOM   3060  C  CA  . THR C  1 122 ? 92.221  111.301 53.907 1.00 31.44  ? 116 THR C CA  1 
ATOM   3061  C  C   . THR C  1 122 ? 91.861  112.784 54.038 1.00 32.62  ? 116 THR C C   1 
ATOM   3062  O  O   . THR C  1 122 ? 92.454  113.636 53.384 1.00 35.31  ? 116 THR C O   1 
ATOM   3063  C  CB  . THR C  1 122 ? 93.495  111.041 54.774 1.00 34.91  ? 116 THR C CB  1 
ATOM   3064  O  OG1 . THR C  1 122 ? 93.704  109.632 54.903 1.00 29.99  ? 116 THR C OG1 1 
ATOM   3065  C  CG2 . THR C  1 122 ? 93.352  111.637 56.177 1.00 24.78  ? 116 THR C CG2 1 
ATOM   3066  N  N   . LEU C  1 123 ? 90.877  113.084 54.881 1.00 30.11  ? 117 LEU C N   1 
ATOM   3067  C  CA  . LEU C  1 123 ? 90.498  114.470 55.142 1.00 24.86  ? 117 LEU C CA  1 
ATOM   3068  C  C   . LEU C  1 123 ? 91.250  114.848 56.426 1.00 26.92  ? 117 LEU C C   1 
ATOM   3069  O  O   . LEU C  1 123 ? 91.306  114.058 57.358 1.00 26.13  ? 117 LEU C O   1 
ATOM   3070  C  CB  . LEU C  1 123 ? 88.999  114.588 55.378 1.00 27.71  ? 117 LEU C CB  1 
ATOM   3071  C  CG  . LEU C  1 123 ? 88.518  115.993 55.740 1.00 26.93  ? 117 LEU C CG  1 
ATOM   3072  C  CD1 . LEU C  1 123 ? 88.661  116.889 54.536 1.00 25.06  ? 117 LEU C CD1 1 
ATOM   3073  C  CD2 . LEU C  1 123 ? 87.076  115.954 56.205 1.00 21.56  ? 117 LEU C CD2 1 
ATOM   3074  N  N   . VAL C  1 124 ? 91.821  116.048 56.478 1.00 30.36  ? 118 VAL C N   1 
ATOM   3075  C  CA  . VAL C  1 124 ? 92.592  116.480 57.644 1.00 24.53  ? 118 VAL C CA  1 
ATOM   3076  C  C   . VAL C  1 124 ? 92.284  117.891 58.101 1.00 28.09  ? 118 VAL C C   1 
ATOM   3077  O  O   . VAL C  1 124 ? 92.214  118.808 57.290 1.00 33.04  ? 118 VAL C O   1 
ATOM   3078  C  CB  . VAL C  1 124 ? 94.091  116.443 57.342 1.00 26.68  ? 118 VAL C CB  1 
ATOM   3079  C  CG1 . VAL C  1 124 ? 94.886  116.838 58.584 1.00 23.47  ? 118 VAL C CG1 1 
ATOM   3080  C  CG2 . VAL C  1 124 ? 94.480  115.063 56.826 1.00 17.27  ? 118 VAL C CG2 1 
ATOM   3081  N  N   . VAL C  1 125 ? 92.086  118.068 59.402 1.00 25.58  ? 119 VAL C N   1 
ATOM   3082  C  CA  . VAL C  1 125 ? 91.847  119.396 59.944 1.00 25.92  ? 119 VAL C CA  1 
ATOM   3083  C  C   . VAL C  1 125 ? 93.159  119.707 60.682 1.00 32.97  ? 119 VAL C C   1 
ATOM   3084  O  O   . VAL C  1 125 ? 93.615  118.929 61.523 1.00 33.32  ? 119 VAL C O   1 
ATOM   3085  C  CB  . VAL C  1 125 ? 90.612  119.433 60.894 1.00 28.50  ? 119 VAL C CB  1 
ATOM   3086  C  CG1 . VAL C  1 125 ? 90.775  118.450 62.044 1.00 31.77  ? 119 VAL C CG1 1 
ATOM   3087  C  CG2 . VAL C  1 125 ? 90.415  120.841 61.418 1.00 29.50  ? 119 VAL C CG2 1 
ATOM   3088  N  N   . HIS C  1 126 ? 93.775  120.834 60.340 1.00 33.80  ? 120 HIS C N   1 
ATOM   3089  C  CA  . HIS C  1 126 ? 95.059  121.213 60.911 1.00 31.61  ? 120 HIS C CA  1 
ATOM   3090  C  C   . HIS C  1 126 ? 95.054  122.109 62.139 1.00 32.84  ? 120 HIS C C   1 
ATOM   3091  O  O   . HIS C  1 126 ? 94.028  122.663 62.536 1.00 33.40  ? 120 HIS C O   1 
ATOM   3092  C  CB  . HIS C  1 126 ? 95.929  121.844 59.818 1.00 29.83  ? 120 HIS C CB  1 
ATOM   3093  C  CG  . HIS C  1 126 ? 96.336  120.887 58.735 1.00 32.54  ? 120 HIS C CG  1 
ATOM   3094  N  ND1 . HIS C  1 126 ? 97.606  120.358 58.648 1.00 30.59  ? 120 HIS C ND1 1 
ATOM   3095  C  CD2 . HIS C  1 126 ? 95.655  120.399 57.670 1.00 37.30  ? 120 HIS C CD2 1 
ATOM   3096  C  CE1 . HIS C  1 126 ? 97.694  119.595 57.572 1.00 32.15  ? 120 HIS C CE1 1 
ATOM   3097  N  NE2 . HIS C  1 126 ? 96.525  119.602 56.959 1.00 35.97  ? 120 HIS C NE2 1 
ATOM   3098  N  N   . GLU C  1 127 ? 96.244  122.235 62.722 1.00 38.30  ? 121 GLU C N   1 
ATOM   3099  C  CA  . GLU C  1 127 ? 96.507  123.025 63.923 1.00 35.88  ? 121 GLU C CA  1 
ATOM   3100  C  C   . GLU C  1 127 ? 96.330  124.531 63.741 1.00 38.65  ? 121 GLU C C   1 
ATOM   3101  O  O   . GLU C  1 127 ? 95.564  125.167 64.467 1.00 30.21  ? 121 GLU C O   1 
ATOM   3102  C  CB  . GLU C  1 127 ? 97.930  122.744 64.384 1.00 38.37  ? 121 GLU C CB  1 
ATOM   3103  C  CG  . GLU C  1 127 ? 98.384  123.545 65.578 1.00 42.64  ? 121 GLU C CG  1 
ATOM   3104  C  CD  . GLU C  1 127 ? 99.893  123.470 65.778 1.00 46.62  ? 121 GLU C CD  1 
ATOM   3105  O  OE1 . GLU C  1 127 ? 100.361 123.804 66.887 1.00 56.91  ? 121 GLU C OE1 1 
ATOM   3106  O  OE2 . GLU C  1 127 ? 100.616 123.087 64.829 1.00 39.26  ? 121 GLU C OE2 1 
ATOM   3107  N  N   . LYS C  1 128 ? 97.047  125.097 62.772 1.00 43.01  ? 122 LYS C N   1 
ATOM   3108  C  CA  . LYS C  1 128 ? 96.994  126.536 62.506 1.00 46.86  ? 122 LYS C CA  1 
ATOM   3109  C  C   . LYS C  1 128 ? 96.176  126.895 61.262 1.00 47.54  ? 122 LYS C C   1 
ATOM   3110  O  O   . LYS C  1 128 ? 95.705  126.031 60.515 1.00 44.63  ? 122 LYS C O   1 
ATOM   3111  C  CB  . LYS C  1 128 ? 98.404  127.111 62.302 1.00 46.15  ? 122 LYS C CB  1 
ATOM   3112  C  CG  . LYS C  1 128 ? 99.467  126.742 63.329 1.00 57.05  ? 122 LYS C CG  1 
ATOM   3113  C  CD  . LYS C  1 128 ? 100.849 127.092 62.771 1.00 63.75  ? 122 LYS C CD  1 
ATOM   3114  C  CE  . LYS C  1 128 ? 101.991 126.472 63.566 1.00 73.07  ? 122 LYS C CE  1 
ATOM   3115  N  NZ  . LYS C  1 128 ? 103.294 126.565 62.819 1.00 75.48  ? 122 LYS C NZ  1 
ATOM   3116  N  N   . ALA C  1 129 ? 96.032  128.198 61.050 1.00 39.77  ? 123 ALA C N   1 
ATOM   3117  C  CA  . ALA C  1 129 ? 95.320  128.703 59.900 1.00 40.31  ? 123 ALA C CA  1 
ATOM   3118  C  C   . ALA C  1 129 ? 96.158  128.403 58.656 1.00 40.71  ? 123 ALA C C   1 
ATOM   3119  O  O   . ALA C  1 129 ? 97.388  128.243 58.722 1.00 34.74  ? 123 ALA C O   1 
ATOM   3120  C  CB  . ALA C  1 129 ? 95.096  130.201 60.034 1.00 25.56  ? 123 ALA C CB  1 
ATOM   3121  N  N   . ASP C  1 130 ? 95.462  128.303 57.531 1.00 37.78  ? 124 ASP C N   1 
ATOM   3122  C  CA  . ASP C  1 130 ? 96.062  128.030 56.241 1.00 40.55  ? 124 ASP C CA  1 
ATOM   3123  C  C   . ASP C  1 130 ? 96.241  129.406 55.607 1.00 43.65  ? 124 ASP C C   1 
ATOM   3124  O  O   . ASP C  1 130 ? 95.265  130.142 55.434 1.00 38.73  ? 124 ASP C O   1 
ATOM   3125  C  CB  . ASP C  1 130 ? 95.098  127.157 55.438 1.00 42.40  ? 124 ASP C CB  1 
ATOM   3126  C  CG  . ASP C  1 130 ? 95.600  126.839 54.051 1.00 37.08  ? 124 ASP C CG  1 
ATOM   3127  O  OD1 . ASP C  1 130 ? 95.019  125.932 53.425 1.00 38.44  ? 124 ASP C OD1 1 
ATOM   3128  O  OD2 . ASP C  1 130 ? 96.552  127.488 53.585 1.00 41.04  ? 124 ASP C OD2 1 
ATOM   3129  N  N   . ASP C  1 131 ? 97.487  129.764 55.289 1.00 43.62  ? 125 ASP C N   1 
ATOM   3130  C  CA  . ASP C  1 131 ? 97.774  131.071 54.703 1.00 42.76  ? 125 ASP C CA  1 
ATOM   3131  C  C   . ASP C  1 131 ? 97.436  131.156 53.214 1.00 47.41  ? 125 ASP C C   1 
ATOM   3132  O  O   . ASP C  1 131 ? 97.785  132.130 52.535 1.00 50.55  ? 125 ASP C O   1 
ATOM   3133  C  CB  . ASP C  1 131 ? 99.239  131.448 54.946 1.00 36.63  ? 125 ASP C CB  1 
ATOM   3134  C  CG  . ASP C  1 131 ? 100.208 130.597 54.152 1.00 42.25  ? 125 ASP C CG  1 
ATOM   3135  O  OD1 . ASP C  1 131 ? 101.390 130.528 54.562 1.00 44.51  ? 125 ASP C OD1 1 
ATOM   3136  O  OD2 . ASP C  1 131 ? 99.802  130.012 53.120 1.00 36.84  ? 125 ASP C OD2 1 
ATOM   3137  N  N   . LEU C  1 132 ? 96.757  130.128 52.712 1.00 43.75  ? 126 LEU C N   1 
ATOM   3138  C  CA  . LEU C  1 132 ? 96.331  130.091 51.322 1.00 41.30  ? 126 LEU C CA  1 
ATOM   3139  C  C   . LEU C  1 132 ? 97.476  130.166 50.317 1.00 41.34  ? 126 LEU C C   1 
ATOM   3140  O  O   . LEU C  1 132 ? 97.252  130.499 49.161 1.00 41.61  ? 126 LEU C O   1 
ATOM   3141  C  CB  . LEU C  1 132 ? 95.337  131.230 51.062 1.00 30.45  ? 126 LEU C CB  1 
ATOM   3142  C  CG  . LEU C  1 132 ? 94.300  131.421 52.175 1.00 41.85  ? 126 LEU C CG  1 
ATOM   3143  C  CD1 . LEU C  1 132 ? 93.227  132.420 51.736 1.00 26.71  ? 126 LEU C CD1 1 
ATOM   3144  C  CD2 . LEU C  1 132 ? 93.667  130.069 52.522 1.00 40.07  ? 126 LEU C CD2 1 
ATOM   3145  N  N   . GLY C  1 133 ? 98.695  129.869 50.759 1.00 42.35  ? 127 GLY C N   1 
ATOM   3146  C  CA  . GLY C  1 133 ? 99.839  129.877 49.862 1.00 53.44  ? 127 GLY C CA  1 
ATOM   3147  C  C   . GLY C  1 133 ? 100.539 131.205 49.613 1.00 62.19  ? 127 GLY C C   1 
ATOM   3148  O  O   . GLY C  1 133 ? 101.568 131.249 48.938 1.00 68.10  ? 127 GLY C O   1 
ATOM   3149  N  N   . LYS C  1 134 ? 99.994  132.288 50.152 1.00 65.94  ? 128 LYS C N   1 
ATOM   3150  C  CA  . LYS C  1 134 ? 100.577 133.612 49.968 1.00 69.31  ? 128 LYS C CA  1 
ATOM   3151  C  C   . LYS C  1 134 ? 101.376 134.031 51.204 1.00 68.39  ? 128 LYS C C   1 
ATOM   3152  O  O   . LYS C  1 134 ? 101.369 135.195 51.599 1.00 60.09  ? 128 LYS C O   1 
ATOM   3153  C  CB  . LYS C  1 134 ? 99.462  134.631 49.683 1.00 71.38  ? 128 LYS C CB  1 
ATOM   3154  C  CG  . LYS C  1 134 ? 98.873  134.562 48.268 1.00 78.59  ? 128 LYS C CG  1 
ATOM   3155  C  CD  . LYS C  1 134 ? 98.329  133.181 47.944 1.00 86.71  ? 128 LYS C CD  1 
ATOM   3156  C  CE  . LYS C  1 134 ? 98.024  133.019 46.461 1.00 88.19  ? 128 LYS C CE  1 
ATOM   3157  N  NZ  . LYS C  1 134 ? 97.757  131.586 46.113 1.00 84.39  ? 128 LYS C NZ  1 
ATOM   3158  N  N   . GLY C  1 135 ? 102.077 133.073 51.800 1.00 68.97  ? 129 GLY C N   1 
ATOM   3159  C  CA  . GLY C  1 135 ? 102.844 133.357 52.999 1.00 68.23  ? 129 GLY C CA  1 
ATOM   3160  C  C   . GLY C  1 135 ? 104.216 133.964 52.791 1.00 70.03  ? 129 GLY C C   1 
ATOM   3161  O  O   . GLY C  1 135 ? 104.742 134.626 53.689 1.00 71.34  ? 129 GLY C O   1 
ATOM   3162  N  N   . GLY C  1 136 ? 104.800 133.744 51.618 1.00 66.20  ? 130 GLY C N   1 
ATOM   3163  C  CA  . GLY C  1 136 ? 106.119 134.285 51.348 1.00 64.51  ? 130 GLY C CA  1 
ATOM   3164  C  C   . GLY C  1 136 ? 107.196 133.213 51.361 1.00 64.33  ? 130 GLY C C   1 
ATOM   3165  O  O   . GLY C  1 136 ? 108.027 133.158 50.457 1.00 71.41  ? 130 GLY C O   1 
ATOM   3166  N  N   . ASN C  1 137 ? 107.185 132.362 52.383 1.00 61.15  ? 131 ASN C N   1 
ATOM   3167  C  CA  . ASN C  1 137 ? 108.159 131.275 52.508 1.00 60.94  ? 131 ASN C CA  1 
ATOM   3168  C  C   . ASN C  1 137 ? 107.761 130.087 51.627 1.00 60.86  ? 131 ASN C C   1 
ATOM   3169  O  O   . ASN C  1 137 ? 106.616 130.001 51.180 1.00 55.68  ? 131 ASN C O   1 
ATOM   3170  C  CB  . ASN C  1 137 ? 108.261 130.844 53.971 1.00 58.98  ? 131 ASN C CB  1 
ATOM   3171  C  CG  . ASN C  1 137 ? 106.904 130.709 54.631 1.00 61.98  ? 131 ASN C CG  1 
ATOM   3172  O  OD1 . ASN C  1 137 ? 106.166 129.757 54.369 1.00 67.57  ? 131 ASN C OD1 1 
ATOM   3173  N  ND2 . ASN C  1 137 ? 106.561 131.670 55.483 1.00 58.54  ? 131 ASN C ND2 1 
ATOM   3174  N  N   . GLU C  1 138 ? 108.693 129.167 51.382 1.00 63.65  ? 132 GLU C N   1 
ATOM   3175  C  CA  . GLU C  1 138 ? 108.390 128.028 50.518 1.00 66.04  ? 132 GLU C CA  1 
ATOM   3176  C  C   . GLU C  1 138 ? 107.379 127.043 51.121 1.00 67.74  ? 132 GLU C C   1 
ATOM   3177  O  O   . GLU C  1 138 ? 106.614 126.404 50.391 1.00 63.36  ? 132 GLU C O   1 
ATOM   3178  C  CB  . GLU C  1 138 ? 109.679 127.298 50.115 1.00 68.47  ? 132 GLU C CB  1 
ATOM   3179  C  CG  . GLU C  1 138 ? 110.042 126.096 50.965 1.00 86.54  ? 132 GLU C CG  1 
ATOM   3180  C  CD  . GLU C  1 138 ? 110.920 125.101 50.214 1.00 94.24  ? 132 GLU C CD  1 
ATOM   3181  O  OE1 . GLU C  1 138 ? 110.525 124.676 49.104 1.00 94.10  ? 132 GLU C OE1 1 
ATOM   3182  O  OE2 . GLU C  1 138 ? 111.999 124.739 50.732 1.00 98.15  ? 132 GLU C OE2 1 
ATOM   3183  N  N   . GLU C  1 139 ? 107.369 126.930 52.447 1.00 64.54  ? 133 GLU C N   1 
ATOM   3184  C  CA  . GLU C  1 139 ? 106.440 126.036 53.133 1.00 62.32  ? 133 GLU C CA  1 
ATOM   3185  C  C   . GLU C  1 139 ? 104.995 126.415 52.795 1.00 59.33  ? 133 GLU C C   1 
ATOM   3186  O  O   . GLU C  1 139 ? 104.123 125.554 52.659 1.00 55.50  ? 133 GLU C O   1 
ATOM   3187  C  CB  . GLU C  1 139 ? 106.646 126.116 54.652 1.00 63.61  ? 133 GLU C CB  1 
ATOM   3188  C  CG  . GLU C  1 139 ? 105.831 125.102 55.443 1.00 71.86  ? 133 GLU C CG  1 
ATOM   3189  C  CD  . GLU C  1 139 ? 106.160 123.660 55.070 1.00 77.17  ? 133 GLU C CD  1 
ATOM   3190  O  OE1 . GLU C  1 139 ? 105.413 122.756 55.494 1.00 80.39  ? 133 GLU C OE1 1 
ATOM   3191  O  OE2 . GLU C  1 139 ? 107.165 123.428 54.360 1.00 80.09  ? 133 GLU C OE2 1 
ATOM   3192  N  N   . SER C  1 140 ? 104.757 127.715 52.662 1.00 54.09  ? 134 SER C N   1 
ATOM   3193  C  CA  . SER C  1 140 ? 103.436 128.230 52.342 1.00 53.12  ? 134 SER C CA  1 
ATOM   3194  C  C   . SER C  1 140 ? 102.912 127.704 51.012 1.00 55.68  ? 134 SER C C   1 
ATOM   3195  O  O   . SER C  1 140 ? 101.702 127.560 50.837 1.00 57.32  ? 134 SER C O   1 
ATOM   3196  C  CB  . SER C  1 140 ? 103.473 129.756 52.303 1.00 51.26  ? 134 SER C CB  1 
ATOM   3197  O  OG  . SER C  1 140 ? 102.228 130.296 51.902 1.00 36.49  ? 134 SER C OG  1 
ATOM   3198  N  N   . THR C  1 141 ? 103.818 127.417 50.080 1.00 52.65  ? 135 THR C N   1 
ATOM   3199  C  CA  . THR C  1 141 ? 103.426 126.923 48.765 1.00 54.49  ? 135 THR C CA  1 
ATOM   3200  C  C   . THR C  1 141 ? 103.147 125.426 48.780 1.00 57.68  ? 135 THR C C   1 
ATOM   3201  O  O   . THR C  1 141 ? 102.699 124.854 47.778 1.00 57.04  ? 135 THR C O   1 
ATOM   3202  C  CB  . THR C  1 141 ? 104.519 127.196 47.718 1.00 58.40  ? 135 THR C CB  1 
ATOM   3203  O  OG1 . THR C  1 141 ? 105.663 126.379 47.996 1.00 64.95  ? 135 THR C OG1 1 
ATOM   3204  C  CG2 . THR C  1 141 ? 104.930 128.651 47.754 1.00 51.03  ? 135 THR C CG2 1 
ATOM   3205  N  N   . LYS C  1 142 ? 103.418 124.792 49.917 1.00 54.44  ? 136 LYS C N   1 
ATOM   3206  C  CA  . LYS C  1 142 ? 103.195 123.358 50.058 1.00 55.88  ? 136 LYS C CA  1 
ATOM   3207  C  C   . LYS C  1 142 ? 102.047 123.008 51.009 1.00 53.79  ? 136 LYS C C   1 
ATOM   3208  O  O   . LYS C  1 142 ? 101.128 122.266 50.661 1.00 52.11  ? 136 LYS C O   1 
ATOM   3209  C  CB  . LYS C  1 142 ? 104.461 122.681 50.570 1.00 55.03  ? 136 LYS C CB  1 
ATOM   3210  C  CG  . LYS C  1 142 ? 105.669 122.798 49.675 1.00 62.86  ? 136 LYS C CG  1 
ATOM   3211  C  CD  . LYS C  1 142 ? 106.821 122.027 50.299 1.00 70.76  ? 136 LYS C CD  1 
ATOM   3212  C  CE  . LYS C  1 142 ? 108.062 122.053 49.434 1.00 82.21  ? 136 LYS C CE  1 
ATOM   3213  N  NZ  . LYS C  1 142 ? 109.195 121.352 50.103 1.00 89.23  ? 136 LYS C NZ  1 
ATOM   3214  N  N   . THR C  1 143 ? 102.108 123.563 52.212 1.00 49.51  ? 137 THR C N   1 
ATOM   3215  C  CA  . THR C  1 143 ? 101.124 123.276 53.234 1.00 43.82  ? 137 THR C CA  1 
ATOM   3216  C  C   . THR C  1 143 ? 100.413 124.503 53.766 1.00 48.27  ? 137 THR C C   1 
ATOM   3217  O  O   . THR C  1 143 ? 99.620  124.393 54.713 1.00 45.89  ? 137 THR C O   1 
ATOM   3218  C  CB  . THR C  1 143 ? 101.794 122.623 54.423 1.00 44.79  ? 137 THR C CB  1 
ATOM   3219  O  OG1 . THR C  1 143 ? 102.524 123.622 55.147 1.00 43.22  ? 137 THR C OG1 1 
ATOM   3220  C  CG2 . THR C  1 143 ? 102.769 121.553 53.953 1.00 32.21  ? 137 THR C CG2 1 
ATOM   3221  N  N   . GLY C  1 144 ? 100.705 125.666 53.186 1.00 45.13  ? 138 GLY C N   1 
ATOM   3222  C  CA  . GLY C  1 144 ? 100.081 126.894 53.651 1.00 38.07  ? 138 GLY C CA  1 
ATOM   3223  C  C   . GLY C  1 144 ? 100.376 127.198 55.116 1.00 36.58  ? 138 GLY C C   1 
ATOM   3224  O  O   . GLY C  1 144 ? 99.659  127.983 55.739 1.00 32.39  ? 138 GLY C O   1 
ATOM   3225  N  N   . ASN C  1 145 ? 101.431 126.585 55.660 1.00 34.64  ? 139 ASN C N   1 
ATOM   3226  C  CA  . ASN C  1 145 ? 101.820 126.770 57.064 1.00 40.09  ? 139 ASN C CA  1 
ATOM   3227  C  C   . ASN C  1 145 ? 100.710 126.459 58.057 1.00 40.48  ? 139 ASN C C   1 
ATOM   3228  O  O   . ASN C  1 145 ? 100.655 127.088 59.114 1.00 38.47  ? 139 ASN C O   1 
ATOM   3229  C  CB  . ASN C  1 145 ? 102.291 128.210 57.309 1.00 42.95  ? 139 ASN C CB  1 
ATOM   3230  C  CG  . ASN C  1 145 ? 103.619 128.507 56.648 1.00 44.98  ? 139 ASN C CG  1 
ATOM   3231  O  OD1 . ASN C  1 145 ? 104.643 127.931 57.014 1.00 57.75  ? 139 ASN C OD1 1 
ATOM   3232  N  ND2 . ASN C  1 145 ? 103.610 129.400 55.660 1.00 44.64  ? 139 ASN C ND2 1 
ATOM   3233  N  N   . ALA C  1 146 ? 99.845  125.494 57.730 1.00 38.54  ? 140 ALA C N   1 
ATOM   3234  C  CA  . ALA C  1 146 ? 98.710  125.112 58.589 1.00 41.14  ? 140 ALA C CA  1 
ATOM   3235  C  C   . ALA C  1 146 ? 99.089  124.273 59.826 1.00 41.65  ? 140 ALA C C   1 
ATOM   3236  O  O   . ALA C  1 146 ? 98.249  123.993 60.694 1.00 36.55  ? 140 ALA C O   1 
ATOM   3237  C  CB  . ALA C  1 146 ? 97.644  124.366 57.756 1.00 41.42  ? 140 ALA C CB  1 
ATOM   3238  N  N   . GLY C  1 147 ? 100.345 123.853 59.897 1.00 35.86  ? 141 GLY C N   1 
ATOM   3239  C  CA  . GLY C  1 147 ? 100.777 123.100 61.050 1.00 40.73  ? 141 GLY C CA  1 
ATOM   3240  C  C   . GLY C  1 147 ? 100.404 121.632 61.098 1.00 47.53  ? 141 GLY C C   1 
ATOM   3241  O  O   . GLY C  1 147 ? 100.093 121.002 60.073 1.00 44.45  ? 141 GLY C O   1 
ATOM   3242  N  N   . SER C  1 148 ? 100.432 121.098 62.317 1.00 39.11  ? 142 SER C N   1 
ATOM   3243  C  CA  . SER C  1 148 ? 100.153 119.696 62.562 1.00 37.80  ? 142 SER C CA  1 
ATOM   3244  C  C   . SER C  1 148 ? 98.733  119.257 62.230 1.00 34.15  ? 142 SER C C   1 
ATOM   3245  O  O   . SER C  1 148 ? 97.823  120.076 62.038 1.00 23.37  ? 142 SER C O   1 
ATOM   3246  C  CB  . SER C  1 148 ? 100.499 119.331 64.021 1.00 33.60  ? 142 SER C CB  1 
ATOM   3247  O  OG  . SER C  1 148 ? 99.695  120.032 64.946 1.00 45.76  ? 142 SER C OG  1 
ATOM   3248  N  N   . ARG C  1 149 ? 98.573  117.938 62.160 1.00 29.49  ? 143 ARG C N   1 
ATOM   3249  C  CA  . ARG C  1 149 ? 97.305  117.311 61.835 1.00 28.33  ? 143 ARG C CA  1 
ATOM   3250  C  C   . ARG C  1 149 ? 96.587  116.972 63.131 1.00 23.29  ? 143 ARG C C   1 
ATOM   3251  O  O   . ARG C  1 149 ? 96.971  116.046 63.826 1.00 26.08  ? 143 ARG C O   1 
ATOM   3252  C  CB  . ARG C  1 149 ? 97.604  116.065 61.010 1.00 27.94  ? 143 ARG C CB  1 
ATOM   3253  C  CG  . ARG C  1 149 ? 98.610  116.379 59.913 1.00 31.05  ? 143 ARG C CG  1 
ATOM   3254  C  CD  . ARG C  1 149 ? 98.991  115.209 59.038 1.00 29.90  ? 143 ARG C CD  1 
ATOM   3255  N  NE  . ARG C  1 149 ? 99.875  115.681 57.976 1.00 27.58  ? 143 ARG C NE  1 
ATOM   3256  C  CZ  . ARG C  1 149 ? 100.185 115.003 56.874 1.00 27.74  ? 143 ARG C CZ  1 
ATOM   3257  N  NH1 . ARG C  1 149 ? 101.004 115.543 55.981 1.00 15.89  ? 143 ARG C NH1 1 
ATOM   3258  N  NH2 . ARG C  1 149 ? 99.689  113.790 56.653 1.00 27.55  ? 143 ARG C NH2 1 
ATOM   3259  N  N   . LEU C  1 150 ? 95.552  117.733 63.466 1.00 24.80  ? 144 LEU C N   1 
ATOM   3260  C  CA  . LEU C  1 150 ? 94.830  117.494 64.716 1.00 29.03  ? 144 LEU C CA  1 
ATOM   3261  C  C   . LEU C  1 150 ? 93.917  116.292 64.668 1.00 30.73  ? 144 LEU C C   1 
ATOM   3262  O  O   . LEU C  1 150 ? 93.721  115.622 65.679 1.00 35.45  ? 144 LEU C O   1 
ATOM   3263  C  CB  . LEU C  1 150 ? 94.006  118.721 65.116 1.00 30.18  ? 144 LEU C CB  1 
ATOM   3264  C  CG  . LEU C  1 150 ? 94.750  120.052 65.291 1.00 34.66  ? 144 LEU C CG  1 
ATOM   3265  C  CD1 . LEU C  1 150 ? 93.821  121.108 65.887 1.00 31.29  ? 144 LEU C CD1 1 
ATOM   3266  C  CD2 . LEU C  1 150 ? 95.939  119.845 66.195 1.00 21.78  ? 144 LEU C CD2 1 
ATOM   3267  N  N   . ALA C  1 151 ? 93.352  116.033 63.493 1.00 31.35  ? 145 ALA C N   1 
ATOM   3268  C  CA  . ALA C  1 151 ? 92.437  114.916 63.306 1.00 27.33  ? 145 ALA C CA  1 
ATOM   3269  C  C   . ALA C  1 151 ? 92.236  114.619 61.824 1.00 31.22  ? 145 ALA C C   1 
ATOM   3270  O  O   . ALA C  1 151 ? 92.340  115.505 60.969 1.00 34.82  ? 145 ALA C O   1 
ATOM   3271  C  CB  . ALA C  1 151 ? 91.096  115.226 63.949 1.00 14.66  ? 145 ALA C CB  1 
ATOM   3272  N  N   . CYS C  1 152 ? 91.936  113.364 61.526 1.00 26.58  ? 146 CYS C N   1 
ATOM   3273  C  CA  . CYS C  1 152 ? 91.708  112.950 60.159 1.00 28.50  ? 146 CYS C CA  1 
ATOM   3274  C  C   . CYS C  1 152 ? 90.791  111.728 60.092 1.00 31.05  ? 146 CYS C C   1 
ATOM   3275  O  O   . CYS C  1 152 ? 90.401  111.156 61.121 1.00 28.66  ? 146 CYS C O   1 
ATOM   3276  C  CB  . CYS C  1 152 ? 93.036  112.642 59.483 1.00 21.23  ? 146 CYS C CB  1 
ATOM   3277  S  SG  . CYS C  1 152 ? 93.924  111.305 60.313 1.00 24.04  ? 146 CYS C SG  1 
ATOM   3278  N  N   . GLY C  1 153 ? 90.436  111.361 58.865 1.00 27.94  ? 147 GLY C N   1 
ATOM   3279  C  CA  . GLY C  1 153 ? 89.573  110.221 58.619 1.00 14.03  ? 147 GLY C CA  1 
ATOM   3280  C  C   . GLY C  1 153 ? 89.614  109.886 57.136 1.00 26.42  ? 147 GLY C C   1 
ATOM   3281  O  O   . GLY C  1 153 ? 89.835  110.765 56.275 1.00 27.12  ? 147 GLY C O   1 
ATOM   3282  N  N   . VAL C  1 154 ? 89.424  108.610 56.820 1.00 27.80  ? 148 VAL C N   1 
ATOM   3283  C  CA  . VAL C  1 154 ? 89.417  108.187 55.427 1.00 22.22  ? 148 VAL C CA  1 
ATOM   3284  C  C   . VAL C  1 154 ? 88.047  108.505 54.849 1.00 20.40  ? 148 VAL C C   1 
ATOM   3285  O  O   . VAL C  1 154 ? 87.026  108.204 55.464 1.00 17.76  ? 148 VAL C O   1 
ATOM   3286  C  CB  . VAL C  1 154 ? 89.715  106.701 55.310 1.00 24.89  ? 148 VAL C CB  1 
ATOM   3287  C  CG1 . VAL C  1 154 ? 89.662  106.273 53.848 1.00 25.70  ? 148 VAL C CG1 1 
ATOM   3288  C  CG2 . VAL C  1 154 ? 91.097  106.427 55.892 1.00 13.64  ? 148 VAL C CG2 1 
ATOM   3289  N  N   . ILE C  1 155 ? 88.024  109.155 53.686 1.00 20.81  ? 149 ILE C N   1 
ATOM   3290  C  CA  . ILE C  1 155 ? 86.753  109.515 53.069 1.00 26.43  ? 149 ILE C CA  1 
ATOM   3291  C  C   . ILE C  1 155 ? 86.106  108.286 52.446 1.00 25.83  ? 149 ILE C C   1 
ATOM   3292  O  O   . ILE C  1 155 ? 86.676  107.648 51.552 1.00 23.06  ? 149 ILE C O   1 
ATOM   3293  C  CB  . ILE C  1 155 ? 86.933  110.603 52.000 1.00 29.45  ? 149 ILE C CB  1 
ATOM   3294  C  CG1 . ILE C  1 155 ? 87.500  111.876 52.649 1.00 22.19  ? 149 ILE C CG1 1 
ATOM   3295  C  CG2 . ILE C  1 155 ? 85.585  110.908 51.353 1.00 26.18  ? 149 ILE C CG2 1 
ATOM   3296  C  CD1 . ILE C  1 155 ? 88.058  112.870 51.667 1.00 20.99  ? 149 ILE C CD1 1 
ATOM   3297  N  N   . GLY C  1 156 ? 84.917  107.954 52.938 1.00 24.86  ? 150 GLY C N   1 
ATOM   3298  C  CA  . GLY C  1 156 ? 84.220  106.780 52.441 1.00 32.92  ? 150 GLY C CA  1 
ATOM   3299  C  C   . GLY C  1 156 ? 82.880  107.000 51.769 1.00 26.75  ? 150 GLY C C   1 
ATOM   3300  O  O   . GLY C  1 156 ? 82.202  108.005 52.007 1.00 25.37  ? 150 GLY C O   1 
ATOM   3301  N  N   . ILE C  1 157 ? 82.507  106.049 50.915 1.00 27.37  ? 151 ILE C N   1 
ATOM   3302  C  CA  . ILE C  1 157 ? 81.239  106.104 50.199 1.00 25.93  ? 151 ILE C CA  1 
ATOM   3303  C  C   . ILE C  1 157 ? 80.110  105.976 51.212 1.00 27.90  ? 151 ILE C C   1 
ATOM   3304  O  O   . ILE C  1 157 ? 80.199  105.186 52.153 1.00 25.84  ? 151 ILE C O   1 
ATOM   3305  C  CB  . ILE C  1 157 ? 81.132  104.958 49.167 1.00 32.71  ? 151 ILE C CB  1 
ATOM   3306  C  CG1 . ILE C  1 157 ? 82.242  105.094 48.123 1.00 39.60  ? 151 ILE C CG1 1 
ATOM   3307  C  CG2 . ILE C  1 157 ? 79.788  105.003 48.471 1.00 30.86  ? 151 ILE C CG2 1 
ATOM   3308  C  CD1 . ILE C  1 157 ? 82.356  103.908 47.183 1.00 49.17  ? 151 ILE C CD1 1 
ATOM   3309  N  N   . ALA C  1 158 ? 79.059  106.771 51.031 1.00 28.07  ? 152 ALA C N   1 
ATOM   3310  C  CA  . ALA C  1 158 ? 77.919  106.726 51.937 1.00 34.67  ? 152 ALA C CA  1 
ATOM   3311  C  C   . ALA C  1 158 ? 76.634  106.502 51.158 1.00 36.71  ? 152 ALA C C   1 
ATOM   3312  O  O   . ALA C  1 158 ? 76.576  106.742 49.957 1.00 32.84  ? 152 ALA C O   1 
ATOM   3313  C  CB  . ALA C  1 158 ? 77.829  108.011 52.734 1.00 21.50  ? 152 ALA C CB  1 
ATOM   3314  N  N   . GLN C  1 159 ? 75.609  106.034 51.858 1.00 42.32  ? 153 GLN C N   1 
ATOM   3315  C  CA  . GLN C  1 159 ? 74.313  105.754 51.252 1.00 48.63  ? 153 GLN C CA  1 
ATOM   3316  C  C   . GLN C  1 159 ? 73.551  107.046 50.967 1.00 52.88  ? 153 GLN C C   1 
ATOM   3317  O  O   . GLN C  1 159 ? 73.571  107.938 51.848 1.00 54.73  ? 153 GLN C O   1 
ATOM   3318  C  CB  . GLN C  1 159 ? 73.499  104.879 52.202 1.00 44.97  ? 153 GLN C CB  1 
ATOM   3319  C  CG  . GLN C  1 159 ? 72.206  104.345 51.638 1.00 52.96  ? 153 GLN C CG  1 
ATOM   3320  C  CD  . GLN C  1 159 ? 71.423  103.551 52.674 1.00 60.74  ? 153 GLN C CD  1 
ATOM   3321  O  OE1 . GLN C  1 159 ? 70.561  102.742 52.332 1.00 64.99  ? 153 GLN C OE1 1 
ATOM   3322  N  NE2 . GLN C  1 159 ? 71.715  103.789 53.951 1.00 57.64  ? 153 GLN C NE2 1 
ATOM   3323  O  OXT . GLN C  1 159 ? 72.933  107.144 49.882 1.00 53.84  ? 153 GLN C OXT 1 
ATOM   3324  N  N   . ALA D  1 7   ? 94.956  102.589 40.910 1.00 60.41  ? 1   ALA D N   1 
ATOM   3325  C  CA  . ALA D  1 7   ? 95.488  102.238 42.266 1.00 58.77  ? 1   ALA D CA  1 
ATOM   3326  C  C   . ALA D  1 7   ? 95.932  100.783 42.319 1.00 52.06  ? 1   ALA D C   1 
ATOM   3327  O  O   . ALA D  1 7   ? 95.192  99.881  41.945 1.00 54.29  ? 1   ALA D O   1 
ATOM   3328  C  CB  . ALA D  1 7   ? 94.432  102.494 43.333 1.00 53.84  ? 1   ALA D CB  1 
ATOM   3329  N  N   . THR D  1 8   ? 97.149  100.563 42.784 1.00 48.40  ? 2   THR D N   1 
ATOM   3330  C  CA  . THR D  1 8   ? 97.682  99.217  42.883 1.00 44.52  ? 2   THR D CA  1 
ATOM   3331  C  C   . THR D  1 8   ? 97.806  98.795  44.342 1.00 42.68  ? 2   THR D C   1 
ATOM   3332  O  O   . THR D  1 8   ? 98.069  97.623  44.625 1.00 38.39  ? 2   THR D O   1 
ATOM   3333  C  CB  . THR D  1 8   ? 99.071  99.133  42.248 1.00 44.13  ? 2   THR D CB  1 
ATOM   3334  O  OG1 . THR D  1 8   ? 99.925  100.107 42.863 1.00 43.24  ? 2   THR D OG1 1 
ATOM   3335  C  CG2 . THR D  1 8   ? 98.992  99.388  40.754 1.00 42.70  ? 2   THR D CG2 1 
ATOM   3336  N  N   . LYS D  1 9   ? 97.635  99.748  45.261 1.00 37.90  ? 3   LYS D N   1 
ATOM   3337  C  CA  . LYS D  1 9   ? 97.742  99.456  46.688 1.00 40.07  ? 3   LYS D CA  1 
ATOM   3338  C  C   . LYS D  1 9   ? 96.712  100.165 47.539 1.00 35.40  ? 3   LYS D C   1 
ATOM   3339  O  O   . LYS D  1 9   ? 96.377  101.321 47.306 1.00 35.05  ? 3   LYS D O   1 
ATOM   3340  C  CB  . LYS D  1 9   ? 99.133  99.798  47.211 1.00 36.11  ? 3   LYS D CB  1 
ATOM   3341  C  CG  . LYS D  1 9   ? 100.209 98.918  46.652 1.00 38.17  ? 3   LYS D CG  1 
ATOM   3342  C  CD  . LYS D  1 9   ? 101.547 99.277  47.243 1.00 53.48  ? 3   LYS D CD  1 
ATOM   3343  C  CE  . LYS D  1 9   ? 102.662 98.480  46.580 1.00 65.98  ? 3   LYS D CE  1 
ATOM   3344  N  NZ  . LYS D  1 9   ? 104.000 98.876  47.108 1.00 77.36  ? 3   LYS D NZ  1 
ATOM   3345  N  N   . ALA D  1 10  ? 96.212  99.451  48.534 1.00 27.56  ? 4   ALA D N   1 
ATOM   3346  C  CA  . ALA D  1 10  ? 95.219  99.997  49.438 1.00 26.19  ? 4   ALA D CA  1 
ATOM   3347  C  C   . ALA D  1 10  ? 95.552  99.491  50.838 1.00 26.64  ? 4   ALA D C   1 
ATOM   3348  O  O   . ALA D  1 10  ? 96.399  98.613  51.008 1.00 19.32  ? 4   ALA D O   1 
ATOM   3349  C  CB  . ALA D  1 10  ? 93.811  99.551  49.017 1.00 21.56  ? 4   ALA D CB  1 
ATOM   3350  N  N   . VAL D  1 11  ? 94.890  100.046 51.845 1.00 24.01  ? 5   VAL D N   1 
ATOM   3351  C  CA  . VAL D  1 11  ? 95.169  99.635  53.200 1.00 18.88  ? 5   VAL D CA  1 
ATOM   3352  C  C   . VAL D  1 11  ? 93.990  99.938  54.089 1.00 23.61  ? 5   VAL D C   1 
ATOM   3353  O  O   . VAL D  1 11  ? 93.152  100.802 53.796 1.00 16.80  ? 5   VAL D O   1 
ATOM   3354  C  CB  . VAL D  1 11  ? 96.431  100.359 53.756 1.00 24.97  ? 5   VAL D CB  1 
ATOM   3355  C  CG1 . VAL D  1 11  ? 96.088  101.783 54.139 1.00 15.99  ? 5   VAL D CG1 1 
ATOM   3356  C  CG2 . VAL D  1 11  ? 96.995  99.602  54.946 1.00 22.43  ? 5   VAL D CG2 1 
ATOM   3357  N  N   . CYS D  1 12  ? 93.944  99.244  55.212 1.00 23.96  ? 6   CYS D N   1 
ATOM   3358  C  CA  . CYS D  1 12  ? 92.839  99.438  56.108 1.00 20.50  ? 6   CYS D CA  1 
ATOM   3359  C  C   . CYS D  1 12  ? 93.251  99.201  57.552 1.00 22.54  ? 6   CYS D C   1 
ATOM   3360  O  O   . CYS D  1 12  ? 93.915  98.209  57.871 1.00 20.74  ? 6   CYS D O   1 
ATOM   3361  C  CB  . CYS D  1 12  ? 91.729  98.469  55.712 1.00 21.81  ? 6   CYS D CB  1 
ATOM   3362  S  SG  . CYS D  1 12  ? 90.280  98.516  56.732 1.00 25.57  ? 6   CYS D SG  1 
ATOM   3363  N  N   . VAL D  1 13  ? 92.861  100.129 58.418 1.00 17.37  ? 7   VAL D N   1 
ATOM   3364  C  CA  . VAL D  1 13  ? 93.140  100.001 59.831 1.00 20.58  ? 7   VAL D CA  1 
ATOM   3365  C  C   . VAL D  1 13  ? 91.846  99.567  60.507 1.00 22.33  ? 7   VAL D C   1 
ATOM   3366  O  O   . VAL D  1 13  ? 90.847  100.281 60.470 1.00 22.90  ? 7   VAL D O   1 
ATOM   3367  C  CB  . VAL D  1 13  ? 93.573  101.326 60.426 1.00 20.05  ? 7   VAL D CB  1 
ATOM   3368  C  CG1 . VAL D  1 13  ? 93.858  101.130 61.910 1.00 9.63   ? 7   VAL D CG1 1 
ATOM   3369  C  CG2 . VAL D  1 13  ? 94.788  101.860 59.661 1.00 13.28  ? 7   VAL D CG2 1 
ATOM   3370  N  N   . LEU D  1 14  ? 91.858  98.395  61.120 1.00 20.56  ? 8   LEU D N   1 
ATOM   3371  C  CA  . LEU D  1 14  ? 90.656  97.898  61.779 1.00 23.96  ? 8   LEU D CA  1 
ATOM   3372  C  C   . LEU D  1 14  ? 90.657  98.224  63.265 1.00 28.26  ? 8   LEU D C   1 
ATOM   3373  O  O   . LEU D  1 14  ? 91.647  97.963  63.956 1.00 23.37  ? 8   LEU D O   1 
ATOM   3374  C  CB  . LEU D  1 14  ? 90.560  96.386  61.609 1.00 20.30  ? 8   LEU D CB  1 
ATOM   3375  C  CG  . LEU D  1 14  ? 90.416  95.858  60.183 1.00 24.88  ? 8   LEU D CG  1 
ATOM   3376  C  CD1 . LEU D  1 14  ? 90.627  94.360  60.155 1.00 36.64  ? 8   LEU D CD1 1 
ATOM   3377  C  CD2 . LEU D  1 14  ? 89.032  96.196  59.678 1.00 36.21  ? 8   LEU D CD2 1 
ATOM   3378  N  N   . LYS D  1 15  ? 89.541  98.779  63.742 1.00 26.11  ? 9   LYS D N   1 
ATOM   3379  C  CA  . LYS D  1 15  ? 89.358  99.130  65.149 1.00 28.80  ? 9   LYS D CA  1 
ATOM   3380  C  C   . LYS D  1 15  ? 87.904  98.897  65.471 1.00 28.18  ? 9   LYS D C   1 
ATOM   3381  O  O   . LYS D  1 15  ? 87.047  98.981  64.590 1.00 23.28  ? 9   LYS D O   1 
ATOM   3382  C  CB  . LYS D  1 15  ? 89.702  100.603 65.419 1.00 23.18  ? 9   LYS D CB  1 
ATOM   3383  C  CG  . LYS D  1 15  ? 91.156  100.936 65.133 1.00 37.65  ? 9   LYS D CG  1 
ATOM   3384  C  CD  . LYS D  1 15  ? 91.519  102.382 65.457 1.00 44.80  ? 9   LYS D CD  1 
ATOM   3385  C  CE  . LYS D  1 15  ? 93.033  102.579 65.358 1.00 52.94  ? 9   LYS D CE  1 
ATOM   3386  N  NZ  . LYS D  1 15  ? 93.485  103.992 65.513 1.00 55.75  ? 9   LYS D NZ  1 
ATOM   3387  N  N   . GLY D  1 16  ? 87.625  98.587  66.731 1.00 28.10  ? 10  GLY D N   1 
ATOM   3388  C  CA  . GLY D  1 16  ? 86.257  98.355  67.138 1.00 26.00  ? 10  GLY D CA  1 
ATOM   3389  C  C   . GLY D  1 16  ? 86.069  98.847  68.554 1.00 32.21  ? 10  GLY D C   1 
ATOM   3390  O  O   . GLY D  1 16  ? 86.883  99.615  69.056 1.00 23.45  ? 10  GLY D O   1 
ATOM   3391  N  N   . ASP D  1 17  ? 85.007  98.410  69.215 1.00 36.79  ? 11  ASP D N   1 
ATOM   3392  C  CA  . ASP D  1 17  ? 84.775  98.854  70.581 1.00 43.16  ? 11  ASP D CA  1 
ATOM   3393  C  C   . ASP D  1 17  ? 85.549  97.989  71.547 1.00 41.16  ? 11  ASP D C   1 
ATOM   3394  O  O   . ASP D  1 17  ? 85.872  98.414  72.648 1.00 43.59  ? 11  ASP D O   1 
ATOM   3395  C  CB  . ASP D  1 17  ? 83.286  98.793  70.902 1.00 52.05  ? 11  ASP D CB  1 
ATOM   3396  C  CG  . ASP D  1 17  ? 82.496  99.863  70.169 1.00 65.50  ? 11  ASP D CG  1 
ATOM   3397  O  OD1 . ASP D  1 17  ? 81.328  99.597  69.797 1.00 66.75  ? 11  ASP D OD1 1 
ATOM   3398  O  OD2 . ASP D  1 17  ? 83.046  100.974 69.977 1.00 62.77  ? 11  ASP D OD2 1 
ATOM   3399  N  N   . GLY D  1 18  ? 85.866  96.777  71.113 1.00 35.73  ? 12  GLY D N   1 
ATOM   3400  C  CA  . GLY D  1 18  ? 86.582  95.851  71.968 1.00 33.09  ? 12  GLY D CA  1 
ATOM   3401  C  C   . GLY D  1 18  ? 88.078  95.807  71.739 1.00 28.26  ? 12  GLY D C   1 
ATOM   3402  O  O   . GLY D  1 18  ? 88.670  96.772  71.285 1.00 27.41  ? 12  GLY D O   1 
ATOM   3403  N  N   . PRO D  1 19  ? 88.714  94.671  72.016 1.00 21.91  ? 13  PRO D N   1 
ATOM   3404  C  CA  . PRO D  1 19  ? 90.159  94.557  71.832 1.00 20.24  ? 13  PRO D CA  1 
ATOM   3405  C  C   . PRO D  1 19  ? 90.624  94.217  70.407 1.00 25.69  ? 13  PRO D C   1 
ATOM   3406  O  O   . PRO D  1 19  ? 91.823  94.163  70.152 1.00 22.95  ? 13  PRO D O   1 
ATOM   3407  C  CB  . PRO D  1 19  ? 90.522  93.467  72.825 1.00 14.29  ? 13  PRO D CB  1 
ATOM   3408  C  CG  . PRO D  1 19  ? 89.361  92.490  72.618 1.00 20.05  ? 13  PRO D CG  1 
ATOM   3409  C  CD  . PRO D  1 19  ? 88.135  93.407  72.511 1.00 19.57  ? 13  PRO D CD  1 
ATOM   3410  N  N   . VAL D  1 20  ? 89.695  93.989  69.480 1.00 25.73  ? 14  VAL D N   1 
ATOM   3411  C  CA  . VAL D  1 20  ? 90.097  93.640  68.125 1.00 20.12  ? 14  VAL D CA  1 
ATOM   3412  C  C   . VAL D  1 20  ? 90.700  94.817  67.373 1.00 23.78  ? 14  VAL D C   1 
ATOM   3413  O  O   . VAL D  1 20  ? 90.141  95.911  67.338 1.00 22.12  ? 14  VAL D O   1 
ATOM   3414  C  CB  . VAL D  1 20  ? 88.921  93.048  67.331 1.00 27.84  ? 14  VAL D CB  1 
ATOM   3415  C  CG1 . VAL D  1 20  ? 89.374  92.660  65.917 1.00 16.38  ? 14  VAL D CG1 1 
ATOM   3416  C  CG2 . VAL D  1 20  ? 88.392  91.822  68.061 1.00 17.04  ? 14  VAL D CG2 1 
ATOM   3417  N  N   . GLN D  1 21  ? 91.865  94.596  66.775 1.00 22.79  ? 15  GLN D N   1 
ATOM   3418  C  CA  . GLN D  1 21  ? 92.510  95.672  66.059 1.00 23.27  ? 15  GLN D CA  1 
ATOM   3419  C  C   . GLN D  1 21  ? 93.579  95.137  65.130 1.00 23.04  ? 15  GLN D C   1 
ATOM   3420  O  O   . GLN D  1 21  ? 94.279  94.178  65.455 1.00 21.18  ? 15  GLN D O   1 
ATOM   3421  C  CB  . GLN D  1 21  ? 93.091  96.650  67.079 1.00 29.58  ? 15  GLN D CB  1 
ATOM   3422  C  CG  . GLN D  1 21  ? 94.580  96.852  67.033 1.00 46.38  ? 15  GLN D CG  1 
ATOM   3423  C  CD  . GLN D  1 21  ? 95.063  97.718  68.189 1.00 57.82  ? 15  GLN D CD  1 
ATOM   3424  O  OE1 . GLN D  1 21  ? 96.240  98.066  68.269 1.00 69.46  ? 15  GLN D OE1 1 
ATOM   3425  N  NE2 . GLN D  1 21  ? 94.152  98.063  69.092 1.00 51.84  ? 15  GLN D NE2 1 
ATOM   3426  N  N   . GLY D  1 22  ? 93.699  95.732  63.952 1.00 19.30  ? 16  GLY D N   1 
ATOM   3427  C  CA  . GLY D  1 22  ? 94.717  95.236  63.045 1.00 14.89  ? 16  GLY D CA  1 
ATOM   3428  C  C   . GLY D  1 22  ? 94.909  96.095  61.822 1.00 17.52  ? 16  GLY D C   1 
ATOM   3429  O  O   . GLY D  1 22  ? 94.268  97.141  61.675 1.00 20.96  ? 16  GLY D O   1 
ATOM   3430  N  N   . ILE D  1 23  ? 95.785  95.639  60.935 1.00 17.55  ? 17  ILE D N   1 
ATOM   3431  C  CA  . ILE D  1 23  ? 96.077  96.350  59.707 1.00 19.24  ? 17  ILE D CA  1 
ATOM   3432  C  C   . ILE D  1 23  ? 96.082  95.367  58.550 1.00 23.94  ? 17  ILE D C   1 
ATOM   3433  O  O   . ILE D  1 23  ? 96.735  94.322  58.614 1.00 22.33  ? 17  ILE D O   1 
ATOM   3434  C  CB  . ILE D  1 23  ? 97.440  97.041  59.787 1.00 19.12  ? 17  ILE D CB  1 
ATOM   3435  C  CG1 . ILE D  1 23  ? 97.363  98.201  60.780 1.00 26.21  ? 17  ILE D CG1 1 
ATOM   3436  C  CG2 . ILE D  1 23  ? 97.867  97.511  58.401 1.00 24.98  ? 17  ILE D CG2 1 
ATOM   3437  C  CD1 . ILE D  1 23  ? 98.703  98.936  60.999 1.00 25.24  ? 17  ILE D CD1 1 
ATOM   3438  N  N   . ILE D  1 24  ? 95.350  95.701  57.494 1.00 16.83  ? 18  ILE D N   1 
ATOM   3439  C  CA  . ILE D  1 24  ? 95.276  94.834  56.326 1.00 16.91  ? 18  ILE D CA  1 
ATOM   3440  C  C   . ILE D  1 24  ? 95.714  95.598  55.074 1.00 19.06  ? 18  ILE D C   1 
ATOM   3441  O  O   . ILE D  1 24  ? 95.288  96.731  54.836 1.00 20.96  ? 18  ILE D O   1 
ATOM   3442  C  CB  . ILE D  1 24  ? 93.838  94.316  56.114 1.00 20.02  ? 18  ILE D CB  1 
ATOM   3443  C  CG1 . ILE D  1 24  ? 93.390  93.531  57.345 1.00 21.79  ? 18  ILE D CG1 1 
ATOM   3444  C  CG2 . ILE D  1 24  ? 93.764  93.439  54.854 1.00 11.13  ? 18  ILE D CG2 1 
ATOM   3445  C  CD1 . ILE D  1 24  ? 94.218  92.279  57.597 1.00 26.86  ? 18  ILE D CD1 1 
ATOM   3446  N  N   . ASN D  1 25  ? 96.561  94.962  54.277 1.00 17.98  ? 19  ASN D N   1 
ATOM   3447  C  CA  . ASN D  1 25  ? 97.073  95.552  53.045 1.00 24.24  ? 19  ASN D CA  1 
ATOM   3448  C  C   . ASN D  1 25  ? 96.449  94.902  51.810 1.00 24.41  ? 19  ASN D C   1 
ATOM   3449  O  O   . ASN D  1 25  ? 96.155  93.707  51.812 1.00 27.69  ? 19  ASN D O   1 
ATOM   3450  C  CB  . ASN D  1 25  ? 98.593  95.384  53.003 1.00 23.39  ? 19  ASN D CB  1 
ATOM   3451  C  CG  . ASN D  1 25  ? 99.282  96.022  54.208 1.00 30.45  ? 19  ASN D CG  1 
ATOM   3452  O  OD1 . ASN D  1 25  ? 99.439  97.237  54.269 1.00 32.76  ? 19  ASN D OD1 1 
ATOM   3453  N  ND2 . ASN D  1 25  ? 99.669  95.205  55.177 1.00 16.10  ? 19  ASN D ND2 1 
ATOM   3454  N  N   . PHE D  1 26  ? 96.250  95.700  50.765 1.00 23.42  ? 20  PHE D N   1 
ATOM   3455  C  CA  . PHE D  1 26  ? 95.685  95.224  49.508 1.00 23.09  ? 20  PHE D CA  1 
ATOM   3456  C  C   . PHE D  1 26  ? 96.645  95.589  48.390 1.00 27.98  ? 20  PHE D C   1 
ATOM   3457  O  O   . PHE D  1 26  ? 97.138  96.716  48.329 1.00 25.68  ? 20  PHE D O   1 
ATOM   3458  C  CB  . PHE D  1 26  ? 94.366  95.914  49.197 1.00 20.74  ? 20  PHE D CB  1 
ATOM   3459  C  CG  . PHE D  1 26  ? 93.284  95.595  50.141 1.00 27.16  ? 20  PHE D CG  1 
ATOM   3460  C  CD1 . PHE D  1 26  ? 92.494  94.469  49.952 1.00 32.38  ? 20  PHE D CD1 1 
ATOM   3461  C  CD2 . PHE D  1 26  ? 93.029  96.428  51.224 1.00 25.97  ? 20  PHE D CD2 1 
ATOM   3462  C  CE1 . PHE D  1 26  ? 91.459  94.172  50.826 1.00 26.95  ? 20  PHE D CE1 1 
ATOM   3463  C  CE2 . PHE D  1 26  ? 91.998  96.142  52.104 1.00 21.03  ? 20  PHE D CE2 1 
ATOM   3464  C  CZ  . PHE D  1 26  ? 91.211  95.013  51.903 1.00 24.27  ? 20  PHE D CZ  1 
ATOM   3465  N  N   . GLU D  1 27  ? 96.881  94.652  47.486 1.00 27.30  ? 21  GLU D N   1 
ATOM   3466  C  CA  . GLU D  1 27  ? 97.758  94.920  46.374 1.00 25.15  ? 21  GLU D CA  1 
ATOM   3467  C  C   . GLU D  1 27  ? 97.248  94.271  45.112 1.00 26.73  ? 21  GLU D C   1 
ATOM   3468  O  O   . GLU D  1 27  ? 96.955  93.077  45.092 1.00 21.25  ? 21  GLU D O   1 
ATOM   3469  C  CB  . GLU D  1 27  ? 99.157  94.409  46.659 1.00 36.23  ? 21  GLU D CB  1 
ATOM   3470  C  CG  . GLU D  1 27  ? 100.186 94.896  45.672 1.00 48.61  ? 21  GLU D CG  1 
ATOM   3471  C  CD  . GLU D  1 27  ? 101.537 94.273  45.925 1.00 63.41  ? 21  GLU D CD  1 
ATOM   3472  O  OE1 . GLU D  1 27  ? 102.535 94.760  45.347 1.00 70.58  ? 21  GLU D OE1 1 
ATOM   3473  O  OE2 . GLU D  1 27  ? 101.592 93.288  46.700 1.00 59.62  ? 21  GLU D OE2 1 
ATOM   3474  N  N   . GLN D  1 28  ? 97.155  95.076  44.061 1.00 24.21  ? 22  GLN D N   1 
ATOM   3475  C  CA  . GLN D  1 28  ? 96.708  94.619  42.760 1.00 31.89  ? 22  GLN D CA  1 
ATOM   3476  C  C   . GLN D  1 28  ? 97.664  95.130  41.647 1.00 36.38  ? 22  GLN D C   1 
ATOM   3477  O  O   . GLN D  1 28  ? 97.560  96.265  41.156 1.00 25.22  ? 22  GLN D O   1 
ATOM   3478  C  CB  . GLN D  1 28  ? 95.263  95.088  42.531 1.00 29.28  ? 22  GLN D CB  1 
ATOM   3479  C  CG  . GLN D  1 28  ? 94.678  94.679  41.186 1.00 21.56  ? 22  GLN D CG  1 
ATOM   3480  C  CD  . GLN D  1 28  ? 93.185  94.928  41.102 1.00 29.14  ? 22  GLN D CD  1 
ATOM   3481  O  OE1 . GLN D  1 28  ? 92.691  95.973  41.537 1.00 27.72  ? 22  GLN D OE1 1 
ATOM   3482  N  NE2 . GLN D  1 28  ? 92.454  93.972  40.529 1.00 22.31  ? 22  GLN D NE2 1 
ATOM   3483  N  N   . LYS D  1 29  ? 98.607  94.278  41.266 1.00 40.10  ? 23  LYS D N   1 
ATOM   3484  C  CA  . LYS D  1 29  ? 99.574  94.620  40.230 1.00 54.73  ? 23  LYS D CA  1 
ATOM   3485  C  C   . LYS D  1 29  ? 98.941  94.935  38.864 1.00 58.57  ? 23  LYS D C   1 
ATOM   3486  O  O   . LYS D  1 29  ? 99.452  95.764  38.119 1.00 63.95  ? 23  LYS D O   1 
ATOM   3487  C  CB  . LYS D  1 29  ? 100.595 93.487  40.093 1.00 57.11  ? 23  LYS D CB  1 
ATOM   3488  C  CG  . LYS D  1 29  ? 101.446 93.312  41.344 1.00 71.08  ? 23  LYS D CG  1 
ATOM   3489  C  CD  . LYS D  1 29  ? 102.310 92.064  41.294 1.00 73.56  ? 23  LYS D CD  1 
ATOM   3490  C  CE  . LYS D  1 29  ? 103.116 91.920  42.582 1.00 80.71  ? 23  LYS D CE  1 
ATOM   3491  N  NZ  . LYS D  1 29  ? 103.856 90.628  42.652 1.00 80.99  ? 23  LYS D NZ  1 
ATOM   3492  N  N   . GLU D  1 30  ? 97.829  94.285  38.540 1.00 61.03  ? 24  GLU D N   1 
ATOM   3493  C  CA  . GLU D  1 30  ? 97.149  94.512  37.267 1.00 60.21  ? 24  GLU D CA  1 
ATOM   3494  C  C   . GLU D  1 30  ? 95.658  94.672  37.472 1.00 59.58  ? 24  GLU D C   1 
ATOM   3495  O  O   . GLU D  1 30  ? 95.038  93.883  38.182 1.00 59.08  ? 24  GLU D O   1 
ATOM   3496  C  CB  . GLU D  1 30  ? 97.412  93.351  36.323 1.00 62.15  ? 24  GLU D CB  1 
ATOM   3497  C  CG  . GLU D  1 30  ? 98.818  93.341  35.795 1.00 77.12  ? 24  GLU D CG  1 
ATOM   3498  C  CD  . GLU D  1 30  ? 99.289  91.951  35.457 1.00 87.28  ? 24  GLU D CD  1 
ATOM   3499  O  OE1 . GLU D  1 30  ? 100.383 91.828  34.864 1.00 93.11  ? 24  GLU D OE1 1 
ATOM   3500  O  OE2 . GLU D  1 30  ? 98.570  90.984  35.794 1.00 90.30  ? 24  GLU D OE2 1 
ATOM   3501  N  N   . SER D  1 31  ? 95.089  95.688  36.834 1.00 58.52  ? 25  SER D N   1 
ATOM   3502  C  CA  . SER D  1 31  ? 93.666  95.982  36.957 1.00 62.22  ? 25  SER D CA  1 
ATOM   3503  C  C   . SER D  1 31  ? 92.728  94.777  36.811 1.00 63.27  ? 25  SER D C   1 
ATOM   3504  O  O   . SER D  1 31  ? 91.721  94.687  37.510 1.00 64.68  ? 25  SER D O   1 
ATOM   3505  C  CB  . SER D  1 31  ? 93.275  97.071  35.954 1.00 62.37  ? 25  SER D CB  1 
ATOM   3506  O  OG  . SER D  1 31  ? 93.576  96.679  34.626 1.00 69.65  ? 25  SER D OG  1 
ATOM   3507  N  N   . ASN D  1 32  ? 93.049  93.848  35.918 1.00 61.41  ? 26  ASN D N   1 
ATOM   3508  C  CA  . ASN D  1 32  ? 92.189  92.685  35.724 1.00 63.21  ? 26  ASN D CA  1 
ATOM   3509  C  C   . ASN D  1 32  ? 92.722  91.487  36.480 1.00 59.63  ? 26  ASN D C   1 
ATOM   3510  O  O   . ASN D  1 32  ? 92.353  90.352  36.182 1.00 62.00  ? 26  ASN D O   1 
ATOM   3511  C  CB  . ASN D  1 32  ? 92.118  92.311  34.245 1.00 75.53  ? 26  ASN D CB  1 
ATOM   3512  C  CG  . ASN D  1 32  ? 92.655  93.397  33.344 1.00 89.52  ? 26  ASN D CG  1 
ATOM   3513  O  OD1 . ASN D  1 32  ? 92.039  94.453  33.187 1.00 93.26  ? 26  ASN D OD1 1 
ATOM   3514  N  ND2 . ASN D  1 32  ? 93.818  93.147  32.747 1.00 94.40  ? 26  ASN D ND2 1 
ATOM   3515  N  N   . GLY D  1 33  ? 93.593  91.727  37.450 1.00 50.58  ? 27  GLY D N   1 
ATOM   3516  C  CA  . GLY D  1 33  ? 94.165  90.616  38.181 1.00 44.17  ? 27  GLY D CA  1 
ATOM   3517  C  C   . GLY D  1 33  ? 93.723  90.467  39.619 1.00 35.15  ? 27  GLY D C   1 
ATOM   3518  O  O   . GLY D  1 33  ? 92.970  91.293  40.147 1.00 28.68  ? 27  GLY D O   1 
ATOM   3519  N  N   . PRO D  1 34  ? 94.186  89.402  40.285 1.00 32.07  ? 28  PRO D N   1 
ATOM   3520  C  CA  . PRO D  1 34  ? 93.828  89.158  41.678 1.00 32.61  ? 28  PRO D CA  1 
ATOM   3521  C  C   . PRO D  1 34  ? 94.367  90.237  42.607 1.00 33.40  ? 28  PRO D C   1 
ATOM   3522  O  O   . PRO D  1 34  ? 95.361  90.904  42.313 1.00 34.98  ? 28  PRO D O   1 
ATOM   3523  C  CB  . PRO D  1 34  ? 94.440  87.789  41.956 1.00 28.93  ? 28  PRO D CB  1 
ATOM   3524  C  CG  . PRO D  1 34  ? 95.633  87.768  41.077 1.00 22.08  ? 28  PRO D CG  1 
ATOM   3525  C  CD  . PRO D  1 34  ? 95.112  88.365  39.798 1.00 33.47  ? 28  PRO D CD  1 
ATOM   3526  N  N   . VAL D  1 35  ? 93.670  90.422  43.716 1.00 32.24  ? 29  VAL D N   1 
ATOM   3527  C  CA  . VAL D  1 35  ? 94.063  91.384  44.724 1.00 29.48  ? 29  VAL D CA  1 
ATOM   3528  C  C   . VAL D  1 35  ? 94.659  90.540  45.851 1.00 28.67  ? 29  VAL D C   1 
ATOM   3529  O  O   . VAL D  1 35  ? 94.059  89.549  46.275 1.00 22.01  ? 29  VAL D O   1 
ATOM   3530  C  CB  . VAL D  1 35  ? 92.838  92.160  45.263 1.00 28.90  ? 29  VAL D CB  1 
ATOM   3531  C  CG1 . VAL D  1 35  ? 93.272  93.102  46.359 1.00 25.20  ? 29  VAL D CG1 1 
ATOM   3532  C  CG2 . VAL D  1 35  ? 92.156  92.933  44.135 1.00 22.38  ? 29  VAL D CG2 1 
ATOM   3533  N  N   . LYS D  1 36  ? 95.855  90.892  46.299 1.00 23.63  ? 30  LYS D N   1 
ATOM   3534  C  CA  . LYS D  1 36  ? 96.466  90.163  47.406 1.00 32.11  ? 30  LYS D CA  1 
ATOM   3535  C  C   . LYS D  1 36  ? 95.972  90.897  48.658 1.00 32.21  ? 30  LYS D C   1 
ATOM   3536  O  O   . LYS D  1 36  ? 95.969  92.141  48.699 1.00 22.93  ? 30  LYS D O   1 
ATOM   3537  C  CB  . LYS D  1 36  ? 97.997  90.213  47.315 1.00 33.09  ? 30  LYS D CB  1 
ATOM   3538  C  CG  . LYS D  1 36  ? 98.734  89.325  48.325 1.00 58.80  ? 30  LYS D CG  1 
ATOM   3539  C  CD  . LYS D  1 36  ? 100.264 89.509  48.231 1.00 65.59  ? 30  LYS D CD  1 
ATOM   3540  C  CE  . LYS D  1 36  ? 101.023 88.878  49.412 1.00 64.02  ? 30  LYS D CE  1 
ATOM   3541  N  NZ  . LYS D  1 36  ? 102.392 89.482  49.564 1.00 57.13  ? 30  LYS D NZ  1 
ATOM   3542  N  N   . VAL D  1 37  ? 95.500  90.137  49.645 1.00 28.12  ? 31  VAL D N   1 
ATOM   3543  C  CA  . VAL D  1 37  ? 95.003  90.717  50.889 1.00 24.71  ? 31  VAL D CA  1 
ATOM   3544  C  C   . VAL D  1 37  ? 95.774  90.075  52.044 1.00 29.75  ? 31  VAL D C   1 
ATOM   3545  O  O   . VAL D  1 37  ? 95.659  88.874  52.286 1.00 34.08  ? 31  VAL D O   1 
ATOM   3546  C  CB  . VAL D  1 37  ? 93.483  90.465  51.048 1.00 24.58  ? 31  VAL D CB  1 
ATOM   3547  C  CG1 . VAL D  1 37  ? 92.937  91.198  52.265 1.00 17.69  ? 31  VAL D CG1 1 
ATOM   3548  C  CG2 . VAL D  1 37  ? 92.757  90.965  49.819 1.00 26.78  ? 31  VAL D CG2 1 
ATOM   3549  N  N   . TRP D  1 38  ? 96.574  90.870  52.748 1.00 27.69  ? 32  TRP D N   1 
ATOM   3550  C  CA  . TRP D  1 38  ? 97.360  90.330  53.846 1.00 21.98  ? 32  TRP D CA  1 
ATOM   3551  C  C   . TRP D  1 38  ? 97.590  91.346  54.948 1.00 23.95  ? 32  TRP D C   1 
ATOM   3552  O  O   . TRP D  1 38  ? 97.609  92.562  54.713 1.00 16.57  ? 32  TRP D O   1 
ATOM   3553  C  CB  . TRP D  1 38  ? 98.709  89.841  53.329 1.00 18.89  ? 32  TRP D CB  1 
ATOM   3554  C  CG  . TRP D  1 38  ? 99.711  90.935  53.150 1.00 25.95  ? 32  TRP D CG  1 
ATOM   3555  C  CD1 . TRP D  1 38  ? 100.736 91.266  54.000 1.00 26.75  ? 32  TRP D CD1 1 
ATOM   3556  C  CD2 . TRP D  1 38  ? 99.792  91.845  52.053 1.00 23.66  ? 32  TRP D CD2 1 
ATOM   3557  N  NE1 . TRP D  1 38  ? 101.455 92.329  53.492 1.00 30.38  ? 32  TRP D NE1 1 
ATOM   3558  C  CE2 . TRP D  1 38  ? 100.898 92.701  52.296 1.00 33.53  ? 32  TRP D CE2 1 
ATOM   3559  C  CE3 . TRP D  1 38  ? 99.042  92.023  50.886 1.00 30.14  ? 32  TRP D CE3 1 
ATOM   3560  C  CZ2 . TRP D  1 38  ? 101.270 93.721  51.407 1.00 36.35  ? 32  TRP D CZ2 1 
ATOM   3561  C  CZ3 . TRP D  1 38  ? 99.414  93.045  49.994 1.00 38.44  ? 32  TRP D CZ3 1 
ATOM   3562  C  CH2 . TRP D  1 38  ? 100.519 93.878  50.264 1.00 34.94  ? 32  TRP D CH2 1 
ATOM   3563  N  N   . GLY D  1 39  ? 97.793  90.840  56.154 1.00 18.14  ? 33  GLY D N   1 
ATOM   3564  C  CA  . GLY D  1 39  ? 98.012  91.733  57.269 1.00 17.02  ? 33  GLY D CA  1 
ATOM   3565  C  C   . GLY D  1 39  ? 97.892  90.957  58.558 1.00 22.49  ? 33  GLY D C   1 
ATOM   3566  O  O   . GLY D  1 39  ? 97.991  89.743  58.557 1.00 24.29  ? 33  GLY D O   1 
ATOM   3567  N  N   . SER D  1 40  ? 97.637  91.650  59.657 1.00 23.31  ? 34  SER D N   1 
ATOM   3568  C  CA  . SER D  1 40  ? 97.554  90.991  60.948 1.00 25.93  ? 34  SER D CA  1 
ATOM   3569  C  C   . SER D  1 40  ? 96.411  91.599  61.743 1.00 24.27  ? 34  SER D C   1 
ATOM   3570  O  O   . SER D  1 40  ? 96.187  92.810  61.693 1.00 29.74  ? 34  SER D O   1 
ATOM   3571  C  CB  . SER D  1 40  ? 98.889  91.186  61.693 1.00 13.97  ? 34  SER D CB  1 
ATOM   3572  O  OG  . SER D  1 40  ? 98.993  90.306  62.784 1.00 39.31  ? 34  SER D OG  1 
ATOM   3573  N  N   . ILE D  1 41  ? 95.679  90.755  62.456 1.00 23.10  ? 35  ILE D N   1 
ATOM   3574  C  CA  . ILE D  1 41  ? 94.563  91.215  63.279 1.00 22.85  ? 35  ILE D CA  1 
ATOM   3575  C  C   . ILE D  1 41  ? 94.689  90.546  64.636 1.00 24.64  ? 35  ILE D C   1 
ATOM   3576  O  O   . ILE D  1 41  ? 94.817  89.316  64.716 1.00 24.71  ? 35  ILE D O   1 
ATOM   3577  C  CB  . ILE D  1 41  ? 93.218  90.811  62.696 1.00 21.81  ? 35  ILE D CB  1 
ATOM   3578  C  CG1 . ILE D  1 41  ? 93.094  91.303  61.255 1.00 19.46  ? 35  ILE D CG1 1 
ATOM   3579  C  CG2 . ILE D  1 41  ? 92.114  91.407  63.539 1.00 11.61  ? 35  ILE D CG2 1 
ATOM   3580  C  CD1 . ILE D  1 41  ? 91.780  90.864  60.617 1.00 18.35  ? 35  ILE D CD1 1 
ATOM   3581  N  N   . LYS D  1 42  ? 94.655  91.327  65.710 1.00 16.55  ? 36  LYS D N   1 
ATOM   3582  C  CA  . LYS D  1 42  ? 94.805  90.709  67.019 1.00 24.51  ? 36  LYS D CA  1 
ATOM   3583  C  C   . LYS D  1 42  ? 93.576  90.866  67.885 1.00 20.88  ? 36  LYS D C   1 
ATOM   3584  O  O   . LYS D  1 42  ? 92.615  91.546  67.508 1.00 26.72  ? 36  LYS D O   1 
ATOM   3585  C  CB  . LYS D  1 42  ? 96.043  91.267  67.732 1.00 22.00  ? 36  LYS D CB  1 
ATOM   3586  C  CG  . LYS D  1 42  ? 95.951  92.724  68.139 1.00 38.17  ? 36  LYS D CG  1 
ATOM   3587  C  CD  . LYS D  1 42  ? 97.166  93.097  68.962 1.00 56.54  ? 36  LYS D CD  1 
ATOM   3588  C  CE  . LYS D  1 42  ? 97.210  94.578  69.293 1.00 64.52  ? 36  LYS D CE  1 
ATOM   3589  N  NZ  . LYS D  1 42  ? 98.504  94.936  69.956 1.00 70.47  ? 36  LYS D NZ  1 
ATOM   3590  N  N   . GLY D  1 43  ? 93.616  90.236  69.052 1.00 25.00  ? 37  GLY D N   1 
ATOM   3591  C  CA  . GLY D  1 43  ? 92.488  90.288  69.973 1.00 26.06  ? 37  GLY D CA  1 
ATOM   3592  C  C   . GLY D  1 43  ? 91.321  89.393  69.556 1.00 21.98  ? 37  GLY D C   1 
ATOM   3593  O  O   . GLY D  1 43  ? 90.209  89.593  70.026 1.00 16.66  ? 37  GLY D O   1 
ATOM   3594  N  N   . LEU D  1 44  ? 91.573  88.413  68.682 1.00 16.36  ? 38  LEU D N   1 
ATOM   3595  C  CA  . LEU D  1 44  ? 90.528  87.502  68.190 1.00 22.58  ? 38  LEU D CA  1 
ATOM   3596  C  C   . LEU D  1 44  ? 90.530  86.152  68.897 1.00 20.46  ? 38  LEU D C   1 
ATOM   3597  O  O   . LEU D  1 44  ? 91.594  85.585  69.166 1.00 29.60  ? 38  LEU D O   1 
ATOM   3598  C  CB  . LEU D  1 44  ? 90.690  87.268  66.670 1.00 17.70  ? 38  LEU D CB  1 
ATOM   3599  C  CG  . LEU D  1 44  ? 90.357  88.455  65.756 1.00 20.62  ? 38  LEU D CG  1 
ATOM   3600  C  CD1 . LEU D  1 44  ? 90.927  88.231  64.379 1.00 17.34  ? 38  LEU D CD1 1 
ATOM   3601  C  CD2 . LEU D  1 44  ? 88.849  88.645  65.686 1.00 11.36  ? 38  LEU D CD2 1 
ATOM   3602  N  N   . THR D  1 45  ? 89.347  85.633  69.211 1.00 19.37  ? 39  THR D N   1 
ATOM   3603  C  CA  . THR D  1 45  ? 89.284  84.324  69.856 1.00 25.35  ? 39  THR D CA  1 
ATOM   3604  C  C   . THR D  1 45  ? 89.789  83.339  68.813 1.00 26.13  ? 39  THR D C   1 
ATOM   3605  O  O   . THR D  1 45  ? 89.566  83.525  67.611 1.00 27.20  ? 39  THR D O   1 
ATOM   3606  C  CB  . THR D  1 45  ? 87.861  83.930  70.234 1.00 19.98  ? 39  THR D CB  1 
ATOM   3607  O  OG1 . THR D  1 45  ? 87.067  83.879  69.044 1.00 46.24  ? 39  THR D OG1 1 
ATOM   3608  C  CG2 . THR D  1 45  ? 87.258  84.953  71.172 1.00 23.77  ? 39  THR D CG2 1 
ATOM   3609  N  N   . GLU D  1 46  ? 90.483  82.307  69.270 1.00 26.85  ? 40  GLU D N   1 
ATOM   3610  C  CA  . GLU D  1 46  ? 91.025  81.302  68.377 1.00 26.63  ? 40  GLU D CA  1 
ATOM   3611  C  C   . GLU D  1 46  ? 89.908  80.713  67.507 1.00 22.52  ? 40  GLU D C   1 
ATOM   3612  O  O   . GLU D  1 46  ? 88.821  80.453  67.989 1.00 19.07  ? 40  GLU D O   1 
ATOM   3613  C  CB  . GLU D  1 46  ? 91.692  80.196  69.198 1.00 25.12  ? 40  GLU D CB  1 
ATOM   3614  C  CG  . GLU D  1 46  ? 92.272  79.077  68.340 1.00 35.95  ? 40  GLU D CG  1 
ATOM   3615  C  CD  . GLU D  1 46  ? 93.007  78.011  69.144 1.00 44.54  ? 40  GLU D CD  1 
ATOM   3616  O  OE1 . GLU D  1 46  ? 93.565  77.107  68.487 1.00 47.18  ? 40  GLU D OE1 1 
ATOM   3617  O  OE2 . GLU D  1 46  ? 93.032  78.069  70.407 1.00 41.91  ? 40  GLU D OE2 1 
ATOM   3618  N  N   . GLY D  1 47  ? 90.181  80.498  66.228 1.00 22.49  ? 41  GLY D N   1 
ATOM   3619  C  CA  . GLY D  1 47  ? 89.162  79.943  65.364 1.00 14.36  ? 41  GLY D CA  1 
ATOM   3620  C  C   . GLY D  1 47  ? 88.862  80.823  64.156 1.00 24.01  ? 41  GLY D C   1 
ATOM   3621  O  O   . GLY D  1 47  ? 89.572  81.804  63.894 1.00 21.39  ? 41  GLY D O   1 
ATOM   3622  N  N   . LEU D  1 48  ? 87.794  80.477  63.434 1.00 24.17  ? 42  LEU D N   1 
ATOM   3623  C  CA  . LEU D  1 48  ? 87.393  81.188  62.219 1.00 25.36  ? 42  LEU D CA  1 
ATOM   3624  C  C   . LEU D  1 48  ? 86.559  82.435  62.466 1.00 25.31  ? 42  LEU D C   1 
ATOM   3625  O  O   . LEU D  1 48  ? 85.694  82.448  63.338 1.00 25.70  ? 42  LEU D O   1 
ATOM   3626  C  CB  . LEU D  1 48  ? 86.603  80.247  61.310 1.00 22.97  ? 42  LEU D CB  1 
ATOM   3627  C  CG  . LEU D  1 48  ? 87.283  78.959  60.852 1.00 25.75  ? 42  LEU D CG  1 
ATOM   3628  C  CD1 . LEU D  1 48  ? 86.300  78.162  60.035 1.00 23.55  ? 42  LEU D CD1 1 
ATOM   3629  C  CD2 . LEU D  1 48  ? 88.514  79.262  60.027 1.00 27.02  ? 42  LEU D CD2 1 
ATOM   3630  N  N   . HIS D  1 49  ? 86.812  83.475  61.676 1.00 23.47  ? 43  HIS D N   1 
ATOM   3631  C  CA  . HIS D  1 49  ? 86.071  84.730  61.794 1.00 21.02  ? 43  HIS D CA  1 
ATOM   3632  C  C   . HIS D  1 49  ? 85.714  85.255  60.412 1.00 20.21  ? 43  HIS D C   1 
ATOM   3633  O  O   . HIS D  1 49  ? 86.596  85.363  59.538 1.00 16.67  ? 43  HIS D O   1 
ATOM   3634  C  CB  . HIS D  1 49  ? 86.915  85.787  62.525 1.00 20.36  ? 43  HIS D CB  1 
ATOM   3635  C  CG  . HIS D  1 49  ? 87.193  85.453  63.954 1.00 19.80  ? 43  HIS D CG  1 
ATOM   3636  N  ND1 . HIS D  1 49  ? 86.377  85.863  64.984 1.00 14.88  ? 43  HIS D ND1 1 
ATOM   3637  C  CD2 . HIS D  1 49  ? 88.160  84.690  64.519 1.00 17.25  ? 43  HIS D CD2 1 
ATOM   3638  C  CE1 . HIS D  1 49  ? 86.827  85.365  66.122 1.00 26.58  ? 43  HIS D CE1 1 
ATOM   3639  N  NE2 . HIS D  1 49  ? 87.906  84.648  65.868 1.00 22.07  ? 43  HIS D NE2 1 
ATOM   3640  N  N   . GLY D  1 50  ? 84.431  85.585  60.230 1.00 14.23  ? 44  GLY D N   1 
ATOM   3641  C  CA  . GLY D  1 50  ? 83.947  86.128  58.969 1.00 12.91  ? 44  GLY D CA  1 
ATOM   3642  C  C   . GLY D  1 50  ? 84.788  87.347  58.621 1.00 18.24  ? 44  GLY D C   1 
ATOM   3643  O  O   . GLY D  1 50  ? 85.170  88.123  59.494 1.00 17.19  ? 44  GLY D O   1 
ATOM   3644  N  N   . PHE D  1 51  ? 85.059  87.528  57.340 1.00 12.96  ? 45  PHE D N   1 
ATOM   3645  C  CA  . PHE D  1 51  ? 85.907  88.613  56.880 1.00 19.50  ? 45  PHE D CA  1 
ATOM   3646  C  C   . PHE D  1 51  ? 85.307  89.122  55.556 1.00 24.18  ? 45  PHE D C   1 
ATOM   3647  O  O   . PHE D  1 51  ? 85.390  88.428  54.543 1.00 16.49  ? 45  PHE D O   1 
ATOM   3648  C  CB  . PHE D  1 51  ? 87.300  88.012  56.672 1.00 15.70  ? 45  PHE D CB  1 
ATOM   3649  C  CG  . PHE D  1 51  ? 88.387  89.014  56.406 1.00 20.11  ? 45  PHE D CG  1 
ATOM   3650  C  CD1 . PHE D  1 51  ? 88.752  89.943  57.368 1.00 21.56  ? 45  PHE D CD1 1 
ATOM   3651  C  CD2 . PHE D  1 51  ? 89.102  88.975  55.217 1.00 9.31   ? 45  PHE D CD2 1 
ATOM   3652  C  CE1 . PHE D  1 51  ? 89.814  90.811  57.151 1.00 14.55  ? 45  PHE D CE1 1 
ATOM   3653  C  CE2 . PHE D  1 51  ? 90.167  89.843  54.998 1.00 16.73  ? 45  PHE D CE2 1 
ATOM   3654  C  CZ  . PHE D  1 51  ? 90.520  90.759  55.967 1.00 14.44  ? 45  PHE D CZ  1 
ATOM   3655  N  N   . HIS D  1 52  ? 84.701  90.315  55.562 1.00 21.98  ? 46  HIS D N   1 
ATOM   3656  C  CA  . HIS D  1 52  ? 84.077  90.842  54.343 1.00 20.26  ? 46  HIS D CA  1 
ATOM   3657  C  C   . HIS D  1 52  ? 84.227  92.318  54.094 1.00 22.79  ? 46  HIS D C   1 
ATOM   3658  O  O   . HIS D  1 52  ? 84.498  93.103  55.007 1.00 25.09  ? 46  HIS D O   1 
ATOM   3659  C  CB  . HIS D  1 52  ? 82.563  90.607  54.325 1.00 19.82  ? 46  HIS D CB  1 
ATOM   3660  C  CG  . HIS D  1 52  ? 82.121  89.384  55.053 1.00 22.62  ? 46  HIS D CG  1 
ATOM   3661  N  ND1 . HIS D  1 52  ? 81.632  89.426  56.339 1.00 24.98  ? 46  HIS D ND1 1 
ATOM   3662  C  CD2 . HIS D  1 52  ? 82.135  88.079  54.693 1.00 18.04  ? 46  HIS D CD2 1 
ATOM   3663  C  CE1 . HIS D  1 52  ? 81.369  88.195  56.742 1.00 23.24  ? 46  HIS D CE1 1 
ATOM   3664  N  NE2 . HIS D  1 52  ? 81.666  87.361  55.761 1.00 19.45  ? 46  HIS D NE2 1 
ATOM   3665  N  N   . VAL D  1 53  ? 84.005  92.692  52.838 1.00 15.00  ? 47  VAL D N   1 
ATOM   3666  C  CA  . VAL D  1 53  ? 84.015  94.096  52.465 1.00 20.08  ? 47  VAL D CA  1 
ATOM   3667  C  C   . VAL D  1 53  ? 82.536  94.506  52.533 1.00 22.06  ? 47  VAL D C   1 
ATOM   3668  O  O   . VAL D  1 53  ? 81.699  93.925  51.842 1.00 19.34  ? 47  VAL D O   1 
ATOM   3669  C  CB  . VAL D  1 53  ? 84.495  94.315  51.034 1.00 15.57  ? 47  VAL D CB  1 
ATOM   3670  C  CG1 . VAL D  1 53  ? 84.343  95.776  50.690 1.00 11.67  ? 47  VAL D CG1 1 
ATOM   3671  C  CG2 . VAL D  1 53  ? 85.937  93.858  50.877 1.00 12.11  ? 47  VAL D CG2 1 
ATOM   3672  N  N   . HIS D  1 54  ? 82.190  95.452  53.395 1.00 21.79  ? 48  HIS D N   1 
ATOM   3673  C  CA  . HIS D  1 54  ? 80.799  95.876  53.452 1.00 23.53  ? 48  HIS D CA  1 
ATOM   3674  C  C   . HIS D  1 54  ? 80.631  97.058  52.509 1.00 27.75  ? 48  HIS D C   1 
ATOM   3675  O  O   . HIS D  1 54  ? 81.605  97.735  52.160 1.00 22.82  ? 48  HIS D O   1 
ATOM   3676  C  CB  . HIS D  1 54  ? 80.377  96.220  54.882 1.00 22.27  ? 48  HIS D CB  1 
ATOM   3677  C  CG  . HIS D  1 54  ? 80.163  95.015  55.747 1.00 26.96  ? 48  HIS D CG  1 
ATOM   3678  N  ND1 . HIS D  1 54  ? 78.968  94.760  56.390 1.00 18.74  ? 48  HIS D ND1 1 
ATOM   3679  C  CD2 . HIS D  1 54  ? 81.004  94.014  56.104 1.00 20.65  ? 48  HIS D CD2 1 
ATOM   3680  C  CE1 . HIS D  1 54  ? 79.086  93.659  57.112 1.00 23.91  ? 48  HIS D CE1 1 
ATOM   3681  N  NE2 . HIS D  1 54  ? 80.313  93.187  56.958 1.00 26.09  ? 48  HIS D NE2 1 
ATOM   3682  N  N   . GLU D  1 55  ? 79.394  97.315  52.111 1.00 27.70  ? 49  GLU D N   1 
ATOM   3683  C  CA  . GLU D  1 55  ? 79.115  98.354  51.136 1.00 30.85  ? 49  GLU D CA  1 
ATOM   3684  C  C   . GLU D  1 55  ? 79.544  99.788  51.387 1.00 31.13  ? 49  GLU D C   1 
ATOM   3685  O  O   . GLU D  1 55  ? 80.085  100.424 50.479 1.00 28.59  ? 49  GLU D O   1 
ATOM   3686  C  CB  . GLU D  1 55  ? 77.626  98.355  50.788 1.00 35.93  ? 49  GLU D CB  1 
ATOM   3687  C  CG  . GLU D  1 55  ? 77.321  99.199  49.578 1.00 38.40  ? 49  GLU D CG  1 
ATOM   3688  C  CD  . GLU D  1 55  ? 75.843  99.300  49.270 1.00 43.84  ? 49  GLU D CD  1 
ATOM   3689  O  OE1 . GLU D  1 55  ? 75.520  100.017 48.299 1.00 42.57  ? 49  GLU D OE1 1 
ATOM   3690  O  OE2 . GLU D  1 55  ? 75.014  98.674  49.977 1.00 36.84  ? 49  GLU D OE2 1 
ATOM   3691  N  N   . PHE D  1 56  ? 79.324  100.300 52.599 1.00 28.29  ? 50  PHE D N   1 
ATOM   3692  C  CA  . PHE D  1 56  ? 79.641  101.698 52.874 1.00 25.52  ? 50  PHE D CA  1 
ATOM   3693  C  C   . PHE D  1 56  ? 80.830  101.984 53.740 1.00 27.88  ? 50  PHE D C   1 
ATOM   3694  O  O   . PHE D  1 56  ? 81.066  101.290 54.721 1.00 31.42  ? 50  PHE D O   1 
ATOM   3695  C  CB  . PHE D  1 56  ? 78.433  102.390 53.502 1.00 30.36  ? 50  PHE D CB  1 
ATOM   3696  C  CG  . PHE D  1 56  ? 77.179  102.275 52.686 1.00 26.75  ? 50  PHE D CG  1 
ATOM   3697  C  CD1 . PHE D  1 56  ? 77.130  102.775 51.387 1.00 30.29  ? 50  PHE D CD1 1 
ATOM   3698  C  CD2 . PHE D  1 56  ? 76.070  101.625 53.192 1.00 24.13  ? 50  PHE D CD2 1 
ATOM   3699  C  CE1 . PHE D  1 56  ? 75.984  102.619 50.599 1.00 31.51  ? 50  PHE D CE1 1 
ATOM   3700  C  CE2 . PHE D  1 56  ? 74.920  101.465 52.414 1.00 32.45  ? 50  PHE D CE2 1 
ATOM   3701  C  CZ  . PHE D  1 56  ? 74.879  101.962 51.113 1.00 26.09  ? 50  PHE D CZ  1 
ATOM   3702  N  N   . GLY D  1 57  ? 81.563  103.033 53.373 1.00 27.70  ? 51  GLY D N   1 
ATOM   3703  C  CA  . GLY D  1 57  ? 82.709  103.462 54.151 1.00 26.00  ? 51  GLY D CA  1 
ATOM   3704  C  C   . GLY D  1 57  ? 82.201  104.521 55.119 1.00 22.85  ? 51  GLY D C   1 
ATOM   3705  O  O   . GLY D  1 57  ? 82.698  105.645 55.190 1.00 27.70  ? 51  GLY D O   1 
ATOM   3706  N  N   . ASP D  1 58  ? 81.188  104.147 55.878 1.00 26.93  ? 52  ASP D N   1 
ATOM   3707  C  CA  . ASP D  1 58  ? 80.561  105.050 56.822 1.00 25.83  ? 52  ASP D CA  1 
ATOM   3708  C  C   . ASP D  1 58  ? 80.691  104.503 58.234 1.00 25.14  ? 52  ASP D C   1 
ATOM   3709  O  O   . ASP D  1 58  ? 80.051  103.518 58.601 1.00 23.38  ? 52  ASP D O   1 
ATOM   3710  C  CB  . ASP D  1 58  ? 79.087  105.230 56.420 1.00 25.28  ? 52  ASP D CB  1 
ATOM   3711  C  CG  . ASP D  1 58  ? 78.298  106.114 57.375 1.00 28.31  ? 52  ASP D CG  1 
ATOM   3712  O  OD1 . ASP D  1 58  ? 77.246  106.630 56.945 1.00 41.24  ? 52  ASP D OD1 1 
ATOM   3713  O  OD2 . ASP D  1 58  ? 78.694  106.289 58.544 1.00 28.04  ? 52  ASP D OD2 1 
ATOM   3714  N  N   . ASN D  1 59  ? 81.523  105.165 59.024 1.00 23.68  ? 53  ASN D N   1 
ATOM   3715  C  CA  . ASN D  1 59  ? 81.745  104.765 60.396 1.00 29.90  ? 53  ASN D CA  1 
ATOM   3716  C  C   . ASN D  1 59  ? 81.066  105.743 61.366 1.00 30.59  ? 53  ASN D C   1 
ATOM   3717  O  O   . ASN D  1 59  ? 81.433  105.803 62.543 1.00 31.79  ? 53  ASN D O   1 
ATOM   3718  C  CB  . ASN D  1 59  ? 83.254  104.710 60.671 1.00 39.28  ? 53  ASN D CB  1 
ATOM   3719  C  CG  . ASN D  1 59  ? 83.587  104.120 62.038 1.00 51.13  ? 53  ASN D CG  1 
ATOM   3720  O  OD1 . ASN D  1 59  ? 84.166  104.790 62.903 1.00 51.75  ? 53  ASN D OD1 1 
ATOM   3721  N  ND2 . ASN D  1 59  ? 83.220  102.861 62.238 1.00 58.87  ? 53  ASN D ND2 1 
ATOM   3722  N  N   . THR D  1 60  ? 80.065  106.486 60.899 1.00 20.66  ? 54  THR D N   1 
ATOM   3723  C  CA  . THR D  1 60  ? 79.413  107.459 61.783 1.00 27.44  ? 54  THR D CA  1 
ATOM   3724  C  C   . THR D  1 60  ? 78.784  106.831 63.013 1.00 27.73  ? 54  THR D C   1 
ATOM   3725  O  O   . THR D  1 60  ? 78.652  107.484 64.047 1.00 35.09  ? 54  THR D O   1 
ATOM   3726  C  CB  . THR D  1 60  ? 78.333  108.296 61.060 1.00 25.41  ? 54  THR D CB  1 
ATOM   3727  O  OG1 . THR D  1 60  ? 77.263  107.446 60.617 1.00 24.76  ? 54  THR D OG1 1 
ATOM   3728  C  CG2 . THR D  1 60  ? 78.956  109.023 59.859 1.00 23.54  ? 54  THR D CG2 1 
ATOM   3729  N  N   . ALA D  1 61  ? 78.401  105.564 62.912 1.00 28.43  ? 55  ALA D N   1 
ATOM   3730  C  CA  . ALA D  1 61  ? 77.812  104.869 64.052 1.00 31.84  ? 55  ALA D CA  1 
ATOM   3731  C  C   . ALA D  1 61  ? 78.535  103.538 64.186 1.00 34.10  ? 55  ALA D C   1 
ATOM   3732  O  O   . ALA D  1 61  ? 77.926  102.468 64.240 1.00 38.29  ? 55  ALA D O   1 
ATOM   3733  C  CB  . ALA D  1 61  ? 76.314  104.662 63.831 1.00 20.78  ? 55  ALA D CB  1 
ATOM   3734  N  N   . GLY D  1 62  ? 79.858  103.615 64.220 1.00 40.13  ? 56  GLY D N   1 
ATOM   3735  C  CA  . GLY D  1 62  ? 80.644  102.407 64.339 1.00 40.20  ? 56  GLY D CA  1 
ATOM   3736  C  C   . GLY D  1 62  ? 80.490  101.564 63.089 1.00 39.87  ? 56  GLY D C   1 
ATOM   3737  O  O   . GLY D  1 62  ? 80.073  102.064 62.036 1.00 32.10  ? 56  GLY D O   1 
ATOM   3738  N  N   . CYS D  1 63  ? 80.814  100.282 63.218 1.00 31.63  ? 57  CYS D N   1 
ATOM   3739  C  CA  . CYS D  1 63  ? 80.747  99.339  62.117 1.00 29.40  ? 57  CYS D CA  1 
ATOM   3740  C  C   . CYS D  1 63  ? 79.329  99.153  61.569 1.00 31.44  ? 57  CYS D C   1 
ATOM   3741  O  O   . CYS D  1 63  ? 79.141  98.899  60.369 1.00 28.01  ? 57  CYS D O   1 
ATOM   3742  C  CB  . CYS D  1 63  ? 81.351  98.013  62.577 1.00 27.71  ? 57  CYS D CB  1 
ATOM   3743  S  SG  . CYS D  1 63  ? 83.074  98.191  63.155 1.00 30.19  ? 57  CYS D SG  1 
ATOM   3744  N  N   . THR D  1 64  ? 78.345  99.325  62.451 1.00 22.98  ? 58  THR D N   1 
ATOM   3745  C  CA  . THR D  1 64  ? 76.931  99.204  62.122 1.00 26.94  ? 58  THR D CA  1 
ATOM   3746  C  C   . THR D  1 64  ? 76.531  99.978  60.868 1.00 30.53  ? 58  THR D C   1 
ATOM   3747  O  O   . THR D  1 64  ? 75.736  99.492  60.053 1.00 29.21  ? 58  THR D O   1 
ATOM   3748  C  CB  . THR D  1 64  ? 76.050  99.734  63.269 1.00 32.37  ? 58  THR D CB  1 
ATOM   3749  O  OG1 . THR D  1 64  ? 76.390  99.067  64.488 1.00 34.21  ? 58  THR D OG1 1 
ATOM   3750  C  CG2 . THR D  1 64  ? 74.581  99.495  62.961 1.00 29.28  ? 58  THR D CG2 1 
ATOM   3751  N  N   . SER D  1 65  ? 77.073  101.184 60.721 1.00 24.83  ? 59  SER D N   1 
ATOM   3752  C  CA  . SER D  1 65  ? 76.746  102.020 59.577 1.00 20.49  ? 59  SER D CA  1 
ATOM   3753  C  C   . SER D  1 65  ? 77.486  101.696 58.281 1.00 26.44  ? 59  SER D C   1 
ATOM   3754  O  O   . SER D  1 65  ? 77.378  102.440 57.311 1.00 32.82  ? 59  SER D O   1 
ATOM   3755  C  CB  . SER D  1 65  ? 76.915  103.508 59.937 1.00 21.81  ? 59  SER D CB  1 
ATOM   3756  O  OG  . SER D  1 65  ? 78.178  103.799 60.508 1.00 31.64  ? 59  SER D OG  1 
ATOM   3757  N  N   . ALA D  1 66  ? 78.226  100.591 58.245 1.00 23.80  ? 60  ALA D N   1 
ATOM   3758  C  CA  . ALA D  1 66  ? 78.923  100.201 57.012 1.00 27.08  ? 60  ALA D CA  1 
ATOM   3759  C  C   . ALA D  1 66  ? 77.989  99.453  56.031 1.00 24.05  ? 60  ALA D C   1 
ATOM   3760  O  O   . ALA D  1 66  ? 78.370  99.119  54.902 1.00 24.96  ? 60  ALA D O   1 
ATOM   3761  C  CB  . ALA D  1 66  ? 80.124  99.318  57.343 1.00 24.62  ? 60  ALA D CB  1 
ATOM   3762  N  N   . GLY D  1 67  ? 76.768  99.185  56.468 1.00 25.62  ? 61  GLY D N   1 
ATOM   3763  C  CA  . GLY D  1 67  ? 75.831  98.485  55.617 1.00 22.41  ? 61  GLY D CA  1 
ATOM   3764  C  C   . GLY D  1 67  ? 76.100  96.994  55.499 1.00 26.43  ? 61  GLY D C   1 
ATOM   3765  O  O   . GLY D  1 67  ? 76.918  96.409  56.232 1.00 23.02  ? 61  GLY D O   1 
ATOM   3766  N  N   . PRO D  1 68  ? 75.402  96.346  54.567 1.00 24.32  ? 62  PRO D N   1 
ATOM   3767  C  CA  . PRO D  1 68  ? 75.538  94.910  54.322 1.00 22.75  ? 62  PRO D CA  1 
ATOM   3768  C  C   . PRO D  1 68  ? 76.780  94.661  53.472 1.00 26.18  ? 62  PRO D C   1 
ATOM   3769  O  O   . PRO D  1 68  ? 77.517  95.603  53.140 1.00 20.86  ? 62  PRO D O   1 
ATOM   3770  C  CB  . PRO D  1 68  ? 74.253  94.584  53.572 1.00 24.15  ? 62  PRO D CB  1 
ATOM   3771  C  CG  . PRO D  1 68  ? 74.100  95.849  52.686 1.00 22.97  ? 62  PRO D CG  1 
ATOM   3772  C  CD  . PRO D  1 68  ? 74.389  96.954  53.673 1.00 25.47  ? 62  PRO D CD  1 
ATOM   3773  N  N   . HIS D  1 69  ? 77.010  93.400  53.123 1.00 19.27  ? 63  HIS D N   1 
ATOM   3774  C  CA  . HIS D  1 69  ? 78.158  93.042  52.295 1.00 20.92  ? 63  HIS D CA  1 
ATOM   3775  C  C   . HIS D  1 69  ? 78.073  93.778  50.953 1.00 23.21  ? 63  HIS D C   1 
ATOM   3776  O  O   . HIS D  1 69  ? 76.992  93.936  50.387 1.00 25.28  ? 63  HIS D O   1 
ATOM   3777  C  CB  . HIS D  1 69  ? 78.180  91.521  52.054 1.00 24.79  ? 63  HIS D CB  1 
ATOM   3778  C  CG  . HIS D  1 69  ? 78.346  90.700  53.304 1.00 27.52  ? 63  HIS D CG  1 
ATOM   3779  N  ND1 . HIS D  1 69  ? 78.298  89.323  53.303 1.00 26.31  ? 63  HIS D ND1 1 
ATOM   3780  C  CD2 . HIS D  1 69  ? 78.597  91.063  54.585 1.00 23.64  ? 63  HIS D CD2 1 
ATOM   3781  C  CE1 . HIS D  1 69  ? 78.515  88.874  54.527 1.00 20.09  ? 63  HIS D CE1 1 
ATOM   3782  N  NE2 . HIS D  1 69  ? 78.701  89.910  55.322 1.00 21.68  ? 63  HIS D NE2 1 
ATOM   3783  N  N   . PHE D  1 70  ? 79.209  94.259  50.466 1.00 22.33  ? 64  PHE D N   1 
ATOM   3784  C  CA  . PHE D  1 70  ? 79.267  94.939  49.187 1.00 19.38  ? 64  PHE D CA  1 
ATOM   3785  C  C   . PHE D  1 70  ? 78.702  93.912  48.183 1.00 28.15  ? 64  PHE D C   1 
ATOM   3786  O  O   . PHE D  1 70  ? 79.307  92.855  47.950 1.00 28.39  ? 64  PHE D O   1 
ATOM   3787  C  CB  . PHE D  1 70  ? 80.733  95.280  48.869 1.00 24.54  ? 64  PHE D CB  1 
ATOM   3788  C  CG  . PHE D  1 70  ? 80.927  95.983  47.555 1.00 25.55  ? 64  PHE D CG  1 
ATOM   3789  C  CD1 . PHE D  1 70  ? 82.074  95.771  46.809 1.00 24.98  ? 64  PHE D CD1 1 
ATOM   3790  C  CD2 . PHE D  1 70  ? 79.971  96.880  47.074 1.00 31.92  ? 64  PHE D CD2 1 
ATOM   3791  C  CE1 . PHE D  1 70  ? 82.280  96.441  45.594 1.00 27.45  ? 64  PHE D CE1 1 
ATOM   3792  C  CE2 . PHE D  1 70  ? 80.163  97.555  45.863 1.00 19.00  ? 64  PHE D CE2 1 
ATOM   3793  C  CZ  . PHE D  1 70  ? 81.320  97.333  45.123 1.00 22.05  ? 64  PHE D CZ  1 
ATOM   3794  N  N   . ASN D  1 71  ? 77.543  94.216  47.605 1.00 25.35  ? 65  ASN D N   1 
ATOM   3795  C  CA  . ASN D  1 71  ? 76.871  93.294  46.685 1.00 28.90  ? 65  ASN D CA  1 
ATOM   3796  C  C   . ASN D  1 71  ? 76.357  94.023  45.454 1.00 33.46  ? 65  ASN D C   1 
ATOM   3797  O  O   . ASN D  1 71  ? 75.149  94.132  45.241 1.00 34.86  ? 65  ASN D O   1 
ATOM   3798  C  CB  . ASN D  1 71  ? 75.699  92.629  47.422 1.00 19.05  ? 65  ASN D CB  1 
ATOM   3799  C  CG  . ASN D  1 71  ? 75.032  91.527  46.605 1.00 27.61  ? 65  ASN D CG  1 
ATOM   3800  O  OD1 . ASN D  1 71  ? 75.612  90.979  45.661 1.00 25.16  ? 65  ASN D OD1 1 
ATOM   3801  N  ND2 . ASN D  1 71  ? 73.810  91.186  46.982 1.00 27.59  ? 65  ASN D ND2 1 
ATOM   3802  N  N   . PRO D  1 72  ? 77.268  94.535  44.622 1.00 30.61  ? 66  PRO D N   1 
ATOM   3803  C  CA  . PRO D  1 72  ? 76.838  95.256  43.429 1.00 32.97  ? 66  PRO D CA  1 
ATOM   3804  C  C   . PRO D  1 72  ? 76.073  94.420  42.400 1.00 37.57  ? 66  PRO D C   1 
ATOM   3805  O  O   . PRO D  1 72  ? 75.271  94.970  41.656 1.00 43.88  ? 66  PRO D O   1 
ATOM   3806  C  CB  . PRO D  1 72  ? 78.140  95.823  42.892 1.00 31.40  ? 66  PRO D CB  1 
ATOM   3807  C  CG  . PRO D  1 72  ? 79.128  94.743  43.258 1.00 38.08  ? 66  PRO D CG  1 
ATOM   3808  C  CD  . PRO D  1 72  ? 78.732  94.412  44.673 1.00 34.84  ? 66  PRO D CD  1 
ATOM   3809  N  N   . LEU D  1 73  ? 76.296  93.107  42.364 1.00 34.01  ? 67  LEU D N   1 
ATOM   3810  C  CA  . LEU D  1 73  ? 75.596  92.234  41.416 1.00 31.13  ? 67  LEU D CA  1 
ATOM   3811  C  C   . LEU D  1 73  ? 74.335  91.619  42.020 1.00 30.84  ? 67  LEU D C   1 
ATOM   3812  O  O   . LEU D  1 73  ? 73.698  90.758  41.415 1.00 31.69  ? 67  LEU D O   1 
ATOM   3813  C  CB  . LEU D  1 73  ? 76.534  91.126  40.915 1.00 33.72  ? 67  LEU D CB  1 
ATOM   3814  C  CG  . LEU D  1 73  ? 77.710  91.611  40.056 1.00 37.92  ? 67  LEU D CG  1 
ATOM   3815  C  CD1 . LEU D  1 73  ? 78.698  90.485  39.790 1.00 37.01  ? 67  LEU D CD1 1 
ATOM   3816  C  CD2 . LEU D  1 73  ? 77.152  92.141  38.744 1.00 43.85  ? 67  LEU D CD2 1 
ATOM   3817  N  N   . SER D  1 74  ? 73.974  92.065  43.216 1.00 34.49  ? 68  SER D N   1 
ATOM   3818  C  CA  . SER D  1 74  ? 72.763  91.583  43.895 1.00 44.94  ? 68  SER D CA  1 
ATOM   3819  C  C   . SER D  1 74  ? 72.660  90.063  43.961 1.00 44.68  ? 68  SER D C   1 
ATOM   3820  O  O   . SER D  1 74  ? 71.627  89.486  43.645 1.00 42.69  ? 68  SER D O   1 
ATOM   3821  C  CB  . SER D  1 74  ? 71.506  92.128  43.200 1.00 47.06  ? 68  SER D CB  1 
ATOM   3822  O  OG  . SER D  1 74  ? 71.433  93.539  43.278 1.00 51.99  ? 68  SER D OG  1 
ATOM   3823  N  N   . ARG D  1 75  ? 73.731  89.418  44.398 1.00 44.19  ? 69  ARG D N   1 
ATOM   3824  C  CA  . ARG D  1 75  ? 73.751  87.974  44.497 1.00 35.63  ? 69  ARG D CA  1 
ATOM   3825  C  C   . ARG D  1 75  ? 73.528  87.519  45.941 1.00 30.90  ? 69  ARG D C   1 
ATOM   3826  O  O   . ARG D  1 75  ? 73.497  88.336  46.853 1.00 34.99  ? 69  ARG D O   1 
ATOM   3827  C  CB  . ARG D  1 75  ? 75.096  87.469  43.979 1.00 34.87  ? 69  ARG D CB  1 
ATOM   3828  C  CG  . ARG D  1 75  ? 74.973  86.462  42.861 1.00 54.02  ? 69  ARG D CG  1 
ATOM   3829  C  CD  . ARG D  1 75  ? 74.889  87.112  41.506 1.00 53.94  ? 69  ARG D CD  1 
ATOM   3830  N  NE  . ARG D  1 75  ? 76.151  86.946  40.794 1.00 66.30  ? 69  ARG D NE  1 
ATOM   3831  C  CZ  . ARG D  1 75  ? 76.368  87.340  39.544 1.00 71.92  ? 69  ARG D CZ  1 
ATOM   3832  N  NH1 . ARG D  1 75  ? 75.391  87.931  38.852 1.00 65.16  ? 69  ARG D NH1 1 
ATOM   3833  N  NH2 . ARG D  1 75  ? 77.566  87.148  38.992 1.00 64.28  ? 69  ARG D NH2 1 
ATOM   3834  N  N   . LYS D  1 76  ? 73.351  86.219  46.156 1.00 32.65  ? 70  LYS D N   1 
ATOM   3835  C  CA  . LYS D  1 76  ? 73.194  85.710  47.517 1.00 33.45  ? 70  LYS D CA  1 
ATOM   3836  C  C   . LYS D  1 76  ? 74.599  85.524  48.127 1.00 32.68  ? 70  LYS D C   1 
ATOM   3837  O  O   . LYS D  1 76  ? 75.587  85.397  47.401 1.00 25.97  ? 70  LYS D O   1 
ATOM   3838  C  CB  . LYS D  1 76  ? 72.467  84.370  47.508 1.00 39.50  ? 70  LYS D CB  1 
ATOM   3839  C  CG  . LYS D  1 76  ? 71.006  84.438  47.120 1.00 51.74  ? 70  LYS D CG  1 
ATOM   3840  C  CD  . LYS D  1 76  ? 70.400  83.039  47.099 1.00 64.85  ? 70  LYS D CD  1 
ATOM   3841  C  CE  . LYS D  1 76  ? 68.939  83.063  46.676 1.00 74.55  ? 70  LYS D CE  1 
ATOM   3842  N  NZ  . LYS D  1 76  ? 68.343  81.696  46.659 1.00 83.19  ? 70  LYS D NZ  1 
ATOM   3843  N  N   . HIS D  1 77  ? 74.684  85.489  49.454 1.00 29.32  ? 71  HIS D N   1 
ATOM   3844  C  CA  . HIS D  1 77  ? 75.966  85.330  50.141 1.00 24.11  ? 71  HIS D CA  1 
ATOM   3845  C  C   . HIS D  1 77  ? 76.634  83.989  49.827 1.00 24.75  ? 71  HIS D C   1 
ATOM   3846  O  O   . HIS D  1 77  ? 75.961  82.975  49.687 1.00 20.65  ? 71  HIS D O   1 
ATOM   3847  C  CB  . HIS D  1 77  ? 75.772  85.440  51.669 1.00 24.56  ? 71  HIS D CB  1 
ATOM   3848  C  CG  . HIS D  1 77  ? 77.047  85.305  52.450 1.00 22.55  ? 71  HIS D CG  1 
ATOM   3849  N  ND1 . HIS D  1 77  ? 78.016  86.287  52.468 1.00 20.43  ? 71  HIS D ND1 1 
ATOM   3850  C  CD2 . HIS D  1 77  ? 77.560  84.260  53.143 1.00 18.45  ? 71  HIS D CD2 1 
ATOM   3851  C  CE1 . HIS D  1 77  ? 79.073  85.849  53.128 1.00 23.69  ? 71  HIS D CE1 1 
ATOM   3852  N  NE2 . HIS D  1 77  ? 78.822  84.621  53.547 1.00 24.58  ? 71  HIS D NE2 1 
ATOM   3853  N  N   . GLY D  1 78  ? 77.960  83.982  49.734 1.00 21.60  ? 72  GLY D N   1 
ATOM   3854  C  CA  . GLY D  1 78  ? 78.670  82.737  49.473 1.00 19.93  ? 72  GLY D CA  1 
ATOM   3855  C  C   . GLY D  1 78  ? 80.117  82.787  49.957 1.00 25.67  ? 72  GLY D C   1 
ATOM   3856  O  O   . GLY D  1 78  ? 80.541  83.766  50.596 1.00 19.65  ? 72  GLY D O   1 
ATOM   3857  N  N   . GLY D  1 79  ? 80.864  81.718  49.682 1.00 20.74  ? 73  GLY D N   1 
ATOM   3858  C  CA  . GLY D  1 79  ? 82.267  81.669  50.038 1.00 11.65  ? 73  GLY D CA  1 
ATOM   3859  C  C   . GLY D  1 79  ? 83.044  82.300  48.884 1.00 20.41  ? 73  GLY D C   1 
ATOM   3860  O  O   . GLY D  1 79  ? 82.517  82.432  47.784 1.00 14.30  ? 73  GLY D O   1 
ATOM   3861  N  N   . PRO D  1 80  ? 84.295  82.716  49.093 1.00 25.20  ? 74  PRO D N   1 
ATOM   3862  C  CA  . PRO D  1 80  ? 85.000  83.317  47.954 1.00 30.53  ? 74  PRO D CA  1 
ATOM   3863  C  C   . PRO D  1 80  ? 85.142  82.437  46.689 1.00 34.78  ? 74  PRO D C   1 
ATOM   3864  O  O   . PRO D  1 80  ? 85.254  82.951  45.563 1.00 25.95  ? 74  PRO D O   1 
ATOM   3865  C  CB  . PRO D  1 80  ? 86.355  83.733  48.558 1.00 23.15  ? 74  PRO D CB  1 
ATOM   3866  C  CG  . PRO D  1 80  ? 86.502  82.841  49.786 1.00 28.39  ? 74  PRO D CG  1 
ATOM   3867  C  CD  . PRO D  1 80  ? 85.095  82.799  50.329 1.00 26.70  ? 74  PRO D CD  1 
ATOM   3868  N  N   . LYS D  1 81  ? 85.118  81.119  46.858 1.00 30.92  ? 75  LYS D N   1 
ATOM   3869  C  CA  . LYS D  1 81  ? 85.267  80.242  45.700 1.00 29.47  ? 75  LYS D CA  1 
ATOM   3870  C  C   . LYS D  1 81  ? 83.978  80.023  44.929 1.00 29.20  ? 75  LYS D C   1 
ATOM   3871  O  O   . LYS D  1 81  ? 84.005  79.464  43.843 1.00 33.50  ? 75  LYS D O   1 
ATOM   3872  C  CB  . LYS D  1 81  ? 85.832  78.876  46.120 1.00 22.34  ? 75  LYS D CB  1 
ATOM   3873  C  CG  . LYS D  1 81  ? 87.276  78.927  46.626 1.00 36.02  ? 75  LYS D CG  1 
ATOM   3874  C  CD  . LYS D  1 81  ? 87.859  77.533  46.868 1.00 47.15  ? 75  LYS D CD  1 
ATOM   3875  C  CE  . LYS D  1 81  ? 87.182  76.814  48.025 1.00 55.81  ? 75  LYS D CE  1 
ATOM   3876  N  NZ  . LYS D  1 81  ? 87.477  75.350  47.999 1.00 52.01  ? 75  LYS D NZ  1 
ATOM   3877  N  N   . ASP D  1 82  ? 82.853  80.461  45.482 1.00 26.95  ? 76  ASP D N   1 
ATOM   3878  C  CA  . ASP D  1 82  ? 81.548  80.262  44.846 1.00 31.69  ? 76  ASP D CA  1 
ATOM   3879  C  C   . ASP D  1 82  ? 81.273  81.198  43.677 1.00 33.95  ? 76  ASP D C   1 
ATOM   3880  O  O   . ASP D  1 82  ? 81.815  82.301  43.606 1.00 36.75  ? 76  ASP D O   1 
ATOM   3881  C  CB  . ASP D  1 82  ? 80.426  80.446  45.885 1.00 30.54  ? 76  ASP D CB  1 
ATOM   3882  C  CG  . ASP D  1 82  ? 80.410  79.352  46.938 1.00 27.41  ? 76  ASP D CG  1 
ATOM   3883  O  OD1 . ASP D  1 82  ? 80.117  79.659  48.111 1.00 27.52  ? 76  ASP D OD1 1 
ATOM   3884  O  OD2 . ASP D  1 82  ? 80.678  78.180  46.597 1.00 40.34  ? 76  ASP D OD2 1 
ATOM   3885  N  N   . GLU D  1 83  ? 80.422  80.756  42.760 1.00 32.25  ? 77  GLU D N   1 
ATOM   3886  C  CA  . GLU D  1 83  ? 80.035  81.603  41.638 1.00 37.62  ? 77  GLU D CA  1 
ATOM   3887  C  C   . GLU D  1 83  ? 79.003  82.560  42.229 1.00 33.06  ? 77  GLU D C   1 
ATOM   3888  O  O   . GLU D  1 83  ? 79.011  83.761  41.958 1.00 37.26  ? 77  GLU D O   1 
ATOM   3889  C  CB  . GLU D  1 83  ? 79.399  80.766  40.528 1.00 48.23  ? 77  GLU D CB  1 
ATOM   3890  C  CG  . GLU D  1 83  ? 78.516  81.556  39.560 1.00 73.01  ? 77  GLU D CG  1 
ATOM   3891  C  CD  . GLU D  1 83  ? 79.304  82.432  38.600 1.00 84.41  ? 77  GLU D CD  1 
ATOM   3892  O  OE1 . GLU D  1 83  ? 80.036  81.879  37.748 1.00 89.34  ? 77  GLU D OE1 1 
ATOM   3893  O  OE2 . GLU D  1 83  ? 79.189  83.674  38.698 1.00 92.89  ? 77  GLU D OE2 1 
ATOM   3894  N  N   . GLU D  1 84  ? 78.127  82.007  43.062 1.00 28.03  ? 78  GLU D N   1 
ATOM   3895  C  CA  . GLU D  1 84  ? 77.083  82.778  43.720 1.00 27.05  ? 78  GLU D CA  1 
ATOM   3896  C  C   . GLU D  1 84  ? 77.668  83.359  45.007 1.00 24.20  ? 78  GLU D C   1 
ATOM   3897  O  O   . GLU D  1 84  ? 77.754  82.666  46.014 1.00 28.02  ? 78  GLU D O   1 
ATOM   3898  C  CB  . GLU D  1 84  ? 75.896  81.863  44.063 1.00 13.91  ? 78  GLU D CB  1 
ATOM   3899  C  CG  . GLU D  1 84  ? 74.666  82.560  44.661 1.00 26.49  ? 78  GLU D CG  1 
ATOM   3900  C  CD  . GLU D  1 84  ? 73.947  83.487  43.667 1.00 44.86  ? 78  GLU D CD  1 
ATOM   3901  O  OE1 . GLU D  1 84  ? 72.932  84.122  44.054 1.00 34.39  ? 78  GLU D OE1 1 
ATOM   3902  O  OE2 . GLU D  1 84  ? 74.397  83.583  42.496 1.00 52.25  ? 78  GLU D OE2 1 
ATOM   3903  N  N   . ARG D  1 85  ? 78.082  84.620  44.971 1.00 29.40  ? 79  ARG D N   1 
ATOM   3904  C  CA  . ARG D  1 85  ? 78.626  85.275  46.163 1.00 26.86  ? 79  ARG D CA  1 
ATOM   3905  C  C   . ARG D  1 85  ? 78.590  86.784  46.044 1.00 26.03  ? 79  ARG D C   1 
ATOM   3906  O  O   . ARG D  1 85  ? 78.437  87.330  44.955 1.00 30.90  ? 79  ARG D O   1 
ATOM   3907  C  CB  . ARG D  1 85  ? 80.065  84.834  46.409 1.00 25.27  ? 79  ARG D CB  1 
ATOM   3908  C  CG  . ARG D  1 85  ? 81.018  85.153  45.252 1.00 19.61  ? 79  ARG D CG  1 
ATOM   3909  C  CD  . ARG D  1 85  ? 82.022  86.212  45.683 1.00 29.88  ? 79  ARG D CD  1 
ATOM   3910  N  NE  . ARG D  1 85  ? 83.387  85.736  45.547 1.00 27.61  ? 79  ARG D NE  1 
ATOM   3911  C  CZ  . ARG D  1 85  ? 84.472  86.432  45.879 1.00 28.17  ? 79  ARG D CZ  1 
ATOM   3912  N  NH1 . ARG D  1 85  ? 84.383  87.652  46.383 1.00 17.16  ? 79  ARG D NH1 1 
ATOM   3913  N  NH2 . ARG D  1 85  ? 85.663  85.898  45.678 1.00 25.57  ? 79  ARG D NH2 1 
ATOM   3914  N  N   . HIS D  1 86  ? 78.723  87.456  47.177 1.00 25.53  ? 80  HIS D N   1 
ATOM   3915  C  CA  . HIS D  1 86  ? 78.743  88.912  47.200 1.00 24.62  ? 80  HIS D CA  1 
ATOM   3916  C  C   . HIS D  1 86  ? 80.163  89.293  46.800 1.00 21.06  ? 80  HIS D C   1 
ATOM   3917  O  O   . HIS D  1 86  ? 81.105  88.539  47.058 1.00 17.54  ? 80  HIS D O   1 
ATOM   3918  C  CB  . HIS D  1 86  ? 78.452  89.414  48.617 1.00 28.41  ? 80  HIS D CB  1 
ATOM   3919  C  CG  . HIS D  1 86  ? 77.073  89.097  49.103 1.00 27.62  ? 80  HIS D CG  1 
ATOM   3920  N  ND1 . HIS D  1 86  ? 76.798  88.810  50.423 1.00 27.50  ? 80  HIS D ND1 1 
ATOM   3921  C  CD2 . HIS D  1 86  ? 75.877  89.111  48.466 1.00 28.16  ? 80  HIS D CD2 1 
ATOM   3922  C  CE1 . HIS D  1 86  ? 75.493  88.666  50.581 1.00 17.68  ? 80  HIS D CE1 1 
ATOM   3923  N  NE2 . HIS D  1 86  ? 74.911  88.845  49.409 1.00 21.43  ? 80  HIS D NE2 1 
ATOM   3924  N  N   . VAL D  1 87  ? 80.330  90.440  46.156 1.00 20.61  ? 81  VAL D N   1 
ATOM   3925  C  CA  . VAL D  1 87  ? 81.669  90.851  45.775 1.00 20.94  ? 81  VAL D CA  1 
ATOM   3926  C  C   . VAL D  1 87  ? 82.529  90.948  47.036 1.00 19.47  ? 81  VAL D C   1 
ATOM   3927  O  O   . VAL D  1 87  ? 83.702  90.588  47.028 1.00 21.02  ? 81  VAL D O   1 
ATOM   3928  C  CB  . VAL D  1 87  ? 81.659  92.215  45.024 1.00 18.96  ? 81  VAL D CB  1 
ATOM   3929  C  CG1 . VAL D  1 87  ? 83.076  92.790  44.932 1.00 17.30  ? 81  VAL D CG1 1 
ATOM   3930  C  CG2 . VAL D  1 87  ? 81.121  92.020  43.613 1.00 16.06  ? 81  VAL D CG2 1 
ATOM   3931  N  N   . GLY D  1 88  ? 81.947  91.409  48.131 1.00 17.84  ? 82  GLY D N   1 
ATOM   3932  C  CA  . GLY D  1 88  ? 82.737  91.526  49.348 1.00 26.22  ? 82  GLY D CA  1 
ATOM   3933  C  C   . GLY D  1 88  ? 82.895  90.265  50.181 1.00 24.84  ? 82  GLY D C   1 
ATOM   3934  O  O   . GLY D  1 88  ? 83.357  90.337  51.320 1.00 28.55  ? 82  GLY D O   1 
ATOM   3935  N  N   . ASP D  1 89  ? 82.525  89.109  49.635 1.00 21.36  ? 83  ASP D N   1 
ATOM   3936  C  CA  . ASP D  1 89  ? 82.637  87.865  50.391 1.00 19.15  ? 83  ASP D CA  1 
ATOM   3937  C  C   . ASP D  1 89  ? 84.041  87.257  50.352 1.00 23.05  ? 83  ASP D C   1 
ATOM   3938  O  O   . ASP D  1 89  ? 84.371  86.487  49.456 1.00 25.17  ? 83  ASP D O   1 
ATOM   3939  C  CB  . ASP D  1 89  ? 81.628  86.848  49.879 1.00 19.10  ? 83  ASP D CB  1 
ATOM   3940  C  CG  . ASP D  1 89  ? 80.204  87.191  50.262 1.00 18.87  ? 83  ASP D CG  1 
ATOM   3941  O  OD1 . ASP D  1 89  ? 80.004  88.157  51.034 1.00 20.38  ? 83  ASP D OD1 1 
ATOM   3942  O  OD2 . ASP D  1 89  ? 79.279  86.487  49.792 1.00 17.26  ? 83  ASP D OD2 1 
ATOM   3943  N  N   . LEU D  1 90  ? 84.861  87.599  51.340 1.00 17.09  ? 84  LEU D N   1 
ATOM   3944  C  CA  . LEU D  1 90  ? 86.215  87.089  51.409 1.00 17.20  ? 84  LEU D CA  1 
ATOM   3945  C  C   . LEU D  1 90  ? 86.385  85.826  52.266 1.00 21.45  ? 84  LEU D C   1 
ATOM   3946  O  O   . LEU D  1 90  ? 87.502  85.336  52.456 1.00 22.53  ? 84  LEU D O   1 
ATOM   3947  C  CB  . LEU D  1 90  ? 87.141  88.199  51.890 1.00 15.13  ? 84  LEU D CB  1 
ATOM   3948  C  CG  . LEU D  1 90  ? 87.289  89.344  50.880 1.00 19.52  ? 84  LEU D CG  1 
ATOM   3949  C  CD1 . LEU D  1 90  ? 88.308  90.328  51.421 1.00 15.18  ? 84  LEU D CD1 1 
ATOM   3950  C  CD2 . LEU D  1 90  ? 87.784  88.810  49.511 1.00 17.80  ? 84  LEU D CD2 1 
ATOM   3951  N  N   . GLY D  1 91  ? 85.279  85.296  52.775 1.00 18.08  ? 85  GLY D N   1 
ATOM   3952  C  CA  . GLY D  1 91  ? 85.344  84.084  53.576 1.00 15.01  ? 85  GLY D CA  1 
ATOM   3953  C  C   . GLY D  1 91  ? 85.740  84.285  55.030 1.00 20.25  ? 85  GLY D C   1 
ATOM   3954  O  O   . GLY D  1 91  ? 85.286  85.227  55.685 1.00 16.05  ? 85  GLY D O   1 
ATOM   3955  N  N   . ASN D  1 92  ? 86.587  83.393  55.540 1.00 17.52  ? 86  ASN D N   1 
ATOM   3956  C  CA  . ASN D  1 92  ? 87.040  83.480  56.931 1.00 22.48  ? 86  ASN D CA  1 
ATOM   3957  C  C   . ASN D  1 92  ? 88.533  83.717  57.052 1.00 22.79  ? 86  ASN D C   1 
ATOM   3958  O  O   . ASN D  1 92  ? 89.318  83.458  56.129 1.00 25.15  ? 86  ASN D O   1 
ATOM   3959  C  CB  . ASN D  1 92  ? 86.728  82.180  57.697 1.00 19.82  ? 86  ASN D CB  1 
ATOM   3960  C  CG  . ASN D  1 92  ? 85.252  81.949  57.881 1.00 25.00  ? 86  ASN D CG  1 
ATOM   3961  O  OD1 . ASN D  1 92  ? 84.587  82.676  58.617 1.00 24.57  ? 86  ASN D OD1 1 
ATOM   3962  N  ND2 . ASN D  1 92  ? 84.723  80.931  57.207 1.00 14.79  ? 86  ASN D ND2 1 
ATOM   3963  N  N   . VAL D  1 93  ? 88.916  84.215  58.213 1.00 20.89  ? 87  VAL D N   1 
ATOM   3964  C  CA  . VAL D  1 93  ? 90.317  84.406  58.531 1.00 21.38  ? 87  VAL D CA  1 
ATOM   3965  C  C   . VAL D  1 93  ? 90.456  83.537  59.776 1.00 25.94  ? 87  VAL D C   1 
ATOM   3966  O  O   . VAL D  1 93  ? 89.478  83.307  60.504 1.00 23.97  ? 87  VAL D O   1 
ATOM   3967  C  CB  . VAL D  1 93  ? 90.693  85.897  58.818 1.00 23.15  ? 87  VAL D CB  1 
ATOM   3968  C  CG1 . VAL D  1 93  ? 90.590  86.698  57.535 1.00 23.13  ? 87  VAL D CG1 1 
ATOM   3969  C  CG2 . VAL D  1 93  ? 89.812  86.498  59.923 1.00 12.75  ? 87  VAL D CG2 1 
ATOM   3970  N  N   . THR D  1 94  ? 91.657  83.036  60.008 1.00 26.19  ? 88  THR D N   1 
ATOM   3971  C  CA  . THR D  1 94  ? 91.888  82.145  61.122 1.00 22.02  ? 88  THR D CA  1 
ATOM   3972  C  C   . THR D  1 94  ? 92.765  82.760  62.192 1.00 24.93  ? 88  THR D C   1 
ATOM   3973  O  O   . THR D  1 94  ? 93.879  83.195  61.917 1.00 26.24  ? 88  THR D O   1 
ATOM   3974  C  CB  . THR D  1 94  ? 92.532  80.850  60.597 1.00 19.08  ? 88  THR D CB  1 
ATOM   3975  O  OG1 . THR D  1 94  ? 91.641  80.247  59.662 1.00 19.07  ? 88  THR D OG1 1 
ATOM   3976  C  CG2 . THR D  1 94  ? 92.794  79.859  61.710 1.00 26.12  ? 88  THR D CG2 1 
ATOM   3977  N  N   . ALA D  1 95  ? 92.245  82.811  63.410 1.00 20.64  ? 89  ALA D N   1 
ATOM   3978  C  CA  . ALA D  1 95  ? 93.003  83.328  64.546 1.00 25.66  ? 89  ALA D CA  1 
ATOM   3979  C  C   . ALA D  1 95  ? 93.581  82.105  65.249 1.00 21.58  ? 89  ALA D C   1 
ATOM   3980  O  O   . ALA D  1 95  ? 92.897  81.107  65.429 1.00 19.04  ? 89  ALA D O   1 
ATOM   3981  C  CB  . ALA D  1 95  ? 92.089  84.086  65.504 1.00 27.11  ? 89  ALA D CB  1 
ATOM   3982  N  N   . ASP D  1 96  ? 94.834  82.195  65.665 1.00 26.49  ? 90  ASP D N   1 
ATOM   3983  C  CA  . ASP D  1 96  ? 95.499  81.089  66.340 1.00 26.14  ? 90  ASP D CA  1 
ATOM   3984  C  C   . ASP D  1 96  ? 95.386  81.163  67.861 1.00 27.76  ? 90  ASP D C   1 
ATOM   3985  O  O   . ASP D  1 96  ? 94.719  82.039  68.397 1.00 29.25  ? 90  ASP D O   1 
ATOM   3986  C  CB  . ASP D  1 96  ? 96.964  81.061  65.905 1.00 26.64  ? 90  ASP D CB  1 
ATOM   3987  C  CG  . ASP D  1 96  ? 97.117  80.800  64.414 1.00 37.25  ? 90  ASP D CG  1 
ATOM   3988  O  OD1 . ASP D  1 96  ? 96.468  79.853  63.903 1.00 48.04  ? 90  ASP D OD1 1 
ATOM   3989  O  OD2 . ASP D  1 96  ? 97.880  81.534  63.745 1.00 46.69  ? 90  ASP D OD2 1 
ATOM   3990  N  N   . LYS D  1 97  ? 96.040  80.247  68.563 1.00 31.06  ? 91  LYS D N   1 
ATOM   3991  C  CA  . LYS D  1 97  ? 95.977  80.248  70.022 1.00 32.86  ? 91  LYS D CA  1 
ATOM   3992  C  C   . LYS D  1 97  ? 96.504  81.556  70.623 1.00 27.52  ? 91  LYS D C   1 
ATOM   3993  O  O   . LYS D  1 97  ? 96.099  81.955  71.700 1.00 29.03  ? 91  LYS D O   1 
ATOM   3994  C  CB  . LYS D  1 97  ? 96.759  79.057  70.582 1.00 37.90  ? 91  LYS D CB  1 
ATOM   3995  C  CG  . LYS D  1 97  ? 98.216  78.993  70.167 1.00 47.51  ? 91  LYS D CG  1 
ATOM   3996  C  CD  . LYS D  1 97  ? 98.871  77.710  70.697 1.00 59.94  ? 91  LYS D CD  1 
ATOM   3997  C  CE  . LYS D  1 97  ? 100.296 77.539  70.178 1.00 64.35  ? 91  LYS D CE  1 
ATOM   3998  N  NZ  . LYS D  1 97  ? 100.853 76.190  70.484 1.00 71.60  ? 91  LYS D NZ  1 
ATOM   3999  N  N   . ASP D  1 98  ? 97.400  82.224  69.912 1.00 29.26  ? 92  ASP D N   1 
ATOM   4000  C  CA  . ASP D  1 98  ? 97.965  83.491  70.366 1.00 25.75  ? 92  ASP D CA  1 
ATOM   4001  C  C   . ASP D  1 98  ? 96.969  84.624  70.102 1.00 26.00  ? 92  ASP D C   1 
ATOM   4002  O  O   . ASP D  1 98  ? 97.313  85.792  70.228 1.00 22.71  ? 92  ASP D O   1 
ATOM   4003  C  CB  . ASP D  1 98  ? 99.259  83.763  69.609 1.00 32.73  ? 92  ASP D CB  1 
ATOM   4004  C  CG  . ASP D  1 98  ? 99.026  83.982  68.111 1.00 48.33  ? 92  ASP D CG  1 
ATOM   4005  O  OD1 . ASP D  1 98  ? 97.967  83.552  67.580 1.00 37.26  ? 92  ASP D OD1 1 
ATOM   4006  O  OD2 . ASP D  1 98  ? 99.916  84.578  67.460 1.00 56.26  ? 92  ASP D OD2 1 
ATOM   4007  N  N   . ALA D  1 99  ? 95.744  84.265  69.714 1.00 22.73  ? 93  ALA D N   1 
ATOM   4008  C  CA  . ALA D  1 99  ? 94.678  85.228  69.431 1.00 21.17  ? 93  ALA D CA  1 
ATOM   4009  C  C   . ALA D  1 99  ? 95.003  86.190  68.301 1.00 21.43  ? 93  ALA D C   1 
ATOM   4010  O  O   . ALA D  1 99  ? 94.454  87.283  68.231 1.00 19.77  ? 93  ALA D O   1 
ATOM   4011  C  CB  . ALA D  1 99  ? 94.333  86.018  70.681 1.00 26.43  ? 93  ALA D CB  1 
ATOM   4012  N  N   . VAL D  1 100 ? 95.900  85.786  67.417 1.00 22.40  ? 94  VAL D N   1 
ATOM   4013  C  CA  . VAL D  1 100 ? 96.262  86.619  66.288 1.00 21.99  ? 94  VAL D CA  1 
ATOM   4014  C  C   . VAL D  1 100 ? 95.887  85.904  64.987 1.00 28.95  ? 94  VAL D C   1 
ATOM   4015  O  O   . VAL D  1 100 ? 96.076  84.691  64.837 1.00 27.21  ? 94  VAL D O   1 
ATOM   4016  C  CB  . VAL D  1 100 ? 97.784  86.918  66.263 1.00 28.50  ? 94  VAL D CB  1 
ATOM   4017  C  CG1 . VAL D  1 100 ? 98.143  87.723  65.000 1.00 22.96  ? 94  VAL D CG1 1 
ATOM   4018  C  CG2 . VAL D  1 100 ? 98.188  87.693  67.523 1.00 24.43  ? 94  VAL D CG2 1 
ATOM   4019  N  N   . ALA D  1 101 ? 95.336  86.660  64.048 1.00 21.50  ? 95  ALA D N   1 
ATOM   4020  C  CA  . ALA D  1 101 ? 94.991  86.095  62.770 1.00 19.95  ? 95  ALA D CA  1 
ATOM   4021  C  C   . ALA D  1 101 ? 95.932  86.688  61.744 1.00 23.47  ? 95  ALA D C   1 
ATOM   4022  O  O   . ALA D  1 101 ? 95.894  87.893  61.469 1.00 25.33  ? 95  ALA D O   1 
ATOM   4023  C  CB  . ALA D  1 101 ? 93.562  86.413  62.413 1.00 18.22  ? 95  ALA D CB  1 
ATOM   4024  N  N   . ASP D  1 102 ? 96.812  85.846  61.215 1.00 24.67  ? 96  ASP D N   1 
ATOM   4025  C  CA  . ASP D  1 102 ? 97.728  86.281  60.176 1.00 23.41  ? 96  ASP D CA  1 
ATOM   4026  C  C   . ASP D  1 102 ? 96.897  86.078  58.930 1.00 25.48  ? 96  ASP D C   1 
ATOM   4027  O  O   . ASP D  1 102 ? 96.453  84.978  58.644 1.00 30.31  ? 96  ASP D O   1 
ATOM   4028  C  CB  . ASP D  1 102 ? 98.977  85.408  60.174 1.00 26.74  ? 96  ASP D CB  1 
ATOM   4029  C  CG  . ASP D  1 102 ? 99.808  85.585  61.447 1.00 38.72  ? 96  ASP D CG  1 
ATOM   4030  O  OD1 . ASP D  1 102 ? 99.953  84.588  62.190 1.00 35.13  ? 96  ASP D OD1 1 
ATOM   4031  O  OD2 . ASP D  1 102 ? 100.305 86.720  61.703 1.00 30.60  ? 96  ASP D OD2 1 
ATOM   4032  N  N   . VAL D  1 103 ? 96.644  87.152  58.209 1.00 25.51  ? 97  VAL D N   1 
ATOM   4033  C  CA  . VAL D  1 103 ? 95.810  87.060  57.026 1.00 21.66  ? 97  VAL D CA  1 
ATOM   4034  C  C   . VAL D  1 103 ? 96.576  87.048  55.712 1.00 28.23  ? 97  VAL D C   1 
ATOM   4035  O  O   . VAL D  1 103 ? 97.427  87.904  55.462 1.00 28.62  ? 97  VAL D O   1 
ATOM   4036  C  CB  . VAL D  1 103 ? 94.808  88.239  57.009 1.00 22.14  ? 97  VAL D CB  1 
ATOM   4037  C  CG1 . VAL D  1 103 ? 93.997  88.251  55.713 1.00 12.28  ? 97  VAL D CG1 1 
ATOM   4038  C  CG2 . VAL D  1 103 ? 93.902  88.149  58.235 1.00 16.51  ? 97  VAL D CG2 1 
ATOM   4039  N  N   . SER D  1 104 ? 96.280  86.059  54.879 1.00 26.09  ? 98  SER D N   1 
ATOM   4040  C  CA  . SER D  1 104 ? 96.880  85.991  53.564 1.00 24.22  ? 98  SER D CA  1 
ATOM   4041  C  C   . SER D  1 104 ? 95.862  85.384  52.615 1.00 25.59  ? 98  SER D C   1 
ATOM   4042  O  O   . SER D  1 104 ? 95.634  84.178  52.587 1.00 18.59  ? 98  SER D O   1 
ATOM   4043  C  CB  . SER D  1 104 ? 98.162  85.169  53.552 1.00 23.69  ? 98  SER D CB  1 
ATOM   4044  O  OG  . SER D  1 104 ? 98.874  85.482  52.363 1.00 26.36  ? 98  SER D OG  1 
ATOM   4045  N  N   . ILE D  1 105 ? 95.248  86.251  51.832 1.00 21.23  ? 99  ILE D N   1 
ATOM   4046  C  CA  . ILE D  1 105 ? 94.238  85.847  50.886 1.00 20.45  ? 99  ILE D CA  1 
ATOM   4047  C  C   . ILE D  1 105 ? 94.519  86.415  49.497 1.00 21.31  ? 99  ILE D C   1 
ATOM   4048  O  O   . ILE D  1 105 ? 95.207  87.425  49.333 1.00 21.91  ? 99  ILE D O   1 
ATOM   4049  C  CB  . ILE D  1 105 ? 92.870  86.381  51.344 1.00 17.70  ? 99  ILE D CB  1 
ATOM   4050  C  CG1 . ILE D  1 105 ? 92.393  85.620  52.580 1.00 19.83  ? 99  ILE D CG1 1 
ATOM   4051  C  CG2 . ILE D  1 105 ? 91.849  86.323  50.191 1.00 20.40  ? 99  ILE D CG2 1 
ATOM   4052  C  CD1 . ILE D  1 105 ? 91.174  86.299  53.227 1.00 6.85   ? 99  ILE D CD1 1 
ATOM   4053  N  N   . GLU D  1 106 ? 93.979  85.756  48.488 1.00 26.38  ? 100 GLU D N   1 
ATOM   4054  C  CA  . GLU D  1 106 ? 94.115  86.255  47.134 1.00 31.65  ? 100 GLU D CA  1 
ATOM   4055  C  C   . GLU D  1 106 ? 92.721  86.097  46.544 1.00 30.83  ? 100 GLU D C   1 
ATOM   4056  O  O   . GLU D  1 106 ? 92.146  84.991  46.559 1.00 20.22  ? 100 GLU D O   1 
ATOM   4057  C  CB  . GLU D  1 106 ? 95.144  85.458  46.343 1.00 32.91  ? 100 GLU D CB  1 
ATOM   4058  C  CG  . GLU D  1 106 ? 95.388  86.063  44.980 1.00 54.48  ? 100 GLU D CG  1 
ATOM   4059  C  CD  . GLU D  1 106 ? 96.558  85.438  44.259 1.00 59.06  ? 100 GLU D CD  1 
ATOM   4060  O  OE1 . GLU D  1 106 ? 97.654  85.359  44.861 1.00 65.13  ? 100 GLU D OE1 1 
ATOM   4061  O  OE2 . GLU D  1 106 ? 96.383  85.039  43.091 1.00 60.53  ? 100 GLU D OE2 1 
ATOM   4062  N  N   . ASP D  1 107 ? 92.165  87.201  46.050 1.00 22.45  ? 101 ASP D N   1 
ATOM   4063  C  CA  . ASP D  1 107 ? 90.813  87.167  45.505 1.00 20.75  ? 101 ASP D CA  1 
ATOM   4064  C  C   . ASP D  1 107 ? 90.742  87.876  44.175 1.00 22.22  ? 101 ASP D C   1 
ATOM   4065  O  O   . ASP D  1 107 ? 91.354  88.917  44.017 1.00 22.08  ? 101 ASP D O   1 
ATOM   4066  C  CB  . ASP D  1 107 ? 89.851  87.838  46.472 1.00 27.54  ? 101 ASP D CB  1 
ATOM   4067  C  CG  . ASP D  1 107 ? 88.416  87.523  46.157 1.00 29.42  ? 101 ASP D CG  1 
ATOM   4068  O  OD1 . ASP D  1 107 ? 87.695  88.409  45.635 1.00 30.59  ? 101 ASP D OD1 1 
ATOM   4069  O  OD2 . ASP D  1 107 ? 88.024  86.371  46.433 1.00 32.16  ? 101 ASP D OD2 1 
ATOM   4070  N  N   . SER D  1 108 ? 89.969  87.330  43.237 1.00 25.33  ? 102 SER D N   1 
ATOM   4071  C  CA  . SER D  1 108 ? 89.853  87.913  41.898 1.00 31.18  ? 102 SER D CA  1 
ATOM   4072  C  C   . SER D  1 108 ? 88.512  88.560  41.609 1.00 26.28  ? 102 SER D C   1 
ATOM   4073  O  O   . SER D  1 108 ? 88.253  88.950  40.478 1.00 32.21  ? 102 SER D O   1 
ATOM   4074  C  CB  . SER D  1 108 ? 90.112  86.846  40.829 1.00 32.96  ? 102 SER D CB  1 
ATOM   4075  O  OG  . SER D  1 108 ? 91.325  86.152  41.071 1.00 50.75  ? 102 SER D OG  1 
ATOM   4076  N  N   . VAL D  1 109 ? 87.649  88.662  42.608 1.00 24.40  ? 103 VAL D N   1 
ATOM   4077  C  CA  . VAL D  1 109 ? 86.343  89.285  42.391 1.00 24.34  ? 103 VAL D CA  1 
ATOM   4078  C  C   . VAL D  1 109 ? 86.365  90.719  42.920 1.00 24.86  ? 103 VAL D C   1 
ATOM   4079  O  O   . VAL D  1 109 ? 85.790  91.620  42.314 1.00 27.07  ? 103 VAL D O   1 
ATOM   4080  C  CB  . VAL D  1 109 ? 85.225  88.454  43.049 1.00 27.74  ? 103 VAL D CB  1 
ATOM   4081  C  CG1 . VAL D  1 109 ? 83.884  89.164  42.931 1.00 21.60  ? 103 VAL D CG1 1 
ATOM   4082  C  CG2 . VAL D  1 109 ? 85.168  87.088  42.377 1.00 16.30  ? 103 VAL D CG2 1 
ATOM   4083  N  N   . ILE D  1 110 ? 87.026  90.943  44.050 1.00 25.57  ? 104 ILE D N   1 
ATOM   4084  C  CA  . ILE D  1 110 ? 87.138  92.308  44.532 1.00 26.07  ? 104 ILE D CA  1 
ATOM   4085  C  C   . ILE D  1 110 ? 88.185  92.934  43.609 1.00 26.59  ? 104 ILE D C   1 
ATOM   4086  O  O   . ILE D  1 110 ? 88.907  92.227  42.893 1.00 25.47  ? 104 ILE D O   1 
ATOM   4087  C  CB  . ILE D  1 110 ? 87.697  92.399  45.967 1.00 20.85  ? 104 ILE D CB  1 
ATOM   4088  C  CG1 . ILE D  1 110 ? 89.016  91.633  46.058 1.00 20.38  ? 104 ILE D CG1 1 
ATOM   4089  C  CG2 . ILE D  1 110 ? 86.690  91.892  46.968 1.00 20.14  ? 104 ILE D CG2 1 
ATOM   4090  C  CD1 . ILE D  1 110 ? 89.721  91.804  47.404 1.00 16.38  ? 104 ILE D CD1 1 
ATOM   4091  N  N   . SER D  1 111 ? 88.281  94.253  43.630 1.00 25.18  ? 105 SER D N   1 
ATOM   4092  C  CA  . SER D  1 111 ? 89.283  94.936  42.827 1.00 23.78  ? 105 SER D CA  1 
ATOM   4093  C  C   . SER D  1 111 ? 89.573  96.300  43.419 1.00 26.15  ? 105 SER D C   1 
ATOM   4094  O  O   . SER D  1 111 ? 88.793  96.819  44.227 1.00 22.16  ? 105 SER D O   1 
ATOM   4095  C  CB  . SER D  1 111 ? 88.804  95.117  41.387 1.00 21.51  ? 105 SER D CB  1 
ATOM   4096  O  OG  . SER D  1 111 ? 89.824  95.720  40.612 1.00 34.83  ? 105 SER D OG  1 
ATOM   4097  N  N   . LEU D  1 112 ? 90.695  96.881  43.006 1.00 25.59  ? 106 LEU D N   1 
ATOM   4098  C  CA  . LEU D  1 112 ? 91.066  98.195  43.476 1.00 33.22  ? 106 LEU D CA  1 
ATOM   4099  C  C   . LEU D  1 112 ? 90.630  99.254  42.451 1.00 34.70  ? 106 LEU D C   1 
ATOM   4100  O  O   . LEU D  1 112 ? 91.002  100.425 42.541 1.00 36.60  ? 106 LEU D O   1 
ATOM   4101  C  CB  . LEU D  1 112 ? 92.575  98.240  43.756 1.00 31.60  ? 106 LEU D CB  1 
ATOM   4102  C  CG  . LEU D  1 112 ? 93.027  97.326  44.913 1.00 29.03  ? 106 LEU D CG  1 
ATOM   4103  C  CD1 . LEU D  1 112 ? 94.450  97.665  45.330 1.00 23.64  ? 106 LEU D CD1 1 
ATOM   4104  C  CD2 . LEU D  1 112 ? 92.098  97.482  46.108 1.00 17.19  ? 106 LEU D CD2 1 
ATOM   4105  N  N   . SER D  1 113 ? 89.819  98.832  41.483 1.00 34.26  ? 107 SER D N   1 
ATOM   4106  C  CA  . SER D  1 113 ? 89.297  99.742  40.461 1.00 37.44  ? 107 SER D CA  1 
ATOM   4107  C  C   . SER D  1 113 ? 88.123  99.108  39.737 1.00 38.53  ? 107 SER D C   1 
ATOM   4108  O  O   . SER D  1 113 ? 87.956  97.892  39.746 1.00 40.71  ? 107 SER D O   1 
ATOM   4109  C  CB  . SER D  1 113 ? 90.377  100.099 39.435 1.00 37.05  ? 107 SER D CB  1 
ATOM   4110  O  OG  . SER D  1 113 ? 90.655  98.998  38.591 1.00 37.36  ? 107 SER D OG  1 
ATOM   4111  N  N   . GLY D  1 114 ? 87.305  99.935  39.106 1.00 41.05  ? 108 GLY D N   1 
ATOM   4112  C  CA  . GLY D  1 114 ? 86.172  99.401  38.381 1.00 37.96  ? 108 GLY D CA  1 
ATOM   4113  C  C   . GLY D  1 114 ? 84.923  99.295  39.225 1.00 44.62  ? 108 GLY D C   1 
ATOM   4114  O  O   . GLY D  1 114 ? 84.840  99.868  40.314 1.00 44.29  ? 108 GLY D O   1 
ATOM   4115  N  N   . ASP D  1 115 ? 83.947  98.556  38.707 1.00 40.68  ? 109 ASP D N   1 
ATOM   4116  C  CA  . ASP D  1 115 ? 82.664  98.356  39.370 1.00 42.58  ? 109 ASP D CA  1 
ATOM   4117  C  C   . ASP D  1 115 ? 82.792  97.628  40.695 1.00 37.53  ? 109 ASP D C   1 
ATOM   4118  O  O   . ASP D  1 115 ? 81.922  97.726  41.546 1.00 35.42  ? 109 ASP D O   1 
ATOM   4119  C  CB  . ASP D  1 115 ? 81.724  97.539  38.467 1.00 47.70  ? 109 ASP D CB  1 
ATOM   4120  C  CG  . ASP D  1 115 ? 81.135  98.353  37.337 1.00 50.60  ? 109 ASP D CG  1 
ATOM   4121  O  OD1 . ASP D  1 115 ? 80.314  97.790  36.579 1.00 52.03  ? 109 ASP D OD1 1 
ATOM   4122  O  OD2 . ASP D  1 115 ? 81.484  99.547  37.210 1.00 51.10  ? 109 ASP D OD2 1 
ATOM   4123  N  N   . HIS D  1 116 ? 83.880  96.885  40.840 1.00 36.82  ? 110 HIS D N   1 
ATOM   4124  C  CA  . HIS D  1 116 ? 84.136  96.087  42.020 1.00 36.60  ? 110 HIS D CA  1 
ATOM   4125  C  C   . HIS D  1 116 ? 85.157  96.695  42.975 1.00 35.85  ? 110 HIS D C   1 
ATOM   4126  O  O   . HIS D  1 116 ? 85.612  96.012  43.885 1.00 36.07  ? 110 HIS D O   1 
ATOM   4127  C  CB  . HIS D  1 116 ? 84.631  94.701  41.593 1.00 38.72  ? 110 HIS D CB  1 
ATOM   4128  C  CG  . HIS D  1 116 ? 83.620  93.894  40.839 1.00 45.86  ? 110 HIS D CG  1 
ATOM   4129  N  ND1 . HIS D  1 116 ? 83.941  92.720  40.189 1.00 47.02  ? 110 HIS D ND1 1 
ATOM   4130  C  CD2 . HIS D  1 116 ? 82.288  94.072  40.657 1.00 46.03  ? 110 HIS D CD2 1 
ATOM   4131  C  CE1 . HIS D  1 116 ? 82.852  92.210  39.641 1.00 38.33  ? 110 HIS D CE1 1 
ATOM   4132  N  NE2 . HIS D  1 116 ? 81.835  93.011  39.909 1.00 32.24  ? 110 HIS D NE2 1 
ATOM   4133  N  N   . CYS D  1 117 ? 85.529  97.958  42.772 1.00 31.56  ? 111 CYS D N   1 
ATOM   4134  C  CA  . CYS D  1 117 ? 86.516  98.606  43.642 1.00 28.82  ? 111 CYS D CA  1 
ATOM   4135  C  C   . CYS D  1 117 ? 86.042  98.532  45.099 1.00 27.28  ? 111 CYS D C   1 
ATOM   4136  O  O   . CYS D  1 117 ? 84.887  98.797  45.396 1.00 22.49  ? 111 CYS D O   1 
ATOM   4137  C  CB  . CYS D  1 117 ? 86.688  100.069 43.234 1.00 27.41  ? 111 CYS D CB  1 
ATOM   4138  S  SG  . CYS D  1 117 ? 88.114  100.957 43.914 1.00 41.89  ? 111 CYS D SG  1 
ATOM   4139  N  N   . ILE D  1 118 ? 86.918  98.152  46.012 1.00 24.91  ? 112 ILE D N   1 
ATOM   4140  C  CA  . ILE D  1 118 ? 86.508  98.103  47.410 1.00 29.40  ? 112 ILE D CA  1 
ATOM   4141  C  C   . ILE D  1 118 ? 87.058  99.311  48.147 1.00 29.19  ? 112 ILE D C   1 
ATOM   4142  O  O   . ILE D  1 118 ? 86.844  99.459  49.354 1.00 31.13  ? 112 ILE D O   1 
ATOM   4143  C  CB  . ILE D  1 118 ? 87.003  96.823  48.103 1.00 29.73  ? 112 ILE D CB  1 
ATOM   4144  C  CG1 . ILE D  1 118 ? 88.511  96.668  47.877 1.00 16.24  ? 112 ILE D CG1 1 
ATOM   4145  C  CG2 . ILE D  1 118 ? 86.202  95.628  47.595 1.00 22.83  ? 112 ILE D CG2 1 
ATOM   4146  C  CD1 . ILE D  1 118 ? 89.111  95.416  48.487 1.00 23.09  ? 112 ILE D CD1 1 
ATOM   4147  N  N   . ILE D  1 119 ? 87.763  100.176 47.416 1.00 24.99  ? 113 ILE D N   1 
ATOM   4148  C  CA  . ILE D  1 119 ? 88.330  101.384 48.011 1.00 23.58  ? 113 ILE D CA  1 
ATOM   4149  C  C   . ILE D  1 119 ? 87.203  102.319 48.416 1.00 19.99  ? 113 ILE D C   1 
ATOM   4150  O  O   . ILE D  1 119 ? 86.249  102.521 47.666 1.00 23.91  ? 113 ILE D O   1 
ATOM   4151  C  CB  . ILE D  1 119 ? 89.233  102.147 47.039 1.00 21.26  ? 113 ILE D CB  1 
ATOM   4152  C  CG1 . ILE D  1 119 ? 90.535  101.394 46.810 1.00 22.34  ? 113 ILE D CG1 1 
ATOM   4153  C  CG2 . ILE D  1 119 ? 89.552  103.489 47.607 1.00 25.40  ? 113 ILE D CG2 1 
ATOM   4154  C  CD1 . ILE D  1 119 ? 91.451  102.114 45.842 1.00 31.61  ? 113 ILE D CD1 1 
ATOM   4155  N  N   . GLY D  1 120 ? 87.317  102.902 49.599 1.00 16.96  ? 114 GLY D N   1 
ATOM   4156  C  CA  . GLY D  1 120 ? 86.267  103.785 50.062 1.00 20.12  ? 114 GLY D CA  1 
ATOM   4157  C  C   . GLY D  1 120 ? 85.116  103.028 50.707 1.00 21.01  ? 114 GLY D C   1 
ATOM   4158  O  O   . GLY D  1 120 ? 84.075  103.607 51.025 1.00 25.57  ? 114 GLY D O   1 
ATOM   4159  N  N   . ARG D  1 121 ? 85.299  101.728 50.896 1.00 20.90  ? 115 ARG D N   1 
ATOM   4160  C  CA  . ARG D  1 121 ? 84.285  100.905 51.531 1.00 23.76  ? 115 ARG D CA  1 
ATOM   4161  C  C   . ARG D  1 121 ? 84.872  100.367 52.834 1.00 21.91  ? 115 ARG D C   1 
ATOM   4162  O  O   . ARG D  1 121 ? 86.034  100.631 53.146 1.00 27.62  ? 115 ARG D O   1 
ATOM   4163  C  CB  . ARG D  1 121 ? 83.853  99.790  50.575 1.00 29.36  ? 115 ARG D CB  1 
ATOM   4164  C  CG  . ARG D  1 121 ? 83.247  100.361 49.283 1.00 31.12  ? 115 ARG D CG  1 
ATOM   4165  C  CD  . ARG D  1 121 ? 82.563  99.311  48.397 1.00 35.36  ? 115 ARG D CD  1 
ATOM   4166  N  NE  . ARG D  1 121 ? 82.158  99.878  47.110 1.00 36.08  ? 115 ARG D NE  1 
ATOM   4167  C  CZ  . ARG D  1 121 ? 81.029  100.549 46.880 1.00 28.35  ? 115 ARG D CZ  1 
ATOM   4168  N  NH1 . ARG D  1 121 ? 80.789  101.022 45.675 1.00 28.27  ? 115 ARG D NH1 1 
ATOM   4169  N  NH2 . ARG D  1 121 ? 80.126  100.725 47.832 1.00 28.05  ? 115 ARG D NH2 1 
ATOM   4170  N  N   . THR D  1 122 ? 84.088  99.619  53.602 1.00 20.17  ? 116 THR D N   1 
ATOM   4171  C  CA  . THR D  1 122 ? 84.566  99.132  54.890 1.00 20.16  ? 116 THR D CA  1 
ATOM   4172  C  C   . THR D  1 122 ? 84.892  97.651  54.980 1.00 24.04  ? 116 THR D C   1 
ATOM   4173  O  O   . THR D  1 122 ? 84.142  96.807  54.474 1.00 25.40  ? 116 THR D O   1 
ATOM   4174  C  CB  . THR D  1 122 ? 83.533  99.465  56.001 1.00 23.49  ? 116 THR D CB  1 
ATOM   4175  O  OG1 . THR D  1 122 ? 83.349  100.883 56.061 1.00 19.65  ? 116 THR D OG1 1 
ATOM   4176  C  CG2 . THR D  1 122 ? 83.994  98.934  57.379 1.00 14.22  ? 116 THR D CG2 1 
ATOM   4177  N  N   . LEU D  1 123 ? 86.022  97.343  55.618 1.00 21.72  ? 117 LEU D N   1 
ATOM   4178  C  CA  . LEU D  1 123 ? 86.420  95.954  55.840 1.00 17.82  ? 117 LEU D CA  1 
ATOM   4179  C  C   . LEU D  1 123 ? 85.936  95.664  57.258 1.00 17.68  ? 117 LEU D C   1 
ATOM   4180  O  O   . LEU D  1 123 ? 86.051  96.509  58.151 1.00 17.57  ? 117 LEU D O   1 
ATOM   4181  C  CB  . LEU D  1 123 ? 87.932  95.793  55.753 1.00 21.25  ? 117 LEU D CB  1 
ATOM   4182  C  CG  . LEU D  1 123 ? 88.446  94.351  55.927 1.00 27.42  ? 117 LEU D CG  1 
ATOM   4183  C  CD1 . LEU D  1 123 ? 87.962  93.451  54.775 1.00 18.12  ? 117 LEU D CD1 1 
ATOM   4184  C  CD2 . LEU D  1 123 ? 89.974  94.374  55.977 1.00 14.43  ? 117 LEU D CD2 1 
ATOM   4185  N  N   . VAL D  1 124 ? 85.381  94.482  57.472 1.00 19.36  ? 118 VAL D N   1 
ATOM   4186  C  CA  . VAL D  1 124 ? 84.842  94.132  58.781 1.00 14.09  ? 118 VAL D CA  1 
ATOM   4187  C  C   . VAL D  1 124 ? 85.258  92.736  59.190 1.00 22.21  ? 118 VAL D C   1 
ATOM   4188  O  O   . VAL D  1 124 ? 85.105  91.806  58.407 1.00 20.61  ? 118 VAL D O   1 
ATOM   4189  C  CB  . VAL D  1 124 ? 83.311  94.120  58.747 1.00 20.52  ? 118 VAL D CB  1 
ATOM   4190  C  CG1 . VAL D  1 124 ? 82.767  93.716  60.109 1.00 17.48  ? 118 VAL D CG1 1 
ATOM   4191  C  CG2 . VAL D  1 124 ? 82.770  95.484  58.283 1.00 18.94  ? 118 VAL D CG2 1 
ATOM   4192  N  N   . VAL D  1 125 ? 85.801  92.576  60.395 1.00 19.73  ? 119 VAL D N   1 
ATOM   4193  C  CA  . VAL D  1 125 ? 86.129  91.235  60.840 1.00 13.26  ? 119 VAL D CA  1 
ATOM   4194  C  C   . VAL D  1 125 ? 85.019  90.866  61.834 1.00 16.67  ? 119 VAL D C   1 
ATOM   4195  O  O   . VAL D  1 125 ? 84.722  91.611  62.782 1.00 12.83  ? 119 VAL D O   1 
ATOM   4196  C  CB  . VAL D  1 125 ? 87.540  91.133  61.486 1.00 20.74  ? 119 VAL D CB  1 
ATOM   4197  C  CG1 . VAL D  1 125 ? 87.627  91.965  62.773 1.00 12.41  ? 119 VAL D CG1 1 
ATOM   4198  C  CG2 . VAL D  1 125 ? 87.854  89.644  61.765 1.00 9.47   ? 119 VAL D CG2 1 
ATOM   4199  N  N   . HIS D  1 126 ? 84.373  89.734  61.576 1.00 17.82  ? 120 HIS D N   1 
ATOM   4200  C  CA  . HIS D  1 126 ? 83.261  89.284  62.392 1.00 17.64  ? 120 HIS D CA  1 
ATOM   4201  C  C   . HIS D  1 126 ? 83.544  88.390  63.595 1.00 18.68  ? 120 HIS D C   1 
ATOM   4202  O  O   . HIS D  1 126 ? 84.607  87.795  63.732 1.00 20.81  ? 120 HIS D O   1 
ATOM   4203  C  CB  . HIS D  1 126 ? 82.221  88.646  61.487 1.00 18.60  ? 120 HIS D CB  1 
ATOM   4204  C  CG  . HIS D  1 126 ? 81.559  89.624  60.569 1.00 20.01  ? 120 HIS D CG  1 
ATOM   4205  N  ND1 . HIS D  1 126 ? 80.337  90.202  60.851 1.00 21.57  ? 120 HIS D ND1 1 
ATOM   4206  C  CD2 . HIS D  1 126 ? 81.941  90.115  59.367 1.00 17.39  ? 120 HIS D CD2 1 
ATOM   4207  C  CE1 . HIS D  1 126 ? 79.992  91.002  59.855 1.00 16.36  ? 120 HIS D CE1 1 
ATOM   4208  N  NE2 . HIS D  1 126 ? 80.947  90.966  58.940 1.00 21.07  ? 120 HIS D NE2 1 
ATOM   4209  N  N   . GLU D  1 127 ? 82.559  88.337  64.479 1.00 25.46  ? 121 GLU D N   1 
ATOM   4210  C  CA  . GLU D  1 127 ? 82.621  87.575  65.713 1.00 26.29  ? 121 GLU D CA  1 
ATOM   4211  C  C   . GLU D  1 127 ? 82.665  86.074  65.517 1.00 23.85  ? 121 GLU D C   1 
ATOM   4212  O  O   . GLU D  1 127 ? 83.366  85.369  66.229 1.00 25.78  ? 121 GLU D O   1 
ATOM   4213  C  CB  . GLU D  1 127 ? 81.410  87.927  66.557 1.00 26.49  ? 121 GLU D CB  1 
ATOM   4214  C  CG  . GLU D  1 127 ? 81.346  87.249  67.897 1.00 46.18  ? 121 GLU D CG  1 
ATOM   4215  C  CD  . GLU D  1 127 ? 79.908  87.100  68.384 1.00 63.21  ? 121 GLU D CD  1 
ATOM   4216  O  OE1 . GLU D  1 127 ? 79.726  86.631  69.529 1.00 64.31  ? 121 GLU D OE1 1 
ATOM   4217  O  OE2 . GLU D  1 127 ? 78.962  87.438  67.619 1.00 61.49  ? 121 GLU D OE2 1 
ATOM   4218  N  N   . LYS D  1 128 ? 81.912  85.587  64.546 1.00 25.00  ? 122 LYS D N   1 
ATOM   4219  C  CA  . LYS D  1 128 ? 81.824  84.155  64.292 1.00 25.10  ? 122 LYS D CA  1 
ATOM   4220  C  C   . LYS D  1 128 ? 82.343  83.762  62.922 1.00 23.53  ? 122 LYS D C   1 
ATOM   4221  O  O   . LYS D  1 128 ? 82.740  84.607  62.124 1.00 24.04  ? 122 LYS D O   1 
ATOM   4222  C  CB  . LYS D  1 128 ? 80.363  83.696  64.378 1.00 24.23  ? 122 LYS D CB  1 
ATOM   4223  C  CG  . LYS D  1 128 ? 79.587  84.093  65.627 1.00 33.61  ? 122 LYS D CG  1 
ATOM   4224  C  CD  . LYS D  1 128 ? 78.119  83.680  65.432 1.00 51.96  ? 122 LYS D CD  1 
ATOM   4225  C  CE  . LYS D  1 128 ? 77.212  84.077  66.586 1.00 60.16  ? 122 LYS D CE  1 
ATOM   4226  N  NZ  . LYS D  1 128 ? 75.806  83.618  66.362 1.00 59.73  ? 122 LYS D NZ  1 
ATOM   4227  N  N   . ALA D  1 129 ? 82.304  82.463  62.655 1.00 19.72  ? 123 ALA D N   1 
ATOM   4228  C  CA  . ALA D  1 129 ? 82.731  81.928  61.383 1.00 25.94  ? 123 ALA D CA  1 
ATOM   4229  C  C   . ALA D  1 129 ? 81.633  82.172  60.360 1.00 26.19  ? 123 ALA D C   1 
ATOM   4230  O  O   . ALA D  1 129 ? 80.451  82.154  60.686 1.00 19.86  ? 123 ALA D O   1 
ATOM   4231  C  CB  . ALA D  1 129 ? 82.974  80.456  61.498 1.00 14.03  ? 123 ALA D CB  1 
ATOM   4232  N  N   . ASP D  1 130 ? 82.049  82.399  59.122 1.00 22.34  ? 124 ASP D N   1 
ATOM   4233  C  CA  . ASP D  1 130 ? 81.144  82.614  58.010 1.00 21.59  ? 124 ASP D CA  1 
ATOM   4234  C  C   . ASP D  1 130 ? 80.851  81.201  57.502 1.00 22.66  ? 124 ASP D C   1 
ATOM   4235  O  O   . ASP D  1 130 ? 81.785  80.470  57.157 1.00 22.50  ? 124 ASP D O   1 
ATOM   4236  C  CB  . ASP D  1 130 ? 81.869  83.452  56.947 1.00 21.66  ? 124 ASP D CB  1 
ATOM   4237  C  CG  . ASP D  1 130 ? 81.021  83.735  55.723 1.00 21.88  ? 124 ASP D CG  1 
ATOM   4238  O  OD1 . ASP D  1 130 ? 81.382  84.672  54.989 1.00 25.61  ? 124 ASP D OD1 1 
ATOM   4239  O  OD2 . ASP D  1 130 ? 80.020  83.029  55.482 1.00 20.11  ? 124 ASP D OD2 1 
ATOM   4240  N  N   . ASP D  1 131 ? 79.576  80.810  57.476 1.00 16.35  ? 125 ASP D N   1 
ATOM   4241  C  CA  . ASP D  1 131 ? 79.195  79.472  57.010 1.00 16.15  ? 125 ASP D CA  1 
ATOM   4242  C  C   . ASP D  1 131 ? 79.168  79.409  55.482 1.00 17.26  ? 125 ASP D C   1 
ATOM   4243  O  O   . ASP D  1 131 ? 78.737  78.426  54.887 1.00 20.19  ? 125 ASP D O   1 
ATOM   4244  C  CB  . ASP D  1 131 ? 77.826  79.041  57.602 1.00 13.04  ? 125 ASP D CB  1 
ATOM   4245  C  CG  . ASP D  1 131 ? 76.633  79.851  57.044 1.00 18.94  ? 125 ASP D CG  1 
ATOM   4246  O  OD1 . ASP D  1 131 ? 75.528  79.750  57.623 1.00 19.95  ? 125 ASP D OD1 1 
ATOM   4247  O  OD2 . ASP D  1 131 ? 76.784  80.577  56.034 1.00 18.43  ? 125 ASP D OD2 1 
ATOM   4248  N  N   . LEU D  1 132 ? 79.624  80.479  54.851 1.00 19.99  ? 126 LEU D N   1 
ATOM   4249  C  CA  . LEU D  1 132 ? 79.710  80.537  53.393 1.00 22.93  ? 126 LEU D CA  1 
ATOM   4250  C  C   . LEU D  1 132 ? 78.407  80.250  52.665 1.00 19.00  ? 126 LEU D C   1 
ATOM   4251  O  O   . LEU D  1 132 ? 78.415  79.749  51.540 1.00 22.62  ? 126 LEU D O   1 
ATOM   4252  C  CB  . LEU D  1 132 ? 80.798  79.575  52.902 1.00 21.64  ? 126 LEU D CB  1 
ATOM   4253  C  CG  . LEU D  1 132 ? 82.058  79.533  53.797 1.00 32.96  ? 126 LEU D CG  1 
ATOM   4254  C  CD1 . LEU D  1 132 ? 82.997  78.428  53.320 1.00 28.73  ? 126 LEU D CD1 1 
ATOM   4255  C  CD2 . LEU D  1 132 ? 82.772  80.877  53.795 1.00 26.31  ? 126 LEU D CD2 1 
ATOM   4256  N  N   . GLY D  1 133 ? 77.295  80.595  53.302 1.00 19.63  ? 127 GLY D N   1 
ATOM   4257  C  CA  . GLY D  1 133 ? 75.988  80.407  52.703 1.00 14.68  ? 127 GLY D CA  1 
ATOM   4258  C  C   . GLY D  1 133 ? 75.497  78.975  52.689 1.00 21.40  ? 127 GLY D C   1 
ATOM   4259  O  O   . GLY D  1 133 ? 74.558  78.635  51.966 1.00 18.15  ? 127 GLY D O   1 
ATOM   4260  N  N   . LYS D  1 134 ? 76.109  78.118  53.491 1.00 16.97  ? 128 LYS D N   1 
ATOM   4261  C  CA  . LYS D  1 134 ? 75.689  76.727  53.497 1.00 22.53  ? 128 LYS D CA  1 
ATOM   4262  C  C   . LYS D  1 134 ? 74.937  76.411  54.776 1.00 22.82  ? 128 LYS D C   1 
ATOM   4263  O  O   . LYS D  1 134 ? 74.815  75.242  55.165 1.00 24.42  ? 128 LYS D O   1 
ATOM   4264  C  CB  . LYS D  1 134 ? 76.921  75.824  53.330 1.00 18.26  ? 128 LYS D CB  1 
ATOM   4265  C  CG  . LYS D  1 134 ? 77.618  76.060  51.972 1.00 27.20  ? 128 LYS D CG  1 
ATOM   4266  C  CD  . LYS D  1 134 ? 79.019  75.461  51.905 1.00 39.32  ? 128 LYS D CD  1 
ATOM   4267  C  CE  . LYS D  1 134 ? 79.020  73.947  52.024 1.00 42.62  ? 128 LYS D CE  1 
ATOM   4268  N  NZ  . LYS D  1 134 ? 80.397  73.395  51.884 1.00 48.43  ? 128 LYS D NZ  1 
ATOM   4269  N  N   . GLY D  1 135 ? 74.416  77.466  55.405 1.00 18.57  ? 129 GLY D N   1 
ATOM   4270  C  CA  . GLY D  1 135 ? 73.709  77.328  56.668 1.00 19.52  ? 129 GLY D CA  1 
ATOM   4271  C  C   . GLY D  1 135 ? 72.247  76.935  56.593 1.00 26.71  ? 129 GLY D C   1 
ATOM   4272  O  O   . GLY D  1 135 ? 71.680  76.478  57.596 1.00 20.13  ? 129 GLY D O   1 
ATOM   4273  N  N   . GLY D  1 136 ? 71.620  77.143  55.432 1.00 21.09  ? 130 GLY D N   1 
ATOM   4274  C  CA  . GLY D  1 136 ? 70.223  76.767  55.281 1.00 20.19  ? 130 GLY D CA  1 
ATOM   4275  C  C   . GLY D  1 136 ? 69.165  77.671  55.892 1.00 25.04  ? 130 GLY D C   1 
ATOM   4276  O  O   . GLY D  1 136 ? 67.977  77.345  55.844 1.00 28.00  ? 130 GLY D O   1 
ATOM   4277  N  N   . ASN D  1 137 ? 69.559  78.789  56.491 1.00 26.90  ? 131 ASN D N   1 
ATOM   4278  C  CA  . ASN D  1 137 ? 68.554  79.699  57.030 1.00 30.21  ? 131 ASN D CA  1 
ATOM   4279  C  C   . ASN D  1 137 ? 68.664  80.993  56.256 1.00 31.94  ? 131 ASN D C   1 
ATOM   4280  O  O   . ASN D  1 137 ? 69.591  81.154  55.460 1.00 39.80  ? 131 ASN D O   1 
ATOM   4281  C  CB  . ASN D  1 137 ? 68.713  79.913  58.544 1.00 26.12  ? 131 ASN D CB  1 
ATOM   4282  C  CG  . ASN D  1 137 ? 69.979  80.635  58.915 1.00 32.87  ? 131 ASN D CG  1 
ATOM   4283  O  OD1 . ASN D  1 137 ? 70.856  80.866  58.079 1.00 34.94  ? 131 ASN D OD1 1 
ATOM   4284  N  ND2 . ASN D  1 137 ? 70.087  80.999  60.190 1.00 18.56  ? 131 ASN D ND2 1 
ATOM   4285  N  N   . GLU D  1 138 ? 67.716  81.903  56.459 1.00 40.06  ? 132 GLU D N   1 
ATOM   4286  C  CA  . GLU D  1 138 ? 67.704  83.171  55.720 1.00 40.55  ? 132 GLU D CA  1 
ATOM   4287  C  C   . GLU D  1 138 ? 69.004  83.939  55.907 1.00 35.97  ? 132 GLU D C   1 
ATOM   4288  O  O   . GLU D  1 138 ? 69.585  84.479  54.951 1.00 28.13  ? 132 GLU D O   1 
ATOM   4289  C  CB  . GLU D  1 138 ? 66.546  84.056  56.189 1.00 45.35  ? 132 GLU D CB  1 
ATOM   4290  C  CG  . GLU D  1 138 ? 65.231  83.343  56.462 1.00 57.70  ? 132 GLU D CG  1 
ATOM   4291  C  CD  . GLU D  1 138 ? 64.088  84.327  56.714 1.00 68.70  ? 132 GLU D CD  1 
ATOM   4292  O  OE1 . GLU D  1 138 ? 63.093  83.940  57.368 1.00 67.81  ? 132 GLU D OE1 1 
ATOM   4293  O  OE2 . GLU D  1 138 ? 64.180  85.487  56.247 1.00 70.18  ? 132 GLU D OE2 1 
ATOM   4294  N  N   . GLU D  1 139 ? 69.443  83.979  57.159 1.00 33.29  ? 133 GLU D N   1 
ATOM   4295  C  CA  . GLU D  1 139 ? 70.657  84.680  57.549 1.00 33.71  ? 133 GLU D CA  1 
ATOM   4296  C  C   . GLU D  1 139 ? 71.867  84.229  56.736 1.00 33.32  ? 133 GLU D C   1 
ATOM   4297  O  O   . GLU D  1 139 ? 72.667  85.060  56.297 1.00 23.96  ? 133 GLU D O   1 
ATOM   4298  C  CB  . GLU D  1 139 ? 70.925  84.456  59.041 1.00 34.36  ? 133 GLU D CB  1 
ATOM   4299  C  CG  . GLU D  1 139 ? 71.825  85.500  59.644 1.00 43.62  ? 133 GLU D CG  1 
ATOM   4300  C  CD  . GLU D  1 139 ? 71.271  86.905  59.444 1.00 54.78  ? 133 GLU D CD  1 
ATOM   4301  O  OE1 . GLU D  1 139 ? 72.050  87.799  59.046 1.00 50.26  ? 133 GLU D OE1 1 
ATOM   4302  O  OE2 . GLU D  1 139 ? 70.058  87.111  59.679 1.00 57.67  ? 133 GLU D OE2 1 
ATOM   4303  N  N   . SER D  1 140 ? 71.983  82.914  56.538 1.00 28.70  ? 134 SER D N   1 
ATOM   4304  C  CA  . SER D  1 140 ? 73.091  82.342  55.807 1.00 26.08  ? 134 SER D CA  1 
ATOM   4305  C  C   . SER D  1 140 ? 73.279  82.968  54.435 1.00 27.63  ? 134 SER D C   1 
ATOM   4306  O  O   . SER D  1 140 ? 74.404  83.285  54.045 1.00 19.82  ? 134 SER D O   1 
ATOM   4307  C  CB  . SER D  1 140 ? 72.901  80.841  55.651 1.00 26.75  ? 134 SER D CB  1 
ATOM   4308  O  OG  . SER D  1 140 ? 74.037  80.258  55.026 1.00 18.89  ? 134 SER D OG  1 
ATOM   4309  N  N   . THR D  1 141 ? 72.181  83.152  53.711 1.00 25.23  ? 135 THR D N   1 
ATOM   4310  C  CA  . THR D  1 141 ? 72.243  83.732  52.365 1.00 31.93  ? 135 THR D CA  1 
ATOM   4311  C  C   . THR D  1 141 ? 72.515  85.231  52.375 1.00 26.20  ? 135 THR D C   1 
ATOM   4312  O  O   . THR D  1 141 ? 72.716  85.832  51.321 1.00 27.30  ? 135 THR D O   1 
ATOM   4313  C  CB  . THR D  1 141 ? 70.928  83.496  51.583 1.00 35.76  ? 135 THR D CB  1 
ATOM   4314  O  OG1 . THR D  1 141 ? 69.843  84.152  52.257 1.00 38.50  ? 135 THR D OG1 1 
ATOM   4315  C  CG2 . THR D  1 141 ? 70.630  82.017  51.489 1.00 41.30  ? 135 THR D CG2 1 
ATOM   4316  N  N   . LYS D  1 142 ? 72.507  85.830  53.561 1.00 26.88  ? 136 LYS D N   1 
ATOM   4317  C  CA  . LYS D  1 142 ? 72.755  87.268  53.699 1.00 29.09  ? 136 LYS D CA  1 
ATOM   4318  C  C   . LYS D  1 142 ? 74.116  87.573  54.330 1.00 26.26  ? 136 LYS D C   1 
ATOM   4319  O  O   . LYS D  1 142 ? 74.941  88.279  53.736 1.00 20.62  ? 136 LYS D O   1 
ATOM   4320  C  CB  . LYS D  1 142 ? 71.687  87.917  54.576 1.00 30.73  ? 136 LYS D CB  1 
ATOM   4321  C  CG  . LYS D  1 142 ? 70.252  87.796  54.099 1.00 45.96  ? 136 LYS D CG  1 
ATOM   4322  C  CD  . LYS D  1 142 ? 69.344  88.495  55.116 1.00 56.01  ? 136 LYS D CD  1 
ATOM   4323  C  CE  . LYS D  1 142 ? 67.869  88.432  54.750 1.00 64.72  ? 136 LYS D CE  1 
ATOM   4324  N  NZ  . LYS D  1 142 ? 67.030  89.121  55.781 1.00 66.70  ? 136 LYS D NZ  1 
ATOM   4325  N  N   . THR D  1 143 ? 74.351  87.014  55.520 1.00 21.04  ? 137 THR D N   1 
ATOM   4326  C  CA  . THR D  1 143 ? 75.582  87.276  56.264 1.00 25.32  ? 137 THR D CA  1 
ATOM   4327  C  C   . THR D  1 143 ? 76.412  86.054  56.639 1.00 27.75  ? 137 THR D C   1 
ATOM   4328  O  O   . THR D  1 143 ? 77.380  86.173  57.382 1.00 25.09  ? 137 THR D O   1 
ATOM   4329  C  CB  . THR D  1 143 ? 75.258  87.972  57.577 1.00 17.95  ? 137 THR D CB  1 
ATOM   4330  O  OG1 . THR D  1 143 ? 74.610  87.035  58.433 1.00 13.66  ? 137 THR D OG1 1 
ATOM   4331  C  CG2 . THR D  1 143 ? 74.306  89.123  57.365 1.00 14.97  ? 137 THR D CG2 1 
ATOM   4332  N  N   . GLY D  1 144 ? 76.022  84.881  56.164 1.00 28.44  ? 138 GLY D N   1 
ATOM   4333  C  CA  . GLY D  1 144 ? 76.757  83.684  56.518 1.00 23.25  ? 138 GLY D CA  1 
ATOM   4334  C  C   . GLY D  1 144 ? 76.742  83.404  58.013 1.00 22.15  ? 138 GLY D C   1 
ATOM   4335  O  O   . GLY D  1 144 ? 77.566  82.629  58.502 1.00 26.41  ? 138 GLY D O   1 
ATOM   4336  N  N   . ASN D  1 145 ? 75.808  84.018  58.739 1.00 18.12  ? 139 ASN D N   1 
ATOM   4337  C  CA  . ASN D  1 145 ? 75.701  83.851  60.199 1.00 23.37  ? 139 ASN D CA  1 
ATOM   4338  C  C   . ASN D  1 145 ? 77.023  84.191  60.897 1.00 21.42  ? 139 ASN D C   1 
ATOM   4339  O  O   . ASN D  1 145 ? 77.368  83.607  61.922 1.00 18.39  ? 139 ASN D O   1 
ATOM   4340  C  CB  . ASN D  1 145 ? 75.284  82.413  60.557 1.00 23.06  ? 139 ASN D CB  1 
ATOM   4341  C  CG  . ASN D  1 145 ? 73.856  82.072  60.098 1.00 31.26  ? 139 ASN D CG  1 
ATOM   4342  O  OD1 . ASN D  1 145 ? 72.883  82.447  60.743 1.00 33.98  ? 139 ASN D OD1 1 
ATOM   4343  N  ND2 . ASN D  1 145 ? 73.738  81.373  58.970 1.00 27.90  ? 139 ASN D ND2 1 
ATOM   4344  N  N   . ALA D  1 146 ? 77.752  85.158  60.348 1.00 23.14  ? 140 ALA D N   1 
ATOM   4345  C  CA  . ALA D  1 146 ? 79.054  85.548  60.900 1.00 23.45  ? 140 ALA D CA  1 
ATOM   4346  C  C   . ALA D  1 146 ? 78.960  86.360  62.187 1.00 24.84  ? 140 ALA D C   1 
ATOM   4347  O  O   . ALA D  1 146 ? 79.980  86.676  62.814 1.00 21.05  ? 140 ALA D O   1 
ATOM   4348  C  CB  . ALA D  1 146 ? 79.848  86.325  59.851 1.00 22.80  ? 140 ALA D CB  1 
ATOM   4349  N  N   . GLY D  1 147 ? 77.742  86.739  62.560 1.00 23.43  ? 141 GLY D N   1 
ATOM   4350  C  CA  . GLY D  1 147 ? 77.556  87.487  63.794 1.00 17.27  ? 141 GLY D CA  1 
ATOM   4351  C  C   . GLY D  1 147 ? 77.989  88.936  63.799 1.00 19.19  ? 141 GLY D C   1 
ATOM   4352  O  O   . GLY D  1 147 ? 78.142  89.564  62.753 1.00 21.71  ? 141 GLY D O   1 
ATOM   4353  N  N   . SER D  1 148 ? 78.243  89.458  64.992 1.00 21.87  ? 142 SER D N   1 
ATOM   4354  C  CA  . SER D  1 148 ? 78.590  90.860  65.128 1.00 27.03  ? 142 SER D CA  1 
ATOM   4355  C  C   . SER D  1 148 ? 79.914  91.323  64.536 1.00 27.04  ? 142 SER D C   1 
ATOM   4356  O  O   . SER D  1 148 ? 80.822  90.530  64.259 1.00 20.09  ? 142 SER D O   1 
ATOM   4357  C  CB  . SER D  1 148 ? 78.467  91.298  66.603 1.00 20.32  ? 142 SER D CB  1 
ATOM   4358  O  OG  . SER D  1 148 ? 79.418  90.670  67.427 1.00 30.39  ? 142 SER D OG  1 
ATOM   4359  N  N   . ARG D  1 149 ? 79.992  92.637  64.346 1.00 27.90  ? 143 ARG D N   1 
ATOM   4360  C  CA  . ARG D  1 149 ? 81.150  93.298  63.756 1.00 26.45  ? 143 ARG D CA  1 
ATOM   4361  C  C   . ARG D  1 149 ? 82.133  93.718  64.842 1.00 26.97  ? 143 ARG D C   1 
ATOM   4362  O  O   . ARG D  1 149 ? 81.986  94.773  65.453 1.00 29.90  ? 143 ARG D O   1 
ATOM   4363  C  CB  . ARG D  1 149 ? 80.655  94.506  62.969 1.00 23.68  ? 143 ARG D CB  1 
ATOM   4364  C  CG  . ARG D  1 149 ? 79.363  94.194  62.238 1.00 24.39  ? 143 ARG D CG  1 
ATOM   4365  C  CD  . ARG D  1 149 ? 78.863  95.313  61.346 1.00 22.68  ? 143 ARG D CD  1 
ATOM   4366  N  NE  . ARG D  1 149 ? 77.734  94.830  60.554 1.00 26.26  ? 143 ARG D NE  1 
ATOM   4367  C  CZ  . ARG D  1 149 ? 77.212  95.455  59.504 1.00 30.39  ? 143 ARG D CZ  1 
ATOM   4368  N  NH1 . ARG D  1 149 ? 76.190  94.904  58.874 1.00 22.17  ? 143 ARG D NH1 1 
ATOM   4369  N  NH2 . ARG D  1 149 ? 77.706  96.617  59.077 1.00 31.34  ? 143 ARG D NH2 1 
ATOM   4370  N  N   . LEU D  1 150 ? 83.140  92.891  65.076 1.00 21.76  ? 144 LEU D N   1 
ATOM   4371  C  CA  . LEU D  1 150 ? 84.115  93.175  66.110 1.00 22.18  ? 144 LEU D CA  1 
ATOM   4372  C  C   . LEU D  1 150 ? 85.001  94.391  65.831 1.00 22.75  ? 144 LEU D C   1 
ATOM   4373  O  O   . LEU D  1 150 ? 85.368  95.120  66.749 1.00 26.17  ? 144 LEU D O   1 
ATOM   4374  C  CB  . LEU D  1 150 ? 85.001  91.948  66.328 1.00 23.50  ? 144 LEU D CB  1 
ATOM   4375  C  CG  . LEU D  1 150 ? 84.326  90.648  66.757 1.00 29.33  ? 144 LEU D CG  1 
ATOM   4376  C  CD1 . LEU D  1 150 ? 85.403  89.634  67.081 1.00 32.27  ? 144 LEU D CD1 1 
ATOM   4377  C  CD2 . LEU D  1 150 ? 83.447  90.882  67.985 1.00 19.77  ? 144 LEU D CD2 1 
ATOM   4378  N  N   . ALA D  1 151 ? 85.351  94.599  64.568 1.00 18.12  ? 145 ALA D N   1 
ATOM   4379  C  CA  . ALA D  1 151 ? 86.216  95.705  64.185 1.00 21.00  ? 145 ALA D CA  1 
ATOM   4380  C  C   . ALA D  1 151 ? 86.077  95.958  62.691 1.00 23.73  ? 145 ALA D C   1 
ATOM   4381  O  O   . ALA D  1 151 ? 85.787  95.038  61.918 1.00 27.54  ? 145 ALA D O   1 
ATOM   4382  C  CB  . ALA D  1 151 ? 87.669  95.368  64.519 1.00 8.34   ? 145 ALA D CB  1 
ATOM   4383  N  N   . CYS D  1 152 ? 86.303  97.206  62.291 1.00 20.38  ? 146 CYS D N   1 
ATOM   4384  C  CA  . CYS D  1 152 ? 86.191  97.601  60.893 1.00 20.23  ? 146 CYS D CA  1 
ATOM   4385  C  C   . CYS D  1 152 ? 87.029  98.840  60.598 1.00 21.62  ? 146 CYS D C   1 
ATOM   4386  O  O   . CYS D  1 152 ? 87.591  99.465  61.501 1.00 23.66  ? 146 CYS D O   1 
ATOM   4387  C  CB  . CYS D  1 152 ? 84.737  97.903  60.569 1.00 21.20  ? 146 CYS D CB  1 
ATOM   4388  S  SG  . CYS D  1 152 ? 84.051  99.207  61.639 1.00 26.26  ? 146 CYS D SG  1 
ATOM   4389  N  N   . GLY D  1 153 ? 87.098  99.193  59.323 1.00 17.45  ? 147 GLY D N   1 
ATOM   4390  C  CA  . GLY D  1 153 ? 87.848  100.361 58.910 1.00 18.09  ? 147 GLY D CA  1 
ATOM   4391  C  C   . GLY D  1 153 ? 87.539  100.679 57.460 1.00 27.07  ? 147 GLY D C   1 
ATOM   4392  O  O   . GLY D  1 153 ? 87.094  99.800  56.701 1.00 24.65  ? 147 GLY D O   1 
ATOM   4393  N  N   . VAL D  1 154 ? 87.750  101.933 57.072 1.00 21.33  ? 148 VAL D N   1 
ATOM   4394  C  CA  . VAL D  1 154 ? 87.498  102.344 55.700 1.00 22.17  ? 148 VAL D CA  1 
ATOM   4395  C  C   . VAL D  1 154 ? 88.745  102.006 54.895 1.00 19.05  ? 148 VAL D C   1 
ATOM   4396  O  O   . VAL D  1 154 ? 89.855  102.321 55.299 1.00 24.03  ? 148 VAL D O   1 
ATOM   4397  C  CB  . VAL D  1 154 ? 87.215  103.873 55.592 1.00 24.21  ? 148 VAL D CB  1 
ATOM   4398  C  CG1 . VAL D  1 154 ? 86.758  104.232 54.147 1.00 18.14  ? 148 VAL D CG1 1 
ATOM   4399  C  CG2 . VAL D  1 154 ? 86.152  104.277 56.599 1.00 11.00  ? 148 VAL D CG2 1 
ATOM   4400  N  N   . ILE D  1 155 ? 88.557  101.355 53.760 1.00 20.44  ? 149 ILE D N   1 
ATOM   4401  C  CA  . ILE D  1 155 ? 89.669  100.960 52.906 1.00 18.63  ? 149 ILE D CA  1 
ATOM   4402  C  C   . ILE D  1 155 ? 90.191  102.162 52.121 1.00 24.84  ? 149 ILE D C   1 
ATOM   4403  O  O   . ILE D  1 155 ? 89.506  102.677 51.248 1.00 19.67  ? 149 ILE D O   1 
ATOM   4404  C  CB  . ILE D  1 155 ? 89.206  99.875  51.934 1.00 24.73  ? 149 ILE D CB  1 
ATOM   4405  C  CG1 . ILE D  1 155 ? 88.790  98.632  52.727 1.00 18.90  ? 149 ILE D CG1 1 
ATOM   4406  C  CG2 . ILE D  1 155 ? 90.289  99.573  50.921 1.00 24.68  ? 149 ILE D CG2 1 
ATOM   4407  C  CD1 . ILE D  1 155 ? 88.219  97.485  51.864 1.00 10.67  ? 149 ILE D CD1 1 
ATOM   4408  N  N   . GLY D  1 156 ? 91.412  102.598 52.423 1.00 30.39  ? 150 GLY D N   1 
ATOM   4409  C  CA  . GLY D  1 156 ? 91.963  103.761 51.744 1.00 23.74  ? 150 GLY D CA  1 
ATOM   4410  C  C   . GLY D  1 156 ? 93.095  103.498 50.772 1.00 27.56  ? 150 GLY D C   1 
ATOM   4411  O  O   . GLY D  1 156 ? 93.782  102.477 50.863 1.00 23.99  ? 150 GLY D O   1 
ATOM   4412  N  N   . ILE D  1 157 ? 93.281  104.422 49.831 1.00 24.96  ? 151 ILE D N   1 
ATOM   4413  C  CA  . ILE D  1 157 ? 94.335  104.296 48.846 1.00 30.42  ? 151 ILE D CA  1 
ATOM   4414  C  C   . ILE D  1 157 ? 95.662  104.405 49.575 1.00 34.14  ? 151 ILE D C   1 
ATOM   4415  O  O   . ILE D  1 157 ? 95.830  105.233 50.488 1.00 29.68  ? 151 ILE D O   1 
ATOM   4416  C  CB  . ILE D  1 157 ? 94.261  105.403 47.780 1.00 40.36  ? 151 ILE D CB  1 
ATOM   4417  C  CG1 . ILE D  1 157 ? 92.931  105.313 47.034 1.00 47.92  ? 151 ILE D CG1 1 
ATOM   4418  C  CG2 . ILE D  1 157 ? 95.403  105.237 46.787 1.00 36.05  ? 151 ILE D CG2 1 
ATOM   4419  C  CD1 . ILE D  1 157 ? 92.714  106.421 46.027 1.00 57.08  ? 151 ILE D CD1 1 
ATOM   4420  N  N   . ALA D  1 158 ? 96.605  103.567 49.171 1.00 29.70  ? 152 ALA D N   1 
ATOM   4421  C  CA  . ALA D  1 158 ? 97.912  103.555 49.804 1.00 39.15  ? 152 ALA D CA  1 
ATOM   4422  C  C   . ALA D  1 158 ? 99.024  103.745 48.800 1.00 40.60  ? 152 ALA D C   1 
ATOM   4423  O  O   . ALA D  1 158 ? 98.822  103.601 47.595 1.00 38.85  ? 152 ALA D O   1 
ATOM   4424  C  CB  . ALA D  1 158 ? 98.107  102.251 50.550 1.00 28.98  ? 152 ALA D CB  1 
ATOM   4425  N  N   . GLN D  1 159 ? 100.209 104.054 49.311 1.00 51.94  ? 153 GLN D N   1 
ATOM   4426  C  CA  . GLN D  1 159 ? 101.371 104.277 48.460 1.00 60.88  ? 153 GLN D CA  1 
ATOM   4427  C  C   . GLN D  1 159 ? 102.109 102.982 48.127 1.00 61.17  ? 153 GLN D C   1 
ATOM   4428  O  O   . GLN D  1 159 ? 102.200 102.110 49.017 1.00 59.71  ? 153 GLN D O   1 
ATOM   4429  C  CB  . GLN D  1 159 ? 102.322 105.249 49.152 1.00 63.96  ? 153 GLN D CB  1 
ATOM   4430  C  CG  . GLN D  1 159 ? 103.437 105.752 48.275 1.00 72.37  ? 153 GLN D CG  1 
ATOM   4431  C  CD  . GLN D  1 159 ? 104.269 106.808 48.961 1.00 73.31  ? 153 GLN D CD  1 
ATOM   4432  O  OE1 . GLN D  1 159 ? 105.053 107.502 48.318 1.00 78.00  ? 153 GLN D OE1 1 
ATOM   4433  N  NE2 . GLN D  1 159 ? 104.107 106.935 50.275 1.00 72.07  ? 153 GLN D NE2 1 
ATOM   4434  O  OXT . GLN D  1 159 ? 102.602 102.865 46.981 1.00 64.52  ? 153 GLN D OXT 1 
ATOM   4435  N  N   . ALA E  1 7   ? 114.174 58.876  41.877 1.00 36.22  ? 1   ALA E N   1 
ATOM   4436  C  CA  . ALA E  1 7   ? 114.586 58.798  43.332 1.00 50.85  ? 1   ALA E CA  1 
ATOM   4437  C  C   . ALA E  1 7   ? 116.090 58.570  43.506 1.00 48.41  ? 1   ALA E C   1 
ATOM   4438  O  O   . ALA E  1 7   ? 116.669 57.632  42.961 1.00 50.05  ? 1   ALA E O   1 
ATOM   4439  C  CB  . ALA E  1 7   ? 113.810 57.698  44.070 1.00 47.36  ? 1   ALA E CB  1 
ATOM   4440  N  N   . THR E  1 8   ? 116.704 59.429  44.303 1.00 43.20  ? 2   THR E N   1 
ATOM   4441  C  CA  . THR E  1 8   ? 118.130 59.385  44.520 1.00 36.67  ? 2   THR E CA  1 
ATOM   4442  C  C   . THR E  1 8   ? 118.474 59.024  45.969 1.00 34.40  ? 2   THR E C   1 
ATOM   4443  O  O   . THR E  1 8   ? 119.574 58.544  46.254 1.00 28.60  ? 2   THR E O   1 
ATOM   4444  C  CB  . THR E  1 8   ? 118.734 60.760  44.111 1.00 36.71  ? 2   THR E CB  1 
ATOM   4445  O  OG1 . THR E  1 8   ? 120.158 60.682  44.076 1.00 54.88  ? 2   THR E OG1 1 
ATOM   4446  C  CG2 . THR E  1 8   ? 118.319 61.842  45.085 1.00 31.82  ? 2   THR E CG2 1 
ATOM   4447  N  N   . LYS E  1 9   ? 117.527 59.223  46.881 1.00 29.70  ? 3   LYS E N   1 
ATOM   4448  C  CA  . LYS E  1 9   ? 117.758 58.910  48.285 1.00 30.77  ? 3   LYS E CA  1 
ATOM   4449  C  C   . LYS E  1 9   ? 116.591 58.198  48.960 1.00 31.50  ? 3   LYS E C   1 
ATOM   4450  O  O   . LYS E  1 9   ? 115.428 58.464  48.663 1.00 31.39  ? 3   LYS E O   1 
ATOM   4451  C  CB  . LYS E  1 9   ? 118.074 60.181  49.069 1.00 38.17  ? 3   LYS E CB  1 
ATOM   4452  C  CG  . LYS E  1 9   ? 119.499 60.659  48.955 1.00 45.36  ? 3   LYS E CG  1 
ATOM   4453  C  CD  . LYS E  1 9   ? 119.704 61.933  49.763 1.00 59.12  ? 3   LYS E CD  1 
ATOM   4454  C  CE  . LYS E  1 9   ? 121.174 62.132  50.159 1.00 73.78  ? 3   LYS E CE  1 
ATOM   4455  N  NZ  . LYS E  1 9   ? 121.655 61.118  51.159 1.00 75.77  ? 3   LYS E NZ  1 
ATOM   4456  N  N   . ALA E  1 10  ? 116.915 57.284  49.869 1.00 30.68  ? 4   ALA E N   1 
ATOM   4457  C  CA  . ALA E  1 10  ? 115.903 56.551  50.620 1.00 26.98  ? 4   ALA E CA  1 
ATOM   4458  C  C   . ALA E  1 10  ? 116.440 56.333  52.037 1.00 24.84  ? 4   ALA E C   1 
ATOM   4459  O  O   . ALA E  1 10  ? 117.638 56.459  52.279 1.00 22.11  ? 4   ALA E O   1 
ATOM   4460  C  CB  . ALA E  1 10  ? 115.612 55.227  49.950 1.00 19.43  ? 4   ALA E CB  1 
ATOM   4461  N  N   . VAL E  1 11  ? 115.556 56.030  52.980 1.00 23.42  ? 5   VAL E N   1 
ATOM   4462  C  CA  . VAL E  1 11  ? 115.984 55.790  54.348 1.00 18.87  ? 5   VAL E CA  1 
ATOM   4463  C  C   . VAL E  1 11  ? 115.080 54.753  54.992 1.00 27.00  ? 5   VAL E C   1 
ATOM   4464  O  O   . VAL E  1 11  ? 113.932 54.553  54.564 1.00 26.57  ? 5   VAL E O   1 
ATOM   4465  C  CB  . VAL E  1 11  ? 115.970 57.087  55.191 1.00 25.39  ? 5   VAL E CB  1 
ATOM   4466  C  CG1 . VAL E  1 11  ? 114.533 57.549  55.443 1.00 23.49  ? 5   VAL E CG1 1 
ATOM   4467  C  CG2 . VAL E  1 11  ? 116.700 56.856  56.497 1.00 21.04  ? 5   VAL E CG2 1 
ATOM   4468  N  N   . CYS E  1 12  ? 115.604 54.087  56.014 1.00 23.01  ? 6   CYS E N   1 
ATOM   4469  C  CA  . CYS E  1 12  ? 114.848 53.060  56.707 1.00 26.09  ? 6   CYS E CA  1 
ATOM   4470  C  C   . CYS E  1 12  ? 115.172 53.039  58.193 1.00 29.49  ? 6   CYS E C   1 
ATOM   4471  O  O   . CYS E  1 12  ? 116.335 53.071  58.588 1.00 29.60  ? 6   CYS E O   1 
ATOM   4472  C  CB  . CYS E  1 12  ? 115.163 51.687  56.110 1.00 26.26  ? 6   CYS E CB  1 
ATOM   4473  S  SG  . CYS E  1 12  ? 114.189 50.324  56.798 1.00 30.82  ? 6   CYS E SG  1 
ATOM   4474  N  N   . VAL E  1 13  ? 114.132 52.992  59.015 1.00 31.31  ? 7   VAL E N   1 
ATOM   4475  C  CA  . VAL E  1 13  ? 114.303 52.947  60.453 1.00 23.52  ? 7   VAL E CA  1 
ATOM   4476  C  C   . VAL E  1 13  ? 113.970 51.528  60.892 1.00 31.04  ? 7   VAL E C   1 
ATOM   4477  O  O   . VAL E  1 13  ? 112.827 51.078  60.766 1.00 26.75  ? 7   VAL E O   1 
ATOM   4478  C  CB  . VAL E  1 13  ? 113.369 53.945  61.145 1.00 24.25  ? 7   VAL E CB  1 
ATOM   4479  C  CG1 . VAL E  1 13  ? 113.475 53.807  62.651 1.00 11.81  ? 7   VAL E CG1 1 
ATOM   4480  C  CG2 . VAL E  1 13  ? 113.738 55.353  60.728 1.00 15.13  ? 7   VAL E CG2 1 
ATOM   4481  N  N   . LEU E  1 14  ? 114.984 50.822  61.382 1.00 27.74  ? 8   LEU E N   1 
ATOM   4482  C  CA  . LEU E  1 14  ? 114.818 49.449  61.832 1.00 30.74  ? 8   LEU E CA  1 
ATOM   4483  C  C   . LEU E  1 14  ? 114.404 49.385  63.297 1.00 23.09  ? 8   LEU E C   1 
ATOM   4484  O  O   . LEU E  1 14  ? 115.034 49.987  64.148 1.00 26.02  ? 8   LEU E O   1 
ATOM   4485  C  CB  . LEU E  1 14  ? 116.128 48.683  61.637 1.00 30.57  ? 8   LEU E CB  1 
ATOM   4486  C  CG  . LEU E  1 14  ? 116.610 48.511  60.197 1.00 34.24  ? 8   LEU E CG  1 
ATOM   4487  C  CD1 . LEU E  1 14  ? 118.069 48.119  60.202 1.00 38.24  ? 8   LEU E CD1 1 
ATOM   4488  C  CD2 . LEU E  1 14  ? 115.779 47.456  59.495 1.00 29.52  ? 8   LEU E CD2 1 
ATOM   4489  N  N   . LYS E  1 15  ? 113.347 48.640  63.582 1.00 26.23  ? 9   LYS E N   1 
ATOM   4490  C  CA  . LYS E  1 15  ? 112.860 48.488  64.947 1.00 33.09  ? 9   LYS E CA  1 
ATOM   4491  C  C   . LYS E  1 15  ? 112.296 47.085  65.091 1.00 29.91  ? 9   LYS E C   1 
ATOM   4492  O  O   . LYS E  1 15  ? 111.914 46.466  64.097 1.00 31.75  ? 9   LYS E O   1 
ATOM   4493  C  CB  . LYS E  1 15  ? 111.765 49.523  65.250 1.00 39.05  ? 9   LYS E CB  1 
ATOM   4494  C  CG  . LYS E  1 15  ? 112.274 50.951  65.368 1.00 55.15  ? 9   LYS E CG  1 
ATOM   4495  C  CD  . LYS E  1 15  ? 111.158 51.948  65.697 1.00 67.19  ? 9   LYS E CD  1 
ATOM   4496  C  CE  . LYS E  1 15  ? 111.736 53.339  66.027 1.00 68.56  ? 9   LYS E CE  1 
ATOM   4497  N  NZ  . LYS E  1 15  ? 110.705 54.350  66.403 1.00 59.18  ? 9   LYS E NZ  1 
ATOM   4498  N  N   . GLY E  1 16  ? 112.250 46.583  66.321 1.00 26.15  ? 10  GLY E N   1 
ATOM   4499  C  CA  . GLY E  1 16  ? 111.716 45.252  66.552 1.00 23.64  ? 10  GLY E CA  1 
ATOM   4500  C  C   . GLY E  1 16  ? 111.217 45.093  67.977 1.00 32.81  ? 10  GLY E C   1 
ATOM   4501  O  O   . GLY E  1 16  ? 111.131 46.070  68.714 1.00 29.70  ? 10  GLY E O   1 
ATOM   4502  N  N   . ASP E  1 17  ? 110.902 43.864  68.376 1.00 36.70  ? 11  ASP E N   1 
ATOM   4503  C  CA  . ASP E  1 17  ? 110.395 43.603  69.719 1.00 40.77  ? 11  ASP E CA  1 
ATOM   4504  C  C   . ASP E  1 17  ? 111.510 43.649  70.751 1.00 43.87  ? 11  ASP E C   1 
ATOM   4505  O  O   . ASP E  1 17  ? 111.252 43.724  71.955 1.00 40.14  ? 11  ASP E O   1 
ATOM   4506  C  CB  . ASP E  1 17  ? 109.715 42.236  69.756 1.00 47.60  ? 11  ASP E CB  1 
ATOM   4507  C  CG  . ASP E  1 17  ? 108.482 42.173  68.865 1.00 59.17  ? 11  ASP E CG  1 
ATOM   4508  O  OD1 . ASP E  1 17  ? 108.148 41.066  68.390 1.00 66.23  ? 11  ASP E OD1 1 
ATOM   4509  O  OD2 . ASP E  1 17  ? 107.838 43.225  68.645 1.00 61.04  ? 11  ASP E OD2 1 
ATOM   4510  N  N   . GLY E  1 18  ? 112.750 43.607  70.274 1.00 35.90  ? 12  GLY E N   1 
ATOM   4511  C  CA  . GLY E  1 18  ? 113.882 43.638  71.174 1.00 35.38  ? 12  GLY E CA  1 
ATOM   4512  C  C   . GLY E  1 18  ? 114.546 45.001  71.207 1.00 39.10  ? 12  GLY E C   1 
ATOM   4513  O  O   . GLY E  1 18  ? 113.919 46.011  70.873 1.00 36.55  ? 12  GLY E O   1 
ATOM   4514  N  N   . PRO E  1 19  ? 115.830 45.058  71.602 1.00 36.59  ? 13  PRO E N   1 
ATOM   4515  C  CA  . PRO E  1 19  ? 116.584 46.311  71.680 1.00 33.40  ? 13  PRO E CA  1 
ATOM   4516  C  C   . PRO E  1 19  ? 117.198 46.734  70.350 1.00 30.41  ? 13  PRO E C   1 
ATOM   4517  O  O   . PRO E  1 19  ? 117.806 47.808  70.284 1.00 24.48  ? 13  PRO E O   1 
ATOM   4518  C  CB  . PRO E  1 19  ? 117.673 45.978  72.688 1.00 31.42  ? 13  PRO E CB  1 
ATOM   4519  C  CG  . PRO E  1 19  ? 118.050 44.583  72.248 1.00 22.41  ? 13  PRO E CG  1 
ATOM   4520  C  CD  . PRO E  1 19  ? 116.658 43.932  72.086 1.00 31.08  ? 13  PRO E CD  1 
ATOM   4521  N  N   . VAL E  1 20  ? 117.068 45.892  69.317 1.00 23.94  ? 14  VAL E N   1 
ATOM   4522  C  CA  . VAL E  1 20  ? 117.648 46.195  68.005 1.00 32.37  ? 14  VAL E CA  1 
ATOM   4523  C  C   . VAL E  1 20  ? 116.993 47.390  67.321 1.00 35.23  ? 14  VAL E C   1 
ATOM   4524  O  O   . VAL E  1 20  ? 115.793 47.404  67.072 1.00 41.30  ? 14  VAL E O   1 
ATOM   4525  C  CB  . VAL E  1 20  ? 117.567 44.996  67.037 1.00 32.90  ? 14  VAL E CB  1 
ATOM   4526  C  CG1 . VAL E  1 20  ? 118.158 45.388  65.694 1.00 25.60  ? 14  VAL E CG1 1 
ATOM   4527  C  CG2 . VAL E  1 20  ? 118.326 43.806  67.603 1.00 33.96  ? 14  VAL E CG2 1 
ATOM   4528  N  N   . GLN E  1 21  ? 117.794 48.398  67.012 1.00 38.65  ? 15  GLN E N   1 
ATOM   4529  C  CA  . GLN E  1 21  ? 117.268 49.587  66.365 1.00 40.28  ? 15  GLN E CA  1 
ATOM   4530  C  C   . GLN E  1 21  ? 118.342 50.259  65.544 1.00 36.64  ? 15  GLN E C   1 
ATOM   4531  O  O   . GLN E  1 21  ? 119.515 50.195  65.883 1.00 34.59  ? 15  GLN E O   1 
ATOM   4532  C  CB  . GLN E  1 21  ? 116.724 50.564  67.411 1.00 41.52  ? 15  GLN E CB  1 
ATOM   4533  C  CG  . GLN E  1 21  ? 117.626 50.780  68.591 1.00 46.31  ? 15  GLN E CG  1 
ATOM   4534  C  CD  . GLN E  1 21  ? 116.991 51.665  69.648 1.00 55.98  ? 15  GLN E CD  1 
ATOM   4535  O  OE1 . GLN E  1 21  ? 117.135 52.889  69.616 1.00 60.69  ? 15  GLN E OE1 1 
ATOM   4536  N  NE2 . GLN E  1 21  ? 116.269 51.048  70.586 1.00 53.46  ? 15  GLN E NE2 1 
ATOM   4537  N  N   . GLY E  1 22  ? 117.939 50.906  64.459 1.00 34.74  ? 16  GLY E N   1 
ATOM   4538  C  CA  . GLY E  1 22  ? 118.918 51.573  63.627 1.00 29.98  ? 16  GLY E CA  1 
ATOM   4539  C  C   . GLY E  1 22  ? 118.327 52.312  62.455 1.00 28.22  ? 16  GLY E C   1 
ATOM   4540  O  O   . GLY E  1 22  ? 117.147 52.182  62.133 1.00 33.58  ? 16  GLY E O   1 
ATOM   4541  N  N   . ILE E  1 23  ? 119.171 53.102  61.814 1.00 27.23  ? 17  ILE E N   1 
ATOM   4542  C  CA  . ILE E  1 23  ? 118.779 53.896  60.668 1.00 25.64  ? 17  ILE E CA  1 
ATOM   4543  C  C   . ILE E  1 23  ? 119.702 53.543  59.514 1.00 25.19  ? 17  ILE E C   1 
ATOM   4544  O  O   . ILE E  1 23  ? 120.920 53.607  59.648 1.00 20.12  ? 17  ILE E O   1 
ATOM   4545  C  CB  . ILE E  1 23  ? 118.939 55.399  60.969 1.00 27.11  ? 17  ILE E CB  1 
ATOM   4546  C  CG1 . ILE E  1 23  ? 117.912 55.832  62.008 1.00 23.57  ? 17  ILE E CG1 1 
ATOM   4547  C  CG2 . ILE E  1 23  ? 118.794 56.214  59.688 1.00 28.26  ? 17  ILE E CG2 1 
ATOM   4548  C  CD1 . ILE E  1 23  ? 118.263 57.142  62.641 1.00 17.86  ? 17  ILE E CD1 1 
ATOM   4549  N  N   . ILE E  1 24  ? 119.122 53.175  58.384 1.00 20.81  ? 18  ILE E N   1 
ATOM   4550  C  CA  . ILE E  1 24  ? 119.912 52.828  57.219 1.00 22.33  ? 18  ILE E CA  1 
ATOM   4551  C  C   . ILE E  1 24  ? 119.590 53.787  56.067 1.00 23.12  ? 18  ILE E C   1 
ATOM   4552  O  O   . ILE E  1 24  ? 118.414 53.983  55.703 1.00 20.06  ? 18  ILE E O   1 
ATOM   4553  C  CB  . ILE E  1 24  ? 119.633 51.367  56.779 1.00 19.65  ? 18  ILE E CB  1 
ATOM   4554  C  CG1 . ILE E  1 24  ? 120.034 50.399  57.893 1.00 22.60  ? 18  ILE E CG1 1 
ATOM   4555  C  CG2 . ILE E  1 24  ? 120.403 51.039  55.521 1.00 18.39  ? 18  ILE E CG2 1 
ATOM   4556  C  CD1 . ILE E  1 24  ? 121.530 50.276  58.097 1.00 23.41  ? 18  ILE E CD1 1 
ATOM   4557  N  N   . ASN E  1 25  ? 120.639 54.391  55.511 1.00 18.23  ? 19  ASN E N   1 
ATOM   4558  C  CA  . ASN E  1 25  ? 120.503 55.320  54.393 1.00 24.17  ? 19  ASN E CA  1 
ATOM   4559  C  C   . ASN E  1 25  ? 120.782 54.631  53.052 1.00 27.89  ? 19  ASN E C   1 
ATOM   4560  O  O   . ASN E  1 25  ? 121.544 53.657  52.980 1.00 25.01  ? 19  ASN E O   1 
ATOM   4561  C  CB  . ASN E  1 25  ? 121.462 56.492  54.571 1.00 21.38  ? 19  ASN E CB  1 
ATOM   4562  C  CG  . ASN E  1 25  ? 121.236 57.220  55.872 1.00 35.58  ? 19  ASN E CG  1 
ATOM   4563  O  OD1 . ASN E  1 25  ? 120.220 57.901  56.048 1.00 37.66  ? 19  ASN E OD1 1 
ATOM   4564  N  ND2 . ASN E  1 25  ? 122.172 57.071  56.805 1.00 34.77  ? 19  ASN E ND2 1 
ATOM   4565  N  N   . PHE E  1 26  ? 120.143 55.137  52.004 1.00 25.67  ? 20  PHE E N   1 
ATOM   4566  C  CA  . PHE E  1 26  ? 120.300 54.620  50.648 1.00 23.99  ? 20  PHE E CA  1 
ATOM   4567  C  C   . PHE E  1 26  ? 120.560 55.814  49.752 1.00 26.92  ? 20  PHE E C   1 
ATOM   4568  O  O   . PHE E  1 26  ? 119.921 56.857  49.885 1.00 26.32  ? 20  PHE E O   1 
ATOM   4569  C  CB  . PHE E  1 26  ? 119.025 53.939  50.173 1.00 20.94  ? 20  PHE E CB  1 
ATOM   4570  C  CG  . PHE E  1 26  ? 118.665 52.724  50.943 1.00 23.17  ? 20  PHE E CG  1 
ATOM   4571  C  CD1 . PHE E  1 26  ? 119.063 51.467  50.507 1.00 23.76  ? 20  PHE E CD1 1 
ATOM   4572  C  CD2 . PHE E  1 26  ? 117.911 52.826  52.104 1.00 23.96  ? 20  PHE E CD2 1 
ATOM   4573  C  CE1 . PHE E  1 26  ? 118.710 50.323  51.222 1.00 28.75  ? 20  PHE E CE1 1 
ATOM   4574  C  CE2 . PHE E  1 26  ? 117.552 51.688  52.826 1.00 25.86  ? 20  PHE E CE2 1 
ATOM   4575  C  CZ  . PHE E  1 26  ? 117.952 50.432  52.384 1.00 19.26  ? 20  PHE E CZ  1 
ATOM   4576  N  N   . GLU E  1 27  ? 121.482 55.666  48.824 1.00 27.24  ? 21  GLU E N   1 
ATOM   4577  C  CA  . GLU E  1 27  ? 121.795 56.777  47.942 1.00 35.74  ? 21  GLU E CA  1 
ATOM   4578  C  C   . GLU E  1 27  ? 122.167 56.227  46.567 1.00 31.26  ? 21  GLU E C   1 
ATOM   4579  O  O   . GLU E  1 27  ? 122.954 55.282  46.456 1.00 25.95  ? 21  GLU E O   1 
ATOM   4580  C  CB  . GLU E  1 27  ? 122.930 57.570  48.570 1.00 35.57  ? 21  GLU E CB  1 
ATOM   4581  C  CG  . GLU E  1 27  ? 123.442 58.747  47.794 1.00 62.22  ? 21  GLU E CG  1 
ATOM   4582  C  CD  . GLU E  1 27  ? 124.655 59.350  48.479 1.00 76.50  ? 21  GLU E CD  1 
ATOM   4583  O  OE1 . GLU E  1 27  ? 124.496 59.880  49.600 1.00 87.82  ? 21  GLU E OE1 1 
ATOM   4584  O  OE2 . GLU E  1 27  ? 125.769 59.275  47.912 1.00 86.88  ? 21  GLU E OE2 1 
ATOM   4585  N  N   . GLN E  1 28  ? 121.573 56.792  45.521 1.00 24.99  ? 22  GLN E N   1 
ATOM   4586  C  CA  . GLN E  1 28  ? 121.845 56.326  44.164 1.00 28.20  ? 22  GLN E CA  1 
ATOM   4587  C  C   . GLN E  1 28  ? 121.979 57.541  43.280 1.00 30.53  ? 22  GLN E C   1 
ATOM   4588  O  O   . GLN E  1 28  ? 120.980 58.096  42.830 1.00 29.93  ? 22  GLN E O   1 
ATOM   4589  C  CB  . GLN E  1 28  ? 120.695 55.436  43.676 1.00 26.48  ? 22  GLN E CB  1 
ATOM   4590  C  CG  . GLN E  1 28  ? 120.931 54.768  42.338 1.00 21.75  ? 22  GLN E CG  1 
ATOM   4591  C  CD  . GLN E  1 28  ? 119.763 53.880  41.913 1.00 33.70  ? 22  GLN E CD  1 
ATOM   4592  O  OE1 . GLN E  1 28  ? 118.627 54.065  42.365 1.00 27.37  ? 22  GLN E OE1 1 
ATOM   4593  N  NE2 . GLN E  1 28  ? 120.035 52.921  41.028 1.00 29.62  ? 22  GLN E NE2 1 
ATOM   4594  N  N   . LYS E  1 29  ? 123.218 57.955  43.038 1.00 39.04  ? 23  LYS E N   1 
ATOM   4595  C  CA  . LYS E  1 29  ? 123.485 59.129  42.217 1.00 39.13  ? 23  LYS E CA  1 
ATOM   4596  C  C   . LYS E  1 29  ? 122.949 59.068  40.797 1.00 34.21  ? 23  LYS E C   1 
ATOM   4597  O  O   . LYS E  1 29  ? 122.591 60.098  40.233 1.00 37.97  ? 23  LYS E O   1 
ATOM   4598  C  CB  . LYS E  1 29  ? 124.987 59.427  42.169 1.00 48.45  ? 23  LYS E CB  1 
ATOM   4599  C  CG  . LYS E  1 29  ? 125.465 60.422  43.239 1.00 65.06  ? 23  LYS E CG  1 
ATOM   4600  C  CD  . LYS E  1 29  ? 125.966 59.729  44.505 1.00 79.70  ? 23  LYS E CD  1 
ATOM   4601  C  CE  . LYS E  1 29  ? 127.299 59.006  44.276 1.00 87.07  ? 23  LYS E CE  1 
ATOM   4602  N  NZ  . LYS E  1 29  ? 127.791 58.289  45.497 1.00 90.34  ? 23  LYS E NZ  1 
ATOM   4603  N  N   . GLU E  1 30  ? 122.886 57.873  40.221 1.00 27.84  ? 24  GLU E N   1 
ATOM   4604  C  CA  . GLU E  1 30  ? 122.406 57.712  38.855 1.00 28.63  ? 24  GLU E CA  1 
ATOM   4605  C  C   . GLU E  1 30  ? 121.413 56.558  38.786 1.00 32.31  ? 24  GLU E C   1 
ATOM   4606  O  O   . GLU E  1 30  ? 121.582 55.547  39.460 1.00 33.58  ? 24  GLU E O   1 
ATOM   4607  C  CB  . GLU E  1 30  ? 123.598 57.459  37.922 1.00 41.82  ? 24  GLU E CB  1 
ATOM   4608  C  CG  . GLU E  1 30  ? 124.600 58.614  37.878 1.00 44.95  ? 24  GLU E CG  1 
ATOM   4609  C  CD  . GLU E  1 30  ? 124.033 59.857  37.187 1.00 60.71  ? 24  GLU E CD  1 
ATOM   4610  O  OE1 . GLU E  1 30  ? 124.659 60.935  37.303 1.00 61.70  ? 24  GLU E OE1 1 
ATOM   4611  O  OE2 . GLU E  1 30  ? 122.968 59.756  36.522 1.00 56.26  ? 24  GLU E OE2 1 
ATOM   4612  N  N   . SER E  1 31  ? 120.381 56.697  37.965 1.00 27.01  ? 25  SER E N   1 
ATOM   4613  C  CA  . SER E  1 31  ? 119.367 55.656  37.893 1.00 32.06  ? 25  SER E CA  1 
ATOM   4614  C  C   . SER E  1 31  ? 119.888 54.342  37.338 1.00 30.63  ? 25  SER E C   1 
ATOM   4615  O  O   . SER E  1 31  ? 119.281 53.295  37.540 1.00 33.04  ? 25  SER E O   1 
ATOM   4616  C  CB  . SER E  1 31  ? 118.158 56.143  37.076 1.00 26.66  ? 25  SER E CB  1 
ATOM   4617  O  OG  . SER E  1 31  ? 118.523 56.403  35.740 1.00 31.47  ? 25  SER E OG  1 
ATOM   4618  N  N   . ASN E  1 32  ? 121.001 54.379  36.625 1.00 33.79  ? 26  ASN E N   1 
ATOM   4619  C  CA  . ASN E  1 32  ? 121.544 53.136  36.094 1.00 39.60  ? 26  ASN E CA  1 
ATOM   4620  C  C   . ASN E  1 32  ? 122.858 52.826  36.794 1.00 38.54  ? 26  ASN E C   1 
ATOM   4621  O  O   . ASN E  1 32  ? 123.680 52.054  36.302 1.00 34.89  ? 26  ASN E O   1 
ATOM   4622  C  CB  . ASN E  1 32  ? 121.712 53.197  34.554 1.00 36.61  ? 26  ASN E CB  1 
ATOM   4623  C  CG  . ASN E  1 32  ? 122.706 54.246  34.090 1.00 29.43  ? 26  ASN E CG  1 
ATOM   4624  O  OD1 . ASN E  1 32  ? 123.156 55.091  34.858 1.00 33.11  ? 26  ASN E OD1 1 
ATOM   4625  N  ND2 . ASN E  1 32  ? 123.041 54.200  32.804 1.00 31.65  ? 26  ASN E ND2 1 
ATOM   4626  N  N   . GLY E  1 33  ? 123.019 53.432  37.969 1.00 40.35  ? 27  GLY E N   1 
ATOM   4627  C  CA  . GLY E  1 33  ? 124.209 53.240  38.775 1.00 37.01  ? 27  GLY E CA  1 
ATOM   4628  C  C   . GLY E  1 33  ? 123.995 52.424  40.045 1.00 35.26  ? 27  GLY E C   1 
ATOM   4629  O  O   . GLY E  1 33  ? 122.889 51.980  40.361 1.00 26.28  ? 27  GLY E O   1 
ATOM   4630  N  N   . PRO E  1 34  ? 125.061 52.231  40.817 1.00 35.17  ? 28  PRO E N   1 
ATOM   4631  C  CA  . PRO E  1 34  ? 124.994 51.461  42.057 1.00 31.40  ? 28  PRO E CA  1 
ATOM   4632  C  C   . PRO E  1 34  ? 124.273 52.215  43.159 1.00 32.51  ? 28  PRO E C   1 
ATOM   4633  O  O   . PRO E  1 34  ? 124.040 53.414  43.051 1.00 31.03  ? 28  PRO E O   1 
ATOM   4634  C  CB  . PRO E  1 34  ? 126.469 51.251  42.422 1.00 27.53  ? 28  PRO E CB  1 
ATOM   4635  C  CG  . PRO E  1 34  ? 127.243 51.737  41.221 1.00 29.01  ? 28  PRO E CG  1 
ATOM   4636  C  CD  . PRO E  1 34  ? 126.402 52.803  40.636 1.00 28.29  ? 28  PRO E CD  1 
ATOM   4637  N  N   . VAL E  1 35  ? 123.965 51.494  44.234 1.00 32.68  ? 29  VAL E N   1 
ATOM   4638  C  CA  . VAL E  1 35  ? 123.309 52.057  45.405 1.00 30.84  ? 29  VAL E CA  1 
ATOM   4639  C  C   . VAL E  1 35  ? 124.196 51.871  46.648 1.00 33.94  ? 29  VAL E C   1 
ATOM   4640  O  O   . VAL E  1 35  ? 124.611 50.756  46.953 1.00 30.44  ? 29  VAL E O   1 
ATOM   4641  C  CB  . VAL E  1 35  ? 121.976 51.344  45.699 1.00 30.81  ? 29  VAL E CB  1 
ATOM   4642  C  CG1 . VAL E  1 35  ? 121.331 51.964  46.928 1.00 16.44  ? 29  VAL E CG1 1 
ATOM   4643  C  CG2 . VAL E  1 35  ? 121.059 51.416  44.497 1.00 34.83  ? 29  VAL E CG2 1 
ATOM   4644  N  N   . LYS E  1 36  ? 124.491 52.956  47.355 1.00 31.70  ? 30  LYS E N   1 
ATOM   4645  C  CA  . LYS E  1 36  ? 125.271 52.870  48.580 1.00 29.19  ? 30  LYS E CA  1 
ATOM   4646  C  C   . LYS E  1 36  ? 124.272 52.709  49.733 1.00 34.77  ? 30  LYS E C   1 
ATOM   4647  O  O   . LYS E  1 36  ? 123.264 53.423  49.818 1.00 30.06  ? 30  LYS E O   1 
ATOM   4648  C  CB  . LYS E  1 36  ? 126.119 54.134  48.768 1.00 32.78  ? 30  LYS E CB  1 
ATOM   4649  C  CG  . LYS E  1 36  ? 127.172 54.299  47.676 1.00 55.17  ? 30  LYS E CG  1 
ATOM   4650  C  CD  . LYS E  1 36  ? 128.013 55.559  47.821 1.00 66.57  ? 30  LYS E CD  1 
ATOM   4651  C  CE  . LYS E  1 36  ? 129.080 55.609  46.727 1.00 74.46  ? 30  LYS E CE  1 
ATOM   4652  N  NZ  . LYS E  1 36  ? 129.845 56.889  46.713 1.00 81.41  ? 30  LYS E NZ  1 
ATOM   4653  N  N   . VAL E  1 37  ? 124.534 51.743  50.601 1.00 28.85  ? 31  VAL E N   1 
ATOM   4654  C  CA  . VAL E  1 37  ? 123.665 51.489  51.737 1.00 25.27  ? 31  VAL E CA  1 
ATOM   4655  C  C   . VAL E  1 37  ? 124.550 51.636  52.957 1.00 33.98  ? 31  VAL E C   1 
ATOM   4656  O  O   . VAL E  1 37  ? 125.510 50.880  53.109 1.00 36.85  ? 31  VAL E O   1 
ATOM   4657  C  CB  . VAL E  1 37  ? 123.136 50.059  51.708 1.00 26.84  ? 31  VAL E CB  1 
ATOM   4658  C  CG1 . VAL E  1 37  ? 122.244 49.806  52.924 1.00 13.20  ? 31  VAL E CG1 1 
ATOM   4659  C  CG2 . VAL E  1 37  ? 122.413 49.807  50.394 1.00 17.25  ? 31  VAL E CG2 1 
ATOM   4660  N  N   . TRP E  1 38  ? 124.251 52.594  53.826 1.00 29.42  ? 32  TRP E N   1 
ATOM   4661  C  CA  . TRP E  1 38  ? 125.095 52.772  54.994 1.00 31.32  ? 32  TRP E CA  1 
ATOM   4662  C  C   . TRP E  1 38  ? 124.347 53.283  56.215 1.00 32.57  ? 32  TRP E C   1 
ATOM   4663  O  O   . TRP E  1 38  ? 123.257 53.854  56.102 1.00 34.37  ? 32  TRP E O   1 
ATOM   4664  C  CB  . TRP E  1 38  ? 126.235 53.730  54.656 1.00 26.82  ? 32  TRP E CB  1 
ATOM   4665  C  CG  . TRP E  1 38  ? 125.857 55.162  54.781 1.00 31.73  ? 32  TRP E CG  1 
ATOM   4666  C  CD1 . TRP E  1 38  ? 126.057 55.975  55.864 1.00 26.56  ? 32  TRP E CD1 1 
ATOM   4667  C  CD2 . TRP E  1 38  ? 125.188 55.954  53.802 1.00 26.92  ? 32  TRP E CD2 1 
ATOM   4668  N  NE1 . TRP E  1 38  ? 125.558 57.223  55.614 1.00 30.44  ? 32  TRP E NE1 1 
ATOM   4669  C  CE2 . TRP E  1 38  ? 125.018 57.243  54.355 1.00 29.85  ? 32  TRP E CE2 1 
ATOM   4670  C  CE3 . TRP E  1 38  ? 124.717 55.702  52.510 1.00 25.51  ? 32  TRP E CE3 1 
ATOM   4671  C  CZ2 . TRP E  1 38  ? 124.396 58.283  53.659 1.00 31.61  ? 32  TRP E CZ2 1 
ATOM   4672  C  CZ3 . TRP E  1 38  ? 124.095 56.743  51.810 1.00 42.42  ? 32  TRP E CZ3 1 
ATOM   4673  C  CH2 . TRP E  1 38  ? 123.943 58.018  52.390 1.00 38.40  ? 32  TRP E CH2 1 
ATOM   4674  N  N   . GLY E  1 39  ? 124.955 53.088  57.379 1.00 26.20  ? 33  GLY E N   1 
ATOM   4675  C  CA  . GLY E  1 39  ? 124.353 53.535  58.621 1.00 30.99  ? 33  GLY E CA  1 
ATOM   4676  C  C   . GLY E  1 39  ? 124.776 52.605  59.734 1.00 30.07  ? 33  GLY E C   1 
ATOM   4677  O  O   . GLY E  1 39  ? 125.810 51.964  59.631 1.00 38.13  ? 33  GLY E O   1 
ATOM   4678  N  N   . SER E  1 40  ? 123.996 52.504  60.797 1.00 31.49  ? 34  SER E N   1 
ATOM   4679  C  CA  . SER E  1 40  ? 124.393 51.610  61.870 1.00 32.07  ? 34  SER E CA  1 
ATOM   4680  C  C   . SER E  1 40  ? 123.200 51.015  62.576 1.00 31.74  ? 34  SER E C   1 
ATOM   4681  O  O   . SER E  1 40  ? 122.131 51.620  62.629 1.00 31.78  ? 34  SER E O   1 
ATOM   4682  C  CB  . SER E  1 40  ? 125.271 52.343  62.879 1.00 31.75  ? 34  SER E CB  1 
ATOM   4683  O  OG  . SER E  1 40  ? 124.514 53.255  63.642 1.00 36.33  ? 34  SER E OG  1 
ATOM   4684  N  N   . ILE E  1 41  ? 123.394 49.820  63.115 1.00 28.21  ? 35  ILE E N   1 
ATOM   4685  C  CA  . ILE E  1 41  ? 122.344 49.123  63.827 1.00 26.14  ? 35  ILE E CA  1 
ATOM   4686  C  C   . ILE E  1 41  ? 122.902 48.739  65.187 1.00 32.60  ? 35  ILE E C   1 
ATOM   4687  O  O   . ILE E  1 41  ? 123.929 48.076  65.266 1.00 42.65  ? 35  ILE E O   1 
ATOM   4688  C  CB  . ILE E  1 41  ? 121.940 47.848  63.072 1.00 24.81  ? 35  ILE E CB  1 
ATOM   4689  C  CG1 . ILE E  1 41  ? 121.644 48.184  61.611 1.00 19.89  ? 35  ILE E CG1 1 
ATOM   4690  C  CG2 . ILE E  1 41  ? 120.731 47.219  63.724 1.00 8.35   ? 35  ILE E CG2 1 
ATOM   4691  C  CD1 . ILE E  1 41  ? 121.417 46.972  60.743 1.00 26.07  ? 35  ILE E CD1 1 
ATOM   4692  N  N   . LYS E  1 42  ? 122.248 49.162  66.262 1.00 38.27  ? 36  LYS E N   1 
ATOM   4693  C  CA  . LYS E  1 42  ? 122.724 48.812  67.594 1.00 35.00  ? 36  LYS E CA  1 
ATOM   4694  C  C   . LYS E  1 42  ? 121.875 47.713  68.225 1.00 36.52  ? 36  LYS E C   1 
ATOM   4695  O  O   . LYS E  1 42  ? 120.810 47.349  67.694 1.00 31.27  ? 36  LYS E O   1 
ATOM   4696  C  CB  . LYS E  1 42  ? 122.775 50.052  68.490 1.00 39.88  ? 36  LYS E CB  1 
ATOM   4697  C  CG  . LYS E  1 42  ? 121.479 50.811  68.655 1.00 58.69  ? 36  LYS E CG  1 
ATOM   4698  C  CD  . LYS E  1 42  ? 121.734 52.117  69.407 1.00 68.82  ? 36  LYS E CD  1 
ATOM   4699  C  CE  . LYS E  1 42  ? 120.437 52.854  69.735 1.00 76.31  ? 36  LYS E CE  1 
ATOM   4700  N  NZ  . LYS E  1 42  ? 120.697 54.187  70.356 1.00 75.54  ? 36  LYS E NZ  1 
ATOM   4701  N  N   . GLY E  1 43  ? 122.367 47.162  69.336 1.00 32.10  ? 37  GLY E N   1 
ATOM   4702  C  CA  . GLY E  1 43  ? 121.654 46.101  70.023 1.00 21.19  ? 37  GLY E CA  1 
ATOM   4703  C  C   . GLY E  1 43  ? 121.801 44.737  69.360 1.00 27.92  ? 37  GLY E C   1 
ATOM   4704  O  O   . GLY E  1 43  ? 121.007 43.829  69.610 1.00 25.09  ? 37  GLY E O   1 
ATOM   4705  N  N   . LEU E  1 44  ? 122.813 44.572  68.517 1.00 25.76  ? 38  LEU E N   1 
ATOM   4706  C  CA  . LEU E  1 44  ? 123.003 43.291  67.843 1.00 31.52  ? 38  LEU E CA  1 
ATOM   4707  C  C   . LEU E  1 44  ? 124.129 42.502  68.482 1.00 33.73  ? 38  LEU E C   1 
ATOM   4708  O  O   . LEU E  1 44  ? 125.234 43.023  68.649 1.00 34.24  ? 38  LEU E O   1 
ATOM   4709  C  CB  . LEU E  1 44  ? 123.342 43.506  66.372 1.00 34.15  ? 38  LEU E CB  1 
ATOM   4710  C  CG  . LEU E  1 44  ? 122.257 43.848  65.360 1.00 33.78  ? 38  LEU E CG  1 
ATOM   4711  C  CD1 . LEU E  1 44  ? 122.936 44.177  64.042 1.00 33.56  ? 38  LEU E CD1 1 
ATOM   4712  C  CD2 . LEU E  1 44  ? 121.286 42.685  65.192 1.00 27.86  ? 38  LEU E CD2 1 
ATOM   4713  N  N   . THR E  1 45  ? 123.869 41.245  68.825 1.00 33.15  ? 39  THR E N   1 
ATOM   4714  C  CA  . THR E  1 45  ? 124.921 40.446  69.429 1.00 39.76  ? 39  THR E CA  1 
ATOM   4715  C  C   . THR E  1 45  ? 126.089 40.414  68.450 1.00 36.56  ? 39  THR E C   1 
ATOM   4716  O  O   . THR E  1 45  ? 125.892 40.399  67.236 1.00 31.65  ? 39  THR E O   1 
ATOM   4717  C  CB  . THR E  1 45  ? 124.469 39.018  69.691 1.00 38.59  ? 39  THR E CB  1 
ATOM   4718  O  OG1 . THR E  1 45  ? 124.339 38.336  68.443 1.00 48.22  ? 39  THR E OG1 1 
ATOM   4719  C  CG2 . THR E  1 45  ? 123.132 39.009  70.417 1.00 37.67  ? 39  THR E CG2 1 
ATOM   4720  N  N   . GLU E  1 46  ? 127.302 40.422  68.988 1.00 38.56  ? 40  GLU E N   1 
ATOM   4721  C  CA  . GLU E  1 46  ? 128.512 40.397  68.177 1.00 41.72  ? 40  GLU E CA  1 
ATOM   4722  C  C   . GLU E  1 46  ? 128.430 39.280  67.144 1.00 39.48  ? 40  GLU E C   1 
ATOM   4723  O  O   . GLU E  1 46  ? 127.972 38.187  67.457 1.00 35.92  ? 40  GLU E O   1 
ATOM   4724  C  CB  . GLU E  1 46  ? 129.727 40.178  69.074 1.00 37.21  ? 40  GLU E CB  1 
ATOM   4725  C  CG  . GLU E  1 46  ? 131.057 40.262  68.368 1.00 46.07  ? 40  GLU E CG  1 
ATOM   4726  C  CD  . GLU E  1 46  ? 132.230 40.111  69.325 1.00 56.03  ? 40  GLU E CD  1 
ATOM   4727  O  OE1 . GLU E  1 46  ? 133.389 40.266  68.881 1.00 64.18  ? 40  GLU E OE1 1 
ATOM   4728  O  OE2 . GLU E  1 46  ? 131.993 39.836  70.521 1.00 52.90  ? 40  GLU E OE2 1 
ATOM   4729  N  N   . GLY E  1 47  ? 128.854 39.563  65.913 1.00 39.21  ? 41  GLY E N   1 
ATOM   4730  C  CA  . GLY E  1 47  ? 128.820 38.543  64.880 1.00 37.34  ? 41  GLY E CA  1 
ATOM   4731  C  C   . GLY E  1 47  ? 128.196 38.945  63.557 1.00 38.71  ? 41  GLY E C   1 
ATOM   4732  O  O   . GLY E  1 47  ? 127.969 40.128  63.288 1.00 39.79  ? 41  GLY E O   1 
ATOM   4733  N  N   . LEU E  1 48  ? 127.920 37.944  62.725 1.00 35.32  ? 42  LEU E N   1 
ATOM   4734  C  CA  . LEU E  1 48  ? 127.318 38.171  61.423 1.00 34.04  ? 42  LEU E CA  1 
ATOM   4735  C  C   . LEU E  1 48  ? 125.807 38.096  61.522 1.00 34.60  ? 42  LEU E C   1 
ATOM   4736  O  O   . LEU E  1 48  ? 125.268 37.280  62.279 1.00 37.65  ? 42  LEU E O   1 
ATOM   4737  C  CB  . LEU E  1 48  ? 127.786 37.118  60.419 1.00 33.36  ? 42  LEU E CB  1 
ATOM   4738  C  CG  . LEU E  1 48  ? 129.246 37.124  59.966 1.00 36.59  ? 42  LEU E CG  1 
ATOM   4739  C  CD1 . LEU E  1 48  ? 129.469 35.977  58.987 1.00 37.69  ? 42  LEU E CD1 1 
ATOM   4740  C  CD2 . LEU E  1 48  ? 129.595 38.453  59.315 1.00 39.62  ? 42  LEU E CD2 1 
ATOM   4741  N  N   . HIS E  1 49  ? 125.132 38.961  60.766 1.00 28.79  ? 43  HIS E N   1 
ATOM   4742  C  CA  . HIS E  1 49  ? 123.666 38.978  60.715 1.00 24.66  ? 43  HIS E CA  1 
ATOM   4743  C  C   . HIS E  1 49  ? 123.184 39.185  59.281 1.00 29.00  ? 43  HIS E C   1 
ATOM   4744  O  O   . HIS E  1 49  ? 123.690 40.059  58.540 1.00 20.54  ? 43  HIS E O   1 
ATOM   4745  C  CB  . HIS E  1 49  ? 123.104 40.082  61.598 1.00 19.46  ? 43  HIS E CB  1 
ATOM   4746  C  CG  . HIS E  1 49  ? 123.295 39.841  63.062 1.00 25.95  ? 43  HIS E CG  1 
ATOM   4747  N  ND1 . HIS E  1 49  ? 122.428 39.073  63.808 1.00 27.61  ? 43  HIS E ND1 1 
ATOM   4748  C  CD2 . HIS E  1 49  ? 124.242 40.287  63.923 1.00 24.14  ? 43  HIS E CD2 1 
ATOM   4749  C  CE1 . HIS E  1 49  ? 122.828 39.063  65.068 1.00 27.72  ? 43  HIS E CE1 1 
ATOM   4750  N  NE2 . HIS E  1 49  ? 123.924 39.792  65.165 1.00 26.81  ? 43  HIS E NE2 1 
ATOM   4751  N  N   . GLY E  1 50  ? 122.226 38.352  58.885 1.00 28.65  ? 44  GLY E N   1 
ATOM   4752  C  CA  . GLY E  1 50  ? 121.659 38.461  57.554 1.00 27.81  ? 44  GLY E CA  1 
ATOM   4753  C  C   . GLY E  1 50  ? 121.035 39.835  57.403 1.00 26.46  ? 44  GLY E C   1 
ATOM   4754  O  O   . GLY E  1 50  ? 120.428 40.357  58.341 1.00 28.70  ? 44  GLY E O   1 
ATOM   4755  N  N   . PHE E  1 51  ? 121.172 40.401  56.211 1.00 25.30  ? 45  PHE E N   1 
ATOM   4756  C  CA  . PHE E  1 51  ? 120.687 41.735  55.890 1.00 23.76  ? 45  PHE E CA  1 
ATOM   4757  C  C   . PHE E  1 51  ? 119.972 41.685  54.535 1.00 27.31  ? 45  PHE E C   1 
ATOM   4758  O  O   . PHE E  1 51  ? 120.618 41.726  53.485 1.00 27.55  ? 45  PHE E O   1 
ATOM   4759  C  CB  . PHE E  1 51  ? 121.900 42.647  55.801 1.00 26.01  ? 45  PHE E CB  1 
ATOM   4760  C  CG  . PHE E  1 51  ? 121.578 44.100  55.790 1.00 31.96  ? 45  PHE E CG  1 
ATOM   4761  C  CD1 . PHE E  1 51  ? 120.846 44.673  56.828 1.00 29.39  ? 45  PHE E CD1 1 
ATOM   4762  C  CD2 . PHE E  1 51  ? 122.101 44.923  54.793 1.00 28.77  ? 45  PHE E CD2 1 
ATOM   4763  C  CE1 . PHE E  1 51  ? 120.649 46.042  56.875 1.00 27.97  ? 45  PHE E CE1 1 
ATOM   4764  C  CE2 . PHE E  1 51  ? 121.918 46.283  54.827 1.00 27.85  ? 45  PHE E CE2 1 
ATOM   4765  C  CZ  . PHE E  1 51  ? 121.187 46.854  55.876 1.00 39.61  ? 45  PHE E CZ  1 
ATOM   4766  N  N   . HIS E  1 52  ? 118.644 41.613  54.555 1.00 28.63  ? 46  HIS E N   1 
ATOM   4767  C  CA  . HIS E  1 52  ? 117.895 41.525  53.310 1.00 28.02  ? 46  HIS E CA  1 
ATOM   4768  C  C   . HIS E  1 52  ? 116.726 42.482  53.143 1.00 32.86  ? 46  HIS E C   1 
ATOM   4769  O  O   . HIS E  1 52  ? 116.144 42.989  54.113 1.00 24.65  ? 46  HIS E O   1 
ATOM   4770  C  CB  . HIS E  1 52  ? 117.310 40.120  53.123 1.00 28.54  ? 46  HIS E CB  1 
ATOM   4771  C  CG  . HIS E  1 52  ? 118.173 39.020  53.648 1.00 40.42  ? 46  HIS E CG  1 
ATOM   4772  N  ND1 . HIS E  1 52  ? 117.793 38.223  54.708 1.00 43.60  ? 46  HIS E ND1 1 
ATOM   4773  C  CD2 . HIS E  1 52  ? 119.395 38.581  53.261 1.00 32.36  ? 46  HIS E CD2 1 
ATOM   4774  C  CE1 . HIS E  1 52  ? 118.746 37.341  54.950 1.00 41.39  ? 46  HIS E CE1 1 
ATOM   4775  N  NE2 . HIS E  1 52  ? 119.727 37.536  54.085 1.00 35.17  ? 46  HIS E NE2 1 
ATOM   4776  N  N   . VAL E  1 53  ? 116.382 42.692  51.877 1.00 29.02  ? 47  VAL E N   1 
ATOM   4777  C  CA  . VAL E  1 53  ? 115.231 43.487  51.509 1.00 25.40  ? 47  VAL E CA  1 
ATOM   4778  C  C   . VAL E  1 53  ? 114.180 42.432  51.175 1.00 26.48  ? 47  VAL E C   1 
ATOM   4779  O  O   . VAL E  1 53  ? 114.352 41.643  50.231 1.00 22.65  ? 47  VAL E O   1 
ATOM   4780  C  CB  . VAL E  1 53  ? 115.482 44.332  50.255 1.00 26.93  ? 47  VAL E CB  1 
ATOM   4781  C  CG1 . VAL E  1 53  ? 114.196 44.993  49.832 1.00 24.77  ? 47  VAL E CG1 1 
ATOM   4782  C  CG2 . VAL E  1 53  ? 116.548 45.386  50.532 1.00 30.43  ? 47  VAL E CG2 1 
ATOM   4783  N  N   . HIS E  1 54  ? 113.124 42.388  51.981 1.00 17.15  ? 48  HIS E N   1 
ATOM   4784  C  CA  . HIS E  1 54  ? 112.036 41.443  51.773 1.00 27.31  ? 48  HIS E CA  1 
ATOM   4785  C  C   . HIS E  1 54  ? 110.981 42.122  50.880 1.00 32.76  ? 48  HIS E C   1 
ATOM   4786  O  O   . HIS E  1 54  ? 110.929 43.354  50.781 1.00 30.09  ? 48  HIS E O   1 
ATOM   4787  C  CB  . HIS E  1 54  ? 111.444 40.993  53.125 1.00 23.39  ? 48  HIS E CB  1 
ATOM   4788  C  CG  . HIS E  1 54  ? 112.364 40.116  53.935 1.00 25.71  ? 48  HIS E CG  1 
ATOM   4789  N  ND1 . HIS E  1 54  ? 111.977 38.887  54.436 1.00 21.75  ? 48  HIS E ND1 1 
ATOM   4790  C  CD2 . HIS E  1 54  ? 113.643 40.302  54.351 1.00 20.48  ? 48  HIS E CD2 1 
ATOM   4791  C  CE1 . HIS E  1 54  ? 112.974 38.359  55.127 1.00 24.58  ? 48  HIS E CE1 1 
ATOM   4792  N  NE2 . HIS E  1 54  ? 113.998 39.195  55.092 1.00 26.83  ? 48  HIS E NE2 1 
ATOM   4793  N  N   . GLU E  1 55  ? 110.147 41.309  50.243 1.00 31.94  ? 49  GLU E N   1 
ATOM   4794  C  CA  . GLU E  1 55  ? 109.144 41.774  49.294 1.00 29.58  ? 49  GLU E CA  1 
ATOM   4795  C  C   . GLU E  1 55  ? 108.126 42.865  49.638 1.00 27.94  ? 49  GLU E C   1 
ATOM   4796  O  O   . GLU E  1 55  ? 107.959 43.817  48.879 1.00 21.66  ? 49  GLU E O   1 
ATOM   4797  C  CB  . GLU E  1 55  ? 108.381 40.569  48.755 1.00 31.01  ? 49  GLU E CB  1 
ATOM   4798  C  CG  . GLU E  1 55  ? 107.512 40.900  47.554 1.00 37.27  ? 49  GLU E CG  1 
ATOM   4799  C  CD  . GLU E  1 55  ? 106.817 39.679  46.980 1.00 41.15  ? 49  GLU E CD  1 
ATOM   4800  O  OE1 . GLU E  1 55  ? 106.318 39.776  45.841 1.00 42.03  ? 49  GLU E OE1 1 
ATOM   4801  O  OE2 . GLU E  1 55  ? 106.762 38.627  47.661 1.00 44.18  ? 49  GLU E OE2 1 
ATOM   4802  N  N   . PHE E  1 56  ? 107.440 42.721  50.760 1.00 27.10  ? 50  PHE E N   1 
ATOM   4803  C  CA  . PHE E  1 56  ? 106.406 43.663  51.147 1.00 28.15  ? 50  PHE E CA  1 
ATOM   4804  C  C   . PHE E  1 56  ? 106.779 44.648  52.234 1.00 31.92  ? 50  PHE E C   1 
ATOM   4805  O  O   . PHE E  1 56  ? 107.478 44.306  53.185 1.00 28.56  ? 50  PHE E O   1 
ATOM   4806  C  CB  . PHE E  1 56  ? 105.168 42.886  51.596 1.00 31.17  ? 50  PHE E CB  1 
ATOM   4807  C  CG  . PHE E  1 56  ? 104.713 41.869  50.597 1.00 34.59  ? 50  PHE E CG  1 
ATOM   4808  C  CD1 . PHE E  1 56  ? 104.319 42.262  49.322 1.00 23.39  ? 50  PHE E CD1 1 
ATOM   4809  C  CD2 . PHE E  1 56  ? 104.742 40.509  50.901 1.00 36.07  ? 50  PHE E CD2 1 
ATOM   4810  C  CE1 . PHE E  1 56  ? 103.972 41.324  48.356 1.00 19.03  ? 50  PHE E CE1 1 
ATOM   4811  C  CE2 . PHE E  1 56  ? 104.392 39.562  49.935 1.00 29.53  ? 50  PHE E CE2 1 
ATOM   4812  C  CZ  . PHE E  1 56  ? 104.010 39.975  48.658 1.00 20.21  ? 50  PHE E CZ  1 
ATOM   4813  N  N   . GLY E  1 57  ? 106.296 45.877  52.076 1.00 28.41  ? 51  GLY E N   1 
ATOM   4814  C  CA  . GLY E  1 57  ? 106.521 46.904  53.076 1.00 23.83  ? 51  GLY E CA  1 
ATOM   4815  C  C   . GLY E  1 57  ? 105.304 46.859  53.997 1.00 28.16  ? 51  GLY E C   1 
ATOM   4816  O  O   . GLY E  1 57  ? 104.668 47.873  54.271 1.00 29.30  ? 51  GLY E O   1 
ATOM   4817  N  N   . ASP E  1 58  ? 104.978 45.662  54.473 1.00 24.20  ? 52  ASP E N   1 
ATOM   4818  C  CA  . ASP E  1 58  ? 103.827 45.446  55.344 1.00 25.66  ? 52  ASP E CA  1 
ATOM   4819  C  C   . ASP E  1 58  ? 104.271 45.011  56.729 1.00 26.13  ? 52  ASP E C   1 
ATOM   4820  O  O   . ASP E  1 58  ? 104.799 43.916  56.915 1.00 27.47  ? 52  ASP E O   1 
ATOM   4821  C  CB  . ASP E  1 58  ? 102.924 44.385  54.722 1.00 22.42  ? 52  ASP E CB  1 
ATOM   4822  C  CG  . ASP E  1 58  ? 101.738 44.032  55.590 1.00 25.96  ? 52  ASP E CG  1 
ATOM   4823  O  OD1 . ASP E  1 58  ? 100.802 43.406  55.053 1.00 25.76  ? 52  ASP E OD1 1 
ATOM   4824  O  OD2 . ASP E  1 58  ? 101.733 44.358  56.795 1.00 26.79  ? 52  ASP E OD2 1 
ATOM   4825  N  N   . ASN E  1 59  ? 104.040 45.877  57.703 1.00 28.80  ? 53  ASN E N   1 
ATOM   4826  C  CA  . ASN E  1 59  ? 104.421 45.603  59.074 1.00 29.53  ? 53  ASN E CA  1 
ATOM   4827  C  C   . ASN E  1 59  ? 103.180 45.392  59.956 1.00 31.49  ? 53  ASN E C   1 
ATOM   4828  O  O   . ASN E  1 59  ? 103.243 45.569  61.180 1.00 22.64  ? 53  ASN E O   1 
ATOM   4829  C  CB  . ASN E  1 59  ? 105.275 46.770  59.591 1.00 41.11  ? 53  ASN E CB  1 
ATOM   4830  C  CG  . ASN E  1 59  ? 105.820 46.537  61.001 1.00 57.15  ? 53  ASN E CG  1 
ATOM   4831  O  OD1 . ASN E  1 59  ? 105.403 47.195  61.959 1.00 57.93  ? 53  ASN E OD1 1 
ATOM   4832  N  ND2 . ASN E  1 59  ? 106.754 45.597  61.131 1.00 58.28  ? 53  ASN E ND2 1 
ATOM   4833  N  N   . THR E  1 60  ? 102.058 45.001  59.346 1.00 25.92  ? 54  THR E N   1 
ATOM   4834  C  CA  . THR E  1 60  ? 100.835 44.794  60.121 1.00 28.83  ? 54  THR E CA  1 
ATOM   4835  C  C   . THR E  1 60  ? 101.009 43.750  61.212 1.00 34.25  ? 54  THR E C   1 
ATOM   4836  O  O   . THR E  1 60  ? 100.425 43.863  62.291 1.00 35.11  ? 54  THR E O   1 
ATOM   4837  C  CB  . THR E  1 60  ? 99.631  44.416  59.224 1.00 28.52  ? 54  THR E CB  1 
ATOM   4838  O  OG1 . THR E  1 60  ? 99.984  43.355  58.329 1.00 25.23  ? 54  THR E OG1 1 
ATOM   4839  C  CG2 . THR E  1 60  ? 99.189  45.626  58.424 1.00 22.30  ? 54  THR E CG2 1 
ATOM   4840  N  N   . ALA E  1 61  ? 101.834 42.743  60.950 1.00 34.68  ? 55  ALA E N   1 
ATOM   4841  C  CA  . ALA E  1 61  ? 102.082 41.711  61.947 1.00 36.47  ? 55  ALA E CA  1 
ATOM   4842  C  C   . ALA E  1 61  ? 103.579 41.650  62.222 1.00 33.99  ? 55  ALA E C   1 
ATOM   4843  O  O   . ALA E  1 61  ? 104.187 40.587  62.173 1.00 44.39  ? 55  ALA E O   1 
ATOM   4844  C  CB  . ALA E  1 61  ? 101.562 40.356  61.450 1.00 27.53  ? 55  ALA E CB  1 
ATOM   4845  N  N   . GLY E  1 62  ? 104.174 42.804  62.499 1.00 37.55  ? 56  GLY E N   1 
ATOM   4846  C  CA  . GLY E  1 62  ? 105.599 42.848  62.769 1.00 33.12  ? 56  GLY E CA  1 
ATOM   4847  C  C   . GLY E  1 62  ? 106.402 42.514  61.533 1.00 35.86  ? 56  GLY E C   1 
ATOM   4848  O  O   . GLY E  1 62  ? 105.863 42.523  60.420 1.00 36.27  ? 56  GLY E O   1 
ATOM   4849  N  N   . CYS E  1 63  ? 107.684 42.207  61.709 1.00 34.42  ? 57  CYS E N   1 
ATOM   4850  C  CA  . CYS E  1 63  ? 108.534 41.875  60.558 1.00 30.83  ? 57  CYS E CA  1 
ATOM   4851  C  C   . CYS E  1 63  ? 108.061 40.646  59.779 1.00 27.66  ? 57  CYS E C   1 
ATOM   4852  O  O   . CYS E  1 63  ? 108.484 40.435  58.651 1.00 24.68  ? 57  CYS E O   1 
ATOM   4853  C  CB  . CYS E  1 63  ? 109.987 41.683  61.010 1.00 27.75  ? 57  CYS E CB  1 
ATOM   4854  S  SG  . CYS E  1 63  ? 110.651 43.192  61.792 1.00 39.63  ? 57  CYS E SG  1 
ATOM   4855  N  N   . THR E  1 64  ? 107.167 39.855  60.371 1.00 22.18  ? 58  THR E N   1 
ATOM   4856  C  CA  . THR E  1 64  ? 106.667 38.644  59.726 1.00 24.50  ? 58  THR E CA  1 
ATOM   4857  C  C   . THR E  1 64  ? 105.883 38.918  58.456 1.00 32.85  ? 58  THR E C   1 
ATOM   4858  O  O   . THR E  1 64  ? 106.003 38.189  57.481 1.00 33.06  ? 58  THR E O   1 
ATOM   4859  C  CB  . THR E  1 64  ? 105.715 37.854  60.640 1.00 29.21  ? 58  THR E CB  1 
ATOM   4860  O  OG1 . THR E  1 64  ? 106.272 37.748  61.955 1.00 36.87  ? 58  THR E OG1 1 
ATOM   4861  C  CG2 . THR E  1 64  ? 105.491 36.465  60.077 1.00 24.02  ? 58  THR E CG2 1 
ATOM   4862  N  N   . SER E  1 65  ? 105.067 39.967  58.472 1.00 36.01  ? 59  SER E N   1 
ATOM   4863  C  CA  . SER E  1 65  ? 104.240 40.272  57.316 1.00 34.96  ? 59  SER E CA  1 
ATOM   4864  C  C   . SER E  1 65  ? 104.999 40.795  56.107 1.00 35.91  ? 59  SER E C   1 
ATOM   4865  O  O   . SER E  1 65  ? 104.424 40.923  55.018 1.00 33.86  ? 59  SER E O   1 
ATOM   4866  C  CB  . SER E  1 65  ? 103.117 41.235  57.721 1.00 27.44  ? 59  SER E CB  1 
ATOM   4867  O  OG  . SER E  1 65  ? 103.581 42.170  58.665 1.00 35.77  ? 59  SER E OG  1 
ATOM   4868  N  N   . ALA E  1 66  ? 106.294 41.059  56.290 1.00 32.23  ? 60  ALA E N   1 
ATOM   4869  C  CA  . ALA E  1 66  ? 107.145 41.556  55.211 1.00 28.59  ? 60  ALA E CA  1 
ATOM   4870  C  C   . ALA E  1 66  ? 107.376 40.510  54.116 1.00 32.97  ? 60  ALA E C   1 
ATOM   4871  O  O   . ALA E  1 66  ? 107.866 40.831  53.030 1.00 27.89  ? 60  ALA E O   1 
ATOM   4872  C  CB  . ALA E  1 66  ? 108.472 42.018  55.777 1.00 24.97  ? 60  ALA E CB  1 
ATOM   4873  N  N   . GLY E  1 67  ? 107.037 39.255  54.402 1.00 36.83  ? 61  GLY E N   1 
ATOM   4874  C  CA  . GLY E  1 67  ? 107.204 38.212  53.405 1.00 30.56  ? 61  GLY E CA  1 
ATOM   4875  C  C   . GLY E  1 67  ? 108.622 37.726  53.147 1.00 32.00  ? 61  GLY E C   1 
ATOM   4876  O  O   . GLY E  1 67  ? 109.546 37.936  53.945 1.00 28.23  ? 61  GLY E O   1 
ATOM   4877  N  N   . PRO E  1 68  ? 108.825 37.059  52.008 1.00 29.78  ? 62  PRO E N   1 
ATOM   4878  C  CA  . PRO E  1 68  ? 110.148 36.539  51.663 1.00 27.99  ? 62  PRO E CA  1 
ATOM   4879  C  C   . PRO E  1 68  ? 111.049 37.597  51.035 1.00 33.53  ? 62  PRO E C   1 
ATOM   4880  O  O   . PRO E  1 68  ? 110.655 38.758  50.868 1.00 32.51  ? 62  PRO E O   1 
ATOM   4881  C  CB  . PRO E  1 68  ? 109.815 35.416  50.700 1.00 24.91  ? 62  PRO E CB  1 
ATOM   4882  C  CG  . PRO E  1 68  ? 108.698 36.042  49.888 1.00 29.14  ? 62  PRO E CG  1 
ATOM   4883  C  CD  . PRO E  1 68  ? 107.826 36.675  50.990 1.00 31.52  ? 62  PRO E CD  1 
ATOM   4884  N  N   . HIS E  1 69  ? 112.261 37.182  50.691 1.00 24.57  ? 63  HIS E N   1 
ATOM   4885  C  CA  . HIS E  1 69  ? 113.236 38.074  50.090 1.00 29.35  ? 63  HIS E CA  1 
ATOM   4886  C  C   . HIS E  1 69  ? 112.713 38.631  48.757 1.00 26.33  ? 63  HIS E C   1 
ATOM   4887  O  O   . HIS E  1 69  ? 112.143 37.891  47.954 1.00 32.97  ? 63  HIS E O   1 
ATOM   4888  C  CB  . HIS E  1 69  ? 114.569 37.315  49.876 1.00 21.85  ? 63  HIS E CB  1 
ATOM   4889  C  CG  . HIS E  1 69  ? 115.218 36.853  51.153 1.00 38.82  ? 63  HIS E CG  1 
ATOM   4890  N  ND1 . HIS E  1 69  ? 116.417 36.169  51.178 1.00 30.89  ? 63  HIS E ND1 1 
ATOM   4891  C  CD2 . HIS E  1 69  ? 114.845 37.000  52.449 1.00 33.03  ? 63  HIS E CD2 1 
ATOM   4892  C  CE1 . HIS E  1 69  ? 116.754 35.921  52.430 1.00 30.75  ? 63  HIS E CE1 1 
ATOM   4893  N  NE2 . HIS E  1 69  ? 115.817 36.415  53.221 1.00 35.46  ? 63  HIS E NE2 1 
ATOM   4894  N  N   . PHE E  1 70  ? 112.874 39.937  48.540 1.00 26.32  ? 64  PHE E N   1 
ATOM   4895  C  CA  . PHE E  1 70  ? 112.447 40.547  47.280 1.00 29.17  ? 64  PHE E CA  1 
ATOM   4896  C  C   . PHE E  1 70  ? 113.083 39.705  46.151 1.00 32.89  ? 64  PHE E C   1 
ATOM   4897  O  O   . PHE E  1 70  ? 114.306 39.701  45.955 1.00 22.88  ? 64  PHE E O   1 
ATOM   4898  C  CB  . PHE E  1 70  ? 112.933 42.001  47.195 1.00 25.13  ? 64  PHE E CB  1 
ATOM   4899  C  CG  . PHE E  1 70  ? 112.468 42.731  45.957 1.00 15.08  ? 64  PHE E CG  1 
ATOM   4900  C  CD1 . PHE E  1 70  ? 113.253 43.723  45.388 1.00 21.85  ? 64  PHE E CD1 1 
ATOM   4901  C  CD2 . PHE E  1 70  ? 111.258 42.403  45.344 1.00 22.88  ? 64  PHE E CD2 1 
ATOM   4902  C  CE1 . PHE E  1 70  ? 112.849 44.380  44.218 1.00 21.73  ? 64  PHE E CE1 1 
ATOM   4903  C  CE2 . PHE E  1 70  ? 110.838 43.054  44.169 1.00 18.37  ? 64  PHE E CE2 1 
ATOM   4904  C  CZ  . PHE E  1 70  ? 111.637 44.041  43.608 1.00 19.19  ? 64  PHE E CZ  1 
ATOM   4905  N  N   . ASN E  1 71  ? 112.245 39.007  45.397 1.00 33.50  ? 65  ASN E N   1 
ATOM   4906  C  CA  . ASN E  1 71  ? 112.749 38.140  44.348 1.00 33.63  ? 65  ASN E CA  1 
ATOM   4907  C  C   . ASN E  1 71  ? 111.985 38.239  43.013 1.00 33.25  ? 65  ASN E C   1 
ATOM   4908  O  O   . ASN E  1 71  ? 111.371 37.274  42.571 1.00 28.28  ? 65  ASN E O   1 
ATOM   4909  C  CB  . ASN E  1 71  ? 112.713 36.705  44.885 1.00 27.19  ? 65  ASN E CB  1 
ATOM   4910  C  CG  . ASN E  1 71  ? 113.405 35.726  43.968 1.00 31.73  ? 65  ASN E CG  1 
ATOM   4911  O  OD1 . ASN E  1 71  ? 114.227 36.120  43.137 1.00 25.96  ? 65  ASN E OD1 1 
ATOM   4912  N  ND2 . ASN E  1 71  ? 113.098 34.441  44.126 1.00 16.45  ? 65  ASN E ND2 1 
ATOM   4913  N  N   . PRO E  1 72  ? 112.039 39.400  42.340 1.00 32.80  ? 66  PRO E N   1 
ATOM   4914  C  CA  . PRO E  1 72  ? 111.323 39.556  41.065 1.00 31.82  ? 66  PRO E CA  1 
ATOM   4915  C  C   . PRO E  1 72  ? 111.759 38.639  39.927 1.00 38.73  ? 66  PRO E C   1 
ATOM   4916  O  O   . PRO E  1 72  ? 111.000 38.411  38.989 1.00 41.90  ? 66  PRO E O   1 
ATOM   4917  C  CB  . PRO E  1 72  ? 111.533 41.030  40.725 1.00 23.56  ? 66  PRO E CB  1 
ATOM   4918  C  CG  . PRO E  1 72  ? 112.877 41.316  41.301 1.00 29.23  ? 66  PRO E CG  1 
ATOM   4919  C  CD  . PRO E  1 72  ? 112.842 40.598  42.645 1.00 30.19  ? 66  PRO E CD  1 
ATOM   4920  N  N   . LEU E  1 73  ? 112.970 38.105  39.999 1.00 42.18  ? 67  LEU E N   1 
ATOM   4921  C  CA  . LEU E  1 73  ? 113.445 37.230  38.936 1.00 41.80  ? 67  LEU E CA  1 
ATOM   4922  C  C   . LEU E  1 73  ? 113.260 35.745  39.242 1.00 40.98  ? 67  LEU E C   1 
ATOM   4923  O  O   . LEU E  1 73  ? 113.695 34.885  38.484 1.00 45.45  ? 67  LEU E O   1 
ATOM   4924  C  CB  . LEU E  1 73  ? 114.905 37.551  38.630 1.00 37.82  ? 67  LEU E CB  1 
ATOM   4925  C  CG  . LEU E  1 73  ? 115.022 38.900  37.917 1.00 42.42  ? 67  LEU E CG  1 
ATOM   4926  C  CD1 . LEU E  1 73  ? 116.433 39.464  37.985 1.00 37.96  ? 67  LEU E CD1 1 
ATOM   4927  C  CD2 . LEU E  1 73  ? 114.582 38.699  36.480 1.00 47.21  ? 67  LEU E CD2 1 
ATOM   4928  N  N   . SER E  1 74  ? 112.610 35.452  40.359 1.00 42.05  ? 68  SER E N   1 
ATOM   4929  C  CA  . SER E  1 74  ? 112.351 34.074  40.754 1.00 44.68  ? 68  SER E CA  1 
ATOM   4930  C  C   . SER E  1 74  ? 113.596 33.214  40.814 1.00 45.69  ? 68  SER E C   1 
ATOM   4931  O  O   . SER E  1 74  ? 113.566 32.069  40.376 1.00 50.40  ? 68  SER E O   1 
ATOM   4932  C  CB  . SER E  1 74  ? 111.372 33.424  39.782 1.00 42.18  ? 68  SER E CB  1 
ATOM   4933  O  OG  . SER E  1 74  ? 110.152 34.133  39.738 1.00 49.78  ? 68  SER E OG  1 
ATOM   4934  N  N   . ARG E  1 75  ? 114.689 33.746  41.348 1.00 42.49  ? 69  ARG E N   1 
ATOM   4935  C  CA  . ARG E  1 75  ? 115.909 32.965  41.435 1.00 42.28  ? 69  ARG E CA  1 
ATOM   4936  C  C   . ARG E  1 75  ? 116.133 32.427  42.837 1.00 40.31  ? 69  ARG E C   1 
ATOM   4937  O  O   . ARG E  1 75  ? 115.321 32.659  43.729 1.00 44.66  ? 69  ARG E O   1 
ATOM   4938  C  CB  . ARG E  1 75  ? 117.090 33.790  40.913 1.00 41.69  ? 69  ARG E CB  1 
ATOM   4939  C  CG  . ARG E  1 75  ? 116.901 34.058  39.413 1.00 53.44  ? 69  ARG E CG  1 
ATOM   4940  C  CD  . ARG E  1 75  ? 118.165 34.374  38.638 1.00 65.35  ? 69  ARG E CD  1 
ATOM   4941  N  NE  . ARG E  1 75  ? 118.617 35.751  38.828 1.00 79.39  ? 69  ARG E NE  1 
ATOM   4942  C  CZ  . ARG E  1 75  ? 119.232 36.473  37.893 1.00 82.49  ? 69  ARG E CZ  1 
ATOM   4943  N  NH1 . ARG E  1 75  ? 119.460 35.949  36.695 1.00 81.46  ? 69  ARG E NH1 1 
ATOM   4944  N  NH2 . ARG E  1 75  ? 119.636 37.712  38.159 1.00 81.35  ? 69  ARG E NH2 1 
ATOM   4945  N  N   . LYS E  1 76  ? 117.197 31.663  43.034 1.00 41.90  ? 70  LYS E N   1 
ATOM   4946  C  CA  . LYS E  1 76  ? 117.460 31.110  44.354 1.00 39.91  ? 70  LYS E CA  1 
ATOM   4947  C  C   . LYS E  1 76  ? 118.310 32.045  45.207 1.00 36.16  ? 70  LYS E C   1 
ATOM   4948  O  O   . LYS E  1 76  ? 119.036 32.897  44.683 1.00 31.31  ? 70  LYS E O   1 
ATOM   4949  C  CB  . LYS E  1 76  ? 118.133 29.745  44.226 1.00 46.39  ? 70  LYS E CB  1 
ATOM   4950  C  CG  . LYS E  1 76  ? 117.198 28.632  43.772 1.00 54.71  ? 70  LYS E CG  1 
ATOM   4951  C  CD  . LYS E  1 76  ? 117.818 27.258  44.016 1.00 66.81  ? 70  LYS E CD  1 
ATOM   4952  C  CE  . LYS E  1 76  ? 116.789 26.134  43.861 1.00 77.30  ? 70  LYS E CE  1 
ATOM   4953  N  NZ  . LYS E  1 76  ? 117.278 24.816  44.389 1.00 84.01  ? 70  LYS E NZ  1 
ATOM   4954  N  N   . HIS E  1 77  ? 118.220 31.890  46.524 1.00 25.13  ? 71  HIS E N   1 
ATOM   4955  C  CA  . HIS E  1 77  ? 118.990 32.744  47.416 1.00 28.43  ? 71  HIS E CA  1 
ATOM   4956  C  C   . HIS E  1 77  ? 120.500 32.621  47.189 1.00 33.11  ? 71  HIS E C   1 
ATOM   4957  O  O   . HIS E  1 77  ? 120.998 31.572  46.777 1.00 35.68  ? 71  HIS E O   1 
ATOM   4958  C  CB  . HIS E  1 77  ? 118.660 32.425  48.874 1.00 25.79  ? 71  HIS E CB  1 
ATOM   4959  C  CG  . HIS E  1 77  ? 119.441 33.234  49.863 1.00 33.35  ? 71  HIS E CG  1 
ATOM   4960  N  ND1 . HIS E  1 77  ? 119.138 34.544  50.166 1.00 35.94  ? 71  HIS E ND1 1 
ATOM   4961  C  CD2 . HIS E  1 77  ? 120.525 32.917  50.612 1.00 34.60  ? 71  HIS E CD2 1 
ATOM   4962  C  CE1 . HIS E  1 77  ? 119.998 34.997  51.061 1.00 33.61  ? 71  HIS E CE1 1 
ATOM   4963  N  NE2 . HIS E  1 77  ? 120.850 34.029  51.349 1.00 32.85  ? 71  HIS E NE2 1 
ATOM   4964  N  N   . GLY E  1 78  ? 121.213 33.717  47.444 1.00 30.31  ? 72  GLY E N   1 
ATOM   4965  C  CA  . GLY E  1 78  ? 122.651 33.746  47.295 1.00 26.54  ? 72  GLY E CA  1 
ATOM   4966  C  C   . GLY E  1 78  ? 123.283 34.928  48.017 1.00 33.36  ? 72  GLY E C   1 
ATOM   4967  O  O   . GLY E  1 78  ? 122.632 35.632  48.796 1.00 36.09  ? 72  GLY E O   1 
ATOM   4968  N  N   . GLY E  1 79  ? 124.572 35.135  47.770 1.00 35.86  ? 73  GLY E N   1 
ATOM   4969  C  CA  . GLY E  1 79  ? 125.283 36.250  48.368 1.00 34.91  ? 73  GLY E CA  1 
ATOM   4970  C  C   . GLY E  1 79  ? 125.222 37.358  47.338 1.00 39.54  ? 73  GLY E C   1 
ATOM   4971  O  O   . GLY E  1 79  ? 125.000 37.074  46.159 1.00 44.81  ? 73  GLY E O   1 
ATOM   4972  N  N   . PRO E  1 80  ? 125.412 38.626  47.728 1.00 36.88  ? 74  PRO E N   1 
ATOM   4973  C  CA  . PRO E  1 80  ? 125.347 39.716  46.750 1.00 32.80  ? 74  PRO E CA  1 
ATOM   4974  C  C   . PRO E  1 80  ? 126.286 39.612  45.549 1.00 36.18  ? 74  PRO E C   1 
ATOM   4975  O  O   . PRO E  1 80  ? 125.988 40.143  44.478 1.00 28.23  ? 74  PRO E O   1 
ATOM   4976  C  CB  . PRO E  1 80  ? 125.604 40.952  47.597 1.00 30.29  ? 74  PRO E CB  1 
ATOM   4977  C  CG  . PRO E  1 80  ? 126.408 40.422  48.754 1.00 28.18  ? 74  PRO E CG  1 
ATOM   4978  C  CD  . PRO E  1 80  ? 125.730 39.138  49.071 1.00 32.47  ? 74  PRO E CD  1 
ATOM   4979  N  N   . LYS E  1 81  ? 127.411 38.924  45.706 1.00 34.89  ? 75  LYS E N   1 
ATOM   4980  C  CA  . LYS E  1 81  ? 128.338 38.798  44.588 1.00 35.74  ? 75  LYS E CA  1 
ATOM   4981  C  C   . LYS E  1 81  ? 127.911 37.700  43.621 1.00 36.80  ? 75  LYS E C   1 
ATOM   4982  O  O   . LYS E  1 81  ? 128.416 37.622  42.508 1.00 40.50  ? 75  LYS E O   1 
ATOM   4983  C  CB  . LYS E  1 81  ? 129.745 38.535  45.108 1.00 41.93  ? 75  LYS E CB  1 
ATOM   4984  C  CG  . LYS E  1 81  ? 130.344 39.705  45.878 1.00 46.27  ? 75  LYS E CG  1 
ATOM   4985  C  CD  . LYS E  1 81  ? 131.382 39.230  46.884 1.00 65.67  ? 75  LYS E CD  1 
ATOM   4986  C  CE  . LYS E  1 81  ? 132.490 38.420  46.218 1.00 71.84  ? 75  LYS E CE  1 
ATOM   4987  N  NZ  . LYS E  1 81  ? 133.437 37.859  47.225 1.00 87.32  ? 75  LYS E NZ  1 
ATOM   4988  N  N   . ASP E  1 82  ? 126.962 36.870  44.043 1.00 38.23  ? 76  ASP E N   1 
ATOM   4989  C  CA  . ASP E  1 82  ? 126.455 35.767  43.227 1.00 47.39  ? 76  ASP E CA  1 
ATOM   4990  C  C   . ASP E  1 82  ? 125.649 36.191  42.004 1.00 49.97  ? 76  ASP E C   1 
ATOM   4991  O  O   . ASP E  1 82  ? 125.070 37.272  41.969 1.00 50.13  ? 76  ASP E O   1 
ATOM   4992  C  CB  . ASP E  1 82  ? 125.548 34.859  44.057 1.00 53.88  ? 76  ASP E CB  1 
ATOM   4993  C  CG  . ASP E  1 82  ? 126.293 33.749  44.744 1.00 57.38  ? 76  ASP E CG  1 
ATOM   4994  O  OD1 . ASP E  1 82  ? 126.528 33.849  45.971 1.00 53.90  ? 76  ASP E OD1 1 
ATOM   4995  O  OD2 . ASP E  1 82  ? 126.635 32.767  44.050 1.00 71.89  ? 76  ASP E OD2 1 
ATOM   4996  N  N   . GLU E  1 83  ? 125.605 35.313  41.006 1.00 55.53  ? 77  GLU E N   1 
ATOM   4997  C  CA  . GLU E  1 83  ? 124.815 35.565  39.811 1.00 58.30  ? 77  GLU E CA  1 
ATOM   4998  C  C   . GLU E  1 83  ? 123.420 35.073  40.195 1.00 56.52  ? 77  GLU E C   1 
ATOM   4999  O  O   . GLU E  1 83  ? 122.416 35.719  39.903 1.00 58.11  ? 77  GLU E O   1 
ATOM   5000  C  CB  . GLU E  1 83  ? 125.374 34.781  38.615 1.00 67.87  ? 77  GLU E CB  1 
ATOM   5001  C  CG  . GLU E  1 83  ? 124.429 33.760  37.962 1.00 79.24  ? 77  GLU E CG  1 
ATOM   5002  C  CD  . GLU E  1 83  ? 123.234 34.395  37.266 1.00 82.78  ? 77  GLU E CD  1 
ATOM   5003  O  OE1 . GLU E  1 83  ? 123.419 35.439  36.597 1.00 79.66  ? 77  GLU E OE1 1 
ATOM   5004  O  OE2 . GLU E  1 83  ? 122.116 33.835  37.381 1.00 80.67  ? 77  GLU E OE2 1 
ATOM   5005  N  N   . GLU E  1 84  ? 123.367 33.928  40.870 1.00 53.65  ? 78  GLU E N   1 
ATOM   5006  C  CA  . GLU E  1 84  ? 122.098 33.378  41.321 1.00 49.17  ? 78  GLU E CA  1 
ATOM   5007  C  C   . GLU E  1 84  ? 121.796 33.967  42.696 1.00 46.36  ? 78  GLU E C   1 
ATOM   5008  O  O   . GLU E  1 84  ? 122.305 33.502  43.720 1.00 42.93  ? 78  GLU E O   1 
ATOM   5009  C  CB  . GLU E  1 84  ? 122.169 31.853  41.412 1.00 49.00  ? 78  GLU E CB  1 
ATOM   5010  C  CG  . GLU E  1 84  ? 120.847 31.177  41.776 1.00 58.15  ? 78  GLU E CG  1 
ATOM   5011  C  CD  . GLU E  1 84  ? 119.785 31.294  40.681 1.00 66.77  ? 78  GLU E CD  1 
ATOM   5012  O  OE1 . GLU E  1 84  ? 118.656 30.801  40.905 1.00 67.97  ? 78  GLU E OE1 1 
ATOM   5013  O  OE2 . GLU E  1 84  ? 120.068 31.872  39.601 1.00 61.80  ? 78  GLU E OE2 1 
ATOM   5014  N  N   . ARG E  1 85  ? 120.979 35.012  42.714 1.00 46.78  ? 79  ARG E N   1 
ATOM   5015  C  CA  . ARG E  1 85  ? 120.609 35.650  43.968 1.00 44.24  ? 79  ARG E CA  1 
ATOM   5016  C  C   . ARG E  1 85  ? 119.304 36.415  43.870 1.00 41.97  ? 79  ARG E C   1 
ATOM   5017  O  O   . ARG E  1 85  ? 118.864 36.788  42.785 1.00 37.61  ? 79  ARG E O   1 
ATOM   5018  C  CB  . ARG E  1 85  ? 121.705 36.613  44.406 1.00 43.44  ? 79  ARG E CB  1 
ATOM   5019  C  CG  . ARG E  1 85  ? 121.940 37.742  43.432 1.00 37.69  ? 79  ARG E CG  1 
ATOM   5020  C  CD  . ARG E  1 85  ? 121.484 39.032  44.032 1.00 37.25  ? 79  ARG E CD  1 
ATOM   5021  N  NE  . ARG E  1 85  ? 122.599 39.939  44.229 1.00 37.23  ? 79  ARG E NE  1 
ATOM   5022  C  CZ  . ARG E  1 85  ? 122.502 41.127  44.815 1.00 31.08  ? 79  ARG E CZ  1 
ATOM   5023  N  NH1 . ARG E  1 85  ? 121.342 41.559  45.273 1.00 20.95  ? 79  ARG E NH1 1 
ATOM   5024  N  NH2 . ARG E  1 85  ? 123.572 41.892  44.922 1.00 31.73  ? 79  ARG E NH2 1 
ATOM   5025  N  N   . HIS E  1 86  ? 118.688 36.634  45.023 1.00 37.25  ? 80  HIS E N   1 
ATOM   5026  C  CA  . HIS E  1 86  ? 117.460 37.401  45.104 1.00 29.81  ? 80  HIS E CA  1 
ATOM   5027  C  C   . HIS E  1 86  ? 117.896 38.860  44.973 1.00 28.22  ? 80  HIS E C   1 
ATOM   5028  O  O   . HIS E  1 86  ? 118.990 39.235  45.426 1.00 19.82  ? 80  HIS E O   1 
ATOM   5029  C  CB  . HIS E  1 86  ? 116.803 37.174  46.460 1.00 25.24  ? 80  HIS E CB  1 
ATOM   5030  C  CG  . HIS E  1 86  ? 116.369 35.764  46.688 1.00 28.20  ? 80  HIS E CG  1 
ATOM   5031  N  ND1 . HIS E  1 86  ? 116.291 35.207  47.944 1.00 21.36  ? 80  HIS E ND1 1 
ATOM   5032  C  CD2 . HIS E  1 86  ? 115.911 34.823  45.827 1.00 30.46  ? 80  HIS E CD2 1 
ATOM   5033  C  CE1 . HIS E  1 86  ? 115.796 33.986  47.850 1.00 29.36  ? 80  HIS E CE1 1 
ATOM   5034  N  NE2 . HIS E  1 86  ? 115.555 33.728  46.575 1.00 25.71  ? 80  HIS E NE2 1 
ATOM   5035  N  N   . VAL E  1 87  ? 117.061 39.681  44.346 1.00 26.21  ? 81  VAL E N   1 
ATOM   5036  C  CA  . VAL E  1 87  ? 117.412 41.079  44.185 1.00 25.19  ? 81  VAL E CA  1 
ATOM   5037  C  C   . VAL E  1 87  ? 117.656 41.701  45.566 1.00 23.27  ? 81  VAL E C   1 
ATOM   5038  O  O   . VAL E  1 87  ? 118.495 42.579  45.722 1.00 21.95  ? 81  VAL E O   1 
ATOM   5039  C  CB  . VAL E  1 87  ? 116.295 41.847  43.426 1.00 31.06  ? 81  VAL E CB  1 
ATOM   5040  C  CG1 . VAL E  1 87  ? 116.527 43.345  43.527 1.00 28.99  ? 81  VAL E CG1 1 
ATOM   5041  C  CG2 . VAL E  1 87  ? 116.285 41.427  41.940 1.00 24.97  ? 81  VAL E CG2 1 
ATOM   5042  N  N   . GLY E  1 88  ? 116.950 41.213  46.575 1.00 17.69  ? 82  GLY E N   1 
ATOM   5043  C  CA  . GLY E  1 88  ? 117.112 41.773  47.900 1.00 19.11  ? 82  GLY E CA  1 
ATOM   5044  C  C   . GLY E  1 88  ? 118.151 41.097  48.771 1.00 25.88  ? 82  GLY E C   1 
ATOM   5045  O  O   . GLY E  1 88  ? 118.168 41.308  49.987 1.00 21.24  ? 82  GLY E O   1 
ATOM   5046  N  N   . ASP E  1 89  ? 119.028 40.297  48.169 1.00 25.80  ? 83  ASP E N   1 
ATOM   5047  C  CA  . ASP E  1 89  ? 120.059 39.608  48.935 1.00 20.26  ? 83  ASP E CA  1 
ATOM   5048  C  C   . ASP E  1 89  ? 121.277 40.504  49.129 1.00 22.83  ? 83  ASP E C   1 
ATOM   5049  O  O   . ASP E  1 89  ? 122.153 40.607  48.258 1.00 25.73  ? 83  ASP E O   1 
ATOM   5050  C  CB  . ASP E  1 89  ? 120.464 38.290  48.244 1.00 20.76  ? 83  ASP E CB  1 
ATOM   5051  C  CG  . ASP E  1 89  ? 119.406 37.189  48.398 1.00 25.20  ? 83  ASP E CG  1 
ATOM   5052  O  OD1 . ASP E  1 89  ? 118.595 37.270  49.337 1.00 19.30  ? 83  ASP E OD1 1 
ATOM   5053  O  OD2 . ASP E  1 89  ? 119.394 36.226  47.603 1.00 26.97  ? 83  ASP E OD2 1 
ATOM   5054  N  N   . LEU E  1 90  ? 121.342 41.146  50.288 1.00 22.34  ? 84  LEU E N   1 
ATOM   5055  C  CA  . LEU E  1 90  ? 122.461 42.021  50.594 1.00 26.81  ? 84  LEU E CA  1 
ATOM   5056  C  C   . LEU E  1 90  ? 123.555 41.358  51.460 1.00 30.86  ? 84  LEU E C   1 
ATOM   5057  O  O   . LEU E  1 90  ? 124.483 42.023  51.922 1.00 29.94  ? 84  LEU E O   1 
ATOM   5058  C  CB  . LEU E  1 90  ? 121.927 43.298  51.255 1.00 20.76  ? 84  LEU E CB  1 
ATOM   5059  C  CG  . LEU E  1 90  ? 121.069 44.121  50.283 1.00 24.82  ? 84  LEU E CG  1 
ATOM   5060  C  CD1 . LEU E  1 90  ? 120.562 45.403  50.935 1.00 25.56  ? 84  LEU E CD1 1 
ATOM   5061  C  CD2 . LEU E  1 90  ? 121.905 44.471  49.068 1.00 19.95  ? 84  LEU E CD2 1 
ATOM   5062  N  N   . GLY E  1 91  ? 123.466 40.048  51.673 1.00 23.70  ? 85  GLY E N   1 
ATOM   5063  C  CA  . GLY E  1 91  ? 124.488 39.390  52.471 1.00 23.23  ? 85  GLY E CA  1 
ATOM   5064  C  C   . GLY E  1 91  ? 124.400 39.550  53.987 1.00 27.83  ? 85  GLY E C   1 
ATOM   5065  O  O   . GLY E  1 91  ? 123.326 39.439  54.581 1.00 28.23  ? 85  GLY E O   1 
ATOM   5066  N  N   . ASN E  1 92  ? 125.537 39.809  54.619 1.00 24.80  ? 86  ASN E N   1 
ATOM   5067  C  CA  . ASN E  1 92  ? 125.588 39.952  56.066 1.00 26.98  ? 86  ASN E CA  1 
ATOM   5068  C  C   . ASN E  1 92  ? 126.161 41.284  56.471 1.00 29.89  ? 86  ASN E C   1 
ATOM   5069  O  O   . ASN E  1 92  ? 126.858 41.944  55.687 1.00 21.91  ? 86  ASN E O   1 
ATOM   5070  C  CB  . ASN E  1 92  ? 126.505 38.895  56.695 1.00 24.52  ? 86  ASN E CB  1 
ATOM   5071  C  CG  . ASN E  1 92  ? 125.915 37.511  56.685 1.00 34.27  ? 86  ASN E CG  1 
ATOM   5072  O  OD1 . ASN E  1 92  ? 124.877 37.256  57.299 1.00 34.50  ? 86  ASN E OD1 1 
ATOM   5073  N  ND2 . ASN E  1 92  ? 126.583 36.595  55.995 1.00 24.51  ? 86  ASN E ND2 1 
ATOM   5074  N  N   . VAL E  1 93  ? 125.859 41.676  57.704 1.00 19.82  ? 87  VAL E N   1 
ATOM   5075  C  CA  . VAL E  1 93  ? 126.449 42.881  58.258 1.00 23.51  ? 87  VAL E CA  1 
ATOM   5076  C  C   . VAL E  1 93  ? 127.150 42.346  59.499 1.00 27.32  ? 87  VAL E C   1 
ATOM   5077  O  O   . VAL E  1 93  ? 126.818 41.257  60.002 1.00 21.30  ? 87  VAL E O   1 
ATOM   5078  C  CB  . VAL E  1 93  ? 125.409 43.967  58.623 1.00 25.36  ? 87  VAL E CB  1 
ATOM   5079  C  CG1 . VAL E  1 93  ? 124.768 44.504  57.336 1.00 19.73  ? 87  VAL E CG1 1 
ATOM   5080  C  CG2 . VAL E  1 93  ? 124.368 43.415  59.581 1.00 17.45  ? 87  VAL E CG2 1 
ATOM   5081  N  N   . THR E  1 94  ? 128.115 43.099  59.993 1.00 24.57  ? 88  THR E N   1 
ATOM   5082  C  CA  . THR E  1 94  ? 128.891 42.642  61.128 1.00 26.56  ? 88  THR E CA  1 
ATOM   5083  C  C   . THR E  1 94  ? 128.795 43.503  62.361 1.00 27.41  ? 88  THR E C   1 
ATOM   5084  O  O   . THR E  1 94  ? 129.185 44.679  62.353 1.00 19.26  ? 88  THR E O   1 
ATOM   5085  C  CB  . THR E  1 94  ? 130.368 42.548  60.742 1.00 27.61  ? 88  THR E CB  1 
ATOM   5086  O  OG1 . THR E  1 94  ? 130.496 41.685  59.606 1.00 29.11  ? 88  THR E OG1 1 
ATOM   5087  C  CG2 . THR E  1 94  ? 131.188 42.008  61.902 1.00 25.64  ? 88  THR E CG2 1 
ATOM   5088  N  N   . ALA E  1 95  ? 128.284 42.916  63.431 1.00 24.82  ? 89  ALA E N   1 
ATOM   5089  C  CA  . ALA E  1 95  ? 128.182 43.657  64.678 1.00 33.97  ? 89  ALA E CA  1 
ATOM   5090  C  C   . ALA E  1 95  ? 129.497 43.440  65.410 1.00 38.43  ? 89  ALA E C   1 
ATOM   5091  O  O   . ALA E  1 95  ? 129.921 42.292  65.580 1.00 33.29  ? 89  ALA E O   1 
ATOM   5092  C  CB  . ALA E  1 95  ? 127.029 43.139  65.505 1.00 31.06  ? 89  ALA E CB  1 
ATOM   5093  N  N   . ASP E  1 96  ? 130.136 44.543  65.813 1.00 41.97  ? 90  ASP E N   1 
ATOM   5094  C  CA  . ASP E  1 96  ? 131.410 44.515  66.536 1.00 40.78  ? 90  ASP E CA  1 
ATOM   5095  C  C   . ASP E  1 96  ? 131.190 44.103  67.996 1.00 40.61  ? 90  ASP E C   1 
ATOM   5096  O  O   . ASP E  1 96  ? 130.062 43.798  68.393 1.00 33.19  ? 90  ASP E O   1 
ATOM   5097  C  CB  . ASP E  1 96  ? 132.132 45.884  66.417 1.00 46.13  ? 90  ASP E CB  1 
ATOM   5098  C  CG  . ASP E  1 96  ? 131.334 47.074  67.027 1.00 52.82  ? 90  ASP E CG  1 
ATOM   5099  O  OD1 . ASP E  1 96  ? 131.481 48.205  66.508 1.00 54.87  ? 90  ASP E OD1 1 
ATOM   5100  O  OD2 . ASP E  1 96  ? 130.590 46.912  68.020 1.00 41.14  ? 90  ASP E OD2 1 
ATOM   5101  N  N   . LYS E  1 97  ? 132.252 44.075  68.799 1.00 45.84  ? 91  LYS E N   1 
ATOM   5102  C  CA  . LYS E  1 97  ? 132.108 43.645  70.194 1.00 47.34  ? 91  LYS E CA  1 
ATOM   5103  C  C   . LYS E  1 97  ? 131.202 44.545  71.032 1.00 44.11  ? 91  LYS E C   1 
ATOM   5104  O  O   . LYS E  1 97  ? 130.726 44.141  72.098 1.00 39.03  ? 91  LYS E O   1 
ATOM   5105  C  CB  . LYS E  1 97  ? 133.479 43.506  70.867 1.00 47.79  ? 91  LYS E CB  1 
ATOM   5106  C  CG  . LYS E  1 97  ? 134.234 44.811  71.035 1.00 66.41  ? 91  LYS E CG  1 
ATOM   5107  C  CD  . LYS E  1 97  ? 135.616 44.569  71.626 1.00 72.80  ? 91  LYS E CD  1 
ATOM   5108  C  CE  . LYS E  1 97  ? 136.460 45.834  71.597 1.00 77.38  ? 91  LYS E CE  1 
ATOM   5109  N  NZ  . LYS E  1 97  ? 137.856 45.569  72.049 1.00 78.59  ? 91  LYS E NZ  1 
ATOM   5110  N  N   . ASP E  1 98  ? 130.946 45.755  70.548 1.00 39.76  ? 92  ASP E N   1 
ATOM   5111  C  CA  . ASP E  1 98  ? 130.080 46.684  71.263 1.00 40.80  ? 92  ASP E CA  1 
ATOM   5112  C  C   . ASP E  1 98  ? 128.621 46.591  70.829 1.00 39.80  ? 92  ASP E C   1 
ATOM   5113  O  O   . ASP E  1 98  ? 127.844 47.516  71.045 1.00 42.22  ? 92  ASP E O   1 
ATOM   5114  C  CB  . ASP E  1 98  ? 130.597 48.100  71.075 1.00 51.01  ? 92  ASP E CB  1 
ATOM   5115  C  CG  . ASP E  1 98  ? 131.987 48.271  71.647 1.00 73.87  ? 92  ASP E CG  1 
ATOM   5116  O  OD1 . ASP E  1 98  ? 132.135 48.122  72.888 1.00 68.71  ? 92  ASP E OD1 1 
ATOM   5117  O  OD2 . ASP E  1 98  ? 132.930 48.534  70.859 1.00 83.36  ? 92  ASP E OD2 1 
ATOM   5118  N  N   . ALA E  1 99  ? 128.262 45.465  70.220 1.00 36.59  ? 93  ALA E N   1 
ATOM   5119  C  CA  . ALA E  1 99  ? 126.901 45.208  69.758 1.00 37.27  ? 93  ALA E CA  1 
ATOM   5120  C  C   . ALA E  1 99  ? 126.431 46.182  68.683 1.00 37.04  ? 93  ALA E C   1 
ATOM   5121  O  O   . ALA E  1 99  ? 125.227 46.373  68.495 1.00 38.24  ? 93  ALA E O   1 
ATOM   5122  C  CB  . ALA E  1 99  ? 125.934 45.224  70.943 1.00 32.40  ? 93  ALA E CB  1 
ATOM   5123  N  N   . VAL E  1 100 ? 127.380 46.797  67.984 1.00 30.56  ? 94  VAL E N   1 
ATOM   5124  C  CA  . VAL E  1 100 ? 127.047 47.734  66.925 1.00 33.23  ? 94  VAL E CA  1 
ATOM   5125  C  C   . VAL E  1 100 ? 127.533 47.296  65.550 1.00 34.74  ? 94  VAL E C   1 
ATOM   5126  O  O   . VAL E  1 100 ? 128.704 46.966  65.352 1.00 31.66  ? 94  VAL E O   1 
ATOM   5127  C  CB  . VAL E  1 100 ? 127.628 49.142  67.178 1.00 36.29  ? 94  VAL E CB  1 
ATOM   5128  C  CG1 . VAL E  1 100 ? 127.422 50.010  65.935 1.00 31.47  ? 94  VAL E CG1 1 
ATOM   5129  C  CG2 . VAL E  1 100 ? 126.962 49.778  68.378 1.00 20.73  ? 94  VAL E CG2 1 
ATOM   5130  N  N   . ALA E  1 101 ? 126.620 47.301  64.595 1.00 31.51  ? 95  ALA E N   1 
ATOM   5131  C  CA  . ALA E  1 101 ? 126.969 46.948  63.236 1.00 34.35  ? 95  ALA E CA  1 
ATOM   5132  C  C   . ALA E  1 101 ? 126.998 48.238  62.440 1.00 33.53  ? 95  ALA E C   1 
ATOM   5133  O  O   . ALA E  1 101 ? 125.961 48.870  62.234 1.00 37.63  ? 95  ALA E O   1 
ATOM   5134  C  CB  . ALA E  1 101 ? 125.942 45.991  62.648 1.00 28.20  ? 95  ALA E CB  1 
ATOM   5135  N  N   . ASP E  1 102 ? 128.191 48.653  62.038 1.00 27.83  ? 96  ASP E N   1 
ATOM   5136  C  CA  . ASP E  1 102 ? 128.342 49.844  61.218 1.00 32.50  ? 96  ASP E CA  1 
ATOM   5137  C  C   . ASP E  1 102 ? 128.227 49.344  59.800 1.00 31.45  ? 96  ASP E C   1 
ATOM   5138  O  O   . ASP E  1 102 ? 129.119 48.679  59.302 1.00 45.01  ? 96  ASP E O   1 
ATOM   5139  C  CB  . ASP E  1 102 ? 129.706 50.467  61.444 1.00 35.75  ? 96  ASP E CB  1 
ATOM   5140  C  CG  . ASP E  1 102 ? 129.785 51.181  62.765 1.00 47.48  ? 96  ASP E CG  1 
ATOM   5141  O  OD1 . ASP E  1 102 ? 129.117 52.227  62.888 1.00 51.63  ? 96  ASP E OD1 1 
ATOM   5142  O  OD2 . ASP E  1 102 ? 130.488 50.697  63.679 1.00 55.64  ? 96  ASP E OD2 1 
ATOM   5143  N  N   . VAL E  1 103 ? 127.122 49.656  59.152 1.00 29.56  ? 97  VAL E N   1 
ATOM   5144  C  CA  . VAL E  1 103 ? 126.883 49.193  57.799 1.00 28.63  ? 97  VAL E CA  1 
ATOM   5145  C  C   . VAL E  1 103 ? 127.432 50.095  56.704 1.00 27.37  ? 97  VAL E C   1 
ATOM   5146  O  O   . VAL E  1 103 ? 127.358 51.312  56.799 1.00 33.02  ? 97  VAL E O   1 
ATOM   5147  C  CB  . VAL E  1 103 ? 125.371 49.001  57.575 1.00 30.18  ? 97  VAL E CB  1 
ATOM   5148  C  CG1 . VAL E  1 103 ? 125.101 48.478  56.170 1.00 23.25  ? 97  VAL E CG1 1 
ATOM   5149  C  CG2 . VAL E  1 103 ? 124.826 48.054  58.626 1.00 17.18  ? 97  VAL E CG2 1 
ATOM   5150  N  N   . SER E  1 104 ? 128.000 49.479  55.674 1.00 22.93  ? 98  SER E N   1 
ATOM   5151  C  CA  . SER E  1 104 ? 128.525 50.198  54.520 1.00 27.25  ? 98  SER E CA  1 
ATOM   5152  C  C   . SER E  1 104 ? 128.600 49.189  53.380 1.00 30.29  ? 98  SER E C   1 
ATOM   5153  O  O   . SER E  1 104 ? 129.476 48.339  53.346 1.00 40.10  ? 98  SER E O   1 
ATOM   5154  C  CB  . SER E  1 104 ? 129.900 50.780  54.806 1.00 28.79  ? 98  SER E CB  1 
ATOM   5155  O  OG  . SER E  1 104 ? 130.259 51.675  53.767 1.00 35.01  ? 98  SER E OG  1 
ATOM   5156  N  N   . ILE E  1 105 ? 127.663 49.300  52.450 1.00 30.20  ? 99  ILE E N   1 
ATOM   5157  C  CA  . ILE E  1 105 ? 127.534 48.382  51.334 1.00 24.85  ? 99  ILE E CA  1 
ATOM   5158  C  C   . ILE E  1 105 ? 127.245 49.120  50.040 1.00 27.01  ? 99  ILE E C   1 
ATOM   5159  O  O   . ILE E  1 105 ? 126.645 50.190  50.054 1.00 25.22  ? 99  ILE E O   1 
ATOM   5160  C  CB  . ILE E  1 105 ? 126.331 47.450  51.578 1.00 27.39  ? 99  ILE E CB  1 
ATOM   5161  C  CG1 . ILE E  1 105 ? 126.635 46.480  52.703 1.00 27.70  ? 99  ILE E CG1 1 
ATOM   5162  C  CG2 . ILE E  1 105 ? 125.929 46.744  50.310 1.00 24.71  ? 99  ILE E CG2 1 
ATOM   5163  C  CD1 . ILE E  1 105 ? 125.421 45.615  53.043 1.00 25.27  ? 99  ILE E CD1 1 
ATOM   5164  N  N   . GLU E  1 106 ? 127.659 48.528  48.925 1.00 31.12  ? 100 GLU E N   1 
ATOM   5165  C  CA  . GLU E  1 106 ? 127.393 49.078  47.600 1.00 31.03  ? 100 GLU E CA  1 
ATOM   5166  C  C   . GLU E  1 106 ? 126.813 47.930  46.780 1.00 30.03  ? 100 GLU E C   1 
ATOM   5167  O  O   . GLU E  1 106 ? 127.364 46.837  46.763 1.00 32.50  ? 100 GLU E O   1 
ATOM   5168  C  CB  . GLU E  1 106 ? 128.664 49.607  46.941 1.00 29.27  ? 100 GLU E CB  1 
ATOM   5169  C  CG  . GLU E  1 106 ? 128.412 50.085  45.516 1.00 48.08  ? 100 GLU E CG  1 
ATOM   5170  C  CD  . GLU E  1 106 ? 129.490 51.019  44.973 1.00 48.43  ? 100 GLU E CD  1 
ATOM   5171  O  OE1 . GLU E  1 106 ? 129.787 52.038  45.637 1.00 43.43  ? 100 GLU E OE1 1 
ATOM   5172  O  OE2 . GLU E  1 106 ? 130.018 50.741  43.869 1.00 46.94  ? 100 GLU E OE2 1 
ATOM   5173  N  N   . ASP E  1 107 ? 125.693 48.160  46.114 1.00 27.98  ? 101 ASP E N   1 
ATOM   5174  C  CA  . ASP E  1 107 ? 125.070 47.095  45.345 1.00 28.29  ? 101 ASP E CA  1 
ATOM   5175  C  C   . ASP E  1 107 ? 124.588 47.571  43.985 1.00 31.84  ? 101 ASP E C   1 
ATOM   5176  O  O   . ASP E  1 107 ? 124.086 48.681  43.852 1.00 35.29  ? 101 ASP E O   1 
ATOM   5177  C  CB  . ASP E  1 107 ? 123.911 46.506  46.142 1.00 25.45  ? 101 ASP E CB  1 
ATOM   5178  C  CG  . ASP E  1 107 ? 123.372 45.234  45.525 1.00 34.59  ? 101 ASP E CG  1 
ATOM   5179  O  OD1 . ASP E  1 107 ? 122.400 45.304  44.741 1.00 35.84  ? 101 ASP E OD1 1 
ATOM   5180  O  OD2 . ASP E  1 107 ? 123.934 44.158  45.819 1.00 34.43  ? 101 ASP E OD2 1 
ATOM   5181  N  N   . SER E  1 108 ? 124.736 46.716  42.980 1.00 31.45  ? 102 SER E N   1 
ATOM   5182  C  CA  . SER E  1 108 ? 124.350 47.053  41.618 1.00 28.43  ? 102 SER E CA  1 
ATOM   5183  C  C   . SER E  1 108 ? 123.108 46.341  41.132 1.00 26.90  ? 102 SER E C   1 
ATOM   5184  O  O   . SER E  1 108 ? 122.706 46.512  39.983 1.00 33.98  ? 102 SER E O   1 
ATOM   5185  C  CB  . SER E  1 108 ? 125.510 46.741  40.671 1.00 23.22  ? 102 SER E CB  1 
ATOM   5186  O  OG  . SER E  1 108 ? 126.554 47.684  40.848 1.00 39.72  ? 102 SER E OG  1 
ATOM   5187  N  N   . VAL E  1 109 ? 122.506 45.531  41.990 1.00 26.85  ? 103 VAL E N   1 
ATOM   5188  C  CA  . VAL E  1 109 ? 121.305 44.800  41.611 1.00 28.44  ? 103 VAL E CA  1 
ATOM   5189  C  C   . VAL E  1 109 ? 120.046 45.507  42.115 1.00 31.43  ? 103 VAL E C   1 
ATOM   5190  O  O   . VAL E  1 109 ? 119.062 45.616  41.379 1.00 36.93  ? 103 VAL E O   1 
ATOM   5191  C  CB  . VAL E  1 109 ? 121.362 43.339  42.134 1.00 31.59  ? 103 VAL E CB  1 
ATOM   5192  C  CG1 . VAL E  1 109 ? 120.108 42.585  41.741 1.00 25.29  ? 103 VAL E CG1 1 
ATOM   5193  C  CG2 . VAL E  1 109 ? 122.604 42.640  41.563 1.00 27.45  ? 103 VAL E CG2 1 
ATOM   5194  N  N   . ILE E  1 110 ? 120.071 45.981  43.361 1.00 30.54  ? 104 ILE E N   1 
ATOM   5195  C  CA  . ILE E  1 110 ? 118.930 46.710  43.920 1.00 28.11  ? 104 ILE E CA  1 
ATOM   5196  C  C   . ILE E  1 110 ? 118.926 48.095  43.269 1.00 29.50  ? 104 ILE E C   1 
ATOM   5197  O  O   . ILE E  1 110 ? 119.916 48.507  42.671 1.00 32.62  ? 104 ILE E O   1 
ATOM   5198  C  CB  . ILE E  1 110 ? 119.052 46.919  45.452 1.00 21.05  ? 104 ILE E CB  1 
ATOM   5199  C  CG1 . ILE E  1 110 ? 120.329 47.680  45.769 1.00 21.60  ? 104 ILE E CG1 1 
ATOM   5200  C  CG2 . ILE E  1 110 ? 119.035 45.603  46.172 1.00 19.50  ? 104 ILE E CG2 1 
ATOM   5201  C  CD1 . ILE E  1 110 ? 120.519 47.989  47.227 1.00 18.38  ? 104 ILE E CD1 1 
ATOM   5202  N  N   . SER E  1 111 ? 117.815 48.813  43.369 1.00 31.52  ? 105 SER E N   1 
ATOM   5203  C  CA  . SER E  1 111 ? 117.751 50.160  42.803 1.00 29.53  ? 105 SER E CA  1 
ATOM   5204  C  C   . SER E  1 111 ? 116.724 50.984  43.577 1.00 23.19  ? 105 SER E C   1 
ATOM   5205  O  O   . SER E  1 111 ? 115.898 50.430  44.289 1.00 22.44  ? 105 SER E O   1 
ATOM   5206  C  CB  . SER E  1 111 ? 117.368 50.105  41.308 1.00 26.35  ? 105 SER E CB  1 
ATOM   5207  O  OG  . SER E  1 111 ? 117.567 51.366  40.667 1.00 23.30  ? 105 SER E OG  1 
ATOM   5208  N  N   . LEU E  1 112 ? 116.797 52.303  43.450 1.00 24.40  ? 106 LEU E N   1 
ATOM   5209  C  CA  . LEU E  1 112 ? 115.844 53.182  44.108 1.00 27.97  ? 106 LEU E CA  1 
ATOM   5210  C  C   . LEU E  1 112 ? 114.780 53.623  43.098 1.00 29.46  ? 106 LEU E C   1 
ATOM   5211  O  O   . LEU E  1 112 ? 113.982 54.509  43.385 1.00 35.31  ? 106 LEU E O   1 
ATOM   5212  C  CB  . LEU E  1 112 ? 116.557 54.397  44.716 1.00 17.39  ? 106 LEU E CB  1 
ATOM   5213  C  CG  . LEU E  1 112 ? 117.569 54.000  45.801 1.00 25.99  ? 106 LEU E CG  1 
ATOM   5214  C  CD1 . LEU E  1 112 ? 118.114 55.233  46.495 1.00 17.93  ? 106 LEU E CD1 1 
ATOM   5215  C  CD2 . LEU E  1 112 ? 116.909 53.073  46.808 1.00 21.64  ? 106 LEU E CD2 1 
ATOM   5216  N  N   . SER E  1 113 ? 114.782 52.995  41.918 1.00 27.29  ? 107 SER E N   1 
ATOM   5217  C  CA  . SER E  1 113 ? 113.807 53.280  40.850 1.00 28.21  ? 107 SER E CA  1 
ATOM   5218  C  C   . SER E  1 113 ? 113.756 52.108  39.875 1.00 28.97  ? 107 SER E C   1 
ATOM   5219  O  O   . SER E  1 113 ? 114.655 51.275  39.841 1.00 31.38  ? 107 SER E O   1 
ATOM   5220  C  CB  . SER E  1 113 ? 114.188 54.541  40.064 1.00 26.93  ? 107 SER E CB  1 
ATOM   5221  O  OG  . SER E  1 113 ? 115.410 54.344  39.368 1.00 32.58  ? 107 SER E OG  1 
ATOM   5222  N  N   . GLY E  1 114 ? 112.708 52.046  39.070 1.00 24.81  ? 108 GLY E N   1 
ATOM   5223  C  CA  . GLY E  1 114 ? 112.611 50.962  38.124 1.00 27.22  ? 108 GLY E CA  1 
ATOM   5224  C  C   . GLY E  1 114 ? 112.161 49.627  38.694 1.00 40.26  ? 108 GLY E C   1 
ATOM   5225  O  O   . GLY E  1 114 ? 111.713 49.512  39.836 1.00 38.82  ? 108 GLY E O   1 
ATOM   5226  N  N   . ASP E  1 115 ? 112.309 48.610  37.856 1.00 45.02  ? 109 ASP E N   1 
ATOM   5227  C  CA  . ASP E  1 115 ? 111.928 47.232  38.125 1.00 53.14  ? 109 ASP E CA  1 
ATOM   5228  C  C   . ASP E  1 115 ? 112.497 46.602  39.395 1.00 52.29  ? 109 ASP E C   1 
ATOM   5229  O  O   . ASP E  1 115 ? 111.858 45.734  39.999 1.00 47.56  ? 109 ASP E O   1 
ATOM   5230  C  CB  . ASP E  1 115 ? 112.312 46.402  36.897 1.00 63.34  ? 109 ASP E CB  1 
ATOM   5231  C  CG  . ASP E  1 115 ? 113.150 47.207  35.892 1.00 72.01  ? 109 ASP E CG  1 
ATOM   5232  O  OD1 . ASP E  1 115 ? 114.298 47.595  36.225 1.00 60.64  ? 109 ASP E OD1 1 
ATOM   5233  O  OD2 . ASP E  1 115 ? 112.654 47.466  34.770 1.00 78.60  ? 109 ASP E OD2 1 
ATOM   5234  N  N   . HIS E  1 116 ? 113.694 47.023  39.793 1.00 42.01  ? 110 HIS E N   1 
ATOM   5235  C  CA  . HIS E  1 116 ? 114.320 46.486  40.996 1.00 42.81  ? 110 HIS E CA  1 
ATOM   5236  C  C   . HIS E  1 116 ? 114.191 47.447  42.169 1.00 36.92  ? 110 HIS E C   1 
ATOM   5237  O  O   . HIS E  1 116 ? 114.896 47.307  43.163 1.00 38.48  ? 110 HIS E O   1 
ATOM   5238  C  CB  . HIS E  1 116 ? 115.811 46.202  40.751 1.00 39.08  ? 110 HIS E CB  1 
ATOM   5239  C  CG  . HIS E  1 116 ? 116.070 45.031  39.856 1.00 43.36  ? 110 HIS E CG  1 
ATOM   5240  N  ND1 . HIS E  1 116 ? 117.339 44.668  39.457 1.00 48.44  ? 110 HIS E ND1 1 
ATOM   5241  C  CD2 . HIS E  1 116 ? 115.226 44.139  39.284 1.00 40.12  ? 110 HIS E CD2 1 
ATOM   5242  C  CE1 . HIS E  1 116 ? 117.266 43.605  38.676 1.00 40.32  ? 110 HIS E CE1 1 
ATOM   5243  N  NE2 . HIS E  1 116 ? 115.995 43.264  38.555 1.00 41.84  ? 110 HIS E NE2 1 
ATOM   5244  N  N   . CYS E  1 117 ? 113.301 48.423  42.046 1.00 34.62  ? 111 CYS E N   1 
ATOM   5245  C  CA  . CYS E  1 117 ? 113.103 49.421  43.091 1.00 31.10  ? 111 CYS E CA  1 
ATOM   5246  C  C   . CYS E  1 117 ? 112.811 48.732  44.426 1.00 26.77  ? 111 CYS E C   1 
ATOM   5247  O  O   . CYS E  1 117 ? 111.987 47.820  44.492 1.00 23.83  ? 111 CYS E O   1 
ATOM   5248  C  CB  . CYS E  1 117 ? 111.941 50.346  42.699 1.00 32.53  ? 111 CYS E CB  1 
ATOM   5249  S  SG  . CYS E  1 117 ? 111.719 51.854  43.682 1.00 43.40  ? 111 CYS E SG  1 
ATOM   5250  N  N   . ILE E  1 118 ? 113.496 49.151  45.488 1.00 18.83  ? 112 ILE E N   1 
ATOM   5251  C  CA  . ILE E  1 118 ? 113.259 48.554  46.791 1.00 25.17  ? 112 ILE E CA  1 
ATOM   5252  C  C   . ILE E  1 118 ? 112.449 49.473  47.682 1.00 24.43  ? 112 ILE E C   1 
ATOM   5253  O  O   . ILE E  1 118 ? 112.062 49.090  48.782 1.00 22.89  ? 112 ILE E O   1 
ATOM   5254  C  CB  . ILE E  1 118 ? 114.571 48.191  47.530 1.00 27.25  ? 112 ILE E CB  1 
ATOM   5255  C  CG1 . ILE E  1 118 ? 115.517 49.393  47.569 1.00 22.32  ? 112 ILE E CG1 1 
ATOM   5256  C  CG2 . ILE E  1 118 ? 115.205 46.978  46.882 1.00 20.35  ? 112 ILE E CG2 1 
ATOM   5257  C  CD1 . ILE E  1 118 ? 116.707 49.189  48.559 1.00 19.86  ? 112 ILE E CD1 1 
ATOM   5258  N  N   . ILE E  1 119 ? 112.202 50.688  47.206 1.00 21.57  ? 113 ILE E N   1 
ATOM   5259  C  CA  . ILE E  1 119 ? 111.412 51.650  47.960 1.00 29.50  ? 113 ILE E CA  1 
ATOM   5260  C  C   . ILE E  1 119 ? 110.001 51.111  48.123 1.00 22.13  ? 113 ILE E C   1 
ATOM   5261  O  O   . ILE E  1 119 ? 109.384 50.659  47.161 1.00 24.40  ? 113 ILE E O   1 
ATOM   5262  C  CB  . ILE E  1 119 ? 111.387 53.027  47.254 1.00 31.48  ? 113 ILE E CB  1 
ATOM   5263  C  CG1 . ILE E  1 119 ? 112.748 53.707  47.454 1.00 27.07  ? 113 ILE E CG1 1 
ATOM   5264  C  CG2 . ILE E  1 119 ? 110.253 53.894  47.813 1.00 28.74  ? 113 ILE E CG2 1 
ATOM   5265  C  CD1 . ILE E  1 119 ? 112.964 54.909  46.615 1.00 27.66  ? 113 ILE E CD1 1 
ATOM   5266  N  N   . GLY E  1 120 ? 109.513 51.134  49.358 1.00 23.64  ? 114 GLY E N   1 
ATOM   5267  C  CA  . GLY E  1 120 ? 108.185 50.622  49.644 1.00 23.57  ? 114 GLY E CA  1 
ATOM   5268  C  C   . GLY E  1 120 ? 108.218 49.176  50.104 1.00 24.57  ? 114 GLY E C   1 
ATOM   5269  O  O   . GLY E  1 120 ? 107.180 48.586  50.406 1.00 25.46  ? 114 GLY E O   1 
ATOM   5270  N  N   . ARG E  1 121 ? 109.412 48.591  50.146 1.00 23.07  ? 115 ARG E N   1 
ATOM   5271  C  CA  . ARG E  1 121 ? 109.566 47.213  50.609 1.00 23.41  ? 115 ARG E CA  1 
ATOM   5272  C  C   . ARG E  1 121 ? 110.210 47.215  52.003 1.00 27.35  ? 115 ARG E C   1 
ATOM   5273  O  O   . ARG E  1 121 ? 110.429 48.289  52.580 1.00 28.27  ? 115 ARG E O   1 
ATOM   5274  C  CB  . ARG E  1 121 ? 110.372 46.421  49.592 1.00 20.42  ? 115 ARG E CB  1 
ATOM   5275  C  CG  . ARG E  1 121 ? 109.656 46.391  48.245 1.00 23.38  ? 115 ARG E CG  1 
ATOM   5276  C  CD  . ARG E  1 121 ? 110.456 45.703  47.174 1.00 28.25  ? 115 ARG E CD  1 
ATOM   5277  N  NE  . ARG E  1 121 ? 109.874 45.841  45.839 1.00 27.88  ? 115 ARG E NE  1 
ATOM   5278  C  CZ  . ARG E  1 121 ? 108.764 45.240  45.420 1.00 21.33  ? 115 ARG E CZ  1 
ATOM   5279  N  NH1 . ARG E  1 121 ? 108.346 45.440  44.180 1.00 17.53  ? 115 ARG E NH1 1 
ATOM   5280  N  NH2 . ARG E  1 121 ? 108.078 44.435  46.226 1.00 24.12  ? 115 ARG E NH2 1 
ATOM   5281  N  N   . THR E  1 122 ? 110.502 46.045  52.561 1.00 21.21  ? 116 THR E N   1 
ATOM   5282  C  CA  . THR E  1 122 ? 111.049 46.011  53.914 1.00 24.99  ? 116 THR E CA  1 
ATOM   5283  C  C   . THR E  1 122 ? 112.499 45.574  54.061 1.00 27.95  ? 116 THR E C   1 
ATOM   5284  O  O   . THR E  1 122 ? 112.929 44.581  53.486 1.00 29.48  ? 116 THR E O   1 
ATOM   5285  C  CB  . THR E  1 122 ? 110.190 45.098  54.834 1.00 23.57  ? 116 THR E CB  1 
ATOM   5286  O  OG1 . THR E  1 122 ? 108.851 45.587  54.879 1.00 24.71  ? 116 THR E OG1 1 
ATOM   5287  C  CG2 . THR E  1 122 ? 110.738 45.080  56.259 1.00 20.15  ? 116 THR E CG2 1 
ATOM   5288  N  N   . LEU E  1 123 ? 113.251 46.329  54.849 1.00 25.01  ? 117 LEU E N   1 
ATOM   5289  C  CA  . LEU E  1 123 ? 114.637 45.988  55.106 1.00 25.28  ? 117 LEU E CA  1 
ATOM   5290  C  C   . LEU E  1 123 ? 114.597 45.210  56.422 1.00 22.89  ? 117 LEU E C   1 
ATOM   5291  O  O   . LEU E  1 123 ? 113.952 45.631  57.385 1.00 24.17  ? 117 LEU E O   1 
ATOM   5292  C  CB  . LEU E  1 123 ? 115.484 47.254  55.258 1.00 17.62  ? 117 LEU E CB  1 
ATOM   5293  C  CG  . LEU E  1 123 ? 116.948 46.933  55.599 1.00 28.46  ? 117 LEU E CG  1 
ATOM   5294  C  CD1 . LEU E  1 123 ? 117.607 46.216  54.416 1.00 14.11  ? 117 LEU E CD1 1 
ATOM   5295  C  CD2 . LEU E  1 123 ? 117.705 48.202  55.945 1.00 21.56  ? 117 LEU E CD2 1 
ATOM   5296  N  N   . VAL E  1 124 ? 115.271 44.074  56.472 1.00 26.27  ? 118 VAL E N   1 
ATOM   5297  C  CA  . VAL E  1 124 ? 115.268 43.258  57.685 1.00 30.30  ? 118 VAL E CA  1 
ATOM   5298  C  C   . VAL E  1 124 ? 116.659 42.845  58.127 1.00 26.40  ? 118 VAL E C   1 
ATOM   5299  O  O   . VAL E  1 124 ? 117.475 42.450  57.299 1.00 26.32  ? 118 VAL E O   1 
ATOM   5300  C  CB  . VAL E  1 124 ? 114.472 41.942  57.481 1.00 34.02  ? 118 VAL E CB  1 
ATOM   5301  C  CG1 . VAL E  1 124 ? 114.507 41.105  58.764 1.00 22.84  ? 118 VAL E CG1 1 
ATOM   5302  C  CG2 . VAL E  1 124 ? 113.051 42.247  57.048 1.00 27.58  ? 118 VAL E CG2 1 
ATOM   5303  N  N   . VAL E  1 125 ? 116.928 42.939  59.426 1.00 23.73  ? 119 VAL E N   1 
ATOM   5304  C  CA  . VAL E  1 125 ? 118.205 42.492  59.951 1.00 17.91  ? 119 VAL E CA  1 
ATOM   5305  C  C   . VAL E  1 125 ? 117.903 41.208  60.730 1.00 21.98  ? 119 VAL E C   1 
ATOM   5306  O  O   . VAL E  1 125 ? 117.070 41.198  61.646 1.00 17.97  ? 119 VAL E O   1 
ATOM   5307  C  CB  . VAL E  1 125 ? 118.880 43.545  60.836 1.00 20.70  ? 119 VAL E CB  1 
ATOM   5308  C  CG1 . VAL E  1 125 ? 118.052 43.825  62.068 1.00 26.40  ? 119 VAL E CG1 1 
ATOM   5309  C  CG2 . VAL E  1 125 ? 120.277 43.053  61.206 1.00 22.79  ? 119 VAL E CG2 1 
ATOM   5310  N  N   . HIS E  1 126 ? 118.565 40.118  60.339 1.00 24.45  ? 120 HIS E N   1 
ATOM   5311  C  CA  . HIS E  1 126 ? 118.318 38.806  60.939 1.00 26.54  ? 120 HIS E CA  1 
ATOM   5312  C  C   . HIS E  1 126 ? 119.148 38.395  62.155 1.00 26.85  ? 120 HIS E C   1 
ATOM   5313  O  O   . HIS E  1 126 ? 120.151 39.008  62.492 1.00 24.38  ? 120 HIS E O   1 
ATOM   5314  C  CB  . HIS E  1 126 ? 118.424 37.730  59.858 1.00 22.87  ? 120 HIS E CB  1 
ATOM   5315  C  CG  . HIS E  1 126 ? 117.337 37.797  58.827 1.00 30.95  ? 120 HIS E CG  1 
ATOM   5316  N  ND1 . HIS E  1 126 ? 116.177 37.056  58.915 1.00 26.46  ? 120 HIS E ND1 1 
ATOM   5317  C  CD2 . HIS E  1 126 ? 117.244 38.505  57.673 1.00 28.19  ? 120 HIS E CD2 1 
ATOM   5318  C  CE1 . HIS E  1 126 ? 115.420 37.299  57.858 1.00 33.03  ? 120 HIS E CE1 1 
ATOM   5319  N  NE2 . HIS E  1 126 ? 116.044 38.174  57.088 1.00 31.98  ? 120 HIS E NE2 1 
ATOM   5320  N  N   . GLU E  1 127 ? 118.683 37.334  62.806 1.00 34.93  ? 121 GLU E N   1 
ATOM   5321  C  CA  . GLU E  1 127 ? 119.281 36.765  64.012 1.00 37.07  ? 121 GLU E CA  1 
ATOM   5322  C  C   . GLU E  1 127 ? 120.659 36.140  63.853 1.00 36.51  ? 121 GLU E C   1 
ATOM   5323  O  O   . GLU E  1 127 ? 121.561 36.396  64.640 1.00 34.90  ? 121 GLU E O   1 
ATOM   5324  C  CB  . GLU E  1 127 ? 118.344 35.705  64.541 1.00 43.07  ? 121 GLU E CB  1 
ATOM   5325  C  CG  . GLU E  1 127 ? 118.764 35.070  65.823 1.00 46.96  ? 121 GLU E CG  1 
ATOM   5326  C  CD  . GLU E  1 127 ? 117.902 33.872  66.132 1.00 55.30  ? 121 GLU E CD  1 
ATOM   5327  O  OE1 . GLU E  1 127 ? 117.755 33.572  67.334 1.00 62.56  ? 121 GLU E OE1 1 
ATOM   5328  O  OE2 . GLU E  1 127 ? 117.382 33.236  65.171 1.00 42.86  ? 121 GLU E OE2 1 
ATOM   5329  N  N   . LYS E  1 128 ? 120.803 35.307  62.832 1.00 36.90  ? 122 LYS E N   1 
ATOM   5330  C  CA  . LYS E  1 128 ? 122.050 34.606  62.567 1.00 36.27  ? 122 LYS E CA  1 
ATOM   5331  C  C   . LYS E  1 128 ? 122.658 35.040  61.248 1.00 36.99  ? 122 LYS E C   1 
ATOM   5332  O  O   . LYS E  1 128 ? 122.071 35.803  60.488 1.00 41.46  ? 122 LYS E O   1 
ATOM   5333  C  CB  . LYS E  1 128 ? 121.799 33.094  62.483 1.00 41.38  ? 122 LYS E CB  1 
ATOM   5334  C  CG  . LYS E  1 128 ? 120.873 32.527  63.540 1.00 41.83  ? 122 LYS E CG  1 
ATOM   5335  C  CD  . LYS E  1 128 ? 120.640 31.016  63.340 1.00 51.95  ? 122 LYS E CD  1 
ATOM   5336  C  CE  . LYS E  1 128 ? 119.853 30.713  62.079 1.00 56.97  ? 122 LYS E CE  1 
ATOM   5337  N  NZ  . LYS E  1 128 ? 119.603 29.259  61.906 1.00 62.62  ? 122 LYS E NZ  1 
ATOM   5338  N  N   . ALA E  1 129 ? 123.838 34.505  60.976 1.00 34.87  ? 123 ALA E N   1 
ATOM   5339  C  CA  . ALA E  1 129 ? 124.556 34.793  59.748 1.00 37.30  ? 123 ALA E CA  1 
ATOM   5340  C  C   . ALA E  1 129 ? 123.804 34.212  58.559 1.00 28.95  ? 123 ALA E C   1 
ATOM   5341  O  O   . ALA E  1 129 ? 123.036 33.271  58.703 1.00 30.64  ? 123 ALA E O   1 
ATOM   5342  C  CB  . ALA E  1 129 ? 125.967 34.192  59.818 1.00 26.30  ? 123 ALA E CB  1 
ATOM   5343  N  N   . ASP E  1 130 ? 124.031 34.788  57.387 1.00 25.39  ? 124 ASP E N   1 
ATOM   5344  C  CA  . ASP E  1 130 ? 123.408 34.321  56.159 1.00 25.55  ? 124 ASP E CA  1 
ATOM   5345  C  C   . ASP E  1 130 ? 124.456 33.420  55.482 1.00 27.92  ? 124 ASP E C   1 
ATOM   5346  O  O   . ASP E  1 130 ? 125.569 33.860  55.188 1.00 29.27  ? 124 ASP E O   1 
ATOM   5347  C  CB  . ASP E  1 130 ? 123.077 35.533  55.293 1.00 28.91  ? 124 ASP E CB  1 
ATOM   5348  C  CG  . ASP E  1 130 ? 122.539 35.163  53.922 1.00 29.79  ? 124 ASP E CG  1 
ATOM   5349  O  OD1 . ASP E  1 130 ? 122.098 36.087  53.207 1.00 37.15  ? 124 ASP E OD1 1 
ATOM   5350  O  OD2 . ASP E  1 130 ? 122.558 33.977  53.549 1.00 27.97  ? 124 ASP E OD2 1 
ATOM   5351  N  N   . ASP E  1 131 ? 124.104 32.162  55.242 1.00 23.44  ? 125 ASP E N   1 
ATOM   5352  C  CA  . ASP E  1 131 ? 125.035 31.222  54.631 1.00 22.61  ? 125 ASP E CA  1 
ATOM   5353  C  C   . ASP E  1 131 ? 125.208 31.421  53.129 1.00 29.12  ? 125 ASP E C   1 
ATOM   5354  O  O   . ASP E  1 131 ? 125.874 30.627  52.452 1.00 25.95  ? 125 ASP E O   1 
ATOM   5355  C  CB  . ASP E  1 131 ? 124.603 29.779  54.951 1.00 13.83  ? 125 ASP E CB  1 
ATOM   5356  C  CG  . ASP E  1 131 ? 123.321 29.358  54.233 1.00 27.96  ? 125 ASP E CG  1 
ATOM   5357  O  OD1 . ASP E  1 131 ? 122.607 28.504  54.794 1.00 22.77  ? 125 ASP E OD1 1 
ATOM   5358  O  OD2 . ASP E  1 131 ? 123.033 29.847  53.111 1.00 24.72  ? 125 ASP E OD2 1 
ATOM   5359  N  N   . LEU E  1 132 ? 124.602 32.481  52.606 1.00 29.63  ? 126 LEU E N   1 
ATOM   5360  C  CA  . LEU E  1 132 ? 124.701 32.804  51.184 1.00 30.33  ? 126 LEU E CA  1 
ATOM   5361  C  C   . LEU E  1 132 ? 124.337 31.669  50.229 1.00 27.47  ? 126 LEU E C   1 
ATOM   5362  O  O   . LEU E  1 132 ? 124.921 31.533  49.146 1.00 28.00  ? 126 LEU E O   1 
ATOM   5363  C  CB  . LEU E  1 132 ? 126.108 33.300  50.863 1.00 28.32  ? 126 LEU E CB  1 
ATOM   5364  C  CG  . LEU E  1 132 ? 126.727 34.268  51.873 1.00 38.26  ? 126 LEU E CG  1 
ATOM   5365  C  CD1 . LEU E  1 132 ? 128.149 34.586  51.393 1.00 29.80  ? 126 LEU E CD1 1 
ATOM   5366  C  CD2 . LEU E  1 132 ? 125.867 35.550  52.041 1.00 27.77  ? 126 LEU E CD2 1 
ATOM   5367  N  N   . GLY E  1 133 ? 123.376 30.851  50.638 1.00 30.75  ? 127 GLY E N   1 
ATOM   5368  C  CA  . GLY E  1 133 ? 122.910 29.758  49.796 1.00 34.39  ? 127 GLY E CA  1 
ATOM   5369  C  C   . GLY E  1 133 ? 123.790 28.528  49.673 1.00 34.93  ? 127 GLY E C   1 
ATOM   5370  O  O   . GLY E  1 133 ? 123.565 27.693  48.791 1.00 29.48  ? 127 GLY E O   1 
ATOM   5371  N  N   . LYS E  1 134 ? 124.759 28.392  50.574 1.00 34.61  ? 128 LYS E N   1 
ATOM   5372  C  CA  . LYS E  1 134 ? 125.688 27.268  50.530 1.00 34.07  ? 128 LYS E CA  1 
ATOM   5373  C  C   . LYS E  1 134 ? 125.521 26.315  51.707 1.00 36.87  ? 128 LYS E C   1 
ATOM   5374  O  O   . LYS E  1 134 ? 126.436 25.545  52.022 1.00 40.52  ? 128 LYS E O   1 
ATOM   5375  C  CB  . LYS E  1 134 ? 127.123 27.807  50.472 1.00 30.75  ? 128 LYS E CB  1 
ATOM   5376  C  CG  . LYS E  1 134 ? 127.306 28.877  49.391 1.00 41.47  ? 128 LYS E CG  1 
ATOM   5377  C  CD  . LYS E  1 134 ? 128.662 29.560  49.420 1.00 40.66  ? 128 LYS E CD  1 
ATOM   5378  C  CE  . LYS E  1 134 ? 129.741 28.684  48.819 1.00 61.14  ? 128 LYS E CE  1 
ATOM   5379  N  NZ  . LYS E  1 134 ? 131.010 29.434  48.551 1.00 72.37  ? 128 LYS E NZ  1 
ATOM   5380  N  N   . GLY E  1 135 ? 124.347 26.354  52.337 1.00 27.32  ? 129 GLY E N   1 
ATOM   5381  C  CA  . GLY E  1 135 ? 124.076 25.501  53.482 1.00 26.64  ? 129 GLY E CA  1 
ATOM   5382  C  C   . GLY E  1 135 ? 123.692 24.057  53.199 1.00 30.72  ? 129 GLY E C   1 
ATOM   5383  O  O   . GLY E  1 135 ? 123.562 23.248  54.133 1.00 26.41  ? 129 GLY E O   1 
ATOM   5384  N  N   . GLY E  1 136 ? 123.465 23.723  51.933 1.00 19.23  ? 130 GLY E N   1 
ATOM   5385  C  CA  . GLY E  1 136 ? 123.126 22.344  51.619 1.00 32.30  ? 130 GLY E CA  1 
ATOM   5386  C  C   . GLY E  1 136 ? 121.694 21.858  51.776 1.00 36.09  ? 130 GLY E C   1 
ATOM   5387  O  O   . GLY E  1 136 ? 121.452 20.651  51.709 1.00 39.39  ? 130 GLY E O   1 
ATOM   5388  N  N   . ASN E  1 137 ? 120.750 22.768  52.005 1.00 41.80  ? 131 ASN E N   1 
ATOM   5389  C  CA  . ASN E  1 137 ? 119.333 22.402  52.125 1.00 41.52  ? 131 ASN E CA  1 
ATOM   5390  C  C   . ASN E  1 137 ? 118.443 23.473  51.497 1.00 42.04  ? 131 ASN E C   1 
ATOM   5391  O  O   . ASN E  1 137 ? 118.929 24.498  51.024 1.00 43.76  ? 131 ASN E O   1 
ATOM   5392  C  CB  . ASN E  1 137 ? 118.913 22.162  53.588 1.00 31.31  ? 131 ASN E CB  1 
ATOM   5393  C  CG  . ASN E  1 137 ? 119.210 23.335  54.490 1.00 35.01  ? 131 ASN E CG  1 
ATOM   5394  O  OD1 . ASN E  1 137 ? 119.088 24.490  54.090 1.00 40.72  ? 131 ASN E OD1 1 
ATOM   5395  N  ND2 . ASN E  1 137 ? 119.581 23.045  55.730 1.00 33.20  ? 131 ASN E ND2 1 
ATOM   5396  N  N   . GLU E  1 138 ? 117.139 23.222  51.487 1.00 48.31  ? 132 GLU E N   1 
ATOM   5397  C  CA  . GLU E  1 138 ? 116.166 24.140  50.899 1.00 48.43  ? 132 GLU E CA  1 
ATOM   5398  C  C   . GLU E  1 138 ? 116.119 25.497  51.605 1.00 43.21  ? 132 GLU E C   1 
ATOM   5399  O  O   . GLU E  1 138 ? 116.093 26.544  50.955 1.00 37.46  ? 132 GLU E O   1 
ATOM   5400  C  CB  . GLU E  1 138 ? 114.797 23.474  50.903 1.00 55.24  ? 132 GLU E CB  1 
ATOM   5401  C  CG  . GLU E  1 138 ? 113.682 24.323  50.368 1.00 79.57  ? 132 GLU E CG  1 
ATOM   5402  C  CD  . GLU E  1 138 ? 112.433 23.510  50.107 1.00 89.24  ? 132 GLU E CD  1 
ATOM   5403  O  OE1 . GLU E  1 138 ? 112.051 22.710  50.991 1.00 91.19  ? 132 GLU E OE1 1 
ATOM   5404  O  OE2 . GLU E  1 138 ? 111.835 23.674  49.019 1.00 95.66  ? 132 GLU E OE2 1 
ATOM   5405  N  N   . GLU E  1 139 ? 116.123 25.477  52.934 1.00 39.01  ? 133 GLU E N   1 
ATOM   5406  C  CA  . GLU E  1 139 ? 116.104 26.709  53.719 1.00 40.78  ? 133 GLU E CA  1 
ATOM   5407  C  C   . GLU E  1 139 ? 117.250 27.674  53.329 1.00 41.94  ? 133 GLU E C   1 
ATOM   5408  O  O   . GLU E  1 139 ? 117.110 28.899  53.403 1.00 41.47  ? 133 GLU E O   1 
ATOM   5409  C  CB  . GLU E  1 139 ? 116.190 26.367  55.212 1.00 34.22  ? 133 GLU E CB  1 
ATOM   5410  C  CG  . GLU E  1 139 ? 116.079 27.572  56.139 1.00 49.71  ? 133 GLU E CG  1 
ATOM   5411  C  CD  . GLU E  1 139 ? 114.676 28.175  56.186 1.00 55.32  ? 133 GLU E CD  1 
ATOM   5412  O  OE1 . GLU E  1 139 ? 114.539 29.325  56.660 1.00 63.08  ? 133 GLU E OE1 1 
ATOM   5413  O  OE2 . GLU E  1 139 ? 113.710 27.502  55.768 1.00 55.85  ? 133 GLU E OE2 1 
ATOM   5414  N  N   . SER E  1 140 ? 118.381 27.117  52.910 1.00 37.44  ? 134 SER E N   1 
ATOM   5415  C  CA  . SER E  1 140 ? 119.521 27.929  52.523 1.00 36.56  ? 134 SER E CA  1 
ATOM   5416  C  C   . SER E  1 140 ? 119.329 28.590  51.154 1.00 32.53  ? 134 SER E C   1 
ATOM   5417  O  O   . SER E  1 140 ? 119.830 29.680  50.919 1.00 28.83  ? 134 SER E O   1 
ATOM   5418  C  CB  . SER E  1 140 ? 120.796 27.080  52.520 1.00 35.53  ? 134 SER E CB  1 
ATOM   5419  O  OG  . SER E  1 140 ? 121.885 27.789  51.957 1.00 32.45  ? 134 SER E OG  1 
ATOM   5420  N  N   . THR E  1 141 ? 118.617 27.938  50.248 1.00 34.74  ? 135 THR E N   1 
ATOM   5421  C  CA  . THR E  1 141 ? 118.395 28.516  48.926 1.00 39.82  ? 135 THR E CA  1 
ATOM   5422  C  C   . THR E  1 141 ? 117.195 29.464  48.936 1.00 39.13  ? 135 THR E C   1 
ATOM   5423  O  O   . THR E  1 141 ? 116.829 30.038  47.906 1.00 36.96  ? 135 THR E O   1 
ATOM   5424  C  CB  . THR E  1 141 ? 118.174 27.421  47.872 1.00 44.26  ? 135 THR E CB  1 
ATOM   5425  O  OG1 . THR E  1 141 ? 117.105 26.558  48.285 1.00 50.78  ? 135 THR E OG1 1 
ATOM   5426  C  CG2 . THR E  1 141 ? 119.429 26.602  47.709 1.00 49.09  ? 135 THR E CG2 1 
ATOM   5427  N  N   . LYS E  1 142 ? 116.600 29.624  50.115 1.00 40.32  ? 136 LYS E N   1 
ATOM   5428  C  CA  . LYS E  1 142 ? 115.455 30.507  50.298 1.00 44.76  ? 136 LYS E CA  1 
ATOM   5429  C  C   . LYS E  1 142 ? 115.803 31.675  51.219 1.00 44.16  ? 136 LYS E C   1 
ATOM   5430  O  O   . LYS E  1 142 ? 115.776 32.843  50.806 1.00 47.08  ? 136 LYS E O   1 
ATOM   5431  C  CB  . LYS E  1 142 ? 114.267 29.735  50.884 1.00 51.09  ? 136 LYS E CB  1 
ATOM   5432  C  CG  . LYS E  1 142 ? 113.482 28.919  49.864 1.00 64.78  ? 136 LYS E CG  1 
ATOM   5433  C  CD  . LYS E  1 142 ? 112.121 28.490  50.414 1.00 74.45  ? 136 LYS E CD  1 
ATOM   5434  C  CE  . LYS E  1 142 ? 111.224 27.933  49.305 1.00 84.06  ? 136 LYS E CE  1 
ATOM   5435  N  NZ  . LYS E  1 142 ? 109.855 27.560  49.784 1.00 85.93  ? 136 LYS E NZ  1 
ATOM   5436  N  N   . THR E  1 143 ? 116.154 31.353  52.458 1.00 36.37  ? 137 THR E N   1 
ATOM   5437  C  CA  . THR E  1 143 ? 116.489 32.368  53.444 1.00 34.20  ? 137 THR E CA  1 
ATOM   5438  C  C   . THR E  1 143 ? 117.966 32.432  53.829 1.00 34.23  ? 137 THR E C   1 
ATOM   5439  O  O   . THR E  1 143 ? 118.361 33.286  54.621 1.00 31.13  ? 137 THR E O   1 
ATOM   5440  C  CB  . THR E  1 143 ? 115.695 32.145  54.738 1.00 37.83  ? 137 THR E CB  1 
ATOM   5441  O  OG1 . THR E  1 143 ? 116.328 31.120  55.527 1.00 35.22  ? 137 THR E OG1 1 
ATOM   5442  C  CG2 . THR E  1 143 ? 114.270 31.728  54.406 1.00 27.14  ? 137 THR E CG2 1 
ATOM   5443  N  N   . GLY E  1 144 ? 118.785 31.540  53.286 1.00 33.07  ? 138 GLY E N   1 
ATOM   5444  C  CA  . GLY E  1 144 ? 120.188 31.556  53.652 1.00 27.26  ? 138 GLY E CA  1 
ATOM   5445  C  C   . GLY E  1 144 ? 120.360 31.131  55.109 1.00 31.22  ? 138 GLY E C   1 
ATOM   5446  O  O   . GLY E  1 144 ? 121.418 31.354  55.700 1.00 25.99  ? 138 GLY E O   1 
ATOM   5447  N  N   . ASN E  1 145 ? 119.325 30.512  55.684 1.00 21.90  ? 139 ASN E N   1 
ATOM   5448  C  CA  . ASN E  1 145 ? 119.353 30.065  57.086 1.00 29.49  ? 139 ASN E CA  1 
ATOM   5449  C  C   . ASN E  1 145 ? 119.634 31.185  58.104 1.00 29.91  ? 139 ASN E C   1 
ATOM   5450  O  O   . ASN E  1 145 ? 120.090 30.908  59.213 1.00 28.31  ? 139 ASN E O   1 
ATOM   5451  C  CB  . ASN E  1 145 ? 120.396 28.941  57.275 1.00 20.74  ? 139 ASN E CB  1 
ATOM   5452  C  CG  . ASN E  1 145 ? 119.886 27.568  56.809 1.00 35.20  ? 139 ASN E CG  1 
ATOM   5453  O  OD1 . ASN E  1 145 ? 118.952 27.015  57.392 1.00 34.80  ? 139 ASN E OD1 1 
ATOM   5454  N  ND2 . ASN E  1 145 ? 120.504 27.016  55.763 1.00 27.20  ? 139 ASN E ND2 1 
ATOM   5455  N  N   . ALA E  1 146 ? 119.333 32.435  57.754 1.00 29.82  ? 140 ALA E N   1 
ATOM   5456  C  CA  . ALA E  1 146 ? 119.612 33.567  58.651 1.00 30.52  ? 140 ALA E CA  1 
ATOM   5457  C  C   . ALA E  1 146 ? 118.740 33.692  59.906 1.00 26.73  ? 140 ALA E C   1 
ATOM   5458  O  O   . ALA E  1 146 ? 118.933 34.597  60.709 1.00 25.20  ? 140 ALA E O   1 
ATOM   5459  C  CB  . ALA E  1 146 ? 119.583 34.885  57.862 1.00 31.25  ? 140 ALA E CB  1 
ATOM   5460  N  N   . GLY E  1 147 ? 117.775 32.806  60.085 1.00 26.86  ? 141 GLY E N   1 
ATOM   5461  C  CA  . GLY E  1 147 ? 116.980 32.883  61.294 1.00 29.59  ? 141 GLY E CA  1 
ATOM   5462  C  C   . GLY E  1 147 ? 115.905 33.957  61.346 1.00 32.96  ? 141 GLY E C   1 
ATOM   5463  O  O   . GLY E  1 147 ? 115.483 34.509  60.322 1.00 30.13  ? 141 GLY E O   1 
ATOM   5464  N  N   . SER E  1 148 ? 115.480 34.258  62.569 1.00 28.22  ? 142 SER E N   1 
ATOM   5465  C  CA  . SER E  1 148 ? 114.414 35.217  62.808 1.00 34.19  ? 142 SER E CA  1 
ATOM   5466  C  C   . SER E  1 148 ? 114.716 36.648  62.417 1.00 33.86  ? 142 SER E C   1 
ATOM   5467  O  O   . SER E  1 148 ? 115.871 37.040  62.207 1.00 38.59  ? 142 SER E O   1 
ATOM   5468  C  CB  . SER E  1 148 ? 113.974 35.172  64.280 1.00 30.44  ? 142 SER E CB  1 
ATOM   5469  O  OG  . SER E  1 148 ? 114.964 35.708  65.143 1.00 44.08  ? 142 SER E OG  1 
ATOM   5470  N  N   . ARG E  1 149 ? 113.640 37.419  62.337 1.00 34.42  ? 143 ARG E N   1 
ATOM   5471  C  CA  . ARG E  1 149 ? 113.676 38.825  61.964 1.00 29.66  ? 143 ARG E CA  1 
ATOM   5472  C  C   . ARG E  1 149 ? 113.739 39.628  63.244 1.00 24.87  ? 143 ARG E C   1 
ATOM   5473  O  O   . ARG E  1 149 ? 112.738 39.743  63.928 1.00 24.47  ? 143 ARG E O   1 
ATOM   5474  C  CB  . ARG E  1 149 ? 112.409 39.139  61.169 1.00 18.16  ? 143 ARG E CB  1 
ATOM   5475  C  CG  . ARG E  1 149 ? 112.290 38.228  59.962 1.00 22.39  ? 143 ARG E CG  1 
ATOM   5476  C  CD  . ARG E  1 149 ? 110.979 38.299  59.215 1.00 23.61  ? 143 ARG E CD  1 
ATOM   5477  N  NE  . ARG E  1 149 ? 111.041 37.323  58.127 1.00 34.66  ? 143 ARG E NE  1 
ATOM   5478  C  CZ  . ARG E  1 149 ? 110.316 37.351  57.011 1.00 32.03  ? 143 ARG E CZ  1 
ATOM   5479  N  NH1 . ARG E  1 149 ? 110.490 36.392  56.111 1.00 22.02  ? 143 ARG E NH1 1 
ATOM   5480  N  NH2 . ARG E  1 149 ? 109.435 38.324  56.783 1.00 26.40  ? 143 ARG E NH2 1 
ATOM   5481  N  N   . LEU E  1 150 ? 114.915 40.180  63.557 1.00 27.71  ? 144 LEU E N   1 
ATOM   5482  C  CA  . LEU E  1 150 ? 115.117 40.944  64.795 1.00 33.37  ? 144 LEU E CA  1 
ATOM   5483  C  C   . LEU E  1 150 ? 114.583 42.362  64.750 1.00 33.15  ? 144 LEU E C   1 
ATOM   5484  O  O   . LEU E  1 150 ? 114.184 42.929  65.775 1.00 32.86  ? 144 LEU E O   1 
ATOM   5485  C  CB  . LEU E  1 150 ? 116.608 40.999  65.157 1.00 32.04  ? 144 LEU E CB  1 
ATOM   5486  C  CG  . LEU E  1 150 ? 117.335 39.669  65.370 1.00 32.87  ? 144 LEU E CG  1 
ATOM   5487  C  CD1 . LEU E  1 150 ? 118.775 39.946  65.774 1.00 31.54  ? 144 LEU E CD1 1 
ATOM   5488  C  CD2 . LEU E  1 150 ? 116.619 38.852  66.442 1.00 28.94  ? 144 LEU E CD2 1 
ATOM   5489  N  N   . ALA E  1 151 ? 114.611 42.938  63.556 1.00 28.81  ? 145 ALA E N   1 
ATOM   5490  C  CA  . ALA E  1 151 ? 114.148 44.295  63.341 1.00 24.24  ? 145 ALA E CA  1 
ATOM   5491  C  C   . ALA E  1 151 ? 113.992 44.506  61.832 1.00 27.25  ? 145 ALA E C   1 
ATOM   5492  O  O   . ALA E  1 151 ? 114.611 43.794  61.023 1.00 21.26  ? 145 ALA E O   1 
ATOM   5493  C  CB  . ALA E  1 151 ? 115.153 45.307  63.930 1.00 14.03  ? 145 ALA E CB  1 
ATOM   5494  N  N   . CYS E  1 152 ? 113.144 45.473  61.481 1.00 17.92  ? 146 CYS E N   1 
ATOM   5495  C  CA  . CYS E  1 152 ? 112.868 45.827  60.106 1.00 23.94  ? 146 CYS E CA  1 
ATOM   5496  C  C   . CYS E  1 152 ? 112.258 47.244  60.058 1.00 26.27  ? 146 CYS E C   1 
ATOM   5497  O  O   . CYS E  1 152 ? 112.072 47.904  61.089 1.00 25.88  ? 146 CYS E O   1 
ATOM   5498  C  CB  . CYS E  1 152 ? 111.903 44.805  59.486 1.00 23.62  ? 146 CYS E CB  1 
ATOM   5499  S  SG  . CYS E  1 152 ? 110.325 44.675  60.390 1.00 34.91  ? 146 CYS E SG  1 
ATOM   5500  N  N   . GLY E  1 153 ? 111.968 47.692  58.843 1.00 19.55  ? 147 GLY E N   1 
ATOM   5501  C  CA  . GLY E  1 153 ? 111.381 48.998  58.608 1.00 24.54  ? 147 GLY E CA  1 
ATOM   5502  C  C   . GLY E  1 153 ? 111.054 49.094  57.121 1.00 27.51  ? 147 GLY E C   1 
ATOM   5503  O  O   . GLY E  1 153 ? 111.650 48.387  56.288 1.00 25.47  ? 147 GLY E O   1 
ATOM   5504  N  N   . VAL E  1 154 ? 110.085 49.931  56.779 1.00 21.02  ? 148 VAL E N   1 
ATOM   5505  C  CA  . VAL E  1 154 ? 109.729 50.098  55.385 1.00 20.55  ? 148 VAL E CA  1 
ATOM   5506  C  C   . VAL E  1 154 ? 110.713 51.100  54.804 1.00 21.63  ? 148 VAL E C   1 
ATOM   5507  O  O   . VAL E  1 154 ? 111.069 52.077  55.458 1.00 19.43  ? 148 VAL E O   1 
ATOM   5508  C  CB  . VAL E  1 154 ? 108.289 50.613  55.220 1.00 29.63  ? 148 VAL E CB  1 
ATOM   5509  C  CG1 . VAL E  1 154 ? 107.964 50.774  53.722 1.00 20.92  ? 148 VAL E CG1 1 
ATOM   5510  C  CG2 . VAL E  1 154 ? 107.307 49.623  55.879 1.00 22.30  ? 148 VAL E CG2 1 
ATOM   5511  N  N   . ILE E  1 155 ? 111.183 50.839  53.589 1.00 23.51  ? 149 ILE E N   1 
ATOM   5512  C  CA  . ILE E  1 155 ? 112.145 51.724  52.949 1.00 20.71  ? 149 ILE E CA  1 
ATOM   5513  C  C   . ILE E  1 155 ? 111.382 52.865  52.299 1.00 24.16  ? 149 ILE E C   1 
ATOM   5514  O  O   . ILE E  1 155 ? 110.558 52.641  51.420 1.00 28.82  ? 149 ILE E O   1 
ATOM   5515  C  CB  . ILE E  1 155 ? 112.939 50.970  51.885 1.00 22.89  ? 149 ILE E CB  1 
ATOM   5516  C  CG1 . ILE E  1 155 ? 113.616 49.744  52.512 1.00 25.77  ? 149 ILE E CG1 1 
ATOM   5517  C  CG2 . ILE E  1 155 ? 113.969 51.878  51.283 1.00 15.67  ? 149 ILE E CG2 1 
ATOM   5518  C  CD1 . ILE E  1 155 ? 114.320 48.842  51.498 1.00 16.22  ? 149 ILE E CD1 1 
ATOM   5519  N  N   . GLY E  1 156 ? 111.649 54.086  52.742 1.00 21.17  ? 150 GLY E N   1 
ATOM   5520  C  CA  . GLY E  1 156 ? 110.948 55.224  52.189 1.00 16.44  ? 150 GLY E CA  1 
ATOM   5521  C  C   . GLY E  1 156 ? 111.826 56.254  51.508 1.00 20.04  ? 150 GLY E C   1 
ATOM   5522  O  O   . GLY E  1 156 ? 113.040 56.319  51.770 1.00 23.75  ? 150 GLY E O   1 
ATOM   5523  N  N   . ILE E  1 157 ? 111.208 57.048  50.627 1.00 17.40  ? 151 ILE E N   1 
ATOM   5524  C  CA  . ILE E  1 157 ? 111.895 58.100  49.877 1.00 21.06  ? 151 ILE E CA  1 
ATOM   5525  C  C   . ILE E  1 157 ? 112.381 59.158  50.859 1.00 22.27  ? 151 ILE E C   1 
ATOM   5526  O  O   . ILE E  1 157 ? 111.653 59.523  51.783 1.00 26.03  ? 151 ILE E O   1 
ATOM   5527  C  CB  . ILE E  1 157 ? 110.946 58.766  48.865 1.00 26.20  ? 151 ILE E CB  1 
ATOM   5528  C  CG1 . ILE E  1 157 ? 110.420 57.712  47.894 1.00 37.40  ? 151 ILE E CG1 1 
ATOM   5529  C  CG2 . ILE E  1 157 ? 111.681 59.863  48.098 1.00 17.97  ? 151 ILE E CG2 1 
ATOM   5530  C  CD1 . ILE E  1 157 ? 109.277 58.190  47.015 1.00 41.82  ? 151 ILE E CD1 1 
ATOM   5531  N  N   . ALA E  1 158 ? 113.600 59.647  50.654 1.00 20.47  ? 152 ALA E N   1 
ATOM   5532  C  CA  . ALA E  1 158 ? 114.178 60.658  51.541 1.00 30.76  ? 152 ALA E CA  1 
ATOM   5533  C  C   . ALA E  1 158 ? 114.682 61.870  50.788 1.00 32.63  ? 152 ALA E C   1 
ATOM   5534  O  O   . ALA E  1 158 ? 114.974 61.808  49.592 1.00 29.03  ? 152 ALA E O   1 
ATOM   5535  C  CB  . ALA E  1 158 ? 115.326 60.066  52.361 1.00 13.61  ? 152 ALA E CB  1 
ATOM   5536  N  N   . GLN E  1 159 ? 114.798 62.968  51.522 1.00 40.67  ? 153 GLN E N   1 
ATOM   5537  C  CA  . GLN E  1 159 ? 115.257 64.229  50.967 1.00 50.05  ? 153 GLN E CA  1 
ATOM   5538  C  C   . GLN E  1 159 ? 116.765 64.171  50.698 1.00 52.26  ? 153 GLN E C   1 
ATOM   5539  O  O   . GLN E  1 159 ? 117.522 63.773  51.615 1.00 51.26  ? 153 GLN E O   1 
ATOM   5540  C  CB  . GLN E  1 159 ? 114.934 65.356  51.953 1.00 51.31  ? 153 GLN E CB  1 
ATOM   5541  C  CG  . GLN E  1 159 ? 114.926 66.755  51.354 1.00 58.36  ? 153 GLN E CG  1 
ATOM   5542  C  CD  . GLN E  1 159 ? 114.682 67.836  52.404 1.00 65.01  ? 153 GLN E CD  1 
ATOM   5543  O  OE1 . GLN E  1 159 ? 114.410 68.986  52.073 1.00 71.61  ? 153 GLN E OE1 1 
ATOM   5544  N  NE2 . GLN E  1 159 ? 114.789 67.467  53.676 1.00 66.14  ? 153 GLN E NE2 1 
ATOM   5545  O  OXT . GLN E  1 159 ? 117.174 64.528  49.570 1.00 58.20  ? 153 GLN E OXT 1 
ATOM   5546  N  N   . ALA F  1 7   ? 96.696  44.832  39.893 1.00 68.70  ? 1   ALA F N   1 
ATOM   5547  C  CA  . ALA F  1 7   ? 95.886  45.183  41.099 1.00 62.25  ? 1   ALA F CA  1 
ATOM   5548  C  C   . ALA F  1 7   ? 96.775  45.537  42.297 1.00 50.51  ? 1   ALA F C   1 
ATOM   5549  O  O   . ALA F  1 7   ? 96.625  44.965  43.372 1.00 43.88  ? 1   ALA F O   1 
ATOM   5550  C  CB  . ALA F  1 7   ? 94.942  44.004  41.455 1.00 61.39  ? 1   ALA F CB  1 
ATOM   5551  N  N   . THR F  1 8   ? 97.687  46.489  42.130 1.00 43.23  ? 2   THR F N   1 
ATOM   5552  C  CA  . THR F  1 8   ? 98.554  46.825  43.244 1.00 36.03  ? 2   THR F CA  1 
ATOM   5553  C  C   . THR F  1 8   ? 97.758  47.172  44.509 1.00 37.98  ? 2   THR F C   1 
ATOM   5554  O  O   . THR F  1 8   ? 96.590  47.595  44.478 1.00 34.44  ? 2   THR F O   1 
ATOM   5555  C  CB  . THR F  1 8   ? 99.570  47.951  42.885 1.00 35.90  ? 2   THR F CB  1 
ATOM   5556  O  OG1 . THR F  1 8   ? 98.935  48.933  42.077 1.00 36.67  ? 2   THR F OG1 1 
ATOM   5557  C  CG2 . THR F  1 8   ? 100.774 47.388  42.110 1.00 40.39  ? 2   THR F CG2 1 
ATOM   5558  N  N   . LYS F  1 9   ? 98.395  46.905  45.635 1.00 35.35  ? 3   LYS F N   1 
ATOM   5559  C  CA  . LYS F  1 9   ? 97.816  47.142  46.936 1.00 30.67  ? 3   LYS F CA  1 
ATOM   5560  C  C   . LYS F  1 9   ? 98.944  47.714  47.747 1.00 28.40  ? 3   LYS F C   1 
ATOM   5561  O  O   . LYS F  1 9   ? 100.120 47.533  47.402 1.00 26.26  ? 3   LYS F O   1 
ATOM   5562  C  CB  . LYS F  1 9   ? 97.357  45.831  47.584 1.00 33.08  ? 3   LYS F CB  1 
ATOM   5563  C  CG  . LYS F  1 9   ? 96.170  45.152  46.921 1.00 44.23  ? 3   LYS F CG  1 
ATOM   5564  C  CD  . LYS F  1 9   ? 95.757  43.916  47.712 1.00 57.99  ? 3   LYS F CD  1 
ATOM   5565  C  CE  . LYS F  1 9   ? 94.729  43.064  46.968 1.00 69.53  ? 3   LYS F CE  1 
ATOM   5566  N  NZ  . LYS F  1 9   ? 95.290  42.447  45.726 1.00 70.38  ? 3   LYS F NZ  1 
ATOM   5567  N  N   . ALA F  1 10  ? 98.588  48.402  48.821 1.00 20.62  ? 4   ALA F N   1 
ATOM   5568  C  CA  . ALA F  1 10  ? 99.580  48.988  49.702 1.00 15.92  ? 4   ALA F CA  1 
ATOM   5569  C  C   . ALA F  1 10  ? 99.000  49.016  51.103 1.00 22.38  ? 4   ALA F C   1 
ATOM   5570  O  O   . ALA F  1 10  ? 97.801  48.785  51.300 1.00 21.72  ? 4   ALA F O   1 
ATOM   5571  C  CB  . ALA F  1 10  ? 99.914  50.375  49.253 1.00 16.71  ? 4   ALA F CB  1 
ATOM   5572  N  N   . VAL F  1 11  ? 99.843  49.292  52.084 1.00 16.17  ? 5   VAL F N   1 
ATOM   5573  C  CA  . VAL F  1 11  ? 99.360  49.330  53.438 1.00 17.71  ? 5   VAL F CA  1 
ATOM   5574  C  C   . VAL F  1 11  ? 100.231 50.246  54.278 1.00 20.48  ? 5   VAL F C   1 
ATOM   5575  O  O   . VAL F  1 11  ? 101.349 50.577  53.900 1.00 18.64  ? 5   VAL F O   1 
ATOM   5576  C  CB  . VAL F  1 11  ? 99.333  47.916  54.035 1.00 23.17  ? 5   VAL F CB  1 
ATOM   5577  C  CG1 . VAL F  1 11  ? 100.765 47.418  54.264 1.00 19.97  ? 5   VAL F CG1 1 
ATOM   5578  C  CG2 . VAL F  1 11  ? 98.498  47.914  55.322 1.00 18.24  ? 5   VAL F CG2 1 
ATOM   5579  N  N   . CYS F  1 12  ? 99.707  50.665  55.420 1.00 22.85  ? 6   CYS F N   1 
ATOM   5580  C  CA  . CYS F  1 12  ? 100.450 51.558  56.280 1.00 24.26  ? 6   CYS F CA  1 
ATOM   5581  C  C   . CYS F  1 12  ? 100.089 51.350  57.741 1.00 26.05  ? 6   CYS F C   1 
ATOM   5582  O  O   . CYS F  1 12  ? 98.913  51.269  58.104 1.00 21.83  ? 6   CYS F O   1 
ATOM   5583  C  CB  . CYS F  1 12  ? 100.148 53.005  55.897 1.00 24.94  ? 6   CYS F CB  1 
ATOM   5584  S  SG  . CYS F  1 12  ? 101.065 54.229  56.834 1.00 29.92  ? 6   CYS F SG  1 
ATOM   5585  N  N   . VAL F  1 13  ? 101.107 51.261  58.580 1.00 20.30  ? 7   VAL F N   1 
ATOM   5586  C  CA  . VAL F  1 13  ? 100.872 51.111  60.005 1.00 24.69  ? 7   VAL F CA  1 
ATOM   5587  C  C   . VAL F  1 13  ? 101.196 52.452  60.644 1.00 28.99  ? 7   VAL F C   1 
ATOM   5588  O  O   . VAL F  1 13  ? 102.352 52.867  60.655 1.00 32.69  ? 7   VAL F O   1 
ATOM   5589  C  CB  . VAL F  1 13  ? 101.781 50.029  60.618 1.00 24.30  ? 7   VAL F CB  1 
ATOM   5590  C  CG1 . VAL F  1 13  ? 101.530 49.906  62.142 1.00 9.69   ? 7   VAL F CG1 1 
ATOM   5591  C  CG2 . VAL F  1 13  ? 101.539 48.706  59.903 1.00 17.64  ? 7   VAL F CG2 1 
ATOM   5592  N  N   . LEU F  1 14  ? 100.178 53.133  61.167 1.00 27.98  ? 8   LEU F N   1 
ATOM   5593  C  CA  . LEU F  1 14  ? 100.390 54.424  61.809 1.00 27.96  ? 8   LEU F CA  1 
ATOM   5594  C  C   . LEU F  1 14  ? 100.734 54.259  63.294 1.00 27.72  ? 8   LEU F C   1 
ATOM   5595  O  O   . LEU F  1 14  ? 100.050 53.541  64.028 1.00 25.96  ? 8   LEU F O   1 
ATOM   5596  C  CB  . LEU F  1 14  ? 99.132  55.283  61.677 1.00 27.80  ? 8   LEU F CB  1 
ATOM   5597  C  CG  . LEU F  1 14  ? 98.660  55.637  60.259 1.00 31.36  ? 8   LEU F CG  1 
ATOM   5598  C  CD1 . LEU F  1 14  ? 97.305  56.282  60.325 1.00 36.20  ? 8   LEU F CD1 1 
ATOM   5599  C  CD2 . LEU F  1 14  ? 99.630  56.597  59.615 1.00 38.10  ? 8   LEU F CD2 1 
ATOM   5600  N  N   . LYS F  1 15  ? 101.796 54.931  63.722 1.00 27.15  ? 9   LYS F N   1 
ATOM   5601  C  CA  . LYS F  1 15  ? 102.246 54.919  65.116 1.00 32.11  ? 9   LYS F CA  1 
ATOM   5602  C  C   . LYS F  1 15  ? 102.741 56.324  65.425 1.00 27.95  ? 9   LYS F C   1 
ATOM   5603  O  O   . LYS F  1 15  ? 103.124 57.067  64.519 1.00 27.43  ? 9   LYS F O   1 
ATOM   5604  C  CB  . LYS F  1 15  ? 103.410 53.934  65.316 1.00 33.45  ? 9   LYS F CB  1 
ATOM   5605  C  CG  . LYS F  1 15  ? 103.057 52.464  65.178 1.00 50.43  ? 9   LYS F CG  1 
ATOM   5606  C  CD  . LYS F  1 15  ? 102.543 51.866  66.492 1.00 64.02  ? 9   LYS F CD  1 
ATOM   5607  C  CE  . LYS F  1 15  ? 101.999 50.448  66.293 1.00 66.97  ? 9   LYS F CE  1 
ATOM   5608  N  NZ  . LYS F  1 15  ? 100.815 50.439  65.370 1.00 69.09  ? 9   LYS F NZ  1 
ATOM   5609  N  N   . GLY F  1 16  ? 102.754 56.691  66.699 1.00 29.22  ? 10  GLY F N   1 
ATOM   5610  C  CA  . GLY F  1 16  ? 103.234 58.015  67.062 1.00 28.73  ? 10  GLY F CA  1 
ATOM   5611  C  C   . GLY F  1 16  ? 103.792 57.992  68.469 1.00 27.40  ? 10  GLY F C   1 
ATOM   5612  O  O   . GLY F  1 16  ? 104.039 56.921  69.006 1.00 31.05  ? 10  GLY F O   1 
ATOM   5613  N  N   . ASP F  1 17  ? 103.988 59.158  69.074 1.00 27.11  ? 11  ASP F N   1 
ATOM   5614  C  CA  . ASP F  1 17  ? 104.518 59.226  70.439 1.00 37.45  ? 11  ASP F CA  1 
ATOM   5615  C  C   . ASP F  1 17  ? 103.451 58.897  71.459 1.00 37.82  ? 11  ASP F C   1 
ATOM   5616  O  O   . ASP F  1 17  ? 103.758 58.449  72.557 1.00 39.37  ? 11  ASP F O   1 
ATOM   5617  C  CB  . ASP F  1 17  ? 105.056 60.620  70.740 1.00 44.15  ? 11  ASP F CB  1 
ATOM   5618  C  CG  . ASP F  1 17  ? 106.408 60.858  70.132 1.00 54.21  ? 11  ASP F CG  1 
ATOM   5619  O  OD1 . ASP F  1 17  ? 106.764 62.045  69.956 1.00 58.43  ? 11  ASP F OD1 1 
ATOM   5620  O  OD2 . ASP F  1 17  ? 107.113 59.857  69.847 1.00 48.45  ? 11  ASP F OD2 1 
ATOM   5621  N  N   . GLY F  1 18  ? 102.199 59.141  71.085 1.00 39.22  ? 12  GLY F N   1 
ATOM   5622  C  CA  . GLY F  1 18  ? 101.085 58.875  71.969 1.00 31.03  ? 12  GLY F CA  1 
ATOM   5623  C  C   . GLY F  1 18  ? 100.436 57.537  71.681 1.00 32.67  ? 12  GLY F C   1 
ATOM   5624  O  O   . GLY F  1 18  ? 101.094 56.627  71.178 1.00 26.02  ? 12  GLY F O   1 
ATOM   5625  N  N   . PRO F  1 19  ? 99.136  57.397  71.988 1.00 27.07  ? 13  PRO F N   1 
ATOM   5626  C  CA  . PRO F  1 19  ? 98.338  56.184  71.787 1.00 27.28  ? 13  PRO F CA  1 
ATOM   5627  C  C   . PRO F  1 19  ? 97.704  56.034  70.412 1.00 28.68  ? 13  PRO F C   1 
ATOM   5628  O  O   . PRO F  1 19  ? 96.973  55.075  70.175 1.00 24.67  ? 13  PRO F O   1 
ATOM   5629  C  CB  . PRO F  1 19  ? 97.265  56.306  72.857 1.00 27.35  ? 13  PRO F CB  1 
ATOM   5630  C  CG  . PRO F  1 19  ? 96.976  57.773  72.807 1.00 26.90  ? 13  PRO F CG  1 
ATOM   5631  C  CD  . PRO F  1 19  ? 98.364  58.412  72.727 1.00 17.16  ? 13  PRO F CD  1 
ATOM   5632  N  N   . VAL F  1 20  ? 97.948  56.967  69.502 1.00 24.10  ? 14  VAL F N   1 
ATOM   5633  C  CA  . VAL F  1 20  ? 97.329  56.829  68.196 1.00 22.03  ? 14  VAL F CA  1 
ATOM   5634  C  C   . VAL F  1 20  ? 97.971  55.694  67.422 1.00 26.51  ? 14  VAL F C   1 
ATOM   5635  O  O   . VAL F  1 20  ? 99.185  55.635  67.299 1.00 33.43  ? 14  VAL F O   1 
ATOM   5636  C  CB  . VAL F  1 20  ? 97.425  58.128  67.390 1.00 25.01  ? 14  VAL F CB  1 
ATOM   5637  C  CG1 . VAL F  1 20  ? 96.663  57.975  66.075 1.00 25.48  ? 14  VAL F CG1 1 
ATOM   5638  C  CG2 . VAL F  1 20  ? 96.842  59.283  68.209 1.00 15.69  ? 14  VAL F CG2 1 
ATOM   5639  N  N   . GLN F  1 21  ? 97.149  54.776  66.923 1.00 24.78  ? 15  GLN F N   1 
ATOM   5640  C  CA  . GLN F  1 21  ? 97.633  53.633  66.165 1.00 26.01  ? 15  GLN F CA  1 
ATOM   5641  C  C   . GLN F  1 21  ? 96.553  53.215  65.186 1.00 30.01  ? 15  GLN F C   1 
ATOM   5642  O  O   . GLN F  1 21  ? 95.366  53.412  65.434 1.00 33.00  ? 15  GLN F O   1 
ATOM   5643  C  CB  . GLN F  1 21  ? 97.889  52.417  67.061 1.00 27.81  ? 15  GLN F CB  1 
ATOM   5644  C  CG  . GLN F  1 21  ? 98.431  52.692  68.425 1.00 38.58  ? 15  GLN F CG  1 
ATOM   5645  C  CD  . GLN F  1 21  ? 98.817  51.408  69.136 1.00 47.65  ? 15  GLN F CD  1 
ATOM   5646  O  OE1 . GLN F  1 21  ? 98.092  50.404  69.072 1.00 34.81  ? 15  GLN F OE1 1 
ATOM   5647  N  NE2 . GLN F  1 21  ? 99.961  51.433  69.826 1.00 51.95  ? 15  GLN F NE2 1 
ATOM   5648  N  N   . GLY F  1 22  ? 96.966  52.596  64.093 1.00 25.15  ? 16  GLY F N   1 
ATOM   5649  C  CA  . GLY F  1 22  ? 96.007  52.136  63.120 1.00 28.92  ? 16  GLY F CA  1 
ATOM   5650  C  C   . GLY F  1 22  ? 96.663  51.498  61.917 1.00 22.93  ? 16  GLY F C   1 
ATOM   5651  O  O   . GLY F  1 22  ? 97.885  51.523  61.762 1.00 27.37  ? 16  GLY F O   1 
ATOM   5652  N  N   . ILE F  1 23  ? 95.827  50.924  61.066 1.00 25.83  ? 17  ILE F N   1 
ATOM   5653  C  CA  . ILE F  1 23  ? 96.276  50.280  59.846 1.00 24.60  ? 17  ILE F CA  1 
ATOM   5654  C  C   . ILE F  1 23  ? 95.425  50.762  58.684 1.00 26.99  ? 17  ILE F C   1 
ATOM   5655  O  O   . ILE F  1 23  ? 94.200  50.603  58.687 1.00 27.88  ? 17  ILE F O   1 
ATOM   5656  C  CB  . ILE F  1 23  ? 96.134  48.760  59.955 1.00 27.46  ? 17  ILE F CB  1 
ATOM   5657  C  CG1 . ILE F  1 23  ? 97.148  48.238  60.977 1.00 27.88  ? 17  ILE F CG1 1 
ATOM   5658  C  CG2 . ILE F  1 23  ? 96.290  48.109  58.568 1.00 25.52  ? 17  ILE F CG2 1 
ATOM   5659  C  CD1 . ILE F  1 23  ? 97.074  46.753  61.214 1.00 18.27  ? 17  ILE F CD1 1 
ATOM   5660  N  N   . ILE F  1 24  ? 96.063  51.372  57.696 1.00 25.80  ? 18  ILE F N   1 
ATOM   5661  C  CA  . ILE F  1 24  ? 95.322  51.821  56.532 1.00 24.88  ? 18  ILE F CA  1 
ATOM   5662  C  C   . ILE F  1 24  ? 95.747  51.042  55.299 1.00 25.07  ? 18  ILE F C   1 
ATOM   5663  O  O   . ILE F  1 24  ? 96.940  50.920  55.003 1.00 29.16  ? 18  ILE F O   1 
ATOM   5664  C  CB  . ILE F  1 24  ? 95.513  53.327  56.256 1.00 25.76  ? 18  ILE F CB  1 
ATOM   5665  C  CG1 . ILE F  1 24  ? 94.920  54.159  57.402 1.00 23.14  ? 18  ILE F CG1 1 
ATOM   5666  C  CG2 . ILE F  1 24  ? 94.813  53.687  54.948 1.00 20.90  ? 18  ILE F CG2 1 
ATOM   5667  C  CD1 . ILE F  1 24  ? 93.361  54.041  57.521 1.00 22.07  ? 18  ILE F CD1 1 
ATOM   5668  N  N   . ASN F  1 25  ? 94.757  50.514  54.588 1.00 24.79  ? 19  ASN F N   1 
ATOM   5669  C  CA  . ASN F  1 25  ? 94.982  49.752  53.363 1.00 24.64  ? 19  ASN F CA  1 
ATOM   5670  C  C   . ASN F  1 25  ? 94.723  50.627  52.143 1.00 20.99  ? 19  ASN F C   1 
ATOM   5671  O  O   . ASN F  1 25  ? 93.944  51.578  52.204 1.00 21.90  ? 19  ASN F O   1 
ATOM   5672  C  CB  . ASN F  1 25  ? 94.038  48.552  53.307 1.00 26.29  ? 19  ASN F CB  1 
ATOM   5673  C  CG  . ASN F  1 25  ? 94.221  47.619  54.479 1.00 27.87  ? 19  ASN F CG  1 
ATOM   5674  O  OD1 . ASN F  1 25  ? 95.215  46.908  54.561 1.00 27.53  ? 19  ASN F OD1 1 
ATOM   5675  N  ND2 . ASN F  1 25  ? 93.267  47.629  55.403 1.00 24.61  ? 19  ASN F ND2 1 
ATOM   5676  N  N   . PHE F  1 26  ? 95.366  50.280  51.036 1.00 16.95  ? 20  PHE F N   1 
ATOM   5677  C  CA  . PHE F  1 26  ? 95.224  50.994  49.769 1.00 16.82  ? 20  PHE F CA  1 
ATOM   5678  C  C   . PHE F  1 26  ? 95.080  49.916  48.711 1.00 24.22  ? 20  PHE F C   1 
ATOM   5679  O  O   . PHE F  1 26  ? 95.794  48.910  48.743 1.00 28.19  ? 20  PHE F O   1 
ATOM   5680  C  CB  . PHE F  1 26  ? 96.491  51.805  49.437 1.00 17.72  ? 20  PHE F CB  1 
ATOM   5681  C  CG  . PHE F  1 26  ? 96.788  52.921  50.403 1.00 22.04  ? 20  PHE F CG  1 
ATOM   5682  C  CD1 . PHE F  1 26  ? 96.351  54.214  50.146 1.00 23.94  ? 20  PHE F CD1 1 
ATOM   5683  C  CD2 . PHE F  1 26  ? 97.493  52.672  51.577 1.00 24.14  ? 20  PHE F CD2 1 
ATOM   5684  C  CE1 . PHE F  1 26  ? 96.604  55.241  51.038 1.00 18.81  ? 20  PHE F CE1 1 
ATOM   5685  C  CE2 . PHE F  1 26  ? 97.754  53.693  52.482 1.00 26.37  ? 20  PHE F CE2 1 
ATOM   5686  C  CZ  . PHE F  1 26  ? 97.309  54.978  52.211 1.00 34.71  ? 20  PHE F CZ  1 
ATOM   5687  N  N   . GLU F  1 27  ? 94.161  50.113  47.781 1.00 28.79  ? 21  GLU F N   1 
ATOM   5688  C  CA  . GLU F  1 27  ? 93.974  49.157  46.699 1.00 35.27  ? 21  GLU F CA  1 
ATOM   5689  C  C   . GLU F  1 27  ? 93.603  49.924  45.441 1.00 34.10  ? 21  GLU F C   1 
ATOM   5690  O  O   . GLU F  1 27  ? 92.761  50.827  45.471 1.00 28.25  ? 21  GLU F O   1 
ATOM   5691  C  CB  . GLU F  1 27  ? 92.874  48.157  47.031 1.00 36.64  ? 21  GLU F CB  1 
ATOM   5692  C  CG  . GLU F  1 27  ? 92.599  47.172  45.913 1.00 50.44  ? 21  GLU F CG  1 
ATOM   5693  C  CD  . GLU F  1 27  ? 91.435  46.246  46.222 1.00 61.54  ? 21  GLU F CD  1 
ATOM   5694  O  OE1 . GLU F  1 27  ? 91.537  45.436  47.172 1.00 60.27  ? 21  GLU F OE1 1 
ATOM   5695  O  OE2 . GLU F  1 27  ? 90.411  46.335  45.513 1.00 68.04  ? 21  GLU F OE2 1 
ATOM   5696  N  N   . GLN F  1 28  ? 94.251  49.578  44.338 1.00 24.42  ? 22  GLN F N   1 
ATOM   5697  C  CA  . GLN F  1 28  ? 93.977  50.248  43.082 1.00 28.10  ? 22  GLN F CA  1 
ATOM   5698  C  C   . GLN F  1 28  ? 93.954  49.223  41.959 1.00 29.33  ? 22  GLN F C   1 
ATOM   5699  O  O   . GLN F  1 28  ? 95.000  48.799  41.473 1.00 26.68  ? 22  GLN F O   1 
ATOM   5700  C  CB  . GLN F  1 28  ? 95.046  51.308  42.822 1.00 29.08  ? 22  GLN F CB  1 
ATOM   5701  C  CG  . GLN F  1 28  ? 94.904  52.024  41.503 1.00 26.46  ? 22  GLN F CG  1 
ATOM   5702  C  CD  . GLN F  1 28  ? 95.985  53.044  41.286 1.00 21.79  ? 22  GLN F CD  1 
ATOM   5703  O  OE1 . GLN F  1 28  ? 97.119  52.866  41.727 1.00 25.44  ? 22  GLN F OE1 1 
ATOM   5704  N  NE2 . GLN F  1 28  ? 95.653  54.111  40.582 1.00 21.62  ? 22  GLN F NE2 1 
ATOM   5705  N  N   . LYS F  1 29  ? 92.746  48.836  41.561 1.00 37.49  ? 23  LYS F N   1 
ATOM   5706  C  CA  . LYS F  1 29  ? 92.520  47.849  40.507 1.00 44.58  ? 23  LYS F CA  1 
ATOM   5707  C  C   . LYS F  1 29  ? 93.096  48.227  39.139 1.00 46.09  ? 23  LYS F C   1 
ATOM   5708  O  O   . LYS F  1 29  ? 93.581  47.366  38.417 1.00 44.64  ? 23  LYS F O   1 
ATOM   5709  C  CB  . LYS F  1 29  ? 91.022  47.592  40.359 1.00 53.89  ? 23  LYS F CB  1 
ATOM   5710  C  CG  . LYS F  1 29  ? 90.303  47.240  41.659 1.00 71.98  ? 23  LYS F CG  1 
ATOM   5711  C  CD  . LYS F  1 29  ? 88.798  47.077  41.431 1.00 77.96  ? 23  LYS F CD  1 
ATOM   5712  C  CE  . LYS F  1 29  ? 88.071  46.649  42.703 1.00 85.77  ? 23  LYS F CE  1 
ATOM   5713  N  NZ  . LYS F  1 29  ? 86.625  46.357  42.456 1.00 88.48  ? 23  LYS F NZ  1 
ATOM   5714  N  N   . GLU F  1 30  ? 93.041  49.507  38.783 1.00 46.71  ? 24  GLU F N   1 
ATOM   5715  C  CA  . GLU F  1 30  ? 93.550  49.968  37.490 1.00 46.49  ? 24  GLU F CA  1 
ATOM   5716  C  C   . GLU F  1 30  ? 94.579  51.073  37.680 1.00 45.68  ? 24  GLU F C   1 
ATOM   5717  O  O   . GLU F  1 30  ? 94.426  51.922  38.555 1.00 45.01  ? 24  GLU F O   1 
ATOM   5718  C  CB  . GLU F  1 30  ? 92.393  50.487  36.625 1.00 55.99  ? 24  GLU F CB  1 
ATOM   5719  C  CG  . GLU F  1 30  ? 91.317  49.451  36.328 1.00 73.53  ? 24  GLU F CG  1 
ATOM   5720  C  CD  . GLU F  1 30  ? 91.835  48.292  35.481 1.00 85.25  ? 24  GLU F CD  1 
ATOM   5721  O  OE1 . GLU F  1 30  ? 91.072  47.321  35.268 1.00 87.92  ? 24  GLU F OE1 1 
ATOM   5722  O  OE2 . GLU F  1 30  ? 93.003  48.354  35.026 1.00 87.32  ? 24  GLU F OE2 1 
ATOM   5723  N  N   . SER F  1 31  ? 95.609  51.078  36.843 1.00 44.88  ? 25  SER F N   1 
ATOM   5724  C  CA  . SER F  1 31  ? 96.678  52.065  36.949 1.00 51.58  ? 25  SER F CA  1 
ATOM   5725  C  C   . SER F  1 31  ? 96.210  53.506  36.830 1.00 53.56  ? 25  SER F C   1 
ATOM   5726  O  O   . SER F  1 31  ? 96.807  54.409  37.412 1.00 54.04  ? 25  SER F O   1 
ATOM   5727  C  CB  . SER F  1 31  ? 97.757  51.795  35.896 1.00 54.84  ? 25  SER F CB  1 
ATOM   5728  O  OG  . SER F  1 31  ? 97.234  51.931  34.587 1.00 59.65  ? 25  SER F OG  1 
ATOM   5729  N  N   . ASN F  1 32  ? 95.150  53.730  36.071 1.00 56.06  ? 26  ASN F N   1 
ATOM   5730  C  CA  . ASN F  1 32  ? 94.631  55.080  35.906 1.00 60.29  ? 26  ASN F CA  1 
ATOM   5731  C  C   . ASN F  1 32  ? 93.230  55.154  36.497 1.00 56.75  ? 26  ASN F C   1 
ATOM   5732  O  O   . ASN F  1 32  ? 92.342  55.832  35.968 1.00 56.94  ? 26  ASN F O   1 
ATOM   5733  C  CB  . ASN F  1 32  ? 94.618  55.453  34.425 1.00 68.47  ? 26  ASN F CB  1 
ATOM   5734  C  CG  . ASN F  1 32  ? 94.117  54.326  33.552 1.00 77.59  ? 26  ASN F CG  1 
ATOM   5735  O  OD1 . ASN F  1 32  ? 92.969  53.891  33.675 1.00 77.87  ? 26  ASN F OD1 1 
ATOM   5736  N  ND2 . ASN F  1 32  ? 94.981  53.838  32.664 1.00 81.49  ? 26  ASN F ND2 1 
ATOM   5737  N  N   . GLY F  1 33  ? 93.051  54.438  37.604 1.00 48.52  ? 27  GLY F N   1 
ATOM   5738  C  CA  . GLY F  1 33  ? 91.776  54.407  38.284 1.00 38.51  ? 27  GLY F CA  1 
ATOM   5739  C  C   . GLY F  1 33  ? 91.874  54.913  39.710 1.00 35.46  ? 27  GLY F C   1 
ATOM   5740  O  O   . GLY F  1 33  ? 92.953  55.236  40.209 1.00 34.70  ? 27  GLY F O   1 
ATOM   5741  N  N   . PRO F  1 34  ? 90.747  54.980  40.410 1.00 32.65  ? 28  PRO F N   1 
ATOM   5742  C  CA  . PRO F  1 34  ? 90.835  55.471  41.785 1.00 27.09  ? 28  PRO F CA  1 
ATOM   5743  C  C   . PRO F  1 34  ? 91.480  54.486  42.749 1.00 24.76  ? 28  PRO F C   1 
ATOM   5744  O  O   . PRO F  1 34  ? 91.567  53.284  42.489 1.00 21.98  ? 28  PRO F O   1 
ATOM   5745  C  CB  . PRO F  1 34  ? 89.378  55.758  42.139 1.00 35.33  ? 28  PRO F CB  1 
ATOM   5746  C  CG  . PRO F  1 34  ? 88.629  54.693  41.353 1.00 32.40  ? 28  PRO F CG  1 
ATOM   5747  C  CD  . PRO F  1 34  ? 89.354  54.677  40.022 1.00 27.75  ? 28  PRO F CD  1 
ATOM   5748  N  N   . VAL F  1 35  ? 91.928  55.017  43.876 1.00 20.98  ? 29  VAL F N   1 
ATOM   5749  C  CA  . VAL F  1 35  ? 92.546  54.213  44.905 1.00 22.08  ? 29  VAL F CA  1 
ATOM   5750  C  C   . VAL F  1 35  ? 91.596  54.164  46.079 1.00 21.99  ? 29  VAL F C   1 
ATOM   5751  O  O   . VAL F  1 35  ? 91.150  55.203  46.552 1.00 26.16  ? 29  VAL F O   1 
ATOM   5752  C  CB  . VAL F  1 35  ? 93.858  54.847  45.397 1.00 21.75  ? 29  VAL F CB  1 
ATOM   5753  C  CG1 . VAL F  1 35  ? 94.491  53.960  46.482 1.00 20.94  ? 29  VAL F CG1 1 
ATOM   5754  C  CG2 . VAL F  1 35  ? 94.805  55.058  44.225 1.00 22.15  ? 29  VAL F CG2 1 
ATOM   5755  N  N   . LYS F  1 36  ? 91.260  52.970  46.540 1.00 23.83  ? 30  LYS F N   1 
ATOM   5756  C  CA  . LYS F  1 36  ? 90.398  52.867  47.714 1.00 26.59  ? 30  LYS F CA  1 
ATOM   5757  C  C   . LYS F  1 36  ? 91.308  52.940  48.938 1.00 23.26  ? 30  LYS F C   1 
ATOM   5758  O  O   . LYS F  1 36  ? 92.306  52.233  49.017 1.00 26.93  ? 30  LYS F O   1 
ATOM   5759  C  CB  . LYS F  1 36  ? 89.631  51.543  47.732 1.00 28.91  ? 30  LYS F CB  1 
ATOM   5760  C  CG  . LYS F  1 36  ? 88.390  51.546  46.867 1.00 53.37  ? 30  LYS F CG  1 
ATOM   5761  C  CD  . LYS F  1 36  ? 87.495  50.344  47.136 1.00 59.86  ? 30  LYS F CD  1 
ATOM   5762  C  CE  . LYS F  1 36  ? 86.132  50.526  46.462 1.00 73.20  ? 30  LYS F CE  1 
ATOM   5763  N  NZ  . LYS F  1 36  ? 85.402  51.738  46.971 1.00 74.14  ? 30  LYS F NZ  1 
ATOM   5764  N  N   . VAL F  1 37  ? 90.970  53.801  49.886 1.00 19.09  ? 31  VAL F N   1 
ATOM   5765  C  CA  . VAL F  1 37  ? 91.767  53.942  51.098 1.00 17.20  ? 31  VAL F CA  1 
ATOM   5766  C  C   . VAL F  1 37  ? 90.867  53.596  52.274 1.00 18.79  ? 31  VAL F C   1 
ATOM   5767  O  O   . VAL F  1 37  ? 89.883  54.289  52.514 1.00 20.18  ? 31  VAL F O   1 
ATOM   5768  C  CB  . VAL F  1 37  ? 92.253  55.381  51.237 1.00 15.90  ? 31  VAL F CB  1 
ATOM   5769  C  CG1 . VAL F  1 37  ? 93.195  55.509  52.427 1.00 16.97  ? 31  VAL F CG1 1 
ATOM   5770  C  CG2 . VAL F  1 37  ? 92.905  55.821  49.933 1.00 14.99  ? 31  VAL F CG2 1 
ATOM   5771  N  N   . TRP F  1 38  ? 91.194  52.544  53.020 1.00 18.98  ? 32  TRP F N   1 
ATOM   5772  C  CA  . TRP F  1 38  ? 90.321  52.145  54.128 1.00 23.22  ? 32  TRP F CA  1 
ATOM   5773  C  C   . TRP F  1 38  ? 91.021  51.451  55.272 1.00 21.34  ? 32  TRP F C   1 
ATOM   5774  O  O   . TRP F  1 38  ? 92.107  50.901  55.107 1.00 32.85  ? 32  TRP F O   1 
ATOM   5775  C  CB  . TRP F  1 38  ? 89.216  51.220  53.611 1.00 21.44  ? 32  TRP F CB  1 
ATOM   5776  C  CG  . TRP F  1 38  ? 89.619  49.761  53.507 1.00 33.19  ? 32  TRP F CG  1 
ATOM   5777  C  CD1 . TRP F  1 38  ? 89.353  48.770  54.415 1.00 24.92  ? 32  TRP F CD1 1 
ATOM   5778  C  CD2 . TRP F  1 38  ? 90.331  49.132  52.423 1.00 25.22  ? 32  TRP F CD2 1 
ATOM   5779  N  NE1 . TRP F  1 38  ? 89.845  47.568  53.956 1.00 33.87  ? 32  TRP F NE1 1 
ATOM   5780  C  CE2 . TRP F  1 38  ? 90.448  47.762  52.740 1.00 23.12  ? 32  TRP F CE2 1 
ATOM   5781  C  CE3 . TRP F  1 38  ? 90.880  49.598  51.217 1.00 36.39  ? 32  TRP F CE3 1 
ATOM   5782  C  CZ2 . TRP F  1 38  ? 91.091  46.847  51.896 1.00 32.61  ? 32  TRP F CZ2 1 
ATOM   5783  C  CZ3 . TRP F  1 38  ? 91.525  48.684  50.372 1.00 35.78  ? 32  TRP F CZ3 1 
ATOM   5784  C  CH2 . TRP F  1 38  ? 91.622  47.325  50.721 1.00 35.45  ? 32  TRP F CH2 1 
ATOM   5785  N  N   . GLY F  1 39  ? 90.372  51.465  56.428 1.00 19.13  ? 33  GLY F N   1 
ATOM   5786  C  CA  . GLY F  1 39  ? 90.924  50.837  57.613 1.00 11.64  ? 33  GLY F CA  1 
ATOM   5787  C  C   . GLY F  1 39  ? 90.376  51.557  58.821 1.00 17.48  ? 33  GLY F C   1 
ATOM   5788  O  O   . GLY F  1 39  ? 89.255  52.034  58.803 1.00 24.39  ? 33  GLY F O   1 
ATOM   5789  N  N   . SER F  1 40  ? 91.155  51.647  59.881 1.00 18.22  ? 34  SER F N   1 
ATOM   5790  C  CA  . SER F  1 40  ? 90.683  52.348  61.053 1.00 28.33  ? 34  SER F CA  1 
ATOM   5791  C  C   . SER F  1 40  ? 91.869  52.824  61.887 1.00 26.63  ? 34  SER F C   1 
ATOM   5792  O  O   . SER F  1 40  ? 92.969  52.271  61.791 1.00 28.62  ? 34  SER F O   1 
ATOM   5793  C  CB  . SER F  1 40  ? 89.741  51.453  61.865 1.00 27.09  ? 34  SER F CB  1 
ATOM   5794  O  OG  . SER F  1 40  ? 90.456  50.568  62.691 1.00 24.80  ? 34  SER F OG  1 
ATOM   5795  N  N   . ILE F  1 41  ? 91.630  53.861  62.684 1.00 24.78  ? 35  ILE F N   1 
ATOM   5796  C  CA  . ILE F  1 41  ? 92.651  54.481  63.526 1.00 28.57  ? 35  ILE F CA  1 
ATOM   5797  C  C   . ILE F  1 41  ? 92.116  54.704  64.949 1.00 27.48  ? 35  ILE F C   1 
ATOM   5798  O  O   . ILE F  1 41  ? 91.090  55.356  65.127 1.00 32.22  ? 35  ILE F O   1 
ATOM   5799  C  CB  . ILE F  1 41  ? 93.037  55.837  62.938 1.00 26.87  ? 35  ILE F CB  1 
ATOM   5800  C  CG1 . ILE F  1 41  ? 93.363  55.672  61.456 1.00 21.22  ? 35  ILE F CG1 1 
ATOM   5801  C  CG2 . ILE F  1 41  ? 94.198  56.432  63.703 1.00 23.94  ? 35  ILE F CG2 1 
ATOM   5802  C  CD1 . ILE F  1 41  ? 93.753  56.984  60.787 1.00 28.51  ? 35  ILE F CD1 1 
ATOM   5803  N  N   . LYS F  1 42  ? 92.799  54.170  65.960 1.00 24.75  ? 36  LYS F N   1 
ATOM   5804  C  CA  . LYS F  1 42  ? 92.324  54.343  67.323 1.00 26.60  ? 36  LYS F CA  1 
ATOM   5805  C  C   . LYS F  1 42  ? 93.177  55.308  68.116 1.00 30.70  ? 36  LYS F C   1 
ATOM   5806  O  O   . LYS F  1 42  ? 94.261  55.709  67.668 1.00 33.77  ? 36  LYS F O   1 
ATOM   5807  C  CB  . LYS F  1 42  ? 92.222  52.998  68.026 1.00 26.75  ? 36  LYS F CB  1 
ATOM   5808  C  CG  . LYS F  1 42  ? 93.527  52.342  68.408 1.00 49.10  ? 36  LYS F CG  1 
ATOM   5809  C  CD  . LYS F  1 42  ? 93.241  51.085  69.223 1.00 43.59  ? 36  LYS F CD  1 
ATOM   5810  C  CE  . LYS F  1 42  ? 94.507  50.347  69.601 1.00 56.65  ? 36  LYS F CE  1 
ATOM   5811  N  NZ  . LYS F  1 42  ? 94.187  49.111  70.375 1.00 63.14  ? 36  LYS F NZ  1 
ATOM   5812  N  N   . GLY F  1 43  ? 92.670  55.710  69.281 1.00 34.76  ? 37  GLY F N   1 
ATOM   5813  C  CA  . GLY F  1 43  ? 93.382  56.661  70.124 1.00 25.96  ? 37  GLY F CA  1 
ATOM   5814  C  C   . GLY F  1 43  ? 93.194  58.108  69.683 1.00 31.19  ? 37  GLY F C   1 
ATOM   5815  O  O   . GLY F  1 43  ? 93.977  58.990  70.068 1.00 31.06  ? 37  GLY F O   1 
ATOM   5816  N  N   . LEU F  1 44  ? 92.159  58.372  68.884 1.00 27.68  ? 38  LEU F N   1 
ATOM   5817  C  CA  . LEU F  1 44  ? 91.900  59.735  68.390 1.00 27.24  ? 38  LEU F CA  1 
ATOM   5818  C  C   . LEU F  1 44  ? 90.747  60.400  69.113 1.00 24.30  ? 38  LEU F C   1 
ATOM   5819  O  O   . LEU F  1 44  ? 89.694  59.799  69.270 1.00 28.86  ? 38  LEU F O   1 
ATOM   5820  C  CB  . LEU F  1 44  ? 91.566  59.714  66.893 1.00 24.17  ? 38  LEU F CB  1 
ATOM   5821  C  CG  . LEU F  1 44  ? 92.665  59.501  65.855 1.00 31.02  ? 38  LEU F CG  1 
ATOM   5822  C  CD1 . LEU F  1 44  ? 92.042  59.320  64.467 1.00 28.44  ? 38  LEU F CD1 1 
ATOM   5823  C  CD2 . LEU F  1 44  ? 93.607  60.698  65.868 1.00 28.03  ? 38  LEU F CD2 1 
ATOM   5824  N  N   . THR F  1 45  ? 90.926  61.640  69.549 1.00 28.41  ? 39  THR F N   1 
ATOM   5825  C  CA  . THR F  1 45  ? 89.830  62.333  70.217 1.00 35.12  ? 39  THR F CA  1 
ATOM   5826  C  C   . THR F  1 45  ? 88.710  62.495  69.195 1.00 37.74  ? 39  THR F C   1 
ATOM   5827  O  O   . THR F  1 45  ? 88.968  62.688  68.004 1.00 33.61  ? 39  THR F O   1 
ATOM   5828  C  CB  . THR F  1 45  ? 90.236  63.726  70.698 1.00 34.41  ? 39  THR F CB  1 
ATOM   5829  O  OG1 . THR F  1 45  ? 90.637  64.518  69.572 1.00 45.29  ? 39  THR F OG1 1 
ATOM   5830  C  CG2 . THR F  1 45  ? 91.382  63.632  71.679 1.00 34.80  ? 39  THR F CG2 1 
ATOM   5831  N  N   . GLU F  1 46  ? 87.470  62.411  69.665 1.00 41.58  ? 40  GLU F N   1 
ATOM   5832  C  CA  . GLU F  1 46  ? 86.304  62.537  68.805 1.00 41.23  ? 40  GLU F CA  1 
ATOM   5833  C  C   . GLU F  1 46  ? 86.351  63.809  67.965 1.00 36.21  ? 40  GLU F C   1 
ATOM   5834  O  O   . GLU F  1 46  ? 86.680  64.882  68.446 1.00 32.63  ? 40  GLU F O   1 
ATOM   5835  C  CB  . GLU F  1 46  ? 85.037  62.530  69.649 1.00 44.07  ? 40  GLU F CB  1 
ATOM   5836  C  CG  . GLU F  1 46  ? 83.772  62.589  68.829 1.00 48.82  ? 40  GLU F CG  1 
ATOM   5837  C  CD  . GLU F  1 46  ? 82.539  62.645  69.693 1.00 52.37  ? 40  GLU F CD  1 
ATOM   5838  O  OE1 . GLU F  1 46  ? 81.429  62.743  69.131 1.00 46.11  ? 40  GLU F OE1 1 
ATOM   5839  O  OE2 . GLU F  1 46  ? 82.687  62.592  70.935 1.00 52.03  ? 40  GLU F OE2 1 
ATOM   5840  N  N   . GLY F  1 47  ? 86.014  63.687  66.695 1.00 35.56  ? 41  GLY F N   1 
ATOM   5841  C  CA  . GLY F  1 47  ? 86.057  64.858  65.850 1.00 33.85  ? 41  GLY F CA  1 
ATOM   5842  C  C   . GLY F  1 47  ? 86.875  64.651  64.591 1.00 34.27  ? 41  GLY F C   1 
ATOM   5843  O  O   . GLY F  1 47  ? 87.372  63.562  64.317 1.00 33.74  ? 41  GLY F O   1 
ATOM   5844  N  N   . LEU F  1 48  ? 87.011  65.723  63.826 1.00 30.75  ? 42  LEU F N   1 
ATOM   5845  C  CA  . LEU F  1 48  ? 87.733  65.696  62.581 1.00 25.99  ? 42  LEU F CA  1 
ATOM   5846  C  C   . LEU F  1 48  ? 89.241  65.774  62.769 1.00 27.19  ? 42  LEU F C   1 
ATOM   5847  O  O   . LEU F  1 48  ? 89.730  66.468  63.665 1.00 26.09  ? 42  LEU F O   1 
ATOM   5848  C  CB  . LEU F  1 48  ? 87.276  66.863  61.726 1.00 23.82  ? 42  LEU F CB  1 
ATOM   5849  C  CG  . LEU F  1 48  ? 85.803  66.887  61.352 1.00 24.88  ? 42  LEU F CG  1 
ATOM   5850  C  CD1 . LEU F  1 48  ? 85.574  68.046  60.391 1.00 19.58  ? 42  LEU F CD1 1 
ATOM   5851  C  CD2 . LEU F  1 48  ? 85.408  65.580  60.688 1.00 24.17  ? 42  LEU F CD2 1 
ATOM   5852  N  N   . HIS F  1 49  ? 89.971  65.065  61.909 1.00 22.17  ? 43  HIS F N   1 
ATOM   5853  C  CA  . HIS F  1 49  ? 91.440  65.063  61.943 1.00 16.00  ? 43  HIS F CA  1 
ATOM   5854  C  C   . HIS F  1 49  ? 92.014  65.075  60.519 1.00 15.57  ? 43  HIS F C   1 
ATOM   5855  O  O   . HIS F  1 49  ? 91.595  64.307  59.650 1.00 14.41  ? 43  HIS F O   1 
ATOM   5856  C  CB  . HIS F  1 49  ? 91.935  63.832  62.680 1.00 14.11  ? 43  HIS F CB  1 
ATOM   5857  C  CG  . HIS F  1 49  ? 91.650  63.850  64.148 1.00 22.81  ? 43  HIS F CG  1 
ATOM   5858  N  ND1 . HIS F  1 49  ? 92.488  64.452  65.063 1.00 23.21  ? 43  HIS F ND1 1 
ATOM   5859  C  CD2 . HIS F  1 49  ? 90.640  63.305  64.866 1.00 23.21  ? 43  HIS F CD2 1 
ATOM   5860  C  CE1 . HIS F  1 49  ? 92.013  64.269  66.281 1.00 21.67  ? 43  HIS F CE1 1 
ATOM   5861  N  NE2 . HIS F  1 49  ? 90.892  63.576  66.190 1.00 30.10  ? 43  HIS F NE2 1 
ATOM   5862  N  N   . GLY F  1 50  ? 92.959  65.965  60.268 1.00 15.89  ? 44  GLY F N   1 
ATOM   5863  C  CA  . GLY F  1 50  ? 93.556  66.018  58.945 1.00 20.47  ? 44  GLY F CA  1 
ATOM   5864  C  C   . GLY F  1 50  ? 94.217  64.684  58.650 1.00 21.56  ? 44  GLY F C   1 
ATOM   5865  O  O   . GLY F  1 50  ? 94.861  64.096  59.517 1.00 18.93  ? 44  GLY F O   1 
ATOM   5866  N  N   . PHE F  1 51  ? 94.059  64.231  57.413 1.00 19.68  ? 45  PHE F N   1 
ATOM   5867  C  CA  . PHE F  1 51  ? 94.577  62.957  56.935 1.00 19.34  ? 45  PHE F CA  1 
ATOM   5868  C  C   . PHE F  1 51  ? 95.337  63.277  55.633 1.00 20.18  ? 45  PHE F C   1 
ATOM   5869  O  O   . PHE F  1 51  ? 94.729  63.582  54.616 1.00 22.59  ? 45  PHE F O   1 
ATOM   5870  C  CB  . PHE F  1 51  ? 93.368  62.041  56.673 1.00 12.18  ? 45  PHE F CB  1 
ATOM   5871  C  CG  . PHE F  1 51  ? 93.705  60.591  56.459 1.00 18.68  ? 45  PHE F CG  1 
ATOM   5872  C  CD1 . PHE F  1 51  ? 94.429  59.871  57.420 1.00 21.14  ? 45  PHE F CD1 1 
ATOM   5873  C  CD2 . PHE F  1 51  ? 93.235  59.923  55.328 1.00 9.39   ? 45  PHE F CD2 1 
ATOM   5874  C  CE1 . PHE F  1 51  ? 94.679  58.500  57.260 1.00 18.20  ? 45  PHE F CE1 1 
ATOM   5875  C  CE2 . PHE F  1 51  ? 93.472  58.557  55.149 1.00 24.90  ? 45  PHE F CE2 1 
ATOM   5876  C  CZ  . PHE F  1 51  ? 94.202  57.835  56.123 1.00 23.59  ? 45  PHE F CZ  1 
ATOM   5877  N  N   . HIS F  1 52  ? 96.665  63.214  55.660 1.00 24.62  ? 46  HIS F N   1 
ATOM   5878  C  CA  . HIS F  1 52  ? 97.437  63.544  54.463 1.00 22.11  ? 46  HIS F CA  1 
ATOM   5879  C  C   . HIS F  1 52  ? 98.638  62.644  54.202 1.00 22.15  ? 46  HIS F C   1 
ATOM   5880  O  O   . HIS F  1 52  ? 99.204  62.045  55.117 1.00 20.47  ? 46  HIS F O   1 
ATOM   5881  C  CB  . HIS F  1 52  ? 97.997  64.974  54.534 1.00 25.16  ? 46  HIS F CB  1 
ATOM   5882  C  CG  . HIS F  1 52  ? 97.105  65.976  55.208 1.00 31.11  ? 46  HIS F CG  1 
ATOM   5883  N  ND1 . HIS F  1 52  ? 97.361  66.458  56.475 1.00 31.57  ? 46  HIS F ND1 1 
ATOM   5884  C  CD2 . HIS F  1 52  ? 96.000  66.629  54.773 1.00 20.60  ? 46  HIS F CD2 1 
ATOM   5885  C  CE1 . HIS F  1 52  ? 96.451  67.364  56.789 1.00 29.89  ? 46  HIS F CE1 1 
ATOM   5886  N  NE2 . HIS F  1 52  ? 95.614  67.486  55.773 1.00 23.84  ? 46  HIS F NE2 1 
ATOM   5887  N  N   . VAL F  1 53  ? 99.036  62.577  52.936 1.00 17.86  ? 47  VAL F N   1 
ATOM   5888  C  CA  . VAL F  1 53  ? 100.224 61.831  52.558 1.00 16.32  ? 47  VAL F CA  1 
ATOM   5889  C  C   . VAL F  1 53  ? 101.307 62.907  52.495 1.00 21.03  ? 47  VAL F C   1 
ATOM   5890  O  O   . VAL F  1 53  ? 101.175 63.886  51.748 1.00 19.15  ? 47  VAL F O   1 
ATOM   5891  C  CB  . VAL F  1 53  ? 100.091 61.187  51.161 1.00 24.71  ? 47  VAL F CB  1 
ATOM   5892  C  CG1 . VAL F  1 53  ? 101.411 60.503  50.770 1.00 16.91  ? 47  VAL F CG1 1 
ATOM   5893  C  CG2 . VAL F  1 53  ? 98.947  60.182  51.151 1.00 17.10  ? 47  VAL F CG2 1 
ATOM   5894  N  N   . HIS F  1 54  ? 102.355 62.755  53.298 1.00 14.22  ? 48  HIS F N   1 
ATOM   5895  C  CA  . HIS F  1 54  ? 103.443 63.725  53.289 1.00 19.75  ? 48  HIS F CA  1 
ATOM   5896  C  C   . HIS F  1 54  ? 104.551 63.247  52.346 1.00 20.62  ? 48  HIS F C   1 
ATOM   5897  O  O   . HIS F  1 54  ? 104.649 62.061  52.032 1.00 20.64  ? 48  HIS F O   1 
ATOM   5898  C  CB  . HIS F  1 54  ? 103.963 63.976  54.721 1.00 22.23  ? 48  HIS F CB  1 
ATOM   5899  C  CG  . HIS F  1 54  ? 103.008 64.758  55.579 1.00 24.77  ? 48  HIS F CG  1 
ATOM   5900  N  ND1 . HIS F  1 54  ? 103.350 65.952  56.183 1.00 22.75  ? 48  HIS F ND1 1 
ATOM   5901  C  CD2 . HIS F  1 54  ? 101.720 64.519  55.926 1.00 23.12  ? 48  HIS F CD2 1 
ATOM   5902  C  CE1 . HIS F  1 54  ? 102.317 66.410  56.869 1.00 22.78  ? 48  HIS F CE1 1 
ATOM   5903  N  NE2 . HIS F  1 54  ? 101.313 65.561  56.730 1.00 23.37  ? 48  HIS F NE2 1 
ATOM   5904  N  N   . GLU F  1 55  ? 105.383 64.177  51.900 1.00 21.80  ? 49  GLU F N   1 
ATOM   5905  C  CA  . GLU F  1 55  ? 106.435 63.883  50.931 1.00 25.80  ? 49  GLU F CA  1 
ATOM   5906  C  C   . GLU F  1 55  ? 107.466 62.772  51.153 1.00 28.65  ? 49  GLU F C   1 
ATOM   5907  O  O   . GLU F  1 55  ? 107.725 61.994  50.239 1.00 14.62  ? 49  GLU F O   1 
ATOM   5908  C  CB  . GLU F  1 55  ? 107.193 65.167  50.598 1.00 22.28  ? 49  GLU F CB  1 
ATOM   5909  C  CG  . GLU F  1 55  ? 108.070 65.012  49.385 1.00 26.37  ? 49  GLU F CG  1 
ATOM   5910  C  CD  . GLU F  1 55  ? 108.795 66.286  48.988 1.00 32.49  ? 49  GLU F CD  1 
ATOM   5911  O  OE1 . GLU F  1 55  ? 109.541 66.221  47.996 1.00 29.85  ? 49  GLU F OE1 1 
ATOM   5912  O  OE2 . GLU F  1 55  ? 108.632 67.338  49.646 1.00 26.38  ? 49  GLU F OE2 1 
ATOM   5913  N  N   . PHE F  1 56  ? 108.061 62.694  52.339 1.00 24.40  ? 50  PHE F N   1 
ATOM   5914  C  CA  . PHE F  1 56  ? 109.100 61.699  52.589 1.00 24.51  ? 50  PHE F CA  1 
ATOM   5915  C  C   . PHE F  1 56  ? 108.705 60.536  53.474 1.00 28.22  ? 50  PHE F C   1 
ATOM   5916  O  O   . PHE F  1 56  ? 107.954 60.702  54.431 1.00 26.89  ? 50  PHE F O   1 
ATOM   5917  C  CB  . PHE F  1 56  ? 110.320 62.390  53.200 1.00 27.02  ? 50  PHE F CB  1 
ATOM   5918  C  CG  . PHE F  1 56  ? 110.828 63.524  52.376 1.00 25.98  ? 50  PHE F CG  1 
ATOM   5919  C  CD1 . PHE F  1 56  ? 111.266 63.303  51.072 1.00 29.77  ? 50  PHE F CD1 1 
ATOM   5920  C  CD2 . PHE F  1 56  ? 110.781 64.822  52.856 1.00 26.73  ? 50  PHE F CD2 1 
ATOM   5921  C  CE1 . PHE F  1 56  ? 111.644 64.361  50.243 1.00 31.77  ? 50  PHE F CE1 1 
ATOM   5922  C  CE2 . PHE F  1 56  ? 111.155 65.891  52.036 1.00 29.44  ? 50  PHE F CE2 1 
ATOM   5923  C  CZ  . PHE F  1 56  ? 111.587 65.657  50.720 1.00 26.05  ? 50  PHE F CZ  1 
ATOM   5924  N  N   . GLY F  1 57  ? 109.222 59.355  53.140 1.00 26.38  ? 51  GLY F N   1 
ATOM   5925  C  CA  . GLY F  1 57  ? 108.957 58.170  53.939 1.00 24.70  ? 51  GLY F CA  1 
ATOM   5926  C  C   . GLY F  1 57  ? 110.138 58.065  54.883 1.00 24.73  ? 51  GLY F C   1 
ATOM   5927  O  O   . GLY F  1 57  ? 110.808 57.039  54.962 1.00 23.08  ? 51  GLY F O   1 
ATOM   5928  N  N   . ASP F  1 58  ? 110.392 59.161  55.591 1.00 23.27  ? 52  ASP F N   1 
ATOM   5929  C  CA  . ASP F  1 58  ? 111.512 59.279  56.511 1.00 23.52  ? 52  ASP F CA  1 
ATOM   5930  C  C   . ASP F  1 58  ? 111.010 59.472  57.946 1.00 23.87  ? 52  ASP F C   1 
ATOM   5931  O  O   . ASP F  1 58  ? 110.439 60.504  58.293 1.00 22.91  ? 52  ASP F O   1 
ATOM   5932  C  CB  . ASP F  1 58  ? 112.374 60.465  56.055 1.00 19.89  ? 52  ASP F CB  1 
ATOM   5933  C  CG  . ASP F  1 58  ? 113.603 60.686  56.922 1.00 33.00  ? 52  ASP F CG  1 
ATOM   5934  O  OD1 . ASP F  1 58  ? 114.528 61.389  56.441 1.00 25.33  ? 52  ASP F OD1 1 
ATOM   5935  O  OD2 . ASP F  1 58  ? 113.647 60.178  58.074 1.00 23.32  ? 52  ASP F OD2 1 
ATOM   5936  N  N   . ASN F  1 59  ? 111.220 58.463  58.775 1.00 24.93  ? 53  ASN F N   1 
ATOM   5937  C  CA  . ASN F  1 59  ? 110.786 58.528  60.159 1.00 28.11  ? 53  ASN F CA  1 
ATOM   5938  C  C   . ASN F  1 59  ? 111.962 58.632  61.136 1.00 22.43  ? 53  ASN F C   1 
ATOM   5939  O  O   . ASN F  1 59  ? 111.807 58.345  62.308 1.00 18.29  ? 53  ASN F O   1 
ATOM   5940  C  CB  . ASN F  1 59  ? 109.934 57.290  60.490 1.00 29.38  ? 53  ASN F CB  1 
ATOM   5941  C  CG  . ASN F  1 59  ? 109.208 57.405  61.848 1.00 51.78  ? 53  ASN F CG  1 
ATOM   5942  O  OD1 . ASN F  1 59  ? 109.547 56.709  62.817 1.00 46.69  ? 53  ASN F OD1 1 
ATOM   5943  N  ND2 . ASN F  1 59  ? 108.212 58.293  61.919 1.00 51.91  ? 53  ASN F ND2 1 
ATOM   5944  N  N   . THR F  1 60  ? 113.128 59.057  60.661 1.00 23.43  ? 54  THR F N   1 
ATOM   5945  C  CA  . THR F  1 60  ? 114.291 59.167  61.537 1.00 22.48  ? 54  THR F CA  1 
ATOM   5946  C  C   . THR F  1 60  ? 114.088 60.103  62.724 1.00 27.89  ? 54  THR F C   1 
ATOM   5947  O  O   . THR F  1 60  ? 114.755 59.983  63.738 1.00 29.26  ? 54  THR F O   1 
ATOM   5948  C  CB  . THR F  1 60  ? 115.522 59.628  60.767 1.00 25.56  ? 54  THR F CB  1 
ATOM   5949  O  OG1 . THR F  1 60  ? 115.215 60.839  60.068 1.00 26.97  ? 54  THR F OG1 1 
ATOM   5950  C  CG2 . THR F  1 60  ? 115.958 58.554  59.783 1.00 24.09  ? 54  THR F CG2 1 
ATOM   5951  N  N   . ALA F  1 61  ? 113.178 61.052  62.598 1.00 30.38  ? 55  ALA F N   1 
ATOM   5952  C  CA  . ALA F  1 61  ? 112.910 61.950  63.705 1.00 32.93  ? 55  ALA F CA  1 
ATOM   5953  C  C   . ALA F  1 61  ? 111.407 61.924  63.967 1.00 32.65  ? 55  ALA F C   1 
ATOM   5954  O  O   . ALA F  1 61  ? 110.806 62.929  64.357 1.00 36.69  ? 55  ALA F O   1 
ATOM   5955  C  CB  . ALA F  1 61  ? 113.378 63.361  63.368 1.00 22.59  ? 55  ALA F CB  1 
ATOM   5956  N  N   . GLY F  1 62  ? 110.804 60.760  63.748 1.00 32.86  ? 56  GLY F N   1 
ATOM   5957  C  CA  . GLY F  1 62  ? 109.371 60.637  63.951 1.00 30.78  ? 56  GLY F CA  1 
ATOM   5958  C  C   . GLY F  1 62  ? 108.622 61.207  62.760 1.00 32.42  ? 56  GLY F C   1 
ATOM   5959  O  O   . GLY F  1 62  ? 109.156 61.274  61.645 1.00 35.69  ? 56  GLY F O   1 
ATOM   5960  N  N   . CYS F  1 63  ? 107.392 61.645  63.002 1.00 28.87  ? 57  CYS F N   1 
ATOM   5961  C  CA  . CYS F  1 63  ? 106.543 62.204  61.955 1.00 27.06  ? 57  CYS F CA  1 
ATOM   5962  C  C   . CYS F  1 63  ? 107.079 63.509  61.361 1.00 26.23  ? 57  CYS F C   1 
ATOM   5963  O  O   . CYS F  1 63  ? 106.852 63.818  60.196 1.00 19.21  ? 57  CYS F O   1 
ATOM   5964  C  CB  . CYS F  1 63  ? 105.125 62.361  62.507 1.00 21.05  ? 57  CYS F CB  1 
ATOM   5965  S  SG  . CYS F  1 63  ? 104.476 60.732  63.020 1.00 30.36  ? 57  CYS F SG  1 
ATOM   5966  N  N   . THR F  1 64  ? 107.834 64.249  62.157 1.00 25.14  ? 58  THR F N   1 
ATOM   5967  C  CA  . THR F  1 64  ? 108.417 65.500  61.705 1.00 22.17  ? 58  THR F CA  1 
ATOM   5968  C  C   . THR F  1 64  ? 109.223 65.363  60.427 1.00 23.95  ? 58  THR F C   1 
ATOM   5969  O  O   . THR F  1 64  ? 109.155 66.229  59.556 1.00 23.84  ? 58  THR F O   1 
ATOM   5970  C  CB  . THR F  1 64  ? 109.359 66.053  62.742 1.00 31.36  ? 58  THR F CB  1 
ATOM   5971  O  OG1 . THR F  1 64  ? 108.691 66.099  64.006 1.00 37.62  ? 58  THR F OG1 1 
ATOM   5972  C  CG2 . THR F  1 64  ? 109.822 67.438  62.329 1.00 19.67  ? 58  THR F CG2 1 
ATOM   5973  N  N   . SER F  1 65  ? 109.981 64.272  60.323 1.00 25.57  ? 59  SER F N   1 
ATOM   5974  C  CA  . SER F  1 65  ? 110.839 64.013  59.168 1.00 26.91  ? 59  SER F CA  1 
ATOM   5975  C  C   . SER F  1 65  ? 110.116 63.721  57.849 1.00 27.70  ? 59  SER F C   1 
ATOM   5976  O  O   . SER F  1 65  ? 110.773 63.639  56.813 1.00 24.38  ? 59  SER F O   1 
ATOM   5977  C  CB  . SER F  1 65  ? 111.769 62.828  59.457 1.00 24.04  ? 59  SER F CB  1 
ATOM   5978  O  OG  . SER F  1 65  ? 112.375 62.938  60.716 1.00 39.86  ? 59  SER F OG  1 
ATOM   5979  N  N   . ALA F  1 66  ? 108.793 63.532  57.888 1.00 20.38  ? 60  ALA F N   1 
ATOM   5980  C  CA  . ALA F  1 66  ? 108.029 63.220  56.683 1.00 20.42  ? 60  ALA F CA  1 
ATOM   5981  C  C   . ALA F  1 66  ? 107.897 64.414  55.767 1.00 21.92  ? 60  ALA F C   1 
ATOM   5982  O  O   . ALA F  1 66  ? 107.460 64.285  54.623 1.00 21.17  ? 60  ALA F O   1 
ATOM   5983  C  CB  . ALA F  1 66  ? 106.645 62.692  57.044 1.00 16.42  ? 60  ALA F CB  1 
ATOM   5984  N  N   . GLY F  1 67  ? 108.259 65.589  56.269 1.00 22.68  ? 61  GLY F N   1 
ATOM   5985  C  CA  . GLY F  1 67  ? 108.190 66.763  55.425 1.00 17.91  ? 61  GLY F CA  1 
ATOM   5986  C  C   . GLY F  1 67  ? 106.798 67.328  55.199 1.00 24.67  ? 61  GLY F C   1 
ATOM   5987  O  O   . GLY F  1 67  ? 105.834 67.018  55.912 1.00 19.88  ? 61  GLY F O   1 
ATOM   5988  N  N   . PRO F  1 68  ? 106.672 68.187  54.192 1.00 21.52  ? 62  PRO F N   1 
ATOM   5989  C  CA  . PRO F  1 68  ? 105.372 68.799  53.893 1.00 23.28  ? 62  PRO F CA  1 
ATOM   5990  C  C   . PRO F  1 68  ? 104.471 67.811  53.159 1.00 21.65  ? 62  PRO F C   1 
ATOM   5991  O  O   . PRO F  1 68  ? 104.868 66.673  52.911 1.00 25.98  ? 62  PRO F O   1 
ATOM   5992  C  CB  . PRO F  1 68  ? 105.761 70.021  53.049 1.00 13.70  ? 62  PRO F CB  1 
ATOM   5993  C  CG  . PRO F  1 68  ? 106.928 69.454  52.210 1.00 23.10  ? 62  PRO F CG  1 
ATOM   5994  C  CD  . PRO F  1 68  ? 107.724 68.636  53.255 1.00 14.70  ? 62  PRO F CD  1 
ATOM   5995  N  N   . HIS F  1 69  ? 103.257 68.238  52.833 1.00 21.16  ? 63  HIS F N   1 
ATOM   5996  C  CA  . HIS F  1 69  ? 102.315 67.382  52.110 1.00 22.62  ? 63  HIS F CA  1 
ATOM   5997  C  C   . HIS F  1 69  ? 102.941 67.006  50.768 1.00 20.82  ? 63  HIS F C   1 
ATOM   5998  O  O   . HIS F  1 69  ? 103.645 67.810  50.177 1.00 22.63  ? 63  HIS F O   1 
ATOM   5999  C  CB  . HIS F  1 69  ? 100.981 68.129  51.852 1.00 12.60  ? 63  HIS F CB  1 
ATOM   6000  C  CG  . HIS F  1 69  ? 100.172 68.389  53.091 1.00 23.60  ? 63  HIS F CG  1 
ATOM   6001  N  ND1 . HIS F  1 69  ? 98.913  68.949  53.053 1.00 26.96  ? 63  HIS F ND1 1 
ATOM   6002  C  CD2 . HIS F  1 69  ? 100.428 68.134  54.399 1.00 18.12  ? 63  HIS F CD2 1 
ATOM   6003  C  CE1 . HIS F  1 69  ? 98.425  69.022  54.280 1.00 24.02  ? 63  HIS F CE1 1 
ATOM   6004  N  NE2 . HIS F  1 69  ? 99.323  68.533  55.115 1.00 26.84  ? 63  HIS F NE2 1 
ATOM   6005  N  N   . PHE F  1 70  ? 102.701 65.783  50.299 1.00 26.83  ? 64  PHE F N   1 
ATOM   6006  C  CA  . PHE F  1 70  ? 103.221 65.337  49.002 1.00 20.97  ? 64  PHE F CA  1 
ATOM   6007  C  C   . PHE F  1 70  ? 102.533 66.245  47.982 1.00 21.61  ? 64  PHE F C   1 
ATOM   6008  O  O   . PHE F  1 70  ? 101.308 66.246  47.852 1.00 21.74  ? 64  PHE F O   1 
ATOM   6009  C  CB  . PHE F  1 70  ? 102.846 63.875  48.774 1.00 25.93  ? 64  PHE F CB  1 
ATOM   6010  C  CG  . PHE F  1 70  ? 103.241 63.343  47.428 1.00 17.54  ? 64  PHE F CG  1 
ATOM   6011  C  CD1 . PHE F  1 70  ? 102.390 62.487  46.737 1.00 9.92   ? 64  PHE F CD1 1 
ATOM   6012  C  CD2 . PHE F  1 70  ? 104.462 63.668  46.868 1.00 19.20  ? 64  PHE F CD2 1 
ATOM   6013  C  CE1 . PHE F  1 70  ? 102.753 61.954  45.491 1.00 22.44  ? 64  PHE F CE1 1 
ATOM   6014  C  CE2 . PHE F  1 70  ? 104.839 63.144  45.623 1.00 20.04  ? 64  PHE F CE2 1 
ATOM   6015  C  CZ  . PHE F  1 70  ? 103.981 62.284  44.936 1.00 16.38  ? 64  PHE F CZ  1 
ATOM   6016  N  N   . ASN F  1 71  ? 103.326 67.011  47.253 1.00 18.62  ? 65  ASN F N   1 
ATOM   6017  C  CA  . ASN F  1 71  ? 102.791 67.979  46.329 1.00 18.88  ? 65  ASN F CA  1 
ATOM   6018  C  C   . ASN F  1 71  ? 103.619 68.038  45.053 1.00 27.85  ? 65  ASN F C   1 
ATOM   6019  O  O   . ASN F  1 71  ? 104.219 69.058  44.725 1.00 32.62  ? 65  ASN F O   1 
ATOM   6020  C  CB  . ASN F  1 71  ? 102.796 69.324  47.055 1.00 19.67  ? 65  ASN F CB  1 
ATOM   6021  C  CG  . ASN F  1 71  ? 102.265 70.461  46.209 1.00 29.70  ? 65  ASN F CG  1 
ATOM   6022  O  OD1 . ASN F  1 71  ? 101.470 70.250  45.288 1.00 17.20  ? 65  ASN F OD1 1 
ATOM   6023  N  ND2 . ASN F  1 71  ? 102.687 71.690  46.538 1.00 11.98  ? 65  ASN F ND2 1 
ATOM   6024  N  N   . PRO F  1 72  ? 103.655 66.938  44.306 1.00 28.91  ? 66  PRO F N   1 
ATOM   6025  C  CA  . PRO F  1 72  ? 104.438 66.926  43.069 1.00 30.96  ? 66  PRO F CA  1 
ATOM   6026  C  C   . PRO F  1 72  ? 104.118 68.017  42.048 1.00 36.02  ? 66  PRO F C   1 
ATOM   6027  O  O   . PRO F  1 72  ? 105.007 68.441  41.325 1.00 37.57  ? 66  PRO F O   1 
ATOM   6028  C  CB  . PRO F  1 72  ? 104.198 65.524  42.520 1.00 31.47  ? 66  PRO F CB  1 
ATOM   6029  C  CG  . PRO F  1 72  ? 102.825 65.163  43.079 1.00 37.05  ? 66  PRO F CG  1 
ATOM   6030  C  CD  . PRO F  1 72  ? 102.881 65.695  44.477 1.00 28.46  ? 66  PRO F CD  1 
ATOM   6031  N  N   . LEU F  1 73  ? 102.871 68.484  42.003 1.00 32.10  ? 67  LEU F N   1 
ATOM   6032  C  CA  . LEU F  1 73  ? 102.463 69.513  41.041 1.00 33.30  ? 67  LEU F CA  1 
ATOM   6033  C  C   . LEU F  1 73  ? 102.554 70.954  41.542 1.00 35.50  ? 67  LEU F C   1 
ATOM   6034  O  O   . LEU F  1 73  ? 102.080 71.878  40.879 1.00 33.48  ? 67  LEU F O   1 
ATOM   6035  C  CB  . LEU F  1 73  ? 101.043 69.217  40.535 1.00 30.22  ? 67  LEU F CB  1 
ATOM   6036  C  CG  . LEU F  1 73  ? 100.965 67.796  39.942 1.00 46.36  ? 67  LEU F CG  1 
ATOM   6037  C  CD1 . LEU F  1 73  ? 99.525  67.383  39.611 1.00 39.45  ? 67  LEU F CD1 1 
ATOM   6038  C  CD2 . LEU F  1 73  ? 101.854 67.746  38.693 1.00 40.51  ? 67  LEU F CD2 1 
ATOM   6039  N  N   . SER F  1 74  ? 103.170 71.144  42.706 1.00 34.51  ? 68  SER F N   1 
ATOM   6040  C  CA  . SER F  1 74  ? 103.354 72.478  43.281 1.00 39.83  ? 68  SER F CA  1 
ATOM   6041  C  C   . SER F  1 74  ? 102.102 73.332  43.384 1.00 40.13  ? 68  SER F C   1 
ATOM   6042  O  O   . SER F  1 74  ? 102.109 74.475  42.942 1.00 42.05  ? 68  SER F O   1 
ATOM   6043  C  CB  . SER F  1 74  ? 104.383 73.281  42.478 1.00 40.60  ? 68  SER F CB  1 
ATOM   6044  O  OG  . SER F  1 74  ? 105.630 72.622  42.397 1.00 47.11  ? 68  SER F OG  1 
ATOM   6045  N  N   . ARG F  1 75  ? 101.038 72.806  43.972 1.00 36.04  ? 69  ARG F N   1 
ATOM   6046  C  CA  . ARG F  1 75  ? 99.821  73.589  44.107 1.00 33.63  ? 69  ARG F CA  1 
ATOM   6047  C  C   . ARG F  1 75  ? 99.558  73.945  45.563 1.00 30.96  ? 69  ARG F C   1 
ATOM   6048  O  O   . ARG F  1 75  ? 100.305 73.544  46.454 1.00 30.83  ? 69  ARG F O   1 
ATOM   6049  C  CB  . ARG F  1 75  ? 98.647  72.826  43.501 1.00 34.41  ? 69  ARG F CB  1 
ATOM   6050  C  CG  . ARG F  1 75  ? 98.717  72.787  41.983 1.00 38.41  ? 69  ARG F CG  1 
ATOM   6051  C  CD  . ARG F  1 75  ? 97.655  71.887  41.401 1.00 63.98  ? 69  ARG F CD  1 
ATOM   6052  N  NE  . ARG F  1 75  ? 97.900  71.590  39.991 1.00 76.53  ? 69  ARG F NE  1 
ATOM   6053  C  CZ  . ARG F  1 75  ? 97.207  70.703  39.279 1.00 79.50  ? 69  ARG F CZ  1 
ATOM   6054  N  NH1 . ARG F  1 75  ? 96.214  70.017  39.838 1.00 82.26  ? 69  ARG F NH1 1 
ATOM   6055  N  NH2 . ARG F  1 75  ? 97.517  70.489  38.007 1.00 76.07  ? 69  ARG F NH2 1 
ATOM   6056  N  N   . LYS F  1 76  ? 98.521  74.734  45.803 1.00 28.71  ? 70  LYS F N   1 
ATOM   6057  C  CA  . LYS F  1 76  ? 98.174  75.130  47.162 1.00 31.23  ? 70  LYS F CA  1 
ATOM   6058  C  C   . LYS F  1 76  ? 97.382  74.010  47.826 1.00 28.55  ? 70  LYS F C   1 
ATOM   6059  O  O   . LYS F  1 76  ? 96.799  73.168  47.141 1.00 22.08  ? 70  LYS F O   1 
ATOM   6060  C  CB  . LYS F  1 76  ? 97.333  76.408  47.149 1.00 33.35  ? 70  LYS F CB  1 
ATOM   6061  C  CG  . LYS F  1 76  ? 98.112  77.698  46.885 1.00 48.64  ? 70  LYS F CG  1 
ATOM   6062  C  CD  . LYS F  1 76  ? 97.149  78.841  46.552 1.00 62.82  ? 70  LYS F CD  1 
ATOM   6063  C  CE  . LYS F  1 76  ? 97.826  80.208  46.566 1.00 73.72  ? 70  LYS F CE  1 
ATOM   6064  N  NZ  . LYS F  1 76  ? 98.037  80.753  47.949 1.00 81.45  ? 70  LYS F NZ  1 
ATOM   6065  N  N   . HIS F  1 77  ? 97.362  74.003  49.155 1.00 16.72  ? 71  HIS F N   1 
ATOM   6066  C  CA  . HIS F  1 77  ? 96.627  72.982  49.892 1.00 23.55  ? 71  HIS F CA  1 
ATOM   6067  C  C   . HIS F  1 77  ? 95.119  73.120  49.607 1.00 22.78  ? 71  HIS F C   1 
ATOM   6068  O  O   . HIS F  1 77  ? 94.621  74.217  49.389 1.00 23.92  ? 71  HIS F O   1 
ATOM   6069  C  CB  . HIS F  1 77  ? 96.897  73.128  51.404 1.00 13.89  ? 71  HIS F CB  1 
ATOM   6070  C  CG  . HIS F  1 77  ? 96.086  72.195  52.256 1.00 25.10  ? 71  HIS F CG  1 
ATOM   6071  N  ND1 . HIS F  1 77  ? 96.392  70.858  52.406 1.00 20.94  ? 71  HIS F ND1 1 
ATOM   6072  C  CD2 . HIS F  1 77  ? 94.958  72.404  52.977 1.00 17.07  ? 71  HIS F CD2 1 
ATOM   6073  C  CE1 . HIS F  1 77  ? 95.492  70.286  53.184 1.00 23.11  ? 71  HIS F CE1 1 
ATOM   6074  N  NE2 . HIS F  1 77  ? 94.611  71.203  53.545 1.00 23.17  ? 71  HIS F NE2 1 
ATOM   6075  N  N   . GLY F  1 78  ? 94.398  72.005  49.609 1.00 28.36  ? 72  GLY F N   1 
ATOM   6076  C  CA  . GLY F  1 78  ? 92.967  72.047  49.366 1.00 21.92  ? 72  GLY F CA  1 
ATOM   6077  C  C   . GLY F  1 78  ? 92.322  70.788  49.909 1.00 27.01  ? 72  GLY F C   1 
ATOM   6078  O  O   . GLY F  1 78  ? 92.983  69.977  50.551 1.00 27.89  ? 72  GLY F O   1 
ATOM   6079  N  N   . GLY F  1 79  ? 91.025  70.632  49.689 1.00 27.61  ? 73  GLY F N   1 
ATOM   6080  C  CA  . GLY F  1 79  ? 90.348  69.437  50.149 1.00 24.32  ? 73  GLY F CA  1 
ATOM   6081  C  C   . GLY F  1 79  ? 90.449  68.419  49.025 1.00 24.72  ? 73  GLY F C   1 
ATOM   6082  O  O   . GLY F  1 79  ? 90.800  68.775  47.902 1.00 19.25  ? 73  GLY F O   1 
ATOM   6083  N  N   . PRO F  1 80  ? 90.154  67.144  49.284 1.00 21.70  ? 74  PRO F N   1 
ATOM   6084  C  CA  . PRO F  1 80  ? 90.258  66.171  48.194 1.00 25.02  ? 74  PRO F CA  1 
ATOM   6085  C  C   . PRO F  1 80  ? 89.404  66.468  46.965 1.00 29.42  ? 74  PRO F C   1 
ATOM   6086  O  O   . PRO F  1 80  ? 89.723  66.013  45.863 1.00 20.61  ? 74  PRO F O   1 
ATOM   6087  C  CB  . PRO F  1 80  ? 89.889  64.846  48.867 1.00 28.04  ? 74  PRO F CB  1 
ATOM   6088  C  CG  . PRO F  1 80  ? 89.073  65.276  50.099 1.00 20.24  ? 74  PRO F CG  1 
ATOM   6089  C  CD  . PRO F  1 80  ? 89.798  66.500  50.559 1.00 21.73  ? 74  PRO F CD  1 
ATOM   6090  N  N   . LYS F  1 81  ? 88.343  67.258  47.127 1.00 29.30  ? 75  LYS F N   1 
ATOM   6091  C  CA  . LYS F  1 81  ? 87.478  67.541  45.982 1.00 30.40  ? 75  LYS F CA  1 
ATOM   6092  C  C   . LYS F  1 81  ? 87.890  68.714  45.082 1.00 30.48  ? 75  LYS F C   1 
ATOM   6093  O  O   . LYS F  1 81  ? 87.453  68.802  43.933 1.00 30.23  ? 75  LYS F O   1 
ATOM   6094  C  CB  . LYS F  1 81  ? 86.046  67.733  46.465 1.00 26.92  ? 75  LYS F CB  1 
ATOM   6095  C  CG  . LYS F  1 81  ? 85.467  66.539  47.219 1.00 35.14  ? 75  LYS F CG  1 
ATOM   6096  C  CD  . LYS F  1 81  ? 84.246  66.965  48.072 1.00 45.87  ? 75  LYS F CD  1 
ATOM   6097  C  CE  . LYS F  1 81  ? 83.081  67.536  47.223 1.00 55.53  ? 75  LYS F CE  1 
ATOM   6098  N  NZ  . LYS F  1 81  ? 82.222  68.531  47.963 1.00 56.10  ? 75  LYS F NZ  1 
ATOM   6099  N  N   . ASP F  1 82  ? 88.741  69.600  45.591 1.00 27.60  ? 76  ASP F N   1 
ATOM   6100  C  CA  . ASP F  1 82  ? 89.197  70.764  44.834 1.00 30.78  ? 76  ASP F CA  1 
ATOM   6101  C  C   . ASP F  1 82  ? 90.116  70.442  43.666 1.00 30.50  ? 76  ASP F C   1 
ATOM   6102  O  O   . ASP F  1 82  ? 90.813  69.440  43.678 1.00 35.42  ? 76  ASP F O   1 
ATOM   6103  C  CB  . ASP F  1 82  ? 89.935  71.725  45.760 1.00 34.10  ? 76  ASP F CB  1 
ATOM   6104  C  CG  . ASP F  1 82  ? 89.046  72.287  46.833 1.00 42.47  ? 76  ASP F CG  1 
ATOM   6105  O  OD1 . ASP F  1 82  ? 89.567  72.587  47.923 1.00 47.38  ? 76  ASP F OD1 1 
ATOM   6106  O  OD2 . ASP F  1 82  ? 87.829  72.438  46.585 1.00 51.29  ? 76  ASP F OD2 1 
ATOM   6107  N  N   . GLU F  1 83  ? 90.122  71.307  42.659 1.00 34.71  ? 77  GLU F N   1 
ATOM   6108  C  CA  . GLU F  1 83  ? 91.009  71.116  41.524 1.00 39.01  ? 77  GLU F CA  1 
ATOM   6109  C  C   . GLU F  1 83  ? 92.375  71.568  42.056 1.00 38.14  ? 77  GLU F C   1 
ATOM   6110  O  O   . GLU F  1 83  ? 93.423  71.015  41.708 1.00 40.00  ? 77  GLU F O   1 
ATOM   6111  C  CB  . GLU F  1 83  ? 90.553  71.980  40.345 1.00 45.15  ? 77  GLU F CB  1 
ATOM   6112  C  CG  . GLU F  1 83  ? 91.541  72.104  39.185 1.00 66.28  ? 77  GLU F CG  1 
ATOM   6113  C  CD  . GLU F  1 83  ? 91.887  70.771  38.533 1.00 85.84  ? 77  GLU F CD  1 
ATOM   6114  O  OE1 . GLU F  1 83  ? 90.956  70.013  38.170 1.00 93.38  ? 77  GLU F OE1 1 
ATOM   6115  O  OE2 . GLU F  1 83  ? 93.096  70.483  38.370 1.00 95.44  ? 77  GLU F OE2 1 
ATOM   6116  N  N   . GLU F  1 84  ? 92.349  72.569  42.930 1.00 34.87  ? 78  GLU F N   1 
ATOM   6117  C  CA  . GLU F  1 84  ? 93.575  73.078  43.525 1.00 29.73  ? 78  GLU F CA  1 
ATOM   6118  C  C   . GLU F  1 84  ? 93.805  72.354  44.851 1.00 27.35  ? 78  GLU F C   1 
ATOM   6119  O  O   . GLU F  1 84  ? 93.203  72.696  45.863 1.00 24.42  ? 78  GLU F O   1 
ATOM   6120  C  CB  . GLU F  1 84  ? 93.473  74.584  43.775 1.00 25.59  ? 78  GLU F CB  1 
ATOM   6121  C  CG  . GLU F  1 84  ? 94.751  75.229  44.304 1.00 35.59  ? 78  GLU F CG  1 
ATOM   6122  C  CD  . GLU F  1 84  ? 95.867  75.243  43.269 1.00 52.06  ? 78  GLU F CD  1 
ATOM   6123  O  OE1 . GLU F  1 84  ? 97.015  75.605  43.628 1.00 43.31  ? 78  GLU F OE1 1 
ATOM   6124  O  OE2 . GLU F  1 84  ? 95.594  74.898  42.091 1.00 60.41  ? 78  GLU F OE2 1 
ATOM   6125  N  N   . ARG F  1 85  ? 94.684  71.357  44.827 1.00 26.45  ? 79  ARG F N   1 
ATOM   6126  C  CA  . ARG F  1 85  ? 95.014  70.579  46.010 1.00 21.43  ? 79  ARG F CA  1 
ATOM   6127  C  C   . ARG F  1 85  ? 96.354  69.882  45.851 1.00 22.67  ? 79  ARG F C   1 
ATOM   6128  O  O   . ARG F  1 85  ? 96.837  69.659  44.747 1.00 26.64  ? 79  ARG F O   1 
ATOM   6129  C  CB  . ARG F  1 85  ? 93.943  69.523  46.266 1.00 25.20  ? 79  ARG F CB  1 
ATOM   6130  C  CG  . ARG F  1 85  ? 93.826  68.464  45.167 1.00 27.61  ? 79  ARG F CG  1 
ATOM   6131  C  CD  . ARG F  1 85  ? 94.289  67.096  45.658 1.00 33.30  ? 79  ARG F CD  1 
ATOM   6132  N  NE  . ARG F  1 85  ? 93.169  66.175  45.736 1.00 27.18  ? 79  ARG F NE  1 
ATOM   6133  C  CZ  . ARG F  1 85  ? 93.250  64.894  46.075 1.00 24.16  ? 79  ARG F CZ  1 
ATOM   6134  N  NH1 . ARG F  1 85  ? 94.403  64.340  46.390 1.00 26.63  ? 79  ARG F NH1 1 
ATOM   6135  N  NH2 . ARG F  1 85  ? 92.160  64.153  46.058 1.00 27.95  ? 79  ARG F NH2 1 
ATOM   6136  N  N   . HIS F  1 86  ? 96.961  69.548  46.975 1.00 26.86  ? 80  HIS F N   1 
ATOM   6137  C  CA  . HIS F  1 86  ? 98.218  68.831  46.956 1.00 20.70  ? 80  HIS F CA  1 
ATOM   6138  C  C   . HIS F  1 86  ? 97.794  67.409  46.604 1.00 25.82  ? 80  HIS F C   1 
ATOM   6139  O  O   . HIS F  1 86  ? 96.661  67.003  46.917 1.00 22.32  ? 80  HIS F O   1 
ATOM   6140  C  CB  . HIS F  1 86  ? 98.833  68.840  48.356 1.00 23.53  ? 80  HIS F CB  1 
ATOM   6141  C  CG  . HIS F  1 86  ? 99.317  70.182  48.805 1.00 21.15  ? 80  HIS F CG  1 
ATOM   6142  N  ND1 . HIS F  1 86  ? 99.240  70.594  50.118 1.00 19.71  ? 80  HIS F ND1 1 
ATOM   6143  C  CD2 . HIS F  1 86  ? 99.962  71.170  48.135 1.00 16.16  ? 80  HIS F CD2 1 
ATOM   6144  C  CE1 . HIS F  1 86  ? 99.821  71.775  50.239 1.00 23.04  ? 80  HIS F CE1 1 
ATOM   6145  N  NE2 . HIS F  1 86  ? 100.267 72.146  49.050 1.00 22.26  ? 80  HIS F NE2 1 
ATOM   6146  N  N   . VAL F  1 87  ? 98.667  66.649  45.952 1.00 20.01  ? 81  VAL F N   1 
ATOM   6147  C  CA  . VAL F  1 87  ? 98.319  65.258  45.642 1.00 19.69  ? 81  VAL F CA  1 
ATOM   6148  C  C   . VAL F  1 87  ? 98.014  64.493  46.938 1.00 17.26  ? 81  VAL F C   1 
ATOM   6149  O  O   . VAL F  1 87  ? 97.107  63.656  46.979 1.00 15.65  ? 81  VAL F O   1 
ATOM   6150  C  CB  . VAL F  1 87  ? 99.461  64.530  44.872 1.00 23.48  ? 81  VAL F CB  1 
ATOM   6151  C  CG1 . VAL F  1 87  ? 99.268  63.004  44.931 1.00 19.08  ? 81  VAL F CG1 1 
ATOM   6152  C  CG2 . VAL F  1 87  ? 99.458  64.983  43.412 1.00 15.64  ? 81  VAL F CG2 1 
ATOM   6153  N  N   . GLY F  1 88  ? 98.747  64.795  48.006 1.00 15.92  ? 82  GLY F N   1 
ATOM   6154  C  CA  . GLY F  1 88  ? 98.513  64.077  49.249 1.00 18.32  ? 82  GLY F CA  1 
ATOM   6155  C  C   . GLY F  1 88  ? 97.358  64.579  50.110 1.00 24.56  ? 82  GLY F C   1 
ATOM   6156  O  O   . GLY F  1 88  ? 97.236  64.128  51.248 1.00 16.85  ? 82  GLY F O   1 
ATOM   6157  N  N   . ASP F  1 89  ? 96.512  65.485  49.600 1.00 23.09  ? 83  ASP F N   1 
ATOM   6158  C  CA  . ASP F  1 89  ? 95.404  66.023  50.416 1.00 20.32  ? 83  ASP F CA  1 
ATOM   6159  C  C   . ASP F  1 89  ? 94.177  65.095  50.429 1.00 22.83  ? 83  ASP F C   1 
ATOM   6160  O  O   . ASP F  1 89  ? 93.343  65.142  49.529 1.00 20.58  ? 83  ASP F O   1 
ATOM   6161  C  CB  . ASP F  1 89  ? 94.966  67.426  49.930 1.00 14.68  ? 83  ASP F CB  1 
ATOM   6162  C  CG  . ASP F  1 89  ? 96.068  68.504  50.085 1.00 26.67  ? 83  ASP F CG  1 
ATOM   6163  O  OD1 . ASP F  1 89  ? 96.948  68.364  50.964 1.00 9.59   ? 83  ASP F OD1 1 
ATOM   6164  O  OD2 . ASP F  1 89  ? 96.043  69.516  49.336 1.00 18.07  ? 83  ASP F OD2 1 
ATOM   6165  N  N   . LEU F  1 90  ? 94.054  64.260  51.457 1.00 19.93  ? 84  LEU F N   1 
ATOM   6166  C  CA  . LEU F  1 90  ? 92.916  63.353  51.532 1.00 17.92  ? 84  LEU F CA  1 
ATOM   6167  C  C   . LEU F  1 90  ? 91.817  63.883  52.459 1.00 21.61  ? 84  LEU F C   1 
ATOM   6168  O  O   . LEU F  1 90  ? 90.882  63.173  52.803 1.00 29.25  ? 84  LEU F O   1 
ATOM   6169  C  CB  . LEU F  1 90  ? 93.373  61.953  51.973 1.00 16.68  ? 84  LEU F CB  1 
ATOM   6170  C  CG  . LEU F  1 90  ? 94.421  61.274  51.070 1.00 23.08  ? 84  LEU F CG  1 
ATOM   6171  C  CD1 . LEU F  1 90  ? 94.712  59.868  51.589 1.00 18.63  ? 84  LEU F CD1 1 
ATOM   6172  C  CD2 . LEU F  1 90  ? 93.924  61.194  49.628 1.00 19.74  ? 84  LEU F CD2 1 
ATOM   6173  N  N   . GLY F  1 91  ? 91.924  65.138  52.862 1.00 16.88  ? 85  GLY F N   1 
ATOM   6174  C  CA  . GLY F  1 91  ? 90.885  65.701  53.693 1.00 19.99  ? 85  GLY F CA  1 
ATOM   6175  C  C   . GLY F  1 91  ? 90.920  65.302  55.151 1.00 23.95  ? 85  GLY F C   1 
ATOM   6176  O  O   . GLY F  1 91  ? 91.984  65.187  55.750 1.00 24.63  ? 85  GLY F O   1 
ATOM   6177  N  N   . ASN F  1 92  ? 89.741  65.088  55.721 1.00 23.99  ? 86  ASN F N   1 
ATOM   6178  C  CA  . ASN F  1 92  ? 89.620  64.726  57.131 1.00 25.88  ? 86  ASN F CA  1 
ATOM   6179  C  C   . ASN F  1 92  ? 89.068  63.332  57.332 1.00 22.69  ? 86  ASN F C   1 
ATOM   6180  O  O   . ASN F  1 92  ? 88.381  62.769  56.466 1.00 22.92  ? 86  ASN F O   1 
ATOM   6181  C  CB  . ASN F  1 92  ? 88.663  65.689  57.871 1.00 14.74  ? 86  ASN F CB  1 
ATOM   6182  C  CG  . ASN F  1 92  ? 89.240  67.062  58.056 1.00 26.42  ? 86  ASN F CG  1 
ATOM   6183  O  OD1 . ASN F  1 92  ? 90.203  67.247  58.805 1.00 27.28  ? 86  ASN F OD1 1 
ATOM   6184  N  ND2 . ASN F  1 92  ? 88.659  68.047  57.373 1.00 24.66  ? 86  ASN F ND2 1 
ATOM   6185  N  N   . VAL F  1 93  ? 89.366  62.786  58.498 1.00 15.54  ? 87  VAL F N   1 
ATOM   6186  C  CA  . VAL F  1 93  ? 88.816  61.509  58.868 1.00 21.72  ? 87  VAL F CA  1 
ATOM   6187  C  C   . VAL F  1 93  ? 88.078  61.845  60.153 1.00 26.12  ? 87  VAL F C   1 
ATOM   6188  O  O   . VAL F  1 93  ? 88.422  62.819  60.849 1.00 19.63  ? 87  VAL F O   1 
ATOM   6189  C  CB  . VAL F  1 93  ? 89.891  60.449  59.081 1.00 17.45  ? 87  VAL F CB  1 
ATOM   6190  C  CG1 . VAL F  1 93  ? 90.414  59.987  57.707 1.00 17.87  ? 87  VAL F CG1 1 
ATOM   6191  C  CG2 . VAL F  1 93  ? 91.005  61.003  59.945 1.00 21.21  ? 87  VAL F CG2 1 
ATOM   6192  N  N   . THR F  1 94  ? 87.058  61.048  60.446 1.00 25.84  ? 88  THR F N   1 
ATOM   6193  C  CA  . THR F  1 94  ? 86.213  61.279  61.590 1.00 24.65  ? 88  THR F CA  1 
ATOM   6194  C  C   . THR F  1 94  ? 86.311  60.263  62.700 1.00 29.37  ? 88  THR F C   1 
ATOM   6195  O  O   . THR F  1 94  ? 86.009  59.078  62.504 1.00 22.69  ? 88  THR F O   1 
ATOM   6196  C  CB  . THR F  1 94  ? 84.748  61.328  61.159 1.00 26.27  ? 88  THR F CB  1 
ATOM   6197  O  OG1 . THR F  1 94  ? 84.595  62.260  60.084 1.00 19.79  ? 88  THR F OG1 1 
ATOM   6198  C  CG2 . THR F  1 94  ? 83.879  61.746  62.338 1.00 22.58  ? 88  THR F CG2 1 
ATOM   6199  N  N   . ALA F  1 95  ? 86.691  60.749  63.876 1.00 23.30  ? 89  ALA F N   1 
ATOM   6200  C  CA  . ALA F  1 95  ? 86.800  59.914  65.057 1.00 26.26  ? 89  ALA F CA  1 
ATOM   6201  C  C   . ALA F  1 95  ? 85.510  60.019  65.878 1.00 28.71  ? 89  ALA F C   1 
ATOM   6202  O  O   . ALA F  1 95  ? 85.125  61.123  66.290 1.00 25.33  ? 89  ALA F O   1 
ATOM   6203  C  CB  . ALA F  1 95  ? 87.991  60.366  65.911 1.00 21.93  ? 89  ALA F CB  1 
ATOM   6204  N  N   . ASP F  1 96  ? 84.870  58.873  66.124 1.00 27.87  ? 90  ASP F N   1 
ATOM   6205  C  CA  . ASP F  1 96  ? 83.632  58.793  66.916 1.00 30.98  ? 90  ASP F CA  1 
ATOM   6206  C  C   . ASP F  1 96  ? 83.880  58.902  68.425 1.00 30.40  ? 90  ASP F C   1 
ATOM   6207  O  O   . ASP F  1 96  ? 85.014  59.117  68.854 1.00 28.81  ? 90  ASP F O   1 
ATOM   6208  C  CB  . ASP F  1 96  ? 82.899  57.492  66.603 1.00 28.37  ? 90  ASP F CB  1 
ATOM   6209  C  CG  . ASP F  1 96  ? 82.514  57.396  65.146 1.00 41.28  ? 90  ASP F CG  1 
ATOM   6210  O  OD1 . ASP F  1 96  ? 82.031  58.411  64.595 1.00 44.89  ? 90  ASP F OD1 1 
ATOM   6211  O  OD2 . ASP F  1 96  ? 82.688  56.313  64.547 1.00 55.58  ? 90  ASP F OD2 1 
ATOM   6212  N  N   . LYS F  1 97  ? 82.825  58.767  69.229 1.00 34.71  ? 91  LYS F N   1 
ATOM   6213  C  CA  . LYS F  1 97  ? 82.967  58.891  70.686 1.00 39.27  ? 91  LYS F CA  1 
ATOM   6214  C  C   . LYS F  1 97  ? 83.783  57.768  71.333 1.00 33.34  ? 91  LYS F C   1 
ATOM   6215  O  O   . LYS F  1 97  ? 84.266  57.912  72.447 1.00 28.77  ? 91  LYS F O   1 
ATOM   6216  C  CB  . LYS F  1 97  ? 81.591  59.015  71.366 1.00 43.91  ? 91  LYS F CB  1 
ATOM   6217  C  CG  . LYS F  1 97  ? 80.544  58.005  70.916 1.00 59.18  ? 91  LYS F CG  1 
ATOM   6218  C  CD  . LYS F  1 97  ? 79.273  58.107  71.766 1.00 65.65  ? 91  LYS F CD  1 
ATOM   6219  C  CE  . LYS F  1 97  ? 78.081  57.384  71.127 1.00 65.88  ? 91  LYS F CE  1 
ATOM   6220  N  NZ  . LYS F  1 97  ? 78.326  55.934  70.897 1.00 68.87  ? 91  LYS F NZ  1 
ATOM   6221  N  N   . ASP F  1 98  ? 83.936  56.657  70.624 1.00 32.15  ? 92  ASP F N   1 
ATOM   6222  C  CA  . ASP F  1 98  ? 84.739  55.529  71.100 1.00 32.05  ? 92  ASP F CA  1 
ATOM   6223  C  C   . ASP F  1 98  ? 86.238  55.792  70.803 1.00 33.58  ? 92  ASP F C   1 
ATOM   6224  O  O   . ASP F  1 98  ? 87.078  54.907  70.967 1.00 26.82  ? 92  ASP F O   1 
ATOM   6225  C  CB  . ASP F  1 98  ? 84.297  54.248  70.385 1.00 31.16  ? 92  ASP F CB  1 
ATOM   6226  C  CG  . ASP F  1 98  ? 84.363  54.374  68.845 1.00 44.71  ? 92  ASP F CG  1 
ATOM   6227  O  OD1 . ASP F  1 98  ? 84.721  55.466  68.329 1.00 35.95  ? 92  ASP F OD1 1 
ATOM   6228  O  OD2 . ASP F  1 98  ? 84.048  53.383  68.145 1.00 43.86  ? 92  ASP F OD2 1 
ATOM   6229  N  N   . ALA F  1 99  ? 86.559  57.003  70.341 1.00 29.01  ? 93  ALA F N   1 
ATOM   6230  C  CA  . ALA F  1 99  ? 87.939  57.375  70.010 1.00 35.29  ? 93  ALA F CA  1 
ATOM   6231  C  C   . ALA F  1 99  ? 88.479  56.635  68.785 1.00 35.31  ? 93  ALA F C   1 
ATOM   6232  O  O   . ALA F  1 99  ? 89.692  56.554  68.572 1.00 41.35  ? 93  ALA F O   1 
ATOM   6233  C  CB  . ALA F  1 99  ? 88.870  57.136  71.210 1.00 26.85  ? 93  ALA F CB  1 
ATOM   6234  N  N   . VAL F  1 100 ? 87.586  56.094  67.975 1.00 27.06  ? 94  VAL F N   1 
ATOM   6235  C  CA  . VAL F  1 100 ? 88.030  55.395  66.790 1.00 31.33  ? 94  VAL F CA  1 
ATOM   6236  C  C   . VAL F  1 100 ? 87.508  56.049  65.532 1.00 32.53  ? 94  VAL F C   1 
ATOM   6237  O  O   . VAL F  1 100 ? 86.346  56.439  65.439 1.00 33.60  ? 94  VAL F O   1 
ATOM   6238  C  CB  . VAL F  1 100 ? 87.554  53.947  66.748 1.00 31.24  ? 94  VAL F CB  1 
ATOM   6239  C  CG1 . VAL F  1 100 ? 87.976  53.309  65.427 1.00 26.12  ? 94  VAL F CG1 1 
ATOM   6240  C  CG2 . VAL F  1 100 ? 88.126  53.192  67.895 1.00 29.45  ? 94  VAL F CG2 1 
ATOM   6241  N  N   . ALA F  1 101 ? 88.391  56.161  64.558 1.00 24.61  ? 95  ALA F N   1 
ATOM   6242  C  CA  . ALA F  1 101 ? 88.026  56.718  63.291 1.00 18.74  ? 95  ALA F CA  1 
ATOM   6243  C  C   . ALA F  1 101 ? 88.005  55.584  62.296 1.00 21.74  ? 95  ALA F C   1 
ATOM   6244  O  O   . ALA F  1 101 ? 89.041  54.994  61.997 1.00 20.62  ? 95  ALA F O   1 
ATOM   6245  C  CB  . ALA F  1 101 ? 89.038  57.765  62.859 1.00 21.28  ? 95  ALA F CB  1 
ATOM   6246  N  N   . ASP F  1 102 ? 86.819  55.241  61.820 1.00 20.38  ? 96  ASP F N   1 
ATOM   6247  C  CA  . ASP F  1 102 ? 86.707  54.214  60.800 1.00 27.51  ? 96  ASP F CA  1 
ATOM   6248  C  C   . ASP F  1 102 ? 87.051  54.983  59.525 1.00 27.61  ? 96  ASP F C   1 
ATOM   6249  O  O   . ASP F  1 102 ? 86.565  56.089  59.325 1.00 32.17  ? 96  ASP F O   1 
ATOM   6250  C  CB  . ASP F  1 102 ? 85.272  53.688  60.758 1.00 28.19  ? 96  ASP F CB  1 
ATOM   6251  C  CG  . ASP F  1 102 ? 84.889  52.994  62.048 1.00 47.77  ? 96  ASP F CG  1 
ATOM   6252  O  OD1 . ASP F  1 102 ? 83.819  53.323  62.633 1.00 42.92  ? 96  ASP F OD1 1 
ATOM   6253  O  OD2 . ASP F  1 102 ? 85.680  52.116  62.473 1.00 46.78  ? 96  ASP F OD2 1 
ATOM   6254  N  N   . VAL F  1 103 ? 87.908  54.434  58.679 1.00 26.79  ? 97  VAL F N   1 
ATOM   6255  C  CA  . VAL F  1 103 ? 88.273  55.148  57.471 1.00 17.54  ? 97  VAL F CA  1 
ATOM   6256  C  C   . VAL F  1 103 ? 87.876  54.427  56.207 1.00 18.77  ? 97  VAL F C   1 
ATOM   6257  O  O   . VAL F  1 103 ? 88.168  53.251  56.045 1.00 25.47  ? 97  VAL F O   1 
ATOM   6258  C  CB  . VAL F  1 103 ? 89.791  55.400  57.397 1.00 15.88  ? 97  VAL F CB  1 
ATOM   6259  C  CG1 . VAL F  1 103 ? 90.131  56.158  56.099 1.00 10.51  ? 97  VAL F CG1 1 
ATOM   6260  C  CG2 . VAL F  1 103 ? 90.275  56.182  58.640 1.00 10.37  ? 97  VAL F CG2 1 
ATOM   6261  N  N   . SER F  1 104 ? 87.220  55.154  55.314 1.00 12.98  ? 98  SER F N   1 
ATOM   6262  C  CA  . SER F  1 104 ? 86.803  54.633  54.009 1.00 27.28  ? 98  SER F CA  1 
ATOM   6263  C  C   . SER F  1 104 ? 86.701  55.812  53.036 1.00 26.70  ? 98  SER F C   1 
ATOM   6264  O  O   . SER F  1 104 ? 85.751  56.581  53.052 1.00 34.49  ? 98  SER F O   1 
ATOM   6265  C  CB  . SER F  1 104 ? 85.460  53.910  54.094 1.00 26.17  ? 98  SER F CB  1 
ATOM   6266  O  OG  . SER F  1 104 ? 85.148  53.358  52.828 1.00 32.40  ? 98  SER F OG  1 
ATOM   6267  N  N   . ILE F  1 105 ? 87.711  55.933  52.194 1.00 32.76  ? 99  ILE F N   1 
ATOM   6268  C  CA  . ILE F  1 105 ? 87.837  57.010  51.235 1.00 23.75  ? 99  ILE F CA  1 
ATOM   6269  C  C   . ILE F  1 105 ? 88.177  56.444  49.872 1.00 29.68  ? 99  ILE F C   1 
ATOM   6270  O  O   . ILE F  1 105 ? 88.725  55.350  49.757 1.00 32.91  ? 99  ILE F O   1 
ATOM   6271  C  CB  . ILE F  1 105 ? 88.995  57.924  51.663 1.00 27.87  ? 99  ILE F CB  1 
ATOM   6272  C  CG1 . ILE F  1 105 ? 88.574  58.740  52.881 1.00 29.61  ? 99  ILE F CG1 1 
ATOM   6273  C  CG2 . ILE F  1 105 ? 89.474  58.783  50.508 1.00 26.74  ? 99  ILE F CG2 1 
ATOM   6274  C  CD1 . ILE F  1 105 ? 89.752  59.408  53.563 1.00 25.72  ? 99  ILE F CD1 1 
ATOM   6275  N  N   . GLU F  1 106 ? 87.849  57.197  48.836 1.00 28.48  ? 100 GLU F N   1 
ATOM   6276  C  CA  . GLU F  1 106 ? 88.181  56.790  47.491 1.00 32.45  ? 100 GLU F CA  1 
ATOM   6277  C  C   . GLU F  1 106 ? 88.738  58.059  46.865 1.00 32.51  ? 100 GLU F C   1 
ATOM   6278  O  O   . GLU F  1 106 ? 88.117  59.114  46.937 1.00 32.58  ? 100 GLU F O   1 
ATOM   6279  C  CB  . GLU F  1 106 ? 86.946  56.310  46.759 1.00 27.48  ? 100 GLU F CB  1 
ATOM   6280  C  CG  . GLU F  1 106 ? 87.269  55.509  45.534 1.00 52.74  ? 100 GLU F CG  1 
ATOM   6281  C  CD  . GLU F  1 106 ? 86.029  54.989  44.848 1.00 58.91  ? 100 GLU F CD  1 
ATOM   6282  O  OE1 . GLU F  1 106 ? 85.326  54.134  45.437 1.00 57.96  ? 100 GLU F OE1 1 
ATOM   6283  O  OE2 . GLU F  1 106 ? 85.761  55.447  43.718 1.00 59.04  ? 100 GLU F OE2 1 
ATOM   6284  N  N   . ASP F  1 107 ? 89.919  57.974  46.274 1.00 25.69  ? 101 ASP F N   1 
ATOM   6285  C  CA  . ASP F  1 107 ? 90.520  59.160  45.699 1.00 22.19  ? 101 ASP F CA  1 
ATOM   6286  C  C   . ASP F  1 107 ? 91.151  58.888  44.344 1.00 25.78  ? 101 ASP F C   1 
ATOM   6287  O  O   . ASP F  1 107 ? 91.730  57.827  44.139 1.00 26.95  ? 101 ASP F O   1 
ATOM   6288  C  CB  . ASP F  1 107 ? 91.570  59.685  46.663 1.00 13.14  ? 101 ASP F CB  1 
ATOM   6289  C  CG  . ASP F  1 107 ? 92.071  61.048  46.277 1.00 23.98  ? 101 ASP F CG  1 
ATOM   6290  O  OD1 . ASP F  1 107 ? 93.177  61.161  45.690 1.00 24.24  ? 101 ASP F OD1 1 
ATOM   6291  O  OD2 . ASP F  1 107 ? 91.335  62.008  46.567 1.00 25.33  ? 101 ASP F OD2 1 
ATOM   6292  N  N   . SER F  1 108 ? 91.066  59.847  43.424 1.00 25.64  ? 102 SER F N   1 
ATOM   6293  C  CA  . SER F  1 108 ? 91.637  59.650  42.097 1.00 25.00  ? 102 SER F CA  1 
ATOM   6294  C  C   . SER F  1 108 ? 92.856  60.477  41.784 1.00 23.44  ? 102 SER F C   1 
ATOM   6295  O  O   . SER F  1 108 ? 93.309  60.479  40.653 1.00 21.36  ? 102 SER F O   1 
ATOM   6296  C  CB  . SER F  1 108 ? 90.587  59.898  41.014 1.00 28.56  ? 102 SER F CB  1 
ATOM   6297  O  OG  . SER F  1 108 ? 89.704  58.792  40.917 1.00 44.74  ? 102 SER F OG  1 
ATOM   6298  N  N   . VAL F  1 109 ? 93.384  61.200  42.761 1.00 23.34  ? 103 VAL F N   1 
ATOM   6299  C  CA  . VAL F  1 109 ? 94.569  61.986  42.500 1.00 20.23  ? 103 VAL F CA  1 
ATOM   6300  C  C   . VAL F  1 109 ? 95.796  61.227  43.016 1.00 22.87  ? 103 VAL F C   1 
ATOM   6301  O  O   . VAL F  1 109 ? 96.883  61.330  42.451 1.00 29.15  ? 103 VAL F O   1 
ATOM   6302  C  CB  . VAL F  1 109 ? 94.479  63.375  43.155 1.00 27.43  ? 103 VAL F CB  1 
ATOM   6303  C  CG1 . VAL F  1 109 ? 95.782  64.144  42.933 1.00 22.13  ? 103 VAL F CG1 1 
ATOM   6304  C  CG2 . VAL F  1 109 ? 93.310  64.147  42.563 1.00 20.29  ? 103 VAL F CG2 1 
ATOM   6305  N  N   . ILE F  1 110 ? 95.641  60.480  44.099 1.00 24.80  ? 104 ILE F N   1 
ATOM   6306  C  CA  . ILE F  1 110 ? 96.778  59.704  44.592 1.00 25.59  ? 104 ILE F CA  1 
ATOM   6307  C  C   . ILE F  1 110 ? 96.789  58.462  43.703 1.00 26.36  ? 104 ILE F C   1 
ATOM   6308  O  O   . ILE F  1 110 ? 95.786  58.150  43.057 1.00 24.22  ? 104 ILE F O   1 
ATOM   6309  C  CB  . ILE F  1 110 ? 96.619  59.247  46.077 1.00 19.51  ? 104 ILE F CB  1 
ATOM   6310  C  CG1 . ILE F  1 110 ? 95.345  58.418  46.252 1.00 12.58  ? 104 ILE F CG1 1 
ATOM   6311  C  CG2 . ILE F  1 110 ? 96.638  60.447  47.015 1.00 24.48  ? 104 ILE F CG2 1 
ATOM   6312  C  CD1 . ILE F  1 110 ? 95.238  57.740  47.635 1.00 11.66  ? 104 ILE F CD1 1 
ATOM   6313  N  N   . SER F  1 111 ? 97.912  57.756  43.661 1.00 24.86  ? 105 SER F N   1 
ATOM   6314  C  CA  . SER F  1 111 ? 98.009  56.554  42.844 1.00 21.77  ? 105 SER F CA  1 
ATOM   6315  C  C   . SER F  1 111 ? 99.055  55.625  43.439 1.00 23.93  ? 105 SER F C   1 
ATOM   6316  O  O   . SER F  1 111 ? 99.805  56.027  44.334 1.00 22.43  ? 105 SER F O   1 
ATOM   6317  C  CB  . SER F  1 111 ? 98.405  56.931  41.409 1.00 17.16  ? 105 SER F CB  1 
ATOM   6318  O  OG  . SER F  1 111 ? 98.286  55.827  40.535 1.00 19.83  ? 105 SER F OG  1 
ATOM   6319  N  N   . LEU F  1 112 ? 99.111  54.392  42.938 1.00 20.55  ? 106 LEU F N   1 
ATOM   6320  C  CA  . LEU F  1 112 ? 100.090 53.430  43.420 1.00 26.88  ? 106 LEU F CA  1 
ATOM   6321  C  C   . LEU F  1 112 ? 101.159 53.175  42.355 1.00 26.66  ? 106 LEU F C   1 
ATOM   6322  O  O   . LEU F  1 112 ? 101.866 52.184  42.401 1.00 33.35  ? 106 LEU F O   1 
ATOM   6323  C  CB  . LEU F  1 112 ? 99.408  52.123  43.833 1.00 22.75  ? 106 LEU F CB  1 
ATOM   6324  C  CG  . LEU F  1 112 ? 98.368  52.217  44.960 1.00 25.11  ? 106 LEU F CG  1 
ATOM   6325  C  CD1 . LEU F  1 112 ? 97.942  50.811  45.355 1.00 23.54  ? 106 LEU F CD1 1 
ATOM   6326  C  CD2 . LEU F  1 112 ? 98.938  52.956  46.182 1.00 14.15  ? 106 LEU F CD2 1 
ATOM   6327  N  N   . SER F  1 113 ? 101.263 54.094  41.404 1.00 29.56  ? 107 SER F N   1 
ATOM   6328  C  CA  . SER F  1 113 ? 102.257 54.045  40.330 1.00 30.76  ? 107 SER F CA  1 
ATOM   6329  C  C   . SER F  1 113 ? 102.281 55.414  39.659 1.00 29.81  ? 107 SER F C   1 
ATOM   6330  O  O   . SER F  1 113 ? 101.361 56.207  39.828 1.00 37.85  ? 107 SER F O   1 
ATOM   6331  C  CB  . SER F  1 113 ? 101.915 52.961  39.290 1.00 29.60  ? 107 SER F CB  1 
ATOM   6332  O  OG  . SER F  1 113 ? 100.647 53.174  38.702 1.00 27.93  ? 107 SER F OG  1 
ATOM   6333  N  N   . GLY F  1 114 ? 103.332 55.697  38.904 1.00 27.24  ? 108 GLY F N   1 
ATOM   6334  C  CA  . GLY F  1 114 ? 103.413 56.978  38.230 1.00 26.59  ? 108 GLY F CA  1 
ATOM   6335  C  C   . GLY F  1 114 ? 103.820 58.162  39.086 1.00 26.53  ? 108 GLY F C   1 
ATOM   6336  O  O   . GLY F  1 114 ? 104.236 58.014  40.233 1.00 28.56  ? 108 GLY F O   1 
ATOM   6337  N  N   . ASP F  1 115 ? 103.688 59.352  38.516 1.00 33.69  ? 109 ASP F N   1 
ATOM   6338  C  CA  . ASP F  1 115 ? 104.055 60.591  39.195 1.00 37.94  ? 109 ASP F CA  1 
ATOM   6339  C  C   . ASP F  1 115 ? 103.382 60.796  40.532 1.00 34.30  ? 109 ASP F C   1 
ATOM   6340  O  O   . ASP F  1 115 ? 103.940 61.433  41.409 1.00 29.95  ? 109 ASP F O   1 
ATOM   6341  C  CB  . ASP F  1 115 ? 103.734 61.792  38.313 1.00 39.24  ? 109 ASP F CB  1 
ATOM   6342  C  CG  . ASP F  1 115 ? 104.776 62.018  37.261 1.00 44.61  ? 109 ASP F CG  1 
ATOM   6343  O  OD1 . ASP F  1 115 ? 105.902 61.528  37.473 1.00 43.64  ? 109 ASP F OD1 1 
ATOM   6344  O  OD2 . ASP F  1 115 ? 104.479 62.689  36.245 1.00 49.21  ? 109 ASP F OD2 1 
ATOM   6345  N  N   . HIS F  1 116 ? 102.177 60.264  40.670 1.00 29.92  ? 110 HIS F N   1 
ATOM   6346  C  CA  . HIS F  1 116 ? 101.422 60.411  41.891 1.00 32.06  ? 110 HIS F CA  1 
ATOM   6347  C  C   . HIS F  1 116 ? 101.537 59.250  42.879 1.00 29.91  ? 110 HIS F C   1 
ATOM   6348  O  O   . HIS F  1 116 ? 100.784 59.201  43.848 1.00 35.50  ? 110 HIS F O   1 
ATOM   6349  C  CB  . HIS F  1 116 ? 99.950  60.635  41.540 1.00 32.24  ? 110 HIS F CB  1 
ATOM   6350  C  CG  . HIS F  1 116 ? 99.709  61.855  40.708 1.00 41.73  ? 110 HIS F CG  1 
ATOM   6351  N  ND1 . HIS F  1 116 ? 98.445  62.337  40.442 1.00 41.43  ? 110 HIS F ND1 1 
ATOM   6352  C  CD2 . HIS F  1 116 ? 100.569 62.689  40.079 1.00 41.19  ? 110 HIS F CD2 1 
ATOM   6353  C  CE1 . HIS F  1 116 ? 98.538  63.413  39.684 1.00 35.94  ? 110 HIS F CE1 1 
ATOM   6354  N  NE2 . HIS F  1 116 ? 99.816  63.648  39.450 1.00 33.94  ? 110 HIS F NE2 1 
ATOM   6355  N  N   . CYS F  1 117 ? 102.469 58.327  42.660 1.00 27.84  ? 111 CYS F N   1 
ATOM   6356  C  CA  . CYS F  1 117 ? 102.603 57.183  43.561 1.00 26.36  ? 111 CYS F CA  1 
ATOM   6357  C  C   . CYS F  1 117 ? 102.845 57.670  44.994 1.00 26.78  ? 111 CYS F C   1 
ATOM   6358  O  O   . CYS F  1 117 ? 103.634 58.582  45.223 1.00 23.37  ? 111 CYS F O   1 
ATOM   6359  C  CB  . CYS F  1 117 ? 103.763 56.295  43.107 1.00 32.81  ? 111 CYS F CB  1 
ATOM   6360  S  SG  . CYS F  1 117 ? 103.838 54.640  43.840 1.00 36.84  ? 111 CYS F SG  1 
ATOM   6361  N  N   . ILE F  1 118 ? 102.159 57.073  45.960 1.00 22.69  ? 112 ILE F N   1 
ATOM   6362  C  CA  . ILE F  1 118 ? 102.334 57.466  47.353 1.00 23.12  ? 112 ILE F CA  1 
ATOM   6363  C  C   . ILE F  1 118 ? 103.119 56.406  48.129 1.00 24.63  ? 112 ILE F C   1 
ATOM   6364  O  O   . ILE F  1 118 ? 103.387 56.573  49.309 1.00 24.16  ? 112 ILE F O   1 
ATOM   6365  C  CB  . ILE F  1 118 ? 100.987 57.680  48.018 1.00 17.50  ? 112 ILE F CB  1 
ATOM   6366  C  CG1 . ILE F  1 118 ? 100.196 56.376  47.971 1.00 9.13   ? 112 ILE F CG1 1 
ATOM   6367  C  CG2 . ILE F  1 118 ? 100.234 58.821  47.289 1.00 15.38  ? 112 ILE F CG2 1 
ATOM   6368  C  CD1 . ILE F  1 118 ? 98.822  56.446  48.623 1.00 19.84  ? 112 ILE F CD1 1 
ATOM   6369  N  N   . ILE F  1 119 ? 103.465 55.312  47.454 1.00 21.94  ? 113 ILE F N   1 
ATOM   6370  C  CA  . ILE F  1 119 ? 104.261 54.234  48.039 1.00 21.40  ? 113 ILE F CA  1 
ATOM   6371  C  C   . ILE F  1 119 ? 105.664 54.758  48.345 1.00 20.94  ? 113 ILE F C   1 
ATOM   6372  O  O   . ILE F  1 119 ? 106.330 55.364  47.500 1.00 17.31  ? 113 ILE F O   1 
ATOM   6373  C  CB  . ILE F  1 119 ? 104.365 53.051  47.059 1.00 22.54  ? 113 ILE F CB  1 
ATOM   6374  C  CG1 . ILE F  1 119 ? 103.010 52.344  46.977 1.00 22.73  ? 113 ILE F CG1 1 
ATOM   6375  C  CG2 . ILE F  1 119 ? 105.440 52.089  47.505 1.00 21.65  ? 113 ILE F CG2 1 
ATOM   6376  C  CD1 . ILE F  1 119 ? 102.921 51.296  45.911 1.00 25.39  ? 113 ILE F CD1 1 
ATOM   6377  N  N   . GLY F  1 120 ? 106.116 54.540  49.564 1.00 20.39  ? 114 GLY F N   1 
ATOM   6378  C  CA  . GLY F  1 120 ? 107.435 55.028  49.940 1.00 23.17  ? 114 GLY F CA  1 
ATOM   6379  C  C   . GLY F  1 120 ? 107.318 56.388  50.603 1.00 21.76  ? 114 GLY F C   1 
ATOM   6380  O  O   . GLY F  1 120 ? 108.306 56.979  51.022 1.00 21.32  ? 114 GLY F O   1 
ATOM   6381  N  N   . ARG F  1 121 ? 106.092 56.889  50.692 1.00 20.68  ? 115 ARG F N   1 
ATOM   6382  C  CA  . ARG F  1 121 ? 105.833 58.178  51.318 1.00 22.92  ? 115 ARG F CA  1 
ATOM   6383  C  C   . ARG F  1 121 ? 105.150 57.946  52.663 1.00 21.62  ? 115 ARG F C   1 
ATOM   6384  O  O   . ARG F  1 121 ? 104.853 56.813  53.017 1.00 30.60  ? 115 ARG F O   1 
ATOM   6385  C  CB  . ARG F  1 121 ? 104.984 59.039  50.376 1.00 23.30  ? 115 ARG F CB  1 
ATOM   6386  C  CG  . ARG F  1 121 ? 105.654 59.267  48.988 1.00 21.99  ? 115 ARG F CG  1 
ATOM   6387  C  CD  . ARG F  1 121 ? 105.912 60.755  48.773 1.00 45.74  ? 115 ARG F CD  1 
ATOM   6388  N  NE  . ARG F  1 121 ? 106.859 61.100  47.702 1.00 37.40  ? 115 ARG F NE  1 
ATOM   6389  C  CZ  . ARG F  1 121 ? 106.726 60.678  46.461 1.00 35.88  ? 115 ARG F CZ  1 
ATOM   6390  N  NH1 . ARG F  1 121 ? 105.709 59.889  46.163 1.00 46.12  ? 115 ARG F NH1 1 
ATOM   6391  N  NH2 . ARG F  1 121 ? 107.558 61.082  45.515 1.00 23.10  ? 115 ARG F NH2 1 
ATOM   6392  N  N   . THR F  1 122 ? 104.904 59.004  53.420 1.00 22.65  ? 116 THR F N   1 
ATOM   6393  C  CA  . THR F  1 122 ? 104.299 58.858  54.733 1.00 20.48  ? 116 THR F CA  1 
ATOM   6394  C  C   . THR F  1 122 ? 102.849 59.307  54.867 1.00 22.12  ? 116 THR F C   1 
ATOM   6395  O  O   . THR F  1 122 ? 102.463 60.384  54.425 1.00 26.07  ? 116 THR F O   1 
ATOM   6396  C  CB  . THR F  1 122 ? 105.134 59.615  55.771 1.00 23.93  ? 116 THR F CB  1 
ATOM   6397  O  OG1 . THR F  1 122 ? 106.455 59.070  55.775 1.00 17.91  ? 116 THR F OG1 1 
ATOM   6398  C  CG2 . THR F  1 122 ? 104.514 59.498  57.182 1.00 17.71  ? 116 THR F CG2 1 
ATOM   6399  N  N   . LEU F  1 123 ? 102.043 58.462  55.486 1.00 21.90  ? 117 LEU F N   1 
ATOM   6400  C  CA  . LEU F  1 123 ? 100.638 58.777  55.728 1.00 22.58  ? 117 LEU F CA  1 
ATOM   6401  C  C   . LEU F  1 123 ? 100.620 59.382  57.141 1.00 18.41  ? 117 LEU F C   1 
ATOM   6402  O  O   . LEU F  1 123 ? 101.184 58.815  58.069 1.00 23.60  ? 117 LEU F O   1 
ATOM   6403  C  CB  . LEU F  1 123 ? 99.794  57.496  55.672 1.00 13.01  ? 117 LEU F CB  1 
ATOM   6404  C  CG  . LEU F  1 123 ? 98.309  57.690  55.988 1.00 21.57  ? 117 LEU F CG  1 
ATOM   6405  C  CD1 . LEU F  1 123 ? 97.665  58.469  54.870 1.00 18.94  ? 117 LEU F CD1 1 
ATOM   6406  C  CD2 . LEU F  1 123 ? 97.609  56.357  56.135 1.00 16.26  ? 117 LEU F CD2 1 
ATOM   6407  N  N   . VAL F  1 124 ? 99.979  60.525  57.311 1.00 20.29  ? 118 VAL F N   1 
ATOM   6408  C  CA  . VAL F  1 124 ? 99.955  61.185  58.612 1.00 17.87  ? 118 VAL F CA  1 
ATOM   6409  C  C   . VAL F  1 124 ? 98.548  61.582  59.053 1.00 25.56  ? 118 VAL F C   1 
ATOM   6410  O  O   . VAL F  1 124 ? 97.753  62.132  58.263 1.00 22.14  ? 118 VAL F O   1 
ATOM   6411  C  CB  . VAL F  1 124 ? 100.822 62.487  58.564 1.00 22.00  ? 118 VAL F CB  1 
ATOM   6412  C  CG1 . VAL F  1 124 ? 100.860 63.180  59.928 1.00 11.25  ? 118 VAL F CG1 1 
ATOM   6413  C  CG2 . VAL F  1 124 ? 102.221 62.157  58.064 1.00 10.77  ? 118 VAL F CG2 1 
ATOM   6414  N  N   . VAL F  1 125 ? 98.224  61.301  60.309 1.00 21.74  ? 119 VAL F N   1 
ATOM   6415  C  CA  . VAL F  1 125 ? 96.932  61.715  60.826 1.00 14.65  ? 119 VAL F CA  1 
ATOM   6416  C  C   . VAL F  1 125 ? 97.235  62.836  61.823 1.00 21.99  ? 119 VAL F C   1 
ATOM   6417  O  O   . VAL F  1 125 ? 98.070  62.669  62.734 1.00 16.94  ? 119 VAL F O   1 
ATOM   6418  C  CB  . VAL F  1 125 ? 96.153  60.546  61.492 1.00 21.74  ? 119 VAL F CB  1 
ATOM   6419  C  CG1 . VAL F  1 125 ? 96.948  59.948  62.654 1.00 22.23  ? 119 VAL F CG1 1 
ATOM   6420  C  CG2 . VAL F  1 125 ? 94.801  61.057  61.969 1.00 21.24  ? 119 VAL F CG2 1 
ATOM   6421  N  N   . HIS F  1 126 ? 96.558  63.975  61.630 1.00 20.22  ? 120 HIS F N   1 
ATOM   6422  C  CA  . HIS F  1 126 ? 96.757  65.180  62.436 1.00 21.71  ? 120 HIS F CA  1 
ATOM   6423  C  C   . HIS F  1 126 ? 95.868  65.404  63.652 1.00 22.12  ? 120 HIS F C   1 
ATOM   6424  O  O   . HIS F  1 126 ? 94.788  64.837  63.761 1.00 26.26  ? 120 HIS F O   1 
ATOM   6425  C  CB  . HIS F  1 126 ? 96.688  66.395  61.517 1.00 20.61  ? 120 HIS F CB  1 
ATOM   6426  C  CG  . HIS F  1 126 ? 97.835  66.475  60.562 1.00 18.83  ? 120 HIS F CG  1 
ATOM   6427  N  ND1 . HIS F  1 126 ? 98.930  67.280  60.782 1.00 17.43  ? 120 HIS F ND1 1 
ATOM   6428  C  CD2 . HIS F  1 126 ? 98.070  65.830  59.394 1.00 11.75  ? 120 HIS F CD2 1 
ATOM   6429  C  CE1 . HIS F  1 126 ? 99.789  67.131  59.786 1.00 18.96  ? 120 HIS F CE1 1 
ATOM   6430  N  NE2 . HIS F  1 126 ? 99.290  66.259  58.930 1.00 16.47  ? 120 HIS F NE2 1 
ATOM   6431  N  N   . GLU F  1 127 ? 96.328  66.262  64.557 1.00 24.73  ? 121 GLU F N   1 
ATOM   6432  C  CA  . GLU F  1 127 ? 95.589  66.547  65.782 1.00 30.46  ? 121 GLU F CA  1 
ATOM   6433  C  C   . GLU F  1 127 ? 94.276  67.305  65.602 1.00 25.63  ? 121 GLU F C   1 
ATOM   6434  O  O   . GLU F  1 127 ? 93.294  66.999  66.270 1.00 27.32  ? 121 GLU F O   1 
ATOM   6435  C  CB  . GLU F  1 127 ? 96.476  67.306  66.779 1.00 35.62  ? 121 GLU F CB  1 
ATOM   6436  C  CG  . GLU F  1 127 ? 96.505  68.815  66.599 1.00 53.21  ? 121 GLU F CG  1 
ATOM   6437  C  CD  . GLU F  1 127 ? 97.338  69.508  67.665 1.00 55.66  ? 121 GLU F CD  1 
ATOM   6438  O  OE1 . GLU F  1 127 ? 97.386  68.966  68.796 1.00 56.37  ? 121 GLU F OE1 1 
ATOM   6439  O  OE2 . GLU F  1 127 ? 97.926  70.584  67.374 1.00 41.40  ? 121 GLU F OE2 1 
ATOM   6440  N  N   . LYS F  1 128 ? 94.258  68.282  64.705 1.00 24.77  ? 122 LYS F N   1 
ATOM   6441  C  CA  . LYS F  1 128 ? 93.065  69.094  64.467 1.00 29.10  ? 122 LYS F CA  1 
ATOM   6442  C  C   . LYS F  1 128 ? 92.457  68.851  63.091 1.00 30.37  ? 122 LYS F C   1 
ATOM   6443  O  O   . LYS F  1 128 ? 93.010  68.118  62.268 1.00 27.74  ? 122 LYS F O   1 
ATOM   6444  C  CB  . LYS F  1 128 ? 93.417  70.583  64.595 1.00 33.53  ? 122 LYS F CB  1 
ATOM   6445  C  CG  . LYS F  1 128 ? 94.007  70.970  65.948 1.00 39.90  ? 122 LYS F CG  1 
ATOM   6446  C  CD  . LYS F  1 128 ? 94.239  72.475  66.083 1.00 42.09  ? 122 LYS F CD  1 
ATOM   6447  C  CE  . LYS F  1 128 ? 95.307  72.981  65.126 1.00 47.50  ? 122 LYS F CE  1 
ATOM   6448  N  NZ  . LYS F  1 128 ? 95.541  74.451  65.249 1.00 47.38  ? 122 LYS F NZ  1 
ATOM   6449  N  N   . ALA F  1 129 ? 91.316  69.483  62.846 1.00 21.18  ? 123 ALA F N   1 
ATOM   6450  C  CA  . ALA F  1 129 ? 90.636  69.361  61.569 1.00 18.73  ? 123 ALA F CA  1 
ATOM   6451  C  C   . ALA F  1 129 ? 91.382  70.126  60.478 1.00 17.56  ? 123 ALA F C   1 
ATOM   6452  O  O   . ALA F  1 129 ? 91.950  71.172  60.741 1.00 14.33  ? 123 ALA F O   1 
ATOM   6453  C  CB  . ALA F  1 129 ? 89.231  69.912  61.688 1.00 10.71  ? 123 ALA F CB  1 
ATOM   6454  N  N   . ASP F  1 130 ? 91.360  69.593  59.258 1.00 16.88  ? 124 ASP F N   1 
ATOM   6455  C  CA  . ASP F  1 130 ? 91.976  70.209  58.078 1.00 19.43  ? 124 ASP F CA  1 
ATOM   6456  C  C   . ASP F  1 130 ? 90.957  71.274  57.647 1.00 24.43  ? 124 ASP F C   1 
ATOM   6457  O  O   . ASP F  1 130 ? 89.792  70.938  57.469 1.00 22.78  ? 124 ASP F O   1 
ATOM   6458  C  CB  . ASP F  1 130 ? 92.098  69.137  56.984 1.00 14.42  ? 124 ASP F CB  1 
ATOM   6459  C  CG  . ASP F  1 130 ? 92.784  69.630  55.705 1.00 19.39  ? 124 ASP F CG  1 
ATOM   6460  O  OD1 . ASP F  1 130 ? 93.330  68.770  54.989 1.00 25.09  ? 124 ASP F OD1 1 
ATOM   6461  O  OD2 . ASP F  1 130 ? 92.781  70.838  55.394 1.00 18.36  ? 124 ASP F OD2 1 
ATOM   6462  N  N   . ASP F  1 131 ? 91.357  72.539  57.482 1.00 25.78  ? 125 ASP F N   1 
ATOM   6463  C  CA  . ASP F  1 131 ? 90.380  73.554  57.056 1.00 22.99  ? 125 ASP F CA  1 
ATOM   6464  C  C   . ASP F  1 131 ? 90.223  73.554  55.533 1.00 24.44  ? 125 ASP F C   1 
ATOM   6465  O  O   . ASP F  1 131 ? 89.620  74.463  54.939 1.00 20.62  ? 125 ASP F O   1 
ATOM   6466  C  CB  . ASP F  1 131 ? 90.746  74.960  57.587 1.00 12.01  ? 125 ASP F CB  1 
ATOM   6467  C  CG  . ASP F  1 131 ? 91.981  75.568  56.913 1.00 23.90  ? 125 ASP F CG  1 
ATOM   6468  O  OD1 . ASP F  1 131 ? 92.478  76.617  57.409 1.00 17.15  ? 125 ASP F OD1 1 
ATOM   6469  O  OD2 . ASP F  1 131 ? 92.451  75.015  55.892 1.00 15.95  ? 125 ASP F OD2 1 
ATOM   6470  N  N   . LEU F  1 132 ? 90.802  72.530  54.910 1.00 14.44  ? 126 LEU F N   1 
ATOM   6471  C  CA  . LEU F  1 132 ? 90.703  72.340  53.473 1.00 20.05  ? 126 LEU F CA  1 
ATOM   6472  C  C   . LEU F  1 132 ? 91.132  73.548  52.664 1.00 19.90  ? 126 LEU F C   1 
ATOM   6473  O  O   . LEU F  1 132 ? 90.644  73.761  51.561 1.00 22.72  ? 126 LEU F O   1 
ATOM   6474  C  CB  . LEU F  1 132 ? 89.261  71.934  53.113 1.00 20.89  ? 126 LEU F CB  1 
ATOM   6475  C  CG  . LEU F  1 132 ? 88.734  70.788  54.022 1.00 27.76  ? 126 LEU F CG  1 
ATOM   6476  C  CD1 . LEU F  1 132 ? 87.335  70.349  53.611 1.00 14.78  ? 126 LEU F CD1 1 
ATOM   6477  C  CD2 . LEU F  1 132 ? 89.676  69.592  53.963 1.00 14.20  ? 126 LEU F CD2 1 
ATOM   6478  N  N   . GLY F  1 133 ? 92.052  74.326  53.234 1.00 19.27  ? 127 GLY F N   1 
ATOM   6479  C  CA  . GLY F  1 133 ? 92.603  75.500  52.581 1.00 15.73  ? 127 GLY F CA  1 
ATOM   6480  C  C   . GLY F  1 133 ? 91.694  76.703  52.531 1.00 21.13  ? 127 GLY F C   1 
ATOM   6481  O  O   . GLY F  1 133 ? 91.914  77.628  51.755 1.00 19.01  ? 127 GLY F O   1 
ATOM   6482  N  N   . LYS F  1 134 ? 90.677  76.714  53.374 1.00 24.79  ? 128 LYS F N   1 
ATOM   6483  C  CA  . LYS F  1 134 ? 89.736  77.828  53.382 1.00 25.72  ? 128 LYS F CA  1 
ATOM   6484  C  C   . LYS F  1 134 ? 89.896  78.728  54.612 1.00 27.51  ? 128 LYS F C   1 
ATOM   6485  O  O   . LYS F  1 134 ? 89.001  79.506  54.913 1.00 30.75  ? 128 LYS F O   1 
ATOM   6486  C  CB  . LYS F  1 134 ? 88.301  77.280  53.349 1.00 22.12  ? 128 LYS F CB  1 
ATOM   6487  C  CG  . LYS F  1 134 ? 87.942  76.444  52.118 1.00 26.90  ? 128 LYS F CG  1 
ATOM   6488  C  CD  . LYS F  1 134 ? 86.486  75.987  52.195 1.00 41.57  ? 128 LYS F CD  1 
ATOM   6489  C  CE  . LYS F  1 134 ? 85.997  75.390  50.887 1.00 54.96  ? 128 LYS F CE  1 
ATOM   6490  N  NZ  . LYS F  1 134 ? 84.599  74.860  50.999 1.00 65.73  ? 128 LYS F NZ  1 
ATOM   6491  N  N   . GLY F  1 135 ? 91.022  78.617  55.316 1.00 28.16  ? 129 GLY F N   1 
ATOM   6492  C  CA  . GLY F  1 135 ? 91.238  79.391  56.527 1.00 22.88  ? 129 GLY F CA  1 
ATOM   6493  C  C   . GLY F  1 135 ? 91.689  80.843  56.419 1.00 30.85  ? 129 GLY F C   1 
ATOM   6494  O  O   . GLY F  1 135 ? 91.812  81.544  57.442 1.00 27.57  ? 129 GLY F O   1 
ATOM   6495  N  N   . GLY F  1 136 ? 91.956  81.307  55.203 1.00 14.28  ? 130 GLY F N   1 
ATOM   6496  C  CA  . GLY F  1 136 ? 92.347  82.697  55.041 1.00 28.09  ? 130 GLY F CA  1 
ATOM   6497  C  C   . GLY F  1 136 ? 93.765  83.120  55.389 1.00 31.37  ? 130 GLY F C   1 
ATOM   6498  O  O   . GLY F  1 136 ? 94.011  84.307  55.595 1.00 28.42  ? 130 GLY F O   1 
ATOM   6499  N  N   . ASN F  1 137 ? 94.688  82.164  55.489 1.00 35.02  ? 131 ASN F N   1 
ATOM   6500  C  CA  . ASN F  1 137 ? 96.092  82.483  55.744 1.00 33.18  ? 131 ASN F CA  1 
ATOM   6501  C  C   . ASN F  1 137 ? 97.001  81.493  55.055 1.00 30.89  ? 131 ASN F C   1 
ATOM   6502  O  O   . ASN F  1 137 ? 96.544  80.468  54.560 1.00 34.90  ? 131 ASN F O   1 
ATOM   6503  C  CB  . ASN F  1 137 ? 96.434  82.535  57.234 1.00 22.52  ? 131 ASN F CB  1 
ATOM   6504  C  CG  . ASN F  1 137 ? 96.140  81.259  57.962 1.00 28.12  ? 131 ASN F CG  1 
ATOM   6505  O  OD1 . ASN F  1 137 ? 96.120  80.169  57.386 1.00 24.91  ? 131 ASN F OD1 1 
ATOM   6506  N  ND2 . ASN F  1 137 ? 95.939  81.381  59.267 1.00 22.81  ? 131 ASN F ND2 1 
ATOM   6507  N  N   . GLU F  1 138 ? 98.289  81.810  55.019 1.00 36.03  ? 132 GLU F N   1 
ATOM   6508  C  CA  . GLU F  1 138 ? 99.277  80.950  54.381 1.00 37.39  ? 132 GLU F CA  1 
ATOM   6509  C  C   . GLU F  1 138 ? 99.310  79.548  54.961 1.00 31.97  ? 132 GLU F C   1 
ATOM   6510  O  O   . GLU F  1 138 ? 99.418  78.569  54.220 1.00 30.06  ? 132 GLU F O   1 
ATOM   6511  C  CB  . GLU F  1 138 ? 100.661 81.577  54.483 1.00 50.15  ? 132 GLU F CB  1 
ATOM   6512  C  CG  . GLU F  1 138 ? 101.067 82.328  53.233 1.00 70.02  ? 132 GLU F CG  1 
ATOM   6513  C  CD  . GLU F  1 138 ? 102.455 82.913  53.353 1.00 81.67  ? 132 GLU F CD  1 
ATOM   6514  O  OE1 . GLU F  1 138 ? 103.394 82.138  53.654 1.00 79.61  ? 132 GLU F OE1 1 
ATOM   6515  O  OE2 . GLU F  1 138 ? 102.605 84.142  53.146 1.00 85.02  ? 132 GLU F OE2 1 
ATOM   6516  N  N   . GLU F  1 139 ? 99.234  79.455  56.287 1.00 17.49  ? 133 GLU F N   1 
ATOM   6517  C  CA  . GLU F  1 139 ? 99.232  78.168  56.947 1.00 23.30  ? 133 GLU F CA  1 
ATOM   6518  C  C   . GLU F  1 139 ? 98.120  77.298  56.346 1.00 25.54  ? 133 GLU F C   1 
ATOM   6519  O  O   . GLU F  1 139 ? 98.309  76.105  56.093 1.00 27.02  ? 133 GLU F O   1 
ATOM   6520  C  CB  . GLU F  1 139 ? 98.995  78.353  58.442 1.00 26.67  ? 133 GLU F CB  1 
ATOM   6521  C  CG  . GLU F  1 139 ? 99.229  77.099  59.241 1.00 39.91  ? 133 GLU F CG  1 
ATOM   6522  C  CD  . GLU F  1 139 ? 100.627 76.541  59.027 1.00 50.69  ? 133 GLU F CD  1 
ATOM   6523  O  OE1 . GLU F  1 139 ? 100.734 75.370  58.608 1.00 59.87  ? 133 GLU F OE1 1 
ATOM   6524  O  OE2 . GLU F  1 139 ? 101.617 77.267  59.276 1.00 46.19  ? 133 GLU F OE2 1 
ATOM   6525  N  N   . SER F  1 140 ? 96.960  77.910  56.122 1.00 22.97  ? 134 SER F N   1 
ATOM   6526  C  CA  . SER F  1 140 ? 95.820  77.213  55.546 1.00 23.39  ? 134 SER F CA  1 
ATOM   6527  C  C   . SER F  1 140 ? 96.142  76.663  54.153 1.00 20.43  ? 134 SER F C   1 
ATOM   6528  O  O   . SER F  1 140 ? 95.804  75.530  53.838 1.00 23.51  ? 134 SER F O   1 
ATOM   6529  C  CB  . SER F  1 140 ? 94.620  78.161  55.452 1.00 19.00  ? 134 SER F CB  1 
ATOM   6530  O  OG  . SER F  1 140 ? 93.487  77.496  54.922 1.00 19.26  ? 134 SER F OG  1 
ATOM   6531  N  N   . THR F  1 141 ? 96.800  77.454  53.320 1.00 18.96  ? 135 THR F N   1 
ATOM   6532  C  CA  . THR F  1 141 ? 97.109  77.000  51.969 1.00 22.88  ? 135 THR F CA  1 
ATOM   6533  C  C   . THR F  1 141 ? 98.309  76.074  51.901 1.00 25.61  ? 135 THR F C   1 
ATOM   6534  O  O   . THR F  1 141 ? 98.686  75.631  50.814 1.00 22.17  ? 135 THR F O   1 
ATOM   6535  C  CB  . THR F  1 141 ? 97.336  78.188  51.011 1.00 25.13  ? 135 THR F CB  1 
ATOM   6536  O  OG1 . THR F  1 141 ? 98.435  78.978  51.471 1.00 37.53  ? 135 THR F OG1 1 
ATOM   6537  C  CG2 . THR F  1 141 ? 96.099  79.058  50.951 1.00 30.01  ? 135 THR F CG2 1 
ATOM   6538  N  N   . LYS F  1 142 ? 98.905  75.779  53.059 1.00 30.65  ? 136 LYS F N   1 
ATOM   6539  C  CA  . LYS F  1 142 ? 100.058 74.867  53.126 1.00 33.84  ? 136 LYS F CA  1 
ATOM   6540  C  C   . LYS F  1 142 ? 99.736  73.584  53.879 1.00 32.45  ? 136 LYS F C   1 
ATOM   6541  O  O   . LYS F  1 142 ? 99.903  72.488  53.338 1.00 34.70  ? 136 LYS F O   1 
ATOM   6542  C  CB  . LYS F  1 142 ? 101.273 75.545  53.780 1.00 34.47  ? 136 LYS F CB  1 
ATOM   6543  C  CG  . LYS F  1 142 ? 101.983 76.546  52.854 1.00 48.53  ? 136 LYS F CG  1 
ATOM   6544  C  CD  . LYS F  1 142 ? 103.312 77.068  53.429 1.00 53.51  ? 136 LYS F CD  1 
ATOM   6545  C  CE  . LYS F  1 142 ? 103.109 77.933  54.675 1.00 64.87  ? 136 LYS F CE  1 
ATOM   6546  N  NZ  . LYS F  1 142 ? 104.383 78.501  55.221 1.00 64.45  ? 136 LYS F NZ  1 
ATOM   6547  N  N   . THR F  1 143 ? 99.252  73.718  55.114 1.00 27.96  ? 137 THR F N   1 
ATOM   6548  C  CA  . THR F  1 143 ? 98.929  72.553  55.937 1.00 26.57  ? 137 THR F CA  1 
ATOM   6549  C  C   . THR F  1 143 ? 97.456  72.395  56.308 1.00 26.14  ? 137 THR F C   1 
ATOM   6550  O  O   . THR F  1 143 ? 97.091  71.445  56.996 1.00 20.96  ? 137 THR F O   1 
ATOM   6551  C  CB  . THR F  1 143 ? 99.687  72.589  57.269 1.00 30.91  ? 137 THR F CB  1 
ATOM   6552  O  OG1 . THR F  1 143 ? 99.108  73.593  58.116 1.00 28.31  ? 137 THR F OG1 1 
ATOM   6553  C  CG2 . THR F  1 143 ? 101.157 72.914  57.046 1.00 15.92  ? 137 THR F CG2 1 
ATOM   6554  N  N   . GLY F  1 144 ? 96.609  73.324  55.889 1.00 25.43  ? 138 GLY F N   1 
ATOM   6555  C  CA  . GLY F  1 144 ? 95.210  73.220  56.263 1.00 17.15  ? 138 GLY F CA  1 
ATOM   6556  C  C   . GLY F  1 144 ? 94.986  73.523  57.748 1.00 24.16  ? 138 GLY F C   1 
ATOM   6557  O  O   . GLY F  1 144 ? 93.875  73.327  58.256 1.00 18.44  ? 138 GLY F O   1 
ATOM   6558  N  N   . ASN F  1 145 ? 96.023  74.001  58.448 1.00 19.50  ? 139 ASN F N   1 
ATOM   6559  C  CA  . ASN F  1 145 ? 95.893  74.314  59.871 1.00 20.14  ? 139 ASN F CA  1 
ATOM   6560  C  C   . ASN F  1 145 ? 95.484  73.049  60.651 1.00 24.15  ? 139 ASN F C   1 
ATOM   6561  O  O   . ASN F  1 145 ? 94.749  73.124  61.640 1.00 23.00  ? 139 ASN F O   1 
ATOM   6562  C  CB  . ASN F  1 145 ? 94.828  75.426  60.063 1.00 15.58  ? 139 ASN F CB  1 
ATOM   6563  C  CG  . ASN F  1 145 ? 95.375  76.819  59.775 1.00 21.68  ? 139 ASN F CG  1 
ATOM   6564  O  OD1 . ASN F  1 145 ? 96.279  77.282  60.462 1.00 27.63  ? 139 ASN F OD1 1 
ATOM   6565  N  ND2 . ASN F  1 145 ? 94.838  77.487  58.749 1.00 17.90  ? 139 ASN F ND2 1 
ATOM   6566  N  N   . ALA F  1 146 ? 95.960  71.888  60.208 1.00 18.20  ? 140 ALA F N   1 
ATOM   6567  C  CA  . ALA F  1 146 ? 95.602  70.626  60.853 1.00 18.58  ? 140 ALA F CA  1 
ATOM   6568  C  C   . ALA F  1 146 ? 96.385  70.306  62.137 1.00 17.92  ? 140 ALA F C   1 
ATOM   6569  O  O   . ALA F  1 146 ? 96.133  69.300  62.821 1.00 13.82  ? 140 ALA F O   1 
ATOM   6570  C  CB  . ALA F  1 146 ? 95.737  69.481  59.843 1.00 21.01  ? 140 ALA F CB  1 
ATOM   6571  N  N   . GLY F  1 147 ? 97.345  71.150  62.465 1.00 17.92  ? 141 GLY F N   1 
ATOM   6572  C  CA  . GLY F  1 147 ? 98.096  70.911  63.681 1.00 24.53  ? 141 GLY F CA  1 
ATOM   6573  C  C   . GLY F  1 147 ? 99.137  69.809  63.625 1.00 27.41  ? 141 GLY F C   1 
ATOM   6574  O  O   . GLY F  1 147 ? 99.544  69.336  62.546 1.00 24.91  ? 141 GLY F O   1 
ATOM   6575  N  N   . SER F  1 148 ? 99.537  69.372  64.814 1.00 23.51  ? 142 SER F N   1 
ATOM   6576  C  CA  . SER F  1 148 ? 100.573 68.372  64.950 1.00 20.75  ? 142 SER F CA  1 
ATOM   6577  C  C   . SER F  1 148 ? 100.266 66.998  64.356 1.00 26.34  ? 142 SER F C   1 
ATOM   6578  O  O   . SER F  1 148 ? 99.119  66.655  64.034 1.00 25.84  ? 142 SER F O   1 
ATOM   6579  C  CB  . SER F  1 148 ? 100.975 68.248  66.427 1.00 17.09  ? 142 SER F CB  1 
ATOM   6580  O  OG  . SER F  1 148 ? 99.997  67.573  67.185 1.00 28.40  ? 142 SER F OG  1 
ATOM   6581  N  N   . ARG F  1 149 ? 101.326 66.218  64.205 1.00 22.09  ? 143 ARG F N   1 
ATOM   6582  C  CA  . ARG F  1 149 ? 101.232 64.891  63.631 1.00 24.88  ? 143 ARG F CA  1 
ATOM   6583  C  C   . ARG F  1 149 ? 101.142 63.916  64.779 1.00 23.52  ? 143 ARG F C   1 
ATOM   6584  O  O   . ARG F  1 149 ? 102.087 63.759  65.530 1.00 32.96  ? 143 ARG F O   1 
ATOM   6585  C  CB  . ARG F  1 149 ? 102.475 64.652  62.783 1.00 16.27  ? 143 ARG F CB  1 
ATOM   6586  C  CG  . ARG F  1 149 ? 102.748 65.842  61.880 1.00 14.38  ? 143 ARG F CG  1 
ATOM   6587  C  CD  . ARG F  1 149 ? 104.025 65.756  61.057 1.00 15.23  ? 143 ARG F CD  1 
ATOM   6588  N  NE  . ARG F  1 149 ? 104.120 66.947  60.214 1.00 22.59  ? 143 ARG F NE  1 
ATOM   6589  C  CZ  . ARG F  1 149 ? 104.925 67.087  59.164 1.00 26.77  ? 143 ARG F CZ  1 
ATOM   6590  N  NH1 . ARG F  1 149 ? 104.915 68.217  58.480 1.00 21.15  ? 143 ARG F NH1 1 
ATOM   6591  N  NH2 . ARG F  1 149 ? 105.741 66.110  58.789 1.00 24.48  ? 143 ARG F NH2 1 
ATOM   6592  N  N   . LEU F  1 150 ? 99.986  63.285  64.936 1.00 28.57  ? 144 LEU F N   1 
ATOM   6593  C  CA  . LEU F  1 150 ? 99.786  62.342  66.028 1.00 27.31  ? 144 LEU F CA  1 
ATOM   6594  C  C   . LEU F  1 150 ? 100.404 60.981  65.738 1.00 24.53  ? 144 LEU F C   1 
ATOM   6595  O  O   . LEU F  1 150 ? 100.960 60.334  66.619 1.00 28.37  ? 144 LEU F O   1 
ATOM   6596  C  CB  . LEU F  1 150 ? 98.292  62.180  66.296 1.00 25.14  ? 144 LEU F CB  1 
ATOM   6597  C  CG  . LEU F  1 150 ? 97.630  63.510  66.627 1.00 34.45  ? 144 LEU F CG  1 
ATOM   6598  C  CD1 . LEU F  1 150 ? 96.145  63.304  66.898 1.00 34.88  ? 144 LEU F CD1 1 
ATOM   6599  C  CD2 . LEU F  1 150 ? 98.330  64.113  67.849 1.00 33.20  ? 144 LEU F CD2 1 
ATOM   6600  N  N   . ALA F  1 151 ? 100.304 60.551  64.491 1.00 23.20  ? 145 ALA F N   1 
ATOM   6601  C  CA  . ALA F  1 151 ? 100.839 59.260  64.099 1.00 26.50  ? 145 ALA F CA  1 
ATOM   6602  C  C   . ALA F  1 151 ? 101.084 59.293  62.604 1.00 27.40  ? 145 ALA F C   1 
ATOM   6603  O  O   . ALA F  1 151 ? 100.450 60.054  61.871 1.00 40.59  ? 145 ALA F O   1 
ATOM   6604  C  CB  . ALA F  1 151 ? 99.844  58.141  64.457 1.00 12.68  ? 145 ALA F CB  1 
ATOM   6605  N  N   . CYS F  1 152 ? 102.007 58.463  62.161 1.00 20.25  ? 146 CYS F N   1 
ATOM   6606  C  CA  . CYS F  1 152 ? 102.361 58.386  60.758 1.00 23.81  ? 146 CYS F CA  1 
ATOM   6607  C  C   . CYS F  1 152 ? 102.979 57.010  60.510 1.00 20.82  ? 146 CYS F C   1 
ATOM   6608  O  O   . CYS F  1 152 ? 103.224 56.259  61.445 1.00 16.88  ? 146 CYS F O   1 
ATOM   6609  C  CB  . CYS F  1 152 ? 103.365 59.505  60.408 1.00 16.80  ? 146 CYS F CB  1 
ATOM   6610  S  SG  . CYS F  1 152 ? 104.892 59.496  61.409 1.00 27.10  ? 146 CYS F SG  1 
ATOM   6611  N  N   . GLY F  1 153 ? 103.189 56.684  59.243 1.00 18.55  ? 147 GLY F N   1 
ATOM   6612  C  CA  . GLY F  1 153 ? 103.794 55.424  58.873 1.00 15.34  ? 147 GLY F CA  1 
ATOM   6613  C  C   . GLY F  1 153 ? 104.205 55.512  57.411 1.00 22.83  ? 147 GLY F C   1 
ATOM   6614  O  O   . GLY F  1 153 ? 103.635 56.311  56.650 1.00 21.89  ? 147 GLY F O   1 
ATOM   6615  N  N   . VAL F  1 154 ? 105.191 54.709  57.019 1.00 15.61  ? 148 VAL F N   1 
ATOM   6616  C  CA  . VAL F  1 154 ? 105.656 54.691  55.641 1.00 16.98  ? 148 VAL F CA  1 
ATOM   6617  C  C   . VAL F  1 154 ? 104.716 53.770  54.856 1.00 23.48  ? 148 VAL F C   1 
ATOM   6618  O  O   . VAL F  1 154 ? 104.406 52.664  55.291 1.00 24.54  ? 148 VAL F O   1 
ATOM   6619  C  CB  . VAL F  1 154 ? 107.108 54.182  55.548 1.00 15.99  ? 148 VAL F CB  1 
ATOM   6620  C  CG1 . VAL F  1 154 ? 107.562 54.156  54.086 1.00 15.66  ? 148 VAL F CG1 1 
ATOM   6621  C  CG2 . VAL F  1 154 ? 108.033 55.113  56.340 1.00 10.64  ? 148 VAL F CG2 1 
ATOM   6622  N  N   . ILE F  1 155 ? 104.249 54.231  53.701 1.00 24.25  ? 149 ILE F N   1 
ATOM   6623  C  CA  . ILE F  1 155 ? 103.314 53.438  52.918 1.00 18.69  ? 149 ILE F CA  1 
ATOM   6624  C  C   . ILE F  1 155 ? 104.092 52.412  52.150 1.00 23.53  ? 149 ILE F C   1 
ATOM   6625  O  O   . ILE F  1 155 ? 104.978 52.760  51.370 1.00 22.69  ? 149 ILE F O   1 
ATOM   6626  C  CB  . ILE F  1 155 ? 102.541 54.319  51.935 1.00 23.36  ? 149 ILE F CB  1 
ATOM   6627  C  CG1 . ILE F  1 155 ? 101.867 55.467  52.696 1.00 17.47  ? 149 ILE F CG1 1 
ATOM   6628  C  CG2 . ILE F  1 155 ? 101.516 53.479  51.171 1.00 26.09  ? 149 ILE F CG2 1 
ATOM   6629  C  CD1 . ILE F  1 155 ? 101.229 56.552  51.769 1.00 14.23  ? 149 ILE F CD1 1 
ATOM   6630  N  N   . GLY F  1 156 ? 103.770 51.143  52.367 1.00 19.28  ? 150 GLY F N   1 
ATOM   6631  C  CA  . GLY F  1 156 ? 104.496 50.105  51.666 1.00 20.65  ? 150 GLY F CA  1 
ATOM   6632  C  C   . GLY F  1 156 ? 103.660 49.209  50.785 1.00 24.88  ? 150 GLY F C   1 
ATOM   6633  O  O   . GLY F  1 156 ? 102.438 49.127  50.940 1.00 24.94  ? 150 GLY F O   1 
ATOM   6634  N  N   . ILE F  1 157 ? 104.335 48.532  49.861 1.00 26.67  ? 151 ILE F N   1 
ATOM   6635  C  CA  . ILE F  1 157 ? 103.688 47.613  48.934 1.00 27.70  ? 151 ILE F CA  1 
ATOM   6636  C  C   . ILE F  1 157 ? 103.119 46.434  49.718 1.00 25.98  ? 151 ILE F C   1 
ATOM   6637  O  O   . ILE F  1 157 ? 103.758 45.922  50.635 1.00 32.51  ? 151 ILE F O   1 
ATOM   6638  C  CB  . ILE F  1 157 ? 104.699 47.112  47.871 1.00 31.79  ? 151 ILE F CB  1 
ATOM   6639  C  CG1 . ILE F  1 157 ? 105.476 48.308  47.313 1.00 39.10  ? 151 ILE F CG1 1 
ATOM   6640  C  CG2 . ILE F  1 157 ? 103.961 46.431  46.711 1.00 27.75  ? 151 ILE F CG2 1 
ATOM   6641  C  CD1 . ILE F  1 157 ? 106.414 47.972  46.157 1.00 44.68  ? 151 ILE F CD1 1 
ATOM   6642  N  N   . ALA F  1 158 ? 101.915 46.004  49.366 1.00 25.23  ? 152 ALA F N   1 
ATOM   6643  C  CA  . ALA F  1 158 ? 101.289 44.899  50.082 1.00 28.56  ? 152 ALA F CA  1 
ATOM   6644  C  C   . ALA F  1 158 ? 100.848 43.807  49.136 1.00 31.70  ? 152 ALA F C   1 
ATOM   6645  O  O   . ALA F  1 158 ? 100.704 44.032  47.933 1.00 26.38  ? 152 ALA F O   1 
ATOM   6646  C  CB  . ALA F  1 158 ? 100.102 45.396  50.878 1.00 16.63  ? 152 ALA F CB  1 
ATOM   6647  N  N   . GLN F  1 159 ? 100.625 42.624  49.700 1.00 42.57  ? 153 GLN F N   1 
ATOM   6648  C  CA  . GLN F  1 159 ? 100.226 41.451  48.933 1.00 45.83  ? 153 GLN F CA  1 
ATOM   6649  C  C   . GLN F  1 159 ? 98.747  41.477  48.555 1.00 48.12  ? 153 GLN F C   1 
ATOM   6650  O  O   . GLN F  1 159 ? 97.916  41.762  49.447 1.00 46.16  ? 153 GLN F O   1 
ATOM   6651  C  CB  . GLN F  1 159 ? 100.529 40.200  49.749 1.00 46.51  ? 153 GLN F CB  1 
ATOM   6652  C  CG  . GLN F  1 159 ? 100.557 38.922  48.940 1.00 64.00  ? 153 GLN F CG  1 
ATOM   6653  C  CD  . GLN F  1 159 ? 100.877 37.705  49.793 1.00 69.71  ? 153 GLN F CD  1 
ATOM   6654  O  OE1 . GLN F  1 159 ? 101.260 36.653  49.276 1.00 71.65  ? 153 GLN F OE1 1 
ATOM   6655  N  NE2 . GLN F  1 159 ? 100.717 37.843  51.108 1.00 69.87  ? 153 GLN F NE2 1 
ATOM   6656  O  OXT . GLN F  1 159 ? 98.442  41.195  47.370 1.00 46.02  ? 153 GLN F OXT 1 
ATOM   6657  N  N   . ALA G  1 7   ? 79.502  161.946 44.592 1.00 96.77  ? 1   ALA G N   1 
ATOM   6658  C  CA  . ALA G  1 7   ? 78.606  162.340 45.717 1.00 90.77  ? 1   ALA G CA  1 
ATOM   6659  C  C   . ALA G  1 7   ? 78.516  161.212 46.739 1.00 85.31  ? 1   ALA G C   1 
ATOM   6660  O  O   . ALA G  1 7   ? 78.332  161.451 47.933 1.00 77.74  ? 1   ALA G O   1 
ATOM   6661  C  CB  . ALA G  1 7   ? 77.212  162.680 45.178 1.00 93.55  ? 1   ALA G CB  1 
ATOM   6662  N  N   . THR G  1 8   ? 78.655  159.980 46.260 1.00 81.21  ? 2   THR G N   1 
ATOM   6663  C  CA  . THR G  1 8   ? 78.582  158.816 47.126 1.00 74.95  ? 2   THR G CA  1 
ATOM   6664  C  C   . THR G  1 8   ? 79.592  158.880 48.280 1.00 73.08  ? 2   THR G C   1 
ATOM   6665  O  O   . THR G  1 8   ? 80.718  159.363 48.130 1.00 70.62  ? 2   THR G O   1 
ATOM   6666  C  CB  . THR G  1 8   ? 78.795  157.503 46.317 1.00 68.07  ? 2   THR G CB  1 
ATOM   6667  O  OG1 . THR G  1 8   ? 79.884  157.683 45.411 1.00 57.52  ? 2   THR G OG1 1 
ATOM   6668  C  CG2 . THR G  1 8   ? 77.539  157.128 45.520 1.00 67.01  ? 2   THR G CG2 1 
ATOM   6669  N  N   . LYS G  1 9   ? 79.145  158.424 49.444 1.00 67.05  ? 3   LYS G N   1 
ATOM   6670  C  CA  . LYS G  1 9   ? 79.969  158.367 50.637 1.00 61.32  ? 3   LYS G CA  1 
ATOM   6671  C  C   . LYS G  1 9   ? 79.950  156.904 51.046 1.00 57.93  ? 3   LYS G C   1 
ATOM   6672  O  O   . LYS G  1 9   ? 78.967  156.203 50.813 1.00 55.45  ? 3   LYS G O   1 
ATOM   6673  C  CB  . LYS G  1 9   ? 79.370  159.208 51.762 1.00 62.77  ? 3   LYS G CB  1 
ATOM   6674  C  CG  . LYS G  1 9   ? 79.301  160.688 51.488 1.00 72.45  ? 3   LYS G CG  1 
ATOM   6675  C  CD  . LYS G  1 9   ? 78.673  161.423 52.661 1.00 81.53  ? 3   LYS G CD  1 
ATOM   6676  C  CE  . LYS G  1 9   ? 78.539  162.913 52.378 1.00 87.66  ? 3   LYS G CE  1 
ATOM   6677  N  NZ  . LYS G  1 9   ? 77.835  163.632 53.479 1.00 90.40  ? 3   LYS G NZ  1 
ATOM   6678  N  N   . ALA G  1 10  ? 81.034  156.437 51.644 1.00 58.58  ? 4   ALA G N   1 
ATOM   6679  C  CA  . ALA G  1 10  ? 81.105  155.052 52.089 1.00 54.42  ? 4   ALA G CA  1 
ATOM   6680  C  C   . ALA G  1 10  ? 81.536  155.025 53.551 1.00 52.50  ? 4   ALA G C   1 
ATOM   6681  O  O   . ALA G  1 10  ? 81.871  156.064 54.137 1.00 51.83  ? 4   ALA G O   1 
ATOM   6682  C  CB  . ALA G  1 10  ? 82.087  154.267 51.223 1.00 52.91  ? 4   ALA G CB  1 
ATOM   6683  N  N   . VAL G  1 11  ? 81.514  153.841 54.146 1.00 45.76  ? 5   VAL G N   1 
ATOM   6684  C  CA  . VAL G  1 11  ? 81.903  153.700 55.539 1.00 43.98  ? 5   VAL G CA  1 
ATOM   6685  C  C   . VAL G  1 11  ? 82.287  152.262 55.848 1.00 37.14  ? 5   VAL G C   1 
ATOM   6686  O  O   . VAL G  1 11  ? 81.856  151.329 55.181 1.00 41.22  ? 5   VAL G O   1 
ATOM   6687  C  CB  . VAL G  1 11  ? 80.772  154.176 56.485 1.00 39.48  ? 5   VAL G CB  1 
ATOM   6688  C  CG1 . VAL G  1 11  ? 79.597  153.223 56.420 1.00 38.51  ? 5   VAL G CG1 1 
ATOM   6689  C  CG2 . VAL G  1 11  ? 81.304  154.325 57.901 1.00 35.07  ? 5   VAL G CG2 1 
ATOM   6690  N  N   . CYS G  1 12  ? 83.112  152.090 56.866 1.00 41.49  ? 6   CYS G N   1 
ATOM   6691  C  CA  . CYS G  1 12  ? 83.584  150.768 57.233 1.00 39.91  ? 6   CYS G CA  1 
ATOM   6692  C  C   . CYS G  1 12  ? 83.860  150.666 58.727 1.00 42.09  ? 6   CYS G C   1 
ATOM   6693  O  O   . CYS G  1 12  ? 84.481  151.557 59.310 1.00 46.66  ? 6   CYS G O   1 
ATOM   6694  C  CB  . CYS G  1 12  ? 84.854  150.476 56.445 1.00 36.01  ? 6   CYS G CB  1 
ATOM   6695  S  SG  . CYS G  1 12  ? 85.759  149.051 56.988 1.00 41.77  ? 6   CYS G SG  1 
ATOM   6696  N  N   . VAL G  1 13  ? 83.382  149.593 59.352 1.00 35.01  ? 7   VAL G N   1 
ATOM   6697  C  CA  . VAL G  1 13  ? 83.626  149.399 60.772 1.00 33.86  ? 7   VAL G CA  1 
ATOM   6698  C  C   . VAL G  1 13  ? 84.681  148.313 60.910 1.00 35.59  ? 7   VAL G C   1 
ATOM   6699  O  O   . VAL G  1 13  ? 84.479  147.177 60.482 1.00 46.07  ? 7   VAL G O   1 
ATOM   6700  C  CB  . VAL G  1 13  ? 82.352  148.982 61.504 1.00 32.32  ? 7   VAL G CB  1 
ATOM   6701  C  CG1 . VAL G  1 13  ? 82.642  148.797 62.972 1.00 36.13  ? 7   VAL G CG1 1 
ATOM   6702  C  CG2 . VAL G  1 13  ? 81.302  150.038 61.326 1.00 23.57  ? 7   VAL G CG2 1 
ATOM   6703  N  N   . LEU G  1 14  ? 85.813  148.669 61.502 1.00 37.55  ? 8   LEU G N   1 
ATOM   6704  C  CA  . LEU G  1 14  ? 86.923  147.737 61.670 1.00 31.32  ? 8   LEU G CA  1 
ATOM   6705  C  C   . LEU G  1 14  ? 86.861  146.964 62.976 1.00 31.09  ? 8   LEU G C   1 
ATOM   6706  O  O   . LEU G  1 14  ? 86.659  147.548 64.048 1.00 26.24  ? 8   LEU G O   1 
ATOM   6707  C  CB  . LEU G  1 14  ? 88.244  148.500 61.614 1.00 38.19  ? 8   LEU G CB  1 
ATOM   6708  C  CG  . LEU G  1 14  ? 88.523  149.325 60.359 1.00 43.41  ? 8   LEU G CG  1 
ATOM   6709  C  CD1 . LEU G  1 14  ? 89.688  150.248 60.625 1.00 50.75  ? 8   LEU G CD1 1 
ATOM   6710  C  CD2 . LEU G  1 14  ? 88.822  148.406 59.182 1.00 47.66  ? 8   LEU G CD2 1 
ATOM   6711  N  N   . LYS G  1 15  ? 87.055  145.651 62.879 1.00 31.24  ? 9   LYS G N   1 
ATOM   6712  C  CA  . LYS G  1 15  ? 87.045  144.771 64.046 1.00 36.25  ? 9   LYS G CA  1 
ATOM   6713  C  C   . LYS G  1 15  ? 87.908  143.542 63.817 1.00 33.05  ? 9   LYS G C   1 
ATOM   6714  O  O   . LYS G  1 15  ? 88.130  143.122 62.684 1.00 36.39  ? 9   LYS G O   1 
ATOM   6715  C  CB  . LYS G  1 15  ? 85.613  144.344 64.382 1.00 37.58  ? 9   LYS G CB  1 
ATOM   6716  C  CG  . LYS G  1 15  ? 84.846  145.393 65.160 1.00 55.87  ? 9   LYS G CG  1 
ATOM   6717  C  CD  . LYS G  1 15  ? 83.365  145.089 65.188 1.00 65.99  ? 9   LYS G CD  1 
ATOM   6718  C  CE  . LYS G  1 15  ? 82.616  146.092 66.057 1.00 66.92  ? 9   LYS G CE  1 
ATOM   6719  N  NZ  . LYS G  1 15  ? 81.151  145.873 65.917 1.00 60.71  ? 9   LYS G NZ  1 
ATOM   6720  N  N   . GLY G  1 16  ? 88.412  142.978 64.902 1.00 34.46  ? 10  GLY G N   1 
ATOM   6721  C  CA  . GLY G  1 16  ? 89.241  141.794 64.798 1.00 35.64  ? 10  GLY G CA  1 
ATOM   6722  C  C   . GLY G  1 16  ? 89.144  141.005 66.084 1.00 45.82  ? 10  GLY G C   1 
ATOM   6723  O  O   . GLY G  1 16  ? 88.219  141.215 66.879 1.00 43.23  ? 10  GLY G O   1 
ATOM   6724  N  N   . ASP G  1 17  ? 90.101  140.107 66.298 1.00 47.15  ? 11  ASP G N   1 
ATOM   6725  C  CA  . ASP G  1 17  ? 90.114  139.279 67.498 1.00 51.65  ? 11  ASP G CA  1 
ATOM   6726  C  C   . ASP G  1 17  ? 90.576  140.060 68.720 1.00 51.17  ? 11  ASP G C   1 
ATOM   6727  O  O   . ASP G  1 17  ? 90.049  139.888 69.820 1.00 54.87  ? 11  ASP G O   1 
ATOM   6728  C  CB  . ASP G  1 17  ? 91.022  138.072 67.279 1.00 55.05  ? 11  ASP G CB  1 
ATOM   6729  C  CG  . ASP G  1 17  ? 90.633  137.281 66.057 1.00 64.27  ? 11  ASP G CG  1 
ATOM   6730  O  OD1 . ASP G  1 17  ? 89.421  136.995 65.908 1.00 65.23  ? 11  ASP G OD1 1 
ATOM   6731  O  OD2 . ASP G  1 17  ? 91.535  136.947 65.254 1.00 67.30  ? 11  ASP G OD2 1 
ATOM   6732  N  N   . GLY G  1 18  ? 91.560  140.925 68.510 1.00 49.28  ? 12  GLY G N   1 
ATOM   6733  C  CA  . GLY G  1 18  ? 92.087  141.728 69.589 1.00 40.27  ? 12  GLY G CA  1 
ATOM   6734  C  C   . GLY G  1 18  ? 91.187  142.899 69.937 1.00 43.11  ? 12  GLY G C   1 
ATOM   6735  O  O   . GLY G  1 18  ? 89.967  142.853 69.720 1.00 42.33  ? 12  GLY G O   1 
ATOM   6736  N  N   . PRO G  1 19  ? 91.779  143.978 70.478 1.00 40.10  ? 13  PRO G N   1 
ATOM   6737  C  CA  . PRO G  1 19  ? 91.078  145.195 70.883 1.00 36.83  ? 13  PRO G CA  1 
ATOM   6738  C  C   . PRO G  1 19  ? 91.039  146.259 69.786 1.00 34.46  ? 13  PRO G C   1 
ATOM   6739  O  O   . PRO G  1 19  ? 90.522  147.357 70.000 1.00 32.32  ? 13  PRO G O   1 
ATOM   6740  C  CB  . PRO G  1 19  ? 91.897  145.654 72.069 1.00 29.01  ? 13  PRO G CB  1 
ATOM   6741  C  CG  . PRO G  1 19  ? 93.305  145.417 71.532 1.00 32.09  ? 13  PRO G CG  1 
ATOM   6742  C  CD  . PRO G  1 19  ? 93.205  144.048 70.869 1.00 28.06  ? 13  PRO G CD  1 
ATOM   6743  N  N   . VAL G  1 20  ? 91.596  145.948 68.621 1.00 32.63  ? 14  VAL G N   1 
ATOM   6744  C  CA  . VAL G  1 20  ? 91.594  146.931 67.539 1.00 36.56  ? 14  VAL G CA  1 
ATOM   6745  C  C   . VAL G  1 20  ? 90.198  147.160 66.987 1.00 35.84  ? 14  VAL G C   1 
ATOM   6746  O  O   . VAL G  1 20  ? 89.511  146.223 66.585 1.00 36.16  ? 14  VAL G O   1 
ATOM   6747  C  CB  . VAL G  1 20  ? 92.486  146.510 66.362 1.00 27.59  ? 14  VAL G CB  1 
ATOM   6748  C  CG1 . VAL G  1 20  ? 92.376  147.535 65.256 1.00 21.89  ? 14  VAL G CG1 1 
ATOM   6749  C  CG2 . VAL G  1 20  ? 93.910  146.374 66.817 1.00 26.45  ? 14  VAL G CG2 1 
ATOM   6750  N  N   . GLN G  1 21  ? 89.775  148.412 66.980 1.00 34.86  ? 15  GLN G N   1 
ATOM   6751  C  CA  . GLN G  1 21  ? 88.469  148.744 66.435 1.00 45.11  ? 15  GLN G CA  1 
ATOM   6752  C  C   . GLN G  1 21  ? 88.423  150.199 65.984 1.00 41.52  ? 15  GLN G C   1 
ATOM   6753  O  O   . GLN G  1 21  ? 89.101  151.051 66.548 1.00 41.25  ? 15  GLN G O   1 
ATOM   6754  C  CB  . GLN G  1 21  ? 87.348  148.429 67.447 1.00 42.48  ? 15  GLN G CB  1 
ATOM   6755  C  CG  . GLN G  1 21  ? 87.602  148.821 68.883 1.00 47.30  ? 15  GLN G CG  1 
ATOM   6756  C  CD  . GLN G  1 21  ? 86.495  148.331 69.818 1.00 47.96  ? 15  GLN G CD  1 
ATOM   6757  O  OE1 . GLN G  1 21  ? 85.673  149.109 70.299 1.00 41.73  ? 15  GLN G OE1 1 
ATOM   6758  N  NE2 . GLN G  1 21  ? 86.470  147.032 70.067 1.00 52.80  ? 15  GLN G NE2 1 
ATOM   6759  N  N   . GLY G  1 22  ? 87.654  150.466 64.935 1.00 36.95  ? 16  GLY G N   1 
ATOM   6760  C  CA  . GLY G  1 22  ? 87.548  151.822 64.439 1.00 38.57  ? 16  GLY G CA  1 
ATOM   6761  C  C   . GLY G  1 22  ? 86.504  152.019 63.357 1.00 37.47  ? 16  GLY G C   1 
ATOM   6762  O  O   . GLY G  1 22  ? 85.929  151.067 62.833 1.00 45.79  ? 16  GLY G O   1 
ATOM   6763  N  N   . ILE G  1 23  ? 86.270  153.278 63.022 1.00 38.79  ? 17  ILE G N   1 
ATOM   6764  C  CA  . ILE G  1 23  ? 85.302  153.657 62.007 1.00 40.43  ? 17  ILE G CA  1 
ATOM   6765  C  C   . ILE G  1 23  ? 85.994  154.527 60.963 1.00 40.55  ? 17  ILE G C   1 
ATOM   6766  O  O   . ILE G  1 23  ? 86.534  155.579 61.291 1.00 42.03  ? 17  ILE G O   1 
ATOM   6767  C  CB  . ILE G  1 23  ? 84.133  154.436 62.657 1.00 37.40  ? 17  ILE G CB  1 
ATOM   6768  C  CG1 . ILE G  1 23  ? 83.343  153.477 63.554 1.00 33.56  ? 17  ILE G CG1 1 
ATOM   6769  C  CG2 . ILE G  1 23  ? 83.255  155.087 61.583 1.00 31.87  ? 17  ILE G CG2 1 
ATOM   6770  C  CD1 . ILE G  1 23  ? 82.108  154.075 64.164 1.00 32.95  ? 17  ILE G CD1 1 
ATOM   6771  N  N   . ILE G  1 24  ? 85.995  154.081 59.711 1.00 37.91  ? 18  ILE G N   1 
ATOM   6772  C  CA  . ILE G  1 24  ? 86.635  154.850 58.648 1.00 37.91  ? 18  ILE G CA  1 
ATOM   6773  C  C   . ILE G  1 24  ? 85.602  155.287 57.629 1.00 39.23  ? 18  ILE G C   1 
ATOM   6774  O  O   . ILE G  1 24  ? 84.846  154.458 57.107 1.00 33.95  ? 18  ILE G O   1 
ATOM   6775  C  CB  . ILE G  1 24  ? 87.728  154.033 57.934 1.00 39.11  ? 18  ILE G CB  1 
ATOM   6776  C  CG1 . ILE G  1 24  ? 88.871  153.716 58.906 1.00 41.82  ? 18  ILE G CG1 1 
ATOM   6777  C  CG2 . ILE G  1 24  ? 88.263  154.813 56.754 1.00 41.44  ? 18  ILE G CG2 1 
ATOM   6778  C  CD1 . ILE G  1 24  ? 89.538  154.958 59.507 1.00 39.34  ? 18  ILE G CD1 1 
ATOM   6779  N  N   . ASN G  1 25  ? 85.576  156.592 57.353 1.00 41.55  ? 19  ASN G N   1 
ATOM   6780  C  CA  . ASN G  1 25  ? 84.624  157.180 56.404 1.00 41.04  ? 19  ASN G CA  1 
ATOM   6781  C  C   . ASN G  1 25  ? 85.254  157.476 55.046 1.00 39.68  ? 19  ASN G C   1 
ATOM   6782  O  O   . ASN G  1 25  ? 86.455  157.724 54.949 1.00 37.53  ? 19  ASN G O   1 
ATOM   6783  C  CB  . ASN G  1 25  ? 84.041  158.457 56.988 1.00 33.43  ? 19  ASN G CB  1 
ATOM   6784  C  CG  . ASN G  1 25  ? 83.361  158.225 58.327 1.00 39.62  ? 19  ASN G CG  1 
ATOM   6785  O  OD1 . ASN G  1 25  ? 82.245  157.707 58.387 1.00 49.92  ? 19  ASN G OD1 1 
ATOM   6786  N  ND2 . ASN G  1 25  ? 84.036  158.603 59.413 1.00 34.19  ? 19  ASN G ND2 1 
ATOM   6787  N  N   . PHE G  1 26  ? 84.435  157.432 54.001 1.00 43.75  ? 20  PHE G N   1 
ATOM   6788  C  CA  . PHE G  1 26  ? 84.902  157.684 52.637 1.00 47.21  ? 20  PHE G CA  1 
ATOM   6789  C  C   . PHE G  1 26  ? 83.983  158.673 51.929 1.00 50.96  ? 20  PHE G C   1 
ATOM   6790  O  O   . PHE G  1 26  ? 82.757  158.577 52.016 1.00 42.98  ? 20  PHE G O   1 
ATOM   6791  C  CB  . PHE G  1 26  ? 84.921  156.392 51.826 1.00 40.80  ? 20  PHE G CB  1 
ATOM   6792  C  CG  . PHE G  1 26  ? 85.862  155.342 52.350 1.00 44.66  ? 20  PHE G CG  1 
ATOM   6793  C  CD1 . PHE G  1 26  ? 87.129  155.187 51.801 1.00 45.10  ? 20  PHE G CD1 1 
ATOM   6794  C  CD2 . PHE G  1 26  ? 85.455  154.460 53.345 1.00 43.08  ? 20  PHE G CD2 1 
ATOM   6795  C  CE1 . PHE G  1 26  ? 87.974  154.162 52.224 1.00 36.49  ? 20  PHE G CE1 1 
ATOM   6796  C  CE2 . PHE G  1 26  ? 86.293  153.435 53.775 1.00 41.06  ? 20  PHE G CE2 1 
ATOM   6797  C  CZ  . PHE G  1 26  ? 87.555  153.284 53.209 1.00 36.96  ? 20  PHE G CZ  1 
ATOM   6798  N  N   . GLU G  1 27  ? 84.580  159.623 51.222 1.00 58.57  ? 21  GLU G N   1 
ATOM   6799  C  CA  . GLU G  1 27  ? 83.802  160.613 50.493 1.00 65.70  ? 21  GLU G CA  1 
ATOM   6800  C  C   . GLU G  1 27  ? 84.467  160.842 49.149 1.00 64.84  ? 21  GLU G C   1 
ATOM   6801  O  O   . GLU G  1 27  ? 85.665  161.102 49.089 1.00 64.43  ? 21  GLU G O   1 
ATOM   6802  C  CB  . GLU G  1 27  ? 83.748  161.925 51.278 1.00 71.70  ? 21  GLU G CB  1 
ATOM   6803  C  CG  . GLU G  1 27  ? 82.727  162.929 50.759 1.00 84.26  ? 21  GLU G CG  1 
ATOM   6804  C  CD  . GLU G  1 27  ? 82.694  164.215 51.578 1.00 92.63  ? 21  GLU G CD  1 
ATOM   6805  O  OE1 . GLU G  1 27  ? 83.692  164.970 51.549 1.00 92.71  ? 21  GLU G OE1 1 
ATOM   6806  O  OE2 . GLU G  1 27  ? 81.671  164.468 52.257 1.00 96.12  ? 21  GLU G OE2 1 
ATOM   6807  N  N   . GLN G  1 28  ? 83.702  160.693 48.073 1.00 65.34  ? 22  GLN G N   1 
ATOM   6808  C  CA  . GLN G  1 28  ? 84.217  160.927 46.727 1.00 68.57  ? 22  GLN G CA  1 
ATOM   6809  C  C   . GLN G  1 28  ? 83.188  161.794 46.037 1.00 76.48  ? 22  GLN G C   1 
ATOM   6810  O  O   . GLN G  1 28  ? 82.347  161.308 45.284 1.00 79.01  ? 22  GLN G O   1 
ATOM   6811  C  CB  . GLN G  1 28  ? 84.398  159.628 45.949 1.00 63.43  ? 22  GLN G CB  1 
ATOM   6812  C  CG  . GLN G  1 28  ? 84.883  159.864 44.524 1.00 61.42  ? 22  GLN G CG  1 
ATOM   6813  C  CD  . GLN G  1 28  ? 85.238  158.580 43.794 1.00 61.66  ? 22  GLN G CD  1 
ATOM   6814  O  OE1 . GLN G  1 28  ? 84.458  157.631 43.783 1.00 61.56  ? 22  GLN G OE1 1 
ATOM   6815  N  NE2 . GLN G  1 28  ? 86.417  158.550 43.171 1.00 55.05  ? 22  GLN G NE2 1 
ATOM   6816  N  N   . LYS G  1 29  ? 83.270  163.089 46.324 1.00 85.74  ? 23  LYS G N   1 
ATOM   6817  C  CA  . LYS G  1 29  ? 82.364  164.100 45.800 1.00 91.43  ? 23  LYS G CA  1 
ATOM   6818  C  C   . LYS G  1 29  ? 82.180  164.125 44.290 1.00 91.83  ? 23  LYS G C   1 
ATOM   6819  O  O   . LYS G  1 29  ? 81.088  164.408 43.812 1.00 89.09  ? 23  LYS G O   1 
ATOM   6820  C  CB  . LYS G  1 29  ? 82.826  165.486 46.257 1.00 98.73  ? 23  LYS G CB  1 
ATOM   6821  C  CG  . LYS G  1 29  ? 82.953  165.653 47.767 1.00 106.30 ? 23  LYS G CG  1 
ATOM   6822  C  CD  . LYS G  1 29  ? 83.555  167.011 48.116 1.00 108.94 ? 23  LYS G CD  1 
ATOM   6823  C  CE  . LYS G  1 29  ? 83.747  167.172 49.615 1.00 109.56 ? 23  LYS G CE  1 
ATOM   6824  N  NZ  . LYS G  1 29  ? 84.421  168.456 49.947 1.00 110.42 ? 23  LYS G NZ  1 
ATOM   6825  N  N   . GLU G  1 30  ? 83.230  163.829 43.534 1.00 95.62  ? 24  GLU G N   1 
ATOM   6826  C  CA  . GLU G  1 30  ? 83.115  163.887 42.083 1.00 100.87 ? 24  GLU G CA  1 
ATOM   6827  C  C   . GLU G  1 30  ? 83.114  162.549 41.362 1.00 100.76 ? 24  GLU G C   1 
ATOM   6828  O  O   . GLU G  1 30  ? 83.844  161.633 41.733 1.00 99.77  ? 24  GLU G O   1 
ATOM   6829  C  CB  . GLU G  1 30  ? 84.221  164.780 41.526 1.00 107.51 ? 24  GLU G CB  1 
ATOM   6830  C  CG  . GLU G  1 30  ? 84.338  166.104 42.267 1.00 114.19 ? 24  GLU G CG  1 
ATOM   6831  C  CD  . GLU G  1 30  ? 85.316  167.057 41.618 1.00 118.42 ? 24  GLU G CD  1 
ATOM   6832  O  OE1 . GLU G  1 30  ? 86.475  166.657 41.385 1.00 119.74 ? 24  GLU G OE1 1 
ATOM   6833  O  OE2 . GLU G  1 30  ? 84.924  168.211 41.345 1.00 121.96 ? 24  GLU G OE2 1 
ATOM   6834  N  N   . SER G  1 31  ? 82.287  162.468 40.320 1.00 102.44 ? 25  SER G N   1 
ATOM   6835  C  CA  . SER G  1 31  ? 82.125  161.274 39.495 1.00 101.90 ? 25  SER G CA  1 
ATOM   6836  C  C   . SER G  1 31  ? 83.350  160.387 39.509 1.00 99.90  ? 25  SER G C   1 
ATOM   6837  O  O   . SER G  1 31  ? 83.239  159.166 39.549 1.00 102.24 ? 25  SER G O   1 
ATOM   6838  C  CB  . SER G  1 31  ? 81.800  161.666 38.053 1.00 106.45 ? 25  SER G CB  1 
ATOM   6839  O  OG  . SER G  1 31  ? 81.674  160.514 37.235 1.00 113.45 ? 25  SER G OG  1 
ATOM   6840  N  N   . ASN G  1 32  ? 84.523  161.001 39.453 1.00 97.82  ? 26  ASN G N   1 
ATOM   6841  C  CA  . ASN G  1 32  ? 85.750  160.233 39.498 1.00 97.32  ? 26  ASN G CA  1 
ATOM   6842  C  C   . ASN G  1 32  ? 86.834  161.023 40.206 1.00 95.63  ? 26  ASN G C   1 
ATOM   6843  O  O   . ASN G  1 32  ? 88.024  160.833 39.955 1.00 95.34  ? 26  ASN G O   1 
ATOM   6844  C  CB  . ASN G  1 32  ? 86.208  159.850 38.095 1.00 99.01  ? 26  ASN G CB  1 
ATOM   6845  C  CG  . ASN G  1 32  ? 87.427  158.953 38.120 1.00 103.89 ? 26  ASN G CG  1 
ATOM   6846  O  OD1 . ASN G  1 32  ? 87.488  157.999 38.898 1.00 105.78 ? 26  ASN G OD1 1 
ATOM   6847  N  ND2 . ASN G  1 32  ? 88.406  159.249 37.272 1.00 104.87 ? 26  ASN G ND2 1 
ATOM   6848  N  N   . GLY G  1 33  ? 86.410  161.904 41.106 1.00 94.22  ? 27  GLY G N   1 
ATOM   6849  C  CA  . GLY G  1 33  ? 87.354  162.718 41.851 1.00 93.30  ? 27  GLY G CA  1 
ATOM   6850  C  C   . GLY G  1 33  ? 88.114  161.949 42.916 1.00 90.58  ? 27  GLY G C   1 
ATOM   6851  O  O   . GLY G  1 33  ? 88.026  160.722 42.984 1.00 94.79  ? 27  GLY G O   1 
ATOM   6852  N  N   . PRO G  1 34  ? 88.889  162.644 43.760 1.00 85.22  ? 28  PRO G N   1 
ATOM   6853  C  CA  . PRO G  1 34  ? 89.650  161.974 44.815 1.00 80.07  ? 28  PRO G CA  1 
ATOM   6854  C  C   . PRO G  1 34  ? 88.711  161.522 45.922 1.00 73.09  ? 28  PRO G C   1 
ATOM   6855  O  O   . PRO G  1 34  ? 87.583  162.007 46.027 1.00 69.01  ? 28  PRO G O   1 
ATOM   6856  C  CB  . PRO G  1 34  ? 90.605  163.064 45.302 1.00 81.79  ? 28  PRO G CB  1 
ATOM   6857  C  CG  . PRO G  1 34  ? 90.716  163.984 44.139 1.00 83.78  ? 28  PRO G CG  1 
ATOM   6858  C  CD  . PRO G  1 34  ? 89.297  164.051 43.654 1.00 83.01  ? 28  PRO G CD  1 
ATOM   6859  N  N   . VAL G  1 35  ? 89.176  160.591 46.746 1.00 67.84  ? 29  VAL G N   1 
ATOM   6860  C  CA  . VAL G  1 35  ? 88.364  160.114 47.853 1.00 59.78  ? 29  VAL G CA  1 
ATOM   6861  C  C   . VAL G  1 35  ? 89.013  160.472 49.181 1.00 51.72  ? 29  VAL G C   1 
ATOM   6862  O  O   . VAL G  1 35  ? 90.166  160.132 49.434 1.00 43.54  ? 29  VAL G O   1 
ATOM   6863  C  CB  . VAL G  1 35  ? 88.172  158.591 47.812 1.00 61.69  ? 29  VAL G CB  1 
ATOM   6864  C  CG1 . VAL G  1 35  ? 87.177  158.176 48.893 1.00 59.99  ? 29  VAL G CG1 1 
ATOM   6865  C  CG2 . VAL G  1 35  ? 87.691  158.161 46.439 1.00 59.18  ? 29  VAL G CG2 1 
ATOM   6866  N  N   . LYS G  1 36  ? 88.271  161.183 50.018 1.00 52.76  ? 30  LYS G N   1 
ATOM   6867  C  CA  . LYS G  1 36  ? 88.763  161.557 51.332 1.00 59.83  ? 30  LYS G CA  1 
ATOM   6868  C  C   . LYS G  1 36  ? 88.502  160.362 52.249 1.00 60.05  ? 30  LYS G C   1 
ATOM   6869  O  O   . LYS G  1 36  ? 87.426  159.759 52.219 1.00 61.01  ? 30  LYS G O   1 
ATOM   6870  C  CB  . LYS G  1 36  ? 88.021  162.791 51.864 1.00 68.51  ? 30  LYS G CB  1 
ATOM   6871  C  CG  . LYS G  1 36  ? 88.279  164.089 51.097 1.00 80.41  ? 30  LYS G CG  1 
ATOM   6872  C  CD  . LYS G  1 36  ? 87.496  165.259 51.705 1.00 90.81  ? 30  LYS G CD  1 
ATOM   6873  C  CE  . LYS G  1 36  ? 87.759  166.575 50.970 1.00 95.30  ? 30  LYS G CE  1 
ATOM   6874  N  NZ  . LYS G  1 36  ? 87.019  167.728 51.575 1.00 94.63  ? 30  LYS G NZ  1 
ATOM   6875  N  N   . VAL G  1 37  ? 89.494  160.021 53.058 1.00 56.37  ? 31  VAL G N   1 
ATOM   6876  C  CA  . VAL G  1 37  ? 89.375  158.906 53.978 1.00 46.61  ? 31  VAL G CA  1 
ATOM   6877  C  C   . VAL G  1 37  ? 89.741  159.356 55.379 1.00 48.33  ? 31  VAL G C   1 
ATOM   6878  O  O   . VAL G  1 37  ? 90.900  159.675 55.650 1.00 43.09  ? 31  VAL G O   1 
ATOM   6879  C  CB  . VAL G  1 37  ? 90.320  157.785 53.577 1.00 49.29  ? 31  VAL G CB  1 
ATOM   6880  C  CG1 . VAL G  1 37  ? 90.046  156.563 54.415 1.00 53.01  ? 31  VAL G CG1 1 
ATOM   6881  C  CG2 . VAL G  1 37  ? 90.167  157.489 52.100 1.00 46.61  ? 31  VAL G CG2 1 
ATOM   6882  N  N   . TRP G  1 38  ? 88.762  159.397 56.274 1.00 46.61  ? 32  TRP G N   1 
ATOM   6883  C  CA  . TRP G  1 38  ? 89.054  159.806 57.643 1.00 48.63  ? 32  TRP G CA  1 
ATOM   6884  C  C   . TRP G  1 38  ? 88.324  158.963 58.672 1.00 52.51  ? 32  TRP G C   1 
ATOM   6885  O  O   . TRP G  1 38  ? 87.327  158.298 58.373 1.00 56.71  ? 32  TRP G O   1 
ATOM   6886  C  CB  . TRP G  1 38  ? 88.699  161.276 57.860 1.00 40.78  ? 32  TRP G CB  1 
ATOM   6887  C  CG  . TRP G  1 38  ? 87.225  161.540 57.960 1.00 47.98  ? 32  TRP G CG  1 
ATOM   6888  C  CD1 . TRP G  1 38  ? 86.506  161.793 59.100 1.00 49.84  ? 32  TRP G CD1 1 
ATOM   6889  C  CD2 . TRP G  1 38  ? 86.290  161.596 56.875 1.00 47.77  ? 32  TRP G CD2 1 
ATOM   6890  N  NE1 . TRP G  1 38  ? 85.179  162.010 58.786 1.00 53.50  ? 32  TRP G NE1 1 
ATOM   6891  C  CE2 . TRP G  1 38  ? 85.021  161.895 57.428 1.00 49.26  ? 32  TRP G CE2 1 
ATOM   6892  C  CE3 . TRP G  1 38  ? 86.401  161.423 55.488 1.00 49.73  ? 32  TRP G CE3 1 
ATOM   6893  C  CZ2 . TRP G  1 38  ? 83.873  162.026 56.640 1.00 56.36  ? 32  TRP G CZ2 1 
ATOM   6894  C  CZ3 . TRP G  1 38  ? 85.258  161.554 54.702 1.00 59.53  ? 32  TRP G CZ3 1 
ATOM   6895  C  CH2 . TRP G  1 38  ? 84.009  161.854 55.282 1.00 56.86  ? 32  TRP G CH2 1 
ATOM   6896  N  N   . GLY G  1 39  ? 88.832  159.009 59.895 1.00 49.30  ? 33  GLY G N   1 
ATOM   6897  C  CA  . GLY G  1 39  ? 88.238  158.264 60.977 1.00 47.50  ? 33  GLY G CA  1 
ATOM   6898  C  C   . GLY G  1 39  ? 89.325  157.977 61.976 1.00 48.49  ? 33  GLY G C   1 
ATOM   6899  O  O   . GLY G  1 39  ? 90.434  158.487 61.851 1.00 51.10  ? 33  GLY G O   1 
ATOM   6900  N  N   . SER G  1 40  ? 89.024  157.154 62.966 1.00 48.21  ? 34  SER G N   1 
ATOM   6901  C  CA  . SER G  1 40  ? 90.019  156.828 63.968 1.00 45.49  ? 34  SER G CA  1 
ATOM   6902  C  C   . SER G  1 40  ? 90.055  155.327 64.178 1.00 41.97  ? 34  SER G C   1 
ATOM   6903  O  O   . SER G  1 40  ? 89.087  154.628 63.888 1.00 43.31  ? 34  SER G O   1 
ATOM   6904  C  CB  . SER G  1 40  ? 89.690  157.540 65.278 1.00 39.55  ? 34  SER G CB  1 
ATOM   6905  O  OG  . SER G  1 40  ? 90.766  157.428 66.186 1.00 64.53  ? 34  SER G OG  1 
ATOM   6906  N  N   . ILE G  1 41  ? 91.183  154.836 64.673 1.00 36.03  ? 35  ILE G N   1 
ATOM   6907  C  CA  . ILE G  1 41  ? 91.361  153.419 64.935 1.00 34.63  ? 35  ILE G CA  1 
ATOM   6908  C  C   . ILE G  1 41  ? 92.089  153.301 66.272 1.00 39.74  ? 35  ILE G C   1 
ATOM   6909  O  O   . ILE G  1 41  ? 93.223  153.769 66.398 1.00 42.15  ? 35  ILE G O   1 
ATOM   6910  C  CB  . ILE G  1 41  ? 92.200  152.758 63.831 1.00 29.15  ? 35  ILE G CB  1 
ATOM   6911  C  CG1 . ILE G  1 41  ? 91.573  153.047 62.463 1.00 27.37  ? 35  ILE G CG1 1 
ATOM   6912  C  CG2 . ILE G  1 41  ? 92.273  151.263 64.064 1.00 28.78  ? 35  ILE G CG2 1 
ATOM   6913  C  CD1 . ILE G  1 41  ? 92.383  152.525 61.279 1.00 34.57  ? 35  ILE G CD1 1 
ATOM   6914  N  N   . LYS G  1 42  ? 91.431  152.709 67.275 1.00 38.98  ? 36  LYS G N   1 
ATOM   6915  C  CA  . LYS G  1 42  ? 92.038  152.549 68.598 1.00 36.91  ? 36  LYS G CA  1 
ATOM   6916  C  C   . LYS G  1 42  ? 92.512  151.116 68.802 1.00 31.69  ? 36  LYS G C   1 
ATOM   6917  O  O   . LYS G  1 42  ? 92.161  150.235 68.018 1.00 32.14  ? 36  LYS G O   1 
ATOM   6918  C  CB  . LYS G  1 42  ? 91.057  152.949 69.692 1.00 39.39  ? 36  LYS G CB  1 
ATOM   6919  C  CG  . LYS G  1 42  ? 89.847  152.060 69.792 1.00 61.43  ? 36  LYS G CG  1 
ATOM   6920  C  CD  . LYS G  1 42  ? 88.987  152.470 70.965 1.00 68.79  ? 36  LYS G CD  1 
ATOM   6921  C  CE  . LYS G  1 42  ? 88.192  151.290 71.494 1.00 71.89  ? 36  LYS G CE  1 
ATOM   6922  N  NZ  . LYS G  1 42  ? 87.560  151.662 72.786 1.00 81.39  ? 36  LYS G NZ  1 
ATOM   6923  N  N   . GLY G  1 43  ? 93.330  150.899 69.836 1.00 29.43  ? 37  GLY G N   1 
ATOM   6924  C  CA  . GLY G  1 43  ? 93.877  149.578 70.115 1.00 25.95  ? 37  GLY G CA  1 
ATOM   6925  C  C   . GLY G  1 43  ? 95.139  149.219 69.315 1.00 35.09  ? 37  GLY G C   1 
ATOM   6926  O  O   . GLY G  1 43  ? 95.598  148.065 69.332 1.00 30.09  ? 37  GLY G O   1 
ATOM   6927  N  N   . LEU G  1 44  ? 95.704  150.193 68.603 1.00 33.54  ? 38  LEU G N   1 
ATOM   6928  C  CA  . LEU G  1 44  ? 96.911  149.961 67.806 1.00 40.00  ? 38  LEU G CA  1 
ATOM   6929  C  C   . LEU G  1 44  ? 98.166  150.323 68.592 1.00 43.01  ? 38  LEU G C   1 
ATOM   6930  O  O   . LEU G  1 44  ? 98.197  151.358 69.255 1.00 41.32  ? 38  LEU G O   1 
ATOM   6931  C  CB  . LEU G  1 44  ? 96.882  150.814 66.539 1.00 38.75  ? 38  LEU G CB  1 
ATOM   6932  C  CG  . LEU G  1 44  ? 95.930  150.389 65.434 1.00 47.20  ? 38  LEU G CG  1 
ATOM   6933  C  CD1 . LEU G  1 44  ? 95.905  151.467 64.369 1.00 43.04  ? 38  LEU G CD1 1 
ATOM   6934  C  CD2 . LEU G  1 44  ? 96.374  149.045 64.861 1.00 41.99  ? 38  LEU G CD2 1 
ATOM   6935  N  N   . THR G  1 45  ? 99.201  149.486 68.513 1.00 43.96  ? 39  THR G N   1 
ATOM   6936  C  CA  . THR G  1 45  ? 100.447 149.789 69.223 1.00 46.10  ? 39  THR G CA  1 
ATOM   6937  C  C   . THR G  1 45  ? 101.070 151.006 68.553 1.00 46.89  ? 39  THR G C   1 
ATOM   6938  O  O   . THR G  1 45  ? 101.051 151.102 67.325 1.00 42.14  ? 39  THR G O   1 
ATOM   6939  C  CB  . THR G  1 45  ? 101.467 148.623 69.161 1.00 41.64  ? 39  THR G CB  1 
ATOM   6940  O  OG1 . THR G  1 45  ? 101.663 148.230 67.796 1.00 43.16  ? 39  THR G OG1 1 
ATOM   6941  C  CG2 . THR G  1 45  ? 100.984 147.436 69.997 1.00 22.64  ? 39  THR G CG2 1 
ATOM   6942  N  N   . GLU G  1 46  ? 101.605 151.931 69.355 1.00 48.49  ? 40  GLU G N   1 
ATOM   6943  C  CA  . GLU G  1 46  ? 102.226 153.147 68.823 1.00 52.08  ? 40  GLU G CA  1 
ATOM   6944  C  C   . GLU G  1 46  ? 103.193 152.825 67.684 1.00 47.53  ? 40  GLU G C   1 
ATOM   6945  O  O   . GLU G  1 46  ? 104.010 151.908 67.781 1.00 46.88  ? 40  GLU G O   1 
ATOM   6946  C  CB  . GLU G  1 46  ? 102.950 153.909 69.934 1.00 56.77  ? 40  GLU G CB  1 
ATOM   6947  C  CG  . GLU G  1 46  ? 103.699 155.127 69.431 1.00 57.08  ? 40  GLU G CG  1 
ATOM   6948  C  CD  . GLU G  1 46  ? 104.313 155.946 70.547 1.00 56.80  ? 40  GLU G CD  1 
ATOM   6949  O  OE1 . GLU G  1 46  ? 104.874 155.355 71.493 1.00 44.18  ? 40  GLU G OE1 1 
ATOM   6950  O  OE2 . GLU G  1 46  ? 104.246 157.188 70.466 1.00 63.65  ? 40  GLU G OE2 1 
ATOM   6951  N  N   . GLY G  1 47  ? 103.086 153.579 66.598 1.00 45.59  ? 41  GLY G N   1 
ATOM   6952  C  CA  . GLY G  1 47  ? 103.932 153.321 65.450 1.00 40.07  ? 41  GLY G CA  1 
ATOM   6953  C  C   . GLY G  1 47  ? 103.143 153.248 64.147 1.00 43.88  ? 41  GLY G C   1 
ATOM   6954  O  O   . GLY G  1 47  ? 101.965 153.615 64.087 1.00 36.39  ? 41  GLY G O   1 
ATOM   6955  N  N   . LEU G  1 48  ? 103.799 152.754 63.101 1.00 46.90  ? 42  LEU G N   1 
ATOM   6956  C  CA  . LEU G  1 48  ? 103.194 152.650 61.784 1.00 49.15  ? 42  LEU G CA  1 
ATOM   6957  C  C   . LEU G  1 48  ? 102.491 151.325 61.546 1.00 50.82  ? 42  LEU G C   1 
ATOM   6958  O  O   . LEU G  1 48  ? 102.977 150.264 61.946 1.00 49.03  ? 42  LEU G O   1 
ATOM   6959  C  CB  . LEU G  1 48  ? 104.259 152.874 60.707 1.00 47.14  ? 42  LEU G CB  1 
ATOM   6960  C  CG  . LEU G  1 48  ? 104.885 154.270 60.713 1.00 50.22  ? 42  LEU G CG  1 
ATOM   6961  C  CD1 . LEU G  1 48  ? 105.896 154.393 59.599 1.00 53.52  ? 42  LEU G CD1 1 
ATOM   6962  C  CD2 . LEU G  1 48  ? 103.798 155.309 60.550 1.00 47.78  ? 42  LEU G CD2 1 
ATOM   6963  N  N   . HIS G  1 49  ? 101.344 151.392 60.878 1.00 49.05  ? 43  HIS G N   1 
ATOM   6964  C  CA  . HIS G  1 49  ? 100.573 150.192 60.596 1.00 48.03  ? 43  HIS G CA  1 
ATOM   6965  C  C   . HIS G  1 49  ? 100.066 150.166 59.161 1.00 46.39  ? 43  HIS G C   1 
ATOM   6966  O  O   . HIS G  1 49  ? 99.468  151.139 58.687 1.00 41.12  ? 43  HIS G O   1 
ATOM   6967  C  CB  . HIS G  1 49  ? 99.390  150.108 61.565 1.00 42.15  ? 43  HIS G CB  1 
ATOM   6968  C  CG  . HIS G  1 49  ? 99.787  149.874 62.989 1.00 38.75  ? 43  HIS G CG  1 
ATOM   6969  N  ND1 . HIS G  1 49  ? 100.099 148.622 63.479 1.00 33.80  ? 43  HIS G ND1 1 
ATOM   6970  C  CD2 . HIS G  1 49  ? 99.920  150.731 64.031 1.00 34.54  ? 43  HIS G CD2 1 
ATOM   6971  C  CE1 . HIS G  1 49  ? 100.402 148.717 64.762 1.00 33.35  ? 43  HIS G CE1 1 
ATOM   6972  N  NE2 . HIS G  1 49  ? 100.302 149.987 65.122 1.00 32.67  ? 43  HIS G NE2 1 
ATOM   6973  N  N   . GLY G  1 50  ? 100.315 149.049 58.477 1.00 49.68  ? 44  GLY G N   1 
ATOM   6974  C  CA  . GLY G  1 50  ? 99.857  148.890 57.107 1.00 48.26  ? 44  GLY G CA  1 
ATOM   6975  C  C   . GLY G  1 50  ? 98.366  149.167 57.033 1.00 51.69  ? 44  GLY G C   1 
ATOM   6976  O  O   . GLY G  1 50  ? 97.617  148.811 57.939 1.00 48.56  ? 44  GLY G O   1 
ATOM   6977  N  N   . PHE G  1 51  ? 97.936  149.800 55.951 1.00 47.95  ? 45  PHE G N   1 
ATOM   6978  C  CA  . PHE G  1 51  ? 96.536  150.159 55.755 1.00 47.20  ? 45  PHE G CA  1 
ATOM   6979  C  C   . PHE G  1 51  ? 96.230  149.821 54.283 1.00 52.70  ? 45  PHE G C   1 
ATOM   6980  O  O   . PHE G  1 51  ? 96.749  150.463 53.362 1.00 51.53  ? 45  PHE G O   1 
ATOM   6981  C  CB  . PHE G  1 51  ? 96.398  151.659 56.040 1.00 42.03  ? 45  PHE G CB  1 
ATOM   6982  C  CG  . PHE G  1 51  ? 95.006  152.121 56.339 1.00 32.65  ? 45  PHE G CG  1 
ATOM   6983  C  CD1 . PHE G  1 51  ? 94.263  151.542 57.351 1.00 35.15  ? 45  PHE G CD1 1 
ATOM   6984  C  CD2 . PHE G  1 51  ? 94.466  153.204 55.649 1.00 32.44  ? 45  PHE G CD2 1 
ATOM   6985  C  CE1 . PHE G  1 51  ? 92.994  152.042 57.678 1.00 40.27  ? 45  PHE G CE1 1 
ATOM   6986  C  CE2 . PHE G  1 51  ? 93.213  153.709 55.963 1.00 26.40  ? 45  PHE G CE2 1 
ATOM   6987  C  CZ  . PHE G  1 51  ? 92.470  153.131 56.979 1.00 32.69  ? 45  PHE G CZ  1 
ATOM   6988  N  N   . HIS G  1 52  ? 95.413  148.790 54.065 1.00 51.26  ? 46  HIS G N   1 
ATOM   6989  C  CA  . HIS G  1 52  ? 95.082  148.356 52.709 1.00 48.62  ? 46  HIS G CA  1 
ATOM   6990  C  C   . HIS G  1 52  ? 93.626  147.965 52.493 1.00 46.11  ? 46  HIS G C   1 
ATOM   6991  O  O   . HIS G  1 52  ? 92.905  147.614 53.424 1.00 43.50  ? 46  HIS G O   1 
ATOM   6992  C  CB  . HIS G  1 52  ? 95.920  147.134 52.304 1.00 48.00  ? 46  HIS G CB  1 
ATOM   6993  C  CG  . HIS G  1 52  ? 97.337  147.169 52.778 1.00 56.98  ? 46  HIS G CG  1 
ATOM   6994  N  ND1 . HIS G  1 52  ? 97.837  146.262 53.687 1.00 59.11  ? 46  HIS G ND1 1 
ATOM   6995  C  CD2 . HIS G  1 52  ? 98.367  147.986 52.456 1.00 55.07  ? 46  HIS G CD2 1 
ATOM   6996  C  CE1 . HIS G  1 52  ? 99.113  146.517 53.905 1.00 56.03  ? 46  HIS G CE1 1 
ATOM   6997  N  NE2 . HIS G  1 52  ? 99.459  147.558 53.170 1.00 56.13  ? 46  HIS G NE2 1 
ATOM   6998  N  N   . VAL G  1 53  ? 93.210  148.012 51.234 1.00 41.93  ? 47  VAL G N   1 
ATOM   6999  C  CA  . VAL G  1 53  ? 91.872  147.588 50.855 1.00 39.44  ? 47  VAL G CA  1 
ATOM   7000  C  C   . VAL G  1 53  ? 92.130  146.256 50.175 1.00 38.75  ? 47  VAL G C   1 
ATOM   7001  O  O   . VAL G  1 53  ? 92.718  146.222 49.097 1.00 39.20  ? 47  VAL G O   1 
ATOM   7002  C  CB  . VAL G  1 53  ? 91.230  148.536 49.832 1.00 42.22  ? 47  VAL G CB  1 
ATOM   7003  C  CG1 . VAL G  1 53  ? 89.919  147.955 49.356 1.00 42.56  ? 47  VAL G CG1 1 
ATOM   7004  C  CG2 . VAL G  1 53  ? 91.011  149.899 50.449 1.00 35.39  ? 47  VAL G CG2 1 
ATOM   7005  N  N   . HIS G  1 54  ? 91.742  145.155 50.809 1.00 36.50  ? 48  HIS G N   1 
ATOM   7006  C  CA  . HIS G  1 54  ? 91.962  143.858 50.189 1.00 36.01  ? 48  HIS G CA  1 
ATOM   7007  C  C   . HIS G  1 54  ? 90.807  143.549 49.241 1.00 39.67  ? 48  HIS G C   1 
ATOM   7008  O  O   . HIS G  1 54  ? 89.735  144.159 49.319 1.00 34.91  ? 48  HIS G O   1 
ATOM   7009  C  CB  . HIS G  1 54  ? 92.125  142.772 51.251 1.00 32.63  ? 48  HIS G CB  1 
ATOM   7010  C  CG  . HIS G  1 54  ? 93.376  142.912 52.064 1.00 32.26  ? 48  HIS G CG  1 
ATOM   7011  N  ND1 . HIS G  1 54  ? 94.282  141.883 52.224 1.00 37.91  ? 48  HIS G ND1 1 
ATOM   7012  C  CD2 . HIS G  1 54  ? 93.864  143.955 52.779 1.00 28.72  ? 48  HIS G CD2 1 
ATOM   7013  C  CE1 . HIS G  1 54  ? 95.272  142.283 53.005 1.00 34.61  ? 48  HIS G CE1 1 
ATOM   7014  N  NE2 . HIS G  1 54  ? 95.042  143.537 53.356 1.00 37.97  ? 48  HIS G NE2 1 
ATOM   7015  N  N   . GLU G  1 55  ? 91.038  142.600 48.344 1.00 41.15  ? 49  GLU G N   1 
ATOM   7016  C  CA  . GLU G  1 55  ? 90.065  142.221 47.327 1.00 44.81  ? 49  GLU G CA  1 
ATOM   7017  C  C   . GLU G  1 55  ? 88.640  141.834 47.730 1.00 43.56  ? 49  GLU G C   1 
ATOM   7018  O  O   . GLU G  1 55  ? 87.672  142.375 47.189 1.00 41.62  ? 49  GLU G O   1 
ATOM   7019  C  CB  . GLU G  1 55  ? 90.641  141.092 46.470 1.00 46.95  ? 49  GLU G CB  1 
ATOM   7020  C  CG  . GLU G  1 55  ? 89.798  140.770 45.244 1.00 56.25  ? 49  GLU G CG  1 
ATOM   7021  C  CD  . GLU G  1 55  ? 90.433  139.715 44.361 1.00 61.98  ? 49  GLU G CD  1 
ATOM   7022  O  OE1 . GLU G  1 55  ? 89.897  139.467 43.256 1.00 63.84  ? 49  GLU G OE1 1 
ATOM   7023  O  OE2 . GLU G  1 55  ? 91.463  139.133 44.773 1.00 56.91  ? 49  GLU G OE2 1 
ATOM   7024  N  N   . PHE G  1 56  ? 88.507  140.897 48.661 1.00 42.68  ? 50  PHE G N   1 
ATOM   7025  C  CA  . PHE G  1 56  ? 87.188  140.415 49.053 1.00 42.99  ? 50  PHE G CA  1 
ATOM   7026  C  C   . PHE G  1 56  ? 86.565  140.943 50.332 1.00 44.36  ? 50  PHE G C   1 
ATOM   7027  O  O   . PHE G  1 56  ? 87.232  141.074 51.367 1.00 47.94  ? 50  PHE G O   1 
ATOM   7028  C  CB  . PHE G  1 56  ? 87.208  138.893 49.151 1.00 42.06  ? 50  PHE G CB  1 
ATOM   7029  C  CG  . PHE G  1 56  ? 87.790  138.217 47.955 1.00 45.19  ? 50  PHE G CG  1 
ATOM   7030  C  CD1 . PHE G  1 56  ? 87.219  138.391 46.692 1.00 42.11  ? 50  PHE G CD1 1 
ATOM   7031  C  CD2 . PHE G  1 56  ? 88.912  137.394 48.087 1.00 40.28  ? 50  PHE G CD2 1 
ATOM   7032  C  CE1 . PHE G  1 56  ? 87.761  137.753 45.571 1.00 42.99  ? 50  PHE G CE1 1 
ATOM   7033  C  CE2 . PHE G  1 56  ? 89.457  136.753 46.979 1.00 39.07  ? 50  PHE G CE2 1 
ATOM   7034  C  CZ  . PHE G  1 56  ? 88.879  136.934 45.714 1.00 42.19  ? 50  PHE G CZ  1 
ATOM   7035  N  N   . GLY G  1 57  ? 85.268  141.230 50.243 1.00 39.06  ? 51  GLY G N   1 
ATOM   7036  C  CA  . GLY G  1 57  ? 84.506  141.669 51.396 1.00 35.16  ? 51  GLY G CA  1 
ATOM   7037  C  C   . GLY G  1 57  ? 83.941  140.382 51.993 1.00 39.11  ? 51  GLY G C   1 
ATOM   7038  O  O   . GLY G  1 57  ? 82.753  140.279 52.304 1.00 35.89  ? 51  GLY G O   1 
ATOM   7039  N  N   . ASP G  1 58  ? 84.810  139.381 52.111 1.00 34.11  ? 52  ASP G N   1 
ATOM   7040  C  CA  . ASP G  1 58  ? 84.446  138.081 52.648 1.00 38.94  ? 52  ASP G CA  1 
ATOM   7041  C  C   . ASP G  1 58  ? 85.062  137.935 54.032 1.00 38.34  ? 52  ASP G C   1 
ATOM   7042  O  O   . ASP G  1 58  ? 86.268  137.746 54.169 1.00 40.73  ? 52  ASP G O   1 
ATOM   7043  C  CB  . ASP G  1 58  ? 84.952  136.971 51.716 1.00 38.48  ? 52  ASP G CB  1 
ATOM   7044  C  CG  . ASP G  1 58  ? 84.703  135.572 52.270 1.00 38.74  ? 52  ASP G CG  1 
ATOM   7045  O  OD1 . ASP G  1 58  ? 84.824  134.599 51.489 1.00 38.05  ? 52  ASP G OD1 1 
ATOM   7046  O  OD2 . ASP G  1 58  ? 84.396  135.442 53.478 1.00 34.13  ? 52  ASP G OD2 1 
ATOM   7047  N  N   . ASN G  1 59  ? 84.219  138.019 55.051 1.00 31.10  ? 53  ASN G N   1 
ATOM   7048  C  CA  . ASN G  1 59  ? 84.667  137.929 56.433 1.00 35.41  ? 53  ASN G CA  1 
ATOM   7049  C  C   . ASN G  1 59  ? 84.333  136.575 57.085 1.00 35.40  ? 53  ASN G C   1 
ATOM   7050  O  O   . ASN G  1 59  ? 84.365  136.442 58.307 1.00 36.50  ? 53  ASN G O   1 
ATOM   7051  C  CB  . ASN G  1 59  ? 84.017  139.069 57.225 1.00 39.58  ? 53  ASN G CB  1 
ATOM   7052  C  CG  . ASN G  1 59  ? 84.402  139.062 58.693 1.00 60.23  ? 53  ASN G CG  1 
ATOM   7053  O  OD1 . ASN G  1 59  ? 83.637  139.513 59.554 1.00 65.57  ? 53  ASN G OD1 1 
ATOM   7054  N  ND2 . ASN G  1 59  ? 85.594  138.558 58.988 1.00 67.63  ? 53  ASN G ND2 1 
ATOM   7055  N  N   . THR G  1 60  ? 84.021  135.567 56.279 1.00 29.09  ? 54  THR G N   1 
ATOM   7056  C  CA  . THR G  1 60  ? 83.661  134.270 56.834 1.00 31.13  ? 54  THR G CA  1 
ATOM   7057  C  C   . THR G  1 60  ? 84.792  133.583 57.582 1.00 41.18  ? 54  THR G C   1 
ATOM   7058  O  O   . THR G  1 60  ? 84.544  132.700 58.405 1.00 40.55  ? 54  THR G O   1 
ATOM   7059  C  CB  . THR G  1 60  ? 83.141  133.316 55.754 1.00 31.91  ? 54  THR G CB  1 
ATOM   7060  O  OG1 . THR G  1 60  ? 84.161  133.093 54.768 1.00 26.87  ? 54  THR G OG1 1 
ATOM   7061  C  CG2 . THR G  1 60  ? 81.893  133.904 55.094 1.00 27.97  ? 54  THR G CG2 1 
ATOM   7062  N  N   . ALA G  1 61  ? 86.034  133.972 57.296 1.00 41.80  ? 55  ALA G N   1 
ATOM   7063  C  CA  . ALA G  1 61  ? 87.184  133.391 57.991 1.00 38.77  ? 55  ALA G CA  1 
ATOM   7064  C  C   . ALA G  1 61  ? 88.092  134.513 58.537 1.00 38.93  ? 55  ALA G C   1 
ATOM   7065  O  O   . ALA G  1 61  ? 89.269  134.611 58.193 1.00 40.57  ? 55  ALA G O   1 
ATOM   7066  C  CB  . ALA G  1 61  ? 87.950  132.474 57.049 1.00 29.17  ? 55  ALA G CB  1 
ATOM   7067  N  N   . GLY G  1 62  ? 87.521  135.352 59.398 1.00 36.12  ? 56  GLY G N   1 
ATOM   7068  C  CA  . GLY G  1 62  ? 88.256  136.463 59.961 1.00 36.79  ? 56  GLY G CA  1 
ATOM   7069  C  C   . GLY G  1 62  ? 88.697  137.354 58.817 1.00 40.98  ? 56  GLY G C   1 
ATOM   7070  O  O   . GLY G  1 62  ? 88.024  137.411 57.783 1.00 40.52  ? 56  GLY G O   1 
ATOM   7071  N  N   . CYS G  1 63  ? 89.828  138.034 58.989 1.00 38.69  ? 57  CYS G N   1 
ATOM   7072  C  CA  . CYS G  1 63  ? 90.362  138.905 57.953 1.00 34.32  ? 57  CYS G CA  1 
ATOM   7073  C  C   . CYS G  1 63  ? 91.141  138.109 56.914 1.00 35.66  ? 57  CYS G C   1 
ATOM   7074  O  O   . CYS G  1 63  ? 91.538  138.638 55.880 1.00 31.75  ? 57  CYS G O   1 
ATOM   7075  C  CB  . CYS G  1 63  ? 91.272  139.957 58.572 1.00 32.79  ? 57  CYS G CB  1 
ATOM   7076  S  SG  . CYS G  1 63  ? 90.432  140.955 59.834 1.00 37.32  ? 57  CYS G SG  1 
ATOM   7077  N  N   . THR G  1 64  ? 91.346  136.827 57.167 1.00 31.24  ? 58  THR G N   1 
ATOM   7078  C  CA  . THR G  1 64  ? 92.104  136.038 56.216 1.00 39.90  ? 58  THR G CA  1 
ATOM   7079  C  C   . THR G  1 64  ? 91.365  135.812 54.913 1.00 45.14  ? 58  THR G C   1 
ATOM   7080  O  O   . THR G  1 64  ? 91.992  135.727 53.846 1.00 44.44  ? 58  THR G O   1 
ATOM   7081  C  CB  . THR G  1 64  ? 92.492  134.689 56.807 1.00 36.21  ? 58  THR G CB  1 
ATOM   7082  O  OG1 . THR G  1 64  ? 93.321  134.908 57.951 1.00 43.07  ? 58  THR G OG1 1 
ATOM   7083  C  CG2 . THR G  1 64  ? 93.247  133.851 55.781 1.00 35.95  ? 58  THR G CG2 1 
ATOM   7084  N  N   . SER G  1 65  ? 90.038  135.713 54.991 1.00 44.52  ? 59  SER G N   1 
ATOM   7085  C  CA  . SER G  1 65  ? 89.244  135.485 53.790 1.00 38.30  ? 59  SER G CA  1 
ATOM   7086  C  C   . SER G  1 65  ? 89.071  136.754 52.959 1.00 36.58  ? 59  SER G C   1 
ATOM   7087  O  O   . SER G  1 65  ? 88.396  136.744 51.929 1.00 36.53  ? 59  SER G O   1 
ATOM   7088  C  CB  . SER G  1 65  ? 87.884  134.864 54.144 1.00 36.88  ? 59  SER G CB  1 
ATOM   7089  O  OG  . SER G  1 65  ? 87.207  135.569 55.171 1.00 40.12  ? 59  SER G OG  1 
ATOM   7090  N  N   . ALA G  1 66  ? 89.689  137.848 53.398 1.00 36.21  ? 60  ALA G N   1 
ATOM   7091  C  CA  . ALA G  1 66  ? 89.618  139.094 52.638 1.00 34.27  ? 60  ALA G CA  1 
ATOM   7092  C  C   . ALA G  1 66  ? 90.567  138.988 51.440 1.00 35.74  ? 60  ALA G C   1 
ATOM   7093  O  O   . ALA G  1 66  ? 90.534  139.816 50.527 1.00 35.28  ? 60  ALA G O   1 
ATOM   7094  C  CB  . ALA G  1 66  ? 90.004  140.266 53.505 1.00 22.27  ? 60  ALA G CB  1 
ATOM   7095  N  N   . GLY G  1 67  ? 91.421  137.964 51.455 1.00 37.54  ? 61  GLY G N   1 
ATOM   7096  C  CA  . GLY G  1 67  ? 92.344  137.758 50.356 1.00 35.86  ? 61  GLY G CA  1 
ATOM   7097  C  C   . GLY G  1 67  ? 93.484  138.753 50.261 1.00 42.26  ? 61  GLY G C   1 
ATOM   7098  O  O   . GLY G  1 67  ? 93.805  139.437 51.238 1.00 34.94  ? 61  GLY G O   1 
ATOM   7099  N  N   . PRO G  1 68  ? 94.117  138.851 49.078 1.00 47.46  ? 62  PRO G N   1 
ATOM   7100  C  CA  . PRO G  1 68  ? 95.240  139.743 48.777 1.00 50.47  ? 62  PRO G CA  1 
ATOM   7101  C  C   . PRO G  1 68  ? 94.837  141.207 48.654 1.00 48.75  ? 62  PRO G C   1 
ATOM   7102  O  O   . PRO G  1 68  ? 93.655  141.537 48.674 1.00 52.89  ? 62  PRO G O   1 
ATOM   7103  C  CB  . PRO G  1 68  ? 95.767  139.180 47.462 1.00 54.44  ? 62  PRO G CB  1 
ATOM   7104  C  CG  . PRO G  1 68  ? 94.519  138.756 46.781 1.00 51.97  ? 62  PRO G CG  1 
ATOM   7105  C  CD  . PRO G  1 68  ? 93.782  138.036 47.894 1.00 51.31  ? 62  PRO G CD  1 
ATOM   7106  N  N   . HIS G  1 69  ? 95.829  142.081 48.536 1.00 49.11  ? 63  HIS G N   1 
ATOM   7107  C  CA  . HIS G  1 69  ? 95.577  143.509 48.399 1.00 52.05  ? 63  HIS G CA  1 
ATOM   7108  C  C   . HIS G  1 69  ? 94.809  143.696 47.089 1.00 50.22  ? 63  HIS G C   1 
ATOM   7109  O  O   . HIS G  1 69  ? 95.065  142.982 46.117 1.00 43.32  ? 63  HIS G O   1 
ATOM   7110  C  CB  . HIS G  1 69  ? 96.911  144.276 48.362 1.00 53.05  ? 63  HIS G CB  1 
ATOM   7111  C  CG  . HIS G  1 69  ? 97.654  144.292 49.668 1.00 61.64  ? 63  HIS G CG  1 
ATOM   7112  N  ND1 . HIS G  1 69  ? 98.941  144.774 49.785 1.00 64.64  ? 63  HIS G ND1 1 
ATOM   7113  C  CD2 . HIS G  1 69  ? 97.287  143.908 50.915 1.00 70.83  ? 63  HIS G CD2 1 
ATOM   7114  C  CE1 . HIS G  1 69  ? 99.333  144.687 51.044 1.00 68.17  ? 63  HIS G CE1 1 
ATOM   7115  N  NE2 . HIS G  1 69  ? 98.348  144.165 51.751 1.00 74.91  ? 63  HIS G NE2 1 
ATOM   7116  N  N   . PHE G  1 70  ? 93.862  144.631 47.057 1.00 48.97  ? 64  PHE G N   1 
ATOM   7117  C  CA  . PHE G  1 70  ? 93.091  144.852 45.838 1.00 57.00  ? 64  PHE G CA  1 
ATOM   7118  C  C   . PHE G  1 70  ? 94.029  145.252 44.695 1.00 64.18  ? 64  PHE G C   1 
ATOM   7119  O  O   . PHE G  1 70  ? 94.577  146.361 44.676 1.00 59.58  ? 64  PHE G O   1 
ATOM   7120  C  CB  . PHE G  1 70  ? 92.034  145.941 46.039 1.00 58.24  ? 64  PHE G CB  1 
ATOM   7121  C  CG  . PHE G  1 70  ? 91.071  146.065 44.887 1.00 61.21  ? 64  PHE G CG  1 
ATOM   7122  C  CD1 . PHE G  1 70  ? 90.453  147.279 44.605 1.00 66.09  ? 64  PHE G CD1 1 
ATOM   7123  C  CD2 . PHE G  1 70  ? 90.799  144.970 44.068 1.00 58.79  ? 64  PHE G CD2 1 
ATOM   7124  C  CE1 . PHE G  1 70  ? 89.579  147.404 43.514 1.00 65.87  ? 64  PHE G CE1 1 
ATOM   7125  C  CE2 . PHE G  1 70  ? 89.934  145.085 42.984 1.00 61.68  ? 64  PHE G CE2 1 
ATOM   7126  C  CZ  . PHE G  1 70  ? 89.323  146.305 42.706 1.00 63.45  ? 64  PHE G CZ  1 
ATOM   7127  N  N   . ASN G  1 71  ? 94.193  144.345 43.736 1.00 65.01  ? 65  ASN G N   1 
ATOM   7128  C  CA  . ASN G  1 71  ? 95.084  144.584 42.618 1.00 67.55  ? 65  ASN G CA  1 
ATOM   7129  C  C   . ASN G  1 71  ? 94.487  144.280 41.239 1.00 72.00  ? 65  ASN G C   1 
ATOM   7130  O  O   . ASN G  1 71  ? 94.795  143.257 40.615 1.00 64.80  ? 65  ASN G O   1 
ATOM   7131  C  CB  . ASN G  1 71  ? 96.349  143.770 42.831 1.00 67.63  ? 65  ASN G CB  1 
ATOM   7132  C  CG  . ASN G  1 71  ? 97.452  144.179 41.907 1.00 67.58  ? 65  ASN G CG  1 
ATOM   7133  O  OD1 . ASN G  1 71  ? 97.499  145.325 41.441 1.00 64.07  ? 65  ASN G OD1 1 
ATOM   7134  N  ND2 . ASN G  1 71  ? 98.368  143.256 41.647 1.00 62.78  ? 65  ASN G ND2 1 
ATOM   7135  N  N   . PRO G  1 72  ? 93.631  145.182 40.740 1.00 74.21  ? 66  PRO G N   1 
ATOM   7136  C  CA  . PRO G  1 72  ? 92.980  145.034 39.439 1.00 79.58  ? 66  PRO G CA  1 
ATOM   7137  C  C   . PRO G  1 72  ? 93.875  145.365 38.242 1.00 85.43  ? 66  PRO G C   1 
ATOM   7138  O  O   . PRO G  1 72  ? 93.410  145.357 37.102 1.00 88.30  ? 66  PRO G O   1 
ATOM   7139  C  CB  . PRO G  1 72  ? 91.796  145.985 39.549 1.00 79.19  ? 66  PRO G CB  1 
ATOM   7140  C  CG  . PRO G  1 72  ? 92.363  147.097 40.358 1.00 80.51  ? 66  PRO G CG  1 
ATOM   7141  C  CD  . PRO G  1 72  ? 93.120  146.369 41.448 1.00 74.96  ? 66  PRO G CD  1 
ATOM   7142  N  N   . LEU G  1 73  ? 95.152  145.652 38.496 1.00 88.90  ? 67  LEU G N   1 
ATOM   7143  C  CA  . LEU G  1 73  ? 96.089  145.984 37.423 1.00 87.33  ? 67  LEU G CA  1 
ATOM   7144  C  C   . LEU G  1 73  ? 97.371  145.156 37.515 1.00 88.26  ? 67  LEU G C   1 
ATOM   7145  O  O   . LEU G  1 73  ? 98.401  145.524 36.951 1.00 86.45  ? 67  LEU G O   1 
ATOM   7146  C  CB  . LEU G  1 73  ? 96.431  147.474 37.470 1.00 87.23  ? 67  LEU G CB  1 
ATOM   7147  C  CG  . LEU G  1 73  ? 95.239  148.429 37.595 1.00 87.88  ? 67  LEU G CG  1 
ATOM   7148  C  CD1 . LEU G  1 73  ? 95.726  149.866 37.592 1.00 88.29  ? 67  LEU G CD1 1 
ATOM   7149  C  CD2 . LEU G  1 73  ? 94.271  148.198 36.456 1.00 90.06  ? 67  LEU G CD2 1 
ATOM   7150  N  N   . SER G  1 74  ? 97.292  144.039 38.234 1.00 88.67  ? 68  SER G N   1 
ATOM   7151  C  CA  . SER G  1 74  ? 98.417  143.121 38.429 1.00 87.89  ? 68  SER G CA  1 
ATOM   7152  C  C   . SER G  1 74  ? 99.786  143.755 38.674 1.00 88.97  ? 68  SER G C   1 
ATOM   7153  O  O   . SER G  1 74  ? 100.813 143.085 38.538 1.00 83.27  ? 68  SER G O   1 
ATOM   7154  C  CB  . SER G  1 74  ? 98.513  142.150 37.251 1.00 86.71  ? 68  SER G CB  1 
ATOM   7155  O  OG  . SER G  1 74  ? 97.393  141.285 37.224 1.00 83.42  ? 68  SER G OG  1 
ATOM   7156  N  N   . ARG G  1 75  ? 99.802  145.034 39.045 1.00 90.55  ? 69  ARG G N   1 
ATOM   7157  C  CA  . ARG G  1 75  ? 101.052 145.736 39.332 1.00 92.12  ? 69  ARG G CA  1 
ATOM   7158  C  C   . ARG G  1 75  ? 101.552 145.341 40.721 1.00 88.07  ? 69  ARG G C   1 
ATOM   7159  O  O   . ARG G  1 75  ? 100.822 144.723 41.489 1.00 89.73  ? 69  ARG G O   1 
ATOM   7160  C  CB  . ARG G  1 75  ? 100.838 147.248 39.258 1.00 98.00  ? 69  ARG G CB  1 
ATOM   7161  C  CG  . ARG G  1 75  ? 100.514 147.743 37.861 1.00 105.08 ? 69  ARG G CG  1 
ATOM   7162  C  CD  . ARG G  1 75  ? 100.158 149.214 37.860 1.00 108.22 ? 69  ARG G CD  1 
ATOM   7163  N  NE  . ARG G  1 75  ? 99.625  149.620 36.566 1.00 114.65 ? 69  ARG G NE  1 
ATOM   7164  C  CZ  . ARG G  1 75  ? 98.981  150.762 36.349 1.00 116.95 ? 69  ARG G CZ  1 
ATOM   7165  N  NH1 . ARG G  1 75  ? 98.791  151.618 37.347 1.00 117.55 ? 69  ARG G NH1 1 
ATOM   7166  N  NH2 . ARG G  1 75  ? 98.514  151.039 35.139 1.00 116.30 ? 69  ARG G NH2 1 
ATOM   7167  N  N   . LYS G  1 76  ? 102.792 145.691 41.047 1.00 83.13  ? 70  LYS G N   1 
ATOM   7168  C  CA  . LYS G  1 76  ? 103.348 145.333 42.344 1.00 76.79  ? 70  LYS G CA  1 
ATOM   7169  C  C   . LYS G  1 76  ? 103.001 146.327 43.448 1.00 72.91  ? 70  LYS G C   1 
ATOM   7170  O  O   . LYS G  1 76  ? 102.604 147.459 43.181 1.00 68.94  ? 70  LYS G O   1 
ATOM   7171  C  CB  . LYS G  1 76  ? 104.865 145.167 42.237 1.00 79.25  ? 70  LYS G CB  1 
ATOM   7172  C  CG  . LYS G  1 76  ? 105.295 144.027 41.322 1.00 78.94  ? 70  LYS G CG  1 
ATOM   7173  C  CD  . LYS G  1 76  ? 106.801 143.791 41.380 1.00 84.15  ? 70  LYS G CD  1 
ATOM   7174  C  CE  . LYS G  1 76  ? 107.585 145.024 40.940 1.00 89.69  ? 70  LYS G CE  1 
ATOM   7175  N  NZ  . LYS G  1 76  ? 109.058 144.896 41.159 1.00 87.60  ? 70  LYS G NZ  1 
ATOM   7176  N  N   . HIS G  1 77  ? 103.150 145.880 44.692 1.00 70.95  ? 71  HIS G N   1 
ATOM   7177  C  CA  . HIS G  1 77  ? 102.845 146.686 45.871 1.00 69.33  ? 71  HIS G CA  1 
ATOM   7178  C  C   . HIS G  1 77  ? 103.652 147.981 45.923 1.00 70.62  ? 71  HIS G C   1 
ATOM   7179  O  O   . HIS G  1 77  ? 104.810 148.014 45.519 1.00 75.50  ? 71  HIS G O   1 
ATOM   7180  C  CB  . HIS G  1 77  ? 103.105 145.851 47.133 1.00 68.39  ? 71  HIS G CB  1 
ATOM   7181  C  CG  . HIS G  1 77  ? 102.829 146.578 48.413 1.00 71.05  ? 71  HIS G CG  1 
ATOM   7182  N  ND1 . HIS G  1 77  ? 101.575 147.030 48.760 1.00 70.47  ? 71  HIS G ND1 1 
ATOM   7183  C  CD2 . HIS G  1 77  ? 103.652 146.946 49.423 1.00 72.53  ? 71  HIS G CD2 1 
ATOM   7184  C  CE1 . HIS G  1 77  ? 101.637 147.647 49.926 1.00 68.71  ? 71  HIS G CE1 1 
ATOM   7185  N  NE2 . HIS G  1 77  ? 102.887 147.609 50.350 1.00 71.15  ? 71  HIS G NE2 1 
ATOM   7186  N  N   . GLY G  1 78  ? 103.034 149.044 46.428 1.00 69.74  ? 72  GLY G N   1 
ATOM   7187  C  CA  . GLY G  1 78  ? 103.707 150.328 46.532 1.00 67.22  ? 72  GLY G CA  1 
ATOM   7188  C  C   . GLY G  1 78  ? 103.001 151.256 47.505 1.00 66.18  ? 72  GLY G C   1 
ATOM   7189  O  O   . GLY G  1 78  ? 102.024 150.860 48.130 1.00 69.60  ? 72  GLY G O   1 
ATOM   7190  N  N   . GLY G  1 79  ? 103.493 152.484 47.643 1.00 65.39  ? 73  GLY G N   1 
ATOM   7191  C  CA  . GLY G  1 79  ? 102.874 153.440 48.545 1.00 61.91  ? 73  GLY G CA  1 
ATOM   7192  C  C   . GLY G  1 79  ? 101.678 154.121 47.903 1.00 64.03  ? 73  GLY G C   1 
ATOM   7193  O  O   . GLY G  1 79  ? 101.492 154.039 46.689 1.00 62.87  ? 73  GLY G O   1 
ATOM   7194  N  N   . PRO G  1 80  ? 100.846 154.813 48.687 1.00 64.89  ? 74  PRO G N   1 
ATOM   7195  C  CA  . PRO G  1 80  ? 99.669  155.494 48.136 1.00 71.33  ? 74  PRO G CA  1 
ATOM   7196  C  C   . PRO G  1 80  ? 99.934  156.497 47.009 1.00 75.01  ? 74  PRO G C   1 
ATOM   7197  O  O   . PRO G  1 80  ? 99.025  156.838 46.253 1.00 74.94  ? 74  PRO G O   1 
ATOM   7198  C  CB  . PRO G  1 80  ? 99.045  156.159 49.366 1.00 67.35  ? 74  PRO G CB  1 
ATOM   7199  C  CG  . PRO G  1 80  ? 100.231 156.401 50.256 1.00 68.68  ? 74  PRO G CG  1 
ATOM   7200  C  CD  . PRO G  1 80  ? 100.996 155.106 50.122 1.00 65.83  ? 74  PRO G CD  1 
ATOM   7201  N  N   . LYS G  1 81  ? 101.168 156.972 46.888 1.00 80.14  ? 75  LYS G N   1 
ATOM   7202  C  CA  . LYS G  1 81  ? 101.471 157.943 45.843 1.00 83.64  ? 75  LYS G CA  1 
ATOM   7203  C  C   . LYS G  1 81  ? 102.432 157.423 44.778 1.00 85.03  ? 75  LYS G C   1 
ATOM   7204  O  O   . LYS G  1 81  ? 102.944 158.199 43.978 1.00 86.61  ? 75  LYS G O   1 
ATOM   7205  C  CB  . LYS G  1 81  ? 102.036 159.231 46.461 1.00 83.88  ? 75  LYS G CB  1 
ATOM   7206  C  CG  . LYS G  1 81  ? 101.112 159.928 47.464 1.00 82.47  ? 75  LYS G CG  1 
ATOM   7207  C  CD  . LYS G  1 81  ? 99.803  160.397 46.828 1.00 82.95  ? 75  LYS G CD  1 
ATOM   7208  C  CE  . LYS G  1 81  ? 98.898  161.083 47.853 1.00 79.67  ? 75  LYS G CE  1 
ATOM   7209  N  NZ  . LYS G  1 81  ? 97.577  161.482 47.279 1.00 76.17  ? 75  LYS G NZ  1 
ATOM   7210  N  N   . ASP G  1 82  ? 102.677 156.117 44.760 1.00 87.97  ? 76  ASP G N   1 
ATOM   7211  C  CA  . ASP G  1 82  ? 103.578 155.544 43.764 1.00 88.10  ? 76  ASP G CA  1 
ATOM   7212  C  C   . ASP G  1 82  ? 102.849 155.213 42.471 1.00 91.24  ? 76  ASP G C   1 
ATOM   7213  O  O   . ASP G  1 82  ? 101.618 155.224 42.412 1.00 88.44  ? 76  ASP G O   1 
ATOM   7214  C  CB  . ASP G  1 82  ? 104.253 154.280 44.299 1.00 84.87  ? 76  ASP G CB  1 
ATOM   7215  C  CG  . ASP G  1 82  ? 105.168 154.562 45.467 1.00 84.80  ? 76  ASP G CG  1 
ATOM   7216  O  OD1 . ASP G  1 82  ? 105.918 153.647 45.871 1.00 81.71  ? 76  ASP G OD1 1 
ATOM   7217  O  OD2 . ASP G  1 82  ? 105.134 155.697 45.986 1.00 87.66  ? 76  ASP G OD2 1 
ATOM   7218  N  N   . GLU G  1 83  ? 103.626 154.922 41.434 1.00 95.48  ? 77  GLU G N   1 
ATOM   7219  C  CA  . GLU G  1 83  ? 103.069 154.582 40.138 1.00 97.91  ? 77  GLU G CA  1 
ATOM   7220  C  C   . GLU G  1 83  ? 102.734 153.106 40.124 1.00 97.86  ? 77  GLU G C   1 
ATOM   7221  O  O   . GLU G  1 83  ? 101.609 152.720 39.811 1.00 101.22 ? 77  GLU G O   1 
ATOM   7222  C  CB  . GLU G  1 83  ? 104.071 154.886 39.028 1.00 105.01 ? 77  GLU G CB  1 
ATOM   7223  C  CG  . GLU G  1 83  ? 103.464 154.785 37.652 1.00 113.49 ? 77  GLU G CG  1 
ATOM   7224  C  CD  . GLU G  1 83  ? 102.199 155.612 37.542 1.00 118.88 ? 77  GLU G CD  1 
ATOM   7225  O  OE1 . GLU G  1 83  ? 102.280 156.850 37.688 1.00 120.47 ? 77  GLU G OE1 1 
ATOM   7226  O  OE2 . GLU G  1 83  ? 101.121 155.024 37.321 1.00 122.92 ? 77  GLU G OE2 1 
ATOM   7227  N  N   . GLU G  1 84  ? 103.719 152.279 40.460 1.00 95.93  ? 78  GLU G N   1 
ATOM   7228  C  CA  . GLU G  1 84  ? 103.513 150.839 40.493 1.00 94.38  ? 78  GLU G CA  1 
ATOM   7229  C  C   . GLU G  1 84  ? 103.040 150.449 41.891 1.00 92.24  ? 78  GLU G C   1 
ATOM   7230  O  O   . GLU G  1 84  ? 103.830 150.033 42.742 1.00 92.18  ? 78  GLU G O   1 
ATOM   7231  C  CB  . GLU G  1 84  ? 104.804 150.090 40.145 1.00 95.79  ? 78  GLU G CB  1 
ATOM   7232  C  CG  . GLU G  1 84  ? 104.570 148.690 39.592 1.00 101.63 ? 78  GLU G CG  1 
ATOM   7233  C  CD  . GLU G  1 84  ? 103.979 148.700 38.182 1.00 106.85 ? 78  GLU G CD  1 
ATOM   7234  O  OE1 . GLU G  1 84  ? 103.034 149.477 37.925 1.00 108.94 ? 78  GLU G OE1 1 
ATOM   7235  O  OE2 . GLU G  1 84  ? 104.455 147.921 37.327 1.00 106.72 ? 78  GLU G OE2 1 
ATOM   7236  N  N   . ARG G  1 85  ? 101.739 150.612 42.112 1.00 86.61  ? 79  ARG G N   1 
ATOM   7237  C  CA  . ARG G  1 85  ? 101.100 150.282 43.378 1.00 77.07  ? 79  ARG G CA  1 
ATOM   7238  C  C   . ARG G  1 85  ? 99.826  149.475 43.111 1.00 72.56  ? 79  ARG G C   1 
ATOM   7239  O  O   . ARG G  1 85  ? 99.369  149.369 41.964 1.00 67.64  ? 79  ARG G O   1 
ATOM   7240  C  CB  . ARG G  1 85  ? 100.727 151.561 44.132 1.00 72.57  ? 79  ARG G CB  1 
ATOM   7241  C  CG  . ARG G  1 85  ? 99.831  152.489 43.329 1.00 70.41  ? 79  ARG G CG  1 
ATOM   7242  C  CD  . ARG G  1 85  ? 99.116  153.518 44.194 1.00 68.03  ? 79  ARG G CD  1 
ATOM   7243  N  NE  . ARG G  1 85  ? 97.852  153.009 44.715 1.00 62.53  ? 79  ARG G NE  1 
ATOM   7244  C  CZ  . ARG G  1 85  ? 96.965  153.740 45.387 1.00 64.14  ? 79  ARG G CZ  1 
ATOM   7245  N  NH1 . ARG G  1 85  ? 97.197  155.021 45.627 1.00 54.69  ? 79  ARG G NH1 1 
ATOM   7246  N  NH2 . ARG G  1 85  ? 95.835  153.190 45.814 1.00 68.34  ? 79  ARG G NH2 1 
ATOM   7247  N  N   . HIS G  1 86  ? 99.272  148.900 44.176 1.00 63.83  ? 80  HIS G N   1 
ATOM   7248  C  CA  . HIS G  1 86  ? 98.032  148.136 44.101 1.00 53.31  ? 80  HIS G CA  1 
ATOM   7249  C  C   . HIS G  1 86  ? 96.957  149.183 44.346 1.00 51.44  ? 80  HIS G C   1 
ATOM   7250  O  O   . HIS G  1 86  ? 97.178  150.113 45.115 1.00 55.22  ? 80  HIS G O   1 
ATOM   7251  C  CB  . HIS G  1 86  ? 97.965  147.102 45.227 1.00 51.99  ? 80  HIS G CB  1 
ATOM   7252  C  CG  . HIS G  1 86  ? 98.949  145.979 45.101 1.00 43.14  ? 80  HIS G CG  1 
ATOM   7253  N  ND1 . HIS G  1 86  ? 99.383  145.250 46.187 1.00 42.42  ? 80  HIS G ND1 1 
ATOM   7254  C  CD2 . HIS G  1 86  ? 99.520  145.406 44.016 1.00 42.55  ? 80  HIS G CD2 1 
ATOM   7255  C  CE1 . HIS G  1 86  ? 100.174 144.274 45.779 1.00 42.16  ? 80  HIS G CE1 1 
ATOM   7256  N  NE2 . HIS G  1 86  ? 100.273 144.345 44.464 1.00 44.30  ? 80  HIS G NE2 1 
ATOM   7257  N  N   . VAL G  1 87  ? 95.805  149.060 43.699 1.00 51.14  ? 81  VAL G N   1 
ATOM   7258  C  CA  . VAL G  1 87  ? 94.742  150.027 43.928 1.00 48.76  ? 81  VAL G CA  1 
ATOM   7259  C  C   . VAL G  1 87  ? 94.402  150.057 45.420 1.00 52.03  ? 81  VAL G C   1 
ATOM   7260  O  O   . VAL G  1 87  ? 94.009  151.092 45.963 1.00 47.15  ? 81  VAL G O   1 
ATOM   7261  C  CB  . VAL G  1 87  ? 93.464  149.661 43.156 1.00 54.48  ? 81  VAL G CB  1 
ATOM   7262  C  CG1 . VAL G  1 87  ? 92.299  150.515 43.648 1.00 55.18  ? 81  VAL G CG1 1 
ATOM   7263  C  CG2 . VAL G  1 87  ? 93.673  149.871 41.661 1.00 54.09  ? 81  VAL G CG2 1 
ATOM   7264  N  N   . GLY G  1 88  ? 94.567  148.918 46.085 1.00 50.62  ? 82  GLY G N   1 
ATOM   7265  C  CA  . GLY G  1 88  ? 94.255  148.850 47.499 1.00 50.56  ? 82  GLY G CA  1 
ATOM   7266  C  C   . GLY G  1 88  ? 95.247  149.478 48.466 1.00 53.50  ? 82  GLY G C   1 
ATOM   7267  O  O   . GLY G  1 88  ? 94.899  149.726 49.618 1.00 52.96  ? 82  GLY G O   1 
ATOM   7268  N  N   . ASP G  1 89  ? 96.462  149.764 48.009 1.00 52.00  ? 83  ASP G N   1 
ATOM   7269  C  CA  . ASP G  1 89  ? 97.494  150.324 48.883 1.00 54.02  ? 83  ASP G CA  1 
ATOM   7270  C  C   . ASP G  1 89  ? 97.322  151.757 49.392 1.00 54.98  ? 83  ASP G C   1 
ATOM   7271  O  O   . ASP G  1 89  ? 97.545  152.716 48.655 1.00 52.21  ? 83  ASP G O   1 
ATOM   7272  C  CB  . ASP G  1 89  ? 98.851  150.209 48.202 1.00 50.10  ? 83  ASP G CB  1 
ATOM   7273  C  CG  . ASP G  1 89  ? 99.170  148.797 47.802 1.00 52.06  ? 83  ASP G CG  1 
ATOM   7274  O  OD1 . ASP G  1 89  ? 98.809  147.875 48.558 1.00 45.95  ? 83  ASP G OD1 1 
ATOM   7275  O  OD2 . ASP G  1 89  ? 99.793  148.605 46.738 1.00 51.95  ? 83  ASP G OD2 1 
ATOM   7276  N  N   . LEU G  1 90  ? 96.959  151.900 50.665 1.00 52.75  ? 84  LEU G N   1 
ATOM   7277  C  CA  . LEU G  1 90  ? 96.793  153.228 51.245 1.00 54.73  ? 84  LEU G CA  1 
ATOM   7278  C  C   . LEU G  1 90  ? 97.956  153.658 52.153 1.00 54.15  ? 84  LEU G C   1 
ATOM   7279  O  O   . LEU G  1 90  ? 97.856  154.665 52.857 1.00 55.22  ? 84  LEU G O   1 
ATOM   7280  C  CB  . LEU G  1 90  ? 95.483  153.305 52.015 1.00 53.39  ? 84  LEU G CB  1 
ATOM   7281  C  CG  . LEU G  1 90  ? 94.259  153.114 51.129 1.00 59.84  ? 84  LEU G CG  1 
ATOM   7282  C  CD1 . LEU G  1 90  ? 93.003  153.295 51.967 1.00 57.70  ? 84  LEU G CD1 1 
ATOM   7283  C  CD2 . LEU G  1 90  ? 94.293  154.117 49.982 1.00 60.85  ? 84  LEU G CD2 1 
ATOM   7284  N  N   . GLY G  1 91  ? 99.047  152.891 52.137 1.00 45.82  ? 85  GLY G N   1 
ATOM   7285  C  CA  . GLY G  1 91  ? 100.211 153.229 52.936 1.00 52.26  ? 85  GLY G CA  1 
ATOM   7286  C  C   . GLY G  1 91  ? 100.203 152.831 54.402 1.00 53.96  ? 85  GLY G C   1 
ATOM   7287  O  O   . GLY G  1 91  ? 99.939  151.681 54.752 1.00 57.11  ? 85  GLY G O   1 
ATOM   7288  N  N   . ASN G  1 92  ? 100.511 153.791 55.266 1.00 50.52  ? 86  ASN G N   1 
ATOM   7289  C  CA  . ASN G  1 92  ? 100.544 153.540 56.699 1.00 48.88  ? 86  ASN G CA  1 
ATOM   7290  C  C   . ASN G  1 92  ? 99.718  154.579 57.418 1.00 49.41  ? 86  ASN G C   1 
ATOM   7291  O  O   . ASN G  1 92  ? 99.555  155.698 56.931 1.00 49.34  ? 86  ASN G O   1 
ATOM   7292  C  CB  . ASN G  1 92  ? 101.973 153.623 57.246 1.00 43.66  ? 86  ASN G CB  1 
ATOM   7293  C  CG  . ASN G  1 92  ? 102.833 152.459 56.829 1.00 53.19  ? 86  ASN G CG  1 
ATOM   7294  O  OD1 . ASN G  1 92  ? 102.616 151.330 57.256 1.00 60.60  ? 86  ASN G OD1 1 
ATOM   7295  N  ND2 . ASN G  1 92  ? 103.824 152.728 55.995 1.00 56.27  ? 86  ASN G ND2 1 
ATOM   7296  N  N   . VAL G  1 93  ? 99.184  154.190 58.571 1.00 46.15  ? 87  VAL G N   1 
ATOM   7297  C  CA  . VAL G  1 93  ? 98.423  155.099 59.414 1.00 41.92  ? 87  VAL G CA  1 
ATOM   7298  C  C   . VAL G  1 93  ? 99.272  155.168 60.674 1.00 41.93  ? 87  VAL G C   1 
ATOM   7299  O  O   . VAL G  1 93  ? 100.058 154.242 60.958 1.00 33.12  ? 87  VAL G O   1 
ATOM   7300  C  CB  . VAL G  1 93  ? 97.007  154.565 59.746 1.00 43.75  ? 87  VAL G CB  1 
ATOM   7301  C  CG1 . VAL G  1 93  ? 96.114  154.736 58.542 1.00 40.89  ? 87  VAL G CG1 1 
ATOM   7302  C  CG2 . VAL G  1 93  ? 97.068  153.094 60.170 1.00 32.71  ? 87  VAL G CG2 1 
ATOM   7303  N  N   . THR G  1 94  ? 99.128  156.241 61.438 1.00 39.35  ? 88  THR G N   1 
ATOM   7304  C  CA  . THR G  1 94  ? 99.969  156.363 62.612 1.00 45.53  ? 88  THR G CA  1 
ATOM   7305  C  C   . THR G  1 94  ? 99.273  156.423 63.943 1.00 41.90  ? 88  THR G C   1 
ATOM   7306  O  O   . THR G  1 94  ? 98.466  157.318 64.216 1.00 41.22  ? 88  THR G O   1 
ATOM   7307  C  CB  . THR G  1 94  ? 100.904 157.589 62.488 1.00 50.79  ? 88  THR G CB  1 
ATOM   7308  O  OG1 . THR G  1 94  ? 101.791 157.396 61.382 1.00 54.35  ? 88  THR G OG1 1 
ATOM   7309  C  CG2 . THR G  1 94  ? 101.732 157.764 63.752 1.00 48.81  ? 88  THR G CG2 1 
ATOM   7310  N  N   . ALA G  1 95  ? 99.617  155.465 64.787 1.00 40.33  ? 89  ALA G N   1 
ATOM   7311  C  CA  . ALA G  1 95  ? 99.046  155.408 66.113 1.00 44.22  ? 89  ALA G CA  1 
ATOM   7312  C  C   . ALA G  1 95  ? 99.914  156.219 67.077 1.00 42.23  ? 89  ALA G C   1 
ATOM   7313  O  O   . ALA G  1 95  ? 101.109 155.952 67.223 1.00 37.74  ? 89  ALA G O   1 
ATOM   7314  C  CB  . ALA G  1 95  ? 98.959  153.959 66.573 1.00 52.23  ? 89  ALA G CB  1 
ATOM   7315  N  N   . ASP G  1 96  ? 99.295  157.204 67.719 1.00 43.70  ? 90  ASP G N   1 
ATOM   7316  C  CA  . ASP G  1 96  ? 99.943  158.072 68.698 1.00 43.35  ? 90  ASP G CA  1 
ATOM   7317  C  C   . ASP G  1 96  ? 100.448 157.243 69.895 1.00 46.10  ? 90  ASP G C   1 
ATOM   7318  O  O   . ASP G  1 96  ? 100.488 156.014 69.837 1.00 45.66  ? 90  ASP G O   1 
ATOM   7319  C  CB  . ASP G  1 96  ? 98.938  159.152 69.161 1.00 48.43  ? 90  ASP G CB  1 
ATOM   7320  C  CG  . ASP G  1 96  ? 97.751  158.577 69.983 1.00 60.96  ? 90  ASP G CG  1 
ATOM   7321  O  OD1 . ASP G  1 96  ? 96.735  159.288 70.168 1.00 61.56  ? 90  ASP G OD1 1 
ATOM   7322  O  OD2 . ASP G  1 96  ? 97.823  157.428 70.465 1.00 56.06  ? 90  ASP G OD2 1 
ATOM   7323  N  N   . LYS G  1 97  ? 100.838 157.899 70.982 1.00 49.17  ? 91  LYS G N   1 
ATOM   7324  C  CA  . LYS G  1 97  ? 101.327 157.162 72.151 1.00 51.73  ? 91  LYS G CA  1 
ATOM   7325  C  C   . LYS G  1 97  ? 100.155 156.587 72.959 1.00 48.34  ? 91  LYS G C   1 
ATOM   7326  O  O   . LYS G  1 97  ? 100.346 155.706 73.799 1.00 42.75  ? 91  LYS G O   1 
ATOM   7327  C  CB  . LYS G  1 97  ? 102.190 158.066 73.046 1.00 51.09  ? 91  LYS G CB  1 
ATOM   7328  C  CG  . LYS G  1 97  ? 101.416 159.209 73.695 1.00 63.75  ? 91  LYS G CG  1 
ATOM   7329  C  CD  . LYS G  1 97  ? 102.277 160.010 74.658 1.00 69.69  ? 91  LYS G CD  1 
ATOM   7330  C  CE  . LYS G  1 97  ? 101.418 160.950 75.506 1.00 78.29  ? 91  LYS G CE  1 
ATOM   7331  N  NZ  . LYS G  1 97  ? 100.605 161.904 74.694 1.00 72.64  ? 91  LYS G NZ  1 
ATOM   7332  N  N   . ASP G  1 98  ? 98.951  157.098 72.700 1.00 45.48  ? 92  ASP G N   1 
ATOM   7333  C  CA  . ASP G  1 98  ? 97.735  156.636 73.367 1.00 46.45  ? 92  ASP G CA  1 
ATOM   7334  C  C   . ASP G  1 98  ? 97.097  155.459 72.611 1.00 44.51  ? 92  ASP G C   1 
ATOM   7335  O  O   . ASP G  1 98  ? 95.929  155.141 72.818 1.00 38.24  ? 92  ASP G O   1 
ATOM   7336  C  CB  . ASP G  1 98  ? 96.717  157.775 73.474 1.00 57.04  ? 92  ASP G CB  1 
ATOM   7337  C  CG  . ASP G  1 98  ? 97.276  158.998 74.194 1.00 70.97  ? 92  ASP G CG  1 
ATOM   7338  O  OD1 . ASP G  1 98  ? 98.043  158.816 75.164 1.00 79.94  ? 92  ASP G OD1 1 
ATOM   7339  O  OD2 . ASP G  1 98  ? 96.942  160.141 73.805 1.00 74.88  ? 92  ASP G OD2 1 
ATOM   7340  N  N   . ALA G  1 99  ? 97.880  154.831 71.732 1.00 42.66  ? 93  ALA G N   1 
ATOM   7341  C  CA  . ALA G  1 99  ? 97.454  153.683 70.929 1.00 44.31  ? 93  ALA G CA  1 
ATOM   7342  C  C   . ALA G  1 99  ? 96.296  153.997 69.996 1.00 42.36  ? 93  ALA G C   1 
ATOM   7343  O  O   . ALA G  1 99  ? 95.489  153.131 69.677 1.00 48.84  ? 93  ALA G O   1 
ATOM   7344  C  CB  . ALA G  1 99  ? 97.091  152.505 71.845 1.00 45.93  ? 93  ALA G CB  1 
ATOM   7345  N  N   . VAL G  1 100 ? 96.230  155.238 69.544 1.00 42.52  ? 94  VAL G N   1 
ATOM   7346  C  CA  . VAL G  1 100 ? 95.161  155.671 68.663 1.00 41.79  ? 94  VAL G CA  1 
ATOM   7347  C  C   . VAL G  1 100 ? 95.707  156.337 67.411 1.00 47.21  ? 94  VAL G C   1 
ATOM   7348  O  O   . VAL G  1 100 ? 96.586  157.199 67.479 1.00 46.02  ? 94  VAL G O   1 
ATOM   7349  C  CB  . VAL G  1 100 ? 94.233  156.674 69.380 1.00 40.80  ? 94  VAL G CB  1 
ATOM   7350  C  CG1 . VAL G  1 100 ? 93.177  157.228 68.406 1.00 38.72  ? 94  VAL G CG1 1 
ATOM   7351  C  CG2 . VAL G  1 100 ? 93.568  155.992 70.558 1.00 42.47  ? 94  VAL G CG2 1 
ATOM   7352  N  N   . ALA G  1 101 ? 95.181  155.928 66.264 1.00 44.10  ? 95  ALA G N   1 
ATOM   7353  C  CA  . ALA G  1 101 ? 95.594  156.497 65.000 1.00 40.46  ? 95  ALA G CA  1 
ATOM   7354  C  C   . ALA G  1 101 ? 94.421  157.288 64.442 1.00 43.83  ? 95  ALA G C   1 
ATOM   7355  O  O   . ALA G  1 101 ? 93.349  156.741 64.220 1.00 44.12  ? 95  ALA G O   1 
ATOM   7356  C  CB  . ALA G  1 101 ? 95.991  155.401 64.045 1.00 33.22  ? 95  ALA G CB  1 
ATOM   7357  N  N   . ASP G  1 102 ? 94.603  158.590 64.262 1.00 53.14  ? 96  ASP G N   1 
ATOM   7358  C  CA  . ASP G  1 102 ? 93.543  159.416 63.695 1.00 57.71  ? 96  ASP G CA  1 
ATOM   7359  C  C   . ASP G  1 102 ? 93.876  159.521 62.216 1.00 58.07  ? 96  ASP G C   1 
ATOM   7360  O  O   . ASP G  1 102 ? 94.887  160.110 61.844 1.00 56.74  ? 96  ASP G O   1 
ATOM   7361  C  CB  . ASP G  1 102 ? 93.517  160.793 64.354 1.00 60.62  ? 96  ASP G CB  1 
ATOM   7362  C  CG  . ASP G  1 102 ? 93.001  160.738 65.781 1.00 72.28  ? 96  ASP G CG  1 
ATOM   7363  O  OD1 . ASP G  1 102 ? 91.825  160.355 65.974 1.00 71.65  ? 96  ASP G OD1 1 
ATOM   7364  O  OD2 . ASP G  1 102 ? 93.771  161.072 66.710 1.00 79.80  ? 96  ASP G OD2 1 
ATOM   7365  N  N   . VAL G  1 103 ? 93.030  158.923 61.381 1.00 59.59  ? 97  VAL G N   1 
ATOM   7366  C  CA  . VAL G  1 103 ? 93.254  158.896 59.942 1.00 55.63  ? 97  VAL G CA  1 
ATOM   7367  C  C   . VAL G  1 103 ? 92.642  160.043 59.148 1.00 55.03  ? 97  VAL G C   1 
ATOM   7368  O  O   . VAL G  1 103 ? 91.486  160.423 59.339 1.00 49.13  ? 97  VAL G O   1 
ATOM   7369  C  CB  . VAL G  1 103 ? 92.774  157.550 59.343 1.00 54.74  ? 97  VAL G CB  1 
ATOM   7370  C  CG1 . VAL G  1 103 ? 93.026  157.518 57.857 1.00 56.06  ? 97  VAL G CG1 1 
ATOM   7371  C  CG2 . VAL G  1 103 ? 93.506  156.397 60.014 1.00 47.31  ? 97  VAL G CG2 1 
ATOM   7372  N  N   . SER G  1 104 ? 93.458  160.594 58.257 1.00 58.82  ? 98  SER G N   1 
ATOM   7373  C  CA  . SER G  1 104 ? 93.061  161.689 57.381 1.00 59.70  ? 98  SER G CA  1 
ATOM   7374  C  C   . SER G  1 104 ? 93.899  161.507 56.124 1.00 58.81  ? 98  SER G C   1 
ATOM   7375  O  O   . SER G  1 104 ? 95.110  161.748 56.116 1.00 60.28  ? 98  SER G O   1 
ATOM   7376  C  CB  . SER G  1 104 ? 93.356  163.037 58.031 1.00 59.04  ? 98  SER G CB  1 
ATOM   7377  O  OG  . SER G  1 104 ? 92.442  164.015 57.570 1.00 61.21  ? 98  SER G OG  1 
ATOM   7378  N  N   . ILE G  1 105 ? 93.244  161.065 55.062 1.00 56.42  ? 99  ILE G N   1 
ATOM   7379  C  CA  . ILE G  1 105 ? 93.935  160.796 53.825 1.00 54.81  ? 99  ILE G CA  1 
ATOM   7380  C  C   . ILE G  1 105 ? 93.120  161.136 52.591 1.00 58.66  ? 99  ILE G C   1 
ATOM   7381  O  O   . ILE G  1 105 ? 91.890  161.187 52.625 1.00 57.71  ? 99  ILE G O   1 
ATOM   7382  C  CB  . ILE G  1 105 ? 94.331  159.302 53.782 1.00 53.80  ? 99  ILE G CB  1 
ATOM   7383  C  CG1 . ILE G  1 105 ? 95.483  159.061 54.751 1.00 56.15  ? 99  ILE G CG1 1 
ATOM   7384  C  CG2 . ILE G  1 105 ? 94.682  158.864 52.370 1.00 53.81  ? 99  ILE G CG2 1 
ATOM   7385  C  CD1 . ILE G  1 105 ? 95.946  157.627 54.811 1.00 62.93  ? 99  ILE G CD1 1 
ATOM   7386  N  N   . GLU G  1 106 ? 93.832  161.400 51.505 1.00 62.32  ? 100 GLU G N   1 
ATOM   7387  C  CA  . GLU G  1 106 ? 93.218  161.670 50.222 1.00 62.33  ? 100 GLU G CA  1 
ATOM   7388  C  C   . GLU G  1 106 ? 93.969  160.787 49.241 1.00 57.17  ? 100 GLU G C   1 
ATOM   7389  O  O   . GLU G  1 106 ? 95.198  160.779 49.207 1.00 54.00  ? 100 GLU G O   1 
ATOM   7390  C  CB  . GLU G  1 106 ? 93.341  163.146 49.827 1.00 68.14  ? 100 GLU G CB  1 
ATOM   7391  C  CG  . GLU G  1 106 ? 92.307  164.065 50.491 1.00 83.94  ? 100 GLU G CG  1 
ATOM   7392  C  CD  . GLU G  1 106 ? 92.081  165.378 49.730 1.00 90.80  ? 100 GLU G CD  1 
ATOM   7393  O  OE1 . GLU G  1 106 ? 91.318  166.241 50.230 1.00 86.95  ? 100 GLU G OE1 1 
ATOM   7394  O  OE2 . GLU G  1 106 ? 92.658  165.543 48.631 1.00 92.09  ? 100 GLU G OE2 1 
ATOM   7395  N  N   . ASP G  1 107 ? 93.222  159.999 48.483 1.00 55.01  ? 101 ASP G N   1 
ATOM   7396  C  CA  . ASP G  1 107 ? 93.814  159.120 47.494 1.00 51.52  ? 101 ASP G CA  1 
ATOM   7397  C  C   . ASP G  1 107 ? 92.928  159.234 46.279 1.00 56.54  ? 101 ASP G C   1 
ATOM   7398  O  O   . ASP G  1 107 ? 91.705  159.350 46.398 1.00 60.34  ? 101 ASP G O   1 
ATOM   7399  C  CB  . ASP G  1 107 ? 93.860  157.689 48.002 1.00 42.57  ? 101 ASP G CB  1 
ATOM   7400  C  CG  . ASP G  1 107 ? 94.493  156.740 47.011 1.00 47.58  ? 101 ASP G CG  1 
ATOM   7401  O  OD1 . ASP G  1 107 ? 93.811  156.355 46.038 1.00 47.36  ? 101 ASP G OD1 1 
ATOM   7402  O  OD2 . ASP G  1 107 ? 95.675  156.379 47.199 1.00 44.36  ? 101 ASP G OD2 1 
ATOM   7403  N  N   . SER G  1 108 ? 93.554  159.222 45.110 1.00 61.17  ? 102 SER G N   1 
ATOM   7404  C  CA  . SER G  1 108 ? 92.842  159.370 43.852 1.00 62.84  ? 102 SER G CA  1 
ATOM   7405  C  C   . SER G  1 108 ? 92.849  158.104 43.009 1.00 64.05  ? 102 SER G C   1 
ATOM   7406  O  O   . SER G  1 108 ? 92.330  158.095 41.894 1.00 63.30  ? 102 SER G O   1 
ATOM   7407  C  CB  . SER G  1 108 ? 93.455  160.532 43.066 1.00 62.96  ? 102 SER G CB  1 
ATOM   7408  O  OG  . SER G  1 108 ? 94.870  160.417 43.025 1.00 56.45  ? 102 SER G OG  1 
ATOM   7409  N  N   . VAL G  1 109 ? 93.439  157.039 43.545 1.00 66.67  ? 103 VAL G N   1 
ATOM   7410  C  CA  . VAL G  1 109 ? 93.494  155.756 42.847 1.00 68.13  ? 103 VAL G CA  1 
ATOM   7411  C  C   . VAL G  1 109 ? 92.270  154.890 43.175 1.00 69.14  ? 103 VAL G C   1 
ATOM   7412  O  O   . VAL G  1 109 ? 91.655  154.307 42.274 1.00 68.61  ? 103 VAL G O   1 
ATOM   7413  C  CB  . VAL G  1 109 ? 94.755  154.990 43.215 1.00 65.88  ? 103 VAL G CB  1 
ATOM   7414  C  CG1 . VAL G  1 109 ? 94.835  153.706 42.405 1.00 63.61  ? 103 VAL G CG1 1 
ATOM   7415  C  CG2 . VAL G  1 109 ? 95.959  155.865 42.970 1.00 62.20  ? 103 VAL G CG2 1 
ATOM   7416  N  N   . ILE G  1 110 ? 91.924  154.791 44.459 1.00 62.19  ? 104 ILE G N   1 
ATOM   7417  C  CA  . ILE G  1 110 ? 90.744  154.028 44.842 1.00 55.00  ? 104 ILE G CA  1 
ATOM   7418  C  C   . ILE G  1 110 ? 89.574  154.879 44.344 1.00 59.77  ? 104 ILE G C   1 
ATOM   7419  O  O   . ILE G  1 110 ? 89.778  155.982 43.832 1.00 63.35  ? 104 ILE G O   1 
ATOM   7420  C  CB  . ILE G  1 110 ? 90.614  153.853 46.380 1.00 41.56  ? 104 ILE G CB  1 
ATOM   7421  C  CG1 . ILE G  1 110 ? 90.505  155.210 47.061 1.00 39.77  ? 104 ILE G CG1 1 
ATOM   7422  C  CG2 . ILE G  1 110 ? 91.796  153.094 46.928 1.00 41.50  ? 104 ILE G CG2 1 
ATOM   7423  C  CD1 . ILE G  1 110 ? 90.240  155.125 48.537 1.00 46.07  ? 104 ILE G CD1 1 
ATOM   7424  N  N   . SER G  1 111 ? 88.355  154.378 44.495 1.00 55.60  ? 105 SER G N   1 
ATOM   7425  C  CA  . SER G  1 111 ? 87.183  155.113 44.050 1.00 52.11  ? 105 SER G CA  1 
ATOM   7426  C  C   . SER G  1 111 ? 85.920  154.473 44.617 1.00 53.64  ? 105 SER G C   1 
ATOM   7427  O  O   . SER G  1 111 ? 85.943  153.344 45.096 1.00 57.50  ? 105 SER G O   1 
ATOM   7428  C  CB  . SER G  1 111 ? 87.116  155.107 42.517 1.00 48.80  ? 105 SER G CB  1 
ATOM   7429  O  OG  . SER G  1 111 ? 86.032  155.896 42.048 1.00 46.77  ? 105 SER G OG  1 
ATOM   7430  N  N   . LEU G  1 112 ? 84.814  155.198 44.564 1.00 51.14  ? 106 LEU G N   1 
ATOM   7431  C  CA  . LEU G  1 112 ? 83.563  154.663 45.053 1.00 49.08  ? 106 LEU G CA  1 
ATOM   7432  C  C   . LEU G  1 112 ? 82.667  154.305 43.867 1.00 51.59  ? 106 LEU G C   1 
ATOM   7433  O  O   . LEU G  1 112 ? 81.450  154.217 44.001 1.00 52.84  ? 106 LEU G O   1 
ATOM   7434  C  CB  . LEU G  1 112 ? 82.888  155.679 45.967 1.00 39.91  ? 106 LEU G CB  1 
ATOM   7435  C  CG  . LEU G  1 112 ? 83.745  156.142 47.154 1.00 40.91  ? 106 LEU G CG  1 
ATOM   7436  C  CD1 . LEU G  1 112 ? 82.891  157.010 48.077 1.00 33.55  ? 106 LEU G CD1 1 
ATOM   7437  C  CD2 . LEU G  1 112 ? 84.290  154.940 47.915 1.00 37.01  ? 106 LEU G CD2 1 
ATOM   7438  N  N   . SER G  1 113 ? 83.292  154.098 42.708 1.00 57.24  ? 107 SER G N   1 
ATOM   7439  C  CA  . SER G  1 113 ? 82.589  153.734 41.474 1.00 61.76  ? 107 SER G CA  1 
ATOM   7440  C  C   . SER G  1 113 ? 83.580  153.344 40.379 1.00 62.85  ? 107 SER G C   1 
ATOM   7441  O  O   . SER G  1 113 ? 84.751  153.732 40.417 1.00 65.44  ? 107 SER G O   1 
ATOM   7442  C  CB  . SER G  1 113 ? 81.728  154.902 40.976 1.00 61.95  ? 107 SER G CB  1 
ATOM   7443  O  OG  . SER G  1 113 ? 82.532  156.001 40.573 1.00 63.21  ? 107 SER G OG  1 
ATOM   7444  N  N   . GLY G  1 114 ? 83.113  152.564 39.410 1.00 64.59  ? 108 GLY G N   1 
ATOM   7445  C  CA  . GLY G  1 114 ? 83.975  152.166 38.310 1.00 71.52  ? 108 GLY G CA  1 
ATOM   7446  C  C   . GLY G  1 114 ? 84.957  151.049 38.593 1.00 73.39  ? 108 GLY G C   1 
ATOM   7447  O  O   . GLY G  1 114 ? 84.788  150.294 39.542 1.00 74.29  ? 108 GLY G O   1 
ATOM   7448  N  N   . ASP G  1 115 ? 85.985  150.950 37.754 1.00 78.97  ? 109 ASP G N   1 
ATOM   7449  C  CA  . ASP G  1 115 ? 87.015  149.919 37.883 1.00 83.01  ? 109 ASP G CA  1 
ATOM   7450  C  C   . ASP G  1 115 ? 87.518  149.712 39.300 1.00 80.89  ? 109 ASP G C   1 
ATOM   7451  O  O   . ASP G  1 115 ? 87.557  148.592 39.806 1.00 81.64  ? 109 ASP G O   1 
ATOM   7452  C  CB  . ASP G  1 115 ? 88.242  150.259 37.026 1.00 91.11  ? 109 ASP G CB  1 
ATOM   7453  C  CG  . ASP G  1 115 ? 88.056  149.933 35.564 1.00 97.90  ? 109 ASP G CG  1 
ATOM   7454  O  OD1 . ASP G  1 115 ? 87.519  148.847 35.255 1.00 101.47 ? 109 ASP G OD1 1 
ATOM   7455  O  OD2 . ASP G  1 115 ? 88.471  150.760 34.723 1.00 101.20 ? 109 ASP G OD2 1 
ATOM   7456  N  N   . HIS G  1 116 ? 87.921  150.812 39.923 1.00 78.57  ? 110 HIS G N   1 
ATOM   7457  C  CA  . HIS G  1 116 ? 88.494  150.795 41.261 1.00 75.88  ? 110 HIS G CA  1 
ATOM   7458  C  C   . HIS G  1 116 ? 87.516  150.890 42.436 1.00 67.81  ? 110 HIS G C   1 
ATOM   7459  O  O   . HIS G  1 116 ? 87.927  151.223 43.545 1.00 63.66  ? 110 HIS G O   1 
ATOM   7460  C  CB  . HIS G  1 116 ? 89.522  151.928 41.363 1.00 85.01  ? 110 HIS G CB  1 
ATOM   7461  C  CG  . HIS G  1 116 ? 90.521  151.941 40.246 1.00 88.92  ? 110 HIS G CG  1 
ATOM   7462  N  ND1 . HIS G  1 116 ? 91.312  153.034 39.969 1.00 89.70  ? 110 HIS G ND1 1 
ATOM   7463  C  CD2 . HIS G  1 116 ? 90.865  150.990 39.344 1.00 91.47  ? 110 HIS G CD2 1 
ATOM   7464  C  CE1 . HIS G  1 116 ? 92.100  152.757 38.945 1.00 92.22  ? 110 HIS G CE1 1 
ATOM   7465  N  NE2 . HIS G  1 116 ? 91.849  151.523 38.547 1.00 90.75  ? 110 HIS G NE2 1 
ATOM   7466  N  N   . CYS G  1 117 ? 86.237  150.603 42.204 1.00 61.18  ? 111 CYS G N   1 
ATOM   7467  C  CA  . CYS G  1 117 ? 85.247  150.673 43.278 1.00 56.13  ? 111 CYS G CA  1 
ATOM   7468  C  C   . CYS G  1 117 ? 85.760  149.795 44.424 1.00 54.06  ? 111 CYS G C   1 
ATOM   7469  O  O   . CYS G  1 117 ? 86.097  148.624 44.216 1.00 45.63  ? 111 CYS G O   1 
ATOM   7470  C  CB  . CYS G  1 117 ? 83.878  150.165 42.780 1.00 54.25  ? 111 CYS G CB  1 
ATOM   7471  S  SG  . CYS G  1 117 ? 82.420  150.528 43.830 1.00 50.37  ? 111 CYS G SG  1 
ATOM   7472  N  N   . ILE G  1 118 ? 85.857  150.376 45.620 1.00 51.10  ? 112 ILE G N   1 
ATOM   7473  C  CA  . ILE G  1 118 ? 86.315  149.636 46.799 1.00 47.40  ? 112 ILE G CA  1 
ATOM   7474  C  C   . ILE G  1 118 ? 85.131  149.205 47.653 1.00 41.58  ? 112 ILE G C   1 
ATOM   7475  O  O   . ILE G  1 118 ? 85.294  148.454 48.610 1.00 39.95  ? 112 ILE G O   1 
ATOM   7476  C  CB  . ILE G  1 118 ? 87.276  150.472 47.689 1.00 44.79  ? 112 ILE G CB  1 
ATOM   7477  C  CG1 . ILE G  1 118 ? 86.600  151.774 48.126 1.00 44.00  ? 112 ILE G CG1 1 
ATOM   7478  C  CG2 . ILE G  1 118 ? 88.565  150.744 46.942 1.00 42.32  ? 112 ILE G CG2 1 
ATOM   7479  C  CD1 . ILE G  1 118 ? 87.455  152.623 49.040 1.00 35.66  ? 112 ILE G CD1 1 
ATOM   7480  N  N   . ILE G  1 119 ? 83.943  149.692 47.300 1.00 40.89  ? 113 ILE G N   1 
ATOM   7481  C  CA  . ILE G  1 119 ? 82.730  149.351 48.022 1.00 37.06  ? 113 ILE G CA  1 
ATOM   7482  C  C   . ILE G  1 119 ? 82.442  147.870 47.842 1.00 41.32  ? 113 ILE G C   1 
ATOM   7483  O  O   . ILE G  1 119 ? 82.335  147.388 46.720 1.00 43.42  ? 113 ILE G O   1 
ATOM   7484  C  CB  . ILE G  1 119 ? 81.527  150.159 47.510 1.00 32.29  ? 113 ILE G CB  1 
ATOM   7485  C  CG1 . ILE G  1 119 ? 81.651  151.612 47.968 1.00 35.41  ? 113 ILE G CG1 1 
ATOM   7486  C  CG2 . ILE G  1 119 ? 80.233  149.544 48.020 1.00 28.51  ? 113 ILE G CG2 1 
ATOM   7487  C  CD1 . ILE G  1 119 ? 80.507  152.506 47.503 1.00 41.31  ? 113 ILE G CD1 1 
ATOM   7488  N  N   . GLY G  1 120 ? 82.319  147.151 48.952 1.00 37.04  ? 114 GLY G N   1 
ATOM   7489  C  CA  . GLY G  1 120 ? 82.054  145.731 48.875 1.00 37.43  ? 114 GLY G CA  1 
ATOM   7490  C  C   . GLY G  1 120 ? 83.321  144.924 49.068 1.00 40.65  ? 114 GLY G C   1 
ATOM   7491  O  O   . GLY G  1 120 ? 83.309  143.699 48.969 1.00 39.96  ? 114 GLY G O   1 
ATOM   7492  N  N   . ARG G  1 121 ? 84.424  145.616 49.321 1.00 37.60  ? 115 ARG G N   1 
ATOM   7493  C  CA  . ARG G  1 121 ? 85.692  144.957 49.559 1.00 39.45  ? 115 ARG G CA  1 
ATOM   7494  C  C   . ARG G  1 121 ? 86.043  145.172 51.026 1.00 37.73  ? 115 ARG G C   1 
ATOM   7495  O  O   . ARG G  1 121 ? 85.234  145.735 51.772 1.00 37.96  ? 115 ARG G O   1 
ATOM   7496  C  CB  . ARG G  1 121 ? 86.751  145.515 48.605 1.00 42.69  ? 115 ARG G CB  1 
ATOM   7497  C  CG  . ARG G  1 121 ? 86.460  145.097 47.161 1.00 41.48  ? 115 ARG G CG  1 
ATOM   7498  C  CD  . ARG G  1 121 ? 87.387  145.728 46.147 1.00 49.57  ? 115 ARG G CD  1 
ATOM   7499  N  NE  . ARG G  1 121 ? 86.873  145.580 44.783 1.00 50.45  ? 115 ARG G NE  1 
ATOM   7500  C  CZ  . ARG G  1 121 ? 86.800  144.430 44.117 1.00 52.28  ? 115 ARG G CZ  1 
ATOM   7501  N  NH1 . ARG G  1 121 ? 86.313  144.408 42.883 1.00 50.66  ? 115 ARG G NH1 1 
ATOM   7502  N  NH2 . ARG G  1 121 ? 87.219  143.302 44.674 1.00 56.09  ? 115 ARG G NH2 1 
ATOM   7503  N  N   . THR G  1 122 ? 87.220  144.724 51.450 1.00 35.81  ? 116 THR G N   1 
ATOM   7504  C  CA  . THR G  1 122 ? 87.606  144.846 52.857 1.00 32.54  ? 116 THR G CA  1 
ATOM   7505  C  C   . THR G  1 122 ? 88.807  145.739 53.144 1.00 35.42  ? 116 THR G C   1 
ATOM   7506  O  O   . THR G  1 122 ? 89.805  145.730 52.425 1.00 35.84  ? 116 THR G O   1 
ATOM   7507  C  CB  . THR G  1 122 ? 87.902  143.453 53.481 1.00 31.07  ? 116 THR G CB  1 
ATOM   7508  O  OG1 . THR G  1 122 ? 86.751  142.613 53.356 1.00 34.58  ? 116 THR G OG1 1 
ATOM   7509  C  CG2 . THR G  1 122 ? 88.247  143.586 54.965 1.00 24.89  ? 116 THR G CG2 1 
ATOM   7510  N  N   . LEU G  1 123 ? 88.679  146.512 54.215 1.00 33.36  ? 117 LEU G N   1 
ATOM   7511  C  CA  . LEU G  1 123 ? 89.719  147.406 54.677 1.00 31.88  ? 117 LEU G CA  1 
ATOM   7512  C  C   . LEU G  1 123 ? 90.420  146.673 55.824 1.00 36.91  ? 117 LEU G C   1 
ATOM   7513  O  O   . LEU G  1 123 ? 89.771  146.178 56.750 1.00 38.35  ? 117 LEU G O   1 
ATOM   7514  C  CB  . LEU G  1 123 ? 89.101  148.707 55.184 1.00 23.76  ? 117 LEU G CB  1 
ATOM   7515  C  CG  . LEU G  1 123 ? 90.091  149.757 55.701 1.00 34.35  ? 117 LEU G CG  1 
ATOM   7516  C  CD1 . LEU G  1 123 ? 90.980  150.211 54.554 1.00 36.25  ? 117 LEU G CD1 1 
ATOM   7517  C  CD2 . LEU G  1 123 ? 89.344  150.951 56.291 1.00 26.44  ? 117 LEU G CD2 1 
ATOM   7518  N  N   . VAL G  1 124 ? 91.742  146.603 55.752 1.00 36.73  ? 118 VAL G N   1 
ATOM   7519  C  CA  . VAL G  1 124 ? 92.544  145.921 56.760 1.00 31.02  ? 118 VAL G CA  1 
ATOM   7520  C  C   . VAL G  1 124 ? 93.600  146.866 57.360 1.00 37.03  ? 118 VAL G C   1 
ATOM   7521  O  O   . VAL G  1 124 ? 94.176  147.714 56.673 1.00 31.90  ? 118 VAL G O   1 
ATOM   7522  C  CB  . VAL G  1 124 ? 93.263  144.704 56.135 1.00 27.24  ? 118 VAL G CB  1 
ATOM   7523  C  CG1 . VAL G  1 124 ? 94.011  143.927 57.190 1.00 32.55  ? 118 VAL G CG1 1 
ATOM   7524  C  CG2 . VAL G  1 124 ? 92.261  143.814 55.438 1.00 22.09  ? 118 VAL G CG2 1 
ATOM   7525  N  N   . VAL G  1 125 ? 93.824  146.729 58.659 1.00 33.53  ? 119 VAL G N   1 
ATOM   7526  C  CA  . VAL G  1 125 ? 94.821  147.515 59.352 1.00 29.28  ? 119 VAL G CA  1 
ATOM   7527  C  C   . VAL G  1 125 ? 95.767  146.451 59.876 1.00 33.44  ? 119 VAL G C   1 
ATOM   7528  O  O   . VAL G  1 125 ? 95.400  145.655 60.735 1.00 40.57  ? 119 VAL G O   1 
ATOM   7529  C  CB  . VAL G  1 125 ? 94.215  148.331 60.516 1.00 27.91  ? 119 VAL G CB  1 
ATOM   7530  C  CG1 . VAL G  1 125 ? 93.541  147.419 61.523 1.00 32.66  ? 119 VAL G CG1 1 
ATOM   7531  C  CG2 . VAL G  1 125 ? 95.295  149.129 61.186 1.00 35.05  ? 119 VAL G CG2 1 
ATOM   7532  N  N   . HIS G  1 126 ? 96.980  146.414 59.335 1.00 38.46  ? 120 HIS G N   1 
ATOM   7533  C  CA  . HIS G  1 126 ? 97.958  145.410 59.728 1.00 35.48  ? 120 HIS G CA  1 
ATOM   7534  C  C   . HIS G  1 126 ? 98.764  145.714 60.990 1.00 40.78  ? 120 HIS G C   1 
ATOM   7535  O  O   . HIS G  1 126 ? 98.770  146.839 61.511 1.00 39.01  ? 120 HIS G O   1 
ATOM   7536  C  CB  . HIS G  1 126 ? 98.898  145.136 58.558 1.00 36.37  ? 120 HIS G CB  1 
ATOM   7537  C  CG  . HIS G  1 126 ? 98.217  144.529 57.365 1.00 43.25  ? 120 HIS G CG  1 
ATOM   7538  N  ND1 . HIS G  1 126 ? 98.354  143.199 57.023 1.00 38.54  ? 120 HIS G ND1 1 
ATOM   7539  C  CD2 . HIS G  1 126 ? 97.413  145.077 56.421 1.00 33.25  ? 120 HIS G CD2 1 
ATOM   7540  C  CE1 . HIS G  1 126 ? 97.671  142.957 55.918 1.00 36.90  ? 120 HIS G CE1 1 
ATOM   7541  N  NE2 . HIS G  1 126 ? 97.091  144.080 55.532 1.00 36.82  ? 120 HIS G NE2 1 
ATOM   7542  N  N   . GLU G  1 127 ? 99.434  144.671 61.463 1.00 40.36  ? 121 GLU G N   1 
ATOM   7543  C  CA  . GLU G  1 127 ? 100.255 144.690 62.662 1.00 52.37  ? 121 GLU G CA  1 
ATOM   7544  C  C   . GLU G  1 127 ? 101.531 145.540 62.535 1.00 57.68  ? 121 GLU G C   1 
ATOM   7545  O  O   . GLU G  1 127 ? 101.807 146.405 63.381 1.00 53.20  ? 121 GLU G O   1 
ATOM   7546  C  CB  . GLU G  1 127 ? 100.618 143.245 63.001 1.00 53.70  ? 121 GLU G CB  1 
ATOM   7547  C  CG  . GLU G  1 127 ? 101.620 143.072 64.108 1.00 63.08  ? 121 GLU G CG  1 
ATOM   7548  C  CD  . GLU G  1 127 ? 102.109 141.638 64.208 1.00 70.54  ? 121 GLU G CD  1 
ATOM   7549  O  OE1 . GLU G  1 127 ? 102.527 141.078 63.166 1.00 68.92  ? 121 GLU G OE1 1 
ATOM   7550  O  OE2 . GLU G  1 127 ? 102.078 141.076 65.326 1.00 70.85  ? 121 GLU G OE2 1 
ATOM   7551  N  N   . LYS G  1 128 ? 102.303 145.275 61.480 1.00 57.08  ? 122 LYS G N   1 
ATOM   7552  C  CA  . LYS G  1 128 ? 103.553 145.983 61.225 1.00 54.75  ? 122 LYS G CA  1 
ATOM   7553  C  C   . LYS G  1 128 ? 103.338 147.149 60.273 1.00 59.28  ? 122 LYS G C   1 
ATOM   7554  O  O   . LYS G  1 128 ? 102.252 147.326 59.703 1.00 60.53  ? 122 LYS G O   1 
ATOM   7555  C  CB  . LYS G  1 128 ? 104.596 145.051 60.593 1.00 49.37  ? 122 LYS G CB  1 
ATOM   7556  C  CG  . LYS G  1 128 ? 104.939 143.789 61.366 1.00 55.00  ? 122 LYS G CG  1 
ATOM   7557  C  CD  . LYS G  1 128 ? 106.035 143.010 60.637 1.00 59.45  ? 122 LYS G CD  1 
ATOM   7558  C  CE  . LYS G  1 128 ? 106.130 141.542 61.073 1.00 69.05  ? 122 LYS G CE  1 
ATOM   7559  N  NZ  . LYS G  1 128 ? 106.468 141.330 62.513 1.00 71.47  ? 122 LYS G NZ  1 
ATOM   7560  N  N   . ALA G  1 129 ? 104.392 147.939 60.100 1.00 54.33  ? 123 ALA G N   1 
ATOM   7561  C  CA  . ALA G  1 129 ? 104.351 149.072 59.196 1.00 54.64  ? 123 ALA G CA  1 
ATOM   7562  C  C   . ALA G  1 129 ? 104.545 148.574 57.769 1.00 53.18  ? 123 ALA G C   1 
ATOM   7563  O  O   . ALA G  1 129 ? 105.242 147.588 57.523 1.00 49.26  ? 123 ALA G O   1 
ATOM   7564  C  CB  . ALA G  1 129 ? 105.438 150.055 59.550 1.00 59.71  ? 123 ALA G CB  1 
ATOM   7565  N  N   . ASP G  1 130 ? 103.908 149.253 56.829 1.00 51.86  ? 124 ASP G N   1 
ATOM   7566  C  CA  . ASP G  1 130 ? 104.015 148.895 55.427 1.00 54.24  ? 124 ASP G CA  1 
ATOM   7567  C  C   . ASP G  1 130 ? 105.255 149.603 54.888 1.00 55.30  ? 124 ASP G C   1 
ATOM   7568  O  O   . ASP G  1 130 ? 105.397 150.814 55.061 1.00 47.92  ? 124 ASP G O   1 
ATOM   7569  C  CB  . ASP G  1 130 ? 102.761 149.367 54.689 1.00 52.61  ? 124 ASP G CB  1 
ATOM   7570  C  CG  . ASP G  1 130 ? 102.800 149.063 53.208 1.00 55.14  ? 124 ASP G CG  1 
ATOM   7571  O  OD1 . ASP G  1 130 ? 101.847 149.466 52.507 1.00 55.20  ? 124 ASP G OD1 1 
ATOM   7572  O  OD2 . ASP G  1 130 ? 103.771 148.427 52.744 1.00 58.09  ? 124 ASP G OD2 1 
ATOM   7573  N  N   . ASP G  1 131 ? 106.153 148.854 54.250 1.00 52.35  ? 125 ASP G N   1 
ATOM   7574  C  CA  . ASP G  1 131 ? 107.368 149.446 53.704 1.00 57.68  ? 125 ASP G CA  1 
ATOM   7575  C  C   . ASP G  1 131 ? 107.177 149.944 52.272 1.00 64.90  ? 125 ASP G C   1 
ATOM   7576  O  O   . ASP G  1 131 ? 108.123 149.996 51.485 1.00 71.09  ? 125 ASP G O   1 
ATOM   7577  C  CB  . ASP G  1 131 ? 108.534 148.444 53.784 1.00 50.47  ? 125 ASP G CB  1 
ATOM   7578  C  CG  . ASP G  1 131 ? 108.397 147.269 52.813 1.00 51.17  ? 125 ASP G CG  1 
ATOM   7579  O  OD1 . ASP G  1 131 ? 109.027 146.221 53.086 1.00 40.93  ? 125 ASP G OD1 1 
ATOM   7580  O  OD2 . ASP G  1 131 ? 107.696 147.385 51.778 1.00 37.50  ? 125 ASP G OD2 1 
ATOM   7581  N  N   . LEU G  1 132 ? 105.946 150.323 51.948 1.00 67.50  ? 126 LEU G N   1 
ATOM   7582  C  CA  . LEU G  1 132 ? 105.608 150.814 50.620 1.00 66.89  ? 126 LEU G CA  1 
ATOM   7583  C  C   . LEU G  1 132 ? 106.245 149.981 49.508 1.00 67.11  ? 126 LEU G C   1 
ATOM   7584  O  O   . LEU G  1 132 ? 106.376 150.433 48.370 1.00 65.82  ? 126 LEU G O   1 
ATOM   7585  C  CB  . LEU G  1 132 ? 106.013 152.279 50.492 1.00 68.87  ? 126 LEU G CB  1 
ATOM   7586  C  CG  . LEU G  1 132 ? 105.435 153.179 51.589 1.00 73.44  ? 126 LEU G CG  1 
ATOM   7587  C  CD1 . LEU G  1 132 ? 105.679 154.633 51.232 1.00 75.66  ? 126 LEU G CD1 1 
ATOM   7588  C  CD2 . LEU G  1 132 ? 103.942 152.928 51.738 1.00 77.17  ? 126 LEU G CD2 1 
ATOM   7589  N  N   . GLY G  1 133 ? 106.635 148.759 49.852 1.00 64.41  ? 127 GLY G N   1 
ATOM   7590  C  CA  . GLY G  1 133 ? 107.230 147.858 48.884 1.00 68.99  ? 127 GLY G CA  1 
ATOM   7591  C  C   . GLY G  1 133 ? 108.594 148.250 48.361 1.00 72.29  ? 127 GLY G C   1 
ATOM   7592  O  O   . GLY G  1 133 ? 108.728 148.579 47.184 1.00 70.90  ? 127 GLY G O   1 
ATOM   7593  N  N   . LYS G  1 134 ? 109.607 148.213 49.224 1.00 74.56  ? 128 LYS G N   1 
ATOM   7594  C  CA  . LYS G  1 134 ? 110.973 148.558 48.828 1.00 72.41  ? 128 LYS G CA  1 
ATOM   7595  C  C   . LYS G  1 134 ? 111.966 147.681 49.588 1.00 72.71  ? 128 LYS G C   1 
ATOM   7596  O  O   . LYS G  1 134 ? 113.157 147.679 49.288 1.00 79.26  ? 128 LYS G O   1 
ATOM   7597  C  CB  . LYS G  1 134 ? 111.280 150.029 49.137 1.00 66.45  ? 128 LYS G CB  1 
ATOM   7598  C  CG  . LYS G  1 134 ? 110.149 151.011 48.859 1.00 65.40  ? 128 LYS G CG  1 
ATOM   7599  C  CD  . LYS G  1 134 ? 109.830 151.166 47.379 1.00 58.07  ? 128 LYS G CD  1 
ATOM   7600  C  CE  . LYS G  1 134 ? 108.626 152.087 47.194 1.00 57.61  ? 128 LYS G CE  1 
ATOM   7601  N  NZ  . LYS G  1 134 ? 108.208 152.210 45.778 1.00 52.72  ? 128 LYS G NZ  1 
ATOM   7602  N  N   . GLY G  1 135 ? 111.463 146.939 50.568 1.00 73.67  ? 129 GLY G N   1 
ATOM   7603  C  CA  . GLY G  1 135 ? 112.300 146.072 51.384 1.00 75.60  ? 129 GLY G CA  1 
ATOM   7604  C  C   . GLY G  1 135 ? 113.268 145.139 50.673 1.00 77.05  ? 129 GLY G C   1 
ATOM   7605  O  O   . GLY G  1 135 ? 113.926 144.319 51.319 1.00 71.86  ? 129 GLY G O   1 
ATOM   7606  N  N   . GLY G  1 136 ? 113.350 145.244 49.350 1.00 78.97  ? 130 GLY G N   1 
ATOM   7607  C  CA  . GLY G  1 136 ? 114.266 144.404 48.600 1.00 85.08  ? 130 GLY G CA  1 
ATOM   7608  C  C   . GLY G  1 136 ? 113.812 142.977 48.365 1.00 89.62  ? 130 GLY G C   1 
ATOM   7609  O  O   . GLY G  1 136 ? 113.990 142.451 47.266 1.00 90.74  ? 130 GLY G O   1 
ATOM   7610  N  N   . ASN G  1 137 ? 113.234 142.347 49.388 1.00 93.55  ? 131 ASN G N   1 
ATOM   7611  C  CA  . ASN G  1 137 ? 112.761 140.967 49.272 1.00 93.98  ? 131 ASN G CA  1 
ATOM   7612  C  C   . ASN G  1 137 ? 111.504 140.820 48.410 1.00 94.20  ? 131 ASN G C   1 
ATOM   7613  O  O   . ASN G  1 137 ? 110.862 141.808 48.044 1.00 94.15  ? 131 ASN G O   1 
ATOM   7614  C  CB  . ASN G  1 137 ? 112.506 140.364 50.663 1.00 95.82  ? 131 ASN G CB  1 
ATOM   7615  C  CG  . ASN G  1 137 ? 111.560 141.203 51.510 1.00 98.62  ? 131 ASN G CG  1 
ATOM   7616  O  OD1 . ASN G  1 137 ? 110.458 141.550 51.082 1.00 96.41  ? 131 ASN G OD1 1 
ATOM   7617  N  ND2 . ASN G  1 137 ? 111.986 141.522 52.727 1.00 100.49 ? 131 ASN G ND2 1 
ATOM   7618  N  N   . GLU G  1 138 ? 111.169 139.574 48.087 1.00 93.87  ? 132 GLU G N   1 
ATOM   7619  C  CA  . GLU G  1 138 ? 110.002 139.256 47.265 1.00 91.10  ? 132 GLU G CA  1 
ATOM   7620  C  C   . GLU G  1 138 ? 108.692 139.606 47.970 1.00 85.85  ? 132 GLU G C   1 
ATOM   7621  O  O   . GLU G  1 138 ? 107.734 140.048 47.336 1.00 76.72  ? 132 GLU G O   1 
ATOM   7622  C  CB  . GLU G  1 138 ? 110.011 137.764 46.919 1.00 96.27  ? 132 GLU G CB  1 
ATOM   7623  C  CG  . GLU G  1 138 ? 108.847 137.299 46.058 1.00 102.81 ? 132 GLU G CG  1 
ATOM   7624  C  CD  . GLU G  1 138 ? 108.665 135.791 46.098 1.00 106.65 ? 132 GLU G CD  1 
ATOM   7625  O  OE1 . GLU G  1 138 ? 108.255 135.268 47.158 1.00 107.67 ? 132 GLU G OE1 1 
ATOM   7626  O  OE2 . GLU G  1 138 ? 108.938 135.129 45.074 1.00 105.73 ? 132 GLU G OE2 1 
ATOM   7627  N  N   . GLU G  1 139 ? 108.654 139.404 49.284 1.00 85.38  ? 133 GLU G N   1 
ATOM   7628  C  CA  . GLU G  1 139 ? 107.454 139.692 50.059 1.00 86.78  ? 133 GLU G CA  1 
ATOM   7629  C  C   . GLU G  1 139 ? 107.112 141.179 50.076 1.00 85.82  ? 133 GLU G C   1 
ATOM   7630  O  O   . GLU G  1 139 ? 105.947 141.549 50.197 1.00 87.73  ? 133 GLU G O   1 
ATOM   7631  C  CB  . GLU G  1 139 ? 107.606 139.187 51.495 1.00 85.31  ? 133 GLU G CB  1 
ATOM   7632  C  CG  . GLU G  1 139 ? 106.337 139.346 52.325 1.00 91.71  ? 133 GLU G CG  1 
ATOM   7633  C  CD  . GLU G  1 139 ? 105.222 138.386 51.918 1.00 93.53  ? 133 GLU G CD  1 
ATOM   7634  O  OE1 . GLU G  1 139 ? 105.033 138.144 50.705 1.00 91.90  ? 133 GLU G OE1 1 
ATOM   7635  O  OE2 . GLU G  1 139 ? 104.520 137.882 52.820 1.00 94.27  ? 133 GLU G OE2 1 
ATOM   7636  N  N   . SER G  1 140 ? 108.122 142.032 49.954 1.00 82.80  ? 134 SER G N   1 
ATOM   7637  C  CA  . SER G  1 140 ? 107.886 143.469 49.955 1.00 81.63  ? 134 SER G CA  1 
ATOM   7638  C  C   . SER G  1 140 ? 107.084 143.903 48.733 1.00 81.37  ? 134 SER G C   1 
ATOM   7639  O  O   . SER G  1 140 ? 106.336 144.876 48.786 1.00 79.68  ? 134 SER G O   1 
ATOM   7640  C  CB  . SER G  1 140 ? 109.215 144.233 49.986 1.00 81.54  ? 134 SER G CB  1 
ATOM   7641  O  OG  . SER G  1 140 ? 109.003 145.636 49.890 1.00 67.35  ? 134 SER G OG  1 
ATOM   7642  N  N   . THR G  1 141 ? 107.236 143.172 47.635 1.00 83.07  ? 135 THR G N   1 
ATOM   7643  C  CA  . THR G  1 141 ? 106.537 143.503 46.396 1.00 85.37  ? 135 THR G CA  1 
ATOM   7644  C  C   . THR G  1 141 ? 105.057 143.129 46.404 1.00 83.62  ? 135 THR G C   1 
ATOM   7645  O  O   . THR G  1 141 ? 104.292 143.584 45.551 1.00 81.41  ? 135 THR G O   1 
ATOM   7646  C  CB  . THR G  1 141 ? 107.206 142.817 45.189 1.00 86.76  ? 135 THR G CB  1 
ATOM   7647  O  OG1 . THR G  1 141 ? 107.332 141.414 45.452 1.00 91.44  ? 135 THR G OG1 1 
ATOM   7648  C  CG2 . THR G  1 141 ? 108.587 143.411 44.926 1.00 81.60  ? 135 THR G CG2 1 
ATOM   7649  N  N   . LYS G  1 142 ? 104.658 142.308 47.370 1.00 81.95  ? 136 LYS G N   1 
ATOM   7650  C  CA  . LYS G  1 142 ? 103.269 141.867 47.477 1.00 79.86  ? 136 LYS G CA  1 
ATOM   7651  C  C   . LYS G  1 142 ? 102.512 142.468 48.669 1.00 76.19  ? 136 LYS G C   1 
ATOM   7652  O  O   . LYS G  1 142 ? 101.557 143.238 48.499 1.00 78.91  ? 136 LYS G O   1 
ATOM   7653  C  CB  . LYS G  1 142 ? 103.215 140.340 47.580 1.00 80.82  ? 136 LYS G CB  1 
ATOM   7654  C  CG  . LYS G  1 142 ? 103.728 139.595 46.365 1.00 82.49  ? 136 LYS G CG  1 
ATOM   7655  C  CD  . LYS G  1 142 ? 103.849 138.113 46.675 1.00 83.31  ? 136 LYS G CD  1 
ATOM   7656  C  CE  . LYS G  1 142 ? 104.371 137.332 45.488 1.00 85.37  ? 136 LYS G CE  1 
ATOM   7657  N  NZ  . LYS G  1 142 ? 104.547 135.898 45.841 1.00 92.66  ? 136 LYS G NZ  1 
ATOM   7658  N  N   . THR G  1 143 ? 102.950 142.110 49.871 1.00 66.92  ? 137 THR G N   1 
ATOM   7659  C  CA  . THR G  1 143 ? 102.311 142.564 51.096 1.00 58.72  ? 137 THR G CA  1 
ATOM   7660  C  C   . THR G  1 143 ? 102.950 143.804 51.713 1.00 61.65  ? 137 THR G C   1 
ATOM   7661  O  O   . THR G  1 143 ? 102.316 144.507 52.505 1.00 60.78  ? 137 THR G O   1 
ATOM   7662  C  CB  . THR G  1 143 ? 102.333 141.451 52.147 1.00 55.64  ? 137 THR G CB  1 
ATOM   7663  O  OG1 . THR G  1 143 ? 103.578 141.480 52.851 1.00 52.68  ? 137 THR G OG1 1 
ATOM   7664  C  CG2 . THR G  1 143 ? 102.193 140.096 51.477 1.00 50.73  ? 137 THR G CG2 1 
ATOM   7665  N  N   . GLY G  1 144 ? 104.204 144.071 51.357 1.00 60.90  ? 138 GLY G N   1 
ATOM   7666  C  CA  . GLY G  1 144 ? 104.897 145.223 51.910 1.00 53.53  ? 138 GLY G CA  1 
ATOM   7667  C  C   . GLY G  1 144 ? 105.387 144.895 53.307 1.00 51.67  ? 138 GLY G C   1 
ATOM   7668  O  O   . GLY G  1 144 ? 105.727 145.785 54.094 1.00 40.90  ? 138 GLY G O   1 
ATOM   7669  N  N   . ASN G  1 145 ? 105.411 143.599 53.608 1.00 49.97  ? 139 ASN G N   1 
ATOM   7670  C  CA  . ASN G  1 145 ? 105.838 143.099 54.910 1.00 52.91  ? 139 ASN G CA  1 
ATOM   7671  C  C   . ASN G  1 145 ? 105.036 143.758 56.041 1.00 51.54  ? 139 ASN G C   1 
ATOM   7672  O  O   . ASN G  1 145 ? 105.552 143.995 57.134 1.00 46.61  ? 139 ASN G O   1 
ATOM   7673  C  CB  . ASN G  1 145 ? 107.339 143.348 55.076 1.00 57.65  ? 139 ASN G CB  1 
ATOM   7674  C  CG  . ASN G  1 145 ? 108.151 142.769 53.924 1.00 65.60  ? 139 ASN G CG  1 
ATOM   7675  O  OD1 . ASN G  1 145 ? 108.228 141.549 53.753 1.00 66.68  ? 139 ASN G OD1 1 
ATOM   7676  N  ND2 . ASN G  1 145 ? 108.748 143.644 53.119 1.00 65.45  ? 139 ASN G ND2 1 
ATOM   7677  N  N   . ALA G  1 146 ? 103.761 144.030 55.765 1.00 49.20  ? 140 ALA G N   1 
ATOM   7678  C  CA  . ALA G  1 146 ? 102.872 144.671 56.723 1.00 42.66  ? 140 ALA G CA  1 
ATOM   7679  C  C   . ALA G  1 146 ? 102.517 143.765 57.896 1.00 47.65  ? 140 ALA G C   1 
ATOM   7680  O  O   . ALA G  1 146 ? 101.916 144.214 58.875 1.00 47.70  ? 140 ALA G O   1 
ATOM   7681  C  CB  . ALA G  1 146 ? 101.613 145.117 56.023 1.00 44.60  ? 140 ALA G CB  1 
ATOM   7682  N  N   . GLY G  1 147 ? 102.879 142.489 57.799 1.00 42.18  ? 141 GLY G N   1 
ATOM   7683  C  CA  . GLY G  1 147 ? 102.577 141.571 58.878 1.00 48.80  ? 141 GLY G CA  1 
ATOM   7684  C  C   . GLY G  1 147 ? 101.130 141.116 58.891 1.00 51.01  ? 141 GLY G C   1 
ATOM   7685  O  O   . GLY G  1 147 ? 100.446 141.192 57.868 1.00 47.93  ? 141 GLY G O   1 
ATOM   7686  N  N   . SER G  1 148 ? 100.653 140.669 60.055 1.00 49.68  ? 142 SER G N   1 
ATOM   7687  C  CA  . SER G  1 148 ? 99.280  140.167 60.180 1.00 46.91  ? 142 SER G CA  1 
ATOM   7688  C  C   . SER G  1 148 ? 98.159  141.229 60.213 1.00 45.65  ? 142 SER G C   1 
ATOM   7689  O  O   . SER G  1 148 ? 98.411  142.433 60.325 1.00 40.16  ? 142 SER G O   1 
ATOM   7690  C  CB  . SER G  1 148 ? 99.175  139.235 61.400 1.00 32.62  ? 142 SER G CB  1 
ATOM   7691  O  OG  . SER G  1 148 ? 99.227  139.953 62.613 1.00 34.37  ? 142 SER G OG  1 
ATOM   7692  N  N   . ARG G  1 149 ? 96.918  140.756 60.103 1.00 45.14  ? 143 ARG G N   1 
ATOM   7693  C  CA  . ARG G  1 149 ? 95.740  141.620 60.070 1.00 38.40  ? 143 ARG G CA  1 
ATOM   7694  C  C   . ARG G  1 149 ? 95.098  141.736 61.438 1.00 35.50  ? 143 ARG G C   1 
ATOM   7695  O  O   . ARG G  1 149 ? 94.580  140.764 61.950 1.00 39.43  ? 143 ARG G O   1 
ATOM   7696  C  CB  . ARG G  1 149 ? 94.757  141.049 59.053 1.00 31.76  ? 143 ARG G CB  1 
ATOM   7697  C  CG  . ARG G  1 149 ? 95.445  140.723 57.743 1.00 30.95  ? 143 ARG G CG  1 
ATOM   7698  C  CD  . ARG G  1 149 ? 94.554  140.031 56.741 1.00 32.12  ? 143 ARG G CD  1 
ATOM   7699  N  NE  . ARG G  1 149 ? 95.336  139.599 55.586 1.00 31.01  ? 143 ARG G NE  1 
ATOM   7700  C  CZ  . ARG G  1 149 ? 94.818  139.153 54.447 1.00 29.95  ? 143 ARG G CZ  1 
ATOM   7701  N  NH1 . ARG G  1 149 ? 95.615  138.783 53.463 1.00 36.16  ? 143 ARG G NH1 1 
ATOM   7702  N  NH2 . ARG G  1 149 ? 93.510  139.085 54.283 1.00 34.02  ? 143 ARG G NH2 1 
ATOM   7703  N  N   . LEU G  1 150 ? 95.139  142.930 62.022 1.00 34.99  ? 144 LEU G N   1 
ATOM   7704  C  CA  . LEU G  1 150 ? 94.582  143.164 63.355 1.00 36.95  ? 144 LEU G CA  1 
ATOM   7705  C  C   . LEU G  1 150 ? 93.082  143.376 63.355 1.00 37.75  ? 144 LEU G C   1 
ATOM   7706  O  O   . LEU G  1 150 ? 92.374  142.915 64.254 1.00 38.60  ? 144 LEU G O   1 
ATOM   7707  C  CB  . LEU G  1 150 ? 95.248  144.384 64.011 1.00 34.50  ? 144 LEU G CB  1 
ATOM   7708  C  CG  . LEU G  1 150 ? 96.776  144.332 64.065 1.00 31.23  ? 144 LEU G CG  1 
ATOM   7709  C  CD1 . LEU G  1 150 ? 97.308  145.562 64.759 1.00 37.00  ? 144 LEU G CD1 1 
ATOM   7710  C  CD2 . LEU G  1 150 ? 97.216  143.086 64.788 1.00 25.23  ? 144 LEU G CD2 1 
ATOM   7711  N  N   . ALA G  1 151 ? 92.601  144.091 62.350 1.00 36.97  ? 145 ALA G N   1 
ATOM   7712  C  CA  . ALA G  1 151 ? 91.186  144.375 62.247 1.00 35.83  ? 145 ALA G CA  1 
ATOM   7713  C  C   . ALA G  1 151 ? 90.825  144.636 60.789 1.00 37.64  ? 145 ALA G C   1 
ATOM   7714  O  O   . ALA G  1 151 ? 91.658  145.089 60.011 1.00 37.68  ? 145 ALA G O   1 
ATOM   7715  C  CB  . ALA G  1 151 ? 90.840  145.586 63.117 1.00 21.04  ? 145 ALA G CB  1 
ATOM   7716  N  N   . CYS G  1 152 ? 89.586  144.320 60.426 1.00 36.25  ? 146 CYS G N   1 
ATOM   7717  C  CA  . CYS G  1 152 ? 89.092  144.533 59.075 1.00 31.36  ? 146 CYS G CA  1 
ATOM   7718  C  C   . CYS G  1 152 ? 87.606  144.818 59.116 1.00 33.36  ? 146 CYS G C   1 
ATOM   7719  O  O   . CYS G  1 152 ? 86.974  144.730 60.166 1.00 35.29  ? 146 CYS G O   1 
ATOM   7720  C  CB  . CYS G  1 152 ? 89.351  143.319 58.195 1.00 22.71  ? 146 CYS G CB  1 
ATOM   7721  S  SG  . CYS G  1 152 ? 88.775  141.729 58.876 1.00 40.89  ? 146 CYS G SG  1 
ATOM   7722  N  N   . GLY G  1 153 ? 87.059  145.186 57.968 1.00 32.65  ? 147 GLY G N   1 
ATOM   7723  C  CA  . GLY G  1 153 ? 85.647  145.479 57.880 1.00 27.44  ? 147 GLY G CA  1 
ATOM   7724  C  C   . GLY G  1 153 ? 85.279  145.569 56.415 1.00 37.91  ? 147 GLY G C   1 
ATOM   7725  O  O   . GLY G  1 153 ? 86.130  145.849 55.562 1.00 36.52  ? 147 GLY G O   1 
ATOM   7726  N  N   . VAL G  1 154 ? 84.019  145.306 56.105 1.00 35.29  ? 148 VAL G N   1 
ATOM   7727  C  CA  . VAL G  1 154 ? 83.582  145.396 54.728 1.00 31.65  ? 148 VAL G CA  1 
ATOM   7728  C  C   . VAL G  1 154 ? 83.128  146.828 54.503 1.00 33.59  ? 148 VAL G C   1 
ATOM   7729  O  O   . VAL G  1 154 ? 82.386  147.385 55.315 1.00 28.78  ? 148 VAL G O   1 
ATOM   7730  C  CB  . VAL G  1 154 ? 82.436  144.423 54.445 1.00 28.49  ? 148 VAL G CB  1 
ATOM   7731  C  CG1 . VAL G  1 154 ? 81.982  144.560 52.995 1.00 26.22  ? 148 VAL G CG1 1 
ATOM   7732  C  CG2 . VAL G  1 154 ? 82.907  143.008 54.719 1.00 23.66  ? 148 VAL G CG2 1 
ATOM   7733  N  N   . ILE G  1 155 ? 83.586  147.418 53.400 1.00 36.74  ? 149 ILE G N   1 
ATOM   7734  C  CA  . ILE G  1 155 ? 83.258  148.799 53.056 1.00 30.48  ? 149 ILE G CA  1 
ATOM   7735  C  C   . ILE G  1 155 ? 81.860  148.863 52.448 1.00 34.89  ? 149 ILE G C   1 
ATOM   7736  O  O   . ILE G  1 155 ? 81.587  148.239 51.416 1.00 29.69  ? 149 ILE G O   1 
ATOM   7737  C  CB  . ILE G  1 155 ? 84.290  149.360 52.052 1.00 30.17  ? 149 ILE G CB  1 
ATOM   7738  C  CG1 . ILE G  1 155 ? 85.695  149.258 52.656 1.00 33.90  ? 149 ILE G CG1 1 
ATOM   7739  C  CG2 . ILE G  1 155 ? 83.967  150.807 51.712 1.00 28.30  ? 149 ILE G CG2 1 
ATOM   7740  C  CD1 . ILE G  1 155 ? 86.819  149.379 51.642 1.00 30.89  ? 149 ILE G CD1 1 
ATOM   7741  N  N   . GLY G  1 156 ? 80.978  149.619 53.090 1.00 30.50  ? 150 GLY G N   1 
ATOM   7742  C  CA  . GLY G  1 156 ? 79.620  149.723 52.599 1.00 32.55  ? 150 GLY G CA  1 
ATOM   7743  C  C   . GLY G  1 156 ? 79.218  151.113 52.161 1.00 35.92  ? 150 GLY G C   1 
ATOM   7744  O  O   . GLY G  1 156 ? 79.898  152.092 52.435 1.00 38.83  ? 150 GLY G O   1 
ATOM   7745  N  N   . ILE G  1 157 ? 78.098  151.194 51.459 1.00 44.44  ? 151 ILE G N   1 
ATOM   7746  C  CA  . ILE G  1 157 ? 77.587  152.468 50.983 1.00 43.34  ? 151 ILE G CA  1 
ATOM   7747  C  C   . ILE G  1 157 ? 76.988  153.199 52.167 1.00 41.80  ? 151 ILE G C   1 
ATOM   7748  O  O   . ILE G  1 157 ? 76.252  152.609 52.952 1.00 42.80  ? 151 ILE G O   1 
ATOM   7749  C  CB  . ILE G  1 157 ? 76.478  152.264 49.939 1.00 45.03  ? 151 ILE G CB  1 
ATOM   7750  C  CG1 . ILE G  1 157 ? 77.014  151.448 48.771 1.00 51.71  ? 151 ILE G CG1 1 
ATOM   7751  C  CG2 . ILE G  1 157 ? 75.961  153.598 49.452 1.00 43.41  ? 151 ILE G CG2 1 
ATOM   7752  C  CD1 . ILE G  1 157 ? 75.951  151.090 47.768 1.00 59.00  ? 151 ILE G CD1 1 
ATOM   7753  N  N   . ALA G  1 158 ? 77.312  154.479 52.301 1.00 43.94  ? 152 ALA G N   1 
ATOM   7754  C  CA  . ALA G  1 158 ? 76.769  155.287 53.385 1.00 50.43  ? 152 ALA G CA  1 
ATOM   7755  C  C   . ALA G  1 158 ? 75.837  156.354 52.811 1.00 50.71  ? 152 ALA G C   1 
ATOM   7756  O  O   . ALA G  1 158 ? 75.904  156.684 51.627 1.00 52.44  ? 152 ALA G O   1 
ATOM   7757  C  CB  . ALA G  1 158 ? 77.899  155.943 54.177 1.00 37.69  ? 152 ALA G CB  1 
ATOM   7758  N  N   . GLN G  1 159 ? 74.967  156.885 53.658 1.00 53.99  ? 153 GLN G N   1 
ATOM   7759  C  CA  . GLN G  1 159 ? 74.035  157.913 53.239 1.00 58.72  ? 153 GLN G CA  1 
ATOM   7760  C  C   . GLN G  1 159 ? 74.745  159.251 53.044 1.00 65.40  ? 153 GLN G C   1 
ATOM   7761  O  O   . GLN G  1 159 ? 75.801  159.473 53.679 1.00 63.97  ? 153 GLN G O   1 
ATOM   7762  C  CB  . GLN G  1 159 ? 72.935  158.051 54.285 1.00 57.99  ? 153 GLN G CB  1 
ATOM   7763  C  CG  . GLN G  1 159 ? 72.164  159.349 54.224 1.00 57.06  ? 153 GLN G CG  1 
ATOM   7764  C  CD  . GLN G  1 159 ? 70.893  159.283 55.036 1.00 61.59  ? 153 GLN G CD  1 
ATOM   7765  O  OE1 . GLN G  1 159 ? 69.831  158.928 54.520 1.00 59.56  ? 153 GLN G OE1 1 
ATOM   7766  N  NE2 . GLN G  1 159 ? 70.993  159.607 56.320 1.00 65.63  ? 153 GLN G NE2 1 
ATOM   7767  O  OXT . GLN G  1 159 ? 74.222  160.071 52.260 1.00 73.76  ? 153 GLN G OXT 1 
ATOM   7768  N  N   . ALA H  1 7   ? 82.120  139.622 39.353 1.00 76.68  ? 1   ALA H N   1 
ATOM   7769  C  CA  . ALA H  1 7   ? 81.078  139.891 40.389 1.00 79.21  ? 1   ALA H CA  1 
ATOM   7770  C  C   . ALA H  1 7   ? 79.960  138.835 40.334 1.00 75.46  ? 1   ALA H C   1 
ATOM   7771  O  O   . ALA H  1 7   ? 78.796  139.163 40.101 1.00 75.75  ? 1   ALA H O   1 
ATOM   7772  C  CB  . ALA H  1 7   ? 80.499  141.297 40.176 1.00 79.55  ? 1   ALA H CB  1 
ATOM   7773  N  N   . THR H  1 8   ? 80.313  137.573 40.568 1.00 67.74  ? 2   THR H N   1 
ATOM   7774  C  CA  . THR H  1 8   ? 79.334  136.498 40.515 1.00 59.61  ? 2   THR H CA  1 
ATOM   7775  C  C   . THR H  1 8   ? 79.025  135.818 41.855 1.00 53.19  ? 2   THR H C   1 
ATOM   7776  O  O   . THR H  1 8   ? 78.036  135.103 41.972 1.00 53.89  ? 2   THR H O   1 
ATOM   7777  C  CB  . THR H  1 8   ? 79.764  135.431 39.485 1.00 62.70  ? 2   THR H CB  1 
ATOM   7778  O  OG1 . THR H  1 8   ? 80.977  134.799 39.913 1.00 61.31  ? 2   THR H OG1 1 
ATOM   7779  C  CG2 . THR H  1 8   ? 79.999  136.083 38.128 1.00 65.52  ? 2   THR H CG2 1 
ATOM   7780  N  N   . LYS H  1 9   ? 79.864  136.026 42.862 1.00 46.64  ? 3   LYS H N   1 
ATOM   7781  C  CA  . LYS H  1 9   ? 79.624  135.441 44.184 1.00 41.20  ? 3   LYS H CA  1 
ATOM   7782  C  C   . LYS H  1 9   ? 79.769  136.526 45.250 1.00 38.42  ? 3   LYS H C   1 
ATOM   7783  O  O   . LYS H  1 9   ? 80.723  137.305 45.228 1.00 36.39  ? 3   LYS H O   1 
ATOM   7784  C  CB  . LYS H  1 9   ? 80.615  134.310 44.469 1.00 46.95  ? 3   LYS H CB  1 
ATOM   7785  C  CG  . LYS H  1 9   ? 80.048  132.884 44.425 1.00 56.87  ? 3   LYS H CG  1 
ATOM   7786  C  CD  . LYS H  1 9   ? 81.191  131.849 44.337 1.00 61.90  ? 3   LYS H CD  1 
ATOM   7787  C  CE  . LYS H  1 9   ? 80.723  130.395 44.455 1.00 63.71  ? 3   LYS H CE  1 
ATOM   7788  N  NZ  . LYS H  1 9   ? 80.443  129.968 45.864 1.00 70.66  ? 3   LYS H NZ  1 
ATOM   7789  N  N   . ALA H  1 10  ? 78.811  136.586 46.168 1.00 32.94  ? 4   ALA H N   1 
ATOM   7790  C  CA  . ALA H  1 10  ? 78.829  137.564 47.246 1.00 29.48  ? 4   ALA H CA  1 
ATOM   7791  C  C   . ALA H  1 10  ? 78.537  136.844 48.539 1.00 30.74  ? 4   ALA H C   1 
ATOM   7792  O  O   . ALA H  1 10  ? 77.936  135.775 48.529 1.00 31.19  ? 4   ALA H O   1 
ATOM   7793  C  CB  . ALA H  1 10  ? 77.791  138.627 47.008 1.00 35.55  ? 4   ALA H CB  1 
ATOM   7794  N  N   . VAL H  1 11  ? 78.941  137.427 49.665 1.00 31.51  ? 5   VAL H N   1 
ATOM   7795  C  CA  . VAL H  1 11  ? 78.715  136.769 50.944 1.00 27.47  ? 5   VAL H CA  1 
ATOM   7796  C  C   . VAL H  1 11  ? 78.440  137.809 51.995 1.00 32.18  ? 5   VAL H C   1 
ATOM   7797  O  O   . VAL H  1 11  ? 78.712  138.986 51.785 1.00 33.03  ? 5   VAL H O   1 
ATOM   7798  C  CB  . VAL H  1 11  ? 79.939  135.914 51.373 1.00 30.45  ? 5   VAL H CB  1 
ATOM   7799  C  CG1 . VAL H  1 11  ? 81.079  136.811 51.819 1.00 30.53  ? 5   VAL H CG1 1 
ATOM   7800  C  CG2 . VAL H  1 11  ? 79.544  134.972 52.469 1.00 26.12  ? 5   VAL H CG2 1 
ATOM   7801  N  N   . CYS H  1 12  ? 77.921  137.365 53.135 1.00 30.52  ? 6   CYS H N   1 
ATOM   7802  C  CA  . CYS H  1 12  ? 77.551  138.274 54.204 1.00 31.15  ? 6   CYS H CA  1 
ATOM   7803  C  C   . CYS H  1 12  ? 77.551  137.583 55.561 1.00 31.06  ? 6   CYS H C   1 
ATOM   7804  O  O   . CYS H  1 12  ? 76.937  136.529 55.728 1.00 33.08  ? 6   CYS H O   1 
ATOM   7805  C  CB  . CYS H  1 12  ? 76.148  138.820 53.913 1.00 28.04  ? 6   CYS H CB  1 
ATOM   7806  S  SG  . CYS H  1 12  ? 75.403  139.778 55.231 1.00 37.06  ? 6   CYS H SG  1 
ATOM   7807  N  N   . VAL H  1 13  ? 78.230  138.177 56.534 1.00 27.27  ? 7   VAL H N   1 
ATOM   7808  C  CA  . VAL H  1 13  ? 78.269  137.595 57.868 1.00 24.57  ? 7   VAL H CA  1 
ATOM   7809  C  C   . VAL H  1 13  ? 77.283  138.365 58.717 1.00 27.20  ? 7   VAL H C   1 
ATOM   7810  O  O   . VAL H  1 13  ? 77.382  139.581 58.845 1.00 27.11  ? 7   VAL H O   1 
ATOM   7811  C  CB  . VAL H  1 13  ? 79.680  137.691 58.491 1.00 28.91  ? 7   VAL H CB  1 
ATOM   7812  C  CG1 . VAL H  1 13  ? 79.643  137.262 59.964 1.00 27.78  ? 7   VAL H CG1 1 
ATOM   7813  C  CG2 . VAL H  1 13  ? 80.653  136.809 57.704 1.00 20.33  ? 7   VAL H CG2 1 
ATOM   7814  N  N   . LEU H  1 14  ? 76.311  137.656 59.279 1.00 31.70  ? 8   LEU H N   1 
ATOM   7815  C  CA  . LEU H  1 14  ? 75.296  138.289 60.110 1.00 30.30  ? 8   LEU H CA  1 
ATOM   7816  C  C   . LEU H  1 14  ? 75.583  138.233 61.608 1.00 30.67  ? 8   LEU H C   1 
ATOM   7817  O  O   . LEU H  1 14  ? 75.895  137.170 62.170 1.00 28.48  ? 8   LEU H O   1 
ATOM   7818  C  CB  . LEU H  1 14  ? 73.939  137.651 59.828 1.00 34.04  ? 8   LEU H CB  1 
ATOM   7819  C  CG  . LEU H  1 14  ? 73.388  137.838 58.416 1.00 30.80  ? 8   LEU H CG  1 
ATOM   7820  C  CD1 . LEU H  1 14  ? 72.053  137.130 58.286 1.00 30.58  ? 8   LEU H CD1 1 
ATOM   7821  C  CD2 . LEU H  1 14  ? 73.219  139.312 58.144 1.00 35.14  ? 8   LEU H CD2 1 
ATOM   7822  N  N   . LYS H  1 15  ? 75.472  139.391 62.249 1.00 29.75  ? 9   LYS H N   1 
ATOM   7823  C  CA  . LYS H  1 15  ? 75.698  139.519 63.687 1.00 30.43  ? 9   LYS H CA  1 
ATOM   7824  C  C   . LYS H  1 15  ? 74.748  140.588 64.205 1.00 31.25  ? 9   LYS H C   1 
ATOM   7825  O  O   . LYS H  1 15  ? 74.303  141.460 63.453 1.00 29.44  ? 9   LYS H O   1 
ATOM   7826  C  CB  . LYS H  1 15  ? 77.144  139.951 63.986 1.00 34.96  ? 9   LYS H CB  1 
ATOM   7827  C  CG  . LYS H  1 15  ? 78.264  139.001 63.501 1.00 49.16  ? 9   LYS H CG  1 
ATOM   7828  C  CD  . LYS H  1 15  ? 78.491  137.803 64.437 1.00 57.58  ? 9   LYS H CD  1 
ATOM   7829  C  CE  . LYS H  1 15  ? 79.656  136.923 63.965 1.00 59.11  ? 9   LYS H CE  1 
ATOM   7830  N  NZ  . LYS H  1 15  ? 80.940  137.684 63.800 1.00 52.36  ? 9   LYS H NZ  1 
ATOM   7831  N  N   . GLY H  1 16  ? 74.433  140.518 65.492 1.00 33.71  ? 10  GLY H N   1 
ATOM   7832  C  CA  . GLY H  1 16  ? 73.549  141.507 66.084 1.00 40.11  ? 10  GLY H CA  1 
ATOM   7833  C  C   . GLY H  1 16  ? 73.834  141.680 67.562 1.00 41.19  ? 10  GLY H C   1 
ATOM   7834  O  O   . GLY H  1 16  ? 74.858  141.208 68.060 1.00 43.28  ? 10  GLY H O   1 
ATOM   7835  N  N   . ASP H  1 17  ? 72.926  142.349 68.267 1.00 41.41  ? 11  ASP H N   1 
ATOM   7836  C  CA  . ASP H  1 17  ? 73.081  142.573 69.707 1.00 48.05  ? 11  ASP H CA  1 
ATOM   7837  C  C   . ASP H  1 17  ? 72.719  141.345 70.530 1.00 48.05  ? 11  ASP H C   1 
ATOM   7838  O  O   . ASP H  1 17  ? 73.119  141.230 71.687 1.00 54.52  ? 11  ASP H O   1 
ATOM   7839  C  CB  . ASP H  1 17  ? 72.213  143.747 70.150 1.00 50.23  ? 11  ASP H CB  1 
ATOM   7840  C  CG  . ASP H  1 17  ? 72.800  145.074 69.744 1.00 59.38  ? 11  ASP H CG  1 
ATOM   7841  O  OD1 . ASP H  1 17  ? 72.027  146.040 69.599 1.00 60.09  ? 11  ASP H OD1 1 
ATOM   7842  O  OD2 . ASP H  1 17  ? 74.039  145.149 69.578 1.00 62.17  ? 11  ASP H OD2 1 
ATOM   7843  N  N   . GLY H  1 18  ? 71.959  140.436 69.926 1.00 42.05  ? 12  GLY H N   1 
ATOM   7844  C  CA  . GLY H  1 18  ? 71.551  139.231 70.613 1.00 33.57  ? 12  GLY H CA  1 
ATOM   7845  C  C   . GLY H  1 18  ? 72.295  138.002 70.133 1.00 35.64  ? 12  GLY H C   1 
ATOM   7846  O  O   . GLY H  1 18  ? 73.423  138.101 69.653 1.00 35.62  ? 12  GLY H O   1 
ATOM   7847  N  N   . PRO H  1 19  ? 71.667  136.820 70.219 1.00 32.46  ? 13  PRO H N   1 
ATOM   7848  C  CA  . PRO H  1 19  ? 72.268  135.552 69.802 1.00 26.74  ? 13  PRO H CA  1 
ATOM   7849  C  C   . PRO H  1 19  ? 72.181  135.246 68.321 1.00 33.01  ? 13  PRO H C   1 
ATOM   7850  O  O   . PRO H  1 19  ? 72.762  134.258 67.870 1.00 36.51  ? 13  PRO H O   1 
ATOM   7851  C  CB  . PRO H  1 19  ? 71.470  134.537 70.595 1.00 26.60  ? 13  PRO H CB  1 
ATOM   7852  C  CG  . PRO H  1 19  ? 70.070  135.120 70.483 1.00 29.28  ? 13  PRO H CG  1 
ATOM   7853  C  CD  . PRO H  1 19  ? 70.302  136.605 70.744 1.00 23.90  ? 13  PRO H CD  1 
ATOM   7854  N  N   . VAL H  1 20  ? 71.444  136.056 67.563 1.00 28.08  ? 14  VAL H N   1 
ATOM   7855  C  CA  . VAL H  1 20  ? 71.299  135.764 66.145 1.00 31.36  ? 14  VAL H CA  1 
ATOM   7856  C  C   . VAL H  1 20  ? 72.576  136.042 65.368 1.00 33.55  ? 14  VAL H C   1 
ATOM   7857  O  O   . VAL H  1 20  ? 73.203  137.080 65.537 1.00 35.83  ? 14  VAL H O   1 
ATOM   7858  C  CB  . VAL H  1 20  ? 70.114  136.531 65.520 1.00 22.71  ? 14  VAL H CB  1 
ATOM   7859  C  CG1 . VAL H  1 20  ? 69.931  136.106 64.065 1.00 22.82  ? 14  VAL H CG1 1 
ATOM   7860  C  CG2 . VAL H  1 20  ? 68.837  136.222 66.293 1.00 24.62  ? 14  VAL H CG2 1 
ATOM   7861  N  N   . GLN H  1 21  ? 72.964  135.087 64.529 1.00 32.48  ? 15  GLN H N   1 
ATOM   7862  C  CA  . GLN H  1 21  ? 74.173  135.219 63.734 1.00 32.61  ? 15  GLN H CA  1 
ATOM   7863  C  C   . GLN H  1 21  ? 74.187  134.138 62.663 1.00 27.26  ? 15  GLN H C   1 
ATOM   7864  O  O   . GLN H  1 21  ? 73.639  133.055 62.857 1.00 24.87  ? 15  GLN H O   1 
ATOM   7865  C  CB  . GLN H  1 21  ? 75.377  135.040 64.631 1.00 40.57  ? 15  GLN H CB  1 
ATOM   7866  C  CG  . GLN H  1 21  ? 75.449  133.645 65.208 1.00 54.38  ? 15  GLN H CG  1 
ATOM   7867  C  CD  . GLN H  1 21  ? 76.520  133.519 66.257 1.00 65.00  ? 15  GLN H CD  1 
ATOM   7868  O  OE1 . GLN H  1 21  ? 77.692  133.804 65.997 1.00 63.43  ? 15  GLN H OE1 1 
ATOM   7869  N  NE2 . GLN H  1 21  ? 76.128  133.094 67.459 1.00 66.79  ? 15  GLN H NE2 1 
ATOM   7870  N  N   . GLY H  1 22  ? 74.816  134.429 61.532 1.00 20.78  ? 16  GLY H N   1 
ATOM   7871  C  CA  . GLY H  1 22  ? 74.873  133.441 60.473 1.00 21.76  ? 16  GLY H CA  1 
ATOM   7872  C  C   . GLY H  1 22  ? 75.692  133.922 59.302 1.00 26.29  ? 16  GLY H C   1 
ATOM   7873  O  O   . GLY H  1 22  ? 76.208  135.044 59.330 1.00 30.22  ? 16  GLY H O   1 
ATOM   7874  N  N   . ILE H  1 23  ? 75.805  133.073 58.283 1.00 16.68  ? 17  ILE H N   1 
ATOM   7875  C  CA  . ILE H  1 23  ? 76.541  133.382 57.071 1.00 24.43  ? 17  ILE H CA  1 
ATOM   7876  C  C   . ILE H  1 23  ? 75.610  133.140 55.883 1.00 32.61  ? 17  ILE H C   1 
ATOM   7877  O  O   . ILE H  1 23  ? 74.994  132.079 55.772 1.00 26.82  ? 17  ILE H O   1 
ATOM   7878  C  CB  . ILE H  1 23  ? 77.773  132.476 56.918 1.00 26.19  ? 17  ILE H CB  1 
ATOM   7879  C  CG1 . ILE H  1 23  ? 78.743  132.728 58.067 1.00 28.95  ? 17  ILE H CG1 1 
ATOM   7880  C  CG2 . ILE H  1 23  ? 78.464  132.735 55.589 1.00 19.36  ? 17  ILE H CG2 1 
ATOM   7881  C  CD1 . ILE H  1 23  ? 80.007  131.906 57.971 1.00 24.46  ? 17  ILE H CD1 1 
ATOM   7882  N  N   . ILE H  1 24  ? 75.514  134.121 54.993 1.00 24.32  ? 18  ILE H N   1 
ATOM   7883  C  CA  . ILE H  1 24  ? 74.649  133.994 53.834 1.00 22.84  ? 18  ILE H CA  1 
ATOM   7884  C  C   . ILE H  1 24  ? 75.422  134.206 52.541 1.00 26.09  ? 18  ILE H C   1 
ATOM   7885  O  O   . ILE H  1 24  ? 76.161  135.182 52.383 1.00 25.75  ? 18  ILE H O   1 
ATOM   7886  C  CB  . ILE H  1 24  ? 73.500  135.008 53.914 1.00 21.33  ? 18  ILE H CB  1 
ATOM   7887  C  CG1 . ILE H  1 24  ? 72.637  134.707 55.145 1.00 28.40  ? 18  ILE H CG1 1 
ATOM   7888  C  CG2 . ILE H  1 24  ? 72.649  134.931 52.682 1.00 19.80  ? 18  ILE H CG2 1 
ATOM   7889  C  CD1 . ILE H  1 24  ? 71.796  133.443 55.011 1.00 11.86  ? 18  ILE H CD1 1 
ATOM   7890  N  N   . ASN H  1 25  ? 75.221  133.287 51.608 1.00 27.87  ? 19  ASN H N   1 
ATOM   7891  C  CA  . ASN H  1 25  ? 75.886  133.314 50.316 1.00 30.83  ? 19  ASN H CA  1 
ATOM   7892  C  C   . ASN H  1 25  ? 74.986  133.754 49.176 1.00 33.73  ? 19  ASN H C   1 
ATOM   7893  O  O   . ASN H  1 25  ? 73.801  133.420 49.136 1.00 34.92  ? 19  ASN H O   1 
ATOM   7894  C  CB  . ASN H  1 25  ? 76.430  131.923 50.011 1.00 34.22  ? 19  ASN H CB  1 
ATOM   7895  C  CG  . ASN H  1 25  ? 77.504  131.496 50.992 1.00 34.77  ? 19  ASN H CG  1 
ATOM   7896  O  OD1 . ASN H  1 25  ? 78.628  131.993 50.944 1.00 37.91  ? 19  ASN H OD1 1 
ATOM   7897  N  ND2 . ASN H  1 25  ? 77.159  130.590 51.899 1.00 30.19  ? 19  ASN H ND2 1 
ATOM   7898  N  N   . PHE H  1 26  ? 75.573  134.491 48.239 1.00 34.54  ? 20  PHE H N   1 
ATOM   7899  C  CA  . PHE H  1 26  ? 74.864  134.984 47.065 1.00 36.22  ? 20  PHE H CA  1 
ATOM   7900  C  C   . PHE H  1 26  ? 75.617  134.549 45.812 1.00 40.73  ? 20  PHE H C   1 
ATOM   7901  O  O   . PHE H  1 26  ? 76.778  134.908 45.625 1.00 39.92  ? 20  PHE H O   1 
ATOM   7902  C  CB  . PHE H  1 26  ? 74.796  136.512 47.077 1.00 35.45  ? 20  PHE H CB  1 
ATOM   7903  C  CG  . PHE H  1 26  ? 74.067  137.083 48.247 1.00 40.06  ? 20  PHE H CG  1 
ATOM   7904  C  CD1 . PHE H  1 26  ? 72.708  137.356 48.168 1.00 38.21  ? 20  PHE H CD1 1 
ATOM   7905  C  CD2 . PHE H  1 26  ? 74.743  137.362 49.432 1.00 38.31  ? 20  PHE H CD2 1 
ATOM   7906  C  CE1 . PHE H  1 26  ? 72.031  137.901 49.248 1.00 32.18  ? 20  PHE H CE1 1 
ATOM   7907  C  CE2 . PHE H  1 26  ? 74.076  137.906 50.517 1.00 30.10  ? 20  PHE H CE2 1 
ATOM   7908  C  CZ  . PHE H  1 26  ? 72.715  138.178 50.425 1.00 31.28  ? 20  PHE H CZ  1 
ATOM   7909  N  N   . GLU H  1 27  ? 74.969  133.781 44.949 1.00 37.58  ? 21  GLU H N   1 
ATOM   7910  C  CA  . GLU H  1 27  ? 75.626  133.360 43.728 1.00 40.95  ? 21  GLU H CA  1 
ATOM   7911  C  C   . GLU H  1 27  ? 74.772  133.784 42.544 1.00 37.72  ? 21  GLU H C   1 
ATOM   7912  O  O   . GLU H  1 27  ? 73.562  133.558 42.524 1.00 38.82  ? 21  GLU H O   1 
ATOM   7913  C  CB  . GLU H  1 27  ? 75.836  131.846 43.725 1.00 47.88  ? 21  GLU H CB  1 
ATOM   7914  C  CG  . GLU H  1 27  ? 76.756  131.370 42.605 1.00 68.98  ? 21  GLU H CG  1 
ATOM   7915  C  CD  . GLU H  1 27  ? 77.003  129.867 42.620 1.00 77.09  ? 21  GLU H CD  1 
ATOM   7916  O  OE1 . GLU H  1 27  ? 77.453  129.335 43.660 1.00 81.95  ? 21  GLU H OE1 1 
ATOM   7917  O  OE2 . GLU H  1 27  ? 76.751  129.217 41.582 1.00 81.82  ? 21  GLU H OE2 1 
ATOM   7918  N  N   . GLN H  1 28  ? 75.395  134.429 41.569 1.00 34.97  ? 22  GLN H N   1 
ATOM   7919  C  CA  . GLN H  1 28  ? 74.681  134.876 40.380 1.00 42.89  ? 22  GLN H CA  1 
ATOM   7920  C  C   . GLN H  1 28  ? 75.432  134.385 39.154 1.00 45.52  ? 22  GLN H C   1 
ATOM   7921  O  O   . GLN H  1 28  ? 76.470  134.934 38.794 1.00 47.92  ? 22  GLN H O   1 
ATOM   7922  C  CB  . GLN H  1 28  ? 74.581  136.405 40.364 1.00 39.62  ? 22  GLN H CB  1 
ATOM   7923  C  CG  . GLN H  1 28  ? 73.844  136.974 39.163 1.00 39.27  ? 22  GLN H CG  1 
ATOM   7924  C  CD  . GLN H  1 28  ? 73.577  138.461 39.286 1.00 41.48  ? 22  GLN H CD  1 
ATOM   7925  O  OE1 . GLN H  1 28  ? 74.494  139.259 39.475 1.00 44.96  ? 22  GLN H OE1 1 
ATOM   7926  N  NE2 . GLN H  1 28  ? 72.310  138.843 39.177 1.00 46.76  ? 22  GLN H NE2 1 
ATOM   7927  N  N   . LYS H  1 29  ? 74.913  133.353 38.505 1.00 51.35  ? 23  LYS H N   1 
ATOM   7928  C  CA  . LYS H  1 29  ? 75.593  132.817 37.333 1.00 59.74  ? 23  LYS H CA  1 
ATOM   7929  C  C   . LYS H  1 29  ? 75.492  133.674 36.063 1.00 57.95  ? 23  LYS H C   1 
ATOM   7930  O  O   . LYS H  1 29  ? 76.285  133.501 35.156 1.00 57.78  ? 23  LYS H O   1 
ATOM   7931  C  CB  . LYS H  1 29  ? 75.114  131.383 37.066 1.00 65.22  ? 23  LYS H CB  1 
ATOM   7932  C  CG  . LYS H  1 29  ? 75.488  130.406 38.185 1.00 73.17  ? 23  LYS H CG  1 
ATOM   7933  C  CD  . LYS H  1 29  ? 74.912  129.002 37.972 1.00 83.48  ? 23  LYS H CD  1 
ATOM   7934  C  CE  . LYS H  1 29  ? 75.280  128.063 39.128 1.00 85.33  ? 23  LYS H CE  1 
ATOM   7935  N  NZ  . LYS H  1 29  ? 74.704  126.691 38.998 1.00 88.50  ? 23  LYS H NZ  1 
ATOM   7936  N  N   . GLU H  1 30  ? 74.537  134.600 36.000 1.00 61.44  ? 24  GLU H N   1 
ATOM   7937  C  CA  . GLU H  1 30  ? 74.390  135.470 34.825 1.00 66.98  ? 24  GLU H CA  1 
ATOM   7938  C  C   . GLU H  1 30  ? 74.105  136.922 35.208 1.00 72.26  ? 24  GLU H C   1 
ATOM   7939  O  O   . GLU H  1 30  ? 73.347  137.188 36.140 1.00 74.82  ? 24  GLU H O   1 
ATOM   7940  C  CB  . GLU H  1 30  ? 73.262  134.978 33.918 1.00 65.51  ? 24  GLU H CB  1 
ATOM   7941  C  CG  . GLU H  1 30  ? 73.543  133.687 33.204 1.00 65.08  ? 24  GLU H CG  1 
ATOM   7942  C  CD  . GLU H  1 30  ? 72.323  133.158 32.489 1.00 63.84  ? 24  GLU H CD  1 
ATOM   7943  O  OE1 . GLU H  1 30  ? 71.323  132.849 33.167 1.00 62.82  ? 24  GLU H OE1 1 
ATOM   7944  O  OE2 . GLU H  1 30  ? 72.361  133.055 31.250 1.00 65.81  ? 24  GLU H OE2 1 
ATOM   7945  N  N   . SER H  1 31  ? 74.702  137.855 34.470 1.00 78.04  ? 25  SER H N   1 
ATOM   7946  C  CA  . SER H  1 31  ? 74.525  139.282 34.728 1.00 83.24  ? 25  SER H CA  1 
ATOM   7947  C  C   . SER H  1 31  ? 73.065  139.643 34.981 1.00 82.58  ? 25  SER H C   1 
ATOM   7948  O  O   . SER H  1 31  ? 72.717  140.110 36.061 1.00 85.77  ? 25  SER H O   1 
ATOM   7949  C  CB  . SER H  1 31  ? 75.075  140.103 33.556 1.00 86.26  ? 25  SER H CB  1 
ATOM   7950  O  OG  . SER H  1 31  ? 74.527  139.675 32.323 1.00 88.59  ? 25  SER H OG  1 
ATOM   7951  N  N   . ASN H  1 32  ? 72.213  139.429 33.989 1.00 81.64  ? 26  ASN H N   1 
ATOM   7952  C  CA  . ASN H  1 32  ? 70.793  139.724 34.141 1.00 84.43  ? 26  ASN H CA  1 
ATOM   7953  C  C   . ASN H  1 32  ? 70.041  138.433 34.488 1.00 80.86  ? 26  ASN H C   1 
ATOM   7954  O  O   . ASN H  1 32  ? 69.027  138.097 33.870 1.00 81.41  ? 26  ASN H O   1 
ATOM   7955  C  CB  . ASN H  1 32  ? 70.239  140.327 32.844 1.00 89.00  ? 26  ASN H CB  1 
ATOM   7956  C  CG  . ASN H  1 32  ? 70.549  139.472 31.620 1.00 96.68  ? 26  ASN H CG  1 
ATOM   7957  O  OD1 . ASN H  1 32  ? 70.293  138.263 31.606 1.00 95.55  ? 26  ASN H OD1 1 
ATOM   7958  N  ND2 . ASN H  1 32  ? 71.097  140.100 30.582 1.00 96.70  ? 26  ASN H ND2 1 
ATOM   7959  N  N   . GLY H  1 33  ? 70.549  137.709 35.480 1.00 72.72  ? 27  GLY H N   1 
ATOM   7960  C  CA  . GLY H  1 33  ? 69.917  136.464 35.871 1.00 63.33  ? 27  GLY H CA  1 
ATOM   7961  C  C   . GLY H  1 33  ? 69.594  136.362 37.348 1.00 57.83  ? 27  GLY H C   1 
ATOM   7962  O  O   . GLY H  1 33  ? 69.878  137.277 38.129 1.00 59.74  ? 27  GLY H O   1 
ATOM   7963  N  N   . PRO H  1 34  ? 68.986  135.246 37.764 1.00 50.56  ? 28  PRO H N   1 
ATOM   7964  C  CA  . PRO H  1 34  ? 68.624  135.037 39.165 1.00 46.43  ? 28  PRO H CA  1 
ATOM   7965  C  C   . PRO H  1 34  ? 69.794  134.764 40.118 1.00 45.35  ? 28  PRO H C   1 
ATOM   7966  O  O   . PRO H  1 34  ? 70.791  134.117 39.765 1.00 44.47  ? 28  PRO H O   1 
ATOM   7967  C  CB  . PRO H  1 34  ? 67.645  133.868 39.090 1.00 45.10  ? 28  PRO H CB  1 
ATOM   7968  C  CG  . PRO H  1 34  ? 68.152  133.090 37.940 1.00 36.21  ? 28  PRO H CG  1 
ATOM   7969  C  CD  . PRO H  1 34  ? 68.446  134.167 36.923 1.00 46.02  ? 28  PRO H CD  1 
ATOM   7970  N  N   . VAL H  1 35  ? 69.636  135.260 41.340 1.00 40.75  ? 29  VAL H N   1 
ATOM   7971  C  CA  . VAL H  1 35  ? 70.618  135.119 42.399 1.00 31.54  ? 29  VAL H CA  1 
ATOM   7972  C  C   . VAL H  1 35  ? 70.201  134.020 43.370 1.00 32.68  ? 29  VAL H C   1 
ATOM   7973  O  O   . VAL H  1 35  ? 69.096  134.060 43.899 1.00 34.31  ? 29  VAL H O   1 
ATOM   7974  C  CB  . VAL H  1 35  ? 70.729  136.443 43.188 1.00 31.17  ? 29  VAL H CB  1 
ATOM   7975  C  CG1 . VAL H  1 35  ? 71.765  136.322 44.297 1.00 20.00  ? 29  VAL H CG1 1 
ATOM   7976  C  CG2 . VAL H  1 35  ? 71.053  137.592 42.235 1.00 25.21  ? 29  VAL H CG2 1 
ATOM   7977  N  N   . LYS H  1 36  ? 71.067  133.031 43.586 1.00 32.34  ? 30  LYS H N   1 
ATOM   7978  C  CA  . LYS H  1 36  ? 70.772  131.983 44.559 1.00 35.25  ? 30  LYS H CA  1 
ATOM   7979  C  C   . LYS H  1 36  ? 71.211  132.587 45.894 1.00 31.37  ? 30  LYS H C   1 
ATOM   7980  O  O   . LYS H  1 36  ? 72.232  133.265 45.965 1.00 30.83  ? 30  LYS H O   1 
ATOM   7981  C  CB  . LYS H  1 36  ? 71.566  130.707 44.268 1.00 44.22  ? 30  LYS H CB  1 
ATOM   7982  C  CG  . LYS H  1 36  ? 71.009  129.869 43.120 1.00 69.89  ? 30  LYS H CG  1 
ATOM   7983  C  CD  . LYS H  1 36  ? 71.859  128.617 42.850 1.00 83.32  ? 30  LYS H CD  1 
ATOM   7984  C  CE  . LYS H  1 36  ? 71.212  127.685 41.815 1.00 87.15  ? 30  LYS H CE  1 
ATOM   7985  N  NZ  . LYS H  1 36  ? 71.014  128.334 40.486 1.00 93.56  ? 30  LYS H NZ  1 
ATOM   7986  N  N   . VAL H  1 37  ? 70.430  132.363 46.944 1.00 28.47  ? 31  VAL H N   1 
ATOM   7987  C  CA  . VAL H  1 37  ? 70.728  132.910 48.263 1.00 25.50  ? 31  VAL H CA  1 
ATOM   7988  C  C   . VAL H  1 37  ? 70.621  131.752 49.233 1.00 31.34  ? 31  VAL H C   1 
ATOM   7989  O  O   . VAL H  1 37  ? 69.532  131.219 49.467 1.00 32.79  ? 31  VAL H O   1 
ATOM   7990  C  CB  . VAL H  1 37  ? 69.713  134.006 48.639 1.00 26.87  ? 31  VAL H CB  1 
ATOM   7991  C  CG1 . VAL H  1 37  ? 70.051  134.599 49.998 1.00 17.67  ? 31  VAL H CG1 1 
ATOM   7992  C  CG2 . VAL H  1 37  ? 69.721  135.107 47.573 1.00 27.27  ? 31  VAL H CG2 1 
ATOM   7993  N  N   . TRP H  1 38  ? 71.750  131.354 49.803 1.00 31.60  ? 32  TRP H N   1 
ATOM   7994  C  CA  . TRP H  1 38  ? 71.739  130.208 50.694 1.00 35.43  ? 32  TRP H CA  1 
ATOM   7995  C  C   . TRP H  1 38  ? 72.694  130.384 51.847 1.00 34.63  ? 32  TRP H C   1 
ATOM   7996  O  O   . TRP H  1 38  ? 73.747  131.006 51.710 1.00 34.01  ? 32  TRP H O   1 
ATOM   7997  C  CB  . TRP H  1 38  ? 72.102  128.938 49.910 1.00 36.07  ? 32  TRP H CB  1 
ATOM   7998  C  CG  . TRP H  1 38  ? 73.593  128.641 49.787 1.00 45.90  ? 32  TRP H CG  1 
ATOM   7999  C  CD1 . TRP H  1 38  ? 74.367  127.913 50.660 1.00 44.93  ? 32  TRP H CD1 1 
ATOM   8000  C  CD2 . TRP H  1 38  ? 74.467  129.044 48.727 1.00 48.66  ? 32  TRP H CD2 1 
ATOM   8001  N  NE1 . TRP H  1 38  ? 75.659  127.836 50.203 1.00 48.58  ? 32  TRP H NE1 1 
ATOM   8002  C  CE2 . TRP H  1 38  ? 75.751  128.522 49.019 1.00 50.66  ? 32  TRP H CE2 1 
ATOM   8003  C  CE3 . TRP H  1 38  ? 74.292  129.796 47.556 1.00 53.88  ? 32  TRP H CE3 1 
ATOM   8004  C  CZ2 . TRP H  1 38  ? 76.856  128.728 48.178 1.00 60.83  ? 32  TRP H CZ2 1 
ATOM   8005  C  CZ3 . TRP H  1 38  ? 75.399  130.002 46.714 1.00 57.98  ? 32  TRP H CZ3 1 
ATOM   8006  C  CH2 . TRP H  1 38  ? 76.660  129.468 47.032 1.00 59.52  ? 32  TRP H CH2 1 
ATOM   8007  N  N   . GLY H  1 39  ? 72.322  129.806 52.980 1.00 27.86  ? 33  GLY H N   1 
ATOM   8008  C  CA  . GLY H  1 39  ? 73.145  129.914 54.156 1.00 24.17  ? 33  GLY H CA  1 
ATOM   8009  C  C   . GLY H  1 39  ? 72.416  129.364 55.354 1.00 28.07  ? 33  GLY H C   1 
ATOM   8010  O  O   . GLY H  1 39  ? 71.348  128.770 55.224 1.00 39.75  ? 33  GLY H O   1 
ATOM   8011  N  N   . SER H  1 40  ? 72.984  129.588 56.528 1.00 26.60  ? 34  SER H N   1 
ATOM   8012  C  CA  . SER H  1 40  ? 72.426  129.079 57.765 1.00 30.00  ? 34  SER H CA  1 
ATOM   8013  C  C   . SER H  1 40  ? 72.379  130.188 58.811 1.00 28.42  ? 34  SER H C   1 
ATOM   8014  O  O   . SER H  1 40  ? 73.348  130.909 58.991 1.00 34.08  ? 34  SER H O   1 
ATOM   8015  C  CB  . SER H  1 40  ? 73.322  127.937 58.242 1.00 28.02  ? 34  SER H CB  1 
ATOM   8016  O  OG  . SER H  1 40  ? 72.742  127.206 59.294 1.00 47.23  ? 34  SER H OG  1 
ATOM   8017  N  N   . ILE H  1 41  ? 71.252  130.349 59.487 1.00 30.86  ? 35  ILE H N   1 
ATOM   8018  C  CA  . ILE H  1 41  ? 71.166  131.370 60.525 1.00 33.98  ? 35  ILE H CA  1 
ATOM   8019  C  C   . ILE H  1 41  ? 70.644  130.736 61.790 1.00 34.73  ? 35  ILE H C   1 
ATOM   8020  O  O   . ILE H  1 41  ? 69.592  130.095 61.779 1.00 42.39  ? 35  ILE H O   1 
ATOM   8021  C  CB  . ILE H  1 41  ? 70.219  132.511 60.160 1.00 34.69  ? 35  ILE H CB  1 
ATOM   8022  C  CG1 . ILE H  1 41  ? 70.606  133.091 58.804 1.00 29.89  ? 35  ILE H CG1 1 
ATOM   8023  C  CG2 . ILE H  1 41  ? 70.282  133.582 61.247 1.00 24.88  ? 35  ILE H CG2 1 
ATOM   8024  C  CD1 . ILE H  1 41  ? 69.735  134.223 58.356 1.00 35.17  ? 35  ILE H CD1 1 
ATOM   8025  N  N   . LYS H  1 42  ? 71.378  130.916 62.880 1.00 34.50  ? 36  LYS H N   1 
ATOM   8026  C  CA  . LYS H  1 42  ? 70.990  130.335 64.160 1.00 33.83  ? 36  LYS H CA  1 
ATOM   8027  C  C   . LYS H  1 42  ? 70.650  131.404 65.180 1.00 28.13  ? 36  LYS H C   1 
ATOM   8028  O  O   . LYS H  1 42  ? 70.973  132.580 64.985 1.00 29.24  ? 36  LYS H O   1 
ATOM   8029  C  CB  . LYS H  1 42  ? 72.117  129.445 64.697 1.00 38.67  ? 36  LYS H CB  1 
ATOM   8030  C  CG  . LYS H  1 42  ? 73.421  130.174 64.993 1.00 43.34  ? 36  LYS H CG  1 
ATOM   8031  C  CD  . LYS H  1 42  ? 74.445  129.222 65.593 1.00 53.88  ? 36  LYS H CD  1 
ATOM   8032  C  CE  . LYS H  1 42  ? 75.761  129.923 65.905 1.00 61.19  ? 36  LYS H CE  1 
ATOM   8033  N  NZ  . LYS H  1 42  ? 76.782  128.976 66.455 1.00 62.98  ? 36  LYS H NZ  1 
ATOM   8034  N  N   . GLY H  1 43  ? 70.012  130.990 66.273 1.00 23.75  ? 37  GLY H N   1 
ATOM   8035  C  CA  . GLY H  1 43  ? 69.625  131.928 67.311 1.00 22.55  ? 37  GLY H CA  1 
ATOM   8036  C  C   . GLY H  1 43  ? 68.257  132.546 67.065 1.00 30.57  ? 37  GLY H C   1 
ATOM   8037  O  O   . GLY H  1 43  ? 67.798  133.402 67.832 1.00 37.46  ? 37  GLY H O   1 
ATOM   8038  N  N   . LEU H  1 44  ? 67.600  132.119 65.989 1.00 30.04  ? 38  LEU H N   1 
ATOM   8039  C  CA  . LEU H  1 44  ? 66.266  132.617 65.642 1.00 32.09  ? 38  LEU H CA  1 
ATOM   8040  C  C   . LEU H  1 44  ? 65.163  131.838 66.350 1.00 30.50  ? 38  LEU H C   1 
ATOM   8041  O  O   . LEU H  1 44  ? 65.315  130.653 66.623 1.00 36.93  ? 38  LEU H O   1 
ATOM   8042  C  CB  . LEU H  1 44  ? 66.028  132.514 64.130 1.00 28.61  ? 38  LEU H CB  1 
ATOM   8043  C  CG  . LEU H  1 44  ? 66.857  133.441 63.251 1.00 33.54  ? 38  LEU H CG  1 
ATOM   8044  C  CD1 . LEU H  1 44  ? 66.641  133.105 61.798 1.00 22.75  ? 38  LEU H CD1 1 
ATOM   8045  C  CD2 . LEU H  1 44  ? 66.477  134.876 63.548 1.00 24.84  ? 38  LEU H CD2 1 
ATOM   8046  N  N   . THR H  1 45  ? 64.053  132.507 66.646 1.00 31.65  ? 39  THR H N   1 
ATOM   8047  C  CA  . THR H  1 45  ? 62.908  131.842 67.266 1.00 28.12  ? 39  THR H CA  1 
ATOM   8048  C  C   . THR H  1 45  ? 62.236  131.017 66.149 1.00 29.81  ? 39  THR H C   1 
ATOM   8049  O  O   . THR H  1 45  ? 62.248  131.414 64.966 1.00 19.10  ? 39  THR H O   1 
ATOM   8050  C  CB  . THR H  1 45  ? 61.896  132.868 67.800 1.00 33.39  ? 39  THR H CB  1 
ATOM   8051  O  OG1 . THR H  1 45  ? 61.518  133.761 66.737 1.00 37.04  ? 39  THR H OG1 1 
ATOM   8052  C  CG2 . THR H  1 45  ? 62.502  133.669 68.937 1.00 23.31  ? 39  THR H CG2 1 
ATOM   8053  N  N   . GLU H  1 46  ? 61.664  129.873 66.504 1.00 28.73  ? 40  GLU H N   1 
ATOM   8054  C  CA  . GLU H  1 46  ? 61.014  129.040 65.497 1.00 33.10  ? 40  GLU H CA  1 
ATOM   8055  C  C   . GLU H  1 46  ? 59.965  129.859 64.736 1.00 33.57  ? 40  GLU H C   1 
ATOM   8056  O  O   . GLU H  1 46  ? 59.222  130.633 65.333 1.00 32.72  ? 40  GLU H O   1 
ATOM   8057  C  CB  . GLU H  1 46  ? 60.365  127.831 66.164 1.00 31.28  ? 40  GLU H CB  1 
ATOM   8058  C  CG  . GLU H  1 46  ? 59.682  126.870 65.208 1.00 37.30  ? 40  GLU H CG  1 
ATOM   8059  C  CD  . GLU H  1 46  ? 59.092  125.669 65.921 1.00 43.34  ? 40  GLU H CD  1 
ATOM   8060  O  OE1 . GLU H  1 46  ? 58.411  124.859 65.260 1.00 45.33  ? 40  GLU H OE1 1 
ATOM   8061  O  OE2 . GLU H  1 46  ? 59.315  125.531 67.145 1.00 48.39  ? 40  GLU H OE2 1 
ATOM   8062  N  N   . GLY H  1 47  ? 59.927  129.711 63.415 1.00 35.52  ? 41  GLY H N   1 
ATOM   8063  C  CA  . GLY H  1 47  ? 58.955  130.453 62.631 1.00 33.34  ? 41  GLY H CA  1 
ATOM   8064  C  C   . GLY H  1 47  ? 59.513  131.367 61.547 1.00 39.43  ? 41  GLY H C   1 
ATOM   8065  O  O   . GLY H  1 47  ? 60.688  131.280 61.154 1.00 39.50  ? 41  GLY H O   1 
ATOM   8066  N  N   . LEU H  1 48  ? 58.646  132.261 61.077 1.00 32.84  ? 42  LEU H N   1 
ATOM   8067  C  CA  . LEU H  1 48  ? 58.949  133.209 60.012 1.00 29.44  ? 42  LEU H CA  1 
ATOM   8068  C  C   . LEU H  1 48  ? 59.614  134.505 60.466 1.00 30.10  ? 42  LEU H C   1 
ATOM   8069  O  O   . LEU H  1 48  ? 59.228  135.090 61.476 1.00 25.63  ? 42  LEU H O   1 
ATOM   8070  C  CB  . LEU H  1 48  ? 57.658  133.550 59.271 1.00 32.27  ? 42  LEU H CB  1 
ATOM   8071  C  CG  . LEU H  1 48  ? 56.930  132.385 58.599 1.00 33.30  ? 42  LEU H CG  1 
ATOM   8072  C  CD1 . LEU H  1 48  ? 55.539  132.837 58.190 1.00 20.78  ? 42  LEU H CD1 1 
ATOM   8073  C  CD2 . LEU H  1 48  ? 57.718  131.915 57.374 1.00 26.80  ? 42  LEU H CD2 1 
ATOM   8074  N  N   . HIS H  1 49  ? 60.595  134.957 59.688 1.00 27.46  ? 43  HIS H N   1 
ATOM   8075  C  CA  . HIS H  1 49  ? 61.340  136.179 59.978 1.00 25.51  ? 43  HIS H CA  1 
ATOM   8076  C  C   . HIS H  1 49  ? 61.596  136.945 58.688 1.00 31.87  ? 43  HIS H C   1 
ATOM   8077  O  O   . HIS H  1 49  ? 62.054  136.369 57.683 1.00 29.76  ? 43  HIS H O   1 
ATOM   8078  C  CB  . HIS H  1 49  ? 62.701  135.853 60.614 1.00 25.60  ? 43  HIS H CB  1 
ATOM   8079  C  CG  . HIS H  1 49  ? 62.610  135.246 61.977 1.00 23.64  ? 43  HIS H CG  1 
ATOM   8080  N  ND1 . HIS H  1 49  ? 62.638  135.999 63.132 1.00 21.33  ? 43  HIS H ND1 1 
ATOM   8081  C  CD2 . HIS H  1 49  ? 62.472  133.959 62.369 1.00 14.18  ? 43  HIS H CD2 1 
ATOM   8082  C  CE1 . HIS H  1 49  ? 62.522  135.202 64.177 1.00 16.84  ? 43  HIS H CE1 1 
ATOM   8083  N  NE2 . HIS H  1 49  ? 62.420  133.958 63.743 1.00 28.35  ? 43  HIS H NE2 1 
ATOM   8084  N  N   . GLY H  1 50  ? 61.304  138.244 58.722 1.00 33.85  ? 44  GLY H N   1 
ATOM   8085  C  CA  . GLY H  1 50  ? 61.532  139.081 57.560 1.00 32.99  ? 44  GLY H CA  1 
ATOM   8086  C  C   . GLY H  1 50  ? 62.990  138.959 57.158 1.00 33.92  ? 44  GLY H C   1 
ATOM   8087  O  O   . GLY H  1 50  ? 63.871  138.836 58.021 1.00 29.26  ? 44  GLY H O   1 
ATOM   8088  N  N   . PHE H  1 51  ? 63.239  139.014 55.854 1.00 28.66  ? 45  PHE H N   1 
ATOM   8089  C  CA  . PHE H  1 51  ? 64.575  138.859 55.302 1.00 30.63  ? 45  PHE H CA  1 
ATOM   8090  C  C   . PHE H  1 51  ? 64.754  139.886 54.182 1.00 28.06  ? 45  PHE H C   1 
ATOM   8091  O  O   . PHE H  1 51  ? 64.281  139.667 53.062 1.00 23.84  ? 45  PHE H O   1 
ATOM   8092  C  CB  . PHE H  1 51  ? 64.687  137.431 54.762 1.00 30.40  ? 45  PHE H CB  1 
ATOM   8093  C  CG  . PHE H  1 51  ? 66.088  136.977 54.500 1.00 31.29  ? 45  PHE H CG  1 
ATOM   8094  C  CD1 . PHE H  1 51  ? 66.996  136.838 55.547 1.00 28.09  ? 45  PHE H CD1 1 
ATOM   8095  C  CD2 . PHE H  1 51  ? 66.485  136.627 53.207 1.00 30.09  ? 45  PHE H CD2 1 
ATOM   8096  C  CE1 . PHE H  1 51  ? 68.270  136.353 55.314 1.00 32.05  ? 45  PHE H CE1 1 
ATOM   8097  C  CE2 . PHE H  1 51  ? 67.767  136.136 52.961 1.00 30.60  ? 45  PHE H CE2 1 
ATOM   8098  C  CZ  . PHE H  1 51  ? 68.660  135.997 54.014 1.00 32.98  ? 45  PHE H CZ  1 
ATOM   8099  N  N   . HIS H  1 52  ? 65.450  140.988 54.473 1.00 22.79  ? 46  HIS H N   1 
ATOM   8100  C  CA  . HIS H  1 52  ? 65.611  142.056 53.488 1.00 23.51  ? 46  HIS H CA  1 
ATOM   8101  C  C   . HIS H  1 52  ? 66.991  142.665 53.331 1.00 28.52  ? 46  HIS H C   1 
ATOM   8102  O  O   . HIS H  1 52  ? 67.805  142.662 54.253 1.00 29.11  ? 46  HIS H O   1 
ATOM   8103  C  CB  . HIS H  1 52  ? 64.684  143.231 53.812 1.00 24.60  ? 46  HIS H CB  1 
ATOM   8104  C  CG  . HIS H  1 52  ? 63.373  142.837 54.412 1.00 29.54  ? 46  HIS H CG  1 
ATOM   8105  N  ND1 . HIS H  1 52  ? 63.036  143.134 55.714 1.00 31.66  ? 46  HIS H ND1 1 
ATOM   8106  C  CD2 . HIS H  1 52  ? 62.311  142.181 53.886 1.00 26.50  ? 46  HIS H CD2 1 
ATOM   8107  C  CE1 . HIS H  1 52  ? 61.822  142.676 55.966 1.00 33.28  ? 46  HIS H CE1 1 
ATOM   8108  N  NE2 . HIS H  1 52  ? 61.361  142.092 54.873 1.00 28.20  ? 46  HIS H NE2 1 
ATOM   8109  N  N   . VAL H  1 53  ? 67.232  143.220 52.146 1.00 27.54  ? 47  VAL H N   1 
ATOM   8110  C  CA  . VAL H  1 53  ? 68.475  143.930 51.877 1.00 30.75  ? 47  VAL H CA  1 
ATOM   8111  C  C   . VAL H  1 53  ? 68.072  145.393 52.101 1.00 30.10  ? 47  VAL H C   1 
ATOM   8112  O  O   . VAL H  1 53  ? 67.193  145.902 51.407 1.00 30.82  ? 47  VAL H O   1 
ATOM   8113  C  CB  . VAL H  1 53  ? 68.960  143.753 50.406 1.00 22.58  ? 47  VAL H CB  1 
ATOM   8114  C  CG1 . VAL H  1 53  ? 70.192  144.625 50.154 1.00 19.22  ? 47  VAL H CG1 1 
ATOM   8115  C  CG2 . VAL H  1 53  ? 69.285  142.297 50.123 1.00 18.22  ? 47  VAL H CG2 1 
ATOM   8116  N  N   . HIS H  1 54  ? 68.656  146.046 53.103 1.00 31.35  ? 48  HIS H N   1 
ATOM   8117  C  CA  . HIS H  1 54  ? 68.338  147.451 53.366 1.00 28.14  ? 48  HIS H CA  1 
ATOM   8118  C  C   . HIS H  1 54  ? 69.306  148.305 52.545 1.00 29.71  ? 48  HIS H C   1 
ATOM   8119  O  O   . HIS H  1 54  ? 70.275  147.789 51.998 1.00 28.39  ? 48  HIS H O   1 
ATOM   8120  C  CB  . HIS H  1 54  ? 68.426  147.788 54.872 1.00 25.98  ? 48  HIS H CB  1 
ATOM   8121  C  CG  . HIS H  1 54  ? 67.342  147.161 55.703 1.00 16.34  ? 48  HIS H CG  1 
ATOM   8122  N  ND1 . HIS H  1 54  ? 66.616  147.871 56.635 1.00 19.46  ? 48  HIS H ND1 1 
ATOM   8123  C  CD2 . HIS H  1 54  ? 66.868  145.890 55.750 1.00 24.29  ? 48  HIS H CD2 1 
ATOM   8124  C  CE1 . HIS H  1 54  ? 65.740  147.067 57.218 1.00 29.93  ? 48  HIS H CE1 1 
ATOM   8125  N  NE2 . HIS H  1 54  ? 65.872  145.857 56.700 1.00 21.32  ? 48  HIS H NE2 1 
ATOM   8126  N  N   . GLU H  1 55  ? 69.049  149.605 52.472 1.00 33.70  ? 49  GLU H N   1 
ATOM   8127  C  CA  . GLU H  1 55  ? 69.847  150.506 51.650 1.00 37.81  ? 49  GLU H CA  1 
ATOM   8128  C  C   . GLU H  1 55  ? 71.335  150.734 51.906 1.00 39.47  ? 49  GLU H C   1 
ATOM   8129  O  O   . GLU H  1 55  ? 72.151  150.662 50.978 1.00 34.36  ? 49  GLU H O   1 
ATOM   8130  C  CB  . GLU H  1 55  ? 69.158  151.874 51.579 1.00 41.75  ? 49  GLU H CB  1 
ATOM   8131  C  CG  . GLU H  1 55  ? 69.872  152.850 50.647 1.00 53.22  ? 49  GLU H CG  1 
ATOM   8132  C  CD  . GLU H  1 55  ? 69.072  154.111 50.335 1.00 52.08  ? 49  GLU H CD  1 
ATOM   8133  O  OE1 . GLU H  1 55  ? 69.556  154.913 49.506 1.00 52.29  ? 49  GLU H OE1 1 
ATOM   8134  O  OE2 . GLU H  1 55  ? 67.976  154.300 50.908 1.00 44.09  ? 49  GLU H OE2 1 
ATOM   8135  N  N   . PHE H  1 56  ? 71.700  151.003 53.150 1.00 39.26  ? 50  PHE H N   1 
ATOM   8136  C  CA  . PHE H  1 56  ? 73.089  151.310 53.447 1.00 34.16  ? 50  PHE H CA  1 
ATOM   8137  C  C   . PHE H  1 56  ? 73.941  150.243 54.116 1.00 30.50  ? 50  PHE H C   1 
ATOM   8138  O  O   . PHE H  1 56  ? 73.492  149.532 55.000 1.00 30.05  ? 50  PHE H O   1 
ATOM   8139  C  CB  . PHE H  1 56  ? 73.128  152.590 54.277 1.00 27.27  ? 50  PHE H CB  1 
ATOM   8140  C  CG  . PHE H  1 56  ? 72.416  153.737 53.634 1.00 29.43  ? 50  PHE H CG  1 
ATOM   8141  C  CD1 . PHE H  1 56  ? 72.871  154.267 52.426 1.00 28.66  ? 50  PHE H CD1 1 
ATOM   8142  C  CD2 . PHE H  1 56  ? 71.279  154.287 54.222 1.00 29.67  ? 50  PHE H CD2 1 
ATOM   8143  C  CE1 . PHE H  1 56  ? 72.200  155.334 51.812 1.00 29.38  ? 50  PHE H CE1 1 
ATOM   8144  C  CE2 . PHE H  1 56  ? 70.604  155.352 53.617 1.00 28.77  ? 50  PHE H CE2 1 
ATOM   8145  C  CZ  . PHE H  1 56  ? 71.070  155.874 52.409 1.00 27.70  ? 50  PHE H CZ  1 
ATOM   8146  N  N   . GLY H  1 57  ? 75.191  150.158 53.676 1.00 31.30  ? 51  GLY H N   1 
ATOM   8147  C  CA  . GLY H  1 57  ? 76.117  149.213 54.259 1.00 33.98  ? 51  GLY H CA  1 
ATOM   8148  C  C   . GLY H  1 57  ? 76.763  149.914 55.432 1.00 34.09  ? 51  GLY H C   1 
ATOM   8149  O  O   . GLY H  1 57  ? 77.972  149.829 55.635 1.00 31.29  ? 51  GLY H O   1 
ATOM   8150  N  N   . ASP H  1 58  ? 75.946  150.623 56.204 1.00 33.86  ? 52  ASP H N   1 
ATOM   8151  C  CA  . ASP H  1 58  ? 76.440  151.363 57.353 1.00 37.34  ? 52  ASP H CA  1 
ATOM   8152  C  C   . ASP H  1 58  ? 76.086  150.670 58.661 1.00 38.89  ? 52  ASP H C   1 
ATOM   8153  O  O   . ASP H  1 58  ? 74.912  150.611 59.076 1.00 30.80  ? 52  ASP H O   1 
ATOM   8154  C  CB  . ASP H  1 58  ? 75.885  152.790 57.338 1.00 37.98  ? 52  ASP H CB  1 
ATOM   8155  C  CG  . ASP H  1 58  ? 76.439  153.646 58.469 1.00 47.44  ? 52  ASP H CG  1 
ATOM   8156  O  OD1 . ASP H  1 58  ? 76.407  154.891 58.332 1.00 50.07  ? 52  ASP H OD1 1 
ATOM   8157  O  OD2 . ASP H  1 58  ? 76.900  153.082 59.493 1.00 42.32  ? 52  ASP H OD2 1 
ATOM   8158  N  N   . ASN H  1 59  ? 77.120  150.164 59.318 1.00 35.02  ? 53  ASN H N   1 
ATOM   8159  C  CA  . ASN H  1 59  ? 76.932  149.453 60.562 1.00 46.32  ? 53  ASN H CA  1 
ATOM   8160  C  C   . ASN H  1 59  ? 77.418  150.207 61.808 1.00 44.87  ? 53  ASN H C   1 
ATOM   8161  O  O   . ASN H  1 59  ? 77.435  149.651 62.907 1.00 42.82  ? 53  ASN H O   1 
ATOM   8162  C  CB  . ASN H  1 59  ? 77.639  148.106 60.470 1.00 50.62  ? 53  ASN H CB  1 
ATOM   8163  C  CG  . ASN H  1 59  ? 77.331  147.216 61.647 1.00 66.67  ? 53  ASN H CG  1 
ATOM   8164  O  OD1 . ASN H  1 59  ? 78.225  146.571 62.207 1.00 69.44  ? 53  ASN H OD1 1 
ATOM   8165  N  ND2 . ASN H  1 59  ? 76.055  147.169 62.033 1.00 67.94  ? 53  ASN H ND2 1 
ATOM   8166  N  N   . THR H  1 60  ? 77.803  151.468 61.660 1.00 43.09  ? 54  THR H N   1 
ATOM   8167  C  CA  . THR H  1 60  ? 78.292  152.200 62.819 1.00 39.22  ? 54  THR H CA  1 
ATOM   8168  C  C   . THR H  1 60  ? 77.299  152.203 63.999 1.00 43.20  ? 54  THR H C   1 
ATOM   8169  O  O   . THR H  1 60  ? 77.711  152.071 65.156 1.00 40.74  ? 54  THR H O   1 
ATOM   8170  C  CB  . THR H  1 60  ? 78.704  153.640 62.434 1.00 37.91  ? 54  THR H CB  1 
ATOM   8171  O  OG1 . THR H  1 60  ? 77.609  154.328 61.818 1.00 29.05  ? 54  THR H OG1 1 
ATOM   8172  C  CG2 . THR H  1 60  ? 79.870  153.596 61.469 1.00 39.15  ? 54  THR H CG2 1 
ATOM   8173  N  N   . ALA H  1 61  ? 76.001  152.328 63.716 1.00 34.28  ? 55  ALA H N   1 
ATOM   8174  C  CA  . ALA H  1 61  ? 74.993  152.312 64.771 1.00 29.03  ? 55  ALA H CA  1 
ATOM   8175  C  C   . ALA H  1 61  ? 74.253  150.968 64.812 1.00 33.22  ? 55  ALA H C   1 
ATOM   8176  O  O   . ALA H  1 61  ? 73.030  150.926 65.000 1.00 33.56  ? 55  ALA H O   1 
ATOM   8177  C  CB  . ALA H  1 61  ? 74.008  153.423 64.548 1.00 32.10  ? 55  ALA H CB  1 
ATOM   8178  N  N   . GLY H  1 62  ? 74.989  149.869 64.654 1.00 29.85  ? 56  GLY H N   1 
ATOM   8179  C  CA  . GLY H  1 62  ? 74.345  148.570 64.644 1.00 36.13  ? 56  GLY H CA  1 
ATOM   8180  C  C   . GLY H  1 62  ? 73.575  148.399 63.338 1.00 45.32  ? 56  GLY H C   1 
ATOM   8181  O  O   . GLY H  1 62  ? 74.011  148.861 62.266 1.00 43.88  ? 56  GLY H O   1 
ATOM   8182  N  N   . CYS H  1 63  ? 72.423  147.742 63.410 1.00 42.30  ? 57  CYS H N   1 
ATOM   8183  C  CA  . CYS H  1 63  ? 71.619  147.532 62.213 1.00 45.54  ? 57  CYS H CA  1 
ATOM   8184  C  C   . CYS H  1 63  ? 70.729  148.735 61.942 1.00 41.59  ? 57  CYS H C   1 
ATOM   8185  O  O   . CYS H  1 63  ? 70.125  148.846 60.888 1.00 43.20  ? 57  CYS H O   1 
ATOM   8186  C  CB  . CYS H  1 63  ? 70.760  146.271 62.357 1.00 44.26  ? 57  CYS H CB  1 
ATOM   8187  S  SG  . CYS H  1 63  ? 71.730  144.761 62.662 1.00 41.42  ? 57  CYS H SG  1 
ATOM   8188  N  N   . THR H  1 64  ? 70.671  149.650 62.895 1.00 43.82  ? 58  THR H N   1 
ATOM   8189  C  CA  . THR H  1 64  ? 69.841  150.832 62.749 1.00 37.41  ? 58  THR H CA  1 
ATOM   8190  C  C   . THR H  1 64  ? 70.285  151.727 61.621 1.00 35.14  ? 58  THR H C   1 
ATOM   8191  O  O   . THR H  1 64  ? 69.458  152.269 60.888 1.00 44.69  ? 58  THR H O   1 
ATOM   8192  C  CB  . THR H  1 64  ? 69.846  151.653 64.024 1.00 40.91  ? 58  THR H CB  1 
ATOM   8193  O  OG1 . THR H  1 64  ? 69.415  150.829 65.115 1.00 42.28  ? 58  THR H OG1 1 
ATOM   8194  C  CG2 . THR H  1 64  ? 68.912  152.834 63.879 1.00 45.41  ? 58  THR H CG2 1 
ATOM   8195  N  N   . SER H  1 65  ? 71.594  151.882 61.472 1.00 27.96  ? 59  SER H N   1 
ATOM   8196  C  CA  . SER H  1 65  ? 72.124  152.746 60.429 1.00 31.46  ? 59  SER H CA  1 
ATOM   8197  C  C   . SER H  1 65  ? 72.123  152.143 59.014 1.00 30.16  ? 59  SER H C   1 
ATOM   8198  O  O   . SER H  1 65  ? 72.741  152.686 58.093 1.00 29.77  ? 59  SER H O   1 
ATOM   8199  C  CB  . SER H  1 65  ? 73.533  153.220 60.826 1.00 29.04  ? 59  SER H CB  1 
ATOM   8200  O  OG  . SER H  1 65  ? 74.229  152.227 61.558 1.00 32.30  ? 59  SER H OG  1 
ATOM   8201  N  N   . ALA H  1 66  ? 71.420  151.031 58.840 1.00 30.69  ? 60  ALA H N   1 
ATOM   8202  C  CA  . ALA H  1 66  ? 71.347  150.381 57.537 1.00 38.21  ? 60  ALA H CA  1 
ATOM   8203  C  C   . ALA H  1 66  ? 70.224  151.015 56.712 1.00 40.66  ? 60  ALA H C   1 
ATOM   8204  O  O   . ALA H  1 66  ? 70.121  150.798 55.507 1.00 39.53  ? 60  ALA H O   1 
ATOM   8205  C  CB  . ALA H  1 66  ? 71.089  148.903 57.713 1.00 27.66  ? 60  ALA H CB  1 
ATOM   8206  N  N   . GLY H  1 67  ? 69.376  151.791 57.380 1.00 40.28  ? 61  GLY H N   1 
ATOM   8207  C  CA  . GLY H  1 67  ? 68.281  152.449 56.696 1.00 33.43  ? 61  GLY H CA  1 
ATOM   8208  C  C   . GLY H  1 67  ? 67.109  151.552 56.342 1.00 36.32  ? 61  GLY H C   1 
ATOM   8209  O  O   . GLY H  1 67  ? 66.945  150.456 56.892 1.00 30.43  ? 61  GLY H O   1 
ATOM   8210  N  N   . PRO H  1 68  ? 66.262  152.007 55.412 1.00 33.59  ? 62  PRO H N   1 
ATOM   8211  C  CA  . PRO H  1 68  ? 65.081  151.262 54.960 1.00 29.87  ? 62  PRO H CA  1 
ATOM   8212  C  C   . PRO H  1 68  ? 65.424  150.168 53.937 1.00 29.26  ? 62  PRO H C   1 
ATOM   8213  O  O   . PRO H  1 68  ? 66.579  149.997 53.536 1.00 21.95  ? 62  PRO H O   1 
ATOM   8214  C  CB  . PRO H  1 68  ? 64.214  152.360 54.354 1.00 32.37  ? 62  PRO H CB  1 
ATOM   8215  C  CG  . PRO H  1 68  ? 65.256  153.230 53.682 1.00 33.22  ? 62  PRO H CG  1 
ATOM   8216  C  CD  . PRO H  1 68  ? 66.344  153.325 54.749 1.00 31.10  ? 62  PRO H CD  1 
ATOM   8217  N  N   . HIS H  1 69  ? 64.413  149.427 53.516 1.00 25.60  ? 63  HIS H N   1 
ATOM   8218  C  CA  . HIS H  1 69  ? 64.620  148.382 52.529 1.00 31.91  ? 63  HIS H CA  1 
ATOM   8219  C  C   . HIS H  1 69  ? 65.204  149.017 51.263 1.00 29.94  ? 63  HIS H C   1 
ATOM   8220  O  O   . HIS H  1 69  ? 64.798  150.116 50.891 1.00 26.30  ? 63  HIS H O   1 
ATOM   8221  C  CB  . HIS H  1 69  ? 63.279  147.700 52.213 1.00 28.61  ? 63  HIS H CB  1 
ATOM   8222  C  CG  . HIS H  1 69  ? 62.668  147.007 53.388 1.00 27.21  ? 63  HIS H CG  1 
ATOM   8223  N  ND1 . HIS H  1 69  ? 61.483  146.306 53.309 1.00 35.06  ? 63  HIS H ND1 1 
ATOM   8224  C  CD2 . HIS H  1 69  ? 63.103  146.868 54.663 1.00 26.64  ? 63  HIS H CD2 1 
ATOM   8225  C  CE1 . HIS H  1 69  ? 61.215  145.761 54.481 1.00 22.94  ? 63  HIS H CE1 1 
ATOM   8226  N  NE2 . HIS H  1 69  ? 62.182  146.086 55.321 1.00 37.26  ? 63  HIS H NE2 1 
ATOM   8227  N  N   . PHE H  1 70  ? 66.164  148.345 50.622 1.00 26.66  ? 64  PHE H N   1 
ATOM   8228  C  CA  . PHE H  1 70  ? 66.769  148.863 49.399 1.00 25.95  ? 64  PHE H CA  1 
ATOM   8229  C  C   . PHE H  1 70  ? 65.611  149.013 48.420 1.00 33.78  ? 64  PHE H C   1 
ATOM   8230  O  O   . PHE H  1 70  ? 64.951  148.029 48.065 1.00 21.39  ? 64  PHE H O   1 
ATOM   8231  C  CB  . PHE H  1 70  ? 67.787  147.877 48.835 1.00 29.67  ? 64  PHE H CB  1 
ATOM   8232  C  CG  . PHE H  1 70  ? 68.533  148.396 47.632 1.00 35.16  ? 64  PHE H CG  1 
ATOM   8233  C  CD1 . PHE H  1 70  ? 68.880  147.541 46.592 1.00 35.38  ? 64  PHE H CD1 1 
ATOM   8234  C  CD2 . PHE H  1 70  ? 68.911  149.731 47.554 1.00 34.27  ? 64  PHE H CD2 1 
ATOM   8235  C  CE1 . PHE H  1 70  ? 69.594  148.004 45.493 1.00 37.79  ? 64  PHE H CE1 1 
ATOM   8236  C  CE2 . PHE H  1 70  ? 69.626  150.204 46.458 1.00 35.99  ? 64  PHE H CE2 1 
ATOM   8237  C  CZ  . PHE H  1 70  ? 69.969  149.339 45.427 1.00 39.64  ? 64  PHE H CZ  1 
ATOM   8238  N  N   . ASN H  1 71  ? 65.371  150.240 47.974 1.00 33.68  ? 65  ASN H N   1 
ATOM   8239  C  CA  . ASN H  1 71  ? 64.240  150.502 47.099 1.00 37.15  ? 65  ASN H CA  1 
ATOM   8240  C  C   . ASN H  1 71  ? 64.527  151.563 46.029 1.00 39.33  ? 65  ASN H C   1 
ATOM   8241  O  O   . ASN H  1 71  ? 63.951  152.655 46.045 1.00 40.90  ? 65  ASN H O   1 
ATOM   8242  C  CB  . ASN H  1 71  ? 63.068  150.919 47.985 1.00 34.02  ? 65  ASN H CB  1 
ATOM   8243  C  CG  . ASN H  1 71  ? 61.852  151.316 47.201 1.00 36.34  ? 65  ASN H CG  1 
ATOM   8244  O  OD1 . ASN H  1 71  ? 61.523  150.700 46.189 1.00 35.84  ? 65  ASN H OD1 1 
ATOM   8245  N  ND2 . ASN H  1 71  ? 61.157  152.337 47.677 1.00 35.85  ? 65  ASN H ND2 1 
ATOM   8246  N  N   . PRO H  1 72  ? 65.408  151.237 45.069 1.00 38.00  ? 66  PRO H N   1 
ATOM   8247  C  CA  . PRO H  1 72  ? 65.771  152.167 43.996 1.00 42.53  ? 66  PRO H CA  1 
ATOM   8248  C  C   . PRO H  1 72  ? 64.634  152.547 43.024 1.00 45.12  ? 66  PRO H C   1 
ATOM   8249  O  O   . PRO H  1 72  ? 64.606  153.674 42.530 1.00 46.24  ? 66  PRO H O   1 
ATOM   8250  C  CB  . PRO H  1 72  ? 66.938  151.458 43.313 1.00 33.60  ? 66  PRO H CB  1 
ATOM   8251  C  CG  . PRO H  1 72  ? 66.558  150.020 43.445 1.00 41.87  ? 66  PRO H CG  1 
ATOM   8252  C  CD  . PRO H  1 72  ? 66.053  149.925 44.871 1.00 33.27  ? 66  PRO H CD  1 
ATOM   8253  N  N   . LEU H  1 73  ? 63.697  151.635 42.760 1.00 45.65  ? 67  LEU H N   1 
ATOM   8254  C  CA  . LEU H  1 73  ? 62.588  151.949 41.854 1.00 44.52  ? 67  LEU H CA  1 
ATOM   8255  C  C   . LEU H  1 73  ? 61.456  152.698 42.560 1.00 44.78  ? 67  LEU H C   1 
ATOM   8256  O  O   . LEU H  1 73  ? 60.442  153.035 41.950 1.00 46.17  ? 67  LEU H O   1 
ATOM   8257  C  CB  . LEU H  1 73  ? 62.042  150.680 41.202 1.00 40.54  ? 67  LEU H CB  1 
ATOM   8258  C  CG  . LEU H  1 73  ? 63.043  149.918 40.331 1.00 53.02  ? 67  LEU H CG  1 
ATOM   8259  C  CD1 . LEU H  1 73  ? 62.323  148.818 39.575 1.00 56.07  ? 67  LEU H CD1 1 
ATOM   8260  C  CD2 . LEU H  1 73  ? 63.712  150.868 39.356 1.00 55.86  ? 67  LEU H CD2 1 
ATOM   8261  N  N   . SER H  1 74  ? 61.632  152.947 43.850 1.00 39.25  ? 68  SER H N   1 
ATOM   8262  C  CA  . SER H  1 74  ? 60.653  153.687 44.632 1.00 42.03  ? 68  SER H CA  1 
ATOM   8263  C  C   . SER H  1 74  ? 59.258  153.112 44.618 1.00 42.96  ? 68  SER H C   1 
ATOM   8264  O  O   . SER H  1 74  ? 58.291  153.839 44.395 1.00 46.93  ? 68  SER H O   1 
ATOM   8265  C  CB  . SER H  1 74  ? 60.583  155.136 44.154 1.00 36.04  ? 68  SER H CB  1 
ATOM   8266  O  OG  . SER H  1 74  ? 61.811  155.793 44.383 1.00 44.73  ? 68  SER H OG  1 
ATOM   8267  N  N   . ARG H  1 75  ? 59.152  151.813 44.863 1.00 45.27  ? 69  ARG H N   1 
ATOM   8268  C  CA  . ARG H  1 75  ? 57.858  151.143 44.901 1.00 45.37  ? 69  ARG H CA  1 
ATOM   8269  C  C   . ARG H  1 75  ? 57.500  150.786 46.352 1.00 46.98  ? 69  ARG H C   1 
ATOM   8270  O  O   . ARG H  1 75  ? 58.317  150.980 47.254 1.00 48.82  ? 69  ARG H O   1 
ATOM   8271  C  CB  . ARG H  1 75  ? 57.916  149.898 44.030 1.00 41.14  ? 69  ARG H CB  1 
ATOM   8272  C  CG  . ARG H  1 75  ? 58.196  150.214 42.577 1.00 49.98  ? 69  ARG H CG  1 
ATOM   8273  C  CD  . ARG H  1 75  ? 58.078  148.977 41.727 1.00 58.34  ? 69  ARG H CD  1 
ATOM   8274  N  NE  . ARG H  1 75  ? 58.462  149.229 40.346 1.00 72.32  ? 69  ARG H NE  1 
ATOM   8275  C  CZ  . ARG H  1 75  ? 58.748  148.271 39.470 1.00 76.21  ? 69  ARG H CZ  1 
ATOM   8276  N  NH1 . ARG H  1 75  ? 58.693  146.996 39.835 1.00 74.88  ? 69  ARG H NH1 1 
ATOM   8277  N  NH2 . ARG H  1 75  ? 59.091  148.588 38.231 1.00 80.62  ? 69  ARG H NH2 1 
ATOM   8278  N  N   . LYS H  1 76  ? 56.287  150.284 46.582 1.00 47.31  ? 70  LYS H N   1 
ATOM   8279  C  CA  . LYS H  1 76  ? 55.866  149.913 47.934 1.00 45.87  ? 70  LYS H CA  1 
ATOM   8280  C  C   . LYS H  1 76  ? 56.475  148.558 48.293 1.00 41.67  ? 70  LYS H C   1 
ATOM   8281  O  O   . LYS H  1 76  ? 56.977  147.847 47.423 1.00 32.43  ? 70  LYS H O   1 
ATOM   8282  C  CB  . LYS H  1 76  ? 54.339  149.791 48.033 1.00 47.29  ? 70  LYS H CB  1 
ATOM   8283  C  CG  . LYS H  1 76  ? 53.536  150.923 47.420 1.00 59.18  ? 70  LYS H CG  1 
ATOM   8284  C  CD  . LYS H  1 76  ? 53.598  152.203 48.232 1.00 67.43  ? 70  LYS H CD  1 
ATOM   8285  C  CE  . LYS H  1 76  ? 52.627  153.241 47.661 1.00 71.71  ? 70  LYS H CE  1 
ATOM   8286  N  NZ  . LYS H  1 76  ? 52.593  154.516 48.432 1.00 72.28  ? 70  LYS H NZ  1 
ATOM   8287  N  N   . HIS H  1 77  ? 56.412  148.204 49.574 1.00 37.09  ? 71  HIS H N   1 
ATOM   8288  C  CA  . HIS H  1 77  ? 56.936  146.929 50.050 1.00 30.72  ? 71  HIS H CA  1 
ATOM   8289  C  C   . HIS H  1 77  ? 56.050  145.784 49.556 1.00 32.74  ? 71  HIS H C   1 
ATOM   8290  O  O   . HIS H  1 77  ? 54.818  145.914 49.498 1.00 34.64  ? 71  HIS H O   1 
ATOM   8291  C  CB  . HIS H  1 77  ? 56.974  146.913 51.588 1.00 23.17  ? 71  HIS H CB  1 
ATOM   8292  C  CG  . HIS H  1 77  ? 57.476  145.623 52.168 1.00 33.19  ? 71  HIS H CG  1 
ATOM   8293  N  ND1 . HIS H  1 77  ? 58.816  145.285 52.204 1.00 20.05  ? 71  HIS H ND1 1 
ATOM   8294  C  CD2 . HIS H  1 77  ? 56.808  144.558 52.671 1.00 26.49  ? 71  HIS H CD2 1 
ATOM   8295  C  CE1 . HIS H  1 77  ? 58.947  144.068 52.698 1.00 28.47  ? 71  HIS H CE1 1 
ATOM   8296  N  NE2 . HIS H  1 77  ? 57.744  143.605 52.989 1.00 32.27  ? 71  HIS H NE2 1 
ATOM   8297  N  N   . GLY H  1 78  ? 56.670  144.660 49.212 1.00 30.93  ? 72  GLY H N   1 
ATOM   8298  C  CA  . GLY H  1 78  ? 55.903  143.512 48.758 1.00 29.69  ? 72  GLY H CA  1 
ATOM   8299  C  C   . GLY H  1 78  ? 56.579  142.172 48.997 1.00 33.97  ? 72  GLY H C   1 
ATOM   8300  O  O   . GLY H  1 78  ? 57.610  142.095 49.662 1.00 38.05  ? 72  GLY H O   1 
ATOM   8301  N  N   . GLY H  1 79  ? 55.984  141.106 48.472 1.00 34.48  ? 73  GLY H N   1 
ATOM   8302  C  CA  . GLY H  1 79  ? 56.569  139.784 48.608 1.00 30.45  ? 73  GLY H CA  1 
ATOM   8303  C  C   . GLY H  1 79  ? 57.547  139.577 47.461 1.00 34.44  ? 73  GLY H C   1 
ATOM   8304  O  O   . GLY H  1 79  ? 57.453  140.264 46.432 1.00 27.61  ? 73  GLY H O   1 
ATOM   8305  N  N   . PRO H  1 80  ? 58.515  138.658 47.597 1.00 34.02  ? 74  PRO H N   1 
ATOM   8306  C  CA  . PRO H  1 80  ? 59.444  138.481 46.479 1.00 36.14  ? 74  PRO H CA  1 
ATOM   8307  C  C   . PRO H  1 80  ? 58.744  138.139 45.162 1.00 39.74  ? 74  PRO H C   1 
ATOM   8308  O  O   . PRO H  1 80  ? 59.157  138.600 44.099 1.00 40.38  ? 74  PRO H O   1 
ATOM   8309  C  CB  . PRO H  1 80  ? 60.391  137.384 46.976 1.00 29.58  ? 74  PRO H CB  1 
ATOM   8310  C  CG  . PRO H  1 80  ? 59.618  136.692 48.059 1.00 34.41  ? 74  PRO H CG  1 
ATOM   8311  C  CD  . PRO H  1 80  ? 58.883  137.805 48.738 1.00 28.90  ? 74  PRO H CD  1 
ATOM   8312  N  N   . LYS H  1 81  ? 57.673  137.351 45.247 1.00 44.64  ? 75  LYS H N   1 
ATOM   8313  C  CA  . LYS H  1 81  ? 56.892  136.945 44.074 1.00 42.02  ? 75  LYS H CA  1 
ATOM   8314  C  C   . LYS H  1 81  ? 56.115  138.098 43.427 1.00 40.91  ? 75  LYS H C   1 
ATOM   8315  O  O   . LYS H  1 81  ? 55.737  138.003 42.272 1.00 42.66  ? 75  LYS H O   1 
ATOM   8316  C  CB  . LYS H  1 81  ? 55.884  135.845 44.454 1.00 43.15  ? 75  LYS H CB  1 
ATOM   8317  C  CG  . LYS H  1 81  ? 56.437  134.428 44.610 1.00 47.76  ? 75  LYS H CG  1 
ATOM   8318  C  CD  . LYS H  1 81  ? 55.408  133.468 45.262 1.00 55.77  ? 75  LYS H CD  1 
ATOM   8319  C  CE  . LYS H  1 81  ? 54.193  133.193 44.367 1.00 67.33  ? 75  LYS H CE  1 
ATOM   8320  N  NZ  . LYS H  1 81  ? 53.054  132.544 45.097 1.00 67.15  ? 75  LYS H NZ  1 
ATOM   8321  N  N   . ASP H  1 82  ? 55.879  139.175 44.173 1.00 42.55  ? 76  ASP H N   1 
ATOM   8322  C  CA  . ASP H  1 82  ? 55.114  140.332 43.691 1.00 45.48  ? 76  ASP H CA  1 
ATOM   8323  C  C   . ASP H  1 82  ? 55.809  141.186 42.649 1.00 47.17  ? 76  ASP H C   1 
ATOM   8324  O  O   . ASP H  1 82  ? 57.033  141.179 42.531 1.00 49.62  ? 76  ASP H O   1 
ATOM   8325  C  CB  . ASP H  1 82  ? 54.729  141.247 44.866 1.00 46.82  ? 76  ASP H CB  1 
ATOM   8326  C  CG  . ASP H  1 82  ? 53.615  140.676 45.715 1.00 55.65  ? 76  ASP H CG  1 
ATOM   8327  O  OD1 . ASP H  1 82  ? 53.563  140.984 46.931 1.00 59.01  ? 76  ASP H OD1 1 
ATOM   8328  O  OD2 . ASP H  1 82  ? 52.781  139.926 45.163 1.00 63.73  ? 76  ASP H OD2 1 
ATOM   8329  N  N   . GLU H  1 83  ? 55.009  141.941 41.908 1.00 50.27  ? 77  GLU H N   1 
ATOM   8330  C  CA  . GLU H  1 83  ? 55.528  142.838 40.890 1.00 51.06  ? 77  GLU H CA  1 
ATOM   8331  C  C   . GLU H  1 83  ? 55.863  144.150 41.607 1.00 48.65  ? 77  GLU H C   1 
ATOM   8332  O  O   . GLU H  1 83  ? 56.906  144.762 41.362 1.00 44.36  ? 77  GLU H O   1 
ATOM   8333  C  CB  . GLU H  1 83  ? 54.466  143.069 39.812 1.00 64.80  ? 77  GLU H CB  1 
ATOM   8334  C  CG  . GLU H  1 83  ? 55.022  143.444 38.442 1.00 77.44  ? 77  GLU H CG  1 
ATOM   8335  C  CD  . GLU H  1 83  ? 55.828  144.728 38.466 1.00 85.47  ? 77  GLU H CD  1 
ATOM   8336  O  OE1 . GLU H  1 83  ? 55.261  145.781 38.832 1.00 89.33  ? 77  GLU H OE1 1 
ATOM   8337  O  OE2 . GLU H  1 83  ? 57.028  144.684 38.118 1.00 88.58  ? 77  GLU H OE2 1 
ATOM   8338  N  N   . GLU H  1 84  ? 54.967  144.579 42.495 1.00 42.24  ? 78  GLU H N   1 
ATOM   8339  C  CA  . GLU H  1 84  ? 55.190  145.797 43.268 1.00 40.21  ? 78  GLU H CA  1 
ATOM   8340  C  C   . GLU H  1 84  ? 55.921  145.361 44.543 1.00 40.92  ? 78  GLU H C   1 
ATOM   8341  O  O   . GLU H  1 84  ? 55.315  144.818 45.468 1.00 41.83  ? 78  GLU H O   1 
ATOM   8342  C  CB  . GLU H  1 84  ? 53.857  146.467 43.618 1.00 30.35  ? 78  GLU H CB  1 
ATOM   8343  C  CG  . GLU H  1 84  ? 53.978  147.831 44.295 1.00 42.56  ? 78  GLU H CG  1 
ATOM   8344  C  CD  . GLU H  1 84  ? 54.458  148.950 43.367 1.00 54.04  ? 78  GLU H CD  1 
ATOM   8345  O  OE1 . GLU H  1 84  ? 54.605  150.099 43.853 1.00 44.38  ? 78  GLU H OE1 1 
ATOM   8346  O  OE2 . GLU H  1 84  ? 54.686  148.692 42.156 1.00 64.64  ? 78  GLU H OE2 1 
ATOM   8347  N  N   . ARG H  1 85  ? 57.230  145.578 44.570 1.00 41.59  ? 79  ARG H N   1 
ATOM   8348  C  CA  . ARG H  1 85  ? 58.053  145.200 45.716 1.00 39.53  ? 79  ARG H CA  1 
ATOM   8349  C  C   . ARG H  1 85  ? 59.358  145.978 45.699 1.00 38.49  ? 79  ARG H C   1 
ATOM   8350  O  O   . ARG H  1 85  ? 59.757  146.523 44.667 1.00 37.31  ? 79  ARG H O   1 
ATOM   8351  C  CB  . ARG H  1 85  ? 58.363  143.715 45.660 1.00 39.30  ? 79  ARG H CB  1 
ATOM   8352  C  CG  . ARG H  1 85  ? 59.116  143.323 44.413 1.00 33.83  ? 79  ARG H CG  1 
ATOM   8353  C  CD  . ARG H  1 85  ? 60.537  142.936 44.753 1.00 45.77  ? 79  ARG H CD  1 
ATOM   8354  N  NE  . ARG H  1 85  ? 60.751  141.507 44.574 1.00 42.46  ? 79  ARG H NE  1 
ATOM   8355  C  CZ  . ARG H  1 85  ? 61.904  140.879 44.784 1.00 37.91  ? 79  ARG H CZ  1 
ATOM   8356  N  NH1 . ARG H  1 85  ? 62.980  141.538 45.198 1.00 25.91  ? 79  ARG H NH1 1 
ATOM   8357  N  NH2 . ARG H  1 85  ? 61.976  139.579 44.550 1.00 37.30  ? 79  ARG H NH2 1 
ATOM   8358  N  N   . HIS H  1 86  ? 60.010  146.047 46.851 1.00 33.70  ? 80  HIS H N   1 
ATOM   8359  C  CA  . HIS H  1 86  ? 61.276  146.750 46.945 1.00 30.27  ? 80  HIS H CA  1 
ATOM   8360  C  C   . HIS H  1 86  ? 62.268  145.789 46.334 1.00 28.65  ? 80  HIS H C   1 
ATOM   8361  O  O   . HIS H  1 86  ? 62.033  144.580 46.347 1.00 26.21  ? 80  HIS H O   1 
ATOM   8362  C  CB  . HIS H  1 86  ? 61.680  146.973 48.409 1.00 35.12  ? 80  HIS H CB  1 
ATOM   8363  C  CG  . HIS H  1 86  ? 60.774  147.882 49.170 1.00 35.76  ? 80  HIS H CG  1 
ATOM   8364  N  ND1 . HIS H  1 86  ? 60.595  147.771 50.532 1.00 35.51  ? 80  HIS H ND1 1 
ATOM   8365  C  CD2 . HIS H  1 86  ? 60.027  148.940 48.776 1.00 38.29  ? 80  HIS H CD2 1 
ATOM   8366  C  CE1 . HIS H  1 86  ? 59.776  148.721 50.944 1.00 36.05  ? 80  HIS H CE1 1 
ATOM   8367  N  NE2 . HIS H  1 86  ? 59.418  149.445 49.899 1.00 35.25  ? 80  HIS H NE2 1 
ATOM   8368  N  N   . VAL H  1 87  ? 63.369  146.304 45.799 1.00 29.50  ? 81  VAL H N   1 
ATOM   8369  C  CA  . VAL H  1 87  ? 64.380  145.419 45.254 1.00 32.59  ? 81  VAL H CA  1 
ATOM   8370  C  C   . VAL H  1 87  ? 64.809  144.498 46.402 1.00 34.37  ? 81  VAL H C   1 
ATOM   8371  O  O   . VAL H  1 87  ? 64.861  143.277 46.249 1.00 31.10  ? 81  VAL H O   1 
ATOM   8372  C  CB  . VAL H  1 87  ? 65.606  146.202 44.733 1.00 38.09  ? 81  VAL H CB  1 
ATOM   8373  C  CG1 . VAL H  1 87  ? 66.775  145.259 44.529 1.00 37.03  ? 81  VAL H CG1 1 
ATOM   8374  C  CG2 . VAL H  1 87  ? 65.264  146.888 43.402 1.00 33.68  ? 81  VAL H CG2 1 
ATOM   8375  N  N   . GLY H  1 88  ? 65.076  145.085 47.566 1.00 32.56  ? 82  GLY H N   1 
ATOM   8376  C  CA  . GLY H  1 88  ? 65.502  144.290 48.707 1.00 27.47  ? 82  GLY H CA  1 
ATOM   8377  C  C   . GLY H  1 88  ? 64.469  143.377 49.360 1.00 29.86  ? 82  GLY H C   1 
ATOM   8378  O  O   . GLY H  1 88  ? 64.778  142.767 50.381 1.00 28.06  ? 82  GLY H O   1 
ATOM   8379  N  N   . ASP H  1 89  ? 63.260  143.261 48.809 1.00 25.09  ? 83  ASP H N   1 
ATOM   8380  C  CA  . ASP H  1 89  ? 62.243  142.399 49.433 1.00 32.48  ? 83  ASP H CA  1 
ATOM   8381  C  C   . ASP H  1 89  ? 62.409  140.901 49.114 1.00 36.37  ? 83  ASP H C   1 
ATOM   8382  O  O   . ASP H  1 89  ? 61.936  140.405 48.080 1.00 37.39  ? 83  ASP H O   1 
ATOM   8383  C  CB  . ASP H  1 89  ? 60.830  142.860 49.039 1.00 34.36  ? 83  ASP H CB  1 
ATOM   8384  C  CG  . ASP H  1 89  ? 60.460  144.213 49.635 1.00 35.70  ? 83  ASP H CG  1 
ATOM   8385  O  OD1 . ASP H  1 89  ? 61.251  144.755 50.433 1.00 26.52  ? 83  ASP H OD1 1 
ATOM   8386  O  OD2 . ASP H  1 89  ? 59.372  144.736 49.305 1.00 31.55  ? 83  ASP H OD2 1 
ATOM   8387  N  N   . LEU H  1 90  ? 63.067  140.176 50.019 1.00 34.29  ? 84  LEU H N   1 
ATOM   8388  C  CA  . LEU H  1 90  ? 63.304  138.754 49.822 1.00 28.02  ? 84  LEU H CA  1 
ATOM   8389  C  C   . LEU H  1 90  ? 62.321  137.869 50.579 1.00 35.34  ? 84  LEU H C   1 
ATOM   8390  O  O   . LEU H  1 90  ? 62.441  136.639 50.565 1.00 39.62  ? 84  LEU H O   1 
ATOM   8391  C  CB  . LEU H  1 90  ? 64.753  138.410 50.195 1.00 27.77  ? 84  LEU H CB  1 
ATOM   8392  C  CG  . LEU H  1 90  ? 65.793  139.146 49.324 1.00 29.48  ? 84  LEU H CG  1 
ATOM   8393  C  CD1 . LEU H  1 90  ? 67.195  138.885 49.846 1.00 21.78  ? 84  LEU H CD1 1 
ATOM   8394  C  CD2 . LEU H  1 90  ? 65.673  138.698 47.868 1.00 14.03  ? 84  LEU H CD2 1 
ATOM   8395  N  N   . GLY H  1 91  ? 61.341  138.487 51.235 1.00 32.99  ? 85  GLY H N   1 
ATOM   8396  C  CA  . GLY H  1 91  ? 60.338  137.712 51.947 1.00 26.15  ? 85  GLY H CA  1 
ATOM   8397  C  C   . GLY H  1 91  ? 60.744  137.234 53.325 1.00 29.63  ? 85  GLY H C   1 
ATOM   8398  O  O   . GLY H  1 91  ? 61.351  137.968 54.113 1.00 24.84  ? 85  GLY H O   1 
ATOM   8399  N  N   . ASN H  1 92  ? 60.385  135.994 53.631 1.00 30.44  ? 86  ASN H N   1 
ATOM   8400  C  CA  . ASN H  1 92  ? 60.724  135.407 54.923 1.00 30.01  ? 86  ASN H CA  1 
ATOM   8401  C  C   . ASN H  1 92  ? 61.690  134.239 54.767 1.00 29.22  ? 86  ASN H C   1 
ATOM   8402  O  O   . ASN H  1 92  ? 61.945  133.746 53.659 1.00 28.46  ? 86  ASN H O   1 
ATOM   8403  C  CB  . ASN H  1 92  ? 59.472  134.871 55.631 1.00 25.01  ? 86  ASN H CB  1 
ATOM   8404  C  CG  . ASN H  1 92  ? 58.514  135.966 56.081 1.00 36.20  ? 86  ASN H CG  1 
ATOM   8405  O  OD1 . ASN H  1 92  ? 58.834  136.787 56.948 1.00 26.12  ? 86  ASN H OD1 1 
ATOM   8406  N  ND2 . ASN H  1 92  ? 57.317  135.971 55.496 1.00 24.72  ? 86  ASN H ND2 1 
ATOM   8407  N  N   . VAL H  1 93  ? 62.238  133.828 55.903 1.00 27.35  ? 87  VAL H N   1 
ATOM   8408  C  CA  . VAL H  1 93  ? 63.108  132.672 56.002 1.00 25.77  ? 87  VAL H CA  1 
ATOM   8409  C  C   . VAL H  1 93  ? 62.454  131.988 57.193 1.00 29.01  ? 87  VAL H C   1 
ATOM   8410  O  O   . VAL H  1 93  ? 61.832  132.654 58.027 1.00 23.96  ? 87  VAL H O   1 
ATOM   8411  C  CB  . VAL H  1 93  ? 64.574  133.022 56.347 1.00 27.52  ? 87  VAL H CB  1 
ATOM   8412  C  CG1 . VAL H  1 93  ? 65.216  133.752 55.192 1.00 24.86  ? 87  VAL H CG1 1 
ATOM   8413  C  CG2 . VAL H  1 93  ? 64.644  133.826 57.633 1.00 28.69  ? 87  VAL H CG2 1 
ATOM   8414  N  N   . THR H  1 94  ? 62.580  130.674 57.273 1.00 28.39  ? 88  THR H N   1 
ATOM   8415  C  CA  . THR H  1 94  ? 61.958  129.935 58.352 1.00 30.25  ? 88  THR H CA  1 
ATOM   8416  C  C   . THR H  1 94  ? 62.948  129.227 59.257 1.00 28.36  ? 88  THR H C   1 
ATOM   8417  O  O   . THR H  1 94  ? 63.773  128.451 58.791 1.00 28.54  ? 88  THR H O   1 
ATOM   8418  C  CB  . THR H  1 94  ? 60.994  128.895 57.783 1.00 29.84  ? 88  THR H CB  1 
ATOM   8419  O  OG1 . THR H  1 94  ? 60.025  129.564 56.979 1.00 27.52  ? 88  THR H OG1 1 
ATOM   8420  C  CG2 . THR H  1 94  ? 60.298  128.120 58.900 1.00 30.89  ? 88  THR H CG2 1 
ATOM   8421  N  N   . ALA H  1 95  ? 62.837  129.496 60.553 1.00 25.70  ? 89  ALA H N   1 
ATOM   8422  C  CA  . ALA H  1 95  ? 63.688  128.879 61.555 1.00 22.92  ? 89  ALA H CA  1 
ATOM   8423  C  C   . ALA H  1 95  ? 62.946  127.677 62.136 1.00 29.08  ? 89  ALA H C   1 
ATOM   8424  O  O   . ALA H  1 95  ? 61.739  127.752 62.383 1.00 31.60  ? 89  ALA H O   1 
ATOM   8425  C  CB  . ALA H  1 95  ? 63.998  129.885 62.660 1.00 23.94  ? 89  ALA H CB  1 
ATOM   8426  N  N   . ASP H  1 96  ? 63.662  126.579 62.364 1.00 24.74  ? 90  ASP H N   1 
ATOM   8427  C  CA  . ASP H  1 96  ? 63.051  125.372 62.911 1.00 26.70  ? 90  ASP H CA  1 
ATOM   8428  C  C   . ASP H  1 96  ? 62.992  125.390 64.445 1.00 32.84  ? 90  ASP H C   1 
ATOM   8429  O  O   . ASP H  1 96  ? 63.328  126.395 65.075 1.00 28.50  ? 90  ASP H O   1 
ATOM   8430  C  CB  . ASP H  1 96  ? 63.805  124.123 62.400 1.00 30.81  ? 90  ASP H CB  1 
ATOM   8431  C  CG  . ASP H  1 96  ? 65.291  124.094 62.805 1.00 44.28  ? 90  ASP H CG  1 
ATOM   8432  O  OD1 . ASP H  1 96  ? 66.059  123.367 62.141 1.00 45.22  ? 90  ASP H OD1 1 
ATOM   8433  O  OD2 . ASP H  1 96  ? 65.704  124.771 63.776 1.00 45.82  ? 90  ASP H OD2 1 
ATOM   8434  N  N   . LYS H  1 97  ? 62.552  124.283 65.041 1.00 36.97  ? 91  LYS H N   1 
ATOM   8435  C  CA  . LYS H  1 97  ? 62.458  124.182 66.494 1.00 40.66  ? 91  LYS H CA  1 
ATOM   8436  C  C   . LYS H  1 97  ? 63.825  124.215 67.180 1.00 40.80  ? 91  LYS H C   1 
ATOM   8437  O  O   . LYS H  1 97  ? 63.904  124.255 68.406 1.00 38.25  ? 91  LYS H O   1 
ATOM   8438  C  CB  . LYS H  1 97  ? 61.720  122.905 66.888 1.00 43.00  ? 91  LYS H CB  1 
ATOM   8439  C  CG  . LYS H  1 97  ? 62.346  121.624 66.361 1.00 53.96  ? 91  LYS H CG  1 
ATOM   8440  C  CD  . LYS H  1 97  ? 61.481  120.422 66.736 1.00 61.19  ? 91  LYS H CD  1 
ATOM   8441  C  CE  . LYS H  1 97  ? 62.095  119.100 66.300 1.00 62.39  ? 91  LYS H CE  1 
ATOM   8442  N  NZ  . LYS H  1 97  ? 61.200  117.953 66.648 1.00 67.47  ? 91  LYS H NZ  1 
ATOM   8443  N  N   . ASP H  1 98  ? 64.895  124.186 66.390 1.00 37.12  ? 92  ASP H N   1 
ATOM   8444  C  CA  . ASP H  1 98  ? 66.250  124.243 66.928 1.00 38.62  ? 92  ASP H CA  1 
ATOM   8445  C  C   . ASP H  1 98  ? 66.862  125.635 66.749 1.00 37.60  ? 92  ASP H C   1 
ATOM   8446  O  O   . ASP H  1 98  ? 68.072  125.818 66.930 1.00 35.69  ? 92  ASP H O   1 
ATOM   8447  C  CB  . ASP H  1 98  ? 67.133  123.204 66.243 1.00 42.14  ? 92  ASP H CB  1 
ATOM   8448  C  CG  . ASP H  1 98  ? 66.812  121.789 66.679 1.00 52.05  ? 92  ASP H CG  1 
ATOM   8449  O  OD1 . ASP H  1 98  ? 67.284  120.841 66.017 1.00 65.08  ? 92  ASP H OD1 1 
ATOM   8450  O  OD2 . ASP H  1 98  ? 66.095  121.619 67.685 1.00 46.96  ? 92  ASP H OD2 1 
ATOM   8451  N  N   . ALA H  1 99  ? 66.023  126.598 66.363 1.00 29.72  ? 93  ALA H N   1 
ATOM   8452  C  CA  . ALA H  1 99  ? 66.444  127.981 66.178 1.00 28.74  ? 93  ALA H CA  1 
ATOM   8453  C  C   . ALA H  1 99  ? 67.321  128.205 64.948 1.00 31.42  ? 93  ALA H C   1 
ATOM   8454  O  O   . ALA H  1 99  ? 67.967  129.250 64.812 1.00 28.32  ? 93  ALA H O   1 
ATOM   8455  C  CB  . ALA H  1 99  ? 67.172  128.477 67.454 1.00 22.07  ? 93  ALA H CB  1 
ATOM   8456  N  N   . VAL H  1 100 ? 67.327  127.238 64.038 1.00 32.33  ? 94  VAL H N   1 
ATOM   8457  C  CA  . VAL H  1 100 ? 68.142  127.347 62.830 1.00 28.27  ? 94  VAL H CA  1 
ATOM   8458  C  C   . VAL H  1 100 ? 67.317  127.599 61.567 1.00 32.67  ? 94  VAL H C   1 
ATOM   8459  O  O   . VAL H  1 100 ? 66.292  126.953 61.330 1.00 28.82  ? 94  VAL H O   1 
ATOM   8460  C  CB  . VAL H  1 100 ? 68.965  126.060 62.610 1.00 27.15  ? 94  VAL H CB  1 
ATOM   8461  C  CG1 . VAL H  1 100 ? 69.641  126.067 61.236 1.00 16.90  ? 94  VAL H CG1 1 
ATOM   8462  C  CG2 . VAL H  1 100 ? 69.984  125.933 63.697 1.00 15.70  ? 94  VAL H CG2 1 
ATOM   8463  N  N   . ALA H  1 101 ? 67.767  128.550 60.760 1.00 29.65  ? 95  ALA H N   1 
ATOM   8464  C  CA  . ALA H  1 101 ? 67.093  128.833 59.511 1.00 29.14  ? 95  ALA H CA  1 
ATOM   8465  C  C   . ALA H  1 101 ? 68.043  128.432 58.401 1.00 27.14  ? 95  ALA H C   1 
ATOM   8466  O  O   . ALA H  1 101 ? 69.067  129.077 58.194 1.00 26.45  ? 95  ALA H O   1 
ATOM   8467  C  CB  . ALA H  1 101 ? 66.754  130.303 59.404 1.00 26.06  ? 95  ALA H CB  1 
ATOM   8468  N  N   . ASP H  1 102 ? 67.728  127.332 57.724 1.00 27.05  ? 96  ASP H N   1 
ATOM   8469  C  CA  . ASP H  1 102 ? 68.545  126.868 56.613 1.00 31.06  ? 96  ASP H CA  1 
ATOM   8470  C  C   . ASP H  1 102 ? 68.000  127.583 55.387 1.00 29.93  ? 96  ASP H C   1 
ATOM   8471  O  O   . ASP H  1 102 ? 67.147  127.078 54.664 1.00 36.78  ? 96  ASP H O   1 
ATOM   8472  C  CB  . ASP H  1 102 ? 68.427  125.354 56.464 1.00 41.17  ? 96  ASP H CB  1 
ATOM   8473  C  CG  . ASP H  1 102 ? 69.241  124.605 57.506 1.00 51.55  ? 96  ASP H CG  1 
ATOM   8474  O  OD1 . ASP H  1 102 ? 68.750  123.570 58.016 1.00 58.37  ? 96  ASP H OD1 1 
ATOM   8475  O  OD2 . ASP H  1 102 ? 70.376  125.049 57.806 1.00 47.35  ? 96  ASP H OD2 1 
ATOM   8476  N  N   . VAL H  1 103 ? 68.502  128.782 55.171 1.00 25.14  ? 97  VAL H N   1 
ATOM   8477  C  CA  . VAL H  1 103 ? 68.050  129.597 54.076 1.00 26.59  ? 97  VAL H CA  1 
ATOM   8478  C  C   . VAL H  1 103 ? 68.387  129.053 52.698 1.00 31.07  ? 97  VAL H C   1 
ATOM   8479  O  O   . VAL H  1 103 ? 69.506  128.627 52.432 1.00 37.50  ? 97  VAL H O   1 
ATOM   8480  C  CB  . VAL H  1 103 ? 68.627  131.019 54.203 1.00 27.49  ? 97  VAL H CB  1 
ATOM   8481  C  CG1 . VAL H  1 103 ? 68.128  131.899 53.046 1.00 20.50  ? 97  VAL H CG1 1 
ATOM   8482  C  CG2 . VAL H  1 103 ? 68.238  131.618 55.571 1.00 14.67  ? 97  VAL H CG2 1 
ATOM   8483  N  N   . SER H  1 104 ? 67.395  129.084 51.821 1.00 32.78  ? 98  SER H N   1 
ATOM   8484  C  CA  . SER H  1 104 ? 67.560  128.656 50.443 1.00 36.29  ? 98  SER H CA  1 
ATOM   8485  C  C   . SER H  1 104 ? 66.518  129.432 49.666 1.00 34.37  ? 98  SER H C   1 
ATOM   8486  O  O   . SER H  1 104 ? 65.343  129.092 49.678 1.00 39.01  ? 98  SER H O   1 
ATOM   8487  C  CB  . SER H  1 104 ? 67.325  127.161 50.291 1.00 35.95  ? 98  SER H CB  1 
ATOM   8488  O  OG  . SER H  1 104 ? 67.691  126.750 48.986 1.00 42.46  ? 98  SER H OG  1 
ATOM   8489  N  N   . ILE H  1 105 ? 66.967  130.487 49.002 1.00 34.53  ? 99  ILE H N   1 
ATOM   8490  C  CA  . ILE H  1 105 ? 66.098  131.364 48.249 1.00 30.93  ? 99  ILE H CA  1 
ATOM   8491  C  C   . ILE H  1 105 ? 66.639  131.615 46.869 1.00 32.61  ? 99  ILE H C   1 
ATOM   8492  O  O   . ILE H  1 105 ? 67.837  131.600 46.652 1.00 33.36  ? 99  ILE H O   1 
ATOM   8493  C  CB  . ILE H  1 105 ? 65.973  132.729 48.967 1.00 34.00  ? 99  ILE H CB  1 
ATOM   8494  C  CG1 . ILE H  1 105 ? 64.976  132.602 50.113 1.00 33.14  ? 99  ILE H CG1 1 
ATOM   8495  C  CG2 . ILE H  1 105 ? 65.553  133.848 47.987 1.00 22.24  ? 99  ILE H CG2 1 
ATOM   8496  C  CD1 . ILE H  1 105 ? 64.835  133.867 50.897 1.00 38.48  ? 99  ILE H CD1 1 
ATOM   8497  N  N   . GLU H  1 106 ? 65.745  131.850 45.926 1.00 37.42  ? 100 GLU H N   1 
ATOM   8498  C  CA  . GLU H  1 106 ? 66.175  132.157 44.580 1.00 43.35  ? 100 GLU H CA  1 
ATOM   8499  C  C   . GLU H  1 106 ? 65.382  133.381 44.196 1.00 38.31  ? 100 GLU H C   1 
ATOM   8500  O  O   . GLU H  1 106 ? 64.160  133.384 44.285 1.00 36.46  ? 100 GLU H O   1 
ATOM   8501  C  CB  . GLU H  1 106 ? 65.895  131.003 43.636 1.00 43.18  ? 100 GLU H CB  1 
ATOM   8502  C  CG  . GLU H  1 106 ? 66.677  131.140 42.367 1.00 60.07  ? 100 GLU H CG  1 
ATOM   8503  C  CD  . GLU H  1 106 ? 66.619  129.902 41.526 1.00 66.06  ? 100 GLU H CD  1 
ATOM   8504  O  OE1 . GLU H  1 106 ? 67.056  128.835 42.017 1.00 70.22  ? 100 GLU H OE1 1 
ATOM   8505  O  OE2 . GLU H  1 106 ? 66.135  130.005 40.378 1.00 62.46  ? 100 GLU H OE2 1 
ATOM   8506  N  N   . ASP H  1 107 ? 66.086  134.423 43.773 1.00 37.52  ? 101 ASP H N   1 
ATOM   8507  C  CA  . ASP H  1 107 ? 65.445  135.682 43.441 1.00 36.00  ? 101 ASP H CA  1 
ATOM   8508  C  C   . ASP H  1 107 ? 65.988  136.304 42.180 1.00 37.88  ? 101 ASP H C   1 
ATOM   8509  O  O   . ASP H  1 107 ? 67.194  136.364 42.000 1.00 46.58  ? 101 ASP H O   1 
ATOM   8510  C  CB  . ASP H  1 107 ? 65.651  136.656 44.594 1.00 41.56  ? 101 ASP H CB  1 
ATOM   8511  C  CG  . ASP H  1 107 ? 64.777  137.863 44.480 1.00 36.31  ? 101 ASP H CG  1 
ATOM   8512  O  OD1 . ASP H  1 107 ? 65.273  138.932 44.055 1.00 40.58  ? 101 ASP H OD1 1 
ATOM   8513  O  OD2 . ASP H  1 107 ? 63.582  137.718 44.810 1.00 34.87  ? 101 ASP H OD2 1 
ATOM   8514  N  N   . SER H  1 108 ? 65.105  136.821 41.331 1.00 42.04  ? 102 SER H N   1 
ATOM   8515  C  CA  . SER H  1 108 ? 65.548  137.415 40.074 1.00 44.02  ? 102 SER H CA  1 
ATOM   8516  C  C   . SER H  1 108 ? 65.490  138.939 40.009 1.00 42.79  ? 102 SER H C   1 
ATOM   8517  O  O   . SER H  1 108 ? 65.670  139.524 38.935 1.00 41.39  ? 102 SER H O   1 
ATOM   8518  C  CB  . SER H  1 108 ? 64.743  136.826 38.919 1.00 41.92  ? 102 SER H CB  1 
ATOM   8519  O  OG  . SER H  1 108 ? 63.369  137.110 39.090 1.00 49.51  ? 102 SER H OG  1 
ATOM   8520  N  N   . VAL H  1 109 ? 65.238  139.589 41.141 1.00 39.84  ? 103 VAL H N   1 
ATOM   8521  C  CA  . VAL H  1 109 ? 65.189  141.047 41.151 1.00 37.10  ? 103 VAL H CA  1 
ATOM   8522  C  C   . VAL H  1 109 ? 66.456  141.657 41.751 1.00 37.83  ? 103 VAL H C   1 
ATOM   8523  O  O   . VAL H  1 109 ? 66.955  142.660 41.246 1.00 36.58  ? 103 VAL H O   1 
ATOM   8524  C  CB  . VAL H  1 109 ? 63.940  141.564 41.891 1.00 35.97  ? 103 VAL H CB  1 
ATOM   8525  C  CG1 . VAL H  1 109 ? 64.067  143.051 42.158 1.00 25.18  ? 103 VAL H CG1 1 
ATOM   8526  C  CG2 . VAL H  1 109 ? 62.698  141.293 41.036 1.00 25.67  ? 103 VAL H CG2 1 
ATOM   8527  N  N   . ILE H  1 110 ? 66.972  141.064 42.825 1.00 35.28  ? 104 ILE H N   1 
ATOM   8528  C  CA  . ILE H  1 110 ? 68.210  141.568 43.413 1.00 41.05  ? 104 ILE H CA  1 
ATOM   8529  C  C   . ILE H  1 110 ? 69.320  141.161 42.446 1.00 41.06  ? 104 ILE H C   1 
ATOM   8530  O  O   . ILE H  1 110 ? 69.182  140.192 41.710 1.00 39.94  ? 104 ILE H O   1 
ATOM   8531  C  CB  . ILE H  1 110 ? 68.538  140.920 44.793 1.00 39.53  ? 104 ILE H CB  1 
ATOM   8532  C  CG1 . ILE H  1 110 ? 68.648  139.402 44.643 1.00 31.46  ? 104 ILE H CG1 1 
ATOM   8533  C  CG2 . ILE H  1 110 ? 67.488  141.301 45.820 1.00 41.21  ? 104 ILE H CG2 1 
ATOM   8534  C  CD1 . ILE H  1 110 ? 69.251  138.698 45.823 1.00 32.20  ? 104 ILE H CD1 1 
ATOM   8535  N  N   . SER H  1 111 ? 70.422  141.892 42.442 1.00 39.57  ? 105 SER H N   1 
ATOM   8536  C  CA  . SER H  1 111 ? 71.513  141.533 41.557 1.00 41.34  ? 105 SER H CA  1 
ATOM   8537  C  C   . SER H  1 111 ? 72.858  141.765 42.223 1.00 32.64  ? 105 SER H C   1 
ATOM   8538  O  O   . SER H  1 111 ? 72.952  142.475 43.221 1.00 36.36  ? 105 SER H O   1 
ATOM   8539  C  CB  . SER H  1 111 ? 71.429  142.338 40.256 1.00 39.42  ? 105 SER H CB  1 
ATOM   8540  O  OG  . SER H  1 111 ? 72.431  141.916 39.347 1.00 37.17  ? 105 SER H OG  1 
ATOM   8541  N  N   . LEU H  1 112 ? 73.896  141.158 41.662 1.00 30.81  ? 106 LEU H N   1 
ATOM   8542  C  CA  . LEU H  1 112 ? 75.245  141.319 42.179 1.00 35.22  ? 106 LEU H CA  1 
ATOM   8543  C  C   . LEU H  1 112 ? 76.034  142.265 41.282 1.00 36.48  ? 106 LEU H C   1 
ATOM   8544  O  O   . LEU H  1 112 ? 77.266  142.284 41.312 1.00 38.82  ? 106 LEU H O   1 
ATOM   8545  C  CB  . LEU H  1 112 ? 75.950  139.959 42.285 1.00 30.59  ? 106 LEU H CB  1 
ATOM   8546  C  CG  . LEU H  1 112 ? 75.259  138.940 43.219 1.00 36.29  ? 106 LEU H CG  1 
ATOM   8547  C  CD1 . LEU H  1 112 ? 76.188  137.755 43.499 1.00 32.30  ? 106 LEU H CD1 1 
ATOM   8548  C  CD2 . LEU H  1 112 ? 74.864  139.613 44.536 1.00 27.54  ? 106 LEU H CD2 1 
ATOM   8549  N  N   . SER H  1 113 ? 75.307  143.058 40.494 1.00 37.71  ? 107 SER H N   1 
ATOM   8550  C  CA  . SER H  1 113 ? 75.894  144.045 39.581 1.00 44.90  ? 107 SER H CA  1 
ATOM   8551  C  C   . SER H  1 113 ? 74.817  144.988 39.020 1.00 48.41  ? 107 SER H C   1 
ATOM   8552  O  O   . SER H  1 113 ? 73.619  144.712 39.114 1.00 48.75  ? 107 SER H O   1 
ATOM   8553  C  CB  . SER H  1 113 ? 76.601  143.331 38.433 1.00 39.95  ? 107 SER H CB  1 
ATOM   8554  O  OG  . SER H  1 113 ? 75.729  142.361 37.882 1.00 52.67  ? 107 SER H OG  1 
ATOM   8555  N  N   . GLY H  1 114 ? 75.241  146.107 38.446 1.00 54.12  ? 108 GLY H N   1 
ATOM   8556  C  CA  . GLY H  1 114 ? 74.286  147.043 37.885 1.00 61.15  ? 108 GLY H CA  1 
ATOM   8557  C  C   . GLY H  1 114 ? 73.718  148.038 38.878 1.00 69.80  ? 108 GLY H C   1 
ATOM   8558  O  O   . GLY H  1 114 ? 74.294  148.282 39.935 1.00 75.29  ? 108 GLY H O   1 
ATOM   8559  N  N   . ASP H  1 115 ? 72.571  148.610 38.529 1.00 76.77  ? 109 ASP H N   1 
ATOM   8560  C  CA  . ASP H  1 115 ? 71.893  149.602 39.361 1.00 76.25  ? 109 ASP H CA  1 
ATOM   8561  C  C   . ASP H  1 115 ? 71.119  148.961 40.508 1.00 74.06  ? 109 ASP H C   1 
ATOM   8562  O  O   . ASP H  1 115 ? 70.640  149.651 41.410 1.00 67.43  ? 109 ASP H O   1 
ATOM   8563  C  CB  . ASP H  1 115 ? 70.945  150.431 38.488 1.00 83.32  ? 109 ASP H CB  1 
ATOM   8564  C  CG  . ASP H  1 115 ? 71.690  151.317 37.492 1.00 90.22  ? 109 ASP H CG  1 
ATOM   8565  O  OD1 . ASP H  1 115 ? 72.739  150.880 36.961 1.00 95.42  ? 109 ASP H OD1 1 
ATOM   8566  O  OD2 . ASP H  1 115 ? 71.219  152.449 37.235 1.00 85.51  ? 109 ASP H OD2 1 
ATOM   8567  N  N   . HIS H  1 116 ? 70.989  147.638 40.457 1.00 72.46  ? 110 HIS H N   1 
ATOM   8568  C  CA  . HIS H  1 116 ? 70.289  146.893 41.498 1.00 70.74  ? 110 HIS H CA  1 
ATOM   8569  C  C   . HIS H  1 116 ? 71.283  146.105 42.342 1.00 66.89  ? 110 HIS H C   1 
ATOM   8570  O  O   . HIS H  1 116 ? 70.873  145.257 43.136 1.00 68.79  ? 110 HIS H O   1 
ATOM   8571  C  CB  . HIS H  1 116 ? 69.290  145.896 40.897 1.00 74.95  ? 110 HIS H CB  1 
ATOM   8572  C  CG  . HIS H  1 116 ? 68.128  146.530 40.201 1.00 81.41  ? 110 HIS H CG  1 
ATOM   8573  N  ND1 . HIS H  1 116 ? 67.033  145.804 39.782 1.00 82.44  ? 110 HIS H ND1 1 
ATOM   8574  C  CD2 . HIS H  1 116 ? 67.891  147.813 39.837 1.00 86.18  ? 110 HIS H CD2 1 
ATOM   8575  C  CE1 . HIS H  1 116 ? 66.172  146.612 39.190 1.00 83.70  ? 110 HIS H CE1 1 
ATOM   8576  N  NE2 . HIS H  1 116 ? 66.669  147.837 39.210 1.00 85.59  ? 110 HIS H NE2 1 
ATOM   8577  N  N   . CYS H  1 117 ? 72.578  146.366 42.153 1.00 53.78  ? 111 CYS H N   1 
ATOM   8578  C  CA  . CYS H  1 117 ? 73.632  145.669 42.890 1.00 47.45  ? 111 CYS H CA  1 
ATOM   8579  C  C   . CYS H  1 117 ? 73.356  145.762 44.401 1.00 46.02  ? 111 CYS H C   1 
ATOM   8580  O  O   . CYS H  1 117 ? 73.086  146.838 44.920 1.00 43.67  ? 111 CYS H O   1 
ATOM   8581  C  CB  . CYS H  1 117 ? 74.981  146.315 42.559 1.00 48.78  ? 111 CYS H CB  1 
ATOM   8582  S  SG  . CYS H  1 117 ? 76.479  145.389 42.952 1.00 56.13  ? 111 CYS H SG  1 
ATOM   8583  N  N   . ILE H  1 118 ? 73.392  144.637 45.104 1.00 40.85  ? 112 ILE H N   1 
ATOM   8584  C  CA  . ILE H  1 118 ? 73.164  144.669 46.542 1.00 40.42  ? 112 ILE H CA  1 
ATOM   8585  C  C   . ILE H  1 118 ? 74.505  144.694 47.276 1.00 41.00  ? 112 ILE H C   1 
ATOM   8586  O  O   . ILE H  1 118 ? 74.544  144.805 48.500 1.00 36.48  ? 112 ILE H O   1 
ATOM   8587  C  CB  . ILE H  1 118 ? 72.339  143.448 47.030 1.00 40.79  ? 112 ILE H CB  1 
ATOM   8588  C  CG1 . ILE H  1 118 ? 73.099  142.152 46.744 1.00 35.84  ? 112 ILE H CG1 1 
ATOM   8589  C  CG2 . ILE H  1 118 ? 70.963  143.448 46.361 1.00 38.76  ? 112 ILE H CG2 1 
ATOM   8590  C  CD1 . ILE H  1 118 ? 72.346  140.894 47.127 1.00 31.05  ? 112 ILE H CD1 1 
ATOM   8591  N  N   . ILE H  1 119 ? 75.599  144.589 46.518 1.00 36.65  ? 113 ILE H N   1 
ATOM   8592  C  CA  . ILE H  1 119 ? 76.952  144.623 47.078 1.00 38.52  ? 113 ILE H CA  1 
ATOM   8593  C  C   . ILE H  1 119 ? 77.154  145.964 47.792 1.00 40.58  ? 113 ILE H C   1 
ATOM   8594  O  O   . ILE H  1 119 ? 76.797  147.013 47.252 1.00 38.25  ? 113 ILE H O   1 
ATOM   8595  C  CB  . ILE H  1 119 ? 78.023  144.493 45.966 1.00 42.42  ? 113 ILE H CB  1 
ATOM   8596  C  CG1 . ILE H  1 119 ? 77.921  143.124 45.301 1.00 39.51  ? 113 ILE H CG1 1 
ATOM   8597  C  CG2 . ILE H  1 119 ? 79.416  144.673 46.542 1.00 37.80  ? 113 ILE H CG2 1 
ATOM   8598  C  CD1 . ILE H  1 119 ? 78.175  142.003 46.233 1.00 47.81  ? 113 ILE H CD1 1 
ATOM   8599  N  N   . GLY H  1 120 ? 77.713  145.925 49.004 1.00 36.66  ? 114 GLY H N   1 
ATOM   8600  C  CA  . GLY H  1 120 ? 77.941  147.145 49.766 1.00 32.53  ? 114 GLY H CA  1 
ATOM   8601  C  C   . GLY H  1 120 ? 76.726  147.610 50.557 1.00 30.28  ? 114 GLY H C   1 
ATOM   8602  O  O   . GLY H  1 120 ? 76.726  148.693 51.150 1.00 23.12  ? 114 GLY H O   1 
ATOM   8603  N  N   . ARG H  1 121 ? 75.676  146.797 50.559 1.00 29.57  ? 115 ARG H N   1 
ATOM   8604  C  CA  . ARG H  1 121 ? 74.463  147.150 51.291 1.00 31.29  ? 115 ARG H CA  1 
ATOM   8605  C  C   . ARG H  1 121 ? 74.350  146.181 52.457 1.00 27.73  ? 115 ARG H C   1 
ATOM   8606  O  O   . ARG H  1 121 ? 75.236  145.344 52.650 1.00 33.97  ? 115 ARG H O   1 
ATOM   8607  C  CB  . ARG H  1 121 ? 73.252  147.078 50.350 1.00 26.77  ? 115 ARG H CB  1 
ATOM   8608  C  CG  . ARG H  1 121 ? 73.641  147.510 48.919 1.00 45.91  ? 115 ARG H CG  1 
ATOM   8609  C  CD  . ARG H  1 121 ? 72.522  148.135 48.088 1.00 33.33  ? 115 ARG H CD  1 
ATOM   8610  N  NE  . ARG H  1 121 ? 72.303  149.522 48.466 1.00 45.05  ? 115 ARG H NE  1 
ATOM   8611  C  CZ  . ARG H  1 121 ? 72.525  150.562 47.671 1.00 40.06  ? 115 ARG H CZ  1 
ATOM   8612  N  NH1 . ARG H  1 121 ? 72.973  150.376 46.440 1.00 30.60  ? 115 ARG H NH1 1 
ATOM   8613  N  NH2 . ARG H  1 121 ? 72.298  151.789 48.118 1.00 36.01  ? 115 ARG H NH2 1 
ATOM   8614  N  N   . THR H  1 122 ? 73.279  146.277 53.232 1.00 25.80  ? 116 THR H N   1 
ATOM   8615  C  CA  . THR H  1 122 ? 73.128  145.406 54.388 1.00 28.54  ? 116 THR H CA  1 
ATOM   8616  C  C   . THR H  1 122 ? 72.024  144.367 54.300 1.00 27.87  ? 116 THR H C   1 
ATOM   8617  O  O   . THR H  1 122 ? 70.907  144.668 53.894 1.00 39.30  ? 116 THR H O   1 
ATOM   8618  C  CB  . THR H  1 122 ? 72.891  146.246 55.687 1.00 32.81  ? 116 THR H CB  1 
ATOM   8619  O  OG1 . THR H  1 122 ? 74.016  147.098 55.909 1.00 25.74  ? 116 THR H OG1 1 
ATOM   8620  C  CG2 . THR H  1 122 ? 72.692  145.335 56.912 1.00 24.48  ? 116 THR H CG2 1 
ATOM   8621  N  N   . LEU H  1 123 ? 72.349  143.133 54.676 1.00 30.91  ? 117 LEU H N   1 
ATOM   8622  C  CA  . LEU H  1 123 ? 71.360  142.068 54.708 1.00 28.77  ? 117 LEU H CA  1 
ATOM   8623  C  C   . LEU H  1 123 ? 70.885  142.106 56.167 1.00 28.56  ? 117 LEU H C   1 
ATOM   8624  O  O   . LEU H  1 123 ? 71.700  142.218 57.088 1.00 29.28  ? 117 LEU H O   1 
ATOM   8625  C  CB  . LEU H  1 123 ? 71.988  140.713 54.376 1.00 27.62  ? 117 LEU H CB  1 
ATOM   8626  C  CG  . LEU H  1 123 ? 70.972  139.558 54.365 1.00 40.48  ? 117 LEU H CG  1 
ATOM   8627  C  CD1 . LEU H  1 123 ? 69.871  139.848 53.326 1.00 29.88  ? 117 LEU H CD1 1 
ATOM   8628  C  CD2 . LEU H  1 123 ? 71.677  138.229 54.077 1.00 25.54  ? 117 LEU H CD2 1 
ATOM   8629  N  N   . VAL H  1 124 ? 69.576  142.024 56.375 1.00 22.04  ? 118 VAL H N   1 
ATOM   8630  C  CA  . VAL H  1 124 ? 69.005  142.112 57.708 1.00 21.12  ? 118 VAL H CA  1 
ATOM   8631  C  C   . VAL H  1 124 ? 67.944  141.069 57.941 1.00 26.96  ? 118 VAL H C   1 
ATOM   8632  O  O   . VAL H  1 124 ? 66.990  140.968 57.163 1.00 30.34  ? 118 VAL H O   1 
ATOM   8633  C  CB  . VAL H  1 124 ? 68.298  143.475 57.935 1.00 22.67  ? 118 VAL H CB  1 
ATOM   8634  C  CG1 . VAL H  1 124 ? 67.671  143.511 59.316 1.00 26.01  ? 118 VAL H CG1 1 
ATOM   8635  C  CG2 . VAL H  1 124 ? 69.258  144.618 57.748 1.00 18.80  ? 118 VAL H CG2 1 
ATOM   8636  N  N   . VAL H  1 125 ? 68.087  140.303 59.017 1.00 22.10  ? 119 VAL H N   1 
ATOM   8637  C  CA  . VAL H  1 125 ? 67.069  139.324 59.339 1.00 24.58  ? 119 VAL H CA  1 
ATOM   8638  C  C   . VAL H  1 125 ? 66.224  139.945 60.470 1.00 29.26  ? 119 VAL H C   1 
ATOM   8639  O  O   . VAL H  1 125 ? 66.761  140.372 61.508 1.00 28.76  ? 119 VAL H O   1 
ATOM   8640  C  CB  . VAL H  1 125 ? 67.685  137.976 59.762 1.00 22.86  ? 119 VAL H CB  1 
ATOM   8641  C  CG1 . VAL H  1 125 ? 68.593  138.154 60.957 1.00 23.93  ? 119 VAL H CG1 1 
ATOM   8642  C  CG2 . VAL H  1 125 ? 66.571  136.984 60.065 1.00 19.63  ? 119 VAL H CG2 1 
ATOM   8643  N  N   . HIS H  1 126 ? 64.907  139.999 60.258 1.00 22.65  ? 120 HIS H N   1 
ATOM   8644  C  CA  . HIS H  1 126 ? 63.992  140.620 61.214 1.00 23.14  ? 120 HIS H CA  1 
ATOM   8645  C  C   . HIS H  1 126 ? 63.364  139.752 62.307 1.00 26.85  ? 120 HIS H C   1 
ATOM   8646  O  O   . HIS H  1 126 ? 63.322  138.523 62.231 1.00 30.32  ? 120 HIS H O   1 
ATOM   8647  C  CB  . HIS H  1 126 ? 62.884  141.363 60.437 1.00 22.69  ? 120 HIS H CB  1 
ATOM   8648  C  CG  . HIS H  1 126 ? 63.369  142.590 59.727 1.00 21.62  ? 120 HIS H CG  1 
ATOM   8649  N  ND1 . HIS H  1 126 ? 63.317  143.846 60.293 1.00 22.98  ? 120 HIS H ND1 1 
ATOM   8650  C  CD2 . HIS H  1 126 ? 63.980  142.745 58.527 1.00 17.25  ? 120 HIS H CD2 1 
ATOM   8651  C  CE1 . HIS H  1 126 ? 63.878  144.722 59.474 1.00 24.29  ? 120 HIS H CE1 1 
ATOM   8652  N  NE2 . HIS H  1 126 ? 64.287  144.080 58.394 1.00 23.44  ? 120 HIS H NE2 1 
ATOM   8653  N  N   . GLU H  1 127 ? 62.856  140.442 63.322 1.00 30.29  ? 121 GLU H N   1 
ATOM   8654  C  CA  . GLU H  1 127 ? 62.202  139.858 64.491 1.00 31.34  ? 121 GLU H CA  1 
ATOM   8655  C  C   . GLU H  1 127 ? 60.929  139.060 64.203 1.00 32.38  ? 121 GLU H C   1 
ATOM   8656  O  O   . GLU H  1 127 ? 60.786  137.934 64.654 1.00 37.13  ? 121 GLU H O   1 
ATOM   8657  C  CB  . GLU H  1 127 ? 61.877  140.992 65.461 1.00 34.22  ? 121 GLU H CB  1 
ATOM   8658  C  CG  . GLU H  1 127 ? 60.999  140.629 66.631 1.00 41.55  ? 121 GLU H CG  1 
ATOM   8659  C  CD  . GLU H  1 127 ? 60.340  141.862 67.238 1.00 51.60  ? 121 GLU H CD  1 
ATOM   8660  O  OE1 . GLU H  1 127 ? 59.829  141.767 68.378 1.00 55.19  ? 121 GLU H OE1 1 
ATOM   8661  O  OE2 . GLU H  1 127 ? 60.325  142.923 66.567 1.00 49.97  ? 121 GLU H OE2 1 
ATOM   8662  N  N   . LYS H  1 128 ? 59.996  139.653 63.466 1.00 35.26  ? 122 LYS H N   1 
ATOM   8663  C  CA  . LYS H  1 128 ? 58.736  138.987 63.162 1.00 34.62  ? 122 LYS H CA  1 
ATOM   8664  C  C   . LYS H  1 128 ? 58.573  138.678 61.683 1.00 30.18  ? 122 LYS H C   1 
ATOM   8665  O  O   . LYS H  1 128 ? 59.353  139.108 60.833 1.00 25.85  ? 122 LYS H O   1 
ATOM   8666  C  CB  . LYS H  1 128 ? 57.530  139.857 63.559 1.00 39.37  ? 122 LYS H CB  1 
ATOM   8667  C  CG  . LYS H  1 128 ? 57.651  140.723 64.798 1.00 42.55  ? 122 LYS H CG  1 
ATOM   8668  C  CD  . LYS H  1 128 ? 56.416  141.641 64.884 1.00 51.06  ? 122 LYS H CD  1 
ATOM   8669  C  CE  . LYS H  1 128 ? 56.526  142.760 65.928 1.00 53.95  ? 122 LYS H CE  1 
ATOM   8670  N  NZ  . LYS H  1 128 ? 56.420  142.297 67.343 1.00 58.78  ? 122 LYS H NZ  1 
ATOM   8671  N  N   . ALA H  1 129 ? 57.507  137.954 61.389 1.00 24.39  ? 123 ALA H N   1 
ATOM   8672  C  CA  . ALA H  1 129 ? 57.185  137.604 60.025 1.00 29.34  ? 123 ALA H CA  1 
ATOM   8673  C  C   . ALA H  1 129 ? 56.891  138.864 59.204 1.00 29.59  ? 123 ALA H C   1 
ATOM   8674  O  O   . ALA H  1 129 ? 56.378  139.864 59.721 1.00 29.90  ? 123 ALA H O   1 
ATOM   8675  C  CB  . ALA H  1 129 ? 55.970  136.688 60.014 1.00 16.76  ? 123 ALA H CB  1 
ATOM   8676  N  N   . ASP H  1 130 ? 57.239  138.801 57.926 1.00 27.25  ? 124 ASP H N   1 
ATOM   8677  C  CA  . ASP H  1 130 ? 56.995  139.879 56.959 1.00 26.38  ? 124 ASP H CA  1 
ATOM   8678  C  C   . ASP H  1 130 ? 55.598  139.552 56.413 1.00 28.23  ? 124 ASP H C   1 
ATOM   8679  O  O   . ASP H  1 130 ? 55.382  138.438 55.937 1.00 28.14  ? 124 ASP H O   1 
ATOM   8680  C  CB  . ASP H  1 130 ? 58.033  139.780 55.833 1.00 25.10  ? 124 ASP H CB  1 
ATOM   8681  C  CG  . ASP H  1 130 ? 57.827  140.795 54.737 1.00 28.23  ? 124 ASP H CG  1 
ATOM   8682  O  OD1 . ASP H  1 130 ? 58.756  140.974 53.927 1.00 33.98  ? 124 ASP H OD1 1 
ATOM   8683  O  OD2 . ASP H  1 130 ? 56.747  141.412 54.671 1.00 35.93  ? 124 ASP H OD2 1 
ATOM   8684  N  N   . ASP H  1 131 ? 54.649  140.484 56.489 1.00 26.58  ? 125 ASP H N   1 
ATOM   8685  C  CA  . ASP H  1 131 ? 53.303  140.193 55.990 1.00 27.21  ? 125 ASP H CA  1 
ATOM   8686  C  C   . ASP H  1 131 ? 53.217  140.398 54.474 1.00 28.39  ? 125 ASP H C   1 
ATOM   8687  O  O   . ASP H  1 131 ? 52.138  140.401 53.878 1.00 32.17  ? 125 ASP H O   1 
ATOM   8688  C  CB  . ASP H  1 131 ? 52.237  141.024 56.749 1.00 23.82  ? 125 ASP H CB  1 
ATOM   8689  C  CG  . ASP H  1 131 ? 52.352  142.523 56.504 1.00 33.19  ? 125 ASP H CG  1 
ATOM   8690  O  OD1 . ASP H  1 131 ? 51.837  143.282 57.364 1.00 25.76  ? 125 ASP H OD1 1 
ATOM   8691  O  OD2 . ASP H  1 131 ? 52.938  142.945 55.469 1.00 26.63  ? 125 ASP H OD2 1 
ATOM   8692  N  N   . LEU H  1 132 ? 54.385  140.557 53.861 1.00 24.43  ? 126 LEU H N   1 
ATOM   8693  C  CA  . LEU H  1 132 ? 54.522  140.721 52.420 1.00 30.41  ? 126 LEU H CA  1 
ATOM   8694  C  C   . LEU H  1 132 ? 53.671  141.823 51.826 1.00 34.92  ? 126 LEU H C   1 
ATOM   8695  O  O   . LEU H  1 132 ? 53.234  141.722 50.675 1.00 37.21  ? 126 LEU H O   1 
ATOM   8696  C  CB  . LEU H  1 132 ? 54.228  139.398 51.704 1.00 24.03  ? 126 LEU H CB  1 
ATOM   8697  C  CG  . LEU H  1 132 ? 54.853  138.149 52.350 1.00 28.45  ? 126 LEU H CG  1 
ATOM   8698  C  CD1 . LEU H  1 132 ? 54.721  136.978 51.412 1.00 31.12  ? 126 LEU H CD1 1 
ATOM   8699  C  CD2 . LEU H  1 132 ? 56.315  138.379 52.667 1.00 38.06  ? 126 LEU H CD2 1 
ATOM   8700  N  N   . GLY H  1 133 ? 53.459  142.877 52.616 1.00 36.63  ? 127 GLY H N   1 
ATOM   8701  C  CA  . GLY H  1 133 ? 52.687  144.027 52.169 1.00 31.42  ? 127 GLY H CA  1 
ATOM   8702  C  C   . GLY H  1 133 ? 51.190  143.817 52.121 1.00 30.82  ? 127 GLY H C   1 
ATOM   8703  O  O   . GLY H  1 133 ? 50.479  144.591 51.495 1.00 28.29  ? 127 GLY H O   1 
ATOM   8704  N  N   . LYS H  1 134 ? 50.705  142.774 52.778 1.00 32.08  ? 128 LYS H N   1 
ATOM   8705  C  CA  . LYS H  1 134 ? 49.272  142.487 52.789 1.00 34.89  ? 128 LYS H CA  1 
ATOM   8706  C  C   . LYS H  1 134 ? 48.654  142.829 54.143 1.00 33.72  ? 128 LYS H C   1 
ATOM   8707  O  O   . LYS H  1 134 ? 47.575  142.344 54.468 1.00 32.35  ? 128 LYS H O   1 
ATOM   8708  C  CB  . LYS H  1 134 ? 49.035  141.000 52.514 1.00 30.30  ? 128 LYS H CB  1 
ATOM   8709  C  CG  . LYS H  1 134 ? 49.606  140.476 51.210 1.00 36.17  ? 128 LYS H CG  1 
ATOM   8710  C  CD  . LYS H  1 134 ? 49.223  139.002 51.034 1.00 36.98  ? 128 LYS H CD  1 
ATOM   8711  C  CE  . LYS H  1 134 ? 49.600  138.495 49.659 1.00 46.47  ? 128 LYS H CE  1 
ATOM   8712  N  NZ  . LYS H  1 134 ? 49.311  137.043 49.480 1.00 53.13  ? 128 LYS H NZ  1 
ATOM   8713  N  N   . GLY H  1 135 ? 49.342  143.650 54.933 1.00 34.21  ? 129 GLY H N   1 
ATOM   8714  C  CA  . GLY H  1 135 ? 48.845  144.000 56.256 1.00 34.79  ? 129 GLY H CA  1 
ATOM   8715  C  C   . GLY H  1 135 ? 47.732  145.035 56.347 1.00 38.76  ? 129 GLY H C   1 
ATOM   8716  O  O   . GLY H  1 135 ? 47.122  145.193 57.409 1.00 36.43  ? 129 GLY H O   1 
ATOM   8717  N  N   . GLY H  1 136 ? 47.470  145.749 55.253 1.00 35.79  ? 130 GLY H N   1 
ATOM   8718  C  CA  . GLY H  1 136 ? 46.412  146.749 55.258 1.00 35.10  ? 130 GLY H CA  1 
ATOM   8719  C  C   . GLY H  1 136 ? 46.729  148.099 55.886 1.00 38.46  ? 130 GLY H C   1 
ATOM   8720  O  O   . GLY H  1 136 ? 45.827  148.925 56.049 1.00 32.76  ? 130 GLY H O   1 
ATOM   8721  N  N   . ASN H  1 137 ? 47.981  148.320 56.283 1.00 37.61  ? 131 ASN H N   1 
ATOM   8722  C  CA  . ASN H  1 137 ? 48.373  149.610 56.841 1.00 36.15  ? 131 ASN H CA  1 
ATOM   8723  C  C   . ASN H  1 137 ? 49.581  150.152 56.104 1.00 38.02  ? 131 ASN H C   1 
ATOM   8724  O  O   . ASN H  1 137 ? 50.135  149.497 55.219 1.00 43.97  ? 131 ASN H O   1 
ATOM   8725  C  CB  . ASN H  1 137 ? 48.645  149.564 58.365 1.00 35.11  ? 131 ASN H CB  1 
ATOM   8726  C  CG  . ASN H  1 137 ? 49.619  148.475 58.791 1.00 36.80  ? 131 ASN H CG  1 
ATOM   8727  O  OD1 . ASN H  1 137 ? 50.470  148.026 58.021 1.00 37.38  ? 131 ASN H OD1 1 
ATOM   8728  N  ND2 . ASN H  1 137 ? 49.510  148.064 60.052 1.00 35.07  ? 131 ASN H ND2 1 
ATOM   8729  N  N   . GLU H  1 138 ? 49.987  151.360 56.454 1.00 41.25  ? 132 GLU H N   1 
ATOM   8730  C  CA  . GLU H  1 138 ? 51.114  151.970 55.784 1.00 48.67  ? 132 GLU H CA  1 
ATOM   8731  C  C   . GLU H  1 138 ? 52.393  151.209 56.125 1.00 46.21  ? 132 GLU H C   1 
ATOM   8732  O  O   . GLU H  1 138 ? 53.267  151.010 55.270 1.00 42.40  ? 132 GLU H O   1 
ATOM   8733  C  CB  . GLU H  1 138 ? 51.206  153.443 56.184 1.00 60.19  ? 132 GLU H CB  1 
ATOM   8734  C  CG  . GLU H  1 138 ? 51.999  154.294 55.212 1.00 78.45  ? 132 GLU H CG  1 
ATOM   8735  C  CD  . GLU H  1 138 ? 51.653  155.759 55.329 1.00 88.98  ? 132 GLU H CD  1 
ATOM   8736  O  OE1 . GLU H  1 138 ? 50.561  156.147 54.855 1.00 93.35  ? 132 GLU H OE1 1 
ATOM   8737  O  OE2 . GLU H  1 138 ? 52.466  156.515 55.906 1.00 93.97  ? 132 GLU H OE2 1 
ATOM   8738  N  N   . GLU H  1 139 ? 52.473  150.766 57.377 1.00 39.94  ? 133 GLU H N   1 
ATOM   8739  C  CA  . GLU H  1 139 ? 53.610  150.004 57.872 1.00 37.56  ? 133 GLU H CA  1 
ATOM   8740  C  C   . GLU H  1 139 ? 53.853  148.770 56.994 1.00 37.00  ? 133 GLU H C   1 
ATOM   8741  O  O   . GLU H  1 139 ? 54.986  148.440 56.667 1.00 35.94  ? 133 GLU H O   1 
ATOM   8742  C  CB  . GLU H  1 139 ? 53.333  149.562 59.303 1.00 38.15  ? 133 GLU H CB  1 
ATOM   8743  C  CG  . GLU H  1 139 ? 54.556  149.118 60.054 1.00 45.97  ? 133 GLU H CG  1 
ATOM   8744  C  CD  . GLU H  1 139 ? 55.622  150.191 60.073 1.00 55.71  ? 133 GLU H CD  1 
ATOM   8745  O  OE1 . GLU H  1 139 ? 56.441  150.243 59.129 1.00 53.96  ? 133 GLU H OE1 1 
ATOM   8746  O  OE2 . GLU H  1 139 ? 55.628  150.996 61.028 1.00 63.44  ? 133 GLU H OE2 1 
ATOM   8747  N  N   . SER H  1 140 ? 52.775  148.092 56.618 1.00 35.91  ? 134 SER H N   1 
ATOM   8748  C  CA  . SER H  1 140 ? 52.849  146.905 55.782 1.00 32.52  ? 134 SER H CA  1 
ATOM   8749  C  C   . SER H  1 140 ? 53.524  147.203 54.446 1.00 35.64  ? 134 SER H C   1 
ATOM   8750  O  O   . SER H  1 140 ? 54.354  146.426 53.956 1.00 31.39  ? 134 SER H O   1 
ATOM   8751  C  CB  . SER H  1 140 ? 51.435  146.371 55.534 1.00 35.39  ? 134 SER H CB  1 
ATOM   8752  O  OG  . SER H  1 140 ? 51.426  145.247 54.670 1.00 23.18  ? 134 SER H OG  1 
ATOM   8753  N  N   . THR H  1 141 ? 53.181  148.339 53.857 1.00 35.25  ? 135 THR H N   1 
ATOM   8754  C  CA  . THR H  1 141 ? 53.744  148.679 52.565 1.00 38.77  ? 135 THR H CA  1 
ATOM   8755  C  C   . THR H  1 141 ? 55.082  149.374 52.627 1.00 34.96  ? 135 THR H C   1 
ATOM   8756  O  O   . THR H  1 141 ? 55.592  149.855 51.609 1.00 33.35  ? 135 THR H O   1 
ATOM   8757  C  CB  . THR H  1 141 ? 52.758  149.513 51.760 1.00 45.86  ? 135 THR H CB  1 
ATOM   8758  O  OG1 . THR H  1 141 ? 52.097  150.438 52.633 1.00 50.74  ? 135 THR H OG1 1 
ATOM   8759  C  CG2 . THR H  1 141 ? 51.737  148.590 51.093 1.00 41.20  ? 135 THR H CG2 1 
ATOM   8760  N  N   . LYS H  1 142 ? 55.648  149.418 53.830 1.00 34.53  ? 136 LYS H N   1 
ATOM   8761  C  CA  . LYS H  1 142 ? 56.960  150.017 54.042 1.00 37.16  ? 136 LYS H CA  1 
ATOM   8762  C  C   . LYS H  1 142 ? 57.968  148.962 54.520 1.00 34.83  ? 136 LYS H C   1 
ATOM   8763  O  O   . LYS H  1 142 ? 59.036  148.796 53.930 1.00 36.19  ? 136 LYS H O   1 
ATOM   8764  C  CB  . LYS H  1 142 ? 56.869  151.161 55.060 1.00 41.39  ? 136 LYS H CB  1 
ATOM   8765  C  CG  . LYS H  1 142 ? 56.267  152.439 54.484 1.00 58.31  ? 136 LYS H CG  1 
ATOM   8766  C  CD  . LYS H  1 142 ? 56.136  153.558 55.521 1.00 69.95  ? 136 LYS H CD  1 
ATOM   8767  C  CE  . LYS H  1 142 ? 57.490  154.096 55.980 1.00 77.89  ? 136 LYS H CE  1 
ATOM   8768  N  NZ  . LYS H  1 142 ? 57.346  155.254 56.919 1.00 78.79  ? 136 LYS H NZ  1 
ATOM   8769  N  N   . THR H  1 143 ? 57.602  148.229 55.563 1.00 24.53  ? 137 THR H N   1 
ATOM   8770  C  CA  . THR H  1 143 ? 58.478  147.222 56.143 1.00 26.50  ? 137 THR H CA  1 
ATOM   8771  C  C   . THR H  1 143 ? 57.810  145.867 56.249 1.00 28.57  ? 137 THR H C   1 
ATOM   8772  O  O   . THR H  1 143 ? 58.433  144.902 56.651 1.00 30.26  ? 137 THR H O   1 
ATOM   8773  C  CB  . THR H  1 143 ? 58.880  147.618 57.560 1.00 28.51  ? 137 THR H CB  1 
ATOM   8774  O  OG1 . THR H  1 143 ? 57.747  147.470 58.436 1.00 20.65  ? 137 THR H OG1 1 
ATOM   8775  C  CG2 . THR H  1 143 ? 59.359  149.075 57.592 1.00 15.71  ? 137 THR H CG2 1 
ATOM   8776  N  N   . GLY H  1 144 ? 56.531  145.803 55.908 1.00 30.32  ? 138 GLY H N   1 
ATOM   8777  C  CA  . GLY H  1 144 ? 55.803  144.554 56.007 1.00 23.43  ? 138 GLY H CA  1 
ATOM   8778  C  C   . GLY H  1 144 ? 55.545  144.166 57.459 1.00 30.50  ? 138 GLY H C   1 
ATOM   8779  O  O   . GLY H  1 144 ? 55.237  143.000 57.734 1.00 25.83  ? 138 GLY H O   1 
ATOM   8780  N  N   . ASN H  1 145 ? 55.673  145.122 58.386 1.00 28.67  ? 139 ASN H N   1 
ATOM   8781  C  CA  . ASN H  1 145 ? 55.453  144.857 59.819 1.00 31.47  ? 139 ASN H CA  1 
ATOM   8782  C  C   . ASN H  1 145 ? 56.361  143.737 60.348 1.00 29.77  ? 139 ASN H C   1 
ATOM   8783  O  O   . ASN H  1 145 ? 55.980  143.012 61.257 1.00 22.57  ? 139 ASN H O   1 
ATOM   8784  C  CB  . ASN H  1 145 ? 53.981  144.466 60.083 1.00 27.41  ? 139 ASN H CB  1 
ATOM   8785  C  CG  . ASN H  1 145 ? 53.004  145.622 59.832 1.00 36.96  ? 139 ASN H CG  1 
ATOM   8786  O  OD1 . ASN H  1 145 ? 53.143  146.691 60.411 1.00 39.19  ? 139 ASN H OD1 1 
ATOM   8787  N  ND2 . ASN H  1 145 ? 52.015  145.402 58.966 1.00 33.09  ? 139 ASN H ND2 1 
ATOM   8788  N  N   . ALA H  1 146 ? 57.558  143.610 59.781 1.00 34.10  ? 140 ALA H N   1 
ATOM   8789  C  CA  . ALA H  1 146 ? 58.505  142.563 60.165 1.00 34.08  ? 140 ALA H CA  1 
ATOM   8790  C  C   . ALA H  1 146 ? 59.174  142.773 61.524 1.00 36.43  ? 140 ALA H C   1 
ATOM   8791  O  O   . ALA H  1 146 ? 59.855  141.876 62.039 1.00 29.75  ? 140 ALA H O   1 
ATOM   8792  C  CB  . ALA H  1 146 ? 59.566  142.415 59.084 1.00 36.36  ? 140 ALA H CB  1 
ATOM   8793  N  N   . GLY H  1 147 ? 59.010  143.959 62.094 1.00 30.60  ? 141 GLY H N   1 
ATOM   8794  C  CA  . GLY H  1 147 ? 59.584  144.206 63.404 1.00 32.63  ? 141 GLY H CA  1 
ATOM   8795  C  C   . GLY H  1 147 ? 61.037  144.610 63.406 1.00 33.43  ? 141 GLY H C   1 
ATOM   8796  O  O   . GLY H  1 147 ? 61.603  144.935 62.361 1.00 34.34  ? 141 GLY H O   1 
ATOM   8797  N  N   . SER H  1 148 ? 61.644  144.556 64.588 1.00 32.66  ? 142 SER H N   1 
ATOM   8798  C  CA  . SER H  1 148 ? 63.043  144.954 64.770 1.00 32.78  ? 142 SER H CA  1 
ATOM   8799  C  C   . SER H  1 148 ? 64.088  144.148 63.993 1.00 27.98  ? 142 SER H C   1 
ATOM   8800  O  O   . SER H  1 148 ? 63.815  143.080 63.442 1.00 27.37  ? 142 SER H O   1 
ATOM   8801  C  CB  . SER H  1 148 ? 63.399  144.953 66.259 1.00 29.23  ? 142 SER H CB  1 
ATOM   8802  O  OG  . SER H  1 148 ? 63.417  143.638 66.767 1.00 36.50  ? 142 SER H OG  1 
ATOM   8803  N  N   . ARG H  1 149 ? 65.296  144.684 63.974 1.00 22.88  ? 143 ARG H N   1 
ATOM   8804  C  CA  . ARG H  1 149 ? 66.405  144.095 63.254 1.00 26.70  ? 143 ARG H CA  1 
ATOM   8805  C  C   . ARG H  1 149 ? 67.231  143.249 64.200 1.00 28.69  ? 143 ARG H C   1 
ATOM   8806  O  O   . ARG H  1 149 ? 67.950  143.789 65.030 1.00 32.92  ? 143 ARG H O   1 
ATOM   8807  C  CB  . ARG H  1 149 ? 67.227  145.236 62.654 1.00 25.01  ? 143 ARG H CB  1 
ATOM   8808  C  CG  . ARG H  1 149 ? 66.337  146.183 61.863 1.00 26.73  ? 143 ARG H CG  1 
ATOM   8809  C  CD  . ARG H  1 149 ? 67.043  147.410 61.298 1.00 29.33  ? 143 ARG H CD  1 
ATOM   8810  N  NE  . ARG H  1 149 ? 66.077  148.233 60.570 1.00 28.35  ? 143 ARG H NE  1 
ATOM   8811  C  CZ  . ARG H  1 149 ? 66.395  149.258 59.788 1.00 33.50  ? 143 ARG H CZ  1 
ATOM   8812  N  NH1 . ARG H  1 149 ? 65.439  149.939 59.165 1.00 26.88  ? 143 ARG H NH1 1 
ATOM   8813  N  NH2 . ARG H  1 149 ? 67.664  149.605 59.628 1.00 30.96  ? 143 ARG H NH2 1 
ATOM   8814  N  N   . LEU H  1 150 ? 67.124  141.925 64.083 1.00 29.70  ? 144 LEU H N   1 
ATOM   8815  C  CA  . LEU H  1 150 ? 67.855  141.037 64.978 1.00 29.42  ? 144 LEU H CA  1 
ATOM   8816  C  C   . LEU H  1 150 ? 69.335  140.939 64.652 1.00 32.12  ? 144 LEU H C   1 
ATOM   8817  O  O   . LEU H  1 150 ? 70.173  140.980 65.550 1.00 33.94  ? 144 LEU H O   1 
ATOM   8818  C  CB  . LEU H  1 150 ? 67.250  139.636 64.974 1.00 33.46  ? 144 LEU H CB  1 
ATOM   8819  C  CG  . LEU H  1 150 ? 65.760  139.467 65.293 1.00 33.19  ? 144 LEU H CG  1 
ATOM   8820  C  CD1 . LEU H  1 150 ? 65.477  137.973 65.475 1.00 33.91  ? 144 LEU H CD1 1 
ATOM   8821  C  CD2 . LEU H  1 150 ? 65.387  140.215 66.555 1.00 25.67  ? 144 LEU H CD2 1 
ATOM   8822  N  N   . ALA H  1 151 ? 69.660  140.789 63.374 1.00 26.84  ? 145 ALA H N   1 
ATOM   8823  C  CA  . ALA H  1 151 ? 71.055  140.693 62.972 1.00 28.23  ? 145 ALA H CA  1 
ATOM   8824  C  C   . ALA H  1 151 ? 71.230  141.235 61.568 1.00 28.95  ? 145 ALA H C   1 
ATOM   8825  O  O   . ALA H  1 151 ? 70.288  141.261 60.769 1.00 33.66  ? 145 ALA H O   1 
ATOM   8826  C  CB  . ALA H  1 151 ? 71.536  139.235 63.041 1.00 16.33  ? 145 ALA H CB  1 
ATOM   8827  N  N   . CYS H  1 152 ? 72.443  141.665 61.263 1.00 23.22  ? 146 CYS H N   1 
ATOM   8828  C  CA  . CYS H  1 152 ? 72.717  142.206 59.953 1.00 31.40  ? 146 CYS H CA  1 
ATOM   8829  C  C   . CYS H  1 152 ? 74.178  142.045 59.627 1.00 31.10  ? 146 CYS H C   1 
ATOM   8830  O  O   . CYS H  1 152 ? 74.953  141.549 60.436 1.00 31.25  ? 146 CYS H O   1 
ATOM   8831  C  CB  . CYS H  1 152 ? 72.341  143.688 59.894 1.00 35.27  ? 146 CYS H CB  1 
ATOM   8832  S  SG  . CYS H  1 152 ? 73.144  144.709 61.167 1.00 35.13  ? 146 CYS H SG  1 
ATOM   8833  N  N   . GLY H  1 153 ? 74.534  142.460 58.421 1.00 31.39  ? 147 GLY H N   1 
ATOM   8834  C  CA  . GLY H  1 153 ? 75.902  142.370 57.968 1.00 31.64  ? 147 GLY H CA  1 
ATOM   8835  C  C   . GLY H  1 153 ? 75.997  143.071 56.634 1.00 34.76  ? 147 GLY H C   1 
ATOM   8836  O  O   . GLY H  1 153 ? 75.004  143.220 55.915 1.00 33.00  ? 147 GLY H O   1 
ATOM   8837  N  N   . VAL H  1 154 ? 77.191  143.524 56.300 1.00 30.61  ? 148 VAL H N   1 
ATOM   8838  C  CA  . VAL H  1 154 ? 77.380  144.194 55.035 1.00 33.72  ? 148 VAL H CA  1 
ATOM   8839  C  C   . VAL H  1 154 ? 77.658  143.125 53.989 1.00 37.03  ? 148 VAL H C   1 
ATOM   8840  O  O   . VAL H  1 154 ? 78.399  142.179 54.248 1.00 30.67  ? 148 VAL H O   1 
ATOM   8841  C  CB  . VAL H  1 154 ? 78.559  145.172 55.102 1.00 29.29  ? 148 VAL H CB  1 
ATOM   8842  C  CG1 . VAL H  1 154 ? 78.711  145.903 53.772 1.00 32.84  ? 148 VAL H CG1 1 
ATOM   8843  C  CG2 . VAL H  1 154 ? 78.330  146.150 56.235 1.00 24.75  ? 148 VAL H CG2 1 
ATOM   8844  N  N   . ILE H  1 155 ? 77.043  143.273 52.817 1.00 39.83  ? 149 ILE H N   1 
ATOM   8845  C  CA  . ILE H  1 155 ? 77.225  142.323 51.724 1.00 35.80  ? 149 ILE H CA  1 
ATOM   8846  C  C   . ILE H  1 155 ? 78.529  142.627 50.991 1.00 34.97  ? 149 ILE H C   1 
ATOM   8847  O  O   . ILE H  1 155 ? 78.729  143.742 50.520 1.00 35.62  ? 149 ILE H O   1 
ATOM   8848  C  CB  . ILE H  1 155 ? 76.046  142.405 50.746 1.00 35.59  ? 149 ILE H CB  1 
ATOM   8849  C  CG1 . ILE H  1 155 ? 74.743  142.114 51.505 1.00 33.29  ? 149 ILE H CG1 1 
ATOM   8850  C  CG2 . ILE H  1 155 ? 76.248  141.429 49.607 1.00 26.93  ? 149 ILE H CG2 1 
ATOM   8851  C  CD1 . ILE H  1 155 ? 73.500  142.097 50.639 1.00 26.32  ? 149 ILE H CD1 1 
ATOM   8852  N  N   . GLY H  1 156 ? 79.417  141.639 50.907 1.00 29.15  ? 150 GLY H N   1 
ATOM   8853  C  CA  . GLY H  1 156 ? 80.693  141.850 50.241 1.00 29.55  ? 150 GLY H CA  1 
ATOM   8854  C  C   . GLY H  1 156 ? 81.022  140.874 49.125 1.00 28.47  ? 150 GLY H C   1 
ATOM   8855  O  O   . GLY H  1 156 ? 80.475  139.772 49.072 1.00 33.61  ? 150 GLY H O   1 
ATOM   8856  N  N   . ILE H  1 157 ? 81.923  141.278 48.232 1.00 29.99  ? 151 ILE H N   1 
ATOM   8857  C  CA  . ILE H  1 157 ? 82.329  140.446 47.101 1.00 38.08  ? 151 ILE H CA  1 
ATOM   8858  C  C   . ILE H  1 157 ? 83.122  139.239 47.573 1.00 40.26  ? 151 ILE H C   1 
ATOM   8859  O  O   . ILE H  1 157 ? 83.984  139.360 48.442 1.00 43.91  ? 151 ILE H O   1 
ATOM   8860  C  CB  . ILE H  1 157 ? 83.201  141.237 46.116 1.00 43.93  ? 151 ILE H CB  1 
ATOM   8861  C  CG1 . ILE H  1 157 ? 82.450  142.485 45.660 1.00 52.36  ? 151 ILE H CG1 1 
ATOM   8862  C  CG2 . ILE H  1 157 ? 83.561  140.365 44.917 1.00 48.84  ? 151 ILE H CG2 1 
ATOM   8863  C  CD1 . ILE H  1 157 ? 83.259  143.406 44.778 1.00 57.04  ? 151 ILE H CD1 1 
ATOM   8864  N  N   . ALA H  1 158 ? 82.851  138.074 46.996 1.00 43.34  ? 152 ALA H N   1 
ATOM   8865  C  CA  . ALA H  1 158 ? 83.566  136.875 47.411 1.00 49.37  ? 152 ALA H CA  1 
ATOM   8866  C  C   . ALA H  1 158 ? 84.173  136.041 46.280 1.00 52.72  ? 152 ALA H C   1 
ATOM   8867  O  O   . ALA H  1 158 ? 85.152  135.328 46.505 1.00 52.10  ? 152 ALA H O   1 
ATOM   8868  C  CB  . ALA H  1 158 ? 82.647  136.011 48.259 1.00 37.88  ? 152 ALA H CB  1 
ATOM   8869  N  N   . GLN H  1 159 ? 83.602  136.142 45.078 1.00 62.82  ? 153 GLN H N   1 
ATOM   8870  C  CA  . GLN H  1 159 ? 84.044  135.372 43.903 1.00 75.94  ? 153 GLN H CA  1 
ATOM   8871  C  C   . GLN H  1 159 ? 85.045  134.258 44.215 1.00 78.95  ? 153 GLN H C   1 
ATOM   8872  O  O   . GLN H  1 159 ? 86.203  134.342 43.748 1.00 81.01  ? 153 GLN H O   1 
ATOM   8873  C  CB  . GLN H  1 159 ? 84.636  136.293 42.837 1.00 83.18  ? 153 GLN H CB  1 
ATOM   8874  C  CG  . GLN H  1 159 ? 83.704  137.376 42.353 1.00 98.00  ? 153 GLN H CG  1 
ATOM   8875  C  CD  . GLN H  1 159 ? 84.362  138.255 41.313 1.00 110.85 ? 153 GLN H CD  1 
ATOM   8876  O  OE1 . GLN H  1 159 ? 83.943  139.391 41.087 1.00 118.72 ? 153 GLN H OE1 1 
ATOM   8877  N  NE2 . GLN H  1 159 ? 85.399  137.730 40.665 1.00 114.84 ? 153 GLN H NE2 1 
ATOM   8878  O  OXT . GLN H  1 159 ? 84.656  133.310 44.930 1.00 82.10  ? 153 GLN H OXT 1 
ATOM   8879  N  N   . ALA I  1 7   ? 58.014  94.973  37.429 1.00 95.59  ? 1   ALA I N   1 
ATOM   8880  C  CA  . ALA I  1 7   ? 58.382  96.391  37.706 1.00 87.94  ? 1   ALA I CA  1 
ATOM   8881  C  C   . ALA I  1 7   ? 57.513  96.977  38.816 1.00 81.55  ? 1   ALA I C   1 
ATOM   8882  O  O   . ALA I  1 7   ? 58.008  97.295  39.898 1.00 82.79  ? 1   ALA I O   1 
ATOM   8883  C  CB  . ALA I  1 7   ? 58.246  97.231  36.427 1.00 89.20  ? 1   ALA I CB  1 
ATOM   8884  N  N   . THR I  1 8   ? 56.217  97.109  38.556 1.00 71.09  ? 2   THR I N   1 
ATOM   8885  C  CA  . THR I  1 8   ? 55.326  97.682  39.551 1.00 63.84  ? 2   THR I CA  1 
ATOM   8886  C  C   . THR I  1 8   ? 55.100  96.775  40.767 1.00 59.26  ? 2   THR I C   1 
ATOM   8887  O  O   . THR I  1 8   ? 55.067  95.546  40.671 1.00 51.15  ? 2   THR I O   1 
ATOM   8888  C  CB  . THR I  1 8   ? 53.965  98.073  38.922 1.00 60.13  ? 2   THR I CB  1 
ATOM   8889  O  OG1 . THR I  1 8   ? 53.301  96.904  38.452 1.00 59.66  ? 2   THR I OG1 1 
ATOM   8890  C  CG2 . THR I  1 8   ? 54.169  99.012  37.743 1.00 63.78  ? 2   THR I CG2 1 
ATOM   8891  N  N   . LYS I  1 9   ? 54.979  97.407  41.926 1.00 54.56  ? 3   LYS I N   1 
ATOM   8892  C  CA  . LYS I  1 9   ? 54.749  96.700  43.171 1.00 51.00  ? 3   LYS I CA  1 
ATOM   8893  C  C   . LYS I  1 9   ? 53.582  97.367  43.864 1.00 49.26  ? 3   LYS I C   1 
ATOM   8894  O  O   . LYS I  1 9   ? 53.361  98.567  43.711 1.00 51.96  ? 3   LYS I O   1 
ATOM   8895  C  CB  . LYS I  1 9   ? 55.975  96.772  44.079 1.00 51.80  ? 3   LYS I CB  1 
ATOM   8896  C  CG  . LYS I  1 9   ? 57.257  96.297  43.430 1.00 64.42  ? 3   LYS I CG  1 
ATOM   8897  C  CD  . LYS I  1 9   ? 58.345  96.033  44.465 1.00 72.17  ? 3   LYS I CD  1 
ATOM   8898  C  CE  . LYS I  1 9   ? 59.629  95.556  43.799 1.00 79.75  ? 3   LYS I CE  1 
ATOM   8899  N  NZ  . LYS I  1 9   ? 60.677  95.172  44.783 1.00 84.87  ? 3   LYS I NZ  1 
ATOM   8900  N  N   . ALA I  1 10  ? 52.835  96.582  44.627 1.00 46.74  ? 4   ALA I N   1 
ATOM   8901  C  CA  . ALA I  1 10  ? 51.689  97.089  45.353 1.00 42.29  ? 4   ALA I CA  1 
ATOM   8902  C  C   . ALA I  1 10  ? 51.717  96.483  46.747 1.00 40.31  ? 4   ALA I C   1 
ATOM   8903  O  O   . ALA I  1 10  ? 52.411  95.506  46.980 1.00 43.28  ? 4   ALA I O   1 
ATOM   8904  C  CB  . ALA I  1 10  ? 50.411  96.706  44.626 1.00 42.57  ? 4   ALA I CB  1 
ATOM   8905  N  N   . VAL I  1 11  ? 50.982  97.072  47.679 1.00 38.36  ? 5   VAL I N   1 
ATOM   8906  C  CA  . VAL I  1 11  ? 50.938  96.546  49.033 1.00 36.40  ? 5   VAL I CA  1 
ATOM   8907  C  C   . VAL I  1 11  ? 49.576  96.858  49.628 1.00 35.19  ? 5   VAL I C   1 
ATOM   8908  O  O   . VAL I  1 11  ? 48.902  97.783  49.194 1.00 36.66  ? 5   VAL I O   1 
ATOM   8909  C  CB  . VAL I  1 11  ? 52.065  97.148  49.931 1.00 39.27  ? 5   VAL I CB  1 
ATOM   8910  C  CG1 . VAL I  1 11  ? 51.842  98.636  50.144 1.00 40.26  ? 5   VAL I CG1 1 
ATOM   8911  C  CG2 . VAL I  1 11  ? 52.114  96.414  51.268 1.00 35.50  ? 5   VAL I CG2 1 
ATOM   8912  N  N   . CYS I  1 12  ? 49.168  96.073  50.615 1.00 37.88  ? 6   CYS I N   1 
ATOM   8913  C  CA  . CYS I  1 12  ? 47.874  96.261  51.244 1.00 36.59  ? 6   CYS I CA  1 
ATOM   8914  C  C   . CYS I  1 12  ? 47.953  95.885  52.702 1.00 34.85  ? 6   CYS I C   1 
ATOM   8915  O  O   . CYS I  1 12  ? 48.527  94.858  53.047 1.00 37.38  ? 6   CYS I O   1 
ATOM   8916  C  CB  . CYS I  1 12  ? 46.822  95.386  50.550 1.00 40.30  ? 6   CYS I CB  1 
ATOM   8917  S  SG  . CYS I  1 12  ? 45.169  95.397  51.311 1.00 48.46  ? 6   CYS I SG  1 
ATOM   8918  N  N   . VAL I  1 13  ? 47.392  96.723  53.563 1.00 32.90  ? 7   VAL I N   1 
ATOM   8919  C  CA  . VAL I  1 13  ? 47.389  96.420  54.984 1.00 32.06  ? 7   VAL I CA  1 
ATOM   8920  C  C   . VAL I  1 13  ? 45.975  95.983  55.324 1.00 38.53  ? 7   VAL I C   1 
ATOM   8921  O  O   . VAL I  1 13  ? 45.012  96.725  55.110 1.00 44.46  ? 7   VAL I O   1 
ATOM   8922  C  CB  . VAL I  1 13  ? 47.768  97.642  55.817 1.00 32.40  ? 7   VAL I CB  1 
ATOM   8923  C  CG1 . VAL I  1 13  ? 47.752  97.294  57.300 1.00 18.18  ? 7   VAL I CG1 1 
ATOM   8924  C  CG2 . VAL I  1 13  ? 49.142  98.134  55.403 1.00 24.70  ? 7   VAL I CG2 1 
ATOM   8925  N  N   . LEU I  1 14  ? 45.848  94.762  55.823 1.00 39.12  ? 8   LEU I N   1 
ATOM   8926  C  CA  . LEU I  1 14  ? 44.546  94.222  56.177 1.00 35.45  ? 8   LEU I CA  1 
ATOM   8927  C  C   . LEU I  1 14  ? 44.233  94.459  57.645 1.00 38.72  ? 8   LEU I C   1 
ATOM   8928  O  O   . LEU I  1 14  ? 45.049  94.181  58.536 1.00 28.88  ? 8   LEU I O   1 
ATOM   8929  C  CB  . LEU I  1 14  ? 44.491  92.717  55.891 1.00 40.90  ? 8   LEU I CB  1 
ATOM   8930  C  CG  . LEU I  1 14  ? 44.650  92.230  54.448 1.00 40.46  ? 8   LEU I CG  1 
ATOM   8931  C  CD1 . LEU I  1 14  ? 44.571  90.718  54.411 1.00 42.88  ? 8   LEU I CD1 1 
ATOM   8932  C  CD2 . LEU I  1 14  ? 43.564  92.815  53.586 1.00 40.68  ? 8   LEU I CD2 1 
ATOM   8933  N  N   . LYS I  1 15  ? 43.041  94.980  57.886 1.00 41.44  ? 9   LYS I N   1 
ATOM   8934  C  CA  . LYS I  1 15  ? 42.575  95.228  59.240 1.00 53.16  ? 9   LYS I CA  1 
ATOM   8935  C  C   . LYS I  1 15  ? 41.082  94.991  59.253 1.00 53.03  ? 9   LYS I C   1 
ATOM   8936  O  O   . LYS I  1 15  ? 40.453  94.923  58.197 1.00 51.89  ? 9   LYS I O   1 
ATOM   8937  C  CB  . LYS I  1 15  ? 42.891  96.661  59.677 1.00 53.97  ? 9   LYS I CB  1 
ATOM   8938  C  CG  . LYS I  1 15  ? 44.283  96.815  60.252 1.00 67.34  ? 9   LYS I CG  1 
ATOM   8939  C  CD  . LYS I  1 15  ? 44.587  98.251  60.645 1.00 74.90  ? 9   LYS I CD  1 
ATOM   8940  C  CE  . LYS I  1 15  ? 45.791  98.311  61.575 1.00 80.57  ? 9   LYS I CE  1 
ATOM   8941  N  NZ  . LYS I  1 15  ? 46.924  97.495  61.054 1.00 85.01  ? 9   LYS I NZ  1 
ATOM   8942  N  N   . GLY I  1 16  ? 40.526  94.840  60.448 1.00 58.73  ? 10  GLY I N   1 
ATOM   8943  C  CA  . GLY I  1 16  ? 39.099  94.622  60.586 1.00 63.51  ? 10  GLY I CA  1 
ATOM   8944  C  C   . GLY I  1 16  ? 38.684  94.894  62.018 1.00 68.41  ? 10  GLY I C   1 
ATOM   8945  O  O   . GLY I  1 16  ? 39.442  95.492  62.783 1.00 67.16  ? 10  GLY I O   1 
ATOM   8946  N  N   . ASP I  1 17  ? 37.488  94.452  62.394 1.00 72.38  ? 11  ASP I N   1 
ATOM   8947  C  CA  . ASP I  1 17  ? 37.008  94.665  63.754 1.00 72.07  ? 11  ASP I CA  1 
ATOM   8948  C  C   . ASP I  1 17  ? 37.538  93.621  64.724 1.00 69.33  ? 11  ASP I C   1 
ATOM   8949  O  O   . ASP I  1 17  ? 37.645  93.879  65.922 1.00 70.69  ? 11  ASP I O   1 
ATOM   8950  C  CB  . ASP I  1 17  ? 35.480  94.688  63.777 1.00 71.92  ? 11  ASP I CB  1 
ATOM   8951  C  CG  . ASP I  1 17  ? 34.922  96.041  63.380 1.00 75.83  ? 11  ASP I CG  1 
ATOM   8952  O  OD1 . ASP I  1 17  ? 35.144  97.010  64.141 1.00 75.94  ? 11  ASP I OD1 1 
ATOM   8953  O  OD2 . ASP I  1 17  ? 34.276  96.138  62.311 1.00 71.95  ? 11  ASP I OD2 1 
ATOM   8954  N  N   . GLY I  1 18  ? 37.881  92.448  64.201 1.00 65.01  ? 12  GLY I N   1 
ATOM   8955  C  CA  . GLY I  1 18  ? 38.408  91.393  65.044 1.00 60.93  ? 12  GLY I CA  1 
ATOM   8956  C  C   . GLY I  1 18  ? 39.914  91.508  65.178 1.00 59.44  ? 12  GLY I C   1 
ATOM   8957  O  O   . GLY I  1 18  ? 40.483  92.558  64.861 1.00 56.60  ? 12  GLY I O   1 
ATOM   8958  N  N   . PRO I  1 19  ? 40.594  90.444  65.642 1.00 54.24  ? 13  PRO I N   1 
ATOM   8959  C  CA  . PRO I  1 19  ? 42.049  90.441  65.812 1.00 53.52  ? 13  PRO I CA  1 
ATOM   8960  C  C   . PRO I  1 19  ? 42.833  90.149  64.510 1.00 51.09  ? 13  PRO I C   1 
ATOM   8961  O  O   . PRO I  1 19  ? 44.064  90.105  64.523 1.00 46.20  ? 13  PRO I O   1 
ATOM   8962  C  CB  . PRO I  1 19  ? 42.250  89.365  66.870 1.00 52.50  ? 13  PRO I CB  1 
ATOM   8963  C  CG  . PRO I  1 19  ? 41.235  88.347  66.468 1.00 45.79  ? 13  PRO I CG  1 
ATOM   8964  C  CD  . PRO I  1 19  ? 40.009  89.192  66.158 1.00 52.44  ? 13  PRO I CD  1 
ATOM   8965  N  N   . VAL I  1 20  ? 42.116  89.960  63.400 1.00 41.91  ? 14  VAL I N   1 
ATOM   8966  C  CA  . VAL I  1 20  ? 42.738  89.680  62.108 1.00 44.29  ? 14  VAL I CA  1 
ATOM   8967  C  C   . VAL I  1 20  ? 43.435  90.890  61.494 1.00 46.46  ? 14  VAL I C   1 
ATOM   8968  O  O   . VAL I  1 20  ? 42.807  91.913  61.230 1.00 52.22  ? 14  VAL I O   1 
ATOM   8969  C  CB  . VAL I  1 20  ? 41.705  89.189  61.079 1.00 40.84  ? 14  VAL I CB  1 
ATOM   8970  C  CG1 . VAL I  1 20  ? 42.395  88.912  59.760 1.00 28.45  ? 14  VAL I CG1 1 
ATOM   8971  C  CG2 . VAL I  1 20  ? 40.998  87.952  61.596 1.00 38.94  ? 14  VAL I CG2 1 
ATOM   8972  N  N   . GLN I  1 21  ? 44.733  90.761  61.246 1.00 49.33  ? 15  GLN I N   1 
ATOM   8973  C  CA  . GLN I  1 21  ? 45.514  91.842  60.653 1.00 51.98  ? 15  GLN I CA  1 
ATOM   8974  C  C   . GLN I  1 21  ? 46.721  91.275  59.909 1.00 48.90  ? 15  GLN I C   1 
ATOM   8975  O  O   . GLN I  1 21  ? 47.269  90.244  60.302 1.00 47.89  ? 15  GLN I O   1 
ATOM   8976  C  CB  . GLN I  1 21  ? 45.990  92.785  61.743 1.00 47.70  ? 15  GLN I CB  1 
ATOM   8977  C  CG  . GLN I  1 21  ? 46.753  92.075  62.826 1.00 62.82  ? 15  GLN I CG  1 
ATOM   8978  C  CD  . GLN I  1 21  ? 47.111  92.994  63.968 1.00 71.65  ? 15  GLN I CD  1 
ATOM   8979  O  OE1 . GLN I  1 21  ? 47.854  93.956  63.788 1.00 77.64  ? 15  GLN I OE1 1 
ATOM   8980  N  NE2 . GLN I  1 21  ? 46.578  92.707  65.153 1.00 69.91  ? 15  GLN I NE2 1 
ATOM   8981  N  N   . GLY I  1 22  ? 47.134  91.945  58.837 1.00 46.18  ? 16  GLY I N   1 
ATOM   8982  C  CA  . GLY I  1 22  ? 48.277  91.465  58.081 1.00 39.09  ? 16  GLY I CA  1 
ATOM   8983  C  C   . GLY I  1 22  ? 48.707  92.368  56.940 1.00 37.40  ? 16  GLY I C   1 
ATOM   8984  O  O   . GLY I  1 22  ? 48.076  93.380  56.658 1.00 38.54  ? 16  GLY I O   1 
ATOM   8985  N  N   . ILE I  1 23  ? 49.788  91.983  56.275 1.00 38.03  ? 17  ILE I N   1 
ATOM   8986  C  CA  . ILE I  1 23  ? 50.327  92.741  55.155 1.00 31.84  ? 17  ILE I CA  1 
ATOM   8987  C  C   . ILE I  1 23  ? 50.486  91.826  53.954 1.00 35.66  ? 17  ILE I C   1 
ATOM   8988  O  O   . ILE I  1 23  ? 51.124  90.767  54.034 1.00 30.82  ? 17  ILE I O   1 
ATOM   8989  C  CB  . ILE I  1 23  ? 51.719  93.334  55.499 1.00 29.31  ? 17  ILE I CB  1 
ATOM   8990  C  CG1 . ILE I  1 23  ? 51.607  94.253  56.716 1.00 27.21  ? 17  ILE I CG1 1 
ATOM   8991  C  CG2 . ILE I  1 23  ? 52.299  94.044  54.289 1.00 27.64  ? 17  ILE I CG2 1 
ATOM   8992  C  CD1 . ILE I  1 23  ? 52.867  95.030  57.029 1.00 26.56  ? 17  ILE I CD1 1 
ATOM   8993  N  N   . ILE I  1 24  ? 49.911  92.228  52.833 1.00 27.77  ? 18  ILE I N   1 
ATOM   8994  C  CA  . ILE I  1 24  ? 50.031  91.423  51.644 1.00 30.85  ? 18  ILE I CA  1 
ATOM   8995  C  C   . ILE I  1 24  ? 50.727  92.231  50.565 1.00 37.97  ? 18  ILE I C   1 
ATOM   8996  O  O   . ILE I  1 24  ? 50.374  93.386  50.311 1.00 35.73  ? 18  ILE I O   1 
ATOM   8997  C  CB  . ILE I  1 24  ? 48.659  90.966  51.140 1.00 30.52  ? 18  ILE I CB  1 
ATOM   8998  C  CG1 . ILE I  1 24  ? 48.023  89.996  52.148 1.00 28.83  ? 18  ILE I CG1 1 
ATOM   8999  C  CG2 . ILE I  1 24  ? 48.804  90.364  49.755 1.00 27.56  ? 18  ILE I CG2 1 
ATOM   9000  C  CD1 . ILE I  1 24  ? 48.683  88.613  52.237 1.00 29.88  ? 18  ILE I CD1 1 
ATOM   9001  N  N   . ASN I  1 25  ? 51.721  91.611  49.937 1.00 37.85  ? 19  ASN I N   1 
ATOM   9002  C  CA  . ASN I  1 25  ? 52.501  92.246  48.888 1.00 33.61  ? 19  ASN I CA  1 
ATOM   9003  C  C   . ASN I  1 25  ? 52.142  91.761  47.505 1.00 37.61  ? 19  ASN I C   1 
ATOM   9004  O  O   . ASN I  1 25  ? 51.646  90.650  47.330 1.00 38.05  ? 19  ASN I O   1 
ATOM   9005  C  CB  . ASN I  1 25  ? 53.978  92.001  49.126 1.00 31.35  ? 19  ASN I CB  1 
ATOM   9006  C  CG  . ASN I  1 25  ? 54.482  92.725  50.332 1.00 39.24  ? 19  ASN I CG  1 
ATOM   9007  O  OD1 . ASN I  1 25  ? 54.613  93.953  50.321 1.00 47.84  ? 19  ASN I OD1 1 
ATOM   9008  N  ND2 . ASN I  1 25  ? 54.756  91.982  51.394 1.00 38.69  ? 19  ASN I ND2 1 
ATOM   9009  N  N   . PHE I  1 26  ? 52.410  92.612  46.521 1.00 39.98  ? 20  PHE I N   1 
ATOM   9010  C  CA  . PHE I  1 26  ? 52.133  92.305  45.128 1.00 42.82  ? 20  PHE I CA  1 
ATOM   9011  C  C   . PHE I  1 26  ? 53.331  92.713  44.293 1.00 45.17  ? 20  PHE I C   1 
ATOM   9012  O  O   . PHE I  1 26  ? 53.928  93.762  44.520 1.00 48.80  ? 20  PHE I O   1 
ATOM   9013  C  CB  . PHE I  1 26  ? 50.904  93.077  44.647 1.00 34.74  ? 20  PHE I CB  1 
ATOM   9014  C  CG  . PHE I  1 26  ? 49.648  92.738  45.391 1.00 36.69  ? 20  PHE I CG  1 
ATOM   9015  C  CD1 . PHE I  1 26  ? 48.733  91.836  44.861 1.00 32.06  ? 20  PHE I CD1 1 
ATOM   9016  C  CD2 . PHE I  1 26  ? 49.380  93.319  46.630 1.00 28.69  ? 20  PHE I CD2 1 
ATOM   9017  C  CE1 . PHE I  1 26  ? 47.563  91.516  45.554 1.00 35.91  ? 20  PHE I CE1 1 
ATOM   9018  C  CE2 . PHE I  1 26  ? 48.215  93.007  47.330 1.00 32.37  ? 20  PHE I CE2 1 
ATOM   9019  C  CZ  . PHE I  1 26  ? 47.304  92.103  46.788 1.00 37.15  ? 20  PHE I CZ  1 
ATOM   9020  N  N   . GLU I  1 27  ? 53.688  91.879  43.332 1.00 45.06  ? 21  GLU I N   1 
ATOM   9021  C  CA  . GLU I  1 27  ? 54.802  92.187  42.461 1.00 45.46  ? 21  GLU I CA  1 
ATOM   9022  C  C   . GLU I  1 27  ? 54.482  91.652  41.083 1.00 46.77  ? 21  GLU I C   1 
ATOM   9023  O  O   . GLU I  1 27  ? 53.857  90.605  40.938 1.00 46.53  ? 21  GLU I O   1 
ATOM   9024  C  CB  . GLU I  1 27  ? 56.081  91.569  42.996 1.00 44.93  ? 21  GLU I CB  1 
ATOM   9025  C  CG  . GLU I  1 27  ? 57.271  91.789  42.098 1.00 64.77  ? 21  GLU I CG  1 
ATOM   9026  C  CD  . GLU I  1 27  ? 58.569  91.457  42.793 1.00 72.50  ? 21  GLU I CD  1 
ATOM   9027  O  OE1 . GLU I  1 27  ? 58.962  92.232  43.690 1.00 76.61  ? 21  GLU I OE1 1 
ATOM   9028  O  OE2 . GLU I  1 27  ? 59.186  90.424  42.454 1.00 75.38  ? 21  GLU I OE2 1 
ATOM   9029  N  N   . GLN I  1 28  ? 54.892  92.386  40.065 1.00 48.83  ? 22  GLN I N   1 
ATOM   9030  C  CA  . GLN I  1 28  ? 54.621  91.975  38.704 1.00 58.46  ? 22  GLN I CA  1 
ATOM   9031  C  C   . GLN I  1 28  ? 55.709  92.524  37.795 1.00 62.68  ? 22  GLN I C   1 
ATOM   9032  O  O   . GLN I  1 28  ? 55.739  93.714  37.513 1.00 62.32  ? 22  GLN I O   1 
ATOM   9033  C  CB  . GLN I  1 28  ? 53.247  92.498  38.286 1.00 55.52  ? 22  GLN I CB  1 
ATOM   9034  C  CG  . GLN I  1 28  ? 52.915  92.297  36.822 1.00 58.68  ? 22  GLN I CG  1 
ATOM   9035  C  CD  . GLN I  1 28  ? 51.549  92.853  36.459 1.00 57.08  ? 22  GLN I CD  1 
ATOM   9036  O  OE1 . GLN I  1 28  ? 51.181  93.946  36.890 1.00 59.88  ? 22  GLN I OE1 1 
ATOM   9037  N  NE2 . GLN I  1 28  ? 50.797  92.111  35.654 1.00 45.38  ? 22  GLN I NE2 1 
ATOM   9038  N  N   . LYS I  1 29  ? 56.605  91.650  37.349 1.00 70.07  ? 23  LYS I N   1 
ATOM   9039  C  CA  . LYS I  1 29  ? 57.703  92.052  36.475 1.00 76.63  ? 23  LYS I CA  1 
ATOM   9040  C  C   . LYS I  1 29  ? 57.225  92.525  35.100 1.00 79.04  ? 23  LYS I C   1 
ATOM   9041  O  O   . LYS I  1 29  ? 57.564  93.624  34.669 1.00 78.46  ? 23  LYS I O   1 
ATOM   9042  C  CB  . LYS I  1 29  ? 58.686  90.892  36.293 1.00 80.01  ? 23  LYS I CB  1 
ATOM   9043  C  CG  . LYS I  1 29  ? 59.193  90.284  37.585 1.00 83.36  ? 23  LYS I CG  1 
ATOM   9044  C  CD  . LYS I  1 29  ? 59.911  91.310  38.434 1.00 91.44  ? 23  LYS I CD  1 
ATOM   9045  C  CE  . LYS I  1 29  ? 60.504  90.668  39.679 1.00 94.67  ? 23  LYS I CE  1 
ATOM   9046  N  NZ  . LYS I  1 29  ? 61.471  89.586  39.338 1.00 90.98  ? 23  LYS I NZ  1 
ATOM   9047  N  N   . GLU I  1 30  ? 56.437  91.698  34.418 1.00 81.70  ? 24  GLU I N   1 
ATOM   9048  C  CA  . GLU I  1 30  ? 55.940  92.043  33.091 1.00 89.78  ? 24  GLU I CA  1 
ATOM   9049  C  C   . GLU I  1 30  ? 54.512  92.576  33.062 1.00 91.09  ? 24  GLU I C   1 
ATOM   9050  O  O   . GLU I  1 30  ? 53.646  92.101  33.790 1.00 91.47  ? 24  GLU I O   1 
ATOM   9051  C  CB  . GLU I  1 30  ? 56.058  90.833  32.161 1.00 98.75  ? 24  GLU I CB  1 
ATOM   9052  C  CG  . GLU I  1 30  ? 57.467  90.602  31.624 1.00 109.78 ? 24  GLU I CG  1 
ATOM   9053  C  CD  . GLU I  1 30  ? 57.878  91.638  30.583 1.00 116.74 ? 24  GLU I CD  1 
ATOM   9054  O  OE1 . GLU I  1 30  ? 59.063  91.648  30.183 1.00 118.55 ? 24  GLU I OE1 1 
ATOM   9055  O  OE2 . GLU I  1 30  ? 57.014  92.437  30.159 1.00 118.57 ? 24  GLU I OE2 1 
ATOM   9056  N  N   . SER I  1 31  ? 54.287  93.561  32.194 1.00 92.85  ? 25  SER I N   1 
ATOM   9057  C  CA  . SER I  1 31  ? 52.990  94.212  32.029 1.00 95.01  ? 25  SER I CA  1 
ATOM   9058  C  C   . SER I  1 31  ? 51.814  93.247  32.041 1.00 96.24  ? 25  SER I C   1 
ATOM   9059  O  O   . SER I  1 31  ? 50.863  93.424  32.803 1.00 97.63  ? 25  SER I O   1 
ATOM   9060  C  CB  . SER I  1 31  ? 52.975  95.012  30.726 1.00 97.36  ? 25  SER I CB  1 
ATOM   9061  O  OG  . SER I  1 31  ? 51.728  95.656  30.539 1.00 101.68 ? 25  SER I OG  1 
ATOM   9062  N  N   . ASN I  1 32  ? 51.864  92.243  31.176 1.00 96.24  ? 26  ASN I N   1 
ATOM   9063  C  CA  . ASN I  1 32  ? 50.802  91.250  31.122 1.00 97.41  ? 26  ASN I CA  1 
ATOM   9064  C  C   . ASN I  1 32  ? 51.348  89.952  31.684 1.00 94.85  ? 26  ASN I C   1 
ATOM   9065  O  O   . ASN I  1 32  ? 51.111  88.876  31.134 1.00 97.41  ? 26  ASN I O   1 
ATOM   9066  C  CB  . ASN I  1 32  ? 50.326  91.034  29.683 1.00 103.24 ? 26  ASN I CB  1 
ATOM   9067  C  CG  . ASN I  1 32  ? 49.437  92.160  29.186 1.00 106.56 ? 26  ASN I CG  1 
ATOM   9068  O  OD1 . ASN I  1 32  ? 48.400  92.458  29.782 1.00 104.87 ? 26  ASN I OD1 1 
ATOM   9069  N  ND2 . ASN I  1 32  ? 49.838  92.787  28.085 1.00 107.18 ? 26  ASN I ND2 1 
ATOM   9070  N  N   . GLY I  1 33  ? 52.088  90.071  32.782 1.00 89.18  ? 27  GLY I N   1 
ATOM   9071  C  CA  . GLY I  1 33  ? 52.675  88.909  33.421 1.00 76.85  ? 27  GLY I CA  1 
ATOM   9072  C  C   . GLY I  1 33  ? 51.960  88.485  34.692 1.00 68.95  ? 27  GLY I C   1 
ATOM   9073  O  O   . GLY I  1 33  ? 50.925  89.046  35.060 1.00 60.82  ? 27  GLY I O   1 
ATOM   9074  N  N   . PRO I  1 34  ? 52.495  87.470  35.384 1.00 65.32  ? 28  PRO I N   1 
ATOM   9075  C  CA  . PRO I  1 34  ? 51.907  86.964  36.625 1.00 59.51  ? 28  PRO I CA  1 
ATOM   9076  C  C   . PRO I  1 34  ? 52.228  87.887  37.794 1.00 53.54  ? 28  PRO I C   1 
ATOM   9077  O  O   . PRO I  1 34  ? 53.307  88.481  37.859 1.00 44.47  ? 28  PRO I O   1 
ATOM   9078  C  CB  . PRO I  1 34  ? 52.572  85.596  36.797 1.00 60.24  ? 28  PRO I CB  1 
ATOM   9079  C  CG  . PRO I  1 34  ? 53.064  85.253  35.427 1.00 64.99  ? 28  PRO I CG  1 
ATOM   9080  C  CD  . PRO I  1 34  ? 53.558  86.568  34.919 1.00 63.91  ? 28  PRO I CD  1 
ATOM   9081  N  N   . VAL I  1 35  ? 51.284  88.006  38.717 1.00 48.66  ? 29  VAL I N   1 
ATOM   9082  C  CA  . VAL I  1 35  ? 51.488  88.834  39.891 1.00 45.01  ? 29  VAL I CA  1 
ATOM   9083  C  C   . VAL I  1 35  ? 51.839  87.920  41.054 1.00 37.50  ? 29  VAL I C   1 
ATOM   9084  O  O   . VAL I  1 35  ? 51.123  86.968  41.325 1.00 36.82  ? 29  VAL I O   1 
ATOM   9085  C  CB  . VAL I  1 35  ? 50.205  89.623  40.272 1.00 48.53  ? 29  VAL I CB  1 
ATOM   9086  C  CG1 . VAL I  1 35  ? 50.485  90.507  41.480 1.00 43.07  ? 29  VAL I CG1 1 
ATOM   9087  C  CG2 . VAL I  1 35  ? 49.721  90.459  39.099 1.00 47.18  ? 29  VAL I CG2 1 
ATOM   9088  N  N   . LYS I  1 36  ? 52.947  88.184  41.726 1.00 35.07  ? 30  LYS I N   1 
ATOM   9089  C  CA  . LYS I  1 36  ? 53.296  87.368  42.879 1.00 40.15  ? 30  LYS I CA  1 
ATOM   9090  C  C   . LYS I  1 36  ? 52.601  88.032  44.062 1.00 39.08  ? 30  LYS I C   1 
ATOM   9091  O  O   . LYS I  1 36  ? 52.750  89.230  44.286 1.00 40.99  ? 30  LYS I O   1 
ATOM   9092  C  CB  . LYS I  1 36  ? 54.809  87.347  43.110 1.00 46.10  ? 30  LYS I CB  1 
ATOM   9093  C  CG  . LYS I  1 36  ? 55.241  86.517  44.315 1.00 53.49  ? 30  LYS I CG  1 
ATOM   9094  C  CD  . LYS I  1 36  ? 56.720  86.717  44.634 1.00 60.19  ? 30  LYS I CD  1 
ATOM   9095  C  CE  . LYS I  1 36  ? 57.119  85.986  45.911 1.00 65.18  ? 30  LYS I CE  1 
ATOM   9096  N  NZ  . LYS I  1 36  ? 58.518  86.305  46.327 1.00 71.58  ? 30  LYS I NZ  1 
ATOM   9097  N  N   . VAL I  1 37  ? 51.827  87.250  44.800 1.00 41.83  ? 31  VAL I N   1 
ATOM   9098  C  CA  . VAL I  1 37  ? 51.100  87.745  45.961 1.00 41.47  ? 31  VAL I CA  1 
ATOM   9099  C  C   . VAL I  1 37  ? 51.596  86.984  47.180 1.00 42.96  ? 31  VAL I C   1 
ATOM   9100  O  O   . VAL I  1 37  ? 51.477  85.759  47.241 1.00 37.93  ? 31  VAL I O   1 
ATOM   9101  C  CB  . VAL I  1 37  ? 49.584  87.497  45.818 1.00 34.18  ? 31  VAL I CB  1 
ATOM   9102  C  CG1 . VAL I  1 37  ? 48.836  88.058  47.024 1.00 23.49  ? 31  VAL I CG1 1 
ATOM   9103  C  CG2 . VAL I  1 37  ? 49.091  88.116  44.543 1.00 35.29  ? 31  VAL I CG2 1 
ATOM   9104  N  N   . TRP I  1 38  ? 52.149  87.697  48.152 1.00 36.90  ? 32  TRP I N   1 
ATOM   9105  C  CA  . TRP I  1 38  ? 52.640  87.017  49.338 1.00 44.83  ? 32  TRP I CA  1 
ATOM   9106  C  C   . TRP I  1 38  ? 52.618  87.904  50.570 1.00 43.08  ? 32  TRP I C   1 
ATOM   9107  O  O   . TRP I  1 38  ? 52.590  89.128  50.480 1.00 46.01  ? 32  TRP I O   1 
ATOM   9108  C  CB  . TRP I  1 38  ? 54.067  86.496  49.106 1.00 44.94  ? 32  TRP I CB  1 
ATOM   9109  C  CG  . TRP I  1 38  ? 55.122  87.542  49.290 1.00 41.50  ? 32  TRP I CG  1 
ATOM   9110  C  CD1 . TRP I  1 38  ? 55.844  87.794  50.426 1.00 41.33  ? 32  TRP I CD1 1 
ATOM   9111  C  CD2 . TRP I  1 38  ? 55.520  88.524  48.333 1.00 39.48  ? 32  TRP I CD2 1 
ATOM   9112  N  NE1 . TRP I  1 38  ? 56.665  88.877  50.234 1.00 41.34  ? 32  TRP I NE1 1 
ATOM   9113  C  CE2 . TRP I  1 38  ? 56.486  89.346  48.957 1.00 45.20  ? 32  TRP I CE2 1 
ATOM   9114  C  CE3 . TRP I  1 38  ? 55.149  88.795  47.010 1.00 44.55  ? 32  TRP I CE3 1 
ATOM   9115  C  CZ2 . TRP I  1 38  ? 57.090  90.425  48.298 1.00 43.74  ? 32  TRP I CZ2 1 
ATOM   9116  C  CZ3 . TRP I  1 38  ? 55.748  89.871  46.354 1.00 51.39  ? 32  TRP I CZ3 1 
ATOM   9117  C  CH2 . TRP I  1 38  ? 56.709  90.672  47.002 1.00 50.37  ? 32  TRP I CH2 1 
ATOM   9118  N  N   . GLY I  1 39  ? 52.648  87.260  51.726 1.00 32.98  ? 33  GLY I N   1 
ATOM   9119  C  CA  . GLY I  1 39  ? 52.633  87.989  52.967 1.00 34.18  ? 33  GLY I CA  1 
ATOM   9120  C  C   . GLY I  1 39  ? 52.196  87.061  54.074 1.00 36.65  ? 33  GLY I C   1 
ATOM   9121  O  O   . GLY I  1 39  ? 52.279  85.833  53.965 1.00 38.11  ? 33  GLY I O   1 
ATOM   9122  N  N   . SER I  1 40  ? 51.708  87.655  55.147 1.00 33.59  ? 34  SER I N   1 
ATOM   9123  C  CA  . SER I  1 40  ? 51.278  86.890  56.293 1.00 36.45  ? 34  SER I CA  1 
ATOM   9124  C  C   . SER I  1 40  ? 50.025  87.529  56.890 1.00 38.08  ? 34  SER I C   1 
ATOM   9125  O  O   . SER I  1 40  ? 49.830  88.741  56.799 1.00 38.16  ? 34  SER I O   1 
ATOM   9126  C  CB  . SER I  1 40  ? 52.417  86.866  57.313 1.00 29.81  ? 34  SER I CB  1 
ATOM   9127  O  OG  . SER I  1 40  ? 52.027  86.204  58.494 1.00 50.67  ? 34  SER I OG  1 
ATOM   9128  N  N   . ILE I  1 41  ? 49.164  86.709  57.480 1.00 41.40  ? 35  ILE I N   1 
ATOM   9129  C  CA  . ILE I  1 41  ? 47.943  87.209  58.102 1.00 35.25  ? 35  ILE I CA  1 
ATOM   9130  C  C   . ILE I  1 41  ? 47.837  86.534  59.456 1.00 36.97  ? 35  ILE I C   1 
ATOM   9131  O  O   . ILE I  1 41  ? 47.883  85.313  59.532 1.00 40.39  ? 35  ILE I O   1 
ATOM   9132  C  CB  . ILE I  1 41  ? 46.684  86.850  57.266 1.00 32.27  ? 35  ILE I CB  1 
ATOM   9133  C  CG1 . ILE I  1 41  ? 46.869  87.289  55.814 1.00 26.64  ? 35  ILE I CG1 1 
ATOM   9134  C  CG2 . ILE I  1 41  ? 45.461  87.537  57.849 1.00 28.04  ? 35  ILE I CG2 1 
ATOM   9135  C  CD1 . ILE I  1 41  ? 45.604  87.204  54.962 1.00 34.21  ? 35  ILE I CD1 1 
ATOM   9136  N  N   . LYS I  1 42  ? 47.709  87.310  60.526 1.00 36.09  ? 36  LYS I N   1 
ATOM   9137  C  CA  . LYS I  1 42  ? 47.594  86.710  61.854 1.00 43.08  ? 36  LYS I CA  1 
ATOM   9138  C  C   . LYS I  1 42  ? 46.189  86.904  62.431 1.00 41.46  ? 36  LYS I C   1 
ATOM   9139  O  O   . LYS I  1 42  ? 45.368  87.602  61.848 1.00 40.76  ? 36  LYS I O   1 
ATOM   9140  C  CB  . LYS I  1 42  ? 48.658  87.285  62.817 1.00 44.03  ? 36  LYS I CB  1 
ATOM   9141  C  CG  . LYS I  1 42  ? 48.574  88.784  63.082 1.00 54.13  ? 36  LYS I CG  1 
ATOM   9142  C  CD  . LYS I  1 42  ? 49.602  89.242  64.135 1.00 63.30  ? 36  LYS I CD  1 
ATOM   9143  C  CE  . LYS I  1 42  ? 49.298  88.658  65.520 1.00 71.71  ? 36  LYS I CE  1 
ATOM   9144  N  NZ  . LYS I  1 42  ? 50.232  89.105  66.600 1.00 68.92  ? 36  LYS I NZ  1 
ATOM   9145  N  N   . GLY I  1 43  ? 45.913  86.255  63.560 1.00 44.23  ? 37  GLY I N   1 
ATOM   9146  C  CA  . GLY I  1 43  ? 44.616  86.382  64.204 1.00 44.36  ? 37  GLY I CA  1 
ATOM   9147  C  C   . GLY I  1 43  ? 43.467  85.612  63.575 1.00 45.84  ? 37  GLY I C   1 
ATOM   9148  O  O   . GLY I  1 43  ? 42.316  85.777  63.981 1.00 45.93  ? 37  GLY I O   1 
ATOM   9149  N  N   . LEU I  1 44  ? 43.764  84.769  62.595 1.00 44.53  ? 38  LEU I N   1 
ATOM   9150  C  CA  . LEU I  1 44  ? 42.726  83.997  61.923 1.00 44.90  ? 38  LEU I CA  1 
ATOM   9151  C  C   . LEU I  1 44  ? 42.419  82.682  62.617 1.00 44.34  ? 38  LEU I C   1 
ATOM   9152  O  O   . LEU I  1 44  ? 43.283  82.107  63.268 1.00 49.78  ? 38  LEU I O   1 
ATOM   9153  C  CB  . LEU I  1 44  ? 43.144  83.697  60.485 1.00 40.59  ? 38  LEU I CB  1 
ATOM   9154  C  CG  . LEU I  1 44  ? 43.040  84.831  59.472 1.00 44.69  ? 38  LEU I CG  1 
ATOM   9155  C  CD1 . LEU I  1 44  ? 43.704  84.398  58.171 1.00 40.55  ? 38  LEU I CD1 1 
ATOM   9156  C  CD2 . LEU I  1 44  ? 41.564  85.192  59.247 1.00 38.15  ? 38  LEU I CD2 1 
ATOM   9157  N  N   . THR I  1 45  ? 41.184  82.209  62.490 1.00 41.04  ? 39  THR I N   1 
ATOM   9158  C  CA  . THR I  1 45  ? 40.832  80.922  63.070 1.00 37.59  ? 39  THR I CA  1 
ATOM   9159  C  C   . THR I  1 45  ? 41.457  79.895  62.121 1.00 39.02  ? 39  THR I C   1 
ATOM   9160  O  O   . THR I  1 45  ? 41.390  80.045  60.889 1.00 35.14  ? 39  THR I O   1 
ATOM   9161  C  CB  . THR I  1 45  ? 39.302  80.712  63.129 1.00 39.30  ? 39  THR I CB  1 
ATOM   9162  O  OG1 . THR I  1 45  ? 38.746  80.831  61.810 1.00 31.78  ? 39  THR I OG1 1 
ATOM   9163  C  CG2 . THR I  1 45  ? 38.658  81.752  64.056 1.00 33.76  ? 39  THR I CG2 1 
ATOM   9164  N  N   . GLU I  1 46  ? 42.085  78.870  62.682 1.00 37.63  ? 40  GLU I N   1 
ATOM   9165  C  CA  . GLU I  1 46  ? 42.726  77.860  61.856 1.00 43.75  ? 40  GLU I CA  1 
ATOM   9166  C  C   . GLU I  1 46  ? 41.770  77.348  60.788 1.00 44.05  ? 40  GLU I C   1 
ATOM   9167  O  O   . GLU I  1 46  ? 40.567  77.256  61.017 1.00 46.46  ? 40  GLU I O   1 
ATOM   9168  C  CB  . GLU I  1 46  ? 43.227  76.714  62.726 1.00 42.06  ? 40  GLU I CB  1 
ATOM   9169  C  CG  . GLU I  1 46  ? 42.165  76.016  63.499 1.00 44.04  ? 40  GLU I CG  1 
ATOM   9170  C  CD  . GLU I  1 46  ? 42.737  74.990  64.455 1.00 56.60  ? 40  GLU I CD  1 
ATOM   9171  O  OE1 . GLU I  1 46  ? 41.945  74.372  65.194 1.00 66.10  ? 40  GLU I OE1 1 
ATOM   9172  O  OE2 . GLU I  1 46  ? 43.973  74.796  64.472 1.00 57.23  ? 40  GLU I OE2 1 
ATOM   9173  N  N   . GLY I  1 47  ? 42.305  77.040  59.610 1.00 43.81  ? 41  GLY I N   1 
ATOM   9174  C  CA  . GLY I  1 47  ? 41.469  76.544  58.529 1.00 38.07  ? 41  GLY I CA  1 
ATOM   9175  C  C   . GLY I  1 47  ? 41.524  77.399  57.280 1.00 35.76  ? 41  GLY I C   1 
ATOM   9176  O  O   . GLY I  1 47  ? 42.305  78.356  57.212 1.00 34.88  ? 41  GLY I O   1 
ATOM   9177  N  N   . LEU I  1 48  ? 40.697  77.054  56.292 1.00 29.23  ? 42  LEU I N   1 
ATOM   9178  C  CA  . LEU I  1 48  ? 40.646  77.795  55.029 1.00 36.54  ? 42  LEU I CA  1 
ATOM   9179  C  C   . LEU I  1 48  ? 39.806  79.071  55.120 1.00 38.66  ? 42  LEU I C   1 
ATOM   9180  O  O   . LEU I  1 48  ? 38.767  79.109  55.790 1.00 39.84  ? 42  LEU I O   1 
ATOM   9181  C  CB  . LEU I  1 48  ? 40.095  76.922  53.902 1.00 34.51  ? 42  LEU I CB  1 
ATOM   9182  C  CG  . LEU I  1 48  ? 40.966  75.789  53.374 1.00 39.89  ? 42  LEU I CG  1 
ATOM   9183  C  CD1 . LEU I  1 48  ? 41.342  74.839  54.488 1.00 38.86  ? 42  LEU I CD1 1 
ATOM   9184  C  CD2 . LEU I  1 48  ? 40.202  75.070  52.280 1.00 35.28  ? 42  LEU I CD2 1 
ATOM   9185  N  N   . HIS I  1 49  ? 40.268  80.109  54.430 1.00 37.37  ? 43  HIS I N   1 
ATOM   9186  C  CA  . HIS I  1 49  ? 39.596  81.400  54.417 1.00 41.22  ? 43  HIS I CA  1 
ATOM   9187  C  C   . HIS I  1 49  ? 39.535  81.980  52.996 1.00 42.43  ? 43  HIS I C   1 
ATOM   9188  O  O   . HIS I  1 49  ? 40.520  81.916  52.236 1.00 33.66  ? 43  HIS I O   1 
ATOM   9189  C  CB  . HIS I  1 49  ? 40.327  82.356  55.361 1.00 40.93  ? 43  HIS I CB  1 
ATOM   9190  C  CG  . HIS I  1 49  ? 40.142  82.031  56.812 1.00 42.37  ? 43  HIS I CG  1 
ATOM   9191  N  ND1 . HIS I  1 49  ? 38.992  82.346  57.504 1.00 38.86  ? 43  HIS I ND1 1 
ATOM   9192  C  CD2 . HIS I  1 49  ? 40.961  81.423  57.702 1.00 48.32  ? 43  HIS I CD2 1 
ATOM   9193  C  CE1 . HIS I  1 49  ? 39.113  81.951  58.760 1.00 44.57  ? 43  HIS I CE1 1 
ATOM   9194  N  NE2 . HIS I  1 49  ? 40.298  81.388  58.907 1.00 47.99  ? 43  HIS I NE2 1 
ATOM   9195  N  N   . GLY I  1 50  ? 38.367  82.516  52.634 1.00 38.45  ? 44  GLY I N   1 
ATOM   9196  C  CA  . GLY I  1 50  ? 38.195  83.092  51.310 1.00 33.38  ? 44  GLY I CA  1 
ATOM   9197  C  C   . GLY I  1 50  ? 39.167  84.242  51.152 1.00 32.29  ? 44  GLY I C   1 
ATOM   9198  O  O   . GLY I  1 50  ? 39.426  84.971  52.106 1.00 29.69  ? 44  GLY I O   1 
ATOM   9199  N  N   . PHE I  1 51  ? 39.697  84.416  49.948 1.00 32.37  ? 45  PHE I N   1 
ATOM   9200  C  CA  . PHE I  1 51  ? 40.678  85.464  49.693 1.00 33.96  ? 45  PHE I CA  1 
ATOM   9201  C  C   . PHE I  1 51  ? 40.315  86.111  48.378 1.00 34.78  ? 45  PHE I C   1 
ATOM   9202  O  O   . PHE I  1 51  ? 40.437  85.468  47.323 1.00 35.22  ? 45  PHE I O   1 
ATOM   9203  C  CB  . PHE I  1 51  ? 42.065  84.819  49.597 1.00 41.00  ? 45  PHE I CB  1 
ATOM   9204  C  CG  . PHE I  1 51  ? 43.208  85.775  49.773 1.00 39.81  ? 45  PHE I CG  1 
ATOM   9205  C  CD1 . PHE I  1 51  ? 43.329  86.532  50.930 1.00 35.02  ? 45  PHE I CD1 1 
ATOM   9206  C  CD2 . PHE I  1 51  ? 44.212  85.861  48.808 1.00 42.47  ? 45  PHE I CD2 1 
ATOM   9207  C  CE1 . PHE I  1 51  ? 44.433  87.354  51.127 1.00 32.61  ? 45  PHE I CE1 1 
ATOM   9208  C  CE2 . PHE I  1 51  ? 45.320  86.678  49.000 1.00 33.35  ? 45  PHE I CE2 1 
ATOM   9209  C  CZ  . PHE I  1 51  ? 45.426  87.423  50.162 1.00 33.75  ? 45  PHE I CZ  1 
ATOM   9210  N  N   . HIS I  1 52  ? 39.868  87.369  48.424 1.00 36.80  ? 46  HIS I N   1 
ATOM   9211  C  CA  . HIS I  1 52  ? 39.461  88.060  47.192 1.00 37.17  ? 46  HIS I CA  1 
ATOM   9212  C  C   . HIS I  1 52  ? 39.715  89.564  47.086 1.00 36.04  ? 46  HIS I C   1 
ATOM   9213  O  O   . HIS I  1 52  ? 39.719  90.293  48.080 1.00 34.47  ? 46  HIS I O   1 
ATOM   9214  C  CB  . HIS I  1 52  ? 37.960  87.857  46.924 1.00 39.33  ? 46  HIS I CB  1 
ATOM   9215  C  CG  . HIS I  1 52  ? 37.418  86.542  47.395 1.00 44.66  ? 46  HIS I CG  1 
ATOM   9216  N  ND1 . HIS I  1 52  ? 36.750  86.400  48.591 1.00 40.73  ? 46  HIS I ND1 1 
ATOM   9217  C  CD2 . HIS I  1 52  ? 37.441  85.313  46.827 1.00 42.89  ? 46  HIS I CD2 1 
ATOM   9218  C  CE1 . HIS I  1 52  ? 36.383  85.140  48.740 1.00 40.67  ? 46  HIS I CE1 1 
ATOM   9219  N  NE2 . HIS I  1 52  ? 36.791  84.460  47.684 1.00 48.47  ? 46  HIS I NE2 1 
ATOM   9220  N  N   . VAL I  1 53  ? 39.925  90.010  45.851 1.00 33.00  ? 47  VAL I N   1 
ATOM   9221  C  CA  . VAL I  1 53  ? 40.078  91.420  45.549 1.00 37.56  ? 47  VAL I CA  1 
ATOM   9222  C  C   . VAL I  1 53  ? 38.632  91.849  45.244 1.00 40.74  ? 47  VAL I C   1 
ATOM   9223  O  O   . VAL I  1 53  ? 38.034  91.341  44.292 1.00 44.89  ? 47  VAL I O   1 
ATOM   9224  C  CB  . VAL I  1 53  ? 40.905  91.660  44.253 1.00 37.70  ? 47  VAL I CB  1 
ATOM   9225  C  CG1 . VAL I  1 53  ? 40.804  93.134  43.833 1.00 30.56  ? 47  VAL I CG1 1 
ATOM   9226  C  CG2 . VAL I  1 53  ? 42.343  91.267  44.458 1.00 35.95  ? 47  VAL I CG2 1 
ATOM   9227  N  N   . HIS I  1 54  ? 38.052  92.739  46.046 1.00 41.51  ? 48  HIS I N   1 
ATOM   9228  C  CA  . HIS I  1 54  ? 36.691  93.201  45.764 1.00 49.53  ? 48  HIS I CA  1 
ATOM   9229  C  C   . HIS I  1 54  ? 36.736  94.438  44.852 1.00 53.57  ? 48  HIS I C   1 
ATOM   9230  O  O   . HIS I  1 54  ? 37.810  95.004  44.615 1.00 52.46  ? 48  HIS I O   1 
ATOM   9231  C  CB  . HIS I  1 54  ? 35.926  93.467  47.062 1.00 43.82  ? 48  HIS I CB  1 
ATOM   9232  C  CG  . HIS I  1 54  ? 35.543  92.213  47.796 1.00 53.67  ? 48  HIS I CG  1 
ATOM   9233  N  ND1 . HIS I  1 54  ? 34.241  91.920  48.147 1.00 50.93  ? 48  HIS I ND1 1 
ATOM   9234  C  CD2 . HIS I  1 54  ? 36.292  91.175  48.240 1.00 52.38  ? 48  HIS I CD2 1 
ATOM   9235  C  CE1 . HIS I  1 54  ? 34.208  90.758  48.776 1.00 51.89  ? 48  HIS I CE1 1 
ATOM   9236  N  NE2 . HIS I  1 54  ? 35.439  90.285  48.846 1.00 50.63  ? 48  HIS I NE2 1 
ATOM   9237  N  N   . GLU I  1 55  ? 35.582  94.852  44.334 1.00 57.95  ? 49  GLU I N   1 
ATOM   9238  C  CA  . GLU I  1 55  ? 35.526  95.974  43.391 1.00 59.52  ? 49  GLU I CA  1 
ATOM   9239  C  C   . GLU I  1 55  ? 35.988  97.378  43.804 1.00 56.74  ? 49  GLU I C   1 
ATOM   9240  O  O   . GLU I  1 55  ? 36.759  98.010  43.078 1.00 46.52  ? 49  GLU I O   1 
ATOM   9241  C  CB  . GLU I  1 55  ? 34.117  96.094  42.809 1.00 61.77  ? 49  GLU I CB  1 
ATOM   9242  C  CG  . GLU I  1 55  ? 34.083  96.910  41.522 1.00 67.70  ? 49  GLU I CG  1 
ATOM   9243  C  CD  . GLU I  1 55  ? 32.695  97.023  40.928 1.00 66.93  ? 49  GLU I CD  1 
ATOM   9244  O  OE1 . GLU I  1 55  ? 32.572  97.513  39.781 1.00 61.41  ? 49  GLU I OE1 1 
ATOM   9245  O  OE2 . GLU I  1 55  ? 31.729  96.626  41.613 1.00 69.71  ? 49  GLU I OE2 1 
ATOM   9246  N  N   . PHE I  1 56  ? 35.527  97.865  44.954 1.00 52.63  ? 50  PHE I N   1 
ATOM   9247  C  CA  . PHE I  1 56  ? 35.870  99.216  45.391 1.00 51.92  ? 50  PHE I CA  1 
ATOM   9248  C  C   . PHE I  1 56  ? 36.811  99.365  46.568 1.00 48.99  ? 50  PHE I C   1 
ATOM   9249  O  O   . PHE I  1 56  ? 36.645  98.713  47.597 1.00 48.76  ? 50  PHE I O   1 
ATOM   9250  C  CB  . PHE I  1 56  ? 34.585  99.995  45.709 1.00 55.37  ? 50  PHE I CB  1 
ATOM   9251  C  CG  . PHE I  1 56  ? 33.587  99.965  44.603 1.00 52.83  ? 50  PHE I CG  1 
ATOM   9252  C  CD1 . PHE I  1 56  ? 33.918  100.464 43.341 1.00 48.84  ? 50  PHE I CD1 1 
ATOM   9253  C  CD2 . PHE I  1 56  ? 32.343  99.382  44.794 1.00 49.99  ? 50  PHE I CD2 1 
ATOM   9254  C  CE1 . PHE I  1 56  ? 33.025  100.378 42.280 1.00 48.57  ? 50  PHE I CE1 1 
ATOM   9255  C  CE2 . PHE I  1 56  ? 31.436  99.289  43.738 1.00 52.83  ? 50  PHE I CE2 1 
ATOM   9256  C  CZ  . PHE I  1 56  ? 31.781  99.789  42.475 1.00 52.46  ? 50  PHE I CZ  1 
ATOM   9257  N  N   . GLY I  1 57  ? 37.786  100.258 46.406 1.00 47.56  ? 51  GLY I N   1 
ATOM   9258  C  CA  . GLY I  1 57  ? 38.733  100.542 47.468 1.00 44.04  ? 51  GLY I CA  1 
ATOM   9259  C  C   . GLY I  1 57  ? 38.057  101.575 48.348 1.00 46.47  ? 51  GLY I C   1 
ATOM   9260  O  O   . GLY I  1 57  ? 38.555  102.686 48.547 1.00 43.39  ? 51  GLY I O   1 
ATOM   9261  N  N   . ASP I  1 58  ? 36.899  101.191 48.869 1.00 42.15  ? 52  ASP I N   1 
ATOM   9262  C  CA  . ASP I  1 58  ? 36.091  102.057 49.702 1.00 40.33  ? 52  ASP I CA  1 
ATOM   9263  C  C   . ASP I  1 58  ? 35.865  101.375 51.023 1.00 37.88  ? 52  ASP I C   1 
ATOM   9264  O  O   . ASP I  1 58  ? 35.136  100.397 51.088 1.00 40.62  ? 52  ASP I O   1 
ATOM   9265  C  CB  . ASP I  1 58  ? 34.756  102.312 48.991 1.00 43.28  ? 52  ASP I CB  1 
ATOM   9266  C  CG  . ASP I  1 58  ? 33.760  103.090 49.842 1.00 50.40  ? 52  ASP I CG  1 
ATOM   9267  O  OD1 . ASP I  1 58  ? 32.811  103.641 49.244 1.00 53.32  ? 52  ASP I OD1 1 
ATOM   9268  O  OD2 . ASP I  1 58  ? 33.901  103.146 51.086 1.00 45.40  ? 52  ASP I OD2 1 
ATOM   9269  N  N   . ASN I  1 59  ? 36.487  101.881 52.080 1.00 38.04  ? 53  ASN I N   1 
ATOM   9270  C  CA  . ASN I  1 59  ? 36.319  101.269 53.391 1.00 44.12  ? 53  ASN I CA  1 
ATOM   9271  C  C   . ASN I  1 59  ? 35.598  102.204 54.360 1.00 43.97  ? 53  ASN I C   1 
ATOM   9272  O  O   . ASN I  1 59  ? 35.822  102.140 55.562 1.00 45.09  ? 53  ASN I O   1 
ATOM   9273  C  CB  . ASN I  1 59  ? 37.687  100.859 53.982 1.00 48.86  ? 53  ASN I CB  1 
ATOM   9274  C  CG  . ASN I  1 59  ? 38.378  99.708  53.194 1.00 61.08  ? 53  ASN I CG  1 
ATOM   9275  O  OD1 . ASN I  1 59  ? 39.534  99.365  53.473 1.00 59.81  ? 53  ASN I OD1 1 
ATOM   9276  N  ND2 . ASN I  1 59  ? 37.671  99.118  52.224 1.00 48.87  ? 53  ASN I ND2 1 
ATOM   9277  N  N   . THR I  1 60  ? 34.730  103.070 53.848 1.00 45.40  ? 54  THR I N   1 
ATOM   9278  C  CA  . THR I  1 60  ? 34.005  103.997 54.719 1.00 47.21  ? 54  THR I CA  1 
ATOM   9279  C  C   . THR I  1 60  ? 33.115  103.281 55.717 1.00 49.60  ? 54  THR I C   1 
ATOM   9280  O  O   . THR I  1 60  ? 32.966  103.727 56.853 1.00 50.97  ? 54  THR I O   1 
ATOM   9281  C  CB  . THR I  1 60  ? 33.129  104.961 53.925 1.00 44.92  ? 54  THR I CB  1 
ATOM   9282  O  OG1 . THR I  1 60  ? 32.371  104.227 52.960 1.00 43.62  ? 54  THR I OG1 1 
ATOM   9283  C  CG2 . THR I  1 60  ? 33.984  105.997 53.228 1.00 51.79  ? 54  THR I CG2 1 
ATOM   9284  N  N   . ALA I  1 61  ? 32.520  102.173 55.291 1.00 51.89  ? 55  ALA I N   1 
ATOM   9285  C  CA  . ALA I  1 61  ? 31.651  101.397 56.163 1.00 56.75  ? 55  ALA I CA  1 
ATOM   9286  C  C   . ALA I  1 61  ? 32.288  100.030 56.415 1.00 57.05  ? 55  ALA I C   1 
ATOM   9287  O  O   . ALA I  1 61  ? 31.702  98.992  56.113 1.00 61.27  ? 55  ALA I O   1 
ATOM   9288  C  CB  . ALA I  1 61  ? 30.281  101.237 55.510 1.00 53.15  ? 55  ALA I CB  1 
ATOM   9289  N  N   . GLY I  1 62  ? 33.491  100.033 56.977 1.00 55.56  ? 56  GLY I N   1 
ATOM   9290  C  CA  . GLY I  1 62  ? 34.182  98.783  57.227 1.00 55.73  ? 56  GLY I CA  1 
ATOM   9291  C  C   . GLY I  1 62  ? 34.435  98.125  55.884 1.00 58.01  ? 56  GLY I C   1 
ATOM   9292  O  O   . GLY I  1 62  ? 34.499  98.817  54.859 1.00 56.55  ? 56  GLY I O   1 
ATOM   9293  N  N   . CYS I  1 63  ? 34.559  96.799  55.867 1.00 52.01  ? 57  CYS I N   1 
ATOM   9294  C  CA  . CYS I  1 63  ? 34.801  96.091  54.610 1.00 49.10  ? 57  CYS I CA  1 
ATOM   9295  C  C   . CYS I  1 63  ? 33.542  95.963  53.764 1.00 45.37  ? 57  CYS I C   1 
ATOM   9296  O  O   . CYS I  1 63  ? 33.617  95.720  52.562 1.00 35.53  ? 57  CYS I O   1 
ATOM   9297  C  CB  . CYS I  1 63  ? 35.384  94.704  54.886 1.00 44.36  ? 57  CYS I CB  1 
ATOM   9298  S  SG  . CYS I  1 63  ? 36.920  94.786  55.855 1.00 49.19  ? 57  CYS I SG  1 
ATOM   9299  N  N   . THR I  1 64  ? 32.391  96.151  54.398 1.00 49.15  ? 58  THR I N   1 
ATOM   9300  C  CA  . THR I  1 64  ? 31.106  96.038  53.722 1.00 51.40  ? 58  THR I CA  1 
ATOM   9301  C  C   . THR I  1 64  ? 31.021  96.870  52.462 1.00 49.81  ? 58  THR I C   1 
ATOM   9302  O  O   . THR I  1 64  ? 30.491  96.409  51.451 1.00 49.44  ? 58  THR I O   1 
ATOM   9303  C  CB  . THR I  1 64  ? 29.951  96.484  54.620 1.00 54.34  ? 58  THR I CB  1 
ATOM   9304  O  OG1 . THR I  1 64  ? 30.184  96.050  55.967 1.00 58.97  ? 58  THR I OG1 1 
ATOM   9305  C  CG2 . THR I  1 64  ? 28.655  95.891  54.112 1.00 57.51  ? 58  THR I CG2 1 
ATOM   9306  N  N   . SER I  1 65  ? 31.540  98.095  52.529 1.00 51.11  ? 59  SER I N   1 
ATOM   9307  C  CA  . SER I  1 65  ? 31.499  99.015  51.394 1.00 50.39  ? 59  SER I CA  1 
ATOM   9308  C  C   . SER I  1 65  ? 32.475  98.718  50.257 1.00 52.31  ? 59  SER I C   1 
ATOM   9309  O  O   . SER I  1 65  ? 32.549  99.475  49.283 1.00 51.44  ? 59  SER I O   1 
ATOM   9310  C  CB  . SER I  1 65  ? 31.674  100.466 51.878 1.00 47.71  ? 59  SER I CB  1 
ATOM   9311  O  OG  . SER I  1 65  ? 32.636  100.576 52.916 1.00 59.35  ? 59  SER I OG  1 
ATOM   9312  N  N   . ALA I  1 66  ? 33.199  97.605  50.363 1.00 53.84  ? 60  ALA I N   1 
ATOM   9313  C  CA  . ALA I  1 66  ? 34.163  97.219  49.333 1.00 51.92  ? 60  ALA I CA  1 
ATOM   9314  C  C   . ALA I  1 66  ? 33.469  96.645  48.100 1.00 50.48  ? 60  ALA I C   1 
ATOM   9315  O  O   . ALA I  1 66  ? 34.096  96.455  47.047 1.00 38.94  ? 60  ALA I O   1 
ATOM   9316  C  CB  . ALA I  1 66  ? 35.136  96.199  49.894 1.00 53.30  ? 60  ALA I CB  1 
ATOM   9317  N  N   . GLY I  1 67  ? 32.174  96.364  48.239 1.00 50.15  ? 61  GLY I N   1 
ATOM   9318  C  CA  . GLY I  1 67  ? 31.409  95.805  47.135 1.00 47.14  ? 61  GLY I CA  1 
ATOM   9319  C  C   . GLY I  1 67  ? 31.590  94.303  46.951 1.00 45.60  ? 61  GLY I C   1 
ATOM   9320  O  O   . GLY I  1 67  ? 31.986  93.595  47.878 1.00 38.27  ? 61  GLY I O   1 
ATOM   9321  N  N   . PRO I  1 68  ? 31.298  93.783  45.753 1.00 46.69  ? 62  PRO I N   1 
ATOM   9322  C  CA  . PRO I  1 68  ? 31.440  92.356  45.474 1.00 47.90  ? 62  PRO I CA  1 
ATOM   9323  C  C   . PRO I  1 68  ? 32.819  92.065  44.885 1.00 49.28  ? 62  PRO I C   1 
ATOM   9324  O  O   . PRO I  1 68  ? 33.616  92.975  44.661 1.00 53.78  ? 62  PRO I O   1 
ATOM   9325  C  CB  . PRO I  1 68  ? 30.329  92.111  44.467 1.00 44.73  ? 62  PRO I CB  1 
ATOM   9326  C  CG  . PRO I  1 68  ? 30.430  93.347  43.611 1.00 43.39  ? 62  PRO I CG  1 
ATOM   9327  C  CD  . PRO I  1 68  ? 30.642  94.472  44.624 1.00 46.24  ? 62  PRO I CD  1 
ATOM   9328  N  N   . HIS I  1 69  ? 33.098  90.797  44.626 1.00 50.16  ? 63  HIS I N   1 
ATOM   9329  C  CA  . HIS I  1 69  ? 34.381  90.424  44.047 1.00 53.51  ? 63  HIS I CA  1 
ATOM   9330  C  C   . HIS I  1 69  ? 34.612  91.237  42.758 1.00 53.19  ? 63  HIS I C   1 
ATOM   9331  O  O   . HIS I  1 69  ? 33.681  91.487  41.996 1.00 49.89  ? 63  HIS I O   1 
ATOM   9332  C  CB  . HIS I  1 69  ? 34.396  88.917  43.732 1.00 48.93  ? 63  HIS I CB  1 
ATOM   9333  C  CG  . HIS I  1 69  ? 34.168  88.032  44.925 1.00 46.94  ? 63  HIS I CG  1 
ATOM   9334  N  ND1 . HIS I  1 69  ? 34.155  86.654  44.837 1.00 39.54  ? 63  HIS I ND1 1 
ATOM   9335  C  CD2 . HIS I  1 69  ? 33.946  88.325  46.229 1.00 48.15  ? 63  HIS I CD2 1 
ATOM   9336  C  CE1 . HIS I  1 69  ? 33.935  86.139  46.033 1.00 45.47  ? 63  HIS I CE1 1 
ATOM   9337  N  NE2 . HIS I  1 69  ? 33.804  87.132  46.896 1.00 46.07  ? 63  HIS I NE2 1 
ATOM   9338  N  N   . PHE I  1 70  ? 35.848  91.666  42.528 1.00 54.11  ? 64  PHE I N   1 
ATOM   9339  C  CA  . PHE I  1 70  ? 36.177  92.427  41.325 1.00 53.02  ? 64  PHE I CA  1 
ATOM   9340  C  C   . PHE I  1 70  ? 35.791  91.534  40.151 1.00 59.32  ? 64  PHE I C   1 
ATOM   9341  O  O   . PHE I  1 70  ? 36.386  90.474  39.953 1.00 59.87  ? 64  PHE I O   1 
ATOM   9342  C  CB  . PHE I  1 70  ? 37.681  92.725  41.284 1.00 46.95  ? 64  PHE I CB  1 
ATOM   9343  C  CG  . PHE I  1 70  ? 38.110  93.548  40.102 1.00 41.86  ? 64  PHE I CG  1 
ATOM   9344  C  CD1 . PHE I  1 70  ? 39.358  93.355  39.525 1.00 42.01  ? 64  PHE I CD1 1 
ATOM   9345  C  CD2 . PHE I  1 70  ? 37.275  94.530  39.573 1.00 39.76  ? 64  PHE I CD2 1 
ATOM   9346  C  CE1 . PHE I  1 70  ? 39.773  94.129  38.436 1.00 39.77  ? 64  PHE I CE1 1 
ATOM   9347  C  CE2 . PHE I  1 70  ? 37.681  95.310  38.486 1.00 34.65  ? 64  PHE I CE2 1 
ATOM   9348  C  CZ  . PHE I  1 70  ? 38.928  95.108  37.918 1.00 38.77  ? 64  PHE I CZ  1 
ATOM   9349  N  N   . ASN I  1 71  ? 34.817  91.967  39.358 1.00 64.74  ? 65  ASN I N   1 
ATOM   9350  C  CA  . ASN I  1 71  ? 34.340  91.152  38.246 1.00 65.10  ? 65  ASN I CA  1 
ATOM   9351  C  C   . ASN I  1 71  ? 34.211  91.900  36.908 1.00 65.51  ? 65  ASN I C   1 
ATOM   9352  O  O   . ASN I  1 71  ? 33.125  92.016  36.347 1.00 62.00  ? 65  ASN I O   1 
ATOM   9353  C  CB  . ASN I  1 71  ? 32.996  90.540  38.672 1.00 68.75  ? 65  ASN I CB  1 
ATOM   9354  C  CG  . ASN I  1 71  ? 32.506  89.465  37.731 1.00 69.18  ? 65  ASN I CG  1 
ATOM   9355  O  OD1 . ASN I  1 71  ? 33.296  88.775  37.086 1.00 63.04  ? 65  ASN I OD1 1 
ATOM   9356  N  ND2 . ASN I  1 71  ? 31.190  89.301  37.665 1.00 67.81  ? 65  ASN I ND2 1 
ATOM   9357  N  N   . PRO I  1 72  ? 35.334  92.390  36.365 1.00 66.48  ? 66  PRO I N   1 
ATOM   9358  C  CA  . PRO I  1 72  ? 35.353  93.126  35.096 1.00 69.45  ? 66  PRO I CA  1 
ATOM   9359  C  C   . PRO I  1 72  ? 35.020  92.374  33.799 1.00 73.06  ? 66  PRO I C   1 
ATOM   9360  O  O   . PRO I  1 72  ? 35.253  92.898  32.708 1.00 76.38  ? 66  PRO I O   1 
ATOM   9361  C  CB  . PRO I  1 72  ? 36.764  93.712  35.065 1.00 67.37  ? 66  PRO I CB  1 
ATOM   9362  C  CG  . PRO I  1 72  ? 37.557  92.677  35.755 1.00 66.96  ? 66  PRO I CG  1 
ATOM   9363  C  CD  . PRO I  1 72  ? 36.683  92.339  36.949 1.00 69.76  ? 66  PRO I CD  1 
ATOM   9364  N  N   . LEU I  1 73  ? 34.494  91.159  33.894 1.00 71.65  ? 67  LEU I N   1 
ATOM   9365  C  CA  . LEU I  1 73  ? 34.144  90.417  32.685 1.00 68.84  ? 67  LEU I CA  1 
ATOM   9366  C  C   . LEU I  1 73  ? 32.773  89.789  32.847 1.00 68.12  ? 67  LEU I C   1 
ATOM   9367  O  O   . LEU I  1 73  ? 32.328  89.022  32.003 1.00 68.07  ? 67  LEU I O   1 
ATOM   9368  C  CB  . LEU I  1 73  ? 35.185  89.338  32.377 1.00 67.43  ? 67  LEU I CB  1 
ATOM   9369  C  CG  . LEU I  1 73  ? 36.636  89.787  32.168 1.00 69.99  ? 67  LEU I CG  1 
ATOM   9370  C  CD1 . LEU I  1 73  ? 37.503  88.565  31.904 1.00 70.22  ? 67  LEU I CD1 1 
ATOM   9371  C  CD2 . LEU I  1 73  ? 36.734  90.769  31.013 1.00 71.71  ? 67  LEU I CD2 1 
ATOM   9372  N  N   . SER I  1 74  ? 32.111  90.122  33.949 1.00 71.65  ? 68  SER I N   1 
ATOM   9373  C  CA  . SER I  1 74  ? 30.766  89.629  34.235 1.00 76.21  ? 68  SER I CA  1 
ATOM   9374  C  C   . SER I  1 74  ? 30.631  88.108  34.221 1.00 78.41  ? 68  SER I C   1 
ATOM   9375  O  O   . SER I  1 74  ? 29.604  87.581  33.792 1.00 78.52  ? 68  SER I O   1 
ATOM   9376  C  CB  . SER I  1 74  ? 29.781  90.227  33.229 1.00 74.25  ? 68  SER I CB  1 
ATOM   9377  O  OG  . SER I  1 74  ? 29.952  91.629  33.133 1.00 70.63  ? 68  SER I OG  1 
ATOM   9378  N  N   . ARG I  1 75  ? 31.655  87.407  34.700 1.00 78.62  ? 69  ARG I N   1 
ATOM   9379  C  CA  . ARG I  1 75  ? 31.629  85.951  34.722 1.00 72.70  ? 69  ARG I CA  1 
ATOM   9380  C  C   . ARG I  1 75  ? 31.203  85.409  36.085 1.00 69.64  ? 69  ARG I C   1 
ATOM   9381  O  O   . ARG I  1 75  ? 30.924  86.175  37.001 1.00 62.25  ? 69  ARG I O   1 
ATOM   9382  C  CB  . ARG I  1 75  ? 32.999  85.411  34.287 1.00 75.25  ? 69  ARG I CB  1 
ATOM   9383  C  CG  . ARG I  1 75  ? 33.419  85.988  32.929 1.00 76.69  ? 69  ARG I CG  1 
ATOM   9384  C  CD  . ARG I  1 75  ? 34.411  85.139  32.141 1.00 81.92  ? 69  ARG I CD  1 
ATOM   9385  N  NE  . ARG I  1 75  ? 35.777  85.209  32.653 1.00 95.38  ? 69  ARG I NE  1 
ATOM   9386  C  CZ  . ARG I  1 75  ? 36.863  84.954  31.925 1.00 98.90  ? 69  ARG I CZ  1 
ATOM   9387  N  NH1 . ARG I  1 75  ? 36.746  84.618  30.646 1.00 98.75  ? 69  ARG I NH1 1 
ATOM   9388  N  NH2 . ARG I  1 75  ? 38.069  85.022  32.478 1.00 100.12 ? 69  ARG I NH2 1 
ATOM   9389  N  N   . LYS I  1 76  ? 31.117  84.089  36.210 1.00 73.42  ? 70  LYS I N   1 
ATOM   9390  C  CA  . LYS I  1 76  ? 30.698  83.468  37.466 1.00 76.67  ? 70  LYS I CA  1 
ATOM   9391  C  C   . LYS I  1 76  ? 31.856  83.326  38.446 1.00 74.00  ? 70  LYS I C   1 
ATOM   9392  O  O   . LYS I  1 76  ? 33.021  83.449  38.069 1.00 70.29  ? 70  LYS I O   1 
ATOM   9393  C  CB  . LYS I  1 76  ? 30.104  82.082  37.194 1.00 82.32  ? 70  LYS I CB  1 
ATOM   9394  C  CG  . LYS I  1 76  ? 28.851  82.080  36.329 1.00 90.24  ? 70  LYS I CG  1 
ATOM   9395  C  CD  . LYS I  1 76  ? 27.583  81.985  37.163 1.00 93.16  ? 70  LYS I CD  1 
ATOM   9396  C  CE  . LYS I  1 76  ? 27.431  83.163  38.106 1.00 95.95  ? 70  LYS I CE  1 
ATOM   9397  N  NZ  . LYS I  1 76  ? 26.185  83.044  38.912 1.00 95.02  ? 70  LYS I NZ  1 
ATOM   9398  N  N   . HIS I  1 77  ? 31.525  83.060  39.705 1.00 73.61  ? 71  HIS I N   1 
ATOM   9399  C  CA  . HIS I  1 77  ? 32.534  82.879  40.740 1.00 74.39  ? 71  HIS I CA  1 
ATOM   9400  C  C   . HIS I  1 77  ? 33.199  81.513  40.594 1.00 73.74  ? 71  HIS I C   1 
ATOM   9401  O  O   . HIS I  1 77  ? 32.554  80.530  40.215 1.00 75.34  ? 71  HIS I O   1 
ATOM   9402  C  CB  . HIS I  1 77  ? 31.898  82.985  42.125 1.00 76.99  ? 71  HIS I CB  1 
ATOM   9403  C  CG  . HIS I  1 77  ? 32.827  82.629  43.244 1.00 84.03  ? 71  HIS I CG  1 
ATOM   9404  N  ND1 . HIS I  1 77  ? 33.965  83.353  43.527 1.00 85.74  ? 71  HIS I ND1 1 
ATOM   9405  C  CD2 . HIS I  1 77  ? 32.792  81.617  44.144 1.00 86.20  ? 71  HIS I CD2 1 
ATOM   9406  C  CE1 . HIS I  1 77  ? 34.590  82.803  44.554 1.00 88.37  ? 71  HIS I CE1 1 
ATOM   9407  N  NE2 . HIS I  1 77  ? 33.899  81.748  44.947 1.00 84.76  ? 71  HIS I NE2 1 
ATOM   9408  N  N   . GLY I  1 78  ? 34.491  81.459  40.898 1.00 69.95  ? 72  GLY I N   1 
ATOM   9409  C  CA  . GLY I  1 78  ? 35.217  80.207  40.801 1.00 67.51  ? 72  GLY I CA  1 
ATOM   9410  C  C   . GLY I  1 78  ? 36.487  80.198  41.627 1.00 63.21  ? 72  GLY I C   1 
ATOM   9411  O  O   . GLY I  1 78  ? 36.655  81.014  42.536 1.00 61.90  ? 72  GLY I O   1 
ATOM   9412  N  N   . GLY I  1 79  ? 37.379  79.263  41.317 1.00 57.93  ? 73  GLY I N   1 
ATOM   9413  C  CA  . GLY I  1 79  ? 38.641  79.176  42.023 1.00 53.77  ? 73  GLY I CA  1 
ATOM   9414  C  C   . GLY I  1 79  ? 39.699  79.781  41.124 1.00 52.78  ? 73  GLY I C   1 
ATOM   9415  O  O   . GLY I  1 79  ? 39.538  79.751  39.900 1.00 49.22  ? 73  GLY I O   1 
ATOM   9416  N  N   . PRO I  1 80  ? 40.792  80.333  41.683 1.00 51.64  ? 74  PRO I N   1 
ATOM   9417  C  CA  . PRO I  1 80  ? 41.839  80.933  40.849 1.00 53.23  ? 74  PRO I CA  1 
ATOM   9418  C  C   . PRO I  1 80  ? 42.209  80.122  39.612 1.00 56.89  ? 74  PRO I C   1 
ATOM   9419  O  O   . PRO I  1 80  ? 42.532  80.687  38.566 1.00 56.19  ? 74  PRO I O   1 
ATOM   9420  C  CB  . PRO I  1 80  ? 43.009  81.104  41.822 1.00 47.85  ? 74  PRO I CB  1 
ATOM   9421  C  CG  . PRO I  1 80  ? 42.715  80.114  42.918 1.00 47.27  ? 74  PRO I CG  1 
ATOM   9422  C  CD  . PRO I  1 80  ? 41.233  80.257  43.084 1.00 44.70  ? 74  PRO I CD  1 
ATOM   9423  N  N   . LYS I  1 81  ? 42.137  78.799  39.727 1.00 62.12  ? 75  LYS I N   1 
ATOM   9424  C  CA  . LYS I  1 81  ? 42.478  77.917  38.615 1.00 66.71  ? 75  LYS I CA  1 
ATOM   9425  C  C   . LYS I  1 81  ? 41.365  77.767  37.571 1.00 66.54  ? 75  LYS I C   1 
ATOM   9426  O  O   . LYS I  1 81  ? 41.645  77.475  36.413 1.00 57.99  ? 75  LYS I O   1 
ATOM   9427  C  CB  . LYS I  1 81  ? 42.874  76.539  39.152 1.00 69.03  ? 75  LYS I CB  1 
ATOM   9428  C  CG  . LYS I  1 81  ? 44.117  76.542  40.035 1.00 78.66  ? 75  LYS I CG  1 
ATOM   9429  C  CD  . LYS I  1 81  ? 44.404  75.158  40.606 1.00 83.55  ? 75  LYS I CD  1 
ATOM   9430  C  CE  . LYS I  1 81  ? 45.697  75.139  41.407 1.00 86.63  ? 75  LYS I CE  1 
ATOM   9431  N  NZ  . LYS I  1 81  ? 45.976  73.794  41.991 1.00 90.16  ? 75  LYS I NZ  1 
ATOM   9432  N  N   . ASP I  1 82  ? 40.113  77.968  37.981 1.00 72.48  ? 76  ASP I N   1 
ATOM   9433  C  CA  . ASP I  1 82  ? 38.967  77.845  37.073 1.00 76.83  ? 76  ASP I CA  1 
ATOM   9434  C  C   . ASP I  1 82  ? 39.045  78.830  35.905 1.00 78.38  ? 76  ASP I C   1 
ATOM   9435  O  O   . ASP I  1 82  ? 39.564  79.936  36.050 1.00 80.67  ? 76  ASP I O   1 
ATOM   9436  C  CB  . ASP I  1 82  ? 37.653  78.067  37.840 1.00 77.20  ? 76  ASP I CB  1 
ATOM   9437  C  CG  . ASP I  1 82  ? 37.328  76.930  38.804 1.00 85.47  ? 76  ASP I CG  1 
ATOM   9438  O  OD1 . ASP I  1 82  ? 36.377  77.069  39.602 1.00 90.16  ? 76  ASP I OD1 1 
ATOM   9439  O  OD2 . ASP I  1 82  ? 38.013  75.888  38.765 1.00 89.75  ? 76  ASP I OD2 1 
ATOM   9440  N  N   . GLU I  1 83  ? 38.542  78.418  34.744 1.00 80.37  ? 77  GLU I N   1 
ATOM   9441  C  CA  . GLU I  1 83  ? 38.538  79.276  33.561 1.00 81.65  ? 77  GLU I CA  1 
ATOM   9442  C  C   . GLU I  1 83  ? 37.429  80.294  33.756 1.00 78.09  ? 77  GLU I C   1 
ATOM   9443  O  O   . GLU I  1 83  ? 37.572  81.474  33.428 1.00 78.55  ? 77  GLU I O   1 
ATOM   9444  C  CB  . GLU I  1 83  ? 38.270  78.448  32.300 1.00 92.07  ? 77  GLU I CB  1 
ATOM   9445  C  CG  . GLU I  1 83  ? 37.837  79.262  31.074 1.00 105.16 ? 77  GLU I CG  1 
ATOM   9446  C  CD  . GLU I  1 83  ? 38.888  80.258  30.603 1.00 112.54 ? 77  GLU I CD  1 
ATOM   9447  O  OE1 . GLU I  1 83  ? 39.218  81.195  31.363 1.00 117.62 ? 77  GLU I OE1 1 
ATOM   9448  O  OE2 . GLU I  1 83  ? 39.384  80.104  29.465 1.00 114.11 ? 77  GLU I OE2 1 
ATOM   9449  N  N   . GLU I  1 84  ? 36.321  79.819  34.307 1.00 70.10  ? 78  GLU I N   1 
ATOM   9450  C  CA  . GLU I  1 84  ? 35.174  80.662  34.571 1.00 66.69  ? 78  GLU I CA  1 
ATOM   9451  C  C   . GLU I  1 84  ? 35.281  81.215  35.988 1.00 64.28  ? 78  GLU I C   1 
ATOM   9452  O  O   . GLU I  1 84  ? 34.903  80.556  36.957 1.00 59.85  ? 78  GLU I O   1 
ATOM   9453  C  CB  . GLU I  1 84  ? 33.887  79.847  34.413 1.00 68.74  ? 78  GLU I CB  1 
ATOM   9454  C  CG  . GLU I  1 84  ? 32.605  80.612  34.710 1.00 72.16  ? 78  GLU I CG  1 
ATOM   9455  C  CD  . GLU I  1 84  ? 32.334  81.719  33.712 1.00 73.68  ? 78  GLU I CD  1 
ATOM   9456  O  OE1 . GLU I  1 84  ? 31.370  82.485  33.933 1.00 71.87  ? 78  GLU I OE1 1 
ATOM   9457  O  OE2 . GLU I  1 84  ? 33.077  81.818  32.709 1.00 71.13  ? 78  GLU I OE2 1 
ATOM   9458  N  N   . ARG I  1 85  ? 35.805  82.427  36.114 1.00 65.04  ? 79  ARG I N   1 
ATOM   9459  C  CA  . ARG I  1 85  ? 35.934  83.027  37.434 1.00 64.12  ? 79  ARG I CA  1 
ATOM   9460  C  C   . ARG I  1 85  ? 36.162  84.540  37.438 1.00 62.07  ? 79  ARG I C   1 
ATOM   9461  O  O   . ARG I  1 85  ? 36.572  85.134  36.433 1.00 55.33  ? 79  ARG I O   1 
ATOM   9462  C  CB  . ARG I  1 85  ? 37.051  82.320  38.208 1.00 61.04  ? 79  ARG I CB  1 
ATOM   9463  C  CG  . ARG I  1 85  ? 38.451  82.467  37.618 1.00 55.97  ? 79  ARG I CG  1 
ATOM   9464  C  CD  . ARG I  1 85  ? 39.185  83.610  38.287 1.00 56.92  ? 79  ARG I CD  1 
ATOM   9465  N  NE  . ARG I  1 85  ? 40.634  83.429  38.307 1.00 53.24  ? 79  ARG I NE  1 
ATOM   9466  C  CZ  . ARG I  1 85  ? 41.472  84.257  38.922 1.00 52.56  ? 79  ARG I CZ  1 
ATOM   9467  N  NH1 . ARG I  1 85  ? 41.005  85.316  39.564 1.00 53.93  ? 79  ARG I NH1 1 
ATOM   9468  N  NH2 . ARG I  1 85  ? 42.776  84.029  38.902 1.00 54.90  ? 79  ARG I NH2 1 
ATOM   9469  N  N   . HIS I  1 86  ? 35.875  85.153  38.583 1.00 60.89  ? 80  HIS I N   1 
ATOM   9470  C  CA  . HIS I  1 86  ? 36.051  86.593  38.772 1.00 58.14  ? 80  HIS I CA  1 
ATOM   9471  C  C   . HIS I  1 86  ? 37.535  86.948  38.711 1.00 57.35  ? 80  HIS I C   1 
ATOM   9472  O  O   . HIS I  1 86  ? 38.392  86.122  39.042 1.00 57.47  ? 80  HIS I O   1 
ATOM   9473  C  CB  . HIS I  1 86  ? 35.494  86.996  40.129 1.00 52.34  ? 80  HIS I CB  1 
ATOM   9474  C  CG  . HIS I  1 86  ? 34.042  86.692  40.296 1.00 53.55  ? 80  HIS I CG  1 
ATOM   9475  N  ND1 . HIS I  1 86  ? 33.448  86.560  41.533 1.00 55.75  ? 80  HIS I ND1 1 
ATOM   9476  C  CD2 . HIS I  1 86  ? 33.051  86.550  39.385 1.00 50.29  ? 80  HIS I CD2 1 
ATOM   9477  C  CE1 . HIS I  1 86  ? 32.152  86.353  41.376 1.00 56.47  ? 80  HIS I CE1 1 
ATOM   9478  N  NE2 . HIS I  1 86  ? 31.886  86.343  40.082 1.00 55.56  ? 80  HIS I NE2 1 
ATOM   9479  N  N   . VAL I  1 87  ? 37.853  88.167  38.293 1.00 54.51  ? 81  VAL I N   1 
ATOM   9480  C  CA  . VAL I  1 87  ? 39.257  88.549  38.227 1.00 57.72  ? 81  VAL I CA  1 
ATOM   9481  C  C   . VAL I  1 87  ? 39.883  88.570  39.623 1.00 54.63  ? 81  VAL I C   1 
ATOM   9482  O  O   . VAL I  1 87  ? 41.076  88.307  39.777 1.00 54.42  ? 81  VAL I O   1 
ATOM   9483  C  CB  . VAL I  1 87  ? 39.447  89.934  37.553 1.00 59.52  ? 81  VAL I CB  1 
ATOM   9484  C  CG1 . VAL I  1 87  ? 40.881  90.432  37.765 1.00 56.48  ? 81  VAL I CG1 1 
ATOM   9485  C  CG2 . VAL I  1 87  ? 39.160  89.823  36.058 1.00 52.37  ? 81  VAL I CG2 1 
ATOM   9486  N  N   . GLY I  1 88  ? 39.067  88.856  40.635 1.00 51.32  ? 82  GLY I N   1 
ATOM   9487  C  CA  . GLY I  1 88  ? 39.565  88.920  41.995 1.00 51.87  ? 82  GLY I CA  1 
ATOM   9488  C  C   . GLY I  1 88  ? 39.437  87.664  42.837 1.00 54.70  ? 82  GLY I C   1 
ATOM   9489  O  O   . GLY I  1 88  ? 39.624  87.722  44.056 1.00 56.10  ? 82  GLY I O   1 
ATOM   9490  N  N   . ASP I  1 89  ? 39.119  86.537  42.204 1.00 51.35  ? 83  ASP I N   1 
ATOM   9491  C  CA  . ASP I  1 89  ? 38.983  85.266  42.909 1.00 48.96  ? 83  ASP I CA  1 
ATOM   9492  C  C   . ASP I  1 89  ? 40.376  84.653  43.100 1.00 49.41  ? 83  ASP I C   1 
ATOM   9493  O  O   . ASP I  1 89  ? 41.026  84.235  42.143 1.00 45.59  ? 83  ASP I O   1 
ATOM   9494  C  CB  . ASP I  1 89  ? 38.072  84.318  42.119 1.00 51.71  ? 83  ASP I CB  1 
ATOM   9495  C  CG  . ASP I  1 89  ? 36.648  84.851  41.981 1.00 53.38  ? 83  ASP I CG  1 
ATOM   9496  O  OD1 . ASP I  1 89  ? 36.316  85.845  42.661 1.00 55.83  ? 83  ASP I OD1 1 
ATOM   9497  O  OD2 . ASP I  1 89  ? 35.855  84.283  41.199 1.00 50.73  ? 83  ASP I OD2 1 
ATOM   9498  N  N   . LEU I  1 90  ? 40.837  84.611  44.344 1.00 51.29  ? 84  LEU I N   1 
ATOM   9499  C  CA  . LEU I  1 90  ? 42.160  84.080  44.630 1.00 52.00  ? 84  LEU I CA  1 
ATOM   9500  C  C   . LEU I  1 90  ? 42.113  82.843  45.517 1.00 49.87  ? 84  LEU I C   1 
ATOM   9501  O  O   . LEU I  1 90  ? 43.103  82.465  46.134 1.00 47.50  ? 84  LEU I O   1 
ATOM   9502  C  CB  . LEU I  1 90  ? 43.034  85.174  45.259 1.00 49.07  ? 84  LEU I CB  1 
ATOM   9503  C  CG  . LEU I  1 90  ? 43.254  86.409  44.379 1.00 47.31  ? 84  LEU I CG  1 
ATOM   9504  C  CD1 . LEU I  1 90  ? 44.154  87.399  45.082 1.00 46.67  ? 84  LEU I CD1 1 
ATOM   9505  C  CD2 . LEU I  1 90  ? 43.874  85.991  43.058 1.00 51.83  ? 84  LEU I CD2 1 
ATOM   9506  N  N   . GLY I  1 91  ? 40.951  82.210  45.575 1.00 49.70  ? 85  GLY I N   1 
ATOM   9507  C  CA  . GLY I  1 91  ? 40.821  81.007  46.370 1.00 44.38  ? 85  GLY I CA  1 
ATOM   9508  C  C   . GLY I  1 91  ? 40.920  81.148  47.879 1.00 42.43  ? 85  GLY I C   1 
ATOM   9509  O  O   . GLY I  1 91  ? 40.370  82.072  48.490 1.00 39.20  ? 85  GLY I O   1 
ATOM   9510  N  N   . ASN I  1 92  ? 41.641  80.212  48.482 1.00 31.49  ? 86  ASN I N   1 
ATOM   9511  C  CA  . ASN I  1 92  ? 41.782  80.177  49.921 1.00 34.87  ? 86  ASN I CA  1 
ATOM   9512  C  C   . ASN I  1 92  ? 43.211  80.258  50.415 1.00 33.37  ? 86  ASN I C   1 
ATOM   9513  O  O   . ASN I  1 92  ? 44.149  79.815  49.753 1.00 40.68  ? 86  ASN I O   1 
ATOM   9514  C  CB  . ASN I  1 92  ? 41.194  78.872  50.457 1.00 35.07  ? 86  ASN I CB  1 
ATOM   9515  C  CG  . ASN I  1 92  ? 39.730  78.697  50.122 1.00 39.52  ? 86  ASN I CG  1 
ATOM   9516  O  OD1 . ASN I  1 92  ? 38.855  79.261  50.783 1.00 38.94  ? 86  ASN I OD1 1 
ATOM   9517  N  ND2 . ASN I  1 92  ? 39.453  77.904  49.091 1.00 33.01  ? 86  ASN I ND2 1 
ATOM   9518  N  N   . VAL I  1 93  ? 43.361  80.826  51.599 1.00 27.68  ? 87  VAL I N   1 
ATOM   9519  C  CA  . VAL I  1 93  ? 44.652  80.897  52.249 1.00 29.51  ? 87  VAL I CA  1 
ATOM   9520  C  C   . VAL I  1 93  ? 44.337  80.010  53.430 1.00 35.69  ? 87  VAL I C   1 
ATOM   9521  O  O   . VAL I  1 93  ? 43.153  79.802  53.746 1.00 33.59  ? 87  VAL I O   1 
ATOM   9522  C  CB  . VAL I  1 93  ? 45.012  82.313  52.717 1.00 30.58  ? 87  VAL I CB  1 
ATOM   9523  C  CG1 . VAL I  1 93  ? 45.217  83.214  51.508 1.00 37.98  ? 87  VAL I CG1 1 
ATOM   9524  C  CG2 . VAL I  1 93  ? 43.918  82.866  53.629 1.00 32.13  ? 87  VAL I CG2 1 
ATOM   9525  N  N   . THR I  1 94  ? 45.370  79.485  54.079 1.00 34.97  ? 88  THR I N   1 
ATOM   9526  C  CA  . THR I  1 94  ? 45.170  78.571  55.187 1.00 33.17  ? 88  THR I CA  1 
ATOM   9527  C  C   . THR I  1 94  ? 45.849  79.046  56.464 1.00 37.66  ? 88  THR I C   1 
ATOM   9528  O  O   . THR I  1 94  ? 47.043  79.350  56.472 1.00 35.99  ? 88  THR I O   1 
ATOM   9529  C  CB  . THR I  1 94  ? 45.702  77.180  54.781 1.00 36.55  ? 88  THR I CB  1 
ATOM   9530  O  OG1 . THR I  1 94  ? 45.071  76.781  53.554 1.00 31.05  ? 88  THR I OG1 1 
ATOM   9531  C  CG2 . THR I  1 94  ? 45.439  76.149  55.861 1.00 32.40  ? 88  THR I CG2 1 
ATOM   9532  N  N   . ALA I  1 95  ? 45.089  79.124  57.549 1.00 31.69  ? 89  ALA I N   1 
ATOM   9533  C  CA  . ALA I  1 95  ? 45.677  79.557  58.804 1.00 33.71  ? 89  ALA I CA  1 
ATOM   9534  C  C   . ALA I  1 95  ? 46.021  78.313  59.593 1.00 34.11  ? 89  ALA I C   1 
ATOM   9535  O  O   . ALA I  1 95  ? 45.209  77.389  59.684 1.00 38.98  ? 89  ALA I O   1 
ATOM   9536  C  CB  . ALA I  1 95  ? 44.703  80.432  59.577 1.00 32.71  ? 89  ALA I CB  1 
ATOM   9537  N  N   . ASP I  1 96  ? 47.228  78.287  60.149 1.00 30.61  ? 90  ASP I N   1 
ATOM   9538  C  CA  . ASP I  1 96  ? 47.695  77.145  60.920 1.00 32.55  ? 90  ASP I CA  1 
ATOM   9539  C  C   . ASP I  1 96  ? 47.098  77.128  62.327 1.00 33.88  ? 90  ASP I C   1 
ATOM   9540  O  O   . ASP I  1 96  ? 46.241  77.945  62.649 1.00 33.23  ? 90  ASP I O   1 
ATOM   9541  C  CB  . ASP I  1 96  ? 49.237  77.127  60.965 1.00 31.92  ? 90  ASP I CB  1 
ATOM   9542  C  CG  . ASP I  1 96  ? 49.853  78.362  61.653 1.00 39.49  ? 90  ASP I CG  1 
ATOM   9543  O  OD1 . ASP I  1 96  ? 51.062  78.586  61.435 1.00 38.37  ? 90  ASP I OD1 1 
ATOM   9544  O  OD2 . ASP I  1 96  ? 49.169  79.095  62.411 1.00 32.69  ? 90  ASP I OD2 1 
ATOM   9545  N  N   . LYS I  1 97  ? 47.544  76.198  63.162 1.00 40.53  ? 91  LYS I N   1 
ATOM   9546  C  CA  . LYS I  1 97  ? 47.009  76.092  64.509 1.00 46.18  ? 91  LYS I CA  1 
ATOM   9547  C  C   . LYS I  1 97  ? 47.304  77.346  65.332 1.00 45.69  ? 91  LYS I C   1 
ATOM   9548  O  O   . LYS I  1 97  ? 46.632  77.622  66.322 1.00 44.51  ? 91  LYS I O   1 
ATOM   9549  C  CB  . LYS I  1 97  ? 47.563  74.836  65.199 1.00 47.98  ? 91  LYS I CB  1 
ATOM   9550  C  CG  . LYS I  1 97  ? 48.985  74.957  65.739 1.00 70.05  ? 91  LYS I CG  1 
ATOM   9551  C  CD  . LYS I  1 97  ? 49.491  73.612  66.299 1.00 77.92  ? 91  LYS I CD  1 
ATOM   9552  C  CE  . LYS I  1 97  ? 50.672  73.775  67.265 1.00 77.99  ? 91  LYS I CE  1 
ATOM   9553  N  NZ  . LYS I  1 97  ? 51.802  74.561  66.698 1.00 76.14  ? 91  LYS I NZ  1 
ATOM   9554  N  N   . ASP I  1 98  ? 48.294  78.120  64.906 1.00 43.37  ? 92  ASP I N   1 
ATOM   9555  C  CA  . ASP I  1 98  ? 48.657  79.337  65.621 1.00 43.51  ? 92  ASP I CA  1 
ATOM   9556  C  C   . ASP I  1 98  ? 47.966  80.591  65.093 1.00 41.07  ? 92  ASP I C   1 
ATOM   9557  O  O   . ASP I  1 98  ? 48.397  81.703  65.396 1.00 38.93  ? 92  ASP I O   1 
ATOM   9558  C  CB  . ASP I  1 98  ? 50.171  79.535  65.571 1.00 48.40  ? 92  ASP I CB  1 
ATOM   9559  C  CG  . ASP I  1 98  ? 50.912  78.539  66.427 1.00 53.50  ? 92  ASP I CG  1 
ATOM   9560  O  OD1 . ASP I  1 98  ? 52.037  78.161  66.039 1.00 58.31  ? 92  ASP I OD1 1 
ATOM   9561  O  OD2 . ASP I  1 98  ? 50.376  78.143  67.491 1.00 60.17  ? 92  ASP I OD2 1 
ATOM   9562  N  N   . ALA I  1 99  ? 46.920  80.406  64.287 1.00 38.24  ? 93  ALA I N   1 
ATOM   9563  C  CA  . ALA I  1 99  ? 46.139  81.511  63.725 1.00 32.28  ? 93  ALA I CA  1 
ATOM   9564  C  C   . ALA I  1 99  ? 46.875  82.317  62.662 1.00 37.05  ? 93  ALA I C   1 
ATOM   9565  O  O   . ALA I  1 99  ? 46.439  83.408  62.277 1.00 38.15  ? 93  ALA I O   1 
ATOM   9566  C  CB  . ALA I  1 99  ? 45.679  82.439  64.848 1.00 30.31  ? 93  ALA I CB  1 
ATOM   9567  N  N   . VAL I  1 100 ? 47.988  81.779  62.182 1.00 38.35  ? 94  VAL I N   1 
ATOM   9568  C  CA  . VAL I  1 100 ? 48.783  82.468  61.176 1.00 35.05  ? 94  VAL I CA  1 
ATOM   9569  C  C   . VAL I  1 100 ? 48.628  81.844  59.809 1.00 32.78  ? 94  VAL I C   1 
ATOM   9570  O  O   . VAL I  1 100 ? 48.613  80.627  59.674 1.00 32.89  ? 94  VAL I O   1 
ATOM   9571  C  CB  . VAL I  1 100 ? 50.279  82.449  61.540 1.00 37.83  ? 94  VAL I CB  1 
ATOM   9572  C  CG1 . VAL I  1 100 ? 51.073  83.194  60.477 1.00 32.98  ? 94  VAL I CG1 1 
ATOM   9573  C  CG2 . VAL I  1 100 ? 50.484  83.062  62.926 1.00 24.57  ? 94  VAL I CG2 1 
ATOM   9574  N  N   . ALA I  1 101 ? 48.503  82.689  58.795 1.00 37.63  ? 95  ALA I N   1 
ATOM   9575  C  CA  . ALA I  1 101 ? 48.376  82.219  57.424 1.00 39.49  ? 95  ALA I CA  1 
ATOM   9576  C  C   . ALA I  1 101 ? 49.473  82.868  56.602 1.00 37.75  ? 95  ALA I C   1 
ATOM   9577  O  O   . ALA I  1 101 ? 49.512  84.095  56.439 1.00 33.05  ? 95  ALA I O   1 
ATOM   9578  C  CB  . ALA I  1 101 ? 47.011  82.576  56.852 1.00 42.41  ? 95  ALA I CB  1 
ATOM   9579  N  N   . ASP I  1 102 ? 50.383  82.035  56.116 1.00 41.43  ? 96  ASP I N   1 
ATOM   9580  C  CA  . ASP I  1 102 ? 51.485  82.504  55.295 1.00 42.87  ? 96  ASP I CA  1 
ATOM   9581  C  C   . ASP I  1 102 ? 51.014  82.399  53.867 1.00 40.28  ? 96  ASP I C   1 
ATOM   9582  O  O   . ASP I  1 102 ? 50.841  81.314  53.316 1.00 46.46  ? 96  ASP I O   1 
ATOM   9583  C  CB  . ASP I  1 102 ? 52.730  81.658  55.550 1.00 49.79  ? 96  ASP I CB  1 
ATOM   9584  C  CG  . ASP I  1 102 ? 53.314  81.902  56.937 1.00 62.55  ? 96  ASP I CG  1 
ATOM   9585  O  OD1 . ASP I  1 102 ? 53.592  80.922  57.664 1.00 73.58  ? 96  ASP I OD1 1 
ATOM   9586  O  OD2 . ASP I  1 102 ? 53.494  83.085  57.304 1.00 66.67  ? 96  ASP I OD2 1 
ATOM   9587  N  N   . VAL I  1 103 ? 50.778  83.558  53.283 1.00 33.92  ? 97  VAL I N   1 
ATOM   9588  C  CA  . VAL I  1 103 ? 50.286  83.646  51.929 1.00 30.17  ? 97  VAL I CA  1 
ATOM   9589  C  C   . VAL I  1 103 ? 51.372  83.598  50.863 1.00 27.65  ? 97  VAL I C   1 
ATOM   9590  O  O   . VAL I  1 103 ? 52.377  84.297  50.950 1.00 31.68  ? 97  VAL I O   1 
ATOM   9591  C  CB  . VAL I  1 103 ? 49.467  84.941  51.769 1.00 27.91  ? 97  VAL I CB  1 
ATOM   9592  C  CG1 . VAL I  1 103 ? 49.147  85.182  50.306 1.00 20.09  ? 97  VAL I CG1 1 
ATOM   9593  C  CG2 . VAL I  1 103 ? 48.191  84.837  52.601 1.00 28.10  ? 97  VAL I CG2 1 
ATOM   9594  N  N   . SER I  1 104 ? 51.154  82.769  49.852 1.00 29.26  ? 98  SER I N   1 
ATOM   9595  C  CA  . SER I  1 104 ? 52.094  82.640  48.748 1.00 37.36  ? 98  SER I CA  1 
ATOM   9596  C  C   . SER I  1 104 ? 51.342  82.158  47.520 1.00 37.98  ? 98  SER I C   1 
ATOM   9597  O  O   . SER I  1 104 ? 51.125  80.959  47.308 1.00 38.10  ? 98  SER I O   1 
ATOM   9598  C  CB  . SER I  1 104 ? 53.217  81.670  49.087 1.00 33.13  ? 98  SER I CB  1 
ATOM   9599  O  OG  . SER I  1 104 ? 54.235  81.808  48.118 1.00 34.73  ? 98  SER I OG  1 
ATOM   9600  N  N   . ILE I  1 105 ? 50.956  83.130  46.713 1.00 39.36  ? 99  ILE I N   1 
ATOM   9601  C  CA  . ILE I  1 105 ? 50.182  82.898  45.522 1.00 38.86  ? 99  ILE I CA  1 
ATOM   9602  C  C   . ILE I  1 105 ? 50.826  83.566  44.321 1.00 42.62  ? 99  ILE I C   1 
ATOM   9603  O  O   . ILE I  1 105 ? 51.585  84.523  44.445 1.00 38.71  ? 99  ILE I O   1 
ATOM   9604  C  CB  . ILE I  1 105 ? 48.745  83.475  45.727 1.00 42.66  ? 99  ILE I CB  1 
ATOM   9605  C  CG1 . ILE I  1 105 ? 47.989  82.612  46.733 1.00 45.05  ? 99  ILE I CG1 1 
ATOM   9606  C  CG2 . ILE I  1 105 ? 47.982  83.585  44.398 1.00 38.36  ? 99  ILE I CG2 1 
ATOM   9607  C  CD1 . ILE I  1 105 ? 46.633  83.164  47.089 1.00 49.87  ? 99  ILE I CD1 1 
ATOM   9608  N  N   . GLU I  1 106 ? 50.528  83.025  43.154 1.00 46.56  ? 100 GLU I N   1 
ATOM   9609  C  CA  . GLU I  1 106 ? 50.995  83.582  41.909 1.00 52.15  ? 100 GLU I CA  1 
ATOM   9610  C  C   . GLU I  1 106 ? 49.726  83.526  41.081 1.00 52.82  ? 100 GLU I C   1 
ATOM   9611  O  O   . GLU I  1 106 ? 49.063  82.493  41.028 1.00 49.41  ? 100 GLU I O   1 
ATOM   9612  C  CB  . GLU I  1 106 ? 52.097  82.724  41.288 1.00 59.23  ? 100 GLU I CB  1 
ATOM   9613  C  CG  . GLU I  1 106 ? 52.661  83.321  40.003 1.00 68.28  ? 100 GLU I CG  1 
ATOM   9614  C  CD  . GLU I  1 106 ? 54.176  83.328  39.976 1.00 72.27  ? 100 GLU I CD  1 
ATOM   9615  O  OE1 . GLU I  1 106 ? 54.784  83.705  41.003 1.00 71.66  ? 100 GLU I OE1 1 
ATOM   9616  O  OE2 . GLU I  1 106 ? 54.754  82.967  38.927 1.00 71.52  ? 100 GLU I OE2 1 
ATOM   9617  N  N   . ASP I  1 107 ? 49.356  84.643  40.468 1.00 55.42  ? 101 ASP I N   1 
ATOM   9618  C  CA  . ASP I  1 107 ? 48.141  84.675  39.677 1.00 51.30  ? 101 ASP I CA  1 
ATOM   9619  C  C   . ASP I  1 107 ? 48.391  85.438  38.396 1.00 50.61  ? 101 ASP I C   1 
ATOM   9620  O  O   . ASP I  1 107 ? 49.199  86.360  38.361 1.00 51.51  ? 101 ASP I O   1 
ATOM   9621  C  CB  . ASP I  1 107 ? 47.024  85.313  40.492 1.00 50.38  ? 101 ASP I CB  1 
ATOM   9622  C  CG  . ASP I  1 107 ? 45.666  85.103  39.877 1.00 52.99  ? 101 ASP I CG  1 
ATOM   9623  O  OD1 . ASP I  1 107 ? 45.197  86.005  39.154 1.00 50.79  ? 101 ASP I OD1 1 
ATOM   9624  O  OD2 . ASP I  1 107 ? 45.071  84.032  40.112 1.00 45.33  ? 101 ASP I OD2 1 
ATOM   9625  N  N   . SER I  1 108 ? 47.705  85.039  37.333 1.00 56.02  ? 102 SER I N   1 
ATOM   9626  C  CA  . SER I  1 108 ? 47.891  85.680  36.038 1.00 59.46  ? 102 SER I CA  1 
ATOM   9627  C  C   . SER I  1 108 ? 46.650  86.398  35.526 1.00 54.99  ? 102 SER I C   1 
ATOM   9628  O  O   . SER I  1 108 ? 46.678  86.991  34.450 1.00 58.77  ? 102 SER I O   1 
ATOM   9629  C  CB  . SER I  1 108 ? 48.362  84.648  35.005 1.00 60.30  ? 102 SER I CB  1 
ATOM   9630  O  OG  . SER I  1 108 ? 47.467  83.550  34.938 1.00 68.76  ? 102 SER I OG  1 
ATOM   9631  N  N   . VAL I  1 109 ? 45.563  86.339  36.287 1.00 49.21  ? 103 VAL I N   1 
ATOM   9632  C  CA  . VAL I  1 109 ? 44.336  87.017  35.899 1.00 48.81  ? 103 VAL I CA  1 
ATOM   9633  C  C   . VAL I  1 109 ? 44.334  88.438  36.472 1.00 53.27  ? 103 VAL I C   1 
ATOM   9634  O  O   . VAL I  1 109 ? 43.927  89.381  35.796 1.00 49.87  ? 103 VAL I O   1 
ATOM   9635  C  CB  . VAL I  1 109 ? 43.110  86.256  36.393 1.00 45.72  ? 103 VAL I CB  1 
ATOM   9636  C  CG1 . VAL I  1 109 ? 41.854  87.033  36.088 1.00 40.21  ? 103 VAL I CG1 1 
ATOM   9637  C  CG2 . VAL I  1 109 ? 43.066  84.906  35.727 1.00 44.35  ? 103 VAL I CG2 1 
ATOM   9638  N  N   . ILE I  1 110 ? 44.777  88.592  37.719 1.00 53.00  ? 104 ILE I N   1 
ATOM   9639  C  CA  . ILE I  1 110 ? 44.854  89.918  38.320 1.00 49.25  ? 104 ILE I CA  1 
ATOM   9640  C  C   . ILE I  1 110 ? 46.097  90.542  37.707 1.00 52.45  ? 104 ILE I C   1 
ATOM   9641  O  O   . ILE I  1 110 ? 46.930  89.832  37.131 1.00 52.27  ? 104 ILE I O   1 
ATOM   9642  C  CB  . ILE I  1 110 ? 45.040  89.881  39.851 1.00 47.05  ? 104 ILE I CB  1 
ATOM   9643  C  CG1 . ILE I  1 110 ? 46.338  89.147  40.203 1.00 45.31  ? 104 ILE I CG1 1 
ATOM   9644  C  CG2 . ILE I  1 110 ? 43.815  89.263  40.514 1.00 43.11  ? 104 ILE I CG2 1 
ATOM   9645  C  CD1 . ILE I  1 110 ? 46.620  89.090  41.694 1.00 47.29  ? 104 ILE I CD1 1 
ATOM   9646  N  N   . SER I  1 111 ? 46.221  91.860  37.830 1.00 50.31  ? 105 SER I N   1 
ATOM   9647  C  CA  . SER I  1 111 ? 47.361  92.578  37.269 1.00 49.62  ? 105 SER I CA  1 
ATOM   9648  C  C   . SER I  1 111 ? 47.557  93.890  38.024 1.00 48.81  ? 105 SER I C   1 
ATOM   9649  O  O   . SER I  1 111 ? 46.693  94.304  38.802 1.00 39.61  ? 105 SER I O   1 
ATOM   9650  C  CB  . SER I  1 111 ? 47.105  92.865  35.781 1.00 50.52  ? 105 SER I CB  1 
ATOM   9651  O  OG  . SER I  1 111 ? 48.201  93.521  35.170 1.00 52.78  ? 105 SER I OG  1 
ATOM   9652  N  N   . LEU I  1 112 ? 48.695  94.539  37.808 1.00 48.17  ? 106 LEU I N   1 
ATOM   9653  C  CA  . LEU I  1 112 ? 48.945  95.808  38.468 1.00 53.26  ? 106 LEU I CA  1 
ATOM   9654  C  C   . LEU I  1 112 ? 48.906  96.929  37.437 1.00 55.78  ? 106 LEU I C   1 
ATOM   9655  O  O   . LEU I  1 112 ? 49.486  97.993  37.630 1.00 57.31  ? 106 LEU I O   1 
ATOM   9656  C  CB  . LEU I  1 112 ? 50.287  95.784  39.211 1.00 50.92  ? 106 LEU I CB  1 
ATOM   9657  C  CG  . LEU I  1 112 ? 50.404  94.787  40.374 1.00 48.27  ? 106 LEU I CG  1 
ATOM   9658  C  CD1 . LEU I  1 112 ? 51.645  95.088  41.199 1.00 41.61  ? 106 LEU I CD1 1 
ATOM   9659  C  CD2 . LEU I  1 112 ? 49.172  94.869  41.248 1.00 45.41  ? 106 LEU I CD2 1 
ATOM   9660  N  N   . SER I  1 113 ? 48.202  96.665  36.340 1.00 61.84  ? 107 SER I N   1 
ATOM   9661  C  CA  . SER I  1 113 ? 48.024  97.614  35.242 1.00 65.97  ? 107 SER I CA  1 
ATOM   9662  C  C   . SER I  1 113 ? 46.966  97.024  34.323 1.00 67.78  ? 107 SER I C   1 
ATOM   9663  O  O   . SER I  1 113 ? 46.610  95.853  34.455 1.00 72.52  ? 107 SER I O   1 
ATOM   9664  C  CB  . SER I  1 113 ? 49.326  97.805  34.459 1.00 64.17  ? 107 SER I CB  1 
ATOM   9665  O  OG  . SER I  1 113 ? 49.687  96.626  33.765 1.00 69.47  ? 107 SER I OG  1 
ATOM   9666  N  N   . GLY I  1 114 ? 46.458  97.827  33.398 1.00 67.05  ? 108 GLY I N   1 
ATOM   9667  C  CA  . GLY I  1 114 ? 45.446  97.321  32.487 1.00 66.46  ? 108 GLY I CA  1 
ATOM   9668  C  C   . GLY I  1 114 ? 44.057  97.307  33.093 1.00 67.36  ? 108 GLY I C   1 
ATOM   9669  O  O   . GLY I  1 114 ? 43.863  97.730  34.234 1.00 63.33  ? 108 GLY I O   1 
ATOM   9670  N  N   . ASP I  1 115 ? 43.091  96.807  32.329 1.00 71.01  ? 109 ASP I N   1 
ATOM   9671  C  CA  . ASP I  1 115 ? 41.701  96.750  32.770 1.00 76.42  ? 109 ASP I CA  1 
ATOM   9672  C  C   . ASP I  1 115 ? 41.495  95.862  33.985 1.00 76.15  ? 109 ASP I C   1 
ATOM   9673  O  O   . ASP I  1 115 ? 40.448  95.925  34.632 1.00 73.98  ? 109 ASP I O   1 
ATOM   9674  C  CB  . ASP I  1 115 ? 40.805  96.249  31.634 1.00 85.43  ? 109 ASP I CB  1 
ATOM   9675  C  CG  . ASP I  1 115 ? 41.013  97.022  30.345 1.00 92.89  ? 109 ASP I CG  1 
ATOM   9676  O  OD1 . ASP I  1 115 ? 40.962  98.271  30.382 1.00 96.29  ? 109 ASP I OD1 1 
ATOM   9677  O  OD2 . ASP I  1 115 ? 41.222  96.379  29.293 1.00 96.78  ? 109 ASP I OD2 1 
ATOM   9678  N  N   . HIS I  1 116 ? 42.494  95.033  34.281 1.00 77.72  ? 110 HIS I N   1 
ATOM   9679  C  CA  . HIS I  1 116 ? 42.433  94.116  35.414 1.00 75.10  ? 110 HIS I CA  1 
ATOM   9680  C  C   . HIS I  1 116 ? 43.247  94.596  36.614 1.00 71.65  ? 110 HIS I C   1 
ATOM   9681  O  O   . HIS I  1 116 ? 43.453  93.846  37.568 1.00 71.69  ? 110 HIS I O   1 
ATOM   9682  C  CB  . HIS I  1 116 ? 42.920  92.732  34.985 1.00 79.74  ? 110 HIS I CB  1 
ATOM   9683  C  CG  . HIS I  1 116 ? 41.995  92.031  34.038 1.00 83.64  ? 110 HIS I CG  1 
ATOM   9684  N  ND1 . HIS I  1 116 ? 42.283  90.797  33.493 1.00 82.80  ? 110 HIS I ND1 1 
ATOM   9685  C  CD2 . HIS I  1 116 ? 40.780  92.380  33.554 1.00 84.44  ? 110 HIS I CD2 1 
ATOM   9686  C  CE1 . HIS I  1 116 ? 41.285  90.417  32.717 1.00 82.78  ? 110 HIS I CE1 1 
ATOM   9687  N  NE2 . HIS I  1 116 ? 40.360  91.359  32.736 1.00 85.93  ? 110 HIS I NE2 1 
ATOM   9688  N  N   . CYS I  1 117 ? 43.707  95.843  36.556 1.00 64.68  ? 111 CYS I N   1 
ATOM   9689  C  CA  . CYS I  1 117 ? 44.489  96.443  37.632 1.00 54.25  ? 111 CYS I CA  1 
ATOM   9690  C  C   . CYS I  1 117 ? 43.690  96.388  38.933 1.00 50.16  ? 111 CYS I C   1 
ATOM   9691  O  O   . CYS I  1 117 ? 42.543  96.818  38.984 1.00 47.79  ? 111 CYS I O   1 
ATOM   9692  C  CB  . CYS I  1 117 ? 44.816  97.892  37.274 1.00 55.79  ? 111 CYS I CB  1 
ATOM   9693  S  SG  . CYS I  1 117 ? 45.833  98.797  38.460 1.00 61.00  ? 111 CYS I SG  1 
ATOM   9694  N  N   . ILE I  1 118 ? 44.297  95.852  39.983 1.00 48.94  ? 112 ILE I N   1 
ATOM   9695  C  CA  . ILE I  1 118 ? 43.626  95.743  41.269 1.00 46.19  ? 112 ILE I CA  1 
ATOM   9696  C  C   . ILE I  1 118 ? 44.022  96.863  42.228 1.00 46.71  ? 112 ILE I C   1 
ATOM   9697  O  O   . ILE I  1 118 ? 43.487  96.962  43.343 1.00 42.48  ? 112 ILE I O   1 
ATOM   9698  C  CB  . ILE I  1 118 ? 43.927  94.392  41.937 1.00 46.65  ? 112 ILE I CB  1 
ATOM   9699  C  CG1 . ILE I  1 118 ? 45.439  94.146  41.965 1.00 42.46  ? 112 ILE I CG1 1 
ATOM   9700  C  CG2 . ILE I  1 118 ? 43.190  93.292  41.206 1.00 48.49  ? 112 ILE I CG2 1 
ATOM   9701  C  CD1 . ILE I  1 118 ? 45.855  92.949  42.810 1.00 38.08  ? 112 ILE I CD1 1 
ATOM   9702  N  N   . ILE I  1 119 ? 44.968  97.696  41.801 1.00 40.52  ? 113 ILE I N   1 
ATOM   9703  C  CA  . ILE I  1 119 ? 45.398  98.816  42.627 1.00 41.49  ? 113 ILE I CA  1 
ATOM   9704  C  C   . ILE I  1 119 ? 44.198  99.733  42.814 1.00 40.45  ? 113 ILE I C   1 
ATOM   9705  O  O   . ILE I  1 119 ? 43.422  99.976  41.883 1.00 33.42  ? 113 ILE I O   1 
ATOM   9706  C  CB  . ILE I  1 119 ? 46.540  99.611  41.960 1.00 48.38  ? 113 ILE I CB  1 
ATOM   9707  C  CG1 . ILE I  1 119 ? 47.770  98.719  41.815 1.00 47.36  ? 113 ILE I CG1 1 
ATOM   9708  C  CG2 . ILE I  1 119 ? 46.891  100.841 42.805 1.00 48.18  ? 113 ILE I CG2 1 
ATOM   9709  C  CD1 . ILE I  1 119 ? 48.927  99.399  41.175 1.00 52.44  ? 113 ILE I CD1 1 
ATOM   9710  N  N   . GLY I  1 120 ? 44.038  100.248 44.020 1.00 38.74  ? 114 GLY I N   1 
ATOM   9711  C  CA  . GLY I  1 120 ? 42.905  101.113 44.268 1.00 40.36  ? 114 GLY I CA  1 
ATOM   9712  C  C   . GLY I  1 120 ? 41.670  100.321 44.658 1.00 40.74  ? 114 GLY I C   1 
ATOM   9713  O  O   . GLY I  1 120 ? 40.631  100.906 44.952 1.00 37.96  ? 114 GLY I O   1 
ATOM   9714  N  N   . ARG I  1 121 ? 41.765  98.992  44.656 1.00 42.09  ? 115 ARG I N   1 
ATOM   9715  C  CA  . ARG I  1 121 ? 40.626  98.171  45.052 1.00 41.46  ? 115 ARG I CA  1 
ATOM   9716  C  C   . ARG I  1 121 ? 40.879  97.567  46.434 1.00 40.29  ? 115 ARG I C   1 
ATOM   9717  O  O   . ARG I  1 121 ? 41.888  97.879  47.060 1.00 40.07  ? 115 ARG I O   1 
ATOM   9718  C  CB  . ARG I  1 121 ? 40.346  97.113  43.989 1.00 43.36  ? 115 ARG I CB  1 
ATOM   9719  C  CG  . ARG I  1 121 ? 39.879  97.741  42.672 1.00 37.24  ? 115 ARG I CG  1 
ATOM   9720  C  CD  . ARG I  1 121 ? 39.762  96.718  41.570 1.00 42.70  ? 115 ARG I CD  1 
ATOM   9721  N  NE  . ARG I  1 121 ? 39.630  97.317  40.240 1.00 42.91  ? 115 ARG I NE  1 
ATOM   9722  C  CZ  . ARG I  1 121 ? 38.648  98.134  39.865 1.00 39.92  ? 115 ARG I CZ  1 
ATOM   9723  N  NH1 . ARG I  1 121 ? 38.622  98.607  38.628 1.00 34.38  ? 115 ARG I NH1 1 
ATOM   9724  N  NH2 . ARG I  1 121 ? 37.698  98.487  40.723 1.00 37.28  ? 115 ARG I NH2 1 
ATOM   9725  N  N   . THR I  1 122 ? 39.981  96.715  46.915 1.00 41.41  ? 116 THR I N   1 
ATOM   9726  C  CA  . THR I  1 122 ? 40.125  96.163  48.266 1.00 45.39  ? 116 THR I CA  1 
ATOM   9727  C  C   . THR I  1 122 ? 40.452  94.678  48.394 1.00 43.83  ? 116 THR I C   1 
ATOM   9728  O  O   . THR I  1 122 ? 39.853  93.845  47.723 1.00 41.31  ? 116 THR I O   1 
ATOM   9729  C  CB  . THR I  1 122 ? 38.829  96.442  49.095 1.00 47.26  ? 116 THR I CB  1 
ATOM   9730  O  OG1 . THR I  1 122 ? 38.586  97.854  49.122 1.00 48.61  ? 116 THR I OG1 1 
ATOM   9731  C  CG2 . THR I  1 122 ? 38.959  95.916  50.548 1.00 36.78  ? 116 THR I CG2 1 
ATOM   9732  N  N   . LEU I  1 123 ? 41.395  94.344  49.272 1.00 41.57  ? 117 LEU I N   1 
ATOM   9733  C  CA  . LEU I  1 123 ? 41.735  92.938  49.487 1.00 37.32  ? 117 LEU I CA  1 
ATOM   9734  C  C   . LEU I  1 123 ? 40.919  92.486  50.685 1.00 37.05  ? 117 LEU I C   1 
ATOM   9735  O  O   . LEU I  1 123 ? 40.899  93.154  51.717 1.00 32.49  ? 117 LEU I O   1 
ATOM   9736  C  CB  . LEU I  1 123 ? 43.225  92.752  49.789 1.00 34.11  ? 117 LEU I CB  1 
ATOM   9737  C  CG  . LEU I  1 123 ? 43.698  91.296  49.925 1.00 32.19  ? 117 LEU I CG  1 
ATOM   9738  C  CD1 . LEU I  1 123 ? 43.402  90.530  48.638 1.00 35.85  ? 117 LEU I CD1 1 
ATOM   9739  C  CD2 . LEU I  1 123 ? 45.174  91.262  50.213 1.00 27.80  ? 117 LEU I CD2 1 
ATOM   9740  N  N   . VAL I  1 124 ? 40.232  91.360  50.551 1.00 35.83  ? 118 VAL I N   1 
ATOM   9741  C  CA  . VAL I  1 124 ? 39.420  90.883  51.651 1.00 34.91  ? 118 VAL I CA  1 
ATOM   9742  C  C   . VAL I  1 124 ? 39.682  89.441  51.998 1.00 31.07  ? 118 VAL I C   1 
ATOM   9743  O  O   . VAL I  1 124 ? 39.782  88.592  51.119 1.00 31.38  ? 118 VAL I O   1 
ATOM   9744  C  CB  . VAL I  1 124 ? 37.906  91.015  51.349 1.00 36.82  ? 118 VAL I CB  1 
ATOM   9745  C  CG1 . VAL I  1 124 ? 37.093  90.561  52.573 1.00 33.34  ? 118 VAL I CG1 1 
ATOM   9746  C  CG2 . VAL I  1 124 ? 37.568  92.448  50.973 1.00 23.31  ? 118 VAL I CG2 1 
ATOM   9747  N  N   . VAL I  1 125 ? 39.806  89.177  53.293 1.00 29.11  ? 119 VAL I N   1 
ATOM   9748  C  CA  . VAL I  1 125 ? 39.987  87.822  53.775 1.00 30.42  ? 119 VAL I CA  1 
ATOM   9749  C  C   . VAL I  1 125 ? 38.668  87.483  54.496 1.00 37.99  ? 119 VAL I C   1 
ATOM   9750  O  O   . VAL I  1 125 ? 38.238  88.191  55.422 1.00 30.37  ? 119 VAL I O   1 
ATOM   9751  C  CB  . VAL I  1 125 ? 41.201  87.701  54.727 1.00 30.41  ? 119 VAL I CB  1 
ATOM   9752  C  CG1 . VAL I  1 125 ? 41.113  88.731  55.852 1.00 30.27  ? 119 VAL I CG1 1 
ATOM   9753  C  CG2 . VAL I  1 125 ? 41.258  86.277  55.291 1.00 29.67  ? 119 VAL I CG2 1 
ATOM   9754  N  N   . HIS I  1 126 ? 38.021  86.407  54.054 1.00 38.04  ? 120 HIS I N   1 
ATOM   9755  C  CA  . HIS I  1 126 ? 36.730  86.002  54.605 1.00 40.50  ? 120 HIS I CA  1 
ATOM   9756  C  C   . HIS I  1 126 ? 36.707  85.065  55.809 1.00 38.76  ? 120 HIS I C   1 
ATOM   9757  O  O   . HIS I  1 126 ? 37.716  84.488  56.199 1.00 43.08  ? 120 HIS I O   1 
ATOM   9758  C  CB  . HIS I  1 126 ? 35.876  85.447  53.464 1.00 29.47  ? 120 HIS I CB  1 
ATOM   9759  C  CG  . HIS I  1 126 ? 35.520  86.480  52.439 1.00 39.83  ? 120 HIS I CG  1 
ATOM   9760  N  ND1 . HIS I  1 126 ? 34.325  87.171  52.458 1.00 36.69  ? 120 HIS I ND1 1 
ATOM   9761  C  CD2 . HIS I  1 126 ? 36.203  86.940  51.361 1.00 35.72  ? 120 HIS I CD2 1 
ATOM   9762  C  CE1 . HIS I  1 126 ? 34.283  88.001  51.429 1.00 37.70  ? 120 HIS I CE1 1 
ATOM   9763  N  NE2 . HIS I  1 126 ? 35.408  87.880  50.746 1.00 32.03  ? 120 HIS I NE2 1 
ATOM   9764  N  N   . GLU I  1 127 ? 35.527  84.937  56.398 1.00 48.08  ? 121 GLU I N   1 
ATOM   9765  C  CA  . GLU I  1 127 ? 35.303  84.113  57.582 1.00 53.32  ? 121 GLU I CA  1 
ATOM   9766  C  C   . GLU I  1 127 ? 35.413  82.615  57.333 1.00 50.98  ? 121 GLU I C   1 
ATOM   9767  O  O   . GLU I  1 127 ? 35.997  81.887  58.132 1.00 48.97  ? 121 GLU I O   1 
ATOM   9768  C  CB  . GLU I  1 127 ? 33.914  84.414  58.141 1.00 58.50  ? 121 GLU I CB  1 
ATOM   9769  C  CG  . GLU I  1 127 ? 33.544  83.652  59.393 1.00 65.36  ? 121 GLU I CG  1 
ATOM   9770  C  CD  . GLU I  1 127 ? 32.049  83.705  59.671 1.00 73.72  ? 121 GLU I CD  1 
ATOM   9771  O  OE1 . GLU I  1 127 ? 31.644  83.340  60.797 1.00 73.61  ? 121 GLU I OE1 1 
ATOM   9772  O  OE2 . GLU I  1 127 ? 31.280  84.101  58.759 1.00 70.34  ? 121 GLU I OE2 1 
ATOM   9773  N  N   . LYS I  1 128 ? 34.835  82.162  56.228 1.00 48.85  ? 122 LYS I N   1 
ATOM   9774  C  CA  . LYS I  1 128 ? 34.833  80.743  55.895 1.00 50.76  ? 122 LYS I CA  1 
ATOM   9775  C  C   . LYS I  1 128 ? 35.650  80.456  54.653 1.00 49.26  ? 122 LYS I C   1 
ATOM   9776  O  O   . LYS I  1 128 ? 36.168  81.365  53.998 1.00 49.70  ? 122 LYS I O   1 
ATOM   9777  C  CB  . LYS I  1 128 ? 33.403  80.258  55.631 1.00 55.16  ? 122 LYS I CB  1 
ATOM   9778  C  CG  . LYS I  1 128 ? 32.379  80.579  56.705 1.00 62.03  ? 122 LYS I CG  1 
ATOM   9779  C  CD  . LYS I  1 128 ? 30.975  80.220  56.221 1.00 67.71  ? 122 LYS I CD  1 
ATOM   9780  C  CE  . LYS I  1 128 ? 29.924  80.477  57.292 1.00 70.87  ? 122 LYS I CE  1 
ATOM   9781  N  NZ  . LYS I  1 128 ? 28.562  80.118  56.819 1.00 75.48  ? 122 LYS I NZ  1 
ATOM   9782  N  N   . ALA I  1 129 ? 35.750  79.173  54.329 1.00 44.77  ? 123 ALA I N   1 
ATOM   9783  C  CA  . ALA I  1 129 ? 36.471  78.759  53.142 1.00 44.54  ? 123 ALA I CA  1 
ATOM   9784  C  C   . ALA I  1 129 ? 35.616  79.122  51.924 1.00 47.50  ? 123 ALA I C   1 
ATOM   9785  O  O   . ALA I  1 129 ? 34.403  79.328  52.022 1.00 43.89  ? 123 ALA I O   1 
ATOM   9786  C  CB  . ALA I  1 129 ? 36.724  77.271  53.186 1.00 33.01  ? 123 ALA I CB  1 
ATOM   9787  N  N   . ASP I  1 130 ? 36.265  79.215  50.778 1.00 46.39  ? 124 ASP I N   1 
ATOM   9788  C  CA  . ASP I  1 130 ? 35.595  79.542  49.541 1.00 45.54  ? 124 ASP I CA  1 
ATOM   9789  C  C   . ASP I  1 130 ? 35.346  78.208  48.862 1.00 49.80  ? 124 ASP I C   1 
ATOM   9790  O  O   . ASP I  1 130 ? 36.271  77.421  48.685 1.00 50.21  ? 124 ASP I O   1 
ATOM   9791  C  CB  . ASP I  1 130 ? 36.521  80.421  48.702 1.00 51.12  ? 124 ASP I CB  1 
ATOM   9792  C  CG  . ASP I  1 130 ? 35.948  80.759  47.345 1.00 52.00  ? 124 ASP I CG  1 
ATOM   9793  O  OD1 . ASP I  1 130 ? 36.607  81.532  46.618 1.00 40.00  ? 124 ASP I OD1 1 
ATOM   9794  O  OD2 . ASP I  1 130 ? 34.855  80.254  47.006 1.00 51.26  ? 124 ASP I OD2 1 
ATOM   9795  N  N   . ASP I  1 131 ? 34.106  77.932  48.485 1.00 51.67  ? 125 ASP I N   1 
ATOM   9796  C  CA  . ASP I  1 131 ? 33.834  76.655  47.845 1.00 53.65  ? 125 ASP I CA  1 
ATOM   9797  C  C   . ASP I  1 131 ? 34.155  76.671  46.357 1.00 53.68  ? 125 ASP I C   1 
ATOM   9798  O  O   . ASP I  1 131 ? 33.836  75.730  45.636 1.00 54.45  ? 125 ASP I O   1 
ATOM   9799  C  CB  . ASP I  1 131 ? 32.382  76.225  48.092 1.00 59.42  ? 125 ASP I CB  1 
ATOM   9800  C  CG  . ASP I  1 131 ? 31.379  77.108  47.392 1.00 57.38  ? 125 ASP I CG  1 
ATOM   9801  O  OD1 . ASP I  1 131 ? 30.230  77.180  47.883 1.00 53.95  ? 125 ASP I OD1 1 
ATOM   9802  O  OD2 . ASP I  1 131 ? 31.730  77.708  46.353 1.00 52.74  ? 125 ASP I OD2 1 
ATOM   9803  N  N   . LEU I  1 132 ? 34.797  77.748  45.912 1.00 53.62  ? 126 LEU I N   1 
ATOM   9804  C  CA  . LEU I  1 132 ? 35.213  77.901  44.522 1.00 54.64  ? 126 LEU I CA  1 
ATOM   9805  C  C   . LEU I  1 132 ? 34.086  77.777  43.492 1.00 58.19  ? 126 LEU I C   1 
ATOM   9806  O  O   . LEU I  1 132 ? 34.329  77.450  42.322 1.00 53.89  ? 126 LEU I O   1 
ATOM   9807  C  CB  . LEU I  1 132 ? 36.310  76.878  44.213 1.00 54.54  ? 126 LEU I CB  1 
ATOM   9808  C  CG  . LEU I  1 132 ? 37.352  76.671  45.320 1.00 57.58  ? 126 LEU I CG  1 
ATOM   9809  C  CD1 . LEU I  1 132 ? 38.459  75.765  44.804 1.00 53.80  ? 126 LEU I CD1 1 
ATOM   9810  C  CD2 . LEU I  1 132 ? 37.928  78.012  45.763 1.00 55.13  ? 126 LEU I CD2 1 
ATOM   9811  N  N   . GLY I  1 133 ? 32.857  78.048  43.921 1.00 59.30  ? 127 GLY I N   1 
ATOM   9812  C  CA  . GLY I  1 133 ? 31.729  77.953  43.011 1.00 69.34  ? 127 GLY I CA  1 
ATOM   9813  C  C   . GLY I  1 133 ? 31.402  76.529  42.586 1.00 75.01  ? 127 GLY I C   1 
ATOM   9814  O  O   . GLY I  1 133 ? 31.263  76.246  41.394 1.00 75.11  ? 127 GLY I O   1 
ATOM   9815  N  N   . LYS I  1 134 ? 31.287  75.635  43.566 1.00 78.60  ? 128 LYS I N   1 
ATOM   9816  C  CA  . LYS I  1 134 ? 30.968  74.223  43.332 1.00 81.02  ? 128 LYS I CA  1 
ATOM   9817  C  C   . LYS I  1 134 ? 30.184  73.740  44.552 1.00 85.04  ? 128 LYS I C   1 
ATOM   9818  O  O   . LYS I  1 134 ? 30.214  72.556  44.895 1.00 85.35  ? 128 LYS I O   1 
ATOM   9819  C  CB  . LYS I  1 134 ? 32.247  73.382  43.207 1.00 76.71  ? 128 LYS I CB  1 
ATOM   9820  C  CG  . LYS I  1 134 ? 33.269  73.865  42.188 1.00 78.09  ? 128 LYS I CG  1 
ATOM   9821  C  CD  . LYS I  1 134 ? 34.547  73.035  42.284 1.00 78.88  ? 128 LYS I CD  1 
ATOM   9822  C  CE  . LYS I  1 134 ? 35.660  73.580  41.400 1.00 80.46  ? 128 LYS I CE  1 
ATOM   9823  N  NZ  . LYS I  1 134 ? 35.327  73.509  39.950 1.00 80.26  ? 128 LYS I NZ  1 
ATOM   9824  N  N   . GLY I  1 135 ? 29.488  74.665  45.207 1.00 86.95  ? 129 GLY I N   1 
ATOM   9825  C  CA  . GLY I  1 135 ? 28.735  74.320  46.400 1.00 92.41  ? 129 GLY I CA  1 
ATOM   9826  C  C   . GLY I  1 135 ? 27.247  74.065  46.242 1.00 94.38  ? 129 GLY I C   1 
ATOM   9827  O  O   . GLY I  1 135 ? 26.545  73.902  47.241 1.00 94.14  ? 129 GLY I O   1 
ATOM   9828  N  N   . GLY I  1 136 ? 26.754  74.034  45.006 1.00 95.34  ? 130 GLY I N   1 
ATOM   9829  C  CA  . GLY I  1 136 ? 25.338  73.783  44.794 1.00 99.16  ? 130 GLY I CA  1 
ATOM   9830  C  C   . GLY I  1 136 ? 24.494  75.020  44.543 1.00 100.73 ? 130 GLY I C   1 
ATOM   9831  O  O   . GLY I  1 136 ? 24.166  75.326  43.395 1.00 102.31 ? 130 GLY I O   1 
ATOM   9832  N  N   . ASN I  1 137 ? 24.140  75.731  45.612 1.00 100.21 ? 131 ASN I N   1 
ATOM   9833  C  CA  . ASN I  1 137 ? 23.323  76.939  45.502 1.00 97.25  ? 131 ASN I CA  1 
ATOM   9834  C  C   . ASN I  1 137 ? 23.912  77.984  44.558 1.00 97.18  ? 131 ASN I C   1 
ATOM   9835  O  O   . ASN I  1 137 ? 24.961  77.771  43.947 1.00 96.61  ? 131 ASN I O   1 
ATOM   9836  C  CB  . ASN I  1 137 ? 23.099  77.559  46.888 1.00 97.19  ? 131 ASN I CB  1 
ATOM   9837  C  CG  . ASN I  1 137 ? 24.381  77.689  47.689 1.00 96.35  ? 131 ASN I CG  1 
ATOM   9838  O  OD1 . ASN I  1 137 ? 25.377  78.217  47.202 1.00 99.93  ? 131 ASN I OD1 1 
ATOM   9839  N  ND2 . ASN I  1 137 ? 24.358  77.212  48.929 1.00 91.43  ? 131 ASN I ND2 1 
ATOM   9840  N  N   . GLU I  1 138 ? 23.223  79.113  44.433 1.00 97.44  ? 132 GLU I N   1 
ATOM   9841  C  CA  . GLU I  1 138 ? 23.681  80.184  43.559 1.00 96.75  ? 132 GLU I CA  1 
ATOM   9842  C  C   . GLU I  1 138 ? 24.592  81.133  44.326 1.00 93.90  ? 132 GLU I C   1 
ATOM   9843  O  O   . GLU I  1 138 ? 25.361  81.887  43.729 1.00 93.38  ? 132 GLU I O   1 
ATOM   9844  C  CB  . GLU I  1 138 ? 22.493  80.958  43.001 1.00 101.59 ? 132 GLU I CB  1 
ATOM   9845  C  CG  . GLU I  1 138 ? 21.724  81.724  44.053 1.00 109.63 ? 132 GLU I CG  1 
ATOM   9846  C  CD  . GLU I  1 138 ? 20.761  82.710  43.441 1.00 112.68 ? 132 GLU I CD  1 
ATOM   9847  O  OE1 . GLU I  1 138 ? 21.214  83.540  42.626 1.00 115.31 ? 132 GLU I OE1 1 
ATOM   9848  O  OE2 . GLU I  1 138 ? 19.558  82.657  43.771 1.00 116.09 ? 132 GLU I OE2 1 
ATOM   9849  N  N   . GLU I  1 139 ? 24.493  81.104  45.650 1.00 88.77  ? 133 GLU I N   1 
ATOM   9850  C  CA  . GLU I  1 139 ? 25.332  81.949  46.484 1.00 87.35  ? 133 GLU I CA  1 
ATOM   9851  C  C   . GLU I  1 139 ? 26.783  81.600  46.167 1.00 87.23  ? 133 GLU I C   1 
ATOM   9852  O  O   . GLU I  1 139 ? 27.671  82.454  46.189 1.00 84.10  ? 133 GLU I O   1 
ATOM   9853  C  CB  . GLU I  1 139 ? 25.048  81.680  47.962 1.00 87.13  ? 133 GLU I CB  1 
ATOM   9854  C  CG  . GLU I  1 139 ? 25.722  82.657  48.907 1.00 88.52  ? 133 GLU I CG  1 
ATOM   9855  C  CD  . GLU I  1 139 ? 25.325  84.092  48.620 1.00 92.34  ? 133 GLU I CD  1 
ATOM   9856  O  OE1 . GLU I  1 139 ? 24.109  84.379  48.607 1.00 93.59  ? 133 GLU I OE1 1 
ATOM   9857  O  OE2 . GLU I  1 139 ? 26.226  84.931  48.404 1.00 88.92  ? 133 GLU I OE2 1 
ATOM   9858  N  N   . SER I  1 140 ? 27.002  80.327  45.855 1.00 85.48  ? 134 SER I N   1 
ATOM   9859  C  CA  . SER I  1 140 ? 28.322  79.812  45.528 1.00 82.83  ? 134 SER I CA  1 
ATOM   9860  C  C   . SER I  1 140 ? 28.821  80.293  44.174 1.00 80.05  ? 134 SER I C   1 
ATOM   9861  O  O   . SER I  1 140 ? 30.019  80.275  43.914 1.00 78.53  ? 134 SER I O   1 
ATOM   9862  C  CB  . SER I  1 140 ? 28.299  78.284  45.548 1.00 85.14  ? 134 SER I CB  1 
ATOM   9863  O  OG  . SER I  1 140 ? 29.518  77.751  45.061 1.00 90.16  ? 134 SER I OG  1 
ATOM   9864  N  N   . THR I  1 141 ? 27.904  80.712  43.309 1.00 79.83  ? 135 THR I N   1 
ATOM   9865  C  CA  . THR I  1 141 ? 28.284  81.197  41.986 1.00 80.42  ? 135 THR I CA  1 
ATOM   9866  C  C   . THR I  1 141 ? 28.586  82.691  42.040 1.00 76.77  ? 135 THR I C   1 
ATOM   9867  O  O   . THR I  1 141 ? 28.997  83.291  41.044 1.00 68.26  ? 135 THR I O   1 
ATOM   9868  C  CB  . THR I  1 141 ? 27.162  80.950  40.940 1.00 83.29  ? 135 THR I CB  1 
ATOM   9869  O  OG1 . THR I  1 141 ? 25.992  81.701  41.291 1.00 80.42  ? 135 THR I OG1 1 
ATOM   9870  C  CG2 . THR I  1 141 ? 26.810  79.469  40.878 1.00 83.95  ? 135 THR I CG2 1 
ATOM   9871  N  N   . LYS I  1 142 ? 28.391  83.277  43.219 1.00 77.25  ? 136 LYS I N   1 
ATOM   9872  C  CA  . LYS I  1 142 ? 28.626  84.702  43.421 1.00 80.38  ? 136 LYS I CA  1 
ATOM   9873  C  C   . LYS I  1 142 ? 29.739  85.025  44.429 1.00 76.17  ? 136 LYS I C   1 
ATOM   9874  O  O   . LYS I  1 142 ? 30.634  85.822  44.136 1.00 72.98  ? 136 LYS I O   1 
ATOM   9875  C  CB  . LYS I  1 142 ? 27.325  85.389  43.867 1.00 83.73  ? 136 LYS I CB  1 
ATOM   9876  C  CG  . LYS I  1 142 ? 26.149  85.187  42.922 1.00 91.48  ? 136 LYS I CG  1 
ATOM   9877  C  CD  . LYS I  1 142 ? 25.001  86.156  43.207 1.00 98.21  ? 136 LYS I CD  1 
ATOM   9878  C  CE  . LYS I  1 142 ? 24.407  85.975  44.600 1.00 101.21 ? 136 LYS I CE  1 
ATOM   9879  N  NZ  . LYS I  1 142 ? 25.333  86.390  45.691 1.00 101.37 ? 136 LYS I NZ  1 
ATOM   9880  N  N   . THR I  1 143 ? 29.682  84.404  45.606 1.00 73.00  ? 137 THR I N   1 
ATOM   9881  C  CA  . THR I  1 143 ? 30.664  84.652  46.659 1.00 64.80  ? 137 THR I CA  1 
ATOM   9882  C  C   . THR I  1 143 ? 31.467  83.426  47.092 1.00 66.65  ? 137 THR I C   1 
ATOM   9883  O  O   . THR I  1 143 ? 32.514  83.558  47.728 1.00 66.89  ? 137 THR I O   1 
ATOM   9884  C  CB  . THR I  1 143 ? 29.981  85.186  47.914 1.00 60.65  ? 137 THR I CB  1 
ATOM   9885  O  OG1 . THR I  1 143 ? 29.299  84.112  48.572 1.00 53.38  ? 137 THR I OG1 1 
ATOM   9886  C  CG2 . THR I  1 143 ? 28.977  86.253  47.555 1.00 53.60  ? 137 THR I CG2 1 
ATOM   9887  N  N   . GLY I  1 144 ? 30.971  82.238  46.764 1.00 66.26  ? 138 GLY I N   1 
ATOM   9888  C  CA  . GLY I  1 144 ? 31.655  81.021  47.164 1.00 62.05  ? 138 GLY I CA  1 
ATOM   9889  C  C   . GLY I  1 144 ? 31.249  80.648  48.578 1.00 61.02  ? 138 GLY I C   1 
ATOM   9890  O  O   . GLY I  1 144 ? 31.784  79.706  49.164 1.00 58.11  ? 138 GLY I O   1 
ATOM   9891  N  N   . ASN I  1 145 ? 30.298  81.404  49.123 1.00 61.60  ? 139 ASN I N   1 
ATOM   9892  C  CA  . ASN I  1 145 ? 29.796  81.182  50.472 1.00 61.73  ? 139 ASN I CA  1 
ATOM   9893  C  C   . ASN I  1 145 ? 30.896  81.369  51.499 1.00 60.95  ? 139 ASN I C   1 
ATOM   9894  O  O   . ASN I  1 145 ? 30.833  80.813  52.599 1.00 60.10  ? 139 ASN I O   1 
ATOM   9895  C  CB  . ASN I  1 145 ? 29.210  79.770  50.601 1.00 67.36  ? 139 ASN I CB  1 
ATOM   9896  C  CG  . ASN I  1 145 ? 27.865  79.627  49.907 1.00 64.26  ? 139 ASN I CG  1 
ATOM   9897  O  OD1 . ASN I  1 145 ? 26.869  80.217  50.329 1.00 68.86  ? 139 ASN I OD1 1 
ATOM   9898  N  ND2 . ASN I  1 145 ? 27.832  78.844  48.838 1.00 45.94  ? 139 ASN I ND2 1 
ATOM   9899  N  N   . ALA I  1 146 ? 31.902  82.160  51.142 1.00 60.33  ? 140 ALA I N   1 
ATOM   9900  C  CA  . ALA I  1 146 ? 33.028  82.410  52.037 1.00 57.19  ? 140 ALA I CA  1 
ATOM   9901  C  C   . ALA I  1 146 ? 32.607  83.083  53.350 1.00 52.25  ? 140 ALA I C   1 
ATOM   9902  O  O   . ALA I  1 146 ? 33.320  83.013  54.350 1.00 49.98  ? 140 ALA I O   1 
ATOM   9903  C  CB  . ALA I  1 146 ? 34.085  83.249  51.317 1.00 58.49  ? 140 ALA I CB  1 
ATOM   9904  N  N   . GLY I  1 147 ? 31.454  83.743  53.351 1.00 50.55  ? 141 GLY I N   1 
ATOM   9905  C  CA  . GLY I  1 147 ? 30.995  84.374  54.577 1.00 50.00  ? 141 GLY I CA  1 
ATOM   9906  C  C   . GLY I  1 147 ? 31.353  85.838  54.768 1.00 50.41  ? 141 GLY I C   1 
ATOM   9907  O  O   . GLY I  1 147 ? 31.656  86.553  53.806 1.00 44.69  ? 141 GLY I O   1 
ATOM   9908  N  N   . SER I  1 148 ? 31.333  86.281  56.023 1.00 47.71  ? 142 SER I N   1 
ATOM   9909  C  CA  . SER I  1 148 ? 31.617  87.673  56.331 1.00 52.00  ? 142 SER I CA  1 
ATOM   9910  C  C   . SER I  1 148 ? 33.034  88.104  55.963 1.00 54.54  ? 142 SER I C   1 
ATOM   9911  O  O   . SER I  1 148 ? 33.836  87.314  55.459 1.00 57.13  ? 142 SER I O   1 
ATOM   9912  C  CB  . SER I  1 148 ? 31.352  87.958  57.812 1.00 48.13  ? 142 SER I CB  1 
ATOM   9913  O  OG  . SER I  1 148 ? 32.298  87.316  58.646 1.00 59.72  ? 142 SER I OG  1 
ATOM   9914  N  N   . ARG I  1 149 ? 33.322  89.376  56.212 1.00 52.48  ? 143 ARG I N   1 
ATOM   9915  C  CA  . ARG I  1 149 ? 34.617  89.964  55.917 1.00 43.29  ? 143 ARG I CA  1 
ATOM   9916  C  C   . ARG I  1 149 ? 35.343  90.278  57.224 1.00 42.67  ? 143 ARG I C   1 
ATOM   9917  O  O   . ARG I  1 149 ? 35.005  91.223  57.919 1.00 42.41  ? 143 ARG I O   1 
ATOM   9918  C  CB  . ARG I  1 149 ? 34.396  91.218  55.081 1.00 40.28  ? 143 ARG I CB  1 
ATOM   9919  C  CG  . ARG I  1 149 ? 33.625  90.908  53.815 1.00 43.48  ? 143 ARG I CG  1 
ATOM   9920  C  CD  . ARG I  1 149 ? 33.128  92.143  53.086 1.00 39.81  ? 143 ARG I CD  1 
ATOM   9921  N  NE  . ARG I  1 149 ? 32.453  91.734  51.862 1.00 38.28  ? 143 ARG I NE  1 
ATOM   9922  C  CZ  . ARG I  1 149 ? 32.093  92.548  50.875 1.00 44.90  ? 143 ARG I CZ  1 
ATOM   9923  N  NH1 . ARG I  1 149 ? 31.489  92.046  49.811 1.00 40.49  ? 143 ARG I NH1 1 
ATOM   9924  N  NH2 . ARG I  1 149 ? 32.332  93.854  50.939 1.00 44.68  ? 143 ARG I NH2 1 
ATOM   9925  N  N   . LEU I  1 150 ? 36.341  89.461  57.550 1.00 46.89  ? 144 LEU I N   1 
ATOM   9926  C  CA  . LEU I  1 150 ? 37.108  89.601  58.782 1.00 45.33  ? 144 LEU I CA  1 
ATOM   9927  C  C   . LEU I  1 150 ? 38.078  90.760  58.752 1.00 44.57  ? 144 LEU I C   1 
ATOM   9928  O  O   . LEU I  1 150 ? 38.278  91.436  59.769 1.00 47.88  ? 144 LEU I O   1 
ATOM   9929  C  CB  . LEU I  1 150 ? 37.883  88.313  59.065 1.00 47.03  ? 144 LEU I CB  1 
ATOM   9930  C  CG  . LEU I  1 150 ? 37.037  87.052  59.215 1.00 49.62  ? 144 LEU I CG  1 
ATOM   9931  C  CD1 . LEU I  1 150 ? 37.925  85.844  59.493 1.00 50.47  ? 144 LEU I CD1 1 
ATOM   9932  C  CD2 . LEU I  1 150 ? 36.038  87.266  60.335 1.00 44.69  ? 144 LEU I CD2 1 
ATOM   9933  N  N   . ALA I  1 151 ? 38.699  90.974  57.594 1.00 36.60  ? 145 ALA I N   1 
ATOM   9934  C  CA  . ALA I  1 151 ? 39.665  92.057  57.431 1.00 32.06  ? 145 ALA I CA  1 
ATOM   9935  C  C   . ALA I  1 151 ? 39.834  92.393  55.969 1.00 32.48  ? 145 ALA I C   1 
ATOM   9936  O  O   . ALA I  1 151 ? 39.621  91.547  55.089 1.00 37.29  ? 145 ALA I O   1 
ATOM   9937  C  CB  . ALA I  1 151 ? 41.009  91.674  58.038 1.00 29.12  ? 145 ALA I CB  1 
ATOM   9938  N  N   . CYS I  1 152 ? 40.201  93.644  55.712 1.00 29.46  ? 146 CYS I N   1 
ATOM   9939  C  CA  . CYS I  1 152 ? 40.404  94.117  54.347 1.00 28.37  ? 146 CYS I CA  1 
ATOM   9940  C  C   . CYS I  1 152 ? 41.304  95.332  54.374 1.00 26.37  ? 146 CYS I C   1 
ATOM   9941  O  O   . CYS I  1 152 ? 41.705  95.807  55.450 1.00 29.92  ? 146 CYS I O   1 
ATOM   9942  C  CB  . CYS I  1 152 ? 39.074  94.504  53.702 1.00 32.35  ? 146 CYS I CB  1 
ATOM   9943  S  SG  . CYS I  1 152 ? 38.205  95.814  54.627 1.00 40.30  ? 146 CYS I SG  1 
ATOM   9944  N  N   . GLY I  1 153 ? 41.602  95.836  53.183 1.00 23.80  ? 147 GLY I N   1 
ATOM   9945  C  CA  . GLY I  1 153 ? 42.450  96.997  53.047 1.00 25.67  ? 147 GLY I CA  1 
ATOM   9946  C  C   . GLY I  1 153 ? 42.516  97.438  51.601 1.00 34.76  ? 147 GLY I C   1 
ATOM   9947  O  O   . GLY I  1 153 ? 42.223  96.660  50.672 1.00 33.27  ? 147 GLY I O   1 
ATOM   9948  N  N   . VAL I  1 154 ? 42.895  98.696  51.402 1.00 33.03  ? 148 VAL I N   1 
ATOM   9949  C  CA  . VAL I  1 154 ? 43.000  99.236  50.062 1.00 36.01  ? 148 VAL I CA  1 
ATOM   9950  C  C   . VAL I  1 154 ? 44.378  98.934  49.477 1.00 37.67  ? 148 VAL I C   1 
ATOM   9951  O  O   . VAL I  1 154 ? 45.411  99.183  50.103 1.00 37.88  ? 148 VAL I O   1 
ATOM   9952  C  CB  . VAL I  1 154 ? 42.754  100.748 50.062 1.00 36.64  ? 148 VAL I CB  1 
ATOM   9953  C  CG1 . VAL I  1 154 ? 42.752  101.259 48.643 1.00 36.08  ? 148 VAL I CG1 1 
ATOM   9954  C  CG2 . VAL I  1 154 ? 41.428  101.058 50.746 1.00 36.15  ? 148 VAL I CG2 1 
ATOM   9955  N  N   . ILE I  1 155 ? 44.383  98.383  48.273 1.00 34.25  ? 149 ILE I N   1 
ATOM   9956  C  CA  . ILE I  1 155 ? 45.621  98.038  47.605 1.00 31.61  ? 149 ILE I CA  1 
ATOM   9957  C  C   . ILE I  1 155 ? 46.254  99.282  46.984 1.00 35.83  ? 149 ILE I C   1 
ATOM   9958  O  O   . ILE I  1 155 ? 45.771  99.807  45.976 1.00 32.71  ? 149 ILE I O   1 
ATOM   9959  C  CB  . ILE I  1 155 ? 45.363  96.976  46.510 1.00 30.49  ? 149 ILE I CB  1 
ATOM   9960  C  CG1 . ILE I  1 155 ? 44.617  95.789  47.124 1.00 36.95  ? 149 ILE I CG1 1 
ATOM   9961  C  CG2 . ILE I  1 155 ? 46.680  96.523  45.894 1.00 30.90  ? 149 ILE I CG2 1 
ATOM   9962  C  CD1 . ILE I  1 155 ? 44.305  94.664  46.161 1.00 36.18  ? 149 ILE I CD1 1 
ATOM   9963  N  N   . GLY I  1 156 ? 47.343  99.743  47.594 1.00 37.31  ? 150 GLY I N   1 
ATOM   9964  C  CA  . GLY I  1 156 ? 48.036  100.920 47.096 1.00 36.08  ? 150 GLY I CA  1 
ATOM   9965  C  C   . GLY I  1 156 ? 49.378  100.650 46.437 1.00 37.60  ? 150 GLY I C   1 
ATOM   9966  O  O   . GLY I  1 156 ? 49.992  99.599  46.649 1.00 37.76  ? 150 GLY I O   1 
ATOM   9967  N  N   . ILE I  1 157 ? 49.826  101.599 45.619 1.00 36.25  ? 151 ILE I N   1 
ATOM   9968  C  CA  . ILE I  1 157 ? 51.108  101.487 44.934 1.00 41.35  ? 151 ILE I CA  1 
ATOM   9969  C  C   . ILE I  1 157 ? 52.239  101.416 45.956 1.00 40.71  ? 151 ILE I C   1 
ATOM   9970  O  O   . ILE I  1 157 ? 52.275  102.175 46.925 1.00 38.10  ? 151 ILE I O   1 
ATOM   9971  C  CB  . ILE I  1 157 ? 51.369  102.692 44.022 1.00 45.39  ? 151 ILE I CB  1 
ATOM   9972  C  CG1 . ILE I  1 157 ? 50.167  102.911 43.105 1.00 52.15  ? 151 ILE I CG1 1 
ATOM   9973  C  CG2 . ILE I  1 157 ? 52.607  102.443 43.174 1.00 38.44  ? 151 ILE I CG2 1 
ATOM   9974  C  CD1 . ILE I  1 157 ? 50.305  104.109 42.189 1.00 53.82  ? 151 ILE I CD1 1 
ATOM   9975  N  N   . ALA I  1 158 ? 53.160  100.492 45.733 1.00 39.44  ? 152 ALA I N   1 
ATOM   9976  C  CA  . ALA I  1 158 ? 54.279  100.317 46.636 1.00 45.38  ? 152 ALA I CA  1 
ATOM   9977  C  C   . ALA I  1 158 ? 55.560  100.746 45.931 1.00 50.85  ? 152 ALA I C   1 
ATOM   9978  O  O   . ALA I  1 158 ? 55.655  100.693 44.699 1.00 46.18  ? 152 ALA I O   1 
ATOM   9979  C  CB  . ALA I  1 158 ? 54.365  98.853  47.076 1.00 37.83  ? 152 ALA I CB  1 
ATOM   9980  N  N   . GLN I  1 159 ? 56.536  101.184 46.720 1.00 57.08  ? 153 GLN I N   1 
ATOM   9981  C  CA  . GLN I  1 159 ? 57.815  101.627 46.186 1.00 64.40  ? 153 GLN I CA  1 
ATOM   9982  C  C   . GLN I  1 159 ? 58.561  100.471 45.532 1.00 68.03  ? 153 GLN I C   1 
ATOM   9983  O  O   . GLN I  1 159 ? 59.092  99.625  46.280 1.00 66.60  ? 153 GLN I O   1 
ATOM   9984  C  CB  . GLN I  1 159 ? 58.675  102.234 47.297 1.00 66.95  ? 153 GLN I CB  1 
ATOM   9985  C  CG  . GLN I  1 159 ? 59.969  102.866 46.788 1.00 72.73  ? 153 GLN I CG  1 
ATOM   9986  C  CD  . GLN I  1 159 ? 60.792  103.511 47.892 1.00 76.54  ? 153 GLN I CD  1 
ATOM   9987  O  OE1 . GLN I  1 159 ? 61.854  104.071 47.635 1.00 73.96  ? 153 GLN I OE1 1 
ATOM   9988  N  NE2 . GLN I  1 159 ? 60.303  103.434 49.127 1.00 82.54  ? 153 GLN I NE2 1 
ATOM   9989  O  OXT . GLN I  1 159 ? 58.591  100.420 44.281 1.00 74.26  ? 153 GLN I OXT 1 
ATOM   9990  N  N   . ALA J  1 7   ? 33.187  109.763 34.834 1.00 88.46  ? 1   ALA J N   1 
ATOM   9991  C  CA  . ALA J  1 7   ? 32.546  110.144 36.125 1.00 85.65  ? 1   ALA J CA  1 
ATOM   9992  C  C   . ALA J  1 7   ? 33.148  109.297 37.238 1.00 82.78  ? 1   ALA J C   1 
ATOM   9993  O  O   . ALA J  1 7   ? 32.480  108.978 38.225 1.00 83.08  ? 1   ALA J O   1 
ATOM   9994  C  CB  . ALA J  1 7   ? 31.017  109.932 36.052 1.00 82.17  ? 1   ALA J CB  1 
ATOM   9995  N  N   . THR J  1 8   ? 34.416  108.930 37.071 1.00 77.06  ? 2   THR J N   1 
ATOM   9996  C  CA  . THR J  1 8   ? 35.093  108.124 38.072 1.00 73.33  ? 2   THR J CA  1 
ATOM   9997  C  C   . THR J  1 8   ? 35.004  108.820 39.430 1.00 68.76  ? 2   THR J C   1 
ATOM   9998  O  O   . THR J  1 8   ? 35.065  110.050 39.530 1.00 62.94  ? 2   THR J O   1 
ATOM   9999  C  CB  . THR J  1 8   ? 36.582  107.893 37.715 1.00 73.03  ? 2   THR J CB  1 
ATOM   10000 O  OG1 . THR J  1 8   ? 36.693  107.476 36.350 1.00 79.04  ? 2   THR J OG1 1 
ATOM   10001 C  CG2 . THR J  1 8   ? 37.171  106.794 38.590 1.00 77.40  ? 2   THR J CG2 1 
ATOM   10002 N  N   . LYS J  1 9   ? 34.824  108.022 40.472 1.00 63.14  ? 3   LYS J N   1 
ATOM   10003 C  CA  . LYS J  1 9   ? 34.739  108.539 41.822 1.00 61.53  ? 3   LYS J CA  1 
ATOM   10004 C  C   . LYS J  1 9   ? 35.757  107.788 42.663 1.00 60.83  ? 3   LYS J C   1 
ATOM   10005 O  O   . LYS J  1 9   ? 36.120  106.653 42.350 1.00 64.83  ? 3   LYS J O   1 
ATOM   10006 C  CB  . LYS J  1 9   ? 33.331  108.338 42.381 1.00 67.72  ? 3   LYS J CB  1 
ATOM   10007 C  CG  . LYS J  1 9   ? 32.264  109.135 41.644 1.00 78.14  ? 3   LYS J CG  1 
ATOM   10008 C  CD  . LYS J  1 9   ? 30.867  108.867 42.191 1.00 82.89  ? 3   LYS J CD  1 
ATOM   10009 C  CE  . LYS J  1 9   ? 30.727  109.318 43.635 1.00 87.22  ? 3   LYS J CE  1 
ATOM   10010 N  NZ  . LYS J  1 9   ? 29.364  109.028 44.164 1.00 89.10  ? 3   LYS J NZ  1 
ATOM   10011 N  N   . ALA J  1 10  ? 36.239  108.429 43.717 1.00 52.69  ? 4   ALA J N   1 
ATOM   10012 C  CA  . ALA J  1 10  ? 37.214  107.801 44.587 1.00 48.09  ? 4   ALA J CA  1 
ATOM   10013 C  C   . ALA J  1 10  ? 36.896  108.215 46.009 1.00 47.66  ? 4   ALA J C   1 
ATOM   10014 O  O   . ALA J  1 10  ? 36.029  109.060 46.230 1.00 48.50  ? 4   ALA J O   1 
ATOM   10015 C  CB  . ALA J  1 10  ? 38.612  108.234 44.204 1.00 37.38  ? 4   ALA J CB  1 
ATOM   10016 N  N   . VAL J  1 11  ? 37.585  107.617 46.972 1.00 39.59  ? 5   VAL J N   1 
ATOM   10017 C  CA  . VAL J  1 11  ? 37.344  107.939 48.361 1.00 30.88  ? 5   VAL J CA  1 
ATOM   10018 C  C   . VAL J  1 11  ? 38.537  107.515 49.214 1.00 36.70  ? 5   VAL J C   1 
ATOM   10019 O  O   . VAL J  1 11  ? 39.380  106.719 48.787 1.00 33.58  ? 5   VAL J O   1 
ATOM   10020 C  CB  . VAL J  1 11  ? 36.061  107.254 48.850 1.00 25.20  ? 5   VAL J CB  1 
ATOM   10021 C  CG1 . VAL J  1 11  ? 36.231  105.759 48.804 1.00 29.42  ? 5   VAL J CG1 1 
ATOM   10022 C  CG2 . VAL J  1 11  ? 35.722  107.716 50.241 1.00 22.26  ? 5   VAL J CG2 1 
ATOM   10023 N  N   . CYS J  1 12  ? 38.610  108.049 50.427 1.00 35.44  ? 6   CYS J N   1 
ATOM   10024 C  CA  . CYS J  1 12  ? 39.728  107.748 51.303 1.00 30.99  ? 6   CYS J CA  1 
ATOM   10025 C  C   . CYS J  1 12  ? 39.383  107.923 52.771 1.00 30.65  ? 6   CYS J C   1 
ATOM   10026 O  O   . CYS J  1 12  ? 38.806  108.931 53.173 1.00 31.38  ? 6   CYS J O   1 
ATOM   10027 C  CB  . CYS J  1 12  ? 40.903  108.663 50.942 1.00 35.12  ? 6   CYS J CB  1 
ATOM   10028 S  SG  . CYS J  1 12  ? 42.294  108.589 52.076 1.00 43.20  ? 6   CYS J SG  1 
ATOM   10029 N  N   . VAL J  1 13  ? 39.739  106.928 53.570 1.00 26.95  ? 7   VAL J N   1 
ATOM   10030 C  CA  . VAL J  1 13  ? 39.498  106.978 55.006 1.00 30.29  ? 7   VAL J CA  1 
ATOM   10031 C  C   . VAL J  1 13  ? 40.825  107.362 55.638 1.00 33.19  ? 7   VAL J C   1 
ATOM   10032 O  O   . VAL J  1 13  ? 41.836  106.695 55.410 1.00 40.92  ? 7   VAL J O   1 
ATOM   10033 C  CB  . VAL J  1 13  ? 39.072  105.600 55.558 1.00 29.71  ? 7   VAL J CB  1 
ATOM   10034 C  CG1 . VAL J  1 13  ? 38.862  105.685 57.045 1.00 17.64  ? 7   VAL J CG1 1 
ATOM   10035 C  CG2 . VAL J  1 13  ? 37.811  105.106 54.841 1.00 25.66  ? 7   VAL J CG2 1 
ATOM   10036 N  N   . LEU J  1 14  ? 40.828  108.434 56.423 1.00 35.97  ? 8   LEU J N   1 
ATOM   10037 C  CA  . LEU J  1 14  ? 42.051  108.901 57.065 1.00 36.03  ? 8   LEU J CA  1 
ATOM   10038 C  C   . LEU J  1 14  ? 42.131  108.501 58.518 1.00 37.75  ? 8   LEU J C   1 
ATOM   10039 O  O   . LEU J  1 14  ? 41.256  108.845 59.316 1.00 39.74  ? 8   LEU J O   1 
ATOM   10040 C  CB  . LEU J  1 14  ? 42.153  110.419 56.971 1.00 39.12  ? 8   LEU J CB  1 
ATOM   10041 C  CG  . LEU J  1 14  ? 42.307  111.016 55.577 1.00 39.18  ? 8   LEU J CG  1 
ATOM   10042 C  CD1 . LEU J  1 14  ? 41.982  112.486 55.616 1.00 43.37  ? 8   LEU J CD1 1 
ATOM   10043 C  CD2 . LEU J  1 14  ? 43.717  110.801 55.095 1.00 45.35  ? 8   LEU J CD2 1 
ATOM   10044 N  N   . LYS J  1 15  ? 43.190  107.775 58.860 1.00 37.68  ? 9   LYS J N   1 
ATOM   10045 C  CA  . LYS J  1 15  ? 43.411  107.340 60.237 1.00 38.71  ? 9   LYS J CA  1 
ATOM   10046 C  C   . LYS J  1 15  ? 44.858  107.637 60.604 1.00 38.72  ? 9   LYS J C   1 
ATOM   10047 O  O   . LYS J  1 15  ? 45.730  107.744 59.729 1.00 38.54  ? 9   LYS J O   1 
ATOM   10048 C  CB  . LYS J  1 15  ? 43.162  105.836 60.380 1.00 42.72  ? 9   LYS J CB  1 
ATOM   10049 C  CG  . LYS J  1 15  ? 41.790  105.350 59.932 1.00 51.74  ? 9   LYS J CG  1 
ATOM   10050 C  CD  . LYS J  1 15  ? 40.705  105.736 60.922 1.00 62.62  ? 9   LYS J CD  1 
ATOM   10051 C  CE  . LYS J  1 15  ? 39.376  105.098 60.552 1.00 70.28  ? 9   LYS J CE  1 
ATOM   10052 N  NZ  . LYS J  1 15  ? 39.464  103.606 60.519 1.00 73.90  ? 9   LYS J NZ  1 
ATOM   10053 N  N   . GLY J  1 16  ? 45.110  107.775 61.898 1.00 37.42  ? 10  GLY J N   1 
ATOM   10054 C  CA  . GLY J  1 16  ? 46.460  108.032 62.363 1.00 45.61  ? 10  GLY J CA  1 
ATOM   10055 C  C   . GLY J  1 16  ? 46.627  107.391 63.721 1.00 45.73  ? 10  GLY J C   1 
ATOM   10056 O  O   . GLY J  1 16  ? 45.781  106.605 64.124 1.00 50.77  ? 10  GLY J O   1 
ATOM   10057 N  N   . ASP J  1 17  ? 47.701  107.706 64.432 1.00 53.55  ? 11  ASP J N   1 
ATOM   10058 C  CA  . ASP J  1 17  ? 47.891  107.129 65.763 1.00 62.77  ? 11  ASP J CA  1 
ATOM   10059 C  C   . ASP J  1 17  ? 47.084  107.910 66.788 1.00 62.55  ? 11  ASP J C   1 
ATOM   10060 O  O   . ASP J  1 17  ? 46.535  107.335 67.727 1.00 66.76  ? 11  ASP J O   1 
ATOM   10061 C  CB  . ASP J  1 17  ? 49.365  107.142 66.164 1.00 69.52  ? 11  ASP J CB  1 
ATOM   10062 C  CG  . ASP J  1 17  ? 50.197  106.183 65.341 1.00 78.23  ? 11  ASP J CG  1 
ATOM   10063 O  OD1 . ASP J  1 17  ? 49.782  105.010 65.202 1.00 81.36  ? 11  ASP J OD1 1 
ATOM   10064 O  OD2 . ASP J  1 17  ? 51.265  106.598 64.842 1.00 81.92  ? 11  ASP J OD2 1 
ATOM   10065 N  N   . GLY J  1 18  ? 47.017  109.224 66.594 1.00 58.61  ? 12  GLY J N   1 
ATOM   10066 C  CA  . GLY J  1 18  ? 46.274  110.075 67.497 1.00 51.96  ? 12  GLY J CA  1 
ATOM   10067 C  C   . GLY J  1 18  ? 44.788  110.058 67.190 1.00 55.00  ? 12  GLY J C   1 
ATOM   10068 O  O   . GLY J  1 18  ? 44.287  109.111 66.573 1.00 52.26  ? 12  GLY J O   1 
ATOM   10069 N  N   . PRO J  1 19  ? 44.059  111.112 67.597 1.00 51.26  ? 13  PRO J N   1 
ATOM   10070 C  CA  . PRO J  1 19  ? 42.614  111.287 67.406 1.00 51.65  ? 13  PRO J CA  1 
ATOM   10071 C  C   . PRO J  1 19  ? 42.160  111.680 65.990 1.00 46.69  ? 13  PRO J C   1 
ATOM   10072 O  O   . PRO J  1 19  ? 40.985  111.552 65.646 1.00 46.92  ? 13  PRO J O   1 
ATOM   10073 C  CB  . PRO J  1 19  ? 42.275  112.359 68.432 1.00 50.72  ? 13  PRO J CB  1 
ATOM   10074 C  CG  . PRO J  1 19  ? 43.481  113.253 68.342 1.00 53.10  ? 13  PRO J CG  1 
ATOM   10075 C  CD  . PRO J  1 19  ? 44.628  112.258 68.332 1.00 50.01  ? 13  PRO J CD  1 
ATOM   10076 N  N   . VAL J  1 20  ? 43.086  112.157 65.173 1.00 44.67  ? 14  VAL J N   1 
ATOM   10077 C  CA  . VAL J  1 20  ? 42.752  112.573 63.814 1.00 40.72  ? 14  VAL J CA  1 
ATOM   10078 C  C   . VAL J  1 20  ? 42.172  111.448 62.956 1.00 39.21  ? 14  VAL J C   1 
ATOM   10079 O  O   . VAL J  1 20  ? 42.773  110.381 62.829 1.00 40.30  ? 14  VAL J O   1 
ATOM   10080 C  CB  . VAL J  1 20  ? 44.006  113.149 63.093 1.00 43.19  ? 14  VAL J CB  1 
ATOM   10081 C  CG1 . VAL J  1 20  ? 43.647  113.610 61.689 1.00 43.78  ? 14  VAL J CG1 1 
ATOM   10082 C  CG2 . VAL J  1 20  ? 44.596  114.299 63.901 1.00 44.20  ? 14  VAL J CG2 1 
ATOM   10083 N  N   . GLN J  1 21  ? 41.001  111.687 62.374 1.00 40.23  ? 15  GLN J N   1 
ATOM   10084 C  CA  . GLN J  1 21  ? 40.375  110.706 61.493 1.00 44.79  ? 15  GLN J CA  1 
ATOM   10085 C  C   . GLN J  1 21  ? 39.274  111.342 60.660 1.00 39.81  ? 15  GLN J C   1 
ATOM   10086 O  O   . GLN J  1 21  ? 38.595  112.240 61.124 1.00 41.47  ? 15  GLN J O   1 
ATOM   10087 C  CB  . GLN J  1 21  ? 39.805  109.543 62.294 1.00 53.53  ? 15  GLN J CB  1 
ATOM   10088 C  CG  . GLN J  1 21  ? 38.803  109.934 63.346 1.00 66.52  ? 15  GLN J CG  1 
ATOM   10089 C  CD  . GLN J  1 21  ? 38.057  108.729 63.882 1.00 75.72  ? 15  GLN J CD  1 
ATOM   10090 O  OE1 . GLN J  1 21  ? 37.263  108.111 63.170 1.00 77.92  ? 15  GLN J OE1 1 
ATOM   10091 N  NE2 . GLN J  1 21  ? 38.316  108.380 65.139 1.00 78.14  ? 15  GLN J NE2 1 
ATOM   10092 N  N   . GLY J  1 22  ? 39.105  110.878 59.426 1.00 38.75  ? 16  GLY J N   1 
ATOM   10093 C  CA  . GLY J  1 22  ? 38.082  111.440 58.563 1.00 35.14  ? 16  GLY J CA  1 
ATOM   10094 C  C   . GLY J  1 22  ? 37.860  110.716 57.244 1.00 35.34  ? 16  GLY J C   1 
ATOM   10095 O  O   . GLY J  1 22  ? 38.492  109.702 56.960 1.00 39.04  ? 16  GLY J O   1 
ATOM   10096 N  N   . ILE J  1 23  ? 36.958  111.248 56.429 1.00 31.55  ? 17  ILE J N   1 
ATOM   10097 C  CA  . ILE J  1 23  ? 36.629  110.660 55.141 1.00 32.33  ? 17  ILE J CA  1 
ATOM   10098 C  C   . ILE J  1 23  ? 36.717  111.746 54.080 1.00 37.32  ? 17  ILE J C   1 
ATOM   10099 O  O   . ILE J  1 23  ? 36.301  112.879 54.319 1.00 42.57  ? 17  ILE J O   1 
ATOM   10100 C  CB  . ILE J  1 23  ? 35.200  110.086 55.161 1.00 36.71  ? 17  ILE J CB  1 
ATOM   10101 C  CG1 . ILE J  1 23  ? 35.141  108.902 56.124 1.00 33.66  ? 17  ILE J CG1 1 
ATOM   10102 C  CG2 . ILE J  1 23  ? 34.753  109.718 53.753 1.00 26.47  ? 17  ILE J CG2 1 
ATOM   10103 C  CD1 . ILE J  1 23  ? 33.789  108.213 56.158 1.00 38.64  ? 17  ILE J CD1 1 
ATOM   10104 N  N   . ILE J  1 24  ? 37.264  111.404 52.915 1.00 37.87  ? 18  ILE J N   1 
ATOM   10105 C  CA  . ILE J  1 24  ? 37.411  112.369 51.831 1.00 37.84  ? 18  ILE J CA  1 
ATOM   10106 C  C   . ILE J  1 24  ? 37.008  111.754 50.511 1.00 39.54  ? 18  ILE J C   1 
ATOM   10107 O  O   . ILE J  1 24  ? 37.466  110.665 50.144 1.00 32.38  ? 18  ILE J O   1 
ATOM   10108 C  CB  . ILE J  1 24  ? 38.859  112.876 51.687 1.00 34.88  ? 18  ILE J CB  1 
ATOM   10109 C  CG1 . ILE J  1 24  ? 39.273  113.653 52.933 1.00 31.04  ? 18  ILE J CG1 1 
ATOM   10110 C  CG2 . ILE J  1 24  ? 38.980  113.748 50.437 1.00 35.92  ? 18  ILE J CG2 1 
ATOM   10111 C  CD1 . ILE J  1 24  ? 38.475  114.919 53.169 1.00 37.31  ? 18  ILE J CD1 1 
ATOM   10112 N  N   . ASN J  1 25  ? 36.167  112.483 49.787 1.00 36.70  ? 19  ASN J N   1 
ATOM   10113 C  CA  . ASN J  1 25  ? 35.658  112.016 48.518 1.00 36.63  ? 19  ASN J CA  1 
ATOM   10114 C  C   . ASN J  1 25  ? 36.294  112.724 47.350 1.00 39.86  ? 19  ASN J C   1 
ATOM   10115 O  O   . ASN J  1 25  ? 36.776  113.849 47.474 1.00 43.30  ? 19  ASN J O   1 
ATOM   10116 C  CB  . ASN J  1 25  ? 34.141  112.181 48.510 1.00 35.47  ? 19  ASN J CB  1 
ATOM   10117 C  CG  . ASN J  1 25  ? 33.476  111.352 49.598 1.00 42.88  ? 19  ASN J CG  1 
ATOM   10118 O  OD1 . ASN J  1 25  ? 33.449  110.126 49.509 1.00 47.63  ? 19  ASN J OD1 1 
ATOM   10119 N  ND2 . ASN J  1 25  ? 32.966  112.011 50.646 1.00 31.12  ? 19  ASN J ND2 1 
ATOM   10120 N  N   . PHE J  1 26  ? 36.315  112.036 46.217 1.00 39.15  ? 20  PHE J N   1 
ATOM   10121 C  CA  . PHE J  1 26  ? 36.886  112.569 44.993 1.00 41.98  ? 20  PHE J CA  1 
ATOM   10122 C  C   . PHE J  1 26  ? 35.890  112.329 43.872 1.00 44.26  ? 20  PHE J C   1 
ATOM   10123 O  O   . PHE J  1 26  ? 35.331  111.245 43.752 1.00 41.25  ? 20  PHE J O   1 
ATOM   10124 C  CB  . PHE J  1 26  ? 38.192  111.848 44.657 1.00 42.01  ? 20  PHE J CB  1 
ATOM   10125 C  CG  . PHE J  1 26  ? 39.271  112.024 45.686 1.00 46.68  ? 20  PHE J CG  1 
ATOM   10126 C  CD1 . PHE J  1 26  ? 40.266  112.988 45.515 1.00 39.59  ? 20  PHE J CD1 1 
ATOM   10127 C  CD2 . PHE J  1 26  ? 39.302  111.218 46.824 1.00 39.71  ? 20  PHE J CD2 1 
ATOM   10128 C  CE1 . PHE J  1 26  ? 41.280  113.143 46.461 1.00 42.53  ? 20  PHE J CE1 1 
ATOM   10129 C  CE2 . PHE J  1 26  ? 40.314  111.368 47.778 1.00 44.16  ? 20  PHE J CE2 1 
ATOM   10130 C  CZ  . PHE J  1 26  ? 41.306  112.333 47.594 1.00 37.60  ? 20  PHE J CZ  1 
ATOM   10131 N  N   . GLU J  1 27  ? 35.653  113.348 43.063 1.00 48.60  ? 21  GLU J N   1 
ATOM   10132 C  CA  . GLU J  1 27  ? 34.742  113.203 41.948 1.00 53.56  ? 21  GLU J CA  1 
ATOM   10133 C  C   . GLU J  1 27  ? 35.285  113.934 40.747 1.00 51.46  ? 21  GLU J C   1 
ATOM   10134 O  O   . GLU J  1 27  ? 35.601  115.116 40.819 1.00 50.02  ? 21  GLU J O   1 
ATOM   10135 C  CB  . GLU J  1 27  ? 33.366  113.748 42.285 1.00 59.36  ? 21  GLU J CB  1 
ATOM   10136 C  CG  . GLU J  1 27  ? 32.419  113.691 41.098 1.00 71.15  ? 21  GLU J CG  1 
ATOM   10137 C  CD  . GLU J  1 27  ? 30.985  113.973 41.482 1.00 78.47  ? 21  GLU J CD  1 
ATOM   10138 O  OE1 . GLU J  1 27  ? 30.147  114.108 40.567 1.00 78.89  ? 21  GLU J OE1 1 
ATOM   10139 O  OE2 . GLU J  1 27  ? 30.695  114.052 42.698 1.00 81.50  ? 21  GLU J OE2 1 
ATOM   10140 N  N   . GLN J  1 28  ? 35.406  113.219 39.641 1.00 50.19  ? 22  GLN J N   1 
ATOM   10141 C  CA  . GLN J  1 28  ? 35.906  113.816 38.419 1.00 50.08  ? 22  GLN J CA  1 
ATOM   10142 C  C   . GLN J  1 28  ? 34.987  113.409 37.279 1.00 51.60  ? 22  GLN J C   1 
ATOM   10143 O  O   . GLN J  1 28  ? 35.233  112.418 36.603 1.00 51.56  ? 22  GLN J O   1 
ATOM   10144 C  CB  . GLN J  1 28  ? 37.338  113.350 38.147 1.00 40.35  ? 22  GLN J CB  1 
ATOM   10145 C  CG  . GLN J  1 28  ? 37.874  113.865 36.838 1.00 43.39  ? 22  GLN J CG  1 
ATOM   10146 C  CD  . GLN J  1 28  ? 39.313  113.480 36.601 1.00 46.29  ? 22  GLN J CD  1 
ATOM   10147 O  OE1 . GLN J  1 28  ? 39.699  112.324 36.778 1.00 52.58  ? 22  GLN J OE1 1 
ATOM   10148 N  NE2 . GLN J  1 28  ? 40.117  114.446 36.183 1.00 47.39  ? 22  GLN J NE2 1 
ATOM   10149 N  N   . LYS J  1 29  ? 33.925  114.179 37.069 1.00 60.41  ? 23  LYS J N   1 
ATOM   10150 C  CA  . LYS J  1 29  ? 32.964  113.876 36.015 1.00 69.74  ? 23  LYS J CA  1 
ATOM   10151 C  C   . LYS J  1 29  ? 33.539  113.782 34.600 1.00 69.18  ? 23  LYS J C   1 
ATOM   10152 O  O   . LYS J  1 29  ? 33.224  112.843 33.881 1.00 66.79  ? 23  LYS J O   1 
ATOM   10153 C  CB  . LYS J  1 29  ? 31.817  114.885 36.054 1.00 78.86  ? 23  LYS J CB  1 
ATOM   10154 C  CG  . LYS J  1 29  ? 30.843  114.669 37.214 1.00 89.99  ? 23  LYS J CG  1 
ATOM   10155 C  CD  . LYS J  1 29  ? 30.083  113.347 37.066 1.00 98.57  ? 23  LYS J CD  1 
ATOM   10156 C  CE  . LYS J  1 29  ? 28.940  113.230 38.074 1.00 98.80  ? 23  LYS J CE  1 
ATOM   10157 N  NZ  . LYS J  1 29  ? 28.145  111.981 37.889 1.00 97.85  ? 23  LYS J NZ  1 
ATOM   10158 N  N   . GLU J  1 30  ? 34.370  114.735 34.188 1.00 72.74  ? 24  GLU J N   1 
ATOM   10159 C  CA  . GLU J  1 30  ? 34.951  114.670 32.848 1.00 81.25  ? 24  GLU J CA  1 
ATOM   10160 C  C   . GLU J  1 30  ? 36.343  114.059 32.871 1.00 82.78  ? 24  GLU J C   1 
ATOM   10161 O  O   . GLU J  1 30  ? 37.067  114.186 33.854 1.00 85.36  ? 24  GLU J O   1 
ATOM   10162 C  CB  . GLU J  1 30  ? 35.010  116.053 32.202 1.00 88.96  ? 24  GLU J CB  1 
ATOM   10163 C  CG  . GLU J  1 30  ? 33.657  116.589 31.764 1.00 102.23 ? 24  GLU J CG  1 
ATOM   10164 C  CD  . GLU J  1 30  ? 33.775  117.859 30.939 1.00 109.35 ? 24  GLU J CD  1 
ATOM   10165 O  OE1 . GLU J  1 30  ? 34.369  118.839 31.435 1.00 112.76 ? 24  GLU J OE1 1 
ATOM   10166 O  OE2 . GLU J  1 30  ? 33.274  117.877 29.795 1.00 111.00 ? 24  GLU J OE2 1 
ATOM   10167 N  N   . SER J  1 31  ? 36.712  113.407 31.774 1.00 85.42  ? 25  SER J N   1 
ATOM   10168 C  CA  . SER J  1 31  ? 38.005  112.739 31.654 1.00 86.25  ? 25  SER J CA  1 
ATOM   10169 C  C   . SER J  1 31  ? 39.183  113.522 32.237 1.00 85.91  ? 25  SER J C   1 
ATOM   10170 O  O   . SER J  1 31  ? 39.908  113.007 33.083 1.00 88.03  ? 25  SER J O   1 
ATOM   10171 C  CB  . SER J  1 31  ? 38.279  112.395 30.187 1.00 87.76  ? 25  SER J CB  1 
ATOM   10172 O  OG  . SER J  1 31  ? 39.288  111.405 30.081 1.00 83.74  ? 25  SER J OG  1 
ATOM   10173 N  N   . ASN J  1 32  ? 39.388  114.754 31.787 1.00 86.74  ? 26  ASN J N   1 
ATOM   10174 C  CA  . ASN J  1 32  ? 40.488  115.557 32.313 1.00 86.19  ? 26  ASN J CA  1 
ATOM   10175 C  C   . ASN J  1 32  ? 40.016  116.840 32.964 1.00 80.52  ? 26  ASN J C   1 
ATOM   10176 O  O   . ASN J  1 32  ? 40.774  117.801 33.087 1.00 80.43  ? 26  ASN J O   1 
ATOM   10177 C  CB  . ASN J  1 32  ? 41.490  115.887 31.213 1.00 96.22  ? 26  ASN J CB  1 
ATOM   10178 C  CG  . ASN J  1 32  ? 42.471  114.766 30.980 1.00 105.94 ? 26  ASN J CG  1 
ATOM   10179 O  OD1 . ASN J  1 32  ? 42.078  113.638 30.684 1.00 114.16 ? 26  ASN J OD1 1 
ATOM   10180 N  ND2 . ASN J  1 32  ? 43.759  115.066 31.117 1.00 109.63 ? 26  ASN J ND2 1 
ATOM   10181 N  N   . GLY J  1 33  ? 38.759  116.849 33.384 1.00 74.19  ? 27  GLY J N   1 
ATOM   10182 C  CA  . GLY J  1 33  ? 38.210  118.023 34.028 1.00 67.82  ? 27  GLY J CA  1 
ATOM   10183 C  C   . GLY J  1 33  ? 38.714  118.139 35.449 1.00 62.82  ? 27  GLY J C   1 
ATOM   10184 O  O   . GLY J  1 33  ? 39.483  117.301 35.914 1.00 59.97  ? 27  GLY J O   1 
ATOM   10185 N  N   . PRO J  1 34  ? 38.295  119.177 36.176 1.00 61.10  ? 28  PRO J N   1 
ATOM   10186 C  CA  . PRO J  1 34  ? 38.781  119.289 37.547 1.00 56.69  ? 28  PRO J CA  1 
ATOM   10187 C  C   . PRO J  1 34  ? 38.275  118.117 38.384 1.00 51.86  ? 28  PRO J C   1 
ATOM   10188 O  O   . PRO J  1 34  ? 37.388  117.365 37.966 1.00 47.36  ? 28  PRO J O   1 
ATOM   10189 C  CB  . PRO J  1 34  ? 38.198  120.623 38.002 1.00 57.74  ? 28  PRO J CB  1 
ATOM   10190 C  CG  . PRO J  1 34  ? 36.859  120.636 37.308 1.00 56.26  ? 28  PRO J CG  1 
ATOM   10191 C  CD  . PRO J  1 34  ? 37.242  120.174 35.907 1.00 60.09  ? 28  PRO J CD  1 
ATOM   10192 N  N   . VAL J  1 35  ? 38.854  117.973 39.568 1.00 46.38  ? 29  VAL J N   1 
ATOM   10193 C  CA  . VAL J  1 35  ? 38.474  116.921 40.487 1.00 41.87  ? 29  VAL J CA  1 
ATOM   10194 C  C   . VAL J  1 35  ? 37.971  117.612 41.741 1.00 41.95  ? 29  VAL J C   1 
ATOM   10195 O  O   . VAL J  1 35  ? 38.620  118.516 42.256 1.00 45.12  ? 29  VAL J O   1 
ATOM   10196 C  CB  . VAL J  1 35  ? 39.684  116.023 40.855 1.00 38.19  ? 29  VAL J CB  1 
ATOM   10197 C  CG1 . VAL J  1 35  ? 39.250  114.941 41.811 1.00 28.17  ? 29  VAL J CG1 1 
ATOM   10198 C  CG2 . VAL J  1 35  ? 40.293  115.408 39.601 1.00 30.74  ? 29  VAL J CG2 1 
ATOM   10199 N  N   . LYS J  1 36  ? 36.810  117.199 42.225 1.00 37.08  ? 30  LYS J N   1 
ATOM   10200 C  CA  . LYS J  1 36  ? 36.251  117.786 43.427 1.00 45.32  ? 30  LYS J CA  1 
ATOM   10201 C  C   . LYS J  1 36  ? 36.716  116.929 44.588 1.00 43.95  ? 30  LYS J C   1 
ATOM   10202 O  O   . LYS J  1 36  ? 36.618  115.707 44.538 1.00 45.88  ? 30  LYS J O   1 
ATOM   10203 C  CB  . LYS J  1 36  ? 34.723  117.814 43.333 1.00 52.73  ? 30  LYS J CB  1 
ATOM   10204 C  CG  . LYS J  1 36  ? 34.236  118.702 42.183 1.00 74.51  ? 30  LYS J CG  1 
ATOM   10205 C  CD  . LYS J  1 36  ? 32.754  118.547 41.877 1.00 82.69  ? 30  LYS J CD  1 
ATOM   10206 C  CE  . LYS J  1 36  ? 32.378  119.344 40.636 1.00 85.53  ? 30  LYS J CE  1 
ATOM   10207 N  NZ  . LYS J  1 36  ? 30.940  119.172 40.291 1.00 90.25  ? 30  LYS J NZ  1 
ATOM   10208 N  N   . VAL J  1 37  ? 37.244  117.577 45.620 1.00 37.81  ? 31  VAL J N   1 
ATOM   10209 C  CA  . VAL J  1 37  ? 37.756  116.890 46.796 1.00 34.10  ? 31  VAL J CA  1 
ATOM   10210 C  C   . VAL J  1 37  ? 36.987  117.408 47.997 1.00 37.41  ? 31  VAL J C   1 
ATOM   10211 O  O   . VAL J  1 37  ? 37.140  118.574 48.379 1.00 42.20  ? 31  VAL J O   1 
ATOM   10212 C  CB  . VAL J  1 37  ? 39.259  117.200 46.976 1.00 37.02  ? 31  VAL J CB  1 
ATOM   10213 C  CG1 . VAL J  1 37  ? 39.854  116.363 48.110 1.00 23.84  ? 31  VAL J CG1 1 
ATOM   10214 C  CG2 . VAL J  1 37  ? 39.991  116.951 45.671 1.00 34.93  ? 31  VAL J CG2 1 
ATOM   10215 N  N   . TRP J  1 38  ? 36.178  116.558 48.618 1.00 33.68  ? 32  TRP J N   1 
ATOM   10216 C  CA  . TRP J  1 38  ? 35.382  117.038 49.743 1.00 38.89  ? 32  TRP J CA  1 
ATOM   10217 C  C   . TRP J  1 38  ? 35.096  116.026 50.832 1.00 35.58  ? 32  TRP J C   1 
ATOM   10218 O  O   . TRP J  1 38  ? 34.961  114.823 50.573 1.00 36.30  ? 32  TRP J O   1 
ATOM   10219 C  CB  . TRP J  1 38  ? 34.044  117.574 49.230 1.00 36.94  ? 32  TRP J CB  1 
ATOM   10220 C  CG  . TRP J  1 38  ? 33.058  116.495 48.930 1.00 36.65  ? 32  TRP J CG  1 
ATOM   10221 C  CD1 . TRP J  1 38  ? 32.056  116.037 49.752 1.00 27.35  ? 32  TRP J CD1 1 
ATOM   10222 C  CD2 . TRP J  1 38  ? 32.967  115.732 47.719 1.00 37.25  ? 32  TRP J CD2 1 
ATOM   10223 N  NE1 . TRP J  1 38  ? 31.345  115.043 49.115 1.00 34.74  ? 32  TRP J NE1 1 
ATOM   10224 C  CE2 . TRP J  1 38  ? 31.883  114.837 47.868 1.00 32.58  ? 32  TRP J CE2 1 
ATOM   10225 C  CE3 . TRP J  1 38  ? 33.699  115.717 46.520 1.00 42.32  ? 32  TRP J CE3 1 
ATOM   10226 C  CZ2 . TRP J  1 38  ? 31.510  113.934 46.858 1.00 40.30  ? 32  TRP J CZ2 1 
ATOM   10227 C  CZ3 . TRP J  1 38  ? 33.325  114.814 45.510 1.00 46.07  ? 32  TRP J CZ3 1 
ATOM   10228 C  CH2 . TRP J  1 38  ? 32.240  113.938 45.690 1.00 46.21  ? 32  TRP J CH2 1 
ATOM   10229 N  N   . GLY J  1 39  ? 34.958  116.535 52.051 1.00 26.31  ? 33  GLY J N   1 
ATOM   10230 C  CA  . GLY J  1 39  ? 34.683  115.665 53.169 1.00 25.13  ? 33  GLY J CA  1 
ATOM   10231 C  C   . GLY J  1 39  ? 34.908  116.347 54.496 1.00 24.23  ? 33  GLY J C   1 
ATOM   10232 O  O   . GLY J  1 39  ? 34.783  117.561 54.611 1.00 27.08  ? 33  GLY J O   1 
ATOM   10233 N  N   . SER J  1 40  ? 35.244  115.560 55.508 1.00 29.77  ? 34  SER J N   1 
ATOM   10234 C  CA  . SER J  1 40  ? 35.458  116.106 56.838 1.00 37.45  ? 34  SER J CA  1 
ATOM   10235 C  C   . SER J  1 40  ? 36.546  115.315 57.557 1.00 39.28  ? 34  SER J C   1 
ATOM   10236 O  O   . SER J  1 40  ? 36.764  114.139 57.263 1.00 40.50  ? 34  SER J O   1 
ATOM   10237 C  CB  . SER J  1 40  ? 34.151  116.042 57.628 1.00 37.69  ? 34  SER J CB  1 
ATOM   10238 O  OG  . SER J  1 40  ? 34.328  116.502 58.953 1.00 56.94  ? 34  SER J OG  1 
ATOM   10239 N  N   . ILE J  1 41  ? 37.215  115.975 58.496 1.00 37.18  ? 35  ILE J N   1 
ATOM   10240 C  CA  . ILE J  1 41  ? 38.288  115.375 59.280 1.00 40.50  ? 35  ILE J CA  1 
ATOM   10241 C  C   . ILE J  1 41  ? 38.205  115.950 60.685 1.00 42.57  ? 35  ILE J C   1 
ATOM   10242 O  O   . ILE J  1 41  ? 38.208  117.168 60.857 1.00 49.45  ? 35  ILE J O   1 
ATOM   10243 C  CB  . ILE J  1 41  ? 39.665  115.737 58.710 1.00 39.50  ? 35  ILE J CB  1 
ATOM   10244 C  CG1 . ILE J  1 41  ? 39.708  115.426 57.210 1.00 39.03  ? 35  ILE J CG1 1 
ATOM   10245 C  CG2 . ILE J  1 41  ? 40.740  114.978 59.463 1.00 33.91  ? 35  ILE J CG2 1 
ATOM   10246 C  CD1 . ILE J  1 41  ? 40.951  115.912 56.525 1.00 33.67  ? 35  ILE J CD1 1 
ATOM   10247 N  N   . LYS J  1 42  ? 38.134  115.091 61.693 1.00 38.94  ? 36  LYS J N   1 
ATOM   10248 C  CA  . LYS J  1 42  ? 38.039  115.582 63.058 1.00 44.39  ? 36  LYS J CA  1 
ATOM   10249 C  C   . LYS J  1 42  ? 39.300  115.270 63.841 1.00 45.17  ? 36  LYS J C   1 
ATOM   10250 O  O   . LYS J  1 42  ? 40.174  114.548 63.355 1.00 43.84  ? 36  LYS J O   1 
ATOM   10251 C  CB  . LYS J  1 42  ? 36.813  114.983 63.759 1.00 49.48  ? 36  LYS J CB  1 
ATOM   10252 C  CG  . LYS J  1 42  ? 36.824  113.472 63.894 1.00 58.51  ? 36  LYS J CG  1 
ATOM   10253 C  CD  . LYS J  1 42  ? 35.577  112.976 64.619 1.00 65.41  ? 36  LYS J CD  1 
ATOM   10254 C  CE  . LYS J  1 42  ? 35.587  111.457 64.782 1.00 69.64  ? 36  LYS J CE  1 
ATOM   10255 N  NZ  . LYS J  1 42  ? 34.427  110.955 65.576 1.00 68.39  ? 36  LYS J NZ  1 
ATOM   10256 N  N   . GLY J  1 43  ? 39.395  115.828 65.045 1.00 44.95  ? 37  GLY J N   1 
ATOM   10257 C  CA  . GLY J  1 43  ? 40.557  115.600 65.888 1.00 41.84  ? 37  GLY J CA  1 
ATOM   10258 C  C   . GLY J  1 43  ? 41.740  116.505 65.597 1.00 46.96  ? 37  GLY J C   1 
ATOM   10259 O  O   . GLY J  1 43  ? 42.830  116.275 66.121 1.00 49.80  ? 37  GLY J O   1 
ATOM   10260 N  N   . LEU J  1 44  ? 41.529  117.530 64.770 1.00 47.00  ? 38  LEU J N   1 
ATOM   10261 C  CA  . LEU J  1 44  ? 42.573  118.486 64.398 1.00 45.63  ? 38  LEU J CA  1 
ATOM   10262 C  C   . LEU J  1 44  ? 42.581  119.756 65.253 1.00 47.53  ? 38  LEU J C   1 
ATOM   10263 O  O   . LEU J  1 44  ? 41.522  120.270 65.628 1.00 49.32  ? 38  LEU J O   1 
ATOM   10264 C  CB  . LEU J  1 44  ? 42.395  118.906 62.939 1.00 44.01  ? 38  LEU J CB  1 
ATOM   10265 C  CG  . LEU J  1 44  ? 42.541  117.866 61.830 1.00 48.12  ? 38  LEU J CG  1 
ATOM   10266 C  CD1 . LEU J  1 44  ? 42.022  118.471 60.522 1.00 38.57  ? 38  LEU J CD1 1 
ATOM   10267 C  CD2 . LEU J  1 44  ? 44.011  117.429 61.697 1.00 38.16  ? 38  LEU J CD2 1 
ATOM   10268 N  N   . THR J  1 45  ? 43.772  120.268 65.559 1.00 46.64  ? 39  THR J N   1 
ATOM   10269 C  CA  . THR J  1 45  ? 43.881  121.512 66.325 1.00 48.08  ? 39  THR J CA  1 
ATOM   10270 C  C   . THR J  1 45  ? 43.371  122.633 65.413 1.00 48.45  ? 39  THR J C   1 
ATOM   10271 O  O   . THR J  1 45  ? 43.571  122.599 64.199 1.00 46.11  ? 39  THR J O   1 
ATOM   10272 C  CB  . THR J  1 45  ? 45.346  121.834 66.718 1.00 44.63  ? 39  THR J CB  1 
ATOM   10273 O  OG1 . THR J  1 45  ? 46.163  121.880 65.541 1.00 47.82  ? 39  THR J OG1 1 
ATOM   10274 C  CG2 . THR J  1 45  ? 45.893  120.792 67.659 1.00 41.08  ? 39  THR J CG2 1 
ATOM   10275 N  N   . GLU J  1 46  ? 42.708  123.626 65.989 1.00 53.95  ? 40  GLU J N   1 
ATOM   10276 C  CA  . GLU J  1 46  ? 42.179  124.719 65.184 1.00 54.81  ? 40  GLU J CA  1 
ATOM   10277 C  C   . GLU J  1 46  ? 43.261  125.400 64.350 1.00 51.01  ? 40  GLU J C   1 
ATOM   10278 O  O   . GLU J  1 46  ? 44.352  125.693 64.841 1.00 45.75  ? 40  GLU J O   1 
ATOM   10279 C  CB  . GLU J  1 46  ? 41.499  125.765 66.072 1.00 59.88  ? 40  GLU J CB  1 
ATOM   10280 C  CG  . GLU J  1 46  ? 40.806  126.860 65.275 1.00 62.35  ? 40  GLU J CG  1 
ATOM   10281 C  CD  . GLU J  1 46  ? 40.209  127.940 66.148 1.00 64.64  ? 40  GLU J CD  1 
ATOM   10282 O  OE1 . GLU J  1 46  ? 39.481  128.803 65.601 1.00 65.49  ? 40  GLU J OE1 1 
ATOM   10283 O  OE2 . GLU J  1 46  ? 40.470  127.926 67.372 1.00 62.18  ? 40  GLU J OE2 1 
ATOM   10284 N  N   . GLY J  1 47  ? 42.953  125.652 63.085 1.00 45.65  ? 41  GLY J N   1 
ATOM   10285 C  CA  . GLY J  1 47  ? 43.913  126.312 62.233 1.00 38.72  ? 41  GLY J CA  1 
ATOM   10286 C  C   . GLY J  1 47  ? 44.184  125.568 60.947 1.00 41.98  ? 41  GLY J C   1 
ATOM   10287 O  O   . GLY J  1 47  ? 43.419  124.677 60.539 1.00 36.05  ? 41  GLY J O   1 
ATOM   10288 N  N   . LEU J  1 48  ? 45.294  125.944 60.314 1.00 37.68  ? 42  LEU J N   1 
ATOM   10289 C  CA  . LEU J  1 48  ? 45.713  125.357 59.053 1.00 38.22  ? 42  LEU J CA  1 
ATOM   10290 C  C   . LEU J  1 48  ? 46.511  124.057 59.178 1.00 38.42  ? 42  LEU J C   1 
ATOM   10291 O  O   . LEU J  1 48  ? 47.312  123.879 60.095 1.00 42.19  ? 42  LEU J O   1 
ATOM   10292 C  CB  . LEU J  1 48  ? 46.517  126.388 58.249 1.00 36.50  ? 42  LEU J CB  1 
ATOM   10293 C  CG  . LEU J  1 48  ? 45.778  127.664 57.813 1.00 32.44  ? 42  LEU J CG  1 
ATOM   10294 C  CD1 . LEU J  1 48  ? 46.646  128.476 56.857 1.00 29.30  ? 42  LEU J CD1 1 
ATOM   10295 C  CD2 . LEU J  1 48  ? 44.484  127.297 57.110 1.00 27.91  ? 42  LEU J CD2 1 
ATOM   10296 N  N   . HIS J  1 49  ? 46.266  123.144 58.243 1.00 39.11  ? 43  HIS J N   1 
ATOM   10297 C  CA  . HIS J  1 49  ? 46.958  121.865 58.202 1.00 32.69  ? 43  HIS J CA  1 
ATOM   10298 C  C   . HIS J  1 49  ? 47.273  121.517 56.754 1.00 30.34  ? 43  HIS J C   1 
ATOM   10299 O  O   . HIS J  1 49  ? 46.400  121.582 55.887 1.00 22.08  ? 43  HIS J O   1 
ATOM   10300 C  CB  . HIS J  1 49  ? 46.088  120.765 58.815 1.00 35.49  ? 43  HIS J CB  1 
ATOM   10301 C  CG  . HIS J  1 49  ? 45.906  120.888 60.294 1.00 35.99  ? 43  HIS J CG  1 
ATOM   10302 N  ND1 . HIS J  1 49  ? 46.798  120.358 61.201 1.00 41.40  ? 43  HIS J ND1 1 
ATOM   10303 C  CD2 . HIS J  1 49  ? 44.940  121.492 61.026 1.00 36.24  ? 43  HIS J CD2 1 
ATOM   10304 C  CE1 . HIS J  1 49  ? 46.390  120.628 62.429 1.00 34.12  ? 43  HIS J CE1 1 
ATOM   10305 N  NE2 . HIS J  1 49  ? 45.265  121.315 62.351 1.00 40.12  ? 43  HIS J NE2 1 
ATOM   10306 N  N   . GLY J  1 50  ? 48.528  121.167 56.488 1.00 32.70  ? 44  GLY J N   1 
ATOM   10307 C  CA  . GLY J  1 50  ? 48.912  120.787 55.139 1.00 32.46  ? 44  GLY J CA  1 
ATOM   10308 C  C   . GLY J  1 50  ? 48.079  119.586 54.720 1.00 31.33  ? 44  GLY J C   1 
ATOM   10309 O  O   . GLY J  1 50  ? 47.824  118.675 55.517 1.00 34.03  ? 44  GLY J O   1 
ATOM   10310 N  N   . PHE J  1 51  ? 47.666  119.580 53.460 1.00 29.45  ? 45  PHE J N   1 
ATOM   10311 C  CA  . PHE J  1 51  ? 46.817  118.526 52.911 1.00 27.84  ? 45  PHE J CA  1 
ATOM   10312 C  C   . PHE J  1 51  ? 47.448  118.095 51.587 1.00 26.01  ? 45  PHE J C   1 
ATOM   10313 O  O   . PHE J  1 51  ? 47.431  118.863 50.621 1.00 22.71  ? 45  PHE J O   1 
ATOM   10314 C  CB  . PHE J  1 51  ? 45.424  119.128 52.683 1.00 27.00  ? 45  PHE J CB  1 
ATOM   10315 C  CG  . PHE J  1 51  ? 44.343  118.129 52.403 1.00 26.19  ? 45  PHE J CG  1 
ATOM   10316 C  CD1 . PHE J  1 51  ? 43.987  117.180 53.349 1.00 34.49  ? 45  PHE J CD1 1 
ATOM   10317 C  CD2 . PHE J  1 51  ? 43.642  118.178 51.207 1.00 21.70  ? 45  PHE J CD2 1 
ATOM   10318 C  CE1 . PHE J  1 51  ? 42.937  116.291 53.107 1.00 33.17  ? 45  PHE J CE1 1 
ATOM   10319 C  CE2 . PHE J  1 51  ? 42.599  117.299 50.954 1.00 33.18  ? 45  PHE J CE2 1 
ATOM   10320 C  CZ  . PHE J  1 51  ? 42.244  116.354 51.907 1.00 30.87  ? 45  PHE J CZ  1 
ATOM   10321 N  N   . HIS J  1 52  ? 48.010  116.885 51.539 1.00 22.86  ? 46  HIS J N   1 
ATOM   10322 C  CA  . HIS J  1 52  ? 48.657  116.415 50.307 1.00 33.45  ? 46  HIS J CA  1 
ATOM   10323 C  C   . HIS J  1 52  ? 48.492  114.945 49.934 1.00 29.73  ? 46  HIS J C   1 
ATOM   10324 O  O   . HIS J  1 52  ? 48.170  114.082 50.752 1.00 29.60  ? 46  HIS J O   1 
ATOM   10325 C  CB  . HIS J  1 52  ? 50.178  116.668 50.325 1.00 31.64  ? 46  HIS J CB  1 
ATOM   10326 C  CG  . HIS J  1 52  ? 50.606  117.858 51.123 1.00 39.89  ? 46  HIS J CG  1 
ATOM   10327 N  ND1 . HIS J  1 52  ? 51.074  117.755 52.416 1.00 44.55  ? 46  HIS J ND1 1 
ATOM   10328 C  CD2 . HIS J  1 52  ? 50.665  119.172 50.805 1.00 41.65  ? 46  HIS J CD2 1 
ATOM   10329 C  CE1 . HIS J  1 52  ? 51.402  118.956 52.859 1.00 37.43  ? 46  HIS J CE1 1 
ATOM   10330 N  NE2 . HIS J  1 52  ? 51.164  119.832 51.900 1.00 45.32  ? 46  HIS J NE2 1 
ATOM   10331 N  N   . VAL J  1 53  ? 48.751  114.678 48.665 1.00 31.67  ? 47  VAL J N   1 
ATOM   10332 C  CA  . VAL J  1 53  ? 48.716  113.327 48.155 1.00 32.51  ? 47  VAL J CA  1 
ATOM   10333 C  C   . VAL J  1 53  ? 50.187  112.911 48.073 1.00 33.12  ? 47  VAL J C   1 
ATOM   10334 O  O   . VAL J  1 53  ? 50.955  113.493 47.298 1.00 25.29  ? 47  VAL J O   1 
ATOM   10335 C  CB  . VAL J  1 53  ? 48.082  113.266 46.745 1.00 35.09  ? 47  VAL J CB  1 
ATOM   10336 C  CG1 . VAL J  1 53  ? 48.132  111.838 46.210 1.00 31.41  ? 47  VAL J CG1 1 
ATOM   10337 C  CG2 . VAL J  1 53  ? 46.640  113.757 46.805 1.00 29.26  ? 47  VAL J CG2 1 
ATOM   10338 N  N   . HIS J  1 54  ? 50.588  111.954 48.912 1.00 26.78  ? 48  HIS J N   1 
ATOM   10339 C  CA  . HIS J  1 54  ? 51.960  111.457 48.887 1.00 30.86  ? 48  HIS J CA  1 
ATOM   10340 C  C   . HIS J  1 54  ? 52.045  110.322 47.869 1.00 34.28  ? 48  HIS J C   1 
ATOM   10341 O  O   . HIS J  1 54  ? 51.033  109.719 47.514 1.00 38.49  ? 48  HIS J O   1 
ATOM   10342 C  CB  . HIS J  1 54  ? 52.398  111.006 50.281 1.00 28.86  ? 48  HIS J CB  1 
ATOM   10343 C  CG  . HIS J  1 54  ? 52.542  112.139 51.260 1.00 38.55  ? 48  HIS J CG  1 
ATOM   10344 N  ND1 . HIS J  1 54  ? 53.711  112.389 51.950 1.00 32.66  ? 48  HIS J ND1 1 
ATOM   10345 C  CD2 . HIS J  1 54  ? 51.658  113.083 51.667 1.00 34.42  ? 48  HIS J CD2 1 
ATOM   10346 C  CE1 . HIS J  1 54  ? 53.538  113.433 52.741 1.00 41.61  ? 48  HIS J CE1 1 
ATOM   10347 N  NE2 . HIS J  1 54  ? 52.300  113.873 52.588 1.00 44.06  ? 48  HIS J NE2 1 
ATOM   10348 N  N   . GLU J  1 55  ? 53.256  110.035 47.403 1.00 37.00  ? 49  GLU J N   1 
ATOM   10349 C  CA  . GLU J  1 55  ? 53.497  109.032 46.362 1.00 35.33  ? 49  GLU J CA  1 
ATOM   10350 C  C   . GLU J  1 55  ? 53.035  107.572 46.497 1.00 31.85  ? 49  GLU J C   1 
ATOM   10351 O  O   . GLU J  1 55  ? 52.560  106.978 45.528 1.00 29.64  ? 49  GLU J O   1 
ATOM   10352 C  CB  . GLU J  1 55  ? 54.989  109.027 46.012 1.00 32.24  ? 49  GLU J CB  1 
ATOM   10353 C  CG  . GLU J  1 55  ? 55.297  108.320 44.703 1.00 43.49  ? 49  GLU J CG  1 
ATOM   10354 C  CD  . GLU J  1 55  ? 56.784  108.265 44.382 1.00 47.11  ? 49  GLU J CD  1 
ATOM   10355 O  OE1 . GLU J  1 55  ? 57.125  107.764 43.290 1.00 44.55  ? 49  GLU J OE1 1 
ATOM   10356 O  OE2 . GLU J  1 55  ? 57.610  108.715 45.211 1.00 44.85  ? 49  GLU J OE2 1 
ATOM   10357 N  N   . PHE J  1 56  ? 53.158  106.977 47.669 1.00 28.21  ? 50  PHE J N   1 
ATOM   10358 C  CA  . PHE J  1 56  ? 52.792  105.575 47.765 1.00 33.34  ? 50  PHE J CA  1 
ATOM   10359 C  C   . PHE J  1 56  ? 51.613  105.237 48.651 1.00 36.85  ? 50  PHE J C   1 
ATOM   10360 O  O   . PHE J  1 56  ? 51.428  105.819 49.722 1.00 37.69  ? 50  PHE J O   1 
ATOM   10361 C  CB  . PHE J  1 56  ? 54.010  104.756 48.224 1.00 37.90  ? 50  PHE J CB  1 
ATOM   10362 C  CG  . PHE J  1 56  ? 55.246  104.972 47.387 1.00 31.16  ? 50  PHE J CG  1 
ATOM   10363 C  CD1 . PHE J  1 56  ? 55.251  104.654 46.030 1.00 41.60  ? 50  PHE J CD1 1 
ATOM   10364 C  CD2 . PHE J  1 56  ? 56.399  105.499 47.954 1.00 39.54  ? 50  PHE J CD2 1 
ATOM   10365 C  CE1 . PHE J  1 56  ? 56.390  104.857 45.242 1.00 41.71  ? 50  PHE J CE1 1 
ATOM   10366 C  CE2 . PHE J  1 56  ? 57.550  105.710 47.181 1.00 46.20  ? 50  PHE J CE2 1 
ATOM   10367 C  CZ  . PHE J  1 56  ? 57.547  105.388 45.822 1.00 40.09  ? 50  PHE J CZ  1 
ATOM   10368 N  N   . GLY J  1 57  ? 50.821  104.277 48.185 1.00 34.54  ? 51  GLY J N   1 
ATOM   10369 C  CA  . GLY J  1 57  ? 49.680  103.812 48.945 1.00 40.85  ? 51  GLY J CA  1 
ATOM   10370 C  C   . GLY J  1 57  ? 50.181  102.671 49.812 1.00 42.27  ? 51  GLY J C   1 
ATOM   10371 O  O   . GLY J  1 57  ? 49.615  101.571 49.833 1.00 44.00  ? 51  GLY J O   1 
ATOM   10372 N  N   . ASP J  1 58  ? 51.269  102.952 50.522 1.00 39.32  ? 52  ASP J N   1 
ATOM   10373 C  CA  . ASP J  1 58  ? 51.922  101.996 51.404 1.00 35.94  ? 52  ASP J CA  1 
ATOM   10374 C  C   . ASP J  1 58  ? 51.787  102.494 52.835 1.00 36.19  ? 52  ASP J C   1 
ATOM   10375 O  O   . ASP J  1 58  ? 52.341  103.525 53.208 1.00 33.19  ? 52  ASP J O   1 
ATOM   10376 C  CB  . ASP J  1 58  ? 53.398  101.867 50.997 1.00 35.99  ? 52  ASP J CB  1 
ATOM   10377 C  CG  . ASP J  1 58  ? 54.180  100.858 51.843 1.00 40.14  ? 52  ASP J CG  1 
ATOM   10378 O  OD1 . ASP J  1 58  ? 55.225  100.391 51.332 1.00 33.38  ? 52  ASP J OD1 1 
ATOM   10379 O  OD2 . ASP J  1 58  ? 53.784  100.544 52.998 1.00 32.22  ? 52  ASP J OD2 1 
ATOM   10380 N  N   . ASN J  1 59  ? 51.044  101.750 53.635 1.00 35.72  ? 53  ASN J N   1 
ATOM   10381 C  CA  . ASN J  1 59  ? 50.832  102.130 55.007 1.00 42.40  ? 53  ASN J CA  1 
ATOM   10382 C  C   . ASN J  1 59  ? 51.452  101.117 55.969 1.00 39.29  ? 53  ASN J C   1 
ATOM   10383 O  O   . ASN J  1 59  ? 51.209  101.166 57.172 1.00 38.82  ? 53  ASN J O   1 
ATOM   10384 C  CB  . ASN J  1 59  ? 49.327  102.256 55.264 1.00 58.58  ? 53  ASN J CB  1 
ATOM   10385 C  CG  . ASN J  1 59  ? 49.016  102.894 56.607 1.00 75.86  ? 53  ASN J CG  1 
ATOM   10386 O  OD1 . ASN J  1 59  ? 48.360  102.293 57.467 1.00 80.82  ? 53  ASN J OD1 1 
ATOM   10387 N  ND2 . ASN J  1 59  ? 49.489  104.121 56.796 1.00 84.39  ? 53  ASN J ND2 1 
ATOM   10388 N  N   . THR J  1 60  ? 52.261  100.204 55.448 1.00 39.96  ? 54  THR J N   1 
ATOM   10389 C  CA  . THR J  1 60  ? 52.879  99.184  56.292 1.00 38.63  ? 54  THR J CA  1 
ATOM   10390 C  C   . THR J  1 60  ? 53.527  99.760  57.556 1.00 44.23  ? 54  THR J C   1 
ATOM   10391 O  O   . THR J  1 60  ? 53.437  99.161  58.629 1.00 42.98  ? 54  THR J O   1 
ATOM   10392 C  CB  . THR J  1 60  ? 53.919  98.370  55.506 1.00 37.52  ? 54  THR J CB  1 
ATOM   10393 O  OG1 . THR J  1 60  ? 54.999  99.219  55.103 1.00 36.07  ? 54  THR J OG1 1 
ATOM   10394 C  CG2 . THR J  1 60  ? 53.273  97.767  54.256 1.00 45.12  ? 54  THR J CG2 1 
ATOM   10395 N  N   . ALA J  1 61  ? 54.167  100.921 57.440 1.00 43.89  ? 55  ALA J N   1 
ATOM   10396 C  CA  . ALA J  1 61  ? 54.791  101.551 58.602 1.00 48.71  ? 55  ALA J CA  1 
ATOM   10397 C  C   . ALA J  1 61  ? 54.082  102.870 58.937 1.00 47.75  ? 55  ALA J C   1 
ATOM   10398 O  O   . ALA J  1 61  ? 54.719  103.858 59.308 1.00 51.00  ? 55  ALA J O   1 
ATOM   10399 C  CB  . ALA J  1 61  ? 56.267  101.802 58.328 1.00 45.96  ? 55  ALA J CB  1 
ATOM   10400 N  N   . GLY J  1 62  ? 52.762  102.879 58.801 1.00 44.99  ? 56  GLY J N   1 
ATOM   10401 C  CA  . GLY J  1 62  ? 52.006  104.084 59.076 1.00 45.26  ? 56  GLY J CA  1 
ATOM   10402 C  C   . GLY J  1 62  ? 52.115  105.088 57.939 1.00 47.86  ? 56  GLY J C   1 
ATOM   10403 O  O   . GLY J  1 62  ? 52.516  104.738 56.821 1.00 45.27  ? 56  GLY J O   1 
ATOM   10404 N  N   . CYS J  1 63  ? 51.771  106.342 58.221 1.00 40.60  ? 57  CYS J N   1 
ATOM   10405 C  CA  . CYS J  1 63  ? 51.824  107.382 57.208 1.00 35.88  ? 57  CYS J CA  1 
ATOM   10406 C  C   . CYS J  1 63  ? 53.239  107.603 56.698 1.00 40.21  ? 57  CYS J C   1 
ATOM   10407 O  O   . CYS J  1 63  ? 53.447  108.084 55.578 1.00 35.38  ? 57  CYS J O   1 
ATOM   10408 C  CB  . CYS J  1 63  ? 51.242  108.676 57.772 1.00 38.73  ? 57  CYS J CB  1 
ATOM   10409 S  SG  . CYS J  1 63  ? 49.502  108.471 58.277 1.00 40.71  ? 57  CYS J SG  1 
ATOM   10410 N  N   . THR J  1 64  ? 54.209  107.216 57.517 1.00 41.43  ? 58  THR J N   1 
ATOM   10411 C  CA  . THR J  1 64  ? 55.615  107.363 57.168 1.00 42.35  ? 58  THR J CA  1 
ATOM   10412 C  C   . THR J  1 64  ? 55.994  106.660 55.877 1.00 38.07  ? 58  THR J C   1 
ATOM   10413 O  O   . THR J  1 64  ? 56.870  107.108 55.152 1.00 43.79  ? 58  THR J O   1 
ATOM   10414 C  CB  . THR J  1 64  ? 56.520  106.802 58.265 1.00 44.31  ? 58  THR J CB  1 
ATOM   10415 O  OG1 . THR J  1 64  ? 56.158  107.369 59.532 1.00 49.21  ? 58  THR J OG1 1 
ATOM   10416 C  CG2 . THR J  1 64  ? 57.966  107.127 57.951 1.00 39.52  ? 58  THR J CG2 1 
ATOM   10417 N  N   . SER J  1 65  ? 55.337  105.553 55.581 1.00 42.09  ? 59  SER J N   1 
ATOM   10418 C  CA  . SER J  1 65  ? 55.677  104.814 54.376 1.00 42.26  ? 59  SER J CA  1 
ATOM   10419 C  C   . SER J  1 65  ? 54.992  105.287 53.103 1.00 43.39  ? 59  SER J C   1 
ATOM   10420 O  O   . SER J  1 65  ? 55.138  104.663 52.054 1.00 47.74  ? 59  SER J O   1 
ATOM   10421 C  CB  . SER J  1 65  ? 55.420  103.316 54.596 1.00 44.74  ? 59  SER J CB  1 
ATOM   10422 O  OG  . SER J  1 65  ? 54.195  103.075 55.275 1.00 56.82  ? 59  SER J OG  1 
ATOM   10423 N  N   . ALA J  1 66  ? 54.254  106.390 53.176 1.00 42.17  ? 60  ALA J N   1 
ATOM   10424 C  CA  . ALA J  1 66  ? 53.570  106.894 51.985 1.00 38.78  ? 60  ALA J CA  1 
ATOM   10425 C  C   . ALA J  1 66  ? 54.550  107.617 51.064 1.00 36.02  ? 60  ALA J C   1 
ATOM   10426 O  O   . ALA J  1 66  ? 54.258  107.860 49.898 1.00 37.34  ? 60  ALA J O   1 
ATOM   10427 C  CB  . ALA J  1 66  ? 52.436  107.820 52.382 1.00 27.53  ? 60  ALA J CB  1 
ATOM   10428 N  N   . GLY J  1 67  ? 55.720  107.956 51.595 1.00 41.61  ? 61  GLY J N   1 
ATOM   10429 C  CA  . GLY J  1 67  ? 56.725  108.632 50.799 1.00 36.48  ? 61  GLY J CA  1 
ATOM   10430 C  C   . GLY J  1 67  ? 56.584  110.140 50.759 1.00 36.83  ? 61  GLY J C   1 
ATOM   10431 O  O   . GLY J  1 67  ? 55.946  110.759 51.618 1.00 32.24  ? 61  GLY J O   1 
ATOM   10432 N  N   . PRO J  1 68  ? 57.195  110.767 49.756 1.00 35.35  ? 62  PRO J N   1 
ATOM   10433 C  CA  . PRO J  1 68  ? 57.135  112.223 49.602 1.00 36.65  ? 62  PRO J CA  1 
ATOM   10434 C  C   . PRO J  1 68  ? 55.841  112.633 48.904 1.00 32.92  ? 62  PRO J C   1 
ATOM   10435 O  O   . PRO J  1 68  ? 55.025  111.792 48.551 1.00 35.68  ? 62  PRO J O   1 
ATOM   10436 C  CB  . PRO J  1 68  ? 58.358  112.512 48.743 1.00 34.29  ? 62  PRO J CB  1 
ATOM   10437 C  CG  . PRO J  1 68  ? 58.342  111.339 47.788 1.00 32.70  ? 62  PRO J CG  1 
ATOM   10438 C  CD  . PRO J  1 68  ? 58.071  110.161 48.734 1.00 35.11  ? 62  PRO J CD  1 
ATOM   10439 N  N   . HIS J  1 69  ? 55.646  113.928 48.725 1.00 32.43  ? 63  HIS J N   1 
ATOM   10440 C  CA  . HIS J  1 69  ? 54.465  114.413 48.021 1.00 37.65  ? 63  HIS J CA  1 
ATOM   10441 C  C   . HIS J  1 69  ? 54.536  113.828 46.590 1.00 34.90  ? 63  HIS J C   1 
ATOM   10442 O  O   . HIS J  1 69  ? 55.613  113.791 45.992 1.00 38.24  ? 63  HIS J O   1 
ATOM   10443 C  CB  . HIS J  1 69  ? 54.481  115.958 47.987 1.00 30.66  ? 63  HIS J CB  1 
ATOM   10444 C  CG  . HIS J  1 69  ? 54.328  116.602 49.339 1.00 31.35  ? 63  HIS J CG  1 
ATOM   10445 N  ND1 . HIS J  1 69  ? 54.343  117.969 49.522 1.00 27.59  ? 63  HIS J ND1 1 
ATOM   10446 C  CD2 . HIS J  1 69  ? 54.142  116.065 50.569 1.00 33.87  ? 63  HIS J CD2 1 
ATOM   10447 C  CE1 . HIS J  1 69  ? 54.172  118.245 50.803 1.00 32.11  ? 63  HIS J CE1 1 
ATOM   10448 N  NE2 . HIS J  1 69  ? 54.047  117.106 51.460 1.00 29.44  ? 63  HIS J NE2 1 
ATOM   10449 N  N   . PHE J  1 70  ? 53.411  113.346 46.062 1.00 32.78  ? 64  PHE J N   1 
ATOM   10450 C  CA  . PHE J  1 70  ? 53.362  112.776 44.707 1.00 34.59  ? 64  PHE J CA  1 
ATOM   10451 C  C   . PHE J  1 70  ? 53.908  113.825 43.729 1.00 38.25  ? 64  PHE J C   1 
ATOM   10452 O  O   . PHE J  1 70  ? 53.304  114.877 43.536 1.00 39.72  ? 64  PHE J O   1 
ATOM   10453 C  CB  . PHE J  1 70  ? 51.917  112.422 44.346 1.00 33.44  ? 64  PHE J CB  1 
ATOM   10454 C  CG  . PHE J  1 70  ? 51.742  111.888 42.947 1.00 40.97  ? 64  PHE J CG  1 
ATOM   10455 C  CD1 . PHE J  1 70  ? 50.608  112.211 42.210 1.00 39.34  ? 64  PHE J CD1 1 
ATOM   10456 C  CD2 . PHE J  1 70  ? 52.693  111.047 42.376 1.00 45.72  ? 64  PHE J CD2 1 
ATOM   10457 C  CE1 . PHE J  1 70  ? 50.417  111.706 40.919 1.00 47.72  ? 64  PHE J CE1 1 
ATOM   10458 C  CE2 . PHE J  1 70  ? 52.513  110.534 41.083 1.00 54.74  ? 64  PHE J CE2 1 
ATOM   10459 C  CZ  . PHE J  1 70  ? 51.371  110.866 40.354 1.00 54.05  ? 64  PHE J CZ  1 
ATOM   10460 N  N   . ASN J  1 71  ? 55.037  113.538 43.098 1.00 38.17  ? 65  ASN J N   1 
ATOM   10461 C  CA  . ASN J  1 71  ? 55.644  114.526 42.222 1.00 42.16  ? 65  ASN J CA  1 
ATOM   10462 C  C   . ASN J  1 71  ? 56.220  113.982 40.910 1.00 43.09  ? 65  ASN J C   1 
ATOM   10463 O  O   . ASN J  1 71  ? 57.422  114.030 40.672 1.00 41.52  ? 65  ASN J O   1 
ATOM   10464 C  CB  . ASN J  1 71  ? 56.720  115.261 43.034 1.00 34.66  ? 65  ASN J CB  1 
ATOM   10465 C  CG  . ASN J  1 71  ? 57.363  116.396 42.276 1.00 40.68  ? 65  ASN J CG  1 
ATOM   10466 O  OD1 . ASN J  1 71  ? 56.744  117.027 41.408 1.00 37.96  ? 65  ASN J OD1 1 
ATOM   10467 N  ND2 . ASN J  1 71  ? 58.612  116.682 42.617 1.00 36.52  ? 65  ASN J ND2 1 
ATOM   10468 N  N   . PRO J  1 72  ? 55.352  113.495 40.019 1.00 44.53  ? 66  PRO J N   1 
ATOM   10469 C  CA  . PRO J  1 72  ? 55.805  112.950 38.739 1.00 49.50  ? 66  PRO J CA  1 
ATOM   10470 C  C   . PRO J  1 72  ? 56.561  113.925 37.829 1.00 55.42  ? 66  PRO J C   1 
ATOM   10471 O  O   . PRO J  1 72  ? 57.514  113.529 37.153 1.00 57.52  ? 66  PRO J O   1 
ATOM   10472 C  CB  . PRO J  1 72  ? 54.513  112.443 38.107 1.00 44.21  ? 66  PRO J CB  1 
ATOM   10473 C  CG  . PRO J  1 72  ? 53.497  113.383 38.637 1.00 50.56  ? 66  PRO J CG  1 
ATOM   10474 C  CD  . PRO J  1 72  ? 53.883  113.518 40.089 1.00 45.71  ? 66  PRO J CD  1 
ATOM   10475 N  N   . LEU J  1 73  ? 56.151  115.190 37.809 1.00 54.10  ? 67  LEU J N   1 
ATOM   10476 C  CA  . LEU J  1 73  ? 56.822  116.167 36.951 1.00 51.64  ? 67  LEU J CA  1 
ATOM   10477 C  C   . LEU J  1 73  ? 58.118  116.698 37.555 1.00 47.41  ? 67  LEU J C   1 
ATOM   10478 O  O   . LEU J  1 73  ? 58.755  117.585 36.989 1.00 44.53  ? 67  LEU J O   1 
ATOM   10479 C  CB  . LEU J  1 73  ? 55.884  117.334 36.644 1.00 52.71  ? 67  LEU J CB  1 
ATOM   10480 C  CG  . LEU J  1 73  ? 54.533  116.916 36.070 1.00 55.77  ? 67  LEU J CG  1 
ATOM   10481 C  CD1 . LEU J  1 73  ? 53.652  118.138 35.870 1.00 60.05  ? 67  LEU J CD1 1 
ATOM   10482 C  CD2 . LEU J  1 73  ? 54.751  116.183 34.763 1.00 53.33  ? 67  LEU J CD2 1 
ATOM   10483 N  N   . SER J  1 74  ? 58.496  116.163 38.712 1.00 45.54  ? 68  SER J N   1 
ATOM   10484 C  CA  . SER J  1 74  ? 59.729  116.573 39.383 1.00 49.06  ? 68  SER J CA  1 
ATOM   10485 C  C   . SER J  1 74  ? 59.865  118.080 39.597 1.00 48.68  ? 68  SER J C   1 
ATOM   10486 O  O   . SER J  1 74  ? 60.835  118.687 39.150 1.00 45.79  ? 68  SER J O   1 
ATOM   10487 C  CB  . SER J  1 74  ? 60.944  116.091 38.585 1.00 47.17  ? 68  SER J CB  1 
ATOM   10488 O  OG  . SER J  1 74  ? 60.834  114.714 38.267 1.00 64.87  ? 68  SER J OG  1 
ATOM   10489 N  N   . ARG J  1 75  ? 58.910  118.692 40.285 1.00 48.52  ? 69  ARG J N   1 
ATOM   10490 C  CA  . ARG J  1 75  ? 58.996  120.127 40.520 1.00 49.03  ? 69  ARG J CA  1 
ATOM   10491 C  C   . ARG J  1 75  ? 59.160  120.463 41.991 1.00 43.66  ? 69  ARG J C   1 
ATOM   10492 O  O   . ARG J  1 75  ? 59.073  119.586 42.840 1.00 50.48  ? 69  ARG J O   1 
ATOM   10493 C  CB  . ARG J  1 75  ? 57.773  120.819 39.930 1.00 53.48  ? 69  ARG J CB  1 
ATOM   10494 C  CG  . ARG J  1 75  ? 57.823  120.815 38.409 1.00 62.01  ? 69  ARG J CG  1 
ATOM   10495 C  CD  . ARG J  1 75  ? 56.650  121.524 37.795 1.00 73.04  ? 69  ARG J CD  1 
ATOM   10496 N  NE  . ARG J  1 75  ? 56.632  121.335 36.351 1.00 80.22  ? 69  ARG J NE  1 
ATOM   10497 C  CZ  . ARG J  1 75  ? 55.570  121.556 35.586 1.00 81.62  ? 69  ARG J CZ  1 
ATOM   10498 N  NH1 . ARG J  1 75  ? 54.433  121.980 36.128 1.00 78.55  ? 69  ARG J NH1 1 
ATOM   10499 N  NH2 . ARG J  1 75  ? 55.642  121.340 34.282 1.00 81.52  ? 69  ARG J NH2 1 
ATOM   10500 N  N   . LYS J  1 76  ? 59.436  121.724 42.294 1.00 42.01  ? 70  LYS J N   1 
ATOM   10501 C  CA  . LYS J  1 76  ? 59.603  122.132 43.680 1.00 35.89  ? 70  LYS J CA  1 
ATOM   10502 C  C   . LYS J  1 76  ? 58.224  122.275 44.290 1.00 34.11  ? 70  LYS J C   1 
ATOM   10503 O  O   . LYS J  1 76  ? 57.232  122.433 43.575 1.00 36.90  ? 70  LYS J O   1 
ATOM   10504 C  CB  . LYS J  1 76  ? 60.379  123.447 43.761 1.00 40.38  ? 70  LYS J CB  1 
ATOM   10505 C  CG  . LYS J  1 76  ? 61.836  123.300 43.365 1.00 42.57  ? 70  LYS J CG  1 
ATOM   10506 C  CD  . LYS J  1 76  ? 62.601  124.622 43.367 1.00 57.85  ? 70  LYS J CD  1 
ATOM   10507 C  CE  . LYS J  1 76  ? 62.249  125.494 42.165 1.00 70.08  ? 70  LYS J CE  1 
ATOM   10508 N  NZ  . LYS J  1 76  ? 63.160  126.671 42.030 1.00 71.57  ? 70  LYS J NZ  1 
ATOM   10509 N  N   . HIS J  1 77  ? 58.157  122.215 45.613 1.00 32.62  ? 71  HIS J N   1 
ATOM   10510 C  CA  . HIS J  1 77  ? 56.881  122.315 46.308 1.00 37.11  ? 71  HIS J CA  1 
ATOM   10511 C  C   . HIS J  1 77  ? 56.222  123.703 46.194 1.00 39.92  ? 71  HIS J C   1 
ATOM   10512 O  O   . HIS J  1 77  ? 56.892  124.732 46.273 1.00 35.42  ? 71  HIS J O   1 
ATOM   10513 C  CB  . HIS J  1 77  ? 57.071  121.954 47.782 1.00 28.77  ? 71  HIS J CB  1 
ATOM   10514 C  CG  . HIS J  1 77  ? 55.830  122.102 48.598 1.00 33.16  ? 71  HIS J CG  1 
ATOM   10515 N  ND1 . HIS J  1 77  ? 54.810  121.175 48.578 1.00 37.35  ? 71  HIS J ND1 1 
ATOM   10516 C  CD2 . HIS J  1 77  ? 55.417  123.098 49.416 1.00 37.84  ? 71  HIS J CD2 1 
ATOM   10517 C  CE1 . HIS J  1 77  ? 53.821  121.595 49.348 1.00 40.67  ? 71  HIS J CE1 1 
ATOM   10518 N  NE2 . HIS J  1 77  ? 54.165  122.760 49.868 1.00 40.03  ? 71  HIS J NE2 1 
ATOM   10519 N  N   . GLY J  1 78  ? 54.905  123.722 46.001 1.00 41.00  ? 72  GLY J N   1 
ATOM   10520 C  CA  . GLY J  1 78  ? 54.192  124.984 45.914 1.00 37.49  ? 72  GLY J CA  1 
ATOM   10521 C  C   . GLY J  1 78  ? 52.764  124.867 46.418 1.00 37.55  ? 72  GLY J C   1 
ATOM   10522 O  O   . GLY J  1 78  ? 52.356  123.825 46.941 1.00 34.02  ? 72  GLY J O   1 
ATOM   10523 N  N   . GLY J  1 79  ? 52.005  125.950 46.281 1.00 38.43  ? 73  GLY J N   1 
ATOM   10524 C  CA  . GLY J  1 79  ? 50.611  125.936 46.683 1.00 35.00  ? 73  GLY J CA  1 
ATOM   10525 C  C   . GLY J  1 79  ? 49.788  125.396 45.517 1.00 39.02  ? 73  GLY J C   1 
ATOM   10526 O  O   . GLY J  1 79  ? 50.244  125.384 44.369 1.00 30.87  ? 73  GLY J O   1 
ATOM   10527 N  N   . PRO J  1 80  ? 48.561  124.947 45.765 1.00 37.27  ? 74  PRO J N   1 
ATOM   10528 C  CA  . PRO J  1 80  ? 47.768  124.421 44.649 1.00 39.06  ? 74  PRO J CA  1 
ATOM   10529 C  C   . PRO J  1 80  ? 47.573  125.363 43.466 1.00 44.19  ? 74  PRO J C   1 
ATOM   10530 O  O   . PRO J  1 80  ? 47.500  124.919 42.326 1.00 45.39  ? 74  PRO J O   1 
ATOM   10531 C  CB  . PRO J  1 80  ? 46.454  124.019 45.314 1.00 36.11  ? 74  PRO J CB  1 
ATOM   10532 C  CG  . PRO J  1 80  ? 46.410  124.873 46.556 1.00 37.55  ? 74  PRO J CG  1 
ATOM   10533 C  CD  . PRO J  1 80  ? 47.826  124.881 47.034 1.00 33.32  ? 74  PRO J CD  1 
ATOM   10534 N  N   . LYS J  1 81  ? 47.507  126.663 43.729 1.00 52.24  ? 75  LYS J N   1 
ATOM   10535 C  CA  . LYS J  1 81  ? 47.310  127.643 42.659 1.00 52.56  ? 75  LYS J CA  1 
ATOM   10536 C  C   . LYS J  1 81  ? 48.574  127.953 41.840 1.00 50.51  ? 75  LYS J C   1 
ATOM   10537 O  O   . LYS J  1 81  ? 48.475  128.480 40.736 1.00 46.09  ? 75  LYS J O   1 
ATOM   10538 C  CB  . LYS J  1 81  ? 46.771  128.960 43.234 1.00 54.61  ? 75  LYS J CB  1 
ATOM   10539 C  CG  . LYS J  1 81  ? 45.491  128.864 44.065 1.00 69.90  ? 75  LYS J CG  1 
ATOM   10540 C  CD  . LYS J  1 81  ? 45.125  130.247 44.634 1.00 79.57  ? 75  LYS J CD  1 
ATOM   10541 C  CE  . LYS J  1 81  ? 43.829  130.249 45.452 1.00 87.81  ? 75  LYS J CE  1 
ATOM   10542 N  NZ  . LYS J  1 81  ? 43.431  131.633 45.899 1.00 88.70  ? 75  LYS J NZ  1 
ATOM   10543 N  N   . ASP J  1 82  ? 49.755  127.630 42.366 1.00 49.24  ? 76  ASP J N   1 
ATOM   10544 C  CA  . ASP J  1 82  ? 51.004  127.928 41.660 1.00 48.80  ? 76  ASP J CA  1 
ATOM   10545 C  C   . ASP J  1 82  ? 51.343  127.090 40.434 1.00 49.28  ? 76  ASP J C   1 
ATOM   10546 O  O   . ASP J  1 82  ? 50.740  126.053 40.160 1.00 49.61  ? 76  ASP J O   1 
ATOM   10547 C  CB  . ASP J  1 82  ? 52.199  127.852 42.618 1.00 47.48  ? 76  ASP J CB  1 
ATOM   10548 C  CG  . ASP J  1 82  ? 52.057  128.780 43.805 1.00 48.43  ? 76  ASP J CG  1 
ATOM   10549 O  OD1 . ASP J  1 82  ? 51.546  129.901 43.611 1.00 60.62  ? 76  ASP J OD1 1 
ATOM   10550 O  OD2 . ASP J  1 82  ? 52.467  128.400 44.927 1.00 43.32  ? 76  ASP J OD2 1 
ATOM   10551 N  N   . GLU J  1 83  ? 52.340  127.569 39.707 1.00 55.32  ? 77  GLU J N   1 
ATOM   10552 C  CA  . GLU J  1 83  ? 52.839  126.902 38.521 1.00 57.94  ? 77  GLU J CA  1 
ATOM   10553 C  C   . GLU J  1 83  ? 53.844  125.850 38.988 1.00 53.12  ? 77  GLU J C   1 
ATOM   10554 O  O   . GLU J  1 83  ? 53.779  124.690 38.593 1.00 52.94  ? 77  GLU J O   1 
ATOM   10555 C  CB  . GLU J  1 83  ? 53.534  127.913 37.614 1.00 72.35  ? 77  GLU J CB  1 
ATOM   10556 C  CG  . GLU J  1 83  ? 54.198  127.288 36.406 1.00 89.64  ? 77  GLU J CG  1 
ATOM   10557 C  CD  . GLU J  1 83  ? 53.204  126.597 35.502 1.00 98.27  ? 77  GLU J CD  1 
ATOM   10558 O  OE1 . GLU J  1 83  ? 52.542  125.640 35.958 1.00 102.79 ? 77  GLU J OE1 1 
ATOM   10559 O  OE2 . GLU J  1 83  ? 53.081  127.018 34.332 1.00 107.01 ? 77  GLU J OE2 1 
ATOM   10560 N  N   . GLU J  1 84  ? 54.786  126.266 39.826 1.00 48.61  ? 78  GLU J N   1 
ATOM   10561 C  CA  . GLU J  1 84  ? 55.771  125.336 40.359 1.00 47.50  ? 78  GLU J CA  1 
ATOM   10562 C  C   . GLU J  1 84  ? 55.132  124.673 41.585 1.00 45.92  ? 78  GLU J C   1 
ATOM   10563 O  O   . GLU J  1 84  ? 55.048  125.269 42.661 1.00 45.53  ? 78  GLU J O   1 
ATOM   10564 C  CB  . GLU J  1 84  ? 57.053  126.080 40.756 1.00 44.88  ? 78  GLU J CB  1 
ATOM   10565 C  CG  . GLU J  1 84  ? 58.232  125.193 41.195 1.00 59.04  ? 78  GLU J CG  1 
ATOM   10566 C  CD  . GLU J  1 84  ? 58.896  124.433 40.035 1.00 71.08  ? 78  GLU J CD  1 
ATOM   10567 O  OE1 . GLU J  1 84  ? 59.945  123.777 40.260 1.00 60.76  ? 78  GLU J OE1 1 
ATOM   10568 O  OE2 . GLU J  1 84  ? 58.372  124.488 38.898 1.00 74.09  ? 78  GLU J OE2 1 
ATOM   10569 N  N   . ARG J  1 85  ? 54.657  123.445 41.412 1.00 44.46  ? 79  ARG J N   1 
ATOM   10570 C  CA  . ARG J  1 85  ? 54.039  122.709 42.514 1.00 41.17  ? 79  ARG J CA  1 
ATOM   10571 C  C   . ARG J  1 85  ? 54.029  121.223 42.231 1.00 37.49  ? 79  ARG J C   1 
ATOM   10572 O  O   . ARG J  1 85  ? 54.157  120.794 41.087 1.00 42.48  ? 79  ARG J O   1 
ATOM   10573 C  CB  . ARG J  1 85  ? 52.603  123.187 42.739 1.00 33.51  ? 79  ARG J CB  1 
ATOM   10574 C  CG  . ARG J  1 85  ? 51.638  122.863 41.595 1.00 32.97  ? 79  ARG J CG  1 
ATOM   10575 C  CD  . ARG J  1 85  ? 50.727  121.680 41.948 1.00 36.86  ? 79  ARG J CD  1 
ATOM   10576 N  NE  . ARG J  1 85  ? 49.327  122.067 41.932 1.00 29.71  ? 79  ARG J NE  1 
ATOM   10577 C  CZ  . ARG J  1 85  ? 48.304  121.263 42.208 1.00 38.39  ? 79  ARG J CZ  1 
ATOM   10578 N  NH1 . ARG J  1 85  ? 48.491  119.992 42.536 1.00 36.93  ? 79  ARG J NH1 1 
ATOM   10579 N  NH2 . ARG J  1 85  ? 47.072  121.746 42.144 1.00 38.94  ? 79  ARG J NH2 1 
ATOM   10580 N  N   . HIS J  1 86  ? 53.879  120.437 43.285 1.00 40.19  ? 80  HIS J N   1 
ATOM   10581 C  CA  . HIS J  1 86  ? 53.826  118.987 43.159 1.00 35.26  ? 80  HIS J CA  1 
ATOM   10582 C  C   . HIS J  1 86  ? 52.414  118.615 42.743 1.00 33.12  ? 80  HIS J C   1 
ATOM   10583 O  O   . HIS J  1 86  ? 51.450  119.240 43.176 1.00 31.40  ? 80  HIS J O   1 
ATOM   10584 C  CB  . HIS J  1 86  ? 54.125  118.328 44.508 1.00 36.50  ? 80  HIS J CB  1 
ATOM   10585 C  CG  . HIS J  1 86  ? 55.508  118.575 45.011 1.00 31.81  ? 80  HIS J CG  1 
ATOM   10586 N  ND1 . HIS J  1 86  ? 55.802  118.668 46.355 1.00 36.78  ? 80  HIS J ND1 1 
ATOM   10587 C  CD2 . HIS J  1 86  ? 56.684  118.723 44.355 1.00 30.80  ? 80  HIS J CD2 1 
ATOM   10588 C  CE1 . HIS J  1 86  ? 57.101  118.864 46.505 1.00 22.71  ? 80  HIS J CE1 1 
ATOM   10589 N  NE2 . HIS J  1 86  ? 57.658  118.900 45.308 1.00 28.31  ? 80  HIS J NE2 1 
ATOM   10590 N  N   . VAL J  1 87  ? 52.280  117.603 41.903 1.00 36.21  ? 81  VAL J N   1 
ATOM   10591 C  CA  . VAL J  1 87  ? 50.950  117.181 41.505 1.00 33.94  ? 81  VAL J CA  1 
ATOM   10592 C  C   . VAL J  1 87  ? 50.066  116.977 42.736 1.00 33.64  ? 81  VAL J C   1 
ATOM   10593 O  O   . VAL J  1 87  ? 48.889  117.306 42.713 1.00 34.79  ? 81  VAL J O   1 
ATOM   10594 C  CB  . VAL J  1 87  ? 51.001  115.871 40.722 1.00 36.82  ? 81  VAL J CB  1 
ATOM   10595 C  CG1 . VAL J  1 87  ? 49.601  115.260 40.623 1.00 34.33  ? 81  VAL J CG1 1 
ATOM   10596 C  CG2 . VAL J  1 87  ? 51.565  116.139 39.341 1.00 36.31  ? 81  VAL J CG2 1 
ATOM   10597 N  N   . GLY J  1 88  ? 50.640  116.463 43.821 1.00 30.55  ? 82  GLY J N   1 
ATOM   10598 C  CA  . GLY J  1 88  ? 49.846  116.216 45.011 1.00 33.37  ? 82  GLY J CA  1 
ATOM   10599 C  C   . GLY J  1 88  ? 49.674  117.361 45.992 1.00 34.79  ? 82  GLY J C   1 
ATOM   10600 O  O   . GLY J  1 88  ? 49.072  117.180 47.060 1.00 30.29  ? 82  GLY J O   1 
ATOM   10601 N  N   . ASP J  1 89  ? 50.189  118.536 45.644 1.00 32.97  ? 83  ASP J N   1 
ATOM   10602 C  CA  . ASP J  1 89  ? 50.094  119.697 46.526 1.00 37.50  ? 83  ASP J CA  1 
ATOM   10603 C  C   . ASP J  1 89  ? 48.695  120.300 46.537 1.00 40.66  ? 83  ASP J C   1 
ATOM   10604 O  O   . ASP J  1 89  ? 48.347  121.097 45.665 1.00 40.37  ? 83  ASP J O   1 
ATOM   10605 C  CB  . ASP J  1 89  ? 51.110  120.758 46.104 1.00 37.37  ? 83  ASP J CB  1 
ATOM   10606 C  CG  . ASP J  1 89  ? 52.538  120.351 46.413 1.00 42.45  ? 83  ASP J CG  1 
ATOM   10607 O  OD1 . ASP J  1 89  ? 52.738  119.343 47.142 1.00 38.58  ? 83  ASP J OD1 1 
ATOM   10608 O  OD2 . ASP J  1 89  ? 53.460  121.051 45.938 1.00 30.39  ? 83  ASP J OD2 1 
ATOM   10609 N  N   . LEU J  1 90  ? 47.890  119.924 47.524 1.00 32.06  ? 84  LEU J N   1 
ATOM   10610 C  CA  . LEU J  1 90  ? 46.541  120.442 47.594 1.00 37.31  ? 84  LEU J CA  1 
ATOM   10611 C  C   . LEU J  1 90  ? 46.416  121.523 48.664 1.00 35.10  ? 84  LEU J C   1 
ATOM   10612 O  O   . LEU J  1 90  ? 45.340  121.751 49.200 1.00 43.38  ? 84  LEU J O   1 
ATOM   10613 C  CB  . LEU J  1 90  ? 45.540  119.300 47.860 1.00 36.72  ? 84  LEU J CB  1 
ATOM   10614 C  CG  . LEU J  1 90  ? 45.422  118.180 46.811 1.00 39.93  ? 84  LEU J CG  1 
ATOM   10615 C  CD1 . LEU J  1 90  ? 44.461  117.118 47.314 1.00 27.98  ? 84  LEU J CD1 1 
ATOM   10616 C  CD2 . LEU J  1 90  ? 44.945  118.728 45.472 1.00 39.10  ? 84  LEU J CD2 1 
ATOM   10617 N  N   . GLY J  1 91  ? 47.523  122.175 48.987 1.00 32.01  ? 85  GLY J N   1 
ATOM   10618 C  CA  . GLY J  1 91  ? 47.485  123.240 49.975 1.00 33.58  ? 85  GLY J CA  1 
ATOM   10619 C  C   . GLY J  1 91  ? 47.112  122.885 51.405 1.00 32.11  ? 85  GLY J C   1 
ATOM   10620 O  O   . GLY J  1 91  ? 47.588  121.894 51.965 1.00 32.69  ? 85  GLY J O   1 
ATOM   10621 N  N   . ASN J  1 92  ? 46.265  123.717 52.002 1.00 29.94  ? 86  ASN J N   1 
ATOM   10622 C  CA  . ASN J  1 92  ? 45.823  123.519 53.380 1.00 30.13  ? 86  ASN J CA  1 
ATOM   10623 C  C   . ASN J  1 92  ? 44.328  123.311 53.518 1.00 31.11  ? 86  ASN J C   1 
ATOM   10624 O  O   . ASN J  1 92  ? 43.560  123.667 52.627 1.00 40.38  ? 86  ASN J O   1 
ATOM   10625 C  CB  . ASN J  1 92  ? 46.151  124.747 54.223 1.00 22.54  ? 86  ASN J CB  1 
ATOM   10626 C  CG  . ASN J  1 92  ? 47.603  124.857 54.555 1.00 34.87  ? 86  ASN J CG  1 
ATOM   10627 O  OD1 . ASN J  1 92  ? 48.123  124.095 55.372 1.00 36.08  ? 86  ASN J OD1 1 
ATOM   10628 N  ND2 . ASN J  1 92  ? 48.283  125.815 53.924 1.00 20.42  ? 86  ASN J ND2 1 
ATOM   10629 N  N   . VAL J  1 93  ? 43.932  122.727 54.646 1.00 28.60  ? 87  VAL J N   1 
ATOM   10630 C  CA  . VAL J  1 93  ? 42.526  122.573 54.993 1.00 33.06  ? 87  VAL J CA  1 
ATOM   10631 C  C   . VAL J  1 93  ? 42.465  123.324 56.330 1.00 36.94  ? 87  VAL J C   1 
ATOM   10632 O  O   . VAL J  1 93  ? 43.509  123.551 56.985 1.00 25.93  ? 87  VAL J O   1 
ATOM   10633 C  CB  . VAL J  1 93  ? 42.066  121.103 55.189 1.00 29.97  ? 87  VAL J CB  1 
ATOM   10634 C  CG1 . VAL J  1 93  ? 42.167  120.362 53.885 1.00 33.56  ? 87  VAL J CG1 1 
ATOM   10635 C  CG2 . VAL J  1 93  ? 42.867  120.426 56.298 1.00 36.50  ? 87  VAL J CG2 1 
ATOM   10636 N  N   . THR J  1 94  ? 41.262  123.723 56.729 1.00 31.65  ? 88  THR J N   1 
ATOM   10637 C  CA  . THR J  1 94  ? 41.121  124.490 57.950 1.00 37.01  ? 88  THR J CA  1 
ATOM   10638 C  C   . THR J  1 94  ? 40.254  123.819 58.992 1.00 37.39  ? 88  THR J C   1 
ATOM   10639 O  O   . THR J  1 94  ? 39.130  123.402 58.713 1.00 33.84  ? 88  THR J O   1 
ATOM   10640 C  CB  . THR J  1 94  ? 40.513  125.874 57.661 1.00 39.68  ? 88  THR J CB  1 
ATOM   10641 O  OG1 . THR J  1 94  ? 41.249  126.524 56.616 1.00 38.58  ? 88  THR J OG1 1 
ATOM   10642 C  CG2 . THR J  1 94  ? 40.557  126.725 58.910 1.00 43.36  ? 88  THR J CG2 1 
ATOM   10643 N  N   . ALA J  1 95  ? 40.780  123.735 60.203 1.00 37.94  ? 89  ALA J N   1 
ATOM   10644 C  CA  . ALA J  1 95  ? 40.044  123.139 61.296 1.00 40.94  ? 89  ALA J CA  1 
ATOM   10645 C  C   . ALA J  1 95  ? 39.463  124.258 62.136 1.00 45.27  ? 89  ALA J C   1 
ATOM   10646 O  O   . ALA J  1 95  ? 40.176  125.193 62.506 1.00 44.24  ? 89  ALA J O   1 
ATOM   10647 C  CB  . ALA J  1 95  ? 40.962  122.288 62.135 1.00 44.62  ? 89  ALA J CB  1 
ATOM   10648 N  N   . ASP J  1 96  ? 38.171  124.159 62.438 1.00 49.09  ? 90  ASP J N   1 
ATOM   10649 C  CA  . ASP J  1 96  ? 37.482  125.164 63.249 1.00 50.69  ? 90  ASP J CA  1 
ATOM   10650 C  C   . ASP J  1 96  ? 37.737  124.926 64.742 1.00 51.43  ? 90  ASP J C   1 
ATOM   10651 O  O   . ASP J  1 96  ? 38.540  124.070 65.113 1.00 45.11  ? 90  ASP J O   1 
ATOM   10652 C  CB  . ASP J  1 96  ? 35.981  125.144 62.934 1.00 47.85  ? 90  ASP J CB  1 
ATOM   10653 C  CG  . ASP J  1 96  ? 35.696  125.216 61.420 1.00 61.72  ? 90  ASP J CG  1 
ATOM   10654 O  OD1 . ASP J  1 96  ? 36.278  126.088 60.718 1.00 52.03  ? 90  ASP J OD1 1 
ATOM   10655 O  OD2 . ASP J  1 96  ? 34.883  124.397 60.929 1.00 64.26  ? 90  ASP J OD2 1 
ATOM   10656 N  N   . LYS J  1 97  ? 37.079  125.691 65.603 1.00 57.14  ? 91  LYS J N   1 
ATOM   10657 C  CA  . LYS J  1 97  ? 37.297  125.527 67.033 1.00 59.63  ? 91  LYS J CA  1 
ATOM   10658 C  C   . LYS J  1 97  ? 36.696  124.226 67.561 1.00 57.61  ? 91  LYS J C   1 
ATOM   10659 O  O   . LYS J  1 97  ? 37.010  123.786 68.664 1.00 51.67  ? 91  LYS J O   1 
ATOM   10660 C  CB  . LYS J  1 97  ? 36.760  126.748 67.800 1.00 66.53  ? 91  LYS J CB  1 
ATOM   10661 C  CG  . LYS J  1 97  ? 35.402  127.273 67.352 1.00 78.44  ? 91  LYS J CG  1 
ATOM   10662 C  CD  . LYS J  1 97  ? 35.111  128.622 68.018 1.00 90.13  ? 91  LYS J CD  1 
ATOM   10663 C  CE  . LYS J  1 97  ? 33.822  129.276 67.510 1.00 95.34  ? 91  LYS J CE  1 
ATOM   10664 N  NZ  . LYS J  1 97  ? 32.587  128.588 67.986 1.00 96.23  ? 91  LYS J NZ  1 
ATOM   10665 N  N   . ASP J  1 98  ? 35.849  123.602 66.751 1.00 59.76  ? 92  ASP J N   1 
ATOM   10666 C  CA  . ASP J  1 98  ? 35.209  122.340 67.108 1.00 56.94  ? 92  ASP J CA  1 
ATOM   10667 C  C   . ASP J  1 98  ? 36.156  121.188 66.753 1.00 57.67  ? 92  ASP J C   1 
ATOM   10668 O  O   . ASP J  1 98  ? 35.769  120.014 66.774 1.00 49.71  ? 92  ASP J O   1 
ATOM   10669 C  CB  . ASP J  1 98  ? 33.892  122.197 66.338 1.00 61.21  ? 92  ASP J CB  1 
ATOM   10670 C  CG  . ASP J  1 98  ? 34.096  122.168 64.825 1.00 67.99  ? 92  ASP J CG  1 
ATOM   10671 O  OD1 . ASP J  1 98  ? 35.097  122.741 64.338 1.00 68.79  ? 92  ASP J OD1 1 
ATOM   10672 O  OD2 . ASP J  1 98  ? 33.244  121.585 64.119 1.00 71.39  ? 92  ASP J OD2 1 
ATOM   10673 N  N   . ALA J  1 99  ? 37.400  121.547 66.430 1.00 54.65  ? 93  ALA J N   1 
ATOM   10674 C  CA  . ALA J  1 99  ? 38.443  120.594 66.053 1.00 51.45  ? 93  ALA J CA  1 
ATOM   10675 C  C   . ALA J  1 99  ? 38.085  119.812 64.795 1.00 47.77  ? 93  ALA J C   1 
ATOM   10676 O  O   . ALA J  1 99  ? 38.621  118.732 64.559 1.00 47.26  ? 93  ALA J O   1 
ATOM   10677 C  CB  . ALA J  1 99  ? 38.722  119.632 67.196 1.00 50.76  ? 93  ALA J CB  1 
ATOM   10678 N  N   . VAL J  1 100 ? 37.184  120.359 63.985 1.00 41.43  ? 94  VAL J N   1 
ATOM   10679 C  CA  . VAL J  1 100 ? 36.775  119.690 62.761 1.00 38.33  ? 94  VAL J CA  1 
ATOM   10680 C  C   . VAL J  1 100 ? 37.112  120.511 61.529 1.00 44.12  ? 94  VAL J C   1 
ATOM   10681 O  O   . VAL J  1 100 ? 37.101  121.742 61.549 1.00 43.98  ? 94  VAL J O   1 
ATOM   10682 C  CB  . VAL J  1 100 ? 35.264  119.412 62.761 1.00 39.78  ? 94  VAL J CB  1 
ATOM   10683 C  CG1 . VAL J  1 100 ? 34.837  118.792 61.428 1.00 30.17  ? 94  VAL J CG1 1 
ATOM   10684 C  CG2 . VAL J  1 100 ? 34.919  118.500 63.933 1.00 41.64  ? 94  VAL J CG2 1 
ATOM   10685 N  N   . ALA J  1 101 ? 37.423  119.823 60.447 1.00 43.44  ? 95  ALA J N   1 
ATOM   10686 C  CA  . ALA J  1 101 ? 37.740  120.513 59.224 1.00 44.56  ? 95  ALA J CA  1 
ATOM   10687 C  C   . ALA J  1 101 ? 36.835  120.023 58.127 1.00 46.29  ? 95  ALA J C   1 
ATOM   10688 O  O   . ALA J  1 101 ? 36.896  118.866 57.711 1.00 52.48  ? 95  ALA J O   1 
ATOM   10689 C  CB  . ALA J  1 101 ? 39.195  120.288 58.834 1.00 46.45  ? 95  ALA J CB  1 
ATOM   10690 N  N   . ASP J  1 102 ? 35.966  120.906 57.674 1.00 41.66  ? 96  ASP J N   1 
ATOM   10691 C  CA  . ASP J  1 102 ? 35.106  120.557 56.582 1.00 40.89  ? 96  ASP J CA  1 
ATOM   10692 C  C   . ASP J  1 102 ? 36.027  120.848 55.418 1.00 38.97  ? 96  ASP J C   1 
ATOM   10693 O  O   . ASP J  1 102 ? 36.735  121.852 55.411 1.00 39.07  ? 96  ASP J O   1 
ATOM   10694 C  CB  . ASP J  1 102 ? 33.868  121.447 56.598 1.00 47.88  ? 96  ASP J CB  1 
ATOM   10695 C  CG  . ASP J  1 102 ? 33.020  121.211 57.837 1.00 55.84  ? 96  ASP J CG  1 
ATOM   10696 O  OD1 . ASP J  1 102 ? 32.401  120.119 57.945 1.00 52.51  ? 96  ASP J OD1 1 
ATOM   10697 O  OD2 . ASP J  1 102 ? 32.996  122.103 58.712 1.00 59.80  ? 96  ASP J OD2 1 
ATOM   10698 N  N   . VAL J  1 103 ? 36.056  119.942 54.457 1.00 35.73  ? 97  VAL J N   1 
ATOM   10699 C  CA  . VAL J  1 103 ? 36.923  120.102 53.316 1.00 35.54  ? 97  VAL J CA  1 
ATOM   10700 C  C   . VAL J  1 103 ? 36.140  120.180 52.027 1.00 37.44  ? 97  VAL J C   1 
ATOM   10701 O  O   . VAL J  1 103 ? 35.212  119.411 51.792 1.00 46.86  ? 97  VAL J O   1 
ATOM   10702 C  CB  . VAL J  1 103 ? 37.915  118.906 53.191 1.00 33.88  ? 97  VAL J CB  1 
ATOM   10703 C  CG1 . VAL J  1 103 ? 38.702  119.008 51.884 1.00 26.12  ? 97  VAL J CG1 1 
ATOM   10704 C  CG2 . VAL J  1 103 ? 38.856  118.875 54.375 1.00 30.80  ? 97  VAL J CG2 1 
ATOM   10705 N  N   . SER J  1 104 ? 36.528  121.116 51.184 1.00 35.03  ? 98  SER J N   1 
ATOM   10706 C  CA  . SER J  1 104 ? 35.911  121.254 49.886 1.00 36.52  ? 98  SER J CA  1 
ATOM   10707 C  C   . SER J  1 104 ? 36.917  122.002 49.045 1.00 30.67  ? 98  SER J C   1 
ATOM   10708 O  O   . SER J  1 104 ? 37.122  123.199 49.194 1.00 31.45  ? 98  SER J O   1 
ATOM   10709 C  CB  . SER J  1 104 ? 34.593  122.021 49.951 1.00 38.20  ? 98  SER J CB  1 
ATOM   10710 O  OG  . SER J  1 104 ? 33.972  121.960 48.675 1.00 39.14  ? 98  SER J OG  1 
ATOM   10711 N  N   . ILE J  1 105 ? 37.548  121.267 48.154 1.00 29.61  ? 99  ILE J N   1 
ATOM   10712 C  CA  . ILE J  1 105 ? 38.562  121.823 47.300 1.00 29.67  ? 99  ILE J CA  1 
ATOM   10713 C  C   . ILE J  1 105 ? 38.287  121.368 45.888 1.00 28.04  ? 99  ILE J C   1 
ATOM   10714 O  O   . ILE J  1 105 ? 37.646  120.346 45.679 1.00 34.67  ? 99  ILE J O   1 
ATOM   10715 C  CB  . ILE J  1 105 ? 39.933  121.293 47.747 1.00 26.65  ? 99  ILE J CB  1 
ATOM   10716 C  CG1 . ILE J  1 105 ? 40.300  121.898 49.105 1.00 33.07  ? 99  ILE J CG1 1 
ATOM   10717 C  CG2 . ILE J  1 105 ? 40.975  121.566 46.711 1.00 19.24  ? 99  ILE J CG2 1 
ATOM   10718 C  CD1 . ILE J  1 105 ? 41.516  121.221 49.782 1.00 25.53  ? 99  ILE J CD1 1 
ATOM   10719 N  N   . GLU J  1 106 ? 38.745  122.142 44.917 1.00 29.04  ? 100 GLU J N   1 
ATOM   10720 C  CA  . GLU J  1 106 ? 38.603  121.734 43.537 1.00 36.19  ? 100 GLU J CA  1 
ATOM   10721 C  C   . GLU J  1 106 ? 39.983  121.906 42.962 1.00 36.93  ? 100 GLU J C   1 
ATOM   10722 O  O   . GLU J  1 106 ? 40.600  122.949 43.135 1.00 34.15  ? 100 GLU J O   1 
ATOM   10723 C  CB  . GLU J  1 106 ? 37.609  122.598 42.771 1.00 45.21  ? 100 GLU J CB  1 
ATOM   10724 C  CG  . GLU J  1 106 ? 36.752  121.761 41.836 1.00 61.31  ? 100 GLU J CG  1 
ATOM   10725 C  CD  . GLU J  1 106 ? 35.985  122.576 40.825 1.00 70.35  ? 100 GLU J CD  1 
ATOM   10726 O  OE1 . GLU J  1 106 ? 36.636  123.166 39.930 1.00 65.63  ? 100 GLU J OE1 1 
ATOM   10727 O  OE2 . GLU J  1 106 ? 34.735  122.619 40.929 1.00 75.82  ? 100 GLU J OE2 1 
ATOM   10728 N  N   . ASP J  1 107 ? 40.484  120.873 42.299 1.00 38.94  ? 101 ASP J N   1 
ATOM   10729 C  CA  . ASP J  1 107 ? 41.812  120.937 41.724 1.00 35.08  ? 101 ASP J CA  1 
ATOM   10730 C  C   . ASP J  1 107 ? 41.780  120.297 40.362 1.00 37.08  ? 101 ASP J C   1 
ATOM   10731 O  O   . ASP J  1 107 ? 41.002  119.379 40.125 1.00 41.37  ? 101 ASP J O   1 
ATOM   10732 C  CB  . ASP J  1 107 ? 42.809  120.211 42.627 1.00 39.50  ? 101 ASP J CB  1 
ATOM   10733 C  CG  . ASP J  1 107 ? 44.244  120.465 42.221 1.00 41.90  ? 101 ASP J CG  1 
ATOM   10734 O  OD1 . ASP J  1 107 ? 44.834  119.593 41.542 1.00 33.37  ? 101 ASP J OD1 1 
ATOM   10735 O  OD2 . ASP J  1 107 ? 44.771  121.551 42.577 1.00 42.83  ? 101 ASP J OD2 1 
ATOM   10736 N  N   . SER J  1 108 ? 42.636  120.770 39.470 1.00 37.93  ? 102 SER J N   1 
ATOM   10737 C  CA  . SER J  1 108 ? 42.662  120.259 38.114 1.00 42.85  ? 102 SER J CA  1 
ATOM   10738 C  C   . SER J  1 108 ? 44.038  119.784 37.678 1.00 44.37  ? 102 SER J C   1 
ATOM   10739 O  O   . SER J  1 108 ? 44.321  119.697 36.480 1.00 44.29  ? 102 SER J O   1 
ATOM   10740 C  CB  . SER J  1 108 ? 42.170  121.345 37.154 1.00 46.35  ? 102 SER J CB  1 
ATOM   10741 O  OG  . SER J  1 108 ? 43.045  122.464 37.181 1.00 49.45  ? 102 SER J OG  1 
ATOM   10742 N  N   . VAL J  1 109 ? 44.902  119.505 38.646 1.00 45.08  ? 103 VAL J N   1 
ATOM   10743 C  CA  . VAL J  1 109 ? 46.234  119.006 38.343 1.00 40.65  ? 103 VAL J CA  1 
ATOM   10744 C  C   . VAL J  1 109 ? 46.254  117.531 38.698 1.00 42.09  ? 103 VAL J C   1 
ATOM   10745 O  O   . VAL J  1 109 ? 46.833  116.723 37.976 1.00 46.05  ? 103 VAL J O   1 
ATOM   10746 C  CB  . VAL J  1 109 ? 47.315  119.763 39.117 1.00 44.83  ? 103 VAL J CB  1 
ATOM   10747 C  CG1 . VAL J  1 109 ? 48.634  118.993 39.075 1.00 43.43  ? 103 VAL J CG1 1 
ATOM   10748 C  CG2 . VAL J  1 109 ? 47.507  121.140 38.484 1.00 34.96  ? 103 VAL J CG2 1 
ATOM   10749 N  N   . ILE J  1 110 ? 45.617  117.179 39.809 1.00 41.55  ? 104 ILE J N   1 
ATOM   10750 C  CA  . ILE J  1 110 ? 45.526  115.784 40.200 1.00 42.29  ? 104 ILE J CA  1 
ATOM   10751 C  C   . ILE J  1 110 ? 44.466  115.184 39.281 1.00 48.72  ? 104 ILE J C   1 
ATOM   10752 O  O   . ILE J  1 110 ? 43.686  115.919 38.674 1.00 50.03  ? 104 ILE J O   1 
ATOM   10753 C  CB  . ILE J  1 110 ? 45.046  115.604 41.659 1.00 39.55  ? 104 ILE J CB  1 
ATOM   10754 C  CG1 . ILE J  1 110 ? 43.741  116.374 41.885 1.00 30.69  ? 104 ILE J CG1 1 
ATOM   10755 C  CG2 . ILE J  1 110 ? 46.145  116.022 42.630 1.00 45.70  ? 104 ILE J CG2 1 
ATOM   10756 C  CD1 . ILE J  1 110 ? 43.087  116.075 43.217 1.00 24.26  ? 104 ILE J CD1 1 
ATOM   10757 N  N   . SER J  1 111 ? 44.428  113.859 39.176 1.00 51.80  ? 105 SER J N   1 
ATOM   10758 C  CA  . SER J  1 111 ? 43.434  113.210 38.329 1.00 50.03  ? 105 SER J CA  1 
ATOM   10759 C  C   . SER J  1 111 ? 43.041  111.843 38.878 1.00 50.96  ? 105 SER J C   1 
ATOM   10760 O  O   . SER J  1 111 ? 43.747  111.278 39.715 1.00 48.59  ? 105 SER J O   1 
ATOM   10761 C  CB  . SER J  1 111 ? 43.978  113.057 36.903 1.00 43.65  ? 105 SER J CB  1 
ATOM   10762 O  OG  . SER J  1 111 ? 42.970  112.604 36.010 1.00 39.08  ? 105 SER J OG  1 
ATOM   10763 N  N   . LEU J  1 112 ? 41.899  111.331 38.423 1.00 49.41  ? 106 LEU J N   1 
ATOM   10764 C  CA  . LEU J  1 112 ? 41.448  110.009 38.831 1.00 47.76  ? 106 LEU J CA  1 
ATOM   10765 C  C   . LEU J  1 112 ? 41.669  109.055 37.653 1.00 47.31  ? 106 LEU J C   1 
ATOM   10766 O  O   . LEU J  1 112 ? 40.963  108.063 37.485 1.00 52.01  ? 106 LEU J O   1 
ATOM   10767 C  CB  . LEU J  1 112 ? 39.976  110.038 39.241 1.00 37.85  ? 106 LEU J CB  1 
ATOM   10768 C  CG  . LEU J  1 112 ? 39.652  110.888 40.472 1.00 42.76  ? 106 LEU J CG  1 
ATOM   10769 C  CD1 . LEU J  1 112 ? 38.199  110.637 40.880 1.00 35.97  ? 106 LEU J CD1 1 
ATOM   10770 C  CD2 . LEU J  1 112 ? 40.597  110.545 41.631 1.00 32.40  ? 106 LEU J CD2 1 
ATOM   10771 N  N   . SER J  1 113 ? 42.678  109.372 36.850 1.00 48.78  ? 107 SER J N   1 
ATOM   10772 C  CA  . SER J  1 113 ? 43.048  108.585 35.680 1.00 49.79  ? 107 SER J CA  1 
ATOM   10773 C  C   . SER J  1 113 ? 44.213  109.283 34.997 1.00 52.03  ? 107 SER J C   1 
ATOM   10774 O  O   . SER J  1 113 ? 44.485  110.452 35.268 1.00 56.83  ? 107 SER J O   1 
ATOM   10775 C  CB  . SER J  1 113 ? 41.879  108.499 34.706 1.00 48.46  ? 107 SER J CB  1 
ATOM   10776 O  OG  . SER J  1 113 ? 41.515  109.790 34.255 1.00 56.56  ? 107 SER J OG  1 
ATOM   10777 N  N   . GLY J  1 114 ? 44.907  108.568 34.120 1.00 54.95  ? 108 GLY J N   1 
ATOM   10778 C  CA  . GLY J  1 114 ? 46.024  109.165 33.409 1.00 56.15  ? 108 GLY J CA  1 
ATOM   10779 C  C   . GLY J  1 114 ? 47.291  109.344 34.220 1.00 61.43  ? 108 GLY J C   1 
ATOM   10780 O  O   . GLY J  1 114 ? 47.392  108.874 35.353 1.00 62.27  ? 108 GLY J O   1 
ATOM   10781 N  N   . ASP J  1 115 ? 48.256  110.047 33.633 1.00 66.11  ? 109 ASP J N   1 
ATOM   10782 C  CA  . ASP J  1 115 ? 49.556  110.289 34.258 1.00 71.82  ? 109 ASP J CA  1 
ATOM   10783 C  C   . ASP J  1 115 ? 49.494  110.804 35.701 1.00 68.70  ? 109 ASP J C   1 
ATOM   10784 O  O   . ASP J  1 115 ? 50.412  110.561 36.495 1.00 60.21  ? 109 ASP J O   1 
ATOM   10785 C  CB  . ASP J  1 115 ? 50.368  111.288 33.416 1.00 83.76  ? 109 ASP J CB  1 
ATOM   10786 C  CG  . ASP J  1 115 ? 50.326  110.980 31.928 1.00 94.05  ? 109 ASP J CG  1 
ATOM   10787 O  OD1 . ASP J  1 115 ? 49.236  111.106 31.320 1.00 99.03  ? 109 ASP J OD1 1 
ATOM   10788 O  OD2 . ASP J  1 115 ? 51.386  110.616 31.369 1.00 95.07  ? 109 ASP J OD2 1 
ATOM   10789 N  N   . HIS J  1 116 ? 48.421  111.521 36.031 1.00 61.38  ? 110 HIS J N   1 
ATOM   10790 C  CA  . HIS J  1 116 ? 48.272  112.083 37.367 1.00 58.80  ? 110 HIS J CA  1 
ATOM   10791 C  C   . HIS J  1 116 ? 47.260  111.370 38.248 1.00 55.43  ? 110 HIS J C   1 
ATOM   10792 O  O   . HIS J  1 116 ? 46.765  111.957 39.211 1.00 52.88  ? 110 HIS J O   1 
ATOM   10793 C  CB  . HIS J  1 116 ? 47.897  113.563 37.272 1.00 58.46  ? 110 HIS J CB  1 
ATOM   10794 C  CG  . HIS J  1 116 ? 48.946  114.409 36.625 1.00 64.26  ? 110 HIS J CG  1 
ATOM   10795 N  ND1 . HIS J  1 116 ? 48.735  115.730 36.291 1.00 67.26  ? 110 HIS J ND1 1 
ATOM   10796 C  CD2 . HIS J  1 116 ? 50.218  114.126 36.257 1.00 64.16  ? 110 HIS J CD2 1 
ATOM   10797 C  CE1 . HIS J  1 116 ? 49.833  116.223 35.746 1.00 67.82  ? 110 HIS J CE1 1 
ATOM   10798 N  NE2 . HIS J  1 116 ? 50.747  115.270 35.713 1.00 67.87  ? 110 HIS J NE2 1 
ATOM   10799 N  N   . CYS J  1 117 ? 46.946  110.116 37.930 1.00 52.85  ? 111 CYS J N   1 
ATOM   10800 C  CA  . CYS J  1 117 ? 45.986  109.372 38.733 1.00 51.10  ? 111 CYS J CA  1 
ATOM   10801 C  C   . CYS J  1 117 ? 46.538  109.283 40.151 1.00 47.11  ? 111 CYS J C   1 
ATOM   10802 O  O   . CYS J  1 117 ? 47.691  108.901 40.353 1.00 47.08  ? 111 CYS J O   1 
ATOM   10803 C  CB  . CYS J  1 117 ? 45.782  107.969 38.162 1.00 54.21  ? 111 CYS J CB  1 
ATOM   10804 S  SG  . CYS J  1 117 ? 44.339  107.087 38.812 1.00 52.26  ? 111 CYS J SG  1 
ATOM   10805 N  N   . ILE J  1 118 ? 45.726  109.672 41.126 1.00 43.05  ? 112 ILE J N   1 
ATOM   10806 C  CA  . ILE J  1 118 ? 46.134  109.618 42.524 1.00 40.27  ? 112 ILE J CA  1 
ATOM   10807 C  C   . ILE J  1 118 ? 45.521  108.395 43.181 1.00 39.65  ? 112 ILE J C   1 
ATOM   10808 O  O   . ILE J  1 118 ? 45.657  108.185 44.388 1.00 42.53  ? 112 ILE J O   1 
ATOM   10809 C  CB  . ILE J  1 118 ? 45.674  110.856 43.306 1.00 42.80  ? 112 ILE J CB  1 
ATOM   10810 C  CG1 . ILE J  1 118 ? 44.171  111.057 43.114 1.00 40.97  ? 112 ILE J CG1 1 
ATOM   10811 C  CG2 . ILE J  1 118 ? 46.473  112.057 42.882 1.00 33.31  ? 112 ILE J CG2 1 
ATOM   10812 C  CD1 . ILE J  1 118 ? 43.572  112.088 44.046 1.00 51.15  ? 112 ILE J CD1 1 
ATOM   10813 N  N   . ILE J  1 119 ? 44.822  107.594 42.387 1.00 41.27  ? 113 ILE J N   1 
ATOM   10814 C  CA  . ILE J  1 119 ? 44.218  106.385 42.911 1.00 43.09  ? 113 ILE J CA  1 
ATOM   10815 C  C   . ILE J  1 119 ? 45.363  105.423 43.193 1.00 45.92  ? 113 ILE J C   1 
ATOM   10816 O  O   . ILE J  1 119 ? 46.280  105.259 42.377 1.00 48.18  ? 113 ILE J O   1 
ATOM   10817 C  CB  . ILE J  1 119 ? 43.226  105.780 41.903 1.00 44.61  ? 113 ILE J CB  1 
ATOM   10818 C  CG1 . ILE J  1 119 ? 41.962  106.643 41.867 1.00 49.98  ? 113 ILE J CG1 1 
ATOM   10819 C  CG2 . ILE J  1 119 ? 42.878  104.359 42.288 1.00 39.24  ? 113 ILE J CG2 1 
ATOM   10820 C  CD1 . ILE J  1 119 ? 41.030  106.325 40.725 1.00 53.57  ? 113 ILE J CD1 1 
ATOM   10821 N  N   . GLY J  1 120 ? 45.331  104.819 44.372 1.00 41.33  ? 114 GLY J N   1 
ATOM   10822 C  CA  . GLY J  1 120 ? 46.382  103.898 44.737 1.00 37.22  ? 114 GLY J CA  1 
ATOM   10823 C  C   . GLY J  1 120 ? 47.471  104.588 45.525 1.00 40.54  ? 114 GLY J C   1 
ATOM   10824 O  O   . GLY J  1 120 ? 48.364  103.922 46.035 1.00 46.12  ? 114 GLY J O   1 
ATOM   10825 N  N   . ARG J  1 121 ? 47.402  105.914 45.639 1.00 38.72  ? 115 ARG J N   1 
ATOM   10826 C  CA  . ARG J  1 121 ? 48.413  106.662 46.388 1.00 35.31  ? 115 ARG J CA  1 
ATOM   10827 C  C   . ARG J  1 121 ? 47.859  107.052 47.756 1.00 29.31  ? 115 ARG J C   1 
ATOM   10828 O  O   . ARG J  1 121 ? 46.776  106.598 48.122 1.00 34.69  ? 115 ARG J O   1 
ATOM   10829 C  CB  . ARG J  1 121 ? 48.873  107.863 45.559 1.00 34.58  ? 115 ARG J CB  1 
ATOM   10830 C  CG  . ARG J  1 121 ? 49.012  107.469 44.071 1.00 42.78  ? 115 ARG J CG  1 
ATOM   10831 C  CD  . ARG J  1 121 ? 49.758  108.481 43.213 1.00 39.99  ? 115 ARG J CD  1 
ATOM   10832 N  NE  . ARG J  1 121 ? 51.156  108.102 43.087 1.00 51.29  ? 115 ARG J NE  1 
ATOM   10833 C  CZ  . ARG J  1 121 ? 51.660  107.387 42.088 1.00 45.12  ? 115 ARG J CZ  1 
ATOM   10834 N  NH1 . ARG J  1 121 ? 50.889  106.969 41.094 1.00 37.53  ? 115 ARG J NH1 1 
ATOM   10835 N  NH2 . ARG J  1 121 ? 52.942  107.068 42.106 1.00 38.02  ? 115 ARG J NH2 1 
ATOM   10836 N  N   . THR J  1 122 ? 48.579  107.862 48.525 1.00 26.88  ? 116 THR J N   1 
ATOM   10837 C  CA  . THR J  1 122 ? 48.104  108.205 49.868 1.00 26.97  ? 116 THR J CA  1 
ATOM   10838 C  C   . THR J  1 122 ? 47.811  109.670 50.165 1.00 30.57  ? 116 THR J C   1 
ATOM   10839 O  O   . THR J  1 122 ? 48.589  110.561 49.831 1.00 34.89  ? 116 THR J O   1 
ATOM   10840 C  CB  . THR J  1 122 ? 49.100  107.688 50.958 1.00 27.41  ? 116 THR J CB  1 
ATOM   10841 O  OG1 . THR J  1 122 ? 49.153  106.259 50.916 1.00 26.57  ? 116 THR J OG1 1 
ATOM   10842 C  CG2 . THR J  1 122 ? 48.656  108.116 52.368 1.00 20.89  ? 116 THR J CG2 1 
ATOM   10843 N  N   . LEU J  1 123 ? 46.677  109.905 50.814 1.00 29.90  ? 117 LEU J N   1 
ATOM   10844 C  CA  . LEU J  1 123 ? 46.274  111.254 51.194 1.00 33.17  ? 117 LEU J CA  1 
ATOM   10845 C  C   . LEU J  1 123 ? 46.727  111.473 52.640 1.00 31.72  ? 117 LEU J C   1 
ATOM   10846 O  O   . LEU J  1 123 ? 46.502  110.628 53.513 1.00 25.51  ? 117 LEU J O   1 
ATOM   10847 C  CB  . LEU J  1 123 ? 44.750  111.403 51.086 1.00 34.67  ? 117 LEU J CB  1 
ATOM   10848 C  CG  . LEU J  1 123 ? 44.142  112.760 51.450 1.00 37.28  ? 117 LEU J CG  1 
ATOM   10849 C  CD1 . LEU J  1 123 ? 44.749  113.868 50.582 1.00 28.24  ? 117 LEU J CD1 1 
ATOM   10850 C  CD2 . LEU J  1 123 ? 42.633  112.682 51.261 1.00 25.02  ? 117 LEU J CD2 1 
ATOM   10851 N  N   . VAL J  1 124 ? 47.359  112.612 52.897 1.00 32.29  ? 118 VAL J N   1 
ATOM   10852 C  CA  . VAL J  1 124 ? 47.861  112.892 54.234 1.00 26.68  ? 118 VAL J CA  1 
ATOM   10853 C  C   . VAL J  1 124 ? 47.535  114.284 54.713 1.00 26.40  ? 118 VAL J C   1 
ATOM   10854 O  O   . VAL J  1 124 ? 47.721  115.256 53.985 1.00 27.77  ? 118 VAL J O   1 
ATOM   10855 C  CB  . VAL J  1 124 ? 49.401  112.752 54.294 1.00 31.04  ? 118 VAL J CB  1 
ATOM   10856 C  CG1 . VAL J  1 124 ? 49.896  113.013 55.721 1.00 24.46  ? 118 VAL J CG1 1 
ATOM   10857 C  CG2 . VAL J  1 124 ? 49.831  111.366 53.798 1.00 24.24  ? 118 VAL J CG2 1 
ATOM   10858 N  N   . VAL J  1 125 ? 47.026  114.371 55.935 1.00 23.13  ? 119 VAL J N   1 
ATOM   10859 C  CA  . VAL J  1 125 ? 46.748  115.661 56.540 1.00 30.53  ? 119 VAL J CA  1 
ATOM   10860 C  C   . VAL J  1 125 ? 47.881  115.808 57.560 1.00 32.24  ? 119 VAL J C   1 
ATOM   10861 O  O   . VAL J  1 125 ? 48.125  114.918 58.383 1.00 32.68  ? 119 VAL J O   1 
ATOM   10862 C  CB  . VAL J  1 125 ? 45.369  115.715 57.245 1.00 30.93  ? 119 VAL J CB  1 
ATOM   10863 C  CG1 . VAL J  1 125 ? 45.191  114.531 58.189 1.00 34.42  ? 119 VAL J CG1 1 
ATOM   10864 C  CG2 . VAL J  1 125 ? 45.257  117.006 58.023 1.00 32.14  ? 119 VAL J CG2 1 
ATOM   10865 N  N   . HIS J  1 126 ? 48.578  116.933 57.488 1.00 33.19  ? 120 HIS J N   1 
ATOM   10866 C  CA  . HIS J  1 126 ? 49.713  117.190 58.351 1.00 32.15  ? 120 HIS J CA  1 
ATOM   10867 C  C   . HIS J  1 126 ? 49.445  117.957 59.646 1.00 32.01  ? 120 HIS J C   1 
ATOM   10868 O  O   . HIS J  1 126 ? 48.372  118.520 59.866 1.00 36.04  ? 120 HIS J O   1 
ATOM   10869 C  CB  . HIS J  1 126 ? 50.798  117.894 57.526 1.00 29.95  ? 120 HIS J CB  1 
ATOM   10870 C  CG  . HIS J  1 126 ? 51.415  117.018 56.475 1.00 37.97  ? 120 HIS J CG  1 
ATOM   10871 N  ND1 . HIS J  1 126 ? 52.591  116.322 56.676 1.00 22.92  ? 120 HIS J ND1 1 
ATOM   10872 C  CD2 . HIS J  1 126 ? 51.026  116.739 55.206 1.00 38.64  ? 120 HIS J CD2 1 
ATOM   10873 C  CE1 . HIS J  1 126 ? 52.903  115.664 55.573 1.00 32.15  ? 120 HIS J CE1 1 
ATOM   10874 N  NE2 . HIS J  1 126 ? 51.972  115.899 54.665 1.00 34.93  ? 120 HIS J NE2 1 
ATOM   10875 N  N   . GLU J  1 127 ? 50.461  117.958 60.493 1.00 36.47  ? 121 GLU J N   1 
ATOM   10876 C  CA  . GLU J  1 127 ? 50.454  118.611 61.790 1.00 40.07  ? 121 GLU J CA  1 
ATOM   10877 C  C   . GLU J  1 127 ? 50.424  120.144 61.727 1.00 41.90  ? 121 GLU J C   1 
ATOM   10878 O  O   . GLU J  1 127 ? 49.739  120.784 62.518 1.00 35.67  ? 121 GLU J O   1 
ATOM   10879 C  CB  . GLU J  1 127 ? 51.694  118.151 62.544 1.00 41.73  ? 121 GLU J CB  1 
ATOM   10880 C  CG  . GLU J  1 127 ? 52.063  118.955 63.765 1.00 55.81  ? 121 GLU J CG  1 
ATOM   10881 C  CD  . GLU J  1 127 ? 53.551  118.833 64.103 1.00 69.19  ? 121 GLU J CD  1 
ATOM   10882 O  OE1 . GLU J  1 127 ? 53.946  119.284 65.198 1.00 79.10  ? 121 GLU J OE1 1 
ATOM   10883 O  OE2 . GLU J  1 127 ? 54.331  118.299 63.273 1.00 67.20  ? 121 GLU J OE2 1 
ATOM   10884 N  N   . LYS J  1 128 ? 51.164  120.729 60.788 1.00 41.32  ? 122 LYS J N   1 
ATOM   10885 C  CA  . LYS J  1 128 ? 51.235  122.184 60.675 1.00 37.37  ? 122 LYS J CA  1 
ATOM   10886 C  C   . LYS J  1 128 ? 50.726  122.756 59.350 1.00 38.17  ? 122 LYS J C   1 
ATOM   10887 O  O   . LYS J  1 128 ? 50.408  122.022 58.413 1.00 38.86  ? 122 LYS J O   1 
ATOM   10888 C  CB  . LYS J  1 128 ? 52.683  122.634 60.907 1.00 37.06  ? 122 LYS J CB  1 
ATOM   10889 C  CG  . LYS J  1 128 ? 53.233  122.232 62.270 1.00 41.80  ? 122 LYS J CG  1 
ATOM   10890 C  CD  . LYS J  1 128 ? 54.652  122.759 62.536 1.00 54.68  ? 122 LYS J CD  1 
ATOM   10891 C  CE  . LYS J  1 128 ? 55.719  122.059 61.693 1.00 55.11  ? 122 LYS J CE  1 
ATOM   10892 N  NZ  . LYS J  1 128 ? 57.098  122.342 62.185 1.00 54.42  ? 122 LYS J NZ  1 
ATOM   10893 N  N   . ALA J  1 129 ? 50.639  124.076 59.277 1.00 32.27  ? 123 ALA J N   1 
ATOM   10894 C  CA  . ALA J  1 129 ? 50.189  124.714 58.047 1.00 38.10  ? 123 ALA J CA  1 
ATOM   10895 C  C   . ALA J  1 129 ? 51.252  124.529 56.974 1.00 33.54  ? 123 ALA J C   1 
ATOM   10896 O  O   . ALA J  1 129 ? 52.431  124.401 57.291 1.00 29.33  ? 123 ALA J O   1 
ATOM   10897 C  CB  . ALA J  1 129 ? 49.953  126.185 58.278 1.00 28.94  ? 123 ALA J CB  1 
ATOM   10898 N  N   . ASP J  1 130 ? 50.818  124.510 55.715 1.00 29.19  ? 124 ASP J N   1 
ATOM   10899 C  CA  . ASP J  1 130 ? 51.702  124.371 54.556 1.00 27.87  ? 124 ASP J CA  1 
ATOM   10900 C  C   . ASP J  1 130 ? 52.061  125.812 54.164 1.00 28.82  ? 124 ASP J C   1 
ATOM   10901 O  O   . ASP J  1 130 ? 51.166  126.621 53.937 1.00 29.91  ? 124 ASP J O   1 
ATOM   10902 C  CB  . ASP J  1 130 ? 50.933  123.666 53.420 1.00 31.00  ? 124 ASP J CB  1 
ATOM   10903 C  CG  . ASP J  1 130 ? 51.786  123.414 52.167 1.00 37.30  ? 124 ASP J CG  1 
ATOM   10904 O  OD1 . ASP J  1 130 ? 51.389  122.547 51.355 1.00 24.80  ? 124 ASP J OD1 1 
ATOM   10905 O  OD2 . ASP J  1 130 ? 52.831  124.076 51.981 1.00 37.71  ? 124 ASP J OD2 1 
ATOM   10906 N  N   . ASP J  1 131 ? 53.347  126.148 54.093 1.00 24.64  ? 125 ASP J N   1 
ATOM   10907 C  CA  . ASP J  1 131 ? 53.720  127.517 53.743 1.00 22.85  ? 125 ASP J CA  1 
ATOM   10908 C  C   . ASP J  1 131 ? 53.706  127.743 52.247 1.00 20.73  ? 125 ASP J C   1 
ATOM   10909 O  O   . ASP J  1 131 ? 54.138  128.779 51.762 1.00 24.52  ? 125 ASP J O   1 
ATOM   10910 C  CB  . ASP J  1 131 ? 55.087  127.907 54.351 1.00 26.81  ? 125 ASP J CB  1 
ATOM   10911 C  CG  . ASP J  1 131 ? 56.275  127.157 53.733 1.00 29.72  ? 125 ASP J CG  1 
ATOM   10912 O  OD1 . ASP J  1 131 ? 57.325  127.097 54.404 1.00 29.62  ? 125 ASP J OD1 1 
ATOM   10913 O  OD2 . ASP J  1 131 ? 56.189  126.647 52.594 1.00 22.48  ? 125 ASP J OD2 1 
ATOM   10914 N  N   . LEU J  1 132 ? 53.201  126.754 51.523 1.00 20.51  ? 126 LEU J N   1 
ATOM   10915 C  CA  . LEU J  1 132 ? 53.081  126.833 50.077 1.00 22.40  ? 126 LEU J CA  1 
ATOM   10916 C  C   . LEU J  1 132 ? 54.388  127.211 49.378 1.00 25.14  ? 126 LEU J C   1 
ATOM   10917 O  O   . LEU J  1 132 ? 54.376  127.807 48.291 1.00 26.39  ? 126 LEU J O   1 
ATOM   10918 C  CB  . LEU J  1 132 ? 51.973  127.827 49.706 1.00 16.79  ? 126 LEU J CB  1 
ATOM   10919 C  CG  . LEU J  1 132 ? 50.713  127.761 50.597 1.00 27.82  ? 126 LEU J CG  1 
ATOM   10920 C  CD1 . LEU J  1 132 ? 49.679  128.747 50.077 1.00 23.88  ? 126 LEU J CD1 1 
ATOM   10921 C  CD2 . LEU J  1 132 ? 50.120  126.346 50.608 1.00 24.82  ? 126 LEU J CD2 1 
ATOM   10922 N  N   . GLY J  1 133 ? 55.509  126.857 50.003 1.00 25.71  ? 127 GLY J N   1 
ATOM   10923 C  CA  . GLY J  1 133 ? 56.817  127.114 49.414 1.00 26.18  ? 127 GLY J CA  1 
ATOM   10924 C  C   . GLY J  1 133 ? 57.313  128.545 49.505 1.00 32.07  ? 127 GLY J C   1 
ATOM   10925 O  O   . GLY J  1 133 ? 58.168  128.962 48.722 1.00 19.28  ? 127 GLY J O   1 
ATOM   10926 N  N   . LYS J  1 134 ? 56.778  129.305 50.455 1.00 30.69  ? 128 LYS J N   1 
ATOM   10927 C  CA  . LYS J  1 134 ? 57.185  130.698 50.631 1.00 31.21  ? 128 LYS J CA  1 
ATOM   10928 C  C   . LYS J  1 134 ? 57.949  130.821 51.940 1.00 29.72  ? 128 LYS J C   1 
ATOM   10929 O  O   . LYS J  1 134 ? 58.128  131.920 52.465 1.00 29.04  ? 128 LYS J O   1 
ATOM   10930 C  CB  . LYS J  1 134 ? 55.945  131.605 50.660 1.00 30.17  ? 128 LYS J CB  1 
ATOM   10931 C  CG  . LYS J  1 134 ? 55.096  131.508 49.388 1.00 35.52  ? 128 LYS J CG  1 
ATOM   10932 C  CD  . LYS J  1 134 ? 53.757  132.216 49.536 1.00 43.73  ? 128 LYS J CD  1 
ATOM   10933 C  CE  . LYS J  1 134 ? 53.909  133.728 49.607 1.00 52.70  ? 128 LYS J CE  1 
ATOM   10934 N  NZ  . LYS J  1 134 ? 52.598  134.425 49.802 1.00 53.22  ? 128 LYS J NZ  1 
ATOM   10935 N  N   . GLY J  1 135 ? 58.403  129.680 52.450 1.00 27.46  ? 129 GLY J N   1 
ATOM   10936 C  CA  . GLY J  1 135 ? 59.111  129.646 53.717 1.00 30.76  ? 129 GLY J CA  1 
ATOM   10937 C  C   . GLY J  1 135 ? 60.521  130.198 53.750 1.00 33.91  ? 129 GLY J C   1 
ATOM   10938 O  O   . GLY J  1 135 ? 60.991  130.597 54.811 1.00 25.93  ? 129 GLY J O   1 
ATOM   10939 N  N   . GLY J  1 136 ? 61.206  130.204 52.610 1.00 29.96  ? 130 GLY J N   1 
ATOM   10940 C  CA  . GLY J  1 136 ? 62.556  130.731 52.585 1.00 43.71  ? 130 GLY J CA  1 
ATOM   10941 C  C   . GLY J  1 136 ? 63.668  129.755 52.934 1.00 47.21  ? 130 GLY J C   1 
ATOM   10942 O  O   . GLY J  1 136 ? 64.836  130.045 52.660 1.00 50.51  ? 130 GLY J O   1 
ATOM   10943 N  N   . ASN J  1 137 ? 63.341  128.626 53.564 1.00 46.78  ? 131 ASN J N   1 
ATOM   10944 C  CA  . ASN J  1 137 ? 64.369  127.630 53.884 1.00 44.66  ? 131 ASN J CA  1 
ATOM   10945 C  C   . ASN J  1 137 ? 64.237  126.477 52.893 1.00 40.65  ? 131 ASN J C   1 
ATOM   10946 O  O   . ASN J  1 137 ? 63.334  126.485 52.057 1.00 43.91  ? 131 ASN J O   1 
ATOM   10947 C  CB  . ASN J  1 137 ? 64.269  127.146 55.347 1.00 35.03  ? 131 ASN J CB  1 
ATOM   10948 C  CG  . ASN J  1 137 ? 62.982  126.402 55.651 1.00 42.43  ? 131 ASN J CG  1 
ATOM   10949 O  OD1 . ASN J  1 137 ? 62.150  126.169 54.765 1.00 38.53  ? 131 ASN J OD1 1 
ATOM   10950 N  ND2 . ASN J  1 137 ? 62.815  126.011 56.921 1.00 29.42  ? 131 ASN J ND2 1 
ATOM   10951 N  N   . GLU J  1 138 ? 65.132  125.497 52.970 1.00 46.62  ? 132 GLU J N   1 
ATOM   10952 C  CA  . GLU J  1 138 ? 65.126  124.366 52.031 1.00 48.61  ? 132 GLU J CA  1 
ATOM   10953 C  C   . GLU J  1 138 ? 63.886  123.470 52.109 1.00 48.03  ? 132 GLU J C   1 
ATOM   10954 O  O   . GLU J  1 138 ? 63.370  122.996 51.083 1.00 39.68  ? 132 GLU J O   1 
ATOM   10955 C  CB  . GLU J  1 138 ? 66.366  123.498 52.254 1.00 51.71  ? 132 GLU J CB  1 
ATOM   10956 C  CG  . GLU J  1 138 ? 67.642  124.271 52.535 1.00 64.21  ? 132 GLU J CG  1 
ATOM   10957 C  CD  . GLU J  1 138 ? 68.775  123.358 52.970 1.00 72.77  ? 132 GLU J CD  1 
ATOM   10958 O  OE1 . GLU J  1 138 ? 68.560  122.567 53.918 1.00 79.97  ? 132 GLU J OE1 1 
ATOM   10959 O  OE2 . GLU J  1 138 ? 69.873  123.429 52.373 1.00 67.62  ? 132 GLU J OE2 1 
ATOM   10960 N  N   . GLU J  1 139 ? 63.420  123.238 53.330 1.00 43.06  ? 133 GLU J N   1 
ATOM   10961 C  CA  . GLU J  1 139 ? 62.270  122.381 53.559 1.00 46.45  ? 133 GLU J CA  1 
ATOM   10962 C  C   . GLU J  1 139 ? 60.961  122.896 52.925 1.00 45.08  ? 133 GLU J C   1 
ATOM   10963 O  O   . GLU J  1 139 ? 60.043  122.115 52.621 1.00 32.69  ? 133 GLU J O   1 
ATOM   10964 C  CB  . GLU J  1 139 ? 62.098  122.179 55.070 1.00 46.00  ? 133 GLU J CB  1 
ATOM   10965 C  CG  . GLU J  1 139 ? 61.259  120.970 55.432 1.00 57.69  ? 133 GLU J CG  1 
ATOM   10966 C  CD  . GLU J  1 139 ? 61.839  119.668 54.891 1.00 60.52  ? 133 GLU J CD  1 
ATOM   10967 O  OE1 . GLU J  1 139 ? 61.139  118.641 54.975 1.00 71.09  ? 133 GLU J OE1 1 
ATOM   10968 O  OE2 . GLU J  1 139 ? 62.988  119.665 54.389 1.00 56.93  ? 133 GLU J OE2 1 
ATOM   10969 N  N   . SER J  1 140 ? 60.898  124.208 52.717 1.00 39.53  ? 134 SER J N   1 
ATOM   10970 C  CA  . SER J  1 140 ? 59.724  124.855 52.146 1.00 39.72  ? 134 SER J CA  1 
ATOM   10971 C  C   . SER J  1 140 ? 59.420  124.405 50.732 1.00 41.54  ? 134 SER J C   1 
ATOM   10972 O  O   . SER J  1 140 ? 58.257  124.204 50.371 1.00 35.49  ? 134 SER J O   1 
ATOM   10973 C  CB  . SER J  1 140 ? 59.916  126.363 52.154 1.00 38.16  ? 134 SER J CB  1 
ATOM   10974 O  OG  . SER J  1 140 ? 58.764  127.015 51.687 1.00 27.77  ? 134 SER J OG  1 
ATOM   10975 N  N   . THR J  1 141 ? 60.469  124.259 49.930 1.00 42.18  ? 135 THR J N   1 
ATOM   10976 C  CA  . THR J  1 141 ? 60.314  123.835 48.543 1.00 40.31  ? 135 THR J CA  1 
ATOM   10977 C  C   . THR J  1 141 ? 60.186  122.331 48.416 1.00 36.45  ? 135 THR J C   1 
ATOM   10978 O  O   . THR J  1 141 ? 60.090  121.802 47.313 1.00 34.26  ? 135 THR J O   1 
ATOM   10979 C  CB  . THR J  1 141 ? 61.501  124.284 47.694 1.00 45.08  ? 135 THR J CB  1 
ATOM   10980 O  OG1 . THR J  1 141 ? 62.721  123.959 48.375 1.00 49.66  ? 135 THR J OG1 1 
ATOM   10981 C  CG2 . THR J  1 141 ? 61.432  125.773 47.442 1.00 48.71  ? 135 THR J CG2 1 
ATOM   10982 N  N   . LYS J  1 142 ? 60.200  121.642 49.549 1.00 37.32  ? 136 LYS J N   1 
ATOM   10983 C  CA  . LYS J  1 142 ? 60.063  120.194 49.556 1.00 42.69  ? 136 LYS J CA  1 
ATOM   10984 C  C   . LYS J  1 142 ? 58.724  119.807 50.178 1.00 42.69  ? 136 LYS J C   1 
ATOM   10985 O  O   . LYS J  1 142 ? 57.861  119.234 49.512 1.00 38.43  ? 136 LYS J O   1 
ATOM   10986 C  CB  . LYS J  1 142 ? 61.184  119.546 50.371 1.00 48.59  ? 136 LYS J CB  1 
ATOM   10987 C  CG  . LYS J  1 142 ? 62.589  119.698 49.814 1.00 55.27  ? 136 LYS J CG  1 
ATOM   10988 C  CD  . LYS J  1 142 ? 63.597  119.032 50.753 1.00 64.48  ? 136 LYS J CD  1 
ATOM   10989 C  CE  . LYS J  1 142 ? 65.036  119.300 50.335 1.00 71.02  ? 136 LYS J CE  1 
ATOM   10990 N  NZ  . LYS J  1 142 ? 66.017  118.717 51.292 1.00 70.64  ? 136 LYS J NZ  1 
ATOM   10991 N  N   . THR J  1 143 ? 58.563  120.140 51.460 1.00 38.08  ? 137 THR J N   1 
ATOM   10992 C  CA  . THR J  1 143 ? 57.357  119.810 52.211 1.00 34.49  ? 137 THR J CA  1 
ATOM   10993 C  C   . THR J  1 143 ? 56.477  120.994 52.615 1.00 33.70  ? 137 THR J C   1 
ATOM   10994 O  O   . THR J  1 143 ? 55.408  120.790 53.180 1.00 30.78  ? 137 THR J O   1 
ATOM   10995 C  CB  . THR J  1 143 ? 57.721  119.079 53.520 1.00 39.09  ? 137 THR J CB  1 
ATOM   10996 O  OG1 . THR J  1 143 ? 58.369  119.998 54.428 1.00 25.58  ? 137 THR J OG1 1 
ATOM   10997 C  CG2 . THR J  1 143 ? 58.645  117.909 53.226 1.00 28.93  ? 137 THR J CG2 1 
ATOM   10998 N  N   . GLY J  1 144 ? 56.923  122.216 52.341 1.00 28.83  ? 138 GLY J N   1 
ATOM   10999 C  CA  . GLY J  1 144 ? 56.163  123.382 52.752 1.00 31.00  ? 138 GLY J CA  1 
ATOM   11000 C  C   . GLY J  1 144 ? 56.213  123.569 54.275 1.00 34.93  ? 138 GLY J C   1 
ATOM   11001 O  O   . GLY J  1 144 ? 55.479  124.389 54.843 1.00 28.08  ? 138 GLY J O   1 
ATOM   11002 N  N   . ASN J  1 145 ? 57.069  122.800 54.946 1.00 35.58  ? 139 ASN J N   1 
ATOM   11003 C  CA  . ASN J  1 145 ? 57.215  122.882 56.406 1.00 36.05  ? 139 ASN J CA  1 
ATOM   11004 C  C   . ASN J  1 145 ? 55.936  122.507 57.141 1.00 32.04  ? 139 ASN J C   1 
ATOM   11005 O  O   . ASN J  1 145 ? 55.680  123.002 58.237 1.00 29.63  ? 139 ASN J O   1 
ATOM   11006 C  CB  . ASN J  1 145 ? 57.647  124.297 56.828 1.00 29.63  ? 139 ASN J CB  1 
ATOM   11007 C  CG  . ASN J  1 145 ? 59.053  124.631 56.377 1.00 33.05  ? 139 ASN J CG  1 
ATOM   11008 O  OD1 . ASN J  1 145 ? 60.034  124.127 56.926 1.00 43.11  ? 139 ASN J OD1 1 
ATOM   11009 N  ND2 . ASN J  1 145 ? 59.160  125.471 55.363 1.00 31.33  ? 139 ASN J ND2 1 
ATOM   11010 N  N   . ALA J  1 146 ? 55.146  121.621 56.546 1.00 33.38  ? 140 ALA J N   1 
ATOM   11011 C  CA  . ALA J  1 146 ? 53.875  121.200 57.138 1.00 28.82  ? 140 ALA J CA  1 
ATOM   11012 C  C   . ALA J  1 146 ? 54.028  120.265 58.333 1.00 29.14  ? 140 ALA J C   1 
ATOM   11013 O  O   . ALA J  1 146 ? 53.051  119.950 59.018 1.00 30.98  ? 140 ALA J O   1 
ATOM   11014 C  CB  . ALA J  1 146 ? 52.991  120.550 56.060 1.00 24.43  ? 140 ALA J CB  1 
ATOM   11015 N  N   . GLY J  1 147 ? 55.248  119.809 58.584 1.00 33.53  ? 141 GLY J N   1 
ATOM   11016 C  CA  . GLY J  1 147 ? 55.470  118.931 59.720 1.00 37.24  ? 141 GLY J CA  1 
ATOM   11017 C  C   . GLY J  1 147 ? 55.017  117.488 59.562 1.00 40.91  ? 141 GLY J C   1 
ATOM   11018 O  O   . GLY J  1 147 ? 54.816  116.993 58.440 1.00 37.49  ? 141 GLY J O   1 
ATOM   11019 N  N   . SER J  1 148 ? 54.826  116.827 60.703 1.00 38.61  ? 142 SER J N   1 
ATOM   11020 C  CA  . SER J  1 148 ? 54.438  115.416 60.748 1.00 43.29  ? 142 SER J CA  1 
ATOM   11021 C  C   . SER J  1 148 ? 53.057  115.052 60.223 1.00 39.64  ? 142 SER J C   1 
ATOM   11022 O  O   . SER J  1 148 ? 52.140  115.866 60.191 1.00 37.48  ? 142 SER J O   1 
ATOM   11023 C  CB  . SER J  1 148 ? 54.588  114.867 62.174 1.00 43.24  ? 142 SER J CB  1 
ATOM   11024 O  OG  . SER J  1 148 ? 53.614  115.409 63.047 1.00 54.05  ? 142 SER J OG  1 
ATOM   11025 N  N   . ARG J  1 149 ? 52.935  113.789 59.834 1.00 36.58  ? 143 ARG J N   1 
ATOM   11026 C  CA  . ARG J  1 149 ? 51.717  113.227 59.277 1.00 37.75  ? 143 ARG J CA  1 
ATOM   11027 C  C   . ARG J  1 149 ? 50.793  112.771 60.382 1.00 37.18  ? 143 ARG J C   1 
ATOM   11028 O  O   . ARG J  1 149 ? 51.109  111.824 61.087 1.00 45.13  ? 143 ARG J O   1 
ATOM   11029 C  CB  . ARG J  1 149 ? 52.104  112.052 58.384 1.00 32.15  ? 143 ARG J CB  1 
ATOM   11030 C  CG  . ARG J  1 149 ? 53.322  112.387 57.581 1.00 31.59  ? 143 ARG J CG  1 
ATOM   11031 C  CD  . ARG J  1 149 ? 53.789  111.291 56.664 1.00 31.95  ? 143 ARG J CD  1 
ATOM   11032 N  NE  . ARG J  1 149 ? 54.886  111.804 55.844 1.00 26.87  ? 143 ARG J NE  1 
ATOM   11033 C  CZ  . ARG J  1 149 ? 55.340  111.231 54.736 1.00 27.13  ? 143 ARG J CZ  1 
ATOM   11034 N  NH1 . ARG J  1 149 ? 56.337  111.798 54.084 1.00 16.79  ? 143 ARG J NH1 1 
ATOM   11035 N  NH2 . ARG J  1 149 ? 54.801  110.103 54.275 1.00 26.43  ? 143 ARG J NH2 1 
ATOM   11036 N  N   . LEU J  1 150 ? 49.652  113.438 60.535 1.00 43.33  ? 144 LEU J N   1 
ATOM   11037 C  CA  . LEU J  1 150 ? 48.698  113.079 61.586 1.00 39.41  ? 144 LEU J CA  1 
ATOM   11038 C  C   . LEU J  1 150 ? 47.773  111.935 61.194 1.00 36.81  ? 144 LEU J C   1 
ATOM   11039 O  O   . LEU J  1 150 ? 47.374  111.140 62.039 1.00 42.39  ? 144 LEU J O   1 
ATOM   11040 C  CB  . LEU J  1 150 ? 47.856  114.290 61.980 1.00 41.11  ? 144 LEU J CB  1 
ATOM   11041 C  CG  . LEU J  1 150 ? 48.621  115.530 62.446 1.00 46.13  ? 144 LEU J CG  1 
ATOM   11042 C  CD1 . LEU J  1 150 ? 47.626  116.576 62.898 1.00 37.26  ? 144 LEU J CD1 1 
ATOM   11043 C  CD2 . LEU J  1 150 ? 49.567  115.185 63.576 1.00 33.32  ? 144 LEU J CD2 1 
ATOM   11044 N  N   . ALA J  1 151 ? 47.417  111.855 59.917 1.00 29.01  ? 145 ALA J N   1 
ATOM   11045 C  CA  . ALA J  1 151 ? 46.534  110.785 59.458 1.00 28.97  ? 145 ALA J CA  1 
ATOM   11046 C  C   . ALA J  1 151 ? 46.639  110.646 57.964 1.00 30.51  ? 145 ALA J C   1 
ATOM   11047 O  O   . ALA J  1 151 ? 46.988  111.599 57.262 1.00 32.03  ? 145 ALA J O   1 
ATOM   11048 C  CB  . ALA J  1 151 ? 45.088  111.056 59.853 1.00 27.06  ? 145 ALA J CB  1 
ATOM   11049 N  N   . CYS J  1 152 ? 46.334  109.451 57.477 1.00 30.66  ? 146 CYS J N   1 
ATOM   11050 C  CA  . CYS J  1 152 ? 46.425  109.184 56.055 1.00 33.27  ? 146 CYS J CA  1 
ATOM   11051 C  C   . CYS J  1 152 ? 45.563  107.981 55.735 1.00 32.78  ? 146 CYS J C   1 
ATOM   11052 O  O   . CYS J  1 152 ? 45.029  107.338 56.627 1.00 33.06  ? 146 CYS J O   1 
ATOM   11053 C  CB  . CYS J  1 152 ? 47.885  108.898 55.673 1.00 37.39  ? 146 CYS J CB  1 
ATOM   11054 S  SG  . CYS J  1 152 ? 48.612  107.552 56.670 1.00 36.22  ? 146 CYS J SG  1 
ATOM   11055 N  N   . GLY J  1 153 ? 45.434  107.700 54.448 1.00 32.84  ? 147 GLY J N   1 
ATOM   11056 C  CA  . GLY J  1 153 ? 44.646  106.585 53.983 1.00 26.07  ? 147 GLY J CA  1 
ATOM   11057 C  C   . GLY J  1 153 ? 45.001  106.405 52.523 1.00 29.73  ? 147 GLY J C   1 
ATOM   11058 O  O   . GLY J  1 153 ? 45.547  107.323 51.895 1.00 26.09  ? 147 GLY J O   1 
ATOM   11059 N  N   . VAL J  1 154 ? 44.722  105.226 51.980 1.00 26.78  ? 148 VAL J N   1 
ATOM   11060 C  CA  . VAL J  1 154 ? 45.014  104.977 50.575 1.00 32.76  ? 148 VAL J CA  1 
ATOM   11061 C  C   . VAL J  1 154 ? 43.820  105.420 49.731 1.00 33.80  ? 148 VAL J C   1 
ATOM   11062 O  O   . VAL J  1 154 ? 42.678  105.202 50.116 1.00 38.43  ? 148 VAL J O   1 
ATOM   11063 C  CB  . VAL J  1 154 ? 45.280  103.494 50.318 1.00 31.22  ? 148 VAL J CB  1 
ATOM   11064 C  CG1 . VAL J  1 154 ? 45.632  103.287 48.848 1.00 27.88  ? 148 VAL J CG1 1 
ATOM   11065 C  CG2 . VAL J  1 154 ? 46.400  103.010 51.221 1.00 14.08  ? 148 VAL J CG2 1 
ATOM   11066 N  N   . ILE J  1 155 ? 44.079  106.043 48.587 1.00 33.26  ? 149 ILE J N   1 
ATOM   11067 C  CA  . ILE J  1 155 ? 42.998  106.517 47.733 1.00 33.48  ? 149 ILE J CA  1 
ATOM   11068 C  C   . ILE J  1 155 ? 42.446  105.392 46.858 1.00 35.84  ? 149 ILE J C   1 
ATOM   11069 O  O   . ILE J  1 155 ? 43.080  104.980 45.884 1.00 36.35  ? 149 ILE J O   1 
ATOM   11070 C  CB  . ILE J  1 155 ? 43.487  107.692 46.854 1.00 35.71  ? 149 ILE J CB  1 
ATOM   11071 C  CG1 . ILE J  1 155 ? 44.011  108.820 47.755 1.00 28.87  ? 149 ILE J CG1 1 
ATOM   11072 C  CG2 . ILE J  1 155 ? 42.354  108.204 45.982 1.00 22.55  ? 149 ILE J CG2 1 
ATOM   11073 C  CD1 . ILE J  1 155 ? 44.649  109.963 47.001 1.00 30.77  ? 149 ILE J CD1 1 
ATOM   11074 N  N   . GLY J  1 156 ? 41.258  104.905 47.208 1.00 32.63  ? 150 GLY J N   1 
ATOM   11075 C  CA  . GLY J  1 156 ? 40.656  103.815 46.458 1.00 34.03  ? 150 GLY J CA  1 
ATOM   11076 C  C   . GLY J  1 156 ? 39.485  104.142 45.549 1.00 40.22  ? 150 GLY J C   1 
ATOM   11077 O  O   . GLY J  1 156 ? 38.729  105.079 45.808 1.00 44.49  ? 150 GLY J O   1 
ATOM   11078 N  N   . ILE J  1 157 ? 39.340  103.364 44.477 1.00 45.14  ? 151 ILE J N   1 
ATOM   11079 C  CA  . ILE J  1 157 ? 38.253  103.556 43.521 1.00 48.68  ? 151 ILE J CA  1 
ATOM   11080 C  C   . ILE J  1 157 ? 36.924  103.398 44.251 1.00 47.88  ? 151 ILE J C   1 
ATOM   11081 O  O   . ILE J  1 157 ? 36.776  102.509 45.098 1.00 44.11  ? 151 ILE J O   1 
ATOM   11082 C  CB  . ILE J  1 157 ? 38.336  102.535 42.367 1.00 52.26  ? 151 ILE J CB  1 
ATOM   11083 C  CG1 . ILE J  1 157 ? 39.720  102.625 41.710 1.00 55.26  ? 151 ILE J CG1 1 
ATOM   11084 C  CG2 . ILE J  1 157 ? 37.239  102.821 41.339 1.00 52.47  ? 151 ILE J CG2 1 
ATOM   11085 C  CD1 . ILE J  1 157 ? 39.932  101.696 40.528 1.00 54.73  ? 151 ILE J CD1 1 
ATOM   11086 N  N   . ALA J  1 158 ? 35.969  104.274 43.936 1.00 45.58  ? 152 ALA J N   1 
ATOM   11087 C  CA  . ALA J  1 158 ? 34.657  104.248 44.579 1.00 45.13  ? 152 ALA J CA  1 
ATOM   11088 C  C   . ALA J  1 158 ? 33.487  104.180 43.601 1.00 49.08  ? 152 ALA J C   1 
ATOM   11089 O  O   . ALA J  1 158 ? 33.628  104.446 42.399 1.00 39.77  ? 152 ALA J O   1 
ATOM   11090 C  CB  . ALA J  1 158 ? 34.504  105.461 45.485 1.00 47.37  ? 152 ALA J CB  1 
ATOM   11091 N  N   . GLN J  1 159 ? 32.324  103.816 44.128 1.00 56.29  ? 153 GLN J N   1 
ATOM   11092 C  CA  . GLN J  1 159 ? 31.130  103.706 43.302 1.00 66.90  ? 153 GLN J CA  1 
ATOM   11093 C  C   . GLN J  1 159 ? 30.436  105.063 43.182 1.00 67.53  ? 153 GLN J C   1 
ATOM   11094 O  O   . GLN J  1 159 ? 30.417  105.804 44.193 1.00 66.80  ? 153 GLN J O   1 
ATOM   11095 C  CB  . GLN J  1 159 ? 30.166  102.687 43.915 1.00 71.02  ? 153 GLN J CB  1 
ATOM   11096 C  CG  . GLN J  1 159 ? 29.083  102.197 42.960 1.00 78.66  ? 153 GLN J CG  1 
ATOM   11097 C  CD  . GLN J  1 159 ? 28.098  101.257 43.632 1.00 83.26  ? 153 GLN J CD  1 
ATOM   11098 O  OE1 . GLN J  1 159 ? 27.418  100.472 42.966 1.00 84.77  ? 153 GLN J OE1 1 
ATOM   11099 N  NE2 . GLN J  1 159 ? 28.010  101.339 44.958 1.00 78.89  ? 153 GLN J NE2 1 
ATOM   11100 O  OXT . GLN J  1 159 ? 29.903  105.354 42.085 1.00 63.64  ? 153 GLN J OXT 1 
HETATM 11101 ZN ZN  . ZN  K  2 .   ? 32.795  63.366  48.879 1.00 33.85  ? 601 ZN  A ZN  1 
HETATM 11102 ZN ZN  . ZN  L  2 .   ? 72.000  61.669  51.790 1.00 23.43  ? 602 ZN  B ZN  1 
HETATM 11103 ZN ZN  . ZN  M  2 .   ? 97.561  122.353 49.466 1.00 35.45  ? 603 ZN  C ZN  1 
HETATM 11104 ZN ZN  . ZN  N  2 .   ? 78.206  88.151  51.754 1.00 20.57  ? 604 ZN  D ZN  1 
HETATM 11105 ZN ZN  . ZN  O  2 .   ? 117.468 35.728  49.523 1.00 28.25  ? 605 ZN  E ZN  1 
HETATM 11106 ZN ZN  . ZN  P  2 .   ? 98.013  69.766  51.551 1.00 20.45  ? 606 ZN  F ZN  1 
HETATM 11107 ZN ZN  . ZN  Q  2 .   ? 99.667  146.187 48.149 1.00 52.81  ? 607 ZN  G ZN  1 
HETATM 11108 ZN ZN  . ZN  R  2 .   ? 60.459  146.098 51.470 1.00 32.20  ? 608 ZN  H ZN  1 
HETATM 11109 ZN ZN  . ZN  S  2 .   ? 34.402  85.505  43.111 1.00 47.58  ? 609 ZN  I ZN  1 
HETATM 11110 ZN ZN  . ZN  T  2 .   ? 54.532  119.287 47.802 1.00 32.90  ? 610 ZN  J ZN  1 
HETATM 11111 O  O   . HOH U  3 .   ? 47.244  54.521  38.256 1.00 20.75  ? 602 HOH A O   1 
HETATM 11112 O  O   . HOH U  3 .   ? 48.421  52.169  34.411 1.00 19.81  ? 603 HOH A O   1 
HETATM 11113 O  O   . HOH U  3 .   ? 36.262  69.443  62.138 1.00 22.97  ? 604 HOH A O   1 
HETATM 11114 O  O   . HOH U  3 .   ? 50.860  68.623  56.393 1.00 20.27  ? 605 HOH A O   1 
HETATM 11115 O  O   . HOH U  3 .   ? 33.647  58.755  67.686 1.00 22.55  ? 606 HOH A O   1 
HETATM 11116 O  O   . HOH U  3 .   ? 28.545  52.988  47.803 1.00 22.25  ? 607 HOH A O   1 
HETATM 11117 O  O   . HOH U  3 .   ? 30.324  44.552  68.258 1.00 33.69  ? 608 HOH A O   1 
HETATM 11118 O  O   . HOH U  3 .   ? 42.254  51.900  41.110 1.00 25.66  ? 609 HOH A O   1 
HETATM 11119 O  O   . HOH U  3 .   ? 35.906  48.556  56.033 1.00 25.27  ? 610 HOH A O   1 
HETATM 11120 O  O   . HOH U  3 .   ? 36.370  63.618  41.490 1.00 30.65  ? 611 HOH A O   1 
HETATM 11121 O  O   . HOH U  3 .   ? 31.021  52.877  71.966 1.00 45.14  ? 612 HOH A O   1 
HETATM 11122 O  O   . HOH U  3 .   ? 44.854  69.249  44.163 1.00 29.43  ? 613 HOH A O   1 
HETATM 11123 O  O   . HOH U  3 .   ? 50.797  59.296  57.954 1.00 19.53  ? 614 HOH A O   1 
HETATM 11124 O  O   . HOH U  3 .   ? 55.486  51.690  47.186 1.00 28.63  ? 615 HOH A O   1 
HETATM 11125 O  O   . HOH U  3 .   ? 31.758  58.200  50.760 1.00 37.30  ? 616 HOH A O   1 
HETATM 11126 O  O   . HOH U  3 .   ? 49.285  75.853  54.425 1.00 32.84  ? 617 HOH A O   1 
HETATM 11127 O  O   . HOH U  3 .   ? 47.188  73.684  51.965 1.00 42.01  ? 618 HOH A O   1 
HETATM 11128 O  O   . HOH U  3 .   ? 33.456  51.536  51.985 1.00 25.50  ? 619 HOH A O   1 
HETATM 11129 O  O   . HOH U  3 .   ? 30.873  52.557  52.476 1.00 36.22  ? 620 HOH A O   1 
HETATM 11130 O  O   . HOH U  3 .   ? 35.761  60.079  69.550 1.00 33.12  ? 621 HOH A O   1 
HETATM 11131 O  O   . HOH U  3 .   ? 50.263  52.489  41.486 1.00 38.52  ? 622 HOH A O   1 
HETATM 11132 O  O   . HOH U  3 .   ? 34.056  50.180  49.660 1.00 35.22  ? 623 HOH A O   1 
HETATM 11133 O  O   . HOH U  3 .   ? 50.679  62.280  59.060 1.00 34.89  ? 624 HOH A O   1 
HETATM 11134 O  O   . HOH U  3 .   ? 35.106  61.449  40.535 1.00 37.41  ? 625 HOH A O   1 
HETATM 11135 O  O   . HOH U  3 .   ? 31.914  60.142  67.115 1.00 35.00  ? 626 HOH A O   1 
HETATM 11136 O  O   . HOH U  3 .   ? 40.472  50.573  38.362 1.00 27.04  ? 627 HOH A O   1 
HETATM 11137 O  O   . HOH U  3 .   ? 29.071  51.804  50.380 1.00 37.59  ? 628 HOH A O   1 
HETATM 11138 O  O   . HOH U  3 .   ? 37.249  70.368  60.084 1.00 42.66  ? 629 HOH A O   1 
HETATM 11139 O  O   . HOH U  3 .   ? 44.809  57.835  38.406 1.00 45.43  ? 630 HOH A O   1 
HETATM 11140 O  O   . HOH U  3 .   ? 51.639  49.895  54.701 1.00 36.43  ? 631 HOH A O   1 
HETATM 11141 O  O   . HOH U  3 .   ? 39.798  68.073  44.983 1.00 40.57  ? 632 HOH A O   1 
HETATM 11142 O  O   . HOH U  3 .   ? 28.621  67.495  57.559 1.00 41.81  ? 633 HOH A O   1 
HETATM 11143 O  O   . HOH U  3 .   ? 33.502  50.169  54.156 1.00 45.60  ? 634 HOH A O   1 
HETATM 11144 O  O   . HOH U  3 .   ? 41.737  48.790  34.229 1.00 43.93  ? 635 HOH A O   1 
HETATM 11145 O  O   . HOH U  3 .   ? 46.209  46.758  41.565 1.00 46.80  ? 636 HOH A O   1 
HETATM 11146 O  O   . HOH U  3 .   ? 32.843  65.308  54.933 1.00 44.27  ? 637 HOH A O   1 
HETATM 11147 O  O   . HOH U  3 .   ? 33.964  67.785  55.742 1.00 23.71  ? 638 HOH A O   1 
HETATM 11148 O  O   . HOH U  3 .   ? 35.027  47.670  49.585 1.00 36.97  ? 639 HOH A O   1 
HETATM 11149 O  O   . HOH U  3 .   ? 40.452  47.930  38.313 1.00 35.46  ? 640 HOH A O   1 
HETATM 11150 O  O   . HOH U  3 .   ? 54.375  53.262  41.870 1.00 42.60  ? 641 HOH A O   1 
HETATM 11151 O  O   . HOH U  3 .   ? 39.954  46.669  35.371 1.00 43.92  ? 642 HOH A O   1 
HETATM 11152 O  O   . HOH U  3 .   ? 37.439  62.365  68.979 1.00 24.94  ? 643 HOH A O   1 
HETATM 11153 O  O   . HOH U  3 .   ? 25.636  54.339  62.796 1.00 33.42  ? 644 HOH A O   1 
HETATM 11154 O  O   . HOH U  3 .   ? 45.470  40.127  44.484 1.00 44.44  ? 645 HOH A O   1 
HETATM 11155 O  O   . HOH U  3 .   ? 57.446  50.120  47.141 1.00 47.58  ? 646 HOH A O   1 
HETATM 11156 O  O   . HOH U  3 .   ? 46.216  68.299  42.286 1.00 42.33  ? 647 HOH A O   1 
HETATM 11157 O  O   . HOH V  3 .   ? 83.974  53.354  57.086 1.00 7.96   ? 603 HOH B O   1 
HETATM 11158 O  O   . HOH V  3 .   ? 76.985  73.393  64.710 1.00 22.68  ? 604 HOH B O   1 
HETATM 11159 O  O   . HOH V  3 .   ? 72.987  66.764  52.532 1.00 21.73  ? 605 HOH B O   1 
HETATM 11160 O  O   . HOH V  3 .   ? 52.960  66.745  57.395 1.00 23.58  ? 606 HOH B O   1 
HETATM 11161 O  O   . HOH V  3 .   ? 58.308  66.984  68.724 1.00 30.11  ? 607 HOH B O   1 
HETATM 11162 O  O   . HOH V  3 .   ? 82.255  63.819  59.996 1.00 22.67  ? 608 HOH B O   1 
HETATM 11163 O  O   . HOH V  3 .   ? 74.486  56.146  50.156 1.00 32.13  ? 609 HOH B O   1 
HETATM 11164 O  O   . HOH V  3 .   ? 71.280  73.591  53.402 1.00 19.73  ? 610 HOH B O   1 
HETATM 11165 O  O   . HOH V  3 .   ? 67.859  80.192  61.973 1.00 25.46  ? 611 HOH B O   1 
HETATM 11166 O  O   . HOH V  3 .   ? 69.894  77.229  49.380 1.00 35.33  ? 612 HOH B O   1 
HETATM 11167 O  O   . HOH V  3 .   ? 76.555  71.599  49.491 1.00 18.99  ? 613 HOH B O   1 
HETATM 11168 O  O   . HOH V  3 .   ? 66.625  57.953  65.184 1.00 21.78  ? 614 HOH B O   1 
HETATM 11169 O  O   . HOH V  3 .   ? 69.628  57.864  60.734 1.00 27.22  ? 615 HOH B O   1 
HETATM 11170 O  O   . HOH V  3 .   ? 68.433  69.680  68.858 1.00 21.73  ? 616 HOH B O   1 
HETATM 11171 O  O   . HOH V  3 .   ? 81.583  54.771  58.527 1.00 24.38  ? 617 HOH B O   1 
HETATM 11172 O  O   . HOH V  3 .   ? 65.271  56.014  47.598 1.00 24.49  ? 618 HOH B O   1 
HETATM 11173 O  O   . HOH V  3 .   ? 52.708  57.588  57.621 1.00 19.77  ? 619 HOH B O   1 
HETATM 11174 O  O   . HOH V  3 .   ? 61.476  64.888  39.026 1.00 24.64  ? 620 HOH B O   1 
HETATM 11175 O  O   . HOH V  3 .   ? 84.294  61.307  52.888 1.00 23.69  ? 621 HOH B O   1 
HETATM 11176 O  O   . HOH V  3 .   ? 49.834  72.411  44.650 1.00 25.80  ? 622 HOH B O   1 
HETATM 11177 O  O   . HOH V  3 .   ? 73.675  69.617  42.496 1.00 35.76  ? 623 HOH B O   1 
HETATM 11178 O  O   . HOH V  3 .   ? 62.199  66.016  69.206 1.00 29.92  ? 624 HOH B O   1 
HETATM 11179 O  O   . HOH V  3 .   ? 81.653  58.068  61.659 1.00 24.63  ? 625 HOH B O   1 
HETATM 11180 O  O   . HOH V  3 .   ? 70.804  62.023  43.131 1.00 21.72  ? 626 HOH B O   1 
HETATM 11181 O  O   . HOH V  3 .   ? 60.663  54.519  46.705 1.00 32.58  ? 627 HOH B O   1 
HETATM 11182 O  O   . HOH V  3 .   ? 60.800  67.836  37.806 1.00 38.18  ? 628 HOH B O   1 
HETATM 11183 O  O   . HOH V  3 .   ? 43.199  78.431  46.879 1.00 25.58  ? 629 HOH B O   1 
HETATM 11184 O  O   . HOH V  3 .   ? 69.428  59.949  44.218 1.00 28.22  ? 630 HOH B O   1 
HETATM 11185 O  O   . HOH V  3 .   ? 79.919  68.341  50.016 1.00 37.04  ? 631 HOH B O   1 
HETATM 11186 O  O   . HOH V  3 .   ? 51.534  78.899  51.685 1.00 45.80  ? 632 HOH B O   1 
HETATM 11187 O  O   . HOH V  3 .   ? 71.795  83.506  67.545 1.00 31.00  ? 633 HOH B O   1 
HETATM 11188 O  O   . HOH V  3 .   ? 82.747  62.806  49.125 1.00 36.63  ? 634 HOH B O   1 
HETATM 11189 O  O   . HOH V  3 .   ? 70.891  57.488  53.931 1.00 29.13  ? 635 HOH B O   1 
HETATM 11190 O  O   . HOH V  3 .   ? 60.188  76.797  40.218 1.00 31.36  ? 636 HOH B O   1 
HETATM 11191 O  O   . HOH V  3 .   ? 73.711  59.945  67.209 1.00 33.64  ? 637 HOH B O   1 
HETATM 11192 O  O   . HOH V  3 .   ? 52.622  75.664  52.260 1.00 29.19  ? 638 HOH B O   1 
HETATM 11193 O  O   . HOH V  3 .   ? 62.087  80.921  57.180 1.00 37.12  ? 639 HOH B O   1 
HETATM 11194 O  O   . HOH V  3 .   ? 70.462  72.782  43.682 1.00 31.88  ? 640 HOH B O   1 
HETATM 11195 O  O   . HOH V  3 .   ? 83.312  55.274  50.006 1.00 48.34  ? 641 HOH B O   1 
HETATM 11196 O  O   . HOH V  3 .   ? 71.065  61.389  57.925 1.00 35.71  ? 642 HOH B O   1 
HETATM 11197 O  O   . HOH V  3 .   ? 75.145  70.853  66.023 1.00 45.25  ? 643 HOH B O   1 
HETATM 11198 O  O   . HOH V  3 .   ? 54.298  63.908  38.607 1.00 49.05  ? 644 HOH B O   1 
HETATM 11199 O  O   . HOH V  3 .   ? 53.780  50.518  57.053 1.00 45.76  ? 645 HOH B O   1 
HETATM 11200 O  O   . HOH V  3 .   ? 70.110  73.584  47.495 1.00 38.33  ? 646 HOH B O   1 
HETATM 11201 O  O   . HOH V  3 .   ? 75.570  73.325  51.312 1.00 18.00  ? 647 HOH B O   1 
HETATM 11202 O  O   . HOH V  3 .   ? 69.666  57.370  56.270 1.00 23.59  ? 648 HOH B O   1 
HETATM 11203 O  O   . HOH V  3 .   ? 86.359  62.375  51.739 1.00 30.22  ? 649 HOH B O   1 
HETATM 11204 O  O   . HOH V  3 .   ? 80.174  65.932  43.566 1.00 33.09  ? 650 HOH B O   1 
HETATM 11205 O  O   . HOH V  3 .   ? 70.525  68.292  68.808 1.00 33.32  ? 651 HOH B O   1 
HETATM 11206 O  O   . HOH V  3 .   ? 76.216  59.527  66.089 1.00 46.78  ? 652 HOH B O   1 
HETATM 11207 O  O   . HOH V  3 .   ? 68.643  75.831  43.171 1.00 47.66  ? 653 HOH B O   1 
HETATM 11208 O  O   . HOH V  3 .   ? 68.789  53.210  45.934 1.00 46.05  ? 654 HOH B O   1 
HETATM 11209 O  O   . HOH V  3 .   ? 77.812  56.540  43.020 1.00 37.64  ? 655 HOH B O   1 
HETATM 11210 O  O   . HOH V  3 .   ? 87.479  65.679  53.811 1.00 35.03  ? 656 HOH B O   1 
HETATM 11211 O  O   . HOH V  3 .   ? 63.659  70.838  40.551 1.00 33.96  ? 657 HOH B O   1 
HETATM 11212 O  O   . HOH V  3 .   ? 59.919  51.346  56.249 1.00 32.75  ? 658 HOH B O   1 
HETATM 11213 O  O   . HOH V  3 .   ? 39.878  74.482  48.333 1.00 43.22  ? 659 HOH B O   1 
HETATM 11214 O  O   . HOH V  3 .   ? 63.967  55.087  45.259 1.00 42.88  ? 660 HOH B O   1 
HETATM 11215 O  O   . HOH V  3 .   ? 66.477  69.091  70.799 1.00 42.39  ? 661 HOH B O   1 
HETATM 11216 O  O   . HOH V  3 .   ? 74.973  59.392  61.672 1.00 31.59  ? 662 HOH B O   1 
HETATM 11217 O  O   . HOH V  3 .   ? 81.212  65.348  49.048 1.00 36.67  ? 663 HOH B O   1 
HETATM 11218 O  O   . HOH V  3 .   ? 51.832  60.928  62.507 1.00 45.20  ? 664 HOH B O   1 
HETATM 11219 O  O   . HOH V  3 .   ? 69.645  58.718  58.620 1.00 23.80  ? 665 HOH B O   1 
HETATM 11220 O  O   . HOH V  3 .   ? 52.687  64.176  59.014 1.00 27.56  ? 666 HOH B O   1 
HETATM 11221 O  O   . HOH V  3 .   ? 80.428  68.620  42.106 1.00 36.37  ? 667 HOH B O   1 
HETATM 11222 O  O   . HOH V  3 .   ? 74.064  75.341  49.976 1.00 28.49  ? 668 HOH B O   1 
HETATM 11223 O  O   . HOH V  3 .   ? 69.585  54.824  57.150 1.00 39.78  ? 669 HOH B O   1 
HETATM 11224 O  O   . HOH V  3 .   ? 64.688  65.825  70.407 1.00 39.07  ? 670 HOH B O   1 
HETATM 11225 O  O   . HOH V  3 .   ? 57.587  51.575  54.926 1.00 44.01  ? 671 HOH B O   1 
HETATM 11226 O  O   . HOH V  3 .   ? 79.457  62.742  47.867 1.00 29.81  ? 672 HOH B O   1 
HETATM 11227 O  O   . HOH V  3 .   ? 65.451  72.156  38.308 1.00 40.23  ? 673 HOH B O   1 
HETATM 11228 O  O   . HOH V  3 .   ? 61.844  56.118  43.709 1.00 39.65  ? 674 HOH B O   1 
HETATM 11229 O  O   . HOH V  3 .   ? 67.171  53.729  57.215 1.00 22.57  ? 675 HOH B O   1 
HETATM 11230 O  O   . HOH V  3 .   ? 81.230  73.740  48.370 1.00 24.97  ? 676 HOH B O   1 
HETATM 11231 O  O   . HOH V  3 .   ? 59.565  54.948  44.559 1.00 44.86  ? 677 HOH B O   1 
HETATM 11232 O  O   . HOH V  3 .   ? 62.318  62.234  68.342 1.00 47.49  ? 678 HOH B O   1 
HETATM 11233 O  O   . HOH V  3 .   ? 69.386  79.562  49.266 1.00 51.25  ? 679 HOH B O   1 
HETATM 11234 O  O   . HOH W  3 .   ? 96.188  118.879 42.150 1.00 35.12  ? 604 HOH C O   1 
HETATM 11235 O  O   . HOH W  3 .   ? 75.975  105.571 54.631 1.00 31.00  ? 605 HOH C O   1 
HETATM 11236 O  O   . HOH W  3 .   ? 93.479  125.642 51.136 1.00 28.81  ? 606 HOH C O   1 
HETATM 11237 O  O   . HOH W  3 .   ? 92.799  115.965 68.227 1.00 24.00  ? 607 HOH C O   1 
HETATM 11238 O  O   . HOH W  3 .   ? 89.727  116.829 40.683 1.00 35.26  ? 608 HOH C O   1 
HETATM 11239 O  O   . HOH W  3 .   ? 81.071  127.636 64.710 1.00 42.44  ? 609 HOH C O   1 
HETATM 11240 O  O   . HOH W  3 .   ? 85.813  108.213 57.906 1.00 33.88  ? 610 HOH C O   1 
HETATM 11241 O  O   . HOH W  3 .   ? 97.708  108.837 44.364 1.00 32.31  ? 611 HOH C O   1 
HETATM 11242 O  O   . HOH W  3 .   ? 89.910  112.932 68.438 1.00 27.16  ? 612 HOH C O   1 
HETATM 11243 O  O   . HOH W  3 .   ? 94.714  108.359 57.501 1.00 48.33  ? 613 HOH C O   1 
HETATM 11244 O  O   . HOH W  3 .   ? 94.015  103.496 56.377 1.00 23.98  ? 614 HOH C O   1 
HETATM 11245 O  O   . HOH W  3 .   ? 90.613  130.982 48.498 1.00 45.10  ? 615 HOH C O   1 
HETATM 11246 O  O   . HOH W  3 .   ? 102.082 106.977 53.358 1.00 36.59  ? 616 HOH C O   1 
HETATM 11247 O  O   . HOH W  3 .   ? 91.268  117.105 38.980 1.00 35.78  ? 617 HOH C O   1 
HETATM 11248 O  O   . HOH W  3 .   ? 92.203  122.606 68.419 1.00 45.25  ? 618 HOH C O   1 
HETATM 11249 O  O   . HOH W  3 .   ? 102.979 123.912 58.351 1.00 32.96  ? 619 HOH C O   1 
HETATM 11250 O  O   . HOH W  3 .   ? 88.485  110.630 68.805 1.00 39.64  ? 620 HOH C O   1 
HETATM 11251 O  O   . HOH W  3 .   ? 81.963  128.087 62.428 1.00 41.12  ? 621 HOH C O   1 
HETATM 11252 O  O   . HOH W  3 .   ? 82.770  106.727 65.542 1.00 47.13  ? 622 HOH C O   1 
HETATM 11253 O  O   . HOH W  3 .   ? 89.257  127.168 41.236 1.00 40.61  ? 623 HOH C O   1 
HETATM 11254 O  O   . HOH W  3 .   ? 96.109  107.736 42.621 1.00 40.21  ? 624 HOH C O   1 
HETATM 11255 O  O   . HOH W  3 .   ? 82.922  119.603 41.310 1.00 49.21  ? 625 HOH C O   1 
HETATM 11256 O  O   . HOH W  3 .   ? 94.748  121.369 41.327 1.00 44.63  ? 626 HOH C O   1 
HETATM 11257 O  O   . HOH W  3 .   ? 101.004 119.522 51.194 1.00 38.53  ? 627 HOH C O   1 
HETATM 11258 O  O   . HOH W  3 .   ? 96.332  104.182 63.982 1.00 43.23  ? 628 HOH C O   1 
HETATM 11259 O  O   . HOH W  3 .   ? 101.872 132.341 56.999 1.00 32.90  ? 629 HOH C O   1 
HETATM 11260 O  O   . HOH W  3 .   ? 83.928  127.137 59.296 1.00 40.31  ? 630 HOH C O   1 
HETATM 11261 O  O   . HOH W  3 .   ? 91.922  104.173 62.472 1.00 44.40  ? 631 HOH C O   1 
HETATM 11262 O  O   . HOH W  3 .   ? 98.525  121.730 55.443 1.00 37.55  ? 632 HOH C O   1 
HETATM 11263 O  O   . HOH W  3 .   ? 73.817  124.701 48.997 1.00 48.39  ? 633 HOH C O   1 
HETATM 11264 O  O   . HOH W  3 .   ? 101.776 125.407 40.117 1.00 40.45  ? 634 HOH C O   1 
HETATM 11265 O  O   . HOH W  3 .   ? 83.146  126.548 56.586 1.00 38.50  ? 635 HOH C O   1 
HETATM 11266 O  O   . HOH W  3 .   ? 85.784  125.893 47.556 1.00 43.49  ? 636 HOH C O   1 
HETATM 11267 O  O   . HOH W  3 .   ? 78.501  107.354 42.451 1.00 46.98  ? 637 HOH C O   1 
HETATM 11268 O  O   . HOH W  3 .   ? 99.173  109.032 65.912 1.00 45.40  ? 638 HOH C O   1 
HETATM 11269 O  O   . HOH W  3 .   ? 100.790 106.511 65.321 1.00 43.42  ? 639 HOH C O   1 
HETATM 11270 O  O   . HOH X  3 .   ? 84.834  79.392  49.332 1.00 13.41  ? 605 HOH D O   1 
HETATM 11271 O  O   . HOH X  3 .   ? 77.523  94.389  65.101 1.00 18.98  ? 606 HOH D O   1 
HETATM 11272 O  O   . HOH X  3 .   ? 89.067  83.311  53.371 1.00 18.84  ? 607 HOH D O   1 
HETATM 11273 O  O   . HOH X  3 .   ? 72.043  77.698  52.745 1.00 23.94  ? 608 HOH D O   1 
HETATM 11274 O  O   . HOH X  3 .   ? 75.318  78.319  59.888 1.00 15.95  ? 609 HOH D O   1 
HETATM 11275 O  O   . HOH X  3 .   ? 86.792  87.287  69.009 1.00 13.93  ? 610 HOH D O   1 
HETATM 11276 O  O   . HOH X  3 .   ? 91.663  102.397 57.418 1.00 21.39  ? 611 HOH D O   1 
HETATM 11277 O  O   . HOH X  3 .   ? 85.722  96.357  39.089 1.00 27.72  ? 612 HOH D O   1 
HETATM 11278 O  O   . HOH X  3 .   ? 86.780  94.546  69.337 1.00 23.34  ? 613 HOH D O   1 
HETATM 11279 O  O   . HOH X  3 .   ? 88.648  103.824 59.100 1.00 25.77  ? 614 HOH D O   1 
HETATM 11280 O  O   . HOH X  3 .   ? 82.380  84.818  52.560 1.00 19.29  ? 615 HOH D O   1 
HETATM 11281 O  O   . HOH X  3 .   ? 78.256  78.554  43.249 1.00 34.57  ? 616 HOH D O   1 
HETATM 11282 O  O   . HOH X  3 .   ? 74.280  72.813  53.746 1.00 20.79  ? 617 HOH D O   1 
HETATM 11283 O  O   . HOH X  3 .   ? 78.622  80.920  62.385 1.00 25.72  ? 618 HOH D O   1 
HETATM 11284 O  O   . HOH X  3 .   ? 78.011  91.271  44.020 1.00 24.29  ? 619 HOH D O   1 
HETATM 11285 O  O   . HOH X  3 .   ? 78.853  89.115  42.924 1.00 27.55  ? 620 HOH D O   1 
HETATM 11286 O  O   . HOH X  3 .   ? 86.267  78.104  64.363 1.00 28.27  ? 621 HOH D O   1 
HETATM 11287 O  O   . HOH X  3 .   ? 72.206  88.202  49.837 1.00 26.85  ? 622 HOH D O   1 
HETATM 11288 O  O   . HOH X  3 .   ? 76.545  73.326  56.213 1.00 28.76  ? 623 HOH D O   1 
HETATM 11289 O  O   . HOH X  3 .   ? 100.480 105.184 52.003 1.00 29.62  ? 624 HOH D O   1 
HETATM 11290 O  O   . HOH X  3 .   ? 89.460  95.775  38.005 1.00 39.01  ? 625 HOH D O   1 
HETATM 11291 O  O   . HOH X  3 .   ? 80.191  78.069  50.012 1.00 29.48  ? 626 HOH D O   1 
HETATM 11292 O  O   . HOH X  3 .   ? 83.427  106.928 57.618 1.00 21.79  ? 627 HOH D O   1 
HETATM 11293 O  O   . HOH X  3 .   ? 75.237  91.255  53.802 1.00 26.16  ? 628 HOH D O   1 
HETATM 11294 O  O   . HOH X  3 .   ? 81.495  99.496  66.105 1.00 51.67  ? 629 HOH D O   1 
HETATM 11295 O  O   . HOH X  3 .   ? 76.302  81.040  47.574 1.00 36.78  ? 630 HOH D O   1 
HETATM 11296 O  O   . HOH X  3 .   ? 83.583  102.204 59.021 1.00 34.65  ? 631 HOH D O   1 
HETATM 11297 O  O   . HOH X  3 .   ? 77.368  78.524  49.142 1.00 34.66  ? 632 HOH D O   1 
HETATM 11298 O  O   . HOH X  3 .   ? 80.727  76.151  55.546 1.00 32.27  ? 633 HOH D O   1 
HETATM 11299 O  O   . HOH X  3 .   ? 101.540 87.264  52.738 1.00 47.89  ? 634 HOH D O   1 
HETATM 11300 O  O   . HOH X  3 .   ? 94.411  82.087  51.837 1.00 28.52  ? 635 HOH D O   1 
HETATM 11301 O  O   . HOH X  3 .   ? 93.236  82.643  48.970 1.00 26.93  ? 636 HOH D O   1 
HETATM 11302 O  O   . HOH X  3 .   ? 99.342  98.387  51.976 1.00 44.72  ? 637 HOH D O   1 
HETATM 11303 O  O   . HOH X  3 .   ? 96.032  89.598  71.187 1.00 35.17  ? 638 HOH D O   1 
HETATM 11304 O  O   . HOH X  3 .   ? 74.496  85.935  65.764 1.00 36.55  ? 639 HOH D O   1 
HETATM 11305 O  O   . HOH X  3 .   ? 60.748  84.575  58.724 1.00 39.86  ? 640 HOH D O   1 
HETATM 11306 O  O   . HOH X  3 .   ? 85.403  92.350  70.501 1.00 22.17  ? 641 HOH D O   1 
HETATM 11307 O  O   . HOH X  3 .   ? 74.922  103.731 56.085 1.00 36.50  ? 642 HOH D O   1 
HETATM 11308 O  O   . HOH X  3 .   ? 71.386  75.396  51.183 1.00 34.42  ? 643 HOH D O   1 
HETATM 11309 O  O   . HOH X  3 .   ? 87.543  89.325  70.440 1.00 23.57  ? 644 HOH D O   1 
HETATM 11310 O  O   . HOH X  3 .   ? 93.781  84.227  58.387 1.00 33.22  ? 645 HOH D O   1 
HETATM 11311 O  O   . HOH X  3 .   ? 98.874  83.781  65.043 1.00 43.23  ? 646 HOH D O   1 
HETATM 11312 O  O   . HOH X  3 .   ? 75.743  92.402  56.661 1.00 39.62  ? 647 HOH D O   1 
HETATM 11313 O  O   . HOH X  3 .   ? 99.210  81.290  60.593 1.00 33.98  ? 648 HOH D O   1 
HETATM 11314 O  O   . HOH X  3 .   ? 96.706  83.074  61.840 1.00 28.38  ? 649 HOH D O   1 
HETATM 11315 O  O   . HOH X  3 .   ? 82.728  97.207  67.106 1.00 44.30  ? 650 HOH D O   1 
HETATM 11316 O  O   . HOH X  3 .   ? 67.864  83.280  59.366 1.00 31.37  ? 651 HOH D O   1 
HETATM 11317 O  O   . HOH X  3 .   ? 91.170  82.361  72.033 1.00 28.82  ? 652 HOH D O   1 
HETATM 11318 O  O   . HOH X  3 .   ? 97.707  103.120 44.956 1.00 31.05  ? 653 HOH D O   1 
HETATM 11319 O  O   . HOH X  3 .   ? 80.182  77.122  43.500 1.00 40.03  ? 654 HOH D O   1 
HETATM 11320 O  O   . HOH X  3 .   ? 81.132  84.833  37.519 1.00 45.79  ? 655 HOH D O   1 
HETATM 11321 O  O   . HOH X  3 .   ? 101.172 95.188  57.798 1.00 48.24  ? 656 HOH D O   1 
HETATM 11322 O  O   . HOH X  3 .   ? 79.176  75.591  57.424 1.00 46.25  ? 657 HOH D O   1 
HETATM 11323 O  O   . HOH X  3 .   ? 76.160  96.561  47.853 1.00 34.47  ? 658 HOH D O   1 
HETATM 11324 O  O   . HOH X  3 .   ? 93.068  82.979  74.035 1.00 34.52  ? 659 HOH D O   1 
HETATM 11325 O  O   . HOH X  3 .   ? 76.582  91.624  59.516 1.00 31.64  ? 660 HOH D O   1 
HETATM 11326 O  O   . HOH X  3 .   ? 78.496  89.195  57.895 1.00 41.48  ? 661 HOH D O   1 
HETATM 11327 O  O   . HOH X  3 .   ? 100.806 98.980  56.022 1.00 27.13  ? 662 HOH D O   1 
HETATM 11328 O  O   . HOH X  3 .   ? 89.559  80.333  72.407 1.00 35.83  ? 663 HOH D O   1 
HETATM 11329 O  O   . HOH X  3 .   ? 86.211  79.163  55.739 1.00 37.81  ? 664 HOH D O   1 
HETATM 11330 O  O   . HOH X  3 .   ? 101.956 99.004  58.200 1.00 45.83  ? 665 HOH D O   1 
HETATM 11331 O  O   . HOH X  3 .   ? 75.627  109.346 57.210 1.00 44.43  ? 666 HOH D O   1 
HETATM 11332 O  O   . HOH X  3 .   ? 72.246  99.344  51.074 1.00 35.35  ? 667 HOH D O   1 
HETATM 11333 O  O   . HOH X  3 .   ? 93.067  98.004  39.388 1.00 43.84  ? 668 HOH D O   1 
HETATM 11334 O  O   . HOH X  3 .   ? 90.587  82.157  51.191 1.00 41.52  ? 669 HOH D O   1 
HETATM 11335 O  O   . HOH X  3 .   ? 92.264  102.885 41.154 1.00 53.01  ? 670 HOH D O   1 
HETATM 11336 O  O   . HOH Y  3 .   ? 103.407 48.674  56.705 1.00 20.59  ? 606 HOH E O   1 
HETATM 11337 O  O   . HOH Y  3 .   ? 113.318 34.802  56.598 1.00 27.19  ? 607 HOH E O   1 
HETATM 11338 O  O   . HOH Y  3 .   ? 121.711 49.400  40.782 1.00 22.52  ? 608 HOH E O   1 
HETATM 11339 O  O   . HOH Y  3 .   ? 128.342 37.560  48.266 1.00 25.41  ? 609 HOH E O   1 
HETATM 11340 O  O   . HOH Y  3 .   ? 109.616 39.195  45.101 1.00 31.17  ? 610 HOH E O   1 
HETATM 11341 O  O   . HOH Y  3 .   ? 111.567 53.327  57.954 1.00 26.43  ? 611 HOH E O   1 
HETATM 11342 O  O   . HOH Y  3 .   ? 121.143 39.853  68.360 1.00 21.13  ? 612 HOH E O   1 
HETATM 11343 O  O   . HOH Y  3 .   ? 127.153 42.401  53.071 1.00 32.77  ? 613 HOH E O   1 
HETATM 11344 O  O   . HOH Y  3 .   ? 130.398 47.050  62.340 1.00 22.96  ? 614 HOH E O   1 
HETATM 11345 O  O   . HOH Y  3 .   ? 135.037 44.223  67.865 1.00 34.15  ? 615 HOH E O   1 
HETATM 11346 O  O   . HOH Y  3 .   ? 108.715 51.265  58.852 1.00 21.75  ? 616 HOH E O   1 
HETATM 11347 O  O   . HOH Y  3 .   ? 114.787 43.894  68.440 1.00 31.49  ? 617 HOH E O   1 
HETATM 11348 O  O   . HOH Y  3 .   ? 115.080 61.174  46.833 1.00 28.09  ? 618 HOH E O   1 
HETATM 11349 O  O   . HOH Y  3 .   ? 125.653 40.126  41.068 1.00 37.99  ? 619 HOH E O   1 
HETATM 11350 O  O   . HOH Y  3 .   ? 124.335 48.520  71.006 1.00 23.51  ? 620 HOH E O   1 
HETATM 11351 O  O   . HOH Y  3 .   ? 115.530 22.946  54.816 1.00 33.67  ? 621 HOH E O   1 
HETATM 11352 O  O   . HOH Y  3 .   ? 127.249 41.112  71.977 1.00 41.98  ? 622 HOH E O   1 
HETATM 11353 O  O   . HOH Y  3 .   ? 128.103 47.923  43.144 1.00 31.50  ? 623 HOH E O   1 
HETATM 11354 O  O   . HOH Y  3 .   ? 115.482 48.430  38.824 1.00 40.23  ? 624 HOH E O   1 
HETATM 11355 O  O   . HOH Y  3 .   ? 102.319 39.515  53.448 1.00 41.57  ? 625 HOH E O   1 
HETATM 11356 O  O   . HOH Y  3 .   ? 119.268 57.869  40.761 1.00 41.97  ? 626 HOH E O   1 
HETATM 11357 O  O   . HOH Y  3 .   ? 105.239 36.405  48.008 1.00 54.80  ? 627 HOH E O   1 
HETATM 11358 O  O   . HOH Y  3 .   ? 114.903 38.265  41.872 1.00 33.15  ? 628 HOH E O   1 
HETATM 11359 O  O   . HOH Y  3 .   ? 132.780 40.266  59.232 1.00 27.02  ? 629 HOH E O   1 
HETATM 11360 O  O   . HOH Y  3 .   ? 117.569 38.509  41.086 1.00 45.28  ? 630 HOH E O   1 
HETATM 11361 O  O   . HOH Y  3 .   ? 128.550 45.395  58.801 1.00 42.22  ? 631 HOH E O   1 
HETATM 11362 O  O   . HOH Y  3 .   ? 113.497 47.699  68.281 1.00 46.15  ? 632 HOH E O   1 
HETATM 11363 O  O   . HOH Y  3 .   ? 125.901 32.056  41.395 1.00 55.44  ? 633 HOH E O   1 
HETATM 11364 O  O   . HOH Y  3 .   ? 115.840 20.664  52.952 1.00 23.73  ? 634 HOH E O   1 
HETATM 11365 O  O   . HOH Y  3 .   ? 125.024 51.043  71.411 1.00 30.80  ? 635 HOH E O   1 
HETATM 11366 O  O   . HOH Y  3 .   ? 129.286 39.030  50.221 1.00 30.88  ? 636 HOH E O   1 
HETATM 11367 O  O   . HOH Y  3 .   ? 119.847 41.391  69.762 1.00 25.41  ? 637 HOH E O   1 
HETATM 11368 O  O   . HOH Y  3 .   ? 122.383 58.021  59.783 1.00 32.55  ? 638 HOH E O   1 
HETATM 11369 O  O   . HOH Y  3 .   ? 119.021 58.702  53.497 1.00 40.74  ? 639 HOH E O   1 
HETATM 11370 O  O   . HOH Y  3 .   ? 114.443 31.232  46.451 1.00 42.05  ? 640 HOH E O   1 
HETATM 11371 O  O   . HOH Y  3 .   ? 128.907 33.136  55.913 1.00 36.45  ? 641 HOH E O   1 
HETATM 11372 O  O   . HOH Y  3 .   ? 122.443 37.625  50.754 1.00 35.36  ? 642 HOH E O   1 
HETATM 11373 O  O   . HOH Y  3 .   ? 116.489 35.450  55.568 1.00 34.92  ? 643 HOH E O   1 
HETATM 11374 O  O   . HOH Y  3 .   ? 116.085 63.392  46.497 1.00 45.62  ? 644 HOH E O   1 
HETATM 11375 O  O   . HOH Y  3 .   ? 126.599 44.424  47.188 1.00 28.83  ? 645 HOH E O   1 
HETATM 11376 O  O   . HOH Y  3 .   ? 116.981 55.771  40.957 1.00 35.81  ? 646 HOH E O   1 
HETATM 11377 O  O   . HOH Y  3 .   ? 114.315 58.492  38.863 1.00 39.45  ? 647 HOH E O   1 
HETATM 11378 O  O   . HOH Y  3 .   ? 110.124 50.784  61.662 1.00 41.61  ? 648 HOH E O   1 
HETATM 11379 O  O   . HOH Y  3 .   ? 128.662 53.335  58.272 1.00 36.05  ? 649 HOH E O   1 
HETATM 11380 O  O   . HOH Y  3 .   ? 113.086 34.278  51.026 1.00 31.93  ? 650 HOH E O   1 
HETATM 11381 O  O   . HOH Y  3 .   ? 111.843 56.482  42.336 1.00 38.17  ? 651 HOH E O   1 
HETATM 11382 O  O   . HOH Y  3 .   ? 125.466 56.348  44.334 1.00 41.59  ? 652 HOH E O   1 
HETATM 11383 O  O   . HOH Y  3 .   ? 116.467 30.673  58.375 1.00 36.83  ? 653 HOH E O   1 
HETATM 11384 O  O   . HOH Y  3 .   ? 115.201 52.940  65.760 1.00 52.83  ? 654 HOH E O   1 
HETATM 11385 O  O   . HOH Y  3 .   ? 118.093 23.327  46.792 1.00 38.74  ? 655 HOH E O   1 
HETATM 11386 O  O   . HOH Y  3 .   ? 105.769 42.407  44.361 1.00 34.35  ? 656 HOH E O   1 
HETATM 11387 O  O   . HOH Y  3 .   ? 120.073 59.372  36.803 1.00 54.13  ? 657 HOH E O   1 
HETATM 11388 O  O   . HOH Y  3 .   ? 122.660 55.807  61.065 1.00 40.74  ? 658 HOH E O   1 
HETATM 11389 O  O   . HOH Y  3 .   ? 108.101 41.910  64.857 1.00 41.03  ? 659 HOH E O   1 
HETATM 11390 O  O   . HOH Y  3 .   ? 133.372 28.912  47.206 1.00 68.47  ? 660 HOH E O   1 
HETATM 11391 O  O   . HOH Y  3 .   ? 133.591 32.168  46.377 1.00 39.36  ? 661 HOH E O   1 
HETATM 11392 O  O   . HOH Y  3 .   ? 122.703 38.725  39.505 1.00 40.10  ? 662 HOH E O   1 
HETATM 11393 O  O   . HOH Y  3 .   ? 128.899 34.988  63.392 1.00 40.17  ? 663 HOH E O   1 
HETATM 11394 O  O   . HOH Y  3 .   ? 105.336 49.743  61.867 1.00 36.29  ? 664 HOH E O   1 
HETATM 11395 O  O   . HOH Y  3 .   ? 132.764 34.874  46.379 1.00 34.40  ? 665 HOH E O   1 
HETATM 11396 O  O   . HOH Z  3 .   ? 84.538  56.720  62.085 1.00 22.46  ? 607 HOH F O   1 
HETATM 11397 O  O   . HOH Z  3 .   ? 87.165  68.366  49.662 1.00 18.51  ? 608 HOH F O   1 
HETATM 11398 O  O   . HOH Z  3 .   ? 111.939 56.020  57.274 1.00 21.11  ? 609 HOH F O   1 
HETATM 11399 O  O   . HOH Z  3 .   ? 93.074  67.716  52.425 1.00 15.00  ? 610 HOH F O   1 
HETATM 11400 O  O   . HOH Z  3 .   ? 99.726  84.212  56.651 1.00 21.35  ? 611 HOH F O   1 
HETATM 11401 O  O   . HOH Z  3 .   ? 114.120 63.054  54.441 1.00 34.41  ? 612 HOH F O   1 
HETATM 11402 O  O   . HOH Z  3 .   ? 106.424 52.994  59.014 1.00 25.23  ? 613 HOH F O   1 
HETATM 11403 O  O   . HOH Z  3 .   ? 102.328 70.974  53.415 1.00 22.05  ? 614 HOH F O   1 
HETATM 11404 O  O   . HOH Z  3 .   ? 88.501  62.754  53.787 1.00 20.30  ? 615 HOH F O   1 
HETATM 11405 O  O   . HOH Z  3 .   ? 101.380 55.641  68.797 1.00 24.48  ? 616 HOH F O   1 
HETATM 11406 O  O   . HOH Z  3 .   ? 91.525  77.523  59.737 1.00 25.00  ? 617 HOH F O   1 
HETATM 11407 O  O   . HOH Z  3 .   ? 101.258 42.166  52.478 1.00 33.69  ? 618 HOH F O   1 
HETATM 11408 O  O   . HOH Z  3 .   ? 100.657 58.880  38.861 1.00 27.60  ? 619 HOH F O   1 
HETATM 11409 O  O   . HOH Z  3 .   ? 98.172  68.367  42.757 1.00 26.22  ? 620 HOH F O   1 
HETATM 11410 O  O   . HOH Z  3 .   ? 100.771 68.276  44.129 1.00 26.55  ? 621 HOH F O   1 
HETATM 11411 O  O   . HOH Z  3 .   ? 96.367  46.282  52.420 1.00 25.40  ? 622 HOH F O   1 
HETATM 11412 O  O   . HOH Z  3 .   ? 87.479  61.477  72.661 1.00 29.87  ? 623 HOH F O   1 
HETATM 11413 O  O   . HOH Z  3 .   ? 96.777  79.789  61.142 1.00 28.34  ? 624 HOH F O   1 
HETATM 11414 O  O   . HOH Z  3 .   ? 86.936  58.595  59.250 1.00 35.12  ? 625 HOH F O   1 
HETATM 11415 O  O   . HOH Z  3 .   ? 92.312  74.977  47.307 1.00 28.13  ? 626 HOH F O   1 
HETATM 11416 O  O   . HOH Z  3 .   ? 92.019  57.892  33.549 1.00 44.39  ? 627 HOH F O   1 
HETATM 11417 O  O   . HOH Z  3 .   ? 93.847  73.921  39.959 1.00 38.01  ? 628 HOH F O   1 
HETATM 11418 O  O   . HOH Z  3 .   ? 86.954  81.032  53.464 1.00 23.41  ? 629 HOH F O   1 
HETATM 11419 O  O   . HOH Z  3 .   ? 105.618 53.483  38.815 1.00 37.67  ? 630 HOH F O   1 
HETATM 11420 O  O   . HOH Z  3 .   ? 99.761  81.686  58.051 1.00 27.09  ? 631 HOH F O   1 
HETATM 11421 O  O   . HOH Z  3 .   ? 95.165  61.444  70.732 1.00 30.11  ? 632 HOH F O   1 
HETATM 11422 O  O   . HOH Z  3 .   ? 103.656 51.245  57.504 1.00 24.96  ? 633 HOH F O   1 
HETATM 11423 O  O   . HOH Z  3 .   ? 117.391 61.314  56.783 1.00 33.27  ? 634 HOH F O   1 
HETATM 11424 O  O   . HOH Z  3 .   ? 101.429 74.497  49.529 1.00 31.97  ? 635 HOH F O   1 
HETATM 11425 O  O   . HOH Z  3 .   ? 92.328  80.155  52.494 1.00 24.53  ? 636 HOH F O   1 
HETATM 11426 O  O   . HOH Z  3 .   ? 98.924  56.494  37.957 1.00 34.33  ? 637 HOH F O   1 
HETATM 11427 O  O   . HOH Z  3 .   ? 107.797 59.020  59.002 1.00 40.40  ? 638 HOH F O   1 
HETATM 11428 O  O   . HOH Z  3 .   ? 105.248 59.609  43.504 1.00 42.44  ? 639 HOH F O   1 
HETATM 11429 O  O   . HOH Z  3 .   ? 113.006 65.382  55.569 1.00 32.57  ? 640 HOH F O   1 
HETATM 11430 O  O   . HOH Z  3 .   ? 90.584  67.146  42.479 1.00 40.41  ? 641 HOH F O   1 
HETATM 11431 O  O   . HOH Z  3 .   ? 100.566 45.167  45.009 1.00 39.19  ? 642 HOH F O   1 
HETATM 11432 O  O   . HOH Z  3 .   ? 85.989  68.261  65.082 1.00 35.68  ? 643 HOH F O   1 
HETATM 11433 O  O   . HOH Z  3 .   ? 93.447  63.452  69.191 1.00 30.62  ? 644 HOH F O   1 
HETATM 11434 O  O   . HOH Z  3 .   ? 87.063  79.592  51.066 1.00 24.44  ? 645 HOH F O   1 
HETATM 11435 O  O   . HOH Z  3 .   ? 86.134  66.327  51.321 1.00 24.00  ? 646 HOH F O   1 
HETATM 11436 O  O   . HOH Z  3 .   ? 82.686  76.989  49.992 1.00 33.14  ? 647 HOH F O   1 
HETATM 11437 O  O   . HOH Z  3 .   ? 84.262  58.531  51.861 1.00 33.07  ? 648 HOH F O   1 
HETATM 11438 O  O   . HOH Z  3 .   ? 91.952  73.406  62.268 1.00 27.20  ? 649 HOH F O   1 
HETATM 11439 O  O   . HOH Z  3 .   ? 106.160 67.038  47.381 1.00 33.56  ? 650 HOH F O   1 
HETATM 11440 O  O   . HOH Z  3 .   ? 87.759  73.182  42.826 1.00 42.60  ? 651 HOH F O   1 
HETATM 11441 O  O   . HOH Z  3 .   ? 88.502  73.303  49.954 1.00 37.75  ? 652 HOH F O   1 
HETATM 11442 O  O   . HOH Z  3 .   ? 106.861 69.313  48.557 1.00 45.41  ? 653 HOH F O   1 
HETATM 11443 O  O   . HOH Z  3 .   ? 84.174  54.501  65.766 1.00 42.51  ? 654 HOH F O   1 
HETATM 11444 O  O   . HOH Z  3 .   ? 79.905  59.285  67.916 1.00 38.81  ? 655 HOH F O   1 
HETATM 11445 O  O   . HOH Z  3 .   ? 95.138  67.636  41.256 1.00 38.63  ? 656 HOH F O   1 
HETATM 11446 O  O   . HOH Z  3 .   ? 91.039  78.093  48.828 1.00 40.80  ? 657 HOH F O   1 
HETATM 11447 O  O   . HOH Z  3 .   ? 89.807  57.691  37.981 1.00 39.23  ? 658 HOH F O   1 
HETATM 11448 O  O   . HOH Z  3 .   ? 103.150 69.488  61.245 1.00 34.89  ? 659 HOH F O   1 
HETATM 11449 O  O   . HOH Z  3 .   ? 101.920 69.515  58.852 1.00 28.61  ? 660 HOH F O   1 
HETATM 11450 O  O   . HOH Z  3 .   ? 89.906  74.344  43.310 1.00 33.80  ? 661 HOH F O   1 
HETATM 11451 O  O   . HOH Z  3 .   ? 85.016  59.124  49.088 1.00 44.07  ? 662 HOH F O   1 
HETATM 11452 O  O   . HOH Z  3 .   ? 98.887  69.153  57.587 1.00 31.08  ? 663 HOH F O   1 
HETATM 11453 O  O   . HOH Z  3 .   ? 93.233  46.032  57.978 1.00 32.45  ? 664 HOH F O   1 
HETATM 11454 O  O   . HOH Z  3 .   ? 86.911  61.630  49.365 1.00 46.32  ? 665 HOH F O   1 
HETATM 11455 O  O   . HOH Z  3 .   ? 85.413  60.037  46.090 1.00 33.48  ? 666 HOH F O   1 
HETATM 11456 O  O   . HOH Z  3 .   ? 82.806  71.896  48.579 1.00 27.99  ? 667 HOH F O   1 
HETATM 11457 O  O   . HOH Z  3 .   ? 88.673  61.900  47.640 1.00 37.83  ? 668 HOH F O   1 
HETATM 11458 O  O   . HOH Z  3 .   ? 99.949  59.382  69.106 1.00 33.53  ? 669 HOH F O   1 
HETATM 11459 O  O   . HOH Z  3 .   ? 99.064  73.489  61.204 1.00 29.07  ? 670 HOH F O   1 
HETATM 11460 O  O   . HOH Z  3 .   ? 98.703  61.547  70.586 1.00 24.85  ? 671 HOH F O   1 
HETATM 11461 O  O   . HOH Z  3 .   ? 101.274 63.402  35.607 1.00 55.11  ? 672 HOH F O   1 
HETATM 11462 O  O   . HOH Z  3 .   ? 87.081  50.084  59.645 1.00 42.64  ? 673 HOH F O   1 
HETATM 11463 O  O   . HOH Z  3 .   ? 85.409  64.216  50.101 1.00 44.01  ? 674 HOH F O   1 
HETATM 11464 O  O   . HOH Z  3 .   ? 98.763  77.094  42.656 1.00 45.99  ? 675 HOH F O   1 
HETATM 11465 O  O   . HOH AA 3 .   ? 88.720  168.182 53.768 1.00 49.47  ? 608 HOH G O   1 
HETATM 11466 O  O   . HOH AA 3 .   ? 88.461  144.164 67.635 1.00 28.03  ? 609 HOH G O   1 
HETATM 11467 O  O   . HOH AA 3 .   ? 101.408 156.332 53.744 1.00 38.63  ? 610 HOH G O   1 
HETATM 11468 O  O   . HOH AA 3 .   ? 99.653  146.716 67.174 1.00 28.03  ? 611 HOH G O   1 
HETATM 11469 O  O   . HOH AA 3 .   ? 103.559 156.900 48.604 1.00 37.47  ? 612 HOH G O   1 
HETATM 11470 O  O   . HOH AA 3 .   ? 96.375  159.248 58.410 1.00 32.20  ? 613 HOH G O   1 
HETATM 11471 O  O   . HOH AA 3 .   ? 101.588 151.493 72.500 1.00 40.55  ? 614 HOH G O   1 
HETATM 11472 O  O   . HOH AA 3 .   ? 92.119  143.537 66.758 1.00 35.27  ? 615 HOH G O   1 
HETATM 11473 O  O   . HOH AA 3 .   ? 86.006  140.936 55.845 1.00 39.12  ? 616 HOH G O   1 
HETATM 11474 O  O   . HOH AA 3 .   ? 92.428  139.606 64.410 1.00 39.16  ? 617 HOH G O   1 
HETATM 11475 O  O   . HOH AA 3 .   ? 81.701  147.591 57.748 1.00 31.03  ? 618 HOH G O   1 
HETATM 11476 O  O   . HOH AA 3 .   ? 85.799  144.507 68.360 1.00 42.23  ? 619 HOH G O   1 
HETATM 11477 O  O   . HOH AA 3 .   ? 81.669  139.128 54.645 1.00 37.87  ? 620 HOH G O   1 
HETATM 11478 O  O   . HOH AA 3 .   ? 100.529 150.918 50.818 1.00 36.61  ? 621 HOH G O   1 
HETATM 11479 O  O   . HOH AA 3 .   ? 103.700 139.783 55.366 1.00 43.40  ? 622 HOH G O   1 
HETATM 11480 O  O   . HOH AA 3 .   ? 82.039  144.727 58.217 1.00 29.85  ? 623 HOH G O   1 
HETATM 11481 O  O   . HOH AA 3 .   ? 97.107  158.222 60.699 1.00 42.86  ? 624 HOH G O   1 
HETATM 11482 O  O   . HOH AA 3 .   ? 93.473  152.524 72.126 1.00 34.96  ? 625 HOH G O   1 
HETATM 11483 O  O   . HOH AA 3 .   ? 91.743  154.423 72.934 1.00 30.22  ? 626 HOH G O   1 
HETATM 11484 O  O   . HOH AA 3 .   ? 86.024  152.764 35.378 1.00 45.17  ? 627 HOH G O   1 
HETATM 11485 O  O   . HOH AA 3 .   ? 89.925  135.016 63.525 1.00 43.58  ? 628 HOH G O   1 
HETATM 11486 O  O   . HOH BA 3 .   ? 56.185  136.531 47.518 1.00 17.97  ? 609 HOH H O   1 
HETATM 11487 O  O   . HOH BA 3 .   ? 61.611  134.099 51.191 1.00 31.94  ? 610 HOH H O   1 
HETATM 11488 O  O   . HOH BA 3 .   ? 65.159  126.336 58.246 1.00 30.93  ? 611 HOH H O   1 
HETATM 11489 O  O   . HOH BA 3 .   ? 75.258  147.243 58.876 1.00 42.13  ? 612 HOH H O   1 
HETATM 11490 O  O   . HOH BA 3 .   ? 79.796  140.478 55.990 1.00 29.35  ? 613 HOH H O   1 
HETATM 11491 O  O   . HOH BA 3 .   ? 61.673  150.114 54.144 1.00 27.06  ? 614 HOH H O   1 
HETATM 11492 O  O   . HOH BA 3 .   ? 62.821  147.873 59.169 1.00 35.30  ? 615 HOH H O   1 
HETATM 11493 O  O   . HOH BA 3 .   ? 59.561  140.779 51.296 1.00 26.68  ? 616 HOH H O   1 
HETATM 11494 O  O   . HOH BA 3 .   ? 57.691  128.447 56.909 1.00 31.79  ? 617 HOH H O   1 
HETATM 11495 O  O   . HOH BA 3 .   ? 72.776  131.650 39.784 1.00 46.21  ? 618 HOH H O   1 
HETATM 11496 O  O   . HOH BA 3 .   ? 79.568  149.472 57.989 1.00 34.24  ? 619 HOH H O   1 
HETATM 11497 O  O   . HOH BA 3 .   ? 61.090  122.309 63.266 1.00 42.88  ? 620 HOH H O   1 
HETATM 11498 O  O   . HOH BA 3 .   ? 75.677  139.741 71.360 1.00 49.91  ? 621 HOH H O   1 
HETATM 11499 O  O   . HOH BA 3 .   ? 62.788  131.551 46.316 1.00 28.58  ? 622 HOH H O   1 
HETATM 11500 O  O   . HOH BA 3 .   ? 61.182  145.082 57.898 1.00 34.27  ? 623 HOH H O   1 
HETATM 11501 O  O   . HOH BA 3 .   ? 71.528  154.622 47.533 1.00 41.99  ? 624 HOH H O   1 
HETATM 11502 O  O   . HOH BA 3 .   ? 48.731  153.493 58.033 1.00 28.25  ? 625 HOH H O   1 
HETATM 11503 O  O   . HOH BA 3 .   ? 58.040  134.374 64.359 1.00 30.36  ? 626 HOH H O   1 
HETATM 11504 O  O   . HOH BA 3 .   ? 50.852  152.013 59.432 1.00 35.79  ? 627 HOH H O   1 
HETATM 11505 O  O   . HOH BA 3 .   ? 64.465  135.186 67.053 1.00 31.54  ? 628 HOH H O   1 
HETATM 11506 O  O   . HOH BA 3 .   ? 72.728  124.142 59.604 1.00 37.42  ? 629 HOH H O   1 
HETATM 11507 O  O   . HOH BA 3 .   ? 79.317  143.386 58.106 1.00 39.21  ? 630 HOH H O   1 
HETATM 11508 O  O   . HOH BA 3 .   ? 66.003  123.944 59.665 1.00 36.56  ? 631 HOH H O   1 
HETATM 11509 O  O   . HOH BA 3 .   ? 86.902  140.648 42.143 1.00 48.60  ? 632 HOH H O   1 
HETATM 11510 O  O   . HOH BA 3 .   ? 57.132  134.615 49.020 1.00 27.36  ? 633 HOH H O   1 
HETATM 11511 O  O   . HOH BA 3 .   ? 54.316  140.391 61.243 1.00 33.81  ? 634 HOH H O   1 
HETATM 11512 O  O   . HOH BA 3 .   ? 70.863  126.171 53.281 1.00 41.72  ? 635 HOH H O   1 
HETATM 11513 O  O   . HOH BA 3 .   ? 80.666  145.509 62.168 1.00 35.33  ? 636 HOH H O   1 
HETATM 11514 O  O   . HOH BA 3 .   ? 70.369  122.410 59.853 1.00 44.26  ? 637 HOH H O   1 
HETATM 11515 O  O   . HOH BA 3 .   ? 74.543  138.534 67.422 1.00 54.53  ? 638 HOH H O   1 
HETATM 11516 O  O   . HOH BA 3 .   ? 57.520  146.968 61.572 1.00 32.04  ? 639 HOH H O   1 
HETATM 11517 O  O   . HOH BA 3 .   ? 66.088  135.932 69.119 1.00 37.58  ? 640 HOH H O   1 
HETATM 11518 O  O   . HOH BA 3 .   ? 66.596  152.285 48.721 1.00 41.70  ? 641 HOH H O   1 
HETATM 11519 O  O   . HOH BA 3 .   ? 74.771  155.591 56.375 1.00 45.45  ? 642 HOH H O   1 
HETATM 11520 O  O   . HOH BA 3 .   ? 52.896  144.968 47.222 1.00 41.48  ? 643 HOH H O   1 
HETATM 11521 O  O   . HOH BA 3 .   ? 61.557  147.558 42.950 1.00 42.17  ? 644 HOH H O   1 
HETATM 11522 O  O   . HOH BA 3 .   ? 48.361  146.152 52.671 1.00 34.13  ? 645 HOH H O   1 
HETATM 11523 O  O   . HOH BA 3 .   ? 55.113  137.529 63.441 1.00 40.78  ? 646 HOH H O   1 
HETATM 11524 O  O   . HOH BA 3 .   ? 46.282  145.228 51.033 1.00 47.59  ? 647 HOH H O   1 
HETATM 11525 O  O   . HOH BA 3 .   ? 70.835  138.995 67.683 1.00 39.07  ? 648 HOH H O   1 
HETATM 11526 O  O   . HOH BA 3 .   ? 62.892  149.359 44.398 1.00 46.29  ? 649 HOH H O   1 
HETATM 11527 O  O   . HOH BA 3 .   ? 72.302  133.806 37.332 1.00 46.62  ? 650 HOH H O   1 
HETATM 11528 O  O   . HOH CA 3 .   ? 48.863  81.106  50.104 1.00 21.47  ? 610 HOH I O   1 
HETATM 11529 O  O   . HOH CA 3 .   ? 44.476  74.167  52.851 1.00 24.71  ? 611 HOH I O   1 
HETATM 11530 O  O   . HOH CA 3 .   ? 58.101  103.610 50.989 1.00 36.71  ? 612 HOH I O   1 
HETATM 11531 O  O   . HOH CA 3 .   ? 45.094  80.523  46.292 1.00 28.07  ? 613 HOH I O   1 
HETATM 11532 O  O   . HOH CA 3 .   ? 40.842  76.922  41.835 1.00 38.31  ? 614 HOH I O   1 
HETATM 11533 O  O   . HOH CA 3 .   ? 31.910  102.918 46.843 1.00 47.45  ? 615 HOH I O   1 
HETATM 11534 O  O   . HOH CA 3 .   ? 55.544  91.671  54.351 1.00 33.85  ? 616 HOH I O   1 
HETATM 11535 O  O   . HOH CA 3 .   ? 37.506  78.507  57.964 1.00 63.36  ? 617 HOH I O   1 
HETATM 11536 O  O   . HOH CA 3 .   ? 36.897  74.707  48.645 1.00 31.30  ? 618 HOH I O   1 
HETATM 11537 O  O   . HOH CA 3 .   ? 43.606  100.532 53.615 1.00 38.07  ? 619 HOH I O   1 
HETATM 11538 O  O   . HOH CA 3 .   ? 37.037  82.961  61.294 1.00 43.49  ? 620 HOH I O   1 
HETATM 11539 O  O   . HOH CA 3 .   ? 55.871  100.217 41.797 1.00 39.09  ? 621 HOH I O   1 
HETATM 11540 O  O   . HOH CA 3 .   ? 38.386  103.685 51.055 1.00 34.42  ? 622 HOH I O   1 
HETATM 11541 O  O   . HOH CA 3 .   ? 49.772  79.142  55.188 1.00 46.63  ? 623 HOH I O   1 
HETATM 11542 O  O   . HOH CA 3 .   ? 46.309  99.180  52.557 1.00 29.52  ? 624 HOH I O   1 
HETATM 11543 O  O   . HOH CA 3 .   ? 38.140  82.123  44.695 1.00 29.78  ? 625 HOH I O   1 
HETATM 11544 O  O   . HOH CA 3 .   ? 54.548  78.329  57.627 1.00 40.96  ? 626 HOH I O   1 
HETATM 11545 O  O   . HOH CA 3 .   ? 38.433  75.281  57.258 1.00 43.77  ? 627 HOH I O   1 
HETATM 11546 O  O   . HOH CA 3 .   ? 51.532  78.779  58.703 1.00 47.65  ? 628 HOH I O   1 
HETATM 11547 O  O   . HOH CA 3 .   ? 42.254  94.161  62.831 1.00 43.26  ? 629 HOH I O   1 
HETATM 11548 O  O   . HOH CA 3 .   ? 33.064  94.816  57.497 1.00 57.52  ? 630 HOH I O   1 
HETATM 11549 O  O   . HOH CA 3 .   ? 47.344  81.768  37.751 1.00 48.40  ? 631 HOH I O   1 
HETATM 11550 O  O   . HOH CA 3 .   ? 33.514  86.209  49.046 1.00 50.72  ? 632 HOH I O   1 
HETATM 11551 O  O   . HOH CA 3 .   ? 59.338  106.187 51.093 1.00 51.37  ? 633 HOH I O   1 
HETATM 11552 O  O   . HOH CA 3 .   ? 55.114  84.272  52.497 1.00 42.53  ? 634 HOH I O   1 
HETATM 11553 O  O   . HOH CA 3 .   ? 46.356  81.986  41.527 1.00 35.60  ? 635 HOH I O   1 
HETATM 11554 O  O   . HOH CA 3 .   ? 35.560  89.144  35.987 1.00 49.49  ? 636 HOH I O   1 
HETATM 11555 O  O   . HOH CA 3 .   ? 38.729  90.936  62.245 1.00 47.02  ? 637 HOH I O   1 
HETATM 11556 O  O   . HOH DA 3 .   ? 50.389  122.721 48.818 1.00 21.07  ? 611 HOH J O   1 
HETATM 11557 O  O   . HOH DA 3 .   ? 60.394  130.003 49.807 1.00 29.54  ? 612 HOH J O   1 
HETATM 11558 O  O   . HOH DA 3 .   ? 48.094  128.274 46.195 1.00 31.46  ? 613 HOH J O   1 
HETATM 11559 O  O   . HOH DA 3 .   ? 56.724  101.846 49.492 1.00 30.46  ? 614 HOH J O   1 
HETATM 11560 O  O   . HOH DA 3 .   ? 43.548  103.554 53.673 1.00 32.96  ? 615 HOH J O   1 
HETATM 11561 O  O   . HOH DA 3 .   ? 39.575  124.865 45.741 1.00 38.64  ? 616 HOH J O   1 
HETATM 11562 O  O   . HOH DA 3 .   ? 39.338  122.996 54.815 1.00 36.97  ? 617 HOH J O   1 
HETATM 11563 O  O   . HOH DA 3 .   ? 48.742  119.591 64.550 1.00 34.02  ? 618 HOH J O   1 
HETATM 11564 O  O   . HOH DA 3 .   ? 57.721  116.168 49.526 1.00 36.41  ? 619 HOH J O   1 
HETATM 11565 O  O   . HOH DA 3 .   ? 45.993  118.615 64.904 1.00 41.71  ? 620 HOH J O   1 
HETATM 11566 O  O   . HOH DA 3 .   ? 58.653  134.664 51.364 1.00 32.16  ? 621 HOH J O   1 
HETATM 11567 O  O   . HOH DA 3 .   ? 56.237  127.219 44.161 1.00 34.04  ? 622 HOH J O   1 
HETATM 11568 O  O   . HOH DA 3 .   ? 49.107  100.247 52.169 1.00 31.11  ? 623 HOH J O   1 
HETATM 11569 O  O   . HOH DA 3 .   ? 43.251  123.633 69.022 1.00 46.03  ? 624 HOH J O   1 
HETATM 11570 O  O   . HOH DA 3 .   ? 37.372  106.107 33.828 1.00 43.81  ? 625 HOH J O   1 
HETATM 11571 O  O   . HOH DA 3 .   ? 34.308  105.111 39.593 1.00 43.00  ? 626 HOH J O   1 
HETATM 11572 O  O   . HOH DA 3 .   ? 36.242  123.520 58.403 1.00 47.05  ? 627 HOH J O   1 
HETATM 11573 O  O   . HOH DA 3 .   ? 42.723  104.086 56.330 1.00 33.42  ? 628 HOH J O   1 
HETATM 11574 O  O   . HOH DA 3 .   ? 46.371  128.305 61.140 1.00 42.88  ? 629 HOH J O   1 
HETATM 11575 O  O   . HOH DA 3 .   ? 35.610  128.195 64.454 1.00 43.98  ? 630 HOH J O   1 
HETATM 11576 O  O   . HOH DA 3 .   ? 41.291  104.705 52.190 1.00 33.83  ? 631 HOH J O   1 
HETATM 11577 O  O   . HOH DA 3 .   ? 41.312  129.371 56.755 1.00 30.26  ? 632 HOH J O   1 
HETATM 11578 O  O   . HOH DA 3 .   ? 32.122  112.031 53.647 1.00 48.93  ? 633 HOH J O   1 
HETATM 11579 O  O   . HOH DA 3 .   ? 54.077  118.164 53.813 1.00 35.23  ? 634 HOH J O   1 
HETATM 11580 O  O   . HOH DA 3 .   ? 55.486  106.133 41.692 1.00 49.27  ? 635 HOH J O   1 
HETATM 11581 O  O   . HOH DA 3 .   ? 45.368  116.120 66.557 1.00 45.16  ? 636 HOH J O   1 
HETATM 11582 O  O   . HOH DA 3 .   ? 53.877  119.144 38.860 1.00 43.99  ? 637 HOH J O   1 
HETATM 11583 O  O   . HOH DA 3 .   ? 43.192  123.648 44.045 1.00 45.14  ? 638 HOH J O   1 
HETATM 11584 O  O   . HOH DA 3 .   ? 56.175  97.496  51.190 1.00 42.91  ? 639 HOH J O   1 
HETATM 11585 O  O   . HOH DA 3 .   ? 38.420  111.877 67.055 1.00 44.77  ? 640 HOH J O   1 
HETATM 11586 O  O   . HOH DA 3 .   ? 32.977  109.570 46.773 1.00 55.27  ? 641 HOH J O   1 
HETATM 11587 O  O   . HOH DA 3 .   ? 49.816  108.158 38.346 1.00 37.59  ? 642 HOH J O   1 
HETATM 11588 O  O   . HOH DA 3 .   ? 54.214  129.838 40.371 1.00 46.27  ? 643 HOH J O   1 
HETATM 11589 O  O   . HOH DA 3 .   ? 58.333  120.904 59.879 1.00 49.88  ? 644 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   GLY 1   -5  ?   ?   ?   A . n 
A 1 2   PRO 2   -4  ?   ?   ?   A . n 
A 1 3   LEU 3   -3  ?   ?   ?   A . n 
A 1 4   GLY 4   -2  ?   ?   ?   A . n 
A 1 5   SER 5   -1  ?   ?   ?   A . n 
A 1 6   MET 6   0   ?   ?   ?   A . n 
A 1 7   ALA 7   1   ?   ?   ?   A . n 
A 1 8   THR 8   2   2   THR THR A . n 
A 1 9   LYS 9   3   3   LYS LYS A . n 
A 1 10  ALA 10  4   4   ALA ALA A . n 
A 1 11  VAL 11  5   5   VAL VAL A . n 
A 1 12  CYS 12  6   6   CYS CYS A . n 
A 1 13  VAL 13  7   7   VAL VAL A . n 
A 1 14  LEU 14  8   8   LEU LEU A . n 
A 1 15  LYS 15  9   9   LYS LYS A . n 
A 1 16  GLY 16  10  10  GLY GLY A . n 
A 1 17  ASP 17  11  11  ASP ASP A . n 
A 1 18  GLY 18  12  12  GLY GLY A . n 
A 1 19  PRO 19  13  13  PRO PRO A . n 
A 1 20  VAL 20  14  14  VAL VAL A . n 
A 1 21  GLN 21  15  15  GLN GLN A . n 
A 1 22  GLY 22  16  16  GLY GLY A . n 
A 1 23  ILE 23  17  17  ILE ILE A . n 
A 1 24  ILE 24  18  18  ILE ILE A . n 
A 1 25  ASN 25  19  19  ASN ASN A . n 
A 1 26  PHE 26  20  20  PHE PHE A . n 
A 1 27  GLU 27  21  21  GLU GLU A . n 
A 1 28  GLN 28  22  22  GLN GLN A . n 
A 1 29  LYS 29  23  23  LYS LYS A . n 
A 1 30  GLU 30  24  24  GLU GLU A . n 
A 1 31  SER 31  25  25  SER SER A . n 
A 1 32  ASN 32  26  26  ASN ASN A . n 
A 1 33  GLY 33  27  27  GLY GLY A . n 
A 1 34  PRO 34  28  28  PRO PRO A . n 
A 1 35  VAL 35  29  29  VAL VAL A . n 
A 1 36  LYS 36  30  30  LYS LYS A . n 
A 1 37  VAL 37  31  31  VAL VAL A . n 
A 1 38  TRP 38  32  32  TRP TRP A . n 
A 1 39  GLY 39  33  33  GLY GLY A . n 
A 1 40  SER 40  34  34  SER SER A . n 
A 1 41  ILE 41  35  35  ILE ILE A . n 
A 1 42  LYS 42  36  36  LYS LYS A . n 
A 1 43  GLY 43  37  37  GLY GLY A . n 
A 1 44  LEU 44  38  38  LEU LEU A . n 
A 1 45  THR 45  39  39  THR THR A . n 
A 1 46  GLU 46  40  40  GLU GLU A . n 
A 1 47  GLY 47  41  41  GLY GLY A . n 
A 1 48  LEU 48  42  42  LEU LEU A . n 
A 1 49  HIS 49  43  43  HIS HIS A . n 
A 1 50  GLY 50  44  44  GLY GLY A . n 
A 1 51  PHE 51  45  45  PHE PHE A . n 
A 1 52  HIS 52  46  46  HIS HIS A . n 
A 1 53  VAL 53  47  47  VAL VAL A . n 
A 1 54  HIS 54  48  48  HIS HIS A . n 
A 1 55  GLU 55  49  49  GLU GLU A . n 
A 1 56  PHE 56  50  50  PHE PHE A . n 
A 1 57  GLY 57  51  51  GLY GLY A . n 
A 1 58  ASP 58  52  52  ASP ASP A . n 
A 1 59  ASN 59  53  53  ASN ASN A . n 
A 1 60  THR 60  54  54  THR THR A . n 
A 1 61  ALA 61  55  55  ALA ALA A . n 
A 1 62  GLY 62  56  56  GLY GLY A . n 
A 1 63  CYS 63  57  57  CYS CYS A . n 
A 1 64  THR 64  58  58  THR THR A . n 
A 1 65  SER 65  59  59  SER SER A . n 
A 1 66  ALA 66  60  60  ALA ALA A . n 
A 1 67  GLY 67  61  61  GLY GLY A . n 
A 1 68  PRO 68  62  62  PRO PRO A . n 
A 1 69  HIS 69  63  63  HIS HIS A . n 
A 1 70  PHE 70  64  64  PHE PHE A . n 
A 1 71  ASN 71  65  65  ASN ASN A . n 
A 1 72  PRO 72  66  66  PRO PRO A . n 
A 1 73  LEU 73  67  67  LEU LEU A . n 
A 1 74  SER 74  68  68  SER SER A . n 
A 1 75  ARG 75  69  69  ARG ARG A . n 
A 1 76  LYS 76  70  70  LYS LYS A . n 
A 1 77  HIS 77  71  71  HIS HIS A . n 
A 1 78  GLY 78  72  72  GLY GLY A . n 
A 1 79  GLY 79  73  73  GLY GLY A . n 
A 1 80  PRO 80  74  74  PRO PRO A . n 
A 1 81  LYS 81  75  75  LYS LYS A . n 
A 1 82  ASP 82  76  76  ASP ASP A . n 
A 1 83  GLU 83  77  77  GLU GLU A . n 
A 1 84  GLU 84  78  78  GLU GLU A . n 
A 1 85  ARG 85  79  79  ARG ARG A . n 
A 1 86  HIS 86  80  80  HIS HIS A . n 
A 1 87  VAL 87  81  81  VAL VAL A . n 
A 1 88  GLY 88  82  82  GLY GLY A . n 
A 1 89  ASP 89  83  83  ASP ASP A . n 
A 1 90  LEU 90  84  84  LEU LEU A . n 
A 1 91  GLY 91  85  85  GLY GLY A . n 
A 1 92  ASN 92  86  86  ASN ASN A . n 
A 1 93  VAL 93  87  87  VAL VAL A . n 
A 1 94  THR 94  88  88  THR THR A . n 
A 1 95  ALA 95  89  89  ALA ALA A . n 
A 1 96  ASP 96  90  90  ASP ASP A . n 
A 1 97  LYS 97  91  91  LYS LYS A . n 
A 1 98  ASP 98  92  92  ASP ASP A . n 
A 1 99  ALA 99  93  93  ALA ALA A . n 
A 1 100 VAL 100 94  94  VAL VAL A . n 
A 1 101 ALA 101 95  95  ALA ALA A . n 
A 1 102 ASP 102 96  96  ASP ASP A . n 
A 1 103 VAL 103 97  97  VAL VAL A . n 
A 1 104 SER 104 98  98  SER SER A . n 
A 1 105 ILE 105 99  99  ILE ILE A . n 
A 1 106 GLU 106 100 100 GLU GLU A . n 
A 1 107 ASP 107 101 101 ASP ASP A . n 
A 1 108 SER 108 102 102 SER SER A . n 
A 1 109 VAL 109 103 103 VAL VAL A . n 
A 1 110 ILE 110 104 104 ILE ILE A . n 
A 1 111 SER 111 105 105 SER SER A . n 
A 1 112 LEU 112 106 106 LEU LEU A . n 
A 1 113 SER 113 107 107 SER SER A . n 
A 1 114 GLY 114 108 108 GLY GLY A . n 
A 1 115 ASP 115 109 109 ASP ASP A . n 
A 1 116 HIS 116 110 110 HIS HIS A . n 
A 1 117 CYS 117 111 111 CYS CYS A . n 
A 1 118 ILE 118 112 112 ILE ILE A . n 
A 1 119 ILE 119 113 113 ILE ILE A . n 
A 1 120 GLY 120 114 114 GLY GLY A . n 
A 1 121 ARG 121 115 115 ARG ARG A . n 
A 1 122 THR 122 116 116 THR THR A . n 
A 1 123 LEU 123 117 117 LEU LEU A . n 
A 1 124 VAL 124 118 118 VAL VAL A . n 
A 1 125 VAL 125 119 119 VAL VAL A . n 
A 1 126 HIS 126 120 120 HIS HIS A . n 
A 1 127 GLU 127 121 121 GLU GLU A . n 
A 1 128 LYS 128 122 122 LYS LYS A . n 
A 1 129 ALA 129 123 123 ALA ALA A . n 
A 1 130 ASP 130 124 124 ASP ASP A . n 
A 1 131 ASP 131 125 125 ASP ASP A . n 
A 1 132 LEU 132 126 126 LEU LEU A . n 
A 1 133 GLY 133 127 127 GLY GLY A . n 
A 1 134 LYS 134 128 128 LYS LYS A . n 
A 1 135 GLY 135 129 129 GLY GLY A . n 
A 1 136 GLY 136 130 130 GLY GLY A . n 
A 1 137 ASN 137 131 131 ASN ASN A . n 
A 1 138 GLU 138 132 132 GLU GLU A . n 
A 1 139 GLU 139 133 133 GLU GLU A . n 
A 1 140 SER 140 134 134 SER SER A . n 
A 1 141 THR 141 135 135 THR THR A . n 
A 1 142 LYS 142 136 136 LYS LYS A . n 
A 1 143 THR 143 137 137 THR THR A . n 
A 1 144 GLY 144 138 138 GLY GLY A . n 
A 1 145 ASN 145 139 139 ASN ASN A . n 
A 1 146 ALA 146 140 140 ALA ALA A . n 
A 1 147 GLY 147 141 141 GLY GLY A . n 
A 1 148 SER 148 142 142 SER SER A . n 
A 1 149 ARG 149 143 143 ARG ARG A . n 
A 1 150 LEU 150 144 144 LEU LEU A . n 
A 1 151 ALA 151 145 145 ALA ALA A . n 
A 1 152 CYS 152 146 146 CYS CYS A . n 
A 1 153 GLY 153 147 147 GLY GLY A . n 
A 1 154 VAL 154 148 148 VAL VAL A . n 
A 1 155 ILE 155 149 149 ILE ILE A . n 
A 1 156 GLY 156 150 150 GLY GLY A . n 
A 1 157 ILE 157 151 151 ILE ILE A . n 
A 1 158 ALA 158 152 152 ALA ALA A . n 
A 1 159 GLN 159 153 153 GLN GLN A . n 
B 1 1   GLY 1   -5  ?   ?   ?   B . n 
B 1 2   PRO 2   -4  ?   ?   ?   B . n 
B 1 3   LEU 3   -3  ?   ?   ?   B . n 
B 1 4   GLY 4   -2  ?   ?   ?   B . n 
B 1 5   SER 5   -1  ?   ?   ?   B . n 
B 1 6   MET 6   0   ?   ?   ?   B . n 
B 1 7   ALA 7   1   ?   ?   ?   B . n 
B 1 8   THR 8   2   2   THR THR B . n 
B 1 9   LYS 9   3   3   LYS LYS B . n 
B 1 10  ALA 10  4   4   ALA ALA B . n 
B 1 11  VAL 11  5   5   VAL VAL B . n 
B 1 12  CYS 12  6   6   CYS CYS B . n 
B 1 13  VAL 13  7   7   VAL VAL B . n 
B 1 14  LEU 14  8   8   LEU LEU B . n 
B 1 15  LYS 15  9   9   LYS LYS B . n 
B 1 16  GLY 16  10  10  GLY GLY B . n 
B 1 17  ASP 17  11  11  ASP ASP B . n 
B 1 18  GLY 18  12  12  GLY GLY B . n 
B 1 19  PRO 19  13  13  PRO PRO B . n 
B 1 20  VAL 20  14  14  VAL VAL B . n 
B 1 21  GLN 21  15  15  GLN GLN B . n 
B 1 22  GLY 22  16  16  GLY GLY B . n 
B 1 23  ILE 23  17  17  ILE ILE B . n 
B 1 24  ILE 24  18  18  ILE ILE B . n 
B 1 25  ASN 25  19  19  ASN ASN B . n 
B 1 26  PHE 26  20  20  PHE PHE B . n 
B 1 27  GLU 27  21  21  GLU GLU B . n 
B 1 28  GLN 28  22  22  GLN GLN B . n 
B 1 29  LYS 29  23  23  LYS LYS B . n 
B 1 30  GLU 30  24  24  GLU GLU B . n 
B 1 31  SER 31  25  25  SER SER B . n 
B 1 32  ASN 32  26  26  ASN ASN B . n 
B 1 33  GLY 33  27  27  GLY GLY B . n 
B 1 34  PRO 34  28  28  PRO PRO B . n 
B 1 35  VAL 35  29  29  VAL VAL B . n 
B 1 36  LYS 36  30  30  LYS LYS B . n 
B 1 37  VAL 37  31  31  VAL VAL B . n 
B 1 38  TRP 38  32  32  TRP TRP B . n 
B 1 39  GLY 39  33  33  GLY GLY B . n 
B 1 40  SER 40  34  34  SER SER B . n 
B 1 41  ILE 41  35  35  ILE ILE B . n 
B 1 42  LYS 42  36  36  LYS LYS B . n 
B 1 43  GLY 43  37  37  GLY GLY B . n 
B 1 44  LEU 44  38  38  LEU LEU B . n 
B 1 45  THR 45  39  39  THR THR B . n 
B 1 46  GLU 46  40  40  GLU GLU B . n 
B 1 47  GLY 47  41  41  GLY GLY B . n 
B 1 48  LEU 48  42  42  LEU LEU B . n 
B 1 49  HIS 49  43  43  HIS HIS B . n 
B 1 50  GLY 50  44  44  GLY GLY B . n 
B 1 51  PHE 51  45  45  PHE PHE B . n 
B 1 52  HIS 52  46  46  HIS HIS B . n 
B 1 53  VAL 53  47  47  VAL VAL B . n 
B 1 54  HIS 54  48  48  HIS HIS B . n 
B 1 55  GLU 55  49  49  GLU GLU B . n 
B 1 56  PHE 56  50  50  PHE PHE B . n 
B 1 57  GLY 57  51  51  GLY GLY B . n 
B 1 58  ASP 58  52  52  ASP ASP B . n 
B 1 59  ASN 59  53  53  ASN ASN B . n 
B 1 60  THR 60  54  54  THR THR B . n 
B 1 61  ALA 61  55  55  ALA ALA B . n 
B 1 62  GLY 62  56  56  GLY GLY B . n 
B 1 63  CYS 63  57  57  CYS CYS B . n 
B 1 64  THR 64  58  58  THR THR B . n 
B 1 65  SER 65  59  59  SER SER B . n 
B 1 66  ALA 66  60  60  ALA ALA B . n 
B 1 67  GLY 67  61  61  GLY GLY B . n 
B 1 68  PRO 68  62  62  PRO PRO B . n 
B 1 69  HIS 69  63  63  HIS HIS B . n 
B 1 70  PHE 70  64  64  PHE PHE B . n 
B 1 71  ASN 71  65  65  ASN ASN B . n 
B 1 72  PRO 72  66  66  PRO PRO B . n 
B 1 73  LEU 73  67  67  LEU LEU B . n 
B 1 74  SER 74  68  68  SER SER B . n 
B 1 75  ARG 75  69  69  ARG ARG B . n 
B 1 76  LYS 76  70  70  LYS LYS B . n 
B 1 77  HIS 77  71  71  HIS HIS B . n 
B 1 78  GLY 78  72  72  GLY GLY B . n 
B 1 79  GLY 79  73  73  GLY GLY B . n 
B 1 80  PRO 80  74  74  PRO PRO B . n 
B 1 81  LYS 81  75  75  LYS LYS B . n 
B 1 82  ASP 82  76  76  ASP ASP B . n 
B 1 83  GLU 83  77  77  GLU GLU B . n 
B 1 84  GLU 84  78  78  GLU GLU B . n 
B 1 85  ARG 85  79  79  ARG ARG B . n 
B 1 86  HIS 86  80  80  HIS HIS B . n 
B 1 87  VAL 87  81  81  VAL VAL B . n 
B 1 88  GLY 88  82  82  GLY GLY B . n 
B 1 89  ASP 89  83  83  ASP ASP B . n 
B 1 90  LEU 90  84  84  LEU LEU B . n 
B 1 91  GLY 91  85  85  GLY GLY B . n 
B 1 92  ASN 92  86  86  ASN ASN B . n 
B 1 93  VAL 93  87  87  VAL VAL B . n 
B 1 94  THR 94  88  88  THR THR B . n 
B 1 95  ALA 95  89  89  ALA ALA B . n 
B 1 96  ASP 96  90  90  ASP ASP B . n 
B 1 97  LYS 97  91  91  LYS LYS B . n 
B 1 98  ASP 98  92  92  ASP ASP B . n 
B 1 99  ALA 99  93  93  ALA ALA B . n 
B 1 100 VAL 100 94  94  VAL VAL B . n 
B 1 101 ALA 101 95  95  ALA ALA B . n 
B 1 102 ASP 102 96  96  ASP ASP B . n 
B 1 103 VAL 103 97  97  VAL VAL B . n 
B 1 104 SER 104 98  98  SER SER B . n 
B 1 105 ILE 105 99  99  ILE ILE B . n 
B 1 106 GLU 106 100 100 GLU GLU B . n 
B 1 107 ASP 107 101 101 ASP ASP B . n 
B 1 108 SER 108 102 102 SER SER B . n 
B 1 109 VAL 109 103 103 VAL VAL B . n 
B 1 110 ILE 110 104 104 ILE ILE B . n 
B 1 111 SER 111 105 105 SER SER B . n 
B 1 112 LEU 112 106 106 LEU LEU B . n 
B 1 113 SER 113 107 107 SER SER B . n 
B 1 114 GLY 114 108 108 GLY GLY B . n 
B 1 115 ASP 115 109 109 ASP ASP B . n 
B 1 116 HIS 116 110 110 HIS HIS B . n 
B 1 117 CYS 117 111 111 CYS CYS B . n 
B 1 118 ILE 118 112 112 ILE ILE B . n 
B 1 119 ILE 119 113 113 ILE ILE B . n 
B 1 120 GLY 120 114 114 GLY GLY B . n 
B 1 121 ARG 121 115 115 ARG ARG B . n 
B 1 122 THR 122 116 116 THR THR B . n 
B 1 123 LEU 123 117 117 LEU LEU B . n 
B 1 124 VAL 124 118 118 VAL VAL B . n 
B 1 125 VAL 125 119 119 VAL VAL B . n 
B 1 126 HIS 126 120 120 HIS HIS B . n 
B 1 127 GLU 127 121 121 GLU GLU B . n 
B 1 128 LYS 128 122 122 LYS LYS B . n 
B 1 129 ALA 129 123 123 ALA ALA B . n 
B 1 130 ASP 130 124 124 ASP ASP B . n 
B 1 131 ASP 131 125 125 ASP ASP B . n 
B 1 132 LEU 132 126 126 LEU LEU B . n 
B 1 133 GLY 133 127 127 GLY GLY B . n 
B 1 134 LYS 134 128 128 LYS LYS B . n 
B 1 135 GLY 135 129 129 GLY GLY B . n 
B 1 136 GLY 136 130 130 GLY GLY B . n 
B 1 137 ASN 137 131 131 ASN ASN B . n 
B 1 138 GLU 138 132 132 GLU GLU B . n 
B 1 139 GLU 139 133 133 GLU GLU B . n 
B 1 140 SER 140 134 134 SER SER B . n 
B 1 141 THR 141 135 135 THR THR B . n 
B 1 142 LYS 142 136 136 LYS LYS B . n 
B 1 143 THR 143 137 137 THR THR B . n 
B 1 144 GLY 144 138 138 GLY GLY B . n 
B 1 145 ASN 145 139 139 ASN ASN B . n 
B 1 146 ALA 146 140 140 ALA ALA B . n 
B 1 147 GLY 147 141 141 GLY GLY B . n 
B 1 148 SER 148 142 142 SER SER B . n 
B 1 149 ARG 149 143 143 ARG ARG B . n 
B 1 150 LEU 150 144 144 LEU LEU B . n 
B 1 151 ALA 151 145 145 ALA ALA B . n 
B 1 152 CYS 152 146 146 CYS CYS B . n 
B 1 153 GLY 153 147 147 GLY GLY B . n 
B 1 154 VAL 154 148 148 VAL VAL B . n 
B 1 155 ILE 155 149 149 ILE ILE B . n 
B 1 156 GLY 156 150 150 GLY GLY B . n 
B 1 157 ILE 157 151 151 ILE ILE B . n 
B 1 158 ALA 158 152 152 ALA ALA B . n 
B 1 159 GLN 159 153 153 GLN GLN B . n 
C 1 1   GLY 1   -5  ?   ?   ?   C . n 
C 1 2   PRO 2   -4  ?   ?   ?   C . n 
C 1 3   LEU 3   -3  ?   ?   ?   C . n 
C 1 4   GLY 4   -2  ?   ?   ?   C . n 
C 1 5   SER 5   -1  ?   ?   ?   C . n 
C 1 6   MET 6   0   ?   ?   ?   C . n 
C 1 7   ALA 7   1   1   ALA ALA C . n 
C 1 8   THR 8   2   2   THR THR C . n 
C 1 9   LYS 9   3   3   LYS LYS C . n 
C 1 10  ALA 10  4   4   ALA ALA C . n 
C 1 11  VAL 11  5   5   VAL VAL C . n 
C 1 12  CYS 12  6   6   CYS CYS C . n 
C 1 13  VAL 13  7   7   VAL VAL C . n 
C 1 14  LEU 14  8   8   LEU LEU C . n 
C 1 15  LYS 15  9   9   LYS LYS C . n 
C 1 16  GLY 16  10  10  GLY GLY C . n 
C 1 17  ASP 17  11  11  ASP ASP C . n 
C 1 18  GLY 18  12  12  GLY GLY C . n 
C 1 19  PRO 19  13  13  PRO PRO C . n 
C 1 20  VAL 20  14  14  VAL VAL C . n 
C 1 21  GLN 21  15  15  GLN GLN C . n 
C 1 22  GLY 22  16  16  GLY GLY C . n 
C 1 23  ILE 23  17  17  ILE ILE C . n 
C 1 24  ILE 24  18  18  ILE ILE C . n 
C 1 25  ASN 25  19  19  ASN ASN C . n 
C 1 26  PHE 26  20  20  PHE PHE C . n 
C 1 27  GLU 27  21  21  GLU GLU C . n 
C 1 28  GLN 28  22  22  GLN GLN C . n 
C 1 29  LYS 29  23  23  LYS LYS C . n 
C 1 30  GLU 30  24  24  GLU GLU C . n 
C 1 31  SER 31  25  25  SER SER C . n 
C 1 32  ASN 32  26  26  ASN ASN C . n 
C 1 33  GLY 33  27  27  GLY GLY C . n 
C 1 34  PRO 34  28  28  PRO PRO C . n 
C 1 35  VAL 35  29  29  VAL VAL C . n 
C 1 36  LYS 36  30  30  LYS LYS C . n 
C 1 37  VAL 37  31  31  VAL VAL C . n 
C 1 38  TRP 38  32  32  TRP TRP C . n 
C 1 39  GLY 39  33  33  GLY GLY C . n 
C 1 40  SER 40  34  34  SER SER C . n 
C 1 41  ILE 41  35  35  ILE ILE C . n 
C 1 42  LYS 42  36  36  LYS LYS C . n 
C 1 43  GLY 43  37  37  GLY GLY C . n 
C 1 44  LEU 44  38  38  LEU LEU C . n 
C 1 45  THR 45  39  39  THR THR C . n 
C 1 46  GLU 46  40  40  GLU GLU C . n 
C 1 47  GLY 47  41  41  GLY GLY C . n 
C 1 48  LEU 48  42  42  LEU LEU C . n 
C 1 49  HIS 49  43  43  HIS HIS C . n 
C 1 50  GLY 50  44  44  GLY GLY C . n 
C 1 51  PHE 51  45  45  PHE PHE C . n 
C 1 52  HIS 52  46  46  HIS HIS C . n 
C 1 53  VAL 53  47  47  VAL VAL C . n 
C 1 54  HIS 54  48  48  HIS HIS C . n 
C 1 55  GLU 55  49  49  GLU GLU C . n 
C 1 56  PHE 56  50  50  PHE PHE C . n 
C 1 57  GLY 57  51  51  GLY GLY C . n 
C 1 58  ASP 58  52  52  ASP ASP C . n 
C 1 59  ASN 59  53  53  ASN ASN C . n 
C 1 60  THR 60  54  54  THR THR C . n 
C 1 61  ALA 61  55  55  ALA ALA C . n 
C 1 62  GLY 62  56  56  GLY GLY C . n 
C 1 63  CYS 63  57  57  CYS CYS C . n 
C 1 64  THR 64  58  58  THR THR C . n 
C 1 65  SER 65  59  59  SER SER C . n 
C 1 66  ALA 66  60  60  ALA ALA C . n 
C 1 67  GLY 67  61  61  GLY GLY C . n 
C 1 68  PRO 68  62  62  PRO PRO C . n 
C 1 69  HIS 69  63  63  HIS HIS C . n 
C 1 70  PHE 70  64  64  PHE PHE C . n 
C 1 71  ASN 71  65  65  ASN ASN C . n 
C 1 72  PRO 72  66  66  PRO PRO C . n 
C 1 73  LEU 73  67  67  LEU LEU C . n 
C 1 74  SER 74  68  68  SER SER C . n 
C 1 75  ARG 75  69  69  ARG ARG C . n 
C 1 76  LYS 76  70  70  LYS LYS C . n 
C 1 77  HIS 77  71  71  HIS HIS C . n 
C 1 78  GLY 78  72  72  GLY GLY C . n 
C 1 79  GLY 79  73  73  GLY GLY C . n 
C 1 80  PRO 80  74  74  PRO PRO C . n 
C 1 81  LYS 81  75  75  LYS LYS C . n 
C 1 82  ASP 82  76  76  ASP ASP C . n 
C 1 83  GLU 83  77  77  GLU GLU C . n 
C 1 84  GLU 84  78  78  GLU GLU C . n 
C 1 85  ARG 85  79  79  ARG ARG C . n 
C 1 86  HIS 86  80  80  HIS HIS C . n 
C 1 87  VAL 87  81  81  VAL VAL C . n 
C 1 88  GLY 88  82  82  GLY GLY C . n 
C 1 89  ASP 89  83  83  ASP ASP C . n 
C 1 90  LEU 90  84  84  LEU LEU C . n 
C 1 91  GLY 91  85  85  GLY GLY C . n 
C 1 92  ASN 92  86  86  ASN ASN C . n 
C 1 93  VAL 93  87  87  VAL VAL C . n 
C 1 94  THR 94  88  88  THR THR C . n 
C 1 95  ALA 95  89  89  ALA ALA C . n 
C 1 96  ASP 96  90  90  ASP ASP C . n 
C 1 97  LYS 97  91  91  LYS LYS C . n 
C 1 98  ASP 98  92  92  ASP ASP C . n 
C 1 99  ALA 99  93  93  ALA ALA C . n 
C 1 100 VAL 100 94  94  VAL VAL C . n 
C 1 101 ALA 101 95  95  ALA ALA C . n 
C 1 102 ASP 102 96  96  ASP ASP C . n 
C 1 103 VAL 103 97  97  VAL VAL C . n 
C 1 104 SER 104 98  98  SER SER C . n 
C 1 105 ILE 105 99  99  ILE ILE C . n 
C 1 106 GLU 106 100 100 GLU GLU C . n 
C 1 107 ASP 107 101 101 ASP ASP C . n 
C 1 108 SER 108 102 102 SER SER C . n 
C 1 109 VAL 109 103 103 VAL VAL C . n 
C 1 110 ILE 110 104 104 ILE ILE C . n 
C 1 111 SER 111 105 105 SER SER C . n 
C 1 112 LEU 112 106 106 LEU LEU C . n 
C 1 113 SER 113 107 107 SER SER C . n 
C 1 114 GLY 114 108 108 GLY GLY C . n 
C 1 115 ASP 115 109 109 ASP ASP C . n 
C 1 116 HIS 116 110 110 HIS HIS C . n 
C 1 117 CYS 117 111 111 CYS CYS C . n 
C 1 118 ILE 118 112 112 ILE ILE C . n 
C 1 119 ILE 119 113 113 ILE ILE C . n 
C 1 120 GLY 120 114 114 GLY GLY C . n 
C 1 121 ARG 121 115 115 ARG ARG C . n 
C 1 122 THR 122 116 116 THR THR C . n 
C 1 123 LEU 123 117 117 LEU LEU C . n 
C 1 124 VAL 124 118 118 VAL VAL C . n 
C 1 125 VAL 125 119 119 VAL VAL C . n 
C 1 126 HIS 126 120 120 HIS HIS C . n 
C 1 127 GLU 127 121 121 GLU GLU C . n 
C 1 128 LYS 128 122 122 LYS LYS C . n 
C 1 129 ALA 129 123 123 ALA ALA C . n 
C 1 130 ASP 130 124 124 ASP ASP C . n 
C 1 131 ASP 131 125 125 ASP ASP C . n 
C 1 132 LEU 132 126 126 LEU LEU C . n 
C 1 133 GLY 133 127 127 GLY GLY C . n 
C 1 134 LYS 134 128 128 LYS LYS C . n 
C 1 135 GLY 135 129 129 GLY GLY C . n 
C 1 136 GLY 136 130 130 GLY GLY C . n 
C 1 137 ASN 137 131 131 ASN ASN C . n 
C 1 138 GLU 138 132 132 GLU GLU C . n 
C 1 139 GLU 139 133 133 GLU GLU C . n 
C 1 140 SER 140 134 134 SER SER C . n 
C 1 141 THR 141 135 135 THR THR C . n 
C 1 142 LYS 142 136 136 LYS LYS C . n 
C 1 143 THR 143 137 137 THR THR C . n 
C 1 144 GLY 144 138 138 GLY GLY C . n 
C 1 145 ASN 145 139 139 ASN ASN C . n 
C 1 146 ALA 146 140 140 ALA ALA C . n 
C 1 147 GLY 147 141 141 GLY GLY C . n 
C 1 148 SER 148 142 142 SER SER C . n 
C 1 149 ARG 149 143 143 ARG ARG C . n 
C 1 150 LEU 150 144 144 LEU LEU C . n 
C 1 151 ALA 151 145 145 ALA ALA C . n 
C 1 152 CYS 152 146 146 CYS CYS C . n 
C 1 153 GLY 153 147 147 GLY GLY C . n 
C 1 154 VAL 154 148 148 VAL VAL C . n 
C 1 155 ILE 155 149 149 ILE ILE C . n 
C 1 156 GLY 156 150 150 GLY GLY C . n 
C 1 157 ILE 157 151 151 ILE ILE C . n 
C 1 158 ALA 158 152 152 ALA ALA C . n 
C 1 159 GLN 159 153 153 GLN GLN C . n 
D 1 1   GLY 1   -5  ?   ?   ?   D . n 
D 1 2   PRO 2   -4  ?   ?   ?   D . n 
D 1 3   LEU 3   -3  ?   ?   ?   D . n 
D 1 4   GLY 4   -2  ?   ?   ?   D . n 
D 1 5   SER 5   -1  ?   ?   ?   D . n 
D 1 6   MET 6   0   ?   ?   ?   D . n 
D 1 7   ALA 7   1   1   ALA ALA D . n 
D 1 8   THR 8   2   2   THR THR D . n 
D 1 9   LYS 9   3   3   LYS LYS D . n 
D 1 10  ALA 10  4   4   ALA ALA D . n 
D 1 11  VAL 11  5   5   VAL VAL D . n 
D 1 12  CYS 12  6   6   CYS CYS D . n 
D 1 13  VAL 13  7   7   VAL VAL D . n 
D 1 14  LEU 14  8   8   LEU LEU D . n 
D 1 15  LYS 15  9   9   LYS LYS D . n 
D 1 16  GLY 16  10  10  GLY GLY D . n 
D 1 17  ASP 17  11  11  ASP ASP D . n 
D 1 18  GLY 18  12  12  GLY GLY D . n 
D 1 19  PRO 19  13  13  PRO PRO D . n 
D 1 20  VAL 20  14  14  VAL VAL D . n 
D 1 21  GLN 21  15  15  GLN GLN D . n 
D 1 22  GLY 22  16  16  GLY GLY D . n 
D 1 23  ILE 23  17  17  ILE ILE D . n 
D 1 24  ILE 24  18  18  ILE ILE D . n 
D 1 25  ASN 25  19  19  ASN ASN D . n 
D 1 26  PHE 26  20  20  PHE PHE D . n 
D 1 27  GLU 27  21  21  GLU GLU D . n 
D 1 28  GLN 28  22  22  GLN GLN D . n 
D 1 29  LYS 29  23  23  LYS LYS D . n 
D 1 30  GLU 30  24  24  GLU GLU D . n 
D 1 31  SER 31  25  25  SER SER D . n 
D 1 32  ASN 32  26  26  ASN ASN D . n 
D 1 33  GLY 33  27  27  GLY GLY D . n 
D 1 34  PRO 34  28  28  PRO PRO D . n 
D 1 35  VAL 35  29  29  VAL VAL D . n 
D 1 36  LYS 36  30  30  LYS LYS D . n 
D 1 37  VAL 37  31  31  VAL VAL D . n 
D 1 38  TRP 38  32  32  TRP TRP D . n 
D 1 39  GLY 39  33  33  GLY GLY D . n 
D 1 40  SER 40  34  34  SER SER D . n 
D 1 41  ILE 41  35  35  ILE ILE D . n 
D 1 42  LYS 42  36  36  LYS LYS D . n 
D 1 43  GLY 43  37  37  GLY GLY D . n 
D 1 44  LEU 44  38  38  LEU LEU D . n 
D 1 45  THR 45  39  39  THR THR D . n 
D 1 46  GLU 46  40  40  GLU GLU D . n 
D 1 47  GLY 47  41  41  GLY GLY D . n 
D 1 48  LEU 48  42  42  LEU LEU D . n 
D 1 49  HIS 49  43  43  HIS HIS D . n 
D 1 50  GLY 50  44  44  GLY GLY D . n 
D 1 51  PHE 51  45  45  PHE PHE D . n 
D 1 52  HIS 52  46  46  HIS HIS D . n 
D 1 53  VAL 53  47  47  VAL VAL D . n 
D 1 54  HIS 54  48  48  HIS HIS D . n 
D 1 55  GLU 55  49  49  GLU GLU D . n 
D 1 56  PHE 56  50  50  PHE PHE D . n 
D 1 57  GLY 57  51  51  GLY GLY D . n 
D 1 58  ASP 58  52  52  ASP ASP D . n 
D 1 59  ASN 59  53  53  ASN ASN D . n 
D 1 60  THR 60  54  54  THR THR D . n 
D 1 61  ALA 61  55  55  ALA ALA D . n 
D 1 62  GLY 62  56  56  GLY GLY D . n 
D 1 63  CYS 63  57  57  CYS CYS D . n 
D 1 64  THR 64  58  58  THR THR D . n 
D 1 65  SER 65  59  59  SER SER D . n 
D 1 66  ALA 66  60  60  ALA ALA D . n 
D 1 67  GLY 67  61  61  GLY GLY D . n 
D 1 68  PRO 68  62  62  PRO PRO D . n 
D 1 69  HIS 69  63  63  HIS HIS D . n 
D 1 70  PHE 70  64  64  PHE PHE D . n 
D 1 71  ASN 71  65  65  ASN ASN D . n 
D 1 72  PRO 72  66  66  PRO PRO D . n 
D 1 73  LEU 73  67  67  LEU LEU D . n 
D 1 74  SER 74  68  68  SER SER D . n 
D 1 75  ARG 75  69  69  ARG ARG D . n 
D 1 76  LYS 76  70  70  LYS LYS D . n 
D 1 77  HIS 77  71  71  HIS HIS D . n 
D 1 78  GLY 78  72  72  GLY GLY D . n 
D 1 79  GLY 79  73  73  GLY GLY D . n 
D 1 80  PRO 80  74  74  PRO PRO D . n 
D 1 81  LYS 81  75  75  LYS LYS D . n 
D 1 82  ASP 82  76  76  ASP ASP D . n 
D 1 83  GLU 83  77  77  GLU GLU D . n 
D 1 84  GLU 84  78  78  GLU GLU D . n 
D 1 85  ARG 85  79  79  ARG ARG D . n 
D 1 86  HIS 86  80  80  HIS HIS D . n 
D 1 87  VAL 87  81  81  VAL VAL D . n 
D 1 88  GLY 88  82  82  GLY GLY D . n 
D 1 89  ASP 89  83  83  ASP ASP D . n 
D 1 90  LEU 90  84  84  LEU LEU D . n 
D 1 91  GLY 91  85  85  GLY GLY D . n 
D 1 92  ASN 92  86  86  ASN ASN D . n 
D 1 93  VAL 93  87  87  VAL VAL D . n 
D 1 94  THR 94  88  88  THR THR D . n 
D 1 95  ALA 95  89  89  ALA ALA D . n 
D 1 96  ASP 96  90  90  ASP ASP D . n 
D 1 97  LYS 97  91  91  LYS LYS D . n 
D 1 98  ASP 98  92  92  ASP ASP D . n 
D 1 99  ALA 99  93  93  ALA ALA D . n 
D 1 100 VAL 100 94  94  VAL VAL D . n 
D 1 101 ALA 101 95  95  ALA ALA D . n 
D 1 102 ASP 102 96  96  ASP ASP D . n 
D 1 103 VAL 103 97  97  VAL VAL D . n 
D 1 104 SER 104 98  98  SER SER D . n 
D 1 105 ILE 105 99  99  ILE ILE D . n 
D 1 106 GLU 106 100 100 GLU GLU D . n 
D 1 107 ASP 107 101 101 ASP ASP D . n 
D 1 108 SER 108 102 102 SER SER D . n 
D 1 109 VAL 109 103 103 VAL VAL D . n 
D 1 110 ILE 110 104 104 ILE ILE D . n 
D 1 111 SER 111 105 105 SER SER D . n 
D 1 112 LEU 112 106 106 LEU LEU D . n 
D 1 113 SER 113 107 107 SER SER D . n 
D 1 114 GLY 114 108 108 GLY GLY D . n 
D 1 115 ASP 115 109 109 ASP ASP D . n 
D 1 116 HIS 116 110 110 HIS HIS D . n 
D 1 117 CYS 117 111 111 CYS CYS D . n 
D 1 118 ILE 118 112 112 ILE ILE D . n 
D 1 119 ILE 119 113 113 ILE ILE D . n 
D 1 120 GLY 120 114 114 GLY GLY D . n 
D 1 121 ARG 121 115 115 ARG ARG D . n 
D 1 122 THR 122 116 116 THR THR D . n 
D 1 123 LEU 123 117 117 LEU LEU D . n 
D 1 124 VAL 124 118 118 VAL VAL D . n 
D 1 125 VAL 125 119 119 VAL VAL D . n 
D 1 126 HIS 126 120 120 HIS HIS D . n 
D 1 127 GLU 127 121 121 GLU GLU D . n 
D 1 128 LYS 128 122 122 LYS LYS D . n 
D 1 129 ALA 129 123 123 ALA ALA D . n 
D 1 130 ASP 130 124 124 ASP ASP D . n 
D 1 131 ASP 131 125 125 ASP ASP D . n 
D 1 132 LEU 132 126 126 LEU LEU D . n 
D 1 133 GLY 133 127 127 GLY GLY D . n 
D 1 134 LYS 134 128 128 LYS LYS D . n 
D 1 135 GLY 135 129 129 GLY GLY D . n 
D 1 136 GLY 136 130 130 GLY GLY D . n 
D 1 137 ASN 137 131 131 ASN ASN D . n 
D 1 138 GLU 138 132 132 GLU GLU D . n 
D 1 139 GLU 139 133 133 GLU GLU D . n 
D 1 140 SER 140 134 134 SER SER D . n 
D 1 141 THR 141 135 135 THR THR D . n 
D 1 142 LYS 142 136 136 LYS LYS D . n 
D 1 143 THR 143 137 137 THR THR D . n 
D 1 144 GLY 144 138 138 GLY GLY D . n 
D 1 145 ASN 145 139 139 ASN ASN D . n 
D 1 146 ALA 146 140 140 ALA ALA D . n 
D 1 147 GLY 147 141 141 GLY GLY D . n 
D 1 148 SER 148 142 142 SER SER D . n 
D 1 149 ARG 149 143 143 ARG ARG D . n 
D 1 150 LEU 150 144 144 LEU LEU D . n 
D 1 151 ALA 151 145 145 ALA ALA D . n 
D 1 152 CYS 152 146 146 CYS CYS D . n 
D 1 153 GLY 153 147 147 GLY GLY D . n 
D 1 154 VAL 154 148 148 VAL VAL D . n 
D 1 155 ILE 155 149 149 ILE ILE D . n 
D 1 156 GLY 156 150 150 GLY GLY D . n 
D 1 157 ILE 157 151 151 ILE ILE D . n 
D 1 158 ALA 158 152 152 ALA ALA D . n 
D 1 159 GLN 159 153 153 GLN GLN D . n 
E 1 1   GLY 1   -5  ?   ?   ?   E . n 
E 1 2   PRO 2   -4  ?   ?   ?   E . n 
E 1 3   LEU 3   -3  ?   ?   ?   E . n 
E 1 4   GLY 4   -2  ?   ?   ?   E . n 
E 1 5   SER 5   -1  ?   ?   ?   E . n 
E 1 6   MET 6   0   ?   ?   ?   E . n 
E 1 7   ALA 7   1   1   ALA ALA E . n 
E 1 8   THR 8   2   2   THR THR E . n 
E 1 9   LYS 9   3   3   LYS LYS E . n 
E 1 10  ALA 10  4   4   ALA ALA E . n 
E 1 11  VAL 11  5   5   VAL VAL E . n 
E 1 12  CYS 12  6   6   CYS CYS E . n 
E 1 13  VAL 13  7   7   VAL VAL E . n 
E 1 14  LEU 14  8   8   LEU LEU E . n 
E 1 15  LYS 15  9   9   LYS LYS E . n 
E 1 16  GLY 16  10  10  GLY GLY E . n 
E 1 17  ASP 17  11  11  ASP ASP E . n 
E 1 18  GLY 18  12  12  GLY GLY E . n 
E 1 19  PRO 19  13  13  PRO PRO E . n 
E 1 20  VAL 20  14  14  VAL VAL E . n 
E 1 21  GLN 21  15  15  GLN GLN E . n 
E 1 22  GLY 22  16  16  GLY GLY E . n 
E 1 23  ILE 23  17  17  ILE ILE E . n 
E 1 24  ILE 24  18  18  ILE ILE E . n 
E 1 25  ASN 25  19  19  ASN ASN E . n 
E 1 26  PHE 26  20  20  PHE PHE E . n 
E 1 27  GLU 27  21  21  GLU GLU E . n 
E 1 28  GLN 28  22  22  GLN GLN E . n 
E 1 29  LYS 29  23  23  LYS LYS E . n 
E 1 30  GLU 30  24  24  GLU GLU E . n 
E 1 31  SER 31  25  25  SER SER E . n 
E 1 32  ASN 32  26  26  ASN ASN E . n 
E 1 33  GLY 33  27  27  GLY GLY E . n 
E 1 34  PRO 34  28  28  PRO PRO E . n 
E 1 35  VAL 35  29  29  VAL VAL E . n 
E 1 36  LYS 36  30  30  LYS LYS E . n 
E 1 37  VAL 37  31  31  VAL VAL E . n 
E 1 38  TRP 38  32  32  TRP TRP E . n 
E 1 39  GLY 39  33  33  GLY GLY E . n 
E 1 40  SER 40  34  34  SER SER E . n 
E 1 41  ILE 41  35  35  ILE ILE E . n 
E 1 42  LYS 42  36  36  LYS LYS E . n 
E 1 43  GLY 43  37  37  GLY GLY E . n 
E 1 44  LEU 44  38  38  LEU LEU E . n 
E 1 45  THR 45  39  39  THR THR E . n 
E 1 46  GLU 46  40  40  GLU GLU E . n 
E 1 47  GLY 47  41  41  GLY GLY E . n 
E 1 48  LEU 48  42  42  LEU LEU E . n 
E 1 49  HIS 49  43  43  HIS HIS E . n 
E 1 50  GLY 50  44  44  GLY GLY E . n 
E 1 51  PHE 51  45  45  PHE PHE E . n 
E 1 52  HIS 52  46  46  HIS HIS E . n 
E 1 53  VAL 53  47  47  VAL VAL E . n 
E 1 54  HIS 54  48  48  HIS HIS E . n 
E 1 55  GLU 55  49  49  GLU GLU E . n 
E 1 56  PHE 56  50  50  PHE PHE E . n 
E 1 57  GLY 57  51  51  GLY GLY E . n 
E 1 58  ASP 58  52  52  ASP ASP E . n 
E 1 59  ASN 59  53  53  ASN ASN E . n 
E 1 60  THR 60  54  54  THR THR E . n 
E 1 61  ALA 61  55  55  ALA ALA E . n 
E 1 62  GLY 62  56  56  GLY GLY E . n 
E 1 63  CYS 63  57  57  CYS CYS E . n 
E 1 64  THR 64  58  58  THR THR E . n 
E 1 65  SER 65  59  59  SER SER E . n 
E 1 66  ALA 66  60  60  ALA ALA E . n 
E 1 67  GLY 67  61  61  GLY GLY E . n 
E 1 68  PRO 68  62  62  PRO PRO E . n 
E 1 69  HIS 69  63  63  HIS HIS E . n 
E 1 70  PHE 70  64  64  PHE PHE E . n 
E 1 71  ASN 71  65  65  ASN ASN E . n 
E 1 72  PRO 72  66  66  PRO PRO E . n 
E 1 73  LEU 73  67  67  LEU LEU E . n 
E 1 74  SER 74  68  68  SER SER E . n 
E 1 75  ARG 75  69  69  ARG ARG E . n 
E 1 76  LYS 76  70  70  LYS LYS E . n 
E 1 77  HIS 77  71  71  HIS HIS E . n 
E 1 78  GLY 78  72  72  GLY GLY E . n 
E 1 79  GLY 79  73  73  GLY GLY E . n 
E 1 80  PRO 80  74  74  PRO PRO E . n 
E 1 81  LYS 81  75  75  LYS LYS E . n 
E 1 82  ASP 82  76  76  ASP ASP E . n 
E 1 83  GLU 83  77  77  GLU GLU E . n 
E 1 84  GLU 84  78  78  GLU GLU E . n 
E 1 85  ARG 85  79  79  ARG ARG E . n 
E 1 86  HIS 86  80  80  HIS HIS E . n 
E 1 87  VAL 87  81  81  VAL VAL E . n 
E 1 88  GLY 88  82  82  GLY GLY E . n 
E 1 89  ASP 89  83  83  ASP ASP E . n 
E 1 90  LEU 90  84  84  LEU LEU E . n 
E 1 91  GLY 91  85  85  GLY GLY E . n 
E 1 92  ASN 92  86  86  ASN ASN E . n 
E 1 93  VAL 93  87  87  VAL VAL E . n 
E 1 94  THR 94  88  88  THR THR E . n 
E 1 95  ALA 95  89  89  ALA ALA E . n 
E 1 96  ASP 96  90  90  ASP ASP E . n 
E 1 97  LYS 97  91  91  LYS LYS E . n 
E 1 98  ASP 98  92  92  ASP ASP E . n 
E 1 99  ALA 99  93  93  ALA ALA E . n 
E 1 100 VAL 100 94  94  VAL VAL E . n 
E 1 101 ALA 101 95  95  ALA ALA E . n 
E 1 102 ASP 102 96  96  ASP ASP E . n 
E 1 103 VAL 103 97  97  VAL VAL E . n 
E 1 104 SER 104 98  98  SER SER E . n 
E 1 105 ILE 105 99  99  ILE ILE E . n 
E 1 106 GLU 106 100 100 GLU GLU E . n 
E 1 107 ASP 107 101 101 ASP ASP E . n 
E 1 108 SER 108 102 102 SER SER E . n 
E 1 109 VAL 109 103 103 VAL VAL E . n 
E 1 110 ILE 110 104 104 ILE ILE E . n 
E 1 111 SER 111 105 105 SER SER E . n 
E 1 112 LEU 112 106 106 LEU LEU E . n 
E 1 113 SER 113 107 107 SER SER E . n 
E 1 114 GLY 114 108 108 GLY GLY E . n 
E 1 115 ASP 115 109 109 ASP ASP E . n 
E 1 116 HIS 116 110 110 HIS HIS E . n 
E 1 117 CYS 117 111 111 CYS CYS E . n 
E 1 118 ILE 118 112 112 ILE ILE E . n 
E 1 119 ILE 119 113 113 ILE ILE E . n 
E 1 120 GLY 120 114 114 GLY GLY E . n 
E 1 121 ARG 121 115 115 ARG ARG E . n 
E 1 122 THR 122 116 116 THR THR E . n 
E 1 123 LEU 123 117 117 LEU LEU E . n 
E 1 124 VAL 124 118 118 VAL VAL E . n 
E 1 125 VAL 125 119 119 VAL VAL E . n 
E 1 126 HIS 126 120 120 HIS HIS E . n 
E 1 127 GLU 127 121 121 GLU GLU E . n 
E 1 128 LYS 128 122 122 LYS LYS E . n 
E 1 129 ALA 129 123 123 ALA ALA E . n 
E 1 130 ASP 130 124 124 ASP ASP E . n 
E 1 131 ASP 131 125 125 ASP ASP E . n 
E 1 132 LEU 132 126 126 LEU LEU E . n 
E 1 133 GLY 133 127 127 GLY GLY E . n 
E 1 134 LYS 134 128 128 LYS LYS E . n 
E 1 135 GLY 135 129 129 GLY GLY E . n 
E 1 136 GLY 136 130 130 GLY GLY E . n 
E 1 137 ASN 137 131 131 ASN ASN E . n 
E 1 138 GLU 138 132 132 GLU GLU E . n 
E 1 139 GLU 139 133 133 GLU GLU E . n 
E 1 140 SER 140 134 134 SER SER E . n 
E 1 141 THR 141 135 135 THR THR E . n 
E 1 142 LYS 142 136 136 LYS LYS E . n 
E 1 143 THR 143 137 137 THR THR E . n 
E 1 144 GLY 144 138 138 GLY GLY E . n 
E 1 145 ASN 145 139 139 ASN ASN E . n 
E 1 146 ALA 146 140 140 ALA ALA E . n 
E 1 147 GLY 147 141 141 GLY GLY E . n 
E 1 148 SER 148 142 142 SER SER E . n 
E 1 149 ARG 149 143 143 ARG ARG E . n 
E 1 150 LEU 150 144 144 LEU LEU E . n 
E 1 151 ALA 151 145 145 ALA ALA E . n 
E 1 152 CYS 152 146 146 CYS CYS E . n 
E 1 153 GLY 153 147 147 GLY GLY E . n 
E 1 154 VAL 154 148 148 VAL VAL E . n 
E 1 155 ILE 155 149 149 ILE ILE E . n 
E 1 156 GLY 156 150 150 GLY GLY E . n 
E 1 157 ILE 157 151 151 ILE ILE E . n 
E 1 158 ALA 158 152 152 ALA ALA E . n 
E 1 159 GLN 159 153 153 GLN GLN E . n 
F 1 1   GLY 1   -5  ?   ?   ?   F . n 
F 1 2   PRO 2   -4  ?   ?   ?   F . n 
F 1 3   LEU 3   -3  ?   ?   ?   F . n 
F 1 4   GLY 4   -2  ?   ?   ?   F . n 
F 1 5   SER 5   -1  ?   ?   ?   F . n 
F 1 6   MET 6   0   ?   ?   ?   F . n 
F 1 7   ALA 7   1   1   ALA ALA F . n 
F 1 8   THR 8   2   2   THR THR F . n 
F 1 9   LYS 9   3   3   LYS LYS F . n 
F 1 10  ALA 10  4   4   ALA ALA F . n 
F 1 11  VAL 11  5   5   VAL VAL F . n 
F 1 12  CYS 12  6   6   CYS CYS F . n 
F 1 13  VAL 13  7   7   VAL VAL F . n 
F 1 14  LEU 14  8   8   LEU LEU F . n 
F 1 15  LYS 15  9   9   LYS LYS F . n 
F 1 16  GLY 16  10  10  GLY GLY F . n 
F 1 17  ASP 17  11  11  ASP ASP F . n 
F 1 18  GLY 18  12  12  GLY GLY F . n 
F 1 19  PRO 19  13  13  PRO PRO F . n 
F 1 20  VAL 20  14  14  VAL VAL F . n 
F 1 21  GLN 21  15  15  GLN GLN F . n 
F 1 22  GLY 22  16  16  GLY GLY F . n 
F 1 23  ILE 23  17  17  ILE ILE F . n 
F 1 24  ILE 24  18  18  ILE ILE F . n 
F 1 25  ASN 25  19  19  ASN ASN F . n 
F 1 26  PHE 26  20  20  PHE PHE F . n 
F 1 27  GLU 27  21  21  GLU GLU F . n 
F 1 28  GLN 28  22  22  GLN GLN F . n 
F 1 29  LYS 29  23  23  LYS LYS F . n 
F 1 30  GLU 30  24  24  GLU GLU F . n 
F 1 31  SER 31  25  25  SER SER F . n 
F 1 32  ASN 32  26  26  ASN ASN F . n 
F 1 33  GLY 33  27  27  GLY GLY F . n 
F 1 34  PRO 34  28  28  PRO PRO F . n 
F 1 35  VAL 35  29  29  VAL VAL F . n 
F 1 36  LYS 36  30  30  LYS LYS F . n 
F 1 37  VAL 37  31  31  VAL VAL F . n 
F 1 38  TRP 38  32  32  TRP TRP F . n 
F 1 39  GLY 39  33  33  GLY GLY F . n 
F 1 40  SER 40  34  34  SER SER F . n 
F 1 41  ILE 41  35  35  ILE ILE F . n 
F 1 42  LYS 42  36  36  LYS LYS F . n 
F 1 43  GLY 43  37  37  GLY GLY F . n 
F 1 44  LEU 44  38  38  LEU LEU F . n 
F 1 45  THR 45  39  39  THR THR F . n 
F 1 46  GLU 46  40  40  GLU GLU F . n 
F 1 47  GLY 47  41  41  GLY GLY F . n 
F 1 48  LEU 48  42  42  LEU LEU F . n 
F 1 49  HIS 49  43  43  HIS HIS F . n 
F 1 50  GLY 50  44  44  GLY GLY F . n 
F 1 51  PHE 51  45  45  PHE PHE F . n 
F 1 52  HIS 52  46  46  HIS HIS F . n 
F 1 53  VAL 53  47  47  VAL VAL F . n 
F 1 54  HIS 54  48  48  HIS HIS F . n 
F 1 55  GLU 55  49  49  GLU GLU F . n 
F 1 56  PHE 56  50  50  PHE PHE F . n 
F 1 57  GLY 57  51  51  GLY GLY F . n 
F 1 58  ASP 58  52  52  ASP ASP F . n 
F 1 59  ASN 59  53  53  ASN ASN F . n 
F 1 60  THR 60  54  54  THR THR F . n 
F 1 61  ALA 61  55  55  ALA ALA F . n 
F 1 62  GLY 62  56  56  GLY GLY F . n 
F 1 63  CYS 63  57  57  CYS CYS F . n 
F 1 64  THR 64  58  58  THR THR F . n 
F 1 65  SER 65  59  59  SER SER F . n 
F 1 66  ALA 66  60  60  ALA ALA F . n 
F 1 67  GLY 67  61  61  GLY GLY F . n 
F 1 68  PRO 68  62  62  PRO PRO F . n 
F 1 69  HIS 69  63  63  HIS HIS F . n 
F 1 70  PHE 70  64  64  PHE PHE F . n 
F 1 71  ASN 71  65  65  ASN ASN F . n 
F 1 72  PRO 72  66  66  PRO PRO F . n 
F 1 73  LEU 73  67  67  LEU LEU F . n 
F 1 74  SER 74  68  68  SER SER F . n 
F 1 75  ARG 75  69  69  ARG ARG F . n 
F 1 76  LYS 76  70  70  LYS LYS F . n 
F 1 77  HIS 77  71  71  HIS HIS F . n 
F 1 78  GLY 78  72  72  GLY GLY F . n 
F 1 79  GLY 79  73  73  GLY GLY F . n 
F 1 80  PRO 80  74  74  PRO PRO F . n 
F 1 81  LYS 81  75  75  LYS LYS F . n 
F 1 82  ASP 82  76  76  ASP ASP F . n 
F 1 83  GLU 83  77  77  GLU GLU F . n 
F 1 84  GLU 84  78  78  GLU GLU F . n 
F 1 85  ARG 85  79  79  ARG ARG F . n 
F 1 86  HIS 86  80  80  HIS HIS F . n 
F 1 87  VAL 87  81  81  VAL VAL F . n 
F 1 88  GLY 88  82  82  GLY GLY F . n 
F 1 89  ASP 89  83  83  ASP ASP F . n 
F 1 90  LEU 90  84  84  LEU LEU F . n 
F 1 91  GLY 91  85  85  GLY GLY F . n 
F 1 92  ASN 92  86  86  ASN ASN F . n 
F 1 93  VAL 93  87  87  VAL VAL F . n 
F 1 94  THR 94  88  88  THR THR F . n 
F 1 95  ALA 95  89  89  ALA ALA F . n 
F 1 96  ASP 96  90  90  ASP ASP F . n 
F 1 97  LYS 97  91  91  LYS LYS F . n 
F 1 98  ASP 98  92  92  ASP ASP F . n 
F 1 99  ALA 99  93  93  ALA ALA F . n 
F 1 100 VAL 100 94  94  VAL VAL F . n 
F 1 101 ALA 101 95  95  ALA ALA F . n 
F 1 102 ASP 102 96  96  ASP ASP F . n 
F 1 103 VAL 103 97  97  VAL VAL F . n 
F 1 104 SER 104 98  98  SER SER F . n 
F 1 105 ILE 105 99  99  ILE ILE F . n 
F 1 106 GLU 106 100 100 GLU GLU F . n 
F 1 107 ASP 107 101 101 ASP ASP F . n 
F 1 108 SER 108 102 102 SER SER F . n 
F 1 109 VAL 109 103 103 VAL VAL F . n 
F 1 110 ILE 110 104 104 ILE ILE F . n 
F 1 111 SER 111 105 105 SER SER F . n 
F 1 112 LEU 112 106 106 LEU LEU F . n 
F 1 113 SER 113 107 107 SER SER F . n 
F 1 114 GLY 114 108 108 GLY GLY F . n 
F 1 115 ASP 115 109 109 ASP ASP F . n 
F 1 116 HIS 116 110 110 HIS HIS F . n 
F 1 117 CYS 117 111 111 CYS CYS F . n 
F 1 118 ILE 118 112 112 ILE ILE F . n 
F 1 119 ILE 119 113 113 ILE ILE F . n 
F 1 120 GLY 120 114 114 GLY GLY F . n 
F 1 121 ARG 121 115 115 ARG ARG F . n 
F 1 122 THR 122 116 116 THR THR F . n 
F 1 123 LEU 123 117 117 LEU LEU F . n 
F 1 124 VAL 124 118 118 VAL VAL F . n 
F 1 125 VAL 125 119 119 VAL VAL F . n 
F 1 126 HIS 126 120 120 HIS HIS F . n 
F 1 127 GLU 127 121 121 GLU GLU F . n 
F 1 128 LYS 128 122 122 LYS LYS F . n 
F 1 129 ALA 129 123 123 ALA ALA F . n 
F 1 130 ASP 130 124 124 ASP ASP F . n 
F 1 131 ASP 131 125 125 ASP ASP F . n 
F 1 132 LEU 132 126 126 LEU LEU F . n 
F 1 133 GLY 133 127 127 GLY GLY F . n 
F 1 134 LYS 134 128 128 LYS LYS F . n 
F 1 135 GLY 135 129 129 GLY GLY F . n 
F 1 136 GLY 136 130 130 GLY GLY F . n 
F 1 137 ASN 137 131 131 ASN ASN F . n 
F 1 138 GLU 138 132 132 GLU GLU F . n 
F 1 139 GLU 139 133 133 GLU GLU F . n 
F 1 140 SER 140 134 134 SER SER F . n 
F 1 141 THR 141 135 135 THR THR F . n 
F 1 142 LYS 142 136 136 LYS LYS F . n 
F 1 143 THR 143 137 137 THR THR F . n 
F 1 144 GLY 144 138 138 GLY GLY F . n 
F 1 145 ASN 145 139 139 ASN ASN F . n 
F 1 146 ALA 146 140 140 ALA ALA F . n 
F 1 147 GLY 147 141 141 GLY GLY F . n 
F 1 148 SER 148 142 142 SER SER F . n 
F 1 149 ARG 149 143 143 ARG ARG F . n 
F 1 150 LEU 150 144 144 LEU LEU F . n 
F 1 151 ALA 151 145 145 ALA ALA F . n 
F 1 152 CYS 152 146 146 CYS CYS F . n 
F 1 153 GLY 153 147 147 GLY GLY F . n 
F 1 154 VAL 154 148 148 VAL VAL F . n 
F 1 155 ILE 155 149 149 ILE ILE F . n 
F 1 156 GLY 156 150 150 GLY GLY F . n 
F 1 157 ILE 157 151 151 ILE ILE F . n 
F 1 158 ALA 158 152 152 ALA ALA F . n 
F 1 159 GLN 159 153 153 GLN GLN F . n 
G 1 1   GLY 1   -5  ?   ?   ?   G . n 
G 1 2   PRO 2   -4  ?   ?   ?   G . n 
G 1 3   LEU 3   -3  ?   ?   ?   G . n 
G 1 4   GLY 4   -2  ?   ?   ?   G . n 
G 1 5   SER 5   -1  ?   ?   ?   G . n 
G 1 6   MET 6   0   ?   ?   ?   G . n 
G 1 7   ALA 7   1   1   ALA ALA G . n 
G 1 8   THR 8   2   2   THR THR G . n 
G 1 9   LYS 9   3   3   LYS LYS G . n 
G 1 10  ALA 10  4   4   ALA ALA G . n 
G 1 11  VAL 11  5   5   VAL VAL G . n 
G 1 12  CYS 12  6   6   CYS CYS G . n 
G 1 13  VAL 13  7   7   VAL VAL G . n 
G 1 14  LEU 14  8   8   LEU LEU G . n 
G 1 15  LYS 15  9   9   LYS LYS G . n 
G 1 16  GLY 16  10  10  GLY GLY G . n 
G 1 17  ASP 17  11  11  ASP ASP G . n 
G 1 18  GLY 18  12  12  GLY GLY G . n 
G 1 19  PRO 19  13  13  PRO PRO G . n 
G 1 20  VAL 20  14  14  VAL VAL G . n 
G 1 21  GLN 21  15  15  GLN GLN G . n 
G 1 22  GLY 22  16  16  GLY GLY G . n 
G 1 23  ILE 23  17  17  ILE ILE G . n 
G 1 24  ILE 24  18  18  ILE ILE G . n 
G 1 25  ASN 25  19  19  ASN ASN G . n 
G 1 26  PHE 26  20  20  PHE PHE G . n 
G 1 27  GLU 27  21  21  GLU GLU G . n 
G 1 28  GLN 28  22  22  GLN GLN G . n 
G 1 29  LYS 29  23  23  LYS LYS G . n 
G 1 30  GLU 30  24  24  GLU GLU G . n 
G 1 31  SER 31  25  25  SER SER G . n 
G 1 32  ASN 32  26  26  ASN ASN G . n 
G 1 33  GLY 33  27  27  GLY GLY G . n 
G 1 34  PRO 34  28  28  PRO PRO G . n 
G 1 35  VAL 35  29  29  VAL VAL G . n 
G 1 36  LYS 36  30  30  LYS LYS G . n 
G 1 37  VAL 37  31  31  VAL VAL G . n 
G 1 38  TRP 38  32  32  TRP TRP G . n 
G 1 39  GLY 39  33  33  GLY GLY G . n 
G 1 40  SER 40  34  34  SER SER G . n 
G 1 41  ILE 41  35  35  ILE ILE G . n 
G 1 42  LYS 42  36  36  LYS LYS G . n 
G 1 43  GLY 43  37  37  GLY GLY G . n 
G 1 44  LEU 44  38  38  LEU LEU G . n 
G 1 45  THR 45  39  39  THR THR G . n 
G 1 46  GLU 46  40  40  GLU GLU G . n 
G 1 47  GLY 47  41  41  GLY GLY G . n 
G 1 48  LEU 48  42  42  LEU LEU G . n 
G 1 49  HIS 49  43  43  HIS HIS G . n 
G 1 50  GLY 50  44  44  GLY GLY G . n 
G 1 51  PHE 51  45  45  PHE PHE G . n 
G 1 52  HIS 52  46  46  HIS HIS G . n 
G 1 53  VAL 53  47  47  VAL VAL G . n 
G 1 54  HIS 54  48  48  HIS HIS G . n 
G 1 55  GLU 55  49  49  GLU GLU G . n 
G 1 56  PHE 56  50  50  PHE PHE G . n 
G 1 57  GLY 57  51  51  GLY GLY G . n 
G 1 58  ASP 58  52  52  ASP ASP G . n 
G 1 59  ASN 59  53  53  ASN ASN G . n 
G 1 60  THR 60  54  54  THR THR G . n 
G 1 61  ALA 61  55  55  ALA ALA G . n 
G 1 62  GLY 62  56  56  GLY GLY G . n 
G 1 63  CYS 63  57  57  CYS CYS G . n 
G 1 64  THR 64  58  58  THR THR G . n 
G 1 65  SER 65  59  59  SER SER G . n 
G 1 66  ALA 66  60  60  ALA ALA G . n 
G 1 67  GLY 67  61  61  GLY GLY G . n 
G 1 68  PRO 68  62  62  PRO PRO G . n 
G 1 69  HIS 69  63  63  HIS HIS G . n 
G 1 70  PHE 70  64  64  PHE PHE G . n 
G 1 71  ASN 71  65  65  ASN ASN G . n 
G 1 72  PRO 72  66  66  PRO PRO G . n 
G 1 73  LEU 73  67  67  LEU LEU G . n 
G 1 74  SER 74  68  68  SER SER G . n 
G 1 75  ARG 75  69  69  ARG ARG G . n 
G 1 76  LYS 76  70  70  LYS LYS G . n 
G 1 77  HIS 77  71  71  HIS HIS G . n 
G 1 78  GLY 78  72  72  GLY GLY G . n 
G 1 79  GLY 79  73  73  GLY GLY G . n 
G 1 80  PRO 80  74  74  PRO PRO G . n 
G 1 81  LYS 81  75  75  LYS LYS G . n 
G 1 82  ASP 82  76  76  ASP ASP G . n 
G 1 83  GLU 83  77  77  GLU GLU G . n 
G 1 84  GLU 84  78  78  GLU GLU G . n 
G 1 85  ARG 85  79  79  ARG ARG G . n 
G 1 86  HIS 86  80  80  HIS HIS G . n 
G 1 87  VAL 87  81  81  VAL VAL G . n 
G 1 88  GLY 88  82  82  GLY GLY G . n 
G 1 89  ASP 89  83  83  ASP ASP G . n 
G 1 90  LEU 90  84  84  LEU LEU G . n 
G 1 91  GLY 91  85  85  GLY GLY G . n 
G 1 92  ASN 92  86  86  ASN ASN G . n 
G 1 93  VAL 93  87  87  VAL VAL G . n 
G 1 94  THR 94  88  88  THR THR G . n 
G 1 95  ALA 95  89  89  ALA ALA G . n 
G 1 96  ASP 96  90  90  ASP ASP G . n 
G 1 97  LYS 97  91  91  LYS LYS G . n 
G 1 98  ASP 98  92  92  ASP ASP G . n 
G 1 99  ALA 99  93  93  ALA ALA G . n 
G 1 100 VAL 100 94  94  VAL VAL G . n 
G 1 101 ALA 101 95  95  ALA ALA G . n 
G 1 102 ASP 102 96  96  ASP ASP G . n 
G 1 103 VAL 103 97  97  VAL VAL G . n 
G 1 104 SER 104 98  98  SER SER G . n 
G 1 105 ILE 105 99  99  ILE ILE G . n 
G 1 106 GLU 106 100 100 GLU GLU G . n 
G 1 107 ASP 107 101 101 ASP ASP G . n 
G 1 108 SER 108 102 102 SER SER G . n 
G 1 109 VAL 109 103 103 VAL VAL G . n 
G 1 110 ILE 110 104 104 ILE ILE G . n 
G 1 111 SER 111 105 105 SER SER G . n 
G 1 112 LEU 112 106 106 LEU LEU G . n 
G 1 113 SER 113 107 107 SER SER G . n 
G 1 114 GLY 114 108 108 GLY GLY G . n 
G 1 115 ASP 115 109 109 ASP ASP G . n 
G 1 116 HIS 116 110 110 HIS HIS G . n 
G 1 117 CYS 117 111 111 CYS CYS G . n 
G 1 118 ILE 118 112 112 ILE ILE G . n 
G 1 119 ILE 119 113 113 ILE ILE G . n 
G 1 120 GLY 120 114 114 GLY GLY G . n 
G 1 121 ARG 121 115 115 ARG ARG G . n 
G 1 122 THR 122 116 116 THR THR G . n 
G 1 123 LEU 123 117 117 LEU LEU G . n 
G 1 124 VAL 124 118 118 VAL VAL G . n 
G 1 125 VAL 125 119 119 VAL VAL G . n 
G 1 126 HIS 126 120 120 HIS HIS G . n 
G 1 127 GLU 127 121 121 GLU GLU G . n 
G 1 128 LYS 128 122 122 LYS LYS G . n 
G 1 129 ALA 129 123 123 ALA ALA G . n 
G 1 130 ASP 130 124 124 ASP ASP G . n 
G 1 131 ASP 131 125 125 ASP ASP G . n 
G 1 132 LEU 132 126 126 LEU LEU G . n 
G 1 133 GLY 133 127 127 GLY GLY G . n 
G 1 134 LYS 134 128 128 LYS LYS G . n 
G 1 135 GLY 135 129 129 GLY GLY G . n 
G 1 136 GLY 136 130 130 GLY GLY G . n 
G 1 137 ASN 137 131 131 ASN ASN G . n 
G 1 138 GLU 138 132 132 GLU GLU G . n 
G 1 139 GLU 139 133 133 GLU GLU G . n 
G 1 140 SER 140 134 134 SER SER G . n 
G 1 141 THR 141 135 135 THR THR G . n 
G 1 142 LYS 142 136 136 LYS LYS G . n 
G 1 143 THR 143 137 137 THR THR G . n 
G 1 144 GLY 144 138 138 GLY GLY G . n 
G 1 145 ASN 145 139 139 ASN ASN G . n 
G 1 146 ALA 146 140 140 ALA ALA G . n 
G 1 147 GLY 147 141 141 GLY GLY G . n 
G 1 148 SER 148 142 142 SER SER G . n 
G 1 149 ARG 149 143 143 ARG ARG G . n 
G 1 150 LEU 150 144 144 LEU LEU G . n 
G 1 151 ALA 151 145 145 ALA ALA G . n 
G 1 152 CYS 152 146 146 CYS CYS G . n 
G 1 153 GLY 153 147 147 GLY GLY G . n 
G 1 154 VAL 154 148 148 VAL VAL G . n 
G 1 155 ILE 155 149 149 ILE ILE G . n 
G 1 156 GLY 156 150 150 GLY GLY G . n 
G 1 157 ILE 157 151 151 ILE ILE G . n 
G 1 158 ALA 158 152 152 ALA ALA G . n 
G 1 159 GLN 159 153 153 GLN GLN G . n 
H 1 1   GLY 1   -5  ?   ?   ?   H . n 
H 1 2   PRO 2   -4  ?   ?   ?   H . n 
H 1 3   LEU 3   -3  ?   ?   ?   H . n 
H 1 4   GLY 4   -2  ?   ?   ?   H . n 
H 1 5   SER 5   -1  ?   ?   ?   H . n 
H 1 6   MET 6   0   ?   ?   ?   H . n 
H 1 7   ALA 7   1   1   ALA ALA H . n 
H 1 8   THR 8   2   2   THR THR H . n 
H 1 9   LYS 9   3   3   LYS LYS H . n 
H 1 10  ALA 10  4   4   ALA ALA H . n 
H 1 11  VAL 11  5   5   VAL VAL H . n 
H 1 12  CYS 12  6   6   CYS CYS H . n 
H 1 13  VAL 13  7   7   VAL VAL H . n 
H 1 14  LEU 14  8   8   LEU LEU H . n 
H 1 15  LYS 15  9   9   LYS LYS H . n 
H 1 16  GLY 16  10  10  GLY GLY H . n 
H 1 17  ASP 17  11  11  ASP ASP H . n 
H 1 18  GLY 18  12  12  GLY GLY H . n 
H 1 19  PRO 19  13  13  PRO PRO H . n 
H 1 20  VAL 20  14  14  VAL VAL H . n 
H 1 21  GLN 21  15  15  GLN GLN H . n 
H 1 22  GLY 22  16  16  GLY GLY H . n 
H 1 23  ILE 23  17  17  ILE ILE H . n 
H 1 24  ILE 24  18  18  ILE ILE H . n 
H 1 25  ASN 25  19  19  ASN ASN H . n 
H 1 26  PHE 26  20  20  PHE PHE H . n 
H 1 27  GLU 27  21  21  GLU GLU H . n 
H 1 28  GLN 28  22  22  GLN GLN H . n 
H 1 29  LYS 29  23  23  LYS LYS H . n 
H 1 30  GLU 30  24  24  GLU GLU H . n 
H 1 31  SER 31  25  25  SER SER H . n 
H 1 32  ASN 32  26  26  ASN ASN H . n 
H 1 33  GLY 33  27  27  GLY GLY H . n 
H 1 34  PRO 34  28  28  PRO PRO H . n 
H 1 35  VAL 35  29  29  VAL VAL H . n 
H 1 36  LYS 36  30  30  LYS LYS H . n 
H 1 37  VAL 37  31  31  VAL VAL H . n 
H 1 38  TRP 38  32  32  TRP TRP H . n 
H 1 39  GLY 39  33  33  GLY GLY H . n 
H 1 40  SER 40  34  34  SER SER H . n 
H 1 41  ILE 41  35  35  ILE ILE H . n 
H 1 42  LYS 42  36  36  LYS LYS H . n 
H 1 43  GLY 43  37  37  GLY GLY H . n 
H 1 44  LEU 44  38  38  LEU LEU H . n 
H 1 45  THR 45  39  39  THR THR H . n 
H 1 46  GLU 46  40  40  GLU GLU H . n 
H 1 47  GLY 47  41  41  GLY GLY H . n 
H 1 48  LEU 48  42  42  LEU LEU H . n 
H 1 49  HIS 49  43  43  HIS HIS H . n 
H 1 50  GLY 50  44  44  GLY GLY H . n 
H 1 51  PHE 51  45  45  PHE PHE H . n 
H 1 52  HIS 52  46  46  HIS HIS H . n 
H 1 53  VAL 53  47  47  VAL VAL H . n 
H 1 54  HIS 54  48  48  HIS HIS H . n 
H 1 55  GLU 55  49  49  GLU GLU H . n 
H 1 56  PHE 56  50  50  PHE PHE H . n 
H 1 57  GLY 57  51  51  GLY GLY H . n 
H 1 58  ASP 58  52  52  ASP ASP H . n 
H 1 59  ASN 59  53  53  ASN ASN H . n 
H 1 60  THR 60  54  54  THR THR H . n 
H 1 61  ALA 61  55  55  ALA ALA H . n 
H 1 62  GLY 62  56  56  GLY GLY H . n 
H 1 63  CYS 63  57  57  CYS CYS H . n 
H 1 64  THR 64  58  58  THR THR H . n 
H 1 65  SER 65  59  59  SER SER H . n 
H 1 66  ALA 66  60  60  ALA ALA H . n 
H 1 67  GLY 67  61  61  GLY GLY H . n 
H 1 68  PRO 68  62  62  PRO PRO H . n 
H 1 69  HIS 69  63  63  HIS HIS H . n 
H 1 70  PHE 70  64  64  PHE PHE H . n 
H 1 71  ASN 71  65  65  ASN ASN H . n 
H 1 72  PRO 72  66  66  PRO PRO H . n 
H 1 73  LEU 73  67  67  LEU LEU H . n 
H 1 74  SER 74  68  68  SER SER H . n 
H 1 75  ARG 75  69  69  ARG ARG H . n 
H 1 76  LYS 76  70  70  LYS LYS H . n 
H 1 77  HIS 77  71  71  HIS HIS H . n 
H 1 78  GLY 78  72  72  GLY GLY H . n 
H 1 79  GLY 79  73  73  GLY GLY H . n 
H 1 80  PRO 80  74  74  PRO PRO H . n 
H 1 81  LYS 81  75  75  LYS LYS H . n 
H 1 82  ASP 82  76  76  ASP ASP H . n 
H 1 83  GLU 83  77  77  GLU GLU H . n 
H 1 84  GLU 84  78  78  GLU GLU H . n 
H 1 85  ARG 85  79  79  ARG ARG H . n 
H 1 86  HIS 86  80  80  HIS HIS H . n 
H 1 87  VAL 87  81  81  VAL VAL H . n 
H 1 88  GLY 88  82  82  GLY GLY H . n 
H 1 89  ASP 89  83  83  ASP ASP H . n 
H 1 90  LEU 90  84  84  LEU LEU H . n 
H 1 91  GLY 91  85  85  GLY GLY H . n 
H 1 92  ASN 92  86  86  ASN ASN H . n 
H 1 93  VAL 93  87  87  VAL VAL H . n 
H 1 94  THR 94  88  88  THR THR H . n 
H 1 95  ALA 95  89  89  ALA ALA H . n 
H 1 96  ASP 96  90  90  ASP ASP H . n 
H 1 97  LYS 97  91  91  LYS LYS H . n 
H 1 98  ASP 98  92  92  ASP ASP H . n 
H 1 99  ALA 99  93  93  ALA ALA H . n 
H 1 100 VAL 100 94  94  VAL VAL H . n 
H 1 101 ALA 101 95  95  ALA ALA H . n 
H 1 102 ASP 102 96  96  ASP ASP H . n 
H 1 103 VAL 103 97  97  VAL VAL H . n 
H 1 104 SER 104 98  98  SER SER H . n 
H 1 105 ILE 105 99  99  ILE ILE H . n 
H 1 106 GLU 106 100 100 GLU GLU H . n 
H 1 107 ASP 107 101 101 ASP ASP H . n 
H 1 108 SER 108 102 102 SER SER H . n 
H 1 109 VAL 109 103 103 VAL VAL H . n 
H 1 110 ILE 110 104 104 ILE ILE H . n 
H 1 111 SER 111 105 105 SER SER H . n 
H 1 112 LEU 112 106 106 LEU LEU H . n 
H 1 113 SER 113 107 107 SER SER H . n 
H 1 114 GLY 114 108 108 GLY GLY H . n 
H 1 115 ASP 115 109 109 ASP ASP H . n 
H 1 116 HIS 116 110 110 HIS HIS H . n 
H 1 117 CYS 117 111 111 CYS CYS H . n 
H 1 118 ILE 118 112 112 ILE ILE H . n 
H 1 119 ILE 119 113 113 ILE ILE H . n 
H 1 120 GLY 120 114 114 GLY GLY H . n 
H 1 121 ARG 121 115 115 ARG ARG H . n 
H 1 122 THR 122 116 116 THR THR H . n 
H 1 123 LEU 123 117 117 LEU LEU H . n 
H 1 124 VAL 124 118 118 VAL VAL H . n 
H 1 125 VAL 125 119 119 VAL VAL H . n 
H 1 126 HIS 126 120 120 HIS HIS H . n 
H 1 127 GLU 127 121 121 GLU GLU H . n 
H 1 128 LYS 128 122 122 LYS LYS H . n 
H 1 129 ALA 129 123 123 ALA ALA H . n 
H 1 130 ASP 130 124 124 ASP ASP H . n 
H 1 131 ASP 131 125 125 ASP ASP H . n 
H 1 132 LEU 132 126 126 LEU LEU H . n 
H 1 133 GLY 133 127 127 GLY GLY H . n 
H 1 134 LYS 134 128 128 LYS LYS H . n 
H 1 135 GLY 135 129 129 GLY GLY H . n 
H 1 136 GLY 136 130 130 GLY GLY H . n 
H 1 137 ASN 137 131 131 ASN ASN H . n 
H 1 138 GLU 138 132 132 GLU GLU H . n 
H 1 139 GLU 139 133 133 GLU GLU H . n 
H 1 140 SER 140 134 134 SER SER H . n 
H 1 141 THR 141 135 135 THR THR H . n 
H 1 142 LYS 142 136 136 LYS LYS H . n 
H 1 143 THR 143 137 137 THR THR H . n 
H 1 144 GLY 144 138 138 GLY GLY H . n 
H 1 145 ASN 145 139 139 ASN ASN H . n 
H 1 146 ALA 146 140 140 ALA ALA H . n 
H 1 147 GLY 147 141 141 GLY GLY H . n 
H 1 148 SER 148 142 142 SER SER H . n 
H 1 149 ARG 149 143 143 ARG ARG H . n 
H 1 150 LEU 150 144 144 LEU LEU H . n 
H 1 151 ALA 151 145 145 ALA ALA H . n 
H 1 152 CYS 152 146 146 CYS CYS H . n 
H 1 153 GLY 153 147 147 GLY GLY H . n 
H 1 154 VAL 154 148 148 VAL VAL H . n 
H 1 155 ILE 155 149 149 ILE ILE H . n 
H 1 156 GLY 156 150 150 GLY GLY H . n 
H 1 157 ILE 157 151 151 ILE ILE H . n 
H 1 158 ALA 158 152 152 ALA ALA H . n 
H 1 159 GLN 159 153 153 GLN GLN H . n 
I 1 1   GLY 1   -5  ?   ?   ?   I . n 
I 1 2   PRO 2   -4  ?   ?   ?   I . n 
I 1 3   LEU 3   -3  ?   ?   ?   I . n 
I 1 4   GLY 4   -2  ?   ?   ?   I . n 
I 1 5   SER 5   -1  ?   ?   ?   I . n 
I 1 6   MET 6   0   ?   ?   ?   I . n 
I 1 7   ALA 7   1   1   ALA ALA I . n 
I 1 8   THR 8   2   2   THR THR I . n 
I 1 9   LYS 9   3   3   LYS LYS I . n 
I 1 10  ALA 10  4   4   ALA ALA I . n 
I 1 11  VAL 11  5   5   VAL VAL I . n 
I 1 12  CYS 12  6   6   CYS CYS I . n 
I 1 13  VAL 13  7   7   VAL VAL I . n 
I 1 14  LEU 14  8   8   LEU LEU I . n 
I 1 15  LYS 15  9   9   LYS LYS I . n 
I 1 16  GLY 16  10  10  GLY GLY I . n 
I 1 17  ASP 17  11  11  ASP ASP I . n 
I 1 18  GLY 18  12  12  GLY GLY I . n 
I 1 19  PRO 19  13  13  PRO PRO I . n 
I 1 20  VAL 20  14  14  VAL VAL I . n 
I 1 21  GLN 21  15  15  GLN GLN I . n 
I 1 22  GLY 22  16  16  GLY GLY I . n 
I 1 23  ILE 23  17  17  ILE ILE I . n 
I 1 24  ILE 24  18  18  ILE ILE I . n 
I 1 25  ASN 25  19  19  ASN ASN I . n 
I 1 26  PHE 26  20  20  PHE PHE I . n 
I 1 27  GLU 27  21  21  GLU GLU I . n 
I 1 28  GLN 28  22  22  GLN GLN I . n 
I 1 29  LYS 29  23  23  LYS LYS I . n 
I 1 30  GLU 30  24  24  GLU GLU I . n 
I 1 31  SER 31  25  25  SER SER I . n 
I 1 32  ASN 32  26  26  ASN ASN I . n 
I 1 33  GLY 33  27  27  GLY GLY I . n 
I 1 34  PRO 34  28  28  PRO PRO I . n 
I 1 35  VAL 35  29  29  VAL VAL I . n 
I 1 36  LYS 36  30  30  LYS LYS I . n 
I 1 37  VAL 37  31  31  VAL VAL I . n 
I 1 38  TRP 38  32  32  TRP TRP I . n 
I 1 39  GLY 39  33  33  GLY GLY I . n 
I 1 40  SER 40  34  34  SER SER I . n 
I 1 41  ILE 41  35  35  ILE ILE I . n 
I 1 42  LYS 42  36  36  LYS LYS I . n 
I 1 43  GLY 43  37  37  GLY GLY I . n 
I 1 44  LEU 44  38  38  LEU LEU I . n 
I 1 45  THR 45  39  39  THR THR I . n 
I 1 46  GLU 46  40  40  GLU GLU I . n 
I 1 47  GLY 47  41  41  GLY GLY I . n 
I 1 48  LEU 48  42  42  LEU LEU I . n 
I 1 49  HIS 49  43  43  HIS HIS I . n 
I 1 50  GLY 50  44  44  GLY GLY I . n 
I 1 51  PHE 51  45  45  PHE PHE I . n 
I 1 52  HIS 52  46  46  HIS HIS I . n 
I 1 53  VAL 53  47  47  VAL VAL I . n 
I 1 54  HIS 54  48  48  HIS HIS I . n 
I 1 55  GLU 55  49  49  GLU GLU I . n 
I 1 56  PHE 56  50  50  PHE PHE I . n 
I 1 57  GLY 57  51  51  GLY GLY I . n 
I 1 58  ASP 58  52  52  ASP ASP I . n 
I 1 59  ASN 59  53  53  ASN ASN I . n 
I 1 60  THR 60  54  54  THR THR I . n 
I 1 61  ALA 61  55  55  ALA ALA I . n 
I 1 62  GLY 62  56  56  GLY GLY I . n 
I 1 63  CYS 63  57  57  CYS CYS I . n 
I 1 64  THR 64  58  58  THR THR I . n 
I 1 65  SER 65  59  59  SER SER I . n 
I 1 66  ALA 66  60  60  ALA ALA I . n 
I 1 67  GLY 67  61  61  GLY GLY I . n 
I 1 68  PRO 68  62  62  PRO PRO I . n 
I 1 69  HIS 69  63  63  HIS HIS I . n 
I 1 70  PHE 70  64  64  PHE PHE I . n 
I 1 71  ASN 71  65  65  ASN ASN I . n 
I 1 72  PRO 72  66  66  PRO PRO I . n 
I 1 73  LEU 73  67  67  LEU LEU I . n 
I 1 74  SER 74  68  68  SER SER I . n 
I 1 75  ARG 75  69  69  ARG ARG I . n 
I 1 76  LYS 76  70  70  LYS LYS I . n 
I 1 77  HIS 77  71  71  HIS HIS I . n 
I 1 78  GLY 78  72  72  GLY GLY I . n 
I 1 79  GLY 79  73  73  GLY GLY I . n 
I 1 80  PRO 80  74  74  PRO PRO I . n 
I 1 81  LYS 81  75  75  LYS LYS I . n 
I 1 82  ASP 82  76  76  ASP ASP I . n 
I 1 83  GLU 83  77  77  GLU GLU I . n 
I 1 84  GLU 84  78  78  GLU GLU I . n 
I 1 85  ARG 85  79  79  ARG ARG I . n 
I 1 86  HIS 86  80  80  HIS HIS I . n 
I 1 87  VAL 87  81  81  VAL VAL I . n 
I 1 88  GLY 88  82  82  GLY GLY I . n 
I 1 89  ASP 89  83  83  ASP ASP I . n 
I 1 90  LEU 90  84  84  LEU LEU I . n 
I 1 91  GLY 91  85  85  GLY GLY I . n 
I 1 92  ASN 92  86  86  ASN ASN I . n 
I 1 93  VAL 93  87  87  VAL VAL I . n 
I 1 94  THR 94  88  88  THR THR I . n 
I 1 95  ALA 95  89  89  ALA ALA I . n 
I 1 96  ASP 96  90  90  ASP ASP I . n 
I 1 97  LYS 97  91  91  LYS LYS I . n 
I 1 98  ASP 98  92  92  ASP ASP I . n 
I 1 99  ALA 99  93  93  ALA ALA I . n 
I 1 100 VAL 100 94  94  VAL VAL I . n 
I 1 101 ALA 101 95  95  ALA ALA I . n 
I 1 102 ASP 102 96  96  ASP ASP I . n 
I 1 103 VAL 103 97  97  VAL VAL I . n 
I 1 104 SER 104 98  98  SER SER I . n 
I 1 105 ILE 105 99  99  ILE ILE I . n 
I 1 106 GLU 106 100 100 GLU GLU I . n 
I 1 107 ASP 107 101 101 ASP ASP I . n 
I 1 108 SER 108 102 102 SER SER I . n 
I 1 109 VAL 109 103 103 VAL VAL I . n 
I 1 110 ILE 110 104 104 ILE ILE I . n 
I 1 111 SER 111 105 105 SER SER I . n 
I 1 112 LEU 112 106 106 LEU LEU I . n 
I 1 113 SER 113 107 107 SER SER I . n 
I 1 114 GLY 114 108 108 GLY GLY I . n 
I 1 115 ASP 115 109 109 ASP ASP I . n 
I 1 116 HIS 116 110 110 HIS HIS I . n 
I 1 117 CYS 117 111 111 CYS CYS I . n 
I 1 118 ILE 118 112 112 ILE ILE I . n 
I 1 119 ILE 119 113 113 ILE ILE I . n 
I 1 120 GLY 120 114 114 GLY GLY I . n 
I 1 121 ARG 121 115 115 ARG ARG I . n 
I 1 122 THR 122 116 116 THR THR I . n 
I 1 123 LEU 123 117 117 LEU LEU I . n 
I 1 124 VAL 124 118 118 VAL VAL I . n 
I 1 125 VAL 125 119 119 VAL VAL I . n 
I 1 126 HIS 126 120 120 HIS HIS I . n 
I 1 127 GLU 127 121 121 GLU GLU I . n 
I 1 128 LYS 128 122 122 LYS LYS I . n 
I 1 129 ALA 129 123 123 ALA ALA I . n 
I 1 130 ASP 130 124 124 ASP ASP I . n 
I 1 131 ASP 131 125 125 ASP ASP I . n 
I 1 132 LEU 132 126 126 LEU LEU I . n 
I 1 133 GLY 133 127 127 GLY GLY I . n 
I 1 134 LYS 134 128 128 LYS LYS I . n 
I 1 135 GLY 135 129 129 GLY GLY I . n 
I 1 136 GLY 136 130 130 GLY GLY I . n 
I 1 137 ASN 137 131 131 ASN ASN I . n 
I 1 138 GLU 138 132 132 GLU GLU I . n 
I 1 139 GLU 139 133 133 GLU GLU I . n 
I 1 140 SER 140 134 134 SER SER I . n 
I 1 141 THR 141 135 135 THR THR I . n 
I 1 142 LYS 142 136 136 LYS LYS I . n 
I 1 143 THR 143 137 137 THR THR I . n 
I 1 144 GLY 144 138 138 GLY GLY I . n 
I 1 145 ASN 145 139 139 ASN ASN I . n 
I 1 146 ALA 146 140 140 ALA ALA I . n 
I 1 147 GLY 147 141 141 GLY GLY I . n 
I 1 148 SER 148 142 142 SER SER I . n 
I 1 149 ARG 149 143 143 ARG ARG I . n 
I 1 150 LEU 150 144 144 LEU LEU I . n 
I 1 151 ALA 151 145 145 ALA ALA I . n 
I 1 152 CYS 152 146 146 CYS CYS I . n 
I 1 153 GLY 153 147 147 GLY GLY I . n 
I 1 154 VAL 154 148 148 VAL VAL I . n 
I 1 155 ILE 155 149 149 ILE ILE I . n 
I 1 156 GLY 156 150 150 GLY GLY I . n 
I 1 157 ILE 157 151 151 ILE ILE I . n 
I 1 158 ALA 158 152 152 ALA ALA I . n 
I 1 159 GLN 159 153 153 GLN GLN I . n 
J 1 1   GLY 1   -5  ?   ?   ?   J . n 
J 1 2   PRO 2   -4  ?   ?   ?   J . n 
J 1 3   LEU 3   -3  ?   ?   ?   J . n 
J 1 4   GLY 4   -2  ?   ?   ?   J . n 
J 1 5   SER 5   -1  ?   ?   ?   J . n 
J 1 6   MET 6   0   ?   ?   ?   J . n 
J 1 7   ALA 7   1   1   ALA ALA J . n 
J 1 8   THR 8   2   2   THR THR J . n 
J 1 9   LYS 9   3   3   LYS LYS J . n 
J 1 10  ALA 10  4   4   ALA ALA J . n 
J 1 11  VAL 11  5   5   VAL VAL J . n 
J 1 12  CYS 12  6   6   CYS CYS J . n 
J 1 13  VAL 13  7   7   VAL VAL J . n 
J 1 14  LEU 14  8   8   LEU LEU J . n 
J 1 15  LYS 15  9   9   LYS LYS J . n 
J 1 16  GLY 16  10  10  GLY GLY J . n 
J 1 17  ASP 17  11  11  ASP ASP J . n 
J 1 18  GLY 18  12  12  GLY GLY J . n 
J 1 19  PRO 19  13  13  PRO PRO J . n 
J 1 20  VAL 20  14  14  VAL VAL J . n 
J 1 21  GLN 21  15  15  GLN GLN J . n 
J 1 22  GLY 22  16  16  GLY GLY J . n 
J 1 23  ILE 23  17  17  ILE ILE J . n 
J 1 24  ILE 24  18  18  ILE ILE J . n 
J 1 25  ASN 25  19  19  ASN ASN J . n 
J 1 26  PHE 26  20  20  PHE PHE J . n 
J 1 27  GLU 27  21  21  GLU GLU J . n 
J 1 28  GLN 28  22  22  GLN GLN J . n 
J 1 29  LYS 29  23  23  LYS LYS J . n 
J 1 30  GLU 30  24  24  GLU GLU J . n 
J 1 31  SER 31  25  25  SER SER J . n 
J 1 32  ASN 32  26  26  ASN ASN J . n 
J 1 33  GLY 33  27  27  GLY GLY J . n 
J 1 34  PRO 34  28  28  PRO PRO J . n 
J 1 35  VAL 35  29  29  VAL VAL J . n 
J 1 36  LYS 36  30  30  LYS LYS J . n 
J 1 37  VAL 37  31  31  VAL VAL J . n 
J 1 38  TRP 38  32  32  TRP TRP J . n 
J 1 39  GLY 39  33  33  GLY GLY J . n 
J 1 40  SER 40  34  34  SER SER J . n 
J 1 41  ILE 41  35  35  ILE ILE J . n 
J 1 42  LYS 42  36  36  LYS LYS J . n 
J 1 43  GLY 43  37  37  GLY GLY J . n 
J 1 44  LEU 44  38  38  LEU LEU J . n 
J 1 45  THR 45  39  39  THR THR J . n 
J 1 46  GLU 46  40  40  GLU GLU J . n 
J 1 47  GLY 47  41  41  GLY GLY J . n 
J 1 48  LEU 48  42  42  LEU LEU J . n 
J 1 49  HIS 49  43  43  HIS HIS J . n 
J 1 50  GLY 50  44  44  GLY GLY J . n 
J 1 51  PHE 51  45  45  PHE PHE J . n 
J 1 52  HIS 52  46  46  HIS HIS J . n 
J 1 53  VAL 53  47  47  VAL VAL J . n 
J 1 54  HIS 54  48  48  HIS HIS J . n 
J 1 55  GLU 55  49  49  GLU GLU J . n 
J 1 56  PHE 56  50  50  PHE PHE J . n 
J 1 57  GLY 57  51  51  GLY GLY J . n 
J 1 58  ASP 58  52  52  ASP ASP J . n 
J 1 59  ASN 59  53  53  ASN ASN J . n 
J 1 60  THR 60  54  54  THR THR J . n 
J 1 61  ALA 61  55  55  ALA ALA J . n 
J 1 62  GLY 62  56  56  GLY GLY J . n 
J 1 63  CYS 63  57  57  CYS CYS J . n 
J 1 64  THR 64  58  58  THR THR J . n 
J 1 65  SER 65  59  59  SER SER J . n 
J 1 66  ALA 66  60  60  ALA ALA J . n 
J 1 67  GLY 67  61  61  GLY GLY J . n 
J 1 68  PRO 68  62  62  PRO PRO J . n 
J 1 69  HIS 69  63  63  HIS HIS J . n 
J 1 70  PHE 70  64  64  PHE PHE J . n 
J 1 71  ASN 71  65  65  ASN ASN J . n 
J 1 72  PRO 72  66  66  PRO PRO J . n 
J 1 73  LEU 73  67  67  LEU LEU J . n 
J 1 74  SER 74  68  68  SER SER J . n 
J 1 75  ARG 75  69  69  ARG ARG J . n 
J 1 76  LYS 76  70  70  LYS LYS J . n 
J 1 77  HIS 77  71  71  HIS HIS J . n 
J 1 78  GLY 78  72  72  GLY GLY J . n 
J 1 79  GLY 79  73  73  GLY GLY J . n 
J 1 80  PRO 80  74  74  PRO PRO J . n 
J 1 81  LYS 81  75  75  LYS LYS J . n 
J 1 82  ASP 82  76  76  ASP ASP J . n 
J 1 83  GLU 83  77  77  GLU GLU J . n 
J 1 84  GLU 84  78  78  GLU GLU J . n 
J 1 85  ARG 85  79  79  ARG ARG J . n 
J 1 86  HIS 86  80  80  HIS HIS J . n 
J 1 87  VAL 87  81  81  VAL VAL J . n 
J 1 88  GLY 88  82  82  GLY GLY J . n 
J 1 89  ASP 89  83  83  ASP ASP J . n 
J 1 90  LEU 90  84  84  LEU LEU J . n 
J 1 91  GLY 91  85  85  GLY GLY J . n 
J 1 92  ASN 92  86  86  ASN ASN J . n 
J 1 93  VAL 93  87  87  VAL VAL J . n 
J 1 94  THR 94  88  88  THR THR J . n 
J 1 95  ALA 95  89  89  ALA ALA J . n 
J 1 96  ASP 96  90  90  ASP ASP J . n 
J 1 97  LYS 97  91  91  LYS LYS J . n 
J 1 98  ASP 98  92  92  ASP ASP J . n 
J 1 99  ALA 99  93  93  ALA ALA J . n 
J 1 100 VAL 100 94  94  VAL VAL J . n 
J 1 101 ALA 101 95  95  ALA ALA J . n 
J 1 102 ASP 102 96  96  ASP ASP J . n 
J 1 103 VAL 103 97  97  VAL VAL J . n 
J 1 104 SER 104 98  98  SER SER J . n 
J 1 105 ILE 105 99  99  ILE ILE J . n 
J 1 106 GLU 106 100 100 GLU GLU J . n 
J 1 107 ASP 107 101 101 ASP ASP J . n 
J 1 108 SER 108 102 102 SER SER J . n 
J 1 109 VAL 109 103 103 VAL VAL J . n 
J 1 110 ILE 110 104 104 ILE ILE J . n 
J 1 111 SER 111 105 105 SER SER J . n 
J 1 112 LEU 112 106 106 LEU LEU J . n 
J 1 113 SER 113 107 107 SER SER J . n 
J 1 114 GLY 114 108 108 GLY GLY J . n 
J 1 115 ASP 115 109 109 ASP ASP J . n 
J 1 116 HIS 116 110 110 HIS HIS J . n 
J 1 117 CYS 117 111 111 CYS CYS J . n 
J 1 118 ILE 118 112 112 ILE ILE J . n 
J 1 119 ILE 119 113 113 ILE ILE J . n 
J 1 120 GLY 120 114 114 GLY GLY J . n 
J 1 121 ARG 121 115 115 ARG ARG J . n 
J 1 122 THR 122 116 116 THR THR J . n 
J 1 123 LEU 123 117 117 LEU LEU J . n 
J 1 124 VAL 124 118 118 VAL VAL J . n 
J 1 125 VAL 125 119 119 VAL VAL J . n 
J 1 126 HIS 126 120 120 HIS HIS J . n 
J 1 127 GLU 127 121 121 GLU GLU J . n 
J 1 128 LYS 128 122 122 LYS LYS J . n 
J 1 129 ALA 129 123 123 ALA ALA J . n 
J 1 130 ASP 130 124 124 ASP ASP J . n 
J 1 131 ASP 131 125 125 ASP ASP J . n 
J 1 132 LEU 132 126 126 LEU LEU J . n 
J 1 133 GLY 133 127 127 GLY GLY J . n 
J 1 134 LYS 134 128 128 LYS LYS J . n 
J 1 135 GLY 135 129 129 GLY GLY J . n 
J 1 136 GLY 136 130 130 GLY GLY J . n 
J 1 137 ASN 137 131 131 ASN ASN J . n 
J 1 138 GLU 138 132 132 GLU GLU J . n 
J 1 139 GLU 139 133 133 GLU GLU J . n 
J 1 140 SER 140 134 134 SER SER J . n 
J 1 141 THR 141 135 135 THR THR J . n 
J 1 142 LYS 142 136 136 LYS LYS J . n 
J 1 143 THR 143 137 137 THR THR J . n 
J 1 144 GLY 144 138 138 GLY GLY J . n 
J 1 145 ASN 145 139 139 ASN ASN J . n 
J 1 146 ALA 146 140 140 ALA ALA J . n 
J 1 147 GLY 147 141 141 GLY GLY J . n 
J 1 148 SER 148 142 142 SER SER J . n 
J 1 149 ARG 149 143 143 ARG ARG J . n 
J 1 150 LEU 150 144 144 LEU LEU J . n 
J 1 151 ALA 151 145 145 ALA ALA J . n 
J 1 152 CYS 152 146 146 CYS CYS J . n 
J 1 153 GLY 153 147 147 GLY GLY J . n 
J 1 154 VAL 154 148 148 VAL VAL J . n 
J 1 155 ILE 155 149 149 ILE ILE J . n 
J 1 156 GLY 156 150 150 GLY GLY J . n 
J 1 157 ILE 157 151 151 ILE ILE J . n 
J 1 158 ALA 158 152 152 ALA ALA J . n 
J 1 159 GLN 159 153 153 GLN GLN J . n 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NPPSFA, National Project on Protein Structural and Functional Analyses' 
_pdbx_SG_project.full_name_of_center   'RIKEN Structural Genomics/Proteomics Initiative' 
_pdbx_SG_project.initial_of_center     RSGI 
# 
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  2 ZN  1  601 601 ZN  ZN  A . 
L  2 ZN  1  602 602 ZN  ZN  B . 
M  2 ZN  1  603 603 ZN  ZN  C . 
N  2 ZN  1  604 604 ZN  ZN  D . 
O  2 ZN  1  605 605 ZN  ZN  E . 
P  2 ZN  1  606 606 ZN  ZN  F . 
Q  2 ZN  1  607 607 ZN  ZN  G . 
R  2 ZN  1  608 608 ZN  ZN  H . 
S  2 ZN  1  609 609 ZN  ZN  I . 
T  2 ZN  1  610 610 ZN  ZN  J . 
U  3 HOH 1  602 2   HOH HOH A . 
U  3 HOH 2  603 7   HOH HOH A . 
U  3 HOH 3  604 10  HOH HOH A . 
U  3 HOH 4  605 24  HOH HOH A . 
U  3 HOH 5  606 42  HOH HOH A . 
U  3 HOH 6  607 49  HOH HOH A . 
U  3 HOH 7  608 61  HOH HOH A . 
U  3 HOH 8  609 63  HOH HOH A . 
U  3 HOH 9  610 66  HOH HOH A . 
U  3 HOH 10 611 71  HOH HOH A . 
U  3 HOH 11 612 83  HOH HOH A . 
U  3 HOH 12 613 90  HOH HOH A . 
U  3 HOH 13 614 99  HOH HOH A . 
U  3 HOH 14 615 100 HOH HOH A . 
U  3 HOH 15 616 106 HOH HOH A . 
U  3 HOH 16 617 109 HOH HOH A . 
U  3 HOH 17 618 165 HOH HOH A . 
U  3 HOH 18 619 206 HOH HOH A . 
U  3 HOH 19 620 218 HOH HOH A . 
U  3 HOH 20 621 219 HOH HOH A . 
U  3 HOH 21 622 222 HOH HOH A . 
U  3 HOH 22 623 244 HOH HOH A . 
U  3 HOH 23 624 245 HOH HOH A . 
U  3 HOH 24 625 250 HOH HOH A . 
U  3 HOH 25 626 252 HOH HOH A . 
U  3 HOH 26 627 253 HOH HOH A . 
U  3 HOH 27 628 254 HOH HOH A . 
U  3 HOH 28 629 272 HOH HOH A . 
U  3 HOH 29 630 283 HOH HOH A . 
U  3 HOH 30 631 293 HOH HOH A . 
U  3 HOH 31 632 296 HOH HOH A . 
U  3 HOH 32 633 302 HOH HOH A . 
U  3 HOH 33 634 321 HOH HOH A . 
U  3 HOH 34 635 334 HOH HOH A . 
U  3 HOH 35 636 347 HOH HOH A . 
U  3 HOH 36 637 353 HOH HOH A . 
U  3 HOH 37 638 364 HOH HOH A . 
U  3 HOH 38 639 373 HOH HOH A . 
U  3 HOH 39 640 385 HOH HOH A . 
U  3 HOH 40 641 411 HOH HOH A . 
U  3 HOH 41 642 426 HOH HOH A . 
U  3 HOH 42 643 433 HOH HOH A . 
U  3 HOH 43 644 436 HOH HOH A . 
U  3 HOH 44 645 463 HOH HOH A . 
U  3 HOH 45 646 469 HOH HOH A . 
U  3 HOH 46 647 479 HOH HOH A . 
V  3 HOH 1  603 1   HOH HOH B . 
V  3 HOH 2  604 17  HOH HOH B . 
V  3 HOH 3  605 20  HOH HOH B . 
V  3 HOH 4  606 21  HOH HOH B . 
V  3 HOH 5  607 25  HOH HOH B . 
V  3 HOH 6  608 26  HOH HOH B . 
V  3 HOH 7  609 29  HOH HOH B . 
V  3 HOH 8  610 30  HOH HOH B . 
V  3 HOH 9  611 34  HOH HOH B . 
V  3 HOH 10 612 35  HOH HOH B . 
V  3 HOH 11 613 36  HOH HOH B . 
V  3 HOH 12 614 38  HOH HOH B . 
V  3 HOH 13 615 40  HOH HOH B . 
V  3 HOH 14 616 41  HOH HOH B . 
V  3 HOH 15 617 46  HOH HOH B . 
V  3 HOH 16 618 56  HOH HOH B . 
V  3 HOH 17 619 58  HOH HOH B . 
V  3 HOH 18 620 81  HOH HOH B . 
V  3 HOH 19 621 87  HOH HOH B . 
V  3 HOH 20 622 89  HOH HOH B . 
V  3 HOH 21 623 96  HOH HOH B . 
V  3 HOH 22 624 97  HOH HOH B . 
V  3 HOH 23 625 104 HOH HOH B . 
V  3 HOH 24 626 107 HOH HOH B . 
V  3 HOH 25 627 108 HOH HOH B . 
V  3 HOH 26 628 128 HOH HOH B . 
V  3 HOH 27 629 133 HOH HOH B . 
V  3 HOH 28 630 138 HOH HOH B . 
V  3 HOH 29 631 139 HOH HOH B . 
V  3 HOH 30 632 152 HOH HOH B . 
V  3 HOH 31 633 153 HOH HOH B . 
V  3 HOH 32 634 157 HOH HOH B . 
V  3 HOH 33 635 164 HOH HOH B . 
V  3 HOH 34 636 169 HOH HOH B . 
V  3 HOH 35 637 173 HOH HOH B . 
V  3 HOH 36 638 179 HOH HOH B . 
V  3 HOH 37 639 180 HOH HOH B . 
V  3 HOH 38 640 181 HOH HOH B . 
V  3 HOH 39 641 185 HOH HOH B . 
V  3 HOH 40 642 192 HOH HOH B . 
V  3 HOH 41 643 193 HOH HOH B . 
V  3 HOH 42 644 196 HOH HOH B . 
V  3 HOH 43 645 214 HOH HOH B . 
V  3 HOH 44 646 226 HOH HOH B . 
V  3 HOH 45 647 231 HOH HOH B . 
V  3 HOH 46 648 236 HOH HOH B . 
V  3 HOH 47 649 239 HOH HOH B . 
V  3 HOH 48 650 243 HOH HOH B . 
V  3 HOH 49 651 247 HOH HOH B . 
V  3 HOH 50 652 261 HOH HOH B . 
V  3 HOH 51 653 264 HOH HOH B . 
V  3 HOH 52 654 270 HOH HOH B . 
V  3 HOH 53 655 279 HOH HOH B . 
V  3 HOH 54 656 291 HOH HOH B . 
V  3 HOH 55 657 295 HOH HOH B . 
V  3 HOH 56 658 297 HOH HOH B . 
V  3 HOH 57 659 312 HOH HOH B . 
V  3 HOH 58 660 314 HOH HOH B . 
V  3 HOH 59 661 333 HOH HOH B . 
V  3 HOH 60 662 345 HOH HOH B . 
V  3 HOH 61 663 352 HOH HOH B . 
V  3 HOH 62 664 355 HOH HOH B . 
V  3 HOH 63 665 363 HOH HOH B . 
V  3 HOH 64 666 368 HOH HOH B . 
V  3 HOH 65 667 371 HOH HOH B . 
V  3 HOH 66 668 374 HOH HOH B . 
V  3 HOH 67 669 375 HOH HOH B . 
V  3 HOH 68 670 376 HOH HOH B . 
V  3 HOH 69 671 384 HOH HOH B . 
V  3 HOH 70 672 389 HOH HOH B . 
V  3 HOH 71 673 401 HOH HOH B . 
V  3 HOH 72 674 425 HOH HOH B . 
V  3 HOH 73 675 430 HOH HOH B . 
V  3 HOH 74 676 435 HOH HOH B . 
V  3 HOH 75 677 439 HOH HOH B . 
V  3 HOH 76 678 452 HOH HOH B . 
V  3 HOH 77 679 471 HOH HOH B . 
W  3 HOH 1  604 44  HOH HOH C . 
W  3 HOH 2  605 45  HOH HOH C . 
W  3 HOH 3  606 48  HOH HOH C . 
W  3 HOH 4  607 68  HOH HOH C . 
W  3 HOH 5  608 95  HOH HOH C . 
W  3 HOH 6  609 121 HOH HOH C . 
W  3 HOH 7  610 141 HOH HOH C . 
W  3 HOH 8  611 155 HOH HOH C . 
W  3 HOH 9  612 161 HOH HOH C . 
W  3 HOH 10 613 176 HOH HOH C . 
W  3 HOH 11 614 211 HOH HOH C . 
W  3 HOH 12 615 212 HOH HOH C . 
W  3 HOH 13 616 227 HOH HOH C . 
W  3 HOH 14 617 240 HOH HOH C . 
W  3 HOH 15 618 284 HOH HOH C . 
W  3 HOH 16 619 288 HOH HOH C . 
W  3 HOH 17 620 298 HOH HOH C . 
W  3 HOH 18 621 308 HOH HOH C . 
W  3 HOH 19 622 315 HOH HOH C . 
W  3 HOH 20 623 317 HOH HOH C . 
W  3 HOH 21 624 318 HOH HOH C . 
W  3 HOH 22 625 319 HOH HOH C . 
W  3 HOH 23 626 330 HOH HOH C . 
W  3 HOH 24 627 341 HOH HOH C . 
W  3 HOH 25 628 343 HOH HOH C . 
W  3 HOH 26 629 361 HOH HOH C . 
W  3 HOH 27 630 388 HOH HOH C . 
W  3 HOH 28 631 394 HOH HOH C . 
W  3 HOH 29 632 404 HOH HOH C . 
W  3 HOH 30 633 416 HOH HOH C . 
W  3 HOH 31 634 423 HOH HOH C . 
W  3 HOH 32 635 440 HOH HOH C . 
W  3 HOH 33 636 447 HOH HOH C . 
W  3 HOH 34 637 454 HOH HOH C . 
W  3 HOH 35 638 465 HOH HOH C . 
W  3 HOH 36 639 476 HOH HOH C . 
X  3 HOH 1  605 3   HOH HOH D . 
X  3 HOH 2  606 4   HOH HOH D . 
X  3 HOH 3  607 6   HOH HOH D . 
X  3 HOH 4  608 8   HOH HOH D . 
X  3 HOH 5  609 12  HOH HOH D . 
X  3 HOH 6  610 18  HOH HOH D . 
X  3 HOH 7  611 37  HOH HOH D . 
X  3 HOH 8  612 59  HOH HOH D . 
X  3 HOH 9  613 67  HOH HOH D . 
X  3 HOH 10 614 73  HOH HOH D . 
X  3 HOH 11 615 74  HOH HOH D . 
X  3 HOH 12 616 86  HOH HOH D . 
X  3 HOH 13 617 91  HOH HOH D . 
X  3 HOH 14 618 102 HOH HOH D . 
X  3 HOH 15 619 116 HOH HOH D . 
X  3 HOH 16 620 122 HOH HOH D . 
X  3 HOH 17 621 124 HOH HOH D . 
X  3 HOH 18 622 126 HOH HOH D . 
X  3 HOH 19 623 127 HOH HOH D . 
X  3 HOH 20 624 131 HOH HOH D . 
X  3 HOH 21 625 136 HOH HOH D . 
X  3 HOH 22 626 137 HOH HOH D . 
X  3 HOH 23 627 143 HOH HOH D . 
X  3 HOH 24 628 150 HOH HOH D . 
X  3 HOH 25 629 166 HOH HOH D . 
X  3 HOH 26 630 171 HOH HOH D . 
X  3 HOH 27 631 177 HOH HOH D . 
X  3 HOH 28 632 187 HOH HOH D . 
X  3 HOH 29 633 188 HOH HOH D . 
X  3 HOH 30 634 189 HOH HOH D . 
X  3 HOH 31 635 195 HOH HOH D . 
X  3 HOH 32 636 201 HOH HOH D . 
X  3 HOH 33 637 204 HOH HOH D . 
X  3 HOH 34 638 205 HOH HOH D . 
X  3 HOH 35 639 209 HOH HOH D . 
X  3 HOH 36 640 225 HOH HOH D . 
X  3 HOH 37 641 232 HOH HOH D . 
X  3 HOH 38 642 234 HOH HOH D . 
X  3 HOH 39 643 237 HOH HOH D . 
X  3 HOH 40 644 241 HOH HOH D . 
X  3 HOH 41 645 257 HOH HOH D . 
X  3 HOH 42 646 258 HOH HOH D . 
X  3 HOH 43 647 259 HOH HOH D . 
X  3 HOH 44 648 260 HOH HOH D . 
X  3 HOH 45 649 265 HOH HOH D . 
X  3 HOH 46 650 280 HOH HOH D . 
X  3 HOH 47 651 294 HOH HOH D . 
X  3 HOH 48 652 301 HOH HOH D . 
X  3 HOH 49 653 307 HOH HOH D . 
X  3 HOH 50 654 320 HOH HOH D . 
X  3 HOH 51 655 323 HOH HOH D . 
X  3 HOH 52 656 325 HOH HOH D . 
X  3 HOH 53 657 327 HOH HOH D . 
X  3 HOH 54 658 337 HOH HOH D . 
X  3 HOH 55 659 365 HOH HOH D . 
X  3 HOH 56 660 367 HOH HOH D . 
X  3 HOH 57 661 381 HOH HOH D . 
X  3 HOH 58 662 406 HOH HOH D . 
X  3 HOH 59 663 415 HOH HOH D . 
X  3 HOH 60 664 429 HOH HOH D . 
X  3 HOH 61 665 438 HOH HOH D . 
X  3 HOH 62 666 444 HOH HOH D . 
X  3 HOH 63 667 445 HOH HOH D . 
X  3 HOH 64 668 448 HOH HOH D . 
X  3 HOH 65 669 451 HOH HOH D . 
X  3 HOH 66 670 461 HOH HOH D . 
Y  3 HOH 1  606 15  HOH HOH E . 
Y  3 HOH 2  607 16  HOH HOH E . 
Y  3 HOH 3  608 22  HOH HOH E . 
Y  3 HOH 4  609 47  HOH HOH E . 
Y  3 HOH 5  610 52  HOH HOH E . 
Y  3 HOH 6  611 53  HOH HOH E . 
Y  3 HOH 7  612 60  HOH HOH E . 
Y  3 HOH 8  613 78  HOH HOH E . 
Y  3 HOH 9  614 88  HOH HOH E . 
Y  3 HOH 10 615 105 HOH HOH E . 
Y  3 HOH 11 616 113 HOH HOH E . 
Y  3 HOH 12 617 118 HOH HOH E . 
Y  3 HOH 13 618 120 HOH HOH E . 
Y  3 HOH 14 619 132 HOH HOH E . 
Y  3 HOH 15 620 134 HOH HOH E . 
Y  3 HOH 16 621 145 HOH HOH E . 
Y  3 HOH 17 622 146 HOH HOH E . 
Y  3 HOH 18 623 154 HOH HOH E . 
Y  3 HOH 19 624 162 HOH HOH E . 
Y  3 HOH 20 625 170 HOH HOH E . 
Y  3 HOH 21 626 172 HOH HOH E . 
Y  3 HOH 22 627 178 HOH HOH E . 
Y  3 HOH 23 628 191 HOH HOH E . 
Y  3 HOH 24 629 197 HOH HOH E . 
Y  3 HOH 25 630 213 HOH HOH E . 
Y  3 HOH 26 631 217 HOH HOH E . 
Y  3 HOH 27 632 220 HOH HOH E . 
Y  3 HOH 28 633 229 HOH HOH E . 
Y  3 HOH 29 634 235 HOH HOH E . 
Y  3 HOH 30 635 238 HOH HOH E . 
Y  3 HOH 31 636 242 HOH HOH E . 
Y  3 HOH 32 637 246 HOH HOH E . 
Y  3 HOH 33 638 255 HOH HOH E . 
Y  3 HOH 34 639 263 HOH HOH E . 
Y  3 HOH 35 640 271 HOH HOH E . 
Y  3 HOH 36 641 275 HOH HOH E . 
Y  3 HOH 37 642 278 HOH HOH E . 
Y  3 HOH 38 643 287 HOH HOH E . 
Y  3 HOH 39 644 303 HOH HOH E . 
Y  3 HOH 40 645 310 HOH HOH E . 
Y  3 HOH 41 646 311 HOH HOH E . 
Y  3 HOH 42 647 331 HOH HOH E . 
Y  3 HOH 43 648 338 HOH HOH E . 
Y  3 HOH 44 649 340 HOH HOH E . 
Y  3 HOH 45 650 346 HOH HOH E . 
Y  3 HOH 46 651 350 HOH HOH E . 
Y  3 HOH 47 652 351 HOH HOH E . 
Y  3 HOH 48 653 358 HOH HOH E . 
Y  3 HOH 49 654 360 HOH HOH E . 
Y  3 HOH 50 655 372 HOH HOH E . 
Y  3 HOH 51 656 378 HOH HOH E . 
Y  3 HOH 52 657 382 HOH HOH E . 
Y  3 HOH 53 658 387 HOH HOH E . 
Y  3 HOH 54 659 420 HOH HOH E . 
Y  3 HOH 55 660 427 HOH HOH E . 
Y  3 HOH 56 661 432 HOH HOH E . 
Y  3 HOH 57 662 442 HOH HOH E . 
Y  3 HOH 58 663 450 HOH HOH E . 
Y  3 HOH 59 664 456 HOH HOH E . 
Y  3 HOH 60 665 458 HOH HOH E . 
Z  3 HOH 1  607 13  HOH HOH F . 
Z  3 HOH 2  608 14  HOH HOH F . 
Z  3 HOH 3  609 23  HOH HOH F . 
Z  3 HOH 4  610 27  HOH HOH F . 
Z  3 HOH 5  611 28  HOH HOH F . 
Z  3 HOH 6  612 33  HOH HOH F . 
Z  3 HOH 7  613 39  HOH HOH F . 
Z  3 HOH 8  614 43  HOH HOH F . 
Z  3 HOH 9  615 50  HOH HOH F . 
Z  3 HOH 10 616 51  HOH HOH F . 
Z  3 HOH 11 617 55  HOH HOH F . 
Z  3 HOH 12 618 62  HOH HOH F . 
Z  3 HOH 13 619 64  HOH HOH F . 
Z  3 HOH 14 620 65  HOH HOH F . 
Z  3 HOH 15 621 70  HOH HOH F . 
Z  3 HOH 16 622 76  HOH HOH F . 
Z  3 HOH 17 623 77  HOH HOH F . 
Z  3 HOH 18 624 84  HOH HOH F . 
Z  3 HOH 19 625 92  HOH HOH F . 
Z  3 HOH 20 626 94  HOH HOH F . 
Z  3 HOH 21 627 98  HOH HOH F . 
Z  3 HOH 22 628 111 HOH HOH F . 
Z  3 HOH 23 629 112 HOH HOH F . 
Z  3 HOH 24 630 123 HOH HOH F . 
Z  3 HOH 25 631 129 HOH HOH F . 
Z  3 HOH 26 632 135 HOH HOH F . 
Z  3 HOH 27 633 140 HOH HOH F . 
Z  3 HOH 28 634 149 HOH HOH F . 
Z  3 HOH 29 635 174 HOH HOH F . 
Z  3 HOH 30 636 175 HOH HOH F . 
Z  3 HOH 31 637 182 HOH HOH F . 
Z  3 HOH 32 638 184 HOH HOH F . 
Z  3 HOH 33 639 194 HOH HOH F . 
Z  3 HOH 34 640 200 HOH HOH F . 
Z  3 HOH 35 641 210 HOH HOH F . 
Z  3 HOH 36 642 223 HOH HOH F . 
Z  3 HOH 37 643 228 HOH HOH F . 
Z  3 HOH 38 644 230 HOH HOH F . 
Z  3 HOH 39 645 233 HOH HOH F . 
Z  3 HOH 40 646 248 HOH HOH F . 
Z  3 HOH 41 647 251 HOH HOH F . 
Z  3 HOH 42 648 276 HOH HOH F . 
Z  3 HOH 43 649 281 HOH HOH F . 
Z  3 HOH 44 650 289 HOH HOH F . 
Z  3 HOH 45 651 290 HOH HOH F . 
Z  3 HOH 46 652 300 HOH HOH F . 
Z  3 HOH 47 653 305 HOH HOH F . 
Z  3 HOH 48 654 309 HOH HOH F . 
Z  3 HOH 49 655 335 HOH HOH F . 
Z  3 HOH 50 656 336 HOH HOH F . 
Z  3 HOH 51 657 339 HOH HOH F . 
Z  3 HOH 52 658 342 HOH HOH F . 
Z  3 HOH 53 659 348 HOH HOH F . 
Z  3 HOH 54 660 366 HOH HOH F . 
Z  3 HOH 55 661 370 HOH HOH F . 
Z  3 HOH 56 662 377 HOH HOH F . 
Z  3 HOH 57 663 386 HOH HOH F . 
Z  3 HOH 58 664 398 HOH HOH F . 
Z  3 HOH 59 665 407 HOH HOH F . 
Z  3 HOH 60 666 419 HOH HOH F . 
Z  3 HOH 61 667 431 HOH HOH F . 
Z  3 HOH 62 668 443 HOH HOH F . 
Z  3 HOH 63 669 446 HOH HOH F . 
Z  3 HOH 64 670 453 HOH HOH F . 
Z  3 HOH 65 671 457 HOH HOH F . 
Z  3 HOH 66 672 459 HOH HOH F . 
Z  3 HOH 67 673 462 HOH HOH F . 
Z  3 HOH 68 674 473 HOH HOH F . 
Z  3 HOH 69 675 474 HOH HOH F . 
AA 3 HOH 1  608 9   HOH HOH G . 
AA 3 HOH 2  609 32  HOH HOH G . 
AA 3 HOH 3  610 75  HOH HOH G . 
AA 3 HOH 4  611 93  HOH HOH G . 
AA 3 HOH 5  612 110 HOH HOH G . 
AA 3 HOH 6  613 119 HOH HOH G . 
AA 3 HOH 7  614 130 HOH HOH G . 
AA 3 HOH 8  615 148 HOH HOH G . 
AA 3 HOH 9  616 151 HOH HOH G . 
AA 3 HOH 10 617 156 HOH HOH G . 
AA 3 HOH 11 618 168 HOH HOH G . 
AA 3 HOH 12 619 186 HOH HOH G . 
AA 3 HOH 13 620 202 HOH HOH G . 
AA 3 HOH 14 621 207 HOH HOH G . 
AA 3 HOH 15 622 208 HOH HOH G . 
AA 3 HOH 16 623 224 HOH HOH G . 
AA 3 HOH 17 624 292 HOH HOH G . 
AA 3 HOH 18 625 324 HOH HOH G . 
AA 3 HOH 19 626 369 HOH HOH G . 
AA 3 HOH 20 627 400 HOH HOH G . 
AA 3 HOH 21 628 405 HOH HOH G . 
BA 3 HOH 1  609 5   HOH HOH H . 
BA 3 HOH 2  610 31  HOH HOH H . 
BA 3 HOH 3  611 54  HOH HOH H . 
BA 3 HOH 4  612 69  HOH HOH H . 
BA 3 HOH 5  613 72  HOH HOH H . 
BA 3 HOH 6  614 80  HOH HOH H . 
BA 3 HOH 7  615 82  HOH HOH H . 
BA 3 HOH 8  616 101 HOH HOH H . 
BA 3 HOH 9  617 103 HOH HOH H . 
BA 3 HOH 10 618 144 HOH HOH H . 
BA 3 HOH 11 619 147 HOH HOH H . 
BA 3 HOH 12 620 158 HOH HOH H . 
BA 3 HOH 13 621 160 HOH HOH H . 
BA 3 HOH 14 622 163 HOH HOH H . 
BA 3 HOH 15 623 167 HOH HOH H . 
BA 3 HOH 16 624 199 HOH HOH H . 
BA 3 HOH 17 625 203 HOH HOH H . 
BA 3 HOH 18 626 249 HOH HOH H . 
BA 3 HOH 19 627 256 HOH HOH H . 
BA 3 HOH 20 628 262 HOH HOH H . 
BA 3 HOH 21 629 269 HOH HOH H . 
BA 3 HOH 22 630 282 HOH HOH H . 
BA 3 HOH 23 631 285 HOH HOH H . 
BA 3 HOH 24 632 286 HOH HOH H . 
BA 3 HOH 25 633 304 HOH HOH H . 
BA 3 HOH 26 634 329 HOH HOH H . 
BA 3 HOH 27 635 332 HOH HOH H . 
BA 3 HOH 28 636 344 HOH HOH H . 
BA 3 HOH 29 637 357 HOH HOH H . 
BA 3 HOH 30 638 359 HOH HOH H . 
BA 3 HOH 31 639 379 HOH HOH H . 
BA 3 HOH 32 640 380 HOH HOH H . 
BA 3 HOH 33 641 383 HOH HOH H . 
BA 3 HOH 34 642 392 HOH HOH H . 
BA 3 HOH 35 643 395 HOH HOH H . 
BA 3 HOH 36 644 408 HOH HOH H . 
BA 3 HOH 37 645 424 HOH HOH H . 
BA 3 HOH 38 646 437 HOH HOH H . 
BA 3 HOH 39 647 441 HOH HOH H . 
BA 3 HOH 40 648 466 HOH HOH H . 
BA 3 HOH 41 649 472 HOH HOH H . 
BA 3 HOH 42 650 475 HOH HOH H . 
CA 3 HOH 1  610 11  HOH HOH I . 
CA 3 HOH 2  611 79  HOH HOH I . 
CA 3 HOH 3  612 114 HOH HOH I . 
CA 3 HOH 4  613 115 HOH HOH I . 
CA 3 HOH 5  614 117 HOH HOH I . 
CA 3 HOH 6  615 125 HOH HOH I . 
CA 3 HOH 7  616 142 HOH HOH I . 
CA 3 HOH 8  617 183 HOH HOH I . 
CA 3 HOH 9  618 215 HOH HOH I . 
CA 3 HOH 10 619 267 HOH HOH I . 
CA 3 HOH 11 620 306 HOH HOH I . 
CA 3 HOH 12 621 313 HOH HOH I . 
CA 3 HOH 13 622 316 HOH HOH I . 
CA 3 HOH 14 623 322 HOH HOH I . 
CA 3 HOH 15 624 328 HOH HOH I . 
CA 3 HOH 16 625 390 HOH HOH I . 
CA 3 HOH 17 626 393 HOH HOH I . 
CA 3 HOH 18 627 396 HOH HOH I . 
CA 3 HOH 19 628 409 HOH HOH I . 
CA 3 HOH 20 629 418 HOH HOH I . 
CA 3 HOH 21 630 421 HOH HOH I . 
CA 3 HOH 22 631 428 HOH HOH I . 
CA 3 HOH 23 632 434 HOH HOH I . 
CA 3 HOH 24 633 460 HOH HOH I . 
CA 3 HOH 25 634 468 HOH HOH I . 
CA 3 HOH 26 635 470 HOH HOH I . 
CA 3 HOH 27 636 477 HOH HOH I . 
CA 3 HOH 28 637 478 HOH HOH I . 
DA 3 HOH 1  611 19  HOH HOH J . 
DA 3 HOH 2  612 57  HOH HOH J . 
DA 3 HOH 3  613 85  HOH HOH J . 
DA 3 HOH 4  614 159 HOH HOH J . 
DA 3 HOH 5  615 190 HOH HOH J . 
DA 3 HOH 6  616 198 HOH HOH J . 
DA 3 HOH 7  617 216 HOH HOH J . 
DA 3 HOH 8  618 221 HOH HOH J . 
DA 3 HOH 9  619 266 HOH HOH J . 
DA 3 HOH 10 620 268 HOH HOH J . 
DA 3 HOH 11 621 273 HOH HOH J . 
DA 3 HOH 12 622 274 HOH HOH J . 
DA 3 HOH 13 623 277 HOH HOH J . 
DA 3 HOH 14 624 299 HOH HOH J . 
DA 3 HOH 15 625 326 HOH HOH J . 
DA 3 HOH 16 626 349 HOH HOH J . 
DA 3 HOH 17 627 354 HOH HOH J . 
DA 3 HOH 18 628 356 HOH HOH J . 
DA 3 HOH 19 629 362 HOH HOH J . 
DA 3 HOH 20 630 391 HOH HOH J . 
DA 3 HOH 21 631 397 HOH HOH J . 
DA 3 HOH 22 632 399 HOH HOH J . 
DA 3 HOH 23 633 402 HOH HOH J . 
DA 3 HOH 24 634 403 HOH HOH J . 
DA 3 HOH 25 635 410 HOH HOH J . 
DA 3 HOH 26 636 412 HOH HOH J . 
DA 3 HOH 27 637 413 HOH HOH J . 
DA 3 HOH 28 638 414 HOH HOH J . 
DA 3 HOH 29 639 417 HOH HOH J . 
DA 3 HOH 30 640 422 HOH HOH J . 
DA 3 HOH 31 641 449 HOH HOH J . 
DA 3 HOH 32 642 455 HOH HOH J . 
DA 3 HOH 33 643 464 HOH HOH J . 
DA 3 HOH 34 644 467 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,U,V   
2 1 C,D,M,N,W,X   
3 1 E,F,O,P,Y,Z   
4 1 G,H,Q,R,AA,BA 
5 1 I,J,S,T,CA,DA 
# 
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)' 1390  ? 
1 MORE         -11.4 ? 
1 'SSA (A^2)'  13890 ? 
2 'ABSA (A^2)' 1400  ? 
2 MORE         -9.4  ? 
2 'SSA (A^2)'  13920 ? 
3 'ABSA (A^2)' 1370  ? 
3 MORE         -11.6 ? 
3 'SSA (A^2)'  13870 ? 
4 'ABSA (A^2)' 1350  ? 
4 MORE         -10.6 ? 
4 'SSA (A^2)'  13730 ? 
5 'ABSA (A^2)' 1360  ? 
5 MORE         -12.1 ? 
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 69 ? A HIS 63 ? 1_555 ZN ? K ZN . ? A ZN 601 ? 1_555 ND1 ? A HIS 77 ? A HIS 71 ? 1_555 99.0  ? 
2  ND1 ? A HIS 69 ? A HIS 63 ? 1_555 ZN ? K ZN . ? A ZN 601 ? 1_555 ND1 ? A HIS 86 ? A HIS 80 ? 1_555 115.8 ? 
3  ND1 ? A HIS 77 ? A HIS 71 ? 1_555 ZN ? K ZN . ? A ZN 601 ? 1_555 ND1 ? A HIS 86 ? A HIS 80 ? 1_555 118.2 ? 
4  ND1 ? A HIS 69 ? A HIS 63 ? 1_555 ZN ? K ZN . ? A ZN 601 ? 1_555 OD1 ? A ASP 89 ? A ASP 83 ? 1_555 103.5 ? 
5  ND1 ? A HIS 77 ? A HIS 71 ? 1_555 ZN ? K ZN . ? A ZN 601 ? 1_555 OD1 ? A ASP 89 ? A ASP 83 ? 1_555 100.5 ? 
6  ND1 ? A HIS 86 ? A HIS 80 ? 1_555 ZN ? K ZN . ? A ZN 601 ? 1_555 OD1 ? A ASP 89 ? A ASP 83 ? 1_555 117.0 ? 
7  ND1 ? B HIS 69 ? B HIS 63 ? 1_555 ZN ? L ZN . ? B ZN 602 ? 1_555 ND1 ? B HIS 77 ? B HIS 71 ? 1_555 102.7 ? 
8  ND1 ? B HIS 69 ? B HIS 63 ? 1_555 ZN ? L ZN . ? B ZN 602 ? 1_555 ND1 ? B HIS 86 ? B HIS 80 ? 1_555 108.0 ? 
9  ND1 ? B HIS 77 ? B HIS 71 ? 1_555 ZN ? L ZN . ? B ZN 602 ? 1_555 ND1 ? B HIS 86 ? B HIS 80 ? 1_555 121.4 ? 
10 ND1 ? B HIS 69 ? B HIS 63 ? 1_555 ZN ? L ZN . ? B ZN 602 ? 1_555 OD1 ? B ASP 89 ? B ASP 83 ? 1_555 108.0 ? 
11 ND1 ? B HIS 77 ? B HIS 71 ? 1_555 ZN ? L ZN . ? B ZN 602 ? 1_555 OD1 ? B ASP 89 ? B ASP 83 ? 1_555 101.9 ? 
12 ND1 ? B HIS 86 ? B HIS 80 ? 1_555 ZN ? L ZN . ? B ZN 602 ? 1_555 OD1 ? B ASP 89 ? B ASP 83 ? 1_555 113.7 ? 
13 ND1 ? C HIS 69 ? C HIS 63 ? 1_555 ZN ? M ZN . ? C ZN 603 ? 1_555 ND1 ? C HIS 77 ? C HIS 71 ? 1_555 99.3  ? 
14 ND1 ? C HIS 69 ? C HIS 63 ? 1_555 ZN ? M ZN . ? C ZN 603 ? 1_555 ND1 ? C HIS 86 ? C HIS 80 ? 1_555 108.6 ? 
15 ND1 ? C HIS 77 ? C HIS 71 ? 1_555 ZN ? M ZN . ? C ZN 603 ? 1_555 ND1 ? C HIS 86 ? C HIS 80 ? 1_555 126.9 ? 
16 ND1 ? C HIS 69 ? C HIS 63 ? 1_555 ZN ? M ZN . ? C ZN 603 ? 1_555 OD1 ? C ASP 89 ? C ASP 83 ? 1_555 102.6 ? 
17 ND1 ? C HIS 77 ? C HIS 71 ? 1_555 ZN ? M ZN . ? C ZN 603 ? 1_555 OD1 ? C ASP 89 ? C ASP 83 ? 1_555 87.1  ? 
18 ND1 ? C HIS 86 ? C HIS 80 ? 1_555 ZN ? M ZN . ? C ZN 603 ? 1_555 OD1 ? C ASP 89 ? C ASP 83 ? 1_555 127.1 ? 
19 ND1 ? D HIS 69 ? D HIS 63 ? 1_555 ZN ? N ZN . ? D ZN 604 ? 1_555 ND1 ? D HIS 77 ? D HIS 71 ? 1_555 106.3 ? 
20 ND1 ? D HIS 69 ? D HIS 63 ? 1_555 ZN ? N ZN . ? D ZN 604 ? 1_555 ND1 ? D HIS 86 ? D HIS 80 ? 1_555 110.9 ? 
21 ND1 ? D HIS 77 ? D HIS 71 ? 1_555 ZN ? N ZN . ? D ZN 604 ? 1_555 ND1 ? D HIS 86 ? D HIS 80 ? 1_555 117.8 ? 
22 ND1 ? D HIS 69 ? D HIS 63 ? 1_555 ZN ? N ZN . ? D ZN 604 ? 1_555 OD1 ? D ASP 89 ? D ASP 83 ? 1_555 104.5 ? 
23 ND1 ? D HIS 77 ? D HIS 71 ? 1_555 ZN ? N ZN . ? D ZN 604 ? 1_555 OD1 ? D ASP 89 ? D ASP 83 ? 1_555 102.9 ? 
24 ND1 ? D HIS 86 ? D HIS 80 ? 1_555 ZN ? N ZN . ? D ZN 604 ? 1_555 OD1 ? D ASP 89 ? D ASP 83 ? 1_555 113.3 ? 
25 ND1 ? E HIS 69 ? E HIS 63 ? 1_555 ZN ? O ZN . ? E ZN 605 ? 1_555 ND1 ? E HIS 77 ? E HIS 71 ? 1_555 106.3 ? 
26 ND1 ? E HIS 69 ? E HIS 63 ? 1_555 ZN ? O ZN . ? E ZN 605 ? 1_555 ND1 ? E HIS 86 ? E HIS 80 ? 1_555 113.1 ? 
27 ND1 ? E HIS 77 ? E HIS 71 ? 1_555 ZN ? O ZN . ? E ZN 605 ? 1_555 ND1 ? E HIS 86 ? E HIS 80 ? 1_555 122.7 ? 
28 ND1 ? E HIS 69 ? E HIS 63 ? 1_555 ZN ? O ZN . ? E ZN 605 ? 1_555 OD1 ? E ASP 89 ? E ASP 83 ? 1_555 102.2 ? 
29 ND1 ? E HIS 77 ? E HIS 71 ? 1_555 ZN ? O ZN . ? E ZN 605 ? 1_555 OD1 ? E ASP 89 ? E ASP 83 ? 1_555 90.9  ? 
30 ND1 ? E HIS 86 ? E HIS 80 ? 1_555 ZN ? O ZN . ? E ZN 605 ? 1_555 OD1 ? E ASP 89 ? E ASP 83 ? 1_555 118.0 ? 
31 ND1 ? F HIS 69 ? F HIS 63 ? 1_555 ZN ? P ZN . ? F ZN 606 ? 1_555 ND1 ? F HIS 77 ? F HIS 71 ? 1_555 105.0 ? 
32 ND1 ? F HIS 69 ? F HIS 63 ? 1_555 ZN ? P ZN . ? F ZN 606 ? 1_555 ND1 ? F HIS 86 ? F HIS 80 ? 1_555 115.7 ? 
33 ND1 ? F HIS 77 ? F HIS 71 ? 1_555 ZN ? P ZN . ? F ZN 606 ? 1_555 ND1 ? F HIS 86 ? F HIS 80 ? 1_555 121.7 ? 
34 ND1 ? F HIS 69 ? F HIS 63 ? 1_555 ZN ? P ZN . ? F ZN 606 ? 1_555 OD1 ? F ASP 89 ? F ASP 83 ? 1_555 101.2 ? 
35 ND1 ? F HIS 77 ? F HIS 71 ? 1_555 ZN ? P ZN . ? F ZN 606 ? 1_555 OD1 ? F ASP 89 ? F ASP 83 ? 1_555 94.4  ? 
36 ND1 ? F HIS 86 ? F HIS 80 ? 1_555 ZN ? P ZN . ? F ZN 606 ? 1_555 OD1 ? F ASP 89 ? F ASP 83 ? 1_555 115.2 ? 
37 ND1 ? G HIS 69 ? G HIS 63 ? 1_555 ZN ? Q ZN . ? G ZN 607 ? 1_555 ND1 ? G HIS 77 ? G HIS 71 ? 1_555 108.5 ? 
38 ND1 ? G HIS 69 ? G HIS 63 ? 1_555 ZN ? Q ZN . ? G ZN 607 ? 1_555 ND1 ? G HIS 86 ? G HIS 80 ? 1_555 109.6 ? 
39 ND1 ? G HIS 77 ? G HIS 71 ? 1_555 ZN ? Q ZN . ? G ZN 607 ? 1_555 ND1 ? G HIS 86 ? G HIS 80 ? 1_555 122.1 ? 
40 ND1 ? G HIS 69 ? G HIS 63 ? 1_555 ZN ? Q ZN . ? G ZN 607 ? 1_555 OD1 ? G ASP 89 ? G ASP 83 ? 1_555 104.3 ? 
41 ND1 ? G HIS 77 ? G HIS 71 ? 1_555 ZN ? Q ZN . ? G ZN 607 ? 1_555 OD1 ? G ASP 89 ? G ASP 83 ? 1_555 89.5  ? 
42 ND1 ? G HIS 86 ? G HIS 80 ? 1_555 ZN ? Q ZN . ? G ZN 607 ? 1_555 OD1 ? G ASP 89 ? G ASP 83 ? 1_555 120.3 ? 
43 ND1 ? H HIS 69 ? H HIS 63 ? 1_555 ZN ? R ZN . ? H ZN 608 ? 1_555 ND1 ? H HIS 77 ? H HIS 71 ? 1_555 96.9  ? 
44 ND1 ? H HIS 69 ? H HIS 63 ? 1_555 ZN ? R ZN . ? H ZN 608 ? 1_555 ND1 ? H HIS 86 ? H HIS 80 ? 1_555 107.7 ? 
45 ND1 ? H HIS 77 ? H HIS 71 ? 1_555 ZN ? R ZN . ? H ZN 608 ? 1_555 ND1 ? H HIS 86 ? H HIS 80 ? 1_555 126.8 ? 
46 ND1 ? H HIS 69 ? H HIS 63 ? 1_555 ZN ? R ZN . ? H ZN 608 ? 1_555 OD1 ? H ASP 89 ? H ASP 83 ? 1_555 110.3 ? 
47 ND1 ? H HIS 77 ? H HIS 71 ? 1_555 ZN ? R ZN . ? H ZN 608 ? 1_555 OD1 ? H ASP 89 ? H ASP 83 ? 1_555 105.2 ? 
48 ND1 ? H HIS 86 ? H HIS 80 ? 1_555 ZN ? R ZN . ? H ZN 608 ? 1_555 OD1 ? H ASP 89 ? H ASP 83 ? 1_555 108.9 ? 
49 ND1 ? I HIS 69 ? I HIS 63 ? 1_555 ZN ? S ZN . ? I ZN 609 ? 1_555 ND1 ? I HIS 77 ? I HIS 71 ? 1_555 110.7 ? 
50 ND1 ? I HIS 69 ? I HIS 63 ? 1_555 ZN ? S ZN . ? I ZN 609 ? 1_555 ND1 ? I HIS 86 ? I HIS 80 ? 1_555 106.7 ? 
51 ND1 ? I HIS 77 ? I HIS 71 ? 1_555 ZN ? S ZN . ? I ZN 609 ? 1_555 ND1 ? I HIS 86 ? I HIS 80 ? 1_555 121.9 ? 
52 ND1 ? I HIS 69 ? I HIS 63 ? 1_555 ZN ? S ZN . ? I ZN 609 ? 1_555 OD1 ? I ASP 89 ? I ASP 83 ? 1_555 101.9 ? 
53 ND1 ? I HIS 77 ? I HIS 71 ? 1_555 ZN ? S ZN . ? I ZN 609 ? 1_555 OD1 ? I ASP 89 ? I ASP 83 ? 1_555 113.2 ? 
54 ND1 ? I HIS 86 ? I HIS 80 ? 1_555 ZN ? S ZN . ? I ZN 609 ? 1_555 OD1 ? I ASP 89 ? I ASP 83 ? 1_555 100.3 ? 
55 ND1 ? I HIS 69 ? I HIS 63 ? 1_555 ZN ? S ZN . ? I ZN 609 ? 1_555 OD2 ? I ASP 89 ? I ASP 83 ? 1_555 154.1 ? 
56 ND1 ? I HIS 77 ? I HIS 71 ? 1_555 ZN ? S ZN . ? I ZN 609 ? 1_555 OD2 ? I ASP 89 ? I ASP 83 ? 1_555 78.5  ? 
57 ND1 ? I HIS 86 ? I HIS 80 ? 1_555 ZN ? S ZN . ? I ZN 609 ? 1_555 OD2 ? I ASP 89 ? I ASP 83 ? 1_555 86.6  ? 
58 OD1 ? I ASP 89 ? I ASP 83 ? 1_555 ZN ? S ZN . ? I ZN 609 ? 1_555 OD2 ? I ASP 89 ? I ASP 83 ? 1_555 53.1  ? 
59 ND1 ? J HIS 69 ? J HIS 63 ? 1_555 ZN ? T ZN . ? J ZN 610 ? 1_555 ND1 ? J HIS 77 ? J HIS 71 ? 1_555 105.6 ? 
60 ND1 ? J HIS 69 ? J HIS 63 ? 1_555 ZN ? T ZN . ? J ZN 610 ? 1_555 ND1 ? J HIS 86 ? J HIS 80 ? 1_555 115.8 ? 
61 ND1 ? J HIS 77 ? J HIS 71 ? 1_555 ZN ? T ZN . ? J ZN 610 ? 1_555 ND1 ? J HIS 86 ? J HIS 80 ? 1_555 117.7 ? 
62 ND1 ? J HIS 69 ? J HIS 63 ? 1_555 ZN ? T ZN . ? J ZN 610 ? 1_555 OD1 ? J ASP 89 ? J ASP 83 ? 1_555 102.1 ? 
63 ND1 ? J HIS 77 ? J HIS 71 ? 1_555 ZN ? T ZN . ? J ZN 610 ? 1_555 OD1 ? J ASP 89 ? J ASP 83 ? 1_555 103.3 ? 
64 ND1 ? J HIS 86 ? J HIS 80 ? 1_555 ZN ? T ZN . ? J ZN 610 ? 1_555 OD1 ? J ASP 89 ? J ASP 83 ? 1_555 110.6 ? 
# 
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 2009-03-24 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2012-04-04 
4 'Structure model' 1 3 2021-11-10 
# 
_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' 'Version format compliance' 
2 3 'Structure model' Other                       
3 4 'Structure model' 'Database references'       
4 4 '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 4 'Structure model' database_2         
2 4 'Structure model' struct_conn        
3 4 'Structure model' struct_ref_seq_dif 
4 4 'Structure model' struct_site        
# 
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  4 'Structure model' '_database_2.pdbx_DOI'                
2  4 'Structure model' '_database_2.pdbx_database_accession' 
3  4 'Structure model' '_struct_conn.pdbx_dist_value'        
4  4 'Structure model' '_struct_conn.ptnr1_auth_asym_id'     
5  4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'     
6  4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'      
7  4 'Structure model' '_struct_conn.ptnr1_label_asym_id'    
8  4 'Structure model' '_struct_conn.ptnr1_label_atom_id'    
9  4 'Structure model' '_struct_conn.ptnr1_label_comp_id'    
10 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'     
11 4 'Structure model' '_struct_conn.ptnr2_auth_asym_id'     
12 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'      
13 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'    
14 4 'Structure model' '_struct_ref_seq_dif.details'         
15 4 'Structure model' '_struct_site.pdbx_auth_asym_id'      
16 4 'Structure model' '_struct_site.pdbx_auth_comp_id'      
17 4 'Structure model' '_struct_site.pdbx_auth_seq_id'       
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CNS       refinement        1.1 ? 1 
HKL-2000  'data collection' .   ? 2 
DENZO     'data reduction'  .   ? 3 
SCALEPACK 'data scaling'    .   ? 4 
MOLREP    phasing           .   ? 5 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 126 ? ? 36.27   28.78   
2  1 ASP C 109 ? ? 8.06    -54.75  
3  1 LEU C 126 ? ? 59.83   18.93   
4  1 SER G 25  ? ? -25.61  -40.98  
5  1 ASN G 26  ? ? -147.08 27.61   
6  1 SER G 68  ? ? 40.92   17.51   
7  1 ASP G 90  ? ? -61.67  -167.82 
8  1 LEU G 126 ? ? 43.24   19.94   
9  1 LYS G 128 ? ? -145.05 -9.29   
10 1 LYS G 136 ? ? -109.29 -65.35  
11 1 ASN H 26  ? ? -97.91  49.52   
12 1 ALA H 55  ? ? -104.07 41.52   
13 1 ASN I 26  ? ? -108.71 42.80   
14 1 ALA I 55  ? ? -114.64 59.14   
15 1 PRO I 66  ? ? -67.50  12.07   
16 1 LYS I 128 ? ? -148.90 27.52   
17 1 ASN I 131 ? ? -55.32  -179.02 
18 1 SER J 107 ? ? 178.27  163.66  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -5 ? A GLY 1 
2  1 Y 1 A PRO -4 ? A PRO 2 
3  1 Y 1 A LEU -3 ? A LEU 3 
4  1 Y 1 A GLY -2 ? A GLY 4 
5  1 Y 1 A SER -1 ? A SER 5 
6  1 Y 1 A MET 0  ? A MET 6 
7  1 Y 1 A ALA 1  ? A ALA 7 
8  1 Y 1 B GLY -5 ? B GLY 1 
9  1 Y 1 B PRO -4 ? B PRO 2 
10 1 Y 1 B LEU -3 ? B LEU 3 
11 1 Y 1 B GLY -2 ? B GLY 4 
12 1 Y 1 B SER -1 ? B SER 5 
13 1 Y 1 B MET 0  ? B MET 6 
14 1 Y 1 B ALA 1  ? B ALA 7 
15 1 Y 1 C GLY -5 ? C GLY 1 
16 1 Y 1 C PRO -4 ? C PRO 2 
17 1 Y 1 C LEU -3 ? C LEU 3 
18 1 Y 1 C GLY -2 ? C GLY 4 
19 1 Y 1 C SER -1 ? C SER 5 
20 1 Y 1 C MET 0  ? C MET 6 
21 1 Y 1 D GLY -5 ? D GLY 1 
22 1 Y 1 D PRO -4 ? D PRO 2 
23 1 Y 1 D LEU -3 ? D LEU 3 
24 1 Y 1 D GLY -2 ? D GLY 4 
25 1 Y 1 D SER -1 ? D SER 5 
26 1 Y 1 D MET 0  ? D MET 6 
27 1 Y 1 E GLY -5 ? E GLY 1 
28 1 Y 1 E PRO -4 ? E PRO 2 
29 1 Y 1 E LEU -3 ? E LEU 3 
30 1 Y 1 E GLY -2 ? E GLY 4 
31 1 Y 1 E SER -1 ? E SER 5 
32 1 Y 1 E MET 0  ? E MET 6 
33 1 Y 1 F GLY -5 ? F GLY 1 
34 1 Y 1 F PRO -4 ? F PRO 2 
35 1 Y 1 F LEU -3 ? F LEU 3 
36 1 Y 1 F GLY -2 ? F GLY 4 
37 1 Y 1 F SER -1 ? F SER 5 
38 1 Y 1 F MET 0  ? F MET 6 
39 1 Y 1 G GLY -5 ? G GLY 1 
40 1 Y 1 G PRO -4 ? G PRO 2 
41 1 Y 1 G LEU -3 ? G LEU 3 
42 1 Y 1 G GLY -2 ? G GLY 4 
43 1 Y 1 G SER -1 ? G SER 5 
44 1 Y 1 G MET 0  ? G MET 6 
45 1 Y 1 H GLY -5 ? H GLY 1 
46 1 Y 1 H PRO -4 ? H PRO 2 
47 1 Y 1 H LEU -3 ? H LEU 3 
48 1 Y 1 H GLY -2 ? H GLY 4 
49 1 Y 1 H SER -1 ? H SER 5 
50 1 Y 1 H MET 0  ? H MET 6 
51 1 Y 1 I GLY -5 ? I GLY 1 
52 1 Y 1 I PRO -4 ? I PRO 2 
53 1 Y 1 I LEU -3 ? I LEU 3 
54 1 Y 1 I GLY -2 ? I GLY 4 
55 1 Y 1 I SER -1 ? I SER 5 
56 1 Y 1 I MET 0  ? I MET 6 
57 1 Y 1 J GLY -5 ? J GLY 1 
58 1 Y 1 J PRO -4 ? J PRO 2 
59 1 Y 1 J LEU -3 ? J LEU 3 
60 1 Y 1 J GLY -2 ? J GLY 4 
61 1 Y 1 J SER -1 ? J SER 5 
62 1 Y 1 J MET 0  ? J MET 6 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION' ZN  
3 water      HOH 
# 
