data_4QAA
# 
_entry.id   4QAA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.289 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4QAA         
RCSB  RCSB085801   
WWPDB D_1000085801 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1UX2 . unspecified 
PDB 1UW6 . unspecified 
PDB 1UV6 . unspecified 
PDB 4QAB . unspecified 
PDB 4QAC . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4QAA 
_pdbx_database_status.recvd_initial_deposition_date   2014-05-03 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Kaczanowska, K.' 1 
'Harel, M.'       2 
'Radic, Z.'       3 
'Changeux, J.-P.' 4 
'Finn, M.G.'      5 
'Taylor, P.'      6 
# 
_citation.id                        primary 
_citation.title                     
'Structural basis for cooperative interactions of substituted 2-aminopyrimidines with the acetylcholine binding protein.' 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_volume            111 
_citation.page_first                10749 
_citation.page_last                 10754 
_citation.year                      2014 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25006260 
_citation.pdbx_database_id_DOI      10.1073/pnas.1410992111 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Kaczanowska, K.' 1 
primary 'Harel, M.'       2 
primary 'Radic, Z.'       3 
primary 'Changeux, J.P.'  4 
primary 'Finn, M.G.'      5 
primary 'Taylor, P.'      6 
# 
_cell.entry_id           4QAA 
_cell.length_a           83.414 
_cell.length_b           129.934 
_cell.length_c           122.752 
_cell.angle_alpha        90.00 
_cell.angle_beta         106.21 
_cell.angle_gamma        90.00 
_cell.Z_PDB              20 
_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                         4QAA 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_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 'Acetylcholine-binding protein'                        24746.338 10  ? ? ? ? 
2 non-polymer syn '6-(4-methoxyphenyl)-N~4~-octylpyrimidine-2,4-diamine' 328.452   10  ? ? ? ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE                                 221.208   10  ? ? ? ? 
4 non-polymer syn 'PHOSPHATE ION'                                        94.971    19  ? ? ? ? 
5 water       nat water                                                  18.015    161 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ACh-binding protein, AchBP' 
# 
_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       
;DYKDDDDKLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPD
QVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISV
DPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;DYKDDDDKLDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPD
QVSVPISSLWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISV
DPTTENSDDSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEI
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F,G,H,I,J 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ASP n 
1 2   TYR n 
1 3   LYS n 
1 4   ASP n 
1 5   ASP n 
1 6   ASP n 
1 7   ASP n 
1 8   LYS n 
1 9   LEU n 
1 10  ASP n 
1 11  ARG n 
1 12  ALA n 
1 13  ASP n 
1 14  ILE n 
1 15  LEU n 
1 16  TYR n 
1 17  ASN n 
1 18  ILE n 
1 19  ARG n 
1 20  GLN n 
1 21  THR n 
1 22  SER n 
1 23  ARG n 
1 24  PRO n 
1 25  ASP n 
1 26  VAL n 
1 27  ILE n 
1 28  PRO n 
1 29  THR n 
1 30  GLN n 
1 31  ARG n 
1 32  ASP n 
1 33  ARG n 
1 34  PRO n 
1 35  VAL n 
1 36  ALA n 
1 37  VAL n 
1 38  SER n 
1 39  VAL n 
1 40  SER n 
1 41  LEU n 
1 42  LYS n 
1 43  PHE n 
1 44  ILE n 
1 45  ASN n 
1 46  ILE n 
1 47  LEU n 
1 48  GLU n 
1 49  VAL n 
1 50  ASN n 
1 51  GLU n 
1 52  ILE n 
1 53  THR n 
1 54  ASN n 
1 55  GLU n 
1 56  VAL n 
1 57  ASP n 
1 58  VAL n 
1 59  VAL n 
1 60  PHE n 
1 61  TRP n 
1 62  GLN n 
1 63  GLN n 
1 64  THR n 
1 65  THR n 
1 66  TRP n 
1 67  SER n 
1 68  ASP n 
1 69  ARG n 
1 70  THR n 
1 71  LEU n 
1 72  ALA n 
1 73  TRP n 
1 74  ASN n 
1 75  SER n 
1 76  SER n 
1 77  HIS n 
1 78  SER n 
1 79  PRO n 
1 80  ASP n 
1 81  GLN n 
1 82  VAL n 
1 83  SER n 
1 84  VAL n 
1 85  PRO n 
1 86  ILE n 
1 87  SER n 
1 88  SER n 
1 89  LEU n 
1 90  TRP n 
1 91  VAL n 
1 92  PRO n 
1 93  ASP n 
1 94  LEU n 
1 95  ALA n 
1 96  ALA n 
1 97  TYR n 
1 98  ASN n 
1 99  ALA n 
1 100 ILE n 
1 101 SER n 
1 102 LYS n 
1 103 PRO n 
1 104 GLU n 
1 105 VAL n 
1 106 LEU n 
1 107 THR n 
1 108 PRO n 
1 109 GLN n 
1 110 LEU n 
1 111 ALA n 
1 112 ARG n 
1 113 VAL n 
1 114 VAL n 
1 115 SER n 
1 116 ASP n 
1 117 GLY n 
1 118 GLU n 
1 119 VAL n 
1 120 LEU n 
1 121 TYR n 
1 122 MET n 
1 123 PRO n 
1 124 SER n 
1 125 ILE n 
1 126 ARG n 
1 127 GLN n 
1 128 ARG n 
1 129 PHE n 
1 130 SER n 
1 131 CYS n 
1 132 ASP n 
1 133 VAL n 
1 134 SER n 
1 135 GLY n 
1 136 VAL n 
1 137 ASP n 
1 138 THR n 
1 139 GLU n 
1 140 SER n 
1 141 GLY n 
1 142 ALA n 
1 143 THR n 
1 144 CYS n 
1 145 ARG n 
1 146 ILE n 
1 147 LYS n 
1 148 ILE n 
1 149 GLY n 
1 150 SER n 
1 151 TRP n 
1 152 THR n 
1 153 HIS n 
1 154 HIS n 
1 155 SER n 
1 156 ARG n 
1 157 GLU n 
1 158 ILE n 
1 159 SER n 
1 160 VAL n 
1 161 ASP n 
1 162 PRO n 
1 163 THR n 
1 164 THR n 
1 165 GLU n 
1 166 ASN n 
1 167 SER n 
1 168 ASP n 
1 169 ASP n 
1 170 SER n 
1 171 GLU n 
1 172 TYR n 
1 173 PHE n 
1 174 SER n 
1 175 GLN n 
1 176 TYR n 
1 177 SER n 
1 178 ARG n 
1 179 PHE n 
1 180 GLU n 
1 181 ILE n 
1 182 LEU n 
1 183 ASP n 
1 184 VAL n 
1 185 THR n 
1 186 GLN n 
1 187 LYS n 
1 188 LYS n 
1 189 ASN n 
1 190 SER n 
1 191 VAL n 
1 192 THR n 
1 193 TYR n 
1 194 SER n 
1 195 CYS n 
1 196 CYS n 
1 197 PRO n 
1 198 GLU n 
1 199 ALA n 
1 200 TYR n 
1 201 GLU n 
1 202 ASP n 
1 203 VAL n 
1 204 GLU n 
1 205 VAL n 
1 206 SER n 
1 207 LEU n 
1 208 ASN n 
1 209 PHE n 
1 210 ARG n 
1 211 LYS n 
1 212 LYS n 
1 213 GLY n 
1 214 ARG n 
1 215 SER n 
1 216 GLU n 
1 217 ILE 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               'Great pond snail' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Lymnaea stagnalis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     6523 
_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               human 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            HEK293S-GNT1 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pFLAG-CMV3 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ACHP_LYMST 
_struct_ref.pdbx_db_accession          P58154 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LDRADILYNIRQTSRPDVIPTQRDRPVAVSVSLKFINILEVNEITNEVDVVFWQQTTWSDRTLAWNSSHSPDQVSVPISS
LWVPDLAAYNAISKPEVLTPQLARVVSDGEVLYMPSIRQRFSCDVSGVDTESGATCRIKIGSWTHHSREISVDPTTENSD
DSEYFSQYSRFEILDVTQKKNSVTYSCCPEAYEDVEVSLNFRKKGRSEI
;
_struct_ref.pdbx_align_begin           20 
_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 4QAA A 9 ? 217 ? P58154 20 ? 228 ? 1 209 
2  1 4QAA B 9 ? 217 ? P58154 20 ? 228 ? 1 209 
3  1 4QAA C 9 ? 217 ? P58154 20 ? 228 ? 1 209 
4  1 4QAA D 9 ? 217 ? P58154 20 ? 228 ? 1 209 
5  1 4QAA E 9 ? 217 ? P58154 20 ? 228 ? 1 209 
6  1 4QAA F 9 ? 217 ? P58154 20 ? 228 ? 1 209 
7  1 4QAA G 9 ? 217 ? P58154 20 ? 228 ? 1 209 
8  1 4QAA H 9 ? 217 ? P58154 20 ? 228 ? 1 209 
9  1 4QAA I 9 ? 217 ? P58154 20 ? 228 ? 1 209 
10 1 4QAA J 9 ? 217 ? P58154 20 ? 228 ? 1 209 
# 
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  4QAA ASP A 1 ? UNP P58154 ? ? 'EXPRESSION TAG' -7 1  
1  4QAA TYR A 2 ? UNP P58154 ? ? 'EXPRESSION TAG' -6 2  
1  4QAA LYS A 3 ? UNP P58154 ? ? 'EXPRESSION TAG' -5 3  
1  4QAA ASP A 4 ? UNP P58154 ? ? 'EXPRESSION TAG' -4 4  
1  4QAA ASP A 5 ? UNP P58154 ? ? 'EXPRESSION TAG' -3 5  
1  4QAA ASP A 6 ? UNP P58154 ? ? 'EXPRESSION TAG' -2 6  
1  4QAA ASP A 7 ? UNP P58154 ? ? 'EXPRESSION TAG' -1 7  
1  4QAA LYS A 8 ? UNP P58154 ? ? 'EXPRESSION TAG' 0  8  
2  4QAA ASP B 1 ? UNP P58154 ? ? 'EXPRESSION TAG' -7 9  
2  4QAA TYR B 2 ? UNP P58154 ? ? 'EXPRESSION TAG' -6 10 
2  4QAA LYS B 3 ? UNP P58154 ? ? 'EXPRESSION TAG' -5 11 
2  4QAA ASP B 4 ? UNP P58154 ? ? 'EXPRESSION TAG' -4 12 
2  4QAA ASP B 5 ? UNP P58154 ? ? 'EXPRESSION TAG' -3 13 
2  4QAA ASP B 6 ? UNP P58154 ? ? 'EXPRESSION TAG' -2 14 
2  4QAA ASP B 7 ? UNP P58154 ? ? 'EXPRESSION TAG' -1 15 
2  4QAA LYS B 8 ? UNP P58154 ? ? 'EXPRESSION TAG' 0  16 
3  4QAA ASP C 1 ? UNP P58154 ? ? 'EXPRESSION TAG' -7 17 
3  4QAA TYR C 2 ? UNP P58154 ? ? 'EXPRESSION TAG' -6 18 
3  4QAA LYS C 3 ? UNP P58154 ? ? 'EXPRESSION TAG' -5 19 
3  4QAA ASP C 4 ? UNP P58154 ? ? 'EXPRESSION TAG' -4 20 
3  4QAA ASP C 5 ? UNP P58154 ? ? 'EXPRESSION TAG' -3 21 
3  4QAA ASP C 6 ? UNP P58154 ? ? 'EXPRESSION TAG' -2 22 
3  4QAA ASP C 7 ? UNP P58154 ? ? 'EXPRESSION TAG' -1 23 
3  4QAA LYS C 8 ? UNP P58154 ? ? 'EXPRESSION TAG' 0  24 
4  4QAA ASP D 1 ? UNP P58154 ? ? 'EXPRESSION TAG' -7 25 
4  4QAA TYR D 2 ? UNP P58154 ? ? 'EXPRESSION TAG' -6 26 
4  4QAA LYS D 3 ? UNP P58154 ? ? 'EXPRESSION TAG' -5 27 
4  4QAA ASP D 4 ? UNP P58154 ? ? 'EXPRESSION TAG' -4 28 
4  4QAA ASP D 5 ? UNP P58154 ? ? 'EXPRESSION TAG' -3 29 
4  4QAA ASP D 6 ? UNP P58154 ? ? 'EXPRESSION TAG' -2 30 
4  4QAA ASP D 7 ? UNP P58154 ? ? 'EXPRESSION TAG' -1 31 
4  4QAA LYS D 8 ? UNP P58154 ? ? 'EXPRESSION TAG' 0  32 
5  4QAA ASP E 1 ? UNP P58154 ? ? 'EXPRESSION TAG' -7 33 
5  4QAA TYR E 2 ? UNP P58154 ? ? 'EXPRESSION TAG' -6 34 
5  4QAA LYS E 3 ? UNP P58154 ? ? 'EXPRESSION TAG' -5 35 
5  4QAA ASP E 4 ? UNP P58154 ? ? 'EXPRESSION TAG' -4 36 
5  4QAA ASP E 5 ? UNP P58154 ? ? 'EXPRESSION TAG' -3 37 
5  4QAA ASP E 6 ? UNP P58154 ? ? 'EXPRESSION TAG' -2 38 
5  4QAA ASP E 7 ? UNP P58154 ? ? 'EXPRESSION TAG' -1 39 
5  4QAA LYS E 8 ? UNP P58154 ? ? 'EXPRESSION TAG' 0  40 
6  4QAA ASP F 1 ? UNP P58154 ? ? 'EXPRESSION TAG' -7 41 
6  4QAA TYR F 2 ? UNP P58154 ? ? 'EXPRESSION TAG' -6 42 
6  4QAA LYS F 3 ? UNP P58154 ? ? 'EXPRESSION TAG' -5 43 
6  4QAA ASP F 4 ? UNP P58154 ? ? 'EXPRESSION TAG' -4 44 
6  4QAA ASP F 5 ? UNP P58154 ? ? 'EXPRESSION TAG' -3 45 
6  4QAA ASP F 6 ? UNP P58154 ? ? 'EXPRESSION TAG' -2 46 
6  4QAA ASP F 7 ? UNP P58154 ? ? 'EXPRESSION TAG' -1 47 
6  4QAA LYS F 8 ? UNP P58154 ? ? 'EXPRESSION TAG' 0  48 
7  4QAA ASP G 1 ? UNP P58154 ? ? 'EXPRESSION TAG' -7 49 
7  4QAA TYR G 2 ? UNP P58154 ? ? 'EXPRESSION TAG' -6 50 
7  4QAA LYS G 3 ? UNP P58154 ? ? 'EXPRESSION TAG' -5 51 
7  4QAA ASP G 4 ? UNP P58154 ? ? 'EXPRESSION TAG' -4 52 
7  4QAA ASP G 5 ? UNP P58154 ? ? 'EXPRESSION TAG' -3 53 
7  4QAA ASP G 6 ? UNP P58154 ? ? 'EXPRESSION TAG' -2 54 
7  4QAA ASP G 7 ? UNP P58154 ? ? 'EXPRESSION TAG' -1 55 
7  4QAA LYS G 8 ? UNP P58154 ? ? 'EXPRESSION TAG' 0  56 
8  4QAA ASP H 1 ? UNP P58154 ? ? 'EXPRESSION TAG' -7 57 
8  4QAA TYR H 2 ? UNP P58154 ? ? 'EXPRESSION TAG' -6 58 
8  4QAA LYS H 3 ? UNP P58154 ? ? 'EXPRESSION TAG' -5 59 
8  4QAA ASP H 4 ? UNP P58154 ? ? 'EXPRESSION TAG' -4 60 
8  4QAA ASP H 5 ? UNP P58154 ? ? 'EXPRESSION TAG' -3 61 
8  4QAA ASP H 6 ? UNP P58154 ? ? 'EXPRESSION TAG' -2 62 
8  4QAA ASP H 7 ? UNP P58154 ? ? 'EXPRESSION TAG' -1 63 
8  4QAA LYS H 8 ? UNP P58154 ? ? 'EXPRESSION TAG' 0  64 
9  4QAA ASP I 1 ? UNP P58154 ? ? 'EXPRESSION TAG' -7 65 
9  4QAA TYR I 2 ? UNP P58154 ? ? 'EXPRESSION TAG' -6 66 
9  4QAA LYS I 3 ? UNP P58154 ? ? 'EXPRESSION TAG' -5 67 
9  4QAA ASP I 4 ? UNP P58154 ? ? 'EXPRESSION TAG' -4 68 
9  4QAA ASP I 5 ? UNP P58154 ? ? 'EXPRESSION TAG' -3 69 
9  4QAA ASP I 6 ? UNP P58154 ? ? 'EXPRESSION TAG' -2 70 
9  4QAA ASP I 7 ? UNP P58154 ? ? 'EXPRESSION TAG' -1 71 
9  4QAA LYS I 8 ? UNP P58154 ? ? 'EXPRESSION TAG' 0  72 
10 4QAA ASP J 1 ? UNP P58154 ? ? 'EXPRESSION TAG' -7 73 
10 4QAA TYR J 2 ? UNP P58154 ? ? 'EXPRESSION TAG' -6 74 
10 4QAA LYS J 3 ? UNP P58154 ? ? 'EXPRESSION TAG' -5 75 
10 4QAA ASP J 4 ? UNP P58154 ? ? 'EXPRESSION TAG' -4 76 
10 4QAA ASP J 5 ? UNP P58154 ? ? 'EXPRESSION TAG' -3 77 
10 4QAA ASP J 6 ? UNP P58154 ? ? 'EXPRESSION TAG' -2 78 
10 4QAA ASP J 7 ? UNP P58154 ? ? 'EXPRESSION TAG' -1 79 
10 4QAA LYS J 8 ? UNP P58154 ? ? 'EXPRESSION TAG' 0  80 
# 
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 
KK1 non-polymer         . '6-(4-methoxyphenyl)-N~4~-octylpyrimidine-2,4-diamine' ? 'C19 H28 N4 O'   328.452 
LEU 'L-peptide linking' y LEUCINE                                                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                             ? 'C5 H11 N O2 S'  149.211 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE                                 ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE                                          ? 'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION'                                        ? 'O4 P -3'        94.971  
PRO 'L-peptide linking' y PROLINE                                                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                 ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          4QAA 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.58 
_exptl_crystal.density_percent_sol   52.35 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            290 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
'0.26 M ammonium phosphate monobasic, 35% v/v glycerol,  VAPOR DIFFUSION, HANGING DROP, temperature 290K' 
# 
_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 315r' 
_diffrn_detector.pdbx_collection_date   2013-08-07 
_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                    SI-111 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.2.2' 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.2.2 
_diffrn_source.pdbx_wavelength             1 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4QAA 
_reflns.observed_criterion_sigma_I   -3.000 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.000 
_reflns.d_resolution_high            2.170 
_reflns.number_obs                   ? 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.15300 
_reflns.pdbx_Rsym_value              0.15300 
_reflns.pdbx_netI_over_sigmaI        11.3000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              7.200 
_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         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4QAA 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     68911 
_refine.ls_number_reflns_all                     68911 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.360 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             49.65 
_refine.ls_d_res_high                            2.70 
_refine.ls_percent_reflns_obs                    99.8 
_refine.ls_R_factor_obs                          0.197 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.193 
_refine.ls_R_factor_R_free                       0.262 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.060 
_refine.ls_number_reflns_R_free                  3486 
_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                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.360 
_refine.pdbx_overall_phase_error                 29.750 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        16675 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         451 
_refine_hist.number_atoms_solvent             161 
_refine_hist.number_atoms_total               17287 
_refine_hist.d_res_high                       2.70 
_refine_hist.d_res_low                        49.65 
# 
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 
f_bond_d           0.008  ? ? 17515 'X-RAY DIFFRACTION' ? 
f_angle_d          1.216  ? ? 23827 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 17.822 ? ? 6496  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.080  ? ? 2672  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.005  ? ? 3041  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.number_reflns_obs 
'X-RAY DIFFRACTION' . 2.7000 2.7370  2579 0.2438 100.00 0.3426 . . 139 . . . . 
'X-RAY DIFFRACTION' . 2.7370 2.7761  2649 0.2485 100.00 0.3398 . . 147 . . . . 
'X-RAY DIFFRACTION' . 2.7761 2.8175  2560 0.2433 100.00 0.3244 . . 148 . . . . 
'X-RAY DIFFRACTION' . 2.8175 2.8615  2624 0.2255 100.00 0.3034 . . 134 . . . . 
'X-RAY DIFFRACTION' . 2.8615 2.9084  2588 0.2284 100.00 0.3326 . . 132 . . . . 
'X-RAY DIFFRACTION' . 2.9084 2.9586  2620 0.2312 100.00 0.3262 . . 129 . . . . 
'X-RAY DIFFRACTION' . 2.9586 3.0124  2594 0.2178 100.00 0.3242 . . 138 . . . . 
'X-RAY DIFFRACTION' . 3.0124 3.0703  2629 0.2032 100.00 0.3112 . . 135 . . . . 
'X-RAY DIFFRACTION' . 3.0703 3.1330  2602 0.2167 100.00 0.3041 . . 132 . . . . 
'X-RAY DIFFRACTION' . 3.1330 3.2011  2635 0.2159 100.00 0.3282 . . 132 . . . . 
'X-RAY DIFFRACTION' . 3.2011 3.2755  2569 0.2138 100.00 0.3200 . . 162 . . . . 
'X-RAY DIFFRACTION' . 3.2755 3.3574  2630 0.2089 100.00 0.2734 . . 135 . . . . 
'X-RAY DIFFRACTION' . 3.3574 3.4482  2606 0.1993 100.00 0.3173 . . 136 . . . . 
'X-RAY DIFFRACTION' . 3.4482 3.5496  2607 0.1908 100.00 0.2654 . . 129 . . . . 
'X-RAY DIFFRACTION' . 3.5496 3.6642  2635 0.1815 100.00 0.2277 . . 134 . . . . 
'X-RAY DIFFRACTION' . 3.6642 3.7951  2631 0.1896 100.00 0.2688 . . 151 . . . . 
'X-RAY DIFFRACTION' . 3.7951 3.9470  2608 0.1844 100.00 0.2442 . . 131 . . . . 
'X-RAY DIFFRACTION' . 3.9470 4.1265  2609 0.1867 100.00 0.3010 . . 146 . . . . 
'X-RAY DIFFRACTION' . 4.1265 4.3440  2614 0.1748 100.00 0.2421 . . 157 . . . . 
'X-RAY DIFFRACTION' . 4.3440 4.6159  2627 0.1723 100.00 0.2521 . . 139 . . . . 
'X-RAY DIFFRACTION' . 4.6159 4.9720  2607 0.1616 100.00 0.2067 . . 157 . . . . 
'X-RAY DIFFRACTION' . 4.9720 5.4718  2623 0.1756 100.00 0.2344 . . 136 . . . . 
'X-RAY DIFFRACTION' . 5.4718 6.2623  2633 0.1835 100.00 0.2267 . . 139 . . . . 
'X-RAY DIFFRACTION' . 6.2623 7.8847  2658 0.1911 100.00 0.2434 . . 142 . . . . 
'X-RAY DIFFRACTION' . 7.8847 49.6604 2688 0.1971 99.00  0.2001 . . 126 . . . . 
# 
_struct.entry_id                  4QAA 
_struct.title                     
'X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP) IN COMPLEX WITH 6-(4-Methoxyphenyl)-N4-octylpyrimidine-2,4-diamine' 
_struct.pdbx_descriptor           'Acetylcholine-binding protein' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4QAA 
_struct_keywords.pdbx_keywords   'Acetylcholine-Binding Protein' 
_struct_keywords.text            'Acetylcholine-Binding Protein' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 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 3 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 4 ? 
P  N N 2 ? 
Q  N N 3 ? 
R  N N 4 ? 
S  N N 2 ? 
T  N N 3 ? 
U  N N 4 ? 
V  N N 4 ? 
W  N N 4 ? 
X  N N 2 ? 
Y  N N 3 ? 
Z  N N 4 ? 
AA N N 4 ? 
BA N N 2 ? 
CA N N 3 ? 
DA N N 4 ? 
EA N N 4 ? 
FA N N 4 ? 
GA N N 2 ? 
HA N N 3 ? 
IA N N 4 ? 
JA N N 4 ? 
KA N N 2 ? 
LA N N 3 ? 
MA N N 4 ? 
NA N N 4 ? 
OA N N 2 ? 
PA N N 3 ? 
QA N N 4 ? 
RA N N 4 ? 
SA N N 2 ? 
TA N N 3 ? 
UA N N 2 ? 
VA N N 3 ? 
WA N N 4 ? 
XA N N 5 ? 
YA N N 5 ? 
ZA N N 5 ? 
AB N N 5 ? 
BB N N 5 ? 
CB N N 5 ? 
DB N N 5 ? 
EB N N 5 ? 
FB N N 5 ? 
GB N N 5 ? 
# 
_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  ASP A 7  ? SER A 22 ? ASP A -1 SER A 14 1 ? 16 
HELX_P HELX_P2  2  ARG A 69 ? ALA A 72 ? ARG A 61 ALA A 64 5 ? 4  
HELX_P HELX_P3  3  SER A 87 ? LEU A 89 ? SER A 79 LEU A 81 5 ? 3  
HELX_P HELX_P4  4  ASP B 7  ? SER B 22 ? ASP B -1 SER B 14 1 ? 16 
HELX_P HELX_P5  5  ARG B 69 ? ALA B 72 ? ARG B 61 ALA B 64 5 ? 4  
HELX_P HELX_P6  6  SER B 87 ? LEU B 89 ? SER B 79 LEU B 81 5 ? 3  
HELX_P HELX_P7  7  ASP C 1  ? ASP C 5  ? ASP C -7 ASP C -3 5 ? 5  
HELX_P HELX_P8  8  ASP C 7  ? SER C 22 ? ASP C -1 SER C 14 1 ? 16 
HELX_P HELX_P9  9  ARG C 69 ? ALA C 72 ? ARG C 61 ALA C 64 5 ? 4  
HELX_P HELX_P10 10 SER C 87 ? LEU C 89 ? SER C 79 LEU C 81 5 ? 3  
HELX_P HELX_P11 11 ASP D 1  ? ASP D 5  ? ASP D -7 ASP D -3 5 ? 5  
HELX_P HELX_P12 12 ASP D 7  ? SER D 22 ? ASP D -1 SER D 14 1 ? 16 
HELX_P HELX_P13 13 ARG D 69 ? ALA D 72 ? ARG D 61 ALA D 64 5 ? 4  
HELX_P HELX_P14 14 SER D 87 ? LEU D 89 ? SER D 79 LEU D 81 5 ? 3  
HELX_P HELX_P15 15 ASP E 1  ? ASP E 5  ? ASP E -7 ASP E -3 5 ? 5  
HELX_P HELX_P16 16 ASP E 7  ? SER E 22 ? ASP E -1 SER E 14 1 ? 16 
HELX_P HELX_P17 17 ARG E 69 ? ALA E 72 ? ARG E 61 ALA E 64 5 ? 4  
HELX_P HELX_P18 18 SER E 87 ? LEU E 89 ? SER E 79 LEU E 81 5 ? 3  
HELX_P HELX_P19 19 LYS F 3  ? ASP F 6  ? LYS F -5 ASP F -2 5 ? 4  
HELX_P HELX_P20 20 ASP F 7  ? SER F 22 ? ASP F -1 SER F 14 1 ? 16 
HELX_P HELX_P21 21 ARG F 69 ? ALA F 72 ? ARG F 61 ALA F 64 5 ? 4  
HELX_P HELX_P22 22 PRO F 85 ? LEU F 89 ? PRO F 77 LEU F 81 5 ? 5  
HELX_P HELX_P23 23 ASP G 1  ? ASP G 5  ? ASP G -7 ASP G -3 5 ? 5  
HELX_P HELX_P24 24 ASP G 7  ? SER G 22 ? ASP G -1 SER G 14 1 ? 16 
HELX_P HELX_P25 25 ARG G 69 ? ALA G 72 ? ARG G 61 ALA G 64 5 ? 4  
HELX_P HELX_P26 26 SER G 87 ? LEU G 89 ? SER G 79 LEU G 81 5 ? 3  
HELX_P HELX_P27 27 ASP H 1  ? ASP H 5  ? ASP H -7 ASP H -3 5 ? 5  
HELX_P HELX_P28 28 ASP H 7  ? SER H 22 ? ASP H -1 SER H 14 1 ? 16 
HELX_P HELX_P29 29 ARG H 69 ? ALA H 72 ? ARG H 61 ALA H 64 5 ? 4  
HELX_P HELX_P30 30 SER H 87 ? LEU H 89 ? SER H 79 LEU H 81 5 ? 3  
HELX_P HELX_P31 31 ASP I 1  ? ASP I 5  ? ASP I -7 ASP I -3 5 ? 5  
HELX_P HELX_P32 32 ASP I 7  ? SER I 22 ? ASP I -1 SER I 14 1 ? 16 
HELX_P HELX_P33 33 ARG I 69 ? ALA I 72 ? ARG I 61 ALA I 64 5 ? 4  
HELX_P HELX_P34 34 SER I 87 ? LEU I 89 ? SER I 79 LEU I 81 5 ? 3  
HELX_P HELX_P35 35 ASP J 7  ? SER J 22 ? ASP J -1 SER J 14 1 ? 16 
HELX_P HELX_P36 36 ARG J 69 ? ALA J 72 ? ARG J 61 ALA J 64 5 ? 4  
HELX_P HELX_P37 37 SER J 87 ? LEU J 89 ? SER J 79 LEU J 81 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 131 SG  ? ? ? 1_555 A  CYS 144 SG ? ? A CYS 123 A CYS 136 1_555 ? ? ? ? ? ? ? 2.460 ? 
disulf2  disulf ? ? B CYS 131 SG  ? ? ? 1_555 B  CYS 144 SG ? ? B CYS 123 B CYS 136 1_555 ? ? ? ? ? ? ? 2.265 ? 
disulf3  disulf ? ? C CYS 131 SG  ? ? ? 1_555 C  CYS 144 SG ? ? C CYS 123 C CYS 136 1_555 ? ? ? ? ? ? ? 2.220 ? 
disulf4  disulf ? ? D CYS 131 SG  ? ? ? 1_555 D  CYS 144 SG ? ? D CYS 123 D CYS 136 1_555 ? ? ? ? ? ? ? 2.569 ? 
disulf5  disulf ? ? D CYS 195 SG  ? ? ? 1_555 D  CYS 196 SG ? ? D CYS 187 D CYS 188 1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf6  disulf ? ? E CYS 131 SG  ? ? ? 1_555 E  CYS 144 SG ? ? E CYS 123 E CYS 136 1_555 ? ? ? ? ? ? ? 2.304 ? 
disulf7  disulf ? ? F CYS 131 SG  ? ? ? 1_555 F  CYS 144 SG ? ? F CYS 123 F CYS 136 1_555 ? ? ? ? ? ? ? 2.370 ? 
disulf8  disulf ? ? G CYS 131 SG  ? ? ? 1_555 G  CYS 144 SG ? ? G CYS 123 G CYS 136 1_555 ? ? ? ? ? ? ? 2.419 ? 
disulf9  disulf ? ? H CYS 131 SG  ? ? ? 1_555 H  CYS 144 SG ? ? H CYS 123 H CYS 136 1_555 ? ? ? ? ? ? ? 2.405 ? 
disulf10 disulf ? ? I CYS 131 SG  ? ? ? 1_555 I  CYS 144 SG ? ? I CYS 123 I CYS 136 1_555 ? ? ? ? ? ? ? 2.375 ? 
disulf11 disulf ? ? J CYS 131 SG  ? ? ? 1_555 J  CYS 144 SG ? ? J CYS 123 J CYS 136 1_555 ? ? ? ? ? ? ? 2.466 ? 
covale1  covale ? ? J ASN 74  ND2 ? ? ? 1_555 VA NAG .   C1 ? ? J ASN 66  J NAG 302 1_555 ? ? ? ? ? ? ? 1.361 ? 
covale2  covale ? ? B ASN 74  ND2 ? ? ? 1_555 Q  NAG .   C1 ? ? B ASN 66  B NAG 302 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale3  covale ? ? A ASN 74  ND2 ? ? ? 1_555 L  NAG .   C1 ? ? A ASN 66  A NAG 302 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale4  covale ? ? E ASN 74  ND2 ? ? ? 1_555 CA NAG .   C1 ? ? E ASN 66  E NAG 302 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale5  covale ? ? F ASN 74  ND2 ? ? ? 1_555 HA NAG .   C1 ? ? F ASN 66  F NAG 302 1_555 ? ? ? ? ? ? ? 1.517 ? 
covale6  covale ? ? G ASN 74  ND2 ? ? ? 1_555 LA NAG .   C1 ? ? G ASN 66  G NAG 302 1_555 ? ? ? ? ? ? ? 1.553 ? 
covale7  covale ? ? I ASN 74  ND2 ? ? ? 1_555 TA NAG .   C1 ? ? I ASN 66  I NAG 302 1_555 ? ? ? ? ? ? ? 1.575 ? 
covale8  covale ? ? C ASN 74  ND2 ? ? ? 1_555 T  NAG .   C1 ? ? C ASN 66  C NAG 302 1_555 ? ? ? ? ? ? ? 1.410 ? 
covale9  covale ? ? D ASN 74  ND2 ? ? ? 1_555 Y  NAG .   C1 ? ? D ASN 66  D NAG 302 1_555 ? ? ? ? ? ? ? 1.504 ? 
covale10 covale ? ? H ASN 74  ND2 ? ? ? 1_555 PA NAG .   C1 ? ? H ASN 66  H NAG 302 1_555 ? ? ? ? ? ? ? 1.536 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 THR 163 A . ? THR 155 A THR 164 A ? THR 156 A 1 -3.13 
2 GLU 165 A . ? GLU 157 A ASN 166 A ? ASN 158 A 1 4.64  
3 ASP 168 A . ? ASP 160 A ASP 169 A ? ASP 161 A 1 7.97  
4 ASP 168 D . ? ASP 160 D ASP 169 D ? ASP 161 D 1 -4.52 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A  ? 6 ? 
B  ? 6 ? 
C  ? 4 ? 
D  ? 6 ? 
E  ? 6 ? 
F  ? 4 ? 
G  ? 6 ? 
H  ? 6 ? 
I  ? 5 ? 
J  ? 6 ? 
K  ? 6 ? 
L  ? 4 ? 
M  ? 6 ? 
N  ? 6 ? 
O  ? 4 ? 
P  ? 6 ? 
Q  ? 6 ? 
R  ? 5 ? 
S  ? 6 ? 
T  ? 6 ? 
U  ? 5 ? 
V  ? 6 ? 
W  ? 6 ? 
X  ? 4 ? 
Y  ? 6 ? 
Z  ? 6 ? 
AA ? 4 ? 
AB ? 6 ? 
AC ? 6 ? 
AD ? 5 ? 
# 
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 
A  5 6 ? anti-parallel 
B  1 2 ? anti-parallel 
B  2 3 ? anti-parallel 
B  3 4 ? anti-parallel 
B  4 5 ? anti-parallel 
B  5 6 ? parallel      
C  1 2 ? anti-parallel 
C  2 3 ? anti-parallel 
C  3 4 ? anti-parallel 
D  1 2 ? anti-parallel 
D  2 3 ? anti-parallel 
D  3 4 ? anti-parallel 
D  4 5 ? anti-parallel 
D  5 6 ? anti-parallel 
E  1 2 ? anti-parallel 
E  2 3 ? anti-parallel 
E  3 4 ? anti-parallel 
E  4 5 ? anti-parallel 
E  5 6 ? 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 
G  5 6 ? anti-parallel 
H  1 2 ? anti-parallel 
H  2 3 ? anti-parallel 
H  3 4 ? anti-parallel 
H  4 5 ? anti-parallel 
H  5 6 ? 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 
J  4 5 ? anti-parallel 
J  5 6 ? anti-parallel 
K  1 2 ? anti-parallel 
K  2 3 ? anti-parallel 
K  3 4 ? anti-parallel 
K  4 5 ? anti-parallel 
K  5 6 ? 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 
M  5 6 ? anti-parallel 
N  1 2 ? anti-parallel 
N  2 3 ? anti-parallel 
N  3 4 ? anti-parallel 
N  4 5 ? anti-parallel 
N  5 6 ? parallel      
O  1 2 ? anti-parallel 
O  2 3 ? anti-parallel 
O  3 4 ? anti-parallel 
P  1 2 ? anti-parallel 
P  2 3 ? anti-parallel 
P  3 4 ? anti-parallel 
P  4 5 ? anti-parallel 
P  5 6 ? anti-parallel 
Q  1 2 ? anti-parallel 
Q  2 3 ? anti-parallel 
Q  3 4 ? anti-parallel 
Q  4 5 ? anti-parallel 
Q  5 6 ? 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 
S  4 5 ? anti-parallel 
S  5 6 ? anti-parallel 
T  1 2 ? anti-parallel 
T  2 3 ? anti-parallel 
T  3 4 ? anti-parallel 
T  4 5 ? anti-parallel 
T  5 6 ? parallel      
U  1 2 ? anti-parallel 
U  2 3 ? anti-parallel 
U  3 4 ? anti-parallel 
U  4 5 ? anti-parallel 
V  1 2 ? anti-parallel 
V  2 3 ? anti-parallel 
V  3 4 ? anti-parallel 
V  4 5 ? anti-parallel 
V  5 6 ? anti-parallel 
W  1 2 ? anti-parallel 
W  2 3 ? anti-parallel 
W  3 4 ? anti-parallel 
W  4 5 ? anti-parallel 
W  5 6 ? parallel      
X  1 2 ? anti-parallel 
X  2 3 ? anti-parallel 
X  3 4 ? anti-parallel 
Y  1 2 ? anti-parallel 
Y  2 3 ? anti-parallel 
Y  3 4 ? anti-parallel 
Y  4 5 ? anti-parallel 
Y  5 6 ? anti-parallel 
Z  1 2 ? anti-parallel 
Z  2 3 ? anti-parallel 
Z  3 4 ? anti-parallel 
Z  4 5 ? anti-parallel 
Z  5 6 ? parallel      
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
AB 4 5 ? anti-parallel 
AB 5 6 ? anti-parallel 
AC 1 2 ? anti-parallel 
AC 2 3 ? anti-parallel 
AC 3 4 ? anti-parallel 
AC 4 5 ? anti-parallel 
AC 5 6 ? parallel      
AD 1 2 ? anti-parallel 
AD 2 3 ? anti-parallel 
AD 3 4 ? anti-parallel 
AD 4 5 ? 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 GLN A 81  ? PRO A 85  ? GLN A 73  PRO A 77  
A  2 LEU A 110 ? VAL A 114 ? LEU A 102 VAL A 106 
A  3 GLU A 118 ? TYR A 121 ? GLU A 110 TYR A 113 
A  4 GLU A 55  ? SER A 67  ? GLU A 47  SER A 59  
A  5 SER A 124 ? SER A 130 ? SER A 116 SER A 122 
A  6 GLU A 104 ? VAL A 105 ? GLU A 96  VAL A 97  
B  1 GLN A 81  ? PRO A 85  ? GLN A 73  PRO A 77  
B  2 LEU A 110 ? VAL A 114 ? LEU A 102 VAL A 106 
B  3 GLU A 118 ? TYR A 121 ? GLU A 110 TYR A 113 
B  4 GLU A 55  ? SER A 67  ? GLU A 47  SER A 59  
B  5 VAL A 35  ? ASN A 50  ? VAL A 27  ASN A 42  
B  6 ILE A 158 ? PRO A 162 ? ILE A 150 PRO A 154 
C  1 LEU A 94  ? ALA A 96  ? LEU A 86  ALA A 88  
C  2 ALA A 142 ? SER A 150 ? ALA A 134 SER A 142 
C  3 ASP A 202 ? LYS A 211 ? ASP A 194 LYS A 203 
C  4 PHE A 179 ? ASN A 189 ? PHE A 171 ASN A 181 
D  1 GLN B 81  ? PRO B 85  ? GLN B 73  PRO B 77  
D  2 LEU B 110 ? VAL B 114 ? LEU B 102 VAL B 106 
D  3 GLU B 118 ? TYR B 121 ? GLU B 110 TYR B 113 
D  4 GLU B 55  ? SER B 67  ? GLU B 47  SER B 59  
D  5 SER B 124 ? SER B 130 ? SER B 116 SER B 122 
D  6 GLU B 104 ? VAL B 105 ? GLU B 96  VAL B 97  
E  1 GLN B 81  ? PRO B 85  ? GLN B 73  PRO B 77  
E  2 LEU B 110 ? VAL B 114 ? LEU B 102 VAL B 106 
E  3 GLU B 118 ? TYR B 121 ? GLU B 110 TYR B 113 
E  4 GLU B 55  ? SER B 67  ? GLU B 47  SER B 59  
E  5 VAL B 35  ? ASN B 50  ? VAL B 27  ASN B 42  
E  6 ILE B 158 ? PRO B 162 ? ILE B 150 PRO B 154 
F  1 LEU B 94  ? ALA B 96  ? LEU B 86  ALA B 88  
F  2 ALA B 142 ? SER B 150 ? ALA B 134 SER B 142 
F  3 TYR B 200 ? LYS B 211 ? TYR B 192 LYS B 203 
F  4 PHE B 179 ? VAL B 191 ? PHE B 171 VAL B 183 
G  1 GLN C 81  ? PRO C 85  ? GLN C 73  PRO C 77  
G  2 LEU C 110 ? VAL C 114 ? LEU C 102 VAL C 106 
G  3 GLU C 118 ? TYR C 121 ? GLU C 110 TYR C 113 
G  4 GLU C 55  ? SER C 67  ? GLU C 47  SER C 59  
G  5 SER C 124 ? SER C 130 ? SER C 116 SER C 122 
G  6 GLU C 104 ? VAL C 105 ? GLU C 96  VAL C 97  
H  1 GLN C 81  ? PRO C 85  ? GLN C 73  PRO C 77  
H  2 LEU C 110 ? VAL C 114 ? LEU C 102 VAL C 106 
H  3 GLU C 118 ? TYR C 121 ? GLU C 110 TYR C 113 
H  4 GLU C 55  ? SER C 67  ? GLU C 47  SER C 59  
H  5 VAL C 35  ? ILE C 46  ? VAL C 27  ILE C 38  
H  6 ILE C 158 ? ASP C 161 ? ILE C 150 ASP C 153 
I  1 LEU C 94  ? ALA C 96  ? LEU C 86  ALA C 88  
I  2 ALA C 142 ? SER C 150 ? ALA C 134 SER C 142 
I  3 TYR C 200 ? LYS C 211 ? TYR C 192 LYS C 203 
I  4 PHE C 179 ? VAL C 191 ? PHE C 171 VAL C 183 
I  5 ASN C 166 ? SER C 167 ? ASN C 158 SER C 159 
J  1 GLN D 81  ? PRO D 85  ? GLN D 73  PRO D 77  
J  2 LEU D 110 ? VAL D 114 ? LEU D 102 VAL D 106 
J  3 GLU D 118 ? TYR D 121 ? GLU D 110 TYR D 113 
J  4 GLU D 55  ? SER D 67  ? GLU D 47  SER D 59  
J  5 SER D 124 ? SER D 130 ? SER D 116 SER D 122 
J  6 GLU D 104 ? VAL D 105 ? GLU D 96  VAL D 97  
K  1 GLN D 81  ? PRO D 85  ? GLN D 73  PRO D 77  
K  2 LEU D 110 ? VAL D 114 ? LEU D 102 VAL D 106 
K  3 GLU D 118 ? TYR D 121 ? GLU D 110 TYR D 113 
K  4 GLU D 55  ? SER D 67  ? GLU D 47  SER D 59  
K  5 VAL D 35  ? ASN D 50  ? VAL D 27  ASN D 42  
K  6 ILE D 158 ? PRO D 162 ? ILE D 150 PRO D 154 
L  1 LEU D 94  ? ALA D 96  ? LEU D 86  ALA D 88  
L  2 ALA D 142 ? SER D 150 ? ALA D 134 SER D 142 
L  3 TYR D 200 ? LYS D 211 ? TYR D 192 LYS D 203 
L  4 PHE D 179 ? VAL D 191 ? PHE D 171 VAL D 183 
M  1 GLN E 81  ? PRO E 85  ? GLN E 73  PRO E 77  
M  2 LEU E 110 ? VAL E 114 ? LEU E 102 VAL E 106 
M  3 GLU E 118 ? TYR E 121 ? GLU E 110 TYR E 113 
M  4 GLU E 55  ? SER E 67  ? GLU E 47  SER E 59  
M  5 SER E 124 ? SER E 130 ? SER E 116 SER E 122 
M  6 GLU E 104 ? VAL E 105 ? GLU E 96  VAL E 97  
N  1 GLN E 81  ? PRO E 85  ? GLN E 73  PRO E 77  
N  2 LEU E 110 ? VAL E 114 ? LEU E 102 VAL E 106 
N  3 GLU E 118 ? TYR E 121 ? GLU E 110 TYR E 113 
N  4 GLU E 55  ? SER E 67  ? GLU E 47  SER E 59  
N  5 VAL E 35  ? ASN E 50  ? VAL E 27  ASN E 42  
N  6 ILE E 158 ? ASP E 161 ? ILE E 150 ASP E 153 
O  1 LEU E 94  ? ALA E 96  ? LEU E 86  ALA E 88  
O  2 ALA E 142 ? SER E 150 ? ALA E 134 SER E 142 
O  3 TYR E 200 ? LYS E 211 ? TYR E 192 LYS E 203 
O  4 PHE E 179 ? VAL E 191 ? PHE E 171 VAL E 183 
P  1 GLN F 81  ? VAL F 84  ? GLN F 73  VAL F 76  
P  2 ALA F 111 ? VAL F 114 ? ALA F 103 VAL F 106 
P  3 GLU F 118 ? TYR F 121 ? GLU F 110 TYR F 113 
P  4 GLU F 55  ? SER F 67  ? GLU F 47  SER F 59  
P  5 SER F 124 ? SER F 130 ? SER F 116 SER F 122 
P  6 GLU F 104 ? VAL F 105 ? GLU F 96  VAL F 97  
Q  1 GLN F 81  ? VAL F 84  ? GLN F 73  VAL F 76  
Q  2 ALA F 111 ? VAL F 114 ? ALA F 103 VAL F 106 
Q  3 GLU F 118 ? TYR F 121 ? GLU F 110 TYR F 113 
Q  4 GLU F 55  ? SER F 67  ? GLU F 47  SER F 59  
Q  5 VAL F 35  ? ASN F 50  ? VAL F 27  ASN F 42  
Q  6 ILE F 158 ? ASP F 161 ? ILE F 150 ASP F 153 
R  1 LEU F 94  ? ALA F 96  ? LEU F 86  ALA F 88  
R  2 ALA F 142 ? SER F 150 ? ALA F 134 SER F 142 
R  3 TYR F 200 ? LYS F 211 ? TYR F 192 LYS F 203 
R  4 PHE F 179 ? VAL F 191 ? PHE F 171 VAL F 183 
R  5 ASN F 166 ? SER F 167 ? ASN F 158 SER F 159 
S  1 GLN G 81  ? PRO G 85  ? GLN G 73  PRO G 77  
S  2 LEU G 110 ? VAL G 114 ? LEU G 102 VAL G 106 
S  3 GLU G 118 ? TYR G 121 ? GLU G 110 TYR G 113 
S  4 GLU G 55  ? SER G 67  ? GLU G 47  SER G 59  
S  5 SER G 124 ? SER G 130 ? SER G 116 SER G 122 
S  6 GLU G 104 ? VAL G 105 ? GLU G 96  VAL G 97  
T  1 GLN G 81  ? PRO G 85  ? GLN G 73  PRO G 77  
T  2 LEU G 110 ? VAL G 114 ? LEU G 102 VAL G 106 
T  3 GLU G 118 ? TYR G 121 ? GLU G 110 TYR G 113 
T  4 GLU G 55  ? SER G 67  ? GLU G 47  SER G 59  
T  5 VAL G 35  ? ASN G 50  ? VAL G 27  ASN G 42  
T  6 ILE G 158 ? ASP G 161 ? ILE G 150 ASP G 153 
U  1 LEU G 94  ? ALA G 96  ? LEU G 86  ALA G 88  
U  2 ALA G 142 ? SER G 150 ? ALA G 134 SER G 142 
U  3 TYR G 200 ? LYS G 211 ? TYR G 192 LYS G 203 
U  4 PHE G 179 ? VAL G 191 ? PHE G 171 VAL G 183 
U  5 ASN G 166 ? SER G 167 ? ASN G 158 SER G 159 
V  1 GLN H 81  ? PRO H 85  ? GLN H 73  PRO H 77  
V  2 LEU H 110 ? VAL H 114 ? LEU H 102 VAL H 106 
V  3 GLU H 118 ? TYR H 121 ? GLU H 110 TYR H 113 
V  4 GLU H 55  ? SER H 67  ? GLU H 47  SER H 59  
V  5 SER H 124 ? SER H 130 ? SER H 116 SER H 122 
V  6 GLU H 104 ? VAL H 105 ? GLU H 96  VAL H 97  
W  1 GLN H 81  ? PRO H 85  ? GLN H 73  PRO H 77  
W  2 LEU H 110 ? VAL H 114 ? LEU H 102 VAL H 106 
W  3 GLU H 118 ? TYR H 121 ? GLU H 110 TYR H 113 
W  4 GLU H 55  ? SER H 67  ? GLU H 47  SER H 59  
W  5 VAL H 35  ? ILE H 46  ? VAL H 27  ILE H 38  
W  6 ILE H 158 ? ASP H 161 ? ILE H 150 ASP H 153 
X  1 LEU H 94  ? ALA H 96  ? LEU H 86  ALA H 88  
X  2 ALA H 142 ? SER H 150 ? ALA H 134 SER H 142 
X  3 ALA H 199 ? LYS H 211 ? ALA H 191 LYS H 203 
X  4 PHE H 179 ? THR H 192 ? PHE H 171 THR H 184 
Y  1 GLN I 81  ? PRO I 85  ? GLN I 73  PRO I 77  
Y  2 LEU I 110 ? VAL I 114 ? LEU I 102 VAL I 106 
Y  3 GLU I 118 ? TYR I 121 ? GLU I 110 TYR I 113 
Y  4 GLU I 55  ? SER I 67  ? GLU I 47  SER I 59  
Y  5 SER I 124 ? SER I 130 ? SER I 116 SER I 122 
Y  6 GLU I 104 ? VAL I 105 ? GLU I 96  VAL I 97  
Z  1 GLN I 81  ? PRO I 85  ? GLN I 73  PRO I 77  
Z  2 LEU I 110 ? VAL I 114 ? LEU I 102 VAL I 106 
Z  3 GLU I 118 ? TYR I 121 ? GLU I 110 TYR I 113 
Z  4 GLU I 55  ? SER I 67  ? GLU I 47  SER I 59  
Z  5 VAL I 35  ? ASN I 50  ? VAL I 27  ASN I 42  
Z  6 ILE I 158 ? VAL I 160 ? ILE I 150 VAL I 152 
AA 1 LEU I 94  ? ALA I 96  ? LEU I 86  ALA I 88  
AA 2 ALA I 142 ? SER I 150 ? ALA I 134 SER I 142 
AA 3 ASP I 202 ? LYS I 211 ? ASP I 194 LYS I 203 
AA 4 PHE I 179 ? ASN I 189 ? PHE I 171 ASN I 181 
AB 1 GLN J 81  ? PRO J 85  ? GLN J 73  PRO J 77  
AB 2 LEU J 110 ? VAL J 114 ? LEU J 102 VAL J 106 
AB 3 GLU J 118 ? TYR J 121 ? GLU J 110 TYR J 113 
AB 4 GLU J 55  ? SER J 67  ? GLU J 47  SER J 59  
AB 5 SER J 124 ? SER J 130 ? SER J 116 SER J 122 
AB 6 GLU J 104 ? VAL J 105 ? GLU J 96  VAL J 97  
AC 1 GLN J 81  ? PRO J 85  ? GLN J 73  PRO J 77  
AC 2 LEU J 110 ? VAL J 114 ? LEU J 102 VAL J 106 
AC 3 GLU J 118 ? TYR J 121 ? GLU J 110 TYR J 113 
AC 4 GLU J 55  ? SER J 67  ? GLU J 47  SER J 59  
AC 5 VAL J 35  ? ASN J 50  ? VAL J 27  ASN J 42  
AC 6 ILE J 158 ? PRO J 162 ? ILE J 150 PRO J 154 
AD 1 LEU J 94  ? ALA J 96  ? LEU J 86  ALA J 88  
AD 2 ALA J 142 ? SER J 150 ? ALA J 134 SER J 142 
AD 3 ASP J 202 ? LYS J 211 ? ASP J 194 LYS J 203 
AD 4 PHE J 179 ? ASN J 189 ? PHE J 171 ASN J 181 
AD 5 ASN J 166 ? SER J 167 ? ASN J 158 SER J 159 
# 
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 N VAL A 84  ? N VAL A 76  O ALA A 111 ? O ALA A 103 
A  2 3 N VAL A 114 ? N VAL A 106 O GLU A 118 ? O GLU A 110 
A  3 4 O TYR A 121 ? O TYR A 113 N THR A 64  ? N THR A 56  
A  4 5 N PHE A 60  ? N PHE A 52  O ILE A 125 ? O ILE A 117 
A  5 6 O ARG A 126 ? O ARG A 118 N GLU A 104 ? N GLU A 96  
B  1 2 N VAL A 84  ? N VAL A 76  O ALA A 111 ? O ALA A 103 
B  2 3 N VAL A 114 ? N VAL A 106 O GLU A 118 ? O GLU A 110 
B  3 4 O TYR A 121 ? O TYR A 113 N THR A 64  ? N THR A 56  
B  4 5 O THR A 65  ? O THR A 57  N SER A 38  ? N SER A 30  
B  5 6 N VAL A 37  ? N VAL A 29  O ASP A 161 ? O ASP A 153 
C  1 2 N ALA A 95  ? N ALA A 87  O GLY A 149 ? O GLY A 141 
C  2 3 N ILE A 146 ? N ILE A 138 O VAL A 205 ? O VAL A 197 
C  3 4 O SER A 206 ? O SER A 198 N THR A 185 ? N THR A 177 
D  1 2 N VAL B 84  ? N VAL B 76  O ALA B 111 ? O ALA B 103 
D  2 3 N VAL B 114 ? N VAL B 106 O GLU B 118 ? O GLU B 110 
D  3 4 O VAL B 119 ? O VAL B 111 N TRP B 66  ? N TRP B 58  
D  4 5 N PHE B 60  ? N PHE B 52  O ILE B 125 ? O ILE B 117 
D  5 6 O ARG B 126 ? O ARG B 118 N GLU B 104 ? N GLU B 96  
E  1 2 N VAL B 84  ? N VAL B 76  O ALA B 111 ? O ALA B 103 
E  2 3 N VAL B 114 ? N VAL B 106 O GLU B 118 ? O GLU B 110 
E  3 4 O VAL B 119 ? O VAL B 111 N TRP B 66  ? N TRP B 58  
E  4 5 O VAL B 59  ? O VAL B 51  N ILE B 44  ? N ILE B 36  
E  5 6 N VAL B 35  ? N VAL B 27  O SER B 159 ? O SER B 151 
F  1 2 N ALA B 95  ? N ALA B 87  O GLY B 149 ? O GLY B 141 
F  2 3 N ILE B 146 ? N ILE B 138 O VAL B 205 ? O VAL B 197 
F  3 4 O ASN B 208 ? O ASN B 200 N ASP B 183 ? N ASP B 175 
G  1 2 N VAL C 84  ? N VAL C 76  O ALA C 111 ? O ALA C 103 
G  2 3 N VAL C 114 ? N VAL C 106 O GLU C 118 ? O GLU C 110 
G  3 4 O VAL C 119 ? O VAL C 111 N TRP C 66  ? N TRP C 58  
G  4 5 N PHE C 60  ? N PHE C 52  O ILE C 125 ? O ILE C 117 
G  5 6 O ARG C 126 ? O ARG C 118 N GLU C 104 ? N GLU C 96  
H  1 2 N VAL C 84  ? N VAL C 76  O ALA C 111 ? O ALA C 103 
H  2 3 N VAL C 114 ? N VAL C 106 O GLU C 118 ? O GLU C 110 
H  3 4 O VAL C 119 ? O VAL C 111 N TRP C 66  ? N TRP C 58  
H  4 5 O VAL C 59  ? O VAL C 51  N ILE C 44  ? N ILE C 36  
H  5 6 N VAL C 37  ? N VAL C 29  O SER C 159 ? O SER C 151 
I  1 2 N ALA C 95  ? N ALA C 87  O GLY C 149 ? O GLY C 141 
I  2 3 N CYS C 144 ? N CYS C 136 O LEU C 207 ? O LEU C 199 
I  3 4 O SER C 206 ? O SER C 198 N THR C 185 ? N THR C 177 
I  4 5 O VAL C 184 ? O VAL C 176 N SER C 167 ? N SER C 159 
J  1 2 N VAL D 84  ? N VAL D 76  O ALA D 111 ? O ALA D 103 
J  2 3 N VAL D 114 ? N VAL D 106 O GLU D 118 ? O GLU D 110 
J  3 4 O TYR D 121 ? O TYR D 113 N THR D 64  ? N THR D 56  
J  4 5 N VAL D 56  ? N VAL D 48  O PHE D 129 ? O PHE D 121 
J  5 6 O ARG D 126 ? O ARG D 118 N GLU D 104 ? N GLU D 96  
K  1 2 N VAL D 84  ? N VAL D 76  O ALA D 111 ? O ALA D 103 
K  2 3 N VAL D 114 ? N VAL D 106 O GLU D 118 ? O GLU D 110 
K  3 4 O TYR D 121 ? O TYR D 113 N THR D 64  ? N THR D 56  
K  4 5 O VAL D 59  ? O VAL D 51  N ILE D 44  ? N ILE D 36  
K  5 6 N VAL D 39  ? N VAL D 31  O ASP D 161 ? O ASP D 153 
L  1 2 N ALA D 95  ? N ALA D 87  O GLY D 149 ? O GLY D 141 
L  2 3 N ALA D 142 ? N ALA D 134 O PHE D 209 ? O PHE D 201 
L  3 4 O ASP D 202 ? O ASP D 194 N ASN D 189 ? N ASN D 181 
M  1 2 N VAL E 84  ? N VAL E 76  O ALA E 111 ? O ALA E 103 
M  2 3 N VAL E 114 ? N VAL E 106 O GLU E 118 ? O GLU E 110 
M  3 4 O TYR E 121 ? O TYR E 113 N THR E 64  ? N THR E 56  
M  4 5 N PHE E 60  ? N PHE E 52  O ILE E 125 ? O ILE E 117 
M  5 6 O ARG E 126 ? O ARG E 118 N GLU E 104 ? N GLU E 96  
N  1 2 N VAL E 84  ? N VAL E 76  O ALA E 111 ? O ALA E 103 
N  2 3 N VAL E 114 ? N VAL E 106 O GLU E 118 ? O GLU E 110 
N  3 4 O TYR E 121 ? O TYR E 113 N THR E 64  ? N THR E 56  
N  4 5 O THR E 65  ? O THR E 57  N SER E 38  ? N SER E 30  
N  5 6 N VAL E 35  ? N VAL E 27  O SER E 159 ? O SER E 151 
O  1 2 N ALA E 95  ? N ALA E 87  O GLY E 149 ? O GLY E 141 
O  2 3 N CYS E 144 ? N CYS E 136 O LEU E 207 ? O LEU E 199 
O  3 4 O ASN E 208 ? O ASN E 200 N LEU E 182 ? N LEU E 174 
P  1 2 N VAL F 84  ? N VAL F 76  O ALA F 111 ? O ALA F 103 
P  2 3 N ARG F 112 ? N ARG F 104 O LEU F 120 ? O LEU F 112 
P  3 4 O VAL F 119 ? O VAL F 111 N TRP F 66  ? N TRP F 58  
P  4 5 N PHE F 60  ? N PHE F 52  O ILE F 125 ? O ILE F 117 
P  5 6 O ARG F 126 ? O ARG F 118 N GLU F 104 ? N GLU F 96  
Q  1 2 N VAL F 84  ? N VAL F 76  O ALA F 111 ? O ALA F 103 
Q  2 3 N ARG F 112 ? N ARG F 104 O LEU F 120 ? O LEU F 112 
Q  3 4 O VAL F 119 ? O VAL F 111 N TRP F 66  ? N TRP F 58  
Q  4 5 O THR F 65  ? O THR F 57  N SER F 38  ? N SER F 30  
Q  5 6 N VAL F 35  ? N VAL F 27  O SER F 159 ? O SER F 151 
R  1 2 N ALA F 95  ? N ALA F 87  O GLY F 149 ? O GLY F 141 
R  2 3 N ILE F 146 ? N ILE F 138 O VAL F 205 ? O VAL F 197 
R  3 4 O GLU F 204 ? O GLU F 196 N LYS F 187 ? N LYS F 179 
R  4 5 O VAL F 184 ? O VAL F 176 N SER F 167 ? N SER F 159 
S  1 2 N VAL G 82  ? N VAL G 74  O VAL G 113 ? O VAL G 105 
S  2 3 N VAL G 114 ? N VAL G 106 O GLU G 118 ? O GLU G 110 
S  3 4 O TYR G 121 ? O TYR G 113 N THR G 64  ? N THR G 56  
S  4 5 N PHE G 60  ? N PHE G 52  O ILE G 125 ? O ILE G 117 
S  5 6 O ARG G 126 ? O ARG G 118 N GLU G 104 ? N GLU G 96  
T  1 2 N VAL G 82  ? N VAL G 74  O VAL G 113 ? O VAL G 105 
T  2 3 N VAL G 114 ? N VAL G 106 O GLU G 118 ? O GLU G 110 
T  3 4 O TYR G 121 ? O TYR G 113 N THR G 64  ? N THR G 56  
T  4 5 O ASP G 57  ? O ASP G 49  N LEU G 47  ? N LEU G 39  
T  5 6 N VAL G 35  ? N VAL G 27  O SER G 159 ? O SER G 151 
U  1 2 N ALA G 95  ? N ALA G 87  O GLY G 149 ? O GLY G 141 
U  2 3 N CYS G 144 ? N CYS G 136 O LEU G 207 ? O LEU G 199 
U  3 4 O SER G 206 ? O SER G 198 N THR G 185 ? N THR G 177 
U  4 5 O VAL G 184 ? O VAL G 176 N SER G 167 ? N SER G 159 
V  1 2 N VAL H 84  ? N VAL H 76  O ALA H 111 ? O ALA H 103 
V  2 3 N VAL H 114 ? N VAL H 106 O GLU H 118 ? O GLU H 110 
V  3 4 O VAL H 119 ? O VAL H 111 N TRP H 66  ? N TRP H 58  
V  4 5 N PHE H 60  ? N PHE H 52  O ILE H 125 ? O ILE H 117 
V  5 6 O ARG H 126 ? O ARG H 118 N GLU H 104 ? N GLU H 96  
W  1 2 N VAL H 84  ? N VAL H 76  O ALA H 111 ? O ALA H 103 
W  2 3 N VAL H 114 ? N VAL H 106 O GLU H 118 ? O GLU H 110 
W  3 4 O VAL H 119 ? O VAL H 111 N TRP H 66  ? N TRP H 58  
W  4 5 O THR H 65  ? O THR H 57  N SER H 38  ? N SER H 30  
W  5 6 N VAL H 35  ? N VAL H 27  O SER H 159 ? O SER H 151 
X  1 2 N ALA H 95  ? N ALA H 87  O GLY H 149 ? O GLY H 141 
X  2 3 N ILE H 148 ? N ILE H 140 O VAL H 203 ? O VAL H 195 
X  3 4 O GLU H 204 ? O GLU H 196 N LYS H 187 ? N LYS H 179 
Y  1 2 N VAL I 84  ? N VAL I 76  O ALA I 111 ? O ALA I 103 
Y  2 3 N VAL I 114 ? N VAL I 106 O GLU I 118 ? O GLU I 110 
Y  3 4 O VAL I 119 ? O VAL I 111 N TRP I 66  ? N TRP I 58  
Y  4 5 N VAL I 56  ? N VAL I 48  O PHE I 129 ? O PHE I 121 
Y  5 6 O ARG I 126 ? O ARG I 118 N GLU I 104 ? N GLU I 96  
Z  1 2 N VAL I 84  ? N VAL I 76  O ALA I 111 ? O ALA I 103 
Z  2 3 N VAL I 114 ? N VAL I 106 O GLU I 118 ? O GLU I 110 
Z  3 4 O VAL I 119 ? O VAL I 111 N TRP I 66  ? N TRP I 58  
Z  4 5 O VAL I 59  ? O VAL I 51  N ILE I 44  ? N ILE I 36  
Z  5 6 N VAL I 35  ? N VAL I 27  O SER I 159 ? O SER I 151 
AA 1 2 N ALA I 95  ? N ALA I 87  O GLY I 149 ? O GLY I 141 
AA 2 3 N ILE I 146 ? N ILE I 138 O VAL I 205 ? O VAL I 197 
AA 3 4 O ASN I 208 ? O ASN I 200 N LEU I 182 ? N LEU I 174 
AB 1 2 N VAL J 84  ? N VAL J 76  O ALA J 111 ? O ALA J 103 
AB 2 3 N VAL J 114 ? N VAL J 106 O GLU J 118 ? O GLU J 110 
AB 3 4 O VAL J 119 ? O VAL J 111 N TRP J 66  ? N TRP J 58  
AB 4 5 N PHE J 60  ? N PHE J 52  O ILE J 125 ? O ILE J 117 
AB 5 6 O ARG J 126 ? O ARG J 118 N GLU J 104 ? N GLU J 96  
AC 1 2 N VAL J 84  ? N VAL J 76  O ALA J 111 ? O ALA J 103 
AC 2 3 N VAL J 114 ? N VAL J 106 O GLU J 118 ? O GLU J 110 
AC 3 4 O VAL J 119 ? O VAL J 111 N TRP J 66  ? N TRP J 58  
AC 4 5 O THR J 65  ? O THR J 57  N SER J 38  ? N SER J 30  
AC 5 6 N VAL J 39  ? N VAL J 31  O ASP J 161 ? O ASP J 153 
AD 1 2 N ALA J 95  ? N ALA J 87  O GLY J 149 ? O GLY J 141 
AD 2 3 N CYS J 144 ? N CYS J 136 O LEU J 207 ? O LEU J 199 
AD 3 4 O SER J 206 ? O SER J 198 N THR J 185 ? N THR J 177 
AD 4 5 O VAL J 184 ? O VAL J 176 N SER J 167 ? N SER J 159 
# 
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 ? ? ? ? 8  'BINDING SITE FOR RESIDUE KK1 A 301' 
AC2 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG A 302' 
AC3 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE PO4 A 303' 
AC4 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE PO4 A 304' 
AC5 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE PO4 A 305' 
AC6 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE KK1 B 301' 
AC7 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG B 302' 
AC8 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE PO4 B 303' 
AC9 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE KK1 C 301' 
BC1 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG C 302' 
BC2 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE PO4 C 303' 
BC3 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE PO4 C 304' 
BC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE PO4 C 305' 
BC5 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE KK1 D 301' 
BC6 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG D 302' 
BC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE PO4 D 303' 
BC8 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE KK1 E 301' 
BC9 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG E 302' 
CC1 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE PO4 E 303' 
CC2 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE PO4 E 304' 
CC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE PO4 E 305' 
CC4 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE KK1 F 301' 
CC5 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG F 302' 
CC6 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE PO4 F 303' 
CC7 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE PO4 F 304' 
CC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE KK1 G 301' 
CC9 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG G 302' 
DC1 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE PO4 G 303' 
DC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE PO4 G 304' 
DC3 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE KK1 H 301' 
DC4 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG H 302' 
DC5 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE PO4 H 303' 
DC6 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE PO4 H 304' 
DC7 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE KK1 I 301' 
DC8 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE NAG I 302' 
DC9 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE KK1 J 301' 
EC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG J 302' 
EC2 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE PO4 J 303' 
# 
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 8  TYR A  97  ? TYR A 89  . ? 1_555 ? 
2   AC1 8  LYS A  147 ? LYS A 139 . ? 1_555 ? 
3   AC1 8  SER A  150 ? SER A 142 . ? 1_555 ? 
4   AC1 8  TRP A  151 ? TRP A 143 . ? 1_555 ? 
5   AC1 8  TYR A  200 ? TYR A 192 . ? 1_555 ? 
6   AC1 8  TRP B  61  ? TRP B 53  . ? 1_555 ? 
7   AC1 8  LEU B  110 ? LEU B 102 . ? 1_555 ? 
8   AC1 8  LEU B  120 ? LEU B 112 . ? 1_555 ? 
9   AC2 3  ASN A  74  ? ASN A 66  . ? 1_555 ? 
10  AC2 3  SER A  76  ? SER A 68  . ? 1_555 ? 
11  AC2 3  ASP I  4   ? ASP I -4  . ? 1_555 ? 
12  AC3 7  ASP A  25  ? ASP A 17  . ? 1_555 ? 
13  AC3 7  VAL A  26  ? VAL A 18  . ? 1_555 ? 
14  AC3 7  ILE A  27  ? ILE A 19  . ? 1_555 ? 
15  AC3 7  HIS A  153 ? HIS A 145 . ? 1_555 ? 
16  AC3 7  ARG B  11  ? ARG B 3   . ? 1_555 ? 
17  AC3 7  VAL B  82  ? VAL B 74  . ? 1_555 ? 
18  AC3 7  SER B  83  ? SER B 75  . ? 1_555 ? 
19  AC4 7  ARG A  11  ? ARG A 3   . ? 1_555 ? 
20  AC4 7  VAL A  82  ? VAL A 74  . ? 1_555 ? 
21  AC4 7  SER A  83  ? SER A 75  . ? 1_555 ? 
22  AC4 7  ASP E  25  ? ASP E 17  . ? 1_555 ? 
23  AC4 7  VAL E  26  ? VAL E 18  . ? 1_555 ? 
24  AC4 7  ILE E  27  ? ILE E 19  . ? 1_555 ? 
25  AC4 7  HIS E  153 ? HIS E 145 . ? 1_555 ? 
26  AC5 3  VAL A  49  ? VAL A 41  . ? 1_555 ? 
27  AC5 3  GLU A  51  ? GLU A 43  . ? 1_555 ? 
28  AC5 3  HOH XA .   ? HOH A 407 . ? 1_555 ? 
29  AC6 9  TYR B  97  ? TYR B 89  . ? 1_555 ? 
30  AC6 9  LYS B  147 ? LYS B 139 . ? 1_555 ? 
31  AC6 9  SER B  150 ? SER B 142 . ? 1_555 ? 
32  AC6 9  TRP B  151 ? TRP B 143 . ? 1_555 ? 
33  AC6 9  VAL B  191 ? VAL B 183 . ? 1_555 ? 
34  AC6 9  TYR B  200 ? TYR B 192 . ? 1_555 ? 
35  AC6 9  TRP C  61  ? TRP C 53  . ? 1_555 ? 
36  AC6 9  LEU C  120 ? LEU C 112 . ? 1_555 ? 
37  AC6 9  MET C  122 ? MET C 114 . ? 1_555 ? 
38  AC7 2  ASN B  74  ? ASN B 66  . ? 1_555 ? 
39  AC7 2  SER B  76  ? SER B 68  . ? 1_555 ? 
40  AC8 7  ILE B  14  ? ILE B 6   . ? 1_555 ? 
41  AC8 7  ASN B  17  ? ASN B 9   . ? 1_555 ? 
42  AC8 7  ASN B  74  ? ASN B 66  . ? 1_555 ? 
43  AC8 7  SER B  78  ? SER B 70  . ? 1_555 ? 
44  AC8 7  LEU H  9   ? LEU H 1   . ? 1_555 ? 
45  AC8 7  ASP H  10  ? ASP H 2   . ? 1_555 ? 
46  AC8 7  ASP H  13  ? ASP H 5   . ? 1_555 ? 
47  AC9 9  TYR C  97  ? TYR C 89  . ? 1_555 ? 
48  AC9 9  SER C  150 ? SER C 142 . ? 1_555 ? 
49  AC9 9  TRP C  151 ? TRP C 143 . ? 1_555 ? 
50  AC9 9  TYR C  200 ? TYR C 192 . ? 1_555 ? 
51  AC9 9  ILE D  44  ? ILE D 36  . ? 1_555 ? 
52  AC9 9  TRP D  61  ? TRP D 53  . ? 1_555 ? 
53  AC9 9  LEU D  120 ? LEU D 112 . ? 1_555 ? 
54  AC9 9  TYR D  172 ? TYR D 164 . ? 1_555 ? 
55  AC9 9  SER D  174 ? SER D 166 . ? 1_555 ? 
56  BC1 6  ASN C  74  ? ASN C 66  . ? 1_555 ? 
57  BC1 6  SER C  76  ? SER C 68  . ? 1_555 ? 
58  BC1 6  HIS C  77  ? HIS C 69  . ? 1_555 ? 
59  BC1 6  SER I  167 ? SER I 159 . ? 1_455 ? 
60  BC1 6  ASP I  168 ? ASP I 160 . ? 1_455 ? 
61  BC1 6  VAL I  184 ? VAL I 176 . ? 1_455 ? 
62  BC2 7  ASP B  25  ? ASP B 17  . ? 1_555 ? 
63  BC2 7  VAL B  26  ? VAL B 18  . ? 1_555 ? 
64  BC2 7  ILE B  27  ? ILE B 19  . ? 1_555 ? 
65  BC2 7  HIS B  153 ? HIS B 145 . ? 1_555 ? 
66  BC2 7  ARG C  11  ? ARG C 3   . ? 1_555 ? 
67  BC2 7  VAL C  82  ? VAL C 74  . ? 1_555 ? 
68  BC2 7  SER C  83  ? SER C 75  . ? 1_555 ? 
69  BC3 7  ASP C  25  ? ASP C 17  . ? 1_555 ? 
70  BC3 7  VAL C  26  ? VAL C 18  . ? 1_555 ? 
71  BC3 7  ILE C  27  ? ILE C 19  . ? 1_555 ? 
72  BC3 7  HIS C  153 ? HIS C 145 . ? 1_555 ? 
73  BC3 7  ARG D  11  ? ARG D 3   . ? 1_555 ? 
74  BC3 7  VAL D  82  ? VAL D 74  . ? 1_555 ? 
75  BC3 7  SER D  83  ? SER D 75  . ? 1_555 ? 
76  BC4 4  VAL C  49  ? VAL C 41  . ? 1_555 ? 
77  BC4 4  VAL C  136 ? VAL C 128 . ? 1_555 ? 
78  BC4 4  ASP C  137 ? ASP C 129 . ? 1_555 ? 
79  BC4 4  ARG C  178 ? ARG C 170 . ? 1_555 ? 
80  BC5 11 TYR D  97  ? TYR D 89  . ? 1_555 ? 
81  BC5 11 SER D  150 ? SER D 142 . ? 1_555 ? 
82  BC5 11 TRP D  151 ? TRP D 143 . ? 1_555 ? 
83  BC5 11 TYR D  193 ? TYR D 185 . ? 1_555 ? 
84  BC5 11 CYS D  196 ? CYS D 188 . ? 1_555 ? 
85  BC5 11 TYR D  200 ? TYR D 192 . ? 1_555 ? 
86  BC5 11 TRP E  61  ? TRP E 53  . ? 1_555 ? 
87  BC5 11 ARG E  112 ? ARG E 104 . ? 1_555 ? 
88  BC5 11 LEU E  120 ? LEU E 112 . ? 1_555 ? 
89  BC5 11 TYR E  172 ? TYR E 164 . ? 1_555 ? 
90  BC5 11 SER E  174 ? SER E 166 . ? 1_555 ? 
91  BC6 2  ASN D  74  ? ASN D 66  . ? 1_555 ? 
92  BC6 2  SER D  76  ? SER D 68  . ? 1_555 ? 
93  BC7 4  VAL D  49  ? VAL D 41  . ? 1_555 ? 
94  BC7 4  HOH AB .   ? HOH D 417 . ? 1_555 ? 
95  BC7 4  HOH AB .   ? HOH D 418 . ? 1_555 ? 
96  BC7 4  HOH AB .   ? HOH D 420 . ? 1_555 ? 
97  BC8 9  TRP A  61  ? TRP A 53  . ? 1_555 ? 
98  BC8 9  LEU A  120 ? LEU A 112 . ? 1_555 ? 
99  BC8 9  MET A  122 ? MET A 114 . ? 1_555 ? 
100 BC8 9  TYR E  97  ? TYR E 89  . ? 1_555 ? 
101 BC8 9  LYS E  147 ? LYS E 139 . ? 1_555 ? 
102 BC8 9  SER E  150 ? SER E 142 . ? 1_555 ? 
103 BC8 9  TRP E  151 ? TRP E 143 . ? 1_555 ? 
104 BC8 9  VAL E  191 ? VAL E 183 . ? 1_555 ? 
105 BC8 9  TYR E  200 ? TYR E 192 . ? 1_555 ? 
106 BC9 3  ASN E  74  ? ASN E 66  . ? 1_555 ? 
107 BC9 3  SER E  76  ? SER E 68  . ? 1_555 ? 
108 BC9 3  HIS J  77  ? HIS J 69  . ? 1_555 ? 
109 CC1 6  ASP D  25  ? ASP D 17  . ? 1_555 ? 
110 CC1 6  VAL D  26  ? VAL D 18  . ? 1_555 ? 
111 CC1 6  ILE D  27  ? ILE D 19  . ? 1_555 ? 
112 CC1 6  HIS D  153 ? HIS D 145 . ? 1_555 ? 
113 CC1 6  ARG E  11  ? ARG E 3   . ? 1_555 ? 
114 CC1 6  SER E  83  ? SER E 75  . ? 1_555 ? 
115 CC2 2  GLU E  48  ? GLU E 40  . ? 1_555 ? 
116 CC2 2  ARG E  128 ? ARG E 120 . ? 1_555 ? 
117 CC3 4  SER D  194 ? SER D 186 . ? 1_555 ? 
118 CC3 4  LYS E  42  ? LYS E 34  . ? 1_555 ? 
119 CC3 4  SER E  167 ? SER E 159 . ? 1_555 ? 
120 CC3 4  TYR E  172 ? TYR E 164 . ? 1_555 ? 
121 CC4 11 TYR F  97  ? TYR F 89  . ? 1_555 ? 
122 CC4 11 LYS F  147 ? LYS F 139 . ? 1_555 ? 
123 CC4 11 SER F  150 ? SER F 142 . ? 1_555 ? 
124 CC4 11 TRP F  151 ? TRP F 143 . ? 1_555 ? 
125 CC4 11 ASN F  189 ? ASN F 181 . ? 1_555 ? 
126 CC4 11 VAL F  191 ? VAL F 183 . ? 1_555 ? 
127 CC4 11 TYR F  200 ? TYR F 192 . ? 1_555 ? 
128 CC4 11 TRP G  61  ? TRP G 53  . ? 1_555 ? 
129 CC4 11 LEU G  120 ? LEU G 112 . ? 1_555 ? 
130 CC4 11 MET G  122 ? MET G 114 . ? 1_555 ? 
131 CC4 11 TYR G  172 ? TYR G 164 . ? 1_555 ? 
132 CC5 2  ASN F  74  ? ASN F 66  . ? 1_555 ? 
133 CC5 2  HIS F  77  ? HIS F 69  . ? 1_555 ? 
134 CC6 6  ARG F  11  ? ARG F 3   . ? 1_555 ? 
135 CC6 6  VAL F  82  ? VAL F 74  . ? 1_555 ? 
136 CC6 6  SER F  83  ? SER F 75  . ? 1_555 ? 
137 CC6 6  ASP J  25  ? ASP J 17  . ? 1_555 ? 
138 CC6 6  ILE J  27  ? ILE J 19  . ? 1_555 ? 
139 CC6 6  HIS J  153 ? HIS J 145 . ? 1_555 ? 
140 CC7 6  ASP D  10  ? ASP D 2   . ? 1_555 ? 
141 CC7 6  ASP D  13  ? ASP D 5   . ? 1_555 ? 
142 CC7 6  ASP F  10  ? ASP F 2   . ? 1_555 ? 
143 CC7 6  ASN F  17  ? ASN F 9   . ? 1_555 ? 
144 CC7 6  ASN F  74  ? ASN F 66  . ? 1_555 ? 
145 CC7 6  SER F  78  ? SER F 70  . ? 1_555 ? 
146 CC8 5  TYR G  97  ? TYR G 89  . ? 1_555 ? 
147 CC8 5  SER G  150 ? SER G 142 . ? 1_555 ? 
148 CC8 5  TRP G  151 ? TRP G 143 . ? 1_555 ? 
149 CC8 5  TYR G  200 ? TYR G 192 . ? 1_555 ? 
150 CC8 5  LEU H  120 ? LEU H 112 . ? 1_555 ? 
151 CC9 4  LYS C  3   ? LYS C -5  . ? 1_555 ? 
152 CC9 4  ASP C  4   ? ASP C -4  . ? 1_555 ? 
153 CC9 4  ASN G  74  ? ASN G 66  . ? 1_555 ? 
154 CC9 4  SER G  76  ? SER G 68  . ? 1_555 ? 
155 DC1 7  ASP F  25  ? ASP F 17  . ? 1_555 ? 
156 DC1 7  VAL F  26  ? VAL F 18  . ? 1_555 ? 
157 DC1 7  ILE F  27  ? ILE F 19  . ? 1_555 ? 
158 DC1 7  HIS F  153 ? HIS F 145 . ? 1_555 ? 
159 DC1 7  ARG G  11  ? ARG G 3   . ? 1_555 ? 
160 DC1 7  VAL G  82  ? VAL G 74  . ? 1_555 ? 
161 DC1 7  SER G  83  ? SER G 75  . ? 1_555 ? 
162 DC2 6  LEU C  9   ? LEU C 1   . ? 1_555 ? 
163 DC2 6  ASP C  10  ? ASP C 2   . ? 1_555 ? 
164 DC2 6  ASP C  13  ? ASP C 5   . ? 1_555 ? 
165 DC2 6  ILE G  14  ? ILE G 6   . ? 1_555 ? 
166 DC2 6  ASN G  74  ? ASN G 66  . ? 1_555 ? 
167 DC2 6  SER G  78  ? SER G 70  . ? 1_555 ? 
168 DC3 6  TYR H  97  ? TYR H 89  . ? 1_555 ? 
169 DC3 6  SER H  150 ? SER H 142 . ? 1_555 ? 
170 DC3 6  TRP H  151 ? TRP H 143 . ? 1_555 ? 
171 DC3 6  TYR H  200 ? TYR H 192 . ? 1_555 ? 
172 DC3 6  ARG I  112 ? ARG I 104 . ? 1_555 ? 
173 DC3 6  LEU I  120 ? LEU I 112 . ? 1_555 ? 
174 DC4 3  ASP B  4   ? ASP B -4  . ? 1_555 ? 
175 DC4 3  ASN H  74  ? ASN H 66  . ? 1_555 ? 
176 DC4 3  SER H  76  ? SER H 68  . ? 1_555 ? 
177 DC5 7  ASP G  25  ? ASP G 17  . ? 1_555 ? 
178 DC5 7  VAL G  26  ? VAL G 18  . ? 1_555 ? 
179 DC5 7  ILE G  27  ? ILE G 19  . ? 1_555 ? 
180 DC5 7  HIS G  153 ? HIS G 145 . ? 1_555 ? 
181 DC5 7  ARG H  11  ? ARG H 3   . ? 1_555 ? 
182 DC5 7  VAL H  82  ? VAL H 74  . ? 1_555 ? 
183 DC5 7  SER H  83  ? SER H 75  . ? 1_555 ? 
184 DC6 7  ASP H  25  ? ASP H 17  . ? 1_555 ? 
185 DC6 7  VAL H  26  ? VAL H 18  . ? 1_555 ? 
186 DC6 7  ILE H  27  ? ILE H 19  . ? 1_555 ? 
187 DC6 7  HIS H  153 ? HIS H 145 . ? 1_555 ? 
188 DC6 7  ARG I  11  ? ARG I 3   . ? 1_555 ? 
189 DC6 7  VAL I  82  ? VAL I 74  . ? 1_555 ? 
190 DC6 7  SER I  83  ? SER I 75  . ? 1_555 ? 
191 DC7 9  TYR I  97  ? TYR I 89  . ? 1_555 ? 
192 DC7 9  LYS I  147 ? LYS I 139 . ? 1_555 ? 
193 DC7 9  SER I  150 ? SER I 142 . ? 1_555 ? 
194 DC7 9  TRP I  151 ? TRP I 143 . ? 1_555 ? 
195 DC7 9  VAL I  191 ? VAL I 183 . ? 1_555 ? 
196 DC7 9  TYR I  200 ? TYR I 192 . ? 1_555 ? 
197 DC7 9  TRP J  61  ? TRP J 53  . ? 1_555 ? 
198 DC7 9  ARG J  112 ? ARG J 104 . ? 1_555 ? 
199 DC7 9  LEU J  120 ? LEU J 112 . ? 1_555 ? 
200 DC8 3  GLU C  171 ? GLU C 163 . ? 1_655 ? 
201 DC8 3  ASN I  74  ? ASN I 66  . ? 1_555 ? 
202 DC8 3  SER I  76  ? SER I 68  . ? 1_555 ? 
203 DC9 8  LEU F  120 ? LEU F 112 . ? 1_555 ? 
204 DC9 8  TYR F  121 ? TYR F 113 . ? 1_555 ? 
205 DC9 8  MET F  122 ? MET F 114 . ? 1_555 ? 
206 DC9 8  HOH CB .   ? HOH F 405 . ? 1_555 ? 
207 DC9 8  TYR J  97  ? TYR J 89  . ? 1_555 ? 
208 DC9 8  SER J  150 ? SER J 142 . ? 1_555 ? 
209 DC9 8  TRP J  151 ? TRP J 143 . ? 1_555 ? 
210 DC9 8  TYR J  200 ? TYR J 192 . ? 1_555 ? 
211 EC1 5  ASP E  4   ? ASP E -4  . ? 1_555 ? 
212 EC1 5  HIS E  77  ? HIS E 69  . ? 1_555 ? 
213 EC1 5  ASN J  74  ? ASN J 66  . ? 1_555 ? 
214 EC1 5  SER J  76  ? SER J 68  . ? 1_555 ? 
215 EC1 5  HIS J  77  ? HIS J 69  . ? 1_555 ? 
216 EC2 7  ASP I  25  ? ASP I 17  . ? 1_555 ? 
217 EC2 7  VAL I  26  ? VAL I 18  . ? 1_555 ? 
218 EC2 7  ILE I  27  ? ILE I 19  . ? 1_555 ? 
219 EC2 7  HIS I  153 ? HIS I 145 . ? 1_555 ? 
220 EC2 7  ARG J  11  ? ARG J 3   . ? 1_555 ? 
221 EC2 7  VAL J  82  ? VAL J 74  . ? 1_555 ? 
222 EC2 7  SER J  83  ? SER J 75  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4QAA 
_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                    4QAA 
_atom_sites.fract_transf_matrix[1][1]   0.011988 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003485 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007696 
_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]   0.008484 
_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 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . ASP A  1 1   ? 35.609  0.910   50.852  1.00 47.16  ? -7  ASP A N   1 
ATOM   2     C CA  . ASP A  1 1   ? 35.707  0.532   52.257  1.00 55.53  ? -7  ASP A CA  1 
ATOM   3     C C   . ASP A  1 1   ? 35.286  1.681   53.167  1.00 58.21  ? -7  ASP A C   1 
ATOM   4     O O   . ASP A  1 1   ? 34.540  2.570   52.756  1.00 56.66  ? -7  ASP A O   1 
ATOM   5     C CB  . ASP A  1 1   ? 37.132  0.089   52.594  1.00 58.97  ? -7  ASP A CB  1 
ATOM   6     C CG  . ASP A  1 1   ? 38.184  0.918   51.884  1.00 57.92  ? -7  ASP A CG  1 
ATOM   7     O OD1 . ASP A  1 1   ? 39.296  1.067   52.432  1.00 55.47  ? -7  ASP A OD1 1 
ATOM   8     O OD2 . ASP A  1 1   ? 37.898  1.421   50.777  1.00 56.55  ? -7  ASP A OD2 1 
ATOM   9     N N   . TYR A  1 2   ? 35.768  1.656   54.405  1.00 60.19  ? -6  TYR A N   1 
ATOM   10    C CA  . TYR A  1 2   ? 35.441  2.697   55.378  1.00 59.44  ? -6  TYR A CA  1 
ATOM   11    C C   . TYR A  1 2   ? 36.164  4.038   55.146  1.00 54.15  ? -6  TYR A C   1 
ATOM   12    O O   . TYR A  1 2   ? 35.646  5.099   55.496  1.00 53.07  ? -6  TYR A O   1 
ATOM   13    C CB  . TYR A  1 2   ? 35.713  2.170   56.796  1.00 67.69  ? -6  TYR A CB  1 
ATOM   14    C CG  . TYR A  1 2   ? 34.818  1.012   57.206  1.00 71.28  ? -6  TYR A CG  1 
ATOM   15    C CD1 . TYR A  1 2   ? 33.594  1.237   57.834  1.00 81.93  ? -6  TYR A CD1 1 
ATOM   16    C CD2 . TYR A  1 2   ? 35.196  -0.306  56.963  1.00 74.54  ? -6  TYR A CD2 1 
ATOM   17    C CE1 . TYR A  1 2   ? 32.769  0.178   58.210  1.00 86.39  ? -6  TYR A CE1 1 
ATOM   18    C CE2 . TYR A  1 2   ? 34.380  -1.370  57.334  1.00 79.13  ? -6  TYR A CE2 1 
ATOM   19    C CZ  . TYR A  1 2   ? 33.170  -1.123  57.958  1.00 82.82  ? -6  TYR A CZ  1 
ATOM   20    O OH  . TYR A  1 2   ? 32.363  -2.179  58.327  1.00 73.48  ? -6  TYR A OH  1 
ATOM   21    N N   . LYS A  1 3   ? 37.353  3.985   54.549  1.00 57.74  ? -5  LYS A N   1 
ATOM   22    C CA  . LYS A  1 3   ? 38.175  5.179   54.340  1.00 49.98  ? -5  LYS A CA  1 
ATOM   23    C C   . LYS A  1 3   ? 37.716  6.037   53.157  1.00 45.92  ? -5  LYS A C   1 
ATOM   24    O O   . LYS A  1 3   ? 37.997  7.237   53.098  1.00 39.59  ? -5  LYS A O   1 
ATOM   25    C CB  . LYS A  1 3   ? 39.646  4.780   54.180  1.00 44.56  ? -5  LYS A CB  1 
ATOM   26    C CG  . LYS A  1 3   ? 40.264  4.258   55.468  1.00 53.45  ? -5  LYS A CG  1 
ATOM   27    C CD  . LYS A  1 3   ? 41.649  3.653   55.273  1.00 42.07  ? -5  LYS A CD  1 
ATOM   28    C CE  . LYS A  1 3   ? 42.214  3.215   56.619  1.00 37.05  ? -5  LYS A CE  1 
ATOM   29    N NZ  . LYS A  1 3   ? 43.264  2.169   56.512  1.00 38.06  ? -5  LYS A NZ  1 
ATOM   30    N N   . ASP A  1 4   ? 37.011  5.416   52.219  1.00 46.48  ? -4  ASP A N   1 
ATOM   31    C CA  . ASP A  1 4   ? 36.495  6.115   51.046  1.00 46.03  ? -4  ASP A CA  1 
ATOM   32    C C   . ASP A  1 4   ? 34.981  6.336   51.172  1.00 48.07  ? -4  ASP A C   1 
ATOM   33    O O   . ASP A  1 4   ? 34.297  6.604   50.179  1.00 46.49  ? -4  ASP A O   1 
ATOM   34    C CB  . ASP A  1 4   ? 36.822  5.333   49.760  1.00 46.29  ? -4  ASP A CB  1 
ATOM   35    C CG  . ASP A  1 4   ? 38.290  5.480   49.321  1.00 56.87  ? -4  ASP A CG  1 
ATOM   36    O OD1 . ASP A  1 4   ? 38.838  6.607   49.390  1.00 57.87  ? -4  ASP A OD1 1 
ATOM   37    O OD2 . ASP A  1 4   ? 38.892  4.465   48.891  1.00 56.98  ? -4  ASP A OD2 1 
ATOM   38    N N   . ASP A  1 5   ? 34.467  6.215   52.396  1.00 44.54  ? -3  ASP A N   1 
ATOM   39    C CA  . ASP A  1 5   ? 33.045  6.412   52.683  1.00 44.13  ? -3  ASP A CA  1 
ATOM   40    C C   . ASP A  1 5   ? 32.587  7.846   52.395  1.00 42.10  ? -3  ASP A C   1 
ATOM   41    O O   . ASP A  1 5   ? 31.478  8.068   51.900  1.00 36.09  ? -3  ASP A O   1 
ATOM   42    C CB  . ASP A  1 5   ? 32.739  6.069   54.150  1.00 50.68  ? -3  ASP A CB  1 
ATOM   43    C CG  . ASP A  1 5   ? 31.808  4.874   54.296  1.00 49.85  ? -3  ASP A CG  1 
ATOM   44    O OD1 . ASP A  1 5   ? 31.872  3.958   53.443  1.00 46.13  ? -3  ASP A OD1 1 
ATOM   45    O OD2 . ASP A  1 5   ? 31.019  4.853   55.266  1.00 43.68  ? -3  ASP A OD2 1 
ATOM   46    N N   . ASP A  1 6   ? 33.447  8.813   52.704  1.00 36.90  ? -2  ASP A N   1 
ATOM   47    C CA  . ASP A  1 6   ? 33.104  10.227  52.559  1.00 36.85  ? -2  ASP A CA  1 
ATOM   48    C C   . ASP A  1 6   ? 33.567  10.845  51.226  1.00 34.90  ? -2  ASP A C   1 
ATOM   49    O O   . ASP A  1 6   ? 33.706  12.069  51.109  1.00 31.04  ? -2  ASP A O   1 
ATOM   50    C CB  . ASP A  1 6   ? 33.645  11.044  53.748  1.00 38.61  ? -2  ASP A CB  1 
ATOM   51    C CG  . ASP A  1 6   ? 32.983  10.677  55.071  1.00 38.68  ? -2  ASP A CG  1 
ATOM   52    O OD1 . ASP A  1 6   ? 32.372  9.591   55.170  1.00 38.38  ? -2  ASP A OD1 1 
ATOM   53    O OD2 . ASP A  1 6   ? 33.089  11.481  56.021  1.00 41.79  ? -2  ASP A OD2 1 
ATOM   54    N N   . ASP A  1 7   ? 33.805  10.008  50.222  1.00 35.01  ? -1  ASP A N   1 
ATOM   55    C CA  . ASP A  1 7   ? 34.132  10.528  48.903  1.00 32.10  ? -1  ASP A CA  1 
ATOM   56    C C   . ASP A  1 7   ? 32.854  10.955  48.170  1.00 27.39  ? -1  ASP A C   1 
ATOM   57    O O   . ASP A  1 7   ? 32.050  10.111  47.771  1.00 23.69  ? -1  ASP A O   1 
ATOM   58    C CB  . ASP A  1 7   ? 34.908  9.502   48.081  1.00 31.34  ? -1  ASP A CB  1 
ATOM   59    C CG  . ASP A  1 7   ? 35.486  10.106  46.812  1.00 33.77  ? -1  ASP A CG  1 
ATOM   60    O OD1 . ASP A  1 7   ? 35.250  9.540   45.727  1.00 37.45  ? -1  ASP A OD1 1 
ATOM   61    O OD2 . ASP A  1 7   ? 36.159  11.161  46.898  1.00 35.41  ? -1  ASP A OD2 1 
ATOM   62    N N   . LYS A  1 8   ? 32.674  12.260  47.988  1.00 21.96  ? 0   LYS A N   1 
ATOM   63    C CA  . LYS A  1 8   ? 31.388  12.774  47.533  1.00 19.20  ? 0   LYS A CA  1 
ATOM   64    C C   . LYS A  1 8   ? 30.964  12.266  46.160  1.00 23.14  ? 0   LYS A C   1 
ATOM   65    O O   . LYS A  1 8   ? 29.812  11.862  45.976  1.00 18.88  ? 0   LYS A O   1 
ATOM   66    C CB  . LYS A  1 8   ? 31.363  14.297  47.552  1.00 19.84  ? 0   LYS A CB  1 
ATOM   67    C CG  . LYS A  1 8   ? 30.023  14.852  47.121  1.00 19.30  ? 0   LYS A CG  1 
ATOM   68    C CD  . LYS A  1 8   ? 29.964  16.365  47.235  1.00 19.12  ? 0   LYS A CD  1 
ATOM   69    C CE  . LYS A  1 8   ? 28.612  16.887  46.782  1.00 16.36  ? 0   LYS A CE  1 
ATOM   70    N NZ  . LYS A  1 8   ? 28.157  17.965  47.699  1.00 27.48  ? 0   LYS A NZ  1 
ATOM   71    N N   . LEU A  1 9   ? 31.893  12.290  45.204  1.00 23.52  ? 1   LEU A N   1 
ATOM   72    C CA  . LEU A  1 9   ? 31.605  11.896  43.826  1.00 17.99  ? 1   LEU A CA  1 
ATOM   73    C C   . LEU A  1 9   ? 31.344  10.390  43.688  1.00 21.32  ? 1   LEU A C   1 
ATOM   74    O O   . LEU A  1 9   ? 30.534  9.961   42.858  1.00 19.51  ? 1   LEU A O   1 
ATOM   75    C CB  . LEU A  1 9   ? 32.745  12.344  42.906  1.00 24.97  ? 1   LEU A CB  1 
ATOM   76    C CG  . LEU A  1 9   ? 32.717  11.991  41.417  1.00 20.69  ? 1   LEU A CG  1 
ATOM   77    C CD1 . LEU A  1 9   ? 31.612  12.750  40.701  1.00 19.72  ? 1   LEU A CD1 1 
ATOM   78    C CD2 . LEU A  1 9   ? 34.076  12.282  40.804  1.00 17.68  ? 1   LEU A CD2 1 
ATOM   79    N N   . ASP A  1 10  ? 32.030  9.586   44.496  1.00 22.75  ? 2   ASP A N   1 
ATOM   80    C CA  . ASP A  1 10  ? 31.755  8.152   44.533  1.00 23.59  ? 2   ASP A CA  1 
ATOM   81    C C   . ASP A  1 10  ? 30.331  7.868   45.030  1.00 21.16  ? 2   ASP A C   1 
ATOM   82    O O   . ASP A  1 10  ? 29.693  6.899   44.606  1.00 19.30  ? 2   ASP A O   1 
ATOM   83    C CB  . ASP A  1 10  ? 32.794  7.406   45.386  1.00 33.00  ? 2   ASP A CB  1 
ATOM   84    C CG  . ASP A  1 10  ? 34.068  7.056   44.600  1.00 37.86  ? 2   ASP A CG  1 
ATOM   85    O OD1 . ASP A  1 10  ? 34.002  7.014   43.349  1.00 37.69  ? 2   ASP A OD1 1 
ATOM   86    O OD2 . ASP A  1 10  ? 35.128  6.820   45.234  1.00 33.34  ? 2   ASP A OD2 1 
ATOM   87    N N   . ARG A  1 11  ? 29.837  8.725   45.921  1.00 20.03  ? 3   ARG A N   1 
ATOM   88    C CA  . ARG A  1 11  ? 28.468  8.623   46.412  1.00 17.23  ? 3   ARG A CA  1 
ATOM   89    C C   . ARG A  1 11  ? 27.442  9.013   45.329  1.00 16.79  ? 3   ARG A C   1 
ATOM   90    O O   . ARG A  1 11  ? 26.456  8.294   45.100  1.00 13.16  ? 3   ARG A O   1 
ATOM   91    C CB  . ARG A  1 11  ? 28.284  9.471   47.679  1.00 18.56  ? 3   ARG A CB  1 
ATOM   92    C CG  . ARG A  1 11  ? 29.036  8.956   48.906  1.00 18.11  ? 3   ARG A CG  1 
ATOM   93    C CD  . ARG A  1 11  ? 28.787  9.801   50.148  1.00 16.24  ? 3   ARG A CD  1 
ATOM   94    N NE  . ARG A  1 11  ? 27.564  9.403   50.832  1.00 15.43  ? 3   ARG A NE  1 
ATOM   95    C CZ  . ARG A  1 11  ? 27.505  8.547   51.848  1.00 17.01  ? 3   ARG A CZ  1 
ATOM   96    N NH1 . ARG A  1 11  ? 28.602  7.995   52.335  1.00 22.27  ? 3   ARG A NH1 1 
ATOM   97    N NH2 . ARG A  1 11  ? 26.335  8.248   52.387  1.00 22.11  ? 3   ARG A NH2 1 
ATOM   98    N N   . ALA A  1 12  ? 27.686  10.143  44.666  1.00 14.65  ? 4   ALA A N   1 
ATOM   99    C CA  . ALA A  1 12  ? 26.822  10.603  43.584  1.00 16.41  ? 4   ALA A CA  1 
ATOM   100   C C   . ALA A  1 12  ? 26.635  9.521   42.527  1.00 16.49  ? 4   ALA A C   1 
ATOM   101   O O   . ALA A  1 12  ? 25.531  9.335   42.015  1.00 15.88  ? 4   ALA A O   1 
ATOM   102   C CB  . ALA A  1 12  ? 27.381  11.865  42.952  1.00 18.05  ? 4   ALA A CB  1 
ATOM   103   N N   . ASP A  1 13  ? 27.711  8.792   42.234  1.00 14.94  ? 5   ASP A N   1 
ATOM   104   C CA  . ASP A  1 13  ? 27.693  7.761   41.199  1.00 14.98  ? 5   ASP A CA  1 
ATOM   105   C C   . ASP A  1 13  ? 26.947  6.496   41.593  1.00 14.98  ? 5   ASP A C   1 
ATOM   106   O O   . ASP A  1 13  ? 26.240  5.907   40.772  1.00 13.42  ? 5   ASP A O   1 
ATOM   107   C CB  . ASP A  1 13  ? 29.111  7.421   40.753  1.00 14.26  ? 5   ASP A CB  1 
ATOM   108   C CG  . ASP A  1 13  ? 29.770  8.568   40.026  1.00 18.48  ? 5   ASP A CG  1 
ATOM   109   O OD1 . ASP A  1 13  ? 29.053  9.485   39.566  1.00 21.86  ? 5   ASP A OD1 1 
ATOM   110   O OD2 . ASP A  1 13  ? 31.003  8.563   39.912  1.00 23.17  ? 5   ASP A OD2 1 
ATOM   111   N N   . ILE A  1 14  ? 27.110  6.071   42.841  1.00 14.24  ? 6   ILE A N   1 
ATOM   112   C CA  . ILE A  1 14  ? 26.317  4.959   43.356  1.00 13.49  ? 6   ILE A CA  1 
ATOM   113   C C   . ILE A  1 14  ? 24.809  5.285   43.296  1.00 12.98  ? 6   ILE A C   1 
ATOM   114   O O   . ILE A  1 14  ? 24.018  4.485   42.793  1.00 10.93  ? 6   ILE A O   1 
ATOM   115   C CB  . ILE A  1 14  ? 26.774  4.561   44.778  1.00 21.26  ? 6   ILE A CB  1 
ATOM   116   C CG1 . ILE A  1 14  ? 28.178  3.939   44.710  1.00 19.47  ? 6   ILE A CG1 1 
ATOM   117   C CG2 . ILE A  1 14  ? 25.746  3.625   45.468  1.00 15.92  ? 6   ILE A CG2 1 
ATOM   118   C CD1 . ILE A  1 14  ? 29.036  4.177   45.947  1.00 20.34  ? 6   ILE A CD1 1 
ATOM   119   N N   . LEU A  1 15  ? 24.423  6.470   43.767  1.00 11.83  ? 7   LEU A N   1 
ATOM   120   C CA  . LEU A  1 15  ? 23.039  6.926   43.651  1.00 10.82  ? 7   LEU A CA  1 
ATOM   121   C C   . LEU A  1 15  ? 22.531  6.824   42.214  1.00 13.20  ? 7   LEU A C   1 
ATOM   122   O O   . LEU A  1 15  ? 21.480  6.221   41.951  1.00 10.94  ? 7   LEU A O   1 
ATOM   123   C CB  . LEU A  1 15  ? 22.921  8.366   44.120  1.00 12.42  ? 7   LEU A CB  1 
ATOM   124   C CG  . LEU A  1 15  ? 21.492  8.792   44.418  1.00 18.65  ? 7   LEU A CG  1 
ATOM   125   C CD1 . LEU A  1 15  ? 20.989  8.075   45.656  1.00 14.16  ? 7   LEU A CD1 1 
ATOM   126   C CD2 . LEU A  1 15  ? 21.426  10.298  44.591  1.00 20.00  ? 7   LEU A CD2 1 
ATOM   127   N N   . TYR A  1 16  ? 23.299  7.412   41.290  1.00 15.83  ? 8   TYR A N   1 
ATOM   128   C CA  . TYR A  1 16  ? 23.039  7.316   39.858  1.00 10.78  ? 8   TYR A CA  1 
ATOM   129   C C   . TYR A  1 16  ? 22.917  5.865   39.401  1.00 12.34  ? 8   TYR A C   1 
ATOM   130   O O   . TYR A  1 16  ? 21.976  5.510   38.682  1.00 13.19  ? 8   TYR A O   1 
ATOM   131   C CB  . TYR A  1 16  ? 24.135  8.027   39.071  1.00 12.71  ? 8   TYR A CB  1 
ATOM   132   C CG  . TYR A  1 16  ? 24.109  7.765   37.576  1.00 15.17  ? 8   TYR A CG  1 
ATOM   133   C CD1 . TYR A  1 16  ? 23.116  8.297   36.771  1.00 12.23  ? 8   TYR A CD1 1 
ATOM   134   C CD2 . TYR A  1 16  ? 25.090  6.991   36.975  1.00 15.86  ? 8   TYR A CD2 1 
ATOM   135   C CE1 . TYR A  1 16  ? 23.095  8.063   35.422  1.00 15.78  ? 8   TYR A CE1 1 
ATOM   136   C CE2 . TYR A  1 16  ? 25.091  6.767   35.621  1.00 17.46  ? 8   TYR A CE2 1 
ATOM   137   C CZ  . TYR A  1 16  ? 24.091  7.296   34.839  1.00 20.13  ? 8   TYR A CZ  1 
ATOM   138   O OH  . TYR A  1 16  ? 24.093  7.046   33.469  1.00 16.30  ? 8   TYR A OH  1 
ATOM   139   N N   . ASN A  1 17  ? 23.852  5.024   39.829  1.00 9.78   ? 9   ASN A N   1 
ATOM   140   C CA  . ASN A  1 17  ? 23.779  3.612   39.493  1.00 9.60   ? 9   ASN A CA  1 
ATOM   141   C C   . ASN A  1 17  ? 22.497  2.980   40.002  1.00 11.77  ? 9   ASN A C   1 
ATOM   142   O O   . ASN A  1 17  ? 21.781  2.340   39.231  1.00 10.43  ? 9   ASN A O   1 
ATOM   143   C CB  . ASN A  1 17  ? 25.027  2.853   39.974  1.00 11.27  ? 9   ASN A CB  1 
ATOM   144   C CG  . ASN A  1 17  ? 26.283  3.268   39.219  1.00 11.55  ? 9   ASN A CG  1 
ATOM   145   O OD1 . ASN A  1 17  ? 26.197  3.910   38.174  1.00 17.04  ? 9   ASN A OD1 1 
ATOM   146   N ND2 . ASN A  1 17  ? 27.442  2.918   39.741  1.00 11.14  ? 9   ASN A ND2 1 
ATOM   147   N N   . ILE A  1 18  ? 22.198  3.189   41.291  1.00 12.32  ? 10  ILE A N   1 
ATOM   148   C CA  . ILE A  1 18  ? 20.969  2.687   41.897  1.00 9.06   ? 10  ILE A CA  1 
ATOM   149   C C   . ILE A  1 18  ? 19.756  3.175   41.107  1.00 11.44  ? 10  ILE A C   1 
ATOM   150   O O   . ILE A  1 18  ? 18.871  2.400   40.746  1.00 12.64  ? 10  ILE A O   1 
ATOM   151   C CB  . ILE A  1 18  ? 20.844  3.111   43.393  1.00 13.80  ? 10  ILE A CB  1 
ATOM   152   C CG1 . ILE A  1 18  ? 21.758  2.261   44.278  1.00 11.07  ? 10  ILE A CG1 1 
ATOM   153   C CG2 . ILE A  1 18  ? 19.376  3.034   43.893  1.00 9.72   ? 10  ILE A CG2 1 
ATOM   154   C CD1 . ILE A  1 18  ? 22.263  2.995   45.491  1.00 8.74   ? 10  ILE A CD1 1 
ATOM   155   N N   . ARG A  1 19  ? 19.711  4.461   40.810  1.00 9.92   ? 11  ARG A N   1 
ATOM   156   C CA  . ARG A  1 19  ? 18.528  4.986   40.142  1.00 12.71  ? 11  ARG A CA  1 
ATOM   157   C C   . ARG A  1 19  ? 18.339  4.453   38.721  1.00 14.26  ? 11  ARG A C   1 
ATOM   158   O O   . ARG A  1 19  ? 17.227  4.417   38.190  1.00 14.31  ? 11  ARG A O   1 
ATOM   159   C CB  . ARG A  1 19  ? 18.536  6.507   40.184  1.00 13.43  ? 11  ARG A CB  1 
ATOM   160   C CG  . ARG A  1 19  ? 18.301  7.053   41.581  1.00 12.81  ? 11  ARG A CG  1 
ATOM   161   C CD  . ARG A  1 19  ? 18.469  8.539   41.587  1.00 13.97  ? 11  ARG A CD  1 
ATOM   162   N NE  . ARG A  1 19  ? 17.887  9.110   42.787  1.00 23.09  ? 11  ARG A NE  1 
ATOM   163   C CZ  . ARG A  1 19  ? 18.137  10.339  43.221  1.00 19.30  ? 11  ARG A CZ  1 
ATOM   164   N NH1 . ARG A  1 19  ? 18.973  11.118  42.548  1.00 17.95  ? 11  ARG A NH1 1 
ATOM   165   N NH2 . ARG A  1 19  ? 17.553  10.778  44.328  1.00 17.39  ? 11  ARG A NH2 1 
ATOM   166   N N   . GLN A  1 20  ? 19.433  4.013   38.113  1.00 18.33  ? 12  GLN A N   1 
ATOM   167   C CA  . GLN A  1 20  ? 19.374  3.471   36.768  1.00 13.32  ? 12  GLN A CA  1 
ATOM   168   C C   . GLN A  1 20  ? 18.959  2.012   36.760  1.00 13.85  ? 12  GLN A C   1 
ATOM   169   O O   . GLN A  1 20  ? 18.345  1.535   35.811  1.00 15.52  ? 12  GLN A O   1 
ATOM   170   C CB  . GLN A  1 20  ? 20.719  3.634   36.109  1.00 11.77  ? 12  GLN A CB  1 
ATOM   171   C CG  . GLN A  1 20  ? 20.982  5.048   35.692  1.00 15.25  ? 12  GLN A CG  1 
ATOM   172   C CD  . GLN A  1 20  ? 21.536  5.091   34.308  1.00 23.00  ? 12  GLN A CD  1 
ATOM   173   O OE1 . GLN A  1 20  ? 22.214  4.160   33.871  1.00 29.78  ? 12  GLN A OE1 1 
ATOM   174   N NE2 . GLN A  1 20  ? 21.238  6.156   33.589  1.00 36.34  ? 12  GLN A NE2 1 
ATOM   175   N N   . THR A  1 21  ? 19.281  1.309   37.836  1.00 12.05  ? 13  THR A N   1 
ATOM   176   C CA  . THR A  1 21  ? 18.984  -0.109  37.925  1.00 17.26  ? 13  THR A CA  1 
ATOM   177   C C   . THR A  1 21  ? 17.669  -0.399  38.669  1.00 14.39  ? 13  THR A C   1 
ATOM   178   O O   . THR A  1 21  ? 16.904  -1.286  38.266  1.00 14.13  ? 13  THR A O   1 
ATOM   179   C CB  . THR A  1 21  ? 20.188  -0.878  38.536  1.00 19.53  ? 13  THR A CB  1 
ATOM   180   O OG1 . THR A  1 21  ? 21.276  -0.831  37.608  1.00 23.39  ? 13  THR A OG1 1 
ATOM   181   C CG2 . THR A  1 21  ? 19.855  -2.337  38.813  1.00 17.97  ? 13  THR A CG2 1 
ATOM   182   N N   . SER A  1 22  ? 17.405  0.365   39.727  1.00 14.76  ? 14  SER A N   1 
ATOM   183   C CA  . SER A  1 22  ? 16.236  0.140   40.580  1.00 12.36  ? 14  SER A CA  1 
ATOM   184   C C   . SER A  1 22  ? 14.939  0.215   39.783  1.00 14.21  ? 14  SER A C   1 
ATOM   185   O O   . SER A  1 22  ? 14.791  1.064   38.899  1.00 17.04  ? 14  SER A O   1 
ATOM   186   C CB  . SER A  1 22  ? 16.219  1.136   41.743  1.00 11.73  ? 14  SER A CB  1 
ATOM   187   O OG  . SER A  1 22  ? 14.905  1.600   42.017  1.00 12.09  ? 14  SER A OG  1 
ATOM   188   N N   . ARG A  1 23  ? 14.033  -0.719  40.057  1.00 11.99  ? 15  ARG A N   1 
ATOM   189   C CA  . ARG A  1 23  ? 12.698  -0.702  39.482  1.00 10.19  ? 15  ARG A CA  1 
ATOM   190   C C   . ARG A  1 23  ? 11.738  -0.543  40.653  1.00 13.47  ? 15  ARG A C   1 
ATOM   191   O O   . ARG A  1 23  ? 11.344  -1.533  41.260  1.00 13.45  ? 15  ARG A O   1 
ATOM   192   C CB  . ARG A  1 23  ? 12.398  -2.015  38.758  1.00 10.39  ? 15  ARG A CB  1 
ATOM   193   C CG  . ARG A  1 23  ? 13.357  -2.381  37.612  1.00 14.93  ? 15  ARG A CG  1 
ATOM   194   C CD  . ARG A  1 23  ? 12.782  -3.535  36.758  1.00 17.89  ? 15  ARG A CD  1 
ATOM   195   N NE  . ARG A  1 23  ? 13.570  -3.820  35.558  1.00 33.72  ? 15  ARG A NE  1 
ATOM   196   C CZ  . ARG A  1 23  ? 13.328  -3.331  34.337  1.00 31.17  ? 15  ARG A CZ  1 
ATOM   197   N NH1 . ARG A  1 23  ? 12.301  -2.510  34.119  1.00 24.42  ? 15  ARG A NH1 1 
ATOM   198   N NH2 . ARG A  1 23  ? 14.127  -3.667  33.326  1.00 34.38  ? 15  ARG A NH2 1 
ATOM   199   N N   . PRO A  1 24  ? 11.358  0.702   40.983  1.00 12.90  ? 16  PRO A N   1 
ATOM   200   C CA  . PRO A  1 24  ? 10.577  0.969   42.197  1.00 11.16  ? 16  PRO A CA  1 
ATOM   201   C C   . PRO A  1 24  ? 9.209   0.282   42.307  1.00 8.56   ? 16  PRO A C   1 
ATOM   202   O O   . PRO A  1 24  ? 8.699   0.207   43.410  1.00 11.39  ? 16  PRO A O   1 
ATOM   203   C CB  . PRO A  1 24  ? 10.412  2.495   42.172  1.00 11.51  ? 16  PRO A CB  1 
ATOM   204   C CG  . PRO A  1 24  ? 11.557  2.976   41.380  1.00 11.15  ? 16  PRO A CG  1 
ATOM   205   C CD  . PRO A  1 24  ? 11.754  1.949   40.309  1.00 10.43  ? 16  PRO A CD  1 
ATOM   206   N N   . ASP A  1 25  ? 8.639   -0.210  41.217  1.00 8.82   ? 17  ASP A N   1 
ATOM   207   C CA  . ASP A  1 25  ? 7.292   -0.789  41.245  1.00 8.39   ? 17  ASP A CA  1 
ATOM   208   C C   . ASP A  1 25  ? 7.284   -2.305  40.996  1.00 11.99  ? 17  ASP A C   1 
ATOM   209   O O   . ASP A  1 25  ? 6.226   -2.943  40.935  1.00 12.95  ? 17  ASP A O   1 
ATOM   210   C CB  . ASP A  1 25  ? 6.405   -0.103  40.205  1.00 8.07   ? 17  ASP A CB  1 
ATOM   211   C CG  . ASP A  1 25  ? 6.274   1.388   40.446  1.00 13.11  ? 17  ASP A CG  1 
ATOM   212   O OD1 . ASP A  1 25  ? 6.258   1.813   41.618  1.00 16.84  ? 17  ASP A OD1 1 
ATOM   213   O OD2 . ASP A  1 25  ? 6.196   2.150   39.464  1.00 19.47  ? 17  ASP A OD2 1 
ATOM   214   N N   . VAL A  1 26  ? 8.465   -2.887  40.844  1.00 9.61   ? 18  VAL A N   1 
ATOM   215   C CA  . VAL A  1 26  ? 8.558   -4.313  40.589  1.00 12.44  ? 18  VAL A CA  1 
ATOM   216   C C   . VAL A  1 26  ? 9.189   -5.015  41.777  1.00 7.13   ? 18  VAL A C   1 
ATOM   217   O O   . VAL A  1 26  ? 10.209  -4.566  42.270  1.00 7.89   ? 18  VAL A O   1 
ATOM   218   C CB  . VAL A  1 26  ? 9.374   -4.589  39.293  1.00 10.82  ? 18  VAL A CB  1 
ATOM   219   C CG1 . VAL A  1 26  ? 9.407   -6.088  38.976  1.00 9.74   ? 18  VAL A CG1 1 
ATOM   220   C CG2 . VAL A  1 26  ? 8.779   -3.803  38.162  1.00 7.35   ? 18  VAL A CG2 1 
ATOM   221   N N   . ILE A  1 27  ? 8.579   -6.097  42.252  1.00 7.53   ? 19  ILE A N   1 
ATOM   222   C CA  . ILE A  1 27  ? 9.198   -6.853  43.336  1.00 10.98  ? 19  ILE A CA  1 
ATOM   223   C C   . ILE A  1 27  ? 10.560  -7.404  42.903  1.00 14.27  ? 19  ILE A C   1 
ATOM   224   O O   . ILE A  1 27  ? 10.706  -7.947  41.802  1.00 14.64  ? 19  ILE A O   1 
ATOM   225   C CB  . ILE A  1 27  ? 8.289   -7.971  43.886  1.00 13.95  ? 19  ILE A CB  1 
ATOM   226   C CG1 . ILE A  1 27  ? 7.893   -8.958  42.785  1.00 11.62  ? 19  ILE A CG1 1 
ATOM   227   C CG2 . ILE A  1 27  ? 7.059   -7.357  44.605  1.00 11.71  ? 19  ILE A CG2 1 
ATOM   228   C CD1 . ILE A  1 27  ? 6.886   -10.009 43.221  1.00 12.21  ? 19  ILE A CD1 1 
ATOM   229   N N   . PRO A  1 28  ? 11.575  -7.226  43.761  1.00 14.48  ? 20  PRO A N   1 
ATOM   230   C CA  . PRO A  1 28  ? 12.963  -7.611  43.489  1.00 10.63  ? 20  PRO A CA  1 
ATOM   231   C C   . PRO A  1 28  ? 13.152  -9.102  43.651  1.00 12.64  ? 20  PRO A C   1 
ATOM   232   O O   . PRO A  1 28  ? 14.067  -9.539  44.328  1.00 18.97  ? 20  PRO A O   1 
ATOM   233   C CB  . PRO A  1 28  ? 13.747  -6.870  44.578  1.00 12.60  ? 20  PRO A CB  1 
ATOM   234   C CG  . PRO A  1 28  ? 12.787  -6.757  45.716  1.00 9.15   ? 20  PRO A CG  1 
ATOM   235   C CD  . PRO A  1 28  ? 11.417  -6.605  45.092  1.00 10.46  ? 20  PRO A CD  1 
ATOM   236   N N   . THR A  1 29  ? 12.288  -9.872  43.018  1.00 16.87  ? 21  THR A N   1 
ATOM   237   C CA  . THR A  1 29  ? 12.312  -11.321 43.118  1.00 22.85  ? 21  THR A CA  1 
ATOM   238   C C   . THR A  1 29  ? 13.512  -11.923 42.373  1.00 29.70  ? 21  THR A C   1 
ATOM   239   O O   . THR A  1 29  ? 13.619  -11.858 41.144  1.00 32.02  ? 21  THR A O   1 
ATOM   240   C CB  . THR A  1 29  ? 10.976  -11.919 42.619  1.00 23.99  ? 21  THR A CB  1 
ATOM   241   O OG1 . THR A  1 29  ? 11.070  -13.342 42.588  1.00 39.49  ? 21  THR A OG1 1 
ATOM   242   C CG2 . THR A  1 29  ? 10.644  -11.415 41.226  1.00 22.27  ? 21  THR A CG2 1 
ATOM   243   N N   . GLN A  1 30  ? 14.423  -12.502 43.140  1.00 32.56  ? 22  GLN A N   1 
ATOM   244   C CA  . GLN A  1 30  ? 15.653  -13.054 42.594  1.00 39.05  ? 22  GLN A CA  1 
ATOM   245   C C   . GLN A  1 30  ? 15.552  -14.575 42.494  1.00 45.06  ? 22  GLN A C   1 
ATOM   246   O O   . GLN A  1 30  ? 15.087  -15.226 43.426  1.00 36.43  ? 22  GLN A O   1 
ATOM   247   C CB  . GLN A  1 30  ? 16.823  -12.662 43.501  1.00 36.92  ? 22  GLN A CB  1 
ATOM   248   C CG  . GLN A  1 30  ? 16.871  -11.167 43.808  1.00 33.37  ? 22  GLN A CG  1 
ATOM   249   C CD  . GLN A  1 30  ? 17.738  -10.825 45.013  1.00 36.14  ? 22  GLN A CD  1 
ATOM   250   O OE1 . GLN A  1 30  ? 18.504  -9.857  44.989  1.00 38.47  ? 22  GLN A OE1 1 
ATOM   251   N NE2 . GLN A  1 30  ? 17.612  -11.611 46.076  1.00 36.92  ? 22  GLN A NE2 1 
ATOM   252   N N   . ARG A  1 31  ? 15.970  -15.132 41.357  1.00 49.48  ? 23  ARG A N   1 
ATOM   253   C CA  . ARG A  1 31  ? 16.062  -16.589 41.172  1.00 55.40  ? 23  ARG A CA  1 
ATOM   254   C C   . ARG A  1 31  ? 14.768  -17.366 41.396  1.00 52.41  ? 23  ARG A C   1 
ATOM   255   O O   . ARG A  1 31  ? 14.817  -18.495 41.891  1.00 48.87  ? 23  ARG A O   1 
ATOM   256   C CB  . ARG A  1 31  ? 17.089  -17.197 42.129  1.00 53.25  ? 23  ARG A CB  1 
ATOM   257   C CG  . ARG A  1 31  ? 18.410  -16.499 42.221  1.00 62.32  ? 23  ARG A CG  1 
ATOM   258   C CD  . ARG A  1 31  ? 19.271  -17.220 43.246  1.00 64.96  ? 23  ARG A CD  1 
ATOM   259   N NE  . ARG A  1 31  ? 20.553  -17.634 42.683  1.00 69.30  ? 23  ARG A NE  1 
ATOM   260   C CZ  . ARG A  1 31  ? 20.709  -18.657 41.849  1.00 66.94  ? 23  ARG A CZ  1 
ATOM   261   N NH1 . ARG A  1 31  ? 19.660  -19.376 41.471  1.00 72.10  ? 23  ARG A NH1 1 
ATOM   262   N NH2 . ARG A  1 31  ? 21.916  -18.959 41.392  1.00 69.73  ? 23  ARG A NH2 1 
ATOM   263   N N   . ASP A  1 32  ? 13.625  -16.786 41.056  1.00 46.14  ? 24  ASP A N   1 
ATOM   264   C CA  . ASP A  1 32  ? 12.349  -17.431 41.369  1.00 48.16  ? 24  ASP A CA  1 
ATOM   265   C C   . ASP A  1 32  ? 12.166  -17.940 42.818  1.00 44.06  ? 24  ASP A C   1 
ATOM   266   O O   . ASP A  1 32  ? 11.710  -19.063 43.045  1.00 41.65  ? 24  ASP A O   1 
ATOM   267   C CB  . ASP A  1 32  ? 12.014  -18.507 40.340  1.00 32.82  ? 24  ASP A CB  1 
ATOM   268   C CG  . ASP A  1 32  ? 11.342  -17.925 39.128  1.00 42.78  ? 24  ASP A CG  1 
ATOM   269   O OD1 . ASP A  1 32  ? 12.066  -17.470 38.218  1.00 53.72  ? 24  ASP A OD1 1 
ATOM   270   O OD2 . ASP A  1 32  ? 10.090  -17.891 39.095  1.00 40.27  ? 24  ASP A OD2 1 
ATOM   271   N N   . ARG A  1 33  ? 12.541  -17.092 43.775  1.00 39.99  ? 25  ARG A N   1 
ATOM   272   C CA  . ARG A  1 33  ? 12.196  -17.247 45.189  1.00 38.97  ? 25  ARG A CA  1 
ATOM   273   C C   . ARG A  1 33  ? 11.549  -15.944 45.646  1.00 33.60  ? 25  ARG A C   1 
ATOM   274   O O   . ARG A  1 33  ? 12.012  -14.864 45.300  1.00 37.22  ? 25  ARG A O   1 
ATOM   275   C CB  . ARG A  1 33  ? 13.445  -17.518 46.033  1.00 39.26  ? 25  ARG A CB  1 
ATOM   276   C CG  . ARG A  1 33  ? 13.969  -18.943 45.927  1.00 56.81  ? 25  ARG A CG  1 
ATOM   277   C CD  . ARG A  1 33  ? 15.502  -19.011 45.942  1.00 61.56  ? 25  ARG A CD  1 
ATOM   278   N NE  . ARG A  1 33  ? 16.020  -19.791 44.811  1.00 62.59  ? 25  ARG A NE  1 
ATOM   279   C CZ  . ARG A  1 33  ? 17.204  -20.402 44.792  1.00 73.58  ? 25  ARG A CZ  1 
ATOM   280   N NH1 . ARG A  1 33  ? 18.004  -20.335 45.850  1.00 75.57  ? 25  ARG A NH1 1 
ATOM   281   N NH2 . ARG A  1 33  ? 17.587  -21.086 43.718  1.00 68.66  ? 25  ARG A NH2 1 
ATOM   282   N N   . PRO A  1 34  ? 10.473  -16.031 46.429  1.00 37.58  ? 26  PRO A N   1 
ATOM   283   C CA  . PRO A  1 34  ? 9.837   -14.791 46.900  1.00 32.73  ? 26  PRO A CA  1 
ATOM   284   C C   . PRO A  1 34  ? 10.809  -13.873 47.653  1.00 23.34  ? 26  PRO A C   1 
ATOM   285   O O   . PRO A  1 34  ? 11.713  -14.343 48.337  1.00 23.50  ? 26  PRO A O   1 
ATOM   286   C CB  . PRO A  1 34  ? 8.730   -15.298 47.836  1.00 29.52  ? 26  PRO A CB  1 
ATOM   287   C CG  . PRO A  1 34  ? 9.157   -16.687 48.219  1.00 31.41  ? 26  PRO A CG  1 
ATOM   288   C CD  . PRO A  1 34  ? 9.856   -17.233 47.012  1.00 37.12  ? 26  PRO A CD  1 
ATOM   289   N N   . VAL A  1 35  ? 10.637  -12.569 47.493  1.00 19.76  ? 27  VAL A N   1 
ATOM   290   C CA  . VAL A  1 35  ? 11.436  -11.611 48.226  1.00 18.24  ? 27  VAL A CA  1 
ATOM   291   C C   . VAL A  1 35  ? 11.288  -11.898 49.697  1.00 18.91  ? 27  VAL A C   1 
ATOM   292   O O   . VAL A  1 35  ? 10.177  -11.926 50.219  1.00 21.28  ? 27  VAL A O   1 
ATOM   293   C CB  . VAL A  1 35  ? 10.940  -10.184 47.992  1.00 17.98  ? 27  VAL A CB  1 
ATOM   294   C CG1 . VAL A  1 35  ? 11.827  -9.189  48.731  1.00 13.19  ? 27  VAL A CG1 1 
ATOM   295   C CG2 . VAL A  1 35  ? 10.910  -9.888  46.519  1.00 17.08  ? 27  VAL A CG2 1 
ATOM   296   N N   . ALA A  1 36  ? 12.401  -12.144 50.366  1.00 20.77  ? 28  ALA A N   1 
ATOM   297   C CA  . ALA A  1 36  ? 12.347  -12.361 51.802  1.00 18.74  ? 28  ALA A CA  1 
ATOM   298   C C   . ALA A  1 36  ? 12.523  -11.032 52.525  1.00 16.55  ? 28  ALA A C   1 
ATOM   299   O O   . ALA A  1 36  ? 13.606  -10.442 52.509  1.00 14.15  ? 28  ALA A O   1 
ATOM   300   C CB  . ALA A  1 36  ? 13.406  -13.368 52.240  1.00 13.11  ? 28  ALA A CB  1 
ATOM   301   N N   . VAL A  1 37  ? 11.444  -10.573 53.153  1.00 17.05  ? 29  VAL A N   1 
ATOM   302   C CA  . VAL A  1 37  ? 11.436  -9.314  53.891  1.00 18.72  ? 29  VAL A CA  1 
ATOM   303   C C   . VAL A  1 37  ? 11.536  -9.534  55.407  1.00 22.34  ? 29  VAL A C   1 
ATOM   304   O O   . VAL A  1 37  ? 10.719  -10.244 55.998  1.00 24.09  ? 29  VAL A O   1 
ATOM   305   C CB  . VAL A  1 37  ? 10.137  -8.516  53.606  1.00 19.47  ? 29  VAL A CB  1 
ATOM   306   C CG1 . VAL A  1 37  ? 10.193  -7.142  54.259  1.00 16.19  ? 29  VAL A CG1 1 
ATOM   307   C CG2 . VAL A  1 37  ? 9.889   -8.401  52.115  1.00 13.57  ? 29  VAL A CG2 1 
ATOM   308   N N   . SER A  1 38  ? 12.538  -8.918  56.027  1.00 22.59  ? 30  SER A N   1 
ATOM   309   C CA  . SER A  1 38  ? 12.684  -8.920  57.484  1.00 22.64  ? 30  SER A CA  1 
ATOM   310   C C   . SER A  1 38  ? 11.973  -7.736  58.120  1.00 22.87  ? 30  SER A C   1 
ATOM   311   O O   . SER A  1 38  ? 12.282  -6.585  57.817  1.00 22.94  ? 30  SER A O   1 
ATOM   312   C CB  . SER A  1 38  ? 14.160  -8.840  57.886  1.00 22.36  ? 30  SER A CB  1 
ATOM   313   O OG  . SER A  1 38  ? 14.834  -10.062 57.664  1.00 34.07  ? 30  SER A OG  1 
ATOM   314   N N   . VAL A  1 39  ? 11.045  -8.020  59.026  1.00 28.79  ? 31  VAL A N   1 
ATOM   315   C CA  . VAL A  1 39  ? 10.380  -6.980  59.807  1.00 29.22  ? 31  VAL A CA  1 
ATOM   316   C C   . VAL A  1 39  ? 10.610  -7.151  61.309  1.00 32.75  ? 31  VAL A C   1 
ATOM   317   O O   . VAL A  1 39  ? 10.509  -8.255  61.845  1.00 39.26  ? 31  VAL A O   1 
ATOM   318   C CB  . VAL A  1 39  ? 8.873   -6.996  59.566  1.00 24.25  ? 31  VAL A CB  1 
ATOM   319   C CG1 . VAL A  1 39  ? 8.280   -5.637  59.892  1.00 20.78  ? 31  VAL A CG1 1 
ATOM   320   C CG2 . VAL A  1 39  ? 8.598   -7.367  58.137  1.00 24.31  ? 31  VAL A CG2 1 
ATOM   321   N N   . SER A  1 40  ? 10.909  -6.053  61.988  1.00 31.90  ? 32  SER A N   1 
ATOM   322   C CA  . SER A  1 40  ? 11.031  -6.060  63.440  1.00 29.91  ? 32  SER A CA  1 
ATOM   323   C C   . SER A  1 40  ? 10.394  -4.786  63.993  1.00 26.24  ? 32  SER A C   1 
ATOM   324   O O   . SER A  1 40  ? 10.735  -3.688  63.566  1.00 28.01  ? 32  SER A O   1 
ATOM   325   C CB  . SER A  1 40  ? 12.509  -6.151  63.844  1.00 35.69  ? 32  SER A CB  1 
ATOM   326   O OG  . SER A  1 40  ? 12.679  -6.041  65.249  1.00 42.18  ? 32  SER A OG  1 
ATOM   327   N N   . LEU A  1 41  ? 9.449   -4.920  64.916  1.00 28.30  ? 33  LEU A N   1 
ATOM   328   C CA  . LEU A  1 41  ? 8.879   -3.741  65.563  1.00 22.47  ? 33  LEU A CA  1 
ATOM   329   C C   . LEU A  1 41  ? 9.619   -3.503  66.863  1.00 21.60  ? 33  LEU A C   1 
ATOM   330   O O   . LEU A  1 41  ? 9.769   -4.415  67.660  1.00 28.09  ? 33  LEU A O   1 
ATOM   331   C CB  . LEU A  1 41  ? 7.379   -3.909  65.808  1.00 23.72  ? 33  LEU A CB  1 
ATOM   332   C CG  . LEU A  1 41  ? 6.524   -4.114  64.543  1.00 21.86  ? 33  LEU A CG  1 
ATOM   333   C CD1 . LEU A  1 41  ? 5.035   -3.887  64.794  1.00 17.11  ? 33  LEU A CD1 1 
ATOM   334   C CD2 . LEU A  1 41  ? 6.999   -3.211  63.435  1.00 22.15  ? 33  LEU A CD2 1 
ATOM   335   N N   . LYS A  1 42  ? 10.116  -2.286  67.051  1.00 20.20  ? 34  LYS A N   1 
ATOM   336   C CA  . LYS A  1 42  ? 10.854  -1.922  68.252  1.00 23.14  ? 34  LYS A CA  1 
ATOM   337   C C   . LYS A  1 42  ? 10.184  -0.736  68.928  1.00 23.76  ? 34  LYS A C   1 
ATOM   338   O O   . LYS A  1 42  ? 10.399  0.417   68.558  1.00 23.23  ? 34  LYS A O   1 
ATOM   339   C CB  . LYS A  1 42  ? 12.321  -1.623  67.930  1.00 25.57  ? 34  LYS A CB  1 
ATOM   340   C CG  . LYS A  1 42  ? 13.196  -2.862  67.929  1.00 31.74  ? 34  LYS A CG  1 
ATOM   341   C CD  . LYS A  1 42  ? 14.509  -2.605  67.232  1.00 47.56  ? 34  LYS A CD  1 
ATOM   342   C CE  . LYS A  1 42  ? 15.524  -3.696  67.549  1.00 63.83  ? 34  LYS A CE  1 
ATOM   343   N NZ  . LYS A  1 42  ? 16.942  -3.217  67.405  1.00 63.32  ? 34  LYS A NZ  1 
ATOM   344   N N   . PHE A  1 43  ? 9.378   -1.035  69.940  1.00 27.97  ? 35  PHE A N   1 
ATOM   345   C CA  . PHE A  1 43  ? 8.483   -0.053  70.539  1.00 20.71  ? 35  PHE A CA  1 
ATOM   346   C C   . PHE A  1 43  ? 9.151   1.092   71.271  1.00 19.19  ? 35  PHE A C   1 
ATOM   347   O O   . PHE A  1 43  ? 10.042  0.890   72.084  1.00 24.58  ? 35  PHE A O   1 
ATOM   348   C CB  . PHE A  1 43  ? 7.509   -0.752  71.456  1.00 19.74  ? 35  PHE A CB  1 
ATOM   349   C CG  . PHE A  1 43  ? 6.501   -1.572  70.729  1.00 15.48  ? 35  PHE A CG  1 
ATOM   350   C CD1 . PHE A  1 43  ? 6.611   -2.946  70.691  1.00 14.71  ? 35  PHE A CD1 1 
ATOM   351   C CD2 . PHE A  1 43  ? 5.447   -0.961  70.077  1.00 15.87  ? 35  PHE A CD2 1 
ATOM   352   C CE1 . PHE A  1 43  ? 5.686   -3.702  70.040  1.00 19.18  ? 35  PHE A CE1 1 
ATOM   353   C CE2 . PHE A  1 43  ? 4.505   -1.710  69.407  1.00 21.51  ? 35  PHE A CE2 1 
ATOM   354   C CZ  . PHE A  1 43  ? 4.625   -3.090  69.382  1.00 24.59  ? 35  PHE A CZ  1 
ATOM   355   N N   . ILE A  1 44  ? 8.693   2.302   70.979  1.00 18.26  ? 36  ILE A N   1 
ATOM   356   C CA  . ILE A  1 44  ? 9.267   3.496   71.571  1.00 19.98  ? 36  ILE A CA  1 
ATOM   357   C C   . ILE A  1 44  ? 8.337   4.036   72.645  1.00 20.49  ? 36  ILE A C   1 
ATOM   358   O O   . ILE A  1 44  ? 8.781   4.451   73.714  1.00 21.59  ? 36  ILE A O   1 
ATOM   359   C CB  . ILE A  1 44  ? 9.486   4.598   70.517  1.00 20.30  ? 36  ILE A CB  1 
ATOM   360   C CG1 . ILE A  1 44  ? 10.139  4.027   69.243  1.00 19.20  ? 36  ILE A CG1 1 
ATOM   361   C CG2 . ILE A  1 44  ? 10.263  5.750   71.108  1.00 14.79  ? 36  ILE A CG2 1 
ATOM   362   C CD1 . ILE A  1 44  ? 11.435  3.271   69.468  1.00 19.17  ? 36  ILE A CD1 1 
ATOM   363   N N   . ASN A  1 45  ? 7.041   4.025   72.368  1.00 20.25  ? 37  ASN A N   1 
ATOM   364   C CA  . ASN A  1 45  ? 6.088   4.613   73.299  1.00 19.08  ? 37  ASN A CA  1 
ATOM   365   C C   . ASN A  1 45  ? 4.661   4.099   73.102  1.00 23.99  ? 37  ASN A C   1 
ATOM   366   O O   . ASN A  1 45  ? 4.255   3.679   72.010  1.00 19.69  ? 37  ASN A O   1 
ATOM   367   C CB  . ASN A  1 45  ? 6.126   6.147   73.200  1.00 17.66  ? 37  ASN A CB  1 
ATOM   368   C CG  . ASN A  1 45  ? 5.918   6.839   74.549  1.00 23.71  ? 37  ASN A CG  1 
ATOM   369   O OD1 . ASN A  1 45  ? 5.055   6.451   75.338  1.00 26.67  ? 37  ASN A OD1 1 
ATOM   370   N ND2 . ASN A  1 45  ? 6.711   7.876   74.812  1.00 18.88  ? 37  ASN A ND2 1 
ATOM   371   N N   . ILE A  1 46  ? 3.914   4.115   74.194  1.00 25.28  ? 38  ILE A N   1 
ATOM   372   C CA  . ILE A  1 46  ? 2.477   3.933   74.158  1.00 26.14  ? 38  ILE A CA  1 
ATOM   373   C C   . ILE A  1 46  ? 1.907   5.230   74.690  1.00 22.91  ? 38  ILE A C   1 
ATOM   374   O O   . ILE A  1 46  ? 2.162   5.584   75.832  1.00 30.56  ? 38  ILE A O   1 
ATOM   375   C CB  . ILE A  1 46  ? 2.063   2.773   75.063  1.00 25.70  ? 38  ILE A CB  1 
ATOM   376   C CG1 . ILE A  1 46  ? 2.767   1.488   74.615  1.00 23.15  ? 38  ILE A CG1 1 
ATOM   377   C CG2 . ILE A  1 46  ? 0.563   2.617   75.071  1.00 25.35  ? 38  ILE A CG2 1 
ATOM   378   C CD1 . ILE A  1 46  ? 2.466   0.287   75.483  1.00 21.74  ? 38  ILE A CD1 1 
ATOM   379   N N   . LEU A  1 47  ? 1.158   5.950   73.865  1.00 24.33  ? 39  LEU A N   1 
ATOM   380   C CA  . LEU A  1 47  ? 0.738   7.316   74.204  1.00 27.01  ? 39  LEU A CA  1 
ATOM   381   C C   . LEU A  1 47  ? -0.625  7.452   74.901  1.00 25.42  ? 39  LEU A C   1 
ATOM   382   O O   . LEU A  1 47  ? -0.827  8.341   75.731  1.00 28.26  ? 39  LEU A O   1 
ATOM   383   C CB  . LEU A  1 47  ? 0.711   8.166   72.935  1.00 23.04  ? 39  LEU A CB  1 
ATOM   384   C CG  . LEU A  1 47  ? 2.049   8.312   72.230  1.00 27.79  ? 39  LEU A CG  1 
ATOM   385   C CD1 . LEU A  1 47  ? 1.839   9.016   70.916  1.00 30.38  ? 39  LEU A CD1 1 
ATOM   386   C CD2 . LEU A  1 47  ? 3.031   9.077   73.107  1.00 24.40  ? 39  LEU A CD2 1 
ATOM   387   N N   . GLU A  1 48  ? -1.560  6.592   74.521  1.00 19.14  ? 40  GLU A N   1 
ATOM   388   C CA  . GLU A  1 48  ? -2.946  6.718   74.907  1.00 18.20  ? 40  GLU A CA  1 
ATOM   389   C C   . GLU A  1 48  ? -3.526  5.333   74.807  1.00 22.90  ? 40  GLU A C   1 
ATOM   390   O O   . GLU A  1 48  ? -3.222  4.596   73.881  1.00 24.32  ? 40  GLU A O   1 
ATOM   391   C CB  . GLU A  1 48  ? -3.682  7.683   73.978  1.00 22.85  ? 40  GLU A CB  1 
ATOM   392   C CG  . GLU A  1 48  ? -5.216  7.634   74.057  1.00 28.32  ? 40  GLU A CG  1 
ATOM   393   C CD  . GLU A  1 48  ? -5.909  8.721   73.199  1.00 52.12  ? 40  GLU A CD  1 
ATOM   394   O OE1 . GLU A  1 48  ? -5.243  9.346   72.339  1.00 58.24  ? 40  GLU A OE1 1 
ATOM   395   O OE2 . GLU A  1 48  ? -7.126  8.950   73.382  1.00 52.54  ? 40  GLU A OE2 1 
ATOM   396   N N   . VAL A  1 49  ? -4.323  4.958   75.794  1.00 26.45  ? 41  VAL A N   1 
ATOM   397   C CA  . VAL A  1 49  ? -4.934  3.647   75.806  1.00 24.00  ? 41  VAL A CA  1 
ATOM   398   C C   . VAL A  1 49  ? -6.382  3.843   76.191  1.00 28.17  ? 41  VAL A C   1 
ATOM   399   O O   . VAL A  1 49  ? -6.670  4.487   77.192  1.00 27.52  ? 41  VAL A O   1 
ATOM   400   C CB  . VAL A  1 49  ? -4.250  2.744   76.832  1.00 23.53  ? 41  VAL A CB  1 
ATOM   401   C CG1 . VAL A  1 49  ? -5.146  1.607   77.192  1.00 22.15  ? 41  VAL A CG1 1 
ATOM   402   C CG2 . VAL A  1 49  ? -2.920  2.246   76.297  1.00 26.00  ? 41  VAL A CG2 1 
ATOM   403   N N   . ASN A  1 50  ? -7.298  3.328   75.382  1.00 30.76  ? 42  ASN A N   1 
ATOM   404   C CA  . ASN A  1 50  ? -8.715  3.516   75.665  1.00 30.76  ? 42  ASN A CA  1 
ATOM   405   C C   . ASN A  1 50  ? -9.413  2.202   75.966  1.00 32.54  ? 42  ASN A C   1 
ATOM   406   O O   . ASN A  1 50  ? -9.643  1.389   75.070  1.00 28.94  ? 42  ASN A O   1 
ATOM   407   C CB  . ASN A  1 50  ? -9.408  4.221   74.509  1.00 34.14  ? 42  ASN A CB  1 
ATOM   408   C CG  . ASN A  1 50  ? -10.776 4.729   74.887  1.00 36.83  ? 42  ASN A CG  1 
ATOM   409   O OD1 . ASN A  1 50  ? -11.409 4.206   75.806  1.00 32.85  ? 42  ASN A OD1 1 
ATOM   410   N ND2 . ASN A  1 50  ? -11.243 5.763   74.184  1.00 30.25  ? 42  ASN A ND2 1 
ATOM   411   N N   . GLU A  1 51  ? -9.767  2.013   77.235  1.00 38.30  ? 43  GLU A N   1 
ATOM   412   C CA  . GLU A  1 51  ? -10.253 0.727   77.723  1.00 32.40  ? 43  GLU A CA  1 
ATOM   413   C C   . GLU A  1 51  ? -11.721 0.558   77.377  1.00 27.51  ? 43  GLU A C   1 
ATOM   414   O O   . GLU A  1 51  ? -12.250 -0.552  77.336  1.00 25.69  ? 43  GLU A O   1 
ATOM   415   C CB  . GLU A  1 51  ? -10.029 0.633   79.229  1.00 35.66  ? 43  GLU A CB  1 
ATOM   416   C CG  . GLU A  1 51  ? -8.619  1.004   79.641  1.00 35.19  ? 43  GLU A CG  1 
ATOM   417   C CD  . GLU A  1 51  ? -8.502  1.294   81.117  1.00 51.19  ? 43  GLU A CD  1 
ATOM   418   O OE1 . GLU A  1 51  ? -7.415  1.742   81.547  1.00 57.73  ? 43  GLU A OE1 1 
ATOM   419   O OE2 . GLU A  1 51  ? -9.498  1.080   81.843  1.00 47.67  ? 43  GLU A OE2 1 
ATOM   420   N N   . ILE A  1 52  ? -12.365 1.684   77.116  1.00 27.29  ? 44  ILE A N   1 
ATOM   421   C CA  . ILE A  1 52  ? -13.757 1.693   76.722  1.00 31.74  ? 44  ILE A CA  1 
ATOM   422   C C   . ILE A  1 52  ? -13.891 1.173   75.299  1.00 33.11  ? 44  ILE A C   1 
ATOM   423   O O   . ILE A  1 52  ? -14.577 0.180   75.068  1.00 35.73  ? 44  ILE A O   1 
ATOM   424   C CB  . ILE A  1 52  ? -14.353 3.119   76.848  1.00 38.13  ? 44  ILE A CB  1 
ATOM   425   C CG1 . ILE A  1 52  ? -14.515 3.496   78.330  1.00 38.32  ? 44  ILE A CG1 1 
ATOM   426   C CG2 . ILE A  1 52  ? -15.667 3.240   76.086  1.00 32.35  ? 44  ILE A CG2 1 
ATOM   427   C CD1 . ILE A  1 52  ? -15.188 2.419   79.186  1.00 33.72  ? 44  ILE A CD1 1 
ATOM   428   N N   . THR A  1 53  ? -13.209 1.834   74.363  1.00 39.33  ? 45  THR A N   1 
ATOM   429   C CA  . THR A  1 53  ? -13.264 1.492   72.939  1.00 32.48  ? 45  THR A CA  1 
ATOM   430   C C   . THR A  1 53  ? -12.194 0.508   72.436  1.00 26.14  ? 45  THR A C   1 
ATOM   431   O O   . THR A  1 53  ? -12.197 0.138   71.262  1.00 24.06  ? 45  THR A O   1 
ATOM   432   C CB  . THR A  1 53  ? -13.215 2.759   72.061  1.00 29.13  ? 45  THR A CB  1 
ATOM   433   O OG1 . THR A  1 53  ? -11.962 3.427   72.250  1.00 31.53  ? 45  THR A OG1 1 
ATOM   434   C CG2 . THR A  1 53  ? -14.349 3.704   72.426  1.00 27.59  ? 45  THR A CG2 1 
ATOM   435   N N   . ASN A  1 54  ? -11.289 0.085   73.314  1.00 28.75  ? 46  ASN A N   1 
ATOM   436   C CA  . ASN A  1 54  ? -10.235 -0.868  72.942  1.00 26.08  ? 46  ASN A CA  1 
ATOM   437   C C   . ASN A  1 54  ? -9.283  -0.426  71.817  1.00 23.42  ? 46  ASN A C   1 
ATOM   438   O O   . ASN A  1 54  ? -8.878  -1.233  70.981  1.00 28.47  ? 46  ASN A O   1 
ATOM   439   C CB  . ASN A  1 54  ? -10.850 -2.227  72.595  1.00 24.28  ? 46  ASN A CB  1 
ATOM   440   C CG  . ASN A  1 54  ? -10.855 -3.181  73.772  1.00 23.08  ? 46  ASN A CG  1 
ATOM   441   O OD1 . ASN A  1 54  ? -9.994  -3.110  74.648  1.00 23.33  ? 46  ASN A OD1 1 
ATOM   442   N ND2 . ASN A  1 54  ? -11.831 -4.082  73.799  1.00 23.41  ? 46  ASN A ND2 1 
ATOM   443   N N   . GLU A  1 55  ? -8.931  0.856   71.815  1.00 27.46  ? 47  GLU A N   1 
ATOM   444   C CA  . GLU A  1 55  ? -7.970  1.425   70.894  1.00 20.13  ? 47  GLU A CA  1 
ATOM   445   C C   . GLU A  1 55  ? -6.704  1.735   71.660  1.00 25.44  ? 47  GLU A C   1 
ATOM   446   O O   . GLU A  1 55  ? -6.749  2.057   72.849  1.00 27.94  ? 47  GLU A O   1 
ATOM   447   C CB  . GLU A  1 55  ? -8.517  2.710   70.284  1.00 17.81  ? 47  GLU A CB  1 
ATOM   448   C CG  . GLU A  1 55  ? -9.822  2.515   69.551  1.00 28.40  ? 47  GLU A CG  1 
ATOM   449   C CD  . GLU A  1 55  ? -10.352 3.802   68.941  1.00 41.27  ? 47  GLU A CD  1 
ATOM   450   O OE1 . GLU A  1 55  ? -9.591  4.797   68.915  1.00 42.77  ? 47  GLU A OE1 1 
ATOM   451   O OE2 . GLU A  1 55  ? -11.526 3.812   68.489  1.00 43.69  ? 47  GLU A OE2 1 
ATOM   452   N N   . VAL A  1 56  ? -5.572  1.646   70.979  1.00 20.69  ? 48  VAL A N   1 
ATOM   453   C CA  . VAL A  1 56  ? -4.311  1.973   71.596  1.00 18.15  ? 48  VAL A CA  1 
ATOM   454   C C   . VAL A  1 56  ? -3.500  2.845   70.619  1.00 20.65  ? 48  VAL A C   1 
ATOM   455   O O   . VAL A  1 56  ? -3.633  2.718   69.411  1.00 18.05  ? 48  VAL A O   1 
ATOM   456   C CB  . VAL A  1 56  ? -3.582  0.686   72.029  1.00 17.30  ? 48  VAL A CB  1 
ATOM   457   C CG1 . VAL A  1 56  ? -3.048  -0.069  70.822  1.00 20.51  ? 48  VAL A CG1 1 
ATOM   458   C CG2 . VAL A  1 56  ? -2.476  1.005   72.992  1.00 17.21  ? 48  VAL A CG2 1 
ATOM   459   N N   . ASP A  1 57  ? -2.704  3.764   71.151  1.00 19.55  ? 49  ASP A N   1 
ATOM   460   C CA  . ASP A  1 57  ? -1.941  4.686   70.335  1.00 17.92  ? 49  ASP A CA  1 
ATOM   461   C C   . ASP A  1 57  ? -0.445  4.507   70.599  1.00 24.67  ? 49  ASP A C   1 
ATOM   462   O O   . ASP A  1 57  ? 0.059   4.853   71.679  1.00 23.04  ? 49  ASP A O   1 
ATOM   463   C CB  . ASP A  1 57  ? -2.359  6.121   70.636  1.00 22.89  ? 49  ASP A CB  1 
ATOM   464   C CG  . ASP A  1 57  ? -2.030  7.071   69.498  1.00 30.13  ? 49  ASP A CG  1 
ATOM   465   O OD1 . ASP A  1 57  ? -1.981  6.606   68.346  1.00 33.50  ? 49  ASP A OD1 1 
ATOM   466   O OD2 . ASP A  1 57  ? -1.821  8.281   69.741  1.00 37.21  ? 49  ASP A OD2 1 
ATOM   467   N N   . VAL A  1 58  ? 0.265   3.986   69.599  1.00 19.42  ? 50  VAL A N   1 
ATOM   468   C CA  . VAL A  1 58  ? 1.640   3.545   69.789  1.00 20.74  ? 50  VAL A CA  1 
ATOM   469   C C   . VAL A  1 58  ? 2.643   4.216   68.847  1.00 18.93  ? 50  VAL A C   1 
ATOM   470   O O   . VAL A  1 58  ? 2.312   4.579   67.720  1.00 15.76  ? 50  VAL A O   1 
ATOM   471   C CB  . VAL A  1 58  ? 1.747   2.010   69.663  1.00 20.38  ? 50  VAL A CB  1 
ATOM   472   C CG1 . VAL A  1 58  ? 0.855   1.338   70.699  1.00 23.91  ? 50  VAL A CG1 1 
ATOM   473   C CG2 . VAL A  1 58  ? 1.340   1.561   68.284  1.00 16.65  ? 50  VAL A CG2 1 
ATOM   474   N N   . VAL A  1 59  ? 3.862   4.397   69.352  1.00 20.51  ? 51  VAL A N   1 
ATOM   475   C CA  . VAL A  1 59  ? 4.995   4.890   68.578  1.00 18.76  ? 51  VAL A CA  1 
ATOM   476   C C   . VAL A  1 59  ? 6.037   3.793   68.489  1.00 19.34  ? 51  VAL A C   1 
ATOM   477   O O   . VAL A  1 59  ? 6.540   3.327   69.515  1.00 18.36  ? 51  VAL A O   1 
ATOM   478   C CB  . VAL A  1 59  ? 5.663   6.108   69.235  1.00 17.39  ? 51  VAL A CB  1 
ATOM   479   C CG1 . VAL A  1 59  ? 6.953   6.445   68.519  1.00 13.76  ? 51  VAL A CG1 1 
ATOM   480   C CG2 . VAL A  1 59  ? 4.714   7.309   69.228  1.00 21.69  ? 51  VAL A CG2 1 
ATOM   481   N N   . PHE A  1 60  ? 6.363   3.385   67.265  1.00 19.04  ? 52  PHE A N   1 
ATOM   482   C CA  . PHE A  1 60  ? 7.347   2.329   67.070  1.00 18.63  ? 52  PHE A CA  1 
ATOM   483   C C   . PHE A  1 60  ? 8.273   2.546   65.884  1.00 17.97  ? 52  PHE A C   1 
ATOM   484   O O   . PHE A  1 60  ? 7.966   3.290   64.950  1.00 16.95  ? 52  PHE A O   1 
ATOM   485   C CB  . PHE A  1 60  ? 6.659   0.977   66.939  1.00 16.45  ? 52  PHE A CB  1 
ATOM   486   C CG  . PHE A  1 60  ? 5.742   0.878   65.759  1.00 18.77  ? 52  PHE A CG  1 
ATOM   487   C CD1 . PHE A  1 60  ? 6.192   0.353   64.554  1.00 22.34  ? 52  PHE A CD1 1 
ATOM   488   C CD2 . PHE A  1 60  ? 4.428   1.298   65.851  1.00 17.78  ? 52  PHE A CD2 1 
ATOM   489   C CE1 . PHE A  1 60  ? 5.342   0.245   63.470  1.00 17.77  ? 52  PHE A CE1 1 
ATOM   490   C CE2 . PHE A  1 60  ? 3.574   1.200   64.768  1.00 15.98  ? 52  PHE A CE2 1 
ATOM   491   C CZ  . PHE A  1 60  ? 4.031   0.674   63.580  1.00 15.93  ? 52  PHE A CZ  1 
ATOM   492   N N   . TRP A  1 61  ? 9.418   1.875   65.947  1.00 21.62  ? 53  TRP A N   1 
ATOM   493   C CA  . TRP A  1 61  ? 10.383  1.842   64.856  1.00 19.56  ? 53  TRP A CA  1 
ATOM   494   C C   . TRP A  1 61  ? 10.193  0.564   64.057  1.00 20.52  ? 53  TRP A C   1 
ATOM   495   O O   . TRP A  1 61  ? 10.405  -0.532  64.572  1.00 20.43  ? 53  TRP A O   1 
ATOM   496   C CB  . TRP A  1 61  ? 11.803  1.904   65.413  1.00 18.32  ? 53  TRP A CB  1 
ATOM   497   C CG  . TRP A  1 61  ? 12.129  3.241   65.984  1.00 19.93  ? 53  TRP A CG  1 
ATOM   498   C CD1 . TRP A  1 61  ? 11.319  4.339   66.001  1.00 18.28  ? 53  TRP A CD1 1 
ATOM   499   C CD2 . TRP A  1 61  ? 13.360  3.640   66.602  1.00 19.91  ? 53  TRP A CD2 1 
ATOM   500   N NE1 . TRP A  1 61  ? 11.964  5.395   66.604  1.00 24.45  ? 53  TRP A NE1 1 
ATOM   501   C CE2 . TRP A  1 61  ? 13.218  4.992   66.985  1.00 20.81  ? 53  TRP A CE2 1 
ATOM   502   C CE3 . TRP A  1 61  ? 14.565  2.986   66.873  1.00 24.37  ? 53  TRP A CE3 1 
ATOM   503   C CZ2 . TRP A  1 61  ? 14.234  5.700   67.628  1.00 19.82  ? 53  TRP A CZ2 1 
ATOM   504   C CZ3 . TRP A  1 61  ? 15.566  3.688   67.516  1.00 28.60  ? 53  TRP A CZ3 1 
ATOM   505   C CH2 . TRP A  1 61  ? 15.397  5.032   67.885  1.00 25.53  ? 53  TRP A CH2 1 
ATOM   506   N N   . GLN A  1 62  ? 9.784   0.699   62.800  1.00 23.10  ? 54  GLN A N   1 
ATOM   507   C CA  . GLN A  1 62  ? 9.498   -0.473  61.969  1.00 21.91  ? 54  GLN A CA  1 
ATOM   508   C C   . GLN A  1 62  ? 10.737  -0.912  61.209  1.00 21.03  ? 54  GLN A C   1 
ATOM   509   O O   . GLN A  1 62  ? 10.964  -0.480  60.081  1.00 26.76  ? 54  GLN A O   1 
ATOM   510   C CB  . GLN A  1 62  ? 8.352   -0.176  60.998  1.00 21.15  ? 54  GLN A CB  1 
ATOM   511   C CG  . GLN A  1 62  ? 7.989   -1.340  60.107  1.00 23.73  ? 54  GLN A CG  1 
ATOM   512   C CD  . GLN A  1 62  ? 6.890   -1.008  59.129  1.00 25.92  ? 54  GLN A CD  1 
ATOM   513   O OE1 . GLN A  1 62  ? 7.057   -1.175  57.926  1.00 34.56  ? 54  GLN A OE1 1 
ATOM   514   N NE2 . GLN A  1 62  ? 5.753   -0.547  59.638  1.00 32.44  ? 54  GLN A NE2 1 
ATOM   515   N N   . GLN A  1 63  ? 11.553  -1.758  61.827  1.00 23.51  ? 55  GLN A N   1 
ATOM   516   C CA  . GLN A  1 63  ? 12.811  -2.162  61.211  1.00 21.94  ? 55  GLN A CA  1 
ATOM   517   C C   . GLN A  1 63  ? 12.565  -3.142  60.075  1.00 27.04  ? 55  GLN A C   1 
ATOM   518   O O   . GLN A  1 63  ? 12.040  -4.240  60.288  1.00 25.79  ? 55  GLN A O   1 
ATOM   519   C CB  . GLN A  1 63  ? 13.766  -2.763  62.228  1.00 24.68  ? 55  GLN A CB  1 
ATOM   520   C CG  . GLN A  1 63  ? 14.995  -3.356  61.583  1.00 33.59  ? 55  GLN A CG  1 
ATOM   521   C CD  . GLN A  1 63  ? 15.996  -3.843  62.596  1.00 48.38  ? 55  GLN A CD  1 
ATOM   522   O OE1 . GLN A  1 63  ? 15.864  -3.564  63.801  1.00 47.20  ? 55  GLN A OE1 1 
ATOM   523   N NE2 . GLN A  1 63  ? 17.013  -4.580  62.121  1.00 36.14  ? 55  GLN A NE2 1 
ATOM   524   N N   . THR A  1 64  ? 12.944  -2.731  58.867  1.00 22.56  ? 56  THR A N   1 
ATOM   525   C CA  . THR A  1 64  ? 12.634  -3.495  57.672  1.00 19.81  ? 56  THR A CA  1 
ATOM   526   C C   . THR A  1 64  ? 13.857  -3.660  56.791  1.00 18.25  ? 56  THR A C   1 
ATOM   527   O O   . THR A  1 64  ? 14.521  -2.687  56.429  1.00 15.43  ? 56  THR A O   1 
ATOM   528   C CB  . THR A  1 64  ? 11.515  -2.828  56.856  1.00 17.79  ? 56  THR A CB  1 
ATOM   529   O OG1 . THR A  1 64  ? 10.336  -2.743  57.658  1.00 25.99  ? 56  THR A OG1 1 
ATOM   530   C CG2 . THR A  1 64  ? 11.193  -3.647  55.650  1.00 16.11  ? 56  THR A CG2 1 
ATOM   531   N N   . THR A  1 65  ? 14.170  -4.905  56.463  1.00 19.34  ? 57  THR A N   1 
ATOM   532   C CA  . THR A  1 65  ? 15.270  -5.186  55.559  1.00 16.76  ? 57  THR A CA  1 
ATOM   533   C C   . THR A  1 65  ? 14.854  -6.245  54.548  1.00 15.35  ? 57  THR A C   1 
ATOM   534   O O   . THR A  1 65  ? 13.952  -7.035  54.801  1.00 16.54  ? 57  THR A O   1 
ATOM   535   C CB  . THR A  1 65  ? 16.544  -5.650  56.309  1.00 20.94  ? 57  THR A CB  1 
ATOM   536   O OG1 . THR A  1 65  ? 16.436  -7.042  56.625  1.00 29.43  ? 57  THR A OG1 1 
ATOM   537   C CG2 . THR A  1 65  ? 16.766  -4.846  57.591  1.00 14.11  ? 57  THR A CG2 1 
ATOM   538   N N   . TRP A  1 66  ? 15.504  -6.240  53.391  1.00 15.81  ? 58  TRP A N   1 
ATOM   539   C CA  . TRP A  1 66  ? 15.266  -7.241  52.354  1.00 14.73  ? 58  TRP A CA  1 
ATOM   540   C C   . TRP A  1 66  ? 16.471  -7.158  51.447  1.00 17.61  ? 58  TRP A C   1 
ATOM   541   O O   . TRP A  1 66  ? 17.378  -6.370  51.710  1.00 20.69  ? 58  TRP A O   1 
ATOM   542   C CB  . TRP A  1 66  ? 13.966  -6.964  51.586  1.00 14.33  ? 58  TRP A CB  1 
ATOM   543   C CG  . TRP A  1 66  ? 13.968  -5.639  50.853  1.00 19.62  ? 58  TRP A CG  1 
ATOM   544   C CD1 . TRP A  1 66  ? 14.368  -5.411  49.555  1.00 18.43  ? 58  TRP A CD1 1 
ATOM   545   C CD2 . TRP A  1 66  ? 13.566  -4.365  51.373  1.00 14.30  ? 58  TRP A CD2 1 
ATOM   546   N NE1 . TRP A  1 66  ? 14.243  -4.078  49.251  1.00 15.21  ? 58  TRP A NE1 1 
ATOM   547   C CE2 . TRP A  1 66  ? 13.754  -3.415  50.345  1.00 15.68  ? 58  TRP A CE2 1 
ATOM   548   C CE3 . TRP A  1 66  ? 13.070  -3.934  52.606  1.00 13.56  ? 58  TRP A CE3 1 
ATOM   549   C CZ2 . TRP A  1 66  ? 13.453  -2.064  50.514  1.00 18.05  ? 58  TRP A CZ2 1 
ATOM   550   C CZ3 . TRP A  1 66  ? 12.781  -2.585  52.775  1.00 12.20  ? 58  TRP A CZ3 1 
ATOM   551   C CH2 . TRP A  1 66  ? 12.967  -1.670  51.737  1.00 16.26  ? 58  TRP A CH2 1 
ATOM   552   N N   . SER A  1 67  ? 16.491  -7.946  50.379  1.00 24.69  ? 59  SER A N   1 
ATOM   553   C CA  . SER A  1 67  ? 17.657  -7.981  49.494  1.00 24.38  ? 59  SER A CA  1 
ATOM   554   C C   . SER A  1 67  ? 17.299  -7.710  48.041  1.00 22.54  ? 59  SER A C   1 
ATOM   555   O O   . SER A  1 67  ? 16.373  -8.331  47.518  1.00 25.05  ? 59  SER A O   1 
ATOM   556   C CB  . SER A  1 67  ? 18.325  -9.352  49.590  1.00 23.55  ? 59  SER A CB  1 
ATOM   557   O OG  . SER A  1 67  ? 19.604  -9.340  48.990  1.00 34.88  ? 59  SER A OG  1 
ATOM   558   N N   . ASP A  1 68  ? 18.024  -6.790  47.396  1.00 22.73  ? 60  ASP A N   1 
ATOM   559   C CA  . ASP A  1 68  ? 18.002  -6.660  45.916  1.00 27.37  ? 60  ASP A CA  1 
ATOM   560   C C   . ASP A  1 68  ? 19.409  -6.640  45.312  1.00 22.20  ? 60  ASP A C   1 
ATOM   561   O O   . ASP A  1 68  ? 20.020  -5.579  45.165  1.00 21.44  ? 60  ASP A O   1 
ATOM   562   C CB  . ASP A  1 68  ? 17.229  -5.421  45.457  1.00 22.99  ? 60  ASP A CB  1 
ATOM   563   C CG  . ASP A  1 68  ? 17.139  -5.316  43.933  1.00 30.80  ? 60  ASP A CG  1 
ATOM   564   O OD1 . ASP A  1 68  ? 17.625  -6.239  43.225  1.00 28.72  ? 60  ASP A OD1 1 
ATOM   565   O OD2 . ASP A  1 68  ? 16.563  -4.315  43.439  1.00 32.67  ? 60  ASP A OD2 1 
ATOM   566   N N   . ARG A  1 69  ? 19.904  -7.812  44.940  1.00 20.74  ? 61  ARG A N   1 
ATOM   567   C CA  . ARG A  1 69  ? 21.319  -7.956  44.601  1.00 29.34  ? 61  ARG A CA  1 
ATOM   568   C C   . ARG A  1 69  ? 21.744  -7.245  43.306  1.00 26.56  ? 61  ARG A C   1 
ATOM   569   O O   . ARG A  1 69  ? 22.918  -6.926  43.133  1.00 22.36  ? 61  ARG A O   1 
ATOM   570   C CB  . ARG A  1 69  ? 21.734  -9.433  44.610  1.00 34.32  ? 61  ARG A CB  1 
ATOM   571   C CG  . ARG A  1 69  ? 21.578  -10.083 45.988  1.00 38.73  ? 61  ARG A CG  1 
ATOM   572   C CD  . ARG A  1 69  ? 21.919  -11.564 45.964  1.00 44.73  ? 61  ARG A CD  1 
ATOM   573   N NE  . ARG A  1 69  ? 23.220  -11.828 46.572  1.00 49.49  ? 61  ARG A NE  1 
ATOM   574   C CZ  . ARG A  1 69  ? 23.395  -12.134 47.856  1.00 56.22  ? 61  ARG A CZ  1 
ATOM   575   N NH1 . ARG A  1 69  ? 22.345  -12.217 48.664  1.00 58.01  ? 61  ARG A NH1 1 
ATOM   576   N NH2 . ARG A  1 69  ? 24.616  -12.359 48.333  1.00 52.34  ? 61  ARG A NH2 1 
ATOM   577   N N   . THR A  1 70  ? 20.786  -6.976  42.421  1.00 26.05  ? 62  THR A N   1 
ATOM   578   C CA  . THR A  1 70  ? 21.033  -6.165  41.229  1.00 20.36  ? 62  THR A CA  1 
ATOM   579   C C   . THR A  1 70  ? 21.450  -4.724  41.569  1.00 21.06  ? 62  THR A C   1 
ATOM   580   O O   . THR A  1 70  ? 21.965  -4.005  40.712  1.00 19.70  ? 62  THR A O   1 
ATOM   581   C CB  . THR A  1 70  ? 19.804  -6.163  40.260  1.00 24.37  ? 62  THR A CB  1 
ATOM   582   O OG1 . THR A  1 70  ? 18.720  -5.400  40.815  1.00 22.56  ? 62  THR A OG1 1 
ATOM   583   C CG2 . THR A  1 70  ? 19.325  -7.587  39.985  1.00 20.10  ? 62  THR A CG2 1 
ATOM   584   N N   . LEU A  1 71  ? 21.218  -4.302  42.815  1.00 23.74  ? 63  LEU A N   1 
ATOM   585   C CA  . LEU A  1 71  ? 21.639  -2.972  43.278  1.00 20.22  ? 63  LEU A CA  1 
ATOM   586   C C   . LEU A  1 71  ? 23.049  -2.985  43.848  1.00 21.71  ? 63  LEU A C   1 
ATOM   587   O O   . LEU A  1 71  ? 23.576  -1.932  44.213  1.00 23.95  ? 63  LEU A O   1 
ATOM   588   C CB  . LEU A  1 71  ? 20.695  -2.422  44.351  1.00 21.32  ? 63  LEU A CB  1 
ATOM   589   C CG  . LEU A  1 71  ? 19.281  -1.995  43.950  1.00 24.11  ? 63  LEU A CG  1 
ATOM   590   C CD1 . LEU A  1 71  ? 18.522  -1.329  45.124  1.00 13.81  ? 63  LEU A CD1 1 
ATOM   591   C CD2 . LEU A  1 71  ? 19.348  -1.090  42.729  1.00 16.69  ? 63  LEU A CD2 1 
ATOM   592   N N   . ALA A  1 72  ? 23.651  -4.172  43.930  1.00 20.49  ? 64  ALA A N   1 
ATOM   593   C CA  . ALA A  1 72  ? 24.971  -4.330  44.540  1.00 21.07  ? 64  ALA A CA  1 
ATOM   594   C C   . ALA A  1 72  ? 26.090  -3.746  43.693  1.00 21.84  ? 64  ALA A C   1 
ATOM   595   O O   . ALA A  1 72  ? 25.979  -3.639  42.472  1.00 19.73  ? 64  ALA A O   1 
ATOM   596   C CB  . ALA A  1 72  ? 25.258  -5.789  44.834  1.00 20.20  ? 64  ALA A CB  1 
ATOM   597   N N   . TRP A  1 73  ? 27.178  -3.387  44.361  1.00 23.54  ? 65  TRP A N   1 
ATOM   598   C CA  . TRP A  1 73  ? 28.355  -2.879  43.687  1.00 20.54  ? 65  TRP A CA  1 
ATOM   599   C C   . TRP A  1 73  ? 29.649  -3.266  44.409  1.00 25.27  ? 65  TRP A C   1 
ATOM   600   O O   . TRP A  1 73  ? 29.624  -3.715  45.551  1.00 24.03  ? 65  TRP A O   1 
ATOM   601   C CB  . TRP A  1 73  ? 28.261  -1.369  43.515  1.00 18.80  ? 65  TRP A CB  1 
ATOM   602   C CG  . TRP A  1 73  ? 28.450  -0.574  44.771  1.00 22.21  ? 65  TRP A CG  1 
ATOM   603   C CD1 . TRP A  1 73  ? 29.614  -0.037  45.230  1.00 23.11  ? 65  TRP A CD1 1 
ATOM   604   C CD2 . TRP A  1 73  ? 27.432  -0.185  45.711  1.00 22.26  ? 65  TRP A CD2 1 
ATOM   605   N NE1 . TRP A  1 73  ? 29.393  0.645   46.411  1.00 24.38  ? 65  TRP A NE1 1 
ATOM   606   C CE2 . TRP A  1 73  ? 28.061  0.573   46.722  1.00 24.23  ? 65  TRP A CE2 1 
ATOM   607   C CE3 . TRP A  1 73  ? 26.059  -0.412  45.799  1.00 16.29  ? 65  TRP A CE3 1 
ATOM   608   C CZ2 . TRP A  1 73  ? 27.362  1.100   47.803  1.00 19.58  ? 65  TRP A CZ2 1 
ATOM   609   C CZ3 . TRP A  1 73  ? 25.378  0.113   46.867  1.00 18.24  ? 65  TRP A CZ3 1 
ATOM   610   C CH2 . TRP A  1 73  ? 26.026  0.860   47.854  1.00 15.64  ? 65  TRP A CH2 1 
ATOM   611   N N   . ASN A  1 74  ? 30.770  -3.091  43.713  1.00 30.18  ? 66  ASN A N   1 
ATOM   612   C CA  . ASN A  1 74  ? 32.090  -3.416  44.229  1.00 29.41  ? 66  ASN A CA  1 
ATOM   613   C C   . ASN A  1 74  ? 32.613  -2.288  45.102  1.00 30.95  ? 66  ASN A C   1 
ATOM   614   O O   . ASN A  1 74  ? 32.961  -1.221  44.597  1.00 26.72  ? 66  ASN A O   1 
ATOM   615   C CB  . ASN A  1 74  ? 33.054  -3.659  43.059  1.00 36.42  ? 66  ASN A CB  1 
ATOM   616   C CG  . ASN A  1 74  ? 34.360  -4.304  43.493  1.00 37.15  ? 66  ASN A CG  1 
ATOM   617   O OD1 . ASN A  1 74  ? 34.860  -4.050  44.589  1.00 30.49  ? 66  ASN A OD1 1 
ATOM   618   N ND2 . ASN A  1 74  ? 34.918  -5.149  42.623  1.00 47.38  ? 66  ASN A ND2 1 
ATOM   619   N N   . SER A  1 75  ? 32.698  -2.537  46.408  1.00 29.56  ? 67  SER A N   1 
ATOM   620   C CA  . SER A  1 75  ? 33.081  -1.494  47.359  1.00 28.67  ? 67  SER A CA  1 
ATOM   621   C C   . SER A  1 75  ? 34.553  -1.488  47.762  1.00 34.48  ? 67  SER A C   1 
ATOM   622   O O   . SER A  1 75  ? 34.903  -0.911  48.788  1.00 38.03  ? 67  SER A O   1 
ATOM   623   C CB  . SER A  1 75  ? 32.220  -1.595  48.615  1.00 31.30  ? 67  SER A CB  1 
ATOM   624   O OG  . SER A  1 75  ? 32.154  -2.934  49.063  1.00 37.45  ? 67  SER A OG  1 
ATOM   625   N N   . SER A  1 76  ? 35.409  -2.120  46.961  1.00 40.98  ? 68  SER A N   1 
ATOM   626   C CA  . SER A  1 76  ? 36.839  -2.187  47.259  1.00 35.26  ? 68  SER A CA  1 
ATOM   627   C C   . SER A  1 76  ? 37.445  -0.820  47.510  1.00 39.97  ? 68  SER A C   1 
ATOM   628   O O   . SER A  1 76  ? 38.325  -0.679  48.352  1.00 49.38  ? 68  SER A O   1 
ATOM   629   C CB  . SER A  1 76  ? 37.602  -2.883  46.133  1.00 35.88  ? 68  SER A CB  1 
ATOM   630   O OG  . SER A  1 76  ? 37.465  -4.285  46.227  1.00 39.21  ? 68  SER A OG  1 
ATOM   631   N N   . HIS A  1 77  ? 36.981  0.187   46.773  1.00 38.91  ? 69  HIS A N   1 
ATOM   632   C CA  . HIS A  1 77  ? 37.524  1.540   46.893  1.00 45.25  ? 69  HIS A CA  1 
ATOM   633   C C   . HIS A  1 77  ? 36.445  2.619   46.798  1.00 40.65  ? 69  HIS A C   1 
ATOM   634   O O   . HIS A  1 77  ? 36.733  3.775   46.489  1.00 42.26  ? 69  HIS A O   1 
ATOM   635   C CB  . HIS A  1 77  ? 38.600  1.780   45.831  1.00 49.50  ? 69  HIS A CB  1 
ATOM   636   C CG  . HIS A  1 77  ? 39.932  1.189   46.176  1.00 52.44  ? 69  HIS A CG  1 
ATOM   637   N ND1 . HIS A  1 77  ? 40.713  1.666   47.207  1.00 48.31  ? 69  HIS A ND1 1 
ATOM   638   C CD2 . HIS A  1 77  ? 40.621  0.161   45.627  1.00 52.23  ? 69  HIS A CD2 1 
ATOM   639   C CE1 . HIS A  1 77  ? 41.825  0.957   47.277  1.00 54.61  ? 69  HIS A CE1 1 
ATOM   640   N NE2 . HIS A  1 77  ? 41.794  0.038   46.330  1.00 63.06  ? 69  HIS A NE2 1 
ATOM   641   N N   . SER A  1 78  ? 35.205  2.229   47.069  1.00 40.19  ? 70  SER A N   1 
ATOM   642   C CA  . SER A  1 78  ? 34.071  3.139   47.053  1.00 40.08  ? 70  SER A CA  1 
ATOM   643   C C   . SER A  1 78  ? 33.340  2.901   48.376  1.00 36.25  ? 70  SER A C   1 
ATOM   644   O O   . SER A  1 78  ? 33.619  1.912   49.049  1.00 37.02  ? 70  SER A O   1 
ATOM   645   C CB  . SER A  1 78  ? 33.174  2.829   45.854  1.00 29.47  ? 70  SER A CB  1 
ATOM   646   O OG  . SER A  1 78  ? 32.756  1.478   45.893  1.00 29.30  ? 70  SER A OG  1 
ATOM   647   N N   . PRO A  1 79  ? 32.429  3.810   48.769  1.00 33.82  ? 71  PRO A N   1 
ATOM   648   C CA  . PRO A  1 79  ? 31.656  3.663   50.012  1.00 35.54  ? 71  PRO A CA  1 
ATOM   649   C C   . PRO A  1 79  ? 30.962  2.307   50.206  1.00 27.75  ? 71  PRO A C   1 
ATOM   650   O O   . PRO A  1 79  ? 30.651  1.636   49.230  1.00 30.84  ? 71  PRO A O   1 
ATOM   651   C CB  . PRO A  1 79  ? 30.620  4.777   49.889  1.00 32.44  ? 71  PRO A CB  1 
ATOM   652   C CG  . PRO A  1 79  ? 31.337  5.842   49.166  1.00 31.10  ? 71  PRO A CG  1 
ATOM   653   C CD  . PRO A  1 79  ? 32.229  5.142   48.169  1.00 33.27  ? 71  PRO A CD  1 
ATOM   654   N N   . ASP A  1 80  ? 30.743  1.921   51.460  1.00 30.86  ? 72  ASP A N   1 
ATOM   655   C CA  . ASP A  1 80  ? 30.074  0.662   51.805  1.00 32.50  ? 72  ASP A CA  1 
ATOM   656   C C   . ASP A  1 80  ? 28.579  0.780   51.602  1.00 27.21  ? 72  ASP A C   1 
ATOM   657   O O   . ASP A  1 80  ? 27.930  -0.161  51.157  1.00 20.70  ? 72  ASP A O   1 
ATOM   658   C CB  . ASP A  1 80  ? 30.297  0.308   53.287  1.00 37.66  ? 72  ASP A CB  1 
ATOM   659   C CG  . ASP A  1 80  ? 31.656  -0.306  53.560  1.00 49.50  ? 72  ASP A CG  1 
ATOM   660   O OD1 . ASP A  1 80  ? 32.554  -0.188  52.702  1.00 52.57  ? 72  ASP A OD1 1 
ATOM   661   O OD2 . ASP A  1 80  ? 31.827  -0.899  54.648  1.00 53.31  ? 72  ASP A OD2 1 
ATOM   662   N N   . GLN A  1 81  ? 28.032  1.929   52.003  1.00 28.89  ? 73  GLN A N   1 
ATOM   663   C CA  . GLN A  1 81  ? 26.596  2.181   51.955  1.00 20.52  ? 73  GLN A CA  1 
ATOM   664   C C   . GLN A  1 81  ? 26.322  3.643   51.657  1.00 22.33  ? 73  GLN A C   1 
ATOM   665   O O   . GLN A  1 81  ? 27.189  4.508   51.831  1.00 21.37  ? 73  GLN A O   1 
ATOM   666   C CB  . GLN A  1 81  ? 25.937  1.873   53.297  1.00 25.39  ? 73  GLN A CB  1 
ATOM   667   C CG  . GLN A  1 81  ? 26.454  0.660   54.023  1.00 33.53  ? 73  GLN A CG  1 
ATOM   668   C CD  . GLN A  1 81  ? 26.387  0.839   55.517  1.00 38.05  ? 73  GLN A CD  1 
ATOM   669   O OE1 . GLN A  1 81  ? 25.341  1.203   56.058  1.00 37.38  ? 73  GLN A OE1 1 
ATOM   670   N NE2 . GLN A  1 81  ? 27.511  0.611   56.194  1.00 40.10  ? 73  GLN A NE2 1 
ATOM   671   N N   . VAL A  1 82  ? 25.091  3.908   51.229  1.00 19.56  ? 74  VAL A N   1 
ATOM   672   C CA  . VAL A  1 82  ? 24.591  5.263   51.068  1.00 18.25  ? 74  VAL A CA  1 
ATOM   673   C C   . VAL A  1 82  ? 23.113  5.353   51.462  1.00 16.10  ? 74  VAL A C   1 
ATOM   674   O O   . VAL A  1 82  ? 22.439  4.335   51.662  1.00 12.59  ? 74  VAL A O   1 
ATOM   675   C CB  . VAL A  1 82  ? 24.702  5.714   49.616  1.00 14.43  ? 74  VAL A CB  1 
ATOM   676   C CG1 . VAL A  1 82  ? 26.147  5.878   49.229  1.00 17.50  ? 74  VAL A CG1 1 
ATOM   677   C CG2 . VAL A  1 82  ? 23.995  4.727   48.721  1.00 9.50   ? 74  VAL A CG2 1 
ATOM   678   N N   . SER A  1 83  ? 22.615  6.582   51.543  1.00 15.48  ? 75  SER A N   1 
ATOM   679   C CA  . SER A  1 83  ? 21.199  6.822   51.782  1.00 15.73  ? 75  SER A CA  1 
ATOM   680   C C   . SER A  1 83  ? 20.489  7.211   50.483  1.00 15.38  ? 75  SER A C   1 
ATOM   681   O O   . SER A  1 83  ? 20.961  8.072   49.745  1.00 16.09  ? 75  SER A O   1 
ATOM   682   C CB  . SER A  1 83  ? 21.019  7.916   52.836  1.00 15.86  ? 75  SER A CB  1 
ATOM   683   O OG  . SER A  1 83  ? 21.744  7.611   54.017  1.00 18.08  ? 75  SER A OG  1 
ATOM   684   N N   . VAL A  1 84  ? 19.353  6.569   50.221  1.00 14.56  ? 76  VAL A N   1 
ATOM   685   C CA  . VAL A  1 84  ? 18.562  6.792   49.019  1.00 11.53  ? 76  VAL A CA  1 
ATOM   686   C C   . VAL A  1 84  ? 17.159  7.266   49.394  1.00 14.37  ? 76  VAL A C   1 
ATOM   687   O O   . VAL A  1 84  ? 16.564  6.758   50.344  1.00 15.14  ? 76  VAL A O   1 
ATOM   688   C CB  . VAL A  1 84  ? 18.415  5.474   48.242  1.00 11.96  ? 76  VAL A CB  1 
ATOM   689   C CG1 . VAL A  1 84  ? 17.762  5.715   46.873  1.00 11.32  ? 76  VAL A CG1 1 
ATOM   690   C CG2 . VAL A  1 84  ? 19.768  4.810   48.088  1.00 11.80  ? 76  VAL A CG2 1 
ATOM   691   N N   . PRO A  1 85  ? 16.614  8.250   48.663  1.00 14.00  ? 77  PRO A N   1 
ATOM   692   C CA  . PRO A  1 85  ? 15.216  8.592   48.945  1.00 10.86  ? 77  PRO A CA  1 
ATOM   693   C C   . PRO A  1 85  ? 14.293  7.430   48.581  1.00 12.93  ? 77  PRO A C   1 
ATOM   694   O O   . PRO A  1 85  ? 14.424  6.871   47.495  1.00 12.11  ? 77  PRO A O   1 
ATOM   695   C CB  . PRO A  1 85  ? 14.964  9.798   48.046  1.00 7.61   ? 77  PRO A CB  1 
ATOM   696   C CG  . PRO A  1 85  ? 16.316  10.410  47.876  1.00 10.25  ? 77  PRO A CG  1 
ATOM   697   C CD  . PRO A  1 85  ? 17.258  9.243   47.792  1.00 13.81  ? 77  PRO A CD  1 
ATOM   698   N N   . ILE A  1 86  ? 13.382  7.082   49.491  1.00 13.48  ? 78  ILE A N   1 
ATOM   699   C CA  . ILE A  1 86  ? 12.494  5.927   49.363  1.00 9.50   ? 78  ILE A CA  1 
ATOM   700   C C   . ILE A  1 86  ? 11.713  5.871   48.055  1.00 9.90   ? 78  ILE A C   1 
ATOM   701   O O   . ILE A  1 86  ? 11.362  4.790   47.585  1.00 12.05  ? 78  ILE A O   1 
ATOM   702   C CB  . ILE A  1 86  ? 11.571  5.845   50.595  1.00 14.61  ? 78  ILE A CB  1 
ATOM   703   C CG1 . ILE A  1 86  ? 12.258  5.014   51.661  1.00 15.82  ? 78  ILE A CG1 1 
ATOM   704   C CG2 . ILE A  1 86  ? 10.230  5.208   50.285  1.00 19.09  ? 78  ILE A CG2 1 
ATOM   705   C CD1 . ILE A  1 86  ? 12.707  3.685   51.130  1.00 17.54  ? 78  ILE A CD1 1 
ATOM   706   N N   . SER A  1 87  ? 11.480  7.031   47.449  1.00 8.62   ? 79  SER A N   1 
ATOM   707   C CA  . SER A  1 87  ? 10.863  7.098   46.120  1.00 10.44  ? 79  SER A CA  1 
ATOM   708   C C   . SER A  1 87  ? 11.703  6.514   44.971  1.00 13.91  ? 79  SER A C   1 
ATOM   709   O O   . SER A  1 87  ? 11.158  6.135   43.934  1.00 13.73  ? 79  SER A O   1 
ATOM   710   C CB  . SER A  1 87  ? 10.494  8.534   45.790  1.00 10.45  ? 79  SER A CB  1 
ATOM   711   O OG  . SER A  1 87  ? 11.500  9.407   46.249  1.00 19.35  ? 79  SER A OG  1 
ATOM   712   N N   . SER A  1 88  ? 13.020  6.453   45.147  1.00 11.38  ? 80  SER A N   1 
ATOM   713   C CA  . SER A  1 88  ? 13.884  5.831   44.161  1.00 8.79   ? 80  SER A CA  1 
ATOM   714   C C   . SER A  1 88  ? 13.923  4.292   44.227  1.00 12.16  ? 80  SER A C   1 
ATOM   715   O O   . SER A  1 88  ? 14.415  3.642   43.297  1.00 10.68  ? 80  SER A O   1 
ATOM   716   C CB  . SER A  1 88  ? 15.291  6.387   44.294  1.00 11.52  ? 80  SER A CB  1 
ATOM   717   O OG  . SER A  1 88  ? 15.304  7.784   44.077  1.00 16.18  ? 80  SER A OG  1 
ATOM   718   N N   . LEU A  1 89  ? 13.415  3.699   45.307  1.00 11.21  ? 81  LEU A N   1 
ATOM   719   C CA  . LEU A  1 89  ? 13.524  2.247   45.477  1.00 9.03   ? 81  LEU A CA  1 
ATOM   720   C C   . LEU A  1 89  ? 12.191  1.561   45.652  1.00 8.86   ? 81  LEU A C   1 
ATOM   721   O O   . LEU A  1 89  ? 11.212  2.169   46.078  1.00 9.63   ? 81  LEU A O   1 
ATOM   722   C CB  . LEU A  1 89  ? 14.345  1.906   46.708  1.00 9.07   ? 81  LEU A CB  1 
ATOM   723   C CG  . LEU A  1 89  ? 15.716  2.510   46.935  1.00 10.31  ? 81  LEU A CG  1 
ATOM   724   C CD1 . LEU A  1 89  ? 16.015  2.321   48.415  1.00 13.13  ? 81  LEU A CD1 1 
ATOM   725   C CD2 . LEU A  1 89  ? 16.743  1.808   46.096  1.00 8.80   ? 81  LEU A CD2 1 
ATOM   726   N N   . TRP A  1 90  ? 12.169  0.271   45.352  1.00 8.79   ? 82  TRP A N   1 
ATOM   727   C CA  . TRP A  1 90  ? 11.013  -0.538  45.672  1.00 10.15  ? 82  TRP A CA  1 
ATOM   728   C C   . TRP A  1 90  ? 10.967  -0.765  47.167  1.00 11.29  ? 82  TRP A C   1 
ATOM   729   O O   . TRP A  1 90  ? 12.005  -0.948  47.804  1.00 12.27  ? 82  TRP A O   1 
ATOM   730   C CB  . TRP A  1 90  ? 11.059  -1.883  44.970  1.00 7.35   ? 82  TRP A CB  1 
ATOM   731   C CG  . TRP A  1 90  ? 9.965   -2.837  45.422  1.00 11.77  ? 82  TRP A CG  1 
ATOM   732   C CD1 . TRP A  1 90  ? 8.718   -2.985  44.862  1.00 7.27   ? 82  TRP A CD1 1 
ATOM   733   C CD2 . TRP A  1 90  ? 10.025  -3.774  46.521  1.00 10.07  ? 82  TRP A CD2 1 
ATOM   734   N NE1 . TRP A  1 90  ? 8.021   -3.964  45.530  1.00 9.38   ? 82  TRP A NE1 1 
ATOM   735   C CE2 . TRP A  1 90  ? 8.793   -4.460  46.551  1.00 9.33   ? 82  TRP A CE2 1 
ATOM   736   C CE3 . TRP A  1 90  ? 11.010  -4.115  47.459  1.00 9.70   ? 82  TRP A CE3 1 
ATOM   737   C CZ2 . TRP A  1 90  ? 8.518   -5.464  47.488  1.00 8.62   ? 82  TRP A CZ2 1 
ATOM   738   C CZ3 . TRP A  1 90  ? 10.734  -5.115  48.387  1.00 8.27   ? 82  TRP A CZ3 1 
ATOM   739   C CH2 . TRP A  1 90  ? 9.498   -5.772  48.397  1.00 6.61   ? 82  TRP A CH2 1 
ATOM   740   N N   . VAL A  1 91  ? 9.750   -0.777  47.703  1.00 11.24  ? 83  VAL A N   1 
ATOM   741   C CA  . VAL A  1 91  ? 9.497   -0.890  49.141  1.00 12.93  ? 83  VAL A CA  1 
ATOM   742   C C   . VAL A  1 91  ? 8.327   -1.857  49.352  1.00 11.31  ? 83  VAL A C   1 
ATOM   743   O O   . VAL A  1 91  ? 7.317   -1.767  48.651  1.00 10.35  ? 83  VAL A O   1 
ATOM   744   C CB  . VAL A  1 91  ? 9.155   0.487   49.732  1.00 10.59  ? 83  VAL A CB  1 
ATOM   745   C CG1 . VAL A  1 91  ? 8.117   0.370   50.825  1.00 19.25  ? 83  VAL A CG1 1 
ATOM   746   C CG2 . VAL A  1 91  ? 10.414  1.175   50.233  1.00 11.87  ? 83  VAL A CG2 1 
ATOM   747   N N   . PRO A  1 92  ? 8.480   -2.820  50.273  1.00 7.45   ? 84  PRO A N   1 
ATOM   748   C CA  . PRO A  1 92  ? 7.386   -3.758  50.521  1.00 9.60   ? 84  PRO A CA  1 
ATOM   749   C C   . PRO A  1 92  ? 6.091   -3.037  50.947  1.00 9.13   ? 84  PRO A C   1 
ATOM   750   O O   . PRO A  1 92  ? 6.141   -2.119  51.762  1.00 7.63   ? 84  PRO A O   1 
ATOM   751   C CB  . PRO A  1 92  ? 7.929   -4.651  51.657  1.00 16.49  ? 84  PRO A CB  1 
ATOM   752   C CG  . PRO A  1 92  ? 9.149   -3.945  52.210  1.00 11.72  ? 84  PRO A CG  1 
ATOM   753   C CD  . PRO A  1 92  ? 9.691   -3.164  51.031  1.00 10.70  ? 84  PRO A CD  1 
ATOM   754   N N   . ASP A  1 93  ? 4.961   -3.445  50.375  1.00 8.00   ? 85  ASP A N   1 
ATOM   755   C CA  . ASP A  1 93  ? 3.675   -2.815  50.656  1.00 11.57  ? 85  ASP A CA  1 
ATOM   756   C C   . ASP A  1 93  ? 3.005   -3.391  51.922  1.00 14.02  ? 85  ASP A C   1 
ATOM   757   O O   . ASP A  1 93  ? 1.906   -3.950  51.873  1.00 12.00  ? 85  ASP A O   1 
ATOM   758   C CB  . ASP A  1 93  ? 2.739   -2.920  49.439  1.00 11.79  ? 85  ASP A CB  1 
ATOM   759   C CG  . ASP A  1 93  ? 2.444   -4.363  49.047  1.00 15.50  ? 85  ASP A CG  1 
ATOM   760   O OD1 . ASP A  1 93  ? 3.410   -5.166  49.022  1.00 13.77  ? 85  ASP A OD1 1 
ATOM   761   O OD2 . ASP A  1 93  ? 1.251   -4.689  48.789  1.00 12.18  ? 85  ASP A OD2 1 
ATOM   762   N N   . LEU A  1 94  ? 3.688   -3.229  53.050  1.00 13.53  ? 86  LEU A N   1 
ATOM   763   C CA  . LEU A  1 94  ? 3.215   -3.711  54.332  1.00 12.94  ? 86  LEU A CA  1 
ATOM   764   C C   . LEU A  1 94  ? 1.981   -2.942  54.783  1.00 14.93  ? 86  LEU A C   1 
ATOM   765   O O   . LEU A  1 94  ? 1.845   -1.759  54.489  1.00 22.36  ? 86  LEU A O   1 
ATOM   766   C CB  . LEU A  1 94  ? 4.319   -3.551  55.374  1.00 12.45  ? 86  LEU A CB  1 
ATOM   767   C CG  . LEU A  1 94  ? 5.607   -4.315  55.107  1.00 14.56  ? 86  LEU A CG  1 
ATOM   768   C CD1 . LEU A  1 94  ? 6.656   -3.992  56.159  1.00 12.97  ? 86  LEU A CD1 1 
ATOM   769   C CD2 . LEU A  1 94  ? 5.336   -5.815  55.030  1.00 14.85  ? 86  LEU A CD2 1 
ATOM   770   N N   . ALA A  1 95  ? 1.090   -3.631  55.492  1.00 15.22  ? 87  ALA A N   1 
ATOM   771   C CA  . ALA A  1 95  ? -0.084  -3.024  56.116  1.00 16.22  ? 87  ALA A CA  1 
ATOM   772   C C   . ALA A  1 95  ? -0.413  -3.729  57.439  1.00 13.48  ? 87  ALA A C   1 
ATOM   773   O O   . ALA A  1 95  ? -0.263  -4.937  57.557  1.00 17.30  ? 87  ALA A O   1 
ATOM   774   C CB  . ALA A  1 95  ? -1.267  -3.089  55.173  1.00 11.94  ? 87  ALA A CB  1 
ATOM   775   N N   . ALA A  1 96  ? -0.845  -2.973  58.439  1.00 14.93  ? 88  ALA A N   1 
ATOM   776   C CA  . ALA A  1 96  ? -1.368  -3.556  59.683  1.00 13.78  ? 88  ALA A CA  1 
ATOM   777   C C   . ALA A  1 96  ? -2.875  -3.777  59.577  1.00 17.25  ? 88  ALA A C   1 
ATOM   778   O O   . ALA A  1 96  ? -3.615  -2.813  59.365  1.00 16.71  ? 88  ALA A O   1 
ATOM   779   C CB  . ALA A  1 96  ? -1.070  -2.644  60.827  1.00 12.19  ? 88  ALA A CB  1 
ATOM   780   N N   . TYR A  1 97  ? -3.335  -5.024  59.717  1.00 20.23  ? 89  TYR A N   1 
ATOM   781   C CA  . TYR A  1 97  ? -4.763  -5.332  59.515  1.00 18.70  ? 89  TYR A CA  1 
ATOM   782   C C   . TYR A  1 97  ? -5.670  -4.696  60.563  1.00 17.51  ? 89  TYR A C   1 
ATOM   783   O O   . TYR A  1 97  ? -6.833  -4.387  60.293  1.00 14.44  ? 89  TYR A O   1 
ATOM   784   C CB  . TYR A  1 97  ? -5.048  -6.835  59.528  1.00 22.48  ? 89  TYR A CB  1 
ATOM   785   C CG  . TYR A  1 97  ? -4.251  -7.685  58.577  1.00 30.56  ? 89  TYR A CG  1 
ATOM   786   C CD1 . TYR A  1 97  ? -3.155  -8.404  59.027  1.00 32.69  ? 89  TYR A CD1 1 
ATOM   787   C CD2 . TYR A  1 97  ? -4.617  -7.811  57.242  1.00 34.20  ? 89  TYR A CD2 1 
ATOM   788   C CE1 . TYR A  1 97  ? -2.426  -9.203  58.173  1.00 34.14  ? 89  TYR A CE1 1 
ATOM   789   C CE2 . TYR A  1 97  ? -3.889  -8.611  56.372  1.00 29.84  ? 89  TYR A CE2 1 
ATOM   790   C CZ  . TYR A  1 97  ? -2.792  -9.302  56.849  1.00 34.18  ? 89  TYR A CZ  1 
ATOM   791   O OH  . TYR A  1 97  ? -2.046  -10.104 56.015  1.00 39.38  ? 89  TYR A OH  1 
ATOM   792   N N   . ASN A  1 98  ? -5.157  -4.538  61.776  1.00 18.83  ? 90  ASN A N   1 
ATOM   793   C CA  . ASN A  1 98  ? -5.972  -3.973  62.845  1.00 19.41  ? 90  ASN A CA  1 
ATOM   794   C C   . ASN A  1 98  ? -5.584  -2.522  63.113  1.00 19.98  ? 90  ASN A C   1 
ATOM   795   O O   . ASN A  1 98  ? -5.682  -2.022  64.243  1.00 16.70  ? 90  ASN A O   1 
ATOM   796   C CB  . ASN A  1 98  ? -5.901  -4.832  64.106  1.00 14.95  ? 90  ASN A CB  1 
ATOM   797   C CG  . ASN A  1 98  ? -4.492  -4.956  64.653  1.00 19.52  ? 90  ASN A CG  1 
ATOM   798   O OD1 . ASN A  1 98  ? -3.558  -5.353  63.952  1.00 20.01  ? 90  ASN A OD1 1 
ATOM   799   N ND2 . ASN A  1 98  ? -4.329  -4.594  65.910  1.00 20.69  ? 90  ASN A ND2 1 
ATOM   800   N N   . ALA A  1 99  ? -5.142  -1.854  62.049  1.00 16.57  ? 91  ALA A N   1 
ATOM   801   C CA  . ALA A  1 99  ? -4.849  -0.431  62.105  1.00 13.53  ? 91  ALA A CA  1 
ATOM   802   C C   . ALA A  1 99  ? -6.156  0.329   61.959  1.00 15.22  ? 91  ALA A C   1 
ATOM   803   O O   . ALA A  1 99  ? -7.052  -0.089  61.221  1.00 14.64  ? 91  ALA A O   1 
ATOM   804   C CB  . ALA A  1 99  ? -3.884  -0.045  61.012  1.00 13.19  ? 91  ALA A CB  1 
ATOM   805   N N   . ILE A  1 100 ? -6.295  1.430   62.684  1.00 16.26  ? 92  ILE A N   1 
ATOM   806   C CA  . ILE A  1 100 ? -7.503  2.224   62.535  1.00 16.38  ? 92  ILE A CA  1 
ATOM   807   C C   . ILE A  1 100 ? -7.201  3.681   62.207  1.00 13.03  ? 92  ILE A C   1 
ATOM   808   O O   . ILE A  1 100 ? -8.089  4.519   62.202  1.00 13.25  ? 92  ILE A O   1 
ATOM   809   C CB  . ILE A  1 100 ? -8.421  2.085   63.760  1.00 15.58  ? 92  ILE A CB  1 
ATOM   810   C CG1 . ILE A  1 100 ? -7.694  2.523   65.030  1.00 16.28  ? 92  ILE A CG1 1 
ATOM   811   C CG2 . ILE A  1 100 ? -8.887  0.656   63.890  1.00 11.11  ? 92  ILE A CG2 1 
ATOM   812   C CD1 . ILE A  1 100 ? -8.590  2.568   66.209  1.00 13.12  ? 92  ILE A CD1 1 
ATOM   813   N N   . SER A  1 101 ? -5.938  3.960   61.914  1.00 15.86  ? 93  SER A N   1 
ATOM   814   C CA  . SER A  1 101 ? -5.502  5.273   61.451  1.00 18.63  ? 93  SER A CA  1 
ATOM   815   C C   . SER A  1 101 ? -4.365  5.066   60.452  1.00 18.66  ? 93  SER A C   1 
ATOM   816   O O   . SER A  1 101 ? -3.713  4.013   60.474  1.00 13.85  ? 93  SER A O   1 
ATOM   817   C CB  . SER A  1 101 ? -5.014  6.131   62.621  1.00 14.31  ? 93  SER A CB  1 
ATOM   818   O OG  . SER A  1 101 ? -3.706  5.751   63.021  1.00 14.64  ? 93  SER A OG  1 
ATOM   819   N N   . LYS A  1 102 ? -4.145  6.057   59.580  1.00 19.32  ? 94  LYS A N   1 
ATOM   820   C CA  . LYS A  1 102 ? -3.036  6.031   58.612  1.00 18.09  ? 94  LYS A CA  1 
ATOM   821   C C   . LYS A  1 102 ? -1.710  6.056   59.344  1.00 20.34  ? 94  LYS A C   1 
ATOM   822   O O   . LYS A  1 102 ? -1.572  6.725   60.370  1.00 18.89  ? 94  LYS A O   1 
ATOM   823   C CB  . LYS A  1 102 ? -3.087  7.228   57.662  1.00 16.09  ? 94  LYS A CB  1 
ATOM   824   C CG  . LYS A  1 102 ? -3.714  6.940   56.317  1.00 25.79  ? 94  LYS A CG  1 
ATOM   825   C CD  . LYS A  1 102 ? -3.536  8.098   55.341  1.00 24.90  ? 94  LYS A CD  1 
ATOM   826   C CE  . LYS A  1 102 ? -3.970  9.413   55.969  1.00 34.67  ? 94  LYS A CE  1 
ATOM   827   N NZ  . LYS A  1 102 ? -3.513  10.593  55.173  1.00 40.52  ? 94  LYS A NZ  1 
ATOM   828   N N   . PRO A  1 103 ? -0.722  5.315   58.831  1.00 23.93  ? 95  PRO A N   1 
ATOM   829   C CA  . PRO A  1 103 ? 0.569   5.363   59.532  1.00 21.95  ? 95  PRO A CA  1 
ATOM   830   C C   . PRO A  1 103 ? 1.208   6.740   59.394  1.00 17.03  ? 95  PRO A C   1 
ATOM   831   O O   . PRO A  1 103 ? 1.512   7.154   58.286  1.00 24.47  ? 95  PRO A O   1 
ATOM   832   C CB  . PRO A  1 103 ? 1.405   4.290   58.823  1.00 16.85  ? 95  PRO A CB  1 
ATOM   833   C CG  . PRO A  1 103 ? 0.674   3.986   57.561  1.00 17.67  ? 95  PRO A CG  1 
ATOM   834   C CD  . PRO A  1 103 ? -0.765  4.288   57.778  1.00 14.75  ? 95  PRO A CD  1 
ATOM   835   N N   . GLU A  1 104 ? 1.378   7.439   60.505  1.00 11.71  ? 96  GLU A N   1 
ATOM   836   C CA  . GLU A  1 104 ? 2.025   8.740   60.531  1.00 13.06  ? 96  GLU A CA  1 
ATOM   837   C C   . GLU A  1 104 ? 3.540   8.495   60.639  1.00 15.57  ? 96  GLU A C   1 
ATOM   838   O O   . GLU A  1 104 ? 4.025   8.004   61.650  1.00 15.46  ? 96  GLU A O   1 
ATOM   839   C CB  . GLU A  1 104 ? 1.455   9.538   61.723  1.00 18.48  ? 96  GLU A CB  1 
ATOM   840   C CG  . GLU A  1 104 ? 2.074   10.901  62.099  1.00 24.62  ? 96  GLU A CG  1 
ATOM   841   C CD  . GLU A  1 104 ? 1.450   11.519  63.406  1.00 40.14  ? 96  GLU A CD  1 
ATOM   842   O OE1 . GLU A  1 104 ? 0.559   10.882  64.037  1.00 30.43  ? 96  GLU A OE1 1 
ATOM   843   O OE2 . GLU A  1 104 ? 1.858   12.647  63.807  1.00 34.95  ? 96  GLU A OE2 1 
ATOM   844   N N   . VAL A  1 105 ? 4.288   8.798   59.578  1.00 13.05  ? 97  VAL A N   1 
ATOM   845   C CA  . VAL A  1 105 ? 5.732   8.586   59.594  1.00 13.44  ? 97  VAL A CA  1 
ATOM   846   C C   . VAL A  1 105 ? 6.454   9.780   60.222  1.00 15.63  ? 97  VAL A C   1 
ATOM   847   O O   . VAL A  1 105 ? 6.309   10.909  59.761  1.00 17.42  ? 97  VAL A O   1 
ATOM   848   C CB  . VAL A  1 105 ? 6.306   8.302   58.171  1.00 12.46  ? 97  VAL A CB  1 
ATOM   849   C CG1 . VAL A  1 105 ? 7.808   8.260   58.203  1.00 12.13  ? 97  VAL A CG1 1 
ATOM   850   C CG2 . VAL A  1 105 ? 5.774   7.008   57.618  1.00 10.57  ? 97  VAL A CG2 1 
ATOM   851   N N   . LEU A  1 106 ? 7.237   9.528   61.268  1.00 14.42  ? 98  LEU A N   1 
ATOM   852   C CA  . LEU A  1 106 ? 7.867   10.609  62.026  1.00 15.26  ? 98  LEU A CA  1 
ATOM   853   C C   . LEU A  1 106 ? 9.302   10.932  61.593  1.00 17.58  ? 98  LEU A C   1 
ATOM   854   O O   . LEU A  1 106 ? 9.874   11.943  62.013  1.00 15.25  ? 98  LEU A O   1 
ATOM   855   C CB  . LEU A  1 106 ? 7.870   10.268  63.518  1.00 17.03  ? 98  LEU A CB  1 
ATOM   856   C CG  . LEU A  1 106 ? 6.558   9.954   64.241  1.00 16.94  ? 98  LEU A CG  1 
ATOM   857   C CD1 . LEU A  1 106 ? 6.848   9.533   65.667  1.00 17.59  ? 98  LEU A CD1 1 
ATOM   858   C CD2 . LEU A  1 106 ? 5.639   11.138  64.228  1.00 16.83  ? 98  LEU A CD2 1 
ATOM   859   N N   . THR A  1 107 ? 9.887   10.068  60.769  1.00 17.46  ? 99  THR A N   1 
ATOM   860   C CA  . THR A  1 107 ? 11.290  10.207  60.380  1.00 16.04  ? 99  THR A CA  1 
ATOM   861   C C   . THR A  1 107 ? 11.492  10.499  58.880  1.00 14.19  ? 99  THR A C   1 
ATOM   862   O O   . THR A  1 107 ? 10.579  10.288  58.078  1.00 12.26  ? 99  THR A O   1 
ATOM   863   C CB  . THR A  1 107 ? 12.084  8.948   60.780  1.00 17.26  ? 99  THR A CB  1 
ATOM   864   O OG1 . THR A  1 107 ? 11.280  7.780   60.566  1.00 17.40  ? 99  THR A OG1 1 
ATOM   865   C CG2 . THR A  1 107 ? 12.478  9.036   62.228  1.00 16.47  ? 99  THR A CG2 1 
ATOM   866   N N   . PRO A  1 108 ? 12.686  11.006  58.504  1.00 14.66  ? 100 PRO A N   1 
ATOM   867   C CA  . PRO A  1 108 ? 12.999  11.223  57.088  1.00 14.29  ? 100 PRO A CA  1 
ATOM   868   C C   . PRO A  1 108 ? 12.835  9.940   56.273  1.00 13.97  ? 100 PRO A C   1 
ATOM   869   O O   . PRO A  1 108 ? 13.225  8.866   56.727  1.00 13.55  ? 100 PRO A O   1 
ATOM   870   C CB  . PRO A  1 108 ? 14.469  11.626  57.129  1.00 14.08  ? 100 PRO A CB  1 
ATOM   871   C CG  . PRO A  1 108 ? 14.649  12.256  58.458  1.00 13.07  ? 100 PRO A CG  1 
ATOM   872   C CD  . PRO A  1 108 ? 13.784  11.472  59.373  1.00 15.02  ? 100 PRO A CD  1 
ATOM   873   N N   . GLN A  1 109 ? 12.254  10.053  55.085  1.00 12.95  ? 101 GLN A N   1 
ATOM   874   C CA  . GLN A  1 109 ? 11.996  8.884   54.251  1.00 13.30  ? 101 GLN A CA  1 
ATOM   875   C C   . GLN A  1 109 ? 13.231  8.444   53.459  1.00 15.68  ? 101 GLN A C   1 
ATOM   876   O O   . GLN A  1 109 ? 13.208  8.403   52.226  1.00 12.80  ? 101 GLN A O   1 
ATOM   877   C CB  . GLN A  1 109 ? 10.885  9.202   53.279  1.00 13.64  ? 101 GLN A CB  1 
ATOM   878   C CG  . GLN A  1 109 ? 9.784   9.998   53.889  1.00 16.51  ? 101 GLN A CG  1 
ATOM   879   C CD  . GLN A  1 109 ? 8.630   9.128   54.254  1.00 23.63  ? 101 GLN A CD  1 
ATOM   880   O OE1 . GLN A  1 109 ? 8.814   7.973   54.676  1.00 22.34  ? 101 GLN A OE1 1 
ATOM   881   N NE2 . GLN A  1 109 ? 7.419   9.653   54.074  1.00 20.00  ? 101 GLN A NE2 1 
ATOM   882   N N   . LEU A  1 110 ? 14.301  8.115   54.176  1.00 14.32  ? 102 LEU A N   1 
ATOM   883   C CA  . LEU A  1 110 ? 15.532  7.668   53.563  1.00 12.32  ? 102 LEU A CA  1 
ATOM   884   C C   . LEU A  1 110 ? 15.784  6.200   53.861  1.00 15.10  ? 102 LEU A C   1 
ATOM   885   O O   . LEU A  1 110 ? 15.513  5.735   54.959  1.00 15.11  ? 102 LEU A O   1 
ATOM   886   C CB  . LEU A  1 110 ? 16.684  8.494   54.094  1.00 12.84  ? 102 LEU A CB  1 
ATOM   887   C CG  . LEU A  1 110 ? 16.619  9.978   53.772  1.00 12.89  ? 102 LEU A CG  1 
ATOM   888   C CD1 . LEU A  1 110 ? 17.900  10.637  54.269  1.00 10.88  ? 102 LEU A CD1 1 
ATOM   889   C CD2 . LEU A  1 110 ? 16.436  10.183  52.260  1.00 13.94  ? 102 LEU A CD2 1 
ATOM   890   N N   . ALA A  1 111 ? 16.298  5.461   52.883  1.00 13.61  ? 103 ALA A N   1 
ATOM   891   C CA  . ALA A  1 111 ? 16.638  4.067   53.129  1.00 12.57  ? 103 ALA A CA  1 
ATOM   892   C C   . ALA A  1 111 ? 18.144  3.962   53.187  1.00 12.58  ? 103 ALA A C   1 
ATOM   893   O O   . ALA A  1 111 ? 18.840  4.940   52.928  1.00 13.40  ? 103 ALA A O   1 
ATOM   894   C CB  . ALA A  1 111 ? 16.077  3.177   52.051  1.00 9.46   ? 103 ALA A CB  1 
ATOM   895   N N   . ARG A  1 112 ? 18.655  2.802   53.568  1.00 10.76  ? 104 ARG A N   1 
ATOM   896   C CA  . ARG A  1 112 ? 20.077  2.554   53.410  1.00 16.06  ? 104 ARG A CA  1 
ATOM   897   C C   . ARG A  1 112 ? 20.252  1.408   52.426  1.00 20.16  ? 104 ARG A C   1 
ATOM   898   O O   . ARG A  1 112 ? 19.599  0.365   52.554  1.00 20.70  ? 104 ARG A O   1 
ATOM   899   C CB  . ARG A  1 112 ? 20.756  2.236   54.737  1.00 17.94  ? 104 ARG A CB  1 
ATOM   900   C CG  . ARG A  1 112 ? 20.886  3.422   55.649  1.00 20.17  ? 104 ARG A CG  1 
ATOM   901   C CD  . ARG A  1 112 ? 21.873  4.437   55.115  1.00 17.87  ? 104 ARG A CD  1 
ATOM   902   N NE  . ARG A  1 112 ? 23.252  4.082   55.424  1.00 18.15  ? 104 ARG A NE  1 
ATOM   903   C CZ  . ARG A  1 112 ? 24.237  4.971   55.490  1.00 22.08  ? 104 ARG A CZ  1 
ATOM   904   N NH1 . ARG A  1 112 ? 23.978  6.253   55.273  1.00 16.10  ? 104 ARG A NH1 1 
ATOM   905   N NH2 . ARG A  1 112 ? 25.475  4.587   55.779  1.00 26.26  ? 104 ARG A NH2 1 
ATOM   906   N N   . VAL A  1 113 ? 21.095  1.617   51.421  1.00 15.12  ? 105 VAL A N   1 
ATOM   907   C CA  . VAL A  1 113 ? 21.395  0.560   50.467  1.00 17.34  ? 105 VAL A CA  1 
ATOM   908   C C   . VAL A  1 113 ? 22.828  0.130   50.706  1.00 17.05  ? 105 VAL A C   1 
ATOM   909   O O   . VAL A  1 113 ? 23.739  0.953   50.642  1.00 16.92  ? 105 VAL A O   1 
ATOM   910   C CB  . VAL A  1 113 ? 21.193  1.018   49.002  1.00 16.28  ? 105 VAL A CB  1 
ATOM   911   C CG1 . VAL A  1 113 ? 21.920  0.102   48.068  1.00 15.48  ? 105 VAL A CG1 1 
ATOM   912   C CG2 . VAL A  1 113 ? 19.705  1.061   48.650  1.00 13.32  ? 105 VAL A CG2 1 
ATOM   913   N N   . VAL A  1 114 ? 23.019  -1.148  51.025  1.00 18.50  ? 106 VAL A N   1 
ATOM   914   C CA  . VAL A  1 114 ? 24.356  -1.685  51.301  1.00 23.54  ? 106 VAL A CA  1 
ATOM   915   C C   . VAL A  1 114 ? 24.981  -2.241  50.010  1.00 23.25  ? 106 VAL A C   1 
ATOM   916   O O   . VAL A  1 114 ? 24.269  -2.743  49.131  1.00 21.92  ? 106 VAL A O   1 
ATOM   917   C CB  . VAL A  1 114 ? 24.325  -2.788  52.396  1.00 22.49  ? 106 VAL A CB  1 
ATOM   918   C CG1 . VAL A  1 114 ? 25.677  -2.920  53.052  1.00 16.88  ? 106 VAL A CG1 1 
ATOM   919   C CG2 . VAL A  1 114 ? 23.280  -2.469  53.446  1.00 25.85  ? 106 VAL A CG2 1 
ATOM   920   N N   . SER A  1 115 ? 26.305  -2.163  49.898  1.00 22.11  ? 107 SER A N   1 
ATOM   921   C CA  . SER A  1 115 ? 26.979  -2.528  48.647  1.00 24.16  ? 107 SER A CA  1 
ATOM   922   C C   . SER A  1 115 ? 26.802  -4.000  48.222  1.00 24.99  ? 107 SER A C   1 
ATOM   923   O O   . SER A  1 115 ? 27.139  -4.354  47.078  1.00 22.43  ? 107 SER A O   1 
ATOM   924   C CB  . SER A  1 115 ? 28.459  -2.116  48.651  1.00 19.30  ? 107 SER A CB  1 
ATOM   925   O OG  . SER A  1 115 ? 29.275  -3.092  49.268  1.00 22.86  ? 107 SER A OG  1 
ATOM   926   N N   . ASP A  1 116 ? 26.259  -4.834  49.114  1.00 16.30  ? 108 ASP A N   1 
ATOM   927   C CA  . ASP A  1 116 ? 25.896  -6.213  48.750  1.00 21.55  ? 108 ASP A CA  1 
ATOM   928   C C   . ASP A  1 116 ? 24.443  -6.405  48.280  1.00 26.59  ? 108 ASP A C   1 
ATOM   929   O O   . ASP A  1 116 ? 24.044  -7.521  47.936  1.00 33.26  ? 108 ASP A O   1 
ATOM   930   C CB  . ASP A  1 116 ? 26.185  -7.190  49.897  1.00 22.41  ? 108 ASP A CB  1 
ATOM   931   C CG  . ASP A  1 116 ? 25.283  -6.964  51.106  1.00 29.83  ? 108 ASP A CG  1 
ATOM   932   O OD1 . ASP A  1 116 ? 25.159  -5.805  51.551  1.00 34.24  ? 108 ASP A OD1 1 
ATOM   933   O OD2 . ASP A  1 116 ? 24.694  -7.941  51.619  1.00 36.87  ? 108 ASP A OD2 1 
ATOM   934   N N   . GLY A  1 117 ? 23.649  -5.335  48.269  1.00 25.27  ? 109 GLY A N   1 
ATOM   935   C CA  . GLY A  1 117 ? 22.264  -5.429  47.824  1.00 24.49  ? 109 GLY A CA  1 
ATOM   936   C C   . GLY A  1 117 ? 21.223  -5.414  48.937  1.00 25.05  ? 109 GLY A C   1 
ATOM   937   O O   . GLY A  1 117 ? 20.017  -5.560  48.703  1.00 25.86  ? 109 GLY A O   1 
ATOM   938   N N   . GLU A  1 118 ? 21.678  -5.238  50.166  1.00 23.23  ? 110 GLU A N   1 
ATOM   939   C CA  . GLU A  1 118 ? 20.743  -5.138  51.274  1.00 26.02  ? 110 GLU A CA  1 
ATOM   940   C C   . GLU A  1 118 ? 20.177  -3.722  51.351  1.00 22.17  ? 110 GLU A C   1 
ATOM   941   O O   . GLU A  1 118 ? 20.911  -2.726  51.268  1.00 20.23  ? 110 GLU A O   1 
ATOM   942   C CB  . GLU A  1 118 ? 21.434  -5.499  52.589  1.00 24.88  ? 110 GLU A CB  1 
ATOM   943   C CG  . GLU A  1 118 ? 20.510  -5.970  53.680  1.00 21.46  ? 110 GLU A CG  1 
ATOM   944   C CD  . GLU A  1 118 ? 21.214  -6.024  55.016  1.00 34.59  ? 110 GLU A CD  1 
ATOM   945   O OE1 . GLU A  1 118 ? 20.523  -6.127  56.056  1.00 33.45  ? 110 GLU A OE1 1 
ATOM   946   O OE2 . GLU A  1 118 ? 22.467  -5.954  55.021  1.00 37.32  ? 110 GLU A OE2 1 
ATOM   947   N N   . VAL A  1 119 ? 18.863  -3.645  51.498  1.00 17.22  ? 111 VAL A N   1 
ATOM   948   C CA  . VAL A  1 119 ? 18.182  -2.382  51.700  1.00 16.19  ? 111 VAL A CA  1 
ATOM   949   C C   . VAL A  1 119 ? 17.630  -2.381  53.129  1.00 15.10  ? 111 VAL A C   1 
ATOM   950   O O   . VAL A  1 119 ? 17.007  -3.345  53.550  1.00 13.77  ? 111 VAL A O   1 
ATOM   951   C CB  . VAL A  1 119 ? 17.043  -2.212  50.672  1.00 16.40  ? 111 VAL A CB  1 
ATOM   952   C CG1 . VAL A  1 119 ? 16.554  -0.776  50.653  1.00 15.80  ? 111 VAL A CG1 1 
ATOM   953   C CG2 . VAL A  1 119 ? 17.519  -2.634  49.286  1.00 14.09  ? 111 VAL A CG2 1 
ATOM   954   N N   . LEU A  1 120 ? 17.911  -1.321  53.876  1.00 13.31  ? 112 LEU A N   1 
ATOM   955   C CA  . LEU A  1 120 ? 17.379  -1.149  55.218  1.00 15.69  ? 112 LEU A CA  1 
ATOM   956   C C   . LEU A  1 120 ? 16.514  0.104   55.229  1.00 15.21  ? 112 LEU A C   1 
ATOM   957   O O   . LEU A  1 120 ? 16.964  1.177   54.836  1.00 15.21  ? 112 LEU A O   1 
ATOM   958   C CB  . LEU A  1 120 ? 18.501  -0.966  56.242  1.00 18.74  ? 112 LEU A CB  1 
ATOM   959   C CG  . LEU A  1 120 ? 19.732  -1.861  56.146  1.00 24.35  ? 112 LEU A CG  1 
ATOM   960   C CD1 . LEU A  1 120 ? 20.974  -1.035  56.438  1.00 28.11  ? 112 LEU A CD1 1 
ATOM   961   C CD2 . LEU A  1 120 ? 19.641  -2.998  57.121  1.00 22.69  ? 112 LEU A CD2 1 
ATOM   962   N N   . TYR A  1 121 ? 15.267  -0.043  55.650  1.00 11.06  ? 113 TYR A N   1 
ATOM   963   C CA  . TYR A  1 121 ? 14.385  1.089   55.840  1.00 11.73  ? 113 TYR A CA  1 
ATOM   964   C C   . TYR A  1 121 ? 13.789  0.935   57.232  1.00 15.66  ? 113 TYR A C   1 
ATOM   965   O O   . TYR A  1 121 ? 13.199  -0.108  57.562  1.00 16.77  ? 113 TYR A O   1 
ATOM   966   C CB  . TYR A  1 121 ? 13.277  1.133   54.767  1.00 10.63  ? 113 TYR A CB  1 
ATOM   967   C CG  . TYR A  1 121 ? 12.351  2.330   54.893  1.00 10.73  ? 113 TYR A CG  1 
ATOM   968   C CD1 . TYR A  1 121 ? 12.874  3.603   55.032  1.00 12.84  ? 113 TYR A CD1 1 
ATOM   969   C CD2 . TYR A  1 121 ? 10.967  2.189   54.891  1.00 7.69   ? 113 TYR A CD2 1 
ATOM   970   C CE1 . TYR A  1 121 ? 12.063  4.702   55.178  1.00 12.70  ? 113 TYR A CE1 1 
ATOM   971   C CE2 . TYR A  1 121 ? 10.138  3.293   55.023  1.00 8.50   ? 113 TYR A CE2 1 
ATOM   972   C CZ  . TYR A  1 121 ? 10.702  4.557   55.171  1.00 13.12  ? 113 TYR A CZ  1 
ATOM   973   O OH  . TYR A  1 121 ? 9.935   5.710   55.315  1.00 14.95  ? 113 TYR A OH  1 
ATOM   974   N N   . MET A  1 122 ? 13.959  1.957   58.061  1.00 13.69  ? 114 MET A N   1 
ATOM   975   C CA  . MET A  1 122 ? 13.422  1.911   59.424  1.00 14.95  ? 114 MET A CA  1 
ATOM   976   C C   . MET A  1 122 ? 12.789  3.222   59.811  1.00 10.56  ? 114 MET A C   1 
ATOM   977   O O   . MET A  1 122 ? 13.422  4.060   60.440  1.00 12.78  ? 114 MET A O   1 
ATOM   978   C CB  . MET A  1 122 ? 14.512  1.582   60.439  1.00 18.83  ? 114 MET A CB  1 
ATOM   979   C CG  . MET A  1 122 ? 13.963  1.263   61.832  1.00 24.47  ? 114 MET A CG  1 
ATOM   980   S SD  . MET A  1 122 ? 15.261  1.078   63.069  1.00 40.47  ? 114 MET A SD  1 
ATOM   981   C CE  . MET A  1 122 ? 15.776  2.773   63.334  1.00 22.00  ? 114 MET A CE  1 
ATOM   982   N N   . PRO A  1 123 ? 11.535  3.417   59.427  1.00 9.85   ? 115 PRO A N   1 
ATOM   983   C CA  . PRO A  1 123 ? 10.892  4.659   59.845  1.00 12.65  ? 115 PRO A CA  1 
ATOM   984   C C   . PRO A  1 123 ? 10.364  4.571   61.290  1.00 14.10  ? 115 PRO A C   1 
ATOM   985   O O   . PRO A  1 123 ? 10.044  3.488   61.799  1.00 12.78  ? 115 PRO A O   1 
ATOM   986   C CB  . PRO A  1 123 ? 9.748   4.797   58.836  1.00 10.71  ? 115 PRO A CB  1 
ATOM   987   C CG  . PRO A  1 123 ? 9.405   3.389   58.485  1.00 9.09   ? 115 PRO A CG  1 
ATOM   988   C CD  . PRO A  1 123 ? 10.675  2.599   58.557  1.00 10.11  ? 115 PRO A CD  1 
ATOM   989   N N   . SER A  1 124 ? 10.306  5.709   61.967  1.00 13.40  ? 116 SER A N   1 
ATOM   990   C CA  . SER A  1 124 ? 9.588   5.755   63.227  1.00 17.74  ? 116 SER A CA  1 
ATOM   991   C C   . SER A  1 124 ? 8.141   6.025   62.871  1.00 16.50  ? 116 SER A C   1 
ATOM   992   O O   . SER A  1 124 ? 7.853   6.923   62.075  1.00 16.61  ? 116 SER A O   1 
ATOM   993   C CB  . SER A  1 124 ? 10.117  6.864   64.123  1.00 18.64  ? 116 SER A CB  1 
ATOM   994   O OG  . SER A  1 124 ? 9.554   6.766   65.420  1.00 23.62  ? 116 SER A OG  1 
ATOM   995   N N   . ILE A  1 125 ? 7.230   5.250   63.441  1.00 11.88  ? 117 ILE A N   1 
ATOM   996   C CA  . ILE A  1 125 ? 5.817   5.410   63.114  1.00 15.39  ? 117 ILE A CA  1 
ATOM   997   C C   . ILE A  1 125 ? 4.900   5.583   64.345  1.00 15.48  ? 117 ILE A C   1 
ATOM   998   O O   . ILE A  1 125 ? 5.066   4.903   65.364  1.00 15.59  ? 117 ILE A O   1 
ATOM   999   C CB  . ILE A  1 125 ? 5.332   4.242   62.217  1.00 14.48  ? 117 ILE A CB  1 
ATOM   1000  C CG1 . ILE A  1 125 ? 6.014   4.321   60.845  1.00 13.75  ? 117 ILE A CG1 1 
ATOM   1001  C CG2 . ILE A  1 125 ? 3.823   4.271   62.051  1.00 12.87  ? 117 ILE A CG2 1 
ATOM   1002  C CD1 . ILE A  1 125 ? 5.724   3.152   59.939  1.00 10.50  ? 117 ILE A CD1 1 
ATOM   1003  N N   . ARG A  1 126 ? 3.953   6.510   64.249  1.00 12.17  ? 118 ARG A N   1 
ATOM   1004  C CA  . ARG A  1 126 ? 2.857   6.572   65.202  1.00 13.35  ? 118 ARG A CA  1 
ATOM   1005  C C   . ARG A  1 126 ? 1.596   6.062   64.536  1.00 11.78  ? 118 ARG A C   1 
ATOM   1006  O O   . ARG A  1 126 ? 1.290   6.464   63.425  1.00 13.40  ? 118 ARG A O   1 
ATOM   1007  C CB  . ARG A  1 126 ? 2.649   8.005   65.690  1.00 19.02  ? 118 ARG A CB  1 
ATOM   1008  C CG  . ARG A  1 126 ? 1.381   8.219   66.532  1.00 19.65  ? 118 ARG A CG  1 
ATOM   1009  C CD  . ARG A  1 126 ? 1.498   9.485   67.339  1.00 22.27  ? 118 ARG A CD  1 
ATOM   1010  N NE  . ARG A  1 126 ? 0.198   10.001  67.744  1.00 38.67  ? 118 ARG A NE  1 
ATOM   1011  C CZ  . ARG A  1 126 ? 0.020   11.021  68.582  1.00 38.39  ? 118 ARG A CZ  1 
ATOM   1012  N NH1 . ARG A  1 126 ? 1.068   11.649  69.119  1.00 26.23  ? 118 ARG A NH1 1 
ATOM   1013  N NH2 . ARG A  1 126 ? -1.214  11.409  68.885  1.00 35.34  ? 118 ARG A NH2 1 
ATOM   1014  N N   . GLN A  1 127 ? 0.853   5.194   65.213  1.00 12.97  ? 119 GLN A N   1 
ATOM   1015  C CA  . GLN A  1 127 ? -0.395  4.675   64.646  1.00 16.26  ? 119 GLN A CA  1 
ATOM   1016  C C   . GLN A  1 127 ? -1.356  4.082   65.699  1.00 16.90  ? 119 GLN A C   1 
ATOM   1017  O O   . GLN A  1 127 ? -0.924  3.415   66.636  1.00 16.42  ? 119 GLN A O   1 
ATOM   1018  C CB  . GLN A  1 127 ? -0.051  3.619   63.600  1.00 12.73  ? 119 GLN A CB  1 
ATOM   1019  C CG  . GLN A  1 127 ? -1.165  3.211   62.680  1.00 16.45  ? 119 GLN A CG  1 
ATOM   1020  C CD  . GLN A  1 127 ? -0.624  2.355   61.551  1.00 16.92  ? 119 GLN A CD  1 
ATOM   1021  O OE1 . GLN A  1 127 ? 0.449   1.773   61.684  1.00 14.86  ? 119 GLN A OE1 1 
ATOM   1022  N NE2 . GLN A  1 127 ? -1.343  2.291   60.433  1.00 14.88  ? 119 GLN A NE2 1 
ATOM   1023  N N   . ARG A  1 128 ? -2.657  4.308   65.526  1.00 17.70  ? 120 ARG A N   1 
ATOM   1024  C CA  . ARG A  1 128 ? -3.669  3.745   66.422  1.00 16.97  ? 120 ARG A CA  1 
ATOM   1025  C C   . ARG A  1 128 ? -4.122  2.352   65.978  1.00 18.14  ? 120 ARG A C   1 
ATOM   1026  O O   . ARG A  1 128 ? -4.374  2.119   64.796  1.00 20.21  ? 120 ARG A O   1 
ATOM   1027  C CB  . ARG A  1 128 ? -4.910  4.641   66.496  1.00 19.29  ? 120 ARG A CB  1 
ATOM   1028  C CG  . ARG A  1 128 ? -4.666  6.090   66.820  1.00 23.80  ? 120 ARG A CG  1 
ATOM   1029  C CD  . ARG A  1 128 ? -6.002  6.813   67.019  1.00 38.74  ? 120 ARG A CD  1 
ATOM   1030  N NE  . ARG A  1 128 ? -6.142  7.323   68.380  1.00 45.04  ? 120 ARG A NE  1 
ATOM   1031  C CZ  . ARG A  1 128 ? -5.600  8.463   68.802  1.00 46.04  ? 120 ARG A CZ  1 
ATOM   1032  N NH1 . ARG A  1 128 ? -4.882  9.211   67.964  1.00 39.04  ? 120 ARG A NH1 1 
ATOM   1033  N NH2 . ARG A  1 128 ? -5.769  8.852   70.062  1.00 39.16  ? 120 ARG A NH2 1 
ATOM   1034  N N   . PHE A  1 129 ? -4.273  1.435   66.927  1.00 19.72  ? 121 PHE A N   1 
ATOM   1035  C CA  . PHE A  1 129 ? -4.746  0.096   66.604  1.00 17.25  ? 121 PHE A CA  1 
ATOM   1036  C C   . PHE A  1 129 ? -6.008  -0.251  67.368  1.00 19.22  ? 121 PHE A C   1 
ATOM   1037  O O   . PHE A  1 129 ? -6.319  0.354   68.377  1.00 23.51  ? 121 PHE A O   1 
ATOM   1038  C CB  . PHE A  1 129 ? -3.652  -0.925  66.889  1.00 14.76  ? 121 PHE A CB  1 
ATOM   1039  C CG  . PHE A  1 129 ? -2.445  -0.750  66.022  1.00 20.11  ? 121 PHE A CG  1 
ATOM   1040  C CD1 . PHE A  1 129 ? -1.468  0.180   66.344  1.00 18.64  ? 121 PHE A CD1 1 
ATOM   1041  C CD2 . PHE A  1 129 ? -2.304  -1.483  64.849  1.00 17.76  ? 121 PHE A CD2 1 
ATOM   1042  C CE1 . PHE A  1 129 ? -0.363  0.353   65.516  1.00 14.69  ? 121 PHE A CE1 1 
ATOM   1043  C CE2 . PHE A  1 129 ? -1.213  -1.315  64.051  1.00 10.72  ? 121 PHE A CE2 1 
ATOM   1044  C CZ  . PHE A  1 129 ? -0.239  -0.401  64.388  1.00 11.42  ? 121 PHE A CZ  1 
ATOM   1045  N N   . SER A  1 130 ? -6.744  -1.227  66.872  1.00 19.77  ? 122 SER A N   1 
ATOM   1046  C CA  . SER A  1 130 ? -7.860  -1.765  67.609  1.00 17.30  ? 122 SER A CA  1 
ATOM   1047  C C   . SER A  1 130 ? -7.445  -3.141  68.114  1.00 23.65  ? 122 SER A C   1 
ATOM   1048  O O   . SER A  1 130 ? -7.290  -4.079  67.324  1.00 21.23  ? 122 SER A O   1 
ATOM   1049  C CB  . SER A  1 130 ? -9.085  -1.880  66.707  1.00 14.55  ? 122 SER A CB  1 
ATOM   1050  O OG  . SER A  1 130 ? -9.449  -3.239  66.517  1.00 17.91  ? 122 SER A OG  1 
ATOM   1051  N N   . CYS A  1 131 ? -7.255  -3.247  69.435  1.00 24.76  ? 123 CYS A N   1 
ATOM   1052  C CA  . CYS A  1 131 ? -6.762  -4.467  70.096  1.00 31.67  ? 123 CYS A CA  1 
ATOM   1053  C C   . CYS A  1 131 ? -7.246  -4.637  71.554  1.00 33.21  ? 123 CYS A C   1 
ATOM   1054  O O   . CYS A  1 131 ? -7.708  -3.680  72.175  1.00 25.33  ? 123 CYS A O   1 
ATOM   1055  C CB  . CYS A  1 131 ? -5.233  -4.520  70.045  1.00 28.43  ? 123 CYS A CB  1 
ATOM   1056  S SG  . CYS A  1 131 ? -4.409  -3.141  70.875  1.00 52.17  ? 123 CYS A SG  1 
ATOM   1057  N N   . ASP A  1 132 ? -7.139  -5.859  72.083  1.00 29.28  ? 124 ASP A N   1 
ATOM   1058  C CA  . ASP A  1 132 ? -7.597  -6.195  73.426  1.00 30.00  ? 124 ASP A CA  1 
ATOM   1059  C C   . ASP A  1 132 ? -6.786  -5.455  74.482  1.00 28.58  ? 124 ASP A C   1 
ATOM   1060  O O   . ASP A  1 132 ? -5.608  -5.736  74.670  1.00 36.07  ? 124 ASP A O   1 
ATOM   1061  C CB  . ASP A  1 132 ? -7.462  -7.705  73.640  1.00 35.01  ? 124 ASP A CB  1 
ATOM   1062  C CG  . ASP A  1 132 ? -8.098  -8.187  74.938  1.00 35.34  ? 124 ASP A CG  1 
ATOM   1063  O OD1 . ASP A  1 132 ? -8.908  -7.443  75.536  1.00 33.95  ? 124 ASP A OD1 1 
ATOM   1064  O OD2 . ASP A  1 132 ? -7.789  -9.327  75.347  1.00 33.27  ? 124 ASP A OD2 1 
ATOM   1065  N N   . VAL A  1 133 ? -7.410  -4.509  75.171  1.00 25.79  ? 125 VAL A N   1 
ATOM   1066  C CA  . VAL A  1 133 ? -6.709  -3.761  76.203  1.00 28.66  ? 125 VAL A CA  1 
ATOM   1067  C C   . VAL A  1 133 ? -7.168  -4.142  77.608  1.00 30.10  ? 125 VAL A C   1 
ATOM   1068  O O   . VAL A  1 133 ? -6.713  -3.566  78.600  1.00 27.05  ? 125 VAL A O   1 
ATOM   1069  C CB  . VAL A  1 133 ? -6.852  -2.246  76.018  1.00 26.74  ? 125 VAL A CB  1 
ATOM   1070  C CG1 . VAL A  1 133 ? -5.537  -1.591  76.306  1.00 30.71  ? 125 VAL A CG1 1 
ATOM   1071  C CG2 . VAL A  1 133 ? -7.250  -1.927  74.612  1.00 31.86  ? 125 VAL A CG2 1 
ATOM   1072  N N   . SER A  1 134 ? -8.070  -5.113  77.688  1.00 30.17  ? 126 SER A N   1 
ATOM   1073  C CA  . SER A  1 134 ? -8.539  -5.592  78.975  1.00 35.91  ? 126 SER A CA  1 
ATOM   1074  C C   . SER A  1 134 ? -7.355  -6.158  79.752  1.00 35.86  ? 126 SER A C   1 
ATOM   1075  O O   . SER A  1 134 ? -6.628  -7.013  79.243  1.00 34.24  ? 126 SER A O   1 
ATOM   1076  C CB  . SER A  1 134 ? -9.636  -6.645  78.795  1.00 34.77  ? 126 SER A CB  1 
ATOM   1077  O OG  . SER A  1 134 ? -9.132  -7.800  78.158  1.00 36.93  ? 126 SER A OG  1 
ATOM   1078  N N   . GLY A  1 135 ? -7.150  -5.647  80.967  1.00 30.11  ? 127 GLY A N   1 
ATOM   1079  C CA  . GLY A  1 135 ? -6.073  -6.101  81.823  1.00 25.46  ? 127 GLY A CA  1 
ATOM   1080  C C   . GLY A  1 135 ? -4.905  -5.140  81.907  1.00 31.40  ? 127 GLY A C   1 
ATOM   1081  O O   . GLY A  1 135 ? -3.927  -5.395  82.607  1.00 33.53  ? 127 GLY A O   1 
ATOM   1082  N N   . VAL A  1 136 ? -5.000  -4.016  81.212  1.00 30.55  ? 128 VAL A N   1 
ATOM   1083  C CA  . VAL A  1 136 ? -3.884  -3.078  81.169  1.00 30.24  ? 128 VAL A CA  1 
ATOM   1084  C C   . VAL A  1 136 ? -3.602  -2.463  82.538  1.00 32.48  ? 128 VAL A C   1 
ATOM   1085  O O   . VAL A  1 136 ? -2.471  -2.063  82.839  1.00 33.41  ? 128 VAL A O   1 
ATOM   1086  C CB  . VAL A  1 136 ? -4.139  -1.974  80.139  1.00 28.39  ? 128 VAL A CB  1 
ATOM   1087  C CG1 . VAL A  1 136 ? -5.406  -1.203  80.501  1.00 27.55  ? 128 VAL A CG1 1 
ATOM   1088  C CG2 . VAL A  1 136 ? -2.922  -1.059  80.015  1.00 19.89  ? 128 VAL A CG2 1 
ATOM   1089  N N   . ASP A  1 137 ? -4.664  -2.323  83.325  1.00 40.88  ? 129 ASP A N   1 
ATOM   1090  C CA  . ASP A  1 137 ? -4.577  -2.020  84.746  1.00 38.11  ? 129 ASP A CA  1 
ATOM   1091  C C   . ASP A  1 137 ? -3.929  -3.186  85.486  1.00 38.41  ? 129 ASP A C   1 
ATOM   1092  O O   . ASP A  1 137 ? -3.142  -2.997  86.414  1.00 37.18  ? 129 ASP A O   1 
ATOM   1093  C CB  . ASP A  1 137 ? -5.964  -1.734  85.322  1.00 36.95  ? 129 ASP A CB  1 
ATOM   1094  C CG  . ASP A  1 137 ? -6.072  -0.346  85.921  1.00 52.17  ? 129 ASP A CG  1 
ATOM   1095  O OD1 . ASP A  1 137 ? -6.167  -0.239  87.162  1.00 48.47  ? 129 ASP A OD1 1 
ATOM   1096  O OD2 . ASP A  1 137 ? -6.061  0.638   85.152  1.00 51.46  ? 129 ASP A OD2 1 
ATOM   1097  N N   . THR A  1 138 ? -4.279  -4.394  85.051  1.00 38.24  ? 130 THR A N   1 
ATOM   1098  C CA  . THR A  1 138 ? -3.871  -5.637  85.704  1.00 32.81  ? 130 THR A CA  1 
ATOM   1099  C C   . THR A  1 138 ? -2.367  -5.876  85.654  1.00 37.78  ? 130 THR A C   1 
ATOM   1100  O O   . THR A  1 138 ? -1.697  -5.505  84.690  1.00 42.82  ? 130 THR A O   1 
ATOM   1101  C CB  . THR A  1 138 ? -4.590  -6.854  85.091  1.00 35.11  ? 130 THR A CB  1 
ATOM   1102  O OG1 . THR A  1 138 ? -6.007  -6.649  85.136  1.00 37.81  ? 130 THR A OG1 1 
ATOM   1103  C CG2 . THR A  1 138 ? -4.241  -8.120  85.859  1.00 26.89  ? 130 THR A CG2 1 
ATOM   1104  N N   . GLU A  1 139 ? -1.843  -6.493  86.709  1.00 37.46  ? 131 GLU A N   1 
ATOM   1105  C CA  . GLU A  1 139 ? -0.408  -6.703  86.842  1.00 41.32  ? 131 GLU A CA  1 
ATOM   1106  C C   . GLU A  1 139 ? 0.168   -7.548  85.710  1.00 37.01  ? 131 GLU A C   1 
ATOM   1107  O O   . GLU A  1 139 ? 1.253   -7.254  85.208  1.00 34.18  ? 131 GLU A O   1 
ATOM   1108  C CB  . GLU A  1 139 ? -0.087  -7.350  88.192  1.00 47.30  ? 131 GLU A CB  1 
ATOM   1109  C CG  . GLU A  1 139 ? 1.302   -7.029  88.719  1.00 50.34  ? 131 GLU A CG  1 
ATOM   1110  C CD  . GLU A  1 139 ? 1.305   -6.716  90.202  1.00 74.77  ? 131 GLU A CD  1 
ATOM   1111  O OE1 . GLU A  1 139 ? 0.390   -6.001  90.662  1.00 74.06  ? 131 GLU A OE1 1 
ATOM   1112  O OE2 . GLU A  1 139 ? 2.222   -7.184  90.909  1.00 81.57  ? 131 GLU A OE2 1 
ATOM   1113  N N   . SER A  1 140 ? -0.547  -8.593  85.302  1.00 34.35  ? 132 SER A N   1 
ATOM   1114  C CA  . SER A  1 140 ? -0.062  -9.421  84.213  1.00 38.32  ? 132 SER A CA  1 
ATOM   1115  C C   . SER A  1 140 ? -0.305  -8.693  82.893  1.00 36.31  ? 132 SER A C   1 
ATOM   1116  O O   . SER A  1 140 ? 0.098   -9.165  81.839  1.00 34.81  ? 132 SER A O   1 
ATOM   1117  C CB  . SER A  1 140 ? -0.765  -10.775 84.210  1.00 36.96  ? 132 SER A CB  1 
ATOM   1118  O OG  . SER A  1 140 ? -2.089  -10.643 83.728  1.00 44.95  ? 132 SER A OG  1 
ATOM   1119  N N   . GLY A  1 141 ? -0.989  -7.551  82.975  1.00 38.80  ? 133 GLY A N   1 
ATOM   1120  C CA  . GLY A  1 141 ? -1.188  -6.651  81.851  1.00 33.86  ? 133 GLY A CA  1 
ATOM   1121  C C   . GLY A  1 141 ? -2.202  -7.034  80.776  1.00 38.02  ? 133 GLY A C   1 
ATOM   1122  O O   . GLY A  1 141 ? -2.848  -8.087  80.831  1.00 34.18  ? 133 GLY A O   1 
ATOM   1123  N N   . ALA A  1 142 ? -2.347  -6.148  79.791  1.00 37.82  ? 134 ALA A N   1 
ATOM   1124  C CA  . ALA A  1 142 ? -3.077  -6.461  78.571  1.00 35.83  ? 134 ALA A CA  1 
ATOM   1125  C C   . ALA A  1 142 ? -2.079  -7.006  77.562  1.00 31.62  ? 134 ALA A C   1 
ATOM   1126  O O   . ALA A  1 142 ? -0.866  -6.825  77.725  1.00 29.13  ? 134 ALA A O   1 
ATOM   1127  C CB  . ALA A  1 142 ? -3.749  -5.215  78.021  1.00 29.18  ? 134 ALA A CB  1 
ATOM   1128  N N   . THR A  1 143 ? -2.586  -7.687  76.538  1.00 31.67  ? 135 THR A N   1 
ATOM   1129  C CA  . THR A  1 143 ? -1.765  -8.081  75.389  1.00 33.31  ? 135 THR A CA  1 
ATOM   1130  C C   . THR A  1 143 ? -2.368  -7.578  74.074  1.00 33.14  ? 135 THR A C   1 
ATOM   1131  O O   . THR A  1 143 ? -3.416  -8.061  73.619  1.00 27.42  ? 135 THR A O   1 
ATOM   1132  C CB  . THR A  1 143 ? -1.606  -9.603  75.274  1.00 31.88  ? 135 THR A CB  1 
ATOM   1133  O OG1 . THR A  1 143 ? -1.130  -10.127 76.512  1.00 31.56  ? 135 THR A OG1 1 
ATOM   1134  C CG2 . THR A  1 143 ? -0.619  -9.963  74.148  1.00 30.66  ? 135 THR A CG2 1 
ATOM   1135  N N   . CYS A  1 144 ? -1.690  -6.632  73.438  1.00 33.76  ? 136 CYS A N   1 
ATOM   1136  C CA  . CYS A  1 144 ? -2.174  -6.119  72.168  1.00 33.01  ? 136 CYS A CA  1 
ATOM   1137  C C   . CYS A  1 144 ? -1.460  -6.827  71.027  1.00 27.43  ? 136 CYS A C   1 
ATOM   1138  O O   . CYS A  1 144 ? -0.235  -6.780  70.920  1.00 28.90  ? 136 CYS A O   1 
ATOM   1139  C CB  . CYS A  1 144 ? -1.948  -4.609  72.076  1.00 34.93  ? 136 CYS A CB  1 
ATOM   1140  S SG  . CYS A  1 144 ? -2.125  -3.927  70.411  1.00 54.30  ? 136 CYS A SG  1 
ATOM   1141  N N   . ARG A  1 145 ? -2.239  -7.482  70.173  1.00 26.47  ? 137 ARG A N   1 
ATOM   1142  C CA  . ARG A  1 145 ? -1.690  -8.180  69.021  1.00 31.40  ? 137 ARG A CA  1 
ATOM   1143  C C   . ARG A  1 145 ? -1.838  -7.356  67.746  1.00 26.16  ? 137 ARG A C   1 
ATOM   1144  O O   . ARG A  1 145 ? -2.949  -7.120  67.281  1.00 25.04  ? 137 ARG A O   1 
ATOM   1145  C CB  . ARG A  1 145 ? -2.352  -9.551  68.853  1.00 33.65  ? 137 ARG A CB  1 
ATOM   1146  C CG  . ARG A  1 145 ? -2.063  -10.491 70.002  1.00 36.33  ? 137 ARG A CG  1 
ATOM   1147  C CD  . ARG A  1 145 ? -2.895  -11.748 69.935  1.00 50.11  ? 137 ARG A CD  1 
ATOM   1148  N NE  . ARG A  1 145 ? -3.290  -12.198 71.271  1.00 55.12  ? 137 ARG A NE  1 
ATOM   1149  C CZ  . ARG A  1 145 ? -2.541  -12.974 72.048  1.00 53.93  ? 137 ARG A CZ  1 
ATOM   1150  N NH1 . ARG A  1 145 ? -1.351  -13.389 71.622  1.00 58.05  ? 137 ARG A NH1 1 
ATOM   1151  N NH2 . ARG A  1 145 ? -2.981  -13.341 73.245  1.00 43.85  ? 137 ARG A NH2 1 
ATOM   1152  N N   . ILE A  1 146 ? -0.711  -6.913  67.198  1.00 28.88  ? 138 ILE A N   1 
ATOM   1153  C CA  . ILE A  1 146 ? -0.681  -6.230  65.902  1.00 28.61  ? 138 ILE A CA  1 
ATOM   1154  C C   . ILE A  1 146 ? -0.253  -7.183  64.787  1.00 24.29  ? 138 ILE A C   1 
ATOM   1155  O O   . ILE A  1 146 ? 0.831   -7.757  64.857  1.00 26.02  ? 138 ILE A O   1 
ATOM   1156  C CB  . ILE A  1 146 ? 0.297   -5.042  65.925  1.00 24.69  ? 138 ILE A CB  1 
ATOM   1157  C CG1 . ILE A  1 146 ? -0.154  -4.011  66.966  1.00 21.47  ? 138 ILE A CG1 1 
ATOM   1158  C CG2 . ILE A  1 146 ? 0.415   -4.435  64.532  1.00 20.13  ? 138 ILE A CG2 1 
ATOM   1159  C CD1 . ILE A  1 146 ? 0.834   -2.903  67.211  1.00 15.77  ? 138 ILE A CD1 1 
ATOM   1160  N N   . LYS A  1 147 ? -1.103  -7.361  63.775  1.00 21.49  ? 139 LYS A N   1 
ATOM   1161  C CA  . LYS A  1 147 ? -0.771  -8.229  62.635  1.00 28.37  ? 139 LYS A CA  1 
ATOM   1162  C C   . LYS A  1 147 ? -0.385  -7.454  61.366  1.00 27.51  ? 139 LYS A C   1 
ATOM   1163  O O   . LYS A  1 147 ? -1.220  -6.750  60.775  1.00 23.61  ? 139 LYS A O   1 
ATOM   1164  C CB  . LYS A  1 147 ? -1.914  -9.201  62.324  1.00 31.74  ? 139 LYS A CB  1 
ATOM   1165  C CG  . LYS A  1 147 ? -1.716  -10.608 62.889  1.00 39.74  ? 139 LYS A CG  1 
ATOM   1166  C CD  . LYS A  1 147 ? -2.582  -11.650 62.165  1.00 47.30  ? 139 LYS A CD  1 
ATOM   1167  C CE  . LYS A  1 147 ? -2.430  -13.042 62.794  1.00 55.41  ? 139 LYS A CE  1 
ATOM   1168  N NZ  . LYS A  1 147 ? -3.199  -14.125 62.105  1.00 48.04  ? 139 LYS A NZ  1 
ATOM   1169  N N   . ILE A  1 148 ? 0.879   -7.607  60.957  1.00 23.55  ? 140 ILE A N   1 
ATOM   1170  C CA  . ILE A  1 148 ? 1.464   -6.889  59.822  1.00 19.74  ? 140 ILE A CA  1 
ATOM   1171  C C   . ILE A  1 148 ? 1.846   -7.813  58.653  1.00 26.65  ? 140 ILE A C   1 
ATOM   1172  O O   . ILE A  1 148 ? 2.699   -8.692  58.789  1.00 27.56  ? 140 ILE A O   1 
ATOM   1173  C CB  . ILE A  1 148 ? 2.744   -6.142  60.246  1.00 20.88  ? 140 ILE A CB  1 
ATOM   1174  C CG1 . ILE A  1 148 ? 2.408   -4.879  61.022  1.00 26.50  ? 140 ILE A CG1 1 
ATOM   1175  C CG2 . ILE A  1 148 ? 3.581   -5.753  59.029  1.00 31.49  ? 140 ILE A CG2 1 
ATOM   1176  C CD1 . ILE A  1 148 ? 3.607   -3.957  61.216  1.00 30.70  ? 140 ILE A CD1 1 
ATOM   1177  N N   . GLY A  1 149 ? 1.241   -7.595  57.493  1.00 27.07  ? 141 GLY A N   1 
ATOM   1178  C CA  . GLY A  1 149 ? 1.625   -8.341  56.308  1.00 24.68  ? 141 GLY A CA  1 
ATOM   1179  C C   . GLY A  1 149 ? 1.691   -7.515  55.034  1.00 19.22  ? 141 GLY A C   1 
ATOM   1180  O O   . GLY A  1 149 ? 1.336   -6.338  55.017  1.00 14.95  ? 141 GLY A O   1 
ATOM   1181  N N   . SER A  1 150 ? 2.155   -8.135  53.956  1.00 18.36  ? 142 SER A N   1 
ATOM   1182  C CA  . SER A  1 150 ? 2.080   -7.501  52.660  1.00 13.78  ? 142 SER A CA  1 
ATOM   1183  C C   . SER A  1 150 ? 0.630   -7.446  52.213  1.00 14.60  ? 142 SER A C   1 
ATOM   1184  O O   . SER A  1 150 ? -0.070  -8.463  52.214  1.00 16.93  ? 142 SER A O   1 
ATOM   1185  C CB  . SER A  1 150 ? 2.893   -8.270  51.632  1.00 15.13  ? 142 SER A CB  1 
ATOM   1186  O OG  . SER A  1 150 ? 2.734   -7.676  50.355  1.00 15.61  ? 142 SER A OG  1 
ATOM   1187  N N   . TRP A  1 151 ? 0.184   -6.260  51.812  1.00 13.27  ? 143 TRP A N   1 
ATOM   1188  C CA  . TRP A  1 151 ? -1.207  -6.066  51.444  1.00 11.49  ? 143 TRP A CA  1 
ATOM   1189  C C   . TRP A  1 151 ? -1.618  -6.739  50.126  1.00 12.90  ? 143 TRP A C   1 
ATOM   1190  O O   . TRP A  1 151 ? -2.698  -7.298  50.031  1.00 12.20  ? 143 TRP A O   1 
ATOM   1191  C CB  . TRP A  1 151 ? -1.559  -4.579  51.429  1.00 11.31  ? 143 TRP A CB  1 
ATOM   1192  C CG  . TRP A  1 151 ? -3.007  -4.353  51.247  1.00 12.34  ? 143 TRP A CG  1 
ATOM   1193  C CD1 . TRP A  1 151 ? -3.614  -3.750  50.193  1.00 13.07  ? 143 TRP A CD1 1 
ATOM   1194  C CD2 . TRP A  1 151 ? -4.053  -4.762  52.137  1.00 12.53  ? 143 TRP A CD2 1 
ATOM   1195  N NE1 . TRP A  1 151 ? -4.984  -3.744  50.371  1.00 12.45  ? 143 TRP A NE1 1 
ATOM   1196  C CE2 . TRP A  1 151 ? -5.275  -4.368  51.555  1.00 12.55  ? 143 TRP A CE2 1 
ATOM   1197  C CE3 . TRP A  1 151 ? -4.074  -5.428  53.366  1.00 15.28  ? 143 TRP A CE3 1 
ATOM   1198  C CZ2 . TRP A  1 151 ? -6.503  -4.612  52.163  1.00 15.68  ? 143 TRP A CZ2 1 
ATOM   1199  C CZ3 . TRP A  1 151 ? -5.296  -5.670  53.974  1.00 16.21  ? 143 TRP A CZ3 1 
ATOM   1200  C CH2 . TRP A  1 151 ? -6.496  -5.265  53.370  1.00 17.89  ? 143 TRP A CH2 1 
ATOM   1201  N N   . THR A  1 152 ? -0.781  -6.697  49.098  1.00 14.98  ? 144 THR A N   1 
ATOM   1202  C CA  . THR A  1 152 ? -1.255  -7.229  47.823  1.00 14.66  ? 144 THR A CA  1 
ATOM   1203  C C   . THR A  1 152 ? -0.492  -8.430  47.321  1.00 13.75  ? 144 THR A C   1 
ATOM   1204  O O   . THR A  1 152 ? -0.954  -9.101  46.415  1.00 16.01  ? 144 THR A O   1 
ATOM   1205  C CB  . THR A  1 152 ? -1.327  -6.158  46.697  1.00 15.29  ? 144 THR A CB  1 
ATOM   1206  O OG1 . THR A  1 152 ? -0.018  -5.647  46.416  1.00 17.21  ? 144 THR A OG1 1 
ATOM   1207  C CG2 . THR A  1 152 ? -2.254  -5.010  47.093  1.00 15.03  ? 144 THR A CG2 1 
ATOM   1208  N N   . HIS A  1 153 ? 0.664   -8.711  47.902  1.00 13.86  ? 145 HIS A N   1 
ATOM   1209  C CA  . HIS A  1 153 ? 1.472   -9.816  47.398  1.00 21.82  ? 145 HIS A CA  1 
ATOM   1210  C C   . HIS A  1 153 ? 1.279   -11.075 48.222  1.00 22.36  ? 145 HIS A C   1 
ATOM   1211  O O   . HIS A  1 153 ? 1.504   -11.063 49.419  1.00 26.04  ? 145 HIS A O   1 
ATOM   1212  C CB  . HIS A  1 153 ? 2.958   -9.428  47.316  1.00 17.90  ? 145 HIS A CB  1 
ATOM   1213  C CG  . HIS A  1 153 ? 3.214   -8.253  46.425  1.00 17.71  ? 145 HIS A CG  1 
ATOM   1214  N ND1 . HIS A  1 153 ? 3.440   -6.982  46.912  1.00 12.68  ? 145 HIS A ND1 1 
ATOM   1215  C CD2 . HIS A  1 153 ? 3.239   -8.151  45.073  1.00 17.12  ? 145 HIS A CD2 1 
ATOM   1216  C CE1 . HIS A  1 153 ? 3.612   -6.151  45.899  1.00 14.55  ? 145 HIS A CE1 1 
ATOM   1217  N NE2 . HIS A  1 153 ? 3.496   -6.835  44.772  1.00 16.58  ? 145 HIS A NE2 1 
ATOM   1218  N N   . HIS A  1 154 ? 0.864   -12.164 47.579  1.00 27.90  ? 146 HIS A N   1 
ATOM   1219  C CA  . HIS A  1 154 ? 0.719   -13.431 48.293  1.00 28.75  ? 146 HIS A CA  1 
ATOM   1220  C C   . HIS A  1 154 ? 2.083   -14.075 48.644  1.00 29.81  ? 146 HIS A C   1 
ATOM   1221  O O   . HIS A  1 154 ? 3.136   -13.477 48.418  1.00 24.59  ? 146 HIS A O   1 
ATOM   1222  C CB  . HIS A  1 154 ? -0.283  -14.389 47.600  1.00 26.94  ? 146 HIS A CB  1 
ATOM   1223  C CG  . HIS A  1 154 ? -0.113  -14.517 46.114  1.00 36.21  ? 146 HIS A CG  1 
ATOM   1224  N ND1 . HIS A  1 154 ? 0.762   -15.413 45.534  1.00 43.59  ? 146 HIS A ND1 1 
ATOM   1225  C CD2 . HIS A  1 154 ? -0.746  -13.897 45.087  1.00 43.34  ? 146 HIS A CD2 1 
ATOM   1226  C CE1 . HIS A  1 154 ? 0.678   -15.324 44.216  1.00 43.61  ? 146 HIS A CE1 1 
ATOM   1227  N NE2 . HIS A  1 154 ? -0.231  -14.413 43.917  1.00 45.02  ? 146 HIS A NE2 1 
ATOM   1228  N N   . SER A  1 155 ? 2.060   -15.274 49.221  1.00 33.72  ? 147 SER A N   1 
ATOM   1229  C CA  . SER A  1 155 ? 3.270   -15.890 49.779  1.00 33.65  ? 147 SER A CA  1 
ATOM   1230  C C   . SER A  1 155 ? 4.335   -16.243 48.742  1.00 32.33  ? 147 SER A C   1 
ATOM   1231  O O   . SER A  1 155 ? 5.530   -16.169 49.028  1.00 32.38  ? 147 SER A O   1 
ATOM   1232  C CB  . SER A  1 155 ? 2.915   -17.140 50.585  1.00 33.42  ? 147 SER A CB  1 
ATOM   1233  O OG  . SER A  1 155 ? 1.886   -16.867 51.523  1.00 44.75  ? 147 SER A OG  1 
ATOM   1234  N N   . ARG A  1 156 ? 3.909   -16.640 47.548  1.00 29.82  ? 148 ARG A N   1 
ATOM   1235  C CA  . ARG A  1 156 ? 4.864   -16.956 46.491  1.00 40.37  ? 148 ARG A CA  1 
ATOM   1236  C C   . ARG A  1 156 ? 5.589   -15.709 45.963  1.00 33.76  ? 148 ARG A C   1 
ATOM   1237  O O   . ARG A  1 156 ? 6.595   -15.819 45.274  1.00 35.89  ? 148 ARG A O   1 
ATOM   1238  C CB  . ARG A  1 156 ? 4.180   -17.708 45.343  1.00 45.46  ? 148 ARG A CB  1 
ATOM   1239  C CG  . ARG A  1 156 ? 3.383   -18.919 45.800  1.00 45.69  ? 148 ARG A CG  1 
ATOM   1240  C CD  . ARG A  1 156 ? 3.261   -19.974 44.706  1.00 54.80  ? 148 ARG A CD  1 
ATOM   1241  N NE  . ARG A  1 156 ? 2.854   -19.394 43.429  1.00 63.55  ? 148 ARG A NE  1 
ATOM   1242  C CZ  . ARG A  1 156 ? 1.607   -19.041 43.126  1.00 66.68  ? 148 ARG A CZ  1 
ATOM   1243  N NH1 . ARG A  1 156 ? 0.632   -19.201 44.018  1.00 56.69  ? 148 ARG A NH1 1 
ATOM   1244  N NH2 . ARG A  1 156 ? 1.335   -18.520 41.930  1.00 65.15  ? 148 ARG A NH2 1 
ATOM   1245  N N   . GLU A  1 157 ? 5.072   -14.531 46.304  1.00 30.09  ? 149 GLU A N   1 
ATOM   1246  C CA  . GLU A  1 157 ? 5.620   -13.266 45.831  1.00 22.95  ? 149 GLU A CA  1 
ATOM   1247  C C   . GLU A  1 157 ? 6.463   -12.549 46.902  1.00 19.41  ? 149 GLU A C   1 
ATOM   1248  O O   . GLU A  1 157 ? 7.591   -12.159 46.647  1.00 15.73  ? 149 GLU A O   1 
ATOM   1249  C CB  . GLU A  1 157 ? 4.480   -12.384 45.285  1.00 25.99  ? 149 GLU A CB  1 
ATOM   1250  C CG  . GLU A  1 157 ? 3.658   -13.067 44.162  1.00 30.84  ? 149 GLU A CG  1 
ATOM   1251  C CD  . GLU A  1 157 ? 2.586   -12.168 43.508  1.00 35.81  ? 149 GLU A CD  1 
ATOM   1252  O OE1 . GLU A  1 157 ? 2.468   -12.166 42.258  1.00 34.85  ? 149 GLU A OE1 1 
ATOM   1253  O OE2 . GLU A  1 157 ? 1.835   -11.484 44.237  1.00 32.59  ? 149 GLU A OE2 1 
ATOM   1254  N N   . ILE A  1 158 ? 5.911   -12.406 48.108  1.00 30.55  ? 150 ILE A N   1 
ATOM   1255  C CA  . ILE A  1 158 ? 6.613   -11.815 49.258  1.00 25.11  ? 150 ILE A CA  1 
ATOM   1256  C C   . ILE A  1 158 ? 6.424   -12.648 50.532  1.00 29.27  ? 150 ILE A C   1 
ATOM   1257  O O   . ILE A  1 158 ? 5.309   -13.080 50.853  1.00 24.94  ? 150 ILE A O   1 
ATOM   1258  C CB  . ILE A  1 158 ? 6.114   -10.379 49.582  1.00 21.66  ? 150 ILE A CB  1 
ATOM   1259  C CG1 . ILE A  1 158 ? 6.348   -9.422  48.412  1.00 17.16  ? 150 ILE A CG1 1 
ATOM   1260  C CG2 . ILE A  1 158 ? 6.793   -9.848  50.833  1.00 20.13  ? 150 ILE A CG2 1 
ATOM   1261  C CD1 . ILE A  1 158 ? 6.223   -7.956  48.792  1.00 13.99  ? 150 ILE A CD1 1 
ATOM   1262  N N   . SER A  1 159 ? 7.520   -12.853 51.260  1.00 31.00  ? 151 SER A N   1 
ATOM   1263  C CA  . SER A  1 159 ? 7.485   -13.587 52.520  1.00 28.15  ? 151 SER A CA  1 
ATOM   1264  C C   . SER A  1 159 ? 8.032   -12.725 53.649  1.00 25.72  ? 151 SER A C   1 
ATOM   1265  O O   . SER A  1 159 ? 9.074   -12.091 53.519  1.00 24.11  ? 151 SER A O   1 
ATOM   1266  C CB  . SER A  1 159 ? 8.271   -14.903 52.417  1.00 30.42  ? 151 SER A CB  1 
ATOM   1267  O OG  . SER A  1 159 ? 9.593   -14.763 52.914  1.00 24.92  ? 151 SER A OG  1 
ATOM   1268  N N   . VAL A  1 160 ? 7.354   -12.757 54.793  1.00 30.86  ? 152 VAL A N   1 
ATOM   1269  C CA  . VAL A  1 160 ? 7.745   -11.945 55.944  1.00 29.05  ? 152 VAL A CA  1 
ATOM   1270  C C   . VAL A  1 160 ? 8.508   -12.745 57.002  1.00 33.04  ? 152 VAL A C   1 
ATOM   1271  O O   . VAL A  1 160 ? 8.090   -13.835 57.393  1.00 42.52  ? 152 VAL A O   1 
ATOM   1272  C CB  . VAL A  1 160 ? 6.523   -11.280 56.604  1.00 33.68  ? 152 VAL A CB  1 
ATOM   1273  C CG1 . VAL A  1 160 ? 6.968   -10.213 57.592  1.00 31.06  ? 152 VAL A CG1 1 
ATOM   1274  C CG2 . VAL A  1 160 ? 5.606   -10.686 55.546  1.00 26.86  ? 152 VAL A CG2 1 
ATOM   1275  N N   . ASP A  1 161 ? 9.628   -12.227 57.486  1.00 31.34  ? 153 ASP A N   1 
ATOM   1276  C CA  . ASP A  1 161 ? 10.328  -12.900 58.580  1.00 34.06  ? 153 ASP A CA  1 
ATOM   1277  C C   . ASP A  1 161 ? 10.504  -11.935 59.742  1.00 37.78  ? 153 ASP A C   1 
ATOM   1278  O O   . ASP A  1 161 ? 10.953  -10.809 59.530  1.00 31.76  ? 153 ASP A O   1 
ATOM   1279  C CB  . ASP A  1 161 ? 11.688  -13.418 58.111  1.00 33.80  ? 153 ASP A CB  1 
ATOM   1280  C CG  . ASP A  1 161 ? 11.574  -14.382 56.947  1.00 45.79  ? 153 ASP A CG  1 
ATOM   1281  O OD1 . ASP A  1 161 ? 10.821  -15.372 57.064  1.00 48.29  ? 153 ASP A OD1 1 
ATOM   1282  O OD2 . ASP A  1 161 ? 12.236  -14.150 55.914  1.00 35.23  ? 153 ASP A OD2 1 
ATOM   1283  N N   . PRO A  1 162 ? 10.167  -12.338 60.968  1.00 44.09  ? 154 PRO A N   1 
ATOM   1284  C CA  . PRO A  1 162 ? 10.372  -11.371 62.050  1.00 41.96  ? 154 PRO A CA  1 
ATOM   1285  C C   . PRO A  1 162 ? 11.473  -11.798 63.016  1.00 44.43  ? 154 PRO A C   1 
ATOM   1286  O O   . PRO A  1 162 ? 11.396  -12.879 63.599  1.00 49.76  ? 154 PRO A O   1 
ATOM   1287  C CB  . PRO A  1 162 ? 9.032   -11.421 62.781  1.00 36.42  ? 154 PRO A CB  1 
ATOM   1288  C CG  . PRO A  1 162 ? 8.630   -12.868 62.711  1.00 37.08  ? 154 PRO A CG  1 
ATOM   1289  C CD  . PRO A  1 162 ? 9.463   -13.532 61.639  1.00 43.29  ? 154 PRO A CD  1 
ATOM   1290  N N   . THR A  1 163 ? 12.481  -10.948 63.186  1.00 56.18  ? 155 THR A N   1 
ATOM   1291  C CA  . THR A  1 163 ? 13.524  -11.167 64.182  1.00 60.20  ? 155 THR A CA  1 
ATOM   1292  C C   . THR A  1 163 ? 13.768  -9.881  64.965  1.00 66.52  ? 155 THR A C   1 
ATOM   1293  O O   . THR A  1 163 ? 13.833  -8.802  64.376  1.00 56.10  ? 155 THR A O   1 
ATOM   1294  C CB  . THR A  1 163 ? 14.842  -11.623 63.531  1.00 60.39  ? 155 THR A CB  1 
ATOM   1295  O OG1 . THR A  1 163 ? 15.374  -10.562 62.727  1.00 63.83  ? 155 THR A OG1 1 
ATOM   1296  C CG2 . THR A  1 163 ? 14.610  -12.847 62.658  1.00 56.81  ? 155 THR A CG2 1 
ATOM   1297  N N   . THR A  1 164 ? 13.921  -9.984  66.282  1.00 74.90  ? 156 THR A N   1 
ATOM   1298  C CA  . THR A  1 164 ? 13.802  -11.243 67.013  1.00 77.09  ? 156 THR A CA  1 
ATOM   1299  C C   . THR A  1 164 ? 12.639  -11.180 68.000  1.00 74.89  ? 156 THR A C   1 
ATOM   1300  O O   . THR A  1 164 ? 12.263  -10.101 68.459  1.00 77.29  ? 156 THR A O   1 
ATOM   1301  C CB  . THR A  1 164 ? 15.096  -11.578 67.776  1.00 76.66  ? 156 THR A CB  1 
ATOM   1302  O OG1 . THR A  1 164 ? 16.208  -10.932 67.144  1.00 71.98  ? 156 THR A OG1 1 
ATOM   1303  C CG2 . THR A  1 164 ? 15.331  -13.081 67.792  1.00 73.31  ? 156 THR A CG2 1 
ATOM   1304  N N   . GLU A  1 165 ? 12.068  -12.347 68.276  1.00 65.37  ? 157 GLU A N   1 
ATOM   1305  C CA  . GLU A  1 165 ? 11.014  -12.510 69.263  1.00 60.71  ? 157 GLU A CA  1 
ATOM   1306  C C   . GLU A  1 165 ? 11.457  -13.585 70.245  1.00 64.51  ? 157 GLU A C   1 
ATOM   1307  O O   . GLU A  1 165 ? 11.994  -14.616 69.841  1.00 64.44  ? 157 GLU A O   1 
ATOM   1308  C CB  . GLU A  1 165 ? 9.701   -12.913 68.590  1.00 60.08  ? 157 GLU A CB  1 
ATOM   1309  C CG  . GLU A  1 165 ? 9.649   -14.367 68.153  1.00 62.25  ? 157 GLU A CG  1 
ATOM   1310  C CD  . GLU A  1 165 ? 10.684  -14.695 67.095  1.00 67.87  ? 157 GLU A CD  1 
ATOM   1311  O OE1 . GLU A  1 165 ? 10.556  -14.190 65.959  1.00 61.72  ? 157 GLU A OE1 1 
ATOM   1312  O OE2 . GLU A  1 165 ? 11.625  -15.458 67.398  1.00 69.10  ? 157 GLU A OE2 1 
ATOM   1313  N N   . ASN A  1 166 ? 11.258  -13.338 71.533  1.00 65.35  ? 158 ASN A N   1 
ATOM   1314  C CA  . ASN A  1 166 ? 10.551  -12.137 72.008  1.00 66.45  ? 158 ASN A CA  1 
ATOM   1315  C C   . ASN A  1 166 ? 11.453  -11.042 72.595  1.00 72.04  ? 158 ASN A C   1 
ATOM   1316  O O   . ASN A  1 166 ? 10.983  -10.121 73.263  1.00 83.36  ? 158 ASN A O   1 
ATOM   1317  C CB  . ASN A  1 166 ? 9.471   -12.522 73.023  1.00 65.66  ? 158 ASN A CB  1 
ATOM   1318  C CG  . ASN A  1 166 ? 8.848   -13.872 72.727  1.00 61.87  ? 158 ASN A CG  1 
ATOM   1319  O OD1 . ASN A  1 166 ? 8.609   -14.670 73.633  1.00 60.61  ? 158 ASN A OD1 1 
ATOM   1320  N ND2 . ASN A  1 166 ? 8.583   -14.135 71.453  1.00 51.00  ? 158 ASN A ND2 1 
ATOM   1321  N N   . SER A  1 167 ? 12.749  -11.175 72.348  1.00 72.32  ? 159 SER A N   1 
ATOM   1322  C CA  . SER A  1 167 ? 13.819  -10.531 73.099  1.00 79.22  ? 159 SER A CA  1 
ATOM   1323  C C   . SER A  1 167 ? 13.557  -9.061  73.422  1.00 78.67  ? 159 SER A C   1 
ATOM   1324  O O   . SER A  1 167 ? 13.847  -8.623  74.536  1.00 70.42  ? 159 SER A O   1 
ATOM   1325  C CB  . SER A  1 167 ? 15.149  -10.670 72.353  1.00 77.61  ? 159 SER A CB  1 
ATOM   1326  O OG  . SER A  1 167 ? 15.906  -11.757 72.858  1.00 68.79  ? 159 SER A OG  1 
ATOM   1327  N N   . ASP A  1 168 ? 13.009  -8.291  72.486  1.00 30.00  ? 160 ASP A N   1 
ATOM   1328  C CA  . ASP A  1 168 ? 12.660  -6.912  72.833  1.00 30.00  ? 160 ASP A CA  1 
ATOM   1329  C C   . ASP A  1 168 ? 11.252  -6.813  73.422  1.00 30.00  ? 160 ASP A C   1 
ATOM   1330  O O   . ASP A  1 168 ? 10.441  -7.723  73.256  1.00 30.00  ? 160 ASP A O   1 
ATOM   1331  C CB  . ASP A  1 168 ? 12.783  -6.004  71.608  1.00 20.00  ? 160 ASP A CB  1 
ATOM   1332  C CG  . ASP A  1 168 ? 14.125  -6.138  70.916  1.00 20.00  ? 160 ASP A CG  1 
ATOM   1333  O OD1 . ASP A  1 168 ? 14.227  -5.746  69.734  1.00 20.00  ? 160 ASP A OD1 1 
ATOM   1334  O OD2 . ASP A  1 168 ? 15.077  -6.636  71.553  1.00 20.00  ? 160 ASP A OD2 1 
ATOM   1335  N N   . ASP A  1 169 ? 10.979  -5.729  74.146  1.00 72.91  ? 161 ASP A N   1 
ATOM   1336  C CA  . ASP A  1 169 ? 11.901  -4.595  74.239  1.00 63.17  ? 161 ASP A CA  1 
ATOM   1337  C C   . ASP A  1 169 ? 12.072  -4.010  75.635  1.00 55.54  ? 161 ASP A C   1 
ATOM   1338  O O   . ASP A  1 169 ? 11.114  -3.892  76.400  1.00 54.76  ? 161 ASP A O   1 
ATOM   1339  C CB  . ASP A  1 169 ? 11.480  -3.483  73.269  1.00 64.63  ? 161 ASP A CB  1 
ATOM   1340  C CG  . ASP A  1 169 ? 10.789  -4.018  72.029  1.00 56.54  ? 161 ASP A CG  1 
ATOM   1341  O OD1 . ASP A  1 169 ? 9.752   -4.699  72.172  1.00 45.70  ? 161 ASP A OD1 1 
ATOM   1342  O OD2 . ASP A  1 169 ? 11.283  -3.757  70.912  1.00 54.96  ? 161 ASP A OD2 1 
ATOM   1343  N N   . SER A  1 170 ? 13.305  -3.625  75.941  1.00 64.63  ? 162 SER A N   1 
ATOM   1344  C CA  . SER A  1 170 ? 13.593  -2.703  77.018  1.00 66.79  ? 162 SER A CA  1 
ATOM   1345  C C   . SER A  1 170 ? 14.633  -1.678  76.577  1.00 64.01  ? 162 SER A C   1 
ATOM   1346  O O   . SER A  1 170 ? 15.124  -0.908  77.403  1.00 64.24  ? 162 SER A O   1 
ATOM   1347  C CB  . SER A  1 170 ? 14.088  -3.458  78.253  1.00 59.99  ? 162 SER A CB  1 
ATOM   1348  O OG  . SER A  1 170 ? 15.487  -3.676  78.190  1.00 49.17  ? 162 SER A OG  1 
ATOM   1349  N N   . GLU A  1 171 ? 14.997  -1.670  75.293  1.00 57.20  ? 163 GLU A N   1 
ATOM   1350  C CA  . GLU A  1 171 ? 16.114  -0.913  74.928  1.00 49.15  ? 163 GLU A CA  1 
ATOM   1351  C C   . GLU A  1 171 ? 15.660  0.416   74.545  1.00 49.99  ? 163 GLU A C   1 
ATOM   1352  O O   . GLU A  1 171 ? 16.268  1.371   74.931  1.00 47.40  ? 163 GLU A O   1 
ATOM   1353  C CB  . GLU A  1 171 ? 16.966  -1.602  73.882  1.00 51.94  ? 163 GLU A CB  1 
ATOM   1354  C CG  . GLU A  1 171 ? 17.846  -2.715  74.370  1.00 48.80  ? 163 GLU A CG  1 
ATOM   1355  C CD  . GLU A  1 171 ? 18.678  -3.278  73.243  1.00 62.65  ? 163 GLU A CD  1 
ATOM   1356  O OE1 . GLU A  1 171 ? 18.963  -4.504  73.229  1.00 68.77  ? 163 GLU A OE1 1 
ATOM   1357  O OE2 . GLU A  1 171 ? 19.049  -2.469  72.372  1.00 55.96  ? 163 GLU A OE2 1 
ATOM   1358  N N   . TYR A  1 172 ? 14.567  0.501   73.801  1.00 45.57  ? 164 TYR A N   1 
ATOM   1359  C CA  . TYR A  1 172 ? 14.274  1.800   73.218  1.00 42.89  ? 164 TYR A CA  1 
ATOM   1360  C C   . TYR A  1 172 ? 13.009  2.416   73.802  1.00 33.29  ? 164 TYR A C   1 
ATOM   1361  O O   . TYR A  1 172 ? 12.699  3.585   73.555  1.00 25.82  ? 164 TYR A O   1 
ATOM   1362  C CB  . TYR A  1 172 ? 14.161  1.710   71.687  1.00 43.84  ? 164 TYR A CB  1 
ATOM   1363  C CG  . TYR A  1 172 ? 15.226  0.878   70.995  1.00 50.13  ? 164 TYR A CG  1 
ATOM   1364  C CD1 . TYR A  1 172 ? 16.528  1.359   70.819  1.00 55.45  ? 164 TYR A CD1 1 
ATOM   1365  C CD2 . TYR A  1 172 ? 14.923  -0.383  70.496  1.00 50.28  ? 164 TYR A CD2 1 
ATOM   1366  C CE1 . TYR A  1 172 ? 17.499  0.590   70.176  1.00 51.34  ? 164 TYR A CE1 1 
ATOM   1367  C CE2 . TYR A  1 172 ? 15.877  -1.152  69.861  1.00 50.79  ? 164 TYR A CE2 1 
ATOM   1368  C CZ  . TYR A  1 172 ? 17.159  -0.668  69.696  1.00 56.02  ? 164 TYR A CZ  1 
ATOM   1369  O OH  . TYR A  1 172 ? 18.088  -1.463  69.055  1.00 51.92  ? 164 TYR A OH  1 
ATOM   1370  N N   . PHE A  1 173 ? 12.283  1.631   74.585  1.00 34.07  ? 165 PHE A N   1 
ATOM   1371  C CA  . PHE A  1 173 ? 11.012  2.095   75.123  1.00 25.49  ? 165 PHE A CA  1 
ATOM   1372  C C   . PHE A  1 173 ? 11.172  3.268   76.104  1.00 26.08  ? 165 PHE A C   1 
ATOM   1373  O O   . PHE A  1 173 ? 12.042  3.262   76.974  1.00 25.65  ? 165 PHE A O   1 
ATOM   1374  C CB  . PHE A  1 173 ? 10.226  0.939   75.738  1.00 25.12  ? 165 PHE A CB  1 
ATOM   1375  C CG  . PHE A  1 173 ? 8.788   1.266   75.969  1.00 28.30  ? 165 PHE A CG  1 
ATOM   1376  C CD1 . PHE A  1 173 ? 7.886   1.238   74.916  1.00 21.78  ? 165 PHE A CD1 1 
ATOM   1377  C CD2 . PHE A  1 173 ? 8.345   1.654   77.224  1.00 21.91  ? 165 PHE A CD2 1 
ATOM   1378  C CE1 . PHE A  1 173 ? 6.564   1.559   75.110  1.00 21.20  ? 165 PHE A CE1 1 
ATOM   1379  C CE2 . PHE A  1 173 ? 7.030   1.979   77.432  1.00 21.41  ? 165 PHE A CE2 1 
ATOM   1380  C CZ  . PHE A  1 173 ? 6.132   1.931   76.371  1.00 27.66  ? 165 PHE A CZ  1 
ATOM   1381  N N   . SER A  1 174 ? 10.342  4.292   75.930  1.00 23.11  ? 166 SER A N   1 
ATOM   1382  C CA  . SER A  1 174 ? 10.431  5.505   76.739  1.00 24.72  ? 166 SER A CA  1 
ATOM   1383  C C   . SER A  1 174 ? 10.206  5.222   78.227  1.00 24.92  ? 166 SER A C   1 
ATOM   1384  O O   . SER A  1 174 ? 9.196   4.639   78.610  1.00 26.85  ? 166 SER A O   1 
ATOM   1385  C CB  . SER A  1 174 ? 9.412   6.541   76.262  1.00 22.38  ? 166 SER A CB  1 
ATOM   1386  O OG  . SER A  1 174 ? 9.635   7.795   76.882  1.00 20.96  ? 166 SER A OG  1 
ATOM   1387  N N   . GLN A  1 175 ? 11.150  5.650   79.057  1.00 24.30  ? 167 GLN A N   1 
ATOM   1388  C CA  . GLN A  1 175 ? 11.051  5.464   80.493  1.00 23.45  ? 167 GLN A CA  1 
ATOM   1389  C C   . GLN A  1 175 ? 9.978   6.381   81.072  1.00 28.03  ? 167 GLN A C   1 
ATOM   1390  O O   . GLN A  1 175 ? 9.428   6.114   82.139  1.00 29.21  ? 167 GLN A O   1 
ATOM   1391  C CB  . GLN A  1 175 ? 12.402  5.739   81.147  1.00 22.28  ? 167 GLN A CB  1 
ATOM   1392  C CG  . GLN A  1 175 ? 12.657  7.199   81.430  1.00 32.09  ? 167 GLN A CG  1 
ATOM   1393  C CD  . GLN A  1 175 ? 14.107  7.482   81.724  1.00 32.06  ? 167 GLN A CD  1 
ATOM   1394  O OE1 . GLN A  1 175 ? 14.991  6.915   81.086  1.00 38.41  ? 167 GLN A OE1 1 
ATOM   1395  N NE2 . GLN A  1 175 ? 14.367  8.367   82.687  1.00 29.15  ? 167 GLN A NE2 1 
ATOM   1396  N N   . TYR A  1 176 ? 9.666   7.442   80.333  1.00 29.40  ? 168 TYR A N   1 
ATOM   1397  C CA  . TYR A  1 176 ? 8.738   8.474   80.778  1.00 24.04  ? 168 TYR A CA  1 
ATOM   1398  C C   . TYR A  1 176 ? 7.289   8.186   80.402  1.00 24.49  ? 168 TYR A C   1 
ATOM   1399  O O   . TYR A  1 176 ? 6.394   8.955   80.758  1.00 27.24  ? 168 TYR A O   1 
ATOM   1400  C CB  . TYR A  1 176 ? 9.156   9.825   80.205  1.00 26.09  ? 168 TYR A CB  1 
ATOM   1401  C CG  . TYR A  1 176 ? 10.550  10.239  80.612  1.00 35.21  ? 168 TYR A CG  1 
ATOM   1402  C CD1 . TYR A  1 176 ? 10.937  10.210  81.951  1.00 32.72  ? 168 TYR A CD1 1 
ATOM   1403  C CD2 . TYR A  1 176 ? 11.488  10.647  79.664  1.00 24.33  ? 168 TYR A CD2 1 
ATOM   1404  C CE1 . TYR A  1 176 ? 12.212  10.586  82.340  1.00 34.06  ? 168 TYR A CE1 1 
ATOM   1405  C CE2 . TYR A  1 176 ? 12.766  11.024  80.044  1.00 24.15  ? 168 TYR A CE2 1 
ATOM   1406  C CZ  . TYR A  1 176 ? 13.124  10.992  81.385  1.00 37.12  ? 168 TYR A CZ  1 
ATOM   1407  O OH  . TYR A  1 176 ? 14.388  11.369  81.791  1.00 39.10  ? 168 TYR A OH  1 
ATOM   1408  N N   . SER A  1 177 ? 7.057   7.094   79.681  1.00 18.92  ? 169 SER A N   1 
ATOM   1409  C CA  . SER A  1 177 ? 5.696   6.643   79.385  1.00 23.95  ? 169 SER A CA  1 
ATOM   1410  C C   . SER A  1 177 ? 4.927   6.153   80.635  1.00 28.24  ? 169 SER A C   1 
ATOM   1411  O O   . SER A  1 177 ? 5.514   5.577   81.551  1.00 34.10  ? 169 SER A O   1 
ATOM   1412  C CB  . SER A  1 177 ? 5.736   5.540   78.325  1.00 24.97  ? 169 SER A CB  1 
ATOM   1413  O OG  . SER A  1 177 ? 4.547   4.769   78.331  1.00 26.17  ? 169 SER A OG  1 
ATOM   1414  N N   . ARG A  1 178 ? 3.612   6.368   80.666  1.00 26.31  ? 170 ARG A N   1 
ATOM   1415  C CA  . ARG A  1 178 ? 2.779   5.882   81.769  1.00 26.10  ? 170 ARG A CA  1 
ATOM   1416  C C   . ARG A  1 178 ? 2.729   4.364   81.787  1.00 28.59  ? 170 ARG A C   1 
ATOM   1417  O O   . ARG A  1 178 ? 2.144   3.761   82.694  1.00 28.27  ? 170 ARG A O   1 
ATOM   1418  C CB  . ARG A  1 178 ? 1.341   6.394   81.650  1.00 25.87  ? 170 ARG A CB  1 
ATOM   1419  C CG  . ARG A  1 178 ? 1.149   7.844   81.973  1.00 30.39  ? 170 ARG A CG  1 
ATOM   1420  C CD  . ARG A  1 178 ? -0.257  8.286   81.602  1.00 35.95  ? 170 ARG A CD  1 
ATOM   1421  N NE  . ARG A  1 178 ? -1.158  8.367   82.751  1.00 43.75  ? 170 ARG A NE  1 
ATOM   1422  C CZ  . ARG A  1 178 ? -2.185  7.547   82.958  1.00 43.89  ? 170 ARG A CZ  1 
ATOM   1423  N NH1 . ARG A  1 178 ? -2.439  6.577   82.089  1.00 55.64  ? 170 ARG A NH1 1 
ATOM   1424  N NH2 . ARG A  1 178 ? -2.957  7.696   84.028  1.00 32.60  ? 170 ARG A NH2 1 
ATOM   1425  N N   . PHE A  1 179 ? 3.315   3.741   80.774  1.00 26.08  ? 171 PHE A N   1 
ATOM   1426  C CA  . PHE A  1 179 ? 3.235   2.294   80.652  1.00 31.52  ? 171 PHE A CA  1 
ATOM   1427  C C   . PHE A  1 179 ? 4.616   1.656   80.704  1.00 30.30  ? 171 PHE A C   1 
ATOM   1428  O O   . PHE A  1 179 ? 5.642   2.334   80.562  1.00 29.87  ? 171 PHE A O   1 
ATOM   1429  C CB  . PHE A  1 179 ? 2.487   1.895   79.367  1.00 29.63  ? 171 PHE A CB  1 
ATOM   1430  C CG  . PHE A  1 179 ? 1.112   2.502   79.255  1.00 27.43  ? 171 PHE A CG  1 
ATOM   1431  C CD1 . PHE A  1 179 ? 0.945   3.790   78.768  1.00 25.66  ? 171 PHE A CD1 1 
ATOM   1432  C CD2 . PHE A  1 179 ? -0.009  1.790   79.646  1.00 26.02  ? 171 PHE A CD2 1 
ATOM   1433  C CE1 . PHE A  1 179 ? -0.308  4.355   78.671  1.00 26.50  ? 171 PHE A CE1 1 
ATOM   1434  C CE2 . PHE A  1 179 ? -1.272  2.355   79.561  1.00 24.93  ? 171 PHE A CE2 1 
ATOM   1435  C CZ  . PHE A  1 179 ? -1.417  3.640   79.071  1.00 27.17  ? 171 PHE A CZ  1 
ATOM   1436  N N   . GLU A  1 180 ? 4.635   0.351   80.931  1.00 27.29  ? 172 GLU A N   1 
ATOM   1437  C CA  . GLU A  1 180 ? 5.874   -0.406  80.841  1.00 28.43  ? 172 GLU A CA  1 
ATOM   1438  C C   . GLU A  1 180 ? 5.608   -1.710  80.121  1.00 30.10  ? 172 GLU A C   1 
ATOM   1439  O O   . GLU A  1 180 ? 4.497   -2.262  80.188  1.00 28.17  ? 172 GLU A O   1 
ATOM   1440  C CB  . GLU A  1 180 ? 6.503   -0.648  82.223  1.00 36.78  ? 172 GLU A CB  1 
ATOM   1441  C CG  . GLU A  1 180 ? 5.519   -0.848  83.381  1.00 43.48  ? 172 GLU A CG  1 
ATOM   1442  C CD  . GLU A  1 180 ? 6.183   -1.423  84.631  1.00 45.47  ? 172 GLU A CD  1 
ATOM   1443  O OE1 . GLU A  1 180 ? 7.438   -1.441  84.688  1.00 44.39  ? 172 GLU A OE1 1 
ATOM   1444  O OE2 . GLU A  1 180 ? 5.444   -1.865  85.546  1.00 44.33  ? 172 GLU A OE2 1 
ATOM   1445  N N   . ILE A  1 181 ? 6.621   -2.186  79.403  1.00 26.64  ? 173 ILE A N   1 
ATOM   1446  C CA  . ILE A  1 181 ? 6.495   -3.438  78.669  1.00 27.49  ? 173 ILE A CA  1 
ATOM   1447  C C   . ILE A  1 181 ? 6.913   -4.618  79.541  1.00 32.73  ? 173 ILE A C   1 
ATOM   1448  O O   . ILE A  1 181 ? 7.965   -4.596  80.191  1.00 35.75  ? 173 ILE A O   1 
ATOM   1449  C CB  . ILE A  1 181 ? 7.333   -3.430  77.385  1.00 29.86  ? 173 ILE A CB  1 
ATOM   1450  C CG1 . ILE A  1 181 ? 6.902   -2.279  76.478  1.00 28.41  ? 173 ILE A CG1 1 
ATOM   1451  C CG2 . ILE A  1 181 ? 7.215   -4.760  76.657  1.00 29.28  ? 173 ILE A CG2 1 
ATOM   1452  C CD1 . ILE A  1 181 ? 7.816   -2.092  75.317  1.00 28.39  ? 173 ILE A CD1 1 
ATOM   1453  N N   . LEU A  1 182 ? 6.070   -5.639  79.560  1.00 29.59  ? 174 LEU A N   1 
ATOM   1454  C CA  . LEU A  1 182 ? 6.364   -6.861  80.277  1.00 30.40  ? 174 LEU A CA  1 
ATOM   1455  C C   . LEU A  1 182 ? 7.063   -7.808  79.321  1.00 35.77  ? 174 LEU A C   1 
ATOM   1456  O O   . LEU A  1 182 ? 7.975   -8.548  79.703  1.00 44.19  ? 174 LEU A O   1 
ATOM   1457  C CB  . LEU A  1 182 ? 5.065   -7.498  80.776  1.00 33.66  ? 174 LEU A CB  1 
ATOM   1458  C CG  . LEU A  1 182 ? 4.108   -6.565  81.519  1.00 25.84  ? 174 LEU A CG  1 
ATOM   1459  C CD1 . LEU A  1 182 ? 2.832   -7.291  81.848  1.00 26.83  ? 174 LEU A CD1 1 
ATOM   1460  C CD2 . LEU A  1 182 ? 4.770   -6.014  82.772  1.00 27.84  ? 174 LEU A CD2 1 
ATOM   1461  N N   . ASP A  1 183 ? 6.544   -7.859  78.100  1.00 40.86  ? 175 ASP A N   1 
ATOM   1462  C CA  . ASP A  1 183 ? 7.104   -8.700  77.056  1.00 37.17  ? 175 ASP A CA  1 
ATOM   1463  C C   . ASP A  1 183 ? 6.675   -8.236  75.669  1.00 36.87  ? 175 ASP A C   1 
ATOM   1464  O O   . ASP A  1 183 ? 5.685   -7.521  75.514  1.00 37.92  ? 175 ASP A O   1 
ATOM   1465  C CB  . ASP A  1 183 ? 6.696   -10.160 77.270  1.00 32.62  ? 175 ASP A CB  1 
ATOM   1466  C CG  . ASP A  1 183 ? 7.442   -11.112 76.357  1.00 39.96  ? 175 ASP A CG  1 
ATOM   1467  O OD1 . ASP A  1 183 ? 8.558   -10.764 75.916  1.00 35.87  ? 175 ASP A OD1 1 
ATOM   1468  O OD2 . ASP A  1 183 ? 6.914   -12.210 76.080  1.00 46.48  ? 175 ASP A OD2 1 
ATOM   1469  N N   . VAL A  1 184 ? 7.428   -8.666  74.666  1.00 36.97  ? 176 VAL A N   1 
ATOM   1470  C CA  . VAL A  1 184 ? 7.045   -8.528  73.268  1.00 30.77  ? 176 VAL A CA  1 
ATOM   1471  C C   . VAL A  1 184 ? 7.294   -9.850  72.562  1.00 33.32  ? 176 VAL A C   1 
ATOM   1472  O O   . VAL A  1 184 ? 8.326   -10.479 72.759  1.00 35.85  ? 176 VAL A O   1 
ATOM   1473  C CB  . VAL A  1 184 ? 7.842   -7.420  72.547  1.00 30.91  ? 176 VAL A CB  1 
ATOM   1474  C CG1 . VAL A  1 184 ? 7.355   -7.263  71.098  1.00 29.26  ? 176 VAL A CG1 1 
ATOM   1475  C CG2 . VAL A  1 184 ? 7.736   -6.096  73.295  1.00 26.80  ? 176 VAL A CG2 1 
ATOM   1476  N N   . THR A  1 185 ? 6.339   -10.261 71.738  1.00 37.42  ? 177 THR A N   1 
ATOM   1477  C CA  . THR A  1 185 ? 6.422   -11.515 70.995  1.00 42.99  ? 177 THR A CA  1 
ATOM   1478  C C   . THR A  1 185 ? 6.088   -11.323 69.496  1.00 44.37  ? 177 THR A C   1 
ATOM   1479  O O   . THR A  1 185 ? 5.013   -10.822 69.135  1.00 40.79  ? 177 THR A O   1 
ATOM   1480  C CB  . THR A  1 185 ? 5.526   -12.607 71.663  1.00 42.65  ? 177 THR A CB  1 
ATOM   1481  O OG1 . THR A  1 185 ? 6.301   -13.325 72.631  1.00 46.18  ? 177 THR A OG1 1 
ATOM   1482  C CG2 . THR A  1 185 ? 4.957   -13.592 70.641  1.00 41.10  ? 177 THR A CG2 1 
ATOM   1483  N N   . GLN A  1 186 ? 7.022   -11.716 68.631  1.00 43.03  ? 178 GLN A N   1 
ATOM   1484  C CA  . GLN A  1 186 ? 6.859   -11.558 67.189  1.00 40.57  ? 178 GLN A CA  1 
ATOM   1485  C C   . GLN A  1 186 ? 6.892   -12.917 66.501  1.00 41.39  ? 178 GLN A C   1 
ATOM   1486  O O   . GLN A  1 186 ? 7.947   -13.544 66.432  1.00 45.03  ? 178 GLN A O   1 
ATOM   1487  C CB  . GLN A  1 186 ? 7.959   -10.651 66.631  1.00 40.99  ? 178 GLN A CB  1 
ATOM   1488  C CG  . GLN A  1 186 ? 8.045   -9.270  67.303  1.00 41.50  ? 178 GLN A CG  1 
ATOM   1489  C CD  . GLN A  1 186 ? 8.961   -8.299  66.567  1.00 36.86  ? 178 GLN A CD  1 
ATOM   1490  O OE1 . GLN A  1 186 ? 9.484   -8.608  65.495  1.00 50.92  ? 178 GLN A OE1 1 
ATOM   1491  N NE2 . GLN A  1 186 ? 9.160   -7.124  67.141  1.00 24.73  ? 178 GLN A NE2 1 
ATOM   1492  N N   . LYS A  1 187 ? 5.738   -13.368 66.000  1.00 38.84  ? 179 LYS A N   1 
ATOM   1493  C CA  . LYS A  1 187 ? 5.611   -14.705 65.395  1.00 43.22  ? 179 LYS A CA  1 
ATOM   1494  C C   . LYS A  1 187 ? 5.077   -14.732 63.956  1.00 41.57  ? 179 LYS A C   1 
ATOM   1495  O O   . LYS A  1 187 ? 4.169   -13.980 63.594  1.00 38.74  ? 179 LYS A O   1 
ATOM   1496  C CB  . LYS A  1 187 ? 4.738   -15.628 66.269  1.00 41.78  ? 179 LYS A CB  1 
ATOM   1497  C CG  . LYS A  1 187 ? 5.459   -16.248 67.470  1.00 48.59  ? 179 LYS A CG  1 
ATOM   1498  C CD  . LYS A  1 187 ? 4.482   -16.990 68.387  1.00 58.99  ? 179 LYS A CD  1 
ATOM   1499  C CE  . LYS A  1 187 ? 5.206   -17.694 69.530  1.00 47.83  ? 179 LYS A CE  1 
ATOM   1500  N NZ  . LYS A  1 187 ? 6.100   -16.760 70.270  1.00 41.09  ? 179 LYS A NZ  1 
ATOM   1501  N N   . LYS A  1 188 ? 5.640   -15.628 63.150  1.00 37.11  ? 180 LYS A N   1 
ATOM   1502  C CA  . LYS A  1 188 ? 5.147   -15.892 61.806  1.00 33.43  ? 180 LYS A CA  1 
ATOM   1503  C C   . LYS A  1 188 ? 3.736   -16.482 61.864  1.00 40.93  ? 180 LYS A C   1 
ATOM   1504  O O   . LYS A  1 188 ? 3.362   -17.114 62.858  1.00 40.73  ? 180 LYS A O   1 
ATOM   1505  C CB  . LYS A  1 188 ? 6.090   -16.873 61.114  1.00 37.59  ? 180 LYS A CB  1 
ATOM   1506  C CG  . LYS A  1 188 ? 6.146   -16.770 59.602  1.00 47.30  ? 180 LYS A CG  1 
ATOM   1507  C CD  . LYS A  1 188 ? 7.160   -17.753 59.035  1.00 46.78  ? 180 LYS A CD  1 
ATOM   1508  C CE  . LYS A  1 188 ? 7.211   -17.671 57.522  1.00 52.58  ? 180 LYS A CE  1 
ATOM   1509  N NZ  . LYS A  1 188 ? 7.567   -16.299 57.068  1.00 46.79  ? 180 LYS A NZ  1 
ATOM   1510  N N   . ASN A  1 189 ? 2.962   -16.271 60.800  1.00 39.75  ? 181 ASN A N   1 
ATOM   1511  C CA  . ASN A  1 189 ? 1.597   -16.793 60.682  1.00 42.20  ? 181 ASN A CA  1 
ATOM   1512  C C   . ASN A  1 189 ? 1.123   -16.621 59.246  1.00 46.00  ? 181 ASN A C   1 
ATOM   1513  O O   . ASN A  1 189 ? 1.726   -15.861 58.497  1.00 53.24  ? 181 ASN A O   1 
ATOM   1514  C CB  . ASN A  1 189 ? 0.656   -16.054 61.631  1.00 43.65  ? 181 ASN A CB  1 
ATOM   1515  C CG  . ASN A  1 189 ? -0.459  -16.938 62.154  1.00 58.13  ? 181 ASN A CG  1 
ATOM   1516  O OD1 . ASN A  1 189 ? -1.634  -16.566 62.114  1.00 65.50  ? 181 ASN A OD1 1 
ATOM   1517  N ND2 . ASN A  1 189 ? -0.097  -18.123 62.646  1.00 53.35  ? 181 ASN A ND2 1 
ATOM   1518  N N   . SER A  1 190 ? 0.062   -17.313 58.841  1.00 44.11  ? 182 SER A N   1 
ATOM   1519  C CA  . SER A  1 190 ? -0.443  -17.148 57.469  1.00 45.04  ? 182 SER A CA  1 
ATOM   1520  C C   . SER A  1 190 ? -1.968  -17.288 57.345  1.00 48.06  ? 182 SER A C   1 
ATOM   1521  O O   . SER A  1 190 ? -2.672  -17.316 58.357  1.00 58.43  ? 182 SER A O   1 
ATOM   1522  C CB  . SER A  1 190 ? 0.290   -18.081 56.497  1.00 42.06  ? 182 SER A CB  1 
ATOM   1523  O OG  . SER A  1 190 ? 0.394   -19.390 57.020  1.00 52.46  ? 182 SER A OG  1 
ATOM   1524  N N   . VAL A  1 191 ? -2.482  -17.359 56.117  1.00 41.25  ? 183 VAL A N   1 
ATOM   1525  C CA  . VAL A  1 191 ? -3.933  -17.424 55.911  1.00 48.00  ? 183 VAL A CA  1 
ATOM   1526  C C   . VAL A  1 191 ? -4.383  -18.382 54.803  1.00 44.21  ? 183 VAL A C   1 
ATOM   1527  O O   . VAL A  1 191 ? -5.580  -18.470 54.495  1.00 38.40  ? 183 VAL A O   1 
ATOM   1528  C CB  . VAL A  1 191 ? -4.518  -16.033 55.612  1.00 48.02  ? 183 VAL A CB  1 
ATOM   1529  C CG1 . VAL A  1 191 ? -4.536  -15.167 56.878  1.00 42.80  ? 183 VAL A CG1 1 
ATOM   1530  C CG2 . VAL A  1 191 ? -3.716  -15.373 54.515  1.00 42.18  ? 183 VAL A CG2 1 
ATOM   1531  N N   . GLU A  1 198 ? -4.996  -19.038 48.180  1.00 44.61  ? 190 GLU A N   1 
ATOM   1532  C CA  . GLU A  1 198 ? -3.583  -18.652 48.179  1.00 47.21  ? 190 GLU A CA  1 
ATOM   1533  C C   . GLU A  1 198 ? -3.278  -17.776 49.395  1.00 43.03  ? 190 GLU A C   1 
ATOM   1534  O O   . GLU A  1 198 ? -4.130  -17.008 49.848  1.00 46.93  ? 190 GLU A O   1 
ATOM   1535  C CB  . GLU A  1 198 ? -3.199  -17.956 46.864  1.00 47.36  ? 190 GLU A CB  1 
ATOM   1536  C CG  . GLU A  1 198 ? -3.137  -18.888 45.632  1.00 49.84  ? 190 GLU A CG  1 
ATOM   1537  C CD  . GLU A  1 198 ? -4.418  -19.711 45.406  1.00 65.72  ? 190 GLU A CD  1 
ATOM   1538  O OE1 . GLU A  1 198 ? -5.514  -19.266 45.825  1.00 67.81  ? 190 GLU A OE1 1 
ATOM   1539  O OE2 . GLU A  1 198 ? -4.329  -20.815 44.819  1.00 62.02  ? 190 GLU A OE2 1 
ATOM   1540  N N   . ALA A  1 199 ? -2.062  -17.901 49.914  1.00 35.29  ? 191 ALA A N   1 
ATOM   1541  C CA  . ALA A  1 199 ? -1.734  -17.434 51.257  1.00 32.84  ? 191 ALA A CA  1 
ATOM   1542  C C   . ALA A  1 199 ? -1.058  -16.068 51.326  1.00 29.42  ? 191 ALA A C   1 
ATOM   1543  O O   . ALA A  1 199 ? -0.290  -15.712 50.453  1.00 31.53  ? 191 ALA A O   1 
ATOM   1544  C CB  . ALA A  1 199 ? -0.866  -18.474 51.963  1.00 30.93  ? 191 ALA A CB  1 
ATOM   1545  N N   . TYR A  1 200 ? -1.352  -15.320 52.388  1.00 37.27  ? 192 TYR A N   1 
ATOM   1546  C CA  . TYR A  1 200 ? -0.636  -14.090 52.722  1.00 33.69  ? 192 TYR A CA  1 
ATOM   1547  C C   . TYR A  1 200 ? 0.107   -14.304 54.029  1.00 33.99  ? 192 TYR A C   1 
ATOM   1548  O O   . TYR A  1 200 ? -0.516  -14.416 55.080  1.00 40.22  ? 192 TYR A O   1 
ATOM   1549  C CB  . TYR A  1 200 ? -1.595  -12.898 52.892  1.00 30.38  ? 192 TYR A CB  1 
ATOM   1550  C CG  . TYR A  1 200 ? -2.334  -12.499 51.636  1.00 28.08  ? 192 TYR A CG  1 
ATOM   1551  C CD1 . TYR A  1 200 ? -3.586  -13.026 51.352  1.00 23.55  ? 192 TYR A CD1 1 
ATOM   1552  C CD2 . TYR A  1 200 ? -1.774  -11.602 50.722  1.00 25.40  ? 192 TYR A CD2 1 
ATOM   1553  C CE1 . TYR A  1 200 ? -4.268  -12.670 50.204  1.00 24.81  ? 192 TYR A CE1 1 
ATOM   1554  C CE2 . TYR A  1 200 ? -2.449  -11.247 49.560  1.00 19.21  ? 192 TYR A CE2 1 
ATOM   1555  C CZ  . TYR A  1 200 ? -3.697  -11.784 49.311  1.00 23.57  ? 192 TYR A CZ  1 
ATOM   1556  O OH  . TYR A  1 200 ? -4.384  -11.446 48.171  1.00 27.48  ? 192 TYR A OH  1 
ATOM   1557  N N   . GLU A  1 201 ? 1.431   -14.374 53.958  1.00 31.94  ? 193 GLU A N   1 
ATOM   1558  C CA  . GLU A  1 201 ? 2.263   -14.410 55.149  1.00 32.32  ? 193 GLU A CA  1 
ATOM   1559  C C   . GLU A  1 201 ? 2.168   -13.093 55.912  1.00 40.08  ? 193 GLU A C   1 
ATOM   1560  O O   . GLU A  1 201 ? 1.901   -12.048 55.322  1.00 40.21  ? 193 GLU A O   1 
ATOM   1561  C CB  . GLU A  1 201 ? 3.714   -14.699 54.781  1.00 26.07  ? 193 GLU A CB  1 
ATOM   1562  C CG  . GLU A  1 201 ? 3.918   -16.092 54.229  1.00 32.07  ? 193 GLU A CG  1 
ATOM   1563  C CD  . GLU A  1 201 ? 5.381   -16.430 54.029  1.00 39.01  ? 193 GLU A CD  1 
ATOM   1564  O OE1 . GLU A  1 201 ? 6.218   -15.849 54.762  1.00 34.82  ? 193 GLU A OE1 1 
ATOM   1565  O OE2 . GLU A  1 201 ? 5.692   -17.266 53.140  1.00 37.70  ? 193 GLU A OE2 1 
ATOM   1566  N N   . ASP A  1 202 ? 2.380   -13.157 57.228  1.00 44.68  ? 194 ASP A N   1 
ATOM   1567  C CA  . ASP A  1 202 ? 2.360   -11.978 58.095  1.00 39.58  ? 194 ASP A CA  1 
ATOM   1568  C C   . ASP A  1 202 ? 3.065   -12.244 59.426  1.00 40.61  ? 194 ASP A C   1 
ATOM   1569  O O   . ASP A  1 202 ? 3.168   -13.391 59.864  1.00 42.38  ? 194 ASP A O   1 
ATOM   1570  C CB  . ASP A  1 202 ? 0.925   -11.525 58.366  1.00 38.35  ? 194 ASP A CB  1 
ATOM   1571  C CG  . ASP A  1 202 ? 0.173   -12.479 59.286  1.00 48.34  ? 194 ASP A CG  1 
ATOM   1572  O OD1 . ASP A  1 202 ? 0.262   -12.322 60.532  1.00 43.22  ? 194 ASP A OD1 1 
ATOM   1573  O OD2 . ASP A  1 202 ? -0.518  -13.381 58.758  1.00 49.62  ? 194 ASP A OD2 1 
ATOM   1574  N N   . VAL A  1 203 ? 3.542   -11.177 60.062  1.00 32.98  ? 195 VAL A N   1 
ATOM   1575  C CA  . VAL A  1 203 ? 4.156   -11.269 61.381  1.00 34.99  ? 195 VAL A CA  1 
ATOM   1576  C C   . VAL A  1 203 ? 3.208   -10.759 62.482  1.00 34.70  ? 195 VAL A C   1 
ATOM   1577  O O   . VAL A  1 203 ? 2.890   -9.574  62.537  1.00 34.03  ? 195 VAL A O   1 
ATOM   1578  C CB  . VAL A  1 203 ? 5.503   -10.512 61.407  1.00 30.12  ? 195 VAL A CB  1 
ATOM   1579  C CG1 . VAL A  1 203 ? 5.999   -10.310 62.826  1.00 32.21  ? 195 VAL A CG1 1 
ATOM   1580  C CG2 . VAL A  1 203 ? 6.527   -11.275 60.613  1.00 38.28  ? 195 VAL A CG2 1 
ATOM   1581  N N   . GLU A  1 204 ? 2.730   -11.652 63.347  1.00 41.48  ? 196 GLU A N   1 
ATOM   1582  C CA  . GLU A  1 204 ? 1.879   -11.224 64.463  1.00 35.87  ? 196 GLU A CA  1 
ATOM   1583  C C   . GLU A  1 204 ? 2.765   -10.752 65.608  1.00 34.32  ? 196 GLU A C   1 
ATOM   1584  O O   . GLU A  1 204 ? 3.620   -11.492 66.086  1.00 34.93  ? 196 GLU A O   1 
ATOM   1585  C CB  . GLU A  1 204 ? 0.944   -12.343 64.931  1.00 36.16  ? 196 GLU A CB  1 
ATOM   1586  C CG  . GLU A  1 204 ? -0.181  -11.863 65.853  1.00 43.85  ? 196 GLU A CG  1 
ATOM   1587  C CD  . GLU A  1 204 ? -0.979  -13.001 66.505  1.00 55.30  ? 196 GLU A CD  1 
ATOM   1588  O OE1 . GLU A  1 204 ? -0.648  -13.381 67.653  1.00 60.23  ? 196 GLU A OE1 1 
ATOM   1589  O OE2 . GLU A  1 204 ? -1.947  -13.502 65.887  1.00 50.08  ? 196 GLU A OE2 1 
ATOM   1590  N N   . VAL A  1 205 ? 2.585   -9.501  66.015  1.00 32.28  ? 197 VAL A N   1 
ATOM   1591  C CA  . VAL A  1 205 ? 3.369   -8.938  67.103  1.00 34.18  ? 197 VAL A CA  1 
ATOM   1592  C C   . VAL A  1 205 ? 2.476   -8.837  68.323  1.00 33.44  ? 197 VAL A C   1 
ATOM   1593  O O   . VAL A  1 205 ? 1.361   -8.333  68.234  1.00 33.74  ? 197 VAL A O   1 
ATOM   1594  C CB  . VAL A  1 205 ? 3.929   -7.547  66.750  1.00 35.22  ? 197 VAL A CB  1 
ATOM   1595  C CG1 . VAL A  1 205 ? 4.597   -6.906  67.963  1.00 29.75  ? 197 VAL A CG1 1 
ATOM   1596  C CG2 . VAL A  1 205 ? 4.909   -7.656  65.600  1.00 36.15  ? 197 VAL A CG2 1 
ATOM   1597  N N   . SER A  1 206 ? 2.959   -9.342  69.453  1.00 36.14  ? 198 SER A N   1 
ATOM   1598  C CA  . SER A  1 206 ? 2.178   -9.362  70.683  1.00 27.18  ? 198 SER A CA  1 
ATOM   1599  C C   . SER A  1 206 ? 2.852   -8.540  71.768  1.00 31.16  ? 198 SER A C   1 
ATOM   1600  O O   . SER A  1 206 ? 3.938   -8.884  72.244  1.00 30.00  ? 198 SER A O   1 
ATOM   1601  C CB  . SER A  1 206 ? 1.971   -10.791 71.150  1.00 27.07  ? 198 SER A CB  1 
ATOM   1602  O OG  . SER A  1 206 ? 0.985   -11.422 70.359  1.00 33.12  ? 198 SER A OG  1 
ATOM   1603  N N   . LEU A  1 207 ? 2.199   -7.445  72.144  1.00 28.43  ? 199 LEU A N   1 
ATOM   1604  C CA  . LEU A  1 207 ? 2.753   -6.506  73.103  1.00 26.72  ? 199 LEU A CA  1 
ATOM   1605  C C   . LEU A  1 207 ? 2.050   -6.675  74.447  1.00 31.82  ? 199 LEU A C   1 
ATOM   1606  O O   . LEU A  1 207 ? 0.848   -6.404  74.586  1.00 31.34  ? 199 LEU A O   1 
ATOM   1607  C CB  . LEU A  1 207 ? 2.624   -5.075  72.568  1.00 24.00  ? 199 LEU A CB  1 
ATOM   1608  C CG  . LEU A  1 207 ? 3.047   -3.880  73.435  1.00 25.64  ? 199 LEU A CG  1 
ATOM   1609  C CD1 . LEU A  1 207 ? 4.437   -4.048  74.031  1.00 22.58  ? 199 LEU A CD1 1 
ATOM   1610  C CD2 . LEU A  1 207 ? 2.964   -2.573  72.625  1.00 18.72  ? 199 LEU A CD2 1 
ATOM   1611  N N   . ASN A  1 208 ? 2.802   -7.165  75.426  1.00 32.78  ? 200 ASN A N   1 
ATOM   1612  C CA  . ASN A  1 208 ? 2.304   -7.321  76.787  1.00 28.30  ? 200 ASN A CA  1 
ATOM   1613  C C   . ASN A  1 208 ? 2.701   -6.095  77.594  1.00 22.96  ? 200 ASN A C   1 
ATOM   1614  O O   . ASN A  1 208 ? 3.875   -5.883  77.881  1.00 20.69  ? 200 ASN A O   1 
ATOM   1615  C CB  . ASN A  1 208 ? 2.896   -8.581  77.418  1.00 33.67  ? 200 ASN A CB  1 
ATOM   1616  C CG  . ASN A  1 208 ? 1.916   -9.300  78.330  1.00 33.78  ? 200 ASN A CG  1 
ATOM   1617  O OD1 . ASN A  1 208 ? 1.594   -8.809  79.407  1.00 30.02  ? 200 ASN A OD1 1 
ATOM   1618  N ND2 . ASN A  1 208 ? 1.447   -10.479 77.904  1.00 32.80  ? 200 ASN A ND2 1 
ATOM   1619  N N   . PHE A  1 209 ? 1.726   -5.268  77.939  1.00 23.66  ? 201 PHE A N   1 
ATOM   1620  C CA  . PHE A  1 209 ? 2.018   -4.039  78.674  1.00 27.56  ? 201 PHE A CA  1 
ATOM   1621  C C   . PHE A  1 209 ? 1.033   -3.820  79.842  1.00 27.27  ? 201 PHE A C   1 
ATOM   1622  O O   . PHE A  1 209 ? -0.035  -4.438  79.890  1.00 27.03  ? 201 PHE A O   1 
ATOM   1623  C CB  . PHE A  1 209 ? 2.024   -2.841  77.719  1.00 20.75  ? 201 PHE A CB  1 
ATOM   1624  C CG  . PHE A  1 209 ? 0.682   -2.531  77.127  1.00 15.47  ? 201 PHE A CG  1 
ATOM   1625  C CD1 . PHE A  1 209 ? 0.099   -3.385  76.224  1.00 16.06  ? 201 PHE A CD1 1 
ATOM   1626  C CD2 . PHE A  1 209 ? 0.006   -1.379  77.486  1.00 20.22  ? 201 PHE A CD2 1 
ATOM   1627  C CE1 . PHE A  1 209 ? -1.128  -3.109  75.689  1.00 21.41  ? 201 PHE A CE1 1 
ATOM   1628  C CE2 . PHE A  1 209 ? -1.224  -1.089  76.949  1.00 16.63  ? 201 PHE A CE2 1 
ATOM   1629  C CZ  . PHE A  1 209 ? -1.795  -1.957  76.053  1.00 18.89  ? 201 PHE A CZ  1 
ATOM   1630  N N   . ARG A  1 210 ? 1.408   -2.959  80.786  1.00 23.45  ? 202 ARG A N   1 
ATOM   1631  C CA  . ARG A  1 210 ? 0.523   -2.597  81.888  1.00 30.72  ? 202 ARG A CA  1 
ATOM   1632  C C   . ARG A  1 210 ? 0.809   -1.192  82.427  1.00 29.78  ? 202 ARG A C   1 
ATOM   1633  O O   . ARG A  1 210 ? 1.911   -0.657  82.247  1.00 25.12  ? 202 ARG A O   1 
ATOM   1634  C CB  . ARG A  1 210 ? 0.627   -3.622  83.023  1.00 35.36  ? 202 ARG A CB  1 
ATOM   1635  C CG  . ARG A  1 210 ? 2.032   -3.804  83.560  1.00 31.25  ? 202 ARG A CG  1 
ATOM   1636  C CD  . ARG A  1 210 ? 1.994   -4.093  85.039  1.00 32.05  ? 202 ARG A CD  1 
ATOM   1637  N NE  . ARG A  1 210 ? 3.327   -4.115  85.633  1.00 33.13  ? 202 ARG A NE  1 
ATOM   1638  C CZ  . ARG A  1 210 ? 3.936   -5.215  86.060  1.00 30.53  ? 202 ARG A CZ  1 
ATOM   1639  N NH1 . ARG A  1 210 ? 3.332   -6.392  85.957  1.00 29.02  ? 202 ARG A NH1 1 
ATOM   1640  N NH2 . ARG A  1 210 ? 5.146   -5.137  86.595  1.00 29.32  ? 202 ARG A NH2 1 
ATOM   1641  N N   . LYS A  1 211 ? -0.180  -0.605  83.099  1.00 28.12  ? 203 LYS A N   1 
ATOM   1642  C CA  . LYS A  1 211 ? 0.005   0.722   83.688  1.00 36.84  ? 203 LYS A CA  1 
ATOM   1643  C C   . LYS A  1 211 ? 0.920   0.656   84.902  1.00 32.73  ? 203 LYS A C   1 
ATOM   1644  O O   . LYS A  1 211 ? 1.160   -0.416  85.446  1.00 34.11  ? 203 LYS A O   1 
ATOM   1645  C CB  . LYS A  1 211 ? -1.330  1.368   84.081  1.00 33.33  ? 203 LYS A CB  1 
ATOM   1646  C CG  . LYS A  1 211 ? -1.282  2.896   84.036  1.00 32.61  ? 203 LYS A CG  1 
ATOM   1647  C CD  . LYS A  1 211 ? -2.506  3.555   84.650  1.00 45.44  ? 203 LYS A CD  1 
ATOM   1648  C CE  . LYS A  1 211 ? -2.363  3.728   86.155  1.00 44.38  ? 203 LYS A CE  1 
ATOM   1649  N NZ  . LYS A  1 211 ? -3.499  4.511   86.732  1.00 57.24  ? 203 LYS A NZ  1 
ATOM   1650  N N   . LYS A  1 212 ? 1.424   1.809   85.326  1.00 34.36  ? 204 LYS A N   1 
ATOM   1651  C CA  . LYS A  1 212 ? 2.302   1.872   86.488  1.00 44.44  ? 204 LYS A CA  1 
ATOM   1652  C C   . LYS A  1 212 ? 1.560   2.232   87.787  1.00 53.79  ? 204 LYS A C   1 
ATOM   1653  O O   . LYS A  1 212 ? 0.684   3.100   87.798  1.00 54.22  ? 204 LYS A O   1 
ATOM   1654  C CB  . LYS A  1 212 ? 3.449   2.849   86.233  1.00 41.23  ? 204 LYS A CB  1 
ATOM   1655  C CG  . LYS A  1 212 ? 4.373   2.445   85.086  1.00 33.13  ? 204 LYS A CG  1 
ATOM   1656  C CD  . LYS A  1 212 ? 5.495   3.454   84.961  1.00 30.66  ? 204 LYS A CD  1 
ATOM   1657  C CE  . LYS A  1 212 ? 6.376   3.204   83.756  1.00 31.46  ? 204 LYS A CE  1 
ATOM   1658  N NZ  . LYS A  1 212 ? 7.383   4.308   83.581  1.00 24.19  ? 204 LYS A NZ  1 
ATOM   1659  N N   . GLY A  1 213 ? 1.920   1.553   88.874  1.00 51.17  ? 205 GLY A N   1 
ATOM   1660  C CA  . GLY A  1 213 ? 1.310   1.786   90.171  1.00 54.67  ? 205 GLY A CA  1 
ATOM   1661  C C   . GLY A  1 213 ? 2.120   1.197   91.318  1.00 57.41  ? 205 GLY A C   1 
ATOM   1662  O O   . GLY A  1 213 ? 1.723   0.214   91.953  1.00 47.52  ? 205 GLY A O   1 
ATOM   1663  N N   . LYS B  1 3   ? 3.249   -20.198 39.691  1.00 41.92  ? -5  LYS B N   1 
ATOM   1664  C CA  . LYS B  1 3   ? 3.552   -20.383 38.277  1.00 52.56  ? -5  LYS B CA  1 
ATOM   1665  C C   . LYS B  1 3   ? 4.986   -19.948 37.952  1.00 54.51  ? -5  LYS B C   1 
ATOM   1666  O O   . LYS B  1 3   ? 5.948   -20.443 38.547  1.00 51.95  ? -5  LYS B O   1 
ATOM   1667  C CB  . LYS B  1 3   ? 2.544   -19.612 37.414  1.00 51.16  ? -5  LYS B CB  1 
ATOM   1668  C CG  . LYS B  1 3   ? 1.745   -20.491 36.477  1.00 54.28  ? -5  LYS B CG  1 
ATOM   1669  C CD  . LYS B  1 3   ? 2.683   -21.339 35.637  1.00 54.98  ? -5  LYS B CD  1 
ATOM   1670  C CE  . LYS B  1 3   ? 1.931   -22.331 34.782  1.00 58.62  ? -5  LYS B CE  1 
ATOM   1671  N NZ  . LYS B  1 3   ? 2.885   -23.166 34.006  1.00 71.75  ? -5  LYS B NZ  1 
ATOM   1672  N N   . ASP B  1 4   ? 5.129   -18.971 37.065  1.00 56.27  ? -4  ASP B N   1 
ATOM   1673  C CA  . ASP B  1 4   ? 6.429   -18.362 36.783  1.00 46.88  ? -4  ASP B CA  1 
ATOM   1674  C C   . ASP B  1 4   ? 6.563   -17.096 37.625  1.00 41.68  ? -4  ASP B C   1 
ATOM   1675  O O   . ASP B  1 4   ? 7.479   -16.293 37.447  1.00 40.09  ? -4  ASP B O   1 
ATOM   1676  C CB  . ASP B  1 4   ? 6.558   -18.028 35.297  1.00 41.66  ? -4  ASP B CB  1 
ATOM   1677  C CG  . ASP B  1 4   ? 6.264   -19.218 34.404  1.00 43.39  ? -4  ASP B CG  1 
ATOM   1678  O OD1 . ASP B  1 4   ? 7.161   -19.622 33.636  1.00 42.58  ? -4  ASP B OD1 1 
ATOM   1679  O OD2 . ASP B  1 4   ? 5.135   -19.749 34.472  1.00 51.20  ? -4  ASP B OD2 1 
ATOM   1680  N N   . ASP B  1 5   ? 5.610   -16.941 38.536  1.00 42.77  ? -3  ASP B N   1 
ATOM   1681  C CA  . ASP B  1 5   ? 5.267   -15.678 39.203  1.00 37.66  ? -3  ASP B CA  1 
ATOM   1682  C C   . ASP B  1 5   ? 6.488   -14.865 39.633  1.00 36.38  ? -3  ASP B C   1 
ATOM   1683  O O   . ASP B  1 5   ? 6.412   -13.644 39.754  1.00 35.10  ? -3  ASP B O   1 
ATOM   1684  C CB  . ASP B  1 5   ? 4.345   -15.923 40.413  1.00 41.31  ? -3  ASP B CB  1 
ATOM   1685  C CG  . ASP B  1 5   ? 2.859   -15.730 40.081  1.00 51.24  ? -3  ASP B CG  1 
ATOM   1686  O OD1 . ASP B  1 5   ? 2.205   -16.708 39.652  1.00 46.05  ? -3  ASP B OD1 1 
ATOM   1687  O OD2 . ASP B  1 5   ? 2.341   -14.599 40.262  1.00 51.48  ? -3  ASP B OD2 1 
ATOM   1688  N N   . ASP B  1 6   ? 7.616   -15.535 39.840  1.00 34.43  ? -2  ASP B N   1 
ATOM   1689  C CA  . ASP B  1 6   ? 8.798   -14.874 40.390  1.00 34.89  ? -2  ASP B CA  1 
ATOM   1690  C C   . ASP B  1 6   ? 9.890   -14.488 39.361  1.00 41.37  ? -2  ASP B C   1 
ATOM   1691  O O   . ASP B  1 6   ? 11.071  -14.379 39.718  1.00 39.43  ? -2  ASP B O   1 
ATOM   1692  C CB  . ASP B  1 6   ? 9.415   -15.735 41.500  1.00 40.24  ? -2  ASP B CB  1 
ATOM   1693  C CG  . ASP B  1 6   ? 8.551   -15.810 42.769  1.00 44.88  ? -2  ASP B CG  1 
ATOM   1694  O OD1 . ASP B  1 6   ? 9.133   -15.715 43.875  1.00 38.07  ? -2  ASP B OD1 1 
ATOM   1695  O OD2 . ASP B  1 6   ? 7.314   -15.990 42.673  1.00 43.90  ? -2  ASP B OD2 1 
ATOM   1696  N N   . ASP B  1 7   ? 9.508   -14.275 38.101  1.00 32.28  ? -1  ASP B N   1 
ATOM   1697  C CA  . ASP B  1 7   ? 10.458  -13.787 37.101  1.00 29.63  ? -1  ASP B CA  1 
ATOM   1698  C C   . ASP B  1 7   ? 10.387  -12.255 37.015  1.00 24.93  ? -1  ASP B C   1 
ATOM   1699  O O   . ASP B  1 7   ? 9.454   -11.696 36.435  1.00 23.49  ? -1  ASP B O   1 
ATOM   1700  C CB  . ASP B  1 7   ? 10.180  -14.429 35.734  1.00 36.37  ? -1  ASP B CB  1 
ATOM   1701  C CG  . ASP B  1 7   ? 11.383  -14.365 34.787  1.00 40.75  ? -1  ASP B CG  1 
ATOM   1702  O OD1 . ASP B  1 7   ? 11.410  -13.465 33.918  1.00 38.55  ? -1  ASP B OD1 1 
ATOM   1703  O OD2 . ASP B  1 7   ? 12.292  -15.221 34.901  1.00 44.20  ? -1  ASP B OD2 1 
ATOM   1704  N N   . LYS B  1 8   ? 11.378  -11.583 37.594  1.00 21.38  ? 0   LYS B N   1 
ATOM   1705  C CA  . LYS B  1 8   ? 11.356  -10.130 37.721  1.00 14.29  ? 0   LYS B CA  1 
ATOM   1706  C C   . LYS B  1 8   ? 11.204  -9.417  36.382  1.00 20.00  ? 0   LYS B C   1 
ATOM   1707  O O   . LYS B  1 8   ? 10.464  -8.429  36.279  1.00 15.78  ? 0   LYS B O   1 
ATOM   1708  C CB  . LYS B  1 8   ? 12.595  -9.631  38.460  1.00 14.12  ? 0   LYS B CB  1 
ATOM   1709  C CG  . LYS B  1 8   ? 12.480  -8.203  38.958  1.00 17.25  ? 0   LYS B CG  1 
ATOM   1710  C CD  . LYS B  1 8   ? 13.730  -7.739  39.721  1.00 14.00  ? 0   LYS B CD  1 
ATOM   1711  C CE  . LYS B  1 8   ? 13.603  -6.283  40.136  1.00 10.52  ? 0   LYS B CE  1 
ATOM   1712  N NZ  . LYS B  1 8   ? 14.879  -5.525  40.005  1.00 21.59  ? 0   LYS B NZ  1 
ATOM   1713  N N   . LEU B  1 9   ? 11.885  -9.927  35.355  1.00 20.83  ? 1   LEU B N   1 
ATOM   1714  C CA  . LEU B  1 9   ? 11.801  -9.333  34.028  1.00 15.96  ? 1   LEU B CA  1 
ATOM   1715  C C   . LEU B  1 9   ? 10.420  -9.537  33.393  1.00 20.38  ? 1   LEU B C   1 
ATOM   1716  O O   . LEU B  1 9   ? 9.860   -8.623  32.795  1.00 19.82  ? 1   LEU B O   1 
ATOM   1717  C CB  . LEU B  1 9   ? 12.892  -9.881  33.120  1.00 22.34  ? 1   LEU B CB  1 
ATOM   1718  C CG  . LEU B  1 9   ? 12.868  -9.298  31.706  1.00 22.09  ? 1   LEU B CG  1 
ATOM   1719  C CD1 . LEU B  1 9   ? 13.265  -7.830  31.730  1.00 21.24  ? 1   LEU B CD1 1 
ATOM   1720  C CD2 . LEU B  1 9   ? 13.757  -10.100 30.775  1.00 22.79  ? 1   LEU B CD2 1 
ATOM   1721  N N   . ASP B  1 10  ? 9.874   -10.739 33.520  1.00 23.24  ? 2   ASP B N   1 
ATOM   1722  C CA  . ASP B  1 10  ? 8.511   -11.007 33.081  1.00 21.48  ? 2   ASP B CA  1 
ATOM   1723  C C   . ASP B  1 10  ? 7.563   -9.966  33.671  1.00 21.20  ? 2   ASP B C   1 
ATOM   1724  O O   . ASP B  1 10  ? 6.767   -9.373  32.945  1.00 23.21  ? 2   ASP B O   1 
ATOM   1725  C CB  . ASP B  1 10  ? 8.074   -12.409 33.531  1.00 29.85  ? 2   ASP B CB  1 
ATOM   1726  C CG  . ASP B  1 10  ? 8.255   -13.472 32.455  1.00 32.55  ? 2   ASP B CG  1 
ATOM   1727  O OD1 . ASP B  1 10  ? 9.078   -13.267 31.532  1.00 36.33  ? 2   ASP B OD1 1 
ATOM   1728  O OD2 . ASP B  1 10  ? 7.578   -14.525 32.549  1.00 27.02  ? 2   ASP B OD2 1 
ATOM   1729  N N   . ARG B  1 11  ? 7.662   -9.744  34.985  1.00 19.56  ? 3   ARG B N   1 
ATOM   1730  C CA  . ARG B  1 11  ? 6.809   -8.785  35.701  1.00 16.52  ? 3   ARG B CA  1 
ATOM   1731  C C   . ARG B  1 11  ? 6.992   -7.335  35.228  1.00 13.82  ? 3   ARG B C   1 
ATOM   1732  O O   . ARG B  1 11  ? 6.022   -6.642  34.940  1.00 9.61   ? 3   ARG B O   1 
ATOM   1733  C CB  . ARG B  1 11  ? 7.064   -8.865  37.212  1.00 16.30  ? 3   ARG B CB  1 
ATOM   1734  C CG  . ARG B  1 11  ? 6.840   -10.239 37.801  1.00 19.13  ? 3   ARG B CG  1 
ATOM   1735  C CD  . ARG B  1 11  ? 7.139   -10.286 39.294  1.00 18.28  ? 3   ARG B CD  1 
ATOM   1736  N NE  . ARG B  1 11  ? 6.093   -9.617  40.065  1.00 24.05  ? 3   ARG B NE  1 
ATOM   1737  C CZ  . ARG B  1 11  ? 4.995   -10.212 40.527  1.00 25.52  ? 3   ARG B CZ  1 
ATOM   1738  N NH1 . ARG B  1 11  ? 4.787   -11.507 40.318  1.00 25.31  ? 3   ARG B NH1 1 
ATOM   1739  N NH2 . ARG B  1 11  ? 4.102   -9.505  41.209  1.00 25.47  ? 3   ARG B NH2 1 
ATOM   1740  N N   . ALA B  1 12  ? 8.247   -6.895  35.145  1.00 17.41  ? 4   ALA B N   1 
ATOM   1741  C CA  . ALA B  1 12  ? 8.571   -5.553  34.674  1.00 13.39  ? 4   ALA B CA  1 
ATOM   1742  C C   . ALA B  1 12  ? 8.040   -5.299  33.265  1.00 13.20  ? 4   ALA B C   1 
ATOM   1743  O O   . ALA B  1 12  ? 7.656   -4.182  32.933  1.00 13.47  ? 4   ALA B O   1 
ATOM   1744  C CB  . ALA B  1 12  ? 10.051  -5.337  34.723  1.00 13.45  ? 4   ALA B CB  1 
ATOM   1745  N N   . ASP B  1 13  ? 8.001   -6.346  32.451  1.00 11.42  ? 5   ASP B N   1 
ATOM   1746  C CA  . ASP B  1 13  ? 7.478   -6.242  31.094  1.00 14.61  ? 5   ASP B CA  1 
ATOM   1747  C C   . ASP B  1 13  ? 5.966   -6.125  31.072  1.00 15.73  ? 5   ASP B C   1 
ATOM   1748  O O   . ASP B  1 13  ? 5.396   -5.456  30.203  1.00 13.79  ? 5   ASP B O   1 
ATOM   1749  C CB  . ASP B  1 13  ? 7.892   -7.451  30.251  1.00 16.25  ? 5   ASP B CB  1 
ATOM   1750  C CG  . ASP B  1 13  ? 9.356   -7.437  29.897  1.00 17.57  ? 5   ASP B CG  1 
ATOM   1751  O OD1 . ASP B  1 13  ? 9.987   -6.355  30.013  1.00 16.61  ? 5   ASP B OD1 1 
ATOM   1752  O OD2 . ASP B  1 13  ? 9.869   -8.508  29.501  1.00 19.22  ? 5   ASP B OD2 1 
ATOM   1753  N N   . ILE B  1 14  ? 5.319   -6.814  32.008  1.00 15.60  ? 6   ILE B N   1 
ATOM   1754  C CA  . ILE B  1 14  ? 3.873   -6.743  32.139  1.00 15.74  ? 6   ILE B CA  1 
ATOM   1755  C C   . ILE B  1 14  ? 3.444   -5.344  32.575  1.00 13.32  ? 6   ILE B C   1 
ATOM   1756  O O   . ILE B  1 14  ? 2.538   -4.750  31.976  1.00 10.75  ? 6   ILE B O   1 
ATOM   1757  C CB  . ILE B  1 14  ? 3.352   -7.811  33.105  1.00 17.02  ? 6   ILE B CB  1 
ATOM   1758  C CG1 . ILE B  1 14  ? 3.549   -9.197  32.481  1.00 15.35  ? 6   ILE B CG1 1 
ATOM   1759  C CG2 . ILE B  1 14  ? 1.880   -7.569  33.435  1.00 13.34  ? 6   ILE B CG2 1 
ATOM   1760  C CD1 . ILE B  1 14  ? 3.043   -10.319 33.338  1.00 21.66  ? 6   ILE B CD1 1 
ATOM   1761  N N   . LEU B  1 15  ? 4.123   -4.814  33.590  1.00 9.11   ? 7   LEU B N   1 
ATOM   1762  C CA  . LEU B  1 15  ? 3.886   -3.456  34.049  1.00 9.62   ? 7   LEU B CA  1 
ATOM   1763  C C   . LEU B  1 15  ? 4.028   -2.440  32.914  1.00 12.85  ? 7   LEU B C   1 
ATOM   1764  O O   . LEU B  1 15  ? 3.163   -1.573  32.734  1.00 11.28  ? 7   LEU B O   1 
ATOM   1765  C CB  . LEU B  1 15  ? 4.840   -3.120  35.182  1.00 15.73  ? 7   LEU B CB  1 
ATOM   1766  C CG  . LEU B  1 15  ? 4.432   -1.952  36.076  1.00 20.77  ? 7   LEU B CG  1 
ATOM   1767  C CD1 . LEU B  1 15  ? 3.213   -2.298  36.934  1.00 10.09  ? 7   LEU B CD1 1 
ATOM   1768  C CD2 . LEU B  1 15  ? 5.619   -1.544  36.926  1.00 16.26  ? 7   LEU B CD2 1 
ATOM   1769  N N   . TYR B  1 16  ? 5.110   -2.564  32.142  1.00 14.17  ? 8   TYR B N   1 
ATOM   1770  C CA  . TYR B  1 16  ? 5.309   -1.784  30.911  1.00 9.54   ? 8   TYR B CA  1 
ATOM   1771  C C   . TYR B  1 16  ? 4.144   -1.869  29.908  1.00 10.97  ? 8   TYR B C   1 
ATOM   1772  O O   . TYR B  1 16  ? 3.664   -0.846  29.441  1.00 11.18  ? 8   TYR B O   1 
ATOM   1773  C CB  . TYR B  1 16  ? 6.618   -2.197  30.227  1.00 11.23  ? 8   TYR B CB  1 
ATOM   1774  C CG  . TYR B  1 16  ? 6.825   -1.624  28.831  1.00 12.40  ? 8   TYR B CG  1 
ATOM   1775  C CD1 . TYR B  1 16  ? 7.174   -0.293  28.638  1.00 9.54   ? 8   TYR B CD1 1 
ATOM   1776  C CD2 . TYR B  1 16  ? 6.689   -2.424  27.712  1.00 15.18  ? 8   TYR B CD2 1 
ATOM   1777  C CE1 . TYR B  1 16  ? 7.359   0.220   27.379  1.00 12.03  ? 8   TYR B CE1 1 
ATOM   1778  C CE2 . TYR B  1 16  ? 6.893   -1.919  26.433  1.00 16.94  ? 8   TYR B CE2 1 
ATOM   1779  C CZ  . TYR B  1 16  ? 7.226   -0.598  26.265  1.00 17.61  ? 8   TYR B CZ  1 
ATOM   1780  O OH  . TYR B  1 16  ? 7.430   -0.109  24.975  1.00 14.73  ? 8   TYR B OH  1 
ATOM   1781  N N   . ASN B  1 17  ? 3.704   -3.080  29.568  1.00 12.05  ? 9   ASN B N   1 
ATOM   1782  C CA  . ASN B  1 17  ? 2.545   -3.270  28.695  1.00 9.34   ? 9   ASN B CA  1 
ATOM   1783  C C   . ASN B  1 17  ? 1.304   -2.575  29.228  1.00 11.64  ? 9   ASN B C   1 
ATOM   1784  O O   . ASN B  1 17  ? 0.653   -1.813  28.512  1.00 12.69  ? 9   ASN B O   1 
ATOM   1785  C CB  . ASN B  1 17  ? 2.217   -4.754  28.517  1.00 12.80  ? 9   ASN B CB  1 
ATOM   1786  C CG  . ASN B  1 17  ? 3.251   -5.505  27.704  1.00 14.61  ? 9   ASN B CG  1 
ATOM   1787  O OD1 . ASN B  1 17  ? 3.990   -4.924  26.907  1.00 22.12  ? 9   ASN B OD1 1 
ATOM   1788  N ND2 . ASN B  1 17  ? 3.302   -6.809  27.898  1.00 15.26  ? 9   ASN B ND2 1 
ATOM   1789  N N   . ILE B  1 18  ? 0.967   -2.861  30.482  1.00 11.34  ? 10  ILE B N   1 
ATOM   1790  C CA  . ILE B  1 18  ? -0.119  -2.174  31.164  1.00 9.16   ? 10  ILE B CA  1 
ATOM   1791  C C   . ILE B  1 18  ? 0.023   -0.643  31.060  1.00 11.93  ? 10  ILE B C   1 
ATOM   1792  O O   . ILE B  1 18  ? -0.908  0.056   30.655  1.00 11.29  ? 10  ILE B O   1 
ATOM   1793  C CB  . ILE B  1 18  ? -0.205  -2.626  32.640  1.00 10.79  ? 10  ILE B CB  1 
ATOM   1794  C CG1 . ILE B  1 18  ? -0.502  -4.126  32.711  1.00 9.23   ? 10  ILE B CG1 1 
ATOM   1795  C CG2 . ILE B  1 18  ? -1.260  -1.825  33.434  1.00 10.53  ? 10  ILE B CG2 1 
ATOM   1796  C CD1 . ILE B  1 18  ? -0.259  -4.717  34.068  1.00 9.73   ? 10  ILE B CD1 1 
ATOM   1797  N N   . ARG B  1 19  ? 1.187   -0.104  31.395  1.00 11.32  ? 11  ARG B N   1 
ATOM   1798  C CA  . ARG B  1 19  ? 1.318   1.349   31.379  1.00 9.76   ? 11  ARG B CA  1 
ATOM   1799  C C   . ARG B  1 19  ? 1.158   1.961   30.010  1.00 10.92  ? 11  ARG B C   1 
ATOM   1800  O O   . ARG B  1 19  ? 0.920   3.151   29.887  1.00 15.53  ? 11  ARG B O   1 
ATOM   1801  C CB  . ARG B  1 19  ? 2.633   1.778   31.991  1.00 8.15   ? 11  ARG B CB  1 
ATOM   1802  C CG  . ARG B  1 19  ? 2.694   1.454   33.461  1.00 11.69  ? 11  ARG B CG  1 
ATOM   1803  C CD  . ARG B  1 19  ? 3.916   2.023   34.120  1.00 9.57   ? 11  ARG B CD  1 
ATOM   1804  N NE  . ARG B  1 19  ? 3.617   2.248   35.518  1.00 17.15  ? 11  ARG B NE  1 
ATOM   1805  C CZ  . ARG B  1 19  ? 4.529   2.264   36.477  1.00 18.50  ? 11  ARG B CZ  1 
ATOM   1806  N NH1 . ARG B  1 19  ? 5.815   2.067   36.180  1.00 15.62  ? 11  ARG B NH1 1 
ATOM   1807  N NH2 . ARG B  1 19  ? 4.143   2.473   37.725  1.00 10.55  ? 11  ARG B NH2 1 
ATOM   1808  N N   . GLN B  1 20  ? 1.297   1.141   28.976  1.00 15.13  ? 12  GLN B N   1 
ATOM   1809  C CA  . GLN B  1 20  ? 1.227   1.620   27.599  1.00 13.05  ? 12  GLN B CA  1 
ATOM   1810  C C   . GLN B  1 20  ? -0.194  1.525   27.050  1.00 13.32  ? 12  GLN B C   1 
ATOM   1811  O O   . GLN B  1 20  ? -0.615  2.357   26.253  1.00 17.01  ? 12  GLN B O   1 
ATOM   1812  C CB  . GLN B  1 20  ? 2.207   0.842   26.726  1.00 11.47  ? 12  GLN B CB  1 
ATOM   1813  C CG  . GLN B  1 20  ? 3.664   1.201   26.986  1.00 13.76  ? 12  GLN B CG  1 
ATOM   1814  C CD  . GLN B  1 20  ? 4.342   1.795   25.756  1.00 18.73  ? 12  GLN B CD  1 
ATOM   1815  O OE1 . GLN B  1 20  ? 4.655   1.081   24.800  1.00 25.70  ? 12  GLN B OE1 1 
ATOM   1816  N NE2 . GLN B  1 20  ? 4.550   3.109   25.767  1.00 16.12  ? 12  GLN B NE2 1 
ATOM   1817  N N   . THR B  1 21  ? -0.942  0.525   27.501  1.00 11.64  ? 13  THR B N   1 
ATOM   1818  C CA  . THR B  1 21  ? -2.317  0.366   27.062  1.00 13.16  ? 13  THR B CA  1 
ATOM   1819  C C   . THR B  1 21  ? -3.304  1.149   27.911  1.00 10.62  ? 13  THR B C   1 
ATOM   1820  O O   . THR B  1 21  ? -4.325  1.622   27.420  1.00 15.75  ? 13  THR B O   1 
ATOM   1821  C CB  . THR B  1 21  ? -2.735  -1.101  27.068  1.00 15.51  ? 13  THR B CB  1 
ATOM   1822  O OG1 . THR B  1 21  ? -1.728  -1.876  26.414  1.00 21.17  ? 13  THR B OG1 1 
ATOM   1823  C CG2 . THR B  1 21  ? -4.047  -1.271  26.325  1.00 19.83  ? 13  THR B CG2 1 
ATOM   1824  N N   . SER B  1 22  ? -2.996  1.293   29.185  1.00 12.67  ? 14  SER B N   1 
ATOM   1825  C CA  . SER B  1 22  ? -3.963  1.818   30.133  1.00 11.09  ? 14  SER B CA  1 
ATOM   1826  C C   . SER B  1 22  ? -4.186  3.298   29.940  1.00 11.83  ? 14  SER B C   1 
ATOM   1827  O O   . SER B  1 22  ? -3.230  4.074   29.852  1.00 11.94  ? 14  SER B O   1 
ATOM   1828  C CB  . SER B  1 22  ? -3.481  1.571   31.555  1.00 11.74  ? 14  SER B CB  1 
ATOM   1829  O OG  . SER B  1 22  ? -3.474  2.783   32.291  1.00 12.65  ? 14  SER B OG  1 
ATOM   1830  N N   . ARG B  1 23  ? -5.453  3.686   29.883  1.00 11.05  ? 15  ARG B N   1 
ATOM   1831  C CA  . ARG B  1 23  ? -5.809  5.093   29.834  1.00 10.86  ? 15  ARG B CA  1 
ATOM   1832  C C   . ARG B  1 23  ? -6.495  5.468   31.140  1.00 10.63  ? 15  ARG B C   1 
ATOM   1833  O O   . ARG B  1 23  ? -7.704  5.310   31.282  1.00 12.52  ? 15  ARG B O   1 
ATOM   1834  C CB  . ARG B  1 23  ? -6.760  5.352   28.671  1.00 16.01  ? 15  ARG B CB  1 
ATOM   1835  C CG  . ARG B  1 23  ? -6.456  4.574   27.405  1.00 16.04  ? 15  ARG B CG  1 
ATOM   1836  C CD  . ARG B  1 23  ? -6.036  5.529   26.311  1.00 27.98  ? 15  ARG B CD  1 
ATOM   1837  N NE  . ARG B  1 23  ? -6.524  5.129   24.994  1.00 27.88  ? 15  ARG B NE  1 
ATOM   1838  C CZ  . ARG B  1 23  ? -6.369  5.865   23.900  1.00 21.63  ? 15  ARG B CZ  1 
ATOM   1839  N NH1 . ARG B  1 23  ? -5.745  7.039   23.974  1.00 14.14  ? 15  ARG B NH1 1 
ATOM   1840  N NH2 . ARG B  1 23  ? -6.846  5.427   22.742  1.00 20.22  ? 15  ARG B NH2 1 
ATOM   1841  N N   . PRO B  1 24  ? -5.726  5.979   32.104  1.00 12.33  ? 16  PRO B N   1 
ATOM   1842  C CA  . PRO B  1 24  ? -6.237  6.203   33.474  1.00 9.85   ? 16  PRO B CA  1 
ATOM   1843  C C   . PRO B  1 24  ? -7.466  7.122   33.590  1.00 9.58   ? 16  PRO B C   1 
ATOM   1844  O O   . PRO B  1 24  ? -8.140  7.103   34.632  1.00 13.50  ? 16  PRO B O   1 
ATOM   1845  C CB  . PRO B  1 24  ? -5.032  6.805   34.220  1.00 8.54   ? 16  PRO B CB  1 
ATOM   1846  C CG  . PRO B  1 24  ? -3.826  6.515   33.325  1.00 9.89   ? 16  PRO B CG  1 
ATOM   1847  C CD  . PRO B  1 24  ? -4.332  6.426   31.923  1.00 6.79   ? 16  PRO B CD  1 
ATOM   1848  N N   . ASP B  1 25  ? -7.781  7.888   32.552  1.00 9.30   ? 17  ASP B N   1 
ATOM   1849  C CA  . ASP B  1 25  ? -8.927  8.799   32.616  1.00 9.98   ? 17  ASP B CA  1 
ATOM   1850  C C   . ASP B  1 25  ? -10.128 8.432   31.757  1.00 9.43   ? 17  ASP B C   1 
ATOM   1851  O O   . ASP B  1 25  ? -11.131 9.141   31.776  1.00 9.63   ? 17  ASP B O   1 
ATOM   1852  C CB  . ASP B  1 25  ? -8.499  10.215  32.268  1.00 12.02  ? 17  ASP B CB  1 
ATOM   1853  C CG  . ASP B  1 25  ? -7.492  10.759  33.237  1.00 19.51  ? 17  ASP B CG  1 
ATOM   1854  O OD1 . ASP B  1 25  ? -7.544  10.344  34.420  1.00 22.71  ? 17  ASP B OD1 1 
ATOM   1855  O OD2 . ASP B  1 25  ? -6.654  11.596  32.821  1.00 23.12  ? 17  ASP B OD2 1 
ATOM   1856  N N   . VAL B  1 26  ? -10.028 7.348   30.995  1.00 9.44   ? 18  VAL B N   1 
ATOM   1857  C CA  . VAL B  1 26  ? -11.112 6.951   30.108  1.00 10.01  ? 18  VAL B CA  1 
ATOM   1858  C C   . VAL B  1 26  ? -11.727 5.658   30.584  1.00 11.74  ? 18  VAL B C   1 
ATOM   1859  O O   . VAL B  1 26  ? -10.995 4.715   30.882  1.00 15.75  ? 18  VAL B O   1 
ATOM   1860  C CB  . VAL B  1 26  ? -10.607 6.732   28.685  1.00 9.65   ? 18  VAL B CB  1 
ATOM   1861  C CG1 . VAL B  1 26  ? -11.766 6.341   27.750  1.00 6.53   ? 18  VAL B CG1 1 
ATOM   1862  C CG2 . VAL B  1 26  ? -9.904  7.982   28.205  1.00 11.14  ? 18  VAL B CG2 1 
ATOM   1863  N N   . ILE B  1 27  ? -13.059 5.601   30.649  1.00 10.59  ? 19  ILE B N   1 
ATOM   1864  C CA  . ILE B  1 27  ? -13.734 4.385   31.117  1.00 14.44  ? 19  ILE B CA  1 
ATOM   1865  C C   . ILE B  1 27  ? -13.490 3.191   30.183  1.00 12.70  ? 19  ILE B C   1 
ATOM   1866  O O   . ILE B  1 27  ? -13.676 3.286   28.979  1.00 11.41  ? 19  ILE B O   1 
ATOM   1867  C CB  . ILE B  1 27  ? -15.275 4.590   31.401  1.00 14.38  ? 19  ILE B CB  1 
ATOM   1868  C CG1 . ILE B  1 27  ? -16.029 5.067   30.149  1.00 12.60  ? 19  ILE B CG1 1 
ATOM   1869  C CG2 . ILE B  1 27  ? -15.504 5.530   32.605  1.00 9.13   ? 19  ILE B CG2 1 
ATOM   1870  C CD1 . ILE B  1 27  ? -17.557 5.229   30.347  1.00 8.17   ? 19  ILE B CD1 1 
ATOM   1871  N N   . PRO B  1 28  ? -13.068 2.052   30.747  1.00 13.51  ? 20  PRO B N   1 
ATOM   1872  C CA  . PRO B  1 28  ? -12.755 0.903   29.896  1.00 12.62  ? 20  PRO B CA  1 
ATOM   1873  C C   . PRO B  1 28  ? -14.010 0.210   29.429  1.00 14.47  ? 20  PRO B C   1 
ATOM   1874  O O   . PRO B  1 28  ? -14.234 -0.925  29.824  1.00 18.89  ? 20  PRO B O   1 
ATOM   1875  C CB  . PRO B  1 28  ? -11.962 -0.020  30.816  1.00 9.95   ? 20  PRO B CB  1 
ATOM   1876  C CG  . PRO B  1 28  ? -12.433 0.319   32.190  1.00 16.57  ? 20  PRO B CG  1 
ATOM   1877  C CD  . PRO B  1 28  ? -12.931 1.748   32.182  1.00 12.54  ? 20  PRO B CD  1 
ATOM   1878  N N   . THR B  1 29  ? -14.818 0.878   28.611  1.00 14.38  ? 21  THR B N   1 
ATOM   1879  C CA  . THR B  1 29  ? -15.984 0.227   28.037  1.00 18.55  ? 21  THR B CA  1 
ATOM   1880  C C   . THR B  1 29  ? -15.524 -0.728  26.934  1.00 31.21  ? 21  THR B C   1 
ATOM   1881  O O   . THR B  1 29  ? -14.568 -0.448  26.210  1.00 31.02  ? 21  THR B O   1 
ATOM   1882  C CB  . THR B  1 29  ? -16.997 1.226   27.458  1.00 18.30  ? 21  THR B CB  1 
ATOM   1883  O OG1 . THR B  1 29  ? -16.395 1.971   26.395  1.00 17.76  ? 21  THR B OG1 1 
ATOM   1884  C CG2 . THR B  1 29  ? -17.503 2.184   28.519  1.00 16.11  ? 21  THR B CG2 1 
ATOM   1885  N N   . GLN B  1 30  ? -16.208 -1.861  26.821  1.00 39.01  ? 22  GLN B N   1 
ATOM   1886  C CA  . GLN B  1 30  ? -15.879 -2.877  25.834  1.00 40.45  ? 22  GLN B CA  1 
ATOM   1887  C C   . GLN B  1 30  ? -17.166 -3.200  25.093  1.00 43.73  ? 22  GLN B C   1 
ATOM   1888  O O   . GLN B  1 30  ? -18.221 -3.308  25.726  1.00 34.36  ? 22  GLN B O   1 
ATOM   1889  C CB  . GLN B  1 30  ? -15.331 -4.127  26.531  1.00 37.53  ? 22  GLN B CB  1 
ATOM   1890  C CG  . GLN B  1 30  ? -14.097 -3.857  27.387  1.00 39.00  ? 22  GLN B CG  1 
ATOM   1891  C CD  . GLN B  1 30  ? -13.752 -5.012  28.316  1.00 38.92  ? 22  GLN B CD  1 
ATOM   1892  O OE1 . GLN B  1 30  ? -12.658 -5.074  28.879  1.00 32.78  ? 22  GLN B OE1 1 
ATOM   1893  N NE2 . GLN B  1 30  ? -14.694 -5.921  28.494  1.00 49.63  ? 22  GLN B NE2 1 
ATOM   1894  N N   . ARG B  1 31  ? -17.100 -3.291  23.772  1.00 45.30  ? 23  ARG B N   1 
ATOM   1895  C CA  . ARG B  1 31  ? -18.278 -3.627  22.990  1.00 45.07  ? 23  ARG B CA  1 
ATOM   1896  C C   . ARG B  1 31  ? -19.393 -2.640  23.306  1.00 43.08  ? 23  ARG B C   1 
ATOM   1897  O O   . ARG B  1 31  ? -20.567 -3.009  23.352  1.00 37.05  ? 23  ARG B O   1 
ATOM   1898  C CB  . ARG B  1 31  ? -18.735 -5.055  23.291  1.00 47.82  ? 23  ARG B CB  1 
ATOM   1899  C CG  . ARG B  1 31  ? -17.650 -6.105  23.109  1.00 53.40  ? 23  ARG B CG  1 
ATOM   1900  C CD  . ARG B  1 31  ? -18.138 -7.481  23.531  1.00 65.24  ? 23  ARG B CD  1 
ATOM   1901  N NE  . ARG B  1 31  ? -17.168 -8.525  23.216  1.00 74.33  ? 23  ARG B NE  1 
ATOM   1902  C CZ  . ARG B  1 31  ? -17.310 -9.403  22.228  1.00 66.78  ? 23  ARG B CZ  1 
ATOM   1903  N NH1 . ARG B  1 31  ? -18.385 -9.364  21.453  1.00 60.78  ? 23  ARG B NH1 1 
ATOM   1904  N NH2 . ARG B  1 31  ? -16.376 -10.320 22.013  1.00 64.84  ? 23  ARG B NH2 1 
ATOM   1905  N N   . ASP B  1 32  ? -19.029 -1.399  23.608  1.00 37.41  ? 24  ASP B N   1 
ATOM   1906  C CA  . ASP B  1 32  ? -20.017 -0.339  23.800  1.00 37.38  ? 24  ASP B CA  1 
ATOM   1907  C C   . ASP B  1 32  ? -21.100 -0.661  24.837  1.00 42.90  ? 24  ASP B C   1 
ATOM   1908  O O   . ASP B  1 32  ? -22.271 -0.344  24.628  1.00 36.19  ? 24  ASP B O   1 
ATOM   1909  C CB  . ASP B  1 32  ? -20.671 0.024   22.463  1.00 34.08  ? 24  ASP B CB  1 
ATOM   1910  C CG  . ASP B  1 32  ? -21.185 1.450   22.435  1.00 45.67  ? 24  ASP B CG  1 
ATOM   1911  O OD1 . ASP B  1 32  ? -21.851 1.863   23.408  1.00 49.34  ? 24  ASP B OD1 1 
ATOM   1912  O OD2 . ASP B  1 32  ? -20.924 2.158   21.440  1.00 46.24  ? 24  ASP B OD2 1 
ATOM   1913  N N   . ARG B  1 33  ? -20.718 -1.281  25.950  1.00 33.15  ? 25  ARG B N   1 
ATOM   1914  C CA  . ARG B  1 33  ? -21.660 -1.581  27.002  1.00 30.11  ? 25  ARG B CA  1 
ATOM   1915  C C   . ARG B  1 33  ? -21.077 -0.940  28.248  1.00 26.10  ? 25  ARG B C   1 
ATOM   1916  O O   . ARG B  1 33  ? -19.876 -0.687  28.296  1.00 22.06  ? 25  ARG B O   1 
ATOM   1917  C CB  . ARG B  1 33  ? -21.774 -3.096  27.189  1.00 37.20  ? 25  ARG B CB  1 
ATOM   1918  C CG  . ARG B  1 33  ? -22.231 -3.845  25.952  1.00 41.98  ? 25  ARG B CG  1 
ATOM   1919  C CD  . ARG B  1 33  ? -22.251 -5.341  26.208  1.00 52.36  ? 25  ARG B CD  1 
ATOM   1920  N NE  . ARG B  1 33  ? -21.965 -6.096  24.993  1.00 69.88  ? 25  ARG B NE  1 
ATOM   1921  C CZ  . ARG B  1 33  ? -21.727 -7.404  24.964  1.00 76.57  ? 25  ARG B CZ  1 
ATOM   1922  N NH1 . ARG B  1 33  ? -21.740 -8.102  26.095  1.00 72.75  ? 25  ARG B NH1 1 
ATOM   1923  N NH2 . ARG B  1 33  ? -21.472 -8.011  23.805  1.00 70.06  ? 25  ARG B NH2 1 
ATOM   1924  N N   . PRO B  1 34  ? -21.917 -0.675  29.262  1.00 23.07  ? 26  PRO B N   1 
ATOM   1925  C CA  . PRO B  1 34  ? -21.421 -0.097  30.513  1.00 19.65  ? 26  PRO B CA  1 
ATOM   1926  C C   . PRO B  1 34  ? -20.314 -0.947  31.141  1.00 18.54  ? 26  PRO B C   1 
ATOM   1927  O O   . PRO B  1 34  ? -20.370 -2.175  31.089  1.00 20.90  ? 26  PRO B O   1 
ATOM   1928  C CB  . PRO B  1 34  ? -22.653 -0.145  31.422  1.00 20.00  ? 26  PRO B CB  1 
ATOM   1929  C CG  . PRO B  1 34  ? -23.809 -0.211  30.506  1.00 20.32  ? 26  PRO B CG  1 
ATOM   1930  C CD  . PRO B  1 34  ? -23.348 -1.007  29.343  1.00 20.35  ? 26  PRO B CD  1 
ATOM   1931  N N   . VAL B  1 35  ? -19.309 -0.300  31.712  1.00 15.49  ? 27  VAL B N   1 
ATOM   1932  C CA  . VAL B  1 35  ? -18.361 -1.008  32.553  1.00 12.62  ? 27  VAL B CA  1 
ATOM   1933  C C   . VAL B  1 35  ? -19.160 -1.603  33.683  1.00 17.04  ? 27  VAL B C   1 
ATOM   1934  O O   . VAL B  1 35  ? -19.963 -0.915  34.331  1.00 18.50  ? 27  VAL B O   1 
ATOM   1935  C CB  . VAL B  1 35  ? -17.329 -0.049  33.153  1.00 14.12  ? 27  VAL B CB  1 
ATOM   1936  C CG1 . VAL B  1 35  ? -16.375 -0.783  34.066  1.00 10.02  ? 27  VAL B CG1 1 
ATOM   1937  C CG2 . VAL B  1 35  ? -16.578 0.650   32.039  1.00 15.34  ? 27  VAL B CG2 1 
ATOM   1938  N N   . ALA B  1 36  ? -18.974 -2.892  33.905  1.00 17.71  ? 28  ALA B N   1 
ATOM   1939  C CA  . ALA B  1 36  ? -19.627 -3.546  35.022  1.00 11.17  ? 28  ALA B CA  1 
ATOM   1940  C C   . ALA B  1 36  ? -18.648 -3.598  36.176  1.00 10.09  ? 28  ALA B C   1 
ATOM   1941  O O   . ALA B  1 36  ? -17.864 -4.531  36.274  1.00 13.15  ? 28  ALA B O   1 
ATOM   1942  C CB  . ALA B  1 36  ? -20.072 -4.951  34.637  1.00 7.05   ? 28  ALA B CB  1 
ATOM   1943  N N   . VAL B  1 37  ? -18.690 -2.587  37.039  1.00 11.52  ? 29  VAL B N   1 
ATOM   1944  C CA  . VAL B  1 37  ? -17.925 -2.590  38.284  1.00 11.25  ? 29  VAL B CA  1 
ATOM   1945  C C   . VAL B  1 37  ? -18.703 -3.371  39.336  1.00 14.18  ? 29  VAL B C   1 
ATOM   1946  O O   . VAL B  1 37  ? -19.925 -3.276  39.399  1.00 18.96  ? 29  VAL B O   1 
ATOM   1947  C CB  . VAL B  1 37  ? -17.713 -1.152  38.815  1.00 11.66  ? 29  VAL B CB  1 
ATOM   1948  C CG1 . VAL B  1 37  ? -17.056 -1.165  40.194  1.00 10.52  ? 29  VAL B CG1 1 
ATOM   1949  C CG2 . VAL B  1 37  ? -16.904 -0.312  37.836  1.00 9.99   ? 29  VAL B CG2 1 
ATOM   1950  N N   . SER B  1 38  ? -18.005 -4.143  40.158  1.00 12.94  ? 30  SER B N   1 
ATOM   1951  C CA  . SER B  1 38  ? -18.635 -4.811  41.276  1.00 12.97  ? 30  SER B CA  1 
ATOM   1952  C C   . SER B  1 38  ? -18.047 -4.284  42.578  1.00 16.49  ? 30  SER B C   1 
ATOM   1953  O O   . SER B  1 38  ? -16.828 -4.244  42.714  1.00 16.72  ? 30  SER B O   1 
ATOM   1954  C CB  . SER B  1 38  ? -18.373 -6.304  41.195  1.00 14.69  ? 30  SER B CB  1 
ATOM   1955  O OG  . SER B  1 38  ? -18.859 -6.839  39.988  1.00 15.66  ? 30  SER B OG  1 
ATOM   1956  N N   . VAL B  1 39  ? -18.900 -3.887  43.527  1.00 17.80  ? 31  VAL B N   1 
ATOM   1957  C CA  . VAL B  1 39  ? -18.434 -3.460  44.852  1.00 17.04  ? 31  VAL B CA  1 
ATOM   1958  C C   . VAL B  1 39  ? -18.999 -4.295  45.978  1.00 16.32  ? 31  VAL B C   1 
ATOM   1959  O O   . VAL B  1 39  ? -20.153 -4.683  45.947  1.00 19.15  ? 31  VAL B O   1 
ATOM   1960  C CB  . VAL B  1 39  ? -18.870 -2.035  45.232  1.00 15.49  ? 31  VAL B CB  1 
ATOM   1961  C CG1 . VAL B  1 39  ? -17.789 -1.390  46.087  1.00 15.72  ? 31  VAL B CG1 1 
ATOM   1962  C CG2 . VAL B  1 39  ? -19.161 -1.210  44.022  1.00 15.07  ? 31  VAL B CG2 1 
ATOM   1963  N N   . SER B  1 40  ? -18.177 -4.516  46.995  1.00 15.36  ? 32  SER B N   1 
ATOM   1964  C CA  . SER B  1 40  ? -18.616 -5.117  48.234  1.00 16.33  ? 32  SER B CA  1 
ATOM   1965  C C   . SER B  1 40  ? -17.823 -4.547  49.416  1.00 16.05  ? 32  SER B C   1 
ATOM   1966  O O   . SER B  1 40  ? -16.600 -4.557  49.412  1.00 17.20  ? 32  SER B O   1 
ATOM   1967  C CB  . SER B  1 40  ? -18.458 -6.636  48.164  1.00 19.02  ? 32  SER B CB  1 
ATOM   1968  O OG  . SER B  1 40  ? -18.849 -7.259  49.375  1.00 17.95  ? 32  SER B OG  1 
ATOM   1969  N N   . LEU B  1 41  ? -18.531 -4.043  50.419  1.00 16.92  ? 33  LEU B N   1 
ATOM   1970  C CA  . LEU B  1 41  ? -17.922 -3.644  51.678  1.00 14.37  ? 33  LEU B CA  1 
ATOM   1971  C C   . LEU B  1 41  ? -17.802 -4.859  52.591  1.00 15.53  ? 33  LEU B C   1 
ATOM   1972  O O   . LEU B  1 41  ? -18.778 -5.572  52.783  1.00 18.44  ? 33  LEU B O   1 
ATOM   1973  C CB  . LEU B  1 41  ? -18.786 -2.582  52.362  1.00 14.81  ? 33  LEU B CB  1 
ATOM   1974  C CG  . LEU B  1 41  ? -19.120 -1.376  51.477  1.00 16.46  ? 33  LEU B CG  1 
ATOM   1975  C CD1 . LEU B  1 41  ? -19.863 -0.288  52.249  1.00 10.42  ? 33  LEU B CD1 1 
ATOM   1976  C CD2 . LEU B  1 41  ? -17.853 -0.842  50.832  1.00 11.33  ? 33  LEU B CD2 1 
ATOM   1977  N N   . LYS B  1 42  ? -16.606 -5.099  53.131  1.00 15.35  ? 34  LYS B N   1 
ATOM   1978  C CA  . LYS B  1 42  ? -16.384 -6.137  54.144  1.00 17.49  ? 34  LYS B CA  1 
ATOM   1979  C C   . LYS B  1 42  ? -16.054 -5.469  55.465  1.00 14.44  ? 34  LYS B C   1 
ATOM   1980  O O   . LYS B  1 42  ? -14.938 -4.983  55.658  1.00 10.43  ? 34  LYS B O   1 
ATOM   1981  C CB  . LYS B  1 42  ? -15.202 -7.058  53.792  1.00 16.71  ? 34  LYS B CB  1 
ATOM   1982  C CG  . LYS B  1 42  ? -15.195 -7.590  52.395  1.00 19.29  ? 34  LYS B CG  1 
ATOM   1983  C CD  . LYS B  1 42  ? -16.407 -8.427  52.088  1.00 17.99  ? 34  LYS B CD  1 
ATOM   1984  C CE  . LYS B  1 42  ? -16.400 -8.768  50.619  1.00 18.68  ? 34  LYS B CE  1 
ATOM   1985  N NZ  . LYS B  1 42  ? -17.561 -9.612  50.260  1.00 25.27  ? 34  LYS B NZ  1 
ATOM   1986  N N   . PHE B  1 43  ? -16.999 -5.478  56.395  1.00 13.72  ? 35  PHE B N   1 
ATOM   1987  C CA  . PHE B  1 43  ? -16.814 -4.684  57.601  1.00 12.46  ? 35  PHE B CA  1 
ATOM   1988  C C   . PHE B  1 43  ? -15.722 -5.205  58.523  1.00 11.77  ? 35  PHE B C   1 
ATOM   1989  O O   . PHE B  1 43  ? -15.550 -6.406  58.679  1.00 15.69  ? 35  PHE B O   1 
ATOM   1990  C CB  . PHE B  1 43  ? -18.142 -4.471  58.300  1.00 12.10  ? 35  PHE B CB  1 
ATOM   1991  C CG  . PHE B  1 43  ? -19.111 -3.688  57.476  1.00 10.42  ? 35  PHE B CG  1 
ATOM   1992  C CD1 . PHE B  1 43  ? -20.021 -4.329  56.660  1.00 10.13  ? 35  PHE B CD1 1 
ATOM   1993  C CD2 . PHE B  1 43  ? -19.083 -2.301  57.492  1.00 10.04  ? 35  PHE B CD2 1 
ATOM   1994  C CE1 . PHE B  1 43  ? -20.909 -3.603  55.886  1.00 12.64  ? 35  PHE B CE1 1 
ATOM   1995  C CE2 . PHE B  1 43  ? -19.969 -1.567  56.732  1.00 9.83   ? 35  PHE B CE2 1 
ATOM   1996  C CZ  . PHE B  1 43  ? -20.882 -2.218  55.921  1.00 11.14  ? 35  PHE B CZ  1 
ATOM   1997  N N   . ILE B  1 44  ? -14.960 -4.278  59.091  1.00 11.82  ? 36  ILE B N   1 
ATOM   1998  C CA  . ILE B  1 44  ? -13.792 -4.604  59.891  1.00 11.43  ? 36  ILE B CA  1 
ATOM   1999  C C   . ILE B  1 44  ? -13.968 -4.045  61.282  1.00 14.76  ? 36  ILE B C   1 
ATOM   2000  O O   . ILE B  1 44  ? -13.569 -4.662  62.270  1.00 18.49  ? 36  ILE B O   1 
ATOM   2001  C CB  . ILE B  1 44  ? -12.535 -3.955  59.306  1.00 11.83  ? 36  ILE B CB  1 
ATOM   2002  C CG1 . ILE B  1 44  ? -12.361 -4.335  57.824  1.00 13.69  ? 36  ILE B CG1 1 
ATOM   2003  C CG2 . ILE B  1 44  ? -11.319 -4.318  60.115  1.00 9.69   ? 36  ILE B CG2 1 
ATOM   2004  C CD1 . ILE B  1 44  ? -12.257 -5.802  57.563  1.00 14.28  ? 36  ILE B CD1 1 
ATOM   2005  N N   . ASN B  1 45  ? -14.568 -2.864  61.370  1.00 15.15  ? 37  ASN B N   1 
ATOM   2006  C CA  . ASN B  1 45  ? -14.739 -2.222  62.664  1.00 13.14  ? 37  ASN B CA  1 
ATOM   2007  C C   . ASN B  1 45  ? -15.831 -1.162  62.686  1.00 16.13  ? 37  ASN B C   1 
ATOM   2008  O O   . ASN B  1 45  ? -16.219 -0.620  61.645  1.00 13.48  ? 37  ASN B O   1 
ATOM   2009  C CB  . ASN B  1 45  ? -13.418 -1.657  63.179  1.00 8.97   ? 37  ASN B CB  1 
ATOM   2010  C CG  . ASN B  1 45  ? -13.279 -1.803  64.690  1.00 18.17  ? 37  ASN B CG  1 
ATOM   2011  O OD1 . ASN B  1 45  ? -14.276 -1.865  65.413  1.00 13.69  ? 37  ASN B OD1 1 
ATOM   2012  N ND2 . ASN B  1 45  ? -12.037 -1.859  65.173  1.00 17.69  ? 37  ASN B ND2 1 
ATOM   2013  N N   . ILE B  1 46  ? -16.351 -0.911  63.886  1.00 15.82  ? 38  ILE B N   1 
ATOM   2014  C CA  . ILE B  1 46  ? -17.265 0.193   64.148  1.00 14.81  ? 38  ILE B CA  1 
ATOM   2015  C C   . ILE B  1 46  ? -16.763 0.881   65.404  1.00 16.21  ? 38  ILE B C   1 
ATOM   2016  O O   . ILE B  1 46  ? -16.767 0.286   66.472  1.00 22.44  ? 38  ILE B O   1 
ATOM   2017  C CB  . ILE B  1 46  ? -18.687 -0.292  64.366  1.00 13.37  ? 38  ILE B CB  1 
ATOM   2018  C CG1 . ILE B  1 46  ? -19.108 -1.208  63.216  1.00 11.53  ? 38  ILE B CG1 1 
ATOM   2019  C CG2 . ILE B  1 46  ? -19.635 0.890   64.508  1.00 11.41  ? 38  ILE B CG2 1 
ATOM   2020  C CD1 . ILE B  1 46  ? -20.459 -1.885  63.434  1.00 14.66  ? 38  ILE B CD1 1 
ATOM   2021  N N   . LEU B  1 47  ? -16.339 2.132   65.276  1.00 16.91  ? 39  LEU B N   1 
ATOM   2022  C CA  . LEU B  1 47  ? -15.493 2.767   66.276  1.00 19.64  ? 39  LEU B CA  1 
ATOM   2023  C C   . LEU B  1 47  ? -16.224 3.706   67.240  1.00 24.58  ? 39  LEU B C   1 
ATOM   2024  O O   . LEU B  1 47  ? -15.992 3.698   68.450  1.00 28.14  ? 39  LEU B O   1 
ATOM   2025  C CB  . LEU B  1 47  ? -14.387 3.544   65.565  1.00 20.71  ? 39  LEU B CB  1 
ATOM   2026  C CG  . LEU B  1 47  ? -13.512 2.694   64.653  1.00 22.72  ? 39  LEU B CG  1 
ATOM   2027  C CD1 . LEU B  1 47  ? -12.389 3.520   64.006  1.00 21.72  ? 39  LEU B CD1 1 
ATOM   2028  C CD2 . LEU B  1 47  ? -12.949 1.503   65.423  1.00 19.32  ? 39  LEU B CD2 1 
ATOM   2029  N N   . GLU B  1 48  ? -17.061 4.562   66.686  1.00 24.52  ? 40  GLU B N   1 
ATOM   2030  C CA  . GLU B  1 48  ? -17.823 5.489   67.489  1.00 21.20  ? 40  GLU B CA  1 
ATOM   2031  C C   . GLU B  1 48  ? -19.177 5.474   66.853  1.00 23.43  ? 40  GLU B C   1 
ATOM   2032  O O   . GLU B  1 48  ? -19.308 5.359   65.635  1.00 30.97  ? 40  GLU B O   1 
ATOM   2033  C CB  . GLU B  1 48  ? -17.239 6.898   67.436  1.00 18.72  ? 40  GLU B CB  1 
ATOM   2034  C CG  . GLU B  1 48  ? -15.817 6.991   67.967  1.00 35.50  ? 40  GLU B CG  1 
ATOM   2035  C CD  . GLU B  1 48  ? -15.137 8.315   67.613  1.00 50.65  ? 40  GLU B CD  1 
ATOM   2036  O OE1 . GLU B  1 48  ? -15.409 9.325   68.302  1.00 51.03  ? 40  GLU B OE1 1 
ATOM   2037  O OE2 . GLU B  1 48  ? -14.331 8.345   66.646  1.00 47.43  ? 40  GLU B OE2 1 
ATOM   2038  N N   . VAL B  1 49  ? -20.191 5.547   67.682  1.00 19.69  ? 41  VAL B N   1 
ATOM   2039  C CA  . VAL B  1 49  ? -21.535 5.651   67.193  1.00 21.34  ? 41  VAL B CA  1 
ATOM   2040  C C   . VAL B  1 49  ? -22.171 6.719   68.066  1.00 23.20  ? 41  VAL B C   1 
ATOM   2041  O O   . VAL B  1 49  ? -22.025 6.707   69.289  1.00 18.37  ? 41  VAL B O   1 
ATOM   2042  C CB  . VAL B  1 49  ? -22.252 4.304   67.322  1.00 22.98  ? 41  VAL B CB  1 
ATOM   2043  C CG1 . VAL B  1 49  ? -23.713 4.498   67.309  1.00 20.71  ? 41  VAL B CG1 1 
ATOM   2044  C CG2 . VAL B  1 49  ? -21.832 3.366   66.206  1.00 19.17  ? 41  VAL B CG2 1 
ATOM   2045  N N   . ASN B  1 50  ? -22.816 7.682   67.433  1.00 21.13  ? 42  ASN B N   1 
ATOM   2046  C CA  . ASN B  1 50  ? -23.513 8.713   68.171  1.00 22.20  ? 42  ASN B CA  1 
ATOM   2047  C C   . ASN B  1 50  ? -24.990 8.600   67.847  1.00 23.82  ? 42  ASN B C   1 
ATOM   2048  O O   . ASN B  1 50  ? -25.396 8.758   66.690  1.00 22.58  ? 42  ASN B O   1 
ATOM   2049  C CB  . ASN B  1 50  ? -22.974 10.090  67.802  1.00 23.21  ? 42  ASN B CB  1 
ATOM   2050  C CG  . ASN B  1 50  ? -23.450 11.180  68.743  1.00 27.77  ? 42  ASN B CG  1 
ATOM   2051  O OD1 . ASN B  1 50  ? -24.558 11.123  69.291  1.00 25.37  ? 42  ASN B OD1 1 
ATOM   2052  N ND2 . ASN B  1 50  ? -22.610 12.190  68.934  1.00 29.48  ? 42  ASN B ND2 1 
ATOM   2053  N N   . GLU B  1 51  ? -25.795 8.310   68.864  1.00 27.61  ? 43  GLU B N   1 
ATOM   2054  C CA  . GLU B  1 51  ? -27.206 8.037   68.631  1.00 26.45  ? 43  GLU B CA  1 
ATOM   2055  C C   . GLU B  1 51  ? -28.015 9.317   68.547  1.00 21.58  ? 43  GLU B C   1 
ATOM   2056  O O   . GLU B  1 51  ? -29.118 9.333   68.003  1.00 19.74  ? 43  GLU B O   1 
ATOM   2057  C CB  . GLU B  1 51  ? -27.764 7.106   69.702  1.00 30.74  ? 43  GLU B CB  1 
ATOM   2058  C CG  . GLU B  1 51  ? -29.092 6.455   69.320  1.00 32.02  ? 43  GLU B CG  1 
ATOM   2059  C CD  . GLU B  1 51  ? -29.646 5.600   70.442  1.00 31.72  ? 43  GLU B CD  1 
ATOM   2060  O OE1 . GLU B  1 51  ? -28.870 5.306   71.377  1.00 33.13  ? 43  GLU B OE1 1 
ATOM   2061  O OE2 . GLU B  1 51  ? -30.846 5.234   70.396  1.00 29.86  ? 43  GLU B OE2 1 
ATOM   2062  N N   . ILE B  1 52  ? -27.452 10.395  69.073  1.00 23.42  ? 44  ILE B N   1 
ATOM   2063  C CA  . ILE B  1 52  ? -28.104 11.697  68.977  1.00 30.85  ? 44  ILE B CA  1 
ATOM   2064  C C   . ILE B  1 52  ? -27.892 12.381  67.612  1.00 28.84  ? 44  ILE B C   1 
ATOM   2065  O O   . ILE B  1 52  ? -28.858 12.791  66.962  1.00 30.19  ? 44  ILE B O   1 
ATOM   2066  C CB  . ILE B  1 52  ? -27.688 12.637  70.128  1.00 29.88  ? 44  ILE B CB  1 
ATOM   2067  C CG1 . ILE B  1 52  ? -28.192 12.101  71.464  1.00 29.11  ? 44  ILE B CG1 1 
ATOM   2068  C CG2 . ILE B  1 52  ? -28.268 14.015  69.916  1.00 29.79  ? 44  ILE B CG2 1 
ATOM   2069  C CD1 . ILE B  1 52  ? -27.932 13.046  72.611  1.00 38.38  ? 44  ILE B CD1 1 
ATOM   2070  N N   . THR B  1 53  ? -26.644 12.509  67.173  1.00 23.90  ? 45  THR B N   1 
ATOM   2071  C CA  . THR B  1 53  ? -26.388 13.117  65.861  1.00 27.40  ? 45  THR B CA  1 
ATOM   2072  C C   . THR B  1 53  ? -26.654 12.171  64.688  1.00 27.95  ? 45  THR B C   1 
ATOM   2073  O O   . THR B  1 53  ? -26.704 12.616  63.540  1.00 26.69  ? 45  THR B O   1 
ATOM   2074  C CB  . THR B  1 53  ? -24.957 13.615  65.741  1.00 20.81  ? 45  THR B CB  1 
ATOM   2075  O OG1 . THR B  1 53  ? -24.065 12.513  65.950  1.00 25.29  ? 45  THR B OG1 1 
ATOM   2076  C CG2 . THR B  1 53  ? -24.691 14.688  66.778  1.00 21.89  ? 45  THR B CG2 1 
ATOM   2077  N N   . ASN B  1 54  ? -26.845 10.882  64.990  1.00 26.75  ? 46  ASN B N   1 
ATOM   2078  C CA  . ASN B  1 54  ? -26.966 9.826   63.981  1.00 21.99  ? 46  ASN B CA  1 
ATOM   2079  C C   . ASN B  1 54  ? -25.722 9.755   63.101  1.00 23.22  ? 46  ASN B C   1 
ATOM   2080  O O   . ASN B  1 54  ? -25.798 9.893   61.885  1.00 21.95  ? 46  ASN B O   1 
ATOM   2081  C CB  . ASN B  1 54  ? -28.233 9.979   63.123  1.00 21.01  ? 46  ASN B CB  1 
ATOM   2082  C CG  . ASN B  1 54  ? -29.456 9.275   63.726  1.00 27.89  ? 46  ASN B CG  1 
ATOM   2083  O OD1 . ASN B  1 54  ? -29.335 8.354   64.541  1.00 22.71  ? 46  ASN B OD1 1 
ATOM   2084  N ND2 . ASN B  1 54  ? -30.646 9.702   63.306  1.00 29.28  ? 46  ASN B ND2 1 
ATOM   2085  N N   . GLU B  1 55  ? -24.571 9.543   63.728  1.00 22.26  ? 47  GLU B N   1 
ATOM   2086  C CA  . GLU B  1 55  ? -23.325 9.440   62.994  1.00 20.65  ? 47  GLU B CA  1 
ATOM   2087  C C   . GLU B  1 55  ? -22.527 8.212   63.413  1.00 21.24  ? 47  GLU B C   1 
ATOM   2088  O O   . GLU B  1 55  ? -22.356 7.961   64.604  1.00 20.36  ? 47  GLU B O   1 
ATOM   2089  C CB  . GLU B  1 55  ? -22.496 10.713  63.185  1.00 20.63  ? 47  GLU B CB  1 
ATOM   2090  C CG  . GLU B  1 55  ? -23.158 11.943  62.587  1.00 20.55  ? 47  GLU B CG  1 
ATOM   2091  C CD  . GLU B  1 55  ? -22.346 13.217  62.773  1.00 25.75  ? 47  GLU B CD  1 
ATOM   2092  O OE1 . GLU B  1 55  ? -21.097 13.161  62.686  1.00 23.02  ? 47  GLU B OE1 1 
ATOM   2093  O OE2 . GLU B  1 55  ? -22.968 14.282  63.002  1.00 30.54  ? 47  GLU B OE2 1 
ATOM   2094  N N   . VAL B  1 56  ? -22.043 7.461   62.420  1.00 20.56  ? 48  VAL B N   1 
ATOM   2095  C CA  . VAL B  1 56  ? -21.206 6.272   62.637  1.00 18.95  ? 48  VAL B CA  1 
ATOM   2096  C C   . VAL B  1 56  ? -19.807 6.409   62.018  1.00 18.94  ? 48  VAL B C   1 
ATOM   2097  O O   . VAL B  1 56  ? -19.614 7.032   60.976  1.00 14.24  ? 48  VAL B O   1 
ATOM   2098  C CB  . VAL B  1 56  ? -21.873 4.971   62.084  1.00 16.04  ? 48  VAL B CB  1 
ATOM   2099  C CG1 . VAL B  1 56  ? -23.307 4.879   62.532  1.00 18.33  ? 48  VAL B CG1 1 
ATOM   2100  C CG2 . VAL B  1 56  ? -21.822 4.933   60.569  1.00 14.69  ? 48  VAL B CG2 1 
ATOM   2101  N N   . ASP B  1 57  ? -18.832 5.800   62.672  1.00 22.38  ? 49  ASP B N   1 
ATOM   2102  C CA  . ASP B  1 57  ? -17.459 5.831   62.209  1.00 20.59  ? 49  ASP B CA  1 
ATOM   2103  C C   . ASP B  1 57  ? -17.043 4.384   61.948  1.00 19.05  ? 49  ASP B C   1 
ATOM   2104  O O   . ASP B  1 57  ? -16.943 3.596   62.886  1.00 23.82  ? 49  ASP B O   1 
ATOM   2105  C CB  . ASP B  1 57  ? -16.606 6.455   63.314  1.00 27.85  ? 49  ASP B CB  1 
ATOM   2106  C CG  . ASP B  1 57  ? -15.205 6.805   62.855  1.00 28.59  ? 49  ASP B CG  1 
ATOM   2107  O OD1 . ASP B  1 57  ? -14.758 6.235   61.842  1.00 20.49  ? 49  ASP B OD1 1 
ATOM   2108  O OD2 . ASP B  1 57  ? -14.549 7.634   63.528  1.00 32.25  ? 49  ASP B OD2 1 
ATOM   2109  N N   . VAL B  1 58  ? -16.827 4.011   60.690  1.00 14.50  ? 50  VAL B N   1 
ATOM   2110  C CA  . VAL B  1 58  ? -16.594 2.596   60.374  1.00 13.42  ? 50  VAL B CA  1 
ATOM   2111  C C   . VAL B  1 58  ? -15.290 2.319   59.628  1.00 12.26  ? 50  VAL B C   1 
ATOM   2112  O O   . VAL B  1 58  ? -14.735 3.198   58.982  1.00 13.11  ? 50  VAL B O   1 
ATOM   2113  C CB  . VAL B  1 58  ? -17.742 1.998   59.552  1.00 10.28  ? 50  VAL B CB  1 
ATOM   2114  C CG1 . VAL B  1 58  ? -19.074 2.413   60.125  1.00 15.10  ? 50  VAL B CG1 1 
ATOM   2115  C CG2 . VAL B  1 58  ? -17.664 2.478   58.159  1.00 12.59  ? 50  VAL B CG2 1 
ATOM   2116  N N   . VAL B  1 59  ? -14.797 1.088   59.737  1.00 11.97  ? 51  VAL B N   1 
ATOM   2117  C CA  . VAL B  1 59  ? -13.665 0.638   58.943  1.00 9.73   ? 51  VAL B CA  1 
ATOM   2118  C C   . VAL B  1 59  ? -14.099 -0.569  58.134  1.00 11.25  ? 51  VAL B C   1 
ATOM   2119  O O   . VAL B  1 59  ? -14.653 -1.517  58.679  1.00 10.95  ? 51  VAL B O   1 
ATOM   2120  C CB  . VAL B  1 59  ? -12.440 0.264   59.795  1.00 9.90   ? 51  VAL B CB  1 
ATOM   2121  C CG1 . VAL B  1 59  ? -11.339 -0.330  58.918  1.00 11.73  ? 51  VAL B CG1 1 
ATOM   2122  C CG2 . VAL B  1 59  ? -11.926 1.475   60.548  1.00 10.56  ? 51  VAL B CG2 1 
ATOM   2123  N N   . PHE B  1 60  ? -13.851 -0.527  56.828  1.00 11.85  ? 52  PHE B N   1 
ATOM   2124  C CA  . PHE B  1 60  ? -14.288 -1.593  55.941  1.00 12.61  ? 52  PHE B CA  1 
ATOM   2125  C C   . PHE B  1 60  ? -13.328 -1.787  54.780  1.00 11.71  ? 52  PHE B C   1 
ATOM   2126  O O   . PHE B  1 60  ? -12.634 -0.866  54.368  1.00 11.31  ? 52  PHE B O   1 
ATOM   2127  C CB  . PHE B  1 60  ? -15.699 -1.310  55.403  1.00 11.38  ? 52  PHE B CB  1 
ATOM   2128  C CG  . PHE B  1 60  ? -15.822 0.011   54.711  1.00 11.30  ? 52  PHE B CG  1 
ATOM   2129  C CD1 . PHE B  1 60  ? -15.607 0.119   53.334  1.00 14.43  ? 52  PHE B CD1 1 
ATOM   2130  C CD2 . PHE B  1 60  ? -16.123 1.152   55.430  1.00 8.99   ? 52  PHE B CD2 1 
ATOM   2131  C CE1 . PHE B  1 60  ? -15.701 1.354   52.680  1.00 12.97  ? 52  PHE B CE1 1 
ATOM   2132  C CE2 . PHE B  1 60  ? -16.222 2.388   54.796  1.00 14.49  ? 52  PHE B CE2 1 
ATOM   2133  C CZ  . PHE B  1 60  ? -16.006 2.494   53.411  1.00 11.91  ? 52  PHE B CZ  1 
ATOM   2134  N N   . TRP B  1 61  ? -13.300 -3.005  54.265  1.00 11.95  ? 53  TRP B N   1 
ATOM   2135  C CA  . TRP B  1 61  ? -12.590 -3.306  53.053  1.00 10.91  ? 53  TRP B CA  1 
ATOM   2136  C C   . TRP B  1 61  ? -13.527 -3.012  51.911  1.00 14.68  ? 53  TRP B C   1 
ATOM   2137  O O   . TRP B  1 61  ? -14.583 -3.639  51.791  1.00 14.47  ? 53  TRP B O   1 
ATOM   2138  C CB  . TRP B  1 61  ? -12.172 -4.763  53.027  1.00 12.45  ? 53  TRP B CB  1 
ATOM   2139  C CG  . TRP B  1 61  ? -11.114 -5.052  54.034  1.00 20.37  ? 53  TRP B CG  1 
ATOM   2140  C CD1 . TRP B  1 61  ? -10.505 -4.149  54.870  1.00 17.37  ? 53  TRP B CD1 1 
ATOM   2141  C CD2 . TRP B  1 61  ? -10.526 -6.332  54.325  1.00 26.36  ? 53  TRP B CD2 1 
ATOM   2142  N NE1 . TRP B  1 61  ? -9.572  -4.790  55.658  1.00 25.09  ? 53  TRP B NE1 1 
ATOM   2143  C CE2 . TRP B  1 61  ? -9.564  -6.126  55.347  1.00 24.55  ? 53  TRP B CE2 1 
ATOM   2144  C CE3 . TRP B  1 61  ? -10.713 -7.629  53.817  1.00 25.00  ? 53  TRP B CE3 1 
ATOM   2145  C CZ2 . TRP B  1 61  ? -8.799  -7.169  55.877  1.00 24.45  ? 53  TRP B CZ2 1 
ATOM   2146  C CZ3 . TRP B  1 61  ? -9.947  -8.665  54.342  1.00 29.11  ? 53  TRP B CZ3 1 
ATOM   2147  C CH2 . TRP B  1 61  ? -9.006  -8.426  55.367  1.00 29.38  ? 53  TRP B CH2 1 
ATOM   2148  N N   . GLN B  1 62  ? -13.149 -2.045  51.081  1.00 12.62  ? 54  GLN B N   1 
ATOM   2149  C CA  . GLN B  1 62  ? -13.963 -1.694  49.935  1.00 12.67  ? 54  GLN B CA  1 
ATOM   2150  C C   . GLN B  1 62  ? -13.470 -2.472  48.714  1.00 15.64  ? 54  GLN B C   1 
ATOM   2151  O O   . GLN B  1 62  ? -12.753 -1.951  47.851  1.00 14.18  ? 54  GLN B O   1 
ATOM   2152  C CB  . GLN B  1 62  ? -13.918 -0.198  49.691  1.00 12.60  ? 54  GLN B CB  1 
ATOM   2153  C CG  . GLN B  1 62  ? -14.964 0.289   48.729  1.00 16.81  ? 54  GLN B CG  1 
ATOM   2154  C CD  . GLN B  1 62  ? -14.616 1.636   48.162  1.00 17.39  ? 54  GLN B CD  1 
ATOM   2155  O OE1 . GLN B  1 62  ? -14.768 2.659   48.831  1.00 17.30  ? 54  GLN B OE1 1 
ATOM   2156  N NE2 . GLN B  1 62  ? -14.104 1.644   46.927  1.00 23.24  ? 54  GLN B NE2 1 
ATOM   2157  N N   . GLN B  1 63  ? -13.856 -3.740  48.679  1.00 15.41  ? 55  GLN B N   1 
ATOM   2158  C CA  . GLN B  1 63  ? -13.517 -4.636  47.603  1.00 14.46  ? 55  GLN B CA  1 
ATOM   2159  C C   . GLN B  1 63  ? -14.190 -4.227  46.304  1.00 13.35  ? 55  GLN B C   1 
ATOM   2160  O O   . GLN B  1 63  ? -15.415 -4.220  46.210  1.00 12.31  ? 55  GLN B O   1 
ATOM   2161  C CB  . GLN B  1 63  ? -13.908 -6.049  47.986  1.00 14.96  ? 55  GLN B CB  1 
ATOM   2162  C CG  . GLN B  1 63  ? -13.962 -6.970  46.806  1.00 23.46  ? 55  GLN B CG  1 
ATOM   2163  C CD  . GLN B  1 63  ? -14.167 -8.397  47.221  1.00 28.06  ? 55  GLN B CD  1 
ATOM   2164  O OE1 . GLN B  1 63  ? -14.067 -8.727  48.406  1.00 26.51  ? 55  GLN B OE1 1 
ATOM   2165  N NE2 . GLN B  1 63  ? -14.451 -9.259  46.251  1.00 31.53  ? 55  GLN B NE2 1 
ATOM   2166  N N   . THR B  1 64  ? -13.373 -3.872  45.309  1.00 12.07  ? 56  THR B N   1 
ATOM   2167  C CA  . THR B  1 64  ? -13.875 -3.415  44.018  1.00 8.58   ? 56  THR B CA  1 
ATOM   2168  C C   . THR B  1 64  ? -13.228 -4.187  42.885  1.00 9.35   ? 56  THR B C   1 
ATOM   2169  O O   . THR B  1 64  ? -12.033 -4.470  42.931  1.00 10.44  ? 56  THR B O   1 
ATOM   2170  C CB  . THR B  1 64  ? -13.584 -1.940  43.824  1.00 8.88   ? 56  THR B CB  1 
ATOM   2171  O OG1 . THR B  1 64  ? -13.934 -1.224  45.016  1.00 16.01  ? 56  THR B OG1 1 
ATOM   2172  C CG2 . THR B  1 64  ? -14.399 -1.404  42.680  1.00 9.98   ? 56  THR B CG2 1 
ATOM   2173  N N   . THR B  1 65  ? -14.008 -4.547  41.870  1.00 10.69  ? 57  THR B N   1 
ATOM   2174  C CA  . THR B  1 65  ? -13.462 -5.258  40.703  1.00 10.46  ? 57  THR B CA  1 
ATOM   2175  C C   . THR B  1 65  ? -14.155 -4.877  39.406  1.00 11.73  ? 57  THR B C   1 
ATOM   2176  O O   . THR B  1 65  ? -15.315 -4.445  39.390  1.00 12.24  ? 57  THR B O   1 
ATOM   2177  C CB  . THR B  1 65  ? -13.540 -6.811  40.826  1.00 11.60  ? 57  THR B CB  1 
ATOM   2178  O OG1 . THR B  1 65  ? -14.913 -7.227  40.925  1.00 11.19  ? 57  THR B OG1 1 
ATOM   2179  C CG2 . THR B  1 65  ? -12.745 -7.326  42.024  1.00 9.45   ? 57  THR B CG2 1 
ATOM   2180  N N   . TRP B  1 66  ? -13.425 -5.050  38.312  1.00 12.43  ? 58  TRP B N   1 
ATOM   2181  C CA  . TRP B  1 66  ? -13.966 -4.834  36.975  1.00 13.27  ? 58  TRP B CA  1 
ATOM   2182  C C   . TRP B  1 66  ? -12.992 -5.455  35.992  1.00 11.13  ? 58  TRP B C   1 
ATOM   2183  O O   . TRP B  1 66  ? -11.904 -5.879  36.376  1.00 11.68  ? 58  TRP B O   1 
ATOM   2184  C CB  . TRP B  1 66  ? -14.160 -3.338  36.686  1.00 11.63  ? 58  TRP B CB  1 
ATOM   2185  C CG  . TRP B  1 66  ? -12.881 -2.568  36.771  1.00 12.21  ? 58  TRP B CG  1 
ATOM   2186  C CD1 . TRP B  1 66  ? -12.054 -2.255  35.740  1.00 10.87  ? 58  TRP B CD1 1 
ATOM   2187  C CD2 . TRP B  1 66  ? -12.263 -2.037  37.958  1.00 11.08  ? 58  TRP B CD2 1 
ATOM   2188  N NE1 . TRP B  1 66  ? -10.967 -1.564  36.203  1.00 13.17  ? 58  TRP B NE1 1 
ATOM   2189  C CE2 . TRP B  1 66  ? -11.071 -1.414  37.560  1.00 9.57   ? 58  TRP B CE2 1 
ATOM   2190  C CE3 . TRP B  1 66  ? -12.609 -2.024  39.312  1.00 9.19   ? 58  TRP B CE3 1 
ATOM   2191  C CZ2 . TRP B  1 66  ? -10.226 -0.776  38.461  1.00 8.23   ? 58  TRP B CZ2 1 
ATOM   2192  C CZ3 . TRP B  1 66  ? -11.764 -1.405  40.204  1.00 8.33   ? 58  TRP B CZ3 1 
ATOM   2193  C CH2 . TRP B  1 66  ? -10.590 -0.780  39.774  1.00 10.03  ? 58  TRP B CH2 1 
ATOM   2194  N N   . SER B  1 67  ? -13.383 -5.525  34.729  1.00 11.82  ? 59  SER B N   1 
ATOM   2195  C CA  . SER B  1 67  ? -12.512 -6.091  33.723  1.00 14.49  ? 59  SER B CA  1 
ATOM   2196  C C   . SER B  1 67  ? -12.149 -5.071  32.634  1.00 17.87  ? 59  SER B C   1 
ATOM   2197  O O   . SER B  1 67  ? -12.983 -4.270  32.197  1.00 15.47  ? 59  SER B O   1 
ATOM   2198  C CB  . SER B  1 67  ? -13.132 -7.355  33.127  1.00 11.88  ? 59  SER B CB  1 
ATOM   2199  O OG  . SER B  1 67  ? -13.631 -7.111  31.827  1.00 18.56  ? 59  SER B OG  1 
ATOM   2200  N N   . ASP B  1 68  ? -10.881 -5.096  32.231  1.00 20.22  ? 60  ASP B N   1 
ATOM   2201  C CA  . ASP B  1 68  ? -10.395 -4.328  31.085  1.00 17.96  ? 60  ASP B CA  1 
ATOM   2202  C C   . ASP B  1 68  ? -9.651  -5.289  30.184  1.00 18.36  ? 60  ASP B C   1 
ATOM   2203  O O   . ASP B  1 68  ? -8.483  -5.592  30.423  1.00 18.63  ? 60  ASP B O   1 
ATOM   2204  C CB  . ASP B  1 68  ? -9.447  -3.219  31.528  1.00 15.49  ? 60  ASP B CB  1 
ATOM   2205  C CG  . ASP B  1 68  ? -9.142  -2.245  30.412  1.00 23.06  ? 60  ASP B CG  1 
ATOM   2206  O OD1 . ASP B  1 68  ? -9.571  -2.509  29.260  1.00 24.29  ? 60  ASP B OD1 1 
ATOM   2207  O OD2 . ASP B  1 68  ? -8.470  -1.221  30.678  1.00 26.59  ? 60  ASP B OD2 1 
ATOM   2208  N N   . ARG B  1 69  ? -10.329 -5.778  29.153  1.00 24.44  ? 61  ARG B N   1 
ATOM   2209  C CA  . ARG B  1 69  ? -9.780  -6.851  28.334  1.00 24.55  ? 61  ARG B CA  1 
ATOM   2210  C C   . ARG B  1 69  ? -8.539  -6.435  27.554  1.00 19.01  ? 61  ARG B C   1 
ATOM   2211  O O   . ARG B  1 69  ? -7.736  -7.278  27.180  1.00 14.38  ? 61  ARG B O   1 
ATOM   2212  C CB  . ARG B  1 69  ? -10.838 -7.428  27.393  1.00 28.56  ? 61  ARG B CB  1 
ATOM   2213  C CG  . ARG B  1 69  ? -11.720 -8.477  28.036  1.00 30.22  ? 61  ARG B CG  1 
ATOM   2214  C CD  . ARG B  1 69  ? -12.538 -9.225  26.992  1.00 51.63  ? 61  ARG B CD  1 
ATOM   2215  N NE  . ARG B  1 69  ? -13.589 -8.403  26.389  1.00 55.80  ? 61  ARG B NE  1 
ATOM   2216  C CZ  . ARG B  1 69  ? -14.832 -8.324  26.858  1.00 58.43  ? 61  ARG B CZ  1 
ATOM   2217  N NH1 . ARG B  1 69  ? -15.172 -9.003  27.948  1.00 54.63  ? 61  ARG B NH1 1 
ATOM   2218  N NH2 . ARG B  1 69  ? -15.731 -7.553  26.254  1.00 60.80  ? 61  ARG B NH2 1 
ATOM   2219  N N   . THR B  1 70  ? -8.368  -5.137  27.335  1.00 17.66  ? 62  THR B N   1 
ATOM   2220  C CA  . THR B  1 70  ? -7.201  -4.660  26.609  1.00 16.72  ? 62  THR B CA  1 
ATOM   2221  C C   . THR B  1 70  ? -5.925  -4.816  27.426  1.00 17.30  ? 62  THR B C   1 
ATOM   2222  O O   . THR B  1 70  ? -4.835  -4.844  26.868  1.00 26.84  ? 62  THR B O   1 
ATOM   2223  C CB  . THR B  1 70  ? -7.359  -3.202  26.157  1.00 17.21  ? 62  THR B CB  1 
ATOM   2224  O OG1 . THR B  1 70  ? -7.352  -2.346  27.301  1.00 19.23  ? 62  THR B OG1 1 
ATOM   2225  C CG2 . THR B  1 70  ? -8.657  -3.019  25.383  1.00 10.94  ? 62  THR B CG2 1 
ATOM   2226  N N   . LEU B  1 71  ? -6.062  -4.922  28.744  1.00 20.82  ? 63  LEU B N   1 
ATOM   2227  C CA  . LEU B  1 71  ? -4.928  -5.161  29.641  1.00 16.72  ? 63  LEU B CA  1 
ATOM   2228  C C   . LEU B  1 71  ? -4.534  -6.637  29.729  1.00 16.86  ? 63  LEU B C   1 
ATOM   2229  O O   . LEU B  1 71  ? -3.713  -7.005  30.566  1.00 20.01  ? 63  LEU B O   1 
ATOM   2230  C CB  . LEU B  1 71  ? -5.250  -4.658  31.055  1.00 14.91  ? 63  LEU B CB  1 
ATOM   2231  C CG  . LEU B  1 71  ? -5.557  -3.168  31.222  1.00 20.32  ? 63  LEU B CG  1 
ATOM   2232  C CD1 . LEU B  1 71  ? -5.916  -2.798  32.682  1.00 7.82   ? 63  LEU B CD1 1 
ATOM   2233  C CD2 . LEU B  1 71  ? -4.399  -2.315  30.684  1.00 14.95  ? 63  LEU B CD2 1 
ATOM   2234  N N   . ALA B  1 72  ? -5.114  -7.487  28.885  1.00 19.37  ? 64  ALA B N   1 
ATOM   2235  C CA  . ALA B  1 72  ? -4.909  -8.934  29.018  1.00 18.43  ? 64  ALA B CA  1 
ATOM   2236  C C   . ALA B  1 72  ? -3.609  -9.405  28.369  1.00 19.61  ? 64  ALA B C   1 
ATOM   2237  O O   . ALA B  1 72  ? -3.046  -8.712  27.523  1.00 23.81  ? 64  ALA B O   1 
ATOM   2238  C CB  . ALA B  1 72  ? -6.101  -9.700  28.463  1.00 14.47  ? 64  ALA B CB  1 
ATOM   2239  N N   . TRP B  1 73  ? -3.127  -10.576 28.769  1.00 17.75  ? 65  TRP B N   1 
ATOM   2240  C CA  . TRP B  1 73  ? -1.897  -11.113 28.194  1.00 22.45  ? 65  TRP B CA  1 
ATOM   2241  C C   . TRP B  1 73  ? -1.777  -12.628 28.327  1.00 25.37  ? 65  TRP B C   1 
ATOM   2242  O O   . TRP B  1 73  ? -2.343  -13.227 29.234  1.00 19.04  ? 65  TRP B O   1 
ATOM   2243  C CB  . TRP B  1 73  ? -0.673  -10.443 28.821  1.00 24.39  ? 65  TRP B CB  1 
ATOM   2244  C CG  . TRP B  1 73  ? -0.390  -10.847 30.237  1.00 21.98  ? 65  TRP B CG  1 
ATOM   2245  C CD1 . TRP B  1 73  ? 0.332   -11.926 30.652  1.00 24.15  ? 65  TRP B CD1 1 
ATOM   2246  C CD2 . TRP B  1 73  ? -0.804  -10.162 31.426  1.00 21.73  ? 65  TRP B CD2 1 
ATOM   2247  N NE1 . TRP B  1 73  ? 0.388   -11.963 32.028  1.00 23.67  ? 65  TRP B NE1 1 
ATOM   2248  C CE2 . TRP B  1 73  ? -0.300  -10.890 32.526  1.00 22.29  ? 65  TRP B CE2 1 
ATOM   2249  C CE3 . TRP B  1 73  ? -1.553  -9.010  31.669  1.00 17.78  ? 65  TRP B CE3 1 
ATOM   2250  C CZ2 . TRP B  1 73  ? -0.515  -10.500 33.838  1.00 16.71  ? 65  TRP B CZ2 1 
ATOM   2251  C CZ3 . TRP B  1 73  ? -1.765  -8.627  32.970  1.00 15.88  ? 65  TRP B CZ3 1 
ATOM   2252  C CH2 . TRP B  1 73  ? -1.253  -9.371  34.038  1.00 16.25  ? 65  TRP B CH2 1 
ATOM   2253  N N   . ASN B  1 74  ? -1.021  -13.234 27.415  1.00 31.44  ? 66  ASN B N   1 
ATOM   2254  C CA  . ASN B  1 74  ? -0.782  -14.674 27.439  1.00 33.73  ? 66  ASN B CA  1 
ATOM   2255  C C   . ASN B  1 74  ? 0.076   -15.082 28.637  1.00 30.39  ? 66  ASN B C   1 
ATOM   2256  O O   . ASN B  1 74  ? 1.248   -14.706 28.721  1.00 29.16  ? 66  ASN B O   1 
ATOM   2257  C CB  . ASN B  1 74  ? -0.111  -15.106 26.136  1.00 44.32  ? 66  ASN B CB  1 
ATOM   2258  C CG  . ASN B  1 74  ? -0.522  -16.500 25.696  1.00 52.08  ? 66  ASN B CG  1 
ATOM   2259  O OD1 . ASN B  1 74  ? -1.089  -17.265 26.472  1.00 42.71  ? 66  ASN B OD1 1 
ATOM   2260  N ND2 . ASN B  1 74  ? -0.223  -16.839 24.441  1.00 67.10  ? 66  ASN B ND2 1 
ATOM   2261  N N   . SER B  1 75  ? -0.503  -15.852 29.559  1.00 30.67  ? 67  SER B N   1 
ATOM   2262  C CA  . SER B  1 75  ? 0.193   -16.183 30.809  1.00 30.13  ? 67  SER B CA  1 
ATOM   2263  C C   . SER B  1 75  ? 0.623   -17.646 30.931  1.00 34.75  ? 67  SER B C   1 
ATOM   2264  O O   . SER B  1 75  ? 0.909   -18.123 32.031  1.00 36.71  ? 67  SER B O   1 
ATOM   2265  C CB  . SER B  1 75  ? -0.628  -15.768 32.037  1.00 27.23  ? 67  SER B CB  1 
ATOM   2266  O OG  . SER B  1 75  ? -1.797  -16.556 32.180  1.00 31.29  ? 67  SER B OG  1 
ATOM   2267  N N   . SER B  1 76  ? 0.664   -18.342 29.797  1.00 37.73  ? 68  SER B N   1 
ATOM   2268  C CA  . SER B  1 76  ? 1.203   -19.698 29.717  1.00 39.06  ? 68  SER B CA  1 
ATOM   2269  C C   . SER B  1 76  ? 2.525   -19.826 30.469  1.00 41.43  ? 68  SER B C   1 
ATOM   2270  O O   . SER B  1 76  ? 2.690   -20.721 31.306  1.00 45.63  ? 68  SER B O   1 
ATOM   2271  C CB  . SER B  1 76  ? 1.435   -20.081 28.253  1.00 45.15  ? 68  SER B CB  1 
ATOM   2272  O OG  . SER B  1 76  ? 0.711   -19.231 27.380  1.00 48.54  ? 68  SER B OG  1 
ATOM   2273  N N   . HIS B  1 77  ? 3.462   -18.927 30.170  1.00 34.75  ? 69  HIS B N   1 
ATOM   2274  C CA  . HIS B  1 77  ? 4.790   -18.996 30.767  1.00 35.61  ? 69  HIS B CA  1 
ATOM   2275  C C   . HIS B  1 77  ? 5.240   -17.686 31.398  1.00 35.73  ? 69  HIS B C   1 
ATOM   2276  O O   . HIS B  1 77  ? 6.438   -17.447 31.602  1.00 32.34  ? 69  HIS B O   1 
ATOM   2277  C CB  . HIS B  1 77  ? 5.798   -19.499 29.742  1.00 37.02  ? 69  HIS B CB  1 
ATOM   2278  C CG  . HIS B  1 77  ? 5.521   -20.895 29.281  1.00 44.16  ? 69  HIS B CG  1 
ATOM   2279  N ND1 . HIS B  1 77  ? 4.769   -21.173 28.159  1.00 45.68  ? 69  HIS B ND1 1 
ATOM   2280  C CD2 . HIS B  1 77  ? 5.860   -22.092 29.816  1.00 41.23  ? 69  HIS B CD2 1 
ATOM   2281  C CE1 . HIS B  1 77  ? 4.677   -22.482 28.008  1.00 45.49  ? 69  HIS B CE1 1 
ATOM   2282  N NE2 . HIS B  1 77  ? 5.329   -23.062 29.001  1.00 44.18  ? 69  HIS B NE2 1 
ATOM   2283  N N   . SER B  1 78  ? 4.257   -16.853 31.721  1.00 34.01  ? 70  SER B N   1 
ATOM   2284  C CA  . SER B  1 78  ? 4.489   -15.577 32.379  1.00 30.59  ? 70  SER B CA  1 
ATOM   2285  C C   . SER B  1 78  ? 3.556   -15.501 33.585  1.00 30.62  ? 70  SER B C   1 
ATOM   2286  O O   . SER B  1 78  ? 2.569   -16.235 33.638  1.00 34.25  ? 70  SER B O   1 
ATOM   2287  C CB  . SER B  1 78  ? 4.261   -14.414 31.394  1.00 33.29  ? 70  SER B CB  1 
ATOM   2288  O OG  . SER B  1 78  ? 2.973   -14.455 30.800  1.00 29.57  ? 70  SER B OG  1 
ATOM   2289  N N   . PRO B  1 79  ? 3.873   -14.636 34.566  1.00 27.45  ? 71  PRO B N   1 
ATOM   2290  C CA  . PRO B  1 79  ? 3.072   -14.496 35.784  1.00 28.36  ? 71  PRO B CA  1 
ATOM   2291  C C   . PRO B  1 79  ? 1.593   -14.285 35.510  1.00 26.34  ? 71  PRO B C   1 
ATOM   2292  O O   . PRO B  1 79  ? 1.235   -13.683 34.493  1.00 24.32  ? 71  PRO B O   1 
ATOM   2293  C CB  . PRO B  1 79  ? 3.665   -13.250 36.437  1.00 27.73  ? 71  PRO B CB  1 
ATOM   2294  C CG  . PRO B  1 79  ? 5.073   -13.266 36.034  1.00 26.25  ? 71  PRO B CG  1 
ATOM   2295  C CD  . PRO B  1 79  ? 5.075   -13.788 34.623  1.00 30.32  ? 71  PRO B CD  1 
ATOM   2296  N N   . ASP B  1 80  ? 0.747   -14.775 36.415  1.00 28.38  ? 72  ASP B N   1 
ATOM   2297  C CA  . ASP B  1 80  ? -0.697  -14.711 36.214  1.00 27.52  ? 72  ASP B CA  1 
ATOM   2298  C C   . ASP B  1 80  ? -1.250  -13.358 36.651  1.00 28.53  ? 72  ASP B C   1 
ATOM   2299  O O   . ASP B  1 80  ? -2.321  -12.935 36.191  1.00 24.40  ? 72  ASP B O   1 
ATOM   2300  C CB  . ASP B  1 80  ? -1.409  -15.849 36.948  1.00 28.79  ? 72  ASP B CB  1 
ATOM   2301  C CG  . ASP B  1 80  ? -0.666  -17.168 36.839  1.00 48.01  ? 72  ASP B CG  1 
ATOM   2302  O OD1 . ASP B  1 80  ? -0.697  -17.794 35.749  1.00 42.73  ? 72  ASP B OD1 1 
ATOM   2303  O OD2 . ASP B  1 80  ? -0.047  -17.575 37.851  1.00 54.46  ? 72  ASP B OD2 1 
ATOM   2304  N N   . GLN B  1 81  ? -0.514  -12.672 37.524  1.00 22.19  ? 73  GLN B N   1 
ATOM   2305  C CA  . GLN B  1 81  ? -0.926  -11.339 37.938  1.00 20.75  ? 73  GLN B CA  1 
ATOM   2306  C C   . GLN B  1 81  ? 0.189   -10.527 38.576  1.00 19.86  ? 73  GLN B C   1 
ATOM   2307  O O   . GLN B  1 81  ? 1.196   -11.079 39.025  1.00 19.71  ? 73  GLN B O   1 
ATOM   2308  C CB  . GLN B  1 81  ? -2.104  -11.432 38.888  1.00 22.97  ? 73  GLN B CB  1 
ATOM   2309  C CG  . GLN B  1 81  ? -1.772  -12.155 40.160  1.00 28.99  ? 73  GLN B CG  1 
ATOM   2310  C CD  . GLN B  1 81  ? -2.963  -12.871 40.720  1.00 31.58  ? 73  GLN B CD  1 
ATOM   2311  O OE1 . GLN B  1 81  ? -4.102  -12.434 40.546  1.00 21.41  ? 73  GLN B OE1 1 
ATOM   2312  N NE2 . GLN B  1 81  ? -2.716  -13.997 41.378  1.00 48.35  ? 73  GLN B NE2 1 
ATOM   2313  N N   . VAL B  1 82  ? 0.001   -9.208  38.588  1.00 16.90  ? 74  VAL B N   1 
ATOM   2314  C CA  . VAL B  1 82  ? 0.970   -8.276  39.160  1.00 15.74  ? 74  VAL B CA  1 
ATOM   2315  C C   . VAL B  1 82  ? 0.287   -7.162  39.959  1.00 13.58  ? 74  VAL B C   1 
ATOM   2316  O O   . VAL B  1 82  ? -0.918  -6.941  39.843  1.00 13.57  ? 74  VAL B O   1 
ATOM   2317  C CB  . VAL B  1 82  ? 1.890   -7.649  38.075  1.00 15.08  ? 74  VAL B CB  1 
ATOM   2318  C CG1 . VAL B  1 82  ? 2.659   -8.726  37.347  1.00 16.48  ? 74  VAL B CG1 1 
ATOM   2319  C CG2 . VAL B  1 82  ? 1.096   -6.819  37.081  1.00 12.52  ? 74  VAL B CG2 1 
ATOM   2320  N N   . SER B  1 83  ? 1.067   -6.479  40.783  1.00 13.76  ? 75  SER B N   1 
ATOM   2321  C CA  . SER B  1 83  ? 0.600   -5.312  41.515  1.00 12.42  ? 75  SER B CA  1 
ATOM   2322  C C   . SER B  1 83  ? 0.915   -4.049  40.709  1.00 15.31  ? 75  SER B C   1 
ATOM   2323  O O   . SER B  1 83  ? 2.036   -3.881  40.199  1.00 15.18  ? 75  SER B O   1 
ATOM   2324  C CB  . SER B  1 83  ? 1.276   -5.234  42.893  1.00 15.07  ? 75  SER B CB  1 
ATOM   2325  O OG  . SER B  1 83  ? 0.662   -6.085  43.853  1.00 15.67  ? 75  SER B OG  1 
ATOM   2326  N N   . VAL B  1 84  ? -0.074  -3.166  40.592  1.00 11.92  ? 76  VAL B N   1 
ATOM   2327  C CA  . VAL B  1 84  ? 0.067   -1.943  39.800  1.00 13.64  ? 76  VAL B CA  1 
ATOM   2328  C C   . VAL B  1 84  ? -0.349  -0.781  40.679  1.00 11.96  ? 76  VAL B C   1 
ATOM   2329  O O   . VAL B  1 84  ? -1.332  -0.894  41.398  1.00 9.65   ? 76  VAL B O   1 
ATOM   2330  C CB  . VAL B  1 84  ? -0.859  -1.980  38.561  1.00 9.70   ? 76  VAL B CB  1 
ATOM   2331  C CG1 . VAL B  1 84  ? -0.718  -0.714  37.729  1.00 6.43   ? 76  VAL B CG1 1 
ATOM   2332  C CG2 . VAL B  1 84  ? -0.569  -3.208  37.748  1.00 8.29   ? 76  VAL B CG2 1 
ATOM   2333  N N   . PRO B  1 85  ? 0.420   0.320   40.665  1.00 14.36  ? 77  PRO B N   1 
ATOM   2334  C CA  . PRO B  1 85  ? -0.012  1.519   41.401  1.00 14.26  ? 77  PRO B CA  1 
ATOM   2335  C C   . PRO B  1 85  ? -1.236  2.100   40.720  1.00 11.13  ? 77  PRO B C   1 
ATOM   2336  O O   . PRO B  1 85  ? -1.220  2.172   39.505  1.00 11.16  ? 77  PRO B O   1 
ATOM   2337  C CB  . PRO B  1 85  ? 1.177   2.473   41.245  1.00 6.83   ? 77  PRO B CB  1 
ATOM   2338  C CG  . PRO B  1 85  ? 2.324   1.581   41.085  1.00 11.78  ? 77  PRO B CG  1 
ATOM   2339  C CD  . PRO B  1 85  ? 1.829   0.409   40.262  1.00 10.60  ? 77  PRO B CD  1 
ATOM   2340  N N   . ILE B  1 86  ? -2.251  2.523   41.468  1.00 12.46  ? 78  ILE B N   1 
ATOM   2341  C CA  . ILE B  1 86  ? -3.514  2.965   40.853  1.00 13.04  ? 78  ILE B CA  1 
ATOM   2342  C C   . ILE B  1 86  ? -3.469  4.216   39.953  1.00 13.70  ? 78  ILE B C   1 
ATOM   2343  O O   . ILE B  1 86  ? -4.356  4.406   39.119  1.00 12.83  ? 78  ILE B O   1 
ATOM   2344  C CB  . ILE B  1 86  ? -4.639  3.082   41.884  1.00 11.61  ? 78  ILE B CB  1 
ATOM   2345  C CG1 . ILE B  1 86  ? -4.238  4.049   42.996  1.00 13.35  ? 78  ILE B CG1 1 
ATOM   2346  C CG2 . ILE B  1 86  ? -4.946  1.707   42.460  1.00 10.49  ? 78  ILE B CG2 1 
ATOM   2347  C CD1 . ILE B  1 86  ? -5.358  4.398   43.918  1.00 8.04   ? 78  ILE B CD1 1 
ATOM   2348  N N   . SER B  1 87  ? -2.441  5.049   40.090  1.00 14.56  ? 79  SER B N   1 
ATOM   2349  C CA  . SER B  1 87  ? -2.228  6.147   39.132  1.00 12.99  ? 79  SER B CA  1 
ATOM   2350  C C   . SER B  1 87  ? -1.964  5.684   37.695  1.00 13.01  ? 79  SER B C   1 
ATOM   2351  O O   . SER B  1 87  ? -2.312  6.381   36.733  1.00 13.45  ? 79  SER B O   1 
ATOM   2352  C CB  . SER B  1 87  ? -1.096  7.052   39.589  1.00 9.40   ? 79  SER B CB  1 
ATOM   2353  O OG  . SER B  1 87  ? -0.179  6.316   40.370  1.00 18.44  ? 79  SER B OG  1 
ATOM   2354  N N   . SER B  1 88  ? -1.348  4.519   37.533  1.00 13.94  ? 80  SER B N   1 
ATOM   2355  C CA  . SER B  1 88  ? -1.128  3.983   36.187  1.00 8.91   ? 80  SER B CA  1 
ATOM   2356  C C   . SER B  1 88  ? -2.393  3.343   35.612  1.00 11.18  ? 80  SER B C   1 
ATOM   2357  O O   . SER B  1 88  ? -2.348  2.825   34.508  1.00 13.08  ? 80  SER B O   1 
ATOM   2358  C CB  . SER B  1 88  ? 0.017   2.971   36.180  1.00 7.76   ? 80  SER B CB  1 
ATOM   2359  O OG  . SER B  1 88  ? 1.212   3.530   36.720  1.00 10.72  ? 80  SER B OG  1 
ATOM   2360  N N   . LEU B  1 89  ? -3.513  3.392   36.347  1.00 9.48   ? 81  LEU B N   1 
ATOM   2361  C CA  . LEU B  1 89  ? -4.756  2.715   35.952  1.00 8.23   ? 81  LEU B CA  1 
ATOM   2362  C C   . LEU B  1 89  ? -6.021  3.555   36.102  1.00 9.71   ? 81  LEU B C   1 
ATOM   2363  O O   . LEU B  1 89  ? -6.063  4.523   36.838  1.00 14.38  ? 81  LEU B O   1 
ATOM   2364  C CB  . LEU B  1 89  ? -4.970  1.457   36.787  1.00 11.48  ? 81  LEU B CB  1 
ATOM   2365  C CG  . LEU B  1 89  ? -4.143  0.213   36.517  1.00 14.18  ? 81  LEU B CG  1 
ATOM   2366  C CD1 . LEU B  1 89  ? -4.364  -0.807  37.617  1.00 7.82   ? 81  LEU B CD1 1 
ATOM   2367  C CD2 . LEU B  1 89  ? -4.539  -0.346  35.176  1.00 15.63  ? 81  LEU B CD2 1 
ATOM   2368  N N   . TRP B  1 90  ? -7.077  3.155   35.420  1.00 8.68   ? 82  TRP B N   1 
ATOM   2369  C CA  . TRP B  1 90  ? -8.364  3.748   35.659  1.00 7.93   ? 82  TRP B CA  1 
ATOM   2370  C C   . TRP B  1 90  ? -9.039  3.038   36.820  1.00 12.96  ? 82  TRP B C   1 
ATOM   2371  O O   . TRP B  1 90  ? -9.107  1.801   36.837  1.00 10.22  ? 82  TRP B O   1 
ATOM   2372  C CB  . TRP B  1 90  ? -9.233  3.611   34.426  1.00 7.94   ? 82  TRP B CB  1 
ATOM   2373  C CG  . TRP B  1 90  ? -10.657 4.055   34.643  1.00 13.06  ? 82  TRP B CG  1 
ATOM   2374  C CD1 . TRP B  1 90  ? -11.154 5.313   34.480  1.00 12.04  ? 82  TRP B CD1 1 
ATOM   2375  C CD2 . TRP B  1 90  ? -11.765 3.238   35.046  1.00 10.54  ? 82  TRP B CD2 1 
ATOM   2376  N NE1 . TRP B  1 90  ? -12.497 5.330   34.745  1.00 10.69  ? 82  TRP B NE1 1 
ATOM   2377  C CE2 . TRP B  1 90  ? -12.897 4.071   35.101  1.00 10.46  ? 82  TRP B CE2 1 
ATOM   2378  C CE3 . TRP B  1 90  ? -11.908 1.885   35.362  1.00 9.70   ? 82  TRP B CE3 1 
ATOM   2379  C CZ2 . TRP B  1 90  ? -14.158 3.597   35.458  1.00 10.36  ? 82  TRP B CZ2 1 
ATOM   2380  C CZ3 . TRP B  1 90  ? -13.157 1.414   35.713  1.00 10.10  ? 82  TRP B CZ3 1 
ATOM   2381  C CH2 . TRP B  1 90  ? -14.267 2.268   35.758  1.00 9.74   ? 82  TRP B CH2 1 
ATOM   2382  N N   . VAL B  1 91  ? -9.524  3.814   37.794  1.00 10.22  ? 83  VAL B N   1 
ATOM   2383  C CA  . VAL B  1 91  ? -10.386 3.265   38.829  1.00 9.26   ? 83  VAL B CA  1 
ATOM   2384  C C   . VAL B  1 91  ? -11.736 3.957   38.709  1.00 10.15  ? 83  VAL B C   1 
ATOM   2385  O O   . VAL B  1 91  ? -11.829 5.074   38.208  1.00 13.49  ? 83  VAL B O   1 
ATOM   2386  C CB  . VAL B  1 91  ? -9.808  3.408   40.260  1.00 9.25   ? 83  VAL B CB  1 
ATOM   2387  C CG1 . VAL B  1 91  ? -8.384  2.874   40.326  1.00 9.69   ? 83  VAL B CG1 1 
ATOM   2388  C CG2 . VAL B  1 91  ? -9.865  4.848   40.718  1.00 10.96  ? 83  VAL B CG2 1 
ATOM   2389  N N   . PRO B  1 92  ? -12.803 3.278   39.121  1.00 8.30   ? 84  PRO B N   1 
ATOM   2390  C CA  . PRO B  1 92  ? -14.098 3.953   39.020  1.00 9.42   ? 84  PRO B CA  1 
ATOM   2391  C C   . PRO B  1 92  ? -14.279 5.035   40.126  1.00 9.57   ? 84  PRO B C   1 
ATOM   2392  O O   . PRO B  1 92  ? -13.707 4.918   41.210  1.00 6.13   ? 84  PRO B O   1 
ATOM   2393  C CB  . PRO B  1 92  ? -15.099 2.794   39.145  1.00 9.47   ? 84  PRO B CB  1 
ATOM   2394  C CG  . PRO B  1 92  ? -14.358 1.732   39.928  1.00 9.04   ? 84  PRO B CG  1 
ATOM   2395  C CD  . PRO B  1 92  ? -12.911 1.871   39.551  1.00 8.56   ? 84  PRO B CD  1 
ATOM   2396  N N   . ASP B  1 93  ? -15.050 6.081   39.827  1.00 7.48   ? 85  ASP B N   1 
ATOM   2397  C CA  . ASP B  1 93  ? -15.153 7.241   40.699  1.00 7.67   ? 85  ASP B CA  1 
ATOM   2398  C C   . ASP B  1 93  ? -16.254 7.052   41.738  1.00 10.40  ? 85  ASP B C   1 
ATOM   2399  O O   . ASP B  1 93  ? -17.254 7.773   41.745  1.00 7.83   ? 85  ASP B O   1 
ATOM   2400  C CB  . ASP B  1 93  ? -15.396 8.515   39.876  1.00 9.08   ? 85  ASP B CB  1 
ATOM   2401  C CG  . ASP B  1 93  ? -16.668 8.447   39.031  1.00 13.07  ? 85  ASP B CG  1 
ATOM   2402  O OD1 . ASP B  1 93  ? -17.033 7.328   38.599  1.00 15.60  ? 85  ASP B OD1 1 
ATOM   2403  O OD2 . ASP B  1 93  ? -17.308 9.510   38.812  1.00 11.49  ? 85  ASP B OD2 1 
ATOM   2404  N N   . LEU B  1 94  ? -16.066 6.071   42.614  1.00 8.57   ? 86  LEU B N   1 
ATOM   2405  C CA  . LEU B  1 94  ? -17.098 5.731   43.569  1.00 8.34   ? 86  LEU B CA  1 
ATOM   2406  C C   . LEU B  1 94  ? -17.213 6.827   44.630  1.00 10.03  ? 86  LEU B C   1 
ATOM   2407  O O   . LEU B  1 94  ? -16.268 7.584   44.877  1.00 8.05   ? 86  LEU B O   1 
ATOM   2408  C CB  . LEU B  1 94  ? -16.861 4.333   44.169  1.00 7.29   ? 86  LEU B CB  1 
ATOM   2409  C CG  . LEU B  1 94  ? -17.005 3.181   43.156  1.00 7.76   ? 86  LEU B CG  1 
ATOM   2410  C CD1 . LEU B  1 94  ? -16.994 1.788   43.771  1.00 4.82   ? 86  LEU B CD1 1 
ATOM   2411  C CD2 . LEU B  1 94  ? -18.259 3.360   42.293  1.00 10.75  ? 86  LEU B CD2 1 
ATOM   2412  N N   . ALA B  1 95  ? -18.393 6.940   45.222  1.00 11.38  ? 87  ALA B N   1 
ATOM   2413  C CA  . ALA B  1 95  ? -18.607 7.883   46.313  1.00 11.33  ? 87  ALA B CA  1 
ATOM   2414  C C   . ALA B  1 95  ? -19.688 7.352   47.227  1.00 6.81   ? 87  ALA B C   1 
ATOM   2415  O O   . ALA B  1 95  ? -20.626 6.721   46.773  1.00 7.22   ? 87  ALA B O   1 
ATOM   2416  C CB  . ALA B  1 95  ? -19.001 9.263   45.760  1.00 11.77  ? 87  ALA B CB  1 
ATOM   2417  N N   . ALA B  1 96  ? -19.563 7.612   48.515  1.00 14.22  ? 88  ALA B N   1 
ATOM   2418  C CA  . ALA B  1 96  ? -20.639 7.269   49.463  1.00 14.10  ? 88  ALA B CA  1 
ATOM   2419  C C   . ALA B  1 96  ? -21.612 8.440   49.571  1.00 13.11  ? 88  ALA B C   1 
ATOM   2420  O O   . ALA B  1 96  ? -21.217 9.529   49.973  1.00 18.76  ? 88  ALA B O   1 
ATOM   2421  C CB  . ALA B  1 96  ? -20.059 6.925   50.818  1.00 8.24   ? 88  ALA B CB  1 
ATOM   2422  N N   . TYR B  1 97  ? -22.874 8.232   49.208  1.00 14.44  ? 89  TYR B N   1 
ATOM   2423  C CA  . TYR B  1 97  ? -23.856 9.334   49.203  1.00 15.41  ? 89  TYR B CA  1 
ATOM   2424  C C   . TYR B  1 97  ? -24.109 9.970   50.579  1.00 15.39  ? 89  TYR B C   1 
ATOM   2425  O O   . TYR B  1 97  ? -24.349 11.169  50.670  1.00 18.61  ? 89  TYR B O   1 
ATOM   2426  C CB  . TYR B  1 97  ? -25.180 8.918   48.536  1.00 16.30  ? 89  TYR B CB  1 
ATOM   2427  C CG  . TYR B  1 97  ? -25.031 8.441   47.085  1.00 25.65  ? 89  TYR B CG  1 
ATOM   2428  C CD1 . TYR B  1 97  ? -23.894 8.732   46.348  1.00 21.02  ? 89  TYR B CD1 1 
ATOM   2429  C CD2 . TYR B  1 97  ? -26.030 7.704   46.463  1.00 28.79  ? 89  TYR B CD2 1 
ATOM   2430  C CE1 . TYR B  1 97  ? -23.757 8.310   45.039  1.00 27.85  ? 89  TYR B CE1 1 
ATOM   2431  C CE2 . TYR B  1 97  ? -25.901 7.273   45.151  1.00 24.13  ? 89  TYR B CE2 1 
ATOM   2432  C CZ  . TYR B  1 97  ? -24.766 7.575   44.437  1.00 31.74  ? 89  TYR B CZ  1 
ATOM   2433  O OH  . TYR B  1 97  ? -24.617 7.138   43.118  1.00 28.62  ? 89  TYR B OH  1 
ATOM   2434  N N   . ASN B  1 98  ? -24.040 9.182   51.649  1.00 15.13  ? 90  ASN B N   1 
ATOM   2435  C CA  . ASN B  1 98  ? -24.308 9.706   52.987  1.00 12.89  ? 90  ASN B CA  1 
ATOM   2436  C C   . ASN B  1 98  ? -23.031 9.879   53.787  1.00 17.00  ? 90  ASN B C   1 
ATOM   2437  O O   . ASN B  1 98  ? -23.065 9.951   55.030  1.00 16.34  ? 90  ASN B O   1 
ATOM   2438  C CB  . ASN B  1 98  ? -25.303 8.817   53.753  1.00 12.95  ? 90  ASN B CB  1 
ATOM   2439  C CG  . ASN B  1 98  ? -24.933 7.339   53.711  1.00 17.16  ? 90  ASN B CG  1 
ATOM   2440  O OD1 . ASN B  1 98  ? -24.575 6.800   52.650  1.00 15.86  ? 90  ASN B OD1 1 
ATOM   2441  N ND2 . ASN B  1 98  ? -25.008 6.676   54.865  1.00 13.38  ? 90  ASN B ND2 1 
ATOM   2442  N N   . ALA B  1 99  ? -21.905 9.933   53.076  1.00 11.64  ? 91  ALA B N   1 
ATOM   2443  C CA  . ALA B  1 99  ? -20.614 10.152  53.718  1.00 13.68  ? 91  ALA B CA  1 
ATOM   2444  C C   . ALA B  1 99  ? -20.486 11.581  54.275  1.00 17.95  ? 91  ALA B C   1 
ATOM   2445  O O   . ALA B  1 99  ? -21.017 12.533  53.695  1.00 14.57  ? 91  ALA B O   1 
ATOM   2446  C CB  . ALA B  1 99  ? -19.497 9.867   52.745  1.00 14.20  ? 91  ALA B CB  1 
ATOM   2447  N N   . ILE B  1 100 ? -19.789 11.732  55.403  1.00 16.37  ? 92  ILE B N   1 
ATOM   2448  C CA  . ILE B  1 100 ? -19.578 13.056  55.983  1.00 14.61  ? 92  ILE B CA  1 
ATOM   2449  C C   . ILE B  1 100 ? -18.116 13.307  56.347  1.00 16.21  ? 92  ILE B C   1 
ATOM   2450  O O   . ILE B  1 100 ? -17.794 14.202  57.130  1.00 18.10  ? 92  ILE B O   1 
ATOM   2451  C CB  . ILE B  1 100 ? -20.493 13.308  57.214  1.00 13.73  ? 92  ILE B CB  1 
ATOM   2452  C CG1 . ILE B  1 100 ? -20.064 12.438  58.397  1.00 15.83  ? 92  ILE B CG1 1 
ATOM   2453  C CG2 . ILE B  1 100 ? -21.962 13.099  56.847  1.00 10.73  ? 92  ILE B CG2 1 
ATOM   2454  C CD1 . ILE B  1 100 ? -21.021 12.465  59.559  1.00 14.58  ? 92  ILE B CD1 1 
ATOM   2455  N N   . SER B  1 101 ? -17.229 12.511  55.772  1.00 14.75  ? 93  SER B N   1 
ATOM   2456  C CA  . SER B  1 101 ? -15.799 12.738  55.915  1.00 14.63  ? 93  SER B CA  1 
ATOM   2457  C C   . SER B  1 101 ? -15.141 12.126  54.695  1.00 13.70  ? 93  SER B C   1 
ATOM   2458  O O   . SER B  1 101 ? -15.709 11.202  54.103  1.00 11.75  ? 93  SER B O   1 
ATOM   2459  C CB  . SER B  1 101 ? -15.272 12.101  57.206  1.00 13.81  ? 93  SER B CB  1 
ATOM   2460  O OG  . SER B  1 101 ? -15.073 10.702  57.074  1.00 13.56  ? 93  SER B OG  1 
ATOM   2461  N N   . LYS B  1 102 ? -13.978 12.658  54.300  1.00 14.87  ? 94  LYS B N   1 
ATOM   2462  C CA  . LYS B  1 102 ? -13.190 12.097  53.196  1.00 11.59  ? 94  LYS B CA  1 
ATOM   2463  C C   . LYS B  1 102 ? -12.874 10.648  53.528  1.00 11.90  ? 94  LYS B C   1 
ATOM   2464  O O   . LYS B  1 102 ? -12.670 10.314  54.687  1.00 12.72  ? 94  LYS B O   1 
ATOM   2465  C CB  . LYS B  1 102 ? -11.870 12.864  53.035  1.00 15.74  ? 94  LYS B CB  1 
ATOM   2466  C CG  . LYS B  1 102 ? -11.979 14.231  52.345  1.00 21.34  ? 94  LYS B CG  1 
ATOM   2467  C CD  . LYS B  1 102 ? -10.652 14.984  52.334  1.00 22.11  ? 94  LYS B CD  1 
ATOM   2468  C CE  . LYS B  1 102 ? -10.317 15.575  50.937  1.00 34.45  ? 94  LYS B CE  1 
ATOM   2469  N NZ  . LYS B  1 102 ? -10.828 16.980  50.709  1.00 25.02  ? 94  LYS B NZ  1 
ATOM   2470  N N   . PRO B  1 103 ? -12.864 9.764   52.527  1.00 13.77  ? 95  PRO B N   1 
ATOM   2471  C CA  . PRO B  1 103 ? -12.352 8.424   52.854  1.00 12.30  ? 95  PRO B CA  1 
ATOM   2472  C C   . PRO B  1 103 ? -10.882 8.488   53.287  1.00 10.84  ? 95  PRO B C   1 
ATOM   2473  O O   . PRO B  1 103 ? -10.093 9.162   52.640  1.00 13.48  ? 95  PRO B O   1 
ATOM   2474  C CB  . PRO B  1 103 ? -12.502 7.647   51.527  1.00 13.34  ? 95  PRO B CB  1 
ATOM   2475  C CG  . PRO B  1 103 ? -12.799 8.667   50.475  1.00 7.30   ? 95  PRO B CG  1 
ATOM   2476  C CD  . PRO B  1 103 ? -13.428 9.842   51.168  1.00 10.88  ? 95  PRO B CD  1 
ATOM   2477  N N   . GLU B  1 104 ? -10.529 7.838   54.387  1.00 10.14  ? 96  GLU B N   1 
ATOM   2478  C CA  . GLU B  1 104 ? -9.141  7.766   54.818  1.00 10.00  ? 96  GLU B CA  1 
ATOM   2479  C C   . GLU B  1 104 ? -8.638  6.386   54.447  1.00 12.79  ? 96  GLU B C   1 
ATOM   2480  O O   . GLU B  1 104 ? -9.043  5.393   55.039  1.00 14.59  ? 96  GLU B O   1 
ATOM   2481  C CB  . GLU B  1 104 ? -9.014  7.963   56.326  1.00 11.56  ? 96  GLU B CB  1 
ATOM   2482  C CG  . GLU B  1 104 ? -7.582  7.902   56.859  1.00 16.33  ? 96  GLU B CG  1 
ATOM   2483  C CD  . GLU B  1 104 ? -7.505  8.095   58.390  1.00 35.71  ? 96  GLU B CD  1 
ATOM   2484  O OE1 . GLU B  1 104 ? -8.544  8.409   59.020  1.00 35.42  ? 96  GLU B OE1 1 
ATOM   2485  O OE2 . GLU B  1 104 ? -6.403  7.932   58.970  1.00 36.83  ? 96  GLU B OE2 1 
ATOM   2486  N N   . VAL B  1 105 ? -7.772  6.321   53.445  1.00 12.84  ? 97  VAL B N   1 
ATOM   2487  C CA  . VAL B  1 105 ? -7.270  5.057   52.963  1.00 10.03  ? 97  VAL B CA  1 
ATOM   2488  C C   . VAL B  1 105 ? -6.112  4.631   53.856  1.00 13.80  ? 97  VAL B C   1 
ATOM   2489  O O   . VAL B  1 105 ? -5.140  5.376   54.012  1.00 15.77  ? 97  VAL B O   1 
ATOM   2490  C CB  . VAL B  1 105 ? -6.853  5.192   51.484  1.00 13.04  ? 97  VAL B CB  1 
ATOM   2491  C CG1 . VAL B  1 105 ? -6.370  3.871   50.918  1.00 10.33  ? 97  VAL B CG1 1 
ATOM   2492  C CG2 . VAL B  1 105 ? -8.025  5.708   50.680  1.00 10.21  ? 97  VAL B CG2 1 
ATOM   2493  N N   . LEU B  1 106 ? -6.226  3.432   54.434  1.00 11.84  ? 98  LEU B N   1 
ATOM   2494  C CA  . LEU B  1 106 ? -5.277  2.930   55.419  1.00 8.27   ? 98  LEU B CA  1 
ATOM   2495  C C   . LEU B  1 106 ? -4.278  1.922   54.845  1.00 13.44  ? 98  LEU B C   1 
ATOM   2496  O O   . LEU B  1 106 ? -3.318  1.552   55.509  1.00 20.23  ? 98  LEU B O   1 
ATOM   2497  C CB  . LEU B  1 106 ? -6.037  2.275   56.573  1.00 11.76  ? 98  LEU B CB  1 
ATOM   2498  C CG  . LEU B  1 106 ? -7.183  3.021   57.284  1.00 12.10  ? 98  LEU B CG  1 
ATOM   2499  C CD1 . LEU B  1 106 ? -8.122  2.051   57.965  1.00 11.89  ? 98  LEU B CD1 1 
ATOM   2500  C CD2 . LEU B  1 106 ? -6.653  3.989   58.299  1.00 15.56  ? 98  LEU B CD2 1 
ATOM   2501  N N   . THR B  1 107 ? -4.497  1.471   53.616  1.00 16.76  ? 99  THR B N   1 
ATOM   2502  C CA  . THR B  1 107 ? -3.613  0.487   52.978  1.00 14.55  ? 99  THR B CA  1 
ATOM   2503  C C   . THR B  1 107 ? -2.841  1.074   51.806  1.00 15.68  ? 99  THR B C   1 
ATOM   2504  O O   . THR B  1 107 ? -3.207  2.129   51.294  1.00 14.43  ? 99  THR B O   1 
ATOM   2505  C CB  . THR B  1 107 ? -4.408  -0.733  52.462  1.00 14.66  ? 99  THR B CB  1 
ATOM   2506  O OG1 . THR B  1 107 ? -5.620  -0.285  51.838  1.00 14.23  ? 99  THR B OG1 1 
ATOM   2507  C CG2 . THR B  1 107 ? -4.753  -1.672  53.618  1.00 17.37  ? 99  THR B CG2 1 
ATOM   2508  N N   . PRO B  1 108 ? -1.754  0.396   51.388  1.00 19.37  ? 100 PRO B N   1 
ATOM   2509  C CA  . PRO B  1 108 ? -1.046  0.769   50.160  1.00 12.64  ? 100 PRO B CA  1 
ATOM   2510  C C   . PRO B  1 108 ? -1.974  0.839   48.956  1.00 12.51  ? 100 PRO B C   1 
ATOM   2511  O O   . PRO B  1 108 ? -2.866  0.001   48.807  1.00 11.54  ? 100 PRO B O   1 
ATOM   2512  C CB  . PRO B  1 108 ? -0.038  -0.366  49.996  1.00 10.14  ? 100 PRO B CB  1 
ATOM   2513  C CG  . PRO B  1 108 ? 0.280   -0.753  51.406  1.00 11.33  ? 100 PRO B CG  1 
ATOM   2514  C CD  . PRO B  1 108 ? -1.017  -0.639  52.143  1.00 16.32  ? 100 PRO B CD  1 
ATOM   2515  N N   . GLN B  1 109 ? -1.749  1.846   48.116  1.00 13.29  ? 101 GLN B N   1 
ATOM   2516  C CA  . GLN B  1 109 ? -2.586  2.147   46.957  1.00 10.95  ? 101 GLN B CA  1 
ATOM   2517  C C   . GLN B  1 109 ? -2.225  1.336   45.705  1.00 14.53  ? 101 GLN B C   1 
ATOM   2518  O O   . GLN B  1 109 ? -1.835  1.906   44.669  1.00 13.66  ? 101 GLN B O   1 
ATOM   2519  C CB  . GLN B  1 109 ? -2.424  3.619   46.636  1.00 12.12  ? 101 GLN B CB  1 
ATOM   2520  C CG  . GLN B  1 109 ? -2.740  4.527   47.778  1.00 10.63  ? 101 GLN B CG  1 
ATOM   2521  C CD  . GLN B  1 109 ? -4.198  4.872   47.799  1.00 17.02  ? 101 GLN B CD  1 
ATOM   2522  O OE1 . GLN B  1 109 ? -5.069  3.992   47.646  1.00 13.58  ? 101 GLN B OE1 1 
ATOM   2523  N NE2 . GLN B  1 109 ? -4.491  6.163   47.950  1.00 17.66  ? 101 GLN B NE2 1 
ATOM   2524  N N   . LEU B  1 110 ? -2.362  0.015   45.804  1.00 12.37  ? 102 LEU B N   1 
ATOM   2525  C CA  . LEU B  1 110 ? -2.000  -0.897  44.729  1.00 9.06   ? 102 LEU B CA  1 
ATOM   2526  C C   . LEU B  1 110 ? -3.228  -1.683  44.311  1.00 11.15  ? 102 LEU B C   1 
ATOM   2527  O O   . LEU B  1 110 ? -4.057  -2.016  45.143  1.00 17.10  ? 102 LEU B O   1 
ATOM   2528  C CB  . LEU B  1 110 ? -0.928  -1.868  45.211  1.00 9.36   ? 102 LEU B CB  1 
ATOM   2529  C CG  . LEU B  1 110 ? 0.416   -1.318  45.701  1.00 10.86  ? 102 LEU B CG  1 
ATOM   2530  C CD1 . LEU B  1 110 ? 1.318   -2.456  46.120  1.00 9.02   ? 102 LEU B CD1 1 
ATOM   2531  C CD2 . LEU B  1 110 ? 1.102   -0.502  44.624  1.00 9.31   ? 102 LEU B CD2 1 
ATOM   2532  N N   . ALA B  1 111 ? -3.349  -1.975  43.024  1.00 10.85  ? 103 ALA B N   1 
ATOM   2533  C CA  . ALA B  1 111 ? -4.379  -2.877  42.533  1.00 10.23  ? 103 ALA B CA  1 
ATOM   2534  C C   . ALA B  1 111 ? -3.684  -4.126  41.990  1.00 11.91  ? 103 ALA B C   1 
ATOM   2535  O O   . ALA B  1 111 ? -2.467  -4.142  41.850  1.00 15.10  ? 103 ALA B O   1 
ATOM   2536  C CB  . ALA B  1 111 ? -5.210  -2.196  41.447  1.00 7.26   ? 103 ALA B CB  1 
ATOM   2537  N N   . ARG B  1 112 ? -4.435  -5.178  41.701  1.00 10.53  ? 104 ARG B N   1 
ATOM   2538  C CA  . ARG B  1 112 ? -3.862  -6.323  41.014  1.00 8.92   ? 104 ARG B CA  1 
ATOM   2539  C C   . ARG B  1 112 ? -4.492  -6.312  39.659  1.00 10.74  ? 104 ARG B C   1 
ATOM   2540  O O   . ARG B  1 112 ? -5.696  -6.084  39.535  1.00 12.84  ? 104 ARG B O   1 
ATOM   2541  C CB  . ARG B  1 112 ? -4.222  -7.658  41.690  1.00 15.12  ? 104 ARG B CB  1 
ATOM   2542  C CG  . ARG B  1 112 ? -3.714  -7.859  43.108  1.00 14.02  ? 104 ARG B CG  1 
ATOM   2543  C CD  . ARG B  1 112 ? -2.189  -8.000  43.148  1.00 16.27  ? 104 ARG B CD  1 
ATOM   2544  N NE  . ARG B  1 112 ? -1.720  -9.351  42.843  1.00 16.80  ? 104 ARG B NE  1 
ATOM   2545  C CZ  . ARG B  1 112 ? -0.456  -9.752  42.987  1.00 21.72  ? 104 ARG B CZ  1 
ATOM   2546  N NH1 . ARG B  1 112 ? 0.466   -8.903  43.422  1.00 16.73  ? 104 ARG B NH1 1 
ATOM   2547  N NH2 . ARG B  1 112 ? -0.106  -11.002 42.696  1.00 26.38  ? 104 ARG B NH2 1 
ATOM   2548  N N   . VAL B  1 113 ? -3.693  -6.550  38.630  1.00 12.80  ? 105 VAL B N   1 
ATOM   2549  C CA  . VAL B  1 113 ? -4.258  -6.827  37.326  1.00 8.73   ? 105 VAL B CA  1 
ATOM   2550  C C   . VAL B  1 113 ? -3.989  -8.298  37.035  1.00 12.90  ? 105 VAL B C   1 
ATOM   2551  O O   . VAL B  1 113 ? -2.855  -8.770  37.140  1.00 13.86  ? 105 VAL B O   1 
ATOM   2552  C CB  . VAL B  1 113 ? -3.687  -5.897  36.251  1.00 11.21  ? 105 VAL B CB  1 
ATOM   2553  C CG1 . VAL B  1 113 ? -4.389  -6.120  34.920  1.00 11.25  ? 105 VAL B CG1 1 
ATOM   2554  C CG2 . VAL B  1 113 ? -3.832  -4.442  36.683  1.00 9.41   ? 105 VAL B CG2 1 
ATOM   2555  N N   . VAL B  1 114 ? -5.058  -9.026  36.742  1.00 13.83  ? 106 VAL B N   1 
ATOM   2556  C CA  . VAL B  1 114 ? -5.001  -10.449 36.406  1.00 17.21  ? 106 VAL B CA  1 
ATOM   2557  C C   . VAL B  1 114 ? -4.886  -10.623 34.875  1.00 18.75  ? 106 VAL B C   1 
ATOM   2558  O O   . VAL B  1 114 ? -5.381  -9.776  34.110  1.00 14.33  ? 106 VAL B O   1 
ATOM   2559  C CB  . VAL B  1 114 ? -6.269  -11.167 36.947  1.00 15.89  ? 106 VAL B CB  1 
ATOM   2560  C CG1 . VAL B  1 114 ? -6.235  -12.650 36.678  1.00 16.80  ? 106 VAL B CG1 1 
ATOM   2561  C CG2 . VAL B  1 114 ? -6.410  -10.917 38.428  1.00 18.00  ? 106 VAL B CG2 1 
ATOM   2562  N N   . SER B  1 115 ? -4.243  -11.706 34.427  1.00 19.48  ? 107 SER B N   1 
ATOM   2563  C CA  . SER B  1 115 ? -3.972  -11.895 32.994  1.00 19.21  ? 107 SER B CA  1 
ATOM   2564  C C   . SER B  1 115 ? -5.216  -11.865 32.096  1.00 15.04  ? 107 SER B C   1 
ATOM   2565  O O   . SER B  1 115 ? -5.156  -11.369 30.987  1.00 15.30  ? 107 SER B O   1 
ATOM   2566  C CB  . SER B  1 115 ? -3.107  -13.140 32.723  1.00 22.26  ? 107 SER B CB  1 
ATOM   2567  O OG  . SER B  1 115 ? -3.739  -14.333 33.145  1.00 29.52  ? 107 SER B OG  1 
ATOM   2568  N N   . ASP B  1 116 ? -6.349  -12.363 32.578  1.00 15.63  ? 108 ASP B N   1 
ATOM   2569  C CA  . ASP B  1 116 ? -7.573  -12.286 31.786  1.00 13.09  ? 108 ASP B CA  1 
ATOM   2570  C C   . ASP B  1 116 ? -8.083  -10.851 31.577  1.00 19.74  ? 108 ASP B C   1 
ATOM   2571  O O   . ASP B  1 116 ? -9.025  -10.634 30.814  1.00 25.54  ? 108 ASP B O   1 
ATOM   2572  C CB  . ASP B  1 116 ? -8.676  -13.184 32.358  1.00 13.42  ? 108 ASP B CB  1 
ATOM   2573  C CG  . ASP B  1 116 ? -8.885  -12.994 33.853  1.00 24.74  ? 108 ASP B CG  1 
ATOM   2574  O OD1 . ASP B  1 116 ? -8.736  -11.860 34.359  1.00 25.24  ? 108 ASP B OD1 1 
ATOM   2575  O OD2 . ASP B  1 116 ? -9.200  -13.991 34.540  1.00 32.30  ? 108 ASP B OD2 1 
ATOM   2576  N N   . GLY B  1 117 ? -7.463  -9.878  32.245  1.00 16.61  ? 109 GLY B N   1 
ATOM   2577  C CA  . GLY B  1 117 ? -7.851  -8.485  32.098  1.00 15.92  ? 109 GLY B CA  1 
ATOM   2578  C C   . GLY B  1 117 ? -8.699  -7.949  33.243  1.00 16.40  ? 109 GLY B C   1 
ATOM   2579  O O   . GLY B  1 117 ? -9.331  -6.890  33.155  1.00 14.85  ? 109 GLY B O   1 
ATOM   2580  N N   . GLU B  1 118 ? -8.720  -8.682  34.341  1.00 16.49  ? 110 GLU B N   1 
ATOM   2581  C CA  . GLU B  1 118 ? -9.543  -8.281  35.456  1.00 13.62  ? 110 GLU B CA  1 
ATOM   2582  C C   . GLU B  1 118 ? -8.705  -7.410  36.376  1.00 12.01  ? 110 GLU B C   1 
ATOM   2583  O O   . GLU B  1 118 ? -7.532  -7.702  36.593  1.00 9.87   ? 110 GLU B O   1 
ATOM   2584  C CB  . GLU B  1 118 ? -10.040 -9.516  36.181  1.00 13.34  ? 110 GLU B CB  1 
ATOM   2585  C CG  . GLU B  1 118 ? -10.944 -9.221  37.348  1.00 22.25  ? 110 GLU B CG  1 
ATOM   2586  C CD  . GLU B  1 118 ? -11.039 -10.395 38.288  1.00 28.88  ? 110 GLU B CD  1 
ATOM   2587  O OE1 . GLU B  1 118 ? -10.469 -11.459 37.944  1.00 34.25  ? 110 GLU B OE1 1 
ATOM   2588  O OE2 . GLU B  1 118 ? -11.663 -10.251 39.368  1.00 27.49  ? 110 GLU B OE2 1 
ATOM   2589  N N   . VAL B  1 119 ? -9.303  -6.332  36.890  1.00 9.29   ? 111 VAL B N   1 
ATOM   2590  C CA  . VAL B  1 119 ? -8.631  -5.438  37.833  1.00 10.37  ? 111 VAL B CA  1 
ATOM   2591  C C   . VAL B  1 119 ? -9.313  -5.507  39.189  1.00 11.13  ? 111 VAL B C   1 
ATOM   2592  O O   . VAL B  1 119 ? -10.540 -5.433  39.282  1.00 11.81  ? 111 VAL B O   1 
ATOM   2593  C CB  . VAL B  1 119 ? -8.669  -3.964  37.353  1.00 11.57  ? 111 VAL B CB  1 
ATOM   2594  C CG1 . VAL B  1 119 ? -7.734  -3.110  38.188  1.00 6.37   ? 111 VAL B CG1 1 
ATOM   2595  C CG2 . VAL B  1 119 ? -8.314  -3.865  35.862  1.00 10.29  ? 111 VAL B CG2 1 
ATOM   2596  N N   . LEU B  1 120 ? -8.531  -5.655  40.248  1.00 11.47  ? 112 LEU B N   1 
ATOM   2597  C CA  . LEU B  1 120 ? -9.106  -5.649  41.593  1.00 13.26  ? 112 LEU B CA  1 
ATOM   2598  C C   . LEU B  1 120 ? -8.426  -4.629  42.469  1.00 12.86  ? 112 LEU B C   1 
ATOM   2599  O O   . LEU B  1 120 ? -7.199  -4.644  42.606  1.00 12.31  ? 112 LEU B O   1 
ATOM   2600  C CB  . LEU B  1 120 ? -9.027  -7.013  42.279  1.00 12.67  ? 112 LEU B CB  1 
ATOM   2601  C CG  . LEU B  1 120 ? -8.348  -8.217  41.642  1.00 14.92  ? 112 LEU B CG  1 
ATOM   2602  C CD1 . LEU B  1 120 ? -8.380  -9.337  42.676  1.00 21.45  ? 112 LEU B CD1 1 
ATOM   2603  C CD2 . LEU B  1 120 ? -9.064  -8.651  40.383  1.00 13.71  ? 112 LEU B CD2 1 
ATOM   2604  N N   . TYR B  1 121 ? -9.233  -3.744  43.050  1.00 10.75  ? 113 TYR B N   1 
ATOM   2605  C CA  . TYR B  1 121 ? -8.746  -2.753  44.006  1.00 10.06  ? 113 TYR B CA  1 
ATOM   2606  C C   . TYR B  1 121 ? -9.525  -2.965  45.294  1.00 11.88  ? 113 TYR B C   1 
ATOM   2607  O O   . TYR B  1 121 ? -10.758 -2.879  45.302  1.00 12.70  ? 113 TYR B O   1 
ATOM   2608  C CB  . TYR B  1 121 ? -8.927  -1.324  43.453  1.00 9.07   ? 113 TYR B CB  1 
ATOM   2609  C CG  . TYR B  1 121 ? -8.415  -0.209  44.353  1.00 12.10  ? 113 TYR B CG  1 
ATOM   2610  C CD1 . TYR B  1 121 ? -7.148  -0.273  44.921  1.00 10.53  ? 113 TYR B CD1 1 
ATOM   2611  C CD2 . TYR B  1 121 ? -9.197  0.925   44.622  1.00 9.95   ? 113 TYR B CD2 1 
ATOM   2612  C CE1 . TYR B  1 121 ? -6.678  0.739   45.748  1.00 9.21   ? 113 TYR B CE1 1 
ATOM   2613  C CE2 . TYR B  1 121 ? -8.726  1.949   45.440  1.00 7.42   ? 113 TYR B CE2 1 
ATOM   2614  C CZ  . TYR B  1 121 ? -7.463  1.847   46.006  1.00 10.05  ? 113 TYR B CZ  1 
ATOM   2615  O OH  . TYR B  1 121 ? -6.968  2.847   46.838  1.00 10.12  ? 113 TYR B OH  1 
ATOM   2616  N N   . MET B  1 122 ? -8.820  -3.302  46.370  1.00 13.51  ? 114 MET B N   1 
ATOM   2617  C CA  . MET B  1 122 ? -9.470  -3.438  47.666  1.00 9.12   ? 114 MET B CA  1 
ATOM   2618  C C   . MET B  1 122 ? -8.775  -2.654  48.763  1.00 7.71   ? 114 MET B C   1 
ATOM   2619  O O   . MET B  1 122 ? -8.093  -3.223  49.607  1.00 10.55  ? 114 MET B O   1 
ATOM   2620  C CB  . MET B  1 122 ? -9.596  -4.902  48.105  1.00 11.32  ? 114 MET B CB  1 
ATOM   2621  C CG  . MET B  1 122 ? -10.515 -4.999  49.358  1.00 17.98  ? 114 MET B CG  1 
ATOM   2622  S SD  . MET B  1 122 ? -10.662 -6.535  50.279  1.00 33.45  ? 114 MET B SD  1 
ATOM   2623  C CE  . MET B  1 122 ? -9.054  -6.662  51.029  1.00 17.55  ? 114 MET B CE  1 
ATOM   2624  N N   . PRO B  1 123 ? -8.963  -1.340  48.781  1.00 7.64   ? 115 PRO B N   1 
ATOM   2625  C CA  . PRO B  1 123 ? -8.392  -0.565  49.893  1.00 10.56  ? 115 PRO B CA  1 
ATOM   2626  C C   . PRO B  1 123 ? -9.150  -0.762  51.226  1.00 10.33  ? 115 PRO B C   1 
ATOM   2627  O O   . PRO B  1 123 ? -10.371 -0.977  51.256  1.00 8.81   ? 115 PRO B O   1 
ATOM   2628  C CB  . PRO B  1 123 ? -8.564  0.878   49.422  1.00 7.28   ? 115 PRO B CB  1 
ATOM   2629  C CG  . PRO B  1 123 ? -9.840  0.829   48.642  1.00 10.41  ? 115 PRO B CG  1 
ATOM   2630  C CD  . PRO B  1 123 ? -9.817  -0.520  47.911  1.00 9.27   ? 115 PRO B CD  1 
ATOM   2631  N N   . SER B  1 124 ? -8.424  -0.679  52.329  1.00 8.94   ? 116 SER B N   1 
ATOM   2632  C CA  . SER B  1 124 ? -9.080  -0.622  53.630  1.00 12.23  ? 116 SER B CA  1 
ATOM   2633  C C   . SER B  1 124 ? -9.352  0.834   53.999  1.00 12.31  ? 116 SER B C   1 
ATOM   2634  O O   . SER B  1 124 ? -8.440  1.676   54.015  1.00 11.65  ? 116 SER B O   1 
ATOM   2635  C CB  . SER B  1 124 ? -8.218  -1.274  54.695  1.00 13.21  ? 116 SER B CB  1 
ATOM   2636  O OG  . SER B  1 124 ? -8.836  -1.153  55.953  1.00 18.78  ? 116 SER B OG  1 
ATOM   2637  N N   . ILE B  1 125 ? -10.613 1.131   54.282  1.00 10.52  ? 117 ILE B N   1 
ATOM   2638  C CA  . ILE B  1 125 ? -11.043 2.513   54.445  1.00 10.13  ? 117 ILE B CA  1 
ATOM   2639  C C   . ILE B  1 125 ? -11.704 2.768   55.788  1.00 11.27  ? 117 ILE B C   1 
ATOM   2640  O O   . ILE B  1 125 ? -12.519 1.973   56.264  1.00 10.34  ? 117 ILE B O   1 
ATOM   2641  C CB  . ILE B  1 125 ? -12.021 2.914   53.317  1.00 12.02  ? 117 ILE B CB  1 
ATOM   2642  C CG1 . ILE B  1 125 ? -11.298 2.978   51.959  1.00 8.94   ? 117 ILE B CG1 1 
ATOM   2643  C CG2 . ILE B  1 125 ? -12.690 4.243   53.618  1.00 11.18  ? 117 ILE B CG2 1 
ATOM   2644  C CD1 . ILE B  1 125 ? -12.245 3.195   50.790  1.00 6.77   ? 117 ILE B CD1 1 
ATOM   2645  N N   . ARG B  1 126 ? -11.331 3.875   56.414  1.00 11.97  ? 118 ARG B N   1 
ATOM   2646  C CA  . ARG B  1 126 ? -12.085 4.379   57.545  1.00 9.64   ? 118 ARG B CA  1 
ATOM   2647  C C   . ARG B  1 126 ? -12.820 5.647   57.131  1.00 11.22  ? 118 ARG B C   1 
ATOM   2648  O O   . ARG B  1 126 ? -12.219 6.565   56.567  1.00 9.48   ? 118 ARG B O   1 
ATOM   2649  C CB  . ARG B  1 126 ? -11.168 4.691   58.709  1.00 10.40  ? 118 ARG B CB  1 
ATOM   2650  C CG  . ARG B  1 126 ? -11.886 5.399   59.835  1.00 11.74  ? 118 ARG B CG  1 
ATOM   2651  C CD  . ARG B  1 126 ? -10.958 5.627   60.981  1.00 14.03  ? 118 ARG B CD  1 
ATOM   2652  N NE  . ARG B  1 126 ? -11.661 6.126   62.146  1.00 19.39  ? 118 ARG B NE  1 
ATOM   2653  C CZ  . ARG B  1 126 ? -11.046 6.514   63.252  1.00 21.16  ? 118 ARG B CZ  1 
ATOM   2654  N NH1 . ARG B  1 126 ? -9.726  6.452   63.323  1.00 20.25  ? 118 ARG B NH1 1 
ATOM   2655  N NH2 . ARG B  1 126 ? -11.746 6.969   64.275  1.00 21.68  ? 118 ARG B NH2 1 
ATOM   2656  N N   . GLN B  1 127 ? -14.115 5.702   57.424  1.00 12.67  ? 119 GLN B N   1 
ATOM   2657  C CA  . GLN B  1 127 ? -14.937 6.845   57.033  1.00 14.34  ? 119 GLN B CA  1 
ATOM   2658  C C   . GLN B  1 127 ? -16.121 7.070   57.985  1.00 13.02  ? 119 GLN B C   1 
ATOM   2659  O O   . GLN B  1 127 ? -16.586 6.131   58.637  1.00 11.07  ? 119 GLN B O   1 
ATOM   2660  C CB  . GLN B  1 127 ? -15.442 6.616   55.619  1.00 10.45  ? 119 GLN B CB  1 
ATOM   2661  C CG  . GLN B  1 127 ? -15.896 7.849   54.910  1.00 12.77  ? 119 GLN B CG  1 
ATOM   2662  C CD  . GLN B  1 127 ? -16.193 7.557   53.466  1.00 12.09  ? 119 GLN B CD  1 
ATOM   2663  O OE1 . GLN B  1 127 ? -16.452 6.417   53.101  1.00 13.47  ? 119 GLN B OE1 1 
ATOM   2664  N NE2 . GLN B  1 127 ? -16.143 8.576   52.633  1.00 14.43  ? 119 GLN B NE2 1 
ATOM   2665  N N   . ARG B  1 128 ? -16.611 8.306   58.070  1.00 14.79  ? 120 ARG B N   1 
ATOM   2666  C CA  . ARG B  1 128 ? -17.813 8.578   58.875  1.00 16.80  ? 120 ARG B CA  1 
ATOM   2667  C C   . ARG B  1 128 ? -19.039 8.760   57.990  1.00 14.43  ? 120 ARG B C   1 
ATOM   2668  O O   . ARG B  1 128 ? -18.953 9.371   56.919  1.00 17.09  ? 120 ARG B O   1 
ATOM   2669  C CB  . ARG B  1 128 ? -17.632 9.779   59.809  1.00 13.45  ? 120 ARG B CB  1 
ATOM   2670  C CG  . ARG B  1 128 ? -16.430 9.663   60.723  1.00 18.92  ? 120 ARG B CG  1 
ATOM   2671  C CD  . ARG B  1 128 ? -16.515 10.627  61.916  1.00 32.77  ? 120 ARG B CD  1 
ATOM   2672  N NE  . ARG B  1 128 ? -17.178 10.029  63.081  1.00 35.08  ? 120 ARG B NE  1 
ATOM   2673  C CZ  . ARG B  1 128 ? -18.363 10.416  63.548  1.00 31.60  ? 120 ARG B CZ  1 
ATOM   2674  N NH1 . ARG B  1 128 ? -19.003 11.408  62.948  1.00 35.60  ? 120 ARG B NH1 1 
ATOM   2675  N NH2 . ARG B  1 128 ? -18.908 9.821   64.610  1.00 26.37  ? 120 ARG B NH2 1 
ATOM   2676  N N   . PHE B  1 129 ? -20.167 8.207   58.428  1.00 12.95  ? 121 PHE B N   1 
ATOM   2677  C CA  . PHE B  1 129 ? -21.429 8.354   57.706  1.00 15.12  ? 121 PHE B CA  1 
ATOM   2678  C C   . PHE B  1 129 ? -22.540 8.947   58.582  1.00 19.59  ? 121 PHE B C   1 
ATOM   2679  O O   . PHE B  1 129 ? -22.427 9.020   59.817  1.00 14.22  ? 121 PHE B O   1 
ATOM   2680  C CB  . PHE B  1 129 ? -21.898 7.017   57.135  1.00 12.66  ? 121 PHE B CB  1 
ATOM   2681  C CG  . PHE B  1 129 ? -20.896 6.353   56.265  1.00 14.21  ? 121 PHE B CG  1 
ATOM   2682  C CD1 . PHE B  1 129 ? -19.839 5.651   56.817  1.00 14.95  ? 121 PHE B CD1 1 
ATOM   2683  C CD2 . PHE B  1 129 ? -20.997 6.435   54.890  1.00 15.46  ? 121 PHE B CD2 1 
ATOM   2684  C CE1 . PHE B  1 129 ? -18.896 5.042   56.014  1.00 12.16  ? 121 PHE B CE1 1 
ATOM   2685  C CE2 . PHE B  1 129 ? -20.066 5.823   54.085  1.00 14.51  ? 121 PHE B CE2 1 
ATOM   2686  C CZ  . PHE B  1 129 ? -19.012 5.125   54.649  1.00 13.91  ? 121 PHE B CZ  1 
ATOM   2687  N N   . SER B  1 130 ? -23.604 9.379   57.909  1.00 18.99  ? 122 SER B N   1 
ATOM   2688  C CA  . SER B  1 130 ? -24.811 9.851   58.552  1.00 16.53  ? 122 SER B CA  1 
ATOM   2689  C C   . SER B  1 130 ? -25.869 8.840   58.222  1.00 18.15  ? 122 SER B C   1 
ATOM   2690  O O   . SER B  1 130 ? -26.089 8.532   57.052  1.00 19.94  ? 122 SER B O   1 
ATOM   2691  C CB  . SER B  1 130 ? -25.226 11.206  57.989  1.00 17.31  ? 122 SER B CB  1 
ATOM   2692  O OG  . SER B  1 130 ? -26.619 11.440  58.176  1.00 16.18  ? 122 SER B OG  1 
ATOM   2693  N N   . CYS B  1 131 ? -26.430 8.215   59.251  1.00 21.81  ? 123 CYS B N   1 
ATOM   2694  C CA  . CYS B  1 131 ? -27.395 7.137   59.062  1.00 25.45  ? 123 CYS B CA  1 
ATOM   2695  C C   . CYS B  1 131 ? -28.235 6.923   60.314  1.00 21.71  ? 123 CYS B C   1 
ATOM   2696  O O   . CYS B  1 131 ? -27.872 7.383   61.397  1.00 22.44  ? 123 CYS B O   1 
ATOM   2697  C CB  . CYS B  1 131 ? -26.680 5.840   58.680  1.00 29.31  ? 123 CYS B CB  1 
ATOM   2698  S SG  . CYS B  1 131 ? -25.426 5.300   59.865  1.00 41.93  ? 123 CYS B SG  1 
ATOM   2699  N N   . ASP B  1 132 ? -29.352 6.216   60.172  1.00 22.46  ? 124 ASP B N   1 
ATOM   2700  C CA  . ASP B  1 132 ? -30.165 5.868   61.340  1.00 28.14  ? 124 ASP B CA  1 
ATOM   2701  C C   . ASP B  1 132 ? -29.387 5.047   62.369  1.00 30.62  ? 124 ASP B C   1 
ATOM   2702  O O   . ASP B  1 132 ? -28.990 3.909   62.109  1.00 31.27  ? 124 ASP B O   1 
ATOM   2703  C CB  . ASP B  1 132 ? -31.427 5.116   60.936  1.00 26.99  ? 124 ASP B CB  1 
ATOM   2704  C CG  . ASP B  1 132 ? -32.560 5.335   61.910  1.00 33.05  ? 124 ASP B CG  1 
ATOM   2705  O OD1 . ASP B  1 132 ? -32.276 5.542   63.112  1.00 32.34  ? 124 ASP B OD1 1 
ATOM   2706  O OD2 . ASP B  1 132 ? -33.727 5.310   61.470  1.00 38.35  ? 124 ASP B OD2 1 
ATOM   2707  N N   . VAL B  1 133 ? -29.174 5.635   63.537  1.00 24.62  ? 125 VAL B N   1 
ATOM   2708  C CA  . VAL B  1 133 ? -28.413 4.978   64.576  1.00 22.67  ? 125 VAL B CA  1 
ATOM   2709  C C   . VAL B  1 133 ? -29.398 4.520   65.645  1.00 28.79  ? 125 VAL B C   1 
ATOM   2710  O O   . VAL B  1 133 ? -29.062 3.742   66.553  1.00 26.10  ? 125 VAL B O   1 
ATOM   2711  C CB  . VAL B  1 133 ? -27.353 5.934   65.145  1.00 22.35  ? 125 VAL B CB  1 
ATOM   2712  C CG1 . VAL B  1 133 ? -26.717 5.377   66.356  1.00 20.53  ? 125 VAL B CG1 1 
ATOM   2713  C CG2 . VAL B  1 133 ? -26.301 6.199   64.113  1.00 23.42  ? 125 VAL B CG2 1 
ATOM   2714  N N   . SER B  1 134 ? -30.642 4.972   65.509  1.00 29.02  ? 126 SER B N   1 
ATOM   2715  C CA  . SER B  1 134 ? -31.650 4.669   66.519  1.00 28.01  ? 126 SER B CA  1 
ATOM   2716  C C   . SER B  1 134 ? -31.870 3.160   66.624  1.00 31.60  ? 126 SER B C   1 
ATOM   2717  O O   . SER B  1 134 ? -32.045 2.483   65.606  1.00 36.54  ? 126 SER B O   1 
ATOM   2718  C CB  . SER B  1 134 ? -32.965 5.381   66.207  1.00 24.63  ? 126 SER B CB  1 
ATOM   2719  O OG  . SER B  1 134 ? -33.778 4.595   65.356  1.00 25.14  ? 126 SER B OG  1 
ATOM   2720  N N   . GLY B  1 135 ? -31.826 2.635   67.848  1.00 22.21  ? 127 GLY B N   1 
ATOM   2721  C CA  . GLY B  1 135 ? -32.072 1.227   68.079  1.00 19.28  ? 127 GLY B CA  1 
ATOM   2722  C C   . GLY B  1 135 ? -30.822 0.489   68.485  1.00 24.32  ? 127 GLY B C   1 
ATOM   2723  O O   . GLY B  1 135 ? -30.829 -0.724  68.643  1.00 28.89  ? 127 GLY B O   1 
ATOM   2724  N N   . VAL B  1 136 ? -29.739 1.228   68.673  1.00 26.68  ? 128 VAL B N   1 
ATOM   2725  C CA  . VAL B  1 136 ? -28.426 0.617   68.830  1.00 24.09  ? 128 VAL B CA  1 
ATOM   2726  C C   . VAL B  1 136 ? -28.279 -0.113  70.166  1.00 26.63  ? 128 VAL B C   1 
ATOM   2727  O O   . VAL B  1 136 ? -27.470 -1.041  70.282  1.00 23.80  ? 128 VAL B O   1 
ATOM   2728  C CB  . VAL B  1 136 ? -27.284 1.664   68.618  1.00 21.95  ? 128 VAL B CB  1 
ATOM   2729  C CG1 . VAL B  1 136 ? -27.303 2.741   69.705  1.00 22.58  ? 128 VAL B CG1 1 
ATOM   2730  C CG2 . VAL B  1 136 ? -25.933 0.986   68.556  1.00 18.23  ? 128 VAL B CG2 1 
ATOM   2731  N N   . ASP B  1 137 ? -29.067 0.305   71.162  1.00 33.48  ? 129 ASP B N   1 
ATOM   2732  C CA  . ASP B  1 137 ? -29.016 -0.279  72.510  1.00 34.10  ? 129 ASP B CA  1 
ATOM   2733  C C   . ASP B  1 137 ? -30.126 -1.286  72.807  1.00 30.27  ? 129 ASP B C   1 
ATOM   2734  O O   . ASP B  1 137 ? -30.302 -1.687  73.950  1.00 34.66  ? 129 ASP B O   1 
ATOM   2735  C CB  . ASP B  1 137 ? -29.048 0.809   73.583  1.00 38.23  ? 129 ASP B CB  1 
ATOM   2736  C CG  . ASP B  1 137 ? -27.867 1.739   73.500  1.00 39.40  ? 129 ASP B CG  1 
ATOM   2737  O OD1 . ASP B  1 137 ? -26.887 1.385   72.816  1.00 42.62  ? 129 ASP B OD1 1 
ATOM   2738  O OD2 . ASP B  1 137 ? -27.915 2.820   74.125  1.00 47.23  ? 129 ASP B OD2 1 
ATOM   2739  N N   . THR B  1 138 ? -30.869 -1.692  71.787  1.00 26.08  ? 130 THR B N   1 
ATOM   2740  C CA  . THR B  1 138 ? -31.893 -2.710  71.958  1.00 32.90  ? 130 THR B CA  1 
ATOM   2741  C C   . THR B  1 138 ? -31.410 -4.071  71.452  1.00 33.45  ? 130 THR B C   1 
ATOM   2742  O O   . THR B  1 138 ? -30.253 -4.221  71.090  1.00 39.36  ? 130 THR B O   1 
ATOM   2743  C CB  . THR B  1 138 ? -33.141 -2.354  71.173  1.00 30.50  ? 130 THR B CB  1 
ATOM   2744  O OG1 . THR B  1 138 ? -32.962 -2.779  69.815  1.00 34.09  ? 130 THR B OG1 1 
ATOM   2745  C CG2 . THR B  1 138 ? -33.405 -0.846  71.245  1.00 23.36  ? 130 THR B CG2 1 
ATOM   2746  N N   . GLU B  1 139 ? -32.310 -5.050  71.419  1.00 33.47  ? 131 GLU B N   1 
ATOM   2747  C CA  . GLU B  1 139 ? -31.989 -6.409  70.992  1.00 32.96  ? 131 GLU B CA  1 
ATOM   2748  C C   . GLU B  1 139 ? -31.894 -6.471  69.468  1.00 33.93  ? 131 GLU B C   1 
ATOM   2749  O O   . GLU B  1 139 ? -30.986 -7.101  68.900  1.00 22.26  ? 131 GLU B O   1 
ATOM   2750  C CB  . GLU B  1 139 ? -33.084 -7.371  71.471  1.00 29.40  ? 131 GLU B CB  1 
ATOM   2751  C CG  . GLU B  1 139 ? -32.609 -8.746  71.916  1.00 35.54  ? 131 GLU B CG  1 
ATOM   2752  C CD  . GLU B  1 139 ? -32.555 -9.771  70.789  1.00 48.84  ? 131 GLU B CD  1 
ATOM   2753  O OE1 . GLU B  1 139 ? -33.428 -9.728  69.889  1.00 50.82  ? 131 GLU B OE1 1 
ATOM   2754  O OE2 . GLU B  1 139 ? -31.635 -10.627 70.811  1.00 51.35  ? 131 GLU B OE2 1 
ATOM   2755  N N   . SER B  1 140 ? -32.853 -5.819  68.816  1.00 30.44  ? 132 SER B N   1 
ATOM   2756  C CA  . SER B  1 140 ? -32.967 -5.886  67.366  1.00 31.07  ? 132 SER B CA  1 
ATOM   2757  C C   . SER B  1 140 ? -32.046 -4.873  66.671  1.00 30.12  ? 132 SER B C   1 
ATOM   2758  O O   . SER B  1 140 ? -31.934 -4.868  65.450  1.00 28.33  ? 132 SER B O   1 
ATOM   2759  C CB  . SER B  1 140 ? -34.431 -5.743  66.912  1.00 30.13  ? 132 SER B CB  1 
ATOM   2760  O OG  . SER B  1 140 ? -35.060 -4.592  67.457  1.00 32.56  ? 132 SER B OG  1 
ATOM   2761  N N   . GLY B  1 141 ? -31.395 -4.023  67.462  1.00 28.63  ? 133 GLY B N   1 
ATOM   2762  C CA  . GLY B  1 141 ? -30.308 -3.185  66.986  1.00 20.47  ? 133 GLY B CA  1 
ATOM   2763  C C   . GLY B  1 141 ? -30.698 -2.055  66.055  1.00 23.51  ? 133 GLY B C   1 
ATOM   2764  O O   . GLY B  1 141 ? -31.878 -1.779  65.859  1.00 27.19  ? 133 GLY B O   1 
ATOM   2765  N N   . ALA B  1 142 ? -29.691 -1.396  65.483  1.00 23.92  ? 134 ALA B N   1 
ATOM   2766  C CA  . ALA B  1 142 ? -29.912 -0.315  64.522  1.00 26.26  ? 134 ALA B CA  1 
ATOM   2767  C C   . ALA B  1 142 ? -29.624 -0.784  63.103  1.00 25.57  ? 134 ALA B C   1 
ATOM   2768  O O   . ALA B  1 142 ? -28.898 -1.758  62.909  1.00 27.00  ? 134 ALA B O   1 
ATOM   2769  C CB  . ALA B  1 142 ? -29.044 0.894   64.864  1.00 22.17  ? 134 ALA B CB  1 
ATOM   2770  N N   . THR B  1 143 ? -30.187 -0.096  62.114  1.00 25.68  ? 135 THR B N   1 
ATOM   2771  C CA  . THR B  1 143 ? -29.885 -0.409  60.719  1.00 26.33  ? 135 THR B CA  1 
ATOM   2772  C C   . THR B  1 143 ? -29.447 0.837   59.954  1.00 24.41  ? 135 THR B C   1 
ATOM   2773  O O   . THR B  1 143 ? -30.279 1.647   59.530  1.00 19.75  ? 135 THR B O   1 
ATOM   2774  C CB  . THR B  1 143 ? -31.077 -1.085  59.999  1.00 24.03  ? 135 THR B CB  1 
ATOM   2775  O OG1 . THR B  1 143 ? -31.428 -2.285  60.688  1.00 28.16  ? 135 THR B OG1 1 
ATOM   2776  C CG2 . THR B  1 143 ? -30.707 -1.450  58.564  1.00 27.27  ? 135 THR B CG2 1 
ATOM   2777  N N   . CYS B  1 144 ? -28.139 0.958   59.741  1.00 23.62  ? 136 CYS B N   1 
ATOM   2778  C CA  . CYS B  1 144 ? -27.562 2.094   59.028  1.00 20.26  ? 136 CYS B CA  1 
ATOM   2779  C C   . CYS B  1 144 ? -27.282 1.735   57.571  1.00 22.46  ? 136 CYS B C   1 
ATOM   2780  O O   . CYS B  1 144 ? -26.694 0.693   57.279  1.00 22.30  ? 136 CYS B O   1 
ATOM   2781  C CB  . CYS B  1 144 ? -26.276 2.561   59.713  1.00 19.68  ? 136 CYS B CB  1 
ATOM   2782  S SG  . CYS B  1 144 ? -25.124 3.430   58.624  1.00 57.82  ? 136 CYS B SG  1 
ATOM   2783  N N   . ARG B  1 145 ? -27.720 2.601   56.663  1.00 22.92  ? 137 ARG B N   1 
ATOM   2784  C CA  . ARG B  1 145 ? -27.669 2.322   55.225  1.00 21.96  ? 137 ARG B CA  1 
ATOM   2785  C C   . ARG B  1 145 ? -26.661 3.193   54.462  1.00 18.22  ? 137 ARG B C   1 
ATOM   2786  O O   . ARG B  1 145 ? -26.688 4.414   54.540  1.00 22.60  ? 137 ARG B O   1 
ATOM   2787  C CB  . ARG B  1 145 ? -29.062 2.444   54.603  1.00 20.84  ? 137 ARG B CB  1 
ATOM   2788  C CG  . ARG B  1 145 ? -30.007 1.336   55.016  1.00 23.25  ? 137 ARG B CG  1 
ATOM   2789  C CD  . ARG B  1 145 ? -31.370 1.495   54.352  1.00 36.35  ? 137 ARG B CD  1 
ATOM   2790  N NE  . ARG B  1 145 ? -32.457 1.348   55.321  1.00 44.60  ? 137 ARG B NE  1 
ATOM   2791  C CZ  . ARG B  1 145 ? -33.174 0.241   55.489  1.00 43.05  ? 137 ARG B CZ  1 
ATOM   2792  N NH1 . ARG B  1 145 ? -32.940 -0.836  54.738  1.00 42.01  ? 137 ARG B NH1 1 
ATOM   2793  N NH2 . ARG B  1 145 ? -34.133 0.215   56.406  1.00 43.22  ? 137 ARG B NH2 1 
ATOM   2794  N N   . ILE B  1 146 ? -25.758 2.551   53.737  1.00 18.94  ? 138 ILE B N   1 
ATOM   2795  C CA  . ILE B  1 146 ? -24.735 3.265   52.975  1.00 18.55  ? 138 ILE B CA  1 
ATOM   2796  C C   . ILE B  1 146 ? -24.914 3.003   51.481  1.00 14.39  ? 138 ILE B C   1 
ATOM   2797  O O   . ILE B  1 146 ? -25.108 1.866   51.060  1.00 14.54  ? 138 ILE B O   1 
ATOM   2798  C CB  . ILE B  1 146 ? -23.326 2.828   53.395  1.00 17.68  ? 138 ILE B CB  1 
ATOM   2799  C CG1 . ILE B  1 146 ? -23.091 3.151   54.866  1.00 13.29  ? 138 ILE B CG1 1 
ATOM   2800  C CG2 . ILE B  1 146 ? -22.255 3.480   52.504  1.00 13.86  ? 138 ILE B CG2 1 
ATOM   2801  C CD1 . ILE B  1 146 ? -21.866 2.456   55.413  1.00 13.93  ? 138 ILE B CD1 1 
ATOM   2802  N N   . LYS B  1 147 ? -24.879 4.063   50.688  1.00 12.87  ? 139 LYS B N   1 
ATOM   2803  C CA  . LYS B  1 147 ? -24.960 3.927   49.243  1.00 14.51  ? 139 LYS B CA  1 
ATOM   2804  C C   . LYS B  1 147 ? -23.636 4.315   48.573  1.00 15.27  ? 139 LYS B C   1 
ATOM   2805  O O   . LYS B  1 147 ? -23.162 5.445   48.699  1.00 12.50  ? 139 LYS B O   1 
ATOM   2806  C CB  . LYS B  1 147 ? -26.121 4.744   48.678  1.00 17.94  ? 139 LYS B CB  1 
ATOM   2807  C CG  . LYS B  1 147 ? -27.480 4.114   48.906  1.00 24.30  ? 139 LYS B CG  1 
ATOM   2808  C CD  . LYS B  1 147 ? -28.558 4.754   48.033  1.00 31.97  ? 139 LYS B CD  1 
ATOM   2809  C CE  . LYS B  1 147 ? -29.948 4.294   48.463  1.00 28.03  ? 139 LYS B CE  1 
ATOM   2810  N NZ  . LYS B  1 147 ? -31.024 5.027   47.756  1.00 32.46  ? 139 LYS B NZ  1 
ATOM   2811  N N   . ILE B  1 148 ? -23.042 3.345   47.882  1.00 16.30  ? 140 ILE B N   1 
ATOM   2812  C CA  . ILE B  1 148 ? -21.810 3.528   47.129  1.00 14.82  ? 140 ILE B CA  1 
ATOM   2813  C C   . ILE B  1 148 ? -22.136 3.387   45.651  1.00 16.09  ? 140 ILE B C   1 
ATOM   2814  O O   . ILE B  1 148 ? -22.551 2.314   45.214  1.00 16.04  ? 140 ILE B O   1 
ATOM   2815  C CB  . ILE B  1 148 ? -20.757 2.448   47.495  1.00 15.61  ? 140 ILE B CB  1 
ATOM   2816  C CG1 . ILE B  1 148 ? -20.476 2.437   49.007  1.00 19.25  ? 140 ILE B CG1 1 
ATOM   2817  C CG2 . ILE B  1 148 ? -19.479 2.656   46.703  1.00 13.50  ? 140 ILE B CG2 1 
ATOM   2818  C CD1 . ILE B  1 148 ? -19.099 3.000   49.415  1.00 16.06  ? 140 ILE B CD1 1 
ATOM   2819  N N   . GLY B  1 149 ? -21.952 4.469   44.893  1.00 16.46  ? 141 GLY B N   1 
ATOM   2820  C CA  . GLY B  1 149 ? -22.208 4.485   43.457  1.00 15.31  ? 141 GLY B CA  1 
ATOM   2821  C C   . GLY B  1 149 ? -21.193 5.324   42.696  1.00 12.92  ? 141 GLY B C   1 
ATOM   2822  O O   . GLY B  1 149 ? -20.310 5.928   43.312  1.00 10.94  ? 141 GLY B O   1 
ATOM   2823  N N   . SER B  1 150 ? -21.295 5.344   41.364  1.00 12.62  ? 142 SER B N   1 
ATOM   2824  C CA  . SER B  1 150 ? -20.479 6.246   40.550  1.00 11.58  ? 142 SER B CA  1 
ATOM   2825  C C   . SER B  1 150 ? -20.935 7.670   40.732  1.00 10.62  ? 142 SER B C   1 
ATOM   2826  O O   . SER B  1 150 ? -22.120 7.964   40.613  1.00 15.59  ? 142 SER B O   1 
ATOM   2827  C CB  . SER B  1 150 ? -20.558 5.910   39.056  1.00 14.94  ? 142 SER B CB  1 
ATOM   2828  O OG  . SER B  1 150 ? -19.893 6.905   38.269  1.00 12.19  ? 142 SER B OG  1 
ATOM   2829  N N   . TRP B  1 151 ? -19.987 8.560   40.988  1.00 9.94   ? 143 TRP B N   1 
ATOM   2830  C CA  . TRP B  1 151 ? -20.303 9.966   41.177  1.00 10.04  ? 143 TRP B CA  1 
ATOM   2831  C C   . TRP B  1 151 ? -20.637 10.707  39.866  1.00 13.82  ? 143 TRP B C   1 
ATOM   2832  O O   . TRP B  1 151 ? -21.621 11.436  39.828  1.00 16.14  ? 143 TRP B O   1 
ATOM   2833  C CB  . TRP B  1 151 ? -19.190 10.662  41.954  1.00 7.98   ? 143 TRP B CB  1 
ATOM   2834  C CG  . TRP B  1 151 ? -19.492 12.071  42.289  1.00 13.25  ? 143 TRP B CG  1 
ATOM   2835  C CD1 . TRP B  1 151 ? -18.866 13.181  41.806  1.00 14.63  ? 143 TRP B CD1 1 
ATOM   2836  C CD2 . TRP B  1 151 ? -20.509 12.540  43.170  1.00 16.51  ? 143 TRP B CD2 1 
ATOM   2837  N NE1 . TRP B  1 151 ? -19.422 14.315  42.341  1.00 12.01  ? 143 TRP B NE1 1 
ATOM   2838  C CE2 . TRP B  1 151 ? -20.433 13.948  43.186  1.00 16.39  ? 143 TRP B CE2 1 
ATOM   2839  C CE3 . TRP B  1 151 ? -21.466 11.908  43.964  1.00 20.09  ? 143 TRP B CE3 1 
ATOM   2840  C CZ2 . TRP B  1 151 ? -21.282 14.733  43.957  1.00 17.89  ? 143 TRP B CZ2 1 
ATOM   2841  C CZ3 . TRP B  1 151 ? -22.312 12.690  44.727  1.00 27.38  ? 143 TRP B CZ3 1 
ATOM   2842  C CH2 . TRP B  1 151 ? -22.214 14.090  44.719  1.00 21.26  ? 143 TRP B CH2 1 
ATOM   2843  N N   . THR B  1 152 ? -19.850 10.517  38.799  1.00 12.03  ? 144 THR B N   1 
ATOM   2844  C CA  . THR B  1 152 ? -20.058 11.286  37.558  1.00 11.69  ? 144 THR B CA  1 
ATOM   2845  C C   . THR B  1 152 ? -20.619 10.484  36.376  1.00 10.34  ? 144 THR B C   1 
ATOM   2846  O O   . THR B  1 152 ? -21.121 11.062  35.420  1.00 7.76   ? 144 THR B O   1 
ATOM   2847  C CB  . THR B  1 152 ? -18.777 12.064  37.100  1.00 9.18   ? 144 THR B CB  1 
ATOM   2848  O OG1 . THR B  1 152 ? -17.773 11.147  36.661  1.00 11.28  ? 144 THR B OG1 1 
ATOM   2849  C CG2 . THR B  1 152 ? -18.212 12.897  38.222  1.00 9.31   ? 144 THR B CG2 1 
ATOM   2850  N N   . HIS B  1 153 ? -20.558 9.159   36.454  1.00 10.75  ? 145 HIS B N   1 
ATOM   2851  C CA  . HIS B  1 153 ? -21.014 8.325   35.352  1.00 10.05  ? 145 HIS B CA  1 
ATOM   2852  C C   . HIS B  1 153 ? -22.370 7.678   35.600  1.00 10.95  ? 145 HIS B C   1 
ATOM   2853  O O   . HIS B  1 153 ? -22.540 6.964   36.561  1.00 13.42  ? 145 HIS B O   1 
ATOM   2854  C CB  . HIS B  1 153 ? -19.974 7.239   35.051  1.00 14.68  ? 145 HIS B CB  1 
ATOM   2855  C CG  . HIS B  1 153 ? -18.610 7.777   34.728  1.00 15.37  ? 145 HIS B CG  1 
ATOM   2856  N ND1 . HIS B  1 153 ? -17.582 7.809   35.650  1.00 13.91  ? 145 HIS B ND1 1 
ATOM   2857  C CD2 . HIS B  1 153 ? -18.109 8.313   33.587  1.00 13.79  ? 145 HIS B CD2 1 
ATOM   2858  C CE1 . HIS B  1 153 ? -16.508 8.339   35.089  1.00 15.41  ? 145 HIS B CE1 1 
ATOM   2859  N NE2 . HIS B  1 153 ? -16.801 8.655   33.839  1.00 13.37  ? 145 HIS B NE2 1 
ATOM   2860  N N   . HIS B  1 154 ? -23.323 7.914   34.706  1.00 15.77  ? 146 HIS B N   1 
ATOM   2861  C CA  . HIS B  1 154 ? -24.656 7.334   34.808  1.00 14.77  ? 146 HIS B CA  1 
ATOM   2862  C C   . HIS B  1 154 ? -24.760 5.894   34.270  1.00 20.64  ? 146 HIS B C   1 
ATOM   2863  O O   . HIS B  1 154 ? -23.812 5.371   33.678  1.00 17.45  ? 146 HIS B O   1 
ATOM   2864  C CB  . HIS B  1 154 ? -25.698 8.253   34.170  1.00 17.87  ? 146 HIS B CB  1 
ATOM   2865  C CG  . HIS B  1 154 ? -25.388 8.658   32.764  1.00 27.22  ? 146 HIS B CG  1 
ATOM   2866  N ND1 . HIS B  1 154 ? -25.234 7.747   31.740  1.00 33.22  ? 146 HIS B ND1 1 
ATOM   2867  C CD2 . HIS B  1 154 ? -25.236 9.884   32.203  1.00 33.97  ? 146 HIS B CD2 1 
ATOM   2868  C CE1 . HIS B  1 154 ? -24.989 8.392   30.610  1.00 34.46  ? 146 HIS B CE1 1 
ATOM   2869  N NE2 . HIS B  1 154 ? -24.981 9.689   30.864  1.00 39.26  ? 146 HIS B NE2 1 
ATOM   2870  N N   . SER B  1 155 ? -25.908 5.252   34.493  1.00 18.37  ? 147 SER B N   1 
ATOM   2871  C CA  . SER B  1 155 ? -26.039 3.812   34.271  1.00 15.85  ? 147 SER B CA  1 
ATOM   2872  C C   . SER B  1 155 ? -25.591 3.319   32.892  1.00 18.61  ? 147 SER B C   1 
ATOM   2873  O O   . SER B  1 155 ? -25.051 2.218   32.767  1.00 22.02  ? 147 SER B O   1 
ATOM   2874  C CB  . SER B  1 155 ? -27.463 3.323   34.579  1.00 15.15  ? 147 SER B CB  1 
ATOM   2875  O OG  . SER B  1 155 ? -28.447 4.088   33.904  1.00 16.18  ? 147 SER B OG  1 
ATOM   2876  N N   . ARG B  1 156 ? -25.804 4.111   31.853  1.00 15.36  ? 148 ARG B N   1 
ATOM   2877  C CA  . ARG B  1 156 ? -25.359 3.673   30.527  1.00 26.37  ? 148 ARG B CA  1 
ATOM   2878  C C   . ARG B  1 156 ? -23.814 3.685   30.348  1.00 22.92  ? 148 ARG B C   1 
ATOM   2879  O O   . ARG B  1 156 ? -23.263 2.911   29.565  1.00 17.90  ? 148 ARG B O   1 
ATOM   2880  C CB  . ARG B  1 156 ? -26.112 4.434   29.432  1.00 34.54  ? 148 ARG B CB  1 
ATOM   2881  C CG  . ARG B  1 156 ? -27.639 4.349   29.645  1.00 36.71  ? 148 ARG B CG  1 
ATOM   2882  C CD  . ARG B  1 156 ? -28.458 5.010   28.542  1.00 42.10  ? 148 ARG B CD  1 
ATOM   2883  N NE  . ARG B  1 156 ? -27.920 6.309   28.153  1.00 50.66  ? 148 ARG B NE  1 
ATOM   2884  C CZ  . ARG B  1 156 ? -27.296 6.537   26.998  1.00 57.92  ? 148 ARG B CZ  1 
ATOM   2885  N NH1 . ARG B  1 156 ? -27.145 5.547   26.121  1.00 47.95  ? 148 ARG B NH1 1 
ATOM   2886  N NH2 . ARG B  1 156 ? -26.824 7.751   26.718  1.00 55.05  ? 148 ARG B NH2 1 
ATOM   2887  N N   . GLU B  1 157 ? -23.126 4.527   31.120  1.00 20.74  ? 149 GLU B N   1 
ATOM   2888  C CA  . GLU B  1 157 ? -21.665 4.534   31.159  1.00 14.16  ? 149 GLU B CA  1 
ATOM   2889  C C   . GLU B  1 157 ? -21.053 3.542   32.166  1.00 15.75  ? 149 GLU B C   1 
ATOM   2890  O O   . GLU B  1 157 ? -20.040 2.914   31.876  1.00 12.80  ? 149 GLU B O   1 
ATOM   2891  C CB  . GLU B  1 157 ? -21.163 5.958   31.413  1.00 13.01  ? 149 GLU B CB  1 
ATOM   2892  C CG  . GLU B  1 157 ? -21.463 6.895   30.253  1.00 14.87  ? 149 GLU B CG  1 
ATOM   2893  C CD  . GLU B  1 157 ? -21.167 8.360   30.543  1.00 24.72  ? 149 GLU B CD  1 
ATOM   2894  O OE1 . GLU B  1 157 ? -21.265 9.168   29.586  1.00 26.60  ? 149 GLU B OE1 1 
ATOM   2895  O OE2 . GLU B  1 157 ? -20.846 8.706   31.709  1.00 20.08  ? 149 GLU B OE2 1 
ATOM   2896  N N   . ILE B  1 158 ? -21.664 3.397   33.344  1.00 15.84  ? 150 ILE B N   1 
ATOM   2897  C CA  . ILE B  1 158 ? -21.119 2.519   34.379  1.00 14.24  ? 150 ILE B CA  1 
ATOM   2898  C C   . ILE B  1 158 ? -22.219 1.844   35.191  1.00 20.92  ? 150 ILE B C   1 
ATOM   2899  O O   . ILE B  1 158 ? -23.132 2.509   35.699  1.00 21.64  ? 150 ILE B O   1 
ATOM   2900  C CB  . ILE B  1 158 ? -20.192 3.287   35.356  1.00 13.57  ? 150 ILE B CB  1 
ATOM   2901  C CG1 . ILE B  1 158 ? -18.846 3.624   34.694  1.00 16.01  ? 150 ILE B CG1 1 
ATOM   2902  C CG2 . ILE B  1 158 ? -19.932 2.473   36.598  1.00 11.07  ? 150 ILE B CG2 1 
ATOM   2903  C CD1 . ILE B  1 158 ? -17.863 4.336   35.629  1.00 11.59  ? 150 ILE B CD1 1 
ATOM   2904  N N   . SER B  1 159 ? -22.135 0.522   35.328  1.00 20.55  ? 151 SER B N   1 
ATOM   2905  C CA  . SER B  1 159 ? -23.096 -0.191  36.165  1.00 18.11  ? 151 SER B CA  1 
ATOM   2906  C C   . SER B  1 159 ? -22.435 -0.794  37.399  1.00 20.28  ? 151 SER B C   1 
ATOM   2907  O O   . SER B  1 159 ? -21.491 -1.578  37.315  1.00 20.07  ? 151 SER B O   1 
ATOM   2908  C CB  . SER B  1 159 ? -23.871 -1.246  35.371  1.00 17.94  ? 151 SER B CB  1 
ATOM   2909  O OG  . SER B  1 159 ? -23.033 -2.305  34.952  1.00 22.05  ? 151 SER B OG  1 
ATOM   2910  N N   . VAL B  1 160 ? -22.950 -0.405  38.555  1.00 25.50  ? 152 VAL B N   1 
ATOM   2911  C CA  . VAL B  1 160 ? -22.380 -0.808  39.830  1.00 26.82  ? 152 VAL B CA  1 
ATOM   2912  C C   . VAL B  1 160 ? -23.238 -1.878  40.482  1.00 21.52  ? 152 VAL B C   1 
ATOM   2913  O O   . VAL B  1 160 ? -24.371 -1.618  40.864  1.00 22.41  ? 152 VAL B O   1 
ATOM   2914  C CB  . VAL B  1 160 ? -22.284 0.392   40.772  1.00 27.72  ? 152 VAL B CB  1 
ATOM   2915  C CG1 . VAL B  1 160 ? -21.858 -0.058  42.152  1.00 15.72  ? 152 VAL B CG1 1 
ATOM   2916  C CG2 . VAL B  1 160 ? -21.324 1.439   40.184  1.00 20.53  ? 152 VAL B CG2 1 
ATOM   2917  N N   . ASP B  1 161 ? -22.686 -3.082  40.587  1.00 20.80  ? 153 ASP B N   1 
ATOM   2918  C CA  . ASP B  1 161 ? -23.395 -4.235  41.125  1.00 19.71  ? 153 ASP B CA  1 
ATOM   2919  C C   . ASP B  1 161 ? -22.676 -4.836  42.330  1.00 20.45  ? 153 ASP B C   1 
ATOM   2920  O O   . ASP B  1 161 ? -21.500 -4.575  42.564  1.00 19.88  ? 153 ASP B O   1 
ATOM   2921  C CB  . ASP B  1 161 ? -23.556 -5.289  40.040  1.00 21.89  ? 153 ASP B CB  1 
ATOM   2922  C CG  . ASP B  1 161 ? -24.699 -4.979  39.099  1.00 38.28  ? 153 ASP B CG  1 
ATOM   2923  O OD1 . ASP B  1 161 ? -25.109 -5.894  38.350  1.00 45.26  ? 153 ASP B OD1 1 
ATOM   2924  O OD2 . ASP B  1 161 ? -25.194 -3.826  39.112  1.00 40.07  ? 153 ASP B OD2 1 
ATOM   2925  N N   . PRO B  1 162 ? -23.384 -5.641  43.118  1.00 23.09  ? 154 PRO B N   1 
ATOM   2926  C CA  . PRO B  1 162 ? -22.640 -6.210  44.238  1.00 22.13  ? 154 PRO B CA  1 
ATOM   2927  C C   . PRO B  1 162 ? -21.888 -7.444  43.793  1.00 19.52  ? 154 PRO B C   1 
ATOM   2928  O O   . PRO B  1 162 ? -22.294 -8.100  42.840  1.00 21.01  ? 154 PRO B O   1 
ATOM   2929  C CB  . PRO B  1 162 ? -23.740 -6.569  45.237  1.00 20.91  ? 154 PRO B CB  1 
ATOM   2930  C CG  . PRO B  1 162 ? -24.943 -6.810  44.406  1.00 20.50  ? 154 PRO B CG  1 
ATOM   2931  C CD  . PRO B  1 162 ? -24.817 -5.981  43.156  1.00 26.29  ? 154 PRO B CD  1 
ATOM   2932  N N   . THR B  1 163 ? -20.787 -7.742  44.466  1.00 20.99  ? 155 THR B N   1 
ATOM   2933  C CA  . THR B  1 163 ? -20.049 -8.960  44.186  1.00 20.59  ? 155 THR B CA  1 
ATOM   2934  C C   . THR B  1 163 ? -20.959 -10.155 44.438  1.00 23.51  ? 155 THR B C   1 
ATOM   2935  O O   . THR B  1 163 ? -21.894 -10.079 45.241  1.00 26.18  ? 155 THR B O   1 
ATOM   2936  C CB  . THR B  1 163 ? -18.805 -9.103  45.084  1.00 24.59  ? 155 THR B CB  1 
ATOM   2937  O OG1 . THR B  1 163 ? -19.213 -9.168  46.456  1.00 25.43  ? 155 THR B OG1 1 
ATOM   2938  C CG2 . THR B  1 163 ? -17.820 -7.937  44.874  1.00 18.99  ? 155 THR B CG2 1 
ATOM   2939  N N   . THR B  1 164 ? -20.619 -11.288 43.842  1.00 24.94  ? 156 THR B N   1 
ATOM   2940  C CA  . THR B  1 164 ? -21.451 -12.471 43.961  1.00 32.19  ? 156 THR B CA  1 
ATOM   2941  C C   . THR B  1 164 ? -21.575 -12.868 45.427  1.00 28.36  ? 156 THR B C   1 
ATOM   2942  O O   . THR B  1 164 ? -22.642 -13.293 45.868  1.00 36.11  ? 156 THR B O   1 
ATOM   2943  C CB  . THR B  1 164 ? -20.872 -13.654 43.163  1.00 29.73  ? 156 THR B CB  1 
ATOM   2944  O OG1 . THR B  1 164 ? -19.444 -13.661 43.283  1.00 24.28  ? 156 THR B OG1 1 
ATOM   2945  C CG2 . THR B  1 164 ? -21.252 -13.543 41.695  1.00 25.09  ? 156 THR B CG2 1 
ATOM   2946  N N   . GLU B  1 165 ? -20.501 -12.684 46.186  1.00 27.96  ? 157 GLU B N   1 
ATOM   2947  C CA  . GLU B  1 165 ? -20.502 -13.104 47.579  1.00 28.32  ? 157 GLU B CA  1 
ATOM   2948  C C   . GLU B  1 165 ? -20.620 -11.953 48.576  1.00 28.26  ? 157 GLU B C   1 
ATOM   2949  O O   . GLU B  1 165 ? -19.802 -11.034 48.601  1.00 25.76  ? 157 GLU B O   1 
ATOM   2950  C CB  . GLU B  1 165 ? -19.248 -13.929 47.885  1.00 21.00  ? 157 GLU B CB  1 
ATOM   2951  C CG  . GLU B  1 165 ? -19.425 -14.930 49.016  1.00 27.67  ? 157 GLU B CG  1 
ATOM   2952  C CD  . GLU B  1 165 ? -18.114 -15.556 49.449  1.00 32.64  ? 157 GLU B CD  1 
ATOM   2953  O OE1 . GLU B  1 165 ? -17.158 -15.552 48.646  1.00 45.49  ? 157 GLU B OE1 1 
ATOM   2954  O OE2 . GLU B  1 165 ? -18.041 -16.053 50.593  1.00 29.23  ? 157 GLU B OE2 1 
ATOM   2955  N N   . ASN B  1 166 ? -21.705 -11.986 49.347  1.00 29.02  ? 158 ASN B N   1 
ATOM   2956  C CA  . ASN B  1 166 ? -21.952 -11.005 50.400  1.00 32.57  ? 158 ASN B CA  1 
ATOM   2957  C C   . ASN B  1 166 ? -21.792 -11.562 51.817  1.00 32.47  ? 158 ASN B C   1 
ATOM   2958  O O   . ASN B  1 166 ? -21.754 -10.802 52.786  1.00 47.95  ? 158 ASN B O   1 
ATOM   2959  C CB  . ASN B  1 166 ? -23.342 -10.385 50.236  1.00 34.64  ? 158 ASN B CB  1 
ATOM   2960  C CG  . ASN B  1 166 ? -23.300 -9.040  49.539  1.00 34.39  ? 158 ASN B CG  1 
ATOM   2961  O OD1 . ASN B  1 166 ? -22.633 -8.111  49.994  1.00 30.66  ? 158 ASN B OD1 1 
ATOM   2962  N ND2 . ASN B  1 166 ? -24.016 -8.928  48.425  1.00 28.89  ? 158 ASN B ND2 1 
ATOM   2963  N N   . SER B  1 167 ? -21.766 -12.890 51.891  1.00 27.17  ? 159 SER B N   1 
ATOM   2964  C CA  . SER B  1 167 ? -21.421 -13.627 53.093  1.00 32.86  ? 159 SER B CA  1 
ATOM   2965  C C   . SER B  1 167 ? -19.928 -13.468 53.304  1.00 30.00  ? 159 SER B C   1 
ATOM   2966  O O   . SER B  1 167 ? -19.178 -13.264 52.349  1.00 35.37  ? 159 SER B O   1 
ATOM   2967  C CB  . SER B  1 167 ? -21.783 -15.104 52.943  1.00 28.00  ? 159 SER B CB  1 
ATOM   2968  O OG  . SER B  1 167 ? -21.306 -15.624 51.714  1.00 26.63  ? 159 SER B OG  1 
ATOM   2969  N N   . ASP B  1 168 ? -19.495 -13.547 54.553  1.00 25.81  ? 160 ASP B N   1 
ATOM   2970  C CA  . ASP B  1 168 ? -18.109 -13.253 54.882  1.00 20.52  ? 160 ASP B CA  1 
ATOM   2971  C C   . ASP B  1 168 ? -17.921 -11.735 54.929  1.00 21.16  ? 160 ASP B C   1 
ATOM   2972  O O   . ASP B  1 168 ? -16.806 -11.240 55.097  1.00 18.55  ? 160 ASP B O   1 
ATOM   2973  C CB  . ASP B  1 168 ? -17.166 -13.873 53.851  1.00 27.55  ? 160 ASP B CB  1 
ATOM   2974  C CG  . ASP B  1 168 ? -16.588 -12.845 52.898  1.00 24.79  ? 160 ASP B CG  1 
ATOM   2975  O OD1 . ASP B  1 168 ? -17.365 -12.032 52.355  1.00 26.99  ? 160 ASP B OD1 1 
ATOM   2976  O OD2 . ASP B  1 168 ? -15.356 -12.851 52.691  1.00 19.31  ? 160 ASP B OD2 1 
ATOM   2977  N N   . ASP B  1 169 ? -19.036 -11.031 54.778  1.00 20.43  ? 161 ASP B N   1 
ATOM   2978  C CA  . ASP B  1 169 ? -19.053 -9.586  54.859  1.00 20.08  ? 161 ASP B CA  1 
ATOM   2979  C C   . ASP B  1 169 ? -18.614 -9.197  56.255  1.00 23.30  ? 161 ASP B C   1 
ATOM   2980  O O   . ASP B  1 169 ? -17.883 -8.222  56.431  1.00 20.95  ? 161 ASP B O   1 
ATOM   2981  C CB  . ASP B  1 169 ? -20.456 -9.048  54.574  1.00 25.08  ? 161 ASP B CB  1 
ATOM   2982  C CG  . ASP B  1 169 ? -20.723 -8.872  53.092  1.00 28.75  ? 161 ASP B CG  1 
ATOM   2983  O OD1 . ASP B  1 169 ? -21.849 -8.467  52.734  1.00 29.96  ? 161 ASP B OD1 1 
ATOM   2984  O OD2 . ASP B  1 169 ? -19.808 -9.140  52.286  1.00 25.60  ? 161 ASP B OD2 1 
ATOM   2985  N N   . SER B  1 170 ? -19.057 -9.955  57.255  1.00 24.57  ? 162 SER B N   1 
ATOM   2986  C CA  . SER B  1 170 ? -18.672 -9.615  58.626  1.00 15.73  ? 162 SER B CA  1 
ATOM   2987  C C   . SER B  1 170 ? -17.640 -10.592 59.178  1.00 20.05  ? 162 SER B C   1 
ATOM   2988  O O   . SER B  1 170 ? -17.322 -10.574 60.363  1.00 16.63  ? 162 SER B O   1 
ATOM   2989  C CB  . SER B  1 170 ? -19.895 -9.535  59.533  1.00 19.40  ? 162 SER B CB  1 
ATOM   2990  O OG  . SER B  1 170 ? -20.862 -10.494 59.161  1.00 31.54  ? 162 SER B OG  1 
ATOM   2991  N N   . GLU B  1 171 ? -17.082 -11.404 58.284  1.00 24.64  ? 163 GLU B N   1 
ATOM   2992  C CA  . GLU B  1 171 ? -16.092 -12.430 58.618  1.00 18.60  ? 163 GLU B CA  1 
ATOM   2993  C C   . GLU B  1 171 ? -14.759 -11.933 59.185  1.00 18.71  ? 163 GLU B C   1 
ATOM   2994  O O   . GLU B  1 171 ? -14.081 -12.658 59.914  1.00 21.06  ? 163 GLU B O   1 
ATOM   2995  C CB  . GLU B  1 171 ? -15.815 -13.269 57.374  1.00 25.53  ? 163 GLU B CB  1 
ATOM   2996  C CG  . GLU B  1 171 ? -14.804 -14.371 57.577  1.00 30.79  ? 163 GLU B CG  1 
ATOM   2997  C CD  . GLU B  1 171 ? -14.924 -15.434 56.526  1.00 38.43  ? 163 GLU B CD  1 
ATOM   2998  O OE1 . GLU B  1 171 ? -15.304 -15.086 55.388  1.00 41.72  ? 163 GLU B OE1 1 
ATOM   2999  O OE2 . GLU B  1 171 ? -14.664 -16.614 56.842  1.00 48.86  ? 163 GLU B OE2 1 
ATOM   3000  N N   . TYR B  1 172 ? -14.349 -10.721 58.834  1.00 19.75  ? 164 TYR B N   1 
ATOM   3001  C CA  . TYR B  1 172 ? -13.084 -10.212 59.352  1.00 16.75  ? 164 TYR B CA  1 
ATOM   3002  C C   . TYR B  1 172 ? -13.356 -9.064  60.297  1.00 15.40  ? 164 TYR B C   1 
ATOM   3003  O O   . TYR B  1 172 ? -12.534 -8.175  60.467  1.00 11.50  ? 164 TYR B O   1 
ATOM   3004  C CB  . TYR B  1 172 ? -12.149 -9.785  58.218  1.00 20.72  ? 164 TYR B CB  1 
ATOM   3005  C CG  . TYR B  1 172 ? -12.259 -10.656 56.984  1.00 22.37  ? 164 TYR B CG  1 
ATOM   3006  C CD1 . TYR B  1 172 ? -11.489 -11.814 56.842  1.00 23.58  ? 164 TYR B CD1 1 
ATOM   3007  C CD2 . TYR B  1 172 ? -13.147 -10.321 55.959  1.00 24.66  ? 164 TYR B CD2 1 
ATOM   3008  C CE1 . TYR B  1 172 ? -11.604 -12.613 55.710  1.00 30.14  ? 164 TYR B CE1 1 
ATOM   3009  C CE2 . TYR B  1 172 ? -13.279 -11.107 54.828  1.00 24.73  ? 164 TYR B CE2 1 
ATOM   3010  C CZ  . TYR B  1 172 ? -12.506 -12.250 54.703  1.00 38.77  ? 164 TYR B CZ  1 
ATOM   3011  O OH  . TYR B  1 172 ? -12.650 -13.016 53.563  1.00 42.35  ? 164 TYR B OH  1 
ATOM   3012  N N   . PHE B  1 173 ? -14.519 -9.101  60.938  1.00 15.45  ? 165 PHE B N   1 
ATOM   3013  C CA  . PHE B  1 173 ? -14.888 -8.016  61.832  1.00 15.59  ? 165 PHE B CA  1 
ATOM   3014  C C   . PHE B  1 173 ? -14.243 -8.175  63.223  1.00 18.59  ? 165 PHE B C   1 
ATOM   3015  O O   . PHE B  1 173 ? -14.255 -9.261  63.810  1.00 21.92  ? 165 PHE B O   1 
ATOM   3016  C CB  . PHE B  1 173 ? -16.405 -7.875  61.897  1.00 15.41  ? 165 PHE B CB  1 
ATOM   3017  C CG  . PHE B  1 173 ? -16.865 -6.733  62.745  1.00 20.29  ? 165 PHE B CG  1 
ATOM   3018  C CD1 . PHE B  1 173 ? -16.847 -5.435  62.252  1.00 15.91  ? 165 PHE B CD1 1 
ATOM   3019  C CD2 . PHE B  1 173 ? -17.314 -6.953  64.043  1.00 20.26  ? 165 PHE B CD2 1 
ATOM   3020  C CE1 . PHE B  1 173 ? -17.268 -4.376  63.032  1.00 15.56  ? 165 PHE B CE1 1 
ATOM   3021  C CE2 . PHE B  1 173 ? -17.749 -5.895  64.831  1.00 22.44  ? 165 PHE B CE2 1 
ATOM   3022  C CZ  . PHE B  1 173 ? -17.727 -4.605  64.324  1.00 20.99  ? 165 PHE B CZ  1 
ATOM   3023  N N   . SER B  1 174 ? -13.650 -7.093  63.726  1.00 17.16  ? 166 SER B N   1 
ATOM   3024  C CA  . SER B  1 174 ? -12.836 -7.151  64.937  1.00 16.49  ? 166 SER B CA  1 
ATOM   3025  C C   . SER B  1 174 ? -13.631 -7.597  66.163  1.00 21.44  ? 166 SER B C   1 
ATOM   3026  O O   . SER B  1 174 ? -14.620 -6.971  66.548  1.00 18.78  ? 166 SER B O   1 
ATOM   3027  C CB  . SER B  1 174 ? -12.206 -5.788  65.202  1.00 19.24  ? 166 SER B CB  1 
ATOM   3028  O OG  . SER B  1 174 ? -11.225 -5.849  66.228  1.00 23.98  ? 166 SER B OG  1 
ATOM   3029  N N   . GLN B  1 175 ? -13.186 -8.681  66.783  1.00 22.11  ? 167 GLN B N   1 
ATOM   3030  C CA  . GLN B  1 175 ? -13.804 -9.158  68.017  1.00 25.69  ? 167 GLN B CA  1 
ATOM   3031  C C   . GLN B  1 175 ? -13.710 -8.155  69.184  1.00 27.52  ? 167 GLN B C   1 
ATOM   3032  O O   . GLN B  1 175 ? -14.390 -8.325  70.206  1.00 22.68  ? 167 GLN B O   1 
ATOM   3033  C CB  . GLN B  1 175 ? -13.193 -10.498 68.440  1.00 26.41  ? 167 GLN B CB  1 
ATOM   3034  C CG  . GLN B  1 175 ? -11.776 -10.393 68.973  1.00 29.09  ? 167 GLN B CG  1 
ATOM   3035  C CD  . GLN B  1 175 ? -11.526 -11.307 70.167  1.00 41.18  ? 167 GLN B CD  1 
ATOM   3036  O OE1 . GLN B  1 175 ? -10.391 -11.732 70.414  1.00 48.71  ? 167 GLN B OE1 1 
ATOM   3037  N NE2 . GLN B  1 175 ? -12.586 -11.607 70.921  1.00 39.39  ? 167 GLN B NE2 1 
ATOM   3038  N N   . TYR B  1 176 ? -12.879 -7.118  69.034  1.00 26.13  ? 168 TYR B N   1 
ATOM   3039  C CA  . TYR B  1 176 ? -12.696 -6.123  70.097  1.00 22.51  ? 168 TYR B CA  1 
ATOM   3040  C C   . TYR B  1 176 ? -13.491 -4.833  69.896  1.00 22.65  ? 168 TYR B C   1 
ATOM   3041  O O   . TYR B  1 176 ? -13.304 -3.866  70.629  1.00 22.82  ? 168 TYR B O   1 
ATOM   3042  C CB  . TYR B  1 176 ? -11.222 -5.796  70.298  1.00 22.24  ? 168 TYR B CB  1 
ATOM   3043  C CG  . TYR B  1 176 ? -10.358 -7.017  70.402  1.00 31.47  ? 168 TYR B CG  1 
ATOM   3044  C CD1 . TYR B  1 176 ? -10.431 -7.843  71.523  1.00 31.43  ? 168 TYR B CD1 1 
ATOM   3045  C CD2 . TYR B  1 176 ? -9.465  -7.356  69.380  1.00 23.66  ? 168 TYR B CD2 1 
ATOM   3046  C CE1 . TYR B  1 176 ? -9.645  -8.980  71.625  1.00 35.91  ? 168 TYR B CE1 1 
ATOM   3047  C CE2 . TYR B  1 176 ? -8.665  -8.488  69.475  1.00 22.59  ? 168 TYR B CE2 1 
ATOM   3048  C CZ  . TYR B  1 176 ? -8.755  -9.293  70.603  1.00 37.43  ? 168 TYR B CZ  1 
ATOM   3049  O OH  . TYR B  1 176 ? -7.974  -10.420 70.726  1.00 39.47  ? 168 TYR B OH  1 
ATOM   3050  N N   . SER B  1 177 ? -14.373 -4.820  68.905  1.00 22.35  ? 169 SER B N   1 
ATOM   3051  C CA  . SER B  1 177 ? -15.331 -3.729  68.747  1.00 18.91  ? 169 SER B CA  1 
ATOM   3052  C C   . SER B  1 177 ? -16.356 -3.754  69.876  1.00 19.04  ? 169 SER B C   1 
ATOM   3053  O O   . SER B  1 177 ? -16.755 -4.825  70.331  1.00 23.95  ? 169 SER B O   1 
ATOM   3054  C CB  . SER B  1 177 ? -16.042 -3.867  67.400  1.00 16.62  ? 169 SER B CB  1 
ATOM   3055  O OG  . SER B  1 177 ? -17.055 -2.898  67.231  1.00 16.43  ? 169 SER B OG  1 
ATOM   3056  N N   . ARG B  1 178 ? -16.803 -2.583  70.317  1.00 19.75  ? 170 ARG B N   1 
ATOM   3057  C CA  . ARG B  1 178 ? -17.887 -2.520  71.304  1.00 20.45  ? 170 ARG B CA  1 
ATOM   3058  C C   . ARG B  1 178 ? -19.209 -2.899  70.662  1.00 19.82  ? 170 ARG B C   1 
ATOM   3059  O O   . ARG B  1 178 ? -20.254 -2.910  71.329  1.00 24.05  ? 170 ARG B O   1 
ATOM   3060  C CB  . ARG B  1 178 ? -18.032 -1.114  71.906  1.00 17.56  ? 170 ARG B CB  1 
ATOM   3061  C CG  . ARG B  1 178 ? -16.928 -0.689  72.836  1.00 24.45  ? 170 ARG B CG  1 
ATOM   3062  C CD  . ARG B  1 178 ? -17.013 0.818   73.117  1.00 36.01  ? 170 ARG B CD  1 
ATOM   3063  N NE  . ARG B  1 178 ? -18.356 1.239   73.518  1.00 44.59  ? 170 ARG B NE  1 
ATOM   3064  C CZ  . ARG B  1 178 ? -18.723 2.502   73.726  1.00 37.29  ? 170 ARG B CZ  1 
ATOM   3065  N NH1 . ARG B  1 178 ? -17.850 3.491   73.569  1.00 36.66  ? 170 ARG B NH1 1 
ATOM   3066  N NH2 . ARG B  1 178 ? -19.973 2.778   74.074  1.00 31.91  ? 170 ARG B NH2 1 
ATOM   3067  N N   . PHE B  1 179 ? -19.174 -3.179  69.365  1.00 14.95  ? 171 PHE B N   1 
ATOM   3068  C CA  . PHE B  1 179 ? -20.390 -3.484  68.618  1.00 17.47  ? 171 PHE B CA  1 
ATOM   3069  C C   . PHE B  1 179 ? -20.344 -4.883  68.007  1.00 16.21  ? 171 PHE B C   1 
ATOM   3070  O O   . PHE B  1 179 ? -19.289 -5.520  67.985  1.00 21.50  ? 171 PHE B O   1 
ATOM   3071  C CB  . PHE B  1 179 ? -20.652 -2.387  67.574  1.00 15.96  ? 171 PHE B CB  1 
ATOM   3072  C CG  . PHE B  1 179 ? -20.837 -1.026  68.187  1.00 16.68  ? 171 PHE B CG  1 
ATOM   3073  C CD1 . PHE B  1 179 ? -19.743 -0.198  68.417  1.00 16.14  ? 171 PHE B CD1 1 
ATOM   3074  C CD2 . PHE B  1 179 ? -22.099 -0.595  68.585  1.00 17.97  ? 171 PHE B CD2 1 
ATOM   3075  C CE1 . PHE B  1 179 ? -19.898 1.050   69.000  1.00 16.66  ? 171 PHE B CE1 1 
ATOM   3076  C CE2 . PHE B  1 179 ? -22.272 0.651   69.186  1.00 20.88  ? 171 PHE B CE2 1 
ATOM   3077  C CZ  . PHE B  1 179 ? -21.169 1.478   69.392  1.00 26.26  ? 171 PHE B CZ  1 
ATOM   3078  N N   . GLU B  1 180 ? -21.492 -5.369  67.548  1.00 13.58  ? 172 GLU B N   1 
ATOM   3079  C CA  . GLU B  1 180 ? -21.575 -6.686  66.921  1.00 16.73  ? 172 GLU B CA  1 
ATOM   3080  C C   . GLU B  1 180 ? -22.536 -6.606  65.750  1.00 19.26  ? 172 GLU B C   1 
ATOM   3081  O O   . GLU B  1 180 ? -23.570 -5.945  65.832  1.00 20.36  ? 172 GLU B O   1 
ATOM   3082  C CB  . GLU B  1 180 ? -22.016 -7.777  67.923  1.00 20.40  ? 172 GLU B CB  1 
ATOM   3083  C CG  . GLU B  1 180 ? -23.519 -7.823  68.244  1.00 23.98  ? 172 GLU B CG  1 
ATOM   3084  C CD  . GLU B  1 180 ? -23.888 -8.754  69.424  1.00 38.10  ? 172 GLU B CD  1 
ATOM   3085  O OE1 . GLU B  1 180 ? -23.474 -9.939  69.436  1.00 42.63  ? 172 GLU B OE1 1 
ATOM   3086  O OE2 . GLU B  1 180 ? -24.619 -8.296  70.338  1.00 37.47  ? 172 GLU B OE2 1 
ATOM   3087  N N   . ILE B  1 181 ? -22.189 -7.261  64.647  1.00 21.22  ? 173 ILE B N   1 
ATOM   3088  C CA  . ILE B  1 181 ? -23.035 -7.204  63.459  1.00 21.71  ? 173 ILE B CA  1 
ATOM   3089  C C   . ILE B  1 181 ? -24.082 -8.313  63.479  1.00 20.37  ? 173 ILE B C   1 
ATOM   3090  O O   . ILE B  1 181 ? -23.757 -9.495  63.588  1.00 23.72  ? 173 ILE B O   1 
ATOM   3091  C CB  . ILE B  1 181 ? -22.222 -7.248  62.130  1.00 21.87  ? 173 ILE B CB  1 
ATOM   3092  C CG1 . ILE B  1 181 ? -21.170 -6.137  62.090  1.00 20.52  ? 173 ILE B CG1 1 
ATOM   3093  C CG2 . ILE B  1 181 ? -23.147 -7.110  60.937  1.00 19.89  ? 173 ILE B CG2 1 
ATOM   3094  C CD1 . ILE B  1 181 ? -20.397 -6.090  60.780  1.00 21.97  ? 173 ILE B CD1 1 
ATOM   3095  N N   . LEU B  1 182 ? -25.340 -7.909  63.377  1.00 18.95  ? 174 LEU B N   1 
ATOM   3096  C CA  . LEU B  1 182 ? -26.455 -8.832  63.402  1.00 20.39  ? 174 LEU B CA  1 
ATOM   3097  C C   . LEU B  1 182 ? -26.734 -9.333  62.005  1.00 22.13  ? 174 LEU B C   1 
ATOM   3098  O O   . LEU B  1 182 ? -26.982 -10.518 61.823  1.00 25.07  ? 174 LEU B O   1 
ATOM   3099  C CB  . LEU B  1 182 ? -27.697 -8.155  63.991  1.00 22.91  ? 174 LEU B CB  1 
ATOM   3100  C CG  . LEU B  1 182 ? -27.446 -7.404  65.311  1.00 21.97  ? 174 LEU B CG  1 
ATOM   3101  C CD1 . LEU B  1 182 ? -28.700 -6.686  65.778  1.00 21.89  ? 174 LEU B CD1 1 
ATOM   3102  C CD2 . LEU B  1 182 ? -26.913 -8.341  66.398  1.00 22.61  ? 174 LEU B CD2 1 
ATOM   3103  N N   . ASP B  1 183 ? -26.677 -8.437  61.017  1.00 23.90  ? 175 ASP B N   1 
ATOM   3104  C CA  . ASP B  1 183 ? -26.916 -8.810  59.614  1.00 25.91  ? 175 ASP B CA  1 
ATOM   3105  C C   . ASP B  1 183 ? -26.442 -7.757  58.585  1.00 26.23  ? 175 ASP B C   1 
ATOM   3106  O O   . ASP B  1 183 ? -26.545 -6.552  58.815  1.00 23.18  ? 175 ASP B O   1 
ATOM   3107  C CB  . ASP B  1 183 ? -28.403 -9.137  59.405  1.00 30.92  ? 175 ASP B CB  1 
ATOM   3108  C CG  . ASP B  1 183 ? -28.680 -9.796  58.063  1.00 39.61  ? 175 ASP B CG  1 
ATOM   3109  O OD1 . ASP B  1 183 ? -27.728 -10.324 57.446  1.00 37.43  ? 175 ASP B OD1 1 
ATOM   3110  O OD2 . ASP B  1 183 ? -29.857 -9.792  57.629  1.00 49.63  ? 175 ASP B OD2 1 
ATOM   3111  N N   . VAL B  1 184 ? -25.914 -8.219  57.453  1.00 25.93  ? 176 VAL B N   1 
ATOM   3112  C CA  . VAL B  1 184 ? -25.554 -7.322  56.363  1.00 19.42  ? 176 VAL B CA  1 
ATOM   3113  C C   . VAL B  1 184 ? -26.201 -7.748  55.051  1.00 20.86  ? 176 VAL B C   1 
ATOM   3114  O O   . VAL B  1 184 ? -26.052 -8.892  54.629  1.00 23.79  ? 176 VAL B O   1 
ATOM   3115  C CB  . VAL B  1 184 ? -24.049 -7.286  56.133  1.00 23.42  ? 176 VAL B CB  1 
ATOM   3116  C CG1 . VAL B  1 184 ? -23.706 -6.167  55.151  1.00 19.42  ? 176 VAL B CG1 1 
ATOM   3117  C CG2 . VAL B  1 184 ? -23.307 -7.097  57.441  1.00 18.20  ? 176 VAL B CG2 1 
ATOM   3118  N N   . THR B  1 185 ? -26.926 -6.837  54.412  1.00 15.05  ? 177 THR B N   1 
ATOM   3119  C CA  . THR B  1 185 ? -27.422 -7.089  53.064  1.00 21.26  ? 177 THR B CA  1 
ATOM   3120  C C   . THR B  1 185 ? -26.854 -6.066  52.064  1.00 24.63  ? 177 THR B C   1 
ATOM   3121  O O   . THR B  1 185 ? -26.641 -4.897  52.402  1.00 23.48  ? 177 THR B O   1 
ATOM   3122  C CB  . THR B  1 185 ? -28.961 -7.103  52.991  1.00 21.50  ? 177 THR B CB  1 
ATOM   3123  O OG1 . THR B  1 185 ? -29.467 -5.787  53.231  1.00 27.02  ? 177 THR B OG1 1 
ATOM   3124  C CG2 . THR B  1 185 ? -29.531 -8.062  54.013  1.00 27.68  ? 177 THR B CG2 1 
ATOM   3125  N N   . GLN B  1 186 ? -26.615 -6.508  50.833  1.00 24.37  ? 178 GLN B N   1 
ATOM   3126  C CA  . GLN B  1 186 ? -25.914 -5.688  49.844  1.00 22.09  ? 178 GLN B CA  1 
ATOM   3127  C C   . GLN B  1 186 ? -26.616 -5.785  48.508  1.00 17.07  ? 178 GLN B C   1 
ATOM   3128  O O   . GLN B  1 186 ? -26.338 -6.702  47.755  1.00 19.35  ? 178 GLN B O   1 
ATOM   3129  C CB  . GLN B  1 186 ? -24.488 -6.205  49.689  1.00 16.62  ? 178 GLN B CB  1 
ATOM   3130  C CG  . GLN B  1 186 ? -23.443 -5.127  49.650  1.00 26.32  ? 178 GLN B CG  1 
ATOM   3131  C CD  . GLN B  1 186 ? -22.327 -5.354  50.652  1.00 23.56  ? 178 GLN B CD  1 
ATOM   3132  O OE1 . GLN B  1 186 ? -21.193 -4.909  50.454  1.00 20.99  ? 178 GLN B OE1 1 
ATOM   3133  N NE2 . GLN B  1 186 ? -22.642 -6.043  51.731  1.00 22.53  ? 178 GLN B NE2 1 
ATOM   3134  N N   . LYS B  1 187 ? -27.507 -4.842  48.210  1.00 20.75  ? 179 LYS B N   1 
ATOM   3135  C CA  . LYS B  1 187 ? -28.392 -4.935  47.034  1.00 23.67  ? 179 LYS B CA  1 
ATOM   3136  C C   . LYS B  1 187 ? -28.179 -3.836  45.974  1.00 24.70  ? 179 LYS B C   1 
ATOM   3137  O O   . LYS B  1 187 ? -27.646 -2.767  46.273  1.00 24.05  ? 179 LYS B O   1 
ATOM   3138  C CB  . LYS B  1 187 ? -29.859 -4.892  47.484  1.00 27.03  ? 179 LYS B CB  1 
ATOM   3139  C CG  . LYS B  1 187 ? -30.260 -5.955  48.509  1.00 38.62  ? 179 LYS B CG  1 
ATOM   3140  C CD  . LYS B  1 187 ? -31.602 -5.607  49.155  1.00 43.30  ? 179 LYS B CD  1 
ATOM   3141  C CE  . LYS B  1 187 ? -32.092 -6.695  50.102  1.00 39.00  ? 179 LYS B CE  1 
ATOM   3142  N NZ  . LYS B  1 187 ? -33.455 -6.379  50.638  1.00 57.53  ? 179 LYS B NZ  1 
ATOM   3143  N N   . LYS B  1 188 ? -28.622 -4.096  44.744  1.00 22.36  ? 180 LYS B N   1 
ATOM   3144  C CA  . LYS B  1 188 ? -28.621 -3.080  43.690  1.00 20.77  ? 180 LYS B CA  1 
ATOM   3145  C C   . LYS B  1 188 ? -29.673 -2.006  43.947  1.00 24.04  ? 180 LYS B C   1 
ATOM   3146  O O   . LYS B  1 188 ? -30.730 -2.274  44.516  1.00 22.97  ? 180 LYS B O   1 
ATOM   3147  C CB  . LYS B  1 188 ? -28.916 -3.702  42.321  1.00 24.91  ? 180 LYS B CB  1 
ATOM   3148  C CG  . LYS B  1 188 ? -27.961 -4.773  41.844  1.00 33.62  ? 180 LYS B CG  1 
ATOM   3149  C CD  . LYS B  1 188 ? -28.268 -5.127  40.386  1.00 42.85  ? 180 LYS B CD  1 
ATOM   3150  C CE  . LYS B  1 188 ? -27.780 -6.527  40.021  1.00 47.49  ? 180 LYS B CE  1 
ATOM   3151  N NZ  . LYS B  1 188 ? -28.052 -6.861  38.583  1.00 54.84  ? 180 LYS B NZ  1 
ATOM   3152  N N   . ASN B  1 189 ? -29.401 -0.801  43.463  1.00 28.79  ? 181 ASN B N   1 
ATOM   3153  C CA  . ASN B  1 189 ? -30.291 0.343   43.639  1.00 26.64  ? 181 ASN B CA  1 
ATOM   3154  C C   . ASN B  1 189 ? -29.952 1.375   42.557  1.00 26.63  ? 181 ASN B C   1 
ATOM   3155  O O   . ASN B  1 189 ? -28.869 1.337   41.985  1.00 28.30  ? 181 ASN B O   1 
ATOM   3156  C CB  . ASN B  1 189 ? -30.080 0.926   45.039  1.00 27.93  ? 181 ASN B CB  1 
ATOM   3157  C CG  . ASN B  1 189 ? -31.142 1.928   45.436  1.00 29.17  ? 181 ASN B CG  1 
ATOM   3158  O OD1 . ASN B  1 189 ? -30.961 3.141   45.290  1.00 31.11  ? 181 ASN B OD1 1 
ATOM   3159  N ND2 . ASN B  1 189 ? -32.249 1.430   45.968  1.00 35.10  ? 181 ASN B ND2 1 
ATOM   3160  N N   . SER B  1 190 ? -30.871 2.282   42.256  1.00 30.30  ? 182 SER B N   1 
ATOM   3161  C CA  . SER B  1 190 ? -30.611 3.293   41.236  1.00 31.76  ? 182 SER B CA  1 
ATOM   3162  C C   . SER B  1 190 ? -31.270 4.621   41.583  1.00 37.40  ? 182 SER B C   1 
ATOM   3163  O O   . SER B  1 190 ? -32.491 4.715   41.643  1.00 42.90  ? 182 SER B O   1 
ATOM   3164  C CB  . SER B  1 190 ? -31.140 2.835   39.887  1.00 31.60  ? 182 SER B CB  1 
ATOM   3165  O OG  . SER B  1 190 ? -32.309 3.577   39.572  1.00 42.06  ? 182 SER B OG  1 
ATOM   3166  N N   . VAL B  1 191 ? -30.453 5.647   41.790  1.00 39.27  ? 183 VAL B N   1 
ATOM   3167  C CA  . VAL B  1 191 ? -30.918 6.983   42.159  1.00 31.22  ? 183 VAL B CA  1 
ATOM   3168  C C   . VAL B  1 191 ? -31.385 7.777   40.935  1.00 34.45  ? 183 VAL B C   1 
ATOM   3169  O O   . VAL B  1 191 ? -30.875 7.582   39.833  1.00 36.68  ? 183 VAL B O   1 
ATOM   3170  C CB  . VAL B  1 191 ? -29.766 7.750   42.840  1.00 33.19  ? 183 VAL B CB  1 
ATOM   3171  C CG1 . VAL B  1 191 ? -30.208 9.117   43.312  1.00 35.23  ? 183 VAL B CG1 1 
ATOM   3172  C CG2 . VAL B  1 191 ? -29.218 6.935   43.993  1.00 36.30  ? 183 VAL B CG2 1 
ATOM   3173  N N   . THR B  1 192 ? -32.356 8.666   41.136  1.00 37.97  ? 184 THR B N   1 
ATOM   3174  C CA  . THR B  1 192 ? -32.802 9.605   40.108  1.00 31.93  ? 184 THR B CA  1 
ATOM   3175  C C   . THR B  1 192 ? -33.414 10.830  40.773  1.00 27.72  ? 184 THR B C   1 
ATOM   3176  O O   . THR B  1 192 ? -32.729 11.820  41.018  1.00 33.80  ? 184 THR B O   1 
ATOM   3177  C CB  . THR B  1 192 ? -33.847 8.979   39.163  1.00 33.23  ? 184 THR B CB  1 
ATOM   3178  O OG1 . THR B  1 192 ? -34.492 7.884   39.821  1.00 46.03  ? 184 THR B OG1 1 
ATOM   3179  C CG2 . THR B  1 192 ? -33.199 8.462   37.921  1.00 26.84  ? 184 THR B CG2 1 
ATOM   3180  N N   . PRO B  1 197 ? -32.938 13.230  33.576  1.00 43.77  ? 189 PRO B N   1 
ATOM   3181  C CA  . PRO B  1 197 ? -33.436 11.978  32.997  1.00 40.43  ? 189 PRO B CA  1 
ATOM   3182  C C   . PRO B  1 197 ? -32.521 10.781  33.259  1.00 41.17  ? 189 PRO B C   1 
ATOM   3183  O O   . PRO B  1 197 ? -33.003 9.658   33.154  1.00 47.02  ? 189 PRO B O   1 
ATOM   3184  C CB  . PRO B  1 197 ? -33.442 12.276  31.499  1.00 44.82  ? 189 PRO B CB  1 
ATOM   3185  C CG  . PRO B  1 197 ? -32.265 13.189  31.321  1.00 41.46  ? 189 PRO B CG  1 
ATOM   3186  C CD  . PRO B  1 197 ? -32.211 14.041  32.580  1.00 46.40  ? 189 PRO B CD  1 
ATOM   3187  N N   . GLU B  1 198 ? -31.245 11.006  33.582  1.00 36.50  ? 190 GLU B N   1 
ATOM   3188  C CA  . GLU B  1 198 ? -30.294 9.902   33.769  1.00 32.95  ? 190 GLU B CA  1 
ATOM   3189  C C   . GLU B  1 198 ? -30.205 9.371   35.204  1.00 28.61  ? 190 GLU B C   1 
ATOM   3190  O O   . GLU B  1 198 ? -30.244 10.127  36.172  1.00 27.84  ? 190 GLU B O   1 
ATOM   3191  C CB  . GLU B  1 198 ? -28.892 10.272  33.253  1.00 37.94  ? 190 GLU B CB  1 
ATOM   3192  C CG  . GLU B  1 198 ? -28.711 10.260  31.705  1.00 45.08  ? 190 GLU B CG  1 
ATOM   3193  C CD  . GLU B  1 198 ? -28.864 8.871   31.047  1.00 46.22  ? 190 GLU B CD  1 
ATOM   3194  O OE1 . GLU B  1 198 ? -28.432 7.848   31.636  1.00 43.77  ? 190 GLU B OE1 1 
ATOM   3195  O OE2 . GLU B  1 198 ? -29.417 8.809   29.923  1.00 48.29  ? 190 GLU B OE2 1 
ATOM   3196  N N   . ALA B  1 199 ? -30.068 8.054   35.312  1.00 29.08  ? 191 ALA B N   1 
ATOM   3197  C CA  . ALA B  1 199 ? -30.005 7.348   36.589  1.00 24.48  ? 191 ALA B CA  1 
ATOM   3198  C C   . ALA B  1 199 ? -28.571 6.986   36.953  1.00 24.29  ? 191 ALA B C   1 
ATOM   3199  O O   . ALA B  1 199 ? -27.740 6.761   36.073  1.00 23.59  ? 191 ALA B O   1 
ATOM   3200  C CB  . ALA B  1 199 ? -30.835 6.082   36.509  1.00 23.23  ? 191 ALA B CB  1 
ATOM   3201  N N   . TYR B  1 200 ? -28.281 6.915   38.246  1.00 23.75  ? 192 TYR B N   1 
ATOM   3202  C CA  . TYR B  1 200 ? -26.977 6.432   38.688  1.00 22.47  ? 192 TYR B CA  1 
ATOM   3203  C C   . TYR B  1 200 ? -27.192 5.188   39.509  1.00 25.06  ? 192 TYR B C   1 
ATOM   3204  O O   . TYR B  1 200 ? -27.958 5.196   40.468  1.00 29.24  ? 192 TYR B O   1 
ATOM   3205  C CB  . TYR B  1 200 ? -26.243 7.477   39.525  1.00 20.86  ? 192 TYR B CB  1 
ATOM   3206  C CG  . TYR B  1 200 ? -26.013 8.756   38.779  1.00 22.02  ? 192 TYR B CG  1 
ATOM   3207  C CD1 . TYR B  1 200 ? -27.051 9.657   38.589  1.00 25.49  ? 192 TYR B CD1 1 
ATOM   3208  C CD2 . TYR B  1 200 ? -24.768 9.067   38.252  1.00 18.52  ? 192 TYR B CD2 1 
ATOM   3209  C CE1 . TYR B  1 200 ? -26.866 10.822  37.903  1.00 24.05  ? 192 TYR B CE1 1 
ATOM   3210  C CE2 . TYR B  1 200 ? -24.568 10.243  37.565  1.00 17.96  ? 192 TYR B CE2 1 
ATOM   3211  C CZ  . TYR B  1 200 ? -25.628 11.117  37.396  1.00 25.00  ? 192 TYR B CZ  1 
ATOM   3212  O OH  . TYR B  1 200 ? -25.477 12.292  36.706  1.00 32.12  ? 192 TYR B OH  1 
ATOM   3213  N N   . GLU B  1 201 ? -26.537 4.110   39.117  1.00 17.85  ? 193 GLU B N   1 
ATOM   3214  C CA  . GLU B  1 201 ? -26.596 2.898   39.894  1.00 20.13  ? 193 GLU B CA  1 
ATOM   3215  C C   . GLU B  1 201 ? -25.676 3.012   41.097  1.00 26.54  ? 193 GLU B C   1 
ATOM   3216  O O   . GLU B  1 201 ? -24.699 3.770   41.092  1.00 22.93  ? 193 GLU B O   1 
ATOM   3217  C CB  . GLU B  1 201 ? -26.186 1.713   39.050  1.00 17.82  ? 193 GLU B CB  1 
ATOM   3218  C CG  . GLU B  1 201 ? -26.996 1.584   37.813  1.00 18.19  ? 193 GLU B CG  1 
ATOM   3219  C CD  . GLU B  1 201 ? -26.749 0.270   37.118  1.00 28.86  ? 193 GLU B CD  1 
ATOM   3220  O OE1 . GLU B  1 201 ? -26.020 -0.580  37.683  1.00 32.73  ? 193 GLU B OE1 1 
ATOM   3221  O OE2 . GLU B  1 201 ? -27.284 0.088   36.006  1.00 31.17  ? 193 GLU B OE2 1 
ATOM   3222  N N   . ASP B  1 202 ? -26.003 2.243   42.127  1.00 23.84  ? 194 ASP B N   1 
ATOM   3223  C CA  . ASP B  1 202 ? -25.241 2.228   43.356  1.00 21.09  ? 194 ASP B CA  1 
ATOM   3224  C C   . ASP B  1 202 ? -25.478 0.879   44.031  1.00 20.84  ? 194 ASP B C   1 
ATOM   3225  O O   . ASP B  1 202 ? -26.394 0.144   43.661  1.00 22.18  ? 194 ASP B O   1 
ATOM   3226  C CB  . ASP B  1 202 ? -25.696 3.373   44.269  1.00 21.99  ? 194 ASP B CB  1 
ATOM   3227  C CG  . ASP B  1 202 ? -26.981 3.046   45.032  1.00 31.74  ? 194 ASP B CG  1 
ATOM   3228  O OD1 . ASP B  1 202 ? -26.886 2.431   46.127  1.00 28.88  ? 194 ASP B OD1 1 
ATOM   3229  O OD2 . ASP B  1 202 ? -28.082 3.407   44.543  1.00 34.81  ? 194 ASP B OD2 1 
ATOM   3230  N N   . VAL B  1 203 ? -24.643 0.544   45.003  1.00 17.78  ? 195 VAL B N   1 
ATOM   3231  C CA  . VAL B  1 203 ? -24.913 -0.606  45.845  1.00 19.78  ? 195 VAL B CA  1 
ATOM   3232  C C   . VAL B  1 203 ? -25.331 -0.120  47.225  1.00 16.19  ? 195 VAL B C   1 
ATOM   3233  O O   . VAL B  1 203 ? -24.583 0.576   47.910  1.00 14.85  ? 195 VAL B O   1 
ATOM   3234  C CB  . VAL B  1 203 ? -23.701 -1.552  45.967  1.00 17.52  ? 195 VAL B CB  1 
ATOM   3235  C CG1 . VAL B  1 203 ? -23.966 -2.600  47.036  1.00 15.47  ? 195 VAL B CG1 1 
ATOM   3236  C CG2 . VAL B  1 203 ? -23.408 -2.220  44.634  1.00 18.66  ? 195 VAL B CG2 1 
ATOM   3237  N N   . GLU B  1 204 ? -26.541 -0.479  47.624  1.00 21.15  ? 196 GLU B N   1 
ATOM   3238  C CA  . GLU B  1 204 ? -27.021 -0.143  48.957  1.00 20.97  ? 196 GLU B CA  1 
ATOM   3239  C C   . GLU B  1 204 ? -26.556 -1.197  49.953  1.00 15.43  ? 196 GLU B C   1 
ATOM   3240  O O   . GLU B  1 204 ? -26.833 -2.382  49.794  1.00 17.76  ? 196 GLU B O   1 
ATOM   3241  C CB  . GLU B  1 204 ? -28.540 -0.004  48.957  1.00 21.46  ? 196 GLU B CB  1 
ATOM   3242  C CG  . GLU B  1 204 ? -29.100 0.531   50.252  1.00 30.22  ? 196 GLU B CG  1 
ATOM   3243  C CD  . GLU B  1 204 ? -30.494 1.090   50.083  1.00 37.79  ? 196 GLU B CD  1 
ATOM   3244  O OE1 . GLU B  1 204 ? -30.967 1.132   48.924  1.00 44.63  ? 196 GLU B OE1 1 
ATOM   3245  O OE2 . GLU B  1 204 ? -31.107 1.497   51.098  1.00 40.18  ? 196 GLU B OE2 1 
ATOM   3246  N N   . VAL B  1 205 ? -25.786 -0.769  50.942  1.00 15.19  ? 197 VAL B N   1 
ATOM   3247  C CA  . VAL B  1 205 ? -25.367 -1.664  52.012  1.00 19.50  ? 197 VAL B CA  1 
ATOM   3248  C C   . VAL B  1 205 ? -26.199 -1.368  53.263  1.00 21.74  ? 197 VAL B C   1 
ATOM   3249  O O   . VAL B  1 205 ? -26.195 -0.238  53.781  1.00 16.02  ? 197 VAL B O   1 
ATOM   3250  C CB  . VAL B  1 205 ? -23.871 -1.522  52.330  1.00 17.06  ? 197 VAL B CB  1 
ATOM   3251  C CG1 . VAL B  1 205 ? -23.508 -2.301  53.585  1.00 15.42  ? 197 VAL B CG1 1 
ATOM   3252  C CG2 . VAL B  1 205 ? -23.051 -2.001  51.169  1.00 20.15  ? 197 VAL B CG2 1 
ATOM   3253  N N   . SER B  1 206 ? -26.949 -2.376  53.708  1.00 23.47  ? 198 SER B N   1 
ATOM   3254  C CA  . SER B  1 206 ? -27.713 -2.282  54.948  1.00 19.96  ? 198 SER B CA  1 
ATOM   3255  C C   . SER B  1 206 ? -26.967 -3.023  56.041  1.00 18.59  ? 198 SER B C   1 
ATOM   3256  O O   . SER B  1 206 ? -26.732 -4.228  55.954  1.00 17.69  ? 198 SER B O   1 
ATOM   3257  C CB  . SER B  1 206 ? -29.126 -2.822  54.771  1.00 19.28  ? 198 SER B CB  1 
ATOM   3258  O OG  . SER B  1 206 ? -29.958 -1.863  54.138  1.00 21.54  ? 198 SER B OG  1 
ATOM   3259  N N   . LEU B  1 207 ? -26.566 -2.275  57.058  1.00 19.49  ? 199 LEU B N   1 
ATOM   3260  C CA  . LEU B  1 207 ? -25.747 -2.819  58.121  1.00 20.58  ? 199 LEU B CA  1 
ATOM   3261  C C   . LEU B  1 207 ? -26.529 -2.765  59.415  1.00 21.25  ? 199 LEU B C   1 
ATOM   3262  O O   . LEU B  1 207 ? -26.739 -1.691  59.975  1.00 23.32  ? 199 LEU B O   1 
ATOM   3263  C CB  . LEU B  1 207 ? -24.465 -2.016  58.248  1.00 18.52  ? 199 LEU B CB  1 
ATOM   3264  C CG  . LEU B  1 207 ? -23.589 -2.320  59.453  1.00 20.00  ? 199 LEU B CG  1 
ATOM   3265  C CD1 . LEU B  1 207 ? -23.083 -3.752  59.410  1.00 16.17  ? 199 LEU B CD1 1 
ATOM   3266  C CD2 . LEU B  1 207 ? -22.430 -1.318  59.512  1.00 17.84  ? 199 LEU B CD2 1 
ATOM   3267  N N   . ASN B  1 208 ? -26.981 -3.936  59.857  1.00 22.47  ? 200 ASN B N   1 
ATOM   3268  C CA  . ASN B  1 208 ? -27.758 -4.105  61.083  1.00 20.73  ? 200 ASN B CA  1 
ATOM   3269  C C   . ASN B  1 208 ? -26.833 -4.501  62.235  1.00 17.53  ? 200 ASN B C   1 
ATOM   3270  O O   . ASN B  1 208 ? -26.331 -5.611  62.269  1.00 20.35  ? 200 ASN B O   1 
ATOM   3271  C CB  . ASN B  1 208 ? -28.830 -5.175  60.839  1.00 24.39  ? 200 ASN B CB  1 
ATOM   3272  C CG  . ASN B  1 208 ? -29.701 -5.443  62.056  1.00 24.58  ? 200 ASN B CG  1 
ATOM   3273  O OD1 . ASN B  1 208 ? -30.180 -6.566  62.250  1.00 25.31  ? 200 ASN B OD1 1 
ATOM   3274  N ND2 . ASN B  1 208 ? -29.914 -4.421  62.875  1.00 21.72  ? 200 ASN B ND2 1 
ATOM   3275  N N   . PHE B  1 209 ? -26.592 -3.578  63.161  1.00 18.53  ? 201 PHE B N   1 
ATOM   3276  C CA  . PHE B  1 209 ? -25.613 -3.777  64.235  1.00 18.60  ? 201 PHE B CA  1 
ATOM   3277  C C   . PHE B  1 209 ? -26.198 -3.356  65.599  1.00 18.05  ? 201 PHE B C   1 
ATOM   3278  O O   . PHE B  1 209 ? -27.211 -2.649  65.658  1.00 16.76  ? 201 PHE B O   1 
ATOM   3279  C CB  . PHE B  1 209 ? -24.332 -2.981  63.931  1.00 15.68  ? 201 PHE B CB  1 
ATOM   3280  C CG  . PHE B  1 209 ? -24.482 -1.485  64.110  1.00 16.38  ? 201 PHE B CG  1 
ATOM   3281  C CD1 . PHE B  1 209 ? -25.197 -0.725  63.196  1.00 14.82  ? 201 PHE B CD1 1 
ATOM   3282  C CD2 . PHE B  1 209 ? -23.910 -0.838  65.205  1.00 17.77  ? 201 PHE B CD2 1 
ATOM   3283  C CE1 . PHE B  1 209 ? -25.343 0.651   63.372  1.00 16.15  ? 201 PHE B CE1 1 
ATOM   3284  C CE2 . PHE B  1 209 ? -24.049 0.539   65.380  1.00 13.94  ? 201 PHE B CE2 1 
ATOM   3285  C CZ  . PHE B  1 209 ? -24.763 1.282   64.462  1.00 12.56  ? 201 PHE B CZ  1 
ATOM   3286  N N   . ARG B  1 210 ? -25.563 -3.780  66.689  1.00 15.16  ? 202 ARG B N   1 
ATOM   3287  C CA  . ARG B  1 210 ? -26.040 -3.423  68.028  1.00 19.30  ? 202 ARG B CA  1 
ATOM   3288  C C   . ARG B  1 210 ? -24.898 -3.378  69.025  1.00 16.39  ? 202 ARG B C   1 
ATOM   3289  O O   . ARG B  1 210 ? -23.887 -4.046  68.836  1.00 16.72  ? 202 ARG B O   1 
ATOM   3290  C CB  . ARG B  1 210 ? -27.150 -4.385  68.519  1.00 24.69  ? 202 ARG B CB  1 
ATOM   3291  C CG  . ARG B  1 210 ? -26.681 -5.689  69.196  1.00 20.37  ? 202 ARG B CG  1 
ATOM   3292  C CD  . ARG B  1 210 ? -27.730 -6.216  70.202  1.00 26.81  ? 202 ARG B CD  1 
ATOM   3293  N NE  . ARG B  1 210 ? -28.495 -7.387  69.750  1.00 28.77  ? 202 ARG B NE  1 
ATOM   3294  C CZ  . ARG B  1 210 ? -28.089 -8.652  69.886  1.00 28.01  ? 202 ARG B CZ  1 
ATOM   3295  N NH1 . ARG B  1 210 ? -26.917 -8.927  70.448  1.00 20.64  ? 202 ARG B NH1 1 
ATOM   3296  N NH2 . ARG B  1 210 ? -28.844 -9.646  69.440  1.00 29.06  ? 202 ARG B NH2 1 
ATOM   3297  N N   . LYS B  1 211 ? -25.056 -2.582  70.081  1.00 19.74  ? 203 LYS B N   1 
ATOM   3298  C CA  . LYS B  1 211 ? -24.051 -2.520  71.150  1.00 21.78  ? 203 LYS B CA  1 
ATOM   3299  C C   . LYS B  1 211 ? -23.978 -3.877  71.856  1.00 21.28  ? 203 LYS B C   1 
ATOM   3300  O O   . LYS B  1 211 ? -24.989 -4.557  72.023  1.00 17.81  ? 203 LYS B O   1 
ATOM   3301  C CB  . LYS B  1 211 ? -24.357 -1.380  72.146  1.00 17.75  ? 203 LYS B CB  1 
ATOM   3302  C CG  . LYS B  1 211 ? -23.144 -0.914  72.968  1.00 22.97  ? 203 LYS B CG  1 
ATOM   3303  C CD  . LYS B  1 211 ? -23.317 0.492   73.570  1.00 30.69  ? 203 LYS B CD  1 
ATOM   3304  C CE  . LYS B  1 211 ? -23.641 1.556   72.499  1.00 41.54  ? 203 LYS B CE  1 
ATOM   3305  N NZ  . LYS B  1 211 ? -23.522 2.984   72.964  1.00 36.78  ? 203 LYS B NZ  1 
ATOM   3306  N N   . LYS B  1 212 ? -22.776 -4.297  72.226  1.00 22.15  ? 204 LYS B N   1 
ATOM   3307  C CA  . LYS B  1 212 ? -22.628 -5.576  72.898  1.00 23.79  ? 204 LYS B CA  1 
ATOM   3308  C C   . LYS B  1 212 ? -23.098 -5.500  74.351  1.00 33.65  ? 204 LYS B C   1 
ATOM   3309  O O   . LYS B  1 212 ? -22.427 -4.903  75.199  1.00 36.26  ? 204 LYS B O   1 
ATOM   3310  C CB  . LYS B  1 212 ? -21.188 -6.057  72.829  1.00 20.02  ? 204 LYS B CB  1 
ATOM   3311  C CG  . LYS B  1 212 ? -20.857 -6.848  71.580  1.00 24.83  ? 204 LYS B CG  1 
ATOM   3312  C CD  . LYS B  1 212 ? -19.355 -7.044  71.518  1.00 27.92  ? 204 LYS B CD  1 
ATOM   3313  C CE  . LYS B  1 212 ? -18.913 -8.002  70.429  1.00 24.17  ? 204 LYS B CE  1 
ATOM   3314  N NZ  . LYS B  1 212 ? -17.522 -8.488  70.735  1.00 27.04  ? 204 LYS B NZ  1 
ATOM   3315  N N   . GLY B  1 213 ? -24.252 -6.111  74.626  1.00 33.88  ? 205 GLY B N   1 
ATOM   3316  C CA  . GLY B  1 213 ? -24.827 -6.130  75.957  1.00 28.40  ? 205 GLY B CA  1 
ATOM   3317  C C   . GLY B  1 213 ? -24.093 -7.128  76.823  1.00 41.81  ? 205 GLY B C   1 
ATOM   3318  O O   . GLY B  1 213 ? -23.045 -7.642  76.421  1.00 43.99  ? 205 GLY B O   1 
ATOM   3319  N N   . ASP C  1 1   ? -24.378 11.108  20.269  1.00 33.12  ? -7  ASP C N   1 
ATOM   3320  C CA  . ASP C  1 1   ? -25.616 10.338  20.363  1.00 47.64  ? -7  ASP C CA  1 
ATOM   3321  C C   . ASP C  1 1   ? -25.474 9.110   21.263  1.00 52.11  ? -7  ASP C C   1 
ATOM   3322  O O   . ASP C  1 1   ? -24.375 8.566   21.424  1.00 44.78  ? -7  ASP C O   1 
ATOM   3323  C CB  . ASP C  1 1   ? -26.117 9.947   18.971  1.00 44.65  ? -7  ASP C CB  1 
ATOM   3324  C CG  . ASP C  1 1   ? -26.681 11.137  18.208  1.00 51.42  ? -7  ASP C CG  1 
ATOM   3325  O OD1 . ASP C  1 1   ? -26.402 12.291  18.615  1.00 41.65  ? -7  ASP C OD1 1 
ATOM   3326  O OD2 . ASP C  1 1   ? -27.400 10.924  17.203  1.00 58.66  ? -7  ASP C OD2 1 
ATOM   3327  N N   . TYR C  1 2   ? -26.598 8.686   21.838  1.00 46.41  ? -6  TYR C N   1 
ATOM   3328  C CA  . TYR C  1 2   ? -26.629 7.624   22.842  1.00 44.09  ? -6  TYR C CA  1 
ATOM   3329  C C   . TYR C  1 2   ? -25.993 6.321   22.367  1.00 38.36  ? -6  TYR C C   1 
ATOM   3330  O O   . TYR C  1 2   ? -25.341 5.618   23.143  1.00 31.89  ? -6  TYR C O   1 
ATOM   3331  C CB  . TYR C  1 2   ? -28.076 7.359   23.275  1.00 58.92  ? -6  TYR C CB  1 
ATOM   3332  C CG  . TYR C  1 2   ? -28.831 8.594   23.737  1.00 68.24  ? -6  TYR C CG  1 
ATOM   3333  C CD1 . TYR C  1 2   ? -28.160 9.687   24.289  1.00 71.58  ? -6  TYR C CD1 1 
ATOM   3334  C CD2 . TYR C  1 2   ? -30.215 8.670   23.619  1.00 69.31  ? -6  TYR C CD2 1 
ATOM   3335  C CE1 . TYR C  1 2   ? -28.850 10.819  24.711  1.00 77.93  ? -6  TYR C CE1 1 
ATOM   3336  C CE2 . TYR C  1 2   ? -30.914 9.796   24.041  1.00 75.45  ? -6  TYR C CE2 1 
ATOM   3337  C CZ  . TYR C  1 2   ? -30.227 10.866  24.586  1.00 77.63  ? -6  TYR C CZ  1 
ATOM   3338  O OH  . TYR C  1 2   ? -30.914 11.984  25.004  1.00 75.35  ? -6  TYR C OH  1 
ATOM   3339  N N   . LYS C  1 3   ? -26.190 6.021   21.084  1.00 45.24  ? -5  LYS C N   1 
ATOM   3340  C CA  . LYS C  1 3   ? -25.720 4.791   20.436  1.00 39.38  ? -5  LYS C CA  1 
ATOM   3341  C C   . LYS C  1 3   ? -24.204 4.587   20.570  1.00 39.55  ? -5  LYS C C   1 
ATOM   3342  O O   . LYS C  1 3   ? -23.728 3.474   20.800  1.00 35.34  ? -5  LYS C O   1 
ATOM   3343  C CB  . LYS C  1 3   ? -26.127 4.822   18.949  1.00 45.49  ? -5  LYS C CB  1 
ATOM   3344  C CG  . LYS C  1 3   ? -26.303 3.456   18.266  1.00 46.77  ? -5  LYS C CG  1 
ATOM   3345  C CD  . LYS C  1 3   ? -26.908 3.579   16.854  1.00 51.32  ? -5  LYS C CD  1 
ATOM   3346  C CE  . LYS C  1 3   ? -25.844 3.850   15.760  1.00 56.79  ? -5  LYS C CE  1 
ATOM   3347  N NZ  . LYS C  1 3   ? -25.523 5.298   15.512  1.00 44.25  ? -5  LYS C NZ  1 
ATOM   3348  N N   . ASP C  1 4   ? -23.454 5.679   20.449  1.00 45.03  ? -4  ASP C N   1 
ATOM   3349  C CA  . ASP C  1 4   ? -21.998 5.623   20.342  1.00 42.74  ? -4  ASP C CA  1 
ATOM   3350  C C   . ASP C  1 4   ? -21.292 6.073   21.628  1.00 35.57  ? -4  ASP C C   1 
ATOM   3351  O O   . ASP C  1 4   ? -20.073 6.268   21.647  1.00 29.84  ? -4  ASP C O   1 
ATOM   3352  C CB  . ASP C  1 4   ? -21.553 6.480   19.150  1.00 35.56  ? -4  ASP C CB  1 
ATOM   3353  C CG  . ASP C  1 4   ? -22.619 6.551   18.055  1.00 40.97  ? -4  ASP C CG  1 
ATOM   3354  O OD1 . ASP C  1 4   ? -22.674 5.639   17.202  1.00 45.81  ? -4  ASP C OD1 1 
ATOM   3355  O OD2 . ASP C  1 4   ? -23.422 7.513   18.056  1.00 45.41  ? -4  ASP C OD2 1 
ATOM   3356  N N   . ASP C  1 5   ? -22.070 6.206   22.703  1.00 39.61  ? -3  ASP C N   1 
ATOM   3357  C CA  . ASP C  1 5   ? -21.594 6.780   23.966  1.00 33.27  ? -3  ASP C CA  1 
ATOM   3358  C C   . ASP C  1 5   ? -20.590 5.929   24.746  1.00 29.56  ? -3  ASP C C   1 
ATOM   3359  O O   . ASP C  1 5   ? -19.825 6.462   25.553  1.00 23.82  ? -3  ASP C O   1 
ATOM   3360  C CB  . ASP C  1 5   ? -22.772 7.148   24.874  1.00 35.62  ? -3  ASP C CB  1 
ATOM   3361  C CG  . ASP C  1 5   ? -22.920 8.651   25.051  1.00 46.02  ? -3  ASP C CG  1 
ATOM   3362  O OD1 . ASP C  1 5   ? -23.900 9.223   24.513  1.00 46.36  ? -3  ASP C OD1 1 
ATOM   3363  O OD2 . ASP C  1 5   ? -22.045 9.263   25.717  1.00 47.17  ? -3  ASP C OD2 1 
ATOM   3364  N N   . ASP C  1 6   ? -20.588 4.619   24.517  1.00 27.42  ? -2  ASP C N   1 
ATOM   3365  C CA  . ASP C  1 6   ? -19.650 3.745   25.218  1.00 26.91  ? -2  ASP C CA  1 
ATOM   3366  C C   . ASP C  1 6   ? -18.539 3.250   24.292  1.00 27.51  ? -2  ASP C C   1 
ATOM   3367  O O   . ASP C  1 6   ? -17.953 2.183   24.522  1.00 26.43  ? -2  ASP C O   1 
ATOM   3368  C CB  . ASP C  1 6   ? -20.370 2.550   25.865  1.00 27.29  ? -2  ASP C CB  1 
ATOM   3369  C CG  . ASP C  1 6   ? -21.190 2.933   27.088  1.00 25.43  ? -2  ASP C CG  1 
ATOM   3370  O OD1 . ASP C  1 6   ? -21.431 4.136   27.323  1.00 17.90  ? -2  ASP C OD1 1 
ATOM   3371  O OD2 . ASP C  1 6   ? -21.610 2.005   27.813  1.00 29.06  ? -2  ASP C OD2 1 
ATOM   3372  N N   . ASP C  1 7   ? -18.269 4.017   23.237  1.00 28.08  ? -1  ASP C N   1 
ATOM   3373  C CA  . ASP C  1 7   ? -17.118 3.768   22.369  1.00 24.64  ? -1  ASP C CA  1 
ATOM   3374  C C   . ASP C  1 7   ? -15.864 4.339   23.028  1.00 22.51  ? -1  ASP C C   1 
ATOM   3375  O O   . ASP C  1 7   ? -15.715 5.553   23.118  1.00 21.72  ? -1  ASP C O   1 
ATOM   3376  C CB  . ASP C  1 7   ? -17.326 4.439   21.008  1.00 30.50  ? -1  ASP C CB  1 
ATOM   3377  C CG  . ASP C  1 7   ? -16.316 3.978   19.966  1.00 33.28  ? -1  ASP C CG  1 
ATOM   3378  O OD1 . ASP C  1 7   ? -15.355 4.731   19.675  1.00 23.84  ? -1  ASP C OD1 1 
ATOM   3379  O OD2 . ASP C  1 7   ? -16.489 2.853   19.447  1.00 47.44  ? -1  ASP C OD2 1 
ATOM   3380  N N   . LYS C  1 8   ? -14.964 3.470   23.482  1.00 20.68  ? 0   LYS C N   1 
ATOM   3381  C CA  . LYS C  1 8   ? -13.813 3.906   24.261  1.00 15.61  ? 0   LYS C CA  1 
ATOM   3382  C C   . LYS C  1 8   ? -12.902 4.856   23.462  1.00 19.23  ? 0   LYS C C   1 
ATOM   3383  O O   . LYS C  1 8   ? -12.558 5.951   23.927  1.00 15.76  ? 0   LYS C O   1 
ATOM   3384  C CB  . LYS C  1 8   ? -13.034 2.694   24.794  1.00 14.27  ? 0   LYS C CB  1 
ATOM   3385  C CG  . LYS C  1 8   ? -11.926 3.052   25.780  1.00 12.70  ? 0   LYS C CG  1 
ATOM   3386  C CD  . LYS C  1 8   ? -11.331 1.819   26.473  1.00 18.41  ? 0   LYS C CD  1 
ATOM   3387  C CE  . LYS C  1 8   ? -10.357 2.226   27.606  1.00 19.41  ? 0   LYS C CE  1 
ATOM   3388  N NZ  . LYS C  1 8   ? -9.054  1.465   27.645  1.00 21.84  ? 0   LYS C NZ  1 
ATOM   3389  N N   . LEU C  1 9   ? -12.528 4.449   22.255  1.00 16.19  ? 1   LEU C N   1 
ATOM   3390  C CA  . LEU C  1 9   ? -11.682 5.283   21.425  1.00 16.63  ? 1   LEU C CA  1 
ATOM   3391  C C   . LEU C  1 9   ? -12.263 6.705   21.276  1.00 16.95  ? 1   LEU C C   1 
ATOM   3392  O O   . LEU C  1 9   ? -11.570 7.705   21.490  1.00 15.36  ? 1   LEU C O   1 
ATOM   3393  C CB  . LEU C  1 9   ? -11.472 4.622   20.064  1.00 21.89  ? 1   LEU C CB  1 
ATOM   3394  C CG  . LEU C  1 9   ? -10.602 5.333   19.033  1.00 16.25  ? 1   LEU C CG  1 
ATOM   3395  C CD1 . LEU C  1 9   ? -9.166  5.350   19.483  1.00 13.58  ? 1   LEU C CD1 1 
ATOM   3396  C CD2 . LEU C  1 9   ? -10.742 4.613   17.725  1.00 20.69  ? 1   LEU C CD2 1 
ATOM   3397  N N   . ASP C  1 10  ? -13.544 6.791   20.943  1.00 19.14  ? 2   ASP C N   1 
ATOM   3398  C CA  . ASP C  1 10  ? -14.219 8.088   20.866  1.00 20.09  ? 2   ASP C CA  1 
ATOM   3399  C C   . ASP C  1 10  ? -14.116 8.895   22.156  1.00 18.54  ? 2   ASP C C   1 
ATOM   3400  O O   . ASP C  1 10  ? -13.904 10.110  22.118  1.00 18.40  ? 2   ASP C O   1 
ATOM   3401  C CB  . ASP C  1 10  ? -15.686 7.896   20.505  1.00 23.24  ? 2   ASP C CB  1 
ATOM   3402  C CG  . ASP C  1 10  ? -15.902 7.815   19.021  1.00 23.77  ? 2   ASP C CG  1 
ATOM   3403  O OD1 . ASP C  1 10  ? -14.978 8.198   18.276  1.00 34.52  ? 2   ASP C OD1 1 
ATOM   3404  O OD2 . ASP C  1 10  ? -16.996 7.391   18.605  1.00 28.77  ? 2   ASP C OD2 1 
ATOM   3405  N N   . ARG C  1 11  ? -14.264 8.213   23.290  1.00 14.71  ? 3   ARG C N   1 
ATOM   3406  C CA  . ARG C  1 11  ? -14.123 8.849   24.583  1.00 12.02  ? 3   ARG C CA  1 
ATOM   3407  C C   . ARG C  1 11  ? -12.699 9.379   24.763  1.00 11.61  ? 3   ARG C C   1 
ATOM   3408  O O   . ARG C  1 11  ? -12.499 10.528  25.156  1.00 10.61  ? 3   ARG C O   1 
ATOM   3409  C CB  . ARG C  1 11  ? -14.530 7.885   25.707  1.00 16.18  ? 3   ARG C CB  1 
ATOM   3410  C CG  . ARG C  1 11  ? -16.041 7.591   25.756  1.00 12.59  ? 3   ARG C CG  1 
ATOM   3411  C CD  . ARG C  1 11  ? -16.455 6.786   27.010  1.00 11.81  ? 3   ARG C CD  1 
ATOM   3412  N NE  . ARG C  1 11  ? -16.678 7.653   28.167  1.00 11.23  ? 3   ARG C NE  1 
ATOM   3413  C CZ  . ARG C  1 11  ? -17.830 8.261   28.468  1.00 9.72   ? 3   ARG C CZ  1 
ATOM   3414  N NH1 . ARG C  1 11  ? -18.912 8.103   27.718  1.00 11.76  ? 3   ARG C NH1 1 
ATOM   3415  N NH2 . ARG C  1 11  ? -17.894 9.045   29.533  1.00 9.58   ? 3   ARG C NH2 1 
ATOM   3416  N N   . ALA C  1 12  ? -11.709 8.558   24.434  1.00 11.55  ? 4   ALA C N   1 
ATOM   3417  C CA  . ALA C  1 12  ? -10.317 8.984   24.528  1.00 9.74   ? 4   ALA C CA  1 
ATOM   3418  C C   . ALA C  1 12  ? -9.948  10.169  23.594  1.00 10.92  ? 4   ALA C C   1 
ATOM   3419  O O   . ALA C  1 12  ? -9.153  11.043  23.977  1.00 7.82   ? 4   ALA C O   1 
ATOM   3420  C CB  . ALA C  1 12  ? -9.399  7.806   24.317  1.00 7.85   ? 4   ALA C CB  1 
ATOM   3421  N N   . ASP C  1 13  ? -10.535 10.215  22.397  1.00 8.73   ? 5   ASP C N   1 
ATOM   3422  C CA  . ASP C  1 13  ? -10.291 11.326  21.473  1.00 9.51   ? 5   ASP C CA  1 
ATOM   3423  C C   . ASP C  1 13  ? -10.881 12.649  21.947  1.00 11.22  ? 5   ASP C C   1 
ATOM   3424  O O   . ASP C  1 13  ? -10.298 13.712  21.709  1.00 8.58   ? 5   ASP C O   1 
ATOM   3425  C CB  . ASP C  1 13  ? -10.850 11.034  20.082  1.00 10.48  ? 5   ASP C CB  1 
ATOM   3426  C CG  . ASP C  1 13  ? -10.163 9.880   19.416  1.00 13.28  ? 5   ASP C CG  1 
ATOM   3427  O OD1 . ASP C  1 13  ? -8.982  9.620   19.714  1.00 11.10  ? 5   ASP C OD1 1 
ATOM   3428  O OD2 . ASP C  1 13  ? -10.821 9.207   18.606  1.00 22.01  ? 5   ASP C OD2 1 
ATOM   3429  N N   . ILE C  1 14  ? -12.053 12.584  22.581  1.00 10.51  ? 6   ILE C N   1 
ATOM   3430  C CA  . ILE C  1 14  ? -12.685 13.775  23.136  1.00 8.14   ? 6   ILE C CA  1 
ATOM   3431  C C   . ILE C  1 14  ? -11.821 14.333  24.263  1.00 6.70   ? 6   ILE C C   1 
ATOM   3432  O O   . ILE C  1 14  ? -11.574 15.542  24.336  1.00 5.45   ? 6   ILE C O   1 
ATOM   3433  C CB  . ILE C  1 14  ? -14.134 13.485  23.610  1.00 10.05  ? 6   ILE C CB  1 
ATOM   3434  C CG1 . ILE C  1 14  ? -15.055 13.303  22.393  1.00 10.20  ? 6   ILE C CG1 1 
ATOM   3435  C CG2 . ILE C  1 14  ? -14.662 14.621  24.497  1.00 7.39   ? 6   ILE C CG2 1 
ATOM   3436  C CD1 . ILE C  1 14  ? -16.177 12.306  22.574  1.00 12.88  ? 6   ILE C CD1 1 
ATOM   3437  N N   . LEU C  1 15  ? -11.336 13.438  25.116  1.00 6.24   ? 7   LEU C N   1 
ATOM   3438  C CA  . LEU C  1 15  ? -10.422 13.806  26.195  1.00 6.91   ? 7   LEU C CA  1 
ATOM   3439  C C   . LEU C  1 15  ? -9.184  14.523  25.669  1.00 7.65   ? 7   LEU C C   1 
ATOM   3440  O O   . LEU C  1 15  ? -8.824  15.589  26.160  1.00 7.80   ? 7   LEU C O   1 
ATOM   3441  C CB  . LEU C  1 15  ? -10.006 12.566  26.976  1.00 7.97   ? 7   LEU C CB  1 
ATOM   3442  C CG  . LEU C  1 15  ? -9.702  12.723  28.461  1.00 13.30  ? 7   LEU C CG  1 
ATOM   3443  C CD1 . LEU C  1 15  ? -10.419 13.927  29.077  1.00 11.78  ? 7   LEU C CD1 1 
ATOM   3444  C CD2 . LEU C  1 15  ? -10.123 11.458  29.169  1.00 13.28  ? 7   LEU C CD2 1 
ATOM   3445  N N   . TYR C  1 16  ? -8.539  13.923  24.667  1.00 8.93   ? 8   TYR C N   1 
ATOM   3446  C CA  . TYR C  1 16  ? -7.445  14.549  23.932  1.00 7.65   ? 8   TYR C CA  1 
ATOM   3447  C C   . TYR C  1 16  ? -7.818  15.917  23.337  1.00 7.99   ? 8   TYR C C   1 
ATOM   3448  O O   . TYR C  1 16  ? -7.089  16.894  23.543  1.00 8.41   ? 8   TYR C O   1 
ATOM   3449  C CB  . TYR C  1 16  ? -6.937  13.589  22.851  1.00 12.98  ? 8   TYR C CB  1 
ATOM   3450  C CG  . TYR C  1 16  ? -6.020  14.181  21.803  1.00 11.88  ? 8   TYR C CG  1 
ATOM   3451  C CD1 . TYR C  1 16  ? -4.695  14.478  22.093  1.00 15.56  ? 8   TYR C CD1 1 
ATOM   3452  C CD2 . TYR C  1 16  ? -6.475  14.415  20.511  1.00 11.64  ? 8   TYR C CD2 1 
ATOM   3453  C CE1 . TYR C  1 16  ? -3.854  15.018  21.119  1.00 16.95  ? 8   TYR C CE1 1 
ATOM   3454  C CE2 . TYR C  1 16  ? -5.647  14.935  19.540  1.00 13.31  ? 8   TYR C CE2 1 
ATOM   3455  C CZ  . TYR C  1 16  ? -4.338  15.235  19.843  1.00 16.05  ? 8   TYR C CZ  1 
ATOM   3456  O OH  . TYR C  1 16  ? -3.515  15.761  18.870  1.00 19.17  ? 8   TYR C OH  1 
ATOM   3457  N N   . ASN C  1 17  ? -8.943  16.000  22.620  1.00 6.87   ? 9   ASN C N   1 
ATOM   3458  C CA  . ASN C  1 17  ? -9.360  17.272  22.035  1.00 4.76   ? 9   ASN C CA  1 
ATOM   3459  C C   . ASN C  1 17  ? -9.436  18.351  23.084  1.00 8.22   ? 9   ASN C C   1 
ATOM   3460  O O   . ASN C  1 17  ? -8.777  19.384  22.931  1.00 8.48   ? 9   ASN C O   1 
ATOM   3461  C CB  . ASN C  1 17  ? -10.672 17.175  21.267  1.00 4.84   ? 9   ASN C CB  1 
ATOM   3462  C CG  . ASN C  1 17  ? -10.593 16.227  20.097  1.00 8.56   ? 9   ASN C CG  1 
ATOM   3463  O OD1 . ASN C  1 17  ? -9.504  15.888  19.624  1.00 11.32  ? 9   ASN C OD1 1 
ATOM   3464  N ND2 . ASN C  1 17  ? -11.745 15.786  19.619  1.00 10.86  ? 9   ASN C ND2 1 
ATOM   3465  N N   . ILE C  1 18  ? -10.187 18.088  24.167  1.00 9.11   ? 10  ILE C N   1 
ATOM   3466  C CA  . ILE C  1 18  ? -10.366 19.040  25.275  1.00 6.38   ? 10  ILE C CA  1 
ATOM   3467  C C   . ILE C  1 18  ? -9.037  19.438  25.927  1.00 8.75   ? 10  ILE C C   1 
ATOM   3468  O O   . ILE C  1 18  ? -8.809  20.606  26.244  1.00 8.52   ? 10  ILE C O   1 
ATOM   3469  C CB  . ILE C  1 18  ? -11.340 18.485  26.355  1.00 9.74   ? 10  ILE C CB  1 
ATOM   3470  C CG1 . ILE C  1 18  ? -12.772 18.391  25.814  1.00 10.95  ? 10  ILE C CG1 1 
ATOM   3471  C CG2 . ILE C  1 18  ? -11.318 19.325  27.632  1.00 7.49   ? 10  ILE C CG2 1 
ATOM   3472  C CD1 . ILE C  1 18  ? -13.613 17.370  26.550  1.00 7.27   ? 10  ILE C CD1 1 
ATOM   3473  N N   . ARG C  1 19  ? -8.140  18.481  26.116  1.00 8.82   ? 11  ARG C N   1 
ATOM   3474  C CA  . ARG C  1 19  ? -6.862  18.820  26.735  1.00 10.47  ? 11  ARG C CA  1 
ATOM   3475  C C   . ARG C  1 19  ? -5.988  19.648  25.838  1.00 12.38  ? 11  ARG C C   1 
ATOM   3476  O O   . ARG C  1 19  ? -4.985  20.191  26.282  1.00 17.61  ? 11  ARG C O   1 
ATOM   3477  C CB  . ARG C  1 19  ? -6.108  17.579  27.168  1.00 11.45  ? 11  ARG C CB  1 
ATOM   3478  C CG  . ARG C  1 19  ? -6.502  17.139  28.552  1.00 14.25  ? 11  ARG C CG  1 
ATOM   3479  C CD  . ARG C  1 19  ? -6.418  15.657  28.661  1.00 12.75  ? 11  ARG C CD  1 
ATOM   3480  N NE  . ARG C  1 19  ? -6.391  15.240  30.048  1.00 14.60  ? 11  ARG C NE  1 
ATOM   3481  C CZ  . ARG C  1 19  ? -6.217  13.982  30.421  1.00 16.67  ? 11  ARG C CZ  1 
ATOM   3482  N NH1 . ARG C  1 19  ? -6.060  13.042  29.489  1.00 15.58  ? 11  ARG C NH1 1 
ATOM   3483  N NH2 . ARG C  1 19  ? -6.217  13.669  31.712  1.00 18.17  ? 11  ARG C NH2 1 
ATOM   3484  N N   . GLN C  1 20  ? -6.358  19.735  24.569  1.00 12.39  ? 12  GLN C N   1 
ATOM   3485  C CA  . GLN C  1 20  ? -5.626  20.577  23.652  1.00 12.48  ? 12  GLN C CA  1 
ATOM   3486  C C   . GLN C  1 20  ? -6.171  21.990  23.638  1.00 10.94  ? 12  GLN C C   1 
ATOM   3487  O O   . GLN C  1 20  ? -5.407  22.933  23.565  1.00 20.64  ? 12  GLN C O   1 
ATOM   3488  C CB  . GLN C  1 20  ? -5.656  19.989  22.250  1.00 13.38  ? 12  GLN C CB  1 
ATOM   3489  C CG  . GLN C  1 20  ? -4.907  18.691  22.140  1.00 12.93  ? 12  GLN C CG  1 
ATOM   3490  C CD  . GLN C  1 20  ? -3.833  18.768  21.095  1.00 23.27  ? 12  GLN C CD  1 
ATOM   3491  O OE1 . GLN C  1 20  ? -4.111  18.694  19.883  1.00 21.34  ? 12  GLN C OE1 1 
ATOM   3492  N NE2 . GLN C  1 20  ? -2.585  18.939  21.547  1.00 22.10  ? 12  GLN C NE2 1 
ATOM   3493  N N   . THR C  1 21  ? -7.487  22.146  23.690  1.00 10.70  ? 13  THR C N   1 
ATOM   3494  C CA  . THR C  1 21  ? -8.074  23.479  23.606  1.00 12.34  ? 13  THR C CA  1 
ATOM   3495  C C   . THR C  1 21  ? -8.188  24.145  24.970  1.00 11.73  ? 13  THR C C   1 
ATOM   3496  O O   . THR C  1 21  ? -8.297  25.356  25.062  1.00 13.76  ? 13  THR C O   1 
ATOM   3497  C CB  . THR C  1 21  ? -9.479  23.455  22.995  1.00 14.47  ? 13  THR C CB  1 
ATOM   3498  O OG1 . THR C  1 21  ? -9.626  22.313  22.154  1.00 13.75  ? 13  THR C OG1 1 
ATOM   3499  C CG2 . THR C  1 21  ? -9.717  24.707  22.174  1.00 24.55  ? 13  THR C CG2 1 
ATOM   3500  N N   . SER C  1 22  ? -8.167  23.345  26.023  1.00 11.07  ? 14  SER C N   1 
ATOM   3501  C CA  . SER C  1 22  ? -8.435  23.846  27.354  1.00 13.25  ? 14  SER C CA  1 
ATOM   3502  C C   . SER C  1 22  ? -7.330  24.749  27.845  1.00 14.95  ? 14  SER C C   1 
ATOM   3503  O O   . SER C  1 22  ? -6.156  24.366  27.845  1.00 12.62  ? 14  SER C O   1 
ATOM   3504  C CB  . SER C  1 22  ? -8.599  22.686  28.339  1.00 14.38  ? 14  SER C CB  1 
ATOM   3505  O OG  . SER C  1 22  ? -8.746  23.159  29.672  1.00 18.26  ? 14  SER C OG  1 
ATOM   3506  N N   . ARG C  1 23  ? -7.720  25.943  28.281  1.00 14.95  ? 15  ARG C N   1 
ATOM   3507  C CA  . ARG C  1 23  ? -6.815  26.813  29.025  1.00 14.78  ? 15  ARG C CA  1 
ATOM   3508  C C   . ARG C  1 23  ? -7.273  26.895  30.488  1.00 11.45  ? 15  ARG C C   1 
ATOM   3509  O O   . ARG C  1 23  ? -8.099  27.728  30.839  1.00 11.88  ? 15  ARG C O   1 
ATOM   3510  C CB  . ARG C  1 23  ? -6.766  28.209  28.406  1.00 12.67  ? 15  ARG C CB  1 
ATOM   3511  C CG  . ARG C  1 23  ? -6.480  28.238  26.924  1.00 13.35  ? 15  ARG C CG  1 
ATOM   3512  C CD  . ARG C  1 23  ? -5.890  29.590  26.565  1.00 19.61  ? 15  ARG C CD  1 
ATOM   3513  N NE  . ARG C  1 23  ? -5.730  29.807  25.129  1.00 24.74  ? 15  ARG C NE  1 
ATOM   3514  C CZ  . ARG C  1 23  ? -4.572  29.756  24.482  1.00 23.99  ? 15  ARG C CZ  1 
ATOM   3515  N NH1 . ARG C  1 23  ? -3.446  29.487  25.131  1.00 23.25  ? 15  ARG C NH1 1 
ATOM   3516  N NH2 . ARG C  1 23  ? -4.542  29.979  23.177  1.00 32.58  ? 15  ARG C NH2 1 
ATOM   3517  N N   . PRO C  1 24  ? -6.718  26.033  31.346  1.00 10.91  ? 16  PRO C N   1 
ATOM   3518  C CA  . PRO C  1 24  ? -7.124  25.903  32.751  1.00 10.44  ? 16  PRO C CA  1 
ATOM   3519  C C   . PRO C  1 24  ? -6.975  27.191  33.555  1.00 9.55   ? 16  PRO C C   1 
ATOM   3520  O O   . PRO C  1 24  ? -7.571  27.332  34.619  1.00 12.81  ? 16  PRO C O   1 
ATOM   3521  C CB  . PRO C  1 24  ? -6.164  24.842  33.307  1.00 11.93  ? 16  PRO C CB  1 
ATOM   3522  C CG  . PRO C  1 24  ? -5.532  24.176  32.091  1.00 11.43  ? 16  PRO C CG  1 
ATOM   3523  C CD  . PRO C  1 24  ? -5.534  25.216  31.024  1.00 13.28  ? 16  PRO C CD  1 
ATOM   3524  N N   . ASP C  1 25  ? -6.203  28.135  33.061  1.00 8.94   ? 17  ASP C N   1 
ATOM   3525  C CA  . ASP C  1 25  ? -5.930  29.318  33.854  1.00 7.99   ? 17  ASP C CA  1 
ATOM   3526  C C   . ASP C  1 25  ? -6.530  30.592  33.282  1.00 7.30   ? 17  ASP C C   1 
ATOM   3527  O O   . ASP C  1 25  ? -6.367  31.667  33.842  1.00 8.22   ? 17  ASP C O   1 
ATOM   3528  C CB  . ASP C  1 25  ? -4.425  29.453  34.073  1.00 8.14   ? 17  ASP C CB  1 
ATOM   3529  C CG  . ASP C  1 25  ? -3.865  28.320  34.940  1.00 13.54  ? 17  ASP C CG  1 
ATOM   3530  O OD1 . ASP C  1 25  ? -4.645  27.728  35.724  1.00 13.60  ? 17  ASP C OD1 1 
ATOM   3531  O OD2 . ASP C  1 25  ? -2.653  28.015  34.845  1.00 17.07  ? 17  ASP C OD2 1 
ATOM   3532  N N   . VAL C  1 26  ? -7.246  30.467  32.177  1.00 7.27   ? 18  VAL C N   1 
ATOM   3533  C CA  . VAL C  1 26  ? -7.783  31.632  31.513  1.00 7.80   ? 18  VAL C CA  1 
ATOM   3534  C C   . VAL C  1 26  ? -9.283  31.521  31.514  1.00 7.40   ? 18  VAL C C   1 
ATOM   3535  O O   . VAL C  1 26  ? -9.822  30.454  31.224  1.00 9.34   ? 18  VAL C O   1 
ATOM   3536  C CB  . VAL C  1 26  ? -7.254  31.741  30.062  1.00 9.26   ? 18  VAL C CB  1 
ATOM   3537  C CG1 . VAL C  1 26  ? -7.762  33.020  29.404  1.00 9.04   ? 18  VAL C CG1 1 
ATOM   3538  C CG2 . VAL C  1 26  ? -5.741  31.696  30.055  1.00 7.24   ? 18  VAL C CG2 1 
ATOM   3539  N N   . ILE C  1 27  ? -9.964  32.605  31.864  1.00 7.37   ? 19  ILE C N   1 
ATOM   3540  C CA  . ILE C  1 27  ? -11.415 32.561  31.916  1.00 10.40  ? 19  ILE C CA  1 
ATOM   3541  C C   . ILE C  1 27  ? -11.965 32.385  30.512  1.00 13.50  ? 19  ILE C C   1 
ATOM   3542  O O   . ILE C  1 27  ? -11.498 33.037  29.579  1.00 12.39  ? 19  ILE C O   1 
ATOM   3543  C CB  . ILE C  1 27  ? -12.023 33.809  32.584  1.00 13.16  ? 19  ILE C CB  1 
ATOM   3544  C CG1 . ILE C  1 27  ? -11.576 35.083  31.875  1.00 12.67  ? 19  ILE C CG1 1 
ATOM   3545  C CG2 . ILE C  1 27  ? -11.649 33.871  34.062  1.00 9.08   ? 19  ILE C CG2 1 
ATOM   3546  C CD1 . ILE C  1 27  ? -12.051 36.331  32.608  1.00 14.04  ? 19  ILE C CD1 1 
ATOM   3547  N N   . PRO C  1 28  ? -12.949 31.478  30.357  1.00 13.66  ? 20  PRO C N   1 
ATOM   3548  C CA  . PRO C  1 28  ? -13.585 31.107  29.091  1.00 11.99  ? 20  PRO C CA  1 
ATOM   3549  C C   . PRO C  1 28  ? -14.545 32.194  28.675  1.00 13.76  ? 20  PRO C C   1 
ATOM   3550  O O   . PRO C  1 28  ? -15.709 31.953  28.371  1.00 15.05  ? 20  PRO C O   1 
ATOM   3551  C CB  . PRO C  1 28  ? -14.360 29.848  29.458  1.00 9.77   ? 20  PRO C CB  1 
ATOM   3552  C CG  . PRO C  1 28  ? -14.721 30.071  30.858  1.00 10.57  ? 20  PRO C CG  1 
ATOM   3553  C CD  . PRO C  1 28  ? -13.562 30.767  31.488  1.00 9.23   ? 20  PRO C CD  1 
ATOM   3554  N N   . THR C  1 29  ? -14.027 33.406  28.663  1.00 17.14  ? 21  THR C N   1 
ATOM   3555  C CA  . THR C  1 29  ? -14.804 34.588  28.378  1.00 18.85  ? 21  THR C CA  1 
ATOM   3556  C C   . THR C  1 29  ? -15.154 34.577  26.894  1.00 22.84  ? 21  THR C C   1 
ATOM   3557  O O   . THR C  1 29  ? -14.358 34.162  26.054  1.00 29.54  ? 21  THR C O   1 
ATOM   3558  C CB  . THR C  1 29  ? -14.006 35.829  28.814  1.00 21.04  ? 21  THR C CB  1 
ATOM   3559  O OG1 . THR C  1 29  ? -14.883 36.839  29.311  1.00 25.42  ? 21  THR C OG1 1 
ATOM   3560  C CG2 . THR C  1 29  ? -13.159 36.350  27.704  1.00 20.18  ? 21  THR C CG2 1 
ATOM   3561  N N   . GLN C  1 30  ? -16.378 34.966  26.570  1.00 35.03  ? 22  GLN C N   1 
ATOM   3562  C CA  . GLN C  1 30  ? -16.857 34.825  25.202  1.00 38.27  ? 22  GLN C CA  1 
ATOM   3563  C C   . GLN C  1 30  ? -17.473 36.108  24.673  1.00 45.26  ? 22  GLN C C   1 
ATOM   3564  O O   . GLN C  1 30  ? -18.376 36.667  25.294  1.00 42.62  ? 22  GLN C O   1 
ATOM   3565  C CB  . GLN C  1 30  ? -17.877 33.694  25.114  1.00 34.56  ? 22  GLN C CB  1 
ATOM   3566  C CG  . GLN C  1 30  ? -18.518 33.567  23.751  1.00 53.86  ? 22  GLN C CG  1 
ATOM   3567  C CD  . GLN C  1 30  ? -18.850 32.132  23.404  1.00 64.35  ? 22  GLN C CD  1 
ATOM   3568  O OE1 . GLN C  1 30  ? -18.867 31.259  24.283  1.00 64.68  ? 22  GLN C OE1 1 
ATOM   3569  N NE2 . GLN C  1 30  ? -19.103 31.870  22.116  1.00 50.48  ? 22  GLN C NE2 1 
ATOM   3570  N N   . ARG C  1 31  ? -16.978 36.570  23.527  1.00 46.85  ? 23  ARG C N   1 
ATOM   3571  C CA  . ARG C  1 31  ? -17.579 37.709  22.831  1.00 55.12  ? 23  ARG C CA  1 
ATOM   3572  C C   . ARG C  1 31  ? -17.553 38.990  23.672  1.00 49.19  ? 23  ARG C C   1 
ATOM   3573  O O   . ARG C  1 31  ? -18.480 39.797  23.602  1.00 50.05  ? 23  ARG C O   1 
ATOM   3574  C CB  . ARG C  1 31  ? -19.027 37.388  22.398  1.00 48.74  ? 23  ARG C CB  1 
ATOM   3575  C CG  . ARG C  1 31  ? -19.163 36.196  21.449  1.00 61.23  ? 23  ARG C CG  1 
ATOM   3576  C CD  . ARG C  1 31  ? -20.530 36.154  20.757  1.00 71.81  ? 23  ARG C CD  1 
ATOM   3577  N NE  . ARG C  1 31  ? -20.596 35.147  19.692  1.00 79.88  ? 23  ARG C NE  1 
ATOM   3578  C CZ  . ARG C  1 31  ? -20.314 35.382  18.411  1.00 75.97  ? 23  ARG C CZ  1 
ATOM   3579  N NH1 . ARG C  1 31  ? -19.941 36.594  18.023  1.00 75.33  ? 23  ARG C NH1 1 
ATOM   3580  N NH2 . ARG C  1 31  ? -20.405 34.404  17.515  1.00 65.14  ? 23  ARG C NH2 1 
ATOM   3581  N N   . ASP C  1 32  ? -16.494 39.169  24.460  1.00 42.40  ? 24  ASP C N   1 
ATOM   3582  C CA  . ASP C  1 32  ? -16.412 40.286  25.401  1.00 37.76  ? 24  ASP C CA  1 
ATOM   3583  C C   . ASP C  1 32  ? -17.628 40.368  26.341  1.00 51.02  ? 24  ASP C C   1 
ATOM   3584  O O   . ASP C  1 32  ? -18.090 41.458  26.706  1.00 52.27  ? 24  ASP C O   1 
ATOM   3585  C CB  . ASP C  1 32  ? -16.197 41.613  24.676  1.00 39.47  ? 24  ASP C CB  1 
ATOM   3586  C CG  . ASP C  1 32  ? -14.778 42.139  24.835  1.00 52.49  ? 24  ASP C CG  1 
ATOM   3587  O OD1 . ASP C  1 32  ? -14.528 42.901  25.802  1.00 51.07  ? 24  ASP C OD1 1 
ATOM   3588  O OD2 . ASP C  1 32  ? -13.911 41.788  23.998  1.00 51.31  ? 24  ASP C OD2 1 
ATOM   3589  N N   . ARG C  1 33  ? -18.144 39.204  26.726  1.00 43.45  ? 25  ARG C N   1 
ATOM   3590  C CA  . ARG C  1 33  ? -19.185 39.122  27.734  1.00 36.28  ? 25  ARG C CA  1 
ATOM   3591  C C   . ARG C  1 33  ? -18.632 38.308  28.899  1.00 36.49  ? 25  ARG C C   1 
ATOM   3592  O O   . ARG C  1 33  ? -17.889 37.349  28.683  1.00 34.20  ? 25  ARG C O   1 
ATOM   3593  C CB  . ARG C  1 33  ? -20.424 38.460  27.142  1.00 37.70  ? 25  ARG C CB  1 
ATOM   3594  C CG  . ARG C  1 33  ? -20.930 39.156  25.885  1.00 45.24  ? 25  ARG C CG  1 
ATOM   3595  C CD  . ARG C  1 33  ? -21.616 38.173  24.946  1.00 56.16  ? 25  ARG C CD  1 
ATOM   3596  N NE  . ARG C  1 33  ? -22.732 38.777  24.216  1.00 68.22  ? 25  ARG C NE  1 
ATOM   3597  C CZ  . ARG C  1 33  ? -23.426 38.158  23.264  1.00 64.87  ? 25  ARG C CZ  1 
ATOM   3598  N NH1 . ARG C  1 33  ? -23.118 36.917  22.910  1.00 57.02  ? 25  ARG C NH1 1 
ATOM   3599  N NH2 . ARG C  1 33  ? -24.427 38.782  22.659  1.00 74.78  ? 25  ARG C NH2 1 
ATOM   3600  N N   . PRO C  1 34  ? -18.962 38.708  30.136  1.00 31.20  ? 26  PRO C N   1 
ATOM   3601  C CA  . PRO C  1 34  ? -18.563 37.991  31.355  1.00 25.83  ? 26  PRO C CA  1 
ATOM   3602  C C   . PRO C  1 34  ? -18.950 36.522  31.281  1.00 24.41  ? 26  PRO C C   1 
ATOM   3603  O O   . PRO C  1 34  ? -19.994 36.203  30.712  1.00 29.72  ? 26  PRO C O   1 
ATOM   3604  C CB  . PRO C  1 34  ? -19.408 38.663  32.441  1.00 25.58  ? 26  PRO C CB  1 
ATOM   3605  C CG  . PRO C  1 34  ? -19.635 40.020  31.932  1.00 32.82  ? 26  PRO C CG  1 
ATOM   3606  C CD  . PRO C  1 34  ? -19.743 39.916  30.438  1.00 26.18  ? 26  PRO C CD  1 
ATOM   3607  N N   . VAL C  1 35  ? -18.126 35.641  31.836  1.00 20.81  ? 27  VAL C N   1 
ATOM   3608  C CA  . VAL C  1 35  ? -18.492 34.235  31.938  1.00 17.95  ? 27  VAL C CA  1 
ATOM   3609  C C   . VAL C  1 35  ? -19.670 34.124  32.882  1.00 18.69  ? 27  VAL C C   1 
ATOM   3610  O O   . VAL C  1 35  ? -19.608 34.597  34.013  1.00 21.06  ? 27  VAL C O   1 
ATOM   3611  C CB  . VAL C  1 35  ? -17.350 33.380  32.514  1.00 16.54  ? 27  VAL C CB  1 
ATOM   3612  C CG1 . VAL C  1 35  ? -17.740 31.917  32.502  1.00 17.26  ? 27  VAL C CG1 1 
ATOM   3613  C CG2 . VAL C  1 35  ? -16.090 33.582  31.721  1.00 18.01  ? 27  VAL C CG2 1 
ATOM   3614  N N   . ALA C  1 36  ? -20.743 33.496  32.426  1.00 20.77  ? 28  ALA C N   1 
ATOM   3615  C CA  . ALA C  1 36  ? -21.929 33.333  33.258  1.00 13.93  ? 28  ALA C CA  1 
ATOM   3616  C C   . ALA C  1 36  ? -21.868 32.008  34.012  1.00 15.20  ? 28  ALA C C   1 
ATOM   3617  O O   . ALA C  1 36  ? -22.078 30.942  33.426  1.00 16.17  ? 28  ALA C O   1 
ATOM   3618  C CB  . ALA C  1 36  ? -23.176 33.394  32.398  1.00 7.32   ? 28  ALA C CB  1 
ATOM   3619  N N   . VAL C  1 37  ? -21.579 32.072  35.307  1.00 15.70  ? 29  VAL C N   1 
ATOM   3620  C CA  . VAL C  1 37  ? -21.515 30.869  36.143  1.00 15.55  ? 29  VAL C CA  1 
ATOM   3621  C C   . VAL C  1 37  ? -22.767 30.695  36.997  1.00 19.45  ? 29  VAL C C   1 
ATOM   3622  O O   . VAL C  1 37  ? -23.093 31.547  37.819  1.00 20.98  ? 29  VAL C O   1 
ATOM   3623  C CB  . VAL C  1 37  ? -20.329 30.910  37.114  1.00 14.07  ? 29  VAL C CB  1 
ATOM   3624  C CG1 . VAL C  1 37  ? -20.326 29.663  37.968  1.00 14.86  ? 29  VAL C CG1 1 
ATOM   3625  C CG2 . VAL C  1 37  ? -19.011 31.057  36.370  1.00 11.78  ? 29  VAL C CG2 1 
ATOM   3626  N N   . SER C  1 38  ? -23.456 29.578  36.811  1.00 19.11  ? 30  SER C N   1 
ATOM   3627  C CA  . SER C  1 38  ? -24.616 29.251  37.622  1.00 19.27  ? 30  SER C CA  1 
ATOM   3628  C C   . SER C  1 38  ? -24.208 28.461  38.858  1.00 23.81  ? 30  SER C C   1 
ATOM   3629  O O   . SER C  1 38  ? -23.586 27.410  38.746  1.00 24.19  ? 30  SER C O   1 
ATOM   3630  C CB  . SER C  1 38  ? -25.624 28.443  36.811  1.00 19.39  ? 30  SER C CB  1 
ATOM   3631  O OG  . SER C  1 38  ? -26.182 29.219  35.770  1.00 26.56  ? 30  SER C OG  1 
ATOM   3632  N N   . VAL C  1 39  ? -24.559 28.966  40.036  1.00 22.41  ? 31  VAL C N   1 
ATOM   3633  C CA  . VAL C  1 39  ? -24.291 28.251  41.271  1.00 22.07  ? 31  VAL C CA  1 
ATOM   3634  C C   . VAL C  1 39  ? -25.579 27.925  41.995  1.00 28.04  ? 31  VAL C C   1 
ATOM   3635  O O   . VAL C  1 39  ? -26.417 28.801  42.219  1.00 32.71  ? 31  VAL C O   1 
ATOM   3636  C CB  . VAL C  1 39  ? -23.437 29.080  42.228  1.00 23.98  ? 31  VAL C CB  1 
ATOM   3637  C CG1 . VAL C  1 39  ? -22.781 28.167  43.248  1.00 16.31  ? 31  VAL C CG1 1 
ATOM   3638  C CG2 . VAL C  1 39  ? -22.389 29.860  41.447  1.00 28.42  ? 31  VAL C CG2 1 
ATOM   3639  N N   . SER C  1 40  ? -25.725 26.665  42.383  1.00 24.26  ? 32  SER C N   1 
ATOM   3640  C CA  . SER C  1 40  ? -26.861 26.260  43.184  1.00 24.64  ? 32  SER C CA  1 
ATOM   3641  C C   . SER C  1 40  ? -26.428 25.290  44.281  1.00 26.98  ? 32  SER C C   1 
ATOM   3642  O O   . SER C  1 40  ? -25.881 24.229  43.984  1.00 29.64  ? 32  SER C O   1 
ATOM   3643  C CB  . SER C  1 40  ? -27.918 25.617  42.295  1.00 28.01  ? 32  SER C CB  1 
ATOM   3644  O OG  . SER C  1 40  ? -29.121 25.424  43.014  1.00 46.03  ? 32  SER C OG  1 
ATOM   3645  N N   . LEU C  1 41  ? -26.664 25.653  45.542  1.00 25.68  ? 33  LEU C N   1 
ATOM   3646  C CA  . LEU C  1 41  ? -26.389 24.753  46.672  1.00 26.09  ? 33  LEU C CA  1 
ATOM   3647  C C   . LEU C  1 41  ? -27.569 23.855  47.032  1.00 20.45  ? 33  LEU C C   1 
ATOM   3648  O O   . LEU C  1 41  ? -28.647 24.343  47.335  1.00 30.68  ? 33  LEU C O   1 
ATOM   3649  C CB  . LEU C  1 41  ? -25.995 25.532  47.932  1.00 20.83  ? 33  LEU C CB  1 
ATOM   3650  C CG  . LEU C  1 41  ? -24.881 26.565  47.813  1.00 25.97  ? 33  LEU C CG  1 
ATOM   3651  C CD1 . LEU C  1 41  ? -24.394 27.041  49.198  1.00 12.21  ? 33  LEU C CD1 1 
ATOM   3652  C CD2 . LEU C  1 41  ? -23.741 26.026  46.943  1.00 20.62  ? 33  LEU C CD2 1 
ATOM   3653  N N   . LYS C  1 42  ? -27.351 22.543  47.014  1.00 22.76  ? 34  LYS C N   1 
ATOM   3654  C CA  . LYS C  1 42  ? -28.328 21.578  47.523  1.00 23.22  ? 34  LYS C CA  1 
ATOM   3655  C C   . LYS C  1 42  ? -27.840 20.977  48.847  1.00 20.66  ? 34  LYS C C   1 
ATOM   3656  O O   . LYS C  1 42  ? -26.885 20.186  48.869  1.00 16.64  ? 34  LYS C O   1 
ATOM   3657  C CB  . LYS C  1 42  ? -28.576 20.464  46.504  1.00 21.57  ? 34  LYS C CB  1 
ATOM   3658  C CG  . LYS C  1 42  ? -28.854 20.955  45.088  1.00 29.16  ? 34  LYS C CG  1 
ATOM   3659  C CD  . LYS C  1 42  ? -30.093 21.852  44.993  1.00 33.76  ? 34  LYS C CD  1 
ATOM   3660  C CE  . LYS C  1 42  ? -30.367 22.259  43.537  1.00 39.13  ? 34  LYS C CE  1 
ATOM   3661  N NZ  . LYS C  1 42  ? -31.573 23.125  43.387  1.00 40.18  ? 34  LYS C NZ  1 
ATOM   3662  N N   . PHE C  1 43  ? -28.495 21.352  49.946  1.00 17.70  ? 35  PHE C N   1 
ATOM   3663  C CA  . PHE C  1 43  ? -28.052 20.939  51.275  1.00 14.42  ? 35  PHE C CA  1 
ATOM   3664  C C   . PHE C  1 43  ? -28.341 19.475  51.575  1.00 12.69  ? 35  PHE C C   1 
ATOM   3665  O O   . PHE C  1 43  ? -29.406 18.966  51.281  1.00 14.75  ? 35  PHE C O   1 
ATOM   3666  C CB  . PHE C  1 43  ? -28.618 21.861  52.358  1.00 15.99  ? 35  PHE C CB  1 
ATOM   3667  C CG  . PHE C  1 43  ? -28.082 23.250  52.291  1.00 17.34  ? 35  PHE C CG  1 
ATOM   3668  C CD1 . PHE C  1 43  ? -28.728 24.221  51.534  1.00 18.90  ? 35  PHE C CD1 1 
ATOM   3669  C CD2 . PHE C  1 43  ? -26.904 23.584  52.948  1.00 16.64  ? 35  PHE C CD2 1 
ATOM   3670  C CE1 . PHE C  1 43  ? -28.217 25.514  51.448  1.00 17.77  ? 35  PHE C CE1 1 
ATOM   3671  C CE2 . PHE C  1 43  ? -26.388 24.882  52.870  1.00 18.12  ? 35  PHE C CE2 1 
ATOM   3672  C CZ  . PHE C  1 43  ? -27.043 25.847  52.117  1.00 12.37  ? 35  PHE C CZ  1 
ATOM   3673  N N   . ILE C  1 44  ? -27.367 18.807  52.172  1.00 13.86  ? 36  ILE C N   1 
ATOM   3674  C CA  . ILE C  1 44  ? -27.421 17.371  52.376  1.00 15.63  ? 36  ILE C CA  1 
ATOM   3675  C C   . ILE C  1 44  ? -27.547 17.076  53.871  1.00 17.30  ? 36  ILE C C   1 
ATOM   3676  O O   . ILE C  1 44  ? -28.277 16.176  54.293  1.00 17.82  ? 36  ILE C O   1 
ATOM   3677  C CB  . ILE C  1 44  ? -26.131 16.698  51.830  1.00 12.13  ? 36  ILE C CB  1 
ATOM   3678  C CG1 . ILE C  1 44  ? -25.805 17.191  50.405  1.00 13.19  ? 36  ILE C CG1 1 
ATOM   3679  C CG2 . ILE C  1 44  ? -26.233 15.193  51.909  1.00 9.71   ? 36  ILE C CG2 1 
ATOM   3680  C CD1 . ILE C  1 44  ? -26.847 16.870  49.335  1.00 12.05  ? 36  ILE C CD1 1 
ATOM   3681  N N   . ASN C  1 45  ? -26.828 17.845  54.673  1.00 11.83  ? 37  ASN C N   1 
ATOM   3682  C CA  . ASN C  1 45  ? -26.796 17.581  56.083  1.00 11.16  ? 37  ASN C CA  1 
ATOM   3683  C C   . ASN C  1 45  ? -26.353 18.825  56.832  1.00 14.67  ? 37  ASN C C   1 
ATOM   3684  O O   . ASN C  1 45  ? -25.571 19.631  56.316  1.00 9.77   ? 37  ASN C O   1 
ATOM   3685  C CB  . ASN C  1 45  ? -25.886 16.390  56.386  1.00 13.07  ? 37  ASN C CB  1 
ATOM   3686  C CG  . ASN C  1 45  ? -26.451 15.478  57.489  1.00 21.05  ? 37  ASN C CG  1 
ATOM   3687  O OD1 . ASN C  1 45  ? -27.028 15.943  58.482  1.00 14.72  ? 37  ASN C OD1 1 
ATOM   3688  N ND2 . ASN C  1 45  ? -26.292 14.171  57.306  1.00 20.13  ? 37  ASN C ND2 1 
ATOM   3689  N N   . ILE C  1 46  ? -26.926 19.002  58.022  1.00 13.88  ? 38  ILE C N   1 
ATOM   3690  C CA  . ILE C  1 46  ? -26.489 20.012  58.959  1.00 12.56  ? 38  ILE C CA  1 
ATOM   3691  C C   . ILE C  1 46  ? -26.029 19.204  60.147  1.00 17.80  ? 38  ILE C C   1 
ATOM   3692  O O   . ILE C  1 46  ? -26.798 18.409  60.673  1.00 23.57  ? 38  ILE C O   1 
ATOM   3693  C CB  . ILE C  1 46  ? -27.645 20.902  59.375  1.00 12.41  ? 38  ILE C CB  1 
ATOM   3694  C CG1 . ILE C  1 46  ? -28.100 21.768  58.203  1.00 12.35  ? 38  ILE C CG1 1 
ATOM   3695  C CG2 . ILE C  1 46  ? -27.237 21.763  60.540  1.00 13.80  ? 38  ILE C CG2 1 
ATOM   3696  C CD1 . ILE C  1 46  ? -29.503 22.324  58.345  1.00 12.21  ? 38  ILE C CD1 1 
ATOM   3697  N N   . LEU C  1 47  ? -24.784 19.383  60.571  1.00 17.75  ? 39  LEU C N   1 
ATOM   3698  C CA  . LEU C  1 47  ? -24.176 18.452  61.513  1.00 17.82  ? 39  LEU C CA  1 
ATOM   3699  C C   . LEU C  1 47  ? -23.986 18.999  62.927  1.00 22.34  ? 39  LEU C C   1 
ATOM   3700  O O   . LEU C  1 47  ? -24.383 18.371  63.905  1.00 28.59  ? 39  LEU C O   1 
ATOM   3701  C CB  . LEU C  1 47  ? -22.828 17.986  60.969  1.00 15.35  ? 39  LEU C CB  1 
ATOM   3702  C CG  . LEU C  1 47  ? -22.885 17.250  59.633  1.00 20.77  ? 39  LEU C CG  1 
ATOM   3703  C CD1 . LEU C  1 47  ? -21.499 17.050  59.096  1.00 16.06  ? 39  LEU C CD1 1 
ATOM   3704  C CD2 . LEU C  1 47  ? -23.602 15.904  59.756  1.00 21.25  ? 39  LEU C CD2 1 
ATOM   3705  N N   . GLU C  1 48  ? -23.328 20.145  63.026  1.00 25.59  ? 40  GLU C N   1 
ATOM   3706  C CA  . GLU C  1 48  ? -22.980 20.732  64.305  1.00 23.10  ? 40  GLU C CA  1 
ATOM   3707  C C   . GLU C  1 48  ? -23.389 22.186  64.297  1.00 26.98  ? 40  GLU C C   1 
ATOM   3708  O O   . GLU C  1 48  ? -22.791 23.006  63.608  1.00 32.77  ? 40  GLU C O   1 
ATOM   3709  C CB  . GLU C  1 48  ? -21.475 20.656  64.537  1.00 22.72  ? 40  GLU C CB  1 
ATOM   3710  C CG  . GLU C  1 48  ? -20.954 19.264  64.756  1.00 34.33  ? 40  GLU C CG  1 
ATOM   3711  C CD  . GLU C  1 48  ? -19.453 19.152  64.542  1.00 44.86  ? 40  GLU C CD  1 
ATOM   3712  O OE1 . GLU C  1 48  ? -18.799 20.170  64.190  1.00 42.21  ? 40  GLU C OE1 1 
ATOM   3713  O OE2 . GLU C  1 48  ? -18.931 18.029  64.724  1.00 47.40  ? 40  GLU C OE2 1 
ATOM   3714  N N   . VAL C  1 49  ? -24.412 22.510  65.059  1.00 18.57  ? 41  VAL C N   1 
ATOM   3715  C CA  . VAL C  1 49  ? -24.828 23.879  65.184  1.00 17.30  ? 41  VAL C CA  1 
ATOM   3716  C C   . VAL C  1 49  ? -24.442 24.327  66.589  1.00 21.45  ? 41  VAL C C   1 
ATOM   3717  O O   . VAL C  1 49  ? -24.551 23.565  67.542  1.00 19.01  ? 41  VAL C O   1 
ATOM   3718  C CB  . VAL C  1 49  ? -26.336 23.965  64.980  1.00 22.78  ? 41  VAL C CB  1 
ATOM   3719  C CG1 . VAL C  1 49  ? -26.898 25.224  65.594  1.00 28.58  ? 41  VAL C CG1 1 
ATOM   3720  C CG2 . VAL C  1 49  ? -26.687 23.843  63.505  1.00 16.14  ? 41  VAL C CG2 1 
ATOM   3721  N N   . ASN C  1 50  ? -23.949 25.551  66.711  1.00 24.58  ? 42  ASN C N   1 
ATOM   3722  C CA  . ASN C  1 50  ? -23.615 26.111  68.014  1.00 21.52  ? 42  ASN C CA  1 
ATOM   3723  C C   . ASN C  1 50  ? -24.329 27.447  68.199  1.00 22.10  ? 42  ASN C C   1 
ATOM   3724  O O   . ASN C  1 50  ? -24.136 28.372  67.409  1.00 19.52  ? 42  ASN C O   1 
ATOM   3725  C CB  . ASN C  1 50  ? -22.103 26.268  68.156  1.00 20.05  ? 42  ASN C CB  1 
ATOM   3726  C CG  . ASN C  1 50  ? -21.680 26.588  69.569  1.00 20.68  ? 42  ASN C CG  1 
ATOM   3727  O OD1 . ASN C  1 50  ? -22.306 27.405  70.240  1.00 25.05  ? 42  ASN C OD1 1 
ATOM   3728  N ND2 . ASN C  1 50  ? -20.608 25.951  70.032  1.00 15.15  ? 42  ASN C ND2 1 
ATOM   3729  N N   . GLU C  1 51  ? -25.160 27.543  69.240  1.00 26.17  ? 43  GLU C N   1 
ATOM   3730  C CA  . GLU C  1 51  ? -26.028 28.707  69.412  1.00 19.02  ? 43  GLU C CA  1 
ATOM   3731  C C   . GLU C  1 51  ? -25.256 29.840  70.086  1.00 19.82  ? 43  GLU C C   1 
ATOM   3732  O O   . GLU C  1 51  ? -25.572 31.021  69.922  1.00 15.92  ? 43  GLU C O   1 
ATOM   3733  C CB  . GLU C  1 51  ? -27.284 28.325  70.189  1.00 23.64  ? 43  GLU C CB  1 
ATOM   3734  C CG  . GLU C  1 51  ? -28.576 28.919  69.637  1.00 32.96  ? 43  GLU C CG  1 
ATOM   3735  C CD  . GLU C  1 51  ? -29.774 28.758  70.586  1.00 41.69  ? 43  GLU C CD  1 
ATOM   3736  O OE1 . GLU C  1 51  ? -29.638 28.096  71.649  1.00 40.05  ? 43  GLU C OE1 1 
ATOM   3737  O OE2 . GLU C  1 51  ? -30.856 29.305  70.259  1.00 41.85  ? 43  GLU C OE2 1 
ATOM   3738  N N   . ILE C  1 52  ? -24.210 29.457  70.808  1.00 18.58  ? 44  ILE C N   1 
ATOM   3739  C CA  . ILE C  1 52  ? -23.320 30.401  71.469  1.00 21.65  ? 44  ILE C CA  1 
ATOM   3740  C C   . ILE C  1 52  ? -22.330 31.090  70.514  1.00 24.84  ? 44  ILE C C   1 
ATOM   3741  O O   . ILE C  1 52  ? -22.289 32.324  70.431  1.00 25.31  ? 44  ILE C O   1 
ATOM   3742  C CB  . ILE C  1 52  ? -22.522 29.702  72.594  1.00 24.26  ? 44  ILE C CB  1 
ATOM   3743  C CG1 . ILE C  1 52  ? -23.475 29.190  73.670  1.00 20.74  ? 44  ILE C CG1 1 
ATOM   3744  C CG2 . ILE C  1 52  ? -21.502 30.645  73.193  1.00 24.61  ? 44  ILE C CG2 1 
ATOM   3745  C CD1 . ILE C  1 52  ? -24.580 30.180  74.012  1.00 21.27  ? 44  ILE C CD1 1 
ATOM   3746  N N   . THR C  1 53  ? -21.526 30.297  69.807  1.00 23.60  ? 45  THR C N   1 
ATOM   3747  C CA  . THR C  1 53  ? -20.533 30.848  68.878  1.00 22.15  ? 45  THR C CA  1 
ATOM   3748  C C   . THR C  1 53  ? -21.075 31.225  67.494  1.00 18.80  ? 45  THR C C   1 
ATOM   3749  O O   . THR C  1 53  ? -20.361 31.825  66.712  1.00 22.68  ? 45  THR C O   1 
ATOM   3750  C CB  . THR C  1 53  ? -19.317 29.906  68.698  1.00 23.27  ? 45  THR C CB  1 
ATOM   3751  O OG1 . THR C  1 53  ? -19.713 28.725  67.985  1.00 22.33  ? 45  THR C OG1 1 
ATOM   3752  C CG2 . THR C  1 53  ? -18.727 29.521  70.054  1.00 20.95  ? 45  THR C CG2 1 
ATOM   3753  N N   . ASN C  1 54  ? -22.327 30.885  67.202  1.00 21.31  ? 46  ASN C N   1 
ATOM   3754  C CA  . ASN C  1 54  ? -22.927 31.177  65.898  1.00 18.97  ? 46  ASN C CA  1 
ATOM   3755  C C   . ASN C  1 54  ? -22.188 30.509  64.742  1.00 21.67  ? 46  ASN C C   1 
ATOM   3756  O O   . ASN C  1 54  ? -21.929 31.138  63.720  1.00 23.52  ? 46  ASN C O   1 
ATOM   3757  C CB  . ASN C  1 54  ? -22.993 32.682  65.645  1.00 16.42  ? 46  ASN C CB  1 
ATOM   3758  C CG  . ASN C  1 54  ? -24.287 33.310  66.121  1.00 20.11  ? 46  ASN C CG  1 
ATOM   3759  O OD1 . ASN C  1 54  ? -25.372 32.724  66.019  1.00 17.86  ? 46  ASN C OD1 1 
ATOM   3760  N ND2 . ASN C  1 54  ? -24.180 34.529  66.626  1.00 19.15  ? 46  ASN C ND2 1 
ATOM   3761  N N   . GLU C  1 55  ? -21.836 29.241  64.903  1.00 18.91  ? 47  GLU C N   1 
ATOM   3762  C CA  . GLU C  1 55  ? -21.188 28.509  63.828  1.00 20.47  ? 47  GLU C CA  1 
ATOM   3763  C C   . GLU C  1 55  ? -22.070 27.342  63.415  1.00 22.29  ? 47  GLU C C   1 
ATOM   3764  O O   . GLU C  1 55  ? -22.953 26.940  64.170  1.00 27.09  ? 47  GLU C O   1 
ATOM   3765  C CB  . GLU C  1 55  ? -19.814 28.031  64.264  1.00 16.67  ? 47  GLU C CB  1 
ATOM   3766  C CG  . GLU C  1 55  ? -18.924 29.163  64.729  1.00 21.82  ? 47  GLU C CG  1 
ATOM   3767  C CD  . GLU C  1 55  ? -17.628 28.662  65.326  1.00 30.37  ? 47  GLU C CD  1 
ATOM   3768  O OE1 . GLU C  1 55  ? -17.365 27.444  65.207  1.00 35.06  ? 47  GLU C OE1 1 
ATOM   3769  O OE2 . GLU C  1 55  ? -16.880 29.478  65.915  1.00 32.59  ? 47  GLU C OE2 1 
ATOM   3770  N N   . VAL C  1 56  ? -21.873 26.840  62.202  1.00 15.86  ? 48  VAL C N   1 
ATOM   3771  C CA  . VAL C  1 56  ? -22.576 25.654  61.732  1.00 14.35  ? 48  VAL C CA  1 
ATOM   3772  C C   . VAL C  1 56  ? -21.602 24.791  60.932  1.00 19.90  ? 48  VAL C C   1 
ATOM   3773  O O   . VAL C  1 56  ? -20.520 25.227  60.573  1.00 17.04  ? 48  VAL C O   1 
ATOM   3774  C CB  . VAL C  1 56  ? -23.760 25.999  60.829  1.00 14.77  ? 48  VAL C CB  1 
ATOM   3775  C CG1 . VAL C  1 56  ? -24.805 26.787  61.566  1.00 16.93  ? 48  VAL C CG1 1 
ATOM   3776  C CG2 . VAL C  1 56  ? -23.282 26.778  59.622  1.00 25.07  ? 48  VAL C CG2 1 
ATOM   3777  N N   . ASP C  1 57  ? -22.000 23.564  60.647  1.00 23.21  ? 49  ASP C N   1 
ATOM   3778  C CA  . ASP C  1 57  ? -21.140 22.604  59.976  1.00 18.94  ? 49  ASP C CA  1 
ATOM   3779  C C   . ASP C  1 57  ? -22.036 21.856  58.996  1.00 19.81  ? 49  ASP C C   1 
ATOM   3780  O O   . ASP C  1 57  ? -22.761 20.924  59.363  1.00 19.76  ? 49  ASP C O   1 
ATOM   3781  C CB  . ASP C  1 57  ? -20.536 21.659  61.017  1.00 28.17  ? 49  ASP C CB  1 
ATOM   3782  C CG  . ASP C  1 57  ? -19.303 20.929  60.515  1.00 28.20  ? 49  ASP C CG  1 
ATOM   3783  O OD1 . ASP C  1 57  ? -18.566 21.502  59.699  1.00 36.13  ? 49  ASP C OD1 1 
ATOM   3784  O OD2 . ASP C  1 57  ? -19.054 19.784  60.954  1.00 33.58  ? 49  ASP C OD2 1 
ATOM   3785  N N   . VAL C  1 58  ? -22.019 22.299  57.749  1.00 20.16  ? 50  VAL C N   1 
ATOM   3786  C CA  . VAL C  1 58  ? -22.986 21.824  56.775  1.00 16.19  ? 50  VAL C CA  1 
ATOM   3787  C C   . VAL C  1 58  ? -22.322 20.930  55.742  1.00 16.75  ? 50  VAL C C   1 
ATOM   3788  O O   . VAL C  1 58  ? -21.096 20.907  55.615  1.00 15.64  ? 50  VAL C O   1 
ATOM   3789  C CB  . VAL C  1 58  ? -23.685 22.999  56.059  1.00 14.36  ? 50  VAL C CB  1 
ATOM   3790  C CG1 . VAL C  1 58  ? -24.319 23.950  57.081  1.00 15.08  ? 50  VAL C CG1 1 
ATOM   3791  C CG2 . VAL C  1 58  ? -22.695 23.746  55.213  1.00 13.77  ? 50  VAL C CG2 1 
ATOM   3792  N N   . VAL C  1 59  ? -23.146 20.167  55.033  1.00 13.09  ? 51  VAL C N   1 
ATOM   3793  C CA  . VAL C  1 59  ? -22.703 19.401  53.897  1.00 11.11  ? 51  VAL C CA  1 
ATOM   3794  C C   . VAL C  1 59  ? -23.662 19.729  52.769  1.00 13.15  ? 51  VAL C C   1 
ATOM   3795  O O   . VAL C  1 59  ? -24.873 19.661  52.949  1.00 13.77  ? 51  VAL C O   1 
ATOM   3796  C CB  . VAL C  1 59  ? -22.689 17.882  54.172  1.00 11.06  ? 51  VAL C CB  1 
ATOM   3797  C CG1 . VAL C  1 59  ? -22.456 17.131  52.886  1.00 11.92  ? 51  VAL C CG1 1 
ATOM   3798  C CG2 . VAL C  1 59  ? -21.589 17.521  55.155  1.00 11.76  ? 51  VAL C CG2 1 
ATOM   3799  N N   . PHE C  1 60  ? -23.122 20.101  51.613  1.00 12.47  ? 52  PHE C N   1 
ATOM   3800  C CA  . PHE C  1 60  ? -23.946 20.480  50.469  1.00 13.06  ? 52  PHE C CA  1 
ATOM   3801  C C   . PHE C  1 60  ? -23.294 20.053  49.147  1.00 14.86  ? 52  PHE C C   1 
ATOM   3802  O O   . PHE C  1 60  ? -22.068 19.973  49.032  1.00 10.83  ? 52  PHE C O   1 
ATOM   3803  C CB  . PHE C  1 60  ? -24.199 21.997  50.467  1.00 11.97  ? 52  PHE C CB  1 
ATOM   3804  C CG  . PHE C  1 60  ? -22.948 22.814  50.554  1.00 9.77   ? 52  PHE C CG  1 
ATOM   3805  C CD1 . PHE C  1 60  ? -22.352 23.315  49.410  1.00 14.73  ? 52  PHE C CD1 1 
ATOM   3806  C CD2 . PHE C  1 60  ? -22.350 23.056  51.769  1.00 11.71  ? 52  PHE C CD2 1 
ATOM   3807  C CE1 . PHE C  1 60  ? -21.187 24.058  49.473  1.00 12.41  ? 52  PHE C CE1 1 
ATOM   3808  C CE2 . PHE C  1 60  ? -21.187 23.792  51.852  1.00 16.32  ? 52  PHE C CE2 1 
ATOM   3809  C CZ  . PHE C  1 60  ? -20.596 24.298  50.692  1.00 13.88  ? 52  PHE C CZ  1 
ATOM   3810  N N   . TRP C  1 61  ? -24.133 19.777  48.160  1.00 13.05  ? 53  TRP C N   1 
ATOM   3811  C CA  . TRP C  1 61  ? -23.675 19.561  46.810  1.00 12.99  ? 53  TRP C CA  1 
ATOM   3812  C C   . TRP C  1 61  ? -23.670 20.900  46.106  1.00 16.26  ? 53  TRP C C   1 
ATOM   3813  O O   . TRP C  1 61  ? -24.719 21.529  45.959  1.00 16.82  ? 53  TRP C O   1 
ATOM   3814  C CB  . TRP C  1 61  ? -24.576 18.560  46.092  1.00 12.63  ? 53  TRP C CB  1 
ATOM   3815  C CG  . TRP C  1 61  ? -24.456 17.195  46.707  1.00 17.47  ? 53  TRP C CG  1 
ATOM   3816  C CD1 . TRP C  1 61  ? -23.626 16.832  47.743  1.00 18.93  ? 53  TRP C CD1 1 
ATOM   3817  C CD2 . TRP C  1 61  ? -25.173 16.010  46.338  1.00 19.09  ? 53  TRP C CD2 1 
ATOM   3818  N NE1 . TRP C  1 61  ? -23.795 15.496  48.045  1.00 24.47  ? 53  TRP C NE1 1 
ATOM   3819  C CE2 . TRP C  1 61  ? -24.735 14.969  47.196  1.00 24.53  ? 53  TRP C CE2 1 
ATOM   3820  C CE3 . TRP C  1 61  ? -26.153 15.729  45.380  1.00 20.68  ? 53  TRP C CE3 1 
ATOM   3821  C CZ2 . TRP C  1 61  ? -25.240 13.674  47.116  1.00 24.96  ? 53  TRP C CZ2 1 
ATOM   3822  C CZ3 . TRP C  1 61  ? -26.649 14.449  45.304  1.00 24.52  ? 53  TRP C CZ3 1 
ATOM   3823  C CH2 . TRP C  1 61  ? -26.192 13.434  46.165  1.00 28.85  ? 53  TRP C CH2 1 
ATOM   3824  N N   . GLN C  1 62  ? -22.481 21.335  45.688  1.00 13.86  ? 54  GLN C N   1 
ATOM   3825  C CA  . GLN C  1 62  ? -22.321 22.618  45.008  1.00 14.69  ? 54  GLN C CA  1 
ATOM   3826  C C   . GLN C  1 62  ? -22.500 22.466  43.508  1.00 11.62  ? 54  GLN C C   1 
ATOM   3827  O O   . GLN C  1 62  ? -21.549 22.226  42.793  1.00 12.78  ? 54  GLN C O   1 
ATOM   3828  C CB  . GLN C  1 62  ? -20.941 23.219  45.303  1.00 13.58  ? 54  GLN C CB  1 
ATOM   3829  C CG  . GLN C  1 62  ? -20.771 24.647  44.801  1.00 13.75  ? 54  GLN C CG  1 
ATOM   3830  C CD  . GLN C  1 62  ? -19.400 25.212  45.111  1.00 23.30  ? 54  GLN C CD  1 
ATOM   3831  O OE1 . GLN C  1 62  ? -19.061 25.458  46.280  1.00 28.76  ? 54  GLN C OE1 1 
ATOM   3832  N NE2 . GLN C  1 62  ? -18.594 25.418  44.067  1.00 16.72  ? 54  GLN C NE2 1 
ATOM   3833  N N   . GLN C  1 63  ? -23.722 22.612  43.031  1.00 15.66  ? 55  GLN C N   1 
ATOM   3834  C CA  . GLN C  1 63  ? -23.983 22.472  41.608  1.00 18.13  ? 55  GLN C CA  1 
ATOM   3835  C C   . GLN C  1 63  ? -23.531 23.705  40.839  1.00 16.39  ? 55  GLN C C   1 
ATOM   3836  O O   . GLN C  1 63  ? -24.154 24.757  40.916  1.00 21.79  ? 55  GLN C O   1 
ATOM   3837  C CB  . GLN C  1 63  ? -25.461 22.206  41.370  1.00 20.62  ? 55  GLN C CB  1 
ATOM   3838  C CG  . GLN C  1 63  ? -25.752 20.858  40.765  1.00 21.62  ? 55  GLN C CG  1 
ATOM   3839  C CD  . GLN C  1 63  ? -27.203 20.731  40.363  1.00 43.98  ? 55  GLN C CD  1 
ATOM   3840  O OE1 . GLN C  1 63  ? -28.080 21.393  40.942  1.00 49.33  ? 55  GLN C OE1 1 
ATOM   3841  N NE2 . GLN C  1 63  ? -27.471 19.901  39.348  1.00 39.67  ? 55  GLN C NE2 1 
ATOM   3842  N N   . THR C  1 64  ? -22.441 23.554  40.095  1.00 15.58  ? 56  THR C N   1 
ATOM   3843  C CA  . THR C  1 64  ? -21.828 24.644  39.343  1.00 13.89  ? 56  THR C CA  1 
ATOM   3844  C C   . THR C  1 64  ? -21.838 24.279  37.878  1.00 15.44  ? 56  THR C C   1 
ATOM   3845  O O   . THR C  1 64  ? -21.433 23.174  37.516  1.00 15.94  ? 56  THR C O   1 
ATOM   3846  C CB  . THR C  1 64  ? -20.358 24.842  39.750  1.00 15.27  ? 56  THR C CB  1 
ATOM   3847  O OG1 . THR C  1 64  ? -20.264 25.012  41.171  1.00 24.81  ? 56  THR C OG1 1 
ATOM   3848  C CG2 . THR C  1 64  ? -19.784 26.058  39.082  1.00 15.93  ? 56  THR C CG2 1 
ATOM   3849  N N   . THR C  1 65  ? -22.328 25.184  37.033  1.00 16.84  ? 57  THR C N   1 
ATOM   3850  C CA  . THR C  1 65  ? -22.267 24.987  35.585  1.00 13.37  ? 57  THR C CA  1 
ATOM   3851  C C   . THR C  1 65  ? -21.871 26.272  34.872  1.00 12.90  ? 57  THR C C   1 
ATOM   3852  O O   . THR C  1 65  ? -22.130 27.371  35.349  1.00 15.63  ? 57  THR C O   1 
ATOM   3853  C CB  . THR C  1 65  ? -23.598 24.511  34.990  1.00 13.75  ? 57  THR C CB  1 
ATOM   3854  O OG1 . THR C  1 65  ? -24.469 25.637  34.822  1.00 15.66  ? 57  THR C OG1 1 
ATOM   3855  C CG2 . THR C  1 65  ? -24.256 23.470  35.886  1.00 17.24  ? 57  THR C CG2 1 
ATOM   3856  N N   . TRP C  1 66  ? -21.221 26.128  33.730  1.00 10.52  ? 58  TRP C N   1 
ATOM   3857  C CA  . TRP C  1 66  ? -20.912 27.275  32.899  1.00 10.96  ? 58  TRP C CA  1 
ATOM   3858  C C   . TRP C  1 66  ? -20.657 26.757  31.507  1.00 11.54  ? 58  TRP C C   1 
ATOM   3859  O O   . TRP C  1 66  ? -20.851 25.566  31.235  1.00 12.34  ? 58  TRP C O   1 
ATOM   3860  C CB  . TRP C  1 66  ? -19.719 28.073  33.441  1.00 12.77  ? 58  TRP C CB  1 
ATOM   3861  C CG  . TRP C  1 66  ? -18.435 27.309  33.516  1.00 11.20  ? 58  TRP C CG  1 
ATOM   3862  C CD1 . TRP C  1 66  ? -17.413 27.360  32.626  1.00 9.33   ? 58  TRP C CD1 1 
ATOM   3863  C CD2 . TRP C  1 66  ? -18.036 26.377  34.535  1.00 10.84  ? 58  TRP C CD2 1 
ATOM   3864  N NE1 . TRP C  1 66  ? -16.402 26.527  33.020  1.00 10.42  ? 58  TRP C NE1 1 
ATOM   3865  C CE2 . TRP C  1 66  ? -16.756 25.909  34.189  1.00 8.10   ? 58  TRP C CE2 1 
ATOM   3866  C CE3 . TRP C  1 66  ? -18.636 25.897  35.705  1.00 10.44  ? 58  TRP C CE3 1 
ATOM   3867  C CZ2 . TRP C  1 66  ? -16.061 24.981  34.960  1.00 7.15   ? 58  TRP C CZ2 1 
ATOM   3868  C CZ3 . TRP C  1 66  ? -17.941 24.967  36.473  1.00 10.62  ? 58  TRP C CZ3 1 
ATOM   3869  C CH2 . TRP C  1 66  ? -16.667 24.522  36.096  1.00 10.00  ? 58  TRP C CH2 1 
ATOM   3870  N N   . SER C  1 67  ? -20.249 27.634  30.607  1.00 10.28  ? 59  SER C N   1 
ATOM   3871  C CA  . SER C  1 67  ? -20.003 27.170  29.254  1.00 12.86  ? 59  SER C CA  1 
ATOM   3872  C C   . SER C  1 67  ? -18.665 27.633  28.696  1.00 10.30  ? 59  SER C C   1 
ATOM   3873  O O   . SER C  1 67  ? -18.226 28.771  28.942  1.00 7.37   ? 59  SER C O   1 
ATOM   3874  C CB  . SER C  1 67  ? -21.139 27.586  28.329  1.00 13.90  ? 59  SER C CB  1 
ATOM   3875  O OG  . SER C  1 67  ? -20.739 28.678  27.534  1.00 17.49  ? 59  SER C OG  1 
ATOM   3876  N N   . ASP C  1 68  ? -17.955 26.692  28.071  1.00 12.47  ? 60  ASP C N   1 
ATOM   3877  C CA  . ASP C  1 68  ? -16.841 26.920  27.143  1.00 14.49  ? 60  ASP C CA  1 
ATOM   3878  C C   . ASP C  1 68  ? -17.129 26.390  25.793  1.00 11.88  ? 60  ASP C C   1 
ATOM   3879  O O   . ASP C  1 68  ? -16.980 25.250  25.540  1.00 11.45  ? 60  ASP C O   1 
ATOM   3880  C CB  . ASP C  1 68  ? -15.565 26.262  27.604  1.00 11.13  ? 60  ASP C CB  1 
ATOM   3881  C CG  . ASP C  1 68  ? -14.325 26.984  27.137  1.00 19.10  ? 60  ASP C CG  1 
ATOM   3882  O OD1 . ASP C  1 68  ? -14.329 27.790  26.223  1.00 15.28  ? 60  ASP C OD1 1 
ATOM   3883  O OD2 . ASP C  1 68  ? -13.310 26.739  27.728  1.00 17.03  ? 60  ASP C OD2 1 
ATOM   3884  N N   . ARG C  1 69  ? -17.493 27.293  24.893  1.00 16.13  ? 61  ARG C N   1 
ATOM   3885  C CA  . ARG C  1 69  ? -17.830 26.917  23.534  1.00 17.38  ? 61  ARG C CA  1 
ATOM   3886  C C   . ARG C  1 69  ? -16.630 26.269  22.863  1.00 14.40  ? 61  ARG C C   1 
ATOM   3887  O O   . ARG C  1 69  ? -16.783 25.311  22.105  1.00 14.24  ? 61  ARG C O   1 
ATOM   3888  C CB  . ARG C  1 69  ? -18.285 28.139  22.735  1.00 20.15  ? 61  ARG C CB  1 
ATOM   3889  C CG  . ARG C  1 69  ? -19.502 27.891  21.859  1.00 27.69  ? 61  ARG C CG  1 
ATOM   3890  C CD  . ARG C  1 69  ? -20.787 27.960  22.667  1.00 31.64  ? 61  ARG C CD  1 
ATOM   3891  N NE  . ARG C  1 69  ? -21.170 29.336  22.970  1.00 39.66  ? 61  ARG C NE  1 
ATOM   3892  C CZ  . ARG C  1 69  ? -22.143 29.673  23.810  1.00 48.13  ? 61  ARG C CZ  1 
ATOM   3893  N NH1 . ARG C  1 69  ? -22.837 28.732  24.435  1.00 42.37  ? 61  ARG C NH1 1 
ATOM   3894  N NH2 . ARG C  1 69  ? -22.423 30.951  24.025  1.00 50.38  ? 61  ARG C NH2 1 
ATOM   3895  N N   . THR C  1 70  ? -15.434 26.789  23.127  1.00 17.02  ? 62  THR C N   1 
ATOM   3896  C CA  . THR C  1 70  ? -14.250 26.265  22.435  1.00 14.17  ? 62  THR C CA  1 
ATOM   3897  C C   . THR C  1 70  ? -13.976 24.766  22.681  1.00 11.48  ? 62  THR C C   1 
ATOM   3898  O O   . THR C  1 70  ? -13.201 24.147  21.944  1.00 16.09  ? 62  THR C O   1 
ATOM   3899  C CB  . THR C  1 70  ? -12.978 27.105  22.716  1.00 10.22  ? 62  THR C CB  1 
ATOM   3900  O OG1 . THR C  1 70  ? -12.498 26.830  24.030  1.00 15.04  ? 62  THR C OG1 1 
ATOM   3901  C CG2 . THR C  1 70  ? -13.266 28.583  22.592  1.00 8.84   ? 62  THR C CG2 1 
ATOM   3902  N N   . LEU C  1 71  ? -14.615 24.189  23.696  1.00 9.35   ? 63  LEU C N   1 
ATOM   3903  C CA  . LEU C  1 71  ? -14.502 22.760  23.975  1.00 6.99   ? 63  LEU C CA  1 
ATOM   3904  C C   . LEU C  1 71  ? -15.572 21.955  23.261  1.00 7.78   ? 63  LEU C C   1 
ATOM   3905  O O   . LEU C  1 71  ? -15.613 20.740  23.386  1.00 8.68   ? 63  LEU C O   1 
ATOM   3906  C CB  . LEU C  1 71  ? -14.640 22.492  25.460  1.00 10.30  ? 63  LEU C CB  1 
ATOM   3907  C CG  . LEU C  1 71  ? -13.737 23.232  26.425  1.00 11.63  ? 63  LEU C CG  1 
ATOM   3908  C CD1 . LEU C  1 71  ? -14.179 22.920  27.848  1.00 7.63   ? 63  LEU C CD1 1 
ATOM   3909  C CD2 . LEU C  1 71  ? -12.300 22.814  26.182  1.00 8.81   ? 63  LEU C CD2 1 
ATOM   3910  N N   . ALA C  1 72  ? -16.438 22.630  22.515  1.00 8.25   ? 64  ALA C N   1 
ATOM   3911  C CA  . ALA C  1 72  ? -17.534 21.964  21.807  1.00 10.32  ? 64  ALA C CA  1 
ATOM   3912  C C   . ALA C  1 72  ? -17.078 21.004  20.698  1.00 14.87  ? 64  ALA C C   1 
ATOM   3913  O O   . ALA C  1 72  ? -16.098 21.263  20.001  1.00 14.84  ? 64  ALA C O   1 
ATOM   3914  C CB  . ALA C  1 72  ? -18.516 22.996  21.242  1.00 6.78   ? 64  ALA C CB  1 
ATOM   3915  N N   . TRP C  1 73  ? -17.803 19.901  20.538  1.00 13.92  ? 65  TRP C N   1 
ATOM   3916  C CA  . TRP C  1 73  ? -17.599 19.009  19.409  1.00 11.95  ? 65  TRP C CA  1 
ATOM   3917  C C   . TRP C  1 73  ? -18.936 18.491  18.869  1.00 17.22  ? 65  TRP C C   1 
ATOM   3918  O O   . TRP C  1 73  ? -19.948 18.544  19.560  1.00 21.57  ? 65  TRP C O   1 
ATOM   3919  C CB  . TRP C  1 73  ? -16.689 17.849  19.792  1.00 11.23  ? 65  TRP C CB  1 
ATOM   3920  C CG  . TRP C  1 73  ? -17.295 16.828  20.714  1.00 12.98  ? 65  TRP C CG  1 
ATOM   3921  C CD1 . TRP C  1 73  ? -17.878 15.645  20.357  1.00 15.00  ? 65  TRP C CD1 1 
ATOM   3922  C CD2 . TRP C  1 73  ? -17.344 16.879  22.148  1.00 14.32  ? 65  TRP C CD2 1 
ATOM   3923  N NE1 . TRP C  1 73  ? -18.299 14.962  21.476  1.00 15.44  ? 65  TRP C NE1 1 
ATOM   3924  C CE2 . TRP C  1 73  ? -17.991 15.703  22.587  1.00 16.84  ? 65  TRP C CE2 1 
ATOM   3925  C CE3 . TRP C  1 73  ? -16.923 17.812  23.097  1.00 9.61   ? 65  TRP C CE3 1 
ATOM   3926  C CZ2 . TRP C  1 73  ? -18.227 15.438  23.933  1.00 13.65  ? 65  TRP C CZ2 1 
ATOM   3927  C CZ3 . TRP C  1 73  ? -17.129 17.541  24.415  1.00 11.51  ? 65  TRP C CZ3 1 
ATOM   3928  C CH2 . TRP C  1 73  ? -17.789 16.363  24.832  1.00 13.91  ? 65  TRP C CH2 1 
ATOM   3929  N N   . ASN C  1 74  ? -18.935 17.849  17.670  1.00 16.05  ? 66  ASN C N   1 
ATOM   3930  C CA  . ASN C  1 74  ? -20.206 17.576  16.974  1.00 18.51  ? 66  ASN C CA  1 
ATOM   3931  C C   . ASN C  1 74  ? -21.261 16.687  17.675  1.00 18.80  ? 66  ASN C C   1 
ATOM   3932  O O   . ASN C  1 74  ? -22.444 17.028  17.673  1.00 19.32  ? 66  ASN C O   1 
ATOM   3933  C CB  . ASN C  1 74  ? -19.927 17.027  15.570  1.00 17.29  ? 66  ASN C CB  1 
ATOM   3934  C CG  . ASN C  1 74  ? -21.170 16.988  14.703  1.00 23.00  ? 66  ASN C CG  1 
ATOM   3935  O OD1 . ASN C  1 74  ? -22.180 17.617  15.017  1.00 27.46  ? 66  ASN C OD1 1 
ATOM   3936  N ND2 . ASN C  1 74  ? -21.100 16.247  13.602  1.00 32.02  ? 66  ASN C ND2 1 
ATOM   3937  N N   . SER C  1 75  ? -20.867 15.606  18.298  1.00 17.67  ? 67  SER C N   1 
ATOM   3938  C CA  . SER C  1 75  ? -21.733 14.834  19.198  1.00 20.76  ? 67  SER C CA  1 
ATOM   3939  C C   . SER C  1 75  ? -22.875 13.998  18.578  1.00 21.59  ? 67  SER C C   1 
ATOM   3940  O O   . SER C  1 75  ? -23.661 13.400  19.313  1.00 27.88  ? 67  SER C O   1 
ATOM   3941  C CB  . SER C  1 75  ? -22.307 15.751  20.284  1.00 23.30  ? 67  SER C CB  1 
ATOM   3942  O OG  . SER C  1 75  ? -23.608 15.339  20.665  1.00 23.37  ? 67  SER C OG  1 
ATOM   3943  N N   . SER C  1 76  ? -22.969 13.942  17.251  1.00 22.63  ? 68  SER C N   1 
ATOM   3944  C CA  . SER C  1 76  ? -23.941 13.076  16.590  1.00 24.45  ? 68  SER C CA  1 
ATOM   3945  C C   . SER C  1 76  ? -23.510 11.608  16.560  1.00 26.27  ? 68  SER C C   1 
ATOM   3946  O O   . SER C  1 76  ? -24.312 10.711  16.821  1.00 31.67  ? 68  SER C O   1 
ATOM   3947  C CB  . SER C  1 76  ? -24.213 13.569  15.167  1.00 24.35  ? 68  SER C CB  1 
ATOM   3948  O OG  . SER C  1 76  ? -23.090 13.358  14.330  1.00 26.90  ? 68  SER C OG  1 
ATOM   3949  N N   . HIS C  1 77  ? -22.265 11.369  16.293  1.00 27.63  ? 69  HIS C N   1 
ATOM   3950  C CA  . HIS C  1 77  ? -21.860 10.017  16.307  1.00 30.05  ? 69  HIS C CA  1 
ATOM   3951  C C   . HIS C  1 77  ? -20.743 9.755   17.245  1.00 29.88  ? 69  HIS C C   1 
ATOM   3952  O O   . HIS C  1 77  ? -20.040 8.832   17.031  1.00 32.30  ? 69  HIS C O   1 
ATOM   3953  C CB  . HIS C  1 77  ? -21.553 9.495   14.895  1.00 27.79  ? 69  HIS C CB  1 
ATOM   3954  C CG  . HIS C  1 77  ? -22.708 9.559   13.954  1.00 28.86  ? 69  HIS C CG  1 
ATOM   3955  N ND1 . HIS C  1 77  ? -22.878 10.582  13.059  1.00 30.15  ? 69  HIS C ND1 1 
ATOM   3956  C CD2 . HIS C  1 77  ? -23.757 8.739   13.781  1.00 30.28  ? 69  HIS C CD2 1 
ATOM   3957  C CE1 . HIS C  1 77  ? -23.981 10.400  12.379  1.00 27.98  ? 69  HIS C CE1 1 
ATOM   3958  N NE2 . HIS C  1 77  ? -24.533 9.289   12.798  1.00 29.46  ? 69  HIS C NE2 1 
ATOM   3959  N N   . SER C  1 78  ? -20.590 10.559  18.289  1.00 24.05  ? 70  SER C N   1 
ATOM   3960  C CA  . SER C  1 78  ? -19.731 10.332  19.445  1.00 26.97  ? 70  SER C CA  1 
ATOM   3961  C C   . SER C  1 78  ? -20.475 10.685  20.726  1.00 23.92  ? 70  SER C C   1 
ATOM   3962  O O   . SER C  1 78  ? -21.414 11.491  20.696  1.00 24.66  ? 70  SER C O   1 
ATOM   3963  C CB  . SER C  1 78  ? -18.450 11.160  19.333  1.00 19.33  ? 70  SER C CB  1 
ATOM   3964  O OG  . SER C  1 78  ? -18.701 12.406  18.706  1.00 18.92  ? 70  SER C OG  1 
ATOM   3965  N N   . PRO C  1 79  ? -20.023 10.040  21.893  1.00 23.91  ? 71  PRO C N   1 
ATOM   3966  C CA  . PRO C  1 79  ? -20.822 10.387  23.084  1.00 23.70  ? 71  PRO C CA  1 
ATOM   3967  C C   . PRO C  1 79  ? -20.733 11.877  23.393  1.00 20.27  ? 71  PRO C C   1 
ATOM   3968  O O   . PRO C  1 79  ? -19.656 12.467  23.313  1.00 19.58  ? 71  PRO C O   1 
ATOM   3969  C CB  . PRO C  1 79  ? -20.173 9.578   24.216  1.00 23.08  ? 71  PRO C CB  1 
ATOM   3970  C CG  . PRO C  1 79  ? -19.568 8.403   23.550  1.00 24.68  ? 71  PRO C CG  1 
ATOM   3971  C CD  . PRO C  1 79  ? -18.940 9.042   22.359  1.00 20.68  ? 71  PRO C CD  1 
ATOM   3972  N N   . ASP C  1 80  ? -21.869 12.471  23.741  1.00 22.77  ? 72  ASP C N   1 
ATOM   3973  C CA  . ASP C  1 80  ? -21.942 13.899  24.023  1.00 23.74  ? 72  ASP C CA  1 
ATOM   3974  C C   . ASP C  1 80  ? -21.106 14.304  25.232  1.00 18.88  ? 72  ASP C C   1 
ATOM   3975  O O   . ASP C  1 80  ? -20.460 15.352  25.227  1.00 15.99  ? 72  ASP C O   1 
ATOM   3976  C CB  . ASP C  1 80  ? -23.397 14.328  24.227  1.00 25.26  ? 72  ASP C CB  1 
ATOM   3977  C CG  . ASP C  1 80  ? -24.002 13.755  25.493  1.00 38.98  ? 72  ASP C CG  1 
ATOM   3978  O OD1 . ASP C  1 80  ? -23.689 12.594  25.830  1.00 38.29  ? 72  ASP C OD1 1 
ATOM   3979  O OD2 . ASP C  1 80  ? -24.789 14.466  26.153  1.00 48.70  ? 72  ASP C OD2 1 
ATOM   3980  N N   . GLN C  1 81  ? -21.129 13.476  26.271  1.00 14.78  ? 73  GLN C N   1 
ATOM   3981  C CA  . GLN C  1 81  ? -20.491 13.814  27.507  1.00 13.49  ? 73  GLN C CA  1 
ATOM   3982  C C   . GLN C  1 81  ? -19.422 12.902  27.919  1.00 14.58  ? 73  GLN C C   1 
ATOM   3983  O O   . GLN C  1 81  ? -19.438 11.795  27.568  1.00 16.24  ? 73  GLN C O   1 
ATOM   3984  C CB  . GLN C  1 81  ? -21.461 13.913  28.660  1.00 17.13  ? 73  GLN C CB  1 
ATOM   3985  C CG  . GLN C  1 81  ? -22.918 13.804  28.376  1.00 18.27  ? 73  GLN C CG  1 
ATOM   3986  C CD  . GLN C  1 81  ? -23.711 14.442  29.466  1.00 20.86  ? 73  GLN C CD  1 
ATOM   3987  O OE1 . GLN C  1 81  ? -23.466 14.213  30.607  1.00 24.67  ? 73  GLN C OE1 1 
ATOM   3988  N NE2 . GLN C  1 81  ? -24.657 15.232  29.114  1.00 22.94  ? 73  GLN C NE2 1 
ATOM   3989  N N   . VAL C  1 82  ? -18.482 13.423  28.667  1.00 9.61   ? 74  VAL C N   1 
ATOM   3990  C CA  . VAL C  1 82  ? -17.391 12.655  29.229  1.00 8.05   ? 74  VAL C CA  1 
ATOM   3991  C C   . VAL C  1 82  ? -17.067 13.264  30.578  1.00 7.43   ? 74  VAL C C   1 
ATOM   3992  O O   . VAL C  1 82  ? -17.408 14.413  30.841  1.00 6.68   ? 74  VAL C O   1 
ATOM   3993  C CB  . VAL C  1 82  ? -16.100 12.722  28.340  1.00 9.03   ? 74  VAL C CB  1 
ATOM   3994  C CG1 . VAL C  1 82  ? -16.290 12.019  26.998  1.00 8.59   ? 74  VAL C CG1 1 
ATOM   3995  C CG2 . VAL C  1 82  ? -15.637 14.160  28.140  1.00 6.62   ? 74  VAL C CG2 1 
ATOM   3996  N N   . SER C  1 83  ? -16.394 12.497  31.425  1.00 8.83   ? 75  SER C N   1 
ATOM   3997  C CA  . SER C  1 83  ? -15.837 13.022  32.673  1.00 9.67   ? 75  SER C CA  1 
ATOM   3998  C C   . SER C  1 83  ? -14.405 13.496  32.438  1.00 7.59   ? 75  SER C C   1 
ATOM   3999  O O   . SER C  1 83  ? -13.621 12.831  31.771  1.00 8.80   ? 75  SER C O   1 
ATOM   4000  C CB  . SER C  1 83  ? -15.849 11.956  33.786  1.00 10.72  ? 75  SER C CB  1 
ATOM   4001  O OG  . SER C  1 83  ? -17.160 11.670  34.251  1.00 9.67   ? 75  SER C OG  1 
ATOM   4002  N N   . VAL C  1 84  ? -14.058 14.648  32.988  1.00 6.17   ? 76  VAL C N   1 
ATOM   4003  C CA  . VAL C  1 84  ? -12.723 15.182  32.803  1.00 7.06   ? 76  VAL C CA  1 
ATOM   4004  C C   . VAL C  1 84  ? -12.198 15.533  34.177  1.00 7.13   ? 76  VAL C C   1 
ATOM   4005  O O   . VAL C  1 84  ? -12.940 16.069  34.988  1.00 9.66   ? 76  VAL C O   1 
ATOM   4006  C CB  . VAL C  1 84  ? -12.763 16.452  31.907  1.00 8.37   ? 76  VAL C CB  1 
ATOM   4007  C CG1 . VAL C  1 84  ? -11.387 17.048  31.738  1.00 6.74   ? 76  VAL C CG1 1 
ATOM   4008  C CG2 . VAL C  1 84  ? -13.380 16.136  30.568  1.00 5.15   ? 76  VAL C CG2 1 
ATOM   4009  N N   . PRO C  1 85  ? -10.931 15.192  34.474  1.00 11.23  ? 77  PRO C N   1 
ATOM   4010  C CA  . PRO C  1 85  ? -10.376 15.647  35.755  1.00 7.08   ? 77  PRO C CA  1 
ATOM   4011  C C   . PRO C  1 85  ? -10.365 17.175  35.758  1.00 7.42   ? 77  PRO C C   1 
ATOM   4012  O O   . PRO C  1 85  ? -10.007 17.739  34.740  1.00 9.47   ? 77  PRO C O   1 
ATOM   4013  C CB  . PRO C  1 85  ? -8.952  15.095  35.712  1.00 4.46   ? 77  PRO C CB  1 
ATOM   4014  C CG  . PRO C  1 85  ? -9.047  13.891  34.866  1.00 5.78   ? 77  PRO C CG  1 
ATOM   4015  C CD  . PRO C  1 85  ? -10.003 14.285  33.774  1.00 8.92   ? 77  PRO C CD  1 
ATOM   4016  N N   . ILE C  1 86  ? -10.761 17.835  36.841  1.00 7.87   ? 78  ILE C N   1 
ATOM   4017  C CA  . ILE C  1 86  ? -10.859 19.301  36.826  1.00 7.29   ? 78  ILE C CA  1 
ATOM   4018  C C   . ILE C  1 86  ? -9.518  20.036  36.718  1.00 8.21   ? 78  ILE C C   1 
ATOM   4019  O O   . ILE C  1 86  ? -9.491  21.229  36.400  1.00 9.24   ? 78  ILE C O   1 
ATOM   4020  C CB  . ILE C  1 86  ? -11.632 19.847  38.042  1.00 6.94   ? 78  ILE C CB  1 
ATOM   4021  C CG1 . ILE C  1 86  ? -10.936 19.433  39.340  1.00 8.28   ? 78  ILE C CG1 1 
ATOM   4022  C CG2 . ILE C  1 86  ? -13.075 19.384  38.000  1.00 5.64   ? 78  ILE C CG2 1 
ATOM   4023  C CD1 . ILE C  1 86  ? -11.475 20.106  40.593  1.00 7.98   ? 78  ILE C CD1 1 
ATOM   4024  N N   . SER C  1 87  ? -8.410  19.343  36.979  1.00 6.63   ? 79  SER C N   1 
ATOM   4025  C CA  . SER C  1 87  ? -7.089  19.934  36.736  1.00 7.11   ? 79  SER C CA  1 
ATOM   4026  C C   . SER C  1 87  ? -6.804  20.170  35.241  1.00 7.77   ? 79  SER C C   1 
ATOM   4027  O O   . SER C  1 87  ? -5.894  20.917  34.880  1.00 6.18   ? 79  SER C O   1 
ATOM   4028  C CB  . SER C  1 87  ? -5.981  19.100  37.365  1.00 4.43   ? 79  SER C CB  1 
ATOM   4029  O OG  . SER C  1 87  ? -5.948  17.818  36.793  1.00 8.98   ? 79  SER C OG  1 
ATOM   4030  N N   . SER C  1 88  ? -7.603  19.538  34.390  1.00 7.17   ? 80  SER C N   1 
ATOM   4031  C CA  . SER C  1 88  ? -7.512  19.692  32.957  1.00 7.51   ? 80  SER C CA  1 
ATOM   4032  C C   . SER C  1 88  ? -8.359  20.847  32.442  1.00 10.39  ? 80  SER C C   1 
ATOM   4033  O O   . SER C  1 88  ? -8.264  21.188  31.260  1.00 13.13  ? 80  SER C O   1 
ATOM   4034  C CB  . SER C  1 88  ? -7.966  18.407  32.264  1.00 8.78   ? 80  SER C CB  1 
ATOM   4035  O OG  . SER C  1 88  ? -7.015  17.364  32.403  1.00 11.02  ? 80  SER C OG  1 
ATOM   4036  N N   . LEU C  1 89  ? -9.177  21.448  33.310  1.00 9.21   ? 81  LEU C N   1 
ATOM   4037  C CA  . LEU C  1 89  ? -10.142 22.482  32.889  1.00 9.93   ? 81  LEU C CA  1 
ATOM   4038  C C   . LEU C  1 89  ? -10.070 23.723  33.736  1.00 9.35   ? 81  LEU C C   1 
ATOM   4039  O O   . LEU C  1 89  ? -9.621  23.679  34.875  1.00 11.12  ? 81  LEU C O   1 
ATOM   4040  C CB  . LEU C  1 89  ? -11.582 22.000  33.042  1.00 10.05  ? 81  LEU C CB  1 
ATOM   4041  C CG  . LEU C  1 89  ? -12.126 20.752  32.378  1.00 11.05  ? 81  LEU C CG  1 
ATOM   4042  C CD1 . LEU C  1 89  ? -13.343 20.331  33.165  1.00 6.14   ? 81  LEU C CD1 1 
ATOM   4043  C CD2 . LEU C  1 89  ? -12.474 21.039  30.921  1.00 11.32  ? 81  LEU C CD2 1 
ATOM   4044  N N   . TRP C  1 90  ? -10.572 24.827  33.194  1.00 9.86   ? 82  TRP C N   1 
ATOM   4045  C CA  . TRP C  1 90  ? -10.819 26.009  34.011  1.00 11.17  ? 82  TRP C CA  1 
ATOM   4046  C C   . TRP C  1 90  ? -12.067 25.788  34.862  1.00 9.88   ? 82  TRP C C   1 
ATOM   4047  O O   . TRP C  1 90  ? -13.119 25.442  34.327  1.00 10.20  ? 82  TRP C O   1 
ATOM   4048  C CB  . TRP C  1 90  ? -11.040 27.246  33.136  1.00 9.15   ? 82  TRP C CB  1 
ATOM   4049  C CG  . TRP C  1 90  ? -11.328 28.488  33.945  1.00 9.51   ? 82  TRP C CG  1 
ATOM   4050  C CD1 . TRP C  1 90  ? -10.409 29.330  34.502  1.00 8.87   ? 82  TRP C CD1 1 
ATOM   4051  C CD2 . TRP C  1 90  ? -12.613 29.007  34.308  1.00 7.86   ? 82  TRP C CD2 1 
ATOM   4052  N NE1 . TRP C  1 90  ? -11.038 30.347  35.166  1.00 9.54   ? 82  TRP C NE1 1 
ATOM   4053  C CE2 . TRP C  1 90  ? -12.392 30.169  35.072  1.00 7.07   ? 82  TRP C CE2 1 
ATOM   4054  C CE3 . TRP C  1 90  ? -13.927 28.614  34.046  1.00 9.52   ? 82  TRP C CE3 1 
ATOM   4055  C CZ2 . TRP C  1 90  ? -13.431 30.934  35.584  1.00 6.15   ? 82  TRP C CZ2 1 
ATOM   4056  C CZ3 . TRP C  1 90  ? -14.966 29.393  34.546  1.00 7.04   ? 82  TRP C CZ3 1 
ATOM   4057  C CH2 . TRP C  1 90  ? -14.707 30.535  35.304  1.00 6.29   ? 82  TRP C CH2 1 
ATOM   4058  N N   . VAL C  1 91  ? -11.949 25.976  36.172  1.00 7.16   ? 83  VAL C N   1 
ATOM   4059  C CA  . VAL C  1 91  ? -13.132 26.052  37.033  1.00 10.01  ? 83  VAL C CA  1 
ATOM   4060  C C   . VAL C  1 91  ? -13.170 27.411  37.731  1.00 8.68   ? 83  VAL C C   1 
ATOM   4061  O O   . VAL C  1 91  ? -12.128 27.990  38.029  1.00 7.89   ? 83  VAL C O   1 
ATOM   4062  C CB  . VAL C  1 91  ? -13.177 24.933  38.096  1.00 8.16   ? 83  VAL C CB  1 
ATOM   4063  C CG1 . VAL C  1 91  ? -13.326 23.573  37.433  1.00 7.46   ? 83  VAL C CG1 1 
ATOM   4064  C CG2 . VAL C  1 91  ? -11.940 24.993  38.947  1.00 6.69   ? 83  VAL C CG2 1 
ATOM   4065  N N   . PRO C  1 92  ? -14.377 27.943  37.965  1.00 7.67   ? 84  PRO C N   1 
ATOM   4066  C CA  . PRO C  1 92  ? -14.414 29.245  38.630  1.00 8.45   ? 84  PRO C CA  1 
ATOM   4067  C C   . PRO C  1 92  ? -13.833 29.213  40.039  1.00 9.55   ? 84  PRO C C   1 
ATOM   4068  O O   . PRO C  1 92  ? -13.972 28.217  40.757  1.00 8.90   ? 84  PRO C O   1 
ATOM   4069  C CB  . PRO C  1 92  ? -15.895 29.613  38.642  1.00 7.41   ? 84  PRO C CB  1 
ATOM   4070  C CG  . PRO C  1 92  ? -16.619 28.467  38.054  1.00 8.77   ? 84  PRO C CG  1 
ATOM   4071  C CD  . PRO C  1 92  ? -15.661 27.584  37.357  1.00 6.79   ? 84  PRO C CD  1 
ATOM   4072  N N   . ASP C  1 93  ? -13.174 30.315  40.397  1.00 7.86   ? 85  ASP C N   1 
ATOM   4073  C CA  . ASP C  1 93  ? -12.534 30.477  41.679  1.00 9.49   ? 85  ASP C CA  1 
ATOM   4074  C C   . ASP C  1 93  ? -13.511 30.982  42.761  1.00 13.98  ? 85  ASP C C   1 
ATOM   4075  O O   . ASP C  1 93  ? -13.212 31.947  43.480  1.00 13.30  ? 85  ASP C O   1 
ATOM   4076  C CB  . ASP C  1 93  ? -11.315 31.396  41.546  1.00 8.60   ? 85  ASP C CB  1 
ATOM   4077  C CG  . ASP C  1 93  ? -11.682 32.803  41.107  1.00 16.39  ? 85  ASP C CG  1 
ATOM   4078  O OD1 . ASP C  1 93  ? -12.669 32.969  40.349  1.00 14.16  ? 85  ASP C OD1 1 
ATOM   4079  O OD2 . ASP C  1 93  ? -10.986 33.750  41.541  1.00 16.47  ? 85  ASP C OD2 1 
ATOM   4080  N N   . LEU C  1 94  ? -14.663 30.316  42.885  1.00 10.92  ? 86  LEU C N   1 
ATOM   4081  C CA  . LEU C  1 94  ? -15.642 30.679  43.899  1.00 11.51  ? 86  LEU C CA  1 
ATOM   4082  C C   . LEU C  1 94  ? -15.074 30.553  45.314  1.00 12.20  ? 86  LEU C C   1 
ATOM   4083  O O   . LEU C  1 94  ? -14.194 29.739  45.579  1.00 12.27  ? 86  LEU C O   1 
ATOM   4084  C CB  . LEU C  1 94  ? -16.890 29.830  43.767  1.00 11.42  ? 86  LEU C CB  1 
ATOM   4085  C CG  . LEU C  1 94  ? -17.493 29.693  42.368  1.00 15.26  ? 86  LEU C CG  1 
ATOM   4086  C CD1 . LEU C  1 94  ? -18.809 28.932  42.458  1.00 16.56  ? 86  LEU C CD1 1 
ATOM   4087  C CD2 . LEU C  1 94  ? -17.688 31.043  41.665  1.00 13.31  ? 86  LEU C CD2 1 
ATOM   4088  N N   . ALA C  1 95  ? -15.564 31.398  46.209  1.00 15.36  ? 87  ALA C N   1 
ATOM   4089  C CA  . ALA C  1 95  ? -15.247 31.313  47.637  1.00 16.98  ? 87  ALA C CA  1 
ATOM   4090  C C   . ALA C  1 95  ? -16.498 31.670  48.421  1.00 12.16  ? 87  ALA C C   1 
ATOM   4091  O O   . ALA C  1 95  ? -17.363 32.372  47.916  1.00 16.13  ? 87  ALA C O   1 
ATOM   4092  C CB  . ALA C  1 95  ? -14.102 32.259  48.004  1.00 11.57  ? 87  ALA C CB  1 
ATOM   4093  N N   . ALA C  1 96  ? -16.607 31.175  49.645  1.00 15.29  ? 88  ALA C N   1 
ATOM   4094  C CA  . ALA C  1 96  ? -17.693 31.581  50.537  1.00 13.65  ? 88  ALA C CA  1 
ATOM   4095  C C   . ALA C  1 96  ? -17.182 32.616  51.533  1.00 15.17  ? 88  ALA C C   1 
ATOM   4096  O O   . ALA C  1 96  ? -16.313 32.323  52.356  1.00 13.88  ? 88  ALA C O   1 
ATOM   4097  C CB  . ALA C  1 96  ? -18.246 30.385  51.260  1.00 13.80  ? 88  ALA C CB  1 
ATOM   4098  N N   . TYR C  1 97  ? -17.724 33.828  51.463  1.00 22.20  ? 89  TYR C N   1 
ATOM   4099  C CA  . TYR C  1 97  ? -17.246 34.934  52.303  1.00 17.47  ? 89  TYR C CA  1 
ATOM   4100  C C   . TYR C  1 97  ? -17.245 34.602  53.792  1.00 13.09  ? 89  TYR C C   1 
ATOM   4101  O O   . TYR C  1 97  ? -16.317 34.975  54.516  1.00 10.78  ? 89  TYR C O   1 
ATOM   4102  C CB  . TYR C  1 97  ? -18.028 36.225  52.001  1.00 19.91  ? 89  TYR C CB  1 
ATOM   4103  C CG  . TYR C  1 97  ? -17.911 36.654  50.542  1.00 28.90  ? 89  TYR C CG  1 
ATOM   4104  C CD1 . TYR C  1 97  ? -16.700 36.558  49.869  1.00 27.18  ? 89  TYR C CD1 1 
ATOM   4105  C CD2 . TYR C  1 97  ? -19.014 37.119  49.831  1.00 29.57  ? 89  TYR C CD2 1 
ATOM   4106  C CE1 . TYR C  1 97  ? -16.583 36.931  48.534  1.00 33.97  ? 89  TYR C CE1 1 
ATOM   4107  C CE2 . TYR C  1 97  ? -18.908 37.492  48.485  1.00 25.15  ? 89  TYR C CE2 1 
ATOM   4108  C CZ  . TYR C  1 97  ? -17.688 37.397  47.843  1.00 32.36  ? 89  TYR C CZ  1 
ATOM   4109  O OH  . TYR C  1 97  ? -17.558 37.757  46.506  1.00 33.85  ? 89  TYR C OH  1 
ATOM   4110  N N   . ASN C  1 98  ? -18.259 33.871  54.255  1.00 13.70  ? 90  ASN C N   1 
ATOM   4111  C CA  . ASN C  1 98  ? -18.331 33.575  55.687  1.00 17.40  ? 90  ASN C CA  1 
ATOM   4112  C C   . ASN C  1 98  ? -17.908 32.161  56.114  1.00 17.09  ? 90  ASN C C   1 
ATOM   4113  O O   . ASN C  1 98  ? -18.290 31.696  57.190  1.00 15.36  ? 90  ASN C O   1 
ATOM   4114  C CB  . ASN C  1 98  ? -19.681 33.979  56.300  1.00 13.56  ? 90  ASN C CB  1 
ATOM   4115  C CG  . ASN C  1 98  ? -20.849 33.246  55.691  1.00 17.50  ? 90  ASN C CG  1 
ATOM   4116  O OD1 . ASN C  1 98  ? -20.938 33.107  54.471  1.00 20.36  ? 90  ASN C OD1 1 
ATOM   4117  N ND2 . ASN C  1 98  ? -21.765 32.775  56.539  1.00 17.01  ? 90  ASN C ND2 1 
ATOM   4118  N N   . ALA C  1 99  ? -17.100 31.501  55.288  1.00 12.51  ? 91  ALA C N   1 
ATOM   4119  C CA  . ALA C  1 99  ? -16.578 30.196  55.643  1.00 11.95  ? 91  ALA C CA  1 
ATOM   4120  C C   . ALA C  1 99  ? -15.484 30.396  56.659  1.00 13.39  ? 91  ALA C C   1 
ATOM   4121  O O   . ALA C  1 99  ? -14.723 31.338  56.551  1.00 10.74  ? 91  ALA C O   1 
ATOM   4122  C CB  . ALA C  1 99  ? -16.031 29.504  54.433  1.00 15.82  ? 91  ALA C CB  1 
ATOM   4123  N N   . ILE C  1 100 ? -15.411 29.524  57.661  1.00 17.07  ? 92  ILE C N   1 
ATOM   4124  C CA  . ILE C  1 100 ? -14.388 29.668  58.694  1.00 14.43  ? 92  ILE C CA  1 
ATOM   4125  C C   . ILE C  1 100 ? -13.462 28.454  58.730  1.00 16.14  ? 92  ILE C C   1 
ATOM   4126  O O   . ILE C  1 100 ? -12.584 28.348  59.586  1.00 17.23  ? 92  ILE C O   1 
ATOM   4127  C CB  . ILE C  1 100 ? -15.006 29.951  60.077  1.00 17.27  ? 92  ILE C CB  1 
ATOM   4128  C CG1 . ILE C  1 100 ? -15.880 28.776  60.524  1.00 20.26  ? 92  ILE C CG1 1 
ATOM   4129  C CG2 . ILE C  1 100 ? -15.814 31.256  60.046  1.00 13.32  ? 92  ILE C CG2 1 
ATOM   4130  C CD1 . ILE C  1 100 ? -16.587 28.996  61.838  1.00 15.13  ? 92  ILE C CD1 1 
ATOM   4131  N N   . SER C  1 101 ? -13.667 27.552  57.775  1.00 15.63  ? 93  SER C N   1 
ATOM   4132  C CA  . SER C  1 101 ? -12.774 26.427  57.529  1.00 12.04  ? 93  SER C CA  1 
ATOM   4133  C C   . SER C  1 101 ? -12.622 26.259  56.028  1.00 12.31  ? 93  SER C C   1 
ATOM   4134  O O   . SER C  1 101 ? -13.412 26.809  55.247  1.00 10.70  ? 93  SER C O   1 
ATOM   4135  C CB  . SER C  1 101 ? -13.351 25.135  58.116  1.00 17.61  ? 93  SER C CB  1 
ATOM   4136  O OG  . SER C  1 101 ? -14.398 24.601  57.299  1.00 16.74  ? 93  SER C OG  1 
ATOM   4137  N N   . LYS C  1 102 ? -11.609 25.494  55.630  1.00 13.80  ? 94  LYS C N   1 
ATOM   4138  C CA  . LYS C  1 102 ? -11.436 25.087  54.240  1.00 13.54  ? 94  LYS C CA  1 
ATOM   4139  C C   . LYS C  1 102 ? -12.590 24.175  53.863  1.00 15.21  ? 94  LYS C C   1 
ATOM   4140  O O   . LYS C  1 102 ? -13.031 23.360  54.671  1.00 17.09  ? 94  LYS C O   1 
ATOM   4141  C CB  . LYS C  1 102 ? -10.153 24.271  54.069  1.00 17.43  ? 94  LYS C CB  1 
ATOM   4142  C CG  . LYS C  1 102 ? -8.843  25.031  54.015  1.00 16.57  ? 94  LYS C CG  1 
ATOM   4143  C CD  . LYS C  1 102 ? -7.697  24.044  53.815  1.00 18.11  ? 94  LYS C CD  1 
ATOM   4144  C CE  . LYS C  1 102 ? -6.357  24.750  53.631  1.00 34.64  ? 94  LYS C CE  1 
ATOM   4145  N NZ  . LYS C  1 102 ? -5.232  24.074  54.373  1.00 38.90  ? 94  LYS C NZ  1 
ATOM   4146  N N   . PRO C  1 103 ? -13.069 24.282  52.625  1.00 13.74  ? 95  PRO C N   1 
ATOM   4147  C CA  . PRO C  1 103 ? -14.060 23.326  52.132  1.00 11.67  ? 95  PRO C CA  1 
ATOM   4148  C C   . PRO C  1 103 ? -13.442 21.935  51.992  1.00 13.14  ? 95  PRO C C   1 
ATOM   4149  O O   . PRO C  1 103 ? -12.355 21.817  51.443  1.00 14.34  ? 95  PRO C O   1 
ATOM   4150  C CB  . PRO C  1 103 ? -14.402 23.881  50.757  1.00 12.71  ? 95  PRO C CB  1 
ATOM   4151  C CG  . PRO C  1 103 ? -13.196 24.637  50.351  1.00 12.79  ? 95  PRO C CG  1 
ATOM   4152  C CD  . PRO C  1 103 ? -12.641 25.235  51.592  1.00 11.45  ? 95  PRO C CD  1 
ATOM   4153  N N   . GLU C  1 104 ? -14.106 20.910  52.516  1.00 13.62  ? 96  GLU C N   1 
ATOM   4154  C CA  A GLU C  1 104 ? -13.623 19.540  52.400  0.40 13.68  ? 96  GLU C CA  1 
ATOM   4155  C CA  B GLU C  1 104 ? -13.623 19.538  52.407  0.60 13.62  ? 96  GLU C CA  1 
ATOM   4156  C C   . GLU C  1 104 ? -14.394 18.852  51.286  1.00 13.99  ? 96  GLU C C   1 
ATOM   4157  O O   . GLU C  1 104 ? -15.586 18.566  51.434  1.00 10.14  ? 96  GLU C O   1 
ATOM   4158  C CB  A GLU C  1 104 ? -13.797 18.771  53.716  0.40 12.97  ? 96  GLU C CB  1 
ATOM   4159  C CB  B GLU C  1 104 ? -13.795 18.775  53.732  0.60 12.79  ? 96  GLU C CB  1 
ATOM   4160  C CG  A GLU C  1 104 ? -12.648 18.935  54.710  0.40 17.31  ? 96  GLU C CG  1 
ATOM   4161  C CG  B GLU C  1 104 ? -13.263 17.338  53.725  0.60 14.16  ? 96  GLU C CG  1 
ATOM   4162  C CD  A GLU C  1 104 ? -13.053 18.648  56.166  0.40 25.50  ? 96  GLU C CD  1 
ATOM   4163  C CD  B GLU C  1 104 ? -13.562 16.535  55.009  0.60 20.93  ? 96  GLU C CD  1 
ATOM   4164  O OE1 A GLU C  1 104 ? -13.514 17.521  56.470  0.40 27.04  ? 96  GLU C OE1 1 
ATOM   4165  O OE1 B GLU C  1 104 ? -14.178 17.072  55.958  0.60 27.17  ? 96  GLU C OE1 1 
ATOM   4166  O OE2 A GLU C  1 104 ? -12.907 19.559  57.012  0.40 25.95  ? 96  GLU C OE2 1 
ATOM   4167  O OE2 B GLU C  1 104 ? -13.178 15.345  55.079  0.60 23.05  ? 96  GLU C OE2 1 
ATOM   4168  N N   . VAL C  1 105 ? -13.716 18.598  50.162  1.00 11.80  ? 97  VAL C N   1 
ATOM   4169  C CA  . VAL C  1 105 ? -14.365 17.924  49.044  1.00 13.12  ? 97  VAL C CA  1 
ATOM   4170  C C   . VAL C  1 105 ? -14.428 16.428  49.364  1.00 12.28  ? 97  VAL C C   1 
ATOM   4171  O O   . VAL C  1 105 ? -13.401 15.802  49.655  1.00 11.00  ? 97  VAL C O   1 
ATOM   4172  C CB  . VAL C  1 105 ? -13.638 18.196  47.687  1.00 14.19  ? 97  VAL C CB  1 
ATOM   4173  C CG1 . VAL C  1 105 ? -14.459 17.682  46.526  1.00 12.90  ? 97  VAL C CG1 1 
ATOM   4174  C CG2 . VAL C  1 105 ? -13.397 19.670  47.507  1.00 12.20  ? 97  VAL C CG2 1 
ATOM   4175  N N   . LEU C  1 106 ? -15.632 15.862  49.339  1.00 9.11   ? 98  LEU C N   1 
ATOM   4176  C CA  . LEU C  1 106 ? -15.811 14.472  49.749  1.00 10.35  ? 98  LEU C CA  1 
ATOM   4177  C C   . LEU C  1 106 ? -16.037 13.545  48.564  1.00 12.18  ? 98  LEU C C   1 
ATOM   4178  O O   . LEU C  1 106 ? -16.325 12.357  48.742  1.00 12.93  ? 98  LEU C O   1 
ATOM   4179  C CB  . LEU C  1 106 ? -16.986 14.341  50.721  1.00 10.76  ? 98  LEU C CB  1 
ATOM   4180  C CG  . LEU C  1 106 ? -16.981 15.293  51.911  1.00 11.23  ? 98  LEU C CG  1 
ATOM   4181  C CD1 . LEU C  1 106 ? -18.332 15.305  52.552  1.00 10.50  ? 98  LEU C CD1 1 
ATOM   4182  C CD2 . LEU C  1 106 ? -15.901 14.945  52.902  1.00 11.20  ? 98  LEU C CD2 1 
ATOM   4183  N N   . THR C  1 107 ? -15.922 14.094  47.356  1.00 12.10  ? 99  THR C N   1 
ATOM   4184  C CA  . THR C  1 107 ? -16.174 13.329  46.145  1.00 9.17   ? 99  THR C CA  1 
ATOM   4185  C C   . THR C  1 107 ? -14.996 13.413  45.158  1.00 8.66   ? 99  THR C C   1 
ATOM   4186  O O   . THR C  1 107 ? -14.122 14.282  45.298  1.00 4.82   ? 99  THR C O   1 
ATOM   4187  C CB  . THR C  1 107 ? -17.462 13.791  45.492  1.00 10.31  ? 99  THR C CB  1 
ATOM   4188  O OG1 . THR C  1 107 ? -17.421 15.216  45.341  1.00 10.80  ? 99  THR C OG1 1 
ATOM   4189  C CG2 . THR C  1 107 ? -18.650 13.377  46.362  1.00 14.78  ? 99  THR C CG2 1 
ATOM   4190  N N   . PRO C  1 108 ? -14.951 12.478  44.184  1.00 7.74   ? 100 PRO C N   1 
ATOM   4191  C CA  . PRO C  1 108 ? -13.836 12.533  43.243  1.00 7.07   ? 100 PRO C CA  1 
ATOM   4192  C C   . PRO C  1 108 ? -13.965 13.820  42.436  1.00 8.37   ? 100 PRO C C   1 
ATOM   4193  O O   . PRO C  1 108 ? -15.086 14.236  42.126  1.00 6.09   ? 100 PRO C O   1 
ATOM   4194  C CB  . PRO C  1 108 ? -14.064 11.301  42.366  1.00 7.29   ? 100 PRO C CB  1 
ATOM   4195  C CG  . PRO C  1 108 ? -14.944 10.397  43.191  1.00 8.02   ? 100 PRO C CG  1 
ATOM   4196  C CD  . PRO C  1 108 ? -15.851 11.346  43.888  1.00 6.76   ? 100 PRO C CD  1 
ATOM   4197  N N   . GLN C  1 109 ? -12.831 14.454  42.141  1.00 6.42   ? 101 GLN C N   1 
ATOM   4198  C CA  . GLN C  1 109 ? -12.813 15.774  41.539  1.00 4.87   ? 101 GLN C CA  1 
ATOM   4199  C C   . GLN C  1 109 ? -12.963 15.675  40.032  1.00 7.16   ? 101 GLN C C   1 
ATOM   4200  O O   . GLN C  1 109 ? -11.983 15.804  39.289  1.00 7.23   ? 101 GLN C O   1 
ATOM   4201  C CB  . GLN C  1 109 ? -11.494 16.446  41.864  1.00 6.15   ? 101 GLN C CB  1 
ATOM   4202  C CG  . GLN C  1 109 ? -11.202 16.584  43.337  1.00 8.40   ? 101 GLN C CG  1 
ATOM   4203  C CD  . GLN C  1 109 ? -11.718 17.899  43.909  1.00 17.50  ? 101 GLN C CD  1 
ATOM   4204  O OE1 . GLN C  1 109 ? -12.859 18.315  43.644  1.00 16.45  ? 101 GLN C OE1 1 
ATOM   4205  N NE2 . GLN C  1 109 ? -10.868 18.573  44.683  1.00 17.26  ? 101 GLN C NE2 1 
ATOM   4206  N N   . LEU C  1 110 ? -14.181 15.434  39.566  1.00 5.80   ? 102 LEU C N   1 
ATOM   4207  C CA  . LEU C  1 110 ? -14.374 15.257  38.135  1.00 8.57   ? 102 LEU C CA  1 
ATOM   4208  C C   . LEU C  1 110 ? -15.472 16.162  37.633  1.00 7.27   ? 102 LEU C C   1 
ATOM   4209  O O   . LEU C  1 110 ? -16.474 16.353  38.294  1.00 7.62   ? 102 LEU C O   1 
ATOM   4210  C CB  . LEU C  1 110 ? -14.682 13.793  37.793  1.00 9.78   ? 102 LEU C CB  1 
ATOM   4211  C CG  . LEU C  1 110 ? -13.586 12.749  38.018  1.00 6.72   ? 102 LEU C CG  1 
ATOM   4212  C CD1 . LEU C  1 110 ? -14.156 11.365  37.852  1.00 7.59   ? 102 LEU C CD1 1 
ATOM   4213  C CD2 . LEU C  1 110 ? -12.519 12.968  36.995  1.00 9.36   ? 102 LEU C CD2 1 
ATOM   4214  N N   . ALA C  1 111 ? -15.276 16.748  36.466  1.00 6.34   ? 103 ALA C N   1 
ATOM   4215  C CA  . ALA C  1 111 ? -16.327 17.572  35.908  1.00 7.18   ? 103 ALA C CA  1 
ATOM   4216  C C   . ALA C  1 111 ? -16.932 16.797  34.758  1.00 7.72   ? 103 ALA C C   1 
ATOM   4217  O O   . ALA C  1 111 ? -16.400 15.766  34.342  1.00 8.74   ? 103 ALA C O   1 
ATOM   4218  C CB  . ALA C  1 111 ? -15.774 18.901  35.440  1.00 6.11   ? 103 ALA C CB  1 
ATOM   4219  N N   . ARG C  1 112 ? -18.060 17.260  34.260  1.00 5.99   ? 104 ARG C N   1 
ATOM   4220  C CA  . ARG C  1 112 ? -18.595 16.688  33.050  1.00 6.75   ? 104 ARG C CA  1 
ATOM   4221  C C   . ARG C  1 112 ? -18.522 17.771  31.993  1.00 6.86   ? 104 ARG C C   1 
ATOM   4222  O O   . ARG C  1 112 ? -18.802 18.936  32.258  1.00 5.96   ? 104 ARG C O   1 
ATOM   4223  C CB  . ARG C  1 112 ? -20.027 16.192  33.262  1.00 9.77   ? 104 ARG C CB  1 
ATOM   4224  C CG  . ARG C  1 112 ? -20.148 15.086  34.296  1.00 8.71   ? 104 ARG C CG  1 
ATOM   4225  C CD  . ARG C  1 112 ? -19.740 13.734  33.722  1.00 8.21   ? 104 ARG C CD  1 
ATOM   4226  N NE  . ARG C  1 112 ? -20.696 13.254  32.732  1.00 9.67   ? 104 ARG C NE  1 
ATOM   4227  C CZ  . ARG C  1 112 ? -20.615 12.077  32.111  1.00 13.02  ? 104 ARG C CZ  1 
ATOM   4228  N NH1 . ARG C  1 112 ? -19.605 11.253  32.375  1.00 9.66   ? 104 ARG C NH1 1 
ATOM   4229  N NH2 . ARG C  1 112 ? -21.542 11.721  31.222  1.00 11.99  ? 104 ARG C NH2 1 
ATOM   4230  N N   . VAL C  1 113 ? -18.090 17.396  30.801  1.00 6.27   ? 105 VAL C N   1 
ATOM   4231  C CA  . VAL C  1 113 ? -18.072 18.340  29.709  1.00 7.70   ? 105 VAL C CA  1 
ATOM   4232  C C   . VAL C  1 113 ? -19.113 17.831  28.738  1.00 9.36   ? 105 VAL C C   1 
ATOM   4233  O O   . VAL C  1 113 ? -19.158 16.638  28.450  1.00 10.89  ? 105 VAL C O   1 
ATOM   4234  C CB  . VAL C  1 113 ? -16.657 18.450  29.078  1.00 7.77   ? 105 VAL C CB  1 
ATOM   4235  C CG1 . VAL C  1 113 ? -16.648 19.390  27.888  1.00 6.79   ? 105 VAL C CG1 1 
ATOM   4236  C CG2 . VAL C  1 113 ? -15.675 18.944  30.118  1.00 9.15   ? 105 VAL C CG2 1 
ATOM   4237  N N   . VAL C  1 114 ? -19.985 18.716  28.276  1.00 8.70   ? 106 VAL C N   1 
ATOM   4238  C CA  . VAL C  1 114 ? -20.960 18.334  27.255  1.00 13.58  ? 106 VAL C CA  1 
ATOM   4239  C C   . VAL C  1 114 ? -20.550 18.850  25.874  1.00 11.60  ? 106 VAL C C   1 
ATOM   4240  O O   . VAL C  1 114 ? -19.936 19.908  25.763  1.00 10.26  ? 106 VAL C O   1 
ATOM   4241  C CB  . VAL C  1 114 ? -22.363 18.869  27.597  1.00 13.61  ? 106 VAL C CB  1 
ATOM   4242  C CG1 . VAL C  1 114 ? -23.411 18.100  26.835  1.00 11.50  ? 106 VAL C CG1 1 
ATOM   4243  C CG2 . VAL C  1 114 ? -22.604 18.757  29.070  1.00 11.06  ? 106 VAL C CG2 1 
ATOM   4244  N N   . SER C  1 115 ? -20.921 18.118  24.825  1.00 12.54  ? 107 SER C N   1 
ATOM   4245  C CA  . SER C  1 115 ? -20.475 18.422  23.463  1.00 13.87  ? 107 SER C CA  1 
ATOM   4246  C C   . SER C  1 115 ? -20.798 19.836  22.968  1.00 14.30  ? 107 SER C C   1 
ATOM   4247  O O   . SER C  1 115 ? -20.189 20.312  22.004  1.00 14.59  ? 107 SER C O   1 
ATOM   4248  C CB  . SER C  1 115 ? -20.978 17.373  22.464  1.00 16.52  ? 107 SER C CB  1 
ATOM   4249  O OG  . SER C  1 115 ? -22.317 16.972  22.739  1.00 19.36  ? 107 SER C OG  1 
ATOM   4250  N N   . ASP C  1 116 ? -21.740 20.501  23.626  1.00 10.90  ? 108 ASP C N   1 
ATOM   4251  C CA  . ASP C  1 116 ? -22.140 21.843  23.230  1.00 10.25  ? 108 ASP C CA  1 
ATOM   4252  C C   . ASP C  1 116 ? -21.372 22.919  23.988  1.00 16.58  ? 108 ASP C C   1 
ATOM   4253  O O   . ASP C  1 116 ? -21.744 24.094  23.938  1.00 22.64  ? 108 ASP C O   1 
ATOM   4254  C CB  . ASP C  1 116 ? -23.636 22.047  23.444  1.00 12.48  ? 108 ASP C CB  1 
ATOM   4255  C CG  . ASP C  1 116 ? -24.011 22.153  24.929  1.00 24.41  ? 108 ASP C CG  1 
ATOM   4256  O OD1 . ASP C  1 116 ? -23.256 21.614  25.775  1.00 22.71  ? 108 ASP C OD1 1 
ATOM   4257  O OD2 . ASP C  1 116 ? -25.058 22.772  25.252  1.00 27.94  ? 108 ASP C OD2 1 
ATOM   4258  N N   . GLY C  1 117 ? -20.319 22.518  24.699  1.00 12.48  ? 109 GLY C N   1 
ATOM   4259  C CA  . GLY C  1 117 ? -19.511 23.455  25.460  1.00 11.63  ? 109 GLY C CA  1 
ATOM   4260  C C   . GLY C  1 117 ? -19.871 23.650  26.925  1.00 11.63  ? 109 GLY C C   1 
ATOM   4261  O O   . GLY C  1 117 ? -19.160 24.348  27.646  1.00 10.85  ? 109 GLY C O   1 
ATOM   4262  N N   . GLU C  1 118 ? -20.968 23.049  27.382  1.00 15.25  ? 110 GLU C N   1 
ATOM   4263  C CA  . GLU C  1 118 ? -21.372 23.212  28.782  1.00 13.07  ? 110 GLU C CA  1 
ATOM   4264  C C   . GLU C  1 118 ? -20.533 22.350  29.722  1.00 14.52  ? 110 GLU C C   1 
ATOM   4265  O O   . GLU C  1 118 ? -20.294 21.158  29.453  1.00 12.18  ? 110 GLU C O   1 
ATOM   4266  C CB  . GLU C  1 118 ? -22.850 22.907  28.986  1.00 13.98  ? 110 GLU C CB  1 
ATOM   4267  C CG  . GLU C  1 118 ? -23.355 23.271  30.385  1.00 16.51  ? 110 GLU C CG  1 
ATOM   4268  C CD  . GLU C  1 118 ? -24.748 22.732  30.683  1.00 21.38  ? 110 GLU C CD  1 
ATOM   4269  O OE1 . GLU C  1 118 ? -25.288 23.013  31.779  1.00 26.43  ? 110 GLU C OE1 1 
ATOM   4270  O OE2 . GLU C  1 118 ? -25.304 22.022  29.819  1.00 31.01  ? 110 GLU C OE2 1 
ATOM   4271  N N   . VAL C  1 119 ? -20.088 22.973  30.816  1.00 11.31  ? 111 VAL C N   1 
ATOM   4272  C CA  . VAL C  1 119 ? -19.275 22.322  31.832  1.00 7.79   ? 111 VAL C CA  1 
ATOM   4273  C C   . VAL C  1 119 ? -20.018 22.282  33.157  1.00 11.99  ? 111 VAL C C   1 
ATOM   4274  O O   . VAL C  1 119 ? -20.457 23.310  33.678  1.00 11.33  ? 111 VAL C O   1 
ATOM   4275  C CB  . VAL C  1 119 ? -17.967 23.076  32.081  1.00 10.91  ? 111 VAL C CB  1 
ATOM   4276  C CG1 . VAL C  1 119 ? -17.162 22.364  33.186  1.00 8.59   ? 111 VAL C CG1 1 
ATOM   4277  C CG2 . VAL C  1 119 ? -17.168 23.239  30.783  1.00 6.11   ? 111 VAL C CG2 1 
ATOM   4278  N N   . LEU C  1 120 ? -20.132 21.078  33.702  1.00 14.56  ? 112 LEU C N   1 
ATOM   4279  C CA  . LEU C  1 120 ? -20.885 20.816  34.909  1.00 8.28   ? 112 LEU C CA  1 
ATOM   4280  C C   . LEU C  1 120 ? -19.934 20.253  35.943  1.00 8.94   ? 112 LEU C C   1 
ATOM   4281  O O   . LEU C  1 120 ? -19.302 19.238  35.712  1.00 9.93   ? 112 LEU C O   1 
ATOM   4282  C CB  . LEU C  1 120 ? -21.949 19.781  34.598  1.00 9.10   ? 112 LEU C CB  1 
ATOM   4283  C CG  . LEU C  1 120 ? -22.639 20.036  33.259  1.00 12.43  ? 112 LEU C CG  1 
ATOM   4284  C CD1 . LEU C  1 120 ? -23.084 18.733  32.662  1.00 16.48  ? 112 LEU C CD1 1 
ATOM   4285  C CD2 . LEU C  1 120 ? -23.821 20.933  33.467  1.00 17.16  ? 112 LEU C CD2 1 
ATOM   4286  N N   . TYR C  1 121 ? -19.824 20.919  37.083  1.00 9.23   ? 113 TYR C N   1 
ATOM   4287  C CA  . TYR C  1 121 ? -18.995 20.429  38.164  1.00 8.14   ? 113 TYR C CA  1 
ATOM   4288  C C   . TYR C  1 121 ? -19.763 20.534  39.480  1.00 11.91  ? 113 TYR C C   1 
ATOM   4289  O O   . TYR C  1 121 ? -20.177 21.633  39.871  1.00 11.19  ? 113 TYR C O   1 
ATOM   4290  C CB  . TYR C  1 121 ? -17.717 21.244  38.240  1.00 5.97   ? 113 TYR C CB  1 
ATOM   4291  C CG  . TYR C  1 121 ? -16.843 20.890  39.414  1.00 6.03   ? 113 TYR C CG  1 
ATOM   4292  C CD1 . TYR C  1 121 ? -16.393 19.588  39.596  1.00 6.28   ? 113 TYR C CD1 1 
ATOM   4293  C CD2 . TYR C  1 121 ? -16.446 21.865  40.332  1.00 5.84   ? 113 TYR C CD2 1 
ATOM   4294  C CE1 . TYR C  1 121 ? -15.582 19.260  40.662  1.00 7.80   ? 113 TYR C CE1 1 
ATOM   4295  C CE2 . TYR C  1 121 ? -15.636 21.555  41.406  1.00 5.29   ? 113 TYR C CE2 1 
ATOM   4296  C CZ  . TYR C  1 121 ? -15.206 20.250  41.570  1.00 9.24   ? 113 TYR C CZ  1 
ATOM   4297  O OH  . TYR C  1 121 ? -14.387 19.919  42.634  1.00 11.61  ? 113 TYR C OH  1 
ATOM   4298  N N   . MET C  1 122 ? -19.940 19.399  40.163  1.00 11.77  ? 114 MET C N   1 
ATOM   4299  C CA  . MET C  1 122 ? -20.730 19.352  41.396  1.00 7.84   ? 114 MET C CA  1 
ATOM   4300  C C   . MET C  1 122 ? -20.074 18.541  42.492  1.00 5.28   ? 114 MET C C   1 
ATOM   4301  O O   . MET C  1 122 ? -20.422 17.390  42.689  1.00 8.14   ? 114 MET C O   1 
ATOM   4302  C CB  . MET C  1 122 ? -22.111 18.754  41.121  1.00 9.36   ? 114 MET C CB  1 
ATOM   4303  C CG  . MET C  1 122 ? -23.106 18.987  42.273  1.00 16.54  ? 114 MET C CG  1 
ATOM   4304  S SD  . MET C  1 122 ? -24.769 18.260  42.113  1.00 34.91  ? 114 MET C SD  1 
ATOM   4305  C CE  . MET C  1 122 ? -24.460 16.508  42.335  1.00 16.81  ? 114 MET C CE  1 
ATOM   4306  N N   . PRO C  1 123 ? -19.135 19.134  43.224  1.00 4.23   ? 115 PRO C N   1 
ATOM   4307  C CA  . PRO C  1 123 ? -18.561 18.416  44.363  1.00 6.94   ? 115 PRO C CA  1 
ATOM   4308  C C   . PRO C  1 123 ? -19.479 18.403  45.607  1.00 11.17  ? 115 PRO C C   1 
ATOM   4309  O O   . PRO C  1 123 ? -20.398 19.224  45.775  1.00 7.17   ? 115 PRO C O   1 
ATOM   4310  C CB  . PRO C  1 123 ? -17.294 19.220  44.674  1.00 5.46   ? 115 PRO C CB  1 
ATOM   4311  C CG  . PRO C  1 123 ? -17.618 20.588  44.258  1.00 5.32   ? 115 PRO C CG  1 
ATOM   4312  C CD  . PRO C  1 123 ? -18.599 20.496  43.107  1.00 5.90   ? 115 PRO C CD  1 
ATOM   4313  N N   . SER C  1 124 ? -19.221 17.446  46.483  1.00 10.67  ? 116 SER C N   1 
ATOM   4314  C CA  . SER C  1 124 ? -19.876 17.434  47.767  1.00 11.07  ? 116 SER C CA  1 
ATOM   4315  C C   . SER C  1 124 ? -18.903 18.068  48.715  1.00 10.27  ? 116 SER C C   1 
ATOM   4316  O O   . SER C  1 124 ? -17.741 17.682  48.768  1.00 12.85  ? 116 SER C O   1 
ATOM   4317  C CB  . SER C  1 124 ? -20.192 16.015  48.215  1.00 12.67  ? 116 SER C CB  1 
ATOM   4318  O OG  . SER C  1 124 ? -21.060 16.033  49.336  1.00 15.54  ? 116 SER C OG  1 
ATOM   4319  N N   . ILE C  1 125 ? -19.373 19.054  49.460  1.00 12.41  ? 117 ILE C N   1 
ATOM   4320  C CA  . ILE C  1 125 ? -18.511 19.791  50.362  1.00 10.73  ? 117 ILE C CA  1 
ATOM   4321  C C   . ILE C  1 125 ? -19.014 19.797  51.813  1.00 13.23  ? 117 ILE C C   1 
ATOM   4322  O O   . ILE C  1 125 ? -20.205 19.983  52.088  1.00 12.54  ? 117 ILE C O   1 
ATOM   4323  C CB  . ILE C  1 125 ? -18.352 21.223  49.868  1.00 8.35   ? 117 ILE C CB  1 
ATOM   4324  C CG1 . ILE C  1 125 ? -17.761 21.217  48.456  1.00 8.14   ? 117 ILE C CG1 1 
ATOM   4325  C CG2 . ILE C  1 125 ? -17.492 22.020  50.823  1.00 10.47  ? 117 ILE C CG2 1 
ATOM   4326  C CD1 . ILE C  1 125 ? -17.592 22.580  47.854  1.00 7.49   ? 117 ILE C CD1 1 
ATOM   4327  N N   . ARG C  1 126 ? -18.094 19.579  52.738  1.00 12.39  ? 118 ARG C N   1 
ATOM   4328  C CA  . ARG C  1 126 ? -18.369 19.839  54.131  1.00 13.16  ? 118 ARG C CA  1 
ATOM   4329  C C   . ARG C  1 126 ? -17.513 21.012  54.597  1.00 13.20  ? 118 ARG C C   1 
ATOM   4330  O O   . ARG C  1 126 ? -16.290 20.966  54.519  1.00 14.91  ? 118 ARG C O   1 
ATOM   4331  C CB  . ARG C  1 126 ? -18.080 18.599  54.978  1.00 17.65  ? 118 ARG C CB  1 
ATOM   4332  C CG  . ARG C  1 126 ? -18.506 18.720  56.441  1.00 14.24  ? 118 ARG C CG  1 
ATOM   4333  C CD  . ARG C  1 126 ? -17.653 17.835  57.265  1.00 13.82  ? 118 ARG C CD  1 
ATOM   4334  N NE  . ARG C  1 126 ? -17.865 18.035  58.685  1.00 29.51  ? 118 ARG C NE  1 
ATOM   4335  C CZ  . ARG C  1 126 ? -18.259 17.078  59.519  1.00 28.92  ? 118 ARG C CZ  1 
ATOM   4336  N NH1 . ARG C  1 126 ? -18.498 15.859  59.048  1.00 24.94  ? 118 ARG C NH1 1 
ATOM   4337  N NH2 . ARG C  1 126 ? -18.421 17.336  60.816  1.00 25.24  ? 118 ARG C NH2 1 
ATOM   4338  N N   . GLN C  1 127 ? -18.167 22.043  55.119  1.00 13.61  ? 119 GLN C N   1 
ATOM   4339  C CA  . GLN C  1 127 ? -17.502 23.276  55.504  1.00 14.20  ? 119 GLN C CA  1 
ATOM   4340  C C   . GLN C  1 127 ? -18.199 23.875  56.748  1.00 15.57  ? 119 GLN C C   1 
ATOM   4341  O O   . GLN C  1 127 ? -19.396 23.687  56.951  1.00 10.16  ? 119 GLN C O   1 
ATOM   4342  C CB  . GLN C  1 127 ? -17.548 24.246  54.314  1.00 10.01  ? 119 GLN C CB  1 
ATOM   4343  C CG  . GLN C  1 127 ? -16.636 25.445  54.399  1.00 12.56  ? 119 GLN C CG  1 
ATOM   4344  C CD  . GLN C  1 127 ? -16.320 26.032  53.020  1.00 14.87  ? 119 GLN C CD  1 
ATOM   4345  O OE1 . GLN C  1 127 ? -17.094 25.867  52.070  1.00 15.71  ? 119 GLN C OE1 1 
ATOM   4346  N NE2 . GLN C  1 127 ? -15.169 26.700  52.901  1.00 11.78  ? 119 GLN C NE2 1 
ATOM   4347  N N   . ARG C  1 128 ? -17.430 24.574  57.576  1.00 15.93  ? 120 ARG C N   1 
ATOM   4348  C CA  . ARG C  1 128 ? -17.964 25.332  58.694  1.00 14.35  ? 120 ARG C CA  1 
ATOM   4349  C C   . ARG C  1 128 ? -18.193 26.805  58.334  1.00 16.93  ? 120 ARG C C   1 
ATOM   4350  O O   . ARG C  1 128 ? -17.447 27.393  57.548  1.00 17.71  ? 120 ARG C O   1 
ATOM   4351  C CB  . ARG C  1 128 ? -17.029 25.229  59.909  1.00 23.01  ? 120 ARG C CB  1 
ATOM   4352  C CG  . ARG C  1 128 ? -17.427 24.140  60.928  1.00 30.60  ? 120 ARG C CG  1 
ATOM   4353  C CD  . ARG C  1 128 ? -16.504 24.085  62.152  1.00 34.26  ? 120 ARG C CD  1 
ATOM   4354  N NE  . ARG C  1 128 ? -15.095 23.919  61.787  1.00 44.64  ? 120 ARG C NE  1 
ATOM   4355  C CZ  . ARG C  1 128 ? -14.565 22.811  61.265  1.00 45.71  ? 120 ARG C CZ  1 
ATOM   4356  N NH1 . ARG C  1 128 ? -15.318 21.739  61.025  1.00 49.01  ? 120 ARG C NH1 1 
ATOM   4357  N NH2 . ARG C  1 128 ? -13.273 22.780  60.970  1.00 38.47  ? 120 ARG C NH2 1 
ATOM   4358  N N   . PHE C  1 129 ? -19.213 27.410  58.933  1.00 19.30  ? 121 PHE C N   1 
ATOM   4359  C CA  . PHE C  1 129 ? -19.539 28.805  58.654  1.00 16.54  ? 121 PHE C CA  1 
ATOM   4360  C C   . PHE C  1 129 ? -19.817 29.651  59.886  1.00 18.57  ? 121 PHE C C   1 
ATOM   4361  O O   . PHE C  1 129 ? -20.185 29.142  60.947  1.00 18.95  ? 121 PHE C O   1 
ATOM   4362  C CB  . PHE C  1 129 ? -20.764 28.886  57.756  1.00 18.18  ? 121 PHE C CB  1 
ATOM   4363  C CG  . PHE C  1 129 ? -20.542 28.342  56.391  1.00 17.48  ? 121 PHE C CG  1 
ATOM   4364  C CD1 . PHE C  1 129 ? -20.823 27.014  56.108  1.00 15.51  ? 121 PHE C CD1 1 
ATOM   4365  C CD2 . PHE C  1 129 ? -20.057 29.157  55.383  1.00 13.56  ? 121 PHE C CD2 1 
ATOM   4366  C CE1 . PHE C  1 129 ? -20.615 26.509  54.840  1.00 14.18  ? 121 PHE C CE1 1 
ATOM   4367  C CE2 . PHE C  1 129 ? -19.851 28.655  54.120  1.00 13.24  ? 121 PHE C CE2 1 
ATOM   4368  C CZ  . PHE C  1 129 ? -20.132 27.330  53.846  1.00 10.74  ? 121 PHE C CZ  1 
ATOM   4369  N N   . SER C  1 130 ? -19.653 30.958  59.708  1.00 19.29  ? 122 SER C N   1 
ATOM   4370  C CA  . SER C  1 130 ? -20.073 31.960  60.677  1.00 16.04  ? 122 SER C CA  1 
ATOM   4371  C C   . SER C  1 130 ? -21.329 32.667  60.161  1.00 19.54  ? 122 SER C C   1 
ATOM   4372  O O   . SER C  1 130 ? -21.280 33.378  59.154  1.00 22.85  ? 122 SER C O   1 
ATOM   4373  C CB  . SER C  1 130 ? -18.960 32.974  60.883  1.00 13.61  ? 122 SER C CB  1 
ATOM   4374  O OG  . SER C  1 130 ? -19.394 34.077  61.653  1.00 15.16  ? 122 SER C OG  1 
ATOM   4375  N N   . CYS C  1 131 ? -22.441 32.480  60.861  1.00 16.47  ? 123 CYS C N   1 
ATOM   4376  C CA  . CYS C  1 131 ? -23.727 33.039  60.463  1.00 19.53  ? 123 CYS C CA  1 
ATOM   4377  C C   . CYS C  1 131 ? -24.763 32.948  61.607  1.00 26.19  ? 123 CYS C C   1 
ATOM   4378  O O   . CYS C  1 131 ? -24.484 32.382  62.679  1.00 18.29  ? 123 CYS C O   1 
ATOM   4379  C CB  . CYS C  1 131 ? -24.243 32.284  59.255  1.00 25.29  ? 123 CYS C CB  1 
ATOM   4380  S SG  . CYS C  1 131 ? -24.010 30.496  59.410  1.00 38.14  ? 123 CYS C SG  1 
ATOM   4381  N N   . ASP C  1 132 ? -25.967 33.473  61.371  1.00 27.54  ? 124 ASP C N   1 
ATOM   4382  C CA  . ASP C  1 132 ? -26.940 33.630  62.460  1.00 24.65  ? 124 ASP C CA  1 
ATOM   4383  C C   . ASP C  1 132 ? -27.677 32.348  62.819  1.00 23.51  ? 124 ASP C C   1 
ATOM   4384  O O   . ASP C  1 132 ? -28.486 31.833  62.049  1.00 23.52  ? 124 ASP C O   1 
ATOM   4385  C CB  . ASP C  1 132 ? -27.938 34.760  62.187  1.00 24.88  ? 124 ASP C CB  1 
ATOM   4386  C CG  . ASP C  1 132 ? -28.774 35.115  63.422  1.00 27.56  ? 124 ASP C CG  1 
ATOM   4387  O OD1 . ASP C  1 132 ? -28.351 34.797  64.553  1.00 27.39  ? 124 ASP C OD1 1 
ATOM   4388  O OD2 . ASP C  1 132 ? -29.854 35.714  63.262  1.00 25.77  ? 124 ASP C OD2 1 
ATOM   4389  N N   . VAL C  1 133 ? -27.408 31.880  64.028  1.00 22.05  ? 125 VAL C N   1 
ATOM   4390  C CA  . VAL C  1 133 ? -27.924 30.620  64.524  1.00 26.59  ? 125 VAL C CA  1 
ATOM   4391  C C   . VAL C  1 133 ? -29.071 30.823  65.549  1.00 30.10  ? 125 VAL C C   1 
ATOM   4392  O O   . VAL C  1 133 ? -29.819 29.896  65.847  1.00 27.27  ? 125 VAL C O   1 
ATOM   4393  C CB  . VAL C  1 133 ? -26.739 29.803  65.100  1.00 22.39  ? 125 VAL C CB  1 
ATOM   4394  C CG1 . VAL C  1 133 ? -27.192 28.697  66.043  1.00 24.54  ? 125 VAL C CG1 1 
ATOM   4395  C CG2 . VAL C  1 133 ? -25.901 29.247  63.962  1.00 23.82  ? 125 VAL C CG2 1 
ATOM   4396  N N   . SER C  1 134 ? -29.220 32.047  66.055  1.00 24.00  ? 126 SER C N   1 
ATOM   4397  C CA  . SER C  1 134 ? -30.266 32.363  67.026  1.00 31.25  ? 126 SER C CA  1 
ATOM   4398  C C   . SER C  1 134 ? -31.650 31.915  66.564  1.00 30.60  ? 126 SER C C   1 
ATOM   4399  O O   . SER C  1 134 ? -31.948 31.951  65.370  1.00 29.01  ? 126 SER C O   1 
ATOM   4400  C CB  . SER C  1 134 ? -30.301 33.863  67.295  1.00 32.54  ? 126 SER C CB  1 
ATOM   4401  O OG  . SER C  1 134 ? -30.727 34.545  66.131  1.00 43.73  ? 126 SER C OG  1 
ATOM   4402  N N   . GLY C  1 135 ? -32.483 31.482  67.511  1.00 26.89  ? 127 GLY C N   1 
ATOM   4403  C CA  . GLY C  1 135 ? -33.835 31.046  67.203  1.00 24.57  ? 127 GLY C CA  1 
ATOM   4404  C C   . GLY C  1 135 ? -33.936 29.661  66.585  1.00 28.09  ? 127 GLY C C   1 
ATOM   4405  O O   . GLY C  1 135 ? -34.978 29.279  66.042  1.00 23.71  ? 127 GLY C O   1 
ATOM   4406  N N   . VAL C  1 136 ? -32.850 28.899  66.671  1.00 27.89  ? 128 VAL C N   1 
ATOM   4407  C CA  . VAL C  1 136 ? -32.792 27.592  66.032  1.00 26.56  ? 128 VAL C CA  1 
ATOM   4408  C C   . VAL C  1 136 ? -33.734 26.589  66.704  1.00 29.78  ? 128 VAL C C   1 
ATOM   4409  O O   . VAL C  1 136 ? -34.349 25.762  66.028  1.00 27.31  ? 128 VAL C O   1 
ATOM   4410  C CB  . VAL C  1 136 ? -31.331 27.053  65.948  1.00 31.90  ? 128 VAL C CB  1 
ATOM   4411  C CG1 . VAL C  1 136 ? -30.707 26.912  67.329  1.00 31.13  ? 128 VAL C CG1 1 
ATOM   4412  C CG2 . VAL C  1 136 ? -31.263 25.738  65.152  1.00 28.67  ? 128 VAL C CG2 1 
ATOM   4413  N N   . ASP C  1 137 ? -33.867 26.686  68.026  1.00 32.22  ? 129 ASP C N   1 
ATOM   4414  C CA  . ASP C  1 137 ? -34.782 25.817  68.760  1.00 30.68  ? 129 ASP C CA  1 
ATOM   4415  C C   . ASP C  1 137 ? -36.256 26.149  68.491  1.00 30.44  ? 129 ASP C C   1 
ATOM   4416  O O   . ASP C  1 137 ? -37.114 25.275  68.572  1.00 41.46  ? 129 ASP C O   1 
ATOM   4417  C CB  . ASP C  1 137 ? -34.491 25.863  70.261  1.00 32.53  ? 129 ASP C CB  1 
ATOM   4418  C CG  . ASP C  1 137 ? -33.105 25.356  70.605  1.00 37.32  ? 129 ASP C CG  1 
ATOM   4419  O OD1 . ASP C  1 137 ? -32.754 24.256  70.143  1.00 39.48  ? 129 ASP C OD1 1 
ATOM   4420  O OD2 . ASP C  1 137 ? -32.366 26.057  71.334  1.00 45.39  ? 129 ASP C OD2 1 
ATOM   4421  N N   . THR C  1 138 ? -36.519 27.410  68.139  1.00 26.32  ? 130 THR C N   1 
ATOM   4422  C CA  . THR C  1 138 ? -37.871 27.946  67.901  1.00 26.38  ? 130 THR C CA  1 
ATOM   4423  C C   . THR C  1 138 ? -38.537 27.465  66.604  1.00 25.46  ? 130 THR C C   1 
ATOM   4424  O O   . THR C  1 138 ? -37.856 27.011  65.684  1.00 30.11  ? 130 THR C O   1 
ATOM   4425  C CB  . THR C  1 138 ? -37.871 29.487  67.916  1.00 27.35  ? 130 THR C CB  1 
ATOM   4426  O OG1 . THR C  1 138 ? -37.540 29.981  66.611  1.00 27.28  ? 130 THR C OG1 1 
ATOM   4427  C CG2 . THR C  1 138 ? -36.859 30.011  68.923  1.00 25.02  ? 130 THR C CG2 1 
ATOM   4428  N N   . GLU C  1 139 ? -39.868 27.554  66.540  1.00 26.70  ? 131 GLU C N   1 
ATOM   4429  C CA  . GLU C  1 139 ? -40.613 26.963  65.436  1.00 30.00  ? 131 GLU C CA  1 
ATOM   4430  C C   . GLU C  1 139 ? -40.243 27.579  64.089  1.00 35.52  ? 131 GLU C C   1 
ATOM   4431  O O   . GLU C  1 139 ? -40.206 26.886  63.066  1.00 31.70  ? 131 GLU C O   1 
ATOM   4432  C CB  . GLU C  1 139 ? -42.124 27.080  65.640  1.00 30.55  ? 131 GLU C CB  1 
ATOM   4433  C CG  . GLU C  1 139 ? -42.917 26.375  64.526  1.00 38.45  ? 131 GLU C CG  1 
ATOM   4434  C CD  . GLU C  1 139 ? -44.404 26.711  64.516  1.00 53.51  ? 131 GLU C CD  1 
ATOM   4435  O OE1 . GLU C  1 139 ? -44.944 27.082  65.584  1.00 63.87  ? 131 GLU C OE1 1 
ATOM   4436  O OE2 . GLU C  1 139 ? -45.031 26.596  63.434  1.00 45.57  ? 131 GLU C OE2 1 
ATOM   4437  N N   . SER C  1 140 ? -39.991 28.885  64.078  1.00 34.46  ? 132 SER C N   1 
ATOM   4438  C CA  . SER C  1 140 ? -39.719 29.574  62.818  1.00 31.53  ? 132 SER C CA  1 
ATOM   4439  C C   . SER C  1 140 ? -38.228 29.541  62.443  1.00 27.63  ? 132 SER C C   1 
ATOM   4440  O O   . SER C  1 140 ? -37.874 29.770  61.290  1.00 25.52  ? 132 SER C O   1 
ATOM   4441  C CB  . SER C  1 140 ? -40.283 30.996  62.842  1.00 26.59  ? 132 SER C CB  1 
ATOM   4442  O OG  . SER C  1 140 ? -40.070 31.587  64.110  1.00 37.62  ? 132 SER C OG  1 
ATOM   4443  N N   . GLY C  1 141 ? -37.374 29.257  63.426  1.00 24.99  ? 133 GLY C N   1 
ATOM   4444  C CA  . GLY C  1 141 ? -36.008 28.824  63.183  1.00 21.20  ? 133 GLY C CA  1 
ATOM   4445  C C   . GLY C  1 141 ? -34.950 29.862  62.844  1.00 24.19  ? 133 GLY C C   1 
ATOM   4446  O O   . GLY C  1 141 ? -35.251 30.995  62.458  1.00 28.88  ? 133 GLY C O   1 
ATOM   4447  N N   . ALA C  1 142 ? -33.690 29.454  62.960  1.00 27.01  ? 134 ALA C N   1 
ATOM   4448  C CA  . ALA C  1 142 ? -32.569 30.301  62.569  1.00 25.77  ? 134 ALA C CA  1 
ATOM   4449  C C   . ALA C  1 142 ? -32.578 30.451  61.064  1.00 21.24  ? 134 ALA C C   1 
ATOM   4450  O O   . ALA C  1 142 ? -33.163 29.629  60.359  1.00 21.13  ? 134 ALA C O   1 
ATOM   4451  C CB  . ALA C  1 142 ? -31.255 29.699  63.026  1.00 24.18  ? 134 ALA C CB  1 
ATOM   4452  N N   . THR C  1 143 ? -31.970 31.523  60.576  1.00 19.76  ? 135 THR C N   1 
ATOM   4453  C CA  . THR C  1 143 ? -31.735 31.659  59.144  1.00 23.26  ? 135 THR C CA  1 
ATOM   4454  C C   . THR C  1 143 ? -30.267 31.962  58.902  1.00 24.02  ? 135 THR C C   1 
ATOM   4455  O O   . THR C  1 143 ? -29.826 33.092  59.079  1.00 26.07  ? 135 THR C O   1 
ATOM   4456  C CB  . THR C  1 143 ? -32.559 32.774  58.512  1.00 18.62  ? 135 THR C CB  1 
ATOM   4457  O OG1 . THR C  1 143 ? -33.942 32.529  58.742  1.00 15.88  ? 135 THR C OG1 1 
ATOM   4458  C CG2 . THR C  1 143 ? -32.319 32.799  57.009  1.00 26.45  ? 135 THR C CG2 1 
ATOM   4459  N N   . CYS C  1 144 ? -29.511 30.945  58.518  1.00 21.06  ? 136 CYS C N   1 
ATOM   4460  C CA  . CYS C  1 144 ? -28.101 31.123  58.223  1.00 23.76  ? 136 CYS C CA  1 
ATOM   4461  C C   . CYS C  1 144 ? -27.903 31.569  56.769  1.00 23.97  ? 136 CYS C C   1 
ATOM   4462  O O   . CYS C  1 144 ? -28.394 30.930  55.834  1.00 21.82  ? 136 CYS C O   1 
ATOM   4463  C CB  . CYS C  1 144 ? -27.342 29.827  58.499  1.00 22.79  ? 136 CYS C CB  1 
ATOM   4464  S SG  . CYS C  1 144 ? -25.610 29.886  57.997  1.00 49.76  ? 136 CYS C SG  1 
ATOM   4465  N N   . ARG C  1 145 ? -27.196 32.676  56.579  1.00 22.23  ? 137 ARG C N   1 
ATOM   4466  C CA  . ARG C  1 145 ? -26.940 33.166  55.227  1.00 25.82  ? 137 ARG C CA  1 
ATOM   4467  C C   . ARG C  1 145 ? -25.495 32.927  54.770  1.00 22.79  ? 137 ARG C C   1 
ATOM   4468  O O   . ARG C  1 145 ? -24.540 33.387  55.409  1.00 23.54  ? 137 ARG C O   1 
ATOM   4469  C CB  . ARG C  1 145 ? -27.328 34.643  55.106  1.00 26.54  ? 137 ARG C CB  1 
ATOM   4470  C CG  . ARG C  1 145 ? -28.787 34.909  55.462  1.00 30.05  ? 137 ARG C CG  1 
ATOM   4471  C CD  . ARG C  1 145 ? -29.239 36.296  55.036  1.00 32.34  ? 137 ARG C CD  1 
ATOM   4472  N NE  . ARG C  1 145 ? -30.213 36.856  55.969  1.00 37.67  ? 137 ARG C NE  1 
ATOM   4473  C CZ  . ARG C  1 145 ? -31.532 36.746  55.838  1.00 42.93  ? 137 ARG C CZ  1 
ATOM   4474  N NH1 . ARG C  1 145 ? -32.045 36.096  54.801  1.00 42.20  ? 137 ARG C NH1 1 
ATOM   4475  N NH2 . ARG C  1 145 ? -32.340 37.293  56.742  1.00 38.81  ? 137 ARG C NH2 1 
ATOM   4476  N N   . ILE C  1 146 ? -25.347 32.185  53.674  1.00 21.86  ? 138 ILE C N   1 
ATOM   4477  C CA  . ILE C  1 146 ? -24.030 31.934  53.073  1.00 23.67  ? 138 ILE C CA  1 
ATOM   4478  C C   . ILE C  1 146 ? -23.826 32.712  51.769  1.00 18.30  ? 138 ILE C C   1 
ATOM   4479  O O   . ILE C  1 146 ? -24.650 32.621  50.863  1.00 19.67  ? 138 ILE C O   1 
ATOM   4480  C CB  . ILE C  1 146 ? -23.809 30.435  52.779  1.00 14.99  ? 138 ILE C CB  1 
ATOM   4481  C CG1 . ILE C  1 146 ? -23.732 29.643  54.081  1.00 13.12  ? 138 ILE C CG1 1 
ATOM   4482  C CG2 . ILE C  1 146 ? -22.522 30.255  51.980  1.00 15.62  ? 138 ILE C CG2 1 
ATOM   4483  C CD1 . ILE C  1 146 ? -23.895 28.182  53.915  1.00 9.95   ? 138 ILE C CD1 1 
ATOM   4484  N N   . LYS C  1 147 ? -22.739 33.475  51.679  1.00 17.75  ? 139 LYS C N   1 
ATOM   4485  C CA  . LYS C  1 147 ? -22.425 34.205  50.443  1.00 24.42  ? 139 LYS C CA  1 
ATOM   4486  C C   . LYS C  1 147 ? -21.270 33.577  49.646  1.00 22.41  ? 139 LYS C C   1 
ATOM   4487  O O   . LYS C  1 147 ? -20.119 33.558  50.099  1.00 21.52  ? 139 LYS C O   1 
ATOM   4488  C CB  . LYS C  1 147 ? -22.127 35.681  50.718  1.00 24.52  ? 139 LYS C CB  1 
ATOM   4489  C CG  . LYS C  1 147 ? -23.337 36.499  51.137  1.00 38.46  ? 139 LYS C CG  1 
ATOM   4490  C CD  . LYS C  1 147 ? -23.477 36.590  52.671  1.00 40.55  ? 139 LYS C CD  1 
ATOM   4491  C CE  . LYS C  1 147 ? -24.149 37.908  53.091  1.00 48.15  ? 139 LYS C CE  1 
ATOM   4492  N NZ  . LYS C  1 147 ? -24.313 38.044  54.570  1.00 48.20  ? 139 LYS C NZ  1 
ATOM   4493  N N   . ILE C  1 148 ? -21.601 33.067  48.463  1.00 18.29  ? 140 ILE C N   1 
ATOM   4494  C CA  . ILE C  1 148 ? -20.649 32.427  47.562  1.00 21.41  ? 140 ILE C CA  1 
ATOM   4495  C C   . ILE C  1 148 ? -20.399 33.336  46.349  1.00 23.65  ? 140 ILE C C   1 
ATOM   4496  O O   . ILE C  1 148 ? -21.340 33.675  45.626  1.00 22.91  ? 140 ILE C O   1 
ATOM   4497  C CB  . ILE C  1 148 ? -21.232 31.093  47.027  1.00 22.64  ? 140 ILE C CB  1 
ATOM   4498  C CG1 . ILE C  1 148 ? -21.757 30.229  48.173  1.00 20.65  ? 140 ILE C CG1 1 
ATOM   4499  C CG2 . ILE C  1 148 ? -20.210 30.344  46.169  1.00 21.63  ? 140 ILE C CG2 1 
ATOM   4500  C CD1 . ILE C  1 148 ? -20.714 29.385  48.842  1.00 23.92  ? 140 ILE C CD1 1 
ATOM   4501  N N   . GLY C  1 149 ? -19.145 33.726  46.121  1.00 19.87  ? 141 GLY C N   1 
ATOM   4502  C CA  . GLY C  1 149 ? -18.810 34.542  44.960  1.00 21.92  ? 141 GLY C CA  1 
ATOM   4503  C C   . GLY C  1 149 ? -17.466 34.241  44.312  1.00 18.34  ? 141 GLY C C   1 
ATOM   4504  O O   . GLY C  1 149 ? -16.642 33.523  44.874  1.00 16.23  ? 141 GLY C O   1 
ATOM   4505  N N   . SER C  1 150 ? -17.245 34.784  43.118  1.00 20.03  ? 142 SER C N   1 
ATOM   4506  C CA  . SER C  1 150 ? -15.926 34.732  42.496  1.00 14.98  ? 142 SER C CA  1 
ATOM   4507  C C   . SER C  1 150 ? -14.960 35.481  43.374  1.00 13.32  ? 142 SER C C   1 
ATOM   4508  O O   . SER C  1 150 ? -15.283 36.545  43.880  1.00 19.84  ? 142 SER C O   1 
ATOM   4509  C CB  . SER C  1 150 ? -15.939 35.380  41.107  1.00 19.16  ? 142 SER C CB  1 
ATOM   4510  O OG  . SER C  1 150 ? -14.611 35.520  40.594  1.00 20.63  ? 142 SER C OG  1 
ATOM   4511  N N   . TRP C  1 151 ? -13.764 34.946  43.554  1.00 16.07  ? 143 TRP C N   1 
ATOM   4512  C CA  . TRP C  1 151 ? -12.831 35.571  44.490  1.00 15.40  ? 143 TRP C CA  1 
ATOM   4513  C C   . TRP C  1 151 ? -11.871 36.611  43.874  1.00 18.14  ? 143 TRP C C   1 
ATOM   4514  O O   . TRP C  1 151 ? -11.591 37.630  44.506  1.00 19.65  ? 143 TRP C O   1 
ATOM   4515  C CB  . TRP C  1 151 ? -12.074 34.509  45.272  1.00 9.68   ? 143 TRP C CB  1 
ATOM   4516  C CG  . TRP C  1 151 ? -11.082 35.057  46.195  1.00 10.88  ? 143 TRP C CG  1 
ATOM   4517  C CD1 . TRP C  1 151 ? -9.732  34.911  46.125  1.00 12.93  ? 143 TRP C CD1 1 
ATOM   4518  C CD2 . TRP C  1 151 ? -11.342 35.838  47.361  1.00 15.02  ? 143 TRP C CD2 1 
ATOM   4519  N NE1 . TRP C  1 151 ? -9.126  35.551  47.184  1.00 12.57  ? 143 TRP C NE1 1 
ATOM   4520  C CE2 . TRP C  1 151 ? -10.099 36.132  47.952  1.00 14.59  ? 143 TRP C CE2 1 
ATOM   4521  C CE3 . TRP C  1 151 ? -12.507 36.309  47.972  1.00 16.73  ? 143 TRP C CE3 1 
ATOM   4522  C CZ2 . TRP C  1 151 ? -9.995  36.874  49.107  1.00 14.07  ? 143 TRP C CZ2 1 
ATOM   4523  C CZ3 . TRP C  1 151 ? -12.399 37.047  49.106  1.00 14.04  ? 143 TRP C CZ3 1 
ATOM   4524  C CH2 . TRP C  1 151 ? -11.159 37.323  49.669  1.00 16.83  ? 143 TRP C CH2 1 
ATOM   4525  N N   . THR C  1 152 ? -11.373 36.380  42.659  1.00 12.26  ? 144 THR C N   1 
ATOM   4526  C CA  . THR C  1 152 ? -10.458 37.352  42.069  1.00 11.31  ? 144 THR C CA  1 
ATOM   4527  C C   . THR C  1 152 ? -11.051 38.048  40.858  1.00 16.68  ? 144 THR C C   1 
ATOM   4528  O O   . THR C  1 152 ? -10.514 39.053  40.408  1.00 20.74  ? 144 THR C O   1 
ATOM   4529  C CB  . THR C  1 152 ? -9.080  36.745  41.662  1.00 10.64  ? 144 THR C CB  1 
ATOM   4530  O OG1 . THR C  1 152 ? -9.250  35.786  40.608  1.00 10.87  ? 144 THR C OG1 1 
ATOM   4531  C CG2 . THR C  1 152 ? -8.392  36.094  42.843  1.00 12.91  ? 144 THR C CG2 1 
ATOM   4532  N N   . HIS C  1 153 ? -12.145 37.526  40.316  1.00 14.03  ? 145 HIS C N   1 
ATOM   4533  C CA  . HIS C  1 153 ? -12.669 38.090  39.085  1.00 13.72  ? 145 HIS C CA  1 
ATOM   4534  C C   . HIS C  1 153 ? -13.879 38.964  39.320  1.00 17.85  ? 145 HIS C C   1 
ATOM   4535  O O   . HIS C  1 153 ? -14.944 38.460  39.633  1.00 21.64  ? 145 HIS C O   1 
ATOM   4536  C CB  . HIS C  1 153 ? -13.008 36.982  38.090  1.00 17.06  ? 145 HIS C CB  1 
ATOM   4537  C CG  . HIS C  1 153 ? -11.840 36.120  37.744  1.00 15.13  ? 145 HIS C CG  1 
ATOM   4538  N ND1 . HIS C  1 153 ? -10.924 36.462  36.770  1.00 18.38  ? 145 HIS C ND1 1 
ATOM   4539  C CD2 . HIS C  1 153 ? -11.417 34.943  38.261  1.00 14.03  ? 145 HIS C CD2 1 
ATOM   4540  C CE1 . HIS C  1 153 ? -9.999  35.524  36.689  1.00 17.12  ? 145 HIS C CE1 1 
ATOM   4541  N NE2 . HIS C  1 153 ? -10.272 34.594  37.589  1.00 21.85  ? 145 HIS C NE2 1 
ATOM   4542  N N   . HIS C  1 154 ? -13.713 40.274  39.149  1.00 21.56  ? 146 HIS C N   1 
ATOM   4543  C CA  . HIS C  1 154 ? -14.821 41.222  39.269  1.00 21.80  ? 146 HIS C CA  1 
ATOM   4544  C C   . HIS C  1 154 ? -15.947 40.945  38.256  1.00 22.76  ? 146 HIS C C   1 
ATOM   4545  O O   . HIS C  1 154 ? -15.803 40.114  37.363  1.00 23.59  ? 146 HIS C O   1 
ATOM   4546  C CB  . HIS C  1 154 ? -14.330 42.689  39.239  1.00 28.59  ? 146 HIS C CB  1 
ATOM   4547  C CG  . HIS C  1 154 ? -13.494 43.048  38.045  1.00 33.79  ? 146 HIS C CG  1 
ATOM   4548  N ND1 . HIS C  1 154 ? -12.153 43.368  38.140  1.00 38.05  ? 146 HIS C ND1 1 
ATOM   4549  C CD2 . HIS C  1 154 ? -13.809 43.172  36.732  1.00 34.23  ? 146 HIS C CD2 1 
ATOM   4550  C CE1 . HIS C  1 154 ? -11.678 43.651  36.941  1.00 37.85  ? 146 HIS C CE1 1 
ATOM   4551  N NE2 . HIS C  1 154 ? -12.664 43.539  36.065  1.00 36.80  ? 146 HIS C NE2 1 
ATOM   4552  N N   . SER C  1 155 ? -17.072 41.631  38.415  1.00 26.35  ? 147 SER C N   1 
ATOM   4553  C CA  . SER C  1 155 ? -18.318 41.276  37.723  1.00 27.53  ? 147 SER C CA  1 
ATOM   4554  C C   . SER C  1 155 ? -18.315 41.502  36.216  1.00 26.59  ? 147 SER C C   1 
ATOM   4555  O O   . SER C  1 155 ? -19.174 40.988  35.501  1.00 27.80  ? 147 SER C O   1 
ATOM   4556  C CB  . SER C  1 155 ? -19.495 42.035  38.334  1.00 31.93  ? 147 SER C CB  1 
ATOM   4557  O OG  . SER C  1 155 ? -19.391 43.430  38.091  1.00 40.33  ? 147 SER C OG  1 
ATOM   4558  N N   . ARG C  1 156 ? -17.363 42.286  35.733  1.00 26.09  ? 148 ARG C N   1 
ATOM   4559  C CA  . ARG C  1 156 ? -17.209 42.473  34.294  1.00 26.06  ? 148 ARG C CA  1 
ATOM   4560  C C   . ARG C  1 156 ? -16.469 41.263  33.654  1.00 26.45  ? 148 ARG C C   1 
ATOM   4561  O O   . ARG C  1 156 ? -16.428 41.123  32.434  1.00 27.69  ? 148 ARG C O   1 
ATOM   4562  C CB  . ARG C  1 156 ? -16.571 43.851  34.022  1.00 21.98  ? 148 ARG C CB  1 
ATOM   4563  C CG  . ARG C  1 156 ? -15.747 43.981  32.766  1.00 42.20  ? 148 ARG C CG  1 
ATOM   4564  C CD  . ARG C  1 156 ? -16.330 45.003  31.795  1.00 53.35  ? 148 ARG C CD  1 
ATOM   4565  N NE  . ARG C  1 156 ? -15.740 44.822  30.470  1.00 55.81  ? 148 ARG C NE  1 
ATOM   4566  C CZ  . ARG C  1 156 ? -16.355 44.250  29.436  1.00 53.49  ? 148 ARG C CZ  1 
ATOM   4567  N NH1 . ARG C  1 156 ? -17.610 43.822  29.551  1.00 43.49  ? 148 ARG C NH1 1 
ATOM   4568  N NH2 . ARG C  1 156 ? -15.713 44.119  28.279  1.00 47.91  ? 148 ARG C NH2 1 
ATOM   4569  N N   . GLU C  1 157 ? -15.944 40.367  34.497  1.00 23.85  ? 149 GLU C N   1 
ATOM   4570  C CA  . GLU C  1 157 ? -15.271 39.136  34.068  1.00 18.60  ? 149 GLU C CA  1 
ATOM   4571  C C   . GLU C  1 157 ? -16.121 37.885  34.329  1.00 18.34  ? 149 GLU C C   1 
ATOM   4572  O O   . GLU C  1 157 ? -16.314 37.061  33.453  1.00 16.91  ? 149 GLU C O   1 
ATOM   4573  C CB  . GLU C  1 157 ? -13.913 38.978  34.778  1.00 20.02  ? 149 GLU C CB  1 
ATOM   4574  C CG  . GLU C  1 157 ? -12.868 40.073  34.492  1.00 22.66  ? 149 GLU C CG  1 
ATOM   4575  C CD  . GLU C  1 157 ? -11.634 39.987  35.404  1.00 23.21  ? 149 GLU C CD  1 
ATOM   4576  O OE1 . GLU C  1 157 ? -11.532 39.039  36.192  1.00 24.55  ? 149 GLU C OE1 1 
ATOM   4577  O OE2 . GLU C  1 157 ? -10.747 40.860  35.338  1.00 30.25  ? 149 GLU C OE2 1 
ATOM   4578  N N   . ILE C  1 158 ? -16.618 37.734  35.552  1.00 25.45  ? 150 ILE C N   1 
ATOM   4579  C CA  . ILE C  1 158 ? -17.460 36.586  35.898  1.00 21.26  ? 150 ILE C CA  1 
ATOM   4580  C C   . ILE C  1 158 ? -18.778 37.059  36.483  1.00 20.94  ? 150 ILE C C   1 
ATOM   4581  O O   . ILE C  1 158 ? -18.803 37.954  37.318  1.00 24.45  ? 150 ILE C O   1 
ATOM   4582  C CB  . ILE C  1 158 ? -16.771 35.657  36.923  1.00 19.97  ? 150 ILE C CB  1 
ATOM   4583  C CG1 . ILE C  1 158 ? -15.579 34.954  36.284  1.00 19.95  ? 150 ILE C CG1 1 
ATOM   4584  C CG2 . ILE C  1 158 ? -17.728 34.609  37.435  1.00 16.44  ? 150 ILE C CG2 1 
ATOM   4585  C CD1 . ILE C  1 158 ? -14.946 33.929  37.176  1.00 16.68  ? 150 ILE C CD1 1 
ATOM   4586  N N   . SER C  1 159 ? -19.873 36.469  36.027  1.00 21.15  ? 151 SER C N   1 
ATOM   4587  C CA  . SER C  1 159 ? -21.178 36.709  36.626  1.00 25.67  ? 151 SER C CA  1 
ATOM   4588  C C   . SER C  1 159 ? -21.677 35.446  37.285  1.00 24.88  ? 151 SER C C   1 
ATOM   4589  O O   . SER C  1 159 ? -21.567 34.360  36.728  1.00 24.77  ? 151 SER C O   1 
ATOM   4590  C CB  . SER C  1 159 ? -22.188 37.141  35.570  1.00 27.62  ? 151 SER C CB  1 
ATOM   4591  O OG  . SER C  1 159 ? -21.844 38.406  35.044  1.00 41.18  ? 151 SER C OG  1 
ATOM   4592  N N   . VAL C  1 160 ? -22.231 35.577  38.475  1.00 23.02  ? 152 VAL C N   1 
ATOM   4593  C CA  . VAL C  1 160 ? -22.790 34.413  39.127  1.00 26.23  ? 152 VAL C CA  1 
ATOM   4594  C C   . VAL C  1 160 ? -24.303 34.572  39.187  1.00 33.24  ? 152 VAL C C   1 
ATOM   4595  O O   . VAL C  1 160 ? -24.817 35.650  39.502  1.00 37.43  ? 152 VAL C O   1 
ATOM   4596  C CB  . VAL C  1 160 ? -22.161 34.188  40.509  1.00 35.56  ? 152 VAL C CB  1 
ATOM   4597  C CG1 . VAL C  1 160 ? -20.616 34.116  40.392  1.00 23.83  ? 152 VAL C CG1 1 
ATOM   4598  C CG2 . VAL C  1 160 ? -22.538 35.302  41.424  1.00 35.12  ? 152 VAL C CG2 1 
ATOM   4599  N N   . ASP C  1 161 ? -25.014 33.514  38.814  1.00 34.05  ? 153 ASP C N   1 
ATOM   4600  C CA  . ASP C  1 161 ? -26.474 33.532  38.797  1.00 34.88  ? 153 ASP C CA  1 
ATOM   4601  C C   . ASP C  1 161 ? -27.032 32.225  39.354  1.00 38.93  ? 153 ASP C C   1 
ATOM   4602  O O   . ASP C  1 161 ? -26.711 31.141  38.877  1.00 36.65  ? 153 ASP C O   1 
ATOM   4603  C CB  . ASP C  1 161 ? -27.020 33.787  37.383  1.00 31.46  ? 153 ASP C CB  1 
ATOM   4604  C CG  . ASP C  1 161 ? -27.138 35.279  37.047  1.00 41.35  ? 153 ASP C CG  1 
ATOM   4605  O OD1 . ASP C  1 161 ? -28.281 35.776  36.881  1.00 36.71  ? 153 ASP C OD1 1 
ATOM   4606  O OD2 . ASP C  1 161 ? -26.087 35.953  36.942  1.00 40.93  ? 153 ASP C OD2 1 
ATOM   4607  N N   . PRO C  1 162 ? -27.969 32.264  40.302  1.00 37.10  ? 154 PRO C N   1 
ATOM   4608  C CA  . PRO C  1 162 ? -28.493 30.996  40.867  1.00 39.09  ? 154 PRO C CA  1 
ATOM   4609  C C   . PRO C  1 162 ? -29.648 30.300  40.093  1.00 41.17  ? 154 PRO C C   1 
ATOM   4610  O O   . PRO C  1 162 ? -30.682 30.925  39.858  1.00 46.10  ? 154 PRO C O   1 
ATOM   4611  C CB  . PRO C  1 162 ? -28.979 31.416  42.257  1.00 46.60  ? 154 PRO C CB  1 
ATOM   4612  C CG  . PRO C  1 162 ? -29.306 32.865  42.116  1.00 49.27  ? 154 PRO C CG  1 
ATOM   4613  C CD  . PRO C  1 162 ? -28.306 33.425  41.144  1.00 34.86  ? 154 PRO C CD  1 
ATOM   4614  N N   . THR C  1 163 ? -29.453 29.035  39.693  1.00 47.08  ? 155 THR C N   1 
ATOM   4615  C CA  . THR C  1 163 ? -30.446 28.260  38.906  1.00 49.87  ? 155 THR C CA  1 
ATOM   4616  C C   . THR C  1 163 ? -31.817 27.858  39.515  1.00 59.89  ? 155 THR C C   1 
ATOM   4617  O O   . THR C  1 163 ? -32.850 28.053  38.873  1.00 65.53  ? 155 THR C O   1 
ATOM   4618  C CB  . THR C  1 163 ? -29.801 26.986  38.320  1.00 43.94  ? 155 THR C CB  1 
ATOM   4619  O OG1 . THR C  1 163 ? -29.862 25.928  39.285  1.00 51.91  ? 155 THR C OG1 1 
ATOM   4620  C CG2 . THR C  1 163 ? -28.349 27.245  37.950  1.00 34.87  ? 155 THR C CG2 1 
ATOM   4621  N N   . THR C  1 164 ? -31.834 27.329  40.740  1.00 63.75  ? 156 THR C N   1 
ATOM   4622  C CA  . THR C  1 164 ? -33.064 27.216  41.538  1.00 69.57  ? 156 THR C CA  1 
ATOM   4623  C C   . THR C  1 164 ? -33.133 28.314  42.613  1.00 70.68  ? 156 THR C C   1 
ATOM   4624  O O   . THR C  1 164 ? -32.216 28.459  43.434  1.00 57.99  ? 156 THR C O   1 
ATOM   4625  C CB  . THR C  1 164 ? -33.208 25.817  42.198  1.00 62.03  ? 156 THR C CB  1 
ATOM   4626  O OG1 . THR C  1 164 ? -33.412 24.821  41.186  1.00 53.45  ? 156 THR C OG1 1 
ATOM   4627  C CG2 . THR C  1 164 ? -34.386 25.796  43.169  1.00 58.66  ? 156 THR C CG2 1 
ATOM   4628  N N   . GLU C  1 165 ? -34.225 29.081  42.592  1.00 75.52  ? 157 GLU C N   1 
ATOM   4629  C CA  . GLU C  1 165 ? -34.389 30.260  43.451  1.00 69.81  ? 157 GLU C CA  1 
ATOM   4630  C C   . GLU C  1 165 ? -35.026 29.908  44.792  1.00 60.53  ? 157 GLU C C   1 
ATOM   4631  O O   . GLU C  1 165 ? -34.732 30.539  45.815  1.00 53.29  ? 157 GLU C O   1 
ATOM   4632  C CB  . GLU C  1 165 ? -35.240 31.322  42.738  1.00 70.94  ? 157 GLU C CB  1 
ATOM   4633  C CG  . GLU C  1 165 ? -34.858 32.770  43.043  1.00 67.22  ? 157 GLU C CG  1 
ATOM   4634  C CD  . GLU C  1 165 ? -33.658 33.250  42.236  1.00 68.68  ? 157 GLU C CD  1 
ATOM   4635  O OE1 . GLU C  1 165 ? -32.991 32.413  41.589  1.00 68.84  ? 157 GLU C OE1 1 
ATOM   4636  O OE2 . GLU C  1 165 ? -33.385 34.470  42.240  1.00 70.12  ? 157 GLU C OE2 1 
ATOM   4637  N N   . ASN C  1 166 ? -35.946 28.944  44.822  1.00 66.63  ? 158 ASN C N   1 
ATOM   4638  C CA  . ASN C  1 166 ? -36.557 28.507  46.085  1.00 67.65  ? 158 ASN C CA  1 
ATOM   4639  C C   . ASN C  1 166 ? -36.943 27.054  46.145  1.00 68.04  ? 158 ASN C C   1 
ATOM   4640  O O   . ASN C  1 166 ? -37.320 26.478  45.164  1.00 73.71  ? 158 ASN C O   1 
ATOM   4641  C CB  . ASN C  1 166 ? -37.747 29.382  46.516  1.00 59.25  ? 158 ASN C CB  1 
ATOM   4642  C CG  . ASN C  1 166 ? -38.439 28.884  47.782  1.00 63.06  ? 158 ASN C CG  1 
ATOM   4643  O OD1 . ASN C  1 166 ? -38.446 29.564  48.799  1.00 64.31  ? 158 ASN C OD1 1 
ATOM   4644  N ND2 . ASN C  1 166 ? -39.081 27.720  47.700  1.00 65.25  ? 158 ASN C ND2 1 
ATOM   4645  N N   . SER C  1 167 ? -36.803 26.461  47.320  1.00 58.19  ? 159 SER C N   1 
ATOM   4646  C CA  . SER C  1 167 ? -37.265 25.121  47.503  1.00 61.56  ? 159 SER C CA  1 
ATOM   4647  C C   . SER C  1 167 ? -37.198 24.676  48.956  1.00 59.54  ? 159 SER C C   1 
ATOM   4648  O O   . SER C  1 167 ? -36.476 25.256  49.748  1.00 49.99  ? 159 SER C O   1 
ATOM   4649  C CB  . SER C  1 167 ? -36.478 24.182  46.585  1.00 57.80  ? 159 SER C CB  1 
ATOM   4650  O OG  . SER C  1 167 ? -36.643 24.530  45.227  1.00 63.80  ? 159 SER C OG  1 
ATOM   4651  N N   . ASP C  1 168 ? -37.935 23.621  49.271  1.00 50.48  ? 160 ASP C N   1 
ATOM   4652  C CA  . ASP C  1 168 ? -37.774 22.813  50.482  1.00 50.55  ? 160 ASP C CA  1 
ATOM   4653  C C   . ASP C  1 168 ? -36.499 22.005  50.634  1.00 48.61  ? 160 ASP C C   1 
ATOM   4654  O O   . ASP C  1 168 ? -36.125 21.715  51.709  1.00 47.98  ? 160 ASP C O   1 
ATOM   4655  C CB  . ASP C  1 168 ? -38.975 21.907  50.721  1.00 55.10  ? 160 ASP C CB  1 
ATOM   4656  C CG  . ASP C  1 168 ? -39.422 21.939  52.137  1.00 58.55  ? 160 ASP C CG  1 
ATOM   4657  O OD1 . ASP C  1 168 ? -38.820 21.280  52.975  1.00 50.13  ? 160 ASP C OD1 1 
ATOM   4658  O OD2 . ASP C  1 168 ? -40.360 22.654  52.449  1.00 52.58  ? 160 ASP C OD2 1 
ATOM   4659  N N   . ASP C  1 169 ? -35.887 21.598  49.554  1.00 43.45  ? 161 ASP C N   1 
ATOM   4660  C CA  . ASP C  1 169 ? -34.674 20.817  49.605  1.00 38.96  ? 161 ASP C CA  1 
ATOM   4661  C C   . ASP C  1 169 ? -34.859 19.353  49.920  1.00 46.76  ? 161 ASP C C   1 
ATOM   4662  O O   . ASP C  1 169 ? -33.916 18.614  50.072  1.00 42.43  ? 161 ASP C O   1 
ATOM   4663  C CB  . ASP C  1 169 ? -33.716 21.445  50.547  1.00 33.91  ? 161 ASP C CB  1 
ATOM   4664  C CG  . ASP C  1 169 ? -32.342 21.373  50.060  1.00 34.27  ? 161 ASP C CG  1 
ATOM   4665  O OD1 . ASP C  1 169 ? -31.853 20.279  50.155  1.00 36.43  ? 161 ASP C OD1 1 
ATOM   4666  O OD2 . ASP C  1 169 ? -31.773 22.368  49.596  1.00 27.09  ? 161 ASP C OD2 1 
ATOM   4667  N N   . SER C  1 170 ? -36.102 18.935  49.886  1.00 53.88  ? 162 SER C N   1 
ATOM   4668  C CA  . SER C  1 170 ? -36.552 17.679  50.406  1.00 52.77  ? 162 SER C CA  1 
ATOM   4669  C C   . SER C  1 170 ? -35.907 16.537  49.732  1.00 50.34  ? 162 SER C C   1 
ATOM   4670  O O   . SER C  1 170 ? -35.917 15.440  50.257  1.00 48.52  ? 162 SER C O   1 
ATOM   4671  C CB  . SER C  1 170 ? -38.051 17.534  50.194  1.00 48.91  ? 162 SER C CB  1 
ATOM   4672  O OG  . SER C  1 170 ? -38.453 18.231  49.050  1.00 46.68  ? 162 SER C OG  1 
ATOM   4673  N N   . GLU C  1 171 ? -35.467 16.758  48.519  1.00 40.99  ? 163 GLU C N   1 
ATOM   4674  C CA  . GLU C  1 171 ? -34.917 15.696  47.772  1.00 42.70  ? 163 GLU C CA  1 
ATOM   4675  C C   . GLU C  1 171 ? -33.659 15.187  48.327  1.00 41.27  ? 163 GLU C C   1 
ATOM   4676  O O   . GLU C  1 171 ? -33.487 14.031  48.356  1.00 44.88  ? 163 GLU C O   1 
ATOM   4677  C CB  . GLU C  1 171 ? -34.795 16.083  46.344  1.00 53.07  ? 163 GLU C CB  1 
ATOM   4678  C CG  . GLU C  1 171 ? -35.498 15.124  45.440  1.00 51.54  ? 163 GLU C CG  1 
ATOM   4679  C CD  . GLU C  1 171 ? -35.704 15.694  44.075  1.00 67.74  ? 163 GLU C CD  1 
ATOM   4680  O OE1 . GLU C  1 171 ? -36.062 16.875  43.981  1.00 71.09  ? 163 GLU C OE1 1 
ATOM   4681  O OE2 . GLU C  1 171 ? -35.510 14.956  43.099  1.00 71.34  ? 163 GLU C OE2 1 
ATOM   4682  N N   . TYR C  1 172 ? -32.769 16.049  48.761  1.00 34.43  ? 164 TYR C N   1 
ATOM   4683  C CA  . TYR C  1 172 ? -31.436 15.618  49.100  1.00 33.29  ? 164 TYR C CA  1 
ATOM   4684  C C   . TYR C  1 172 ? -31.087 15.651  50.556  1.00 23.59  ? 164 TYR C C   1 
ATOM   4685  O O   . TYR C  1 172 ? -30.141 15.052  50.970  1.00 21.72  ? 164 TYR C O   1 
ATOM   4686  C CB  . TYR C  1 172 ? -30.386 16.409  48.321  1.00 39.53  ? 164 TYR C CB  1 
ATOM   4687  C CG  . TYR C  1 172 ? -30.703 16.688  46.902  1.00 39.56  ? 164 TYR C CG  1 
ATOM   4688  C CD1 . TYR C  1 172 ? -31.028 17.934  46.503  1.00 41.03  ? 164 TYR C CD1 1 
ATOM   4689  C CD2 . TYR C  1 172 ? -30.706 15.712  45.989  1.00 41.42  ? 164 TYR C CD2 1 
ATOM   4690  C CE1 . TYR C  1 172 ? -31.357 18.183  45.218  1.00 42.11  ? 164 TYR C CE1 1 
ATOM   4691  C CE2 . TYR C  1 172 ? -31.060 15.951  44.715  1.00 46.26  ? 164 TYR C CE2 1 
ATOM   4692  C CZ  . TYR C  1 172 ? -31.367 17.191  44.343  1.00 45.93  ? 164 TYR C CZ  1 
ATOM   4693  O OH  . TYR C  1 172 ? -31.697 17.433  43.058  1.00 58.81  ? 164 TYR C OH  1 
ATOM   4694  N N   . PHE C  1 173 ? -31.867 16.341  51.339  1.00 23.14  ? 165 PHE C N   1 
ATOM   4695  C CA  . PHE C  1 173 ? -31.513 16.514  52.730  1.00 18.46  ? 165 PHE C CA  1 
ATOM   4696  C C   . PHE C  1 173 ? -31.706 15.225  53.524  1.00 21.91  ? 165 PHE C C   1 
ATOM   4697  O O   . PHE C  1 173 ? -32.737 14.550  53.400  1.00 21.68  ? 165 PHE C O   1 
ATOM   4698  C CB  . PHE C  1 173 ? -32.296 17.653  53.354  1.00 18.55  ? 165 PHE C CB  1 
ATOM   4699  C CG  . PHE C  1 173 ? -31.763 18.077  54.685  1.00 16.26  ? 165 PHE C CG  1 
ATOM   4700  C CD1 . PHE C  1 173 ? -30.515 18.666  54.784  1.00 14.58  ? 165 PHE C CD1 1 
ATOM   4701  C CD2 . PHE C  1 173 ? -32.502 17.882  55.839  1.00 17.60  ? 165 PHE C CD2 1 
ATOM   4702  C CE1 . PHE C  1 173 ? -30.012 19.064  56.018  1.00 16.51  ? 165 PHE C CE1 1 
ATOM   4703  C CE2 . PHE C  1 173 ? -32.006 18.284  57.083  1.00 17.41  ? 165 PHE C CE2 1 
ATOM   4704  C CZ  . PHE C  1 173 ? -30.758 18.870  57.169  1.00 15.23  ? 165 PHE C CZ  1 
ATOM   4705  N N   . SER C  1 174 ? -30.700 14.889  54.330  1.00 20.03  ? 166 SER C N   1 
ATOM   4706  C CA  . SER C  1 174 ? -30.715 13.673  55.143  1.00 20.88  ? 166 SER C CA  1 
ATOM   4707  C C   . SER C  1 174 ? -31.862 13.659  56.125  1.00 20.83  ? 166 SER C C   1 
ATOM   4708  O O   . SER C  1 174 ? -32.031 14.587  56.914  1.00 22.54  ? 166 SER C O   1 
ATOM   4709  C CB  . SER C  1 174 ? -29.414 13.515  55.929  1.00 19.26  ? 166 SER C CB  1 
ATOM   4710  O OG  . SER C  1 174 ? -29.435 12.315  56.686  1.00 18.65  ? 166 SER C OG  1 
ATOM   4711  N N   . GLN C  1 175 ? -32.638 12.589  56.099  1.00 22.95  ? 167 GLN C N   1 
ATOM   4712  C CA  . GLN C  1 175 ? -33.755 12.488  57.014  1.00 25.41  ? 167 GLN C CA  1 
ATOM   4713  C C   . GLN C  1 175 ? -33.281 12.176  58.439  1.00 25.03  ? 167 GLN C C   1 
ATOM   4714  O O   . GLN C  1 175 ? -34.080 12.210  59.365  1.00 23.40  ? 167 GLN C O   1 
ATOM   4715  C CB  . GLN C  1 175 ? -34.767 11.450  56.523  1.00 28.06  ? 167 GLN C CB  1 
ATOM   4716  C CG  . GLN C  1 175 ? -34.438 10.010  56.896  1.00 35.66  ? 167 GLN C CG  1 
ATOM   4717  C CD  . GLN C  1 175 ? -35.323 8.998   56.170  1.00 47.89  ? 167 GLN C CD  1 
ATOM   4718  O OE1 . GLN C  1 175 ? -34.903 8.405   55.169  1.00 35.72  ? 167 GLN C OE1 1 
ATOM   4719  N NE2 . GLN C  1 175 ? -36.553 8.795   56.673  1.00 42.44  ? 167 GLN C NE2 1 
ATOM   4720  N N   . TYR C  1 176 ? -31.983 11.905  58.617  1.00 21.68  ? 168 TYR C N   1 
ATOM   4721  C CA  . TYR C  1 176 ? -31.460 11.512  59.928  1.00 22.56  ? 168 TYR C CA  1 
ATOM   4722  C C   . TYR C  1 176 ? -30.717 12.637  60.628  1.00 23.08  ? 168 TYR C C   1 
ATOM   4723  O O   . TYR C  1 176 ? -30.118 12.444  61.685  1.00 24.44  ? 168 TYR C O   1 
ATOM   4724  C CB  . TYR C  1 176 ? -30.579 10.262  59.841  1.00 21.38  ? 168 TYR C CB  1 
ATOM   4725  C CG  . TYR C  1 176 ? -31.248 9.128   59.097  1.00 27.65  ? 168 TYR C CG  1 
ATOM   4726  C CD1 . TYR C  1 176 ? -32.273 8.388   59.686  1.00 25.15  ? 168 TYR C CD1 1 
ATOM   4727  C CD2 . TYR C  1 176 ? -30.870 8.811   57.792  1.00 23.65  ? 168 TYR C CD2 1 
ATOM   4728  C CE1 . TYR C  1 176 ? -32.896 7.363   58.993  1.00 31.51  ? 168 TYR C CE1 1 
ATOM   4729  C CE2 . TYR C  1 176 ? -31.481 7.797   57.099  1.00 20.09  ? 168 TYR C CE2 1 
ATOM   4730  C CZ  . TYR C  1 176 ? -32.483 7.073   57.697  1.00 27.78  ? 168 TYR C CZ  1 
ATOM   4731  O OH  . TYR C  1 176 ? -33.081 6.061   56.996  1.00 28.79  ? 168 TYR C OH  1 
ATOM   4732  N N   . SER C  1 177 ? -30.766 13.819  60.046  1.00 17.33  ? 169 SER C N   1 
ATOM   4733  C CA  . SER C  1 177 ? -30.216 14.974  60.718  1.00 17.73  ? 169 SER C CA  1 
ATOM   4734  C C   . SER C  1 177 ? -31.033 15.338  61.980  1.00 21.60  ? 169 SER C C   1 
ATOM   4735  O O   . SER C  1 177 ? -32.220 15.010  62.086  1.00 17.83  ? 169 SER C O   1 
ATOM   4736  C CB  . SER C  1 177 ? -30.172 16.151  59.746  1.00 15.63  ? 169 SER C CB  1 
ATOM   4737  O OG  . SER C  1 177 ? -29.848 17.343  60.429  1.00 19.76  ? 169 SER C OG  1 
ATOM   4738  N N   . ARG C  1 178 ? -30.388 16.014  62.931  1.00 20.26  ? 170 ARG C N   1 
ATOM   4739  C CA  . ARG C  1 178 ? -31.083 16.589  64.074  1.00 14.22  ? 170 ARG C CA  1 
ATOM   4740  C C   . ARG C  1 178 ? -31.942 17.759  63.629  1.00 18.33  ? 170 ARG C C   1 
ATOM   4741  O O   . ARG C  1 178 ? -32.795 18.227  64.378  1.00 25.67  ? 170 ARG C O   1 
ATOM   4742  C CB  . ARG C  1 178 ? -30.096 17.100  65.130  1.00 14.63  ? 170 ARG C CB  1 
ATOM   4743  C CG  . ARG C  1 178 ? -29.797 16.138  66.239  1.00 16.82  ? 170 ARG C CG  1 
ATOM   4744  C CD  . ARG C  1 178 ? -28.530 16.511  66.976  1.00 20.03  ? 170 ARG C CD  1 
ATOM   4745  N NE  . ARG C  1 178 ? -28.509 17.919  67.358  1.00 38.85  ? 170 ARG C NE  1 
ATOM   4746  C CZ  . ARG C  1 178 ? -27.972 18.381  68.487  1.00 41.19  ? 170 ARG C CZ  1 
ATOM   4747  N NH1 . ARG C  1 178 ? -27.411 17.542  69.346  1.00 32.76  ? 170 ARG C NH1 1 
ATOM   4748  N NH2 . ARG C  1 178 ? -27.988 19.683  68.757  1.00 37.89  ? 170 ARG C NH2 1 
ATOM   4749  N N   . PHE C  1 179 ? -31.722 18.260  62.425  1.00 14.81  ? 171 PHE C N   1 
ATOM   4750  C CA  . PHE C  1 179 ? -32.378 19.498  62.060  1.00 15.12  ? 171 PHE C CA  1 
ATOM   4751  C C   . PHE C  1 179 ? -33.310 19.278  60.896  1.00 15.63  ? 171 PHE C C   1 
ATOM   4752  O O   . PHE C  1 179 ? -33.233 18.249  60.229  1.00 19.16  ? 171 PHE C O   1 
ATOM   4753  C CB  . PHE C  1 179 ? -31.338 20.587  61.793  1.00 15.43  ? 171 PHE C CB  1 
ATOM   4754  C CG  . PHE C  1 179 ? -30.407 20.829  62.963  1.00 15.19  ? 171 PHE C CG  1 
ATOM   4755  C CD1 . PHE C  1 179 ? -29.240 20.088  63.110  1.00 14.34  ? 171 PHE C CD1 1 
ATOM   4756  C CD2 . PHE C  1 179 ? -30.704 21.787  63.920  1.00 14.55  ? 171 PHE C CD2 1 
ATOM   4757  C CE1 . PHE C  1 179 ? -28.387 20.298  64.182  1.00 14.56  ? 171 PHE C CE1 1 
ATOM   4758  C CE2 . PHE C  1 179 ? -29.854 22.001  65.000  1.00 17.31  ? 171 PHE C CE2 1 
ATOM   4759  C CZ  . PHE C  1 179 ? -28.696 21.253  65.128  1.00 18.78  ? 171 PHE C CZ  1 
ATOM   4760  N N   . GLU C  1 180 ? -34.229 20.212  60.684  1.00 15.57  ? 172 GLU C N   1 
ATOM   4761  C CA  . GLU C  1 180 ? -35.118 20.146  59.526  1.00 19.18  ? 172 GLU C CA  1 
ATOM   4762  C C   . GLU C  1 180 ? -35.001 21.432  58.725  1.00 21.75  ? 172 GLU C C   1 
ATOM   4763  O O   . GLU C  1 180 ? -34.627 22.479  59.262  1.00 22.73  ? 172 GLU C O   1 
ATOM   4764  C CB  . GLU C  1 180 ? -36.587 19.841  59.918  1.00 21.93  ? 172 GLU C CB  1 
ATOM   4765  C CG  . GLU C  1 180 ? -37.173 20.627  61.110  1.00 25.99  ? 172 GLU C CG  1 
ATOM   4766  C CD  . GLU C  1 180 ? -38.553 20.097  61.613  1.00 34.07  ? 172 GLU C CD  1 
ATOM   4767  O OE1 . GLU C  1 180 ? -39.379 19.626  60.796  1.00 24.77  ? 172 GLU C OE1 1 
ATOM   4768  O OE2 . GLU C  1 180 ? -38.813 20.157  62.845  1.00 42.22  ? 172 GLU C OE2 1 
ATOM   4769  N N   . ILE C  1 181 ? -35.300 21.352  57.436  1.00 19.21  ? 173 ILE C N   1 
ATOM   4770  C CA  . ILE C  1 181 ? -35.217 22.526  56.585  1.00 20.16  ? 173 ILE C CA  1 
ATOM   4771  C C   . ILE C  1 181 ? -36.599 23.094  56.268  1.00 24.12  ? 173 ILE C C   1 
ATOM   4772  O O   . ILE C  1 181 ? -37.479 22.384  55.773  1.00 21.86  ? 173 ILE C O   1 
ATOM   4773  C CB  . ILE C  1 181 ? -34.457 22.207  55.295  1.00 21.52  ? 173 ILE C CB  1 
ATOM   4774  C CG1 . ILE C  1 181 ? -32.967 22.065  55.592  1.00 16.62  ? 173 ILE C CG1 1 
ATOM   4775  C CG2 . ILE C  1 181 ? -34.694 23.277  54.237  1.00 24.29  ? 173 ILE C CG2 1 
ATOM   4776  C CD1 . ILE C  1 181 ? -32.164 21.775  54.366  1.00 23.59  ? 173 ILE C CD1 1 
ATOM   4777  N N   . LEU C  1 182 ? -36.772 24.382  56.565  1.00 25.31  ? 174 LEU C N   1 
ATOM   4778  C CA  . LEU C  1 182 ? -38.030 25.087  56.347  1.00 22.24  ? 174 LEU C CA  1 
ATOM   4779  C C   . LEU C  1 182 ? -38.045 25.687  54.959  1.00 29.57  ? 174 LEU C C   1 
ATOM   4780  O O   . LEU C  1 182 ? -38.942 25.401  54.157  1.00 33.22  ? 174 LEU C O   1 
ATOM   4781  C CB  . LEU C  1 182 ? -38.198 26.191  57.395  1.00 24.47  ? 174 LEU C CB  1 
ATOM   4782  C CG  . LEU C  1 182 ? -38.079 25.698  58.847  1.00 24.04  ? 174 LEU C CG  1 
ATOM   4783  C CD1 . LEU C  1 182 ? -37.946 26.843  59.842  1.00 22.72  ? 174 LEU C CD1 1 
ATOM   4784  C CD2 . LEU C  1 182 ? -39.256 24.803  59.200  1.00 17.36  ? 174 LEU C CD2 1 
ATOM   4785  N N   . ASP C  1 183 ? -37.034 26.505  54.666  1.00 31.88  ? 175 ASP C N   1 
ATOM   4786  C CA  . ASP C  1 183 ? -36.912 27.134  53.351  1.00 32.44  ? 175 ASP C CA  1 
ATOM   4787  C C   . ASP C  1 183 ? -35.453 27.347  52.941  1.00 31.52  ? 175 ASP C C   1 
ATOM   4788  O O   . ASP C  1 183 ? -34.593 27.635  53.769  1.00 28.94  ? 175 ASP C O   1 
ATOM   4789  C CB  . ASP C  1 183 ? -37.650 28.474  53.341  1.00 30.22  ? 175 ASP C CB  1 
ATOM   4790  C CG  . ASP C  1 183 ? -37.764 29.084  51.947  1.00 45.79  ? 175 ASP C CG  1 
ATOM   4791  O OD1 . ASP C  1 183 ? -37.954 28.339  50.949  1.00 45.10  ? 175 ASP C OD1 1 
ATOM   4792  O OD2 . ASP C  1 183 ? -37.678 30.328  51.857  1.00 50.37  ? 175 ASP C OD2 1 
ATOM   4793  N N   . VAL C  1 184 ? -35.175 27.194  51.656  1.00 31.90  ? 176 VAL C N   1 
ATOM   4794  C CA  . VAL C  1 184 ? -33.907 27.654  51.131  1.00 33.86  ? 176 VAL C CA  1 
ATOM   4795  C C   . VAL C  1 184 ? -34.184 28.697  50.053  1.00 34.17  ? 176 VAL C C   1 
ATOM   4796  O O   . VAL C  1 184 ? -34.906 28.438  49.097  1.00 36.58  ? 176 VAL C O   1 
ATOM   4797  C CB  . VAL C  1 184 ? -33.038 26.499  50.590  1.00 29.72  ? 176 VAL C CB  1 
ATOM   4798  C CG1 . VAL C  1 184 ? -31.717 27.044  50.079  1.00 29.81  ? 176 VAL C CG1 1 
ATOM   4799  C CG2 . VAL C  1 184 ? -32.782 25.469  51.682  1.00 22.86  ? 176 VAL C CG2 1 
ATOM   4800  N N   . THR C  1 185 ? -33.640 29.893  50.244  1.00 32.52  ? 177 THR C N   1 
ATOM   4801  C CA  . THR C  1 185 ? -33.779 30.972  49.273  1.00 38.83  ? 177 THR C CA  1 
ATOM   4802  C C   . THR C  1 185 ? -32.400 31.394  48.769  1.00 35.55  ? 177 THR C C   1 
ATOM   4803  O O   . THR C  1 185 ? -31.466 31.565  49.559  1.00 34.98  ? 177 THR C O   1 
ATOM   4804  C CB  . THR C  1 185 ? -34.512 32.204  49.878  1.00 37.49  ? 177 THR C CB  1 
ATOM   4805  O OG1 . THR C  1 185 ? -34.128 32.377  51.249  1.00 31.78  ? 177 THR C OG1 1 
ATOM   4806  C CG2 . THR C  1 185 ? -36.012 32.019  49.813  1.00 29.93  ? 177 THR C CG2 1 
ATOM   4807  N N   . GLN C  1 186 ? -32.261 31.549  47.458  1.00 34.42  ? 178 GLN C N   1 
ATOM   4808  C CA  . GLN C  1 186 ? -30.985 31.982  46.894  1.00 30.99  ? 178 GLN C CA  1 
ATOM   4809  C C   . GLN C  1 186 ? -31.213 33.207  46.034  1.00 33.86  ? 178 GLN C C   1 
ATOM   4810  O O   . GLN C  1 186 ? -31.968 33.157  45.063  1.00 34.98  ? 178 GLN C O   1 
ATOM   4811  C CB  . GLN C  1 186 ? -30.356 30.873  46.051  1.00 34.35  ? 178 GLN C CB  1 
ATOM   4812  C CG  . GLN C  1 186 ? -30.340 29.501  46.714  1.00 37.36  ? 178 GLN C CG  1 
ATOM   4813  C CD  . GLN C  1 186 ? -29.553 28.472  45.908  1.00 45.76  ? 178 GLN C CD  1 
ATOM   4814  O OE1 . GLN C  1 186 ? -28.655 27.814  46.436  1.00 40.12  ? 178 GLN C OE1 1 
ATOM   4815  N NE2 . GLN C  1 186 ? -29.885 28.336  44.622  1.00 48.01  ? 178 GLN C NE2 1 
ATOM   4816  N N   . LYS C  1 187 ? -30.570 34.311  46.394  1.00 29.98  ? 179 LYS C N   1 
ATOM   4817  C CA  . LYS C  1 187 ? -30.699 35.544  45.624  1.00 33.97  ? 179 LYS C CA  1 
ATOM   4818  C C   . LYS C  1 187 ? -29.361 36.035  45.048  1.00 36.15  ? 179 LYS C C   1 
ATOM   4819  O O   . LYS C  1 187 ? -28.303 35.914  45.676  1.00 32.30  ? 179 LYS C O   1 
ATOM   4820  C CB  . LYS C  1 187 ? -31.360 36.643  46.468  1.00 32.06  ? 179 LYS C CB  1 
ATOM   4821  C CG  . LYS C  1 187 ? -32.832 36.372  46.814  1.00 41.88  ? 179 LYS C CG  1 
ATOM   4822  C CD  . LYS C  1 187 ? -33.785 36.970  45.777  1.00 55.52  ? 179 LYS C CD  1 
ATOM   4823  C CE  . LYS C  1 187 ? -33.715 38.502  45.769  1.00 65.82  ? 179 LYS C CE  1 
ATOM   4824  N NZ  . LYS C  1 187 ? -34.633 39.152  44.780  1.00 58.51  ? 179 LYS C NZ  1 
ATOM   4825  N N   . LYS C  1 188 ? -29.424 36.580  43.840  1.00 33.11  ? 180 LYS C N   1 
ATOM   4826  C CA  . LYS C  1 188 ? -28.295 37.274  43.243  1.00 34.05  ? 180 LYS C CA  1 
ATOM   4827  C C   . LYS C  1 188 ? -28.141 38.618  43.926  1.00 33.17  ? 180 LYS C C   1 
ATOM   4828  O O   . LYS C  1 188 ? -29.058 39.421  43.937  1.00 44.32  ? 180 LYS C O   1 
ATOM   4829  C CB  . LYS C  1 188 ? -28.533 37.468  41.746  1.00 35.28  ? 180 LYS C CB  1 
ATOM   4830  C CG  . LYS C  1 188 ? -27.762 38.619  41.128  1.00 51.56  ? 180 LYS C CG  1 
ATOM   4831  C CD  . LYS C  1 188 ? -26.256 38.343  41.059  1.00 54.45  ? 180 LYS C CD  1 
ATOM   4832  C CE  . LYS C  1 188 ? -25.609 39.158  39.943  1.00 45.01  ? 180 LYS C CE  1 
ATOM   4833  N NZ  . LYS C  1 188 ? -26.246 38.874  38.616  1.00 38.73  ? 180 LYS C NZ  1 
ATOM   4834  N N   . ASN C  1 189 ? -26.977 38.851  44.505  1.00 34.11  ? 181 ASN C N   1 
ATOM   4835  C CA  . ASN C  1 189 ? -26.699 40.077  45.227  1.00 34.76  ? 181 ASN C CA  1 
ATOM   4836  C C   . ASN C  1 189 ? -25.388 40.600  44.669  1.00 46.54  ? 181 ASN C C   1 
ATOM   4837  O O   . ASN C  1 189 ? -24.815 39.986  43.770  1.00 51.85  ? 181 ASN C O   1 
ATOM   4838  C CB  . ASN C  1 189 ? -26.583 39.776  46.725  1.00 40.26  ? 181 ASN C CB  1 
ATOM   4839  C CG  . ASN C  1 189 ? -26.587 41.030  47.588  1.00 49.54  ? 181 ASN C CG  1 
ATOM   4840  O OD1 . ASN C  1 189 ? -25.872 41.989  47.305  1.00 49.14  ? 181 ASN C OD1 1 
ATOM   4841  N ND2 . ASN C  1 189 ? -27.396 41.026  48.648  1.00 42.34  ? 181 ASN C ND2 1 
ATOM   4842  N N   . SER C  1 190 ? -24.906 41.726  45.179  1.00 48.10  ? 182 SER C N   1 
ATOM   4843  C CA  . SER C  1 190 ? -23.654 42.293  44.683  1.00 49.59  ? 182 SER C CA  1 
ATOM   4844  C C   . SER C  1 190 ? -22.955 43.118  45.749  1.00 54.64  ? 182 SER C C   1 
ATOM   4845  O O   . SER C  1 190 ? -23.603 43.692  46.619  1.00 64.16  ? 182 SER C O   1 
ATOM   4846  C CB  . SER C  1 190 ? -23.904 43.166  43.453  1.00 47.21  ? 182 SER C CB  1 
ATOM   4847  O OG  . SER C  1 190 ? -22.830 44.069  43.269  1.00 47.31  ? 182 SER C OG  1 
ATOM   4848  N N   . VAL C  1 191 ? -21.632 43.185  45.677  1.00 54.46  ? 183 VAL C N   1 
ATOM   4849  C CA  . VAL C  1 191 ? -20.864 44.006  46.607  1.00 59.07  ? 183 VAL C CA  1 
ATOM   4850  C C   . VAL C  1 191 ? -19.663 44.635  45.917  1.00 56.82  ? 183 VAL C C   1 
ATOM   4851  O O   . VAL C  1 191 ? -18.928 43.961  45.189  1.00 51.25  ? 183 VAL C O   1 
ATOM   4852  C CB  . VAL C  1 191 ? -20.376 43.206  47.839  1.00 58.52  ? 183 VAL C CB  1 
ATOM   4853  C CG1 . VAL C  1 191 ? -21.509 43.024  48.849  1.00 56.78  ? 183 VAL C CG1 1 
ATOM   4854  C CG2 . VAL C  1 191 ? -19.761 41.861  47.417  1.00 49.17  ? 183 VAL C CG2 1 
ATOM   4855  N N   . THR C  1 192 ? -19.469 45.930  46.152  1.00 58.76  ? 184 THR C N   1 
ATOM   4856  C CA  . THR C  1 192 ? -18.339 46.649  45.581  1.00 55.79  ? 184 THR C CA  1 
ATOM   4857  C C   . THR C  1 192 ? -17.319 46.962  46.673  1.00 56.53  ? 184 THR C C   1 
ATOM   4858  O O   . THR C  1 192 ? -17.354 46.363  47.751  1.00 54.43  ? 184 THR C O   1 
ATOM   4859  C CB  . THR C  1 192 ? -18.792 47.947  44.873  1.00 49.97  ? 184 THR C CB  1 
ATOM   4860  O OG1 . THR C  1 192 ? -18.849 49.020  45.818  1.00 57.48  ? 184 THR C OG1 1 
ATOM   4861  C CG2 . THR C  1 192 ? -20.169 47.759  44.231  1.00 46.28  ? 184 THR C CG2 1 
ATOM   4862  N N   . PRO C  1 197 ? -13.073 49.376  44.423  1.00 57.51  ? 189 PRO C N   1 
ATOM   4863  C CA  . PRO C  1 197 ? -13.076 49.909  43.052  1.00 66.76  ? 189 PRO C CA  1 
ATOM   4864  C C   . PRO C  1 197 ? -14.185 49.323  42.154  1.00 66.06  ? 189 PRO C C   1 
ATOM   4865  O O   . PRO C  1 197 ? -15.140 50.034  41.834  1.00 60.89  ? 189 PRO C O   1 
ATOM   4866  C CB  . PRO C  1 197 ? -11.668 49.555  42.518  1.00 59.24  ? 189 PRO C CB  1 
ATOM   4867  C CG  . PRO C  1 197 ? -11.043 48.645  43.562  1.00 55.59  ? 189 PRO C CG  1 
ATOM   4868  C CD  . PRO C  1 197 ? -11.723 48.982  44.860  1.00 62.81  ? 189 PRO C CD  1 
ATOM   4869  N N   . GLU C  1 198 ? -14.057 48.058  41.751  1.00 65.30  ? 190 GLU C N   1 
ATOM   4870  C CA  . GLU C  1 198 ? -15.067 47.408  40.906  1.00 54.93  ? 190 GLU C CA  1 
ATOM   4871  C C   . GLU C  1 198 ? -16.044 46.525  41.683  1.00 44.30  ? 190 GLU C C   1 
ATOM   4872  O O   . GLU C  1 198 ? -16.097 46.562  42.910  1.00 52.27  ? 190 GLU C O   1 
ATOM   4873  C CB  . GLU C  1 198 ? -14.409 46.588  39.794  1.00 54.12  ? 190 GLU C CB  1 
ATOM   4874  C CG  . GLU C  1 198 ? -13.845 47.421  38.648  1.00 66.09  ? 190 GLU C CG  1 
ATOM   4875  C CD  . GLU C  1 198 ? -12.328 47.299  38.527  1.00 78.24  ? 190 GLU C CD  1 
ATOM   4876  O OE1 . GLU C  1 198 ? -11.658 47.157  39.578  1.00 77.42  ? 190 GLU C OE1 1 
ATOM   4877  O OE2 . GLU C  1 198 ? -11.811 47.338  37.382  1.00 70.65  ? 190 GLU C OE2 1 
ATOM   4878  N N   . ALA C  1 199 ? -16.810 45.719  40.958  1.00 39.08  ? 191 ALA C N   1 
ATOM   4879  C CA  . ALA C  1 199 ? -17.908 44.976  41.563  1.00 37.13  ? 191 ALA C CA  1 
ATOM   4880  C C   . ALA C  1 199 ? -17.699 43.465  41.538  1.00 32.73  ? 191 ALA C C   1 
ATOM   4881  O O   . ALA C  1 199 ? -17.273 42.909  40.529  1.00 26.60  ? 191 ALA C O   1 
ATOM   4882  C CB  . ALA C  1 199 ? -19.230 45.337  40.872  1.00 34.55  ? 191 ALA C CB  1 
ATOM   4883  N N   . TYR C  1 200 ? -18.013 42.812  42.655  1.00 30.61  ? 192 TYR C N   1 
ATOM   4884  C CA  . TYR C  1 200 ? -18.047 41.352  42.724  1.00 26.48  ? 192 TYR C CA  1 
ATOM   4885  C C   . TYR C  1 200 ? -19.481 40.823  42.913  1.00 31.80  ? 192 TYR C C   1 
ATOM   4886  O O   . TYR C  1 200 ? -20.158 41.167  43.880  1.00 40.01  ? 192 TYR C O   1 
ATOM   4887  C CB  . TYR C  1 200 ? -17.139 40.850  43.853  1.00 28.88  ? 192 TYR C CB  1 
ATOM   4888  C CG  . TYR C  1 200 ? -15.702 41.305  43.732  1.00 27.06  ? 192 TYR C CG  1 
ATOM   4889  C CD1 . TYR C  1 200 ? -14.790 40.593  42.962  1.00 25.19  ? 192 TYR C CD1 1 
ATOM   4890  C CD2 . TYR C  1 200 ? -15.258 42.448  44.381  1.00 24.81  ? 192 TYR C CD2 1 
ATOM   4891  C CE1 . TYR C  1 200 ? -13.480 41.011  42.850  1.00 27.15  ? 192 TYR C CE1 1 
ATOM   4892  C CE2 . TYR C  1 200 ? -13.955 42.875  44.274  1.00 18.50  ? 192 TYR C CE2 1 
ATOM   4893  C CZ  . TYR C  1 200 ? -13.068 42.156  43.511  1.00 28.72  ? 192 TYR C CZ  1 
ATOM   4894  O OH  . TYR C  1 200 ? -11.760 42.580  43.394  1.00 30.95  ? 192 TYR C OH  1 
ATOM   4895  N N   . GLU C  1 201 ? -19.942 39.993  41.985  1.00 25.13  ? 193 GLU C N   1 
ATOM   4896  C CA  . GLU C  1 201 ? -21.252 39.368  42.098  1.00 31.27  ? 193 GLU C CA  1 
ATOM   4897  C C   . GLU C  1 201 ? -21.184 38.122  42.975  1.00 30.32  ? 193 GLU C C   1 
ATOM   4898  O O   . GLU C  1 201 ? -20.203 37.384  42.940  1.00 29.60  ? 193 GLU C O   1 
ATOM   4899  C CB  . GLU C  1 201 ? -21.790 38.979  40.713  1.00 32.23  ? 193 GLU C CB  1 
ATOM   4900  C CG  . GLU C  1 201 ? -21.923 40.125  39.736  1.00 25.28  ? 193 GLU C CG  1 
ATOM   4901  C CD  . GLU C  1 201 ? -22.644 39.741  38.448  1.00 39.29  ? 193 GLU C CD  1 
ATOM   4902  O OE1 . GLU C  1 201 ? -23.013 38.557  38.281  1.00 37.63  ? 193 GLU C OE1 1 
ATOM   4903  O OE2 . GLU C  1 201 ? -22.857 40.634  37.598  1.00 46.78  ? 193 GLU C OE2 1 
ATOM   4904  N N   . ASP C  1 202 ? -22.236 37.886  43.753  1.00 37.01  ? 194 ASP C N   1 
ATOM   4905  C CA  . ASP C  1 202 ? -22.346 36.650  44.539  1.00 37.93  ? 194 ASP C CA  1 
ATOM   4906  C C   . ASP C  1 202 ? -23.731 35.986  44.465  1.00 34.81  ? 194 ASP C C   1 
ATOM   4907  O O   . ASP C  1 202 ? -24.608 36.399  43.699  1.00 37.90  ? 194 ASP C O   1 
ATOM   4908  C CB  . ASP C  1 202 ? -21.899 36.853  46.003  1.00 33.41  ? 194 ASP C CB  1 
ATOM   4909  C CG  . ASP C  1 202 ? -22.778 37.829  46.765  1.00 33.72  ? 194 ASP C CG  1 
ATOM   4910  O OD1 . ASP C  1 202 ? -24.011 37.733  46.655  1.00 37.61  ? 194 ASP C OD1 1 
ATOM   4911  O OD2 . ASP C  1 202 ? -22.231 38.688  47.489  1.00 42.36  ? 194 ASP C OD2 1 
ATOM   4912  N N   . VAL C  1 203 ? -23.902 34.924  45.238  1.00 28.94  ? 195 VAL C N   1 
ATOM   4913  C CA  . VAL C  1 203 ? -25.219 34.370  45.467  1.00 30.37  ? 195 VAL C CA  1 
ATOM   4914  C C   . VAL C  1 203 ? -25.413 34.277  46.973  1.00 28.25  ? 195 VAL C C   1 
ATOM   4915  O O   . VAL C  1 203 ? -24.650 33.597  47.657  1.00 25.56  ? 195 VAL C O   1 
ATOM   4916  C CB  . VAL C  1 203 ? -25.377 32.997  44.813  1.00 25.47  ? 195 VAL C CB  1 
ATOM   4917  C CG1 . VAL C  1 203 ? -26.776 32.464  45.042  1.00 31.97  ? 195 VAL C CG1 1 
ATOM   4918  C CG2 . VAL C  1 203 ? -25.114 33.111  43.345  1.00 28.15  ? 195 VAL C CG2 1 
ATOM   4919  N N   . GLU C  1 204 ? -26.396 35.001  47.498  1.00 30.05  ? 196 GLU C N   1 
ATOM   4920  C CA  . GLU C  1 204 ? -26.722 34.892  48.912  1.00 26.56  ? 196 GLU C CA  1 
ATOM   4921  C C   . GLU C  1 204 ? -27.616 33.683  49.085  1.00 18.95  ? 196 GLU C C   1 
ATOM   4922  O O   . GLU C  1 204 ? -28.692 33.624  48.504  1.00 23.11  ? 196 GLU C O   1 
ATOM   4923  C CB  . GLU C  1 204 ? -27.431 36.150  49.398  1.00 32.14  ? 196 GLU C CB  1 
ATOM   4924  C CG  . GLU C  1 204 ? -26.804 36.805  50.618  1.00 35.77  ? 196 GLU C CG  1 
ATOM   4925  C CD  . GLU C  1 204 ? -27.849 37.388  51.565  1.00 47.78  ? 196 GLU C CD  1 
ATOM   4926  O OE1 . GLU C  1 204 ? -29.032 36.988  51.457  1.00 41.13  ? 196 GLU C OE1 1 
ATOM   4927  O OE2 . GLU C  1 204 ? -27.492 38.238  52.418  1.00 55.48  ? 196 GLU C OE2 1 
ATOM   4928  N N   . VAL C  1 205 ? -27.158 32.693  49.841  1.00 17.91  ? 197 VAL C N   1 
ATOM   4929  C CA  . VAL C  1 205 ? -27.989 31.521  50.106  1.00 23.84  ? 197 VAL C CA  1 
ATOM   4930  C C   . VAL C  1 205 ? -28.505 31.540  51.543  1.00 23.64  ? 197 VAL C C   1 
ATOM   4931  O O   . VAL C  1 205 ? -27.726 31.459  52.495  1.00 23.14  ? 197 VAL C O   1 
ATOM   4932  C CB  . VAL C  1 205 ? -27.243 30.199  49.858  1.00 25.72  ? 197 VAL C CB  1 
ATOM   4933  C CG1 . VAL C  1 205 ? -28.193 29.018  50.053  1.00 23.64  ? 197 VAL C CG1 1 
ATOM   4934  C CG2 . VAL C  1 205 ? -26.645 30.171  48.467  1.00 24.17  ? 197 VAL C CG2 1 
ATOM   4935  N N   . SER C  1 206 ? -29.817 31.674  51.699  1.00 25.21  ? 198 SER C N   1 
ATOM   4936  C CA  . SER C  1 206 ? -30.418 31.719  53.032  1.00 23.12  ? 198 SER C CA  1 
ATOM   4937  C C   . SER C  1 206 ? -31.007 30.376  53.426  1.00 21.14  ? 198 SER C C   1 
ATOM   4938  O O   . SER C  1 206 ? -31.997 29.919  52.847  1.00 20.92  ? 198 SER C O   1 
ATOM   4939  C CB  . SER C  1 206 ? -31.478 32.810  53.112  1.00 25.87  ? 198 SER C CB  1 
ATOM   4940  O OG  . SER C  1 206 ? -30.867 34.078  53.249  1.00 32.94  ? 198 SER C OG  1 
ATOM   4941  N N   . LEU C  1 207 ? -30.377 29.736  54.402  1.00 20.12  ? 199 LEU C N   1 
ATOM   4942  C CA  . LEU C  1 207 ? -30.831 28.433  54.863  1.00 21.07  ? 199 LEU C CA  1 
ATOM   4943  C C   . LEU C  1 207 ? -31.650 28.589  56.123  1.00 16.76  ? 199 LEU C C   1 
ATOM   4944  O O   . LEU C  1 207 ? -31.120 28.875  57.193  1.00 17.89  ? 199 LEU C O   1 
ATOM   4945  C CB  . LEU C  1 207 ? -29.652 27.488  55.098  1.00 20.96  ? 199 LEU C CB  1 
ATOM   4946  C CG  . LEU C  1 207 ? -29.973 26.181  55.832  1.00 17.90  ? 199 LEU C CG  1 
ATOM   4947  C CD1 . LEU C  1 207 ? -30.941 25.311  55.039  1.00 16.54  ? 199 LEU C CD1 1 
ATOM   4948  C CD2 . LEU C  1 207 ? -28.681 25.430  56.123  1.00 17.89  ? 199 LEU C CD2 1 
ATOM   4949  N N   . ASN C  1 208 ? -32.956 28.434  55.971  1.00 19.21  ? 200 ASN C N   1 
ATOM   4950  C CA  . ASN C  1 208 ? -33.880 28.515  57.086  1.00 19.83  ? 200 ASN C CA  1 
ATOM   4951  C C   . ASN C  1 208 ? -34.139 27.112  57.643  1.00 20.48  ? 200 ASN C C   1 
ATOM   4952  O O   . ASN C  1 208 ? -34.707 26.248  56.968  1.00 21.04  ? 200 ASN C O   1 
ATOM   4953  C CB  . ASN C  1 208 ? -35.176 29.218  56.650  1.00 24.07  ? 200 ASN C CB  1 
ATOM   4954  C CG  . ASN C  1 208 ? -36.175 29.430  57.815  1.00 29.94  ? 200 ASN C CG  1 
ATOM   4955  O OD1 . ASN C  1 208 ? -37.382 29.261  57.630  1.00 29.25  ? 200 ASN C OD1 1 
ATOM   4956  N ND2 . ASN C  1 208 ? -35.672 29.803  59.004  1.00 18.43  ? 200 ASN C ND2 1 
ATOM   4957  N N   . PHE C  1 209 ? -33.696 26.892  58.875  1.00 16.74  ? 201 PHE C N   1 
ATOM   4958  C CA  . PHE C  1 209 ? -33.747 25.573  59.489  1.00 21.18  ? 201 PHE C CA  1 
ATOM   4959  C C   . PHE C  1 209 ? -34.066 25.678  60.980  1.00 18.45  ? 201 PHE C C   1 
ATOM   4960  O O   . PHE C  1 209 ? -33.867 26.737  61.586  1.00 19.06  ? 201 PHE C O   1 
ATOM   4961  C CB  . PHE C  1 209 ? -32.411 24.837  59.270  1.00 16.29  ? 201 PHE C CB  1 
ATOM   4962  C CG  . PHE C  1 209 ? -31.247 25.421  60.045  1.00 16.03  ? 201 PHE C CG  1 
ATOM   4963  C CD1 . PHE C  1 209 ? -30.780 26.700  59.780  1.00 13.28  ? 201 PHE C CD1 1 
ATOM   4964  C CD2 . PHE C  1 209 ? -30.613 24.683  61.032  1.00 15.94  ? 201 PHE C CD2 1 
ATOM   4965  C CE1 . PHE C  1 209 ? -29.729 27.237  60.492  1.00 10.97  ? 201 PHE C CE1 1 
ATOM   4966  C CE2 . PHE C  1 209 ? -29.543 25.217  61.736  1.00 15.91  ? 201 PHE C CE2 1 
ATOM   4967  C CZ  . PHE C  1 209 ? -29.107 26.498  61.464  1.00 12.12  ? 201 PHE C CZ  1 
ATOM   4968  N N   . ARG C  1 210 ? -34.563 24.586  61.561  1.00 19.79  ? 202 ARG C N   1 
ATOM   4969  C CA  . ARG C  1 210 ? -34.747 24.487  63.025  1.00 23.85  ? 202 ARG C CA  1 
ATOM   4970  C C   . ARG C  1 210 ? -34.435 23.076  63.532  1.00 19.98  ? 202 ARG C C   1 
ATOM   4971  O O   . ARG C  1 210 ? -34.511 22.103  62.774  1.00 20.74  ? 202 ARG C O   1 
ATOM   4972  C CB  . ARG C  1 210 ? -36.180 24.853  63.432  1.00 23.10  ? 202 ARG C CB  1 
ATOM   4973  C CG  . ARG C  1 210 ? -37.158 23.680  63.319  1.00 24.76  ? 202 ARG C CG  1 
ATOM   4974  C CD  . ARG C  1 210 ? -38.617 24.105  63.310  1.00 29.91  ? 202 ARG C CD  1 
ATOM   4975  N NE  . ARG C  1 210 ? -39.471 23.019  62.832  1.00 34.81  ? 202 ARG C NE  1 
ATOM   4976  C CZ  . ARG C  1 210 ? -40.633 23.187  62.206  1.00 30.15  ? 202 ARG C CZ  1 
ATOM   4977  N NH1 . ARG C  1 210 ? -41.108 24.403  61.978  1.00 26.44  ? 202 ARG C NH1 1 
ATOM   4978  N NH2 . ARG C  1 210 ? -41.322 22.130  61.808  1.00 32.04  ? 202 ARG C NH2 1 
ATOM   4979  N N   . LYS C  1 211 ? -34.074 22.968  64.807  1.00 19.87  ? 203 LYS C N   1 
ATOM   4980  C CA  . LYS C  1 211 ? -33.959 21.666  65.460  1.00 21.22  ? 203 LYS C CA  1 
ATOM   4981  C C   . LYS C  1 211 ? -35.326 20.985  65.482  1.00 26.08  ? 203 LYS C C   1 
ATOM   4982  O O   . LYS C  1 211 ? -36.321 21.603  65.866  1.00 28.76  ? 203 LYS C O   1 
ATOM   4983  C CB  . LYS C  1 211 ? -33.436 21.830  66.884  1.00 22.43  ? 203 LYS C CB  1 
ATOM   4984  C CG  . LYS C  1 211 ? -33.156 20.513  67.601  1.00 32.49  ? 203 LYS C CG  1 
ATOM   4985  C CD  . LYS C  1 211 ? -32.569 20.745  69.000  1.00 40.77  ? 203 LYS C CD  1 
ATOM   4986  C CE  . LYS C  1 211 ? -32.289 19.430  69.732  1.00 47.59  ? 203 LYS C CE  1 
ATOM   4987  N NZ  . LYS C  1 211 ? -32.580 19.517  71.209  1.00 52.61  ? 203 LYS C NZ  1 
ATOM   4988  N N   . LYS C  1 212 ? -35.378 19.728  65.047  1.00 25.59  ? 204 LYS C N   1 
ATOM   4989  C CA  . LYS C  1 212 ? -36.621 18.949  65.080  1.00 33.47  ? 204 LYS C CA  1 
ATOM   4990  C C   . LYS C  1 212 ? -37.262 18.908  66.474  1.00 33.37  ? 204 LYS C C   1 
ATOM   4991  O O   . LYS C  1 212 ? -36.567 18.816  67.483  1.00 34.33  ? 204 LYS C O   1 
ATOM   4992  C CB  . LYS C  1 212 ? -36.365 17.523  64.602  1.00 29.07  ? 204 LYS C CB  1 
ATOM   4993  C CG  . LYS C  1 212 ? -36.176 17.386  63.093  1.00 26.74  ? 204 LYS C CG  1 
ATOM   4994  C CD  . LYS C  1 212 ? -35.358 16.147  62.789  1.00 19.97  ? 204 LYS C CD  1 
ATOM   4995  C CE  . LYS C  1 212 ? -35.760 15.496  61.491  1.00 21.43  ? 204 LYS C CE  1 
ATOM   4996  N NZ  . LYS C  1 212 ? -34.845 14.340  61.199  1.00 24.91  ? 204 LYS C NZ  1 
ATOM   4997  N N   . GLY C  1 213 ? -38.588 18.983  66.518  1.00 37.35  ? 205 GLY C N   1 
ATOM   4998  C CA  . GLY C  1 213 ? -39.319 18.958  67.774  1.00 37.30  ? 205 GLY C CA  1 
ATOM   4999  C C   . GLY C  1 213 ? -40.768 18.531  67.601  1.00 44.15  ? 205 GLY C C   1 
ATOM   5000  O O   . GLY C  1 213 ? -41.689 19.182  68.101  1.00 43.18  ? 205 GLY C O   1 
ATOM   5001  N N   . ASP D  1 1   ? -7.349  48.669  28.126  1.00 45.90  ? -7  ASP D N   1 
ATOM   5002  C CA  . ASP D  1 1   ? -8.435  49.409  28.770  1.00 54.63  ? -7  ASP D CA  1 
ATOM   5003  C C   . ASP D  1 1   ? -9.531  48.467  29.272  1.00 47.93  ? -7  ASP D C   1 
ATOM   5004  O O   . ASP D  1 1   ? -9.429  47.253  29.117  1.00 42.79  ? -7  ASP D O   1 
ATOM   5005  C CB  . ASP D  1 1   ? -9.013  50.460  27.811  1.00 56.06  ? -7  ASP D CB  1 
ATOM   5006  C CG  . ASP D  1 1   ? -9.745  49.840  26.630  1.00 55.36  ? -7  ASP D CG  1 
ATOM   5007  O OD1 . ASP D  1 1   ? -10.998 49.897  26.628  1.00 53.43  ? -7  ASP D OD1 1 
ATOM   5008  O OD2 . ASP D  1 1   ? -9.074  49.299  25.713  1.00 47.03  ? -7  ASP D OD2 1 
ATOM   5009  N N   . TYR D  1 2   ? -10.579 49.029  29.866  1.00 54.26  ? -6  TYR D N   1 
ATOM   5010  C CA  . TYR D  1 2   ? -11.645 48.216  30.461  1.00 55.57  ? -6  TYR D CA  1 
ATOM   5011  C C   . TYR D  1 2   ? -12.612 47.600  29.439  1.00 52.92  ? -6  TYR D C   1 
ATOM   5012  O O   . TYR D  1 2   ? -13.406 46.728  29.783  1.00 57.62  ? -6  TYR D O   1 
ATOM   5013  C CB  . TYR D  1 2   ? -12.412 49.001  31.550  1.00 58.18  ? -6  TYR D CB  1 
ATOM   5014  C CG  . TYR D  1 2   ? -13.141 50.247  31.066  1.00 66.79  ? -6  TYR D CG  1 
ATOM   5015  C CD1 . TYR D  1 2   ? -14.534 50.309  31.063  1.00 60.02  ? -6  TYR D CD1 1 
ATOM   5016  C CD2 . TYR D  1 2   ? -12.434 51.366  30.619  1.00 68.75  ? -6  TYR D CD2 1 
ATOM   5017  C CE1 . TYR D  1 2   ? -15.202 51.450  30.627  1.00 65.56  ? -6  TYR D CE1 1 
ATOM   5018  C CE2 . TYR D  1 2   ? -13.091 52.505  30.176  1.00 70.32  ? -6  TYR D CE2 1 
ATOM   5019  C CZ  . TYR D  1 2   ? -14.473 52.544  30.183  1.00 73.97  ? -6  TYR D CZ  1 
ATOM   5020  O OH  . TYR D  1 2   ? -15.118 53.681  29.743  1.00 70.95  ? -6  TYR D OH  1 
ATOM   5021  N N   . LYS D  1 3   ? -12.547 48.038  28.186  1.00 52.78  ? -5  LYS D N   1 
ATOM   5022  C CA  . LYS D  1 3   ? -13.457 47.511  27.169  1.00 52.61  ? -5  LYS D CA  1 
ATOM   5023  C C   . LYS D  1 3   ? -12.920 46.218  26.541  1.00 52.03  ? -5  LYS D C   1 
ATOM   5024  O O   . LYS D  1 3   ? -13.618 45.548  25.777  1.00 49.25  ? -5  LYS D O   1 
ATOM   5025  C CB  . LYS D  1 3   ? -13.737 48.567  26.095  1.00 56.17  ? -5  LYS D CB  1 
ATOM   5026  C CG  . LYS D  1 3   ? -15.074 48.408  25.379  1.00 63.18  ? -5  LYS D CG  1 
ATOM   5027  C CD  . LYS D  1 3   ? -15.325 49.574  24.430  1.00 66.33  ? -5  LYS D CD  1 
ATOM   5028  C CE  . LYS D  1 3   ? -16.760 49.582  23.922  1.00 73.23  ? -5  LYS D CE  1 
ATOM   5029  N NZ  . LYS D  1 3   ? -17.037 50.773  23.067  1.00 74.05  ? -5  LYS D NZ  1 
ATOM   5030  N N   . ASP D  1 4   ? -11.684 45.864  26.884  1.00 48.53  ? -4  ASP D N   1 
ATOM   5031  C CA  . ASP D  1 4   ? -11.055 44.657  26.358  1.00 44.04  ? -4  ASP D CA  1 
ATOM   5032  C C   . ASP D  1 4   ? -10.817 43.586  27.425  1.00 35.40  ? -4  ASP D C   1 
ATOM   5033  O O   . ASP D  1 4   ? -10.159 42.590  27.152  1.00 34.06  ? -4  ASP D O   1 
ATOM   5034  C CB  . ASP D  1 4   ? -9.721  44.999  25.681  1.00 44.06  ? -4  ASP D CB  1 
ATOM   5035  C CG  . ASP D  1 4   ? -9.901  45.722  24.357  1.00 44.88  ? -4  ASP D CG  1 
ATOM   5036  O OD1 . ASP D  1 4   ? -10.638 45.205  23.485  1.00 52.15  ? -4  ASP D OD1 1 
ATOM   5037  O OD2 . ASP D  1 4   ? -9.300  46.806  24.192  1.00 40.92  ? -4  ASP D OD2 1 
ATOM   5038  N N   . ASP D  1 5   ? -11.343 43.795  28.631  1.00 39.62  ? -3  ASP D N   1 
ATOM   5039  C CA  . ASP D  1 5   ? -11.165 42.849  29.748  1.00 38.89  ? -3  ASP D CA  1 
ATOM   5040  C C   . ASP D  1 5   ? -11.546 41.399  29.403  1.00 30.39  ? -3  ASP D C   1 
ATOM   5041  O O   . ASP D  1 5   ? -10.919 40.453  29.885  1.00 24.23  ? -3  ASP D O   1 
ATOM   5042  C CB  . ASP D  1 5   ? -11.942 43.305  30.997  1.00 38.12  ? -3  ASP D CB  1 
ATOM   5043  C CG  . ASP D  1 5   ? -11.284 44.484  31.716  1.00 43.95  ? -3  ASP D CG  1 
ATOM   5044  O OD1 . ASP D  1 5   ? -10.346 45.092  31.146  1.00 31.94  ? -3  ASP D OD1 1 
ATOM   5045  O OD2 . ASP D  1 5   ? -11.724 44.807  32.851  1.00 48.40  ? -3  ASP D OD2 1 
ATOM   5046  N N   . ASP D  1 6   ? -12.567 41.230  28.570  1.00 32.06  ? -2  ASP D N   1 
ATOM   5047  C CA  . ASP D  1 6   ? -13.020 39.894  28.184  1.00 32.44  ? -2  ASP D CA  1 
ATOM   5048  C C   . ASP D  1 6   ? -12.555 39.472  26.780  1.00 34.57  ? -2  ASP D C   1 
ATOM   5049  O O   . ASP D  1 6   ? -13.283 38.822  26.025  1.00 37.54  ? -2  ASP D O   1 
ATOM   5050  C CB  . ASP D  1 6   ? -14.537 39.790  28.309  1.00 32.93  ? -2  ASP D CB  1 
ATOM   5051  C CG  . ASP D  1 6   ? -15.038 40.210  29.681  1.00 34.86  ? -2  ASP D CG  1 
ATOM   5052  O OD1 . ASP D  1 6   ? -16.274 40.265  29.868  1.00 38.63  ? -2  ASP D OD1 1 
ATOM   5053  O OD2 . ASP D  1 6   ? -14.199 40.493  30.567  1.00 29.54  ? -2  ASP D OD2 1 
ATOM   5054  N N   . ASP D  1 7   ? -11.337 39.866  26.437  1.00 32.36  ? -1  ASP D N   1 
ATOM   5055  C CA  . ASP D  1 7   ? -10.670 39.359  25.257  1.00 32.23  ? -1  ASP D CA  1 
ATOM   5056  C C   . ASP D  1 7   ? -9.861  38.153  25.728  1.00 29.72  ? -1  ASP D C   1 
ATOM   5057  O O   . ASP D  1 7   ? -8.834  38.304  26.411  1.00 25.34  ? -1  ASP D O   1 
ATOM   5058  C CB  . ASP D  1 7   ? -9.750  40.435  24.676  1.00 32.67  ? -1  ASP D CB  1 
ATOM   5059  C CG  . ASP D  1 7   ? -9.371  40.170  23.234  1.00 34.28  ? -1  ASP D CG  1 
ATOM   5060  O OD1 . ASP D  1 7   ? -9.222  38.986  22.844  1.00 28.28  ? -1  ASP D OD1 1 
ATOM   5061  O OD2 . ASP D  1 7   ? -9.221  41.166  22.492  1.00 39.04  ? -1  ASP D OD2 1 
ATOM   5062  N N   . LYS D  1 8   ? -10.330 36.955  25.388  1.00 25.53  ? 0   LYS D N   1 
ATOM   5063  C CA  . LYS D  1 8   ? -9.707  35.752  25.922  1.00 19.94  ? 0   LYS D CA  1 
ATOM   5064  C C   . LYS D  1 8   ? -8.290  35.556  25.381  1.00 21.32  ? 0   LYS D C   1 
ATOM   5065  O O   . LYS D  1 8   ? -7.360  35.264  26.145  1.00 16.63  ? 0   LYS D O   1 
ATOM   5066  C CB  . LYS D  1 8   ? -10.566 34.517  25.666  1.00 15.71  ? 0   LYS D CB  1 
ATOM   5067  C CG  . LYS D  1 8   ? -10.009 33.278  26.328  1.00 16.37  ? 0   LYS D CG  1 
ATOM   5068  C CD  . LYS D  1 8   ? -10.951 32.105  26.229  1.00 15.86  ? 0   LYS D CD  1 
ATOM   5069  C CE  . LYS D  1 8   ? -10.508 30.987  27.149  1.00 13.98  ? 0   LYS D CE  1 
ATOM   5070  N NZ  . LYS D  1 8   ? -10.748 29.668  26.507  1.00 18.33  ? 0   LYS D NZ  1 
ATOM   5071  N N   . LEU D  1 9   ? -8.125  35.736  24.072  1.00 20.81  ? 1   LEU D N   1 
ATOM   5072  C CA  . LEU D  1 9   ? -6.819  35.550  23.474  1.00 15.89  ? 1   LEU D CA  1 
ATOM   5073  C C   . LEU D  1 9   ? -5.821  36.565  24.040  1.00 19.82  ? 1   LEU D C   1 
ATOM   5074  O O   . LEU D  1 9   ? -4.660  36.234  24.267  1.00 20.14  ? 1   LEU D O   1 
ATOM   5075  C CB  . LEU D  1 9   ? -6.882  35.582  21.947  1.00 21.12  ? 1   LEU D CB  1 
ATOM   5076  C CG  . LEU D  1 9   ? -5.578  35.145  21.263  1.00 23.21  ? 1   LEU D CG  1 
ATOM   5077  C CD1 . LEU D  1 9   ? -5.071  33.803  21.809  1.00 17.53  ? 1   LEU D CD1 1 
ATOM   5078  C CD2 . LEU D  1 9   ? -5.755  35.091  19.763  1.00 20.12  ? 1   LEU D CD2 1 
ATOM   5079  N N   . ASP D  1 10  ? -6.275  37.785  24.312  1.00 22.32  ? 2   ASP D N   1 
ATOM   5080  C CA  . ASP D  1 10  ? -5.433  38.742  25.040  1.00 22.41  ? 2   ASP D CA  1 
ATOM   5081  C C   . ASP D  1 10  ? -5.062  38.260  26.445  1.00 20.32  ? 2   ASP D C   1 
ATOM   5082  O O   . ASP D  1 10  ? -3.885  38.302  26.821  1.00 19.27  ? 2   ASP D O   1 
ATOM   5083  C CB  . ASP D  1 10  ? -6.089  40.119  25.143  1.00 25.02  ? 2   ASP D CB  1 
ATOM   5084  C CG  . ASP D  1 10  ? -5.983  40.918  23.867  1.00 34.03  ? 2   ASP D CG  1 
ATOM   5085  O OD1 . ASP D  1 10  ? -5.208  40.529  22.961  1.00 43.36  ? 2   ASP D OD1 1 
ATOM   5086  O OD2 . ASP D  1 10  ? -6.674  41.955  23.781  1.00 38.36  ? 2   ASP D OD2 1 
ATOM   5087  N N   . ARG D  1 11  ? -6.054  37.816  27.221  1.00 17.61  ? 3   ARG D N   1 
ATOM   5088  C CA  . ARG D  1 11  ? -5.781  37.331  28.577  1.00 16.33  ? 3   ARG D CA  1 
ATOM   5089  C C   . ARG D  1 11  ? -4.805  36.170  28.536  1.00 10.81  ? 3   ARG D C   1 
ATOM   5090  O O   . ARG D  1 11  ? -3.812  36.166  29.242  1.00 8.17   ? 3   ARG D O   1 
ATOM   5091  C CB  . ARG D  1 11  ? -7.065  36.917  29.310  1.00 18.50  ? 3   ARG D CB  1 
ATOM   5092  C CG  . ARG D  1 11  ? -8.062  38.035  29.514  1.00 16.06  ? 3   ARG D CG  1 
ATOM   5093  C CD  . ARG D  1 11  ? -9.302  37.542  30.229  1.00 15.31  ? 3   ARG D CD  1 
ATOM   5094  N NE  . ARG D  1 11  ? -9.025  37.449  31.651  1.00 18.62  ? 3   ARG D NE  1 
ATOM   5095  C CZ  . ARG D  1 11  ? -9.177  38.455  32.504  1.00 17.38  ? 3   ARG D CZ  1 
ATOM   5096  N NH1 . ARG D  1 11  ? -9.630  39.622  32.072  1.00 18.85  ? 3   ARG D NH1 1 
ATOM   5097  N NH2 . ARG D  1 11  ? -8.868  38.292  33.784  1.00 14.48  ? 3   ARG D NH2 1 
ATOM   5098  N N   . ALA D  1 12  ? -5.081  35.202  27.672  1.00 12.39  ? 4   ALA D N   1 
ATOM   5099  C CA  . ALA D  1 12  ? -4.191  34.064  27.499  1.00 11.72  ? 4   ALA D CA  1 
ATOM   5100  C C   . ALA D  1 12  ? -2.762  34.481  27.108  1.00 14.19  ? 4   ALA D C   1 
ATOM   5101  O O   . ALA D  1 12  ? -1.795  33.946  27.657  1.00 13.31  ? 4   ALA D O   1 
ATOM   5102  C CB  . ALA D  1 12  ? -4.768  33.095  26.487  1.00 11.18  ? 4   ALA D CB  1 
ATOM   5103  N N   . ASP D  1 13  ? -2.624  35.442  26.193  1.00 10.02  ? 5   ASP D N   1 
ATOM   5104  C CA  . ASP D  1 13  ? -1.291  35.900  25.772  1.00 12.55  ? 5   ASP D CA  1 
ATOM   5105  C C   . ASP D  1 13  ? -0.528  36.677  26.845  1.00 15.07  ? 5   ASP D C   1 
ATOM   5106  O O   . ASP D  1 13  ? 0.711   36.622  26.897  1.00 10.17  ? 5   ASP D O   1 
ATOM   5107  C CB  . ASP D  1 13  ? -1.361  36.765  24.514  1.00 14.87  ? 5   ASP D CB  1 
ATOM   5108  C CG  . ASP D  1 13  ? -1.737  35.978  23.289  1.00 17.54  ? 5   ASP D CG  1 
ATOM   5109  O OD1 . ASP D  1 13  ? -1.742  34.735  23.369  1.00 18.40  ? 5   ASP D OD1 1 
ATOM   5110  O OD2 . ASP D  1 13  ? -2.032  36.603  22.250  1.00 24.91  ? 5   ASP D OD2 1 
ATOM   5111  N N   . ILE D  1 14  ? -1.267  37.421  27.672  1.00 14.53  ? 6   ILE D N   1 
ATOM   5112  C CA  . ILE D  1 14  ? -0.691  38.101  28.824  1.00 9.88   ? 6   ILE D CA  1 
ATOM   5113  C C   . ILE D  1 14  ? -0.180  37.084  29.818  1.00 8.86   ? 6   ILE D C   1 
ATOM   5114  O O   . ILE D  1 14  ? 0.856   37.280  30.439  1.00 7.98   ? 6   ILE D O   1 
ATOM   5115  C CB  . ILE D  1 14  ? -1.712  39.027  29.508  1.00 14.67  ? 6   ILE D CB  1 
ATOM   5116  C CG1 . ILE D  1 14  ? -1.954  40.266  28.636  1.00 13.15  ? 6   ILE D CG1 1 
ATOM   5117  C CG2 . ILE D  1 14  ? -1.218  39.450  30.896  1.00 12.01  ? 6   ILE D CG2 1 
ATOM   5118  C CD1 . ILE D  1 14  ? -3.138  41.090  29.040  1.00 16.77  ? 6   ILE D CD1 1 
ATOM   5119  N N   . LEU D  1 15  ? -0.899  35.978  29.950  1.00 10.33  ? 7   LEU D N   1 
ATOM   5120  C CA  . LEU D  1 15  ? -0.484  34.936  30.877  1.00 10.18  ? 7   LEU D CA  1 
ATOM   5121  C C   . LEU D  1 15  ? 0.817   34.337  30.397  1.00 9.04   ? 7   LEU D C   1 
ATOM   5122  O O   . LEU D  1 15  ? 1.747   34.135  31.173  1.00 8.83   ? 7   LEU D O   1 
ATOM   5123  C CB  . LEU D  1 15  ? -1.541  33.845  30.992  1.00 10.74  ? 7   LEU D CB  1 
ATOM   5124  C CG  . LEU D  1 15  ? -1.378  33.029  32.269  1.00 12.95  ? 7   LEU D CG  1 
ATOM   5125  C CD1 . LEU D  1 15  ? -1.760  33.877  33.484  1.00 12.40  ? 7   LEU D CD1 1 
ATOM   5126  C CD2 . LEU D  1 15  ? -2.190  31.752  32.203  1.00 12.26  ? 7   LEU D CD2 1 
ATOM   5127  N N   . TYR D  1 16  ? 0.867   34.054  29.101  1.00 10.81  ? 8   TYR D N   1 
ATOM   5128  C CA  . TYR D  1 16  ? 2.097   33.635  28.435  1.00 8.36   ? 8   TYR D CA  1 
ATOM   5129  C C   . TYR D  1 16  ? 3.268   34.587  28.686  1.00 9.01   ? 8   TYR D C   1 
ATOM   5130  O O   . TYR D  1 16  ? 4.346   34.153  29.079  1.00 10.08  ? 8   TYR D O   1 
ATOM   5131  C CB  . TYR D  1 16  ? 1.858   33.461  26.939  1.00 9.54   ? 8   TYR D CB  1 
ATOM   5132  C CG  . TYR D  1 16  ? 3.115   33.172  26.138  1.00 16.26  ? 8   TYR D CG  1 
ATOM   5133  C CD1 . TYR D  1 16  ? 3.812   31.967  26.285  1.00 13.21  ? 8   TYR D CD1 1 
ATOM   5134  C CD2 . TYR D  1 16  ? 3.599   34.101  25.216  1.00 12.61  ? 8   TYR D CD2 1 
ATOM   5135  C CE1 . TYR D  1 16  ? 4.949   31.710  25.550  1.00 10.87  ? 8   TYR D CE1 1 
ATOM   5136  C CE2 . TYR D  1 16  ? 4.717   33.848  24.478  1.00 12.32  ? 8   TYR D CE2 1 
ATOM   5137  C CZ  . TYR D  1 16  ? 5.389   32.659  24.642  1.00 12.66  ? 8   TYR D CZ  1 
ATOM   5138  O OH  . TYR D  1 16  ? 6.511   32.446  23.888  1.00 9.50   ? 8   TYR D OH  1 
ATOM   5139  N N   . ASN D  1 17  ? 3.066   35.884  28.485  1.00 8.98   ? 9   ASN D N   1 
ATOM   5140  C CA  . ASN D  1 17  ? 4.143   36.828  28.739  1.00 6.43   ? 9   ASN D CA  1 
ATOM   5141  C C   . ASN D  1 17  ? 4.589   36.803  30.194  1.00 9.40   ? 9   ASN D C   1 
ATOM   5142  O O   . ASN D  1 17  ? 5.781   36.700  30.465  1.00 12.67  ? 9   ASN D O   1 
ATOM   5143  C CB  . ASN D  1 17  ? 3.765   38.244  28.322  1.00 6.59   ? 9   ASN D CB  1 
ATOM   5144  C CG  . ASN D  1 17  ? 3.295   38.332  26.891  1.00 12.13  ? 9   ASN D CG  1 
ATOM   5145  O OD1 . ASN D  1 17  ? 2.609   39.273  26.524  1.00 18.97  ? 9   ASN D OD1 1 
ATOM   5146  N ND2 . ASN D  1 17  ? 3.657   37.353  26.072  1.00 14.44  ? 9   ASN D ND2 1 
ATOM   5147  N N   . ILE D  1 18  ? 3.639   36.879  31.129  1.00 8.73   ? 10  ILE D N   1 
ATOM   5148  C CA  . ILE D  1 18  ? 3.958   36.826  32.557  1.00 7.30   ? 10  ILE D CA  1 
ATOM   5149  C C   . ILE D  1 18  ? 4.740   35.565  32.906  1.00 8.24   ? 10  ILE D C   1 
ATOM   5150  O O   . ILE D  1 18  ? 5.764   35.648  33.547  1.00 13.23  ? 10  ILE D O   1 
ATOM   5151  C CB  . ILE D  1 18  ? 2.697   36.964  33.454  1.00 10.29  ? 10  ILE D CB  1 
ATOM   5152  C CG1 . ILE D  1 18  ? 2.111   38.369  33.339  1.00 9.40   ? 10  ILE D CG1 1 
ATOM   5153  C CG2 . ILE D  1 18  ? 3.026   36.674  34.905  1.00 11.05  ? 10  ILE D CG2 1 
ATOM   5154  C CD1 . ILE D  1 18  ? 0.696   38.493  33.823  1.00 6.85   ? 10  ILE D CD1 1 
ATOM   5155  N N   . ARG D  1 19  ? 4.304   34.399  32.447  1.00 8.64   ? 11  ARG D N   1 
ATOM   5156  C CA  . ARG D  1 19  ? 5.033   33.162  32.766  1.00 10.71  ? 11  ARG D CA  1 
ATOM   5157  C C   . ARG D  1 19  ? 6.429   33.035  32.135  1.00 12.41  ? 11  ARG D C   1 
ATOM   5158  O O   . ARG D  1 19  ? 7.214   32.155  32.496  1.00 15.12  ? 11  ARG D O   1 
ATOM   5159  C CB  . ARG D  1 19  ? 4.193   31.944  32.406  1.00 11.19  ? 11  ARG D CB  1 
ATOM   5160  C CG  . ARG D  1 19  ? 3.055   31.691  33.375  1.00 14.16  ? 11  ARG D CG  1 
ATOM   5161  C CD  . ARG D  1 19  ? 2.130   30.624  32.876  1.00 12.31  ? 11  ARG D CD  1 
ATOM   5162  N NE  . ARG D  1 19  ? 1.274   30.152  33.949  1.00 15.04  ? 11  ARG D NE  1 
ATOM   5163  C CZ  . ARG D  1 19  ? 0.161   29.449  33.761  1.00 18.32  ? 11  ARG D CZ  1 
ATOM   5164  N NH1 . ARG D  1 19  ? -0.241  29.128  32.526  1.00 17.32  ? 11  ARG D NH1 1 
ATOM   5165  N NH2 . ARG D  1 19  ? -0.554  29.072  34.809  1.00 11.25  ? 11  ARG D NH2 1 
ATOM   5166  N N   . GLN D  1 20  ? 6.743   33.902  31.187  1.00 12.57  ? 12  GLN D N   1 
ATOM   5167  C CA  . GLN D  1 20  ? 8.051   33.859  30.549  1.00 11.32  ? 12  GLN D CA  1 
ATOM   5168  C C   . GLN D  1 20  ? 9.040   34.797  31.229  1.00 12.08  ? 12  GLN D C   1 
ATOM   5169  O O   . GLN D  1 20  ? 10.220  34.491  31.376  1.00 12.44  ? 12  GLN D O   1 
ATOM   5170  C CB  . GLN D  1 20  ? 7.901   34.259  29.109  1.00 10.79  ? 12  GLN D CB  1 
ATOM   5171  C CG  . GLN D  1 20  ? 7.130   33.272  28.301  1.00 13.12  ? 12  GLN D CG  1 
ATOM   5172  C CD  . GLN D  1 20  ? 7.895   32.846  27.100  1.00 12.87  ? 12  GLN D CD  1 
ATOM   5173  O OE1 . GLN D  1 20  ? 8.156   33.653  26.201  1.00 15.69  ? 12  GLN D OE1 1 
ATOM   5174  N NE2 . GLN D  1 20  ? 8.309   31.585  27.084  1.00 11.23  ? 12  GLN D NE2 1 
ATOM   5175  N N   . THR D  1 21  ? 8.540   35.947  31.646  1.00 9.94   ? 13  THR D N   1 
ATOM   5176  C CA  . THR D  1 21  ? 9.354   36.914  32.332  1.00 11.74  ? 13  THR D CA  1 
ATOM   5177  C C   . THR D  1 21  ? 9.607   36.494  33.771  1.00 13.47  ? 13  THR D C   1 
ATOM   5178  O O   . THR D  1 21  ? 10.715  36.629  34.280  1.00 18.27  ? 13  THR D O   1 
ATOM   5179  C CB  . THR D  1 21  ? 8.638   38.248  32.358  1.00 17.46  ? 13  THR D CB  1 
ATOM   5180  O OG1 . THR D  1 21  ? 8.713   38.829  31.059  1.00 14.84  ? 13  THR D OG1 1 
ATOM   5181  C CG2 . THR D  1 21  ? 9.269   39.191  33.400  1.00 18.46  ? 13  THR D CG2 1 
ATOM   5182  N N   . SER D  1 22  ? 8.567   35.974  34.411  1.00 12.69  ? 14  SER D N   1 
ATOM   5183  C CA  . SER D  1 22  ? 8.558   35.740  35.851  1.00 11.37  ? 14  SER D CA  1 
ATOM   5184  C C   . SER D  1 22  ? 9.596   34.751  36.378  1.00 11.91  ? 14  SER D C   1 
ATOM   5185  O O   . SER D  1 22  ? 9.677   33.599  35.941  1.00 11.39  ? 14  SER D O   1 
ATOM   5186  C CB  . SER D  1 22  ? 7.160   35.325  36.306  1.00 10.68  ? 14  SER D CB  1 
ATOM   5187  O OG  . SER D  1 22  ? 7.225   34.530  37.474  1.00 15.91  ? 14  SER D OG  1 
ATOM   5188  N N   . ARG D  1 23  ? 10.392  35.226  37.325  1.00 12.53  ? 15  ARG D N   1 
ATOM   5189  C CA  . ARG D  1 23  ? 11.287  34.369  38.084  1.00 14.09  ? 15  ARG D CA  1 
ATOM   5190  C C   . ARG D  1 23  ? 10.718  34.193  39.497  1.00 12.07  ? 15  ARG D C   1 
ATOM   5191  O O   . ARG D  1 23  ? 10.959  35.028  40.363  1.00 11.08  ? 15  ARG D O   1 
ATOM   5192  C CB  . ARG D  1 23  ? 12.673  34.998  38.184  1.00 13.54  ? 15  ARG D CB  1 
ATOM   5193  C CG  . ARG D  1 23  ? 13.151  35.697  36.939  1.00 12.67  ? 15  ARG D CG  1 
ATOM   5194  C CD  . ARG D  1 23  ? 14.520  35.166  36.524  1.00 20.71  ? 15  ARG D CD  1 
ATOM   5195  N NE  . ARG D  1 23  ? 15.195  36.116  35.649  1.00 25.79  ? 15  ARG D NE  1 
ATOM   5196  C CZ  . ARG D  1 23  ? 16.262  35.845  34.910  1.00 21.82  ? 15  ARG D CZ  1 
ATOM   5197  N NH1 . ARG D  1 23  ? 16.801  34.630  34.915  1.00 19.82  ? 15  ARG D NH1 1 
ATOM   5198  N NH2 . ARG D  1 23  ? 16.783  36.803  34.154  1.00 26.74  ? 15  ARG D NH2 1 
ATOM   5199  N N   . PRO D  1 24  ? 9.975   33.097  39.724  1.00 11.09  ? 16  PRO D N   1 
ATOM   5200  C CA  . PRO D  1 24  ? 9.299   32.736  40.967  1.00 10.71  ? 16  PRO D CA  1 
ATOM   5201  C C   . PRO D  1 24  ? 10.198  32.655  42.197  1.00 10.98  ? 16  PRO D C   1 
ATOM   5202  O O   . PRO D  1 24  ? 9.704   32.772  43.330  1.00 15.19  ? 16  PRO D O   1 
ATOM   5203  C CB  . PRO D  1 24  ? 8.747   31.350  40.647  1.00 12.41  ? 16  PRO D CB  1 
ATOM   5204  C CG  . PRO D  1 24  ? 8.552   31.361  39.207  1.00 9.29   ? 16  PRO D CG  1 
ATOM   5205  C CD  . PRO D  1 24  ? 9.710   32.095  38.678  1.00 10.97  ? 16  PRO D CD  1 
ATOM   5206  N N   . ASP D  1 25  ? 11.491  32.459  41.995  1.00 9.74   ? 17  ASP D N   1 
ATOM   5207  C CA  . ASP D  1 25  ? 12.396  32.271  43.118  1.00 7.38   ? 17  ASP D CA  1 
ATOM   5208  C C   . ASP D  1 25  ? 13.353  33.432  43.349  1.00 9.97   ? 17  ASP D C   1 
ATOM   5209  O O   . ASP D  1 25  ? 14.173  33.376  44.256  1.00 11.59  ? 17  ASP D O   1 
ATOM   5210  C CB  . ASP D  1 25  ? 13.170  30.970  42.954  1.00 8.51   ? 17  ASP D CB  1 
ATOM   5211  C CG  . ASP D  1 25  ? 12.263  29.744  42.996  1.00 15.20  ? 17  ASP D CG  1 
ATOM   5212  O OD1 . ASP D  1 25  ? 11.214  29.822  43.682  1.00 23.45  ? 17  ASP D OD1 1 
ATOM   5213  O OD2 . ASP D  1 25  ? 12.595  28.704  42.364  1.00 13.42  ? 17  ASP D OD2 1 
ATOM   5214  N N   . VAL D  1 26  ? 13.241  34.489  42.547  1.00 10.37  ? 18  VAL D N   1 
ATOM   5215  C CA  . VAL D  1 26  ? 14.179  35.607  42.630  1.00 11.44  ? 18  VAL D CA  1 
ATOM   5216  C C   . VAL D  1 26  ? 13.463  36.886  43.004  1.00 11.00  ? 18  VAL D C   1 
ATOM   5217  O O   . VAL D  1 26  ? 12.466  37.230  42.373  1.00 12.85  ? 18  VAL D O   1 
ATOM   5218  C CB  . VAL D  1 26  ? 14.914  35.846  41.281  1.00 12.51  ? 18  VAL D CB  1 
ATOM   5219  C CG1 . VAL D  1 26  ? 15.955  36.957  41.439  1.00 10.14  ? 18  VAL D CG1 1 
ATOM   5220  C CG2 . VAL D  1 26  ? 15.531  34.557  40.769  1.00 7.49   ? 18  VAL D CG2 1 
ATOM   5221  N N   . ILE D  1 27  ? 13.964  37.597  44.016  1.00 13.79  ? 19  ILE D N   1 
ATOM   5222  C CA  . ILE D  1 27  ? 13.299  38.826  44.481  1.00 14.96  ? 19  ILE D CA  1 
ATOM   5223  C C   . ILE D  1 27  ? 13.332  39.951  43.435  1.00 14.97  ? 19  ILE D C   1 
ATOM   5224  O O   . ILE D  1 27  ? 14.385  40.275  42.905  1.00 15.87  ? 19  ILE D O   1 
ATOM   5225  C CB  . ILE D  1 27  ? 13.858  39.324  45.843  1.00 13.31  ? 19  ILE D CB  1 
ATOM   5226  C CG1 . ILE D  1 27  ? 15.301  39.786  45.727  1.00 16.39  ? 19  ILE D CG1 1 
ATOM   5227  C CG2 . ILE D  1 27  ? 13.793  38.227  46.878  1.00 16.35  ? 19  ILE D CG2 1 
ATOM   5228  C CD1 . ILE D  1 27  ? 15.828  40.387  46.997  1.00 15.97  ? 19  ILE D CD1 1 
ATOM   5229  N N   . PRO D  1 28  ? 12.165  40.543  43.136  1.00 16.28  ? 20  PRO D N   1 
ATOM   5230  C CA  . PRO D  1 28  ? 11.999  41.549  42.079  1.00 16.05  ? 20  PRO D CA  1 
ATOM   5231  C C   . PRO D  1 28  ? 12.549  42.925  42.448  1.00 16.84  ? 20  PRO D C   1 
ATOM   5232  O O   . PRO D  1 28  ? 11.830  43.918  42.369  1.00 19.93  ? 20  PRO D O   1 
ATOM   5233  C CB  . PRO D  1 28  ? 10.472  41.623  41.906  1.00 14.25  ? 20  PRO D CB  1 
ATOM   5234  C CG  . PRO D  1 28  ? 9.932   41.249  43.210  1.00 9.32   ? 20  PRO D CG  1 
ATOM   5235  C CD  . PRO D  1 28  ? 10.885  40.225  43.788  1.00 12.03  ? 20  PRO D CD  1 
ATOM   5236  N N   . THR D  1 29  ? 13.811  42.983  42.847  1.00 21.65  ? 21  THR D N   1 
ATOM   5237  C CA  . THR D  1 29  ? 14.448  44.247  43.185  1.00 26.41  ? 21  THR D CA  1 
ATOM   5238  C C   . THR D  1 29  ? 14.750  45.024  41.917  1.00 33.07  ? 21  THR D C   1 
ATOM   5239  O O   . THR D  1 29  ? 15.669  44.674  41.190  1.00 27.15  ? 21  THR D O   1 
ATOM   5240  C CB  . THR D  1 29  ? 15.793  44.007  43.869  1.00 21.81  ? 21  THR D CB  1 
ATOM   5241  O OG1 . THR D  1 29  ? 16.502  43.008  43.139  1.00 22.92  ? 21  THR D OG1 1 
ATOM   5242  C CG2 . THR D  1 29  ? 15.596  43.503  45.268  1.00 27.34  ? 21  THR D CG2 1 
ATOM   5243  N N   . GLN D  1 30  ? 14.069  46.147  41.726  1.00 38.57  ? 22  GLN D N   1 
ATOM   5244  C CA  . GLN D  1 30  ? 14.387  47.042  40.621  1.00 43.09  ? 22  GLN D CA  1 
ATOM   5245  C C   . GLN D  1 30  ? 15.345  48.154  41.062  1.00 47.94  ? 22  GLN D C   1 
ATOM   5246  O O   . GLN D  1 30  ? 15.127  48.807  42.083  1.00 50.08  ? 22  GLN D O   1 
ATOM   5247  C CB  . GLN D  1 30  ? 13.109  47.649  40.038  1.00 47.03  ? 22  GLN D CB  1 
ATOM   5248  C CG  . GLN D  1 30  ? 12.193  48.281  41.073  1.00 48.50  ? 22  GLN D CG  1 
ATOM   5249  C CD  . GLN D  1 30  ? 10.907  48.809  40.469  1.00 53.08  ? 22  GLN D CD  1 
ATOM   5250  O OE1 . GLN D  1 30  ? 10.721  50.019  40.336  1.00 56.68  ? 22  GLN D OE1 1 
ATOM   5251  N NE2 . GLN D  1 30  ? 10.010  47.902  40.099  1.00 32.30  ? 22  GLN D NE2 1 
ATOM   5252  N N   . ARG D  1 31  ? 16.401  48.363  40.279  1.00 50.21  ? 23  ARG D N   1 
ATOM   5253  C CA  . ARG D  1 31  ? 17.372  49.434  40.524  1.00 53.56  ? 23  ARG D CA  1 
ATOM   5254  C C   . ARG D  1 31  ? 18.096  49.404  41.877  1.00 54.17  ? 23  ARG D C   1 
ATOM   5255  O O   . ARG D  1 31  ? 18.308  50.449  42.492  1.00 54.34  ? 23  ARG D O   1 
ATOM   5256  C CB  . ARG D  1 31  ? 16.707  50.801  40.328  1.00 48.74  ? 23  ARG D CB  1 
ATOM   5257  C CG  . ARG D  1 31  ? 16.050  50.982  38.969  1.00 48.13  ? 23  ARG D CG  1 
ATOM   5258  C CD  . ARG D  1 31  ? 15.269  52.285  38.903  1.00 57.28  ? 23  ARG D CD  1 
ATOM   5259  N NE  . ARG D  1 31  ? 13.833  52.055  38.771  1.00 64.76  ? 23  ARG D NE  1 
ATOM   5260  C CZ  . ARG D  1 31  ? 12.906  52.987  38.969  1.00 63.27  ? 23  ARG D CZ  1 
ATOM   5261  N NH1 . ARG D  1 31  ? 13.263  54.218  39.310  1.00 65.63  ? 23  ARG D NH1 1 
ATOM   5262  N NH2 . ARG D  1 31  ? 11.622  52.689  38.826  1.00 65.42  ? 23  ARG D NH2 1 
ATOM   5263  N N   . ASP D  1 32  ? 18.478  48.214  42.333  1.00 51.94  ? 24  ASP D N   1 
ATOM   5264  C CA  . ASP D  1 32  ? 19.244  48.075  43.581  1.00 47.52  ? 24  ASP D CA  1 
ATOM   5265  C C   . ASP D  1 32  ? 18.541  48.620  44.833  1.00 48.74  ? 24  ASP D C   1 
ATOM   5266  O O   . ASP D  1 32  ? 19.191  48.928  45.835  1.00 48.35  ? 24  ASP D O   1 
ATOM   5267  C CB  . ASP D  1 32  ? 20.653  48.671  43.453  1.00 42.99  ? 24  ASP D CB  1 
ATOM   5268  C CG  . ASP D  1 32  ? 21.734  47.603  43.428  1.00 45.94  ? 24  ASP D CG  1 
ATOM   5269  O OD1 . ASP D  1 32  ? 22.154  47.145  44.511  1.00 44.07  ? 24  ASP D OD1 1 
ATOM   5270  O OD2 . ASP D  1 32  ? 22.162  47.214  42.323  1.00 49.94  ? 24  ASP D OD2 1 
ATOM   5271  N N   . ARG D  1 33  ? 17.218  48.741  44.765  1.00 46.47  ? 25  ARG D N   1 
ATOM   5272  C CA  . ARG D  1 33  ? 16.423  49.104  45.928  1.00 38.03  ? 25  ARG D CA  1 
ATOM   5273  C C   . ARG D  1 33  ? 15.689  47.865  46.420  1.00 31.84  ? 25  ARG D C   1 
ATOM   5274  O O   . ARG D  1 33  ? 15.351  46.989  45.624  1.00 26.30  ? 25  ARG D O   1 
ATOM   5275  C CB  . ARG D  1 33  ? 15.417  50.204  45.577  1.00 46.81  ? 25  ARG D CB  1 
ATOM   5276  C CG  . ARG D  1 33  ? 16.036  51.565  45.310  1.00 55.17  ? 25  ARG D CG  1 
ATOM   5277  C CD  . ARG D  1 33  ? 14.969  52.606  44.960  1.00 65.10  ? 25  ARG D CD  1 
ATOM   5278  N NE  . ARG D  1 33  ? 15.306  53.322  43.728  1.00 80.89  ? 25  ARG D NE  1 
ATOM   5279  C CZ  . ARG D  1 33  ? 14.572  54.295  43.192  1.00 79.93  ? 25  ARG D CZ  1 
ATOM   5280  N NH1 . ARG D  1 33  ? 13.445  54.684  43.784  1.00 70.11  ? 25  ARG D NH1 1 
ATOM   5281  N NH2 . ARG D  1 33  ? 14.971  54.881  42.061  1.00 64.55  ? 25  ARG D NH2 1 
ATOM   5282  N N   . PRO D  1 34  ? 15.448  47.785  47.738  1.00 29.83  ? 26  PRO D N   1 
ATOM   5283  C CA  . PRO D  1 34  ? 14.683  46.686  48.332  1.00 27.48  ? 26  PRO D CA  1 
ATOM   5284  C C   . PRO D  1 34  ? 13.305  46.606  47.696  1.00 19.52  ? 26  PRO D C   1 
ATOM   5285  O O   . PRO D  1 34  ? 12.769  47.639  47.317  1.00 23.88  ? 26  PRO D O   1 
ATOM   5286  C CB  . PRO D  1 34  ? 14.537  47.120  49.796  1.00 26.21  ? 26  PRO D CB  1 
ATOM   5287  C CG  . PRO D  1 34  ? 15.638  48.075  50.035  1.00 22.84  ? 26  PRO D CG  1 
ATOM   5288  C CD  . PRO D  1 34  ? 15.869  48.772  48.746  1.00 27.60  ? 26  PRO D CD  1 
ATOM   5289  N N   . VAL D  1 35  ? 12.742  45.417  47.558  1.00 15.26  ? 27  VAL D N   1 
ATOM   5290  C CA  . VAL D  1 35  ? 11.359  45.335  47.118  1.00 16.86  ? 27  VAL D CA  1 
ATOM   5291  C C   . VAL D  1 35  ? 10.460  45.936  48.216  1.00 19.46  ? 27  VAL D C   1 
ATOM   5292  O O   . VAL D  1 35  ? 10.549  45.558  49.382  1.00 17.16  ? 27  VAL D O   1 
ATOM   5293  C CB  . VAL D  1 35  ? 10.944  43.885  46.838  1.00 12.53  ? 27  VAL D CB  1 
ATOM   5294  C CG1 . VAL D  1 35  ? 9.572   43.835  46.242  1.00 11.24  ? 27  VAL D CG1 1 
ATOM   5295  C CG2 . VAL D  1 35  ? 11.907  43.263  45.899  1.00 19.32  ? 27  VAL D CG2 1 
ATOM   5296  N N   . ALA D  1 36  ? 9.616   46.889  47.837  1.00 18.29  ? 28  ALA D N   1 
ATOM   5297  C CA  . ALA D  1 36  ? 8.670   47.489  48.757  1.00 13.12  ? 28  ALA D CA  1 
ATOM   5298  C C   . ALA D  1 36  ? 7.406   46.657  48.776  1.00 16.79  ? 28  ALA D C   1 
ATOM   5299  O O   . ALA D  1 36  ? 6.621   46.689  47.826  1.00 17.50  ? 28  ALA D O   1 
ATOM   5300  C CB  . ALA D  1 36  ? 8.349   48.894  48.331  1.00 9.52   ? 28  ALA D CB  1 
ATOM   5301  N N   . VAL D  1 37  ? 7.211   45.923  49.867  1.00 16.78  ? 29  VAL D N   1 
ATOM   5302  C CA  . VAL D  1 37  ? 6.025   45.099  50.055  1.00 15.54  ? 29  VAL D CA  1 
ATOM   5303  C C   . VAL D  1 37  ? 5.071   45.780  51.046  1.00 16.67  ? 29  VAL D C   1 
ATOM   5304  O O   . VAL D  1 37  ? 5.469   46.184  52.132  1.00 17.16  ? 29  VAL D O   1 
ATOM   5305  C CB  . VAL D  1 37  ? 6.417   43.676  50.561  1.00 18.21  ? 29  VAL D CB  1 
ATOM   5306  C CG1 . VAL D  1 37  ? 5.182   42.807  50.827  1.00 13.16  ? 29  VAL D CG1 1 
ATOM   5307  C CG2 . VAL D  1 37  ? 7.361   42.990  49.577  1.00 13.37  ? 29  VAL D CG2 1 
ATOM   5308  N N   . SER D  1 38  ? 3.816   45.926  50.640  1.00 18.02  ? 30  SER D N   1 
ATOM   5309  C CA  . SER D  1 38  ? 2.764   46.475  51.479  1.00 18.67  ? 30  SER D CA  1 
ATOM   5310  C C   . SER D  1 38  ? 1.914   45.353  52.035  1.00 17.60  ? 30  SER D C   1 
ATOM   5311  O O   . SER D  1 38  ? 1.360   44.574  51.273  1.00 21.35  ? 30  SER D O   1 
ATOM   5312  C CB  . SER D  1 38  ? 1.854   47.378  50.648  1.00 16.59  ? 30  SER D CB  1 
ATOM   5313  O OG  . SER D  1 38  ? 2.431   48.650  50.466  1.00 20.75  ? 30  SER D OG  1 
ATOM   5314  N N   . VAL D  1 39  ? 1.791   45.274  53.353  1.00 17.37  ? 31  VAL D N   1 
ATOM   5315  C CA  . VAL D  1 39  ? 0.862   44.323  53.967  1.00 20.91  ? 31  VAL D CA  1 
ATOM   5316  C C   . VAL D  1 39  ? -0.186  45.024  54.820  1.00 19.36  ? 31  VAL D C   1 
ATOM   5317  O O   . VAL D  1 39  ? 0.125   45.986  55.518  1.00 21.28  ? 31  VAL D O   1 
ATOM   5318  C CB  . VAL D  1 39  ? 1.592   43.328  54.885  1.00 21.33  ? 31  VAL D CB  1 
ATOM   5319  C CG1 . VAL D  1 39  ? 0.837   42.013  54.938  1.00 16.91  ? 31  VAL D CG1 1 
ATOM   5320  C CG2 . VAL D  1 39  ? 2.997   43.107  54.394  1.00 22.71  ? 31  VAL D CG2 1 
ATOM   5321  N N   . SER D  1 40  ? -1.424  44.540  54.762  1.00 19.15  ? 32  SER D N   1 
ATOM   5322  C CA  . SER D  1 40  ? -2.454  44.950  55.712  1.00 18.18  ? 32  SER D CA  1 
ATOM   5323  C C   . SER D  1 40  ? -3.368  43.785  56.047  1.00 21.13  ? 32  SER D C   1 
ATOM   5324  O O   . SER D  1 40  ? -3.850  43.113  55.137  1.00 21.30  ? 32  SER D O   1 
ATOM   5325  C CB  . SER D  1 40  ? -3.296  46.077  55.142  1.00 21.56  ? 32  SER D CB  1 
ATOM   5326  O OG  . SER D  1 40  ? -4.444  46.283  55.943  1.00 24.31  ? 32  SER D OG  1 
ATOM   5327  N N   . LEU D  1 41  ? -3.624  43.552  57.338  1.00 19.45  ? 33  LEU D N   1 
ATOM   5328  C CA  . LEU D  1 41  ? -4.557  42.498  57.752  1.00 14.42  ? 33  LEU D CA  1 
ATOM   5329  C C   . LEU D  1 41  ? -5.967  43.037  57.924  1.00 17.37  ? 33  LEU D C   1 
ATOM   5330  O O   . LEU D  1 41  ? -6.153  44.051  58.573  1.00 21.32  ? 33  LEU D O   1 
ATOM   5331  C CB  . LEU D  1 41  ? -4.116  41.861  59.060  1.00 13.98  ? 33  LEU D CB  1 
ATOM   5332  C CG  . LEU D  1 41  ? -2.683  41.349  59.147  1.00 19.08  ? 33  LEU D CG  1 
ATOM   5333  C CD1 . LEU D  1 41  ? -2.548  40.503  60.388  1.00 16.56  ? 33  LEU D CD1 1 
ATOM   5334  C CD2 . LEU D  1 41  ? -2.255  40.567  57.886  1.00 18.65  ? 33  LEU D CD2 1 
ATOM   5335  N N   . LYS D  1 42  ? -6.956  42.353  57.353  1.00 16.15  ? 34  LYS D N   1 
ATOM   5336  C CA  . LYS D  1 42  ? -8.348  42.770  57.448  1.00 13.20  ? 34  LYS D CA  1 
ATOM   5337  C C   . LYS D  1 42  ? -9.151  41.664  58.104  1.00 14.78  ? 34  LYS D C   1 
ATOM   5338  O O   . LYS D  1 42  ? -9.444  40.647  57.485  1.00 14.70  ? 34  LYS D O   1 
ATOM   5339  C CB  . LYS D  1 42  ? -8.925  43.066  56.072  1.00 14.99  ? 34  LYS D CB  1 
ATOM   5340  C CG  . LYS D  1 42  ? -8.015  43.841  55.168  1.00 20.29  ? 34  LYS D CG  1 
ATOM   5341  C CD  . LYS D  1 42  ? -7.995  45.315  55.503  1.00 23.54  ? 34  LYS D CD  1 
ATOM   5342  C CE  . LYS D  1 42  ? -7.242  46.091  54.433  1.00 22.70  ? 34  LYS D CE  1 
ATOM   5343  N NZ  . LYS D  1 42  ? -7.047  47.480  54.882  1.00 27.86  ? 34  LYS D NZ  1 
ATOM   5344  N N   . PHE D  1 43  ? -9.529  41.879  59.360  1.00 18.03  ? 35  PHE D N   1 
ATOM   5345  C CA  . PHE D  1 43  ? -10.015 40.798  60.201  1.00 9.85   ? 35  PHE D CA  1 
ATOM   5346  C C   . PHE D  1 43  ? -11.445 40.452  59.901  1.00 11.39  ? 35  PHE D C   1 
ATOM   5347  O O   . PHE D  1 43  ? -12.296 41.334  59.785  1.00 14.33  ? 35  PHE D O   1 
ATOM   5348  C CB  . PHE D  1 43  ? -9.864  41.165  61.661  1.00 10.41  ? 35  PHE D CB  1 
ATOM   5349  C CG  . PHE D  1 43  ? -8.450  41.367  62.085  1.00 10.91  ? 35  PHE D CG  1 
ATOM   5350  C CD1 . PHE D  1 43  ? -7.859  42.619  61.991  1.00 10.81  ? 35  PHE D CD1 1 
ATOM   5351  C CD2 . PHE D  1 43  ? -7.711  40.309  62.599  1.00 10.31  ? 35  PHE D CD2 1 
ATOM   5352  C CE1 . PHE D  1 43  ? -6.543  42.815  62.394  1.00 13.68  ? 35  PHE D CE1 1 
ATOM   5353  C CE2 . PHE D  1 43  ? -6.391  40.492  63.001  1.00 11.04  ? 35  PHE D CE2 1 
ATOM   5354  C CZ  . PHE D  1 43  ? -5.803  41.744  62.896  1.00 13.01  ? 35  PHE D CZ  1 
ATOM   5355  N N   . ILE D  1 44  ? -11.706 39.155  59.796  1.00 11.36  ? 36  ILE D N   1 
ATOM   5356  C CA  . ILE D  1 44  ? -13.018 38.676  59.415  1.00 13.23  ? 36  ILE D CA  1 
ATOM   5357  C C   . ILE D  1 44  ? -13.711 38.016  60.595  1.00 14.16  ? 36  ILE D C   1 
ATOM   5358  O O   . ILE D  1 44  ? -14.936 38.113  60.741  1.00 15.80  ? 36  ILE D O   1 
ATOM   5359  C CB  . ILE D  1 44  ? -12.936 37.672  58.248  1.00 13.13  ? 36  ILE D CB  1 
ATOM   5360  C CG1 . ILE D  1 44  ? -12.013 38.209  57.151  1.00 19.04  ? 36  ILE D CG1 1 
ATOM   5361  C CG2 . ILE D  1 44  ? -14.305 37.405  57.680  1.00 11.01  ? 36  ILE D CG2 1 
ATOM   5362  C CD1 . ILE D  1 44  ? -12.456 39.525  56.563  1.00 17.22  ? 36  ILE D CD1 1 
ATOM   5363  N N   . ASN D  1 45  ? -12.939 37.343  61.437  1.00 11.08  ? 37  ASN D N   1 
ATOM   5364  C CA  . ASN D  1 45  ? -13.533 36.648  62.570  1.00 12.75  ? 37  ASN D CA  1 
ATOM   5365  C C   . ASN D  1 45  ? -12.507 36.293  63.641  1.00 14.05  ? 37  ASN D C   1 
ATOM   5366  O O   . ASN D  1 45  ? -11.311 36.201  63.361  1.00 12.44  ? 37  ASN D O   1 
ATOM   5367  C CB  . ASN D  1 45  ? -14.299 35.399  62.100  1.00 12.08  ? 37  ASN D CB  1 
ATOM   5368  C CG  . ASN D  1 45  ? -15.600 35.183  62.877  1.00 14.19  ? 37  ASN D CG  1 
ATOM   5369  O OD1 . ASN D  1 45  ? -15.657 35.431  64.072  1.00 14.95  ? 37  ASN D OD1 1 
ATOM   5370  N ND2 . ASN D  1 45  ? -16.643 34.734  62.195  1.00 11.59  ? 37  ASN D ND2 1 
ATOM   5371  N N   . ILE D  1 46  ? -12.982 36.131  64.873  1.00 14.99  ? 38  ILE D N   1 
ATOM   5372  C CA  . ILE D  1 46  ? -12.190 35.573  65.968  1.00 14.00  ? 38  ILE D CA  1 
ATOM   5373  C C   . ILE D  1 46  ? -13.051 34.442  66.468  1.00 15.90  ? 38  ILE D C   1 
ATOM   5374  O O   . ILE D  1 46  ? -14.227 34.656  66.751  1.00 17.31  ? 38  ILE D O   1 
ATOM   5375  C CB  . ILE D  1 46  ? -11.997 36.594  67.102  1.00 14.46  ? 38  ILE D CB  1 
ATOM   5376  C CG1 . ILE D  1 46  ? -11.346 37.870  66.569  1.00 9.81   ? 38  ILE D CG1 1 
ATOM   5377  C CG2 . ILE D  1 46  ? -11.174 36.009  68.220  1.00 16.45  ? 38  ILE D CG2 1 
ATOM   5378  C CD1 . ILE D  1 46  ? -10.966 38.838  67.617  1.00 7.48   ? 38  ILE D CD1 1 
ATOM   5379  N N   . LEU D  1 47  ? -12.502 33.236  66.559  1.00 18.29  ? 39  LEU D N   1 
ATOM   5380  C CA  . LEU D  1 47  ? -13.351 32.048  66.704  1.00 21.27  ? 39  LEU D CA  1 
ATOM   5381  C C   . LEU D  1 47  ? -13.208 31.344  68.042  1.00 26.17  ? 39  LEU D C   1 
ATOM   5382  O O   . LEU D  1 47  ? -14.139 30.704  68.540  1.00 29.79  ? 39  LEU D O   1 
ATOM   5383  C CB  . LEU D  1 47  ? -13.039 31.042  65.601  1.00 24.82  ? 39  LEU D CB  1 
ATOM   5384  C CG  . LEU D  1 47  ? -13.010 31.494  64.145  1.00 23.91  ? 39  LEU D CG  1 
ATOM   5385  C CD1 . LEU D  1 47  ? -12.268 30.437  63.364  1.00 24.56  ? 39  LEU D CD1 1 
ATOM   5386  C CD2 . LEU D  1 47  ? -14.416 31.662  63.597  1.00 19.20  ? 39  LEU D CD2 1 
ATOM   5387  N N   . GLU D  1 48  ? -12.016 31.439  68.599  1.00 24.45  ? 40  GLU D N   1 
ATOM   5388  C CA  . GLU D  1 48  ? -11.672 30.715  69.797  1.00 30.02  ? 40  GLU D CA  1 
ATOM   5389  C C   . GLU D  1 48  ? -10.610 31.543  70.468  1.00 29.47  ? 40  GLU D C   1 
ATOM   5390  O O   . GLU D  1 48  ? -9.565  31.839  69.889  1.00 30.16  ? 40  GLU D O   1 
ATOM   5391  C CB  . GLU D  1 48  ? -11.131 29.314  69.475  1.00 32.54  ? 40  GLU D CB  1 
ATOM   5392  C CG  . GLU D  1 48  ? -12.199 28.264  69.170  1.00 38.31  ? 40  GLU D CG  1 
ATOM   5393  C CD  . GLU D  1 48  ? -11.764 27.246  68.106  1.00 51.73  ? 40  GLU D CD  1 
ATOM   5394  O OE1 . GLU D  1 48  ? -10.539 27.058  67.896  1.00 49.30  ? 40  GLU D OE1 1 
ATOM   5395  O OE2 . GLU D  1 48  ? -12.659 26.636  67.473  1.00 53.18  ? 40  GLU D OE2 1 
ATOM   5396  N N   . VAL D  1 49  ? -10.915 31.940  71.688  1.00 32.42  ? 41  VAL D N   1 
ATOM   5397  C CA  . VAL D  1 49  ? -10.007 32.679  72.529  1.00 25.99  ? 41  VAL D CA  1 
ATOM   5398  C C   . VAL D  1 49  ? -9.839  31.784  73.754  1.00 25.92  ? 41  VAL D C   1 
ATOM   5399  O O   . VAL D  1 49  ? -10.820 31.454  74.424  1.00 26.15  ? 41  VAL D O   1 
ATOM   5400  C CB  . VAL D  1 49  ? -10.647 34.046  72.894  1.00 27.32  ? 41  VAL D CB  1 
ATOM   5401  C CG1 . VAL D  1 49  ? -10.218 34.517  74.259  1.00 21.91  ? 41  VAL D CG1 1 
ATOM   5402  C CG2 . VAL D  1 49  ? -10.358 35.088  71.825  1.00 20.29  ? 41  VAL D CG2 1 
ATOM   5403  N N   . ASN D  1 50  ? -8.611  31.346  74.008  1.00 22.80  ? 42  ASN D N   1 
ATOM   5404  C CA  . ASN D  1 50  ? -8.320  30.463  75.137  1.00 24.44  ? 42  ASN D CA  1 
ATOM   5405  C C   . ASN D  1 50  ? -7.666  31.210  76.274  1.00 23.04  ? 42  ASN D C   1 
ATOM   5406  O O   . ASN D  1 50  ? -6.456  31.407  76.267  1.00 21.00  ? 42  ASN D O   1 
ATOM   5407  C CB  . ASN D  1 50  ? -7.394  29.314  74.728  1.00 27.89  ? 42  ASN D CB  1 
ATOM   5408  C CG  . ASN D  1 50  ? -7.294  28.237  75.802  1.00 31.69  ? 42  ASN D CG  1 
ATOM   5409  O OD1 . ASN D  1 50  ? -6.745  28.463  76.880  1.00 33.44  ? 42  ASN D OD1 1 
ATOM   5410  N ND2 . ASN D  1 50  ? -7.829  27.060  75.509  1.00 28.97  ? 42  ASN D ND2 1 
ATOM   5411  N N   . GLU D  1 51  ? -8.478  31.584  77.263  1.00 38.17  ? 43  GLU D N   1 
ATOM   5412  C CA  . GLU D  1 51  ? -8.053  32.372  78.427  1.00 32.37  ? 43  GLU D CA  1 
ATOM   5413  C C   . GLU D  1 51  ? -6.996  31.663  79.257  1.00 27.01  ? 43  GLU D C   1 
ATOM   5414  O O   . GLU D  1 51  ? -6.174  32.308  79.906  1.00 25.98  ? 43  GLU D O   1 
ATOM   5415  C CB  . GLU D  1 51  ? -9.261  32.670  79.307  1.00 36.25  ? 43  GLU D CB  1 
ATOM   5416  C CG  . GLU D  1 51  ? -9.660  34.123  79.382  1.00 39.75  ? 43  GLU D CG  1 
ATOM   5417  C CD  . GLU D  1 51  ? -10.943 34.296  80.171  1.00 51.60  ? 43  GLU D CD  1 
ATOM   5418  O OE1 . GLU D  1 51  ? -11.697 33.301  80.282  1.00 43.47  ? 43  GLU D OE1 1 
ATOM   5419  O OE2 . GLU D  1 51  ? -11.189 35.412  80.684  1.00 56.98  ? 43  GLU D OE2 1 
ATOM   5420  N N   . ILE D  1 52  ? -7.028  30.333  79.223  1.00 29.08  ? 44  ILE D N   1 
ATOM   5421  C CA  . ILE D  1 52  ? -6.084  29.506  79.963  1.00 31.62  ? 44  ILE D CA  1 
ATOM   5422  C C   . ILE D  1 52  ? -4.673  29.613  79.383  1.00 34.50  ? 44  ILE D C   1 
ATOM   5423  O O   . ILE D  1 52  ? -3.718  29.930  80.099  1.00 39.30  ? 44  ILE D O   1 
ATOM   5424  C CB  . ILE D  1 52  ? -6.519  28.020  79.948  1.00 33.69  ? 44  ILE D CB  1 
ATOM   5425  C CG1 . ILE D  1 52  ? -7.990  27.873  80.359  1.00 33.37  ? 44  ILE D CG1 1 
ATOM   5426  C CG2 . ILE D  1 52  ? -5.605  27.174  80.817  1.00 27.80  ? 44  ILE D CG2 1 
ATOM   5427  C CD1 . ILE D  1 52  ? -8.318  28.447  81.736  1.00 44.81  ? 44  ILE D CD1 1 
ATOM   5428  N N   . THR D  1 53  ? -4.555  29.376  78.078  1.00 36.37  ? 45  THR D N   1 
ATOM   5429  C CA  . THR D  1 53  ? -3.251  29.187  77.424  1.00 33.21  ? 45  THR D CA  1 
ATOM   5430  C C   . THR D  1 53  ? -2.707  30.370  76.603  1.00 26.91  ? 45  THR D C   1 
ATOM   5431  O O   . THR D  1 53  ? -1.639  30.268  76.015  1.00 27.56  ? 45  THR D O   1 
ATOM   5432  C CB  . THR D  1 53  ? -3.311  27.970  76.514  1.00 26.34  ? 45  THR D CB  1 
ATOM   5433  O OG1 . THR D  1 53  ? -4.151  28.267  75.397  1.00 26.83  ? 45  THR D OG1 1 
ATOM   5434  C CG2 . THR D  1 53  ? -3.919  26.804  77.273  1.00 35.00  ? 45  THR D CG2 1 
ATOM   5435  N N   . ASN D  1 54  ? -3.427  31.486  76.583  1.00 28.49  ? 46  ASN D N   1 
ATOM   5436  C CA  . ASN D  1 54  ? -3.026  32.642  75.792  1.00 28.73  ? 46  ASN D CA  1 
ATOM   5437  C C   . ASN D  1 54  ? -2.957  32.339  74.284  1.00 25.19  ? 46  ASN D C   1 
ATOM   5438  O O   . ASN D  1 54  ? -1.939  32.561  73.649  1.00 28.44  ? 46  ASN D O   1 
ATOM   5439  C CB  . ASN D  1 54  ? -1.696  33.226  76.298  1.00 31.28  ? 46  ASN D CB  1 
ATOM   5440  C CG  . ASN D  1 54  ? -1.881  34.245  77.413  1.00 29.61  ? 46  ASN D CG  1 
ATOM   5441  O OD1 . ASN D  1 54  ? -2.813  35.043  77.391  1.00 32.12  ? 46  ASN D OD1 1 
ATOM   5442  N ND2 . ASN D  1 54  ? -0.978  34.232  78.382  1.00 25.24  ? 46  ASN D ND2 1 
ATOM   5443  N N   . GLU D  1 55  ? -4.045  31.829  73.719  1.00 22.86  ? 47  GLU D N   1 
ATOM   5444  C CA  . GLU D  1 55  ? -4.093  31.522  72.295  1.00 27.57  ? 47  GLU D CA  1 
ATOM   5445  C C   . GLU D  1 55  ? -5.352  32.132  71.687  1.00 27.75  ? 47  GLU D C   1 
ATOM   5446  O O   . GLU D  1 55  ? -6.378  32.195  72.355  1.00 23.07  ? 47  GLU D O   1 
ATOM   5447  C CB  . GLU D  1 55  ? -4.098  30.006  72.043  1.00 26.72  ? 47  GLU D CB  1 
ATOM   5448  C CG  . GLU D  1 55  ? -2.914  29.218  72.596  1.00 23.66  ? 47  GLU D CG  1 
ATOM   5449  C CD  . GLU D  1 55  ? -3.036  27.715  72.310  1.00 31.15  ? 47  GLU D CD  1 
ATOM   5450  O OE1 . GLU D  1 55  ? -3.815  27.344  71.405  1.00 38.36  ? 47  GLU D OE1 1 
ATOM   5451  O OE2 . GLU D  1 55  ? -2.358  26.903  72.983  1.00 30.49  ? 47  GLU D OE2 1 
ATOM   5452  N N   . VAL D  1 56  ? -5.252  32.596  70.437  1.00 24.85  ? 48  VAL D N   1 
ATOM   5453  C CA  . VAL D  1 56  ? -6.402  33.041  69.640  1.00 22.22  ? 48  VAL D CA  1 
ATOM   5454  C C   . VAL D  1 56  ? -6.400  32.324  68.299  1.00 20.68  ? 48  VAL D C   1 
ATOM   5455  O O   . VAL D  1 56  ? -5.353  31.962  67.784  1.00 18.57  ? 48  VAL D O   1 
ATOM   5456  C CB  . VAL D  1 56  ? -6.342  34.551  69.284  1.00 23.27  ? 48  VAL D CB  1 
ATOM   5457  C CG1 . VAL D  1 56  ? -7.294  35.360  70.120  1.00 21.05  ? 48  VAL D CG1 1 
ATOM   5458  C CG2 . VAL D  1 56  ? -4.927  35.072  69.382  1.00 24.71  ? 48  VAL D CG2 1 
ATOM   5459  N N   . ASP D  1 57  ? -7.577  32.150  67.725  1.00 19.21  ? 49  ASP D N   1 
ATOM   5460  C CA  . ASP D  1 57  ? -7.716  31.554  66.416  1.00 18.39  ? 49  ASP D CA  1 
ATOM   5461  C C   . ASP D  1 57  ? -8.436  32.622  65.624  1.00 20.45  ? 49  ASP D C   1 
ATOM   5462  O O   . ASP D  1 57  ? -9.555  32.990  65.973  1.00 26.91  ? 49  ASP D O   1 
ATOM   5463  C CB  . ASP D  1 57  ? -8.580  30.297  66.526  1.00 26.81  ? 49  ASP D CB  1 
ATOM   5464  C CG  . ASP D  1 57  ? -8.566  29.455  65.268  1.00 28.29  ? 49  ASP D CG  1 
ATOM   5465  O OD1 . ASP D  1 57  ? -8.017  29.904  64.245  1.00 30.46  ? 49  ASP D OD1 1 
ATOM   5466  O OD2 . ASP D  1 57  ? -9.120  28.335  65.301  1.00 35.47  ? 49  ASP D OD2 1 
ATOM   5467  N N   . VAL D  1 58  ? -7.800  33.169  64.593  1.00 15.83  ? 50  VAL D N   1 
ATOM   5468  C CA  . VAL D  1 58  ? -8.411  34.289  63.888  1.00 14.33  ? 50  VAL D CA  1 
ATOM   5469  C C   . VAL D  1 58  ? -8.549  34.013  62.401  1.00 14.86  ? 50  VAL D C   1 
ATOM   5470  O O   . VAL D  1 58  ? -7.850  33.162  61.869  1.00 15.47  ? 50  VAL D O   1 
ATOM   5471  C CB  . VAL D  1 58  ? -7.613  35.588  64.095  1.00 13.40  ? 50  VAL D CB  1 
ATOM   5472  C CG1 . VAL D  1 58  ? -7.324  35.812  65.570  1.00 16.97  ? 50  VAL D CG1 1 
ATOM   5473  C CG2 . VAL D  1 58  ? -6.332  35.516  63.354  1.00 19.23  ? 50  VAL D CG2 1 
ATOM   5474  N N   . VAL D  1 59  ? -9.476  34.712  61.748  1.00 12.63  ? 51  VAL D N   1 
ATOM   5475  C CA  . VAL D  1 59  ? -9.618  34.674  60.302  1.00 11.00  ? 51  VAL D CA  1 
ATOM   5476  C C   . VAL D  1 59  ? -9.450  36.087  59.792  1.00 11.32  ? 51  VAL D C   1 
ATOM   5477  O O   . VAL D  1 59  ? -10.172 36.984  60.211  1.00 14.44  ? 51  VAL D O   1 
ATOM   5478  C CB  . VAL D  1 59  ? -11.011 34.166  59.842  1.00 14.29  ? 51  VAL D CB  1 
ATOM   5479  C CG1 . VAL D  1 59  ? -11.171 34.341  58.322  1.00 12.74  ? 51  VAL D CG1 1 
ATOM   5480  C CG2 . VAL D  1 59  ? -11.237 32.715  60.249  1.00 12.25  ? 51  VAL D CG2 1 
ATOM   5481  N N   . PHE D  1 60  ? -8.498  36.283  58.886  1.00 15.42  ? 52  PHE D N   1 
ATOM   5482  C CA  . PHE D  1 60  ? -8.227  37.594  58.296  1.00 13.79  ? 52  PHE D CA  1 
ATOM   5483  C C   . PHE D  1 60  ? -7.880  37.523  56.820  1.00 16.07  ? 52  PHE D C   1 
ATOM   5484  O O   . PHE D  1 60  ? -7.292  36.548  56.366  1.00 14.62  ? 52  PHE D O   1 
ATOM   5485  C CB  . PHE D  1 60  ? -7.066  38.261  59.009  1.00 12.50  ? 52  PHE D CB  1 
ATOM   5486  C CG  . PHE D  1 60  ? -5.829  37.420  59.087  1.00 11.15  ? 52  PHE D CG  1 
ATOM   5487  C CD1 . PHE D  1 60  ? -4.884  37.457  58.086  1.00 13.53  ? 52  PHE D CD1 1 
ATOM   5488  C CD2 . PHE D  1 60  ? -5.593  36.624  60.189  1.00 13.46  ? 52  PHE D CD2 1 
ATOM   5489  C CE1 . PHE D  1 60  ? -3.719  36.702  58.175  1.00 15.60  ? 52  PHE D CE1 1 
ATOM   5490  C CE2 . PHE D  1 60  ? -4.441  35.864  60.294  1.00 16.46  ? 52  PHE D CE2 1 
ATOM   5491  C CZ  . PHE D  1 60  ? -3.500  35.899  59.279  1.00 15.74  ? 52  PHE D CZ  1 
ATOM   5492  N N   . TRP D  1 61  ? -8.239  38.572  56.085  1.00 17.51  ? 53  TRP D N   1 
ATOM   5493  C CA  . TRP D  1 61  ? -7.788  38.767  54.715  1.00 13.57  ? 53  TRP D CA  1 
ATOM   5494  C C   . TRP D  1 61  ? -6.397  39.385  54.757  1.00 14.10  ? 53  TRP D C   1 
ATOM   5495  O O   . TRP D  1 61  ? -6.257  40.548  55.085  1.00 15.76  ? 53  TRP D O   1 
ATOM   5496  C CB  . TRP D  1 61  ? -8.773  39.669  53.955  1.00 14.87  ? 53  TRP D CB  1 
ATOM   5497  C CG  . TRP D  1 61  ? -10.162 39.008  53.777  1.00 26.98  ? 53  TRP D CG  1 
ATOM   5498  C CD1 . TRP D  1 61  ? -10.501 37.716  54.108  1.00 26.17  ? 53  TRP D CD1 1 
ATOM   5499  C CD2 . TRP D  1 61  ? -11.371 39.607  53.247  1.00 26.89  ? 53  TRP D CD2 1 
ATOM   5500  N NE1 . TRP D  1 61  ? -11.829 37.473  53.813  1.00 30.51  ? 53  TRP D NE1 1 
ATOM   5501  C CE2 . TRP D  1 61  ? -12.386 38.609  53.286  1.00 27.09  ? 53  TRP D CE2 1 
ATOM   5502  C CE3 . TRP D  1 61  ? -11.693 40.880  52.750  1.00 23.69  ? 53  TRP D CE3 1 
ATOM   5503  C CZ2 . TRP D  1 61  ? -13.694 38.847  52.849  1.00 23.76  ? 53  TRP D CZ2 1 
ATOM   5504  C CZ3 . TRP D  1 61  ? -12.999 41.111  52.303  1.00 29.03  ? 53  TRP D CZ3 1 
ATOM   5505  C CH2 . TRP D  1 61  ? -13.980 40.097  52.356  1.00 29.13  ? 53  TRP D CH2 1 
ATOM   5506  N N   . GLN D  1 62  ? -5.363  38.606  54.444  1.00 13.73  ? 54  GLN D N   1 
ATOM   5507  C CA  . GLN D  1 62  ? -3.998  39.132  54.434  1.00 16.06  ? 54  GLN D CA  1 
ATOM   5508  C C   . GLN D  1 62  ? -3.699  39.848  53.118  1.00 18.52  ? 54  GLN D C   1 
ATOM   5509  O O   . GLN D  1 62  ? -3.344  39.224  52.124  1.00 19.44  ? 54  GLN D O   1 
ATOM   5510  C CB  . GLN D  1 62  ? -2.973  38.025  54.677  1.00 14.11  ? 54  GLN D CB  1 
ATOM   5511  C CG  . GLN D  1 62  ? -1.530  38.497  54.579  1.00 16.23  ? 54  GLN D CG  1 
ATOM   5512  C CD  . GLN D  1 62  ? -0.515  37.391  54.832  1.00 18.20  ? 54  GLN D CD  1 
ATOM   5513  O OE1 . GLN D  1 62  ? -0.553  36.696  55.861  1.00 25.17  ? 54  GLN D OE1 1 
ATOM   5514  N NE2 . GLN D  1 62  ? 0.397   37.216  53.887  1.00 17.66  ? 54  GLN D NE2 1 
ATOM   5515  N N   . GLN D  1 63  ? -3.852  41.165  53.123  1.00 18.99  ? 55  GLN D N   1 
ATOM   5516  C CA  . GLN D  1 63  ? -3.745  41.956  51.914  1.00 18.16  ? 55  GLN D CA  1 
ATOM   5517  C C   . GLN D  1 63  ? -2.288  42.285  51.635  1.00 20.31  ? 55  GLN D C   1 
ATOM   5518  O O   . GLN D  1 63  ? -1.632  42.933  52.457  1.00 18.37  ? 55  GLN D O   1 
ATOM   5519  C CB  . GLN D  1 63  ? -4.571  43.224  52.060  1.00 18.80  ? 55  GLN D CB  1 
ATOM   5520  C CG  . GLN D  1 63  ? -4.520  44.131  50.872  1.00 24.44  ? 55  GLN D CG  1 
ATOM   5521  C CD  . GLN D  1 63  ? -5.701  45.065  50.826  1.00 29.30  ? 55  GLN D CD  1 
ATOM   5522  O OE1 . GLN D  1 63  ? -6.821  44.693  51.199  1.00 27.01  ? 55  GLN D OE1 1 
ATOM   5523  N NE2 . GLN D  1 63  ? -5.462  46.292  50.375  1.00 29.27  ? 55  GLN D NE2 1 
ATOM   5524  N N   . THR D  1 64  ? -1.783  41.826  50.484  1.00 16.96  ? 56  THR D N   1 
ATOM   5525  C CA  . THR D  1 64  ? -0.357  41.957  50.169  1.00 14.26  ? 56  THR D CA  1 
ATOM   5526  C C   . THR D  1 64  ? -0.148  42.511  48.768  1.00 16.56  ? 56  THR D C   1 
ATOM   5527  O O   . THR D  1 64  ? -0.701  41.989  47.803  1.00 18.50  ? 56  THR D O   1 
ATOM   5528  C CB  . THR D  1 64  ? 0.386   40.615  50.253  1.00 11.99  ? 56  THR D CB  1 
ATOM   5529  O OG1 . THR D  1 64  ? 0.005   39.910  51.439  1.00 19.55  ? 56  THR D OG1 1 
ATOM   5530  C CG2 . THR D  1 64  ? 1.874   40.855  50.305  1.00 15.21  ? 56  THR D CG2 1 
ATOM   5531  N N   . THR D  1 65  ? 0.644   43.570  48.642  1.00 15.43  ? 57  THR D N   1 
ATOM   5532  C CA  . THR D  1 65  ? 0.908   44.144  47.326  1.00 15.56  ? 57  THR D CA  1 
ATOM   5533  C C   . THR D  1 65  ? 2.383   44.509  47.166  1.00 16.54  ? 57  THR D C   1 
ATOM   5534  O O   . THR D  1 65  ? 3.054   44.872  48.124  1.00 19.67  ? 57  THR D O   1 
ATOM   5535  C CB  . THR D  1 65  ? 0.040   45.392  47.036  1.00 16.23  ? 57  THR D CB  1 
ATOM   5536  O OG1 . THR D  1 65  ? 0.411   46.448  47.929  1.00 22.91  ? 57  THR D OG1 1 
ATOM   5537  C CG2 . THR D  1 65  ? -1.436  45.091  47.205  1.00 15.63  ? 57  THR D CG2 1 
ATOM   5538  N N   . TRP D  1 66  ? 2.894   44.380  45.950  1.00 17.01  ? 58  TRP D N   1 
ATOM   5539  C CA  . TRP D  1 66  ? 4.248   44.820  45.651  1.00 16.36  ? 58  TRP D CA  1 
ATOM   5540  C C   . TRP D  1 66  ? 4.298   45.157  44.177  1.00 14.09  ? 58  TRP D C   1 
ATOM   5541  O O   . TRP D  1 66  ? 3.309   45.006  43.464  1.00 15.26  ? 58  TRP D O   1 
ATOM   5542  C CB  . TRP D  1 66  ? 5.285   43.750  46.017  1.00 14.25  ? 58  TRP D CB  1 
ATOM   5543  C CG  . TRP D  1 66  ? 5.096   42.438  45.320  1.00 16.33  ? 58  TRP D CG  1 
ATOM   5544  C CD1 . TRP D  1 66  ? 5.791   41.977  44.229  1.00 12.87  ? 58  TRP D CD1 1 
ATOM   5545  C CD2 . TRP D  1 66  ? 4.149   41.411  45.654  1.00 15.39  ? 58  TRP D CD2 1 
ATOM   5546  N NE1 . TRP D  1 66  ? 5.335   40.733  43.873  1.00 12.74  ? 58  TRP D NE1 1 
ATOM   5547  C CE2 . TRP D  1 66  ? 4.333   40.357  44.729  1.00 15.46  ? 58  TRP D CE2 1 
ATOM   5548  C CE3 . TRP D  1 66  ? 3.176   41.272  46.653  1.00 10.70  ? 58  TRP D CE3 1 
ATOM   5549  C CZ2 . TRP D  1 66  ? 3.573   39.183  44.772  1.00 13.30  ? 58  TRP D CZ2 1 
ATOM   5550  C CZ3 . TRP D  1 66  ? 2.424   40.116  46.691  1.00 10.65  ? 58  TRP D CZ3 1 
ATOM   5551  C CH2 . TRP D  1 66  ? 2.620   39.086  45.755  1.00 12.79  ? 58  TRP D CH2 1 
ATOM   5552  N N   . SER D  1 67  ? 5.444   45.620  43.719  1.00 16.66  ? 59  SER D N   1 
ATOM   5553  C CA  . SER D  1 67  ? 5.574   45.992  42.324  1.00 16.95  ? 59  SER D CA  1 
ATOM   5554  C C   . SER D  1 67  ? 6.663   45.156  41.693  1.00 17.75  ? 59  SER D C   1 
ATOM   5555  O O   . SER D  1 67  ? 7.701   44.931  42.309  1.00 22.02  ? 59  SER D O   1 
ATOM   5556  C CB  . SER D  1 67  ? 5.934   47.469  42.218  1.00 13.57  ? 59  SER D CB  1 
ATOM   5557  O OG  . SER D  1 67  ? 5.136   48.087  41.235  1.00 28.12  ? 59  SER D OG  1 
ATOM   5558  N N   . ASP D  1 68  ? 6.422   44.673  40.479  1.00 19.27  ? 60  ASP D N   1 
ATOM   5559  C CA  . ASP D  1 68  ? 7.485   44.092  39.661  1.00 18.37  ? 60  ASP D CA  1 
ATOM   5560  C C   . ASP D  1 68  ? 7.254   44.550  38.238  1.00 22.36  ? 60  ASP D C   1 
ATOM   5561  O O   . ASP D  1 68  ? 6.398   44.013  37.525  1.00 20.83  ? 60  ASP D O   1 
ATOM   5562  C CB  . ASP D  1 68  ? 7.501   42.565  39.745  1.00 17.61  ? 60  ASP D CB  1 
ATOM   5563  C CG  . ASP D  1 68  ? 8.538   41.937  38.819  1.00 21.97  ? 60  ASP D CG  1 
ATOM   5564  O OD1 . ASP D  1 68  ? 9.392   42.674  38.284  1.00 23.87  ? 60  ASP D OD1 1 
ATOM   5565  O OD2 . ASP D  1 68  ? 8.511   40.698  38.632  1.00 22.60  ? 60  ASP D OD2 1 
ATOM   5566  N N   . ARG D  1 69  ? 8.032   45.541  37.821  1.00 24.21  ? 61  ARG D N   1 
ATOM   5567  C CA  . ARG D  1 69  ? 7.794   46.197  36.543  1.00 21.74  ? 61  ARG D CA  1 
ATOM   5568  C C   . ARG D  1 69  ? 8.166   45.403  35.284  1.00 21.80  ? 61  ARG D C   1 
ATOM   5569  O O   . ARG D  1 69  ? 7.665   45.708  34.199  1.00 22.77  ? 61  ARG D O   1 
ATOM   5570  C CB  . ARG D  1 69  ? 8.399   47.598  36.542  1.00 21.16  ? 61  ARG D CB  1 
ATOM   5571  C CG  . ARG D  1 69  ? 7.443   48.610  37.129  1.00 35.83  ? 61  ARG D CG  1 
ATOM   5572  C CD  . ARG D  1 69  ? 8.104   49.913  37.480  1.00 42.48  ? 61  ARG D CD  1 
ATOM   5573  N NE  . ARG D  1 69  ? 7.290   50.643  38.448  1.00 55.72  ? 61  ARG D NE  1 
ATOM   5574  C CZ  . ARG D  1 69  ? 7.427   51.938  38.719  1.00 63.40  ? 61  ARG D CZ  1 
ATOM   5575  N NH1 . ARG D  1 69  ? 8.351   52.658  38.094  1.00 61.48  ? 61  ARG D NH1 1 
ATOM   5576  N NH2 . ARG D  1 69  ? 6.635   52.516  39.612  1.00 59.73  ? 61  ARG D NH2 1 
ATOM   5577  N N   . THR D  1 70  ? 9.009   44.383  35.412  1.00 18.16  ? 62  THR D N   1 
ATOM   5578  C CA  . THR D  1 70  ? 9.311   43.544  34.250  1.00 21.05  ? 62  THR D CA  1 
ATOM   5579  C C   . THR D  1 70  ? 8.041   42.886  33.670  1.00 24.02  ? 62  THR D C   1 
ATOM   5580  O O   . THR D  1 70  ? 7.982   42.564  32.470  1.00 29.00  ? 62  THR D O   1 
ATOM   5581  C CB  . THR D  1 70  ? 10.325  42.442  34.580  1.00 17.49  ? 62  THR D CB  1 
ATOM   5582  O OG1 . THR D  1 70  ? 9.798   41.624  35.630  1.00 22.06  ? 62  THR D OG1 1 
ATOM   5583  C CG2 . THR D  1 70  ? 11.654  43.033  35.014  1.00 13.08  ? 62  THR D CG2 1 
ATOM   5584  N N   . LEU D  1 71  ? 7.029   42.697  34.515  1.00 17.80  ? 63  LEU D N   1 
ATOM   5585  C CA  . LEU D  1 71  ? 5.799   42.032  34.102  1.00 15.07  ? 63  LEU D CA  1 
ATOM   5586  C C   . LEU D  1 71  ? 4.819   43.019  33.484  1.00 13.62  ? 63  LEU D C   1 
ATOM   5587  O O   . LEU D  1 71  ? 3.762   42.630  33.005  1.00 13.20  ? 63  LEU D O   1 
ATOM   5588  C CB  . LEU D  1 71  ? 5.127   41.359  35.298  1.00 18.43  ? 63  LEU D CB  1 
ATOM   5589  C CG  . LEU D  1 71  ? 5.954   40.465  36.216  1.00 16.12  ? 63  LEU D CG  1 
ATOM   5590  C CD1 . LEU D  1 71  ? 5.172   40.139  37.484  1.00 8.52   ? 63  LEU D CD1 1 
ATOM   5591  C CD2 . LEU D  1 71  ? 6.337   39.204  35.470  1.00 14.21  ? 63  LEU D CD2 1 
ATOM   5592  N N   . ALA D  1 72  ? 5.164   44.298  33.497  1.00 14.28  ? 64  ALA D N   1 
ATOM   5593  C CA  . ALA D  1 72  ? 4.255   45.311  32.991  1.00 12.99  ? 64  ALA D CA  1 
ATOM   5594  C C   . ALA D  1 72  ? 4.052   45.187  31.473  1.00 16.86  ? 64  ALA D C   1 
ATOM   5595  O O   . ALA D  1 72  ? 4.977   44.856  30.733  1.00 14.48  ? 64  ALA D O   1 
ATOM   5596  C CB  . ALA D  1 72  ? 4.757   46.694  33.355  1.00 10.83  ? 64  ALA D CB  1 
ATOM   5597  N N   . TRP D  1 73  ? 2.829   45.433  31.023  1.00 13.08  ? 65  TRP D N   1 
ATOM   5598  C CA  . TRP D  1 73  ? 2.565   45.538  29.606  1.00 13.22  ? 65  TRP D CA  1 
ATOM   5599  C C   . TRP D  1 73  ? 1.700   46.754  29.297  1.00 18.71  ? 65  TRP D C   1 
ATOM   5600  O O   . TRP D  1 73  ? 1.260   47.452  30.197  1.00 24.79  ? 65  TRP D O   1 
ATOM   5601  C CB  . TRP D  1 73  ? 1.913   44.275  29.074  1.00 13.74  ? 65  TRP D CB  1 
ATOM   5602  C CG  . TRP D  1 73  ? 0.538   44.094  29.534  1.00 15.55  ? 65  TRP D CG  1 
ATOM   5603  C CD1 . TRP D  1 73  ? -0.594  44.401  28.852  1.00 14.27  ? 65  TRP D CD1 1 
ATOM   5604  C CD2 . TRP D  1 73  ? 0.120   43.548  30.797  1.00 16.56  ? 65  TRP D CD2 1 
ATOM   5605  N NE1 . TRP D  1 73  ? -1.698  44.091  29.612  1.00 20.84  ? 65  TRP D NE1 1 
ATOM   5606  C CE2 . TRP D  1 73  ? -1.286  43.561  30.808  1.00 18.52  ? 65  TRP D CE2 1 
ATOM   5607  C CE3 . TRP D  1 73  ? 0.799   43.061  31.915  1.00 11.09  ? 65  TRP D CE3 1 
ATOM   5608  C CZ2 . TRP D  1 73  ? -2.028  43.095  31.892  1.00 16.22  ? 65  TRP D CZ2 1 
ATOM   5609  C CZ3 . TRP D  1 73  ? 0.069   42.602  32.979  1.00 13.29  ? 65  TRP D CZ3 1 
ATOM   5610  C CH2 . TRP D  1 73  ? -1.334  42.624  32.966  1.00 15.89  ? 65  TRP D CH2 1 
ATOM   5611  N N   . ASN D  1 74  ? 1.472   46.997  28.008  1.00 25.94  ? 66  ASN D N   1 
ATOM   5612  C CA  . ASN D  1 74  ? 0.616   48.093  27.554  1.00 30.30  ? 66  ASN D CA  1 
ATOM   5613  C C   . ASN D  1 74  ? -0.871  47.876  27.846  1.00 28.97  ? 66  ASN D C   1 
ATOM   5614  O O   . ASN D  1 74  ? -1.377  46.759  27.742  1.00 25.47  ? 66  ASN D O   1 
ATOM   5615  C CB  . ASN D  1 74  ? 0.823   48.348  26.059  1.00 41.61  ? 66  ASN D CB  1 
ATOM   5616  C CG  . ASN D  1 74  ? 0.543   49.785  25.669  1.00 46.27  ? 66  ASN D CG  1 
ATOM   5617  O OD1 . ASN D  1 74  ? -0.415  50.395  26.145  1.00 49.90  ? 66  ASN D OD1 1 
ATOM   5618  N ND2 . ASN D  1 74  ? 1.380   50.336  24.796  1.00 57.37  ? 66  ASN D ND2 1 
ATOM   5619  N N   . SER D  1 75  ? -1.560  48.953  28.210  1.00 27.29  ? 67  SER D N   1 
ATOM   5620  C CA  . SER D  1 75  ? -2.992  48.907  28.505  1.00 26.09  ? 67  SER D CA  1 
ATOM   5621  C C   . SER D  1 75  ? -3.869  49.479  27.387  1.00 32.68  ? 67  SER D C   1 
ATOM   5622  O O   . SER D  1 75  ? -5.072  49.667  27.573  1.00 37.44  ? 67  SER D O   1 
ATOM   5623  C CB  . SER D  1 75  ? -3.288  49.630  29.822  1.00 31.03  ? 67  SER D CB  1 
ATOM   5624  O OG  . SER D  1 75  ? -4.001  48.792  30.715  1.00 37.74  ? 67  SER D OG  1 
ATOM   5625  N N   . SER D  1 76  ? -3.195  49.697  26.257  1.00 41.74  ? 68  SER D N   1 
ATOM   5626  C CA  . SER D  1 76  ? -3.733  50.322  25.065  1.00 41.15  ? 68  SER D CA  1 
ATOM   5627  C C   . SER D  1 76  ? -4.869  49.526  24.461  1.00 41.44  ? 68  SER D C   1 
ATOM   5628  O O   . SER D  1 76  ? -5.872  50.117  24.062  1.00 46.13  ? 68  SER D O   1 
ATOM   5629  C CB  . SER D  1 76  ? -2.628  50.527  24.025  1.00 48.23  ? 68  SER D CB  1 
ATOM   5630  O OG  . SER D  1 76  ? -2.505  51.894  23.674  1.00 53.59  ? 68  SER D OG  1 
ATOM   5631  N N   . HIS D  1 77  ? -4.766  48.199  24.395  1.00 35.27  ? 69  HIS D N   1 
ATOM   5632  C CA  . HIS D  1 77  ? -5.956  47.546  23.995  1.00 35.76  ? 69  HIS D CA  1 
ATOM   5633  C C   . HIS D  1 77  ? -5.904  46.143  24.389  1.00 34.79  ? 69  HIS D C   1 
ATOM   5634  O O   . HIS D  1 77  ? -6.454  45.332  23.735  1.00 36.43  ? 69  HIS D O   1 
ATOM   5635  C CB  . HIS D  1 77  ? -6.209  47.721  22.499  1.00 45.49  ? 69  HIS D CB  1 
ATOM   5636  C CG  . HIS D  1 77  ? -6.362  49.143  22.060  1.00 49.13  ? 69  HIS D CG  1 
ATOM   5637  N ND1 . HIS D  1 77  ? -5.296  49.965  21.817  1.00 47.55  ? 69  HIS D ND1 1 
ATOM   5638  C CD2 . HIS D  1 77  ? -7.454  49.881  21.798  1.00 44.41  ? 69  HIS D CD2 1 
ATOM   5639  C CE1 . HIS D  1 77  ? -5.714  51.163  21.487  1.00 47.93  ? 69  HIS D CE1 1 
ATOM   5640  N NE2 . HIS D  1 77  ? -7.021  51.137  21.460  1.00 43.37  ? 69  HIS D NE2 1 
ATOM   5641  N N   . SER D  1 78  ? -5.205  45.866  25.479  1.00 35.63  ? 70  SER D N   1 
ATOM   5642  C CA  . SER D  1 78  ? -5.317  44.623  26.257  1.00 32.01  ? 70  SER D CA  1 
ATOM   5643  C C   . SER D  1 78  ? -5.804  44.828  27.700  1.00 27.72  ? 70  SER D C   1 
ATOM   5644  O O   . SER D  1 78  ? -5.702  45.928  28.244  1.00 31.06  ? 70  SER D O   1 
ATOM   5645  C CB  . SER D  1 78  ? -3.982  43.874  26.259  1.00 27.81  ? 70  SER D CB  1 
ATOM   5646  O OG  . SER D  1 78  ? -2.974  44.631  26.906  1.00 30.33  ? 70  SER D OG  1 
ATOM   5647  N N   . PRO D  1 79  ? -6.342  43.768  28.308  1.00 24.95  ? 71  PRO D N   1 
ATOM   5648  C CA  . PRO D  1 79  ? -6.979  43.870  29.627  1.00 20.78  ? 71  PRO D CA  1 
ATOM   5649  C C   . PRO D  1 79  ? -6.031  44.473  30.661  1.00 22.50  ? 71  PRO D C   1 
ATOM   5650  O O   . PRO D  1 79  ? -4.840  44.161  30.660  1.00 26.39  ? 71  PRO D O   1 
ATOM   5651  C CB  . PRO D  1 79  ? -7.284  42.413  29.977  1.00 21.44  ? 71  PRO D CB  1 
ATOM   5652  C CG  . PRO D  1 79  ? -7.443  41.740  28.656  1.00 24.23  ? 71  PRO D CG  1 
ATOM   5653  C CD  . PRO D  1 79  ? -6.473  42.419  27.731  1.00 22.63  ? 71  PRO D CD  1 
ATOM   5654  N N   . ASP D  1 80  ? -6.560  45.335  31.526  1.00 24.63  ? 72  ASP D N   1 
ATOM   5655  C CA  . ASP D  1 80  ? -5.728  46.082  32.485  1.00 23.90  ? 72  ASP D CA  1 
ATOM   5656  C C   . ASP D  1 80  ? -5.042  45.148  33.462  1.00 25.91  ? 72  ASP D C   1 
ATOM   5657  O O   . ASP D  1 80  ? -3.914  45.403  33.903  1.00 23.33  ? 72  ASP D O   1 
ATOM   5658  C CB  . ASP D  1 80  ? -6.566  47.042  33.322  1.00 23.63  ? 72  ASP D CB  1 
ATOM   5659  C CG  . ASP D  1 80  ? -7.470  47.901  32.492  1.00 40.09  ? 72  ASP D CG  1 
ATOM   5660  O OD1 . ASP D  1 80  ? -8.664  48.007  32.849  1.00 50.36  ? 72  ASP D OD1 1 
ATOM   5661  O OD2 . ASP D  1 80  ? -6.989  48.479  31.494  1.00 46.67  ? 72  ASP D OD2 1 
ATOM   5662  N N   . GLN D  1 81  ? -5.760  44.087  33.830  1.00 26.82  ? 73  GLN D N   1 
ATOM   5663  C CA  . GLN D  1 81  ? -5.244  43.075  34.734  1.00 18.63  ? 73  GLN D CA  1 
ATOM   5664  C C   . GLN D  1 81  ? -5.838  41.690  34.531  1.00 18.95  ? 73  GLN D C   1 
ATOM   5665  O O   . GLN D  1 81  ? -6.910  41.541  33.932  1.00 20.42  ? 73  GLN D O   1 
ATOM   5666  C CB  . GLN D  1 81  ? -5.434  43.513  36.169  1.00 19.06  ? 73  GLN D CB  1 
ATOM   5667  C CG  . GLN D  1 81  ? -6.726  44.218  36.467  1.00 23.00  ? 73  GLN D CG  1 
ATOM   5668  C CD  . GLN D  1 81  ? -6.832  44.495  37.949  1.00 24.62  ? 73  GLN D CD  1 
ATOM   5669  O OE1 . GLN D  1 81  ? -6.613  43.602  38.767  1.00 27.01  ? 73  GLN D OE1 1 
ATOM   5670  N NE2 . GLN D  1 81  ? -7.125  45.736  38.307  1.00 26.02  ? 73  GLN D NE2 1 
ATOM   5671  N N   . VAL D  1 82  ? -5.124  40.682  35.037  1.00 16.88  ? 74  VAL D N   1 
ATOM   5672  C CA  . VAL D  1 82  ? -5.542  39.284  34.946  1.00 13.85  ? 74  VAL D CA  1 
ATOM   5673  C C   . VAL D  1 82  ? -5.183  38.535  36.215  1.00 11.47  ? 74  VAL D C   1 
ATOM   5674  O O   . VAL D  1 82  ? -4.324  38.971  36.981  1.00 10.87  ? 74  VAL D O   1 
ATOM   5675  C CB  . VAL D  1 82  ? -4.831  38.537  33.779  1.00 15.16  ? 74  VAL D CB  1 
ATOM   5676  C CG1 . VAL D  1 82  ? -5.300  39.046  32.429  1.00 17.21  ? 74  VAL D CG1 1 
ATOM   5677  C CG2 . VAL D  1 82  ? -3.328  38.651  33.909  1.00 10.12  ? 74  VAL D CG2 1 
ATOM   5678  N N   . SER D  1 83  ? -5.808  37.377  36.406  1.00 11.95  ? 75  SER D N   1 
ATOM   5679  C CA  . SER D  1 83  ? -5.504  36.523  37.553  1.00 12.52  ? 75  SER D CA  1 
ATOM   5680  C C   . SER D  1 83  ? -4.451  35.493  37.181  1.00 9.86   ? 75  SER D C   1 
ATOM   5681  O O   . SER D  1 83  ? -4.455  34.987  36.058  1.00 10.18  ? 75  SER D O   1 
ATOM   5682  C CB  . SER D  1 83  ? -6.759  35.815  38.071  1.00 12.10  ? 75  SER D CB  1 
ATOM   5683  O OG  . SER D  1 83  ? -7.728  36.738  38.544  1.00 14.25  ? 75  SER D OG  1 
ATOM   5684  N N   . VAL D  1 84  ? -3.568  35.183  38.135  1.00 7.14   ? 76  VAL D N   1 
ATOM   5685  C CA  . VAL D  1 84  ? -2.447  34.267  37.937  1.00 9.51   ? 76  VAL D CA  1 
ATOM   5686  C C   . VAL D  1 84  ? -2.261  33.328  39.139  1.00 8.93   ? 76  VAL D C   1 
ATOM   5687  O O   . VAL D  1 84  ? -2.248  33.776  40.281  1.00 8.93   ? 76  VAL D O   1 
ATOM   5688  C CB  . VAL D  1 84  ? -1.109  35.061  37.741  1.00 11.07  ? 76  VAL D CB  1 
ATOM   5689  C CG1 . VAL D  1 84  ? 0.002   34.145  37.286  1.00 6.37   ? 76  VAL D CG1 1 
ATOM   5690  C CG2 . VAL D  1 84  ? -1.287  36.217  36.763  1.00 8.81   ? 76  VAL D CG2 1 
ATOM   5691  N N   . PRO D  1 85  ? -2.102  32.018  38.887  1.00 11.27  ? 77  PRO D N   1 
ATOM   5692  C CA  . PRO D  1 85  ? -1.780  31.095  39.982  1.00 6.78   ? 77  PRO D CA  1 
ATOM   5693  C C   . PRO D  1 85  ? -0.483  31.523  40.665  1.00 10.75  ? 77  PRO D C   1 
ATOM   5694  O O   . PRO D  1 85  ? 0.487   31.808  39.974  1.00 10.53  ? 77  PRO D O   1 
ATOM   5695  C CB  . PRO D  1 85  ? -1.569  29.764  39.263  1.00 5.31   ? 77  PRO D CB  1 
ATOM   5696  C CG  . PRO D  1 85  ? -2.348  29.895  37.992  1.00 7.53   ? 77  PRO D CG  1 
ATOM   5697  C CD  . PRO D  1 85  ? -2.200  31.326  37.587  1.00 9.65   ? 77  PRO D CD  1 
ATOM   5698  N N   . ILE D  1 86  ? -0.448  31.570  41.994  1.00 12.66  ? 78  ILE D N   1 
ATOM   5699  C CA  . ILE D  1 86  ? 0.764   32.025  42.662  1.00 9.02   ? 78  ILE D CA  1 
ATOM   5700  C C   . ILE D  1 86  ? 1.988   31.152  42.410  1.00 11.25  ? 78  ILE D C   1 
ATOM   5701  O O   . ILE D  1 86  ? 3.111   31.591  42.637  1.00 18.47  ? 78  ILE D O   1 
ATOM   5702  C CB  . ILE D  1 86  ? 0.568   32.247  44.173  1.00 12.86  ? 78  ILE D CB  1 
ATOM   5703  C CG1 . ILE D  1 86  ? -0.215  31.092  44.791  1.00 14.09  ? 78  ILE D CG1 1 
ATOM   5704  C CG2 . ILE D  1 86  ? -0.139  33.567  44.423  1.00 9.05   ? 78  ILE D CG2 1 
ATOM   5705  C CD1 . ILE D  1 86  ? -0.074  31.012  46.282  1.00 9.63   ? 78  ILE D CD1 1 
ATOM   5706  N N   . SER D  1 87  ? 1.812   29.934  41.916  1.00 10.10  ? 79  SER D N   1 
ATOM   5707  C CA  . SER D  1 87  ? 2.991   29.148  41.569  1.00 9.26   ? 79  SER D CA  1 
ATOM   5708  C C   . SER D  1 87  ? 3.774   29.761  40.385  1.00 12.24  ? 79  SER D C   1 
ATOM   5709  O O   . SER D  1 87  ? 4.966   29.493  40.209  1.00 13.93  ? 79  SER D O   1 
ATOM   5710  C CB  . SER D  1 87  ? 2.634   27.683  41.318  1.00 9.72   ? 79  SER D CB  1 
ATOM   5711  O OG  . SER D  1 87  ? 1.788   27.539  40.193  1.00 16.06  ? 79  SER D OG  1 
ATOM   5712  N N   . SER D  1 88  ? 3.118   30.601  39.591  1.00 10.20  ? 80  SER D N   1 
ATOM   5713  C CA  . SER D  1 88  ? 3.785   31.256  38.466  1.00 9.30   ? 80  SER D CA  1 
ATOM   5714  C C   . SER D  1 88  ? 4.529   32.541  38.849  1.00 15.83  ? 80  SER D C   1 
ATOM   5715  O O   . SER D  1 88  ? 5.307   33.077  38.048  1.00 11.41  ? 80  SER D O   1 
ATOM   5716  C CB  . SER D  1 88  ? 2.778   31.588  37.372  1.00 7.97   ? 80  SER D CB  1 
ATOM   5717  O OG  . SER D  1 88  ? 2.383   30.423  36.683  1.00 13.25  ? 80  SER D OG  1 
ATOM   5718  N N   . LEU D  1 89  ? 4.288   33.052  40.057  1.00 11.88  ? 81  LEU D N   1 
ATOM   5719  C CA  . LEU D  1 89  ? 4.886   34.322  40.439  1.00 10.61  ? 81  LEU D CA  1 
ATOM   5720  C C   . LEU D  1 89  ? 5.834   34.143  41.597  1.00 12.66  ? 81  LEU D C   1 
ATOM   5721  O O   . LEU D  1 89  ? 5.803   33.127  42.290  1.00 16.76  ? 81  LEU D O   1 
ATOM   5722  C CB  . LEU D  1 89  ? 3.814   35.339  40.835  1.00 10.18  ? 81  LEU D CB  1 
ATOM   5723  C CG  . LEU D  1 89  ? 2.703   35.664  39.842  1.00 11.16  ? 81  LEU D CG  1 
ATOM   5724  C CD1 . LEU D  1 89  ? 1.604   36.429  40.545  1.00 12.77  ? 81  LEU D CD1 1 
ATOM   5725  C CD2 . LEU D  1 89  ? 3.229   36.462  38.669  1.00 13.16  ? 81  LEU D CD2 1 
ATOM   5726  N N   . TRP D  1 90  ? 6.688   35.134  41.796  1.00 10.93  ? 82  TRP D N   1 
ATOM   5727  C CA  . TRP D  1 90  ? 7.367   35.279  43.061  1.00 12.09  ? 82  TRP D CA  1 
ATOM   5728  C C   . TRP D  1 90  ? 6.354   35.843  44.045  1.00 12.28  ? 82  TRP D C   1 
ATOM   5729  O O   . TRP D  1 90  ? 5.625   36.775  43.713  1.00 11.60  ? 82  TRP D O   1 
ATOM   5730  C CB  . TRP D  1 90  ? 8.542   36.235  42.929  1.00 7.35   ? 82  TRP D CB  1 
ATOM   5731  C CG  . TRP D  1 90  ? 9.230   36.569  44.224  1.00 9.67   ? 82  TRP D CG  1 
ATOM   5732  C CD1 . TRP D  1 90  ? 10.254  35.882  44.810  1.00 11.37  ? 82  TRP D CD1 1 
ATOM   5733  C CD2 . TRP D  1 90  ? 8.956   37.685  45.086  1.00 11.81  ? 82  TRP D CD2 1 
ATOM   5734  N NE1 . TRP D  1 90  ? 10.647  36.507  45.974  1.00 9.75   ? 82  TRP D NE1 1 
ATOM   5735  C CE2 . TRP D  1 90  ? 9.858   37.609  46.171  1.00 10.94  ? 82  TRP D CE2 1 
ATOM   5736  C CE3 . TRP D  1 90  ? 8.037   38.748  45.046  1.00 10.89  ? 82  TRP D CE3 1 
ATOM   5737  C CZ2 . TRP D  1 90  ? 9.865   38.550  47.200  1.00 8.62   ? 82  TRP D CZ2 1 
ATOM   5738  C CZ3 . TRP D  1 90  ? 8.055   39.682  46.063  1.00 6.02   ? 82  TRP D CZ3 1 
ATOM   5739  C CH2 . TRP D  1 90  ? 8.962   39.579  47.122  1.00 5.81   ? 82  TRP D CH2 1 
ATOM   5740  N N   . VAL D  1 91  ? 6.325   35.266  45.247  1.00 12.40  ? 83  VAL D N   1 
ATOM   5741  C CA  . VAL D  1 91  ? 5.513   35.749  46.370  1.00 12.10  ? 83  VAL D CA  1 
ATOM   5742  C C   . VAL D  1 91  ? 6.434   35.936  47.588  1.00 12.33  ? 83  VAL D C   1 
ATOM   5743  O O   . VAL D  1 91  ? 7.294   35.087  47.852  1.00 15.51  ? 83  VAL D O   1 
ATOM   5744  C CB  . VAL D  1 91  ? 4.369   34.758  46.713  1.00 8.83   ? 83  VAL D CB  1 
ATOM   5745  C CG1 . VAL D  1 91  ? 3.947   34.924  48.126  1.00 12.60  ? 83  VAL D CG1 1 
ATOM   5746  C CG2 . VAL D  1 91  ? 3.176   34.974  45.789  1.00 8.79   ? 83  VAL D CG2 1 
ATOM   5747  N N   . PRO D  1 92  ? 6.284   37.056  48.317  1.00 8.03   ? 84  PRO D N   1 
ATOM   5748  C CA  . PRO D  1 92  ? 7.217   37.297  49.422  1.00 10.56  ? 84  PRO D CA  1 
ATOM   5749  C C   . PRO D  1 92  ? 7.036   36.282  50.561  1.00 10.90  ? 84  PRO D C   1 
ATOM   5750  O O   . PRO D  1 92  ? 5.932   35.783  50.766  1.00 9.53   ? 84  PRO D O   1 
ATOM   5751  C CB  . PRO D  1 92  ? 6.880   38.724  49.867  1.00 9.49   ? 84  PRO D CB  1 
ATOM   5752  C CG  . PRO D  1 92  ? 5.526   39.004  49.316  1.00 8.09   ? 84  PRO D CG  1 
ATOM   5753  C CD  . PRO D  1 92  ? 5.310   38.150  48.140  1.00 8.46   ? 84  PRO D CD  1 
ATOM   5754  N N   . ASP D  1 93  ? 8.111   35.963  51.271  1.00 9.35   ? 85  ASP D N   1 
ATOM   5755  C CA  . ASP D  1 93  ? 8.055   34.877  52.245  1.00 12.17  ? 85  ASP D CA  1 
ATOM   5756  C C   . ASP D  1 93  ? 7.676   35.377  53.643  1.00 14.67  ? 85  ASP D C   1 
ATOM   5757  O O   . ASP D  1 93  ? 8.453   35.276  54.592  1.00 13.78  ? 85  ASP D O   1 
ATOM   5758  C CB  . ASP D  1 93  ? 9.377   34.102  52.276  1.00 11.61  ? 85  ASP D CB  1 
ATOM   5759  C CG  . ASP D  1 93  ? 10.578  35.015  52.410  1.00 17.63  ? 85  ASP D CG  1 
ATOM   5760  O OD1 . ASP D  1 93  ? 10.503  36.146  51.874  1.00 18.64  ? 85  ASP D OD1 1 
ATOM   5761  O OD2 . ASP D  1 93  ? 11.582  34.612  53.052  1.00 16.21  ? 85  ASP D OD2 1 
ATOM   5762  N N   . LEU D  1 94  ? 6.466   35.913  53.754  1.00 14.55  ? 86  LEU D N   1 
ATOM   5763  C CA  . LEU D  1 94  ? 5.973   36.438  55.011  1.00 13.13  ? 86  LEU D CA  1 
ATOM   5764  C C   . LEU D  1 94  ? 5.731   35.311  56.019  1.00 16.78  ? 86  LEU D C   1 
ATOM   5765  O O   . LEU D  1 94  ? 5.343   34.187  55.665  1.00 15.55  ? 86  LEU D O   1 
ATOM   5766  C CB  . LEU D  1 94  ? 4.704   37.265  54.779  1.00 11.73  ? 86  LEU D CB  1 
ATOM   5767  C CG  . LEU D  1 94  ? 4.917   38.389  53.763  1.00 11.87  ? 86  LEU D CG  1 
ATOM   5768  C CD1 . LEU D  1 94  ? 3.652   39.198  53.530  1.00 13.32  ? 86  LEU D CD1 1 
ATOM   5769  C CD2 . LEU D  1 94  ? 6.035   39.287  54.222  1.00 9.93   ? 86  LEU D CD2 1 
ATOM   5770  N N   . ALA D  1 95  ? 5.995   35.619  57.280  1.00 18.25  ? 87  ALA D N   1 
ATOM   5771  C CA  . ALA D  1 95  ? 5.689   34.719  58.377  1.00 19.74  ? 87  ALA D CA  1 
ATOM   5772  C C   . ALA D  1 95  ? 5.245   35.583  59.545  1.00 17.24  ? 87  ALA D C   1 
ATOM   5773  O O   . ALA D  1 95  ? 5.644   36.742  59.654  1.00 16.91  ? 87  ALA D O   1 
ATOM   5774  C CB  . ALA D  1 95  ? 6.925   33.874  58.751  1.00 13.61  ? 87  ALA D CB  1 
ATOM   5775  N N   . ALA D  1 96  ? 4.408   35.022  60.407  1.00 23.11  ? 88  ALA D N   1 
ATOM   5776  C CA  . ALA D  1 96  ? 4.014   35.685  61.647  1.00 16.28  ? 88  ALA D CA  1 
ATOM   5777  C C   . ALA D  1 96  ? 4.853   35.113  62.779  1.00 20.36  ? 88  ALA D C   1 
ATOM   5778  O O   . ALA D  1 96  ? 4.837   33.905  63.009  1.00 27.10  ? 88  ALA D O   1 
ATOM   5779  C CB  . ALA D  1 96  ? 2.550   35.454  61.905  1.00 15.97  ? 88  ALA D CB  1 
ATOM   5780  N N   . TYR D  1 97  ? 5.585   35.964  63.491  1.00 20.42  ? 89  TYR D N   1 
ATOM   5781  C CA  . TYR D  1 97  ? 6.575   35.479  64.460  1.00 19.46  ? 89  TYR D CA  1 
ATOM   5782  C C   . TYR D  1 97  ? 5.951   34.728  65.636  1.00 23.68  ? 89  TYR D C   1 
ATOM   5783  O O   . TYR D  1 97  ? 6.600   33.883  66.262  1.00 23.30  ? 89  TYR D O   1 
ATOM   5784  C CB  . TYR D  1 97  ? 7.451   36.626  64.971  1.00 21.03  ? 89  TYR D CB  1 
ATOM   5785  C CG  . TYR D  1 97  ? 8.173   37.395  63.879  1.00 29.22  ? 89  TYR D CG  1 
ATOM   5786  C CD1 . TYR D  1 97  ? 8.670   38.668  64.114  1.00 36.21  ? 89  TYR D CD1 1 
ATOM   5787  C CD2 . TYR D  1 97  ? 8.357   36.849  62.612  1.00 32.35  ? 89  TYR D CD2 1 
ATOM   5788  C CE1 . TYR D  1 97  ? 9.338   39.378  63.123  1.00 34.50  ? 89  TYR D CE1 1 
ATOM   5789  C CE2 . TYR D  1 97  ? 9.013   37.556  61.612  1.00 38.19  ? 89  TYR D CE2 1 
ATOM   5790  C CZ  . TYR D  1 97  ? 9.508   38.821  61.881  1.00 37.17  ? 89  TYR D CZ  1 
ATOM   5791  O OH  . TYR D  1 97  ? 10.166  39.531  60.898  1.00 44.13  ? 89  TYR D OH  1 
ATOM   5792  N N   . ASN D  1 98  ? 4.691   35.041  65.928  1.00 20.72  ? 90  ASN D N   1 
ATOM   5793  C CA  . ASN D  1 98  ? 3.994   34.434  67.046  1.00 19.48  ? 90  ASN D CA  1 
ATOM   5794  C C   . ASN D  1 98  ? 2.895   33.483  66.570  1.00 22.88  ? 90  ASN D C   1 
ATOM   5795  O O   . ASN D  1 98  ? 1.938   33.179  67.305  1.00 21.64  ? 90  ASN D O   1 
ATOM   5796  C CB  . ASN D  1 98  ? 3.445   35.510  67.995  1.00 19.12  ? 90  ASN D CB  1 
ATOM   5797  C CG  . ASN D  1 98  ? 2.654   36.584  67.272  1.00 22.67  ? 90  ASN D CG  1 
ATOM   5798  O OD1 . ASN D  1 98  ? 3.118   37.161  66.283  1.00 26.44  ? 90  ASN D OD1 1 
ATOM   5799  N ND2 . ASN D  1 98  ? 1.448   36.847  67.750  1.00 14.50  ? 90  ASN D ND2 1 
ATOM   5800  N N   . ALA D  1 99  ? 3.038   33.011  65.336  1.00 19.01  ? 91  ALA D N   1 
ATOM   5801  C CA  . ALA D  1 99  ? 2.123   32.012  64.807  1.00 17.43  ? 91  ALA D CA  1 
ATOM   5802  C C   . ALA D  1 99  ? 2.371   30.686  65.516  1.00 19.37  ? 91  ALA D C   1 
ATOM   5803  O O   . ALA D  1 99  ? 3.520   30.279  65.685  1.00 19.59  ? 91  ALA D O   1 
ATOM   5804  C CB  . ALA D  1 99  ? 2.315   31.858  63.308  1.00 14.71  ? 91  ALA D CB  1 
ATOM   5805  N N   . ILE D  1 100 ? 1.310   30.014  65.949  1.00 16.19  ? 92  ILE D N   1 
ATOM   5806  C CA  . ILE D  1 100 ? 1.495   28.697  66.545  1.00 17.72  ? 92  ILE D CA  1 
ATOM   5807  C C   . ILE D  1 100 ? 0.865   27.563  65.743  1.00 16.04  ? 92  ILE D C   1 
ATOM   5808  O O   . ILE D  1 100 ? 1.050   26.399  66.066  1.00 16.95  ? 92  ILE D O   1 
ATOM   5809  C CB  . ILE D  1 100 ? 1.045   28.642  68.016  1.00 16.73  ? 92  ILE D CB  1 
ATOM   5810  C CG1 . ILE D  1 100 ? -0.466  28.813  68.148  1.00 15.98  ? 92  ILE D CG1 1 
ATOM   5811  C CG2 . ILE D  1 100 ? 1.771   29.694  68.808  1.00 17.02  ? 92  ILE D CG2 1 
ATOM   5812  C CD1 . ILE D  1 100 ? -0.939  28.536  69.544  1.00 18.71  ? 92  ILE D CD1 1 
ATOM   5813  N N   . SER D  1 101 ? 0.122   27.912  64.703  1.00 14.99  ? 93  SER D N   1 
ATOM   5814  C CA  . SER D  1 101 ? -0.355  26.942  63.736  1.00 14.70  ? 93  SER D CA  1 
ATOM   5815  C C   . SER D  1 101 ? 0.162   27.376  62.354  1.00 16.36  ? 93  SER D C   1 
ATOM   5816  O O   . SER D  1 101 ? 0.701   28.481  62.212  1.00 11.78  ? 93  SER D O   1 
ATOM   5817  C CB  . SER D  1 101 ? -1.875  26.921  63.753  1.00 13.81  ? 93  SER D CB  1 
ATOM   5818  O OG  . SER D  1 101 ? -2.383  28.145  63.242  1.00 14.05  ? 93  SER D OG  1 
ATOM   5819  N N   . LYS D  1 102 ? 0.013   26.517  61.345  1.00 19.66  ? 94  LYS D N   1 
ATOM   5820  C CA  . LYS D  1 102 ? 0.339   26.903  59.962  1.00 17.95  ? 94  LYS D CA  1 
ATOM   5821  C C   . LYS D  1 102 ? -0.725  27.853  59.481  1.00 18.05  ? 94  LYS D C   1 
ATOM   5822  O O   . LYS D  1 102 ? -1.856  27.801  59.947  1.00 20.33  ? 94  LYS D O   1 
ATOM   5823  C CB  . LYS D  1 102 ? 0.310   25.705  59.002  1.00 18.75  ? 94  LYS D CB  1 
ATOM   5824  C CG  . LYS D  1 102 ? 1.408   24.682  59.142  1.00 22.22  ? 94  LYS D CG  1 
ATOM   5825  C CD  . LYS D  1 102 ? 1.163   23.551  58.162  1.00 30.63  ? 94  LYS D CD  1 
ATOM   5826  C CE  . LYS D  1 102 ? 2.234   22.473  58.257  1.00 41.51  ? 94  LYS D CE  1 
ATOM   5827  N NZ  . LYS D  1 102 ? 2.147   21.547  57.084  1.00 54.64  ? 94  LYS D NZ  1 
ATOM   5828  N N   . PRO D  1 103 ? -0.388  28.706  58.511  1.00 19.99  ? 95  PRO D N   1 
ATOM   5829  C CA  . PRO D  1 103 ? -1.463  29.479  57.879  1.00 20.28  ? 95  PRO D CA  1 
ATOM   5830  C C   . PRO D  1 103 ? -2.395  28.587  57.057  1.00 18.18  ? 95  PRO D C   1 
ATOM   5831  O O   . PRO D  1 103 ? -1.939  27.915  56.139  1.00 25.23  ? 95  PRO D O   1 
ATOM   5832  C CB  . PRO D  1 103 ? -0.702  30.456  56.976  1.00 14.94  ? 95  PRO D CB  1 
ATOM   5833  C CG  . PRO D  1 103 ? 0.644   29.842  56.807  1.00 14.70  ? 95  PRO D CG  1 
ATOM   5834  C CD  . PRO D  1 103 ? 0.944   29.122  58.055  1.00 13.27  ? 95  PRO D CD  1 
ATOM   5835  N N   . GLU D  1 104 ? -3.677  28.564  57.402  1.00 17.28  ? 96  GLU D N   1 
ATOM   5836  C CA  . GLU D  1 104 ? -4.679  27.866  56.597  1.00 20.38  ? 96  GLU D CA  1 
ATOM   5837  C C   . GLU D  1 104 ? -5.431  28.802  55.635  1.00 17.47  ? 96  GLU D C   1 
ATOM   5838  O O   . GLU D  1 104 ? -6.257  29.618  56.045  1.00 13.74  ? 96  GLU D O   1 
ATOM   5839  C CB  . GLU D  1 104 ? -5.640  27.066  57.486  1.00 24.42  ? 96  GLU D CB  1 
ATOM   5840  C CG  . GLU D  1 104 ? -5.147  25.634  57.747  1.00 41.14  ? 96  GLU D CG  1 
ATOM   5841  C CD  . GLU D  1 104 ? -5.761  24.986  58.987  1.00 67.52  ? 96  GLU D CD  1 
ATOM   5842  O OE1 . GLU D  1 104 ? -6.873  25.392  59.405  1.00 65.46  ? 96  GLU D OE1 1 
ATOM   5843  O OE2 . GLU D  1 104 ? -5.117  24.064  59.546  1.00 78.37  ? 96  GLU D OE2 1 
ATOM   5844  N N   . VAL D  1 105 ? -5.123  28.666  54.348  1.00 15.86  ? 97  VAL D N   1 
ATOM   5845  C CA  . VAL D  1 105 ? -5.634  29.547  53.313  1.00 13.09  ? 97  VAL D CA  1 
ATOM   5846  C C   . VAL D  1 105 ? -7.029  29.106  52.878  1.00 18.19  ? 97  VAL D C   1 
ATOM   5847  O O   . VAL D  1 105 ? -7.209  27.976  52.425  1.00 24.92  ? 97  VAL D O   1 
ATOM   5848  C CB  . VAL D  1 105 ? -4.677  29.525  52.101  1.00 16.92  ? 97  VAL D CB  1 
ATOM   5849  C CG1 . VAL D  1 105 ? -5.235  30.337  50.915  1.00 11.51  ? 97  VAL D CG1 1 
ATOM   5850  C CG2 . VAL D  1 105 ? -3.314  30.022  52.522  1.00 12.10  ? 97  VAL D CG2 1 
ATOM   5851  N N   . LEU D  1 106 ? -8.015  29.993  52.991  1.00 12.59  ? 98  LEU D N   1 
ATOM   5852  C CA  . LEU D  1 106 ? -9.403  29.598  52.768  1.00 13.39  ? 98  LEU D CA  1 
ATOM   5853  C C   . LEU D  1 106 ? -9.900  29.860  51.339  1.00 16.10  ? 98  LEU D C   1 
ATOM   5854  O O   . LEU D  1 106 ? -11.053 29.556  51.008  1.00 11.84  ? 98  LEU D O   1 
ATOM   5855  C CB  . LEU D  1 106 ? -10.326 30.304  53.776  1.00 15.34  ? 98  LEU D CB  1 
ATOM   5856  C CG  . LEU D  1 106 ? -9.973  30.162  55.264  1.00 17.75  ? 98  LEU D CG  1 
ATOM   5857  C CD1 . LEU D  1 106 ? -11.056 30.731  56.184  1.00 10.99  ? 98  LEU D CD1 1 
ATOM   5858  C CD2 . LEU D  1 106 ? -9.664  28.705  55.598  1.00 15.62  ? 98  LEU D CD2 1 
ATOM   5859  N N   . THR D  1 107 ? -9.023  30.416  50.503  1.00 16.30  ? 99  THR D N   1 
ATOM   5860  C CA  . THR D  1 107 ? -9.416  30.990  49.221  1.00 12.89  ? 99  THR D CA  1 
ATOM   5861  C C   . THR D  1 107 ? -8.625  30.391  48.055  1.00 13.05  ? 99  THR D C   1 
ATOM   5862  O O   . THR D  1 107 ? -7.666  29.660  48.281  1.00 11.75  ? 99  THR D O   1 
ATOM   5863  C CB  . THR D  1 107 ? -9.263  32.525  49.255  1.00 12.33  ? 99  THR D CB  1 
ATOM   5864  O OG1 . THR D  1 107 ? -8.119  32.865  50.038  1.00 13.83  ? 99  THR D OG1 1 
ATOM   5865  C CG2 . THR D  1 107 ? -10.493 33.165  49.890  1.00 11.29  ? 99  THR D CG2 1 
ATOM   5866  N N   . PRO D  1 108 ? -9.061  30.654  46.802  1.00 13.72  ? 100 PRO D N   1 
ATOM   5867  C CA  . PRO D  1 108 ? -8.263  30.183  45.670  1.00 9.48   ? 100 PRO D CA  1 
ATOM   5868  C C   . PRO D  1 108 ? -6.930  30.903  45.673  1.00 11.10  ? 100 PRO D C   1 
ATOM   5869  O O   . PRO D  1 108 ? -6.898  32.048  46.102  1.00 12.49  ? 100 PRO D O   1 
ATOM   5870  C CB  . PRO D  1 108 ? -9.096  30.616  44.465  1.00 11.44  ? 100 PRO D CB  1 
ATOM   5871  C CG  . PRO D  1 108 ? -10.485 30.665  44.961  1.00 10.09  ? 100 PRO D CG  1 
ATOM   5872  C CD  . PRO D  1 108 ? -10.362 31.192  46.357  1.00 10.03  ? 100 PRO D CD  1 
ATOM   5873  N N   . GLN D  1 109 ? -5.853  30.255  45.233  1.00 14.03  ? 101 GLN D N   1 
ATOM   5874  C CA  . GLN D  1 109 ? -4.521  30.868  45.310  1.00 11.91  ? 101 GLN D CA  1 
ATOM   5875  C C   . GLN D  1 109 ? -4.161  31.559  44.016  1.00 10.93  ? 101 GLN D C   1 
ATOM   5876  O O   . GLN D  1 109 ? -3.216  31.168  43.336  1.00 15.37  ? 101 GLN D O   1 
ATOM   5877  C CB  . GLN D  1 109 ? -3.447  29.836  45.669  1.00 11.01  ? 101 GLN D CB  1 
ATOM   5878  C CG  . GLN D  1 109 ? -3.893  28.860  46.744  1.00 16.40  ? 101 GLN D CG  1 
ATOM   5879  C CD  . GLN D  1 109 ? -3.067  28.931  48.001  1.00 20.17  ? 101 GLN D CD  1 
ATOM   5880  O OE1 . GLN D  1 109 ? -2.634  30.009  48.421  1.00 19.97  ? 101 GLN D OE1 1 
ATOM   5881  N NE2 . GLN D  1 109 ? -2.835  27.774  48.616  1.00 25.63  ? 101 GLN D NE2 1 
ATOM   5882  N N   . LEU D  1 110 ? -4.920  32.587  43.670  1.00 11.05  ? 102 LEU D N   1 
ATOM   5883  C CA  . LEU D  1 110 ? -4.639  33.363  42.469  1.00 10.92  ? 102 LEU D CA  1 
ATOM   5884  C C   . LEU D  1 110 ? -4.250  34.752  42.932  1.00 10.33  ? 102 LEU D C   1 
ATOM   5885  O O   . LEU D  1 110 ? -4.818  35.255  43.892  1.00 10.91  ? 102 LEU D O   1 
ATOM   5886  C CB  . LEU D  1 110 ? -5.881  33.471  41.581  1.00 10.12  ? 102 LEU D CB  1 
ATOM   5887  C CG  . LEU D  1 110 ? -6.750  32.236  41.373  1.00 8.70   ? 102 LEU D CG  1 
ATOM   5888  C CD1 . LEU D  1 110 ? -7.961  32.579  40.536  1.00 8.51   ? 102 LEU D CD1 1 
ATOM   5889  C CD2 . LEU D  1 110 ? -5.935  31.181  40.709  1.00 10.69  ? 102 LEU D CD2 1 
ATOM   5890  N N   . ALA D  1 111 ? -3.279  35.361  42.265  1.00 8.13   ? 103 ALA D N   1 
ATOM   5891  C CA  . ALA D  1 111 ? -2.933  36.746  42.534  1.00 8.65   ? 103 ALA D CA  1 
ATOM   5892  C C   . ALA D  1 111 ? -3.519  37.576  41.402  1.00 9.33   ? 103 ALA D C   1 
ATOM   5893  O O   . ALA D  1 111 ? -4.010  37.018  40.431  1.00 10.23  ? 103 ALA D O   1 
ATOM   5894  C CB  . ALA D  1 111 ? -1.421  36.911  42.613  1.00 9.18   ? 103 ALA D CB  1 
ATOM   5895  N N   . ARG D  1 112 ? -3.522  38.898  41.528  1.00 10.49  ? 104 ARG D N   1 
ATOM   5896  C CA  . ARG D  1 112 ? -3.875  39.729  40.384  1.00 13.03  ? 104 ARG D CA  1 
ATOM   5897  C C   . ARG D  1 112 ? -2.633  40.475  39.930  1.00 13.61  ? 104 ARG D C   1 
ATOM   5898  O O   . ARG D  1 112 ? -1.931  41.081  40.738  1.00 14.66  ? 104 ARG D O   1 
ATOM   5899  C CB  . ARG D  1 112 ? -5.000  40.718  40.706  1.00 12.91  ? 104 ARG D CB  1 
ATOM   5900  C CG  . ARG D  1 112 ? -6.323  40.079  41.092  1.00 16.24  ? 104 ARG D CG  1 
ATOM   5901  C CD  . ARG D  1 112 ? -7.132  39.504  39.914  1.00 13.34  ? 104 ARG D CD  1 
ATOM   5902  N NE  . ARG D  1 112 ? -7.635  40.523  38.993  1.00 18.43  ? 104 ARG D NE  1 
ATOM   5903  C CZ  . ARG D  1 112 ? -8.446  40.265  37.964  1.00 20.96  ? 104 ARG D CZ  1 
ATOM   5904  N NH1 . ARG D  1 112 ? -8.862  39.028  37.744  1.00 20.21  ? 104 ARG D NH1 1 
ATOM   5905  N NH2 . ARG D  1 112 ? -8.852  41.235  37.155  1.00 20.12  ? 104 ARG D NH2 1 
ATOM   5906  N N   . VAL D  1 113 ? -2.344  40.414  38.640  1.00 12.30  ? 105 VAL D N   1 
ATOM   5907  C CA  . VAL D  1 113 ? -1.285  41.247  38.098  1.00 13.59  ? 105 VAL D CA  1 
ATOM   5908  C C   . VAL D  1 113 ? -1.881  42.393  37.278  1.00 16.07  ? 105 VAL D C   1 
ATOM   5909  O O   . VAL D  1 113 ? -2.716  42.174  36.385  1.00 12.81  ? 105 VAL D O   1 
ATOM   5910  C CB  . VAL D  1 113 ? -0.300  40.440  37.243  1.00 12.91  ? 105 VAL D CB  1 
ATOM   5911  C CG1 . VAL D  1 113 ? 0.829   41.323  36.796  1.00 17.20  ? 105 VAL D CG1 1 
ATOM   5912  C CG2 . VAL D  1 113 ? 0.250   39.262  38.028  1.00 15.05  ? 105 VAL D CG2 1 
ATOM   5913  N N   . VAL D  1 114 ? -1.448  43.610  37.597  1.00 15.11  ? 106 VAL D N   1 
ATOM   5914  C CA  . VAL D  1 114 ? -1.895  44.810  36.887  1.00 17.11  ? 106 VAL D CA  1 
ATOM   5915  C C   . VAL D  1 114 ? -0.908  45.227  35.770  1.00 19.34  ? 106 VAL D C   1 
ATOM   5916  O O   . VAL D  1 114 ? 0.322   45.043  35.900  1.00 13.36  ? 106 VAL D O   1 
ATOM   5917  C CB  . VAL D  1 114 ? -2.147  45.959  37.898  1.00 18.08  ? 106 VAL D CB  1 
ATOM   5918  C CG1 . VAL D  1 114 ? -2.787  47.168  37.228  1.00 13.42  ? 106 VAL D CG1 1 
ATOM   5919  C CG2 . VAL D  1 114 ? -3.024  45.452  39.042  1.00 15.65  ? 106 VAL D CG2 1 
ATOM   5920  N N   . SER D  1 115 ? -1.445  45.788  34.680  1.00 18.51  ? 107 SER D N   1 
ATOM   5921  C CA  . SER D  1 115 ? -0.633  46.123  33.497  1.00 16.76  ? 107 SER D CA  1 
ATOM   5922  C C   . SER D  1 115 ? 0.593   46.984  33.771  1.00 13.96  ? 107 SER D C   1 
ATOM   5923  O O   . SER D  1 115 ? 1.538   46.978  32.986  1.00 14.37  ? 107 SER D O   1 
ATOM   5924  C CB  . SER D  1 115 ? -1.479  46.749  32.381  1.00 19.87  ? 107 SER D CB  1 
ATOM   5925  O OG  . SER D  1 115 ? -1.778  48.102  32.658  1.00 24.94  ? 107 SER D OG  1 
ATOM   5926  N N   . ASP D  1 116 ? 0.588   47.719  34.875  1.00 13.93  ? 108 ASP D N   1 
ATOM   5927  C CA  . ASP D  1 116 ? 1.772   48.493  35.260  1.00 14.07  ? 108 ASP D CA  1 
ATOM   5928  C C   . ASP D  1 116 ? 2.721   47.710  36.159  1.00 16.35  ? 108 ASP D C   1 
ATOM   5929  O O   . ASP D  1 116 ? 3.583   48.291  36.812  1.00 20.53  ? 108 ASP D O   1 
ATOM   5930  C CB  . ASP D  1 116 ? 1.381   49.813  35.933  1.00 18.47  ? 108 ASP D CB  1 
ATOM   5931  C CG  . ASP D  1 116 ? 0.346   49.633  37.051  1.00 26.29  ? 108 ASP D CG  1 
ATOM   5932  O OD1 . ASP D  1 116 ? 0.487   48.709  37.889  1.00 27.61  ? 108 ASP D OD1 1 
ATOM   5933  O OD2 . ASP D  1 116 ? -0.619  50.429  37.091  1.00 29.00  ? 108 ASP D OD2 1 
ATOM   5934  N N   . GLY D  1 117 ? 2.544   46.394  36.220  1.00 15.75  ? 109 GLY D N   1 
ATOM   5935  C CA  . GLY D  1 117 ? 3.479   45.544  36.931  1.00 14.10  ? 109 GLY D CA  1 
ATOM   5936  C C   . GLY D  1 117 ? 3.205   45.391  38.411  1.00 17.53  ? 109 GLY D C   1 
ATOM   5937  O O   . GLY D  1 117 ? 4.015   44.815  39.146  1.00 18.09  ? 109 GLY D O   1 
ATOM   5938  N N   . GLU D  1 118 ? 2.069   45.908  38.860  1.00 16.80  ? 110 GLU D N   1 
ATOM   5939  C CA  . GLU D  1 118 ? 1.687   45.746  40.250  1.00 18.36  ? 110 GLU D CA  1 
ATOM   5940  C C   . GLU D  1 118 ? 1.075   44.357  40.439  1.00 16.63  ? 110 GLU D C   1 
ATOM   5941  O O   . GLU D  1 118 ? 0.303   43.888  39.593  1.00 16.56  ? 110 GLU D O   1 
ATOM   5942  C CB  . GLU D  1 118 ? 0.696   46.831  40.655  1.00 18.52  ? 110 GLU D CB  1 
ATOM   5943  C CG  . GLU D  1 118 ? 0.360   46.856  42.135  1.00 19.93  ? 110 GLU D CG  1 
ATOM   5944  C CD  . GLU D  1 118 ? -0.831  47.773  42.451  1.00 42.97  ? 110 GLU D CD  1 
ATOM   5945  O OE1 . GLU D  1 118 ? -1.269  48.532  41.549  1.00 43.84  ? 110 GLU D OE1 1 
ATOM   5946  O OE2 . GLU D  1 118 ? -1.339  47.728  43.598  1.00 45.45  ? 110 GLU D OE2 1 
ATOM   5947  N N   . VAL D  1 119 ? 1.438   43.703  41.539  1.00 12.06  ? 111 VAL D N   1 
ATOM   5948  C CA  . VAL D  1 119 ? 0.916   42.386  41.885  1.00 11.46  ? 111 VAL D CA  1 
ATOM   5949  C C   . VAL D  1 119 ? 0.219   42.470  43.237  1.00 13.89  ? 111 VAL D C   1 
ATOM   5950  O O   . VAL D  1 119 ? 0.785   42.995  44.209  1.00 13.11  ? 111 VAL D O   1 
ATOM   5951  C CB  . VAL D  1 119 ? 2.060   41.335  41.982  1.00 12.22  ? 111 VAL D CB  1 
ATOM   5952  C CG1 . VAL D  1 119 ? 1.497   39.926  42.113  1.00 8.74   ? 111 VAL D CG1 1 
ATOM   5953  C CG2 . VAL D  1 119 ? 2.965   41.432  40.777  1.00 10.20  ? 111 VAL D CG2 1 
ATOM   5954  N N   . LEU D  1 120 ? -1.014  41.983  43.304  1.00 12.79  ? 112 LEU D N   1 
ATOM   5955  C CA  . LEU D  1 120 ? -1.683  41.861  44.596  1.00 15.20  ? 112 LEU D CA  1 
ATOM   5956  C C   . LEU D  1 120 ? -2.140  40.445  44.865  1.00 12.33  ? 112 LEU D C   1 
ATOM   5957  O O   . LEU D  1 120 ? -2.706  39.784  44.002  1.00 11.51  ? 112 LEU D O   1 
ATOM   5958  C CB  . LEU D  1 120 ? -2.844  42.850  44.782  1.00 14.05  ? 112 LEU D CB  1 
ATOM   5959  C CG  . LEU D  1 120 ? -3.724  43.272  43.607  1.00 21.25  ? 112 LEU D CG  1 
ATOM   5960  C CD1 . LEU D  1 120 ? -5.140  43.508  44.091  1.00 21.35  ? 112 LEU D CD1 1 
ATOM   5961  C CD2 . LEU D  1 120 ? -3.180  44.532  42.946  1.00 19.15  ? 112 LEU D CD2 1 
ATOM   5962  N N   . TYR D  1 121 ? -1.858  39.995  46.078  1.00 10.93  ? 113 TYR D N   1 
ATOM   5963  C CA  . TYR D  1 121 ? -2.266  38.688  46.552  1.00 12.56  ? 113 TYR D CA  1 
ATOM   5964  C C   . TYR D  1 121 ? -2.896  38.845  47.938  1.00 13.70  ? 113 TYR D C   1 
ATOM   5965  O O   . TYR D  1 121 ? -2.235  39.270  48.893  1.00 12.89  ? 113 TYR D O   1 
ATOM   5966  C CB  . TYR D  1 121 ? -1.062  37.737  46.582  1.00 11.93  ? 113 TYR D CB  1 
ATOM   5967  C CG  . TYR D  1 121 ? -1.365  36.360  47.113  1.00 10.01  ? 113 TYR D CG  1 
ATOM   5968  C CD1 . TYR D  1 121 ? -2.332  35.559  46.512  1.00 9.18   ? 113 TYR D CD1 1 
ATOM   5969  C CD2 . TYR D  1 121 ? -0.677  35.857  48.209  1.00 9.40   ? 113 TYR D CD2 1 
ATOM   5970  C CE1 . TYR D  1 121 ? -2.605  34.301  46.987  1.00 10.39  ? 113 TYR D CE1 1 
ATOM   5971  C CE2 . TYR D  1 121 ? -0.944  34.596  48.697  1.00 11.42  ? 113 TYR D CE2 1 
ATOM   5972  C CZ  . TYR D  1 121 ? -1.911  33.825  48.086  1.00 12.70  ? 113 TYR D CZ  1 
ATOM   5973  O OH  . TYR D  1 121 ? -2.174  32.565  48.568  1.00 15.13  ? 113 TYR D OH  1 
ATOM   5974  N N   . MET D  1 122 ? -4.188  38.532  48.024  1.00 14.58  ? 114 MET D N   1 
ATOM   5975  C CA  . MET D  1 122 ? -4.929  38.643  49.268  1.00 12.85  ? 114 MET D CA  1 
ATOM   5976  C C   . MET D  1 122 ? -5.682  37.369  49.614  1.00 11.27  ? 114 MET D C   1 
ATOM   5977  O O   . MET D  1 122 ? -6.880  37.247  49.323  1.00 11.29  ? 114 MET D O   1 
ATOM   5978  C CB  . MET D  1 122 ? -5.920  39.798  49.218  1.00 18.01  ? 114 MET D CB  1 
ATOM   5979  C CG  . MET D  1 122 ? -6.485  40.139  50.638  1.00 22.41  ? 114 MET D CG  1 
ATOM   5980  S SD  . MET D  1 122 ? -7.895  41.290  50.684  1.00 41.11  ? 114 MET D SD  1 
ATOM   5981  C CE  . MET D  1 122 ? -9.257  40.157  50.544  1.00 14.77  ? 114 MET D CE  1 
ATOM   5982  N N   . PRO D  1 123 ? -4.984  36.413  50.233  1.00 9.46   ? 115 PRO D N   1 
ATOM   5983  C CA  . PRO D  1 123 ? -5.640  35.210  50.755  1.00 12.37  ? 115 PRO D CA  1 
ATOM   5984  C C   . PRO D  1 123 ? -6.425  35.490  52.043  1.00 15.14  ? 115 PRO D C   1 
ATOM   5985  O O   . PRO D  1 123 ? -6.026  36.305  52.889  1.00 13.96  ? 115 PRO D O   1 
ATOM   5986  C CB  . PRO D  1 123 ? -4.459  34.282  51.078  1.00 11.70  ? 115 PRO D CB  1 
ATOM   5987  C CG  . PRO D  1 123 ? -3.337  35.215  51.405  1.00 12.39  ? 115 PRO D CG  1 
ATOM   5988  C CD  . PRO D  1 123 ? -3.529  36.397  50.463  1.00 11.61  ? 115 PRO D CD  1 
ATOM   5989  N N   . SER D  1 124 ? -7.554  34.815  52.182  1.00 14.10  ? 116 SER D N   1 
ATOM   5990  C CA  . SER D  1 124 ? -8.201  34.714  53.473  1.00 15.54  ? 116 SER D CA  1 
ATOM   5991  C C   . SER D  1 124 ? -7.429  33.643  54.223  1.00 14.40  ? 116 SER D C   1 
ATOM   5992  O O   . SER D  1 124 ? -7.141  32.584  53.663  1.00 16.31  ? 116 SER D O   1 
ATOM   5993  C CB  . SER D  1 124 ? -9.651  34.286  53.300  1.00 15.57  ? 116 SER D CB  1 
ATOM   5994  O OG  . SER D  1 124 ? -10.377 34.486  54.499  1.00 28.85  ? 116 SER D OG  1 
ATOM   5995  N N   . ILE D  1 125 ? -7.067  33.924  55.470  1.00 11.53  ? 117 ILE D N   1 
ATOM   5996  C CA  . ILE D  1 125 ? -6.270  33.000  56.266  1.00 12.66  ? 117 ILE D CA  1 
ATOM   5997  C C   . ILE D  1 125 ? -6.906  32.775  57.641  1.00 14.07  ? 117 ILE D C   1 
ATOM   5998  O O   . ILE D  1 125 ? -7.331  33.707  58.301  1.00 11.63  ? 117 ILE D O   1 
ATOM   5999  C CB  . ILE D  1 125 ? -4.817  33.521  56.461  1.00 11.39  ? 117 ILE D CB  1 
ATOM   6000  C CG1 . ILE D  1 125 ? -4.054  33.577  55.133  1.00 12.06  ? 117 ILE D CG1 1 
ATOM   6001  C CG2 . ILE D  1 125 ? -4.040  32.669  57.480  1.00 12.11  ? 117 ILE D CG2 1 
ATOM   6002  C CD1 . ILE D  1 125 ? -2.540  33.871  55.300  1.00 9.54   ? 117 ILE D CD1 1 
ATOM   6003  N N   . ARG D  1 126 ? -6.979  31.526  58.066  1.00 15.56  ? 118 ARG D N   1 
ATOM   6004  C CA  . ARG D  1 126 ? -7.310  31.233  59.442  1.00 13.82  ? 118 ARG D CA  1 
ATOM   6005  C C   . ARG D  1 126 ? -6.062  30.703  60.115  1.00 13.70  ? 118 ARG D C   1 
ATOM   6006  O O   . ARG D  1 126 ? -5.478  29.749  59.642  1.00 15.49  ? 118 ARG D O   1 
ATOM   6007  C CB  . ARG D  1 126 ? -8.424  30.198  59.528  1.00 16.98  ? 118 ARG D CB  1 
ATOM   6008  C CG  . ARG D  1 126 ? -8.701  29.728  60.947  1.00 21.47  ? 118 ARG D CG  1 
ATOM   6009  C CD  . ARG D  1 126 ? -9.684  28.583  60.958  1.00 25.01  ? 118 ARG D CD  1 
ATOM   6010  N NE  . ARG D  1 126 ? -9.782  27.989  62.285  1.00 38.76  ? 118 ARG D NE  1 
ATOM   6011  C CZ  . ARG D  1 126 ? -10.815 27.266  62.713  1.00 41.99  ? 118 ARG D CZ  1 
ATOM   6012  N NH1 . ARG D  1 126 ? -11.857 27.056  61.912  1.00 35.82  ? 118 ARG D NH1 1 
ATOM   6013  N NH2 . ARG D  1 126 ? -10.810 26.759  63.946  1.00 37.86  ? 118 ARG D NH2 1 
ATOM   6014  N N   . GLN D  1 127 ? -5.664  31.315  61.227  1.00 16.02  ? 119 GLN D N   1 
ATOM   6015  C CA  . GLN D  1 127 ? -4.419  30.952  61.898  1.00 15.88  ? 119 GLN D CA  1 
ATOM   6016  C C   . GLN D  1 127 ? -4.483  31.151  63.432  1.00 17.30  ? 119 GLN D C   1 
ATOM   6017  O O   . GLN D  1 127 ? -5.211  32.001  63.943  1.00 17.31  ? 119 GLN D O   1 
ATOM   6018  C CB  . GLN D  1 127 ? -3.266  31.743  61.277  1.00 11.13  ? 119 GLN D CB  1 
ATOM   6019  C CG  . GLN D  1 127 ? -1.901  31.408  61.811  1.00 15.16  ? 119 GLN D CG  1 
ATOM   6020  C CD  . GLN D  1 127 ? -0.773  31.737  60.842  1.00 13.84  ? 119 GLN D CD  1 
ATOM   6021  O OE1 . GLN D  1 127 ? -0.802  32.750  60.136  1.00 15.98  ? 119 GLN D OE1 1 
ATOM   6022  N NE2 . GLN D  1 127 ? 0.228   30.871  60.806  1.00 12.40  ? 119 GLN D NE2 1 
ATOM   6023  N N   . ARG D  1 128 ? -3.719  30.361  64.166  1.00 15.86  ? 120 ARG D N   1 
ATOM   6024  C CA  . ARG D  1 128 ? -3.748  30.430  65.615  1.00 17.92  ? 120 ARG D CA  1 
ATOM   6025  C C   . ARG D  1 128 ? -2.557  31.262  66.060  1.00 16.95  ? 120 ARG D C   1 
ATOM   6026  O O   . ARG D  1 128 ? -1.469  31.137  65.485  1.00 19.41  ? 120 ARG D O   1 
ATOM   6027  C CB  . ARG D  1 128 ? -3.690  29.015  66.215  1.00 20.65  ? 120 ARG D CB  1 
ATOM   6028  C CG  . ARG D  1 128 ? -4.546  28.805  67.463  1.00 31.46  ? 120 ARG D CG  1 
ATOM   6029  C CD  . ARG D  1 128 ? -4.675  27.316  67.794  1.00 37.58  ? 120 ARG D CD  1 
ATOM   6030  N NE  . ARG D  1 128 ? -4.977  26.528  66.596  1.00 44.38  ? 120 ARG D NE  1 
ATOM   6031  C CZ  . ARG D  1 128 ? -6.138  25.916  66.357  1.00 53.02  ? 120 ARG D CZ  1 
ATOM   6032  N NH1 . ARG D  1 128 ? -7.135  25.982  67.245  1.00 41.21  ? 120 ARG D NH1 1 
ATOM   6033  N NH2 . ARG D  1 128 ? -6.295  25.231  65.223  1.00 50.84  ? 120 ARG D NH2 1 
ATOM   6034  N N   . PHE D  1 129 ? -2.758  32.123  67.054  1.00 15.31  ? 121 PHE D N   1 
ATOM   6035  C CA  . PHE D  1 129 ? -1.666  32.947  67.582  1.00 17.28  ? 121 PHE D CA  1 
ATOM   6036  C C   . PHE D  1 129 ? -1.473  32.814  69.085  1.00 20.86  ? 121 PHE D C   1 
ATOM   6037  O O   . PHE D  1 129 ? -2.378  32.410  69.823  1.00 22.26  ? 121 PHE D O   1 
ATOM   6038  C CB  . PHE D  1 129 ? -1.856  34.421  67.225  1.00 14.52  ? 121 PHE D CB  1 
ATOM   6039  C CG  . PHE D  1 129 ? -1.822  34.687  65.766  1.00 13.32  ? 121 PHE D CG  1 
ATOM   6040  C CD1 . PHE D  1 129 ? -2.979  34.627  65.014  1.00 14.28  ? 121 PHE D CD1 1 
ATOM   6041  C CD2 . PHE D  1 129 ? -0.627  34.966  65.134  1.00 16.79  ? 121 PHE D CD2 1 
ATOM   6042  C CE1 . PHE D  1 129 ? -2.944  34.855  63.658  1.00 16.68  ? 121 PHE D CE1 1 
ATOM   6043  C CE2 . PHE D  1 129 ? -0.583  35.189  63.775  1.00 14.48  ? 121 PHE D CE2 1 
ATOM   6044  C CZ  . PHE D  1 129 ? -1.742  35.134  63.034  1.00 15.39  ? 121 PHE D CZ  1 
ATOM   6045  N N   . SER D  1 130 ? -0.277  33.174  69.523  1.00 20.50  ? 122 SER D N   1 
ATOM   6046  C CA  . SER D  1 130 ? 0.065   33.198  70.928  1.00 21.56  ? 122 SER D CA  1 
ATOM   6047  C C   . SER D  1 130 ? 0.251   34.650  71.362  1.00 29.88  ? 122 SER D C   1 
ATOM   6048  O O   . SER D  1 130 ? 1.252   35.290  71.027  1.00 29.74  ? 122 SER D O   1 
ATOM   6049  C CB  . SER D  1 130 ? 1.347   32.408  71.151  1.00 24.71  ? 122 SER D CB  1 
ATOM   6050  O OG  . SER D  1 130 ? 1.865   32.626  72.444  1.00 34.89  ? 122 SER D OG  1 
ATOM   6051  N N   . CYS D  1 131 ? -0.737  35.183  72.086  1.00 36.44  ? 123 CYS D N   1 
ATOM   6052  C CA  . CYS D  1 131 ? -0.751  36.596  72.497  1.00 42.13  ? 123 CYS D CA  1 
ATOM   6053  C C   . CYS D  1 131 ? -1.542  36.858  73.792  1.00 39.24  ? 123 CYS D C   1 
ATOM   6054  O O   . CYS D  1 131 ? -2.346  36.025  74.209  1.00 39.88  ? 123 CYS D O   1 
ATOM   6055  C CB  . CYS D  1 131 ? -1.293  37.474  71.367  1.00 45.25  ? 123 CYS D CB  1 
ATOM   6056  S SG  . CYS D  1 131 ? -2.307  36.594  70.156  1.00 50.92  ? 123 CYS D SG  1 
ATOM   6057  N N   . ASP D  1 132 ? -1.310  38.013  74.422  1.00 38.92  ? 124 ASP D N   1 
ATOM   6058  C CA  . ASP D  1 132 ? -1.985  38.359  75.682  1.00 36.97  ? 124 ASP D CA  1 
ATOM   6059  C C   . ASP D  1 132 ? -3.504  38.411  75.525  1.00 32.49  ? 124 ASP D C   1 
ATOM   6060  O O   . ASP D  1 132 ? -4.027  39.163  74.705  1.00 34.91  ? 124 ASP D O   1 
ATOM   6061  C CB  . ASP D  1 132 ? -1.479  39.693  76.231  1.00 37.60  ? 124 ASP D CB  1 
ATOM   6062  C CG  . ASP D  1 132 ? -1.493  39.741  77.752  1.00 43.70  ? 124 ASP D CG  1 
ATOM   6063  O OD1 . ASP D  1 132 ? -2.242  38.944  78.370  1.00 35.27  ? 124 ASP D OD1 1 
ATOM   6064  O OD2 . ASP D  1 132 ? -0.745  40.574  78.322  1.00 42.30  ? 124 ASP D OD2 1 
ATOM   6065  N N   . VAL D  1 133 ? -4.199  37.615  76.327  1.00 28.84  ? 125 VAL D N   1 
ATOM   6066  C CA  . VAL D  1 133 ? -5.637  37.424  76.197  1.00 29.51  ? 125 VAL D CA  1 
ATOM   6067  C C   . VAL D  1 133 ? -6.359  37.987  77.422  1.00 33.57  ? 125 VAL D C   1 
ATOM   6068  O O   . VAL D  1 133 ? -7.595  38.037  77.483  1.00 29.44  ? 125 VAL D O   1 
ATOM   6069  C CB  . VAL D  1 133 ? -5.960  35.921  76.051  1.00 31.57  ? 125 VAL D CB  1 
ATOM   6070  C CG1 . VAL D  1 133 ? -7.382  35.719  75.668  1.00 27.23  ? 125 VAL D CG1 1 
ATOM   6071  C CG2 . VAL D  1 133 ? -5.088  35.306  74.991  1.00 36.36  ? 125 VAL D CG2 1 
ATOM   6072  N N   . SER D  1 134 ? -5.575  38.410  78.408  1.00 35.35  ? 126 SER D N   1 
ATOM   6073  C CA  . SER D  1 134 ? -6.136  39.010  79.611  1.00 35.21  ? 126 SER D CA  1 
ATOM   6074  C C   . SER D  1 134 ? -6.874  40.309  79.283  1.00 31.04  ? 126 SER D C   1 
ATOM   6075  O O   . SER D  1 134 ? -6.368  41.165  78.552  1.00 33.56  ? 126 SER D O   1 
ATOM   6076  C CB  . SER D  1 134 ? -5.037  39.254  80.649  1.00 35.19  ? 126 SER D CB  1 
ATOM   6077  O OG  . SER D  1 134 ? -3.785  39.460  80.016  1.00 42.37  ? 126 SER D OG  1 
ATOM   6078  N N   . GLY D  1 135 ? -8.081  40.445  79.818  1.00 23.52  ? 127 GLY D N   1 
ATOM   6079  C CA  . GLY D  1 135 ? -8.858  41.646  79.603  1.00 24.72  ? 127 GLY D CA  1 
ATOM   6080  C C   . GLY D  1 135 ? -10.017 41.405  78.663  1.00 28.44  ? 127 GLY D C   1 
ATOM   6081  O O   . GLY D  1 135 ? -10.924 42.233  78.565  1.00 26.14  ? 127 GLY D O   1 
ATOM   6082  N N   . VAL D  1 136 ? -9.986  40.259  77.982  1.00 28.19  ? 128 VAL D N   1 
ATOM   6083  C CA  . VAL D  1 136 ? -11.004 39.896  77.002  1.00 23.07  ? 128 VAL D CA  1 
ATOM   6084  C C   . VAL D  1 136 ? -12.420 40.072  77.552  1.00 23.39  ? 128 VAL D C   1 
ATOM   6085  O O   . VAL D  1 136 ? -13.353 40.372  76.815  1.00 24.72  ? 128 VAL D O   1 
ATOM   6086  C CB  . VAL D  1 136 ? -10.778 38.450  76.450  1.00 19.95  ? 128 VAL D CB  1 
ATOM   6087  C CG1 . VAL D  1 136 ? -10.760 37.433  77.563  1.00 18.66  ? 128 VAL D CG1 1 
ATOM   6088  C CG2 . VAL D  1 136 ? -11.823 38.079  75.388  1.00 17.68  ? 128 VAL D CG2 1 
ATOM   6089  N N   . ASP D  1 137 ? -12.570 39.918  78.858  1.00 27.51  ? 129 ASP D N   1 
ATOM   6090  C CA  . ASP D  1 137 ? -13.893 39.972  79.458  1.00 34.69  ? 129 ASP D CA  1 
ATOM   6091  C C   . ASP D  1 137 ? -14.183 41.300  80.155  1.00 35.70  ? 129 ASP D C   1 
ATOM   6092  O O   . ASP D  1 137 ? -15.196 41.424  80.845  1.00 33.09  ? 129 ASP D O   1 
ATOM   6093  C CB  . ASP D  1 137 ? -14.081 38.810  80.436  1.00 40.08  ? 129 ASP D CB  1 
ATOM   6094  C CG  . ASP D  1 137 ? -15.189 37.858  80.007  1.00 54.29  ? 129 ASP D CG  1 
ATOM   6095  O OD1 . ASP D  1 137 ? -16.363 38.305  79.960  1.00 50.64  ? 129 ASP D OD1 1 
ATOM   6096  O OD2 . ASP D  1 137 ? -14.885 36.669  79.728  1.00 46.20  ? 129 ASP D OD2 1 
ATOM   6097  N N   . THR D  1 138 ? -13.301 42.285  79.971  1.00 29.75  ? 130 THR D N   1 
ATOM   6098  C CA  . THR D  1 138 ? -13.470 43.596  80.593  1.00 25.85  ? 130 THR D CA  1 
ATOM   6099  C C   . THR D  1 138 ? -13.869 44.659  79.580  1.00 32.33  ? 130 THR D C   1 
ATOM   6100  O O   . THR D  1 138 ? -13.965 44.390  78.385  1.00 32.94  ? 130 THR D O   1 
ATOM   6101  C CB  . THR D  1 138 ? -12.183 44.080  81.307  1.00 29.03  ? 130 THR D CB  1 
ATOM   6102  O OG1 . THR D  1 138 ? -11.324 44.755  80.372  1.00 34.59  ? 130 THR D OG1 1 
ATOM   6103  C CG2 . THR D  1 138 ? -11.442 42.915  81.966  1.00 25.46  ? 130 THR D CG2 1 
ATOM   6104  N N   . GLU D  1 139 ? -14.097 45.873  80.072  1.00 35.04  ? 131 GLU D N   1 
ATOM   6105  C CA  . GLU D  1 139 ? -14.440 47.004  79.222  1.00 33.61  ? 131 GLU D CA  1 
ATOM   6106  C C   . GLU D  1 139 ? -13.358 47.235  78.194  1.00 32.31  ? 131 GLU D C   1 
ATOM   6107  O O   . GLU D  1 139 ? -13.632 47.357  76.998  1.00 31.03  ? 131 GLU D O   1 
ATOM   6108  C CB  . GLU D  1 139 ? -14.563 48.275  80.062  1.00 37.57  ? 131 GLU D CB  1 
ATOM   6109  C CG  . GLU D  1 139 ? -15.864 48.416  80.809  1.00 46.58  ? 131 GLU D CG  1 
ATOM   6110  C CD  . GLU D  1 139 ? -17.011 48.773  79.894  1.00 51.98  ? 131 GLU D CD  1 
ATOM   6111  O OE1 . GLU D  1 139 ? -16.751 49.084  78.707  1.00 43.44  ? 131 GLU D OE1 1 
ATOM   6112  O OE2 . GLU D  1 139 ? -18.170 48.743  80.366  1.00 69.22  ? 131 GLU D OE2 1 
ATOM   6113  N N   . SER D  1 140 ? -12.125 47.299  78.683  1.00 27.09  ? 132 SER D N   1 
ATOM   6114  C CA  . SER D  1 140 ? -10.999 47.737  77.879  1.00 28.14  ? 132 SER D CA  1 
ATOM   6115  C C   . SER D  1 140 ? -10.548 46.695  76.843  1.00 25.12  ? 132 SER D C   1 
ATOM   6116  O O   . SER D  1 140 ? -9.827  47.035  75.921  1.00 20.04  ? 132 SER D O   1 
ATOM   6117  C CB  . SER D  1 140 ? -9.827  48.133  78.789  1.00 34.51  ? 132 SER D CB  1 
ATOM   6118  O OG  . SER D  1 140 ? -9.005  47.016  79.118  1.00 38.75  ? 132 SER D OG  1 
ATOM   6119  N N   . GLY D  1 141 ? -10.962 45.439  77.018  1.00 26.02  ? 133 GLY D N   1 
ATOM   6120  C CA  . GLY D  1 141 ? -10.670 44.366  76.085  1.00 20.52  ? 133 GLY D CA  1 
ATOM   6121  C C   . GLY D  1 141 ? -9.244  43.834  76.133  1.00 25.53  ? 133 GLY D C   1 
ATOM   6122  O O   . GLY D  1 141 ? -8.393  44.389  76.825  1.00 28.70  ? 133 GLY D O   1 
ATOM   6123  N N   . ALA D  1 142 ? -8.983  42.755  75.390  1.00 24.45  ? 134 ALA D N   1 
ATOM   6124  C CA  . ALA D  1 142 ? -7.637  42.194  75.277  1.00 23.55  ? 134 ALA D CA  1 
ATOM   6125  C C   . ALA D  1 142 ? -6.926  42.873  74.124  1.00 21.83  ? 134 ALA D C   1 
ATOM   6126  O O   . ALA D  1 142 ? -7.582  43.405  73.238  1.00 25.91  ? 134 ALA D O   1 
ATOM   6127  C CB  . ALA D  1 142 ? -7.706  40.703  75.039  1.00 20.64  ? 134 ALA D CB  1 
ATOM   6128  N N   . THR D  1 143 ? -5.596  42.868  74.130  1.00 22.63  ? 135 THR D N   1 
ATOM   6129  C CA  . THR D  1 143 ? -4.832  43.422  73.002  1.00 28.45  ? 135 THR D CA  1 
ATOM   6130  C C   . THR D  1 143 ? -3.745  42.461  72.481  1.00 27.26  ? 135 THR D C   1 
ATOM   6131  O O   . THR D  1 143 ? -2.651  42.381  73.046  1.00 22.17  ? 135 THR D O   1 
ATOM   6132  C CB  . THR D  1 143 ? -4.180  44.786  73.352  1.00 27.95  ? 135 THR D CB  1 
ATOM   6133  O OG1 . THR D  1 143 ? -5.188  45.722  73.747  1.00 32.61  ? 135 THR D OG1 1 
ATOM   6134  C CG2 . THR D  1 143 ? -3.437  45.352  72.156  1.00 26.50  ? 135 THR D CG2 1 
ATOM   6135  N N   . CYS D  1 144 ? -4.039  41.768  71.386  1.00 22.46  ? 136 CYS D N   1 
ATOM   6136  C CA  . CYS D  1 144 ? -3.097  40.805  70.825  1.00 23.61  ? 136 CYS D CA  1 
ATOM   6137  C C   . CYS D  1 144 ? -2.290  41.417  69.684  1.00 25.07  ? 136 CYS D C   1 
ATOM   6138  O O   . CYS D  1 144 ? -2.850  41.987  68.747  1.00 21.93  ? 136 CYS D O   1 
ATOM   6139  C CB  . CYS D  1 144 ? -3.835  39.557  70.336  1.00 29.97  ? 136 CYS D CB  1 
ATOM   6140  S SG  . CYS D  1 144 ? -3.052  38.728  68.934  1.00 71.14  ? 136 CYS D SG  1 
ATOM   6141  N N   . ARG D  1 145 ? -0.969  41.296  69.776  1.00 26.06  ? 137 ARG D N   1 
ATOM   6142  C CA  . ARG D  1 145 ? -0.072  41.869  68.788  1.00 26.97  ? 137 ARG D CA  1 
ATOM   6143  C C   . ARG D  1 145 ? 0.495   40.791  67.869  1.00 24.25  ? 137 ARG D C   1 
ATOM   6144  O O   . ARG D  1 145 ? 1.152   39.860  68.336  1.00 25.30  ? 137 ARG D O   1 
ATOM   6145  C CB  . ARG D  1 145 ? 1.070   42.645  69.467  1.00 27.75  ? 137 ARG D CB  1 
ATOM   6146  C CG  . ARG D  1 145 ? 0.634   43.937  70.157  1.00 26.63  ? 137 ARG D CG  1 
ATOM   6147  C CD  . ARG D  1 145 ? 1.822   44.739  70.703  1.00 36.13  ? 137 ARG D CD  1 
ATOM   6148  N NE  . ARG D  1 145 ? 2.508   44.063  71.807  1.00 48.64  ? 137 ARG D NE  1 
ATOM   6149  C CZ  . ARG D  1 145 ? 3.599   43.310  71.674  1.00 48.92  ? 137 ARG D CZ  1 
ATOM   6150  N NH1 . ARG D  1 145 ? 4.147   43.132  70.477  1.00 51.15  ? 137 ARG D NH1 1 
ATOM   6151  N NH2 . ARG D  1 145 ? 4.146   42.732  72.738  1.00 42.20  ? 137 ARG D NH2 1 
ATOM   6152  N N   . ILE D  1 146 ? 0.239   40.938  66.566  1.00 23.47  ? 138 ILE D N   1 
ATOM   6153  C CA  . ILE D  1 146 ? 0.746   40.030  65.532  1.00 20.80  ? 138 ILE D CA  1 
ATOM   6154  C C   . ILE D  1 146 ? 1.836   40.686  64.655  1.00 21.78  ? 138 ILE D C   1 
ATOM   6155  O O   . ILE D  1 146 ? 1.589   41.691  63.991  1.00 23.90  ? 138 ILE D O   1 
ATOM   6156  C CB  . ILE D  1 146 ? -0.397  39.565  64.612  1.00 18.95  ? 138 ILE D CB  1 
ATOM   6157  C CG1 . ILE D  1 146 ? -1.507  38.888  65.408  1.00 15.91  ? 138 ILE D CG1 1 
ATOM   6158  C CG2 . ILE D  1 146 ? 0.116   38.606  63.558  1.00 19.56  ? 138 ILE D CG2 1 
ATOM   6159  C CD1 . ILE D  1 146 ? -2.669  38.426  64.528  1.00 12.55  ? 138 ILE D CD1 1 
ATOM   6160  N N   . LYS D  1 147 ? 3.039   40.120  64.636  1.00 21.43  ? 139 LYS D N   1 
ATOM   6161  C CA  . LYS D  1 147 ? 4.086   40.645  63.759  1.00 20.75  ? 139 LYS D CA  1 
ATOM   6162  C C   . LYS D  1 147 ? 4.228   39.807  62.489  1.00 20.84  ? 139 LYS D C   1 
ATOM   6163  O O   . LYS D  1 147 ? 4.407   38.594  62.568  1.00 19.30  ? 139 LYS D O   1 
ATOM   6164  C CB  . LYS D  1 147 ? 5.427   40.682  64.492  1.00 27.42  ? 139 LYS D CB  1 
ATOM   6165  C CG  . LYS D  1 147 ? 5.817   42.039  65.054  1.00 32.51  ? 139 LYS D CG  1 
ATOM   6166  C CD  . LYS D  1 147 ? 7.072   41.914  65.909  1.00 38.15  ? 139 LYS D CD  1 
ATOM   6167  C CE  . LYS D  1 147 ? 7.490   43.250  66.500  1.00 41.81  ? 139 LYS D CE  1 
ATOM   6168  N NZ  . LYS D  1 147 ? 8.719   43.125  67.333  1.00 41.92  ? 139 LYS D NZ  1 
ATOM   6169  N N   . ILE D  1 148 ? 4.147   40.460  61.326  1.00 24.70  ? 140 ILE D N   1 
ATOM   6170  C CA  . ILE D  1 148 ? 4.369   39.814  60.023  1.00 24.56  ? 140 ILE D CA  1 
ATOM   6171  C C   . ILE D  1 148 ? 5.538   40.444  59.251  1.00 28.92  ? 140 ILE D C   1 
ATOM   6172  O O   . ILE D  1 148 ? 5.500   41.629  58.912  1.00 29.96  ? 140 ILE D O   1 
ATOM   6173  C CB  . ILE D  1 148 ? 3.112   39.874  59.113  1.00 21.46  ? 140 ILE D CB  1 
ATOM   6174  C CG1 . ILE D  1 148 ? 2.031   38.923  59.612  1.00 21.14  ? 140 ILE D CG1 1 
ATOM   6175  C CG2 . ILE D  1 148 ? 3.470   39.506  57.672  1.00 19.36  ? 140 ILE D CG2 1 
ATOM   6176  C CD1 . ILE D  1 148 ? 0.882   38.736  58.628  1.00 25.72  ? 140 ILE D CD1 1 
ATOM   6177  N N   . GLY D  1 149 ? 6.565   39.652  58.957  1.00 27.62  ? 141 GLY D N   1 
ATOM   6178  C CA  . GLY D  1 149 ? 7.712   40.153  58.215  1.00 29.07  ? 141 GLY D CA  1 
ATOM   6179  C C   . GLY D  1 149 ? 8.229   39.154  57.201  1.00 24.15  ? 141 GLY D C   1 
ATOM   6180  O O   . GLY D  1 149 ? 7.602   38.123  56.975  1.00 22.82  ? 141 GLY D O   1 
ATOM   6181  N N   . SER D  1 150 ? 9.363   39.449  56.572  1.00 22.85  ? 142 SER D N   1 
ATOM   6182  C CA  . SER D  1 150 ? 9.979   38.452  55.706  1.00 17.40  ? 142 SER D CA  1 
ATOM   6183  C C   . SER D  1 150 ? 10.838  37.539  56.548  1.00 14.83  ? 142 SER D C   1 
ATOM   6184  O O   . SER D  1 150 ? 11.636  37.991  57.361  1.00 19.01  ? 142 SER D O   1 
ATOM   6185  C CB  . SER D  1 150 ? 10.821  39.082  54.577  1.00 19.66  ? 142 SER D CB  1 
ATOM   6186  O OG  . SER D  1 150 ? 11.604  38.091  53.890  1.00 15.75  ? 142 SER D OG  1 
ATOM   6187  N N   . TRP D  1 151 ? 10.685  36.246  56.326  1.00 14.40  ? 143 TRP D N   1 
ATOM   6188  C CA  . TRP D  1 151 ? 11.448  35.252  57.054  1.00 15.65  ? 143 TRP D CA  1 
ATOM   6189  C C   . TRP D  1 151 ? 12.947  35.216  56.696  1.00 18.20  ? 143 TRP D C   1 
ATOM   6190  O O   . TRP D  1 151 ? 13.787  35.122  57.573  1.00 22.41  ? 143 TRP D O   1 
ATOM   6191  C CB  . TRP D  1 151 ? 10.786  33.882  56.890  1.00 14.44  ? 143 TRP D CB  1 
ATOM   6192  C CG  . TRP D  1 151 ? 11.378  32.834  57.749  1.00 17.88  ? 143 TRP D CG  1 
ATOM   6193  C CD1 . TRP D  1 151 ? 11.977  31.687  57.339  1.00 16.19  ? 143 TRP D CD1 1 
ATOM   6194  C CD2 . TRP D  1 151 ? 11.444  32.836  59.176  1.00 23.55  ? 143 TRP D CD2 1 
ATOM   6195  N NE1 . TRP D  1 151 ? 12.406  30.967  58.419  1.00 19.95  ? 143 TRP D NE1 1 
ATOM   6196  C CE2 . TRP D  1 151 ? 12.096  31.653  59.563  1.00 27.67  ? 143 TRP D CE2 1 
ATOM   6197  C CE3 . TRP D  1 151 ? 11.018  33.723  60.166  1.00 26.02  ? 143 TRP D CE3 1 
ATOM   6198  C CZ2 . TRP D  1 151 ? 12.329  31.330  60.903  1.00 25.58  ? 143 TRP D CZ2 1 
ATOM   6199  C CZ3 . TRP D  1 151 ? 11.254  33.402  61.493  1.00 27.65  ? 143 TRP D CZ3 1 
ATOM   6200  C CH2 . TRP D  1 151 ? 11.904  32.219  61.847  1.00 22.18  ? 143 TRP D CH2 1 
ATOM   6201  N N   . THR D  1 152 ? 13.306  35.304  55.421  1.00 19.43  ? 144 THR D N   1 
ATOM   6202  C CA  . THR D  1 152 ? 14.714  35.106  55.082  1.00 16.22  ? 144 THR D CA  1 
ATOM   6203  C C   . THR D  1 152 ? 15.418  36.332  54.497  1.00 15.49  ? 144 THR D C   1 
ATOM   6204  O O   . THR D  1 152 ? 16.650  36.400  54.495  1.00 16.03  ? 144 THR D O   1 
ATOM   6205  C CB  . THR D  1 152 ? 14.922  33.848  54.192  1.00 14.64  ? 144 THR D CB  1 
ATOM   6206  O OG1 . THR D  1 152 ? 14.183  33.978  52.967  1.00 16.43  ? 144 THR D OG1 1 
ATOM   6207  C CG2 . THR D  1 152 ? 14.454  32.607  54.931  1.00 12.38  ? 144 THR D CG2 1 
ATOM   6208  N N   . HIS D  1 153 ? 14.647  37.310  54.034  1.00 14.97  ? 145 HIS D N   1 
ATOM   6209  C CA  . HIS D  1 153 ? 15.240  38.481  53.391  1.00 18.18  ? 145 HIS D CA  1 
ATOM   6210  C C   . HIS D  1 153 ? 15.325  39.685  54.338  1.00 24.42  ? 145 HIS D C   1 
ATOM   6211  O O   . HIS D  1 153 ? 14.304  40.136  54.873  1.00 21.81  ? 145 HIS D O   1 
ATOM   6212  C CB  . HIS D  1 153 ? 14.461  38.850  52.124  1.00 15.76  ? 145 HIS D CB  1 
ATOM   6213  C CG  . HIS D  1 153 ? 14.361  37.735  51.123  1.00 18.00  ? 145 HIS D CG  1 
ATOM   6214  N ND1 . HIS D  1 153 ? 13.277  36.883  51.057  1.00 18.12  ? 145 HIS D ND1 1 
ATOM   6215  C CD2 . HIS D  1 153 ? 15.206  37.341  50.141  1.00 19.65  ? 145 HIS D CD2 1 
ATOM   6216  C CE1 . HIS D  1 153 ? 13.461  36.012  50.084  1.00 17.59  ? 145 HIS D CE1 1 
ATOM   6217  N NE2 . HIS D  1 153 ? 14.620  36.272  49.506  1.00 22.58  ? 145 HIS D NE2 1 
ATOM   6218  N N   . HIS D  1 154 ? 16.541  40.195  54.551  1.00 24.37  ? 146 HIS D N   1 
ATOM   6219  C CA  . HIS D  1 154 ? 16.742  41.354  55.429  1.00 23.50  ? 146 HIS D CA  1 
ATOM   6220  C C   . HIS D  1 154 ? 16.345  42.677  54.745  1.00 26.74  ? 146 HIS D C   1 
ATOM   6221  O O   . HIS D  1 154 ? 15.890  42.673  53.595  1.00 25.25  ? 146 HIS D O   1 
ATOM   6222  C CB  . HIS D  1 154 ? 18.165  41.388  56.020  1.00 26.81  ? 146 HIS D CB  1 
ATOM   6223  C CG  . HIS D  1 154 ? 19.262  41.197  55.009  1.00 38.49  ? 146 HIS D CG  1 
ATOM   6224  N ND1 . HIS D  1 154 ? 19.558  42.132  54.036  1.00 34.40  ? 146 HIS D ND1 1 
ATOM   6225  C CD2 . HIS D  1 154 ? 20.147  40.184  54.834  1.00 36.62  ? 146 HIS D CD2 1 
ATOM   6226  C CE1 . HIS D  1 154 ? 20.570  41.700  53.302  1.00 31.56  ? 146 HIS D CE1 1 
ATOM   6227  N NE2 . HIS D  1 154 ? 20.945  40.520  53.764  1.00 36.76  ? 146 HIS D NE2 1 
ATOM   6228  N N   . SER D  1 155 ? 16.510  43.796  55.451  1.00 27.70  ? 147 SER D N   1 
ATOM   6229  C CA  . SER D  1 155 ? 15.900  45.076  55.055  1.00 25.89  ? 147 SER D CA  1 
ATOM   6230  C C   . SER D  1 155 ? 16.494  45.722  53.809  1.00 28.92  ? 147 SER D C   1 
ATOM   6231  O O   . SER D  1 155 ? 15.836  46.552  53.162  1.00 25.50  ? 147 SER D O   1 
ATOM   6232  C CB  . SER D  1 155 ? 15.929  46.081  56.210  1.00 29.74  ? 147 SER D CB  1 
ATOM   6233  O OG  . SER D  1 155 ? 17.260  46.384  56.598  1.00 33.23  ? 147 SER D OG  1 
ATOM   6234  N N   . ARG D  1 156 ? 17.736  45.364  53.485  1.00 28.96  ? 148 ARG D N   1 
ATOM   6235  C CA  . ARG D  1 156 ? 18.311  45.732  52.188  1.00 31.15  ? 148 ARG D CA  1 
ATOM   6236  C C   . ARG D  1 156 ? 17.562  45.039  51.045  1.00 26.23  ? 148 ARG D C   1 
ATOM   6237  O O   . ARG D  1 156 ? 17.452  45.581  49.958  1.00 28.16  ? 148 ARG D O   1 
ATOM   6238  C CB  . ARG D  1 156 ? 19.802  45.377  52.118  1.00 36.92  ? 148 ARG D CB  1 
ATOM   6239  C CG  . ARG D  1 156 ? 20.665  46.120  53.121  1.00 37.98  ? 148 ARG D CG  1 
ATOM   6240  C CD  . ARG D  1 156 ? 22.143  45.837  52.910  1.00 43.06  ? 148 ARG D CD  1 
ATOM   6241  N NE  . ARG D  1 156 ? 22.960  46.520  53.910  1.00 56.33  ? 148 ARG D NE  1 
ATOM   6242  C CZ  . ARG D  1 156 ? 23.243  47.823  53.891  1.00 64.57  ? 148 ARG D CZ  1 
ATOM   6243  N NH1 . ARG D  1 156 ? 22.777  48.594  52.914  1.00 66.45  ? 148 ARG D NH1 1 
ATOM   6244  N NH2 . ARG D  1 156 ? 23.993  48.360  54.849  1.00 58.99  ? 148 ARG D NH2 1 
ATOM   6245  N N   . GLU D  1 157 ? 17.038  43.844  51.312  1.00 27.25  ? 149 GLU D N   1 
ATOM   6246  C CA  . GLU D  1 157 ? 16.389  43.019  50.301  1.00 20.77  ? 149 GLU D CA  1 
ATOM   6247  C C   . GLU D  1 157 ? 14.886  43.284  50.192  1.00 22.32  ? 149 GLU D C   1 
ATOM   6248  O O   . GLU D  1 157 ? 14.370  43.585  49.113  1.00 22.33  ? 149 GLU D O   1 
ATOM   6249  C CB  . GLU D  1 157 ? 16.675  41.539  50.591  1.00 21.50  ? 149 GLU D CB  1 
ATOM   6250  C CG  . GLU D  1 157 ? 18.172  41.211  50.529  1.00 26.20  ? 149 GLU D CG  1 
ATOM   6251  C CD  . GLU D  1 157 ? 18.533  39.779  50.916  1.00 25.33  ? 149 GLU D CD  1 
ATOM   6252  O OE1 . GLU D  1 157 ? 17.671  39.039  51.421  1.00 27.27  ? 149 GLU D OE1 1 
ATOM   6253  O OE2 . GLU D  1 157 ? 19.703  39.390  50.709  1.00 23.21  ? 149 GLU D OE2 1 
ATOM   6254  N N   . ILE D  1 158 ? 14.180  43.182  51.310  1.00 23.25  ? 150 ILE D N   1 
ATOM   6255  C CA  . ILE D  1 158 ? 12.746  43.449  51.305  1.00 21.73  ? 150 ILE D CA  1 
ATOM   6256  C C   . ILE D  1 158 ? 12.337  44.399  52.419  1.00 19.51  ? 150 ILE D C   1 
ATOM   6257  O O   . ILE D  1 158 ? 12.723  44.237  53.579  1.00 20.59  ? 150 ILE D O   1 
ATOM   6258  C CB  . ILE D  1 158 ? 11.902  42.147  51.429  1.00 20.37  ? 150 ILE D CB  1 
ATOM   6259  C CG1 . ILE D  1 158 ? 12.271  41.146  50.333  1.00 18.22  ? 150 ILE D CG1 1 
ATOM   6260  C CG2 . ILE D  1 158 ? 10.431  42.456  51.319  1.00 15.64  ? 150 ILE D CG2 1 
ATOM   6261  C CD1 . ILE D  1 158 ? 11.490  39.857  50.416  1.00 11.41  ? 150 ILE D CD1 1 
ATOM   6262  N N   . SER D  1 159 ? 11.542  45.393  52.060  1.00 20.87  ? 151 SER D N   1 
ATOM   6263  C CA  . SER D  1 159 ? 10.897  46.226  53.064  1.00 27.46  ? 151 SER D CA  1 
ATOM   6264  C C   . SER D  1 159 ? 9.398   45.899  53.177  1.00 23.27  ? 151 SER D C   1 
ATOM   6265  O O   . SER D  1 159 ? 8.674   45.834  52.177  1.00 16.85  ? 151 SER D O   1 
ATOM   6266  C CB  . SER D  1 159 ? 11.119  47.706  52.758  1.00 25.53  ? 151 SER D CB  1 
ATOM   6267  O OG  . SER D  1 159 ? 10.357  48.101  51.642  1.00 31.80  ? 151 SER D OG  1 
ATOM   6268  N N   . VAL D  1 160 ? 8.955   45.675  54.408  1.00 26.17  ? 152 VAL D N   1 
ATOM   6269  C CA  . VAL D  1 160 ? 7.560   45.380  54.701  1.00 24.55  ? 152 VAL D CA  1 
ATOM   6270  C C   . VAL D  1 160 ? 6.903   46.616  55.277  1.00 22.96  ? 152 VAL D C   1 
ATOM   6271  O O   . VAL D  1 160 ? 7.368   47.146  56.270  1.00 33.12  ? 152 VAL D O   1 
ATOM   6272  C CB  . VAL D  1 160 ? 7.456   44.284  55.755  1.00 28.66  ? 152 VAL D CB  1 
ATOM   6273  C CG1 . VAL D  1 160 ? 6.011   43.954  56.007  1.00 29.02  ? 152 VAL D CG1 1 
ATOM   6274  C CG2 . VAL D  1 160 ? 8.237   43.043  55.324  1.00 26.16  ? 152 VAL D CG2 1 
ATOM   6275  N N   . ASP D  1 161 ? 5.824   47.083  54.665  1.00 25.01  ? 153 ASP D N   1 
ATOM   6276  C CA  . ASP D  1 161 ? 5.170   48.322  55.099  1.00 26.13  ? 153 ASP D CA  1 
ATOM   6277  C C   . ASP D  1 161 ? 3.674   48.140  55.310  1.00 26.97  ? 153 ASP D C   1 
ATOM   6278  O O   . ASP D  1 161 ? 3.070   47.252  54.712  1.00 27.25  ? 153 ASP D O   1 
ATOM   6279  C CB  . ASP D  1 161 ? 5.375   49.418  54.056  1.00 28.20  ? 153 ASP D CB  1 
ATOM   6280  C CG  . ASP D  1 161 ? 6.729   50.076  54.160  1.00 36.43  ? 153 ASP D CG  1 
ATOM   6281  O OD1 . ASP D  1 161 ? 7.687   49.396  54.592  1.00 39.37  ? 153 ASP D OD1 1 
ATOM   6282  O OD2 . ASP D  1 161 ? 6.830   51.277  53.814  1.00 41.72  ? 153 ASP D OD2 1 
ATOM   6283  N N   . PRO D  1 162 ? 3.065   48.977  56.167  1.00 25.91  ? 154 PRO D N   1 
ATOM   6284  C CA  . PRO D  1 162 ? 1.602   48.953  56.252  1.00 21.26  ? 154 PRO D CA  1 
ATOM   6285  C C   . PRO D  1 162 ? 1.013   49.662  55.047  1.00 24.42  ? 154 PRO D C   1 
ATOM   6286  O O   . PRO D  1 162 ? 1.732   50.399  54.378  1.00 28.13  ? 154 PRO D O   1 
ATOM   6287  C CB  . PRO D  1 162 ? 1.307   49.730  57.533  1.00 19.15  ? 154 PRO D CB  1 
ATOM   6288  C CG  . PRO D  1 162 ? 2.501   50.558  57.767  1.00 23.41  ? 154 PRO D CG  1 
ATOM   6289  C CD  . PRO D  1 162 ? 3.674   49.831  57.201  1.00 25.96  ? 154 PRO D CD  1 
ATOM   6290  N N   . THR D  1 163 ? -0.264  49.442  54.765  1.00 24.99  ? 155 THR D N   1 
ATOM   6291  C CA  . THR D  1 163 ? -0.884  50.026  53.585  1.00 23.89  ? 155 THR D CA  1 
ATOM   6292  C C   . THR D  1 163 ? -1.497  51.398  53.865  1.00 31.03  ? 155 THR D C   1 
ATOM   6293  O O   . THR D  1 163 ? -1.731  51.758  55.019  1.00 32.84  ? 155 THR D O   1 
ATOM   6294  C CB  . THR D  1 163 ? -1.930  49.073  52.973  1.00 24.88  ? 155 THR D CB  1 
ATOM   6295  O OG1 . THR D  1 163 ? -3.089  48.990  53.817  1.00 27.71  ? 155 THR D OG1 1 
ATOM   6296  C CG2 . THR D  1 163 ? -1.326  47.700  52.811  1.00 24.20  ? 155 THR D CG2 1 
ATOM   6297  N N   . THR D  1 164 ? -1.749  52.164  52.805  1.00 34.54  ? 156 THR D N   1 
ATOM   6298  C CA  . THR D  1 164 ? -2.294  53.518  52.954  1.00 38.22  ? 156 THR D CA  1 
ATOM   6299  C C   . THR D  1 164 ? -3.703  53.561  53.584  1.00 34.32  ? 156 THR D C   1 
ATOM   6300  O O   . THR D  1 164 ? -4.088  54.559  54.199  1.00 32.58  ? 156 THR D O   1 
ATOM   6301  C CB  . THR D  1 164 ? -2.257  54.311  51.618  1.00 34.36  ? 156 THR D CB  1 
ATOM   6302  O OG1 . THR D  1 164 ? -3.077  53.666  50.631  1.00 34.33  ? 156 THR D OG1 1 
ATOM   6303  C CG2 . THR D  1 164 ? -0.828  54.408  51.114  1.00 32.47  ? 156 THR D CG2 1 
ATOM   6304  N N   . GLU D  1 165 ? -4.462  52.475  53.477  1.00 35.38  ? 157 GLU D N   1 
ATOM   6305  C CA  . GLU D  1 165 ? -5.769  52.450  54.130  1.00 31.81  ? 157 GLU D CA  1 
ATOM   6306  C C   . GLU D  1 165 ? -5.808  51.506  55.333  1.00 32.72  ? 157 GLU D C   1 
ATOM   6307  O O   . GLU D  1 165 ? -5.656  50.293  55.191  1.00 41.37  ? 157 GLU D O   1 
ATOM   6308  C CB  . GLU D  1 165 ? -6.860  52.065  53.128  1.00 28.05  ? 157 GLU D CB  1 
ATOM   6309  C CG  . GLU D  1 165 ? -8.174  52.802  53.328  1.00 33.77  ? 157 GLU D CG  1 
ATOM   6310  C CD  . GLU D  1 165 ? -9.346  52.091  52.680  1.00 41.67  ? 157 GLU D CD  1 
ATOM   6311  O OE1 . GLU D  1 165 ? -9.379  52.011  51.434  1.00 51.79  ? 157 GLU D OE1 1 
ATOM   6312  O OE2 . GLU D  1 165 ? -10.233 51.612  53.416  1.00 30.31  ? 157 GLU D OE2 1 
ATOM   6313  N N   . ASN D  1 166 ? -5.775  52.134  56.505  1.00 31.70  ? 158 ASN D N   1 
ATOM   6314  C CA  . ASN D  1 166 ? -5.476  51.468  57.763  1.00 35.43  ? 158 ASN D CA  1 
ATOM   6315  C C   . ASN D  1 166 ? -6.596  51.449  58.791  1.00 30.94  ? 158 ASN D C   1 
ATOM   6316  O O   . ASN D  1 166 ? -6.362  51.096  59.947  1.00 43.10  ? 158 ASN D O   1 
ATOM   6317  C CB  . ASN D  1 166 ? -4.212  52.067  58.390  1.00 31.75  ? 158 ASN D CB  1 
ATOM   6318  C CG  . ASN D  1 166 ? -3.202  51.009  58.787  1.00 33.14  ? 158 ASN D CG  1 
ATOM   6319  O OD1 . ASN D  1 166 ? -2.335  50.634  57.997  1.00 33.22  ? 158 ASN D OD1 1 
ATOM   6320  N ND2 . ASN D  1 166 ? -3.308  50.521  60.017  1.00 34.40  ? 158 ASN D ND2 1 
ATOM   6321  N N   . SER D  1 167 ? -7.784  51.866  58.373  1.00 24.80  ? 159 SER D N   1 
ATOM   6322  C CA  . SER D  1 167 ? -8.973  51.711  59.184  1.00 37.54  ? 159 SER D CA  1 
ATOM   6323  C C   . SER D  1 167 ? -9.166  50.215  59.335  1.00 40.63  ? 159 SER D C   1 
ATOM   6324  O O   . SER D  1 167 ? -9.551  49.721  60.395  1.00 32.43  ? 159 SER D O   1 
ATOM   6325  C CB  . SER D  1 167 ? -10.184 52.339  58.497  1.00 45.24  ? 159 SER D CB  1 
ATOM   6326  O OG  . SER D  1 167 ? -9.789  53.137  57.395  1.00 42.29  ? 159 SER D OG  1 
ATOM   6327  N N   . ASP D  1 168 ? -8.869  49.514  58.244  1.00 41.76  ? 160 ASP D N   1 
ATOM   6328  C CA  . ASP D  1 168 ? -9.113  48.083  58.081  1.00 26.50  ? 160 ASP D CA  1 
ATOM   6329  C C   . ASP D  1 168 ? -8.184  47.146  58.875  1.00 25.43  ? 160 ASP D C   1 
ATOM   6330  O O   . ASP D  1 168 ? -7.092  47.549  59.275  1.00 42.27  ? 160 ASP D O   1 
ATOM   6331  C CB  . ASP D  1 168 ? -9.076  47.708  56.596  1.00 34.63  ? 160 ASP D CB  1 
ATOM   6332  C CG  . ASP D  1 168 ? -9.705  48.768  55.712  1.00 33.91  ? 160 ASP D CG  1 
ATOM   6333  O OD1 . ASP D  1 168 ? -10.895 48.622  55.362  1.00 33.66  ? 160 ASP D OD1 1 
ATOM   6334  O OD2 . ASP D  1 168 ? -9.009  49.746  55.368  1.00 26.63  ? 160 ASP D OD2 1 
ATOM   6335  N N   . ASP D  1 169 ? -8.707  45.972  59.195  1.00 20.79  ? 161 ASP D N   1 
ATOM   6336  C CA  . ASP D  1 169 ? -10.099 45.713  58.872  1.00 21.19  ? 161 ASP D CA  1 
ATOM   6337  C C   . ASP D  1 169 ? -10.965 45.802  60.127  1.00 24.31  ? 161 ASP D C   1 
ATOM   6338  O O   . ASP D  1 169 ? -10.798 45.021  61.064  1.00 19.41  ? 161 ASP D O   1 
ATOM   6339  C CB  . ASP D  1 169 ? -10.253 44.337  58.222  1.00 19.37  ? 161 ASP D CB  1 
ATOM   6340  C CG  . ASP D  1 169 ? -11.696 44.002  57.901  1.00 28.35  ? 161 ASP D CG  1 
ATOM   6341  O OD1 . ASP D  1 169 ? -12.574 44.859  58.138  1.00 27.82  ? 161 ASP D OD1 1 
ATOM   6342  O OD2 . ASP D  1 169 ? -11.953 42.883  57.411  1.00 30.75  ? 161 ASP D OD2 1 
ATOM   6343  N N   . SER D  1 170 ? -11.890 46.759  60.134  1.00 20.43  ? 162 SER D N   1 
ATOM   6344  C CA  . SER D  1 170 ? -12.939 46.811  61.146  1.00 14.14  ? 162 SER D CA  1 
ATOM   6345  C C   . SER D  1 170 ? -14.318 46.415  60.599  1.00 18.13  ? 162 SER D C   1 
ATOM   6346  O O   . SER D  1 170 ? -15.042 45.634  61.216  1.00 15.24  ? 162 SER D O   1 
ATOM   6347  C CB  . SER D  1 170 ? -13.006 48.205  61.774  1.00 15.85  ? 162 SER D CB  1 
ATOM   6348  O OG  . SER D  1 170 ? -13.100 49.209  60.778  1.00 25.84  ? 162 SER D OG  1 
ATOM   6349  N N   . GLU D  1 171 ? -14.672 46.974  59.443  1.00 14.85  ? 163 GLU D N   1 
ATOM   6350  C CA  . GLU D  1 171 ? -16.018 46.843  58.871  1.00 19.34  ? 163 GLU D CA  1 
ATOM   6351  C C   . GLU D  1 171 ? -16.477 45.439  58.455  1.00 21.60  ? 163 GLU D C   1 
ATOM   6352  O O   . GLU D  1 171 ? -17.622 45.059  58.701  1.00 20.87  ? 163 GLU D O   1 
ATOM   6353  C CB  . GLU D  1 171 ? -16.180 47.804  57.688  1.00 28.98  ? 163 GLU D CB  1 
ATOM   6354  C CG  . GLU D  1 171 ? -15.175 47.586  56.569  1.00 27.00  ? 163 GLU D CG  1 
ATOM   6355  C CD  . GLU D  1 171 ? -15.647 48.150  55.244  1.00 41.20  ? 163 GLU D CD  1 
ATOM   6356  O OE1 . GLU D  1 171 ? -15.178 47.669  54.191  1.00 45.25  ? 163 GLU D OE1 1 
ATOM   6357  O OE2 . GLU D  1 171 ? -16.488 49.073  55.254  1.00 43.73  ? 163 GLU D OE2 1 
ATOM   6358  N N   . TYR D  1 172 ? -15.589 44.679  57.823  1.00 21.51  ? 164 TYR D N   1 
ATOM   6359  C CA  . TYR D  1 172 ? -15.936 43.362  57.288  1.00 18.45  ? 164 TYR D CA  1 
ATOM   6360  C C   . TYR D  1 172 ? -16.279 42.375  58.396  1.00 15.15  ? 164 TYR D C   1 
ATOM   6361  O O   . TYR D  1 172 ? -17.211 41.579  58.282  1.00 16.98  ? 164 TYR D O   1 
ATOM   6362  C CB  . TYR D  1 172 ? -14.791 42.814  56.432  1.00 23.74  ? 164 TYR D CB  1 
ATOM   6363  C CG  . TYR D  1 172 ? -14.356 43.745  55.323  1.00 23.54  ? 164 TYR D CG  1 
ATOM   6364  C CD1 . TYR D  1 172 ? -15.206 44.043  54.266  1.00 21.28  ? 164 TYR D CD1 1 
ATOM   6365  C CD2 . TYR D  1 172 ? -13.095 44.327  55.333  1.00 29.01  ? 164 TYR D CD2 1 
ATOM   6366  C CE1 . TYR D  1 172 ? -14.812 44.893  53.251  1.00 28.07  ? 164 TYR D CE1 1 
ATOM   6367  C CE2 . TYR D  1 172 ? -12.692 45.178  54.322  1.00 26.33  ? 164 TYR D CE2 1 
ATOM   6368  C CZ  . TYR D  1 172 ? -13.555 45.458  53.283  1.00 34.41  ? 164 TYR D CZ  1 
ATOM   6369  O OH  . TYR D  1 172 ? -13.158 46.305  52.274  1.00 41.00  ? 164 TYR D OH  1 
ATOM   6370  N N   . PHE D  1 173 ? -15.568 42.483  59.512  1.00 17.64  ? 165 PHE D N   1 
ATOM   6371  C CA  . PHE D  1 173 ? -15.522 41.405  60.482  1.00 16.58  ? 165 PHE D CA  1 
ATOM   6372  C C   . PHE D  1 173 ? -16.940 41.038  60.873  1.00 16.72  ? 165 PHE D C   1 
ATOM   6373  O O   . PHE D  1 173 ? -17.793 41.902  61.073  1.00 16.14  ? 165 PHE D O   1 
ATOM   6374  C CB  . PHE D  1 173 ? -14.726 41.827  61.718  1.00 16.85  ? 165 PHE D CB  1 
ATOM   6375  C CG  . PHE D  1 173 ? -14.755 40.818  62.831  1.00 14.84  ? 165 PHE D CG  1 
ATOM   6376  C CD1 . PHE D  1 173 ? -13.709 39.928  63.004  1.00 14.50  ? 165 PHE D CD1 1 
ATOM   6377  C CD2 . PHE D  1 173 ? -15.829 40.761  63.704  1.00 13.98  ? 165 PHE D CD2 1 
ATOM   6378  C CE1 . PHE D  1 173 ? -13.732 38.999  64.027  1.00 18.12  ? 165 PHE D CE1 1 
ATOM   6379  C CE2 . PHE D  1 173 ? -15.859 39.834  64.729  1.00 15.48  ? 165 PHE D CE2 1 
ATOM   6380  C CZ  . PHE D  1 173 ? -14.809 38.952  64.891  1.00 16.45  ? 165 PHE D CZ  1 
ATOM   6381  N N   . SER D  1 174 ? -17.183 39.735  60.957  1.00 16.40  ? 166 SER D N   1 
ATOM   6382  C CA  . SER D  1 174 ? -18.534 39.209  61.018  1.00 14.79  ? 166 SER D CA  1 
ATOM   6383  C C   . SER D  1 174 ? -19.286 39.714  62.234  1.00 13.67  ? 166 SER D C   1 
ATOM   6384  O O   . SER D  1 174 ? -18.749 39.781  63.340  1.00 17.19  ? 166 SER D O   1 
ATOM   6385  C CB  . SER D  1 174 ? -18.511 37.678  61.016  1.00 11.38  ? 166 SER D CB  1 
ATOM   6386  O OG  . SER D  1 174 ? -19.780 37.149  61.360  1.00 11.81  ? 166 SER D OG  1 
ATOM   6387  N N   . GLN D  1 175 ? -20.544 40.068  62.007  1.00 13.23  ? 167 GLN D N   1 
ATOM   6388  C CA  . GLN D  1 175 ? -21.412 40.555  63.059  1.00 17.58  ? 167 GLN D CA  1 
ATOM   6389  C C   . GLN D  1 175 ? -21.852 39.418  63.977  1.00 18.98  ? 167 GLN D C   1 
ATOM   6390  O O   . GLN D  1 175 ? -22.543 39.652  64.962  1.00 19.19  ? 167 GLN D O   1 
ATOM   6391  C CB  . GLN D  1 175 ? -22.625 41.254  62.472  1.00 16.29  ? 167 GLN D CB  1 
ATOM   6392  C CG  . GLN D  1 175 ? -23.575 40.324  61.791  1.00 18.98  ? 167 GLN D CG  1 
ATOM   6393  C CD  . GLN D  1 175 ? -24.274 40.998  60.639  1.00 30.81  ? 167 GLN D CD  1 
ATOM   6394  O OE1 . GLN D  1 175 ? -25.346 41.575  60.808  1.00 37.02  ? 167 GLN D OE1 1 
ATOM   6395  N NE2 . GLN D  1 175 ? -23.663 40.940  59.453  1.00 36.57  ? 167 GLN D NE2 1 
ATOM   6396  N N   . TYR D  1 176 ? -21.428 38.197  63.667  1.00 14.82  ? 168 TYR D N   1 
ATOM   6397  C CA  . TYR D  1 176 ? -21.907 37.023  64.379  1.00 15.43  ? 168 TYR D CA  1 
ATOM   6398  C C   . TYR D  1 176 ? -20.870 36.464  65.343  1.00 16.69  ? 168 TYR D C   1 
ATOM   6399  O O   . TYR D  1 176 ? -21.172 35.615  66.194  1.00 14.41  ? 168 TYR D O   1 
ATOM   6400  C CB  . TYR D  1 176 ? -22.389 35.972  63.383  1.00 15.51  ? 168 TYR D CB  1 
ATOM   6401  C CG  . TYR D  1 176 ? -23.532 36.491  62.554  1.00 18.99  ? 168 TYR D CG  1 
ATOM   6402  C CD1 . TYR D  1 176 ? -24.677 36.962  63.175  1.00 16.81  ? 168 TYR D CD1 1 
ATOM   6403  C CD2 . TYR D  1 176 ? -23.472 36.535  61.155  1.00 17.84  ? 168 TYR D CD2 1 
ATOM   6404  C CE1 . TYR D  1 176 ? -25.735 37.448  62.456  1.00 17.02  ? 168 TYR D CE1 1 
ATOM   6405  C CE2 . TYR D  1 176 ? -24.543 37.027  60.417  1.00 16.03  ? 168 TYR D CE2 1 
ATOM   6406  C CZ  . TYR D  1 176 ? -25.672 37.483  61.091  1.00 18.90  ? 168 TYR D CZ  1 
ATOM   6407  O OH  . TYR D  1 176 ? -26.768 37.973  60.429  1.00 26.44  ? 168 TYR D OH  1 
ATOM   6408  N N   . SER D  1 177 ? -19.647 36.959  65.214  1.00 15.51  ? 169 SER D N   1 
ATOM   6409  C CA  . SER D  1 177 ? -18.591 36.617  66.150  1.00 14.99  ? 169 SER D CA  1 
ATOM   6410  C C   . SER D  1 177 ? -19.047 36.893  67.589  1.00 17.28  ? 169 SER D C   1 
ATOM   6411  O O   . SER D  1 177 ? -19.822 37.809  67.834  1.00 18.71  ? 169 SER D O   1 
ATOM   6412  C CB  . SER D  1 177 ? -17.343 37.435  65.819  1.00 13.22  ? 169 SER D CB  1 
ATOM   6413  O OG  . SER D  1 177 ? -16.276 37.154  66.716  1.00 18.35  ? 169 SER D OG  1 
ATOM   6414  N N   . ARG D  1 178 ? -18.574 36.091  68.537  1.00 23.58  ? 170 ARG D N   1 
ATOM   6415  C CA  . ARG D  1 178 ? -18.807 36.366  69.952  1.00 19.68  ? 170 ARG D CA  1 
ATOM   6416  C C   . ARG D  1 178 ? -18.072 37.638  70.346  1.00 19.10  ? 170 ARG D C   1 
ATOM   6417  O O   . ARG D  1 178 ? -18.393 38.262  71.345  1.00 24.81  ? 170 ARG D O   1 
ATOM   6418  C CB  . ARG D  1 178 ? -18.286 35.225  70.841  1.00 21.82  ? 170 ARG D CB  1 
ATOM   6419  C CG  . ARG D  1 178 ? -19.128 33.961  70.893  1.00 18.90  ? 170 ARG D CG  1 
ATOM   6420  C CD  . ARG D  1 178 ? -18.701 33.075  72.073  1.00 23.61  ? 170 ARG D CD  1 
ATOM   6421  N NE  . ARG D  1 178 ? -19.113 33.655  73.353  1.00 38.79  ? 170 ARG D NE  1 
ATOM   6422  C CZ  . ARG D  1 178 ? -19.165 33.003  74.517  1.00 35.53  ? 170 ARG D CZ  1 
ATOM   6423  N NH1 . ARG D  1 178 ? -18.828 31.725  74.596  1.00 34.10  ? 170 ARG D NH1 1 
ATOM   6424  N NH2 . ARG D  1 178 ? -19.563 33.638  75.610  1.00 32.78  ? 170 ARG D NH2 1 
ATOM   6425  N N   . PHE D  1 179 ? -17.062 38.012  69.578  1.00 18.21  ? 171 PHE D N   1 
ATOM   6426  C CA  . PHE D  1 179 ? -16.214 39.137  69.962  1.00 19.04  ? 171 PHE D CA  1 
ATOM   6427  C C   . PHE D  1 179 ? -16.539 40.377  69.134  1.00 14.32  ? 171 PHE D C   1 
ATOM   6428  O O   . PHE D  1 179 ? -17.281 40.303  68.166  1.00 16.33  ? 171 PHE D O   1 
ATOM   6429  C CB  . PHE D  1 179 ? -14.736 38.742  69.856  1.00 15.46  ? 171 PHE D CB  1 
ATOM   6430  C CG  . PHE D  1 179 ? -14.411 37.482  70.594  1.00 20.31  ? 171 PHE D CG  1 
ATOM   6431  C CD1 . PHE D  1 179 ? -14.694 36.239  70.035  1.00 24.39  ? 171 PHE D CD1 1 
ATOM   6432  C CD2 . PHE D  1 179 ? -13.865 37.528  71.864  1.00 22.43  ? 171 PHE D CD2 1 
ATOM   6433  C CE1 . PHE D  1 179 ? -14.427 35.062  70.716  1.00 18.70  ? 171 PHE D CE1 1 
ATOM   6434  C CE2 . PHE D  1 179 ? -13.593 36.356  72.549  1.00 24.35  ? 171 PHE D CE2 1 
ATOM   6435  C CZ  . PHE D  1 179 ? -13.870 35.116  71.965  1.00 20.34  ? 171 PHE D CZ  1 
ATOM   6436  N N   . GLU D  1 180 ? -16.023 41.524  69.543  1.00 13.37  ? 172 GLU D N   1 
ATOM   6437  C CA  . GLU D  1 180 ? -16.176 42.736  68.750  1.00 17.15  ? 172 GLU D CA  1 
ATOM   6438  C C   . GLU D  1 180 ? -14.849 43.454  68.793  1.00 16.69  ? 172 GLU D C   1 
ATOM   6439  O O   . GLU D  1 180 ? -14.077 43.270  69.729  1.00 15.90  ? 172 GLU D O   1 
ATOM   6440  C CB  . GLU D  1 180 ? -17.316 43.621  69.271  1.00 18.19  ? 172 GLU D CB  1 
ATOM   6441  C CG  . GLU D  1 180 ? -17.158 44.106  70.710  1.00 24.62  ? 172 GLU D CG  1 
ATOM   6442  C CD  . GLU D  1 180 ? -18.456 44.687  71.283  1.00 38.32  ? 172 GLU D CD  1 
ATOM   6443  O OE1 . GLU D  1 180 ? -19.405 44.923  70.498  1.00 41.28  ? 172 GLU D OE1 1 
ATOM   6444  O OE2 . GLU D  1 180 ? -18.532 44.899  72.518  1.00 41.59  ? 172 GLU D OE2 1 
ATOM   6445  N N   . ILE D  1 181 ? -14.535 44.335  67.842  1.00 18.65  ? 173 ILE D N   1 
ATOM   6446  C CA  . ILE D  1 181 ? -13.207 44.990  67.895  1.00 18.53  ? 173 ILE D CA  1 
ATOM   6447  C C   . ILE D  1 181 ? -13.155 46.496  68.238  1.00 15.10  ? 173 ILE D C   1 
ATOM   6448  O O   . ILE D  1 181 ? -13.687 47.327  67.503  1.00 21.03  ? 173 ILE D O   1 
ATOM   6449  C CB  . ILE D  1 181 ? -12.426 44.765  66.584  1.00 17.16  ? 173 ILE D CB  1 
ATOM   6450  C CG1 . ILE D  1 181 ? -12.421 43.280  66.214  1.00 12.71  ? 173 ILE D CG1 1 
ATOM   6451  C CG2 . ILE D  1 181 ? -11.005 45.292  66.713  1.00 20.16  ? 173 ILE D CG2 1 
ATOM   6452  C CD1 . ILE D  1 181 ? -11.889 42.999  64.826  1.00 20.09  ? 173 ILE D CD1 1 
ATOM   6453  N N   . LEU D  1 182 ? -12.529 46.831  69.372  1.00 15.46  ? 174 LEU D N   1 
ATOM   6454  C CA  . LEU D  1 182 ? -12.320 48.230  69.809  1.00 22.28  ? 174 LEU D CA  1 
ATOM   6455  C C   . LEU D  1 182 ? -11.373 49.161  69.005  1.00 21.66  ? 174 LEU D C   1 
ATOM   6456  O O   . LEU D  1 182 ? -11.722 50.310  68.734  1.00 24.44  ? 174 LEU D O   1 
ATOM   6457  C CB  . LEU D  1 182 ? -11.918 48.256  71.288  1.00 17.91  ? 174 LEU D CB  1 
ATOM   6458  C CG  . LEU D  1 182 ? -12.510 47.156  72.171  1.00 16.12  ? 174 LEU D CG  1 
ATOM   6459  C CD1 . LEU D  1 182 ? -11.824 47.127  73.528  1.00 24.77  ? 174 LEU D CD1 1 
ATOM   6460  C CD2 . LEU D  1 182 ? -14.011 47.343  72.329  1.00 16.32  ? 174 LEU D CD2 1 
ATOM   6461  N N   . ASP D  1 183 ? -10.193 48.665  68.628  1.00 22.65  ? 175 ASP D N   1 
ATOM   6462  C CA  . ASP D  1 183 ? -9.236  49.407  67.802  1.00 28.34  ? 175 ASP D CA  1 
ATOM   6463  C C   . ASP D  1 183 ? -8.338  48.457  66.996  1.00 26.74  ? 175 ASP D C   1 
ATOM   6464  O O   . ASP D  1 183 ? -8.034  47.354  67.441  1.00 28.01  ? 175 ASP D O   1 
ATOM   6465  C CB  . ASP D  1 183 ? -8.330  50.283  68.675  1.00 24.54  ? 175 ASP D CB  1 
ATOM   6466  C CG  . ASP D  1 183 ? -9.079  51.410  69.353  1.00 38.05  ? 175 ASP D CG  1 
ATOM   6467  O OD1 . ASP D  1 183 ? -9.246  51.365  70.594  1.00 40.60  ? 175 ASP D OD1 1 
ATOM   6468  O OD2 . ASP D  1 183 ? -9.503  52.350  68.644  1.00 46.17  ? 175 ASP D OD2 1 
ATOM   6469  N N   . VAL D  1 184 ? -7.902  48.884  65.817  1.00 22.41  ? 176 VAL D N   1 
ATOM   6470  C CA  . VAL D  1 184 ? -6.799  48.199  65.161  1.00 18.88  ? 176 VAL D CA  1 
ATOM   6471  C C   . VAL D  1 184 ? -5.772  49.228  64.731  1.00 20.82  ? 176 VAL D C   1 
ATOM   6472  O O   . VAL D  1 184 ? -6.127  50.228  64.104  1.00 24.03  ? 176 VAL D O   1 
ATOM   6473  C CB  . VAL D  1 184 ? -7.232  47.386  63.907  1.00 22.90  ? 176 VAL D CB  1 
ATOM   6474  C CG1 . VAL D  1 184 ? -6.050  46.619  63.355  1.00 23.83  ? 176 VAL D CG1 1 
ATOM   6475  C CG2 . VAL D  1 184 ? -8.337  46.414  64.223  1.00 20.17  ? 176 VAL D CG2 1 
ATOM   6476  N N   . THR D  1 185 ? -4.503  48.989  65.066  1.00 19.42  ? 177 THR D N   1 
ATOM   6477  C CA  . THR D  1 185 ? -3.408  49.795  64.527  1.00 20.86  ? 177 THR D CA  1 
ATOM   6478  C C   . THR D  1 185 ? -2.350  48.918  63.860  1.00 22.23  ? 177 THR D C   1 
ATOM   6479  O O   . THR D  1 185 ? -2.092  47.801  64.300  1.00 21.21  ? 177 THR D O   1 
ATOM   6480  C CB  . THR D  1 185 ? -2.724  50.687  65.600  1.00 22.75  ? 177 THR D CB  1 
ATOM   6481  O OG1 . THR D  1 185 ? -1.817  49.903  66.385  1.00 21.81  ? 177 THR D OG1 1 
ATOM   6482  C CG2 . THR D  1 185 ? -3.758  51.366  66.492  1.00 18.75  ? 177 THR D CG2 1 
ATOM   6483  N N   . GLN D  1 186 ? -1.741  49.434  62.792  1.00 27.39  ? 178 GLN D N   1 
ATOM   6484  C CA  . GLN D  1 186 ? -0.725  48.698  62.039  1.00 18.20  ? 178 GLN D CA  1 
ATOM   6485  C C   . GLN D  1 186 ? 0.464   49.604  61.759  1.00 23.20  ? 178 GLN D C   1 
ATOM   6486  O O   . GLN D  1 186 ? 0.465   50.402  60.822  1.00 24.28  ? 178 GLN D O   1 
ATOM   6487  C CB  . GLN D  1 186 ? -1.317  48.104  60.763  1.00 16.40  ? 178 GLN D CB  1 
ATOM   6488  C CG  . GLN D  1 186 ? -2.292  46.981  61.072  1.00 20.28  ? 178 GLN D CG  1 
ATOM   6489  C CD  . GLN D  1 186 ? -2.941  46.340  59.861  1.00 21.74  ? 178 GLN D CD  1 
ATOM   6490  O OE1 . GLN D  1 186 ? -2.319  46.180  58.799  1.00 24.90  ? 178 GLN D OE1 1 
ATOM   6491  N NE2 . GLN D  1 186 ? -4.212  45.971  60.012  1.00 16.67  ? 178 GLN D NE2 1 
ATOM   6492  N N   . LYS D  1 187 ? 1.465   49.471  62.618  1.00 25.56  ? 179 LYS D N   1 
ATOM   6493  C CA  . LYS D  1 187 ? 2.626   50.334  62.655  1.00 27.45  ? 179 LYS D CA  1 
ATOM   6494  C C   . LYS D  1 187 ? 3.786   49.584  62.020  1.00 37.29  ? 179 LYS D C   1 
ATOM   6495  O O   . LYS D  1 187 ? 3.898   48.372  62.158  1.00 40.54  ? 179 LYS D O   1 
ATOM   6496  C CB  . LYS D  1 187 ? 2.983   50.655  64.118  1.00 32.68  ? 179 LYS D CB  1 
ATOM   6497  C CG  . LYS D  1 187 ? 2.775   52.103  64.573  1.00 38.80  ? 179 LYS D CG  1 
ATOM   6498  C CD  . LYS D  1 187 ? 1.331   52.422  64.954  1.00 35.82  ? 179 LYS D CD  1 
ATOM   6499  C CE  . LYS D  1 187 ? 1.209   53.847  65.518  1.00 45.51  ? 179 LYS D CE  1 
ATOM   6500  N NZ  . LYS D  1 187 ? 1.615   54.923  64.552  1.00 40.72  ? 179 LYS D NZ  1 
ATOM   6501  N N   . LYS D  1 188 ? 4.650   50.308  61.323  1.00 41.52  ? 180 LYS D N   1 
ATOM   6502  C CA  . LYS D  1 188 ? 5.877   49.746  60.793  1.00 33.35  ? 180 LYS D CA  1 
ATOM   6503  C C   . LYS D  1 188 ? 6.811   49.454  61.969  1.00 35.98  ? 180 LYS D C   1 
ATOM   6504  O O   . LYS D  1 188 ? 6.928   50.260  62.884  1.00 51.24  ? 180 LYS D O   1 
ATOM   6505  C CB  . LYS D  1 188 ? 6.499   50.768  59.835  1.00 43.30  ? 180 LYS D CB  1 
ATOM   6506  C CG  . LYS D  1 188 ? 7.309   50.189  58.704  1.00 40.77  ? 180 LYS D CG  1 
ATOM   6507  C CD  . LYS D  1 188 ? 8.678   49.872  59.207  1.00 45.15  ? 180 LYS D CD  1 
ATOM   6508  C CE  . LYS D  1 188 ? 9.391   48.908  58.312  1.00 40.59  ? 180 LYS D CE  1 
ATOM   6509  N NZ  . LYS D  1 188 ? 10.723  48.640  58.914  1.00 47.78  ? 180 LYS D NZ  1 
ATOM   6510  N N   . ASN D  1 189 ? 7.457   48.297  61.964  1.00 36.51  ? 181 ASN D N   1 
ATOM   6511  C CA  . ASN D  1 189 ? 8.401   47.948  63.021  1.00 38.32  ? 181 ASN D CA  1 
ATOM   6512  C C   . ASN D  1 189 ? 9.662   47.326  62.401  1.00 44.04  ? 181 ASN D C   1 
ATOM   6513  O O   . ASN D  1 189 ? 9.680   47.047  61.204  1.00 43.31  ? 181 ASN D O   1 
ATOM   6514  C CB  . ASN D  1 189 ? 7.734   47.007  64.030  1.00 40.23  ? 181 ASN D CB  1 
ATOM   6515  C CG  . ASN D  1 189 ? 8.541   46.844  65.311  1.00 48.21  ? 181 ASN D CG  1 
ATOM   6516  O OD1 . ASN D  1 189 ? 9.139   45.789  65.554  1.00 48.79  ? 181 ASN D OD1 1 
ATOM   6517  N ND2 . ASN D  1 189 ? 8.564   47.892  66.136  1.00 49.88  ? 181 ASN D ND2 1 
ATOM   6518  N N   . SER D  1 190 ? 10.712  47.118  63.197  1.00 43.85  ? 182 SER D N   1 
ATOM   6519  C CA  . SER D  1 190 ? 11.993  46.660  62.655  1.00 43.13  ? 182 SER D CA  1 
ATOM   6520  C C   . SER D  1 190 ? 12.841  45.896  63.668  1.00 43.31  ? 182 SER D C   1 
ATOM   6521  O O   . SER D  1 190 ? 13.593  46.501  64.427  1.00 48.58  ? 182 SER D O   1 
ATOM   6522  C CB  . SER D  1 190 ? 12.793  47.849  62.116  1.00 44.39  ? 182 SER D CB  1 
ATOM   6523  O OG  . SER D  1 190 ? 13.906  47.411  61.359  1.00 49.63  ? 182 SER D OG  1 
ATOM   6524  N N   . VAL D  1 191 ? 12.736  44.568  63.658  1.00 44.10  ? 183 VAL D N   1 
ATOM   6525  C CA  . VAL D  1 191 ? 13.476  43.715  64.593  1.00 44.20  ? 183 VAL D CA  1 
ATOM   6526  C C   . VAL D  1 191 ? 14.922  43.434  64.161  1.00 52.38  ? 183 VAL D C   1 
ATOM   6527  O O   . VAL D  1 191 ? 15.171  42.959  63.048  1.00 50.58  ? 183 VAL D O   1 
ATOM   6528  C CB  . VAL D  1 191 ? 12.750  42.366  64.823  1.00 46.84  ? 183 VAL D CB  1 
ATOM   6529  C CG1 . VAL D  1 191 ? 11.706  42.486  65.936  1.00 49.17  ? 183 VAL D CG1 1 
ATOM   6530  C CG2 . VAL D  1 191 ? 12.111  41.884  63.531  1.00 45.74  ? 183 VAL D CG2 1 
ATOM   6531  N N   . THR D  1 192 ? 15.869  43.733  65.048  1.00 55.90  ? 184 THR D N   1 
ATOM   6532  C CA  . THR D  1 192 ? 17.276  43.394  64.832  1.00 55.14  ? 184 THR D CA  1 
ATOM   6533  C C   . THR D  1 192 ? 17.621  42.250  65.801  1.00 53.05  ? 184 THR D C   1 
ATOM   6534  O O   . THR D  1 192 ? 16.749  41.803  66.542  1.00 47.38  ? 184 THR D O   1 
ATOM   6535  C CB  . THR D  1 192 ? 18.190  44.638  65.007  1.00 55.89  ? 184 THR D CB  1 
ATOM   6536  O OG1 . THR D  1 192 ? 17.524  45.797  64.479  1.00 49.65  ? 184 THR D OG1 1 
ATOM   6537  C CG2 . THR D  1 192 ? 19.521  44.457  64.275  1.00 52.97  ? 184 THR D CG2 1 
ATOM   6538  N N   . TYR D  1 193 ? 18.858  41.757  65.795  1.00 59.46  ? 185 TYR D N   1 
ATOM   6539  C CA  . TYR D  1 193 ? 19.146  40.534  66.542  1.00 63.69  ? 185 TYR D CA  1 
ATOM   6540  C C   . TYR D  1 193 ? 20.601  40.148  66.808  1.00 78.07  ? 185 TYR D C   1 
ATOM   6541  O O   . TYR D  1 193 ? 21.530  40.648  66.170  1.00 83.65  ? 185 TYR D O   1 
ATOM   6542  C CB  . TYR D  1 193 ? 18.458  39.353  65.868  1.00 69.83  ? 185 TYR D CB  1 
ATOM   6543  C CG  . TYR D  1 193 ? 17.343  38.818  66.706  1.00 70.62  ? 185 TYR D CG  1 
ATOM   6544  C CD1 . TYR D  1 193 ? 16.445  37.901  66.201  1.00 67.93  ? 185 TYR D CD1 1 
ATOM   6545  C CD2 . TYR D  1 193 ? 17.190  39.238  68.019  1.00 71.94  ? 185 TYR D CD2 1 
ATOM   6546  C CE1 . TYR D  1 193 ? 15.430  37.410  66.987  1.00 61.79  ? 185 TYR D CE1 1 
ATOM   6547  C CE2 . TYR D  1 193 ? 16.171  38.760  68.807  1.00 70.67  ? 185 TYR D CE2 1 
ATOM   6548  C CZ  . TYR D  1 193 ? 15.288  37.849  68.289  1.00 60.30  ? 185 TYR D CZ  1 
ATOM   6549  O OH  . TYR D  1 193 ? 14.270  37.372  69.089  1.00 60.45  ? 185 TYR D OH  1 
ATOM   6550  N N   . SER D  1 194 ? 20.767  39.228  67.757  1.00 74.31  ? 186 SER D N   1 
ATOM   6551  C CA  . SER D  1 194 ? 22.054  38.599  68.032  1.00 78.58  ? 186 SER D CA  1 
ATOM   6552  C C   . SER D  1 194 ? 22.250  37.360  67.147  1.00 85.51  ? 186 SER D C   1 
ATOM   6553  O O   . SER D  1 194 ? 23.383  36.958  66.872  1.00 88.58  ? 186 SER D O   1 
ATOM   6554  C CB  . SER D  1 194 ? 22.157  38.216  69.511  1.00 76.73  ? 186 SER D CB  1 
ATOM   6555  O OG  . SER D  1 194 ? 21.160  37.272  69.869  1.00 79.84  ? 186 SER D OG  1 
ATOM   6556  N N   . CYS D  1 195 ? 21.139  36.763  66.710  1.00 83.69  ? 187 CYS D N   1 
ATOM   6557  C CA  . CYS D  1 195 ? 21.162  35.627  65.783  1.00 81.25  ? 187 CYS D CA  1 
ATOM   6558  C C   . CYS D  1 195 ? 21.863  35.996  64.475  1.00 87.46  ? 187 CYS D C   1 
ATOM   6559  O O   . CYS D  1 195 ? 22.757  35.281  64.008  1.00 86.17  ? 187 CYS D O   1 
ATOM   6560  C CB  . CYS D  1 195 ? 19.729  35.124  65.500  1.00 74.78  ? 187 CYS D CB  1 
ATOM   6561  S SG  . CYS D  1 195 ? 19.156  35.192  63.744  1.00 77.21  ? 187 CYS D SG  1 
ATOM   6562  N N   . CYS D  1 196 ? 21.445  37.121  63.895  1.00 90.55  ? 188 CYS D N   1 
ATOM   6563  C CA  . CYS D  1 196 ? 21.913  37.566  62.583  1.00 85.88  ? 188 CYS D CA  1 
ATOM   6564  C C   . CYS D  1 196 ? 22.211  39.065  62.646  1.00 80.29  ? 188 CYS D C   1 
ATOM   6565  O O   . CYS D  1 196 ? 21.499  39.812  63.320  1.00 85.69  ? 188 CYS D O   1 
ATOM   6566  C CB  . CYS D  1 196 ? 20.848  37.262  61.519  1.00 72.14  ? 188 CYS D CB  1 
ATOM   6567  S SG  . CYS D  1 196 ? 19.839  35.787  61.906  1.00 76.26  ? 188 CYS D SG  1 
ATOM   6568  N N   . PRO D  1 197 ? 23.269  39.512  61.953  1.00 76.97  ? 189 PRO D N   1 
ATOM   6569  C CA  . PRO D  1 197 ? 23.704  40.908  62.083  1.00 70.04  ? 189 PRO D CA  1 
ATOM   6570  C C   . PRO D  1 197 ? 22.883  41.881  61.236  1.00 67.31  ? 189 PRO D C   1 
ATOM   6571  O O   . PRO D  1 197 ? 23.256  43.051  61.134  1.00 65.07  ? 189 PRO D O   1 
ATOM   6572  C CB  . PRO D  1 197 ? 25.146  40.860  61.573  1.00 73.38  ? 189 PRO D CB  1 
ATOM   6573  C CG  . PRO D  1 197 ? 25.133  39.770  60.545  1.00 59.97  ? 189 PRO D CG  1 
ATOM   6574  C CD  . PRO D  1 197 ? 24.135  38.744  61.037  1.00 77.77  ? 189 PRO D CD  1 
ATOM   6575  N N   . GLU D  1 198 ? 21.795  41.408  60.634  1.00 63.04  ? 190 GLU D N   1 
ATOM   6576  C CA  . GLU D  1 198 ? 20.956  42.274  59.807  1.00 55.19  ? 190 GLU D CA  1 
ATOM   6577  C C   . GLU D  1 198 ? 19.556  42.479  60.376  1.00 47.92  ? 190 GLU D C   1 
ATOM   6578  O O   . GLU D  1 198 ? 19.123  41.745  61.260  1.00 48.51  ? 190 GLU D O   1 
ATOM   6579  C CB  . GLU D  1 198 ? 20.889  41.766  58.366  1.00 51.72  ? 190 GLU D CB  1 
ATOM   6580  C CG  . GLU D  1 198 ? 21.996  42.321  57.462  1.00 58.02  ? 190 GLU D CG  1 
ATOM   6581  C CD  . GLU D  1 198 ? 21.810  43.803  57.107  1.00 61.56  ? 190 GLU D CD  1 
ATOM   6582  O OE1 . GLU D  1 198 ? 20.788  44.412  57.514  1.00 56.21  ? 190 GLU D OE1 1 
ATOM   6583  O OE2 . GLU D  1 198 ? 22.692  44.355  56.406  1.00 53.44  ? 190 GLU D OE2 1 
ATOM   6584  N N   . ALA D  1 199 ? 18.859  43.488  59.861  1.00 41.80  ? 191 ALA D N   1 
ATOM   6585  C CA  . ALA D  1 199 ? 17.585  43.918  60.423  1.00 37.49  ? 191 ALA D CA  1 
ATOM   6586  C C   . ALA D  1 199 ? 16.392  43.522  59.556  1.00 36.66  ? 191 ALA D C   1 
ATOM   6587  O O   . ALA D  1 199 ? 16.342  43.850  58.375  1.00 35.21  ? 191 ALA D O   1 
ATOM   6588  C CB  . ALA D  1 199 ? 17.599  45.416  60.633  1.00 31.89  ? 191 ALA D CB  1 
ATOM   6589  N N   . TYR D  1 200 ? 15.419  42.834  60.146  1.00 39.58  ? 192 TYR D N   1 
ATOM   6590  C CA  . TYR D  1 200 ? 14.220  42.430  59.408  1.00 35.92  ? 192 TYR D CA  1 
ATOM   6591  C C   . TYR D  1 200 ? 13.071  43.407  59.631  1.00 36.50  ? 192 TYR D C   1 
ATOM   6592  O O   . TYR D  1 200 ? 12.638  43.620  60.757  1.00 39.53  ? 192 TYR D O   1 
ATOM   6593  C CB  . TYR D  1 200 ? 13.805  40.996  59.768  1.00 33.52  ? 192 TYR D CB  1 
ATOM   6594  C CG  . TYR D  1 200 ? 14.870  39.980  59.418  1.00 31.38  ? 192 TYR D CG  1 
ATOM   6595  C CD1 . TYR D  1 200 ? 14.801  39.243  58.243  1.00 27.94  ? 192 TYR D CD1 1 
ATOM   6596  C CD2 . TYR D  1 200 ? 15.959  39.780  60.252  1.00 28.72  ? 192 TYR D CD2 1 
ATOM   6597  C CE1 . TYR D  1 200 ? 15.783  38.328  57.919  1.00 25.62  ? 192 TYR D CE1 1 
ATOM   6598  C CE2 . TYR D  1 200 ? 16.939  38.875  59.937  1.00 34.25  ? 192 TYR D CE2 1 
ATOM   6599  C CZ  . TYR D  1 200 ? 16.851  38.152  58.769  1.00 31.27  ? 192 TYR D CZ  1 
ATOM   6600  O OH  . TYR D  1 200 ? 17.846  37.260  58.462  1.00 34.78  ? 192 TYR D OH  1 
ATOM   6601  N N   . GLU D  1 201 ? 12.598  44.020  58.552  1.00 36.70  ? 193 GLU D N   1 
ATOM   6602  C CA  . GLU D  1 201 ? 11.433  44.885  58.629  1.00 34.61  ? 193 GLU D CA  1 
ATOM   6603  C C   . GLU D  1 201 ? 10.191  44.039  58.802  1.00 37.79  ? 193 GLU D C   1 
ATOM   6604  O O   . GLU D  1 201 ? 10.177  42.862  58.440  1.00 44.97  ? 193 GLU D O   1 
ATOM   6605  C CB  . GLU D  1 201 ? 11.294  45.722  57.366  1.00 30.52  ? 193 GLU D CB  1 
ATOM   6606  C CG  . GLU D  1 201 ? 12.471  46.622  57.103  1.00 29.28  ? 193 GLU D CG  1 
ATOM   6607  C CD  . GLU D  1 201 ? 12.082  47.836  56.294  1.00 38.32  ? 193 GLU D CD  1 
ATOM   6608  O OE1 . GLU D  1 201 ? 10.957  47.844  55.746  1.00 35.88  ? 193 GLU D OE1 1 
ATOM   6609  O OE2 . GLU D  1 201 ? 12.890  48.790  56.218  1.00 50.89  ? 193 GLU D OE2 1 
ATOM   6610  N N   . ASP D  1 202 ? 9.149   44.644  59.359  1.00 43.14  ? 194 ASP D N   1 
ATOM   6611  C CA  . ASP D  1 202 ? 7.858   43.977  59.511  1.00 41.61  ? 194 ASP D CA  1 
ATOM   6612  C C   . ASP D  1 202 ? 6.744   44.966  59.874  1.00 37.42  ? 194 ASP D C   1 
ATOM   6613  O O   . ASP D  1 202 ? 7.000   46.134  60.164  1.00 41.17  ? 194 ASP D O   1 
ATOM   6614  C CB  . ASP D  1 202 ? 7.941   42.833  60.534  1.00 38.47  ? 194 ASP D CB  1 
ATOM   6615  C CG  . ASP D  1 202 ? 8.353   43.304  61.913  1.00 44.02  ? 194 ASP D CG  1 
ATOM   6616  O OD1 . ASP D  1 202 ? 7.651   44.152  62.498  1.00 45.38  ? 194 ASP D OD1 1 
ATOM   6617  O OD2 . ASP D  1 202 ? 9.387   42.819  62.418  1.00 48.60  ? 194 ASP D OD2 1 
ATOM   6618  N N   . VAL D  1 203 ? 5.507   44.496  59.828  1.00 33.92  ? 195 VAL D N   1 
ATOM   6619  C CA  . VAL D  1 203 ? 4.397   45.269  60.344  1.00 32.60  ? 195 VAL D CA  1 
ATOM   6620  C C   . VAL D  1 203 ? 3.905   44.635  61.631  1.00 29.07  ? 195 VAL D C   1 
ATOM   6621  O O   . VAL D  1 203 ? 3.629   43.436  61.682  1.00 27.05  ? 195 VAL D O   1 
ATOM   6622  C CB  . VAL D  1 203 ? 3.241   45.333  59.353  1.00 27.37  ? 195 VAL D CB  1 
ATOM   6623  C CG1 . VAL D  1 203 ? 3.455   46.469  58.397  1.00 33.87  ? 195 VAL D CG1 1 
ATOM   6624  C CG2 . VAL D  1 203 ? 3.126   44.015  58.604  1.00 34.61  ? 195 VAL D CG2 1 
ATOM   6625  N N   . GLU D  1 204 ? 3.817   45.442  62.679  1.00 30.25  ? 196 GLU D N   1 
ATOM   6626  C CA  . GLU D  1 204 ? 3.213   44.982  63.915  1.00 30.82  ? 196 GLU D CA  1 
ATOM   6627  C C   . GLU D  1 204 ? 1.751   45.358  63.878  1.00 24.06  ? 196 GLU D C   1 
ATOM   6628  O O   . GLU D  1 204 ? 1.409   46.494  63.549  1.00 25.75  ? 196 GLU D O   1 
ATOM   6629  C CB  . GLU D  1 204 ? 3.894   45.610  65.118  1.00 33.68  ? 196 GLU D CB  1 
ATOM   6630  C CG  . GLU D  1 204 ? 3.597   44.893  66.405  1.00 33.14  ? 196 GLU D CG  1 
ATOM   6631  C CD  . GLU D  1 204 ? 4.618   45.204  67.470  1.00 42.19  ? 196 GLU D CD  1 
ATOM   6632  O OE1 . GLU D  1 204 ? 5.536   46.006  67.191  1.00 41.95  ? 196 GLU D OE1 1 
ATOM   6633  O OE2 . GLU D  1 204 ? 4.507   44.640  68.580  1.00 48.59  ? 196 GLU D OE2 1 
ATOM   6634  N N   . VAL D  1 205 ? 0.891   44.390  64.174  1.00 19.69  ? 197 VAL D N   1 
ATOM   6635  C CA  . VAL D  1 205 ? -0.546  44.603  64.130  1.00 19.91  ? 197 VAL D CA  1 
ATOM   6636  C C   . VAL D  1 205 ? -1.086  44.427  65.526  1.00 23.21  ? 197 VAL D C   1 
ATOM   6637  O O   . VAL D  1 205 ? -0.833  43.402  66.156  1.00 22.46  ? 197 VAL D O   1 
ATOM   6638  C CB  . VAL D  1 205 ? -1.256  43.595  63.204  1.00 18.96  ? 197 VAL D CB  1 
ATOM   6639  C CG1 . VAL D  1 205 ? -2.764  43.656  63.406  1.00 18.99  ? 197 VAL D CG1 1 
ATOM   6640  C CG2 . VAL D  1 205 ? -0.916  43.877  61.770  1.00 20.25  ? 197 VAL D CG2 1 
ATOM   6641  N N   . SER D  1 206 ? -1.818  45.427  66.012  1.00 22.64  ? 198 SER D N   1 
ATOM   6642  C CA  . SER D  1 206 ? -2.386  45.386  67.356  1.00 19.24  ? 198 SER D CA  1 
ATOM   6643  C C   . SER D  1 206 ? -3.896  45.300  67.303  1.00 21.67  ? 198 SER D C   1 
ATOM   6644  O O   . SER D  1 206 ? -4.576  46.241  66.883  1.00 20.87  ? 198 SER D O   1 
ATOM   6645  C CB  . SER D  1 206 ? -1.952  46.597  68.177  1.00 20.05  ? 198 SER D CB  1 
ATOM   6646  O OG  . SER D  1 206 ? -0.557  46.551  68.423  1.00 21.74  ? 198 SER D OG  1 
ATOM   6647  N N   . LEU D  1 207 ? -4.405  44.154  67.745  1.00 20.99  ? 199 LEU D N   1 
ATOM   6648  C CA  . LEU D  1 207 ? -5.820  43.851  67.677  1.00 18.92  ? 199 LEU D CA  1 
ATOM   6649  C C   . LEU D  1 207 ? -6.435  43.963  69.064  1.00 25.26  ? 199 LEU D C   1 
ATOM   6650  O O   . LEU D  1 207 ? -6.112  43.184  69.966  1.00 25.75  ? 199 LEU D O   1 
ATOM   6651  C CB  . LEU D  1 207 ? -6.009  42.445  67.119  1.00 16.20  ? 199 LEU D CB  1 
ATOM   6652  C CG  . LEU D  1 207 ? -7.448  41.967  67.012  1.00 15.93  ? 199 LEU D CG  1 
ATOM   6653  C CD1 . LEU D  1 207 ? -8.272  42.968  66.235  1.00 17.14  ? 199 LEU D CD1 1 
ATOM   6654  C CD2 . LEU D  1 207 ? -7.490  40.593  66.356  1.00 14.61  ? 199 LEU D CD2 1 
ATOM   6655  N N   . ASN D  1 208 ? -7.319  44.945  69.225  1.00 28.29  ? 200 ASN D N   1 
ATOM   6656  C CA  . ASN D  1 208 ? -7.945  45.257  70.508  1.00 19.14  ? 200 ASN D CA  1 
ATOM   6657  C C   . ASN D  1 208 ? -9.414  44.851  70.443  1.00 17.38  ? 200 ASN D C   1 
ATOM   6658  O O   . ASN D  1 208 ? -10.203 45.449  69.704  1.00 15.73  ? 200 ASN D O   1 
ATOM   6659  C CB  . ASN D  1 208 ? -7.761  46.759  70.803  1.00 23.90  ? 200 ASN D CB  1 
ATOM   6660  C CG  . ASN D  1 208 ? -8.279  47.188  72.183  1.00 24.30  ? 200 ASN D CG  1 
ATOM   6661  O OD1 . ASN D  1 208 ? -8.840  48.272  72.321  1.00 27.17  ? 200 ASN D OD1 1 
ATOM   6662  N ND2 . ASN D  1 208 ? -8.086  46.353  73.193  1.00 18.39  ? 200 ASN D ND2 1 
ATOM   6663  N N   . PHE D  1 209 ? -9.772  43.814  71.199  1.00 17.79  ? 201 PHE D N   1 
ATOM   6664  C CA  . PHE D  1 209 ? -11.112 43.210  71.120  1.00 18.03  ? 201 PHE D CA  1 
ATOM   6665  C C   . PHE D  1 209 ? -11.583 42.760  72.504  1.00 14.25  ? 201 PHE D C   1 
ATOM   6666  O O   . PHE D  1 209 ? -10.760 42.550  73.400  1.00 13.64  ? 201 PHE D O   1 
ATOM   6667  C CB  . PHE D  1 209 ? -11.111 42.005  70.155  1.00 13.20  ? 201 PHE D CB  1 
ATOM   6668  C CG  . PHE D  1 209 ? -10.286 40.831  70.645  1.00 14.00  ? 201 PHE D CG  1 
ATOM   6669  C CD1 . PHE D  1 209 ? -8.895  40.887  70.641  1.00 13.05  ? 201 PHE D CD1 1 
ATOM   6670  C CD2 . PHE D  1 209 ? -10.902 39.687  71.137  1.00 13.69  ? 201 PHE D CD2 1 
ATOM   6671  C CE1 . PHE D  1 209 ? -8.136  39.831  71.112  1.00 11.28  ? 201 PHE D CE1 1 
ATOM   6672  C CE2 . PHE D  1 209 ? -10.148 38.630  71.599  1.00 13.32  ? 201 PHE D CE2 1 
ATOM   6673  C CZ  . PHE D  1 209 ? -8.761  38.702  71.581  1.00 11.35  ? 201 PHE D CZ  1 
ATOM   6674  N N   . ARG D  1 210 ? -12.899 42.612  72.664  1.00 12.75  ? 202 ARG D N   1 
ATOM   6675  C CA  . ARG D  1 210 ? -13.484 42.081  73.901  1.00 20.18  ? 202 ARG D CA  1 
ATOM   6676  C C   . ARG D  1 210 ? -14.687 41.203  73.607  1.00 19.07  ? 202 ARG D C   1 
ATOM   6677  O O   . ARG D  1 210 ? -15.305 41.322  72.549  1.00 20.44  ? 202 ARG D O   1 
ATOM   6678  C CB  . ARG D  1 210 ? -13.926 43.212  74.835  1.00 22.55  ? 202 ARG D CB  1 
ATOM   6679  C CG  . ARG D  1 210 ? -15.065 44.059  74.276  1.00 24.36  ? 202 ARG D CG  1 
ATOM   6680  C CD  . ARG D  1 210 ? -15.947 44.620  75.375  1.00 32.72  ? 202 ARG D CD  1 
ATOM   6681  N NE  . ARG D  1 210 ? -16.971 45.519  74.849  1.00 37.39  ? 202 ARG D NE  1 
ATOM   6682  C CZ  . ARG D  1 210 ? -16.853 46.845  74.831  1.00 37.73  ? 202 ARG D CZ  1 
ATOM   6683  N NH1 . ARG D  1 210 ? -15.758 47.420  75.322  1.00 34.56  ? 202 ARG D NH1 1 
ATOM   6684  N NH2 . ARG D  1 210 ? -17.828 47.598  74.331  1.00 28.83  ? 202 ARG D NH2 1 
ATOM   6685  N N   . LYS D  1 211 ? -15.032 40.329  74.548  1.00 21.07  ? 203 LYS D N   1 
ATOM   6686  C CA  . LYS D  1 211 ? -16.277 39.573  74.431  1.00 25.84  ? 203 LYS D CA  1 
ATOM   6687  C C   . LYS D  1 211 ? -17.452 40.547  74.494  1.00 25.76  ? 203 LYS D C   1 
ATOM   6688  O O   . LYS D  1 211 ? -17.329 41.639  75.032  1.00 25.62  ? 203 LYS D O   1 
ATOM   6689  C CB  . LYS D  1 211 ? -16.401 38.512  75.537  1.00 24.94  ? 203 LYS D CB  1 
ATOM   6690  C CG  . LYS D  1 211 ? -17.393 37.391  75.202  1.00 28.63  ? 203 LYS D CG  1 
ATOM   6691  C CD  . LYS D  1 211 ? -17.971 36.703  76.442  1.00 39.42  ? 203 LYS D CD  1 
ATOM   6692  C CE  . LYS D  1 211 ? -18.956 37.603  77.183  1.00 38.46  ? 203 LYS D CE  1 
ATOM   6693  N NZ  . LYS D  1 211 ? -19.666 36.904  78.287  1.00 37.05  ? 203 LYS D NZ  1 
ATOM   6694  N N   . LYS D  1 212 ? -18.589 40.155  73.940  1.00 30.45  ? 204 LYS D N   1 
ATOM   6695  C CA  . LYS D  1 212 ? -19.769 41.005  73.970  1.00 29.61  ? 204 LYS D CA  1 
ATOM   6696  C C   . LYS D  1 212 ? -20.648 40.663  75.170  1.00 44.09  ? 204 LYS D C   1 
ATOM   6697  O O   . LYS D  1 212 ? -20.702 39.503  75.593  1.00 43.11  ? 204 LYS D O   1 
ATOM   6698  C CB  . LYS D  1 212 ? -20.539 40.890  72.650  1.00 25.09  ? 204 LYS D CB  1 
ATOM   6699  C CG  . LYS D  1 212 ? -19.698 41.310  71.456  1.00 24.93  ? 204 LYS D CG  1 
ATOM   6700  C CD  . LYS D  1 212 ? -20.505 41.493  70.183  1.00 22.88  ? 204 LYS D CD  1 
ATOM   6701  C CE  . LYS D  1 212 ? -20.887 40.170  69.581  1.00 21.67  ? 204 LYS D CE  1 
ATOM   6702  N NZ  . LYS D  1 212 ? -21.592 40.358  68.284  1.00 25.54  ? 204 LYS D NZ  1 
ATOM   6703  N N   . GLY D  1 213 ? -21.320 41.675  75.725  1.00 49.59  ? 205 GLY D N   1 
ATOM   6704  C CA  . GLY D  1 213 ? -22.172 41.488  76.890  1.00 43.70  ? 205 GLY D CA  1 
ATOM   6705  C C   . GLY D  1 213 ? -22.988 42.718  77.242  1.00 61.44  ? 205 GLY D C   1 
ATOM   6706  O O   . GLY D  1 213 ? -22.526 43.609  77.960  1.00 64.80  ? 205 GLY D O   1 
ATOM   6707  N N   . ASP E  1 1   ? 29.380  41.904  48.430  1.00 45.27  ? -7  ASP E N   1 
ATOM   6708  C CA  . ASP E  1 1   ? 29.257  43.169  49.151  1.00 54.67  ? -7  ASP E CA  1 
ATOM   6709  C C   . ASP E  1 1   ? 27.820  43.682  49.129  1.00 55.51  ? -7  ASP E C   1 
ATOM   6710  O O   . ASP E  1 1   ? 27.077  43.431  48.173  1.00 52.54  ? -7  ASP E O   1 
ATOM   6711  C CB  . ASP E  1 1   ? 30.202  44.225  48.572  1.00 53.00  ? -7  ASP E CB  1 
ATOM   6712  C CG  . ASP E  1 1   ? 29.994  44.437  47.091  1.00 50.45  ? -7  ASP E CG  1 
ATOM   6713  O OD1 . ASP E  1 1   ? 29.801  45.600  46.669  1.00 50.30  ? -7  ASP E OD1 1 
ATOM   6714  O OD2 . ASP E  1 1   ? 30.027  43.431  46.352  1.00 53.01  ? -7  ASP E OD2 1 
ATOM   6715  N N   . TYR E  1 2   ? 27.436  44.457  50.131  1.00 56.21  ? -6  TYR E N   1 
ATOM   6716  C CA  . TYR E  1 2   ? 26.047  44.870  50.244  1.00 53.60  ? -6  TYR E CA  1 
ATOM   6717  C C   . TYR E  1 2   ? 25.645  45.646  48.996  1.00 42.93  ? -6  TYR E C   1 
ATOM   6718  O O   . TYR E  1 2   ? 24.517  45.532  48.517  1.00 40.74  ? -6  TYR E O   1 
ATOM   6719  C CB  . TYR E  1 2   ? 25.841  45.731  51.491  1.00 56.54  ? -6  TYR E CB  1 
ATOM   6720  C CG  . TYR E  1 2   ? 26.261  45.056  52.777  1.00 71.28  ? -6  TYR E CG  1 
ATOM   6721  C CD1 . TYR E  1 2   ? 27.477  45.356  53.377  1.00 78.31  ? -6  TYR E CD1 1 
ATOM   6722  C CD2 . TYR E  1 2   ? 25.441  44.119  53.392  1.00 74.38  ? -6  TYR E CD2 1 
ATOM   6723  C CE1 . TYR E  1 2   ? 27.865  44.742  54.553  1.00 71.83  ? -6  TYR E CE1 1 
ATOM   6724  C CE2 . TYR E  1 2   ? 25.820  43.500  54.568  1.00 75.74  ? -6  TYR E CE2 1 
ATOM   6725  C CZ  . TYR E  1 2   ? 27.033  43.815  55.143  1.00 78.87  ? -6  TYR E CZ  1 
ATOM   6726  O OH  . TYR E  1 2   ? 27.414  43.201  56.314  1.00 94.85  ? -6  TYR E OH  1 
ATOM   6727  N N   . LYS E  1 3   ? 26.574  46.442  48.483  1.00 47.69  ? -5  LYS E N   1 
ATOM   6728  C CA  . LYS E  1 3   ? 26.295  47.353  47.376  1.00 48.66  ? -5  LYS E CA  1 
ATOM   6729  C C   . LYS E  1 3   ? 25.518  46.690  46.241  1.00 45.31  ? -5  LYS E C   1 
ATOM   6730  O O   . LYS E  1 3   ? 24.628  47.302  45.650  1.00 41.47  ? -5  LYS E O   1 
ATOM   6731  C CB  . LYS E  1 3   ? 27.608  47.929  46.826  1.00 50.35  ? -5  LYS E CB  1 
ATOM   6732  C CG  . LYS E  1 3   ? 28.587  48.444  47.884  1.00 49.62  ? -5  LYS E CG  1 
ATOM   6733  C CD  . LYS E  1 3   ? 28.558  49.970  47.988  1.00 58.54  ? -5  LYS E CD  1 
ATOM   6734  C CE  . LYS E  1 3   ? 29.809  50.507  48.686  1.00 57.37  ? -5  LYS E CE  1 
ATOM   6735  N NZ  . LYS E  1 3   ? 30.051  51.960  48.430  1.00 45.23  ? -5  LYS E NZ  1 
ATOM   6736  N N   . ASP E  1 4   ? 25.858  45.439  45.945  1.00 44.51  ? -4  ASP E N   1 
ATOM   6737  C CA  . ASP E  1 4   ? 25.292  44.744  44.793  1.00 43.01  ? -4  ASP E CA  1 
ATOM   6738  C C   . ASP E  1 4   ? 24.250  43.685  45.170  1.00 43.99  ? -4  ASP E C   1 
ATOM   6739  O O   . ASP E  1 4   ? 23.816  42.919  44.306  1.00 41.22  ? -4  ASP E O   1 
ATOM   6740  C CB  . ASP E  1 4   ? 26.402  44.098  43.943  1.00 48.15  ? -4  ASP E CB  1 
ATOM   6741  C CG  . ASP E  1 4   ? 27.415  45.113  43.407  1.00 45.30  ? -4  ASP E CG  1 
ATOM   6742  O OD1 . ASP E  1 4   ? 27.018  45.987  42.602  1.00 46.45  ? -4  ASP E OD1 1 
ATOM   6743  O OD2 . ASP E  1 4   ? 28.612  45.021  43.776  1.00 40.63  ? -4  ASP E OD2 1 
ATOM   6744  N N   . ASP E  1 5   ? 23.862  43.645  46.449  1.00 45.17  ? -3  ASP E N   1 
ATOM   6745  C CA  . ASP E  1 5   ? 22.846  42.710  46.959  1.00 39.65  ? -3  ASP E CA  1 
ATOM   6746  C C   . ASP E  1 5   ? 21.550  42.672  46.122  1.00 41.26  ? -3  ASP E C   1 
ATOM   6747  O O   . ASP E  1 5   ? 20.937  41.611  45.955  1.00 36.58  ? -3  ASP E O   1 
ATOM   6748  C CB  . ASP E  1 5   ? 22.490  43.050  48.420  1.00 49.03  ? -3  ASP E CB  1 
ATOM   6749  C CG  . ASP E  1 5   ? 23.150  42.114  49.437  1.00 50.81  ? -3  ASP E CG  1 
ATOM   6750  O OD1 . ASP E  1 5   ? 24.016  41.302  49.041  1.00 48.87  ? -3  ASP E OD1 1 
ATOM   6751  O OD2 . ASP E  1 5   ? 22.806  42.208  50.640  1.00 45.09  ? -3  ASP E OD2 1 
ATOM   6752  N N   . ASP E  1 6   ? 21.136  43.824  45.596  1.00 38.85  ? -2  ASP E N   1 
ATOM   6753  C CA  . ASP E  1 6   ? 19.836  43.940  44.931  1.00 36.40  ? -2  ASP E CA  1 
ATOM   6754  C C   . ASP E  1 6   ? 19.899  43.954  43.403  1.00 37.95  ? -2  ASP E C   1 
ATOM   6755  O O   . ASP E  1 6   ? 18.989  44.466  42.744  1.00 37.89  ? -2  ASP E O   1 
ATOM   6756  C CB  . ASP E  1 6   ? 19.093  45.185  45.422  1.00 37.90  ? -2  ASP E CB  1 
ATOM   6757  C CG  . ASP E  1 6   ? 18.658  45.081  46.882  1.00 37.81  ? -2  ASP E CG  1 
ATOM   6758  O OD1 . ASP E  1 6   ? 19.039  44.105  47.575  1.00 30.07  ? -2  ASP E OD1 1 
ATOM   6759  O OD2 . ASP E  1 6   ? 17.934  45.996  47.334  1.00 35.22  ? -2  ASP E OD2 1 
ATOM   6760  N N   . ASP E  1 7   ? 20.974  43.406  42.846  1.00 35.72  ? -1  ASP E N   1 
ATOM   6761  C CA  . ASP E  1 7   ? 21.067  43.185  41.412  1.00 31.00  ? -1  ASP E CA  1 
ATOM   6762  C C   . ASP E  1 7   ? 20.291  41.906  41.072  1.00 28.73  ? -1  ASP E C   1 
ATOM   6763  O O   . ASP E  1 7   ? 20.728  40.807  41.423  1.00 29.10  ? -1  ASP E O   1 
ATOM   6764  C CB  . ASP E  1 7   ? 22.538  43.050  40.994  1.00 35.38  ? -1  ASP E CB  1 
ATOM   6765  C CG  . ASP E  1 7   ? 22.752  43.310  39.508  1.00 37.51  ? -1  ASP E CG  1 
ATOM   6766  O OD1 . ASP E  1 7   ? 22.635  42.357  38.707  1.00 32.35  ? -1  ASP E OD1 1 
ATOM   6767  O OD2 . ASP E  1 7   ? 23.029  44.474  39.141  1.00 41.62  ? -1  ASP E OD2 1 
ATOM   6768  N N   . LYS E  1 8   ? 19.146  42.045  40.397  1.00 23.33  ? 0   LYS E N   1 
ATOM   6769  C CA  . LYS E  1 8   ? 18.253  40.906  40.152  1.00 22.10  ? 0   LYS E CA  1 
ATOM   6770  C C   . LYS E  1 8   ? 18.871  39.836  39.252  1.00 23.43  ? 0   LYS E C   1 
ATOM   6771  O O   . LYS E  1 8   ? 18.760  38.629  39.521  1.00 16.96  ? 0   LYS E O   1 
ATOM   6772  C CB  . LYS E  1 8   ? 16.928  41.378  39.554  1.00 23.71  ? 0   LYS E CB  1 
ATOM   6773  C CG  . LYS E  1 8   ? 15.814  40.339  39.556  1.00 16.22  ? 0   LYS E CG  1 
ATOM   6774  C CD  . LYS E  1 8   ? 14.811  40.643  38.448  1.00 20.69  ? 0   LYS E CD  1 
ATOM   6775  C CE  . LYS E  1 8   ? 13.360  40.493  38.898  1.00 16.34  ? 0   LYS E CE  1 
ATOM   6776  N NZ  . LYS E  1 8   ? 12.957  39.072  38.931  1.00 17.74  ? 0   LYS E NZ  1 
ATOM   6777  N N   . LEU E  1 9   ? 19.521  40.280  38.181  1.00 24.85  ? 1   LEU E N   1 
ATOM   6778  C CA  . LEU E  1 9   ? 20.159  39.353  37.261  1.00 18.70  ? 1   LEU E CA  1 
ATOM   6779  C C   . LEU E  1 9   ? 21.316  38.635  37.951  1.00 21.03  ? 1   LEU E C   1 
ATOM   6780  O O   . LEU E  1 9   ? 21.551  37.447  37.702  1.00 22.33  ? 1   LEU E O   1 
ATOM   6781  C CB  . LEU E  1 9   ? 20.612  40.065  35.981  1.00 25.78  ? 1   LEU E CB  1 
ATOM   6782  C CG  . LEU E  1 9   ? 21.120  39.180  34.836  1.00 25.79  ? 1   LEU E CG  1 
ATOM   6783  C CD1 . LEU E  1 9   ? 20.067  38.152  34.422  1.00 20.88  ? 1   LEU E CD1 1 
ATOM   6784  C CD2 . LEU E  1 9   ? 21.555  40.034  33.653  1.00 24.12  ? 1   LEU E CD2 1 
ATOM   6785  N N   . ASP E  1 10  ? 22.028  39.339  38.829  1.00 21.07  ? 2   ASP E N   1 
ATOM   6786  C CA  . ASP E  1 10  ? 23.103  38.706  39.600  1.00 25.47  ? 2   ASP E CA  1 
ATOM   6787  C C   . ASP E  1 10  ? 22.525  37.630  40.510  1.00 20.98  ? 2   ASP E C   1 
ATOM   6788  O O   . ASP E  1 10  ? 23.131  36.575  40.710  1.00 19.46  ? 2   ASP E O   1 
ATOM   6789  C CB  . ASP E  1 10  ? 23.894  39.731  40.432  1.00 32.84  ? 2   ASP E CB  1 
ATOM   6790  C CG  . ASP E  1 10  ? 24.812  40.610  39.580  1.00 40.47  ? 2   ASP E CG  1 
ATOM   6791  O OD1 . ASP E  1 10  ? 24.925  40.360  38.355  1.00 38.97  ? 2   ASP E OD1 1 
ATOM   6792  O OD2 . ASP E  1 10  ? 25.421  41.550  40.141  1.00 40.11  ? 2   ASP E OD2 1 
ATOM   6793  N N   . ARG E  1 11  ? 21.345  37.918  41.054  1.00 18.99  ? 3   ARG E N   1 
ATOM   6794  C CA  . ARG E  1 11  ? 20.638  36.985  41.911  1.00 17.84  ? 3   ARG E CA  1 
ATOM   6795  C C   . ARG E  1 11  ? 20.149  35.756  41.141  1.00 15.40  ? 3   ARG E C   1 
ATOM   6796  O O   . ARG E  1 11  ? 20.336  34.611  41.574  1.00 9.77   ? 3   ARG E O   1 
ATOM   6797  C CB  . ARG E  1 11  ? 19.459  37.685  42.585  1.00 21.03  ? 3   ARG E CB  1 
ATOM   6798  C CG  . ARG E  1 11  ? 19.816  38.395  43.874  1.00 20.51  ? 3   ARG E CG  1 
ATOM   6799  C CD  . ARG E  1 11  ? 18.595  38.666  44.761  1.00 19.34  ? 3   ARG E CD  1 
ATOM   6800  N NE  . ARG E  1 11  ? 19.046  39.234  46.026  1.00 28.42  ? 3   ARG E NE  1 
ATOM   6801  C CZ  . ARG E  1 11  ? 19.162  38.572  47.176  1.00 22.56  ? 3   ARG E CZ  1 
ATOM   6802  N NH1 . ARG E  1 11  ? 18.819  37.294  47.282  1.00 17.89  ? 3   ARG E NH1 1 
ATOM   6803  N NH2 . ARG E  1 11  ? 19.620  39.209  48.239  1.00 30.01  ? 3   ARG E NH2 1 
ATOM   6804  N N   . ALA E  1 12  ? 19.521  36.000  39.996  1.00 13.53  ? 4   ALA E N   1 
ATOM   6805  C CA  . ALA E  1 12  ? 19.025  34.916  39.179  1.00 10.21  ? 4   ALA E CA  1 
ATOM   6806  C C   . ALA E  1 12  ? 20.168  33.992  38.773  1.00 14.97  ? 4   ALA E C   1 
ATOM   6807  O O   . ALA E  1 12  ? 20.009  32.765  38.788  1.00 14.98  ? 4   ALA E O   1 
ATOM   6808  C CB  . ALA E  1 12  ? 18.323  35.458  37.973  1.00 13.73  ? 4   ALA E CB  1 
ATOM   6809  N N   . ASP E  1 13  ? 21.322  34.580  38.441  1.00 14.10  ? 5   ASP E N   1 
ATOM   6810  C CA  . ASP E  1 13  ? 22.484  33.811  37.988  1.00 13.88  ? 5   ASP E CA  1 
ATOM   6811  C C   . ASP E  1 13  ? 23.154  32.996  39.087  1.00 13.28  ? 5   ASP E C   1 
ATOM   6812  O O   . ASP E  1 13  ? 23.630  31.896  38.825  1.00 12.50  ? 5   ASP E O   1 
ATOM   6813  C CB  . ASP E  1 13  ? 23.526  34.708  37.308  1.00 16.91  ? 5   ASP E CB  1 
ATOM   6814  C CG  . ASP E  1 13  ? 23.024  35.297  36.008  1.00 19.63  ? 5   ASP E CG  1 
ATOM   6815  O OD1 . ASP E  1 13  ? 22.009  34.794  35.490  1.00 20.47  ? 5   ASP E OD1 1 
ATOM   6816  O OD2 . ASP E  1 13  ? 23.638  36.258  35.505  1.00 22.82  ? 5   ASP E OD2 1 
ATOM   6817  N N   . ILE E  1 14  ? 23.218  33.548  40.300  1.00 13.20  ? 6   ILE E N   1 
ATOM   6818  C CA  . ILE E  1 14  ? 23.721  32.814  41.461  1.00 11.59  ? 6   ILE E CA  1 
ATOM   6819  C C   . ILE E  1 14  ? 22.840  31.601  41.722  1.00 13.52  ? 6   ILE E C   1 
ATOM   6820  O O   . ILE E  1 14  ? 23.319  30.494  42.023  1.00 10.86  ? 6   ILE E O   1 
ATOM   6821  C CB  . ILE E  1 14  ? 23.715  33.694  42.719  1.00 16.95  ? 6   ILE E CB  1 
ATOM   6822  C CG1 . ILE E  1 14  ? 24.922  34.626  42.706  1.00 21.15  ? 6   ILE E CG1 1 
ATOM   6823  C CG2 . ILE E  1 14  ? 23.729  32.838  44.000  1.00 14.01  ? 6   ILE E CG2 1 
ATOM   6824  C CD1 . ILE E  1 14  ? 24.801  35.792  43.665  1.00 22.50  ? 6   ILE E CD1 1 
ATOM   6825  N N   . LEU E  1 15  ? 21.539  31.813  41.589  1.00 12.12  ? 7   LEU E N   1 
ATOM   6826  C CA  . LEU E  1 15  ? 20.592  30.753  41.853  1.00 13.15  ? 7   LEU E CA  1 
ATOM   6827  C C   . LEU E  1 15  ? 20.728  29.695  40.774  1.00 13.27  ? 7   LEU E C   1 
ATOM   6828  O O   . LEU E  1 15  ? 20.635  28.487  41.045  1.00 11.24  ? 7   LEU E O   1 
ATOM   6829  C CB  . LEU E  1 15  ? 19.179  31.315  41.882  1.00 14.56  ? 7   LEU E CB  1 
ATOM   6830  C CG  . LEU E  1 15  ? 18.100  30.272  42.085  1.00 15.30  ? 7   LEU E CG  1 
ATOM   6831  C CD1 . LEU E  1 15  ? 18.299  29.589  43.422  1.00 11.36  ? 7   LEU E CD1 1 
ATOM   6832  C CD2 . LEU E  1 15  ? 16.741  30.943  41.993  1.00 17.86  ? 7   LEU E CD2 1 
ATOM   6833  N N   . TYR E  1 16  ? 20.964  30.153  39.547  1.00 13.37  ? 8   TYR E N   1 
ATOM   6834  C CA  . TYR E  1 16  ? 21.213  29.234  38.438  1.00 11.18  ? 8   TYR E CA  1 
ATOM   6835  C C   . TYR E  1 16  ? 22.467  28.408  38.708  1.00 11.82  ? 8   TYR E C   1 
ATOM   6836  O O   . TYR E  1 16  ? 22.421  27.183  38.606  1.00 12.62  ? 8   TYR E O   1 
ATOM   6837  C CB  . TYR E  1 16  ? 21.306  29.990  37.117  1.00 13.58  ? 8   TYR E CB  1 
ATOM   6838  C CG  . TYR E  1 16  ? 21.851  29.187  35.954  1.00 18.52  ? 8   TYR E CG  1 
ATOM   6839  C CD1 . TYR E  1 16  ? 21.094  28.191  35.336  1.00 15.42  ? 8   TYR E CD1 1 
ATOM   6840  C CD2 . TYR E  1 16  ? 23.128  29.444  35.457  1.00 13.86  ? 8   TYR E CD2 1 
ATOM   6841  C CE1 . TYR E  1 16  ? 21.610  27.474  34.270  1.00 14.74  ? 8   TYR E CE1 1 
ATOM   6842  C CE2 . TYR E  1 16  ? 23.635  28.741  34.400  1.00 14.01  ? 8   TYR E CE2 1 
ATOM   6843  C CZ  . TYR E  1 16  ? 22.888  27.762  33.804  1.00 15.33  ? 8   TYR E CZ  1 
ATOM   6844  O OH  . TYR E  1 16  ? 23.442  27.085  32.732  1.00 13.81  ? 8   TYR E OH  1 
ATOM   6845  N N   . ASN E  1 17  ? 23.566  29.066  39.089  1.00 10.68  ? 9   ASN E N   1 
ATOM   6846  C CA  . ASN E  1 17  ? 24.794  28.350  39.456  1.00 9.44   ? 9   ASN E CA  1 
ATOM   6847  C C   . ASN E  1 17  ? 24.575  27.335  40.596  1.00 13.42  ? 9   ASN E C   1 
ATOM   6848  O O   . ASN E  1 17  ? 24.977  26.180  40.472  1.00 13.69  ? 9   ASN E O   1 
ATOM   6849  C CB  . ASN E  1 17  ? 25.960  29.310  39.747  1.00 5.81   ? 9   ASN E CB  1 
ATOM   6850  C CG  . ASN E  1 17  ? 26.245  30.259  38.596  1.00 10.54  ? 9   ASN E CG  1 
ATOM   6851  O OD1 . ASN E  1 17  ? 26.120  29.892  37.427  1.00 15.58  ? 9   ASN E OD1 1 
ATOM   6852  N ND2 . ASN E  1 17  ? 26.628  31.483  38.916  1.00 9.32   ? 9   ASN E ND2 1 
ATOM   6853  N N   . ILE E  1 18  ? 23.918  27.744  41.685  1.00 11.10  ? 10  ILE E N   1 
ATOM   6854  C CA  . ILE E  1 18  ? 23.619  26.811  42.772  1.00 11.69  ? 10  ILE E CA  1 
ATOM   6855  C C   . ILE E  1 18  ? 22.839  25.571  42.295  1.00 15.20  ? 10  ILE E C   1 
ATOM   6856  O O   . ILE E  1 18  ? 23.261  24.438  42.534  1.00 16.10  ? 10  ILE E O   1 
ATOM   6857  C CB  . ILE E  1 18  ? 22.883  27.501  43.956  1.00 15.21  ? 10  ILE E CB  1 
ATOM   6858  C CG1 . ILE E  1 18  ? 23.831  28.470  44.668  1.00 13.80  ? 10  ILE E CG1 1 
ATOM   6859  C CG2 . ILE E  1 18  ? 22.335  26.467  44.948  1.00 9.31   ? 10  ILE E CG2 1 
ATOM   6860  C CD1 . ILE E  1 18  ? 23.144  29.434  45.587  1.00 11.34  ? 10  ILE E CD1 1 
ATOM   6861  N N   . ARG E  1 19  ? 21.722  25.771  41.603  1.00 14.34  ? 11  ARG E N   1 
ATOM   6862  C CA  . ARG E  1 19  ? 20.941  24.631  41.127  1.00 13.40  ? 11  ARG E CA  1 
ATOM   6863  C C   . ARG E  1 19  ? 21.726  23.738  40.149  1.00 16.07  ? 11  ARG E C   1 
ATOM   6864  O O   . ARG E  1 19  ? 21.517  22.522  40.097  1.00 18.58  ? 11  ARG E O   1 
ATOM   6865  C CB  . ARG E  1 19  ? 19.631  25.105  40.507  1.00 10.36  ? 11  ARG E CB  1 
ATOM   6866  C CG  . ARG E  1 19  ? 18.746  25.851  41.480  1.00 14.27  ? 11  ARG E CG  1 
ATOM   6867  C CD  . ARG E  1 19  ? 17.468  26.334  40.824  1.00 14.31  ? 11  ARG E CD  1 
ATOM   6868  N NE  . ARG E  1 19  ? 16.362  26.340  41.771  1.00 19.99  ? 11  ARG E NE  1 
ATOM   6869  C CZ  . ARG E  1 19  ? 15.275  27.101  41.657  1.00 21.01  ? 11  ARG E CZ  1 
ATOM   6870  N NH1 . ARG E  1 19  ? 15.160  27.936  40.635  1.00 15.94  ? 11  ARG E NH1 1 
ATOM   6871  N NH2 . ARG E  1 19  ? 14.306  27.030  42.573  1.00 14.64  ? 11  ARG E NH2 1 
ATOM   6872  N N   . GLN E  1 20  ? 22.642  24.326  39.387  1.00 15.30  ? 12  GLN E N   1 
ATOM   6873  C CA  . GLN E  1 20  ? 23.448  23.522  38.463  1.00 16.06  ? 12  GLN E CA  1 
ATOM   6874  C C   . GLN E  1 20  ? 24.495  22.654  39.149  1.00 14.42  ? 12  GLN E C   1 
ATOM   6875  O O   . GLN E  1 20  ? 24.768  21.552  38.696  1.00 18.69  ? 12  GLN E O   1 
ATOM   6876  C CB  . GLN E  1 20  ? 24.067  24.367  37.350  1.00 10.08  ? 12  GLN E CB  1 
ATOM   6877  C CG  . GLN E  1 20  ? 23.064  24.723  36.286  1.00 12.98  ? 12  GLN E CG  1 
ATOM   6878  C CD  . GLN E  1 20  ? 23.637  24.627  34.903  1.00 28.39  ? 12  GLN E CD  1 
ATOM   6879  O OE1 . GLN E  1 20  ? 24.776  25.041  34.654  1.00 36.55  ? 12  GLN E OE1 1 
ATOM   6880  N NE2 . GLN E  1 20  ? 22.861  24.063  33.983  1.00 35.80  ? 12  GLN E NE2 1 
ATOM   6881  N N   . THR E  1 21  ? 25.068  23.113  40.253  1.00 13.69  ? 13  THR E N   1 
ATOM   6882  C CA  . THR E  1 21  ? 26.041  22.263  40.927  1.00 15.32  ? 13  THR E CA  1 
ATOM   6883  C C   . THR E  1 21  ? 25.526  21.517  42.182  1.00 14.57  ? 13  THR E C   1 
ATOM   6884  O O   . THR E  1 21  ? 26.130  20.536  42.610  1.00 14.92  ? 13  THR E O   1 
ATOM   6885  C CB  . THR E  1 21  ? 27.392  22.986  41.186  1.00 15.92  ? 13  THR E CB  1 
ATOM   6886  O OG1 . THR E  1 21  ? 27.533  23.280  42.577  1.00 20.86  ? 13  THR E OG1 1 
ATOM   6887  C CG2 . THR E  1 21  ? 27.520  24.270  40.352  1.00 13.72  ? 13  THR E CG2 1 
ATOM   6888  N N   . SER E  1 22  ? 24.405  21.951  42.750  1.00 16.33  ? 14  SER E N   1 
ATOM   6889  C CA  . SER E  1 22  ? 23.864  21.299  43.951  1.00 13.22  ? 14  SER E CA  1 
ATOM   6890  C C   . SER E  1 22  ? 23.374  19.869  43.707  1.00 16.79  ? 14  SER E C   1 
ATOM   6891  O O   . SER E  1 22  ? 22.627  19.603  42.761  1.00 13.01  ? 14  SER E O   1 
ATOM   6892  C CB  . SER E  1 22  ? 22.728  22.129  44.549  1.00 15.66  ? 14  SER E CB  1 
ATOM   6893  O OG  . SER E  1 22  ? 21.704  21.309  45.103  1.00 15.55  ? 14  SER E OG  1 
ATOM   6894  N N   . ARG E  1 23  ? 23.802  18.955  44.571  1.00 17.97  ? 15  ARG E N   1 
ATOM   6895  C CA  . ARG E  1 23  ? 23.329  17.578  44.540  1.00 13.34  ? 15  ARG E CA  1 
ATOM   6896  C C   . ARG E  1 23  ? 22.508  17.362  45.810  1.00 13.57  ? 15  ARG E C   1 
ATOM   6897  O O   . ARG E  1 23  ? 23.050  17.022  46.848  1.00 12.92  ? 15  ARG E O   1 
ATOM   6898  C CB  . ARG E  1 23  ? 24.503  16.589  44.485  1.00 12.86  ? 15  ARG E CB  1 
ATOM   6899  C CG  . ARG E  1 23  ? 25.512  16.803  43.323  1.00 14.29  ? 15  ARG E CG  1 
ATOM   6900  C CD  . ARG E  1 23  ? 26.288  15.505  43.003  1.00 16.35  ? 15  ARG E CD  1 
ATOM   6901  N NE  . ARG E  1 23  ? 27.274  15.649  41.924  1.00 32.77  ? 15  ARG E NE  1 
ATOM   6902  C CZ  . ARG E  1 23  ? 27.203  15.067  40.722  1.00 30.12  ? 15  ARG E CZ  1 
ATOM   6903  N NH1 . ARG E  1 23  ? 26.184  14.276  40.404  1.00 25.59  ? 15  ARG E NH1 1 
ATOM   6904  N NH2 . ARG E  1 23  ? 28.166  15.274  39.828  1.00 30.86  ? 15  ARG E NH2 1 
ATOM   6905  N N   . PRO E  1 24  ? 21.189  17.565  45.723  1.00 14.02  ? 16  PRO E N   1 
ATOM   6906  C CA  . PRO E  1 24  ? 20.250  17.538  46.854  1.00 16.13  ? 16  PRO E CA  1 
ATOM   6907  C C   . PRO E  1 24  ? 20.207  16.244  47.659  1.00 13.43  ? 16  PRO E C   1 
ATOM   6908  O O   . PRO E  1 24  ? 19.749  16.277  48.802  1.00 14.60  ? 16  PRO E O   1 
ATOM   6909  C CB  . PRO E  1 24  ? 18.888  17.749  46.180  1.00 14.21  ? 16  PRO E CB  1 
ATOM   6910  C CG  . PRO E  1 24  ? 19.203  18.416  44.900  1.00 13.75  ? 16  PRO E CG  1 
ATOM   6911  C CD  . PRO E  1 24  ? 20.505  17.863  44.455  1.00 12.99  ? 16  PRO E CD  1 
ATOM   6912  N N   . ASP E  1 25  ? 20.659  15.137  47.084  1.00 12.25  ? 17  ASP E N   1 
ATOM   6913  C CA  . ASP E  1 25  ? 20.444  13.836  47.698  1.00 10.46  ? 17  ASP E CA  1 
ATOM   6914  C C   . ASP E  1 25  ? 21.731  13.189  48.129  1.00 14.69  ? 17  ASP E C   1 
ATOM   6915  O O   . ASP E  1 25  ? 21.750  11.999  48.450  1.00 20.30  ? 17  ASP E O   1 
ATOM   6916  C CB  . ASP E  1 25  ? 19.710  12.905  46.740  1.00 10.73  ? 17  ASP E CB  1 
ATOM   6917  C CG  . ASP E  1 25  ? 18.243  13.271  46.584  1.00 16.81  ? 17  ASP E CG  1 
ATOM   6918  O OD1 . ASP E  1 25  ? 17.647  13.779  47.558  1.00 23.84  ? 17  ASP E OD1 1 
ATOM   6919  O OD2 . ASP E  1 25  ? 17.676  13.055  45.493  1.00 19.45  ? 17  ASP E OD2 1 
ATOM   6920  N N   . VAL E  1 26  ? 22.806  13.970  48.140  1.00 13.38  ? 18  VAL E N   1 
ATOM   6921  C CA  . VAL E  1 26  ? 24.129  13.449  48.465  1.00 13.75  ? 18  VAL E CA  1 
ATOM   6922  C C   . VAL E  1 26  ? 24.789  14.331  49.495  1.00 10.81  ? 18  VAL E C   1 
ATOM   6923  O O   . VAL E  1 26  ? 24.806  15.542  49.334  1.00 11.52  ? 18  VAL E O   1 
ATOM   6924  C CB  . VAL E  1 26  ? 25.056  13.420  47.217  1.00 12.91  ? 18  VAL E CB  1 
ATOM   6925  C CG1 . VAL E  1 26  ? 26.398  12.801  47.572  1.00 10.92  ? 18  VAL E CG1 1 
ATOM   6926  C CG2 . VAL E  1 26  ? 24.396  12.671  46.071  1.00 10.03  ? 18  VAL E CG2 1 
ATOM   6927  N N   . ILE E  1 27  ? 25.340  13.731  50.547  1.00 13.39  ? 19  ILE E N   1 
ATOM   6928  C CA  . ILE E  1 27  ? 26.038  14.510  51.574  1.00 16.37  ? 19  ILE E CA  1 
ATOM   6929  C C   . ILE E  1 27  ? 27.228  15.288  50.994  1.00 16.14  ? 19  ILE E C   1 
ATOM   6930  O O   . ILE E  1 27  ? 28.044  14.732  50.266  1.00 17.30  ? 19  ILE E O   1 
ATOM   6931  C CB  . ILE E  1 27  ? 26.498  13.637  52.793  1.00 18.98  ? 19  ILE E CB  1 
ATOM   6932  C CG1 . ILE E  1 27  ? 27.333  12.434  52.340  1.00 18.24  ? 19  ILE E CG1 1 
ATOM   6933  C CG2 . ILE E  1 27  ? 25.309  13.175  53.613  1.00 13.61  ? 19  ILE E CG2 1 
ATOM   6934  C CD1 . ILE E  1 27  ? 27.811  11.551  53.487  1.00 14.51  ? 19  ILE E CD1 1 
ATOM   6935  N N   . PRO E  1 28  ? 27.316  16.584  51.315  1.00 13.66  ? 20  PRO E N   1 
ATOM   6936  C CA  . PRO E  1 28  ? 28.414  17.451  50.883  1.00 18.02  ? 20  PRO E CA  1 
ATOM   6937  C C   . PRO E  1 28  ? 29.658  17.258  51.738  1.00 20.94  ? 20  PRO E C   1 
ATOM   6938  O O   . PRO E  1 28  ? 30.210  18.224  52.253  1.00 25.12  ? 20  PRO E O   1 
ATOM   6939  C CB  . PRO E  1 28  ? 27.850  18.853  51.106  1.00 18.22  ? 20  PRO E CB  1 
ATOM   6940  C CG  . PRO E  1 28  ? 26.912  18.688  52.248  1.00 14.60  ? 20  PRO E CG  1 
ATOM   6941  C CD  . PRO E  1 28  ? 26.331  17.307  52.130  1.00 13.32  ? 20  PRO E CD  1 
ATOM   6942  N N   . THR E  1 29  ? 30.078  16.014  51.914  1.00 24.55  ? 21  THR E N   1 
ATOM   6943  C CA  . THR E  1 29  ? 31.337  15.750  52.579  1.00 29.32  ? 21  THR E CA  1 
ATOM   6944  C C   . THR E  1 29  ? 32.426  16.419  51.772  1.00 32.19  ? 21  THR E C   1 
ATOM   6945  O O   . THR E  1 29  ? 32.431  16.353  50.546  1.00 29.39  ? 21  THR E O   1 
ATOM   6946  C CB  . THR E  1 29  ? 31.671  14.257  52.607  1.00 30.34  ? 21  THR E CB  1 
ATOM   6947  O OG1 . THR E  1 29  ? 31.587  13.732  51.277  1.00 22.22  ? 21  THR E OG1 1 
ATOM   6948  C CG2 . THR E  1 29  ? 30.722  13.505  53.522  1.00 28.92  ? 21  THR E CG2 1 
ATOM   6949  N N   . GLN E  1 30  ? 33.342  17.069  52.474  1.00 37.06  ? 22  GLN E N   1 
ATOM   6950  C CA  . GLN E  1 30  ? 34.492  17.679  51.853  1.00 33.25  ? 22  GLN E CA  1 
ATOM   6951  C C   . GLN E  1 30  ? 35.743  16.952  52.333  1.00 41.30  ? 22  GLN E C   1 
ATOM   6952  O O   . GLN E  1 30  ? 35.895  16.692  53.531  1.00 38.35  ? 22  GLN E O   1 
ATOM   6953  C CB  . GLN E  1 30  ? 34.566  19.152  52.246  1.00 36.61  ? 22  GLN E CB  1 
ATOM   6954  C CG  . GLN E  1 30  ? 33.252  19.904  52.101  1.00 32.78  ? 22  GLN E CG  1 
ATOM   6955  C CD  . GLN E  1 30  ? 33.386  21.398  52.391  1.00 37.80  ? 22  GLN E CD  1 
ATOM   6956  O OE1 . GLN E  1 30  ? 34.486  21.911  52.623  1.00 51.21  ? 22  GLN E OE1 1 
ATOM   6957  N NE2 . GLN E  1 30  ? 32.261  22.097  52.381  1.00 32.72  ? 22  GLN E NE2 1 
ATOM   6958  N N   . ARG E  1 31  ? 36.617  16.609  51.389  1.00 45.52  ? 23  ARG E N   1 
ATOM   6959  C CA  . ARG E  1 31  ? 37.954  16.097  51.695  1.00 46.84  ? 23  ARG E CA  1 
ATOM   6960  C C   . ARG E  1 31  ? 37.973  14.880  52.620  1.00 45.74  ? 23  ARG E C   1 
ATOM   6961  O O   . ARG E  1 31  ? 38.700  14.874  53.616  1.00 45.55  ? 23  ARG E O   1 
ATOM   6962  C CB  . ARG E  1 31  ? 38.815  17.215  52.294  1.00 47.57  ? 23  ARG E CB  1 
ATOM   6963  C CG  . ARG E  1 31  ? 39.084  18.367  51.331  1.00 58.11  ? 23  ARG E CG  1 
ATOM   6964  C CD  . ARG E  1 31  ? 40.001  17.956  50.172  1.00 61.55  ? 23  ARG E CD  1 
ATOM   6965  N NE  . ARG E  1 31  ? 39.930  18.913  49.065  1.00 76.41  ? 23  ARG E NE  1 
ATOM   6966  C CZ  . ARG E  1 31  ? 40.862  19.060  48.125  1.00 64.20  ? 23  ARG E CZ  1 
ATOM   6967  N NH1 . ARG E  1 31  ? 41.962  18.315  48.151  1.00 63.57  ? 23  ARG E NH1 1 
ATOM   6968  N NH2 . ARG E  1 31  ? 40.697  19.962  47.162  1.00 41.88  ? 23  ARG E NH2 1 
ATOM   6969  N N   . ASP E  1 32  ? 37.171  13.867  52.297  1.00 41.39  ? 24  ASP E N   1 
ATOM   6970  C CA  . ASP E  1 32  ? 37.121  12.635  53.088  1.00 43.82  ? 24  ASP E CA  1 
ATOM   6971  C C   . ASP E  1 32  ? 36.822  12.841  54.594  1.00 46.26  ? 24  ASP E C   1 
ATOM   6972  O O   . ASP E  1 32  ? 37.191  12.014  55.431  1.00 40.35  ? 24  ASP E O   1 
ATOM   6973  C CB  . ASP E  1 32  ? 38.419  11.852  52.900  1.00 41.92  ? 24  ASP E CB  1 
ATOM   6974  C CG  . ASP E  1 32  ? 38.227  10.616  52.055  1.00 50.60  ? 24  ASP E CG  1 
ATOM   6975  O OD1 . ASP E  1 32  ? 37.238  9.896   52.311  1.00 45.23  ? 24  ASP E OD1 1 
ATOM   6976  O OD2 . ASP E  1 32  ? 39.051  10.368  51.139  1.00 52.64  ? 24  ASP E OD2 1 
ATOM   6977  N N   . ARG E  1 33  ? 36.154  13.943  54.923  1.00 37.05  ? 25  ARG E N   1 
ATOM   6978  C CA  . ARG E  1 33  ? 35.803  14.252  56.302  1.00 40.37  ? 25  ARG E CA  1 
ATOM   6979  C C   . ARG E  1 33  ? 34.297  14.515  56.434  1.00 36.55  ? 25  ARG E C   1 
ATOM   6980  O O   . ARG E  1 33  ? 33.687  15.118  55.547  1.00 35.26  ? 25  ARG E O   1 
ATOM   6981  C CB  . ARG E  1 33  ? 36.623  15.446  56.808  1.00 42.92  ? 25  ARG E CB  1 
ATOM   6982  C CG  . ARG E  1 33  ? 38.092  15.122  57.006  1.00 44.53  ? 25  ARG E CG  1 
ATOM   6983  C CD  . ARG E  1 33  ? 38.792  16.118  57.931  1.00 59.01  ? 25  ARG E CD  1 
ATOM   6984  N NE  . ARG E  1 33  ? 39.293  17.301  57.224  1.00 70.37  ? 25  ARG E NE  1 
ATOM   6985  C CZ  . ARG E  1 33  ? 40.235  18.119  57.696  1.00 68.99  ? 25  ARG E CZ  1 
ATOM   6986  N NH1 . ARG E  1 33  ? 40.794  17.888  58.881  1.00 68.40  ? 25  ARG E NH1 1 
ATOM   6987  N NH2 . ARG E  1 33  ? 40.622  19.169  56.984  1.00 49.48  ? 25  ARG E NH2 1 
ATOM   6988  N N   . PRO E  1 34  ? 33.690  14.054  57.538  1.00 31.14  ? 26  PRO E N   1 
ATOM   6989  C CA  . PRO E  1 34  ? 32.237  14.170  57.729  1.00 31.37  ? 26  PRO E CA  1 
ATOM   6990  C C   . PRO E  1 34  ? 31.721  15.608  57.609  1.00 28.23  ? 26  PRO E C   1 
ATOM   6991  O O   . PRO E  1 34  ? 32.440  16.558  57.922  1.00 27.80  ? 26  PRO E O   1 
ATOM   6992  C CB  . PRO E  1 34  ? 32.024  13.653  59.162  1.00 29.73  ? 26  PRO E CB  1 
ATOM   6993  C CG  . PRO E  1 34  ? 33.377  13.678  59.795  1.00 27.59  ? 26  PRO E CG  1 
ATOM   6994  C CD  . PRO E  1 34  ? 34.351  13.439  58.700  1.00 27.76  ? 26  PRO E CD  1 
ATOM   6995  N N   . VAL E  1 35  ? 30.488  15.767  57.146  1.00 21.55  ? 27  VAL E N   1 
ATOM   6996  C CA  . VAL E  1 35  ? 29.874  17.078  57.136  1.00 17.34  ? 27  VAL E CA  1 
ATOM   6997  C C   . VAL E  1 35  ? 29.653  17.533  58.577  1.00 22.09  ? 27  VAL E C   1 
ATOM   6998  O O   . VAL E  1 35  ? 29.124  16.792  59.412  1.00 21.73  ? 27  VAL E O   1 
ATOM   6999  C CB  . VAL E  1 35  ? 28.531  17.056  56.415  1.00 16.26  ? 27  VAL E CB  1 
ATOM   7000  C CG1 . VAL E  1 35  ? 28.051  18.469  56.173  1.00 14.32  ? 27  VAL E CG1 1 
ATOM   7001  C CG2 . VAL E  1 35  ? 28.658  16.309  55.114  1.00 20.99  ? 27  VAL E CG2 1 
ATOM   7002  N N   . ALA E  1 36  ? 30.066  18.755  58.868  1.00 19.95  ? 28  ALA E N   1 
ATOM   7003  C CA  . ALA E  1 36  ? 29.936  19.285  60.206  1.00 15.64  ? 28  ALA E CA  1 
ATOM   7004  C C   . ALA E  1 36  ? 28.712  20.186  60.253  1.00 17.58  ? 28  ALA E C   1 
ATOM   7005  O O   . ALA E  1 36  ? 28.765  21.339  59.826  1.00 16.61  ? 28  ALA E O   1 
ATOM   7006  C CB  . ALA E  1 36  ? 31.192  20.056  60.579  1.00 9.20   ? 28  ALA E CB  1 
ATOM   7007  N N   . VAL E  1 37  ? 27.609  19.650  60.763  1.00 15.61  ? 29  VAL E N   1 
ATOM   7008  C CA  . VAL E  1 37  ? 26.354  20.393  60.852  1.00 21.26  ? 29  VAL E CA  1 
ATOM   7009  C C   . VAL E  1 37  ? 26.153  21.065  62.217  1.00 23.07  ? 29  VAL E C   1 
ATOM   7010  O O   . VAL E  1 37  ? 26.195  20.394  63.244  1.00 23.98  ? 29  VAL E O   1 
ATOM   7011  C CB  . VAL E  1 37  ? 25.159  19.446  60.650  1.00 24.80  ? 29  VAL E CB  1 
ATOM   7012  C CG1 . VAL E  1 37  ? 23.826  20.196  60.840  1.00 18.07  ? 29  VAL E CG1 1 
ATOM   7013  C CG2 . VAL E  1 37  ? 25.248  18.752  59.298  1.00 20.34  ? 29  VAL E CG2 1 
ATOM   7014  N N   . SER E  1 38  ? 25.907  22.373  62.218  1.00 20.69  ? 30  SER E N   1 
ATOM   7015  C CA  . SER E  1 38  ? 25.619  23.118  63.444  1.00 22.41  ? 30  SER E CA  1 
ATOM   7016  C C   . SER E  1 38  ? 24.123  23.165  63.777  1.00 27.44  ? 30  SER E C   1 
ATOM   7017  O O   . SER E  1 38  ? 23.324  23.618  62.965  1.00 30.43  ? 30  SER E O   1 
ATOM   7018  C CB  . SER E  1 38  ? 26.144  24.547  63.336  1.00 17.04  ? 30  SER E CB  1 
ATOM   7019  O OG  . SER E  1 38  ? 27.519  24.609  63.672  1.00 22.95  ? 30  SER E OG  1 
ATOM   7020  N N   . VAL E  1 39  ? 23.755  22.716  64.976  1.00 24.94  ? 31  VAL E N   1 
ATOM   7021  C CA  . VAL E  1 39  ? 22.364  22.736  65.416  1.00 21.80  ? 31  VAL E CA  1 
ATOM   7022  C C   . VAL E  1 39  ? 22.186  23.453  66.749  1.00 30.19  ? 31  VAL E C   1 
ATOM   7023  O O   . VAL E  1 39  ? 22.886  23.161  67.720  1.00 34.16  ? 31  VAL E O   1 
ATOM   7024  C CB  . VAL E  1 39  ? 21.824  21.323  65.602  1.00 23.80  ? 31  VAL E CB  1 
ATOM   7025  C CG1 . VAL E  1 39  ? 20.508  21.360  66.377  1.00 25.68  ? 31  VAL E CG1 1 
ATOM   7026  C CG2 . VAL E  1 39  ? 21.650  20.642  64.259  1.00 20.59  ? 31  VAL E CG2 1 
ATOM   7027  N N   . SER E  1 40  ? 21.233  24.380  66.793  1.00 30.78  ? 32  SER E N   1 
ATOM   7028  C CA  . SER E  1 40  ? 20.917  25.105  68.010  1.00 24.94  ? 32  SER E CA  1 
ATOM   7029  C C   . SER E  1 40  ? 19.434  25.439  68.079  1.00 27.66  ? 32  SER E C   1 
ATOM   7030  O O   . SER E  1 40  ? 18.924  26.161  67.222  1.00 25.79  ? 32  SER E O   1 
ATOM   7031  C CB  . SER E  1 40  ? 21.732  26.388  68.073  1.00 34.10  ? 32  SER E CB  1 
ATOM   7032  O OG  . SER E  1 40  ? 20.918  27.473  68.473  1.00 43.00  ? 32  SER E OG  1 
ATOM   7033  N N   . LEU E  1 41  ? 18.752  24.924  69.106  1.00 29.79  ? 33  LEU E N   1 
ATOM   7034  C CA  . LEU E  1 41  ? 17.316  25.159  69.286  1.00 23.59  ? 33  LEU E CA  1 
ATOM   7035  C C   . LEU E  1 41  ? 17.041  26.447  70.050  1.00 25.56  ? 33  LEU E C   1 
ATOM   7036  O O   . LEU E  1 41  ? 17.611  26.687  71.100  1.00 36.29  ? 33  LEU E O   1 
ATOM   7037  C CB  . LEU E  1 41  ? 16.639  23.982  69.985  1.00 17.69  ? 33  LEU E CB  1 
ATOM   7038  C CG  . LEU E  1 41  ? 16.711  22.592  69.330  1.00 21.02  ? 33  LEU E CG  1 
ATOM   7039  C CD1 . LEU E  1 41  ? 15.590  21.695  69.837  1.00 23.50  ? 33  LEU E CD1 1 
ATOM   7040  C CD2 . LEU E  1 41  ? 16.663  22.665  67.815  1.00 22.61  ? 33  LEU E CD2 1 
ATOM   7041  N N   . LYS E  1 42  ? 16.175  27.281  69.495  1.00 27.47  ? 34  LYS E N   1 
ATOM   7042  C CA  . LYS E  1 42  ? 15.829  28.560  70.086  1.00 25.90  ? 34  LYS E CA  1 
ATOM   7043  C C   . LYS E  1 42  ? 14.380  28.485  70.470  1.00 26.93  ? 34  LYS E C   1 
ATOM   7044  O O   . LYS E  1 42  ? 13.510  28.558  69.608  1.00 24.22  ? 34  LYS E O   1 
ATOM   7045  C CB  . LYS E  1 42  ? 16.027  29.694  69.075  1.00 28.76  ? 34  LYS E CB  1 
ATOM   7046  C CG  . LYS E  1 42  ? 17.480  30.099  68.912  1.00 36.74  ? 34  LYS E CG  1 
ATOM   7047  C CD  . LYS E  1 42  ? 18.170  30.006  70.276  1.00 51.31  ? 34  LYS E CD  1 
ATOM   7048  C CE  . LYS E  1 42  ? 19.537  30.706  70.343  1.00 63.23  ? 34  LYS E CE  1 
ATOM   7049  N NZ  . LYS E  1 42  ? 20.038  30.846  71.765  1.00 71.61  ? 34  LYS E NZ  1 
ATOM   7050  N N   . PHE E  1 43  ? 14.106  28.327  71.760  1.00 28.30  ? 35  PHE E N   1 
ATOM   7051  C CA  . PHE E  1 43  ? 12.730  28.135  72.180  1.00 20.25  ? 35  PHE E CA  1 
ATOM   7052  C C   . PHE E  1 43  ? 11.906  29.400  72.081  1.00 20.13  ? 35  PHE E C   1 
ATOM   7053  O O   . PHE E  1 43  ? 12.348  30.463  72.488  1.00 26.90  ? 35  PHE E O   1 
ATOM   7054  C CB  . PHE E  1 43  ? 12.672  27.487  73.549  1.00 22.17  ? 35  PHE E CB  1 
ATOM   7055  C CG  . PHE E  1 43  ? 13.120  26.068  73.532  1.00 17.53  ? 35  PHE E CG  1 
ATOM   7056  C CD1 . PHE E  1 43  ? 14.428  25.739  73.815  1.00 21.76  ? 35  PHE E CD1 1 
ATOM   7057  C CD2 . PHE E  1 43  ? 12.245  25.065  73.167  1.00 17.25  ? 35  PHE E CD2 1 
ATOM   7058  C CE1 . PHE E  1 43  ? 14.849  24.424  73.775  1.00 23.89  ? 35  PHE E CE1 1 
ATOM   7059  C CE2 . PHE E  1 43  ? 12.657  23.751  73.123  1.00 18.33  ? 35  PHE E CE2 1 
ATOM   7060  C CZ  . PHE E  1 43  ? 13.959  23.427  73.427  1.00 17.88  ? 35  PHE E CZ  1 
ATOM   7061  N N   . ILE E  1 44  ? 10.721  29.265  71.489  1.00 20.64  ? 36  ILE E N   1 
ATOM   7062  C CA  . ILE E  1 44  ? 9.814   30.379  71.235  1.00 24.43  ? 36  ILE E CA  1 
ATOM   7063  C C   . ILE E  1 44  ? 8.582   30.298  72.143  1.00 26.42  ? 36  ILE E C   1 
ATOM   7064  O O   . ILE E  1 44  ? 8.069   31.323  72.602  1.00 28.48  ? 36  ILE E O   1 
ATOM   7065  C CB  . ILE E  1 44  ? 9.309   30.390  69.771  1.00 22.27  ? 36  ILE E CB  1 
ATOM   7066  C CG1 . ILE E  1 44  ? 10.476  30.350  68.780  1.00 22.79  ? 36  ILE E CG1 1 
ATOM   7067  C CG2 . ILE E  1 44  ? 8.426   31.606  69.524  1.00 20.90  ? 36  ILE E CG2 1 
ATOM   7068  C CD1 . ILE E  1 44  ? 11.226  31.657  68.643  1.00 23.88  ? 36  ILE E CD1 1 
ATOM   7069  N N   . ASN E  1 45  ? 8.104   29.083  72.402  1.00 19.56  ? 37  ASN E N   1 
ATOM   7070  C CA  . ASN E  1 45  ? 6.895   28.924  73.193  1.00 18.79  ? 37  ASN E CA  1 
ATOM   7071  C C   . ASN E  1 45  ? 6.695   27.501  73.652  1.00 19.72  ? 37  ASN E C   1 
ATOM   7072  O O   . ASN E  1 45  ? 7.221   26.577  73.055  1.00 20.91  ? 37  ASN E O   1 
ATOM   7073  C CB  . ASN E  1 45  ? 5.679   29.366  72.390  1.00 23.51  ? 37  ASN E CB  1 
ATOM   7074  C CG  . ASN E  1 45  ? 4.591   29.970  73.261  1.00 29.95  ? 37  ASN E CG  1 
ATOM   7075  O OD1 . ASN E  1 45  ? 4.504   29.689  74.465  1.00 21.53  ? 37  ASN E OD1 1 
ATOM   7076  N ND2 . ASN E  1 45  ? 3.745   30.804  72.650  1.00 27.79  ? 37  ASN E ND2 1 
ATOM   7077  N N   . ILE E  1 46  ? 5.934   27.334  74.729  1.00 24.34  ? 38  ILE E N   1 
ATOM   7078  C CA  . ILE E  1 46  ? 5.582   26.018  75.258  1.00 19.95  ? 38  ILE E CA  1 
ATOM   7079  C C   . ILE E  1 46  ? 4.074   26.077  75.453  1.00 19.01  ? 38  ILE E C   1 
ATOM   7080  O O   . ILE E  1 46  ? 3.586   26.948  76.148  1.00 27.10  ? 38  ILE E O   1 
ATOM   7081  C CB  . ILE E  1 46  ? 6.337   25.732  76.591  1.00 20.72  ? 38  ILE E CB  1 
ATOM   7082  C CG1 . ILE E  1 46  ? 7.853   25.886  76.388  1.00 20.31  ? 38  ILE E CG1 1 
ATOM   7083  C CG2 . ILE E  1 46  ? 6.008   24.354  77.135  1.00 21.76  ? 38  ILE E CG2 1 
ATOM   7084  C CD1 . ILE E  1 46  ? 8.699   25.539  77.587  1.00 20.76  ? 38  ILE E CD1 1 
ATOM   7085  N N   . LEU E  1 47  ? 3.333   25.179  74.820  1.00 18.02  ? 39  LEU E N   1 
ATOM   7086  C CA  . LEU E  1 47  ? 1.887   25.353  74.691  1.00 21.33  ? 39  LEU E CA  1 
ATOM   7087  C C   . LEU E  1 47  ? 1.017   24.445  75.582  1.00 27.97  ? 39  LEU E C   1 
ATOM   7088  O O   . LEU E  1 47  ? 0.078   24.912  76.219  1.00 28.21  ? 39  LEU E O   1 
ATOM   7089  C CB  . LEU E  1 47  ? 1.472   25.129  73.239  1.00 25.01  ? 39  LEU E CB  1 
ATOM   7090  C CG  . LEU E  1 47  ? 2.237   25.790  72.093  1.00 24.79  ? 39  LEU E CG  1 
ATOM   7091  C CD1 . LEU E  1 47  ? 1.650   25.285  70.817  1.00 20.79  ? 39  LEU E CD1 1 
ATOM   7092  C CD2 . LEU E  1 47  ? 2.165   27.317  72.135  1.00 26.43  ? 39  LEU E CD2 1 
ATOM   7093  N N   . GLU E  1 48  ? 1.295   23.143  75.561  1.00 32.16  ? 40  GLU E N   1 
ATOM   7094  C CA  . GLU E  1 48  ? 0.553   22.150  76.329  1.00 24.44  ? 40  GLU E CA  1 
ATOM   7095  C C   . GLU E  1 48  ? 1.604   21.352  77.059  1.00 25.90  ? 40  GLU E C   1 
ATOM   7096  O O   . GLU E  1 48  ? 2.644   21.019  76.501  1.00 30.78  ? 40  GLU E O   1 
ATOM   7097  C CB  . GLU E  1 48  ? -0.235  21.172  75.432  1.00 29.65  ? 40  GLU E CB  1 
ATOM   7098  C CG  . GLU E  1 48  ? -1.287  21.774  74.486  1.00 45.20  ? 40  GLU E CG  1 
ATOM   7099  C CD  . GLU E  1 48  ? -1.721  20.811  73.351  1.00 49.93  ? 40  GLU E CD  1 
ATOM   7100  O OE1 . GLU E  1 48  ? -1.519  19.579  73.474  1.00 45.16  ? 40  GLU E OE1 1 
ATOM   7101  O OE2 . GLU E  1 48  ? -2.267  21.294  72.331  1.00 43.42  ? 40  GLU E OE2 1 
ATOM   7102  N N   . VAL E  1 49  ? 1.320   21.031  78.306  1.00 27.14  ? 41  VAL E N   1 
ATOM   7103  C CA  . VAL E  1 49  ? 2.204   20.235  79.120  1.00 22.83  ? 41  VAL E CA  1 
ATOM   7104  C C   . VAL E  1 49  ? 1.305   19.287  79.896  1.00 22.86  ? 41  VAL E C   1 
ATOM   7105  O O   . VAL E  1 49  ? 0.252   19.684  80.381  1.00 22.54  ? 41  VAL E O   1 
ATOM   7106  C CB  . VAL E  1 49  ? 2.998   21.145  80.067  1.00 25.93  ? 41  VAL E CB  1 
ATOM   7107  C CG1 . VAL E  1 49  ? 3.170   20.504  81.420  1.00 29.86  ? 41  VAL E CG1 1 
ATOM   7108  C CG2 . VAL E  1 49  ? 4.332   21.524  79.447  1.00 24.79  ? 41  VAL E CG2 1 
ATOM   7109  N N   . ASN E  1 50  ? 1.690   18.025  79.975  1.00 26.05  ? 42  ASN E N   1 
ATOM   7110  C CA  . ASN E  1 50  ? 0.894   17.053  80.700  1.00 22.10  ? 42  ASN E CA  1 
ATOM   7111  C C   . ASN E  1 50  ? 1.810   16.264  81.613  1.00 28.78  ? 42  ASN E C   1 
ATOM   7112  O O   . ASN E  1 50  ? 2.575   15.406  81.154  1.00 28.00  ? 42  ASN E O   1 
ATOM   7113  C CB  . ASN E  1 50  ? 0.153   16.134  79.732  1.00 23.86  ? 42  ASN E CB  1 
ATOM   7114  C CG  . ASN E  1 50  ? -0.882  15.268  80.424  1.00 25.61  ? 42  ASN E CG  1 
ATOM   7115  O OD1 . ASN E  1 50  ? -0.659  14.780  81.529  1.00 26.73  ? 42  ASN E OD1 1 
ATOM   7116  N ND2 . ASN E  1 50  ? -2.024  15.071  79.772  1.00 19.67  ? 42  ASN E ND2 1 
ATOM   7117  N N   . GLU E  1 51  ? 1.739   16.578  82.906  1.00 30.27  ? 43  GLU E N   1 
ATOM   7118  C CA  . GLU E  1 51  ? 2.620   15.979  83.906  1.00 31.87  ? 43  GLU E CA  1 
ATOM   7119  C C   . GLU E  1 51  ? 2.217   14.529  84.168  1.00 28.72  ? 43  GLU E C   1 
ATOM   7120  O O   . GLU E  1 51  ? 3.013   13.740  84.681  1.00 27.83  ? 43  GLU E O   1 
ATOM   7121  C CB  . GLU E  1 51  ? 2.611   16.799  85.202  1.00 33.34  ? 43  GLU E CB  1 
ATOM   7122  C CG  . GLU E  1 51  ? 3.714   16.433  86.201  1.00 40.08  ? 43  GLU E CG  1 
ATOM   7123  C CD  . GLU E  1 51  ? 3.573   17.163  87.541  1.00 49.11  ? 43  GLU E CD  1 
ATOM   7124  O OE1 . GLU E  1 51  ? 2.799   18.148  87.603  1.00 46.32  ? 43  GLU E OE1 1 
ATOM   7125  O OE2 . GLU E  1 51  ? 4.236   16.751  88.528  1.00 48.93  ? 43  GLU E OE2 1 
ATOM   7126  N N   . ILE E  1 52  ? 0.986   14.190  83.788  1.00 24.39  ? 44  ILE E N   1 
ATOM   7127  C CA  . ILE E  1 52  ? 0.476   12.832  83.917  1.00 23.43  ? 44  ILE E CA  1 
ATOM   7128  C C   . ILE E  1 52  ? 1.022   11.926  82.820  1.00 27.50  ? 44  ILE E C   1 
ATOM   7129  O O   . ILE E  1 52  ? 1.531   10.843  83.100  1.00 30.31  ? 44  ILE E O   1 
ATOM   7130  C CB  . ILE E  1 52  ? -1.061  12.807  83.876  1.00 25.91  ? 44  ILE E CB  1 
ATOM   7131  C CG1 . ILE E  1 52  ? -1.638  13.591  85.058  1.00 29.92  ? 44  ILE E CG1 1 
ATOM   7132  C CG2 . ILE E  1 52  ? -1.572  11.381  83.863  1.00 22.89  ? 44  ILE E CG2 1 
ATOM   7133  C CD1 . ILE E  1 52  ? -3.138  13.694  85.044  1.00 29.92  ? 44  ILE E CD1 1 
ATOM   7134  N N   . THR E  1 53  ? 0.924   12.366  81.568  1.00 31.63  ? 45  THR E N   1 
ATOM   7135  C CA  . THR E  1 53  ? 1.389   11.543  80.446  1.00 32.26  ? 45  THR E CA  1 
ATOM   7136  C C   . THR E  1 53  ? 2.819   11.872  80.033  1.00 25.19  ? 45  THR E C   1 
ATOM   7137  O O   . THR E  1 53  ? 3.378   11.219  79.154  1.00 25.17  ? 45  THR E O   1 
ATOM   7138  C CB  . THR E  1 53  ? 0.465   11.642  79.212  1.00 29.84  ? 45  THR E CB  1 
ATOM   7139  O OG1 . THR E  1 53  ? 0.477   12.985  78.708  1.00 31.33  ? 45  THR E OG1 1 
ATOM   7140  C CG2 . THR E  1 53  ? -0.961  11.227  79.570  1.00 21.66  ? 45  THR E CG2 1 
ATOM   7141  N N   . ASN E  1 54  ? 3.404   12.876  80.675  1.00 23.65  ? 46  ASN E N   1 
ATOM   7142  C CA  . ASN E  1 54  ? 4.789   13.243  80.404  1.00 30.27  ? 46  ASN E CA  1 
ATOM   7143  C C   . ASN E  1 54  ? 5.007   13.683  78.952  1.00 28.01  ? 46  ASN E C   1 
ATOM   7144  O O   . ASN E  1 54  ? 5.954   13.268  78.295  1.00 29.45  ? 46  ASN E O   1 
ATOM   7145  C CB  . ASN E  1 54  ? 5.727   12.094  80.780  1.00 29.38  ? 46  ASN E CB  1 
ATOM   7146  C CG  . ASN E  1 54  ? 6.423   12.327  82.096  1.00 32.04  ? 46  ASN E CG  1 
ATOM   7147  O OD1 . ASN E  1 54  ? 6.830   13.447  82.397  1.00 32.73  ? 46  ASN E OD1 1 
ATOM   7148  N ND2 . ASN E  1 54  ? 6.561   11.273  82.895  1.00 34.58  ? 46  ASN E ND2 1 
ATOM   7149  N N   . GLU E  1 55  ? 4.102   14.520  78.465  1.00 28.55  ? 47  GLU E N   1 
ATOM   7150  C CA  . GLU E  1 55  ? 4.118   14.970  77.086  1.00 25.92  ? 47  GLU E CA  1 
ATOM   7151  C C   . GLU E  1 55  ? 4.109   16.488  77.009  1.00 25.89  ? 47  GLU E C   1 
ATOM   7152  O O   . GLU E  1 55  ? 3.524   17.169  77.849  1.00 28.09  ? 47  GLU E O   1 
ATOM   7153  C CB  . GLU E  1 55  ? 2.919   14.410  76.337  1.00 24.35  ? 47  GLU E CB  1 
ATOM   7154  C CG  . GLU E  1 55  ? 2.995   12.931  76.094  1.00 27.08  ? 47  GLU E CG  1 
ATOM   7155  C CD  . GLU E  1 55  ? 1.694   12.380  75.568  1.00 35.46  ? 47  GLU E CD  1 
ATOM   7156  O OE1 . GLU E  1 55  ? 0.718   13.164  75.467  1.00 42.05  ? 47  GLU E OE1 1 
ATOM   7157  O OE2 . GLU E  1 55  ? 1.645   11.166  75.269  1.00 30.82  ? 47  GLU E OE2 1 
ATOM   7158  N N   . VAL E  1 56  ? 4.738   17.006  75.967  1.00 26.87  ? 48  VAL E N   1 
ATOM   7159  C CA  . VAL E  1 56  ? 5.051   18.418  75.871  1.00 26.69  ? 48  VAL E CA  1 
ATOM   7160  C C   . VAL E  1 56  ? 4.897   18.892  74.419  1.00 26.16  ? 48  VAL E C   1 
ATOM   7161  O O   . VAL E  1 56  ? 5.339   18.221  73.496  1.00 25.82  ? 48  VAL E O   1 
ATOM   7162  C CB  . VAL E  1 56  ? 6.483   18.649  76.403  1.00 22.64  ? 48  VAL E CB  1 
ATOM   7163  C CG1 . VAL E  1 56  ? 7.226   19.675  75.594  1.00 27.43  ? 48  VAL E CG1 1 
ATOM   7164  C CG2 . VAL E  1 56  ? 6.432   19.043  77.842  1.00 27.05  ? 48  VAL E CG2 1 
ATOM   7165  N N   . ASP E  1 57  ? 4.255   20.039  74.228  1.00 25.87  ? 49  ASP E N   1 
ATOM   7166  C CA  . ASP E  1 57  ? 4.000   20.600  72.902  1.00 20.34  ? 49  ASP E CA  1 
ATOM   7167  C C   . ASP E  1 57  ? 4.736   21.937  72.818  1.00 24.32  ? 49  ASP E C   1 
ATOM   7168  O O   . ASP E  1 57  ? 4.379   22.889  73.508  1.00 27.30  ? 49  ASP E O   1 
ATOM   7169  C CB  . ASP E  1 57  ? 2.492   20.800  72.736  1.00 27.49  ? 49  ASP E CB  1 
ATOM   7170  C CG  . ASP E  1 57  ? 2.073   21.049  71.296  1.00 33.17  ? 49  ASP E CG  1 
ATOM   7171  O OD1 . ASP E  1 57  ? 2.950   21.125  70.427  1.00 30.79  ? 49  ASP E OD1 1 
ATOM   7172  O OD2 . ASP E  1 57  ? 0.854   21.181  71.033  1.00 39.88  ? 49  ASP E OD2 1 
ATOM   7173  N N   . VAL E  1 58  ? 5.776   22.008  71.992  1.00 24.07  ? 50  VAL E N   1 
ATOM   7174  C CA  . VAL E  1 58  ? 6.635   23.188  71.951  1.00 20.22  ? 50  VAL E CA  1 
ATOM   7175  C C   . VAL E  1 58  ? 6.777   23.805  70.568  1.00 22.51  ? 50  VAL E C   1 
ATOM   7176  O O   . VAL E  1 58  ? 6.510   23.165  69.556  1.00 23.40  ? 50  VAL E O   1 
ATOM   7177  C CB  . VAL E  1 58  ? 8.047   22.860  72.438  1.00 17.33  ? 50  VAL E CB  1 
ATOM   7178  C CG1 . VAL E  1 58  ? 8.103   22.924  73.926  1.00 26.90  ? 50  VAL E CG1 1 
ATOM   7179  C CG2 . VAL E  1 58  ? 8.436   21.492  71.976  1.00 19.42  ? 50  VAL E CG2 1 
ATOM   7180  N N   . VAL E  1 59  ? 7.215   25.060  70.556  1.00 21.24  ? 51  VAL E N   1 
ATOM   7181  C CA  . VAL E  1 59  ? 7.528   25.802  69.349  1.00 16.72  ? 51  VAL E CA  1 
ATOM   7182  C C   . VAL E  1 59  ? 8.951   26.327  69.494  1.00 18.65  ? 51  VAL E C   1 
ATOM   7183  O O   . VAL E  1 59  ? 9.284   26.975  70.486  1.00 17.40  ? 51  VAL E O   1 
ATOM   7184  C CB  . VAL E  1 59  ? 6.570   26.996  69.145  1.00 14.63  ? 51  VAL E CB  1 
ATOM   7185  C CG1 . VAL E  1 59  ? 7.103   27.923  68.078  1.00 16.68  ? 51  VAL E CG1 1 
ATOM   7186  C CG2 . VAL E  1 59  ? 5.188   26.514  68.775  1.00 15.96  ? 51  VAL E CG2 1 
ATOM   7187  N N   . PHE E  1 60  ? 9.792   26.050  68.505  1.00 19.72  ? 52  PHE E N   1 
ATOM   7188  C CA  . PHE E  1 60  ? 11.176  26.506  68.550  1.00 22.34  ? 52  PHE E CA  1 
ATOM   7189  C C   . PHE E  1 60  ? 11.703  26.839  67.151  1.00 22.31  ? 52  PHE E C   1 
ATOM   7190  O O   . PHE E  1 60  ? 11.217  26.318  66.149  1.00 21.85  ? 52  PHE E O   1 
ATOM   7191  C CB  . PHE E  1 60  ? 12.058  25.456  69.234  1.00 17.69  ? 52  PHE E CB  1 
ATOM   7192  C CG  . PHE E  1 60  ? 11.965  24.100  68.612  1.00 17.08  ? 52  PHE E CG  1 
ATOM   7193  C CD1 . PHE E  1 60  ? 12.900  23.684  67.677  1.00 24.50  ? 52  PHE E CD1 1 
ATOM   7194  C CD2 . PHE E  1 60  ? 10.940  23.246  68.940  1.00 16.98  ? 52  PHE E CD2 1 
ATOM   7195  C CE1 . PHE E  1 60  ? 12.813  22.431  67.086  1.00 19.09  ? 52  PHE E CE1 1 
ATOM   7196  C CE2 . PHE E  1 60  ? 10.847  21.993  68.353  1.00 22.37  ? 52  PHE E CE2 1 
ATOM   7197  C CZ  . PHE E  1 60  ? 11.786  21.587  67.421  1.00 17.04  ? 52  PHE E CZ  1 
ATOM   7198  N N   . TRP E  1 61  ? 12.672  27.741  67.090  1.00 23.32  ? 53  TRP E N   1 
ATOM   7199  C CA  . TRP E  1 61  ? 13.411  27.979  65.864  1.00 21.01  ? 53  TRP E CA  1 
ATOM   7200  C C   . TRP E  1 61  ? 14.597  27.047  65.889  1.00 23.74  ? 53  TRP E C   1 
ATOM   7201  O O   . TRP E  1 61  ? 15.390  27.065  66.832  1.00 21.35  ? 53  TRP E O   1 
ATOM   7202  C CB  . TRP E  1 61  ? 13.894  29.422  65.782  1.00 21.98  ? 53  TRP E CB  1 
ATOM   7203  C CG  . TRP E  1 61  ? 12.784  30.412  65.598  1.00 27.02  ? 53  TRP E CG  1 
ATOM   7204  C CD1 . TRP E  1 61  ? 11.458  30.134  65.366  1.00 29.27  ? 53  TRP E CD1 1 
ATOM   7205  C CD2 . TRP E  1 61  ? 12.894  31.843  65.630  1.00 32.24  ? 53  TRP E CD2 1 
ATOM   7206  N NE1 . TRP E  1 61  ? 10.736  31.308  65.256  1.00 31.34  ? 53  TRP E NE1 1 
ATOM   7207  C CE2 . TRP E  1 61  ? 11.591  32.370  65.408  1.00 33.91  ? 53  TRP E CE2 1 
ATOM   7208  C CE3 . TRP E  1 61  ? 13.960  32.733  65.831  1.00 31.32  ? 53  TRP E CE3 1 
ATOM   7209  C CZ2 . TRP E  1 61  ? 11.332  33.744  65.384  1.00 32.06  ? 53  TRP E CZ2 1 
ATOM   7210  C CZ3 . TRP E  1 61  ? 13.704  34.097  65.791  1.00 39.71  ? 53  TRP E CZ3 1 
ATOM   7211  C CH2 . TRP E  1 61  ? 12.397  34.588  65.573  1.00 40.10  ? 53  TRP E CH2 1 
ATOM   7212  N N   . GLN E  1 62  ? 14.714  26.223  64.852  1.00 24.77  ? 54  GLN E N   1 
ATOM   7213  C CA  . GLN E  1 62  ? 15.808  25.270  64.765  1.00 19.71  ? 54  GLN E CA  1 
ATOM   7214  C C   . GLN E  1 62  ? 16.923  25.843  63.914  1.00 18.88  ? 54  GLN E C   1 
ATOM   7215  O O   . GLN E  1 62  ? 16.824  25.844  62.701  1.00 22.19  ? 54  GLN E O   1 
ATOM   7216  C CB  . GLN E  1 62  ? 15.308  23.952  64.179  1.00 17.54  ? 54  GLN E CB  1 
ATOM   7217  C CG  . GLN E  1 62  ? 16.352  22.861  64.164  1.00 21.00  ? 54  GLN E CG  1 
ATOM   7218  C CD  . GLN E  1 62  ? 15.898  21.643  63.394  1.00 28.82  ? 54  GLN E CD  1 
ATOM   7219  O OE1 . GLN E  1 62  ? 14.847  21.070  63.681  1.00 32.38  ? 54  GLN E OE1 1 
ATOM   7220  N NE2 . GLN E  1 62  ? 16.690  21.239  62.401  1.00 26.28  ? 54  GLN E NE2 1 
ATOM   7221  N N   . GLN E  1 63  ? 17.976  26.354  64.542  1.00 23.11  ? 55  GLN E N   1 
ATOM   7222  C CA  . GLN E  1 63  ? 19.084  26.911  63.775  1.00 22.99  ? 55  GLN E CA  1 
ATOM   7223  C C   . GLN E  1 63  ? 19.966  25.795  63.283  1.00 22.67  ? 55  GLN E C   1 
ATOM   7224  O O   . GLN E  1 63  ? 20.477  25.007  64.071  1.00 22.62  ? 55  GLN E O   1 
ATOM   7225  C CB  . GLN E  1 63  ? 19.913  27.895  64.588  1.00 28.67  ? 55  GLN E CB  1 
ATOM   7226  C CG  . GLN E  1 63  ? 19.586  29.345  64.308  1.00 38.29  ? 55  GLN E CG  1 
ATOM   7227  C CD  . GLN E  1 63  ? 20.828  30.226  64.219  1.00 58.90  ? 55  GLN E CD  1 
ATOM   7228  O OE1 . GLN E  1 63  ? 21.831  29.980  64.897  1.00 50.19  ? 55  GLN E OE1 1 
ATOM   7229  N NE2 . GLN E  1 63  ? 20.767  31.255  63.370  1.00 63.49  ? 55  GLN E NE2 1 
ATOM   7230  N N   . THR E  1 64  ? 20.145  25.736  61.969  1.00 21.99  ? 56  THR E N   1 
ATOM   7231  C CA  . THR E  1 64  ? 20.918  24.670  61.354  1.00 19.45  ? 56  THR E CA  1 
ATOM   7232  C C   . THR E  1 64  ? 21.867  25.247  60.316  1.00 19.50  ? 56  THR E C   1 
ATOM   7233  O O   . THR E  1 64  ? 21.425  25.895  59.370  1.00 20.77  ? 56  THR E O   1 
ATOM   7234  C CB  . THR E  1 64  ? 19.985  23.644  60.707  1.00 17.59  ? 56  THR E CB  1 
ATOM   7235  O OG1 . THR E  1 64  ? 18.907  23.355  61.610  1.00 26.29  ? 56  THR E OG1 1 
ATOM   7236  C CG2 . THR E  1 64  ? 20.717  22.377  60.412  1.00 17.07  ? 56  THR E CG2 1 
ATOM   7237  N N   . THR E  1 65  ? 23.171  25.050  60.496  1.00 17.00  ? 57  THR E N   1 
ATOM   7238  C CA  . THR E  1 65  ? 24.112  25.473  59.466  1.00 18.37  ? 57  THR E CA  1 
ATOM   7239  C C   . THR E  1 65  ? 25.142  24.400  59.116  1.00 21.94  ? 57  THR E C   1 
ATOM   7240  O O   . THR E  1 65  ? 25.404  23.489  59.900  1.00 23.04  ? 57  THR E O   1 
ATOM   7241  C CB  . THR E  1 65  ? 24.838  26.791  59.815  1.00 21.65  ? 57  THR E CB  1 
ATOM   7242  O OG1 . THR E  1 65  ? 25.760  26.564  60.881  1.00 29.55  ? 57  THR E OG1 1 
ATOM   7243  C CG2 . THR E  1 65  ? 23.856  27.868  60.222  1.00 19.72  ? 57  THR E CG2 1 
ATOM   7244  N N   . TRP E  1 66  ? 25.716  24.519  57.922  1.00 19.86  ? 58  TRP E N   1 
ATOM   7245  C CA  . TRP E  1 66  ? 26.730  23.589  57.446  1.00 19.94  ? 58  TRP E CA  1 
ATOM   7246  C C   . TRP E  1 66  ? 27.452  24.193  56.247  1.00 19.62  ? 58  TRP E C   1 
ATOM   7247  O O   . TRP E  1 66  ? 27.153  25.321  55.845  1.00 22.10  ? 58  TRP E O   1 
ATOM   7248  C CB  . TRP E  1 66  ? 26.099  22.241  57.077  1.00 23.58  ? 58  TRP E CB  1 
ATOM   7249  C CG  . TRP E  1 66  ? 25.094  22.315  55.954  1.00 23.90  ? 58  TRP E CG  1 
ATOM   7250  C CD1 . TRP E  1 66  ? 25.339  22.181  54.614  1.00 19.26  ? 58  TRP E CD1 1 
ATOM   7251  C CD2 . TRP E  1 66  ? 23.691  22.547  56.082  1.00 20.17  ? 58  TRP E CD2 1 
ATOM   7252  N NE1 . TRP E  1 66  ? 24.175  22.315  53.905  1.00 17.57  ? 58  TRP E NE1 1 
ATOM   7253  C CE2 . TRP E  1 66  ? 23.146  22.535  54.783  1.00 17.90  ? 58  TRP E CE2 1 
ATOM   7254  C CE3 . TRP E  1 66  ? 22.843  22.757  57.169  1.00 13.68  ? 58  TRP E CE3 1 
ATOM   7255  C CZ2 . TRP E  1 66  ? 21.793  22.723  54.544  1.00 11.85  ? 58  TRP E CZ2 1 
ATOM   7256  C CZ3 . TRP E  1 66  ? 21.513  22.943  56.928  1.00 16.51  ? 58  TRP E CZ3 1 
ATOM   7257  C CH2 . TRP E  1 66  ? 20.996  22.925  55.623  1.00 14.25  ? 58  TRP E CH2 1 
ATOM   7258  N N   . SER E  1 67  ? 28.395  23.461  55.666  1.00 18.58  ? 59  SER E N   1 
ATOM   7259  C CA  . SER E  1 67  ? 29.124  24.012  54.522  1.00 24.63  ? 59  SER E CA  1 
ATOM   7260  C C   . SER E  1 67  ? 29.108  23.119  53.298  1.00 22.69  ? 59  SER E C   1 
ATOM   7261  O O   . SER E  1 67  ? 29.171  21.891  53.401  1.00 19.69  ? 59  SER E O   1 
ATOM   7262  C CB  . SER E  1 67  ? 30.571  24.332  54.895  1.00 23.52  ? 59  SER E CB  1 
ATOM   7263  O OG  . SER E  1 67  ? 30.614  25.035  56.125  1.00 41.07  ? 59  SER E OG  1 
ATOM   7264  N N   . ASP E  1 68  ? 29.020  23.765  52.139  1.00 24.45  ? 60  ASP E N   1 
ATOM   7265  C CA  . ASP E  1 68  ? 29.231  23.118  50.846  1.00 22.45  ? 60  ASP E CA  1 
ATOM   7266  C C   . ASP E  1 68  ? 30.005  24.095  49.990  1.00 18.47  ? 60  ASP E C   1 
ATOM   7267  O O   . ASP E  1 68  ? 29.429  24.999  49.397  1.00 21.87  ? 60  ASP E O   1 
ATOM   7268  C CB  . ASP E  1 68  ? 27.901  22.794  50.174  1.00 20.03  ? 60  ASP E CB  1 
ATOM   7269  C CG  . ASP E  1 68  ? 28.056  21.813  49.033  1.00 29.56  ? 60  ASP E CG  1 
ATOM   7270  O OD1 . ASP E  1 68  ? 29.206  21.635  48.540  1.00 24.25  ? 60  ASP E OD1 1 
ATOM   7271  O OD2 . ASP E  1 68  ? 27.025  21.216  48.635  1.00 28.51  ? 60  ASP E OD2 1 
ATOM   7272  N N   . ARG E  1 69  ? 31.317  23.925  49.939  1.00 23.90  ? 61  ARG E N   1 
ATOM   7273  C CA  . ARG E  1 69  ? 32.192  24.916  49.316  1.00 26.44  ? 61  ARG E CA  1 
ATOM   7274  C C   . ARG E  1 69  ? 31.995  25.003  47.802  1.00 23.79  ? 61  ARG E C   1 
ATOM   7275  O O   . ARG E  1 69  ? 32.292  26.026  47.184  1.00 23.08  ? 61  ARG E O   1 
ATOM   7276  C CB  . ARG E  1 69  ? 33.657  24.642  49.677  1.00 27.91  ? 61  ARG E CB  1 
ATOM   7277  C CG  . ARG E  1 69  ? 33.899  24.538  51.184  1.00 29.77  ? 61  ARG E CG  1 
ATOM   7278  C CD  . ARG E  1 69  ? 35.073  25.384  51.667  1.00 36.05  ? 61  ARG E CD  1 
ATOM   7279  N NE  . ARG E  1 69  ? 34.752  26.812  51.769  1.00 39.69  ? 61  ARG E NE  1 
ATOM   7280  C CZ  . ARG E  1 69  ? 34.973  27.710  50.807  1.00 39.42  ? 61  ARG E CZ  1 
ATOM   7281  N NH1 . ARG E  1 69  ? 35.509  27.335  49.648  1.00 35.50  ? 61  ARG E NH1 1 
ATOM   7282  N NH2 . ARG E  1 69  ? 34.659  28.990  50.998  1.00 29.94  ? 61  ARG E NH2 1 
ATOM   7283  N N   . THR E  1 70  ? 31.462  23.935  47.219  1.00 22.80  ? 62  THR E N   1 
ATOM   7284  C CA  . THR E  1 70  ? 31.153  23.908  45.799  1.00 19.07  ? 62  THR E CA  1 
ATOM   7285  C C   . THR E  1 70  ? 30.027  24.881  45.434  1.00 21.45  ? 62  THR E C   1 
ATOM   7286  O O   . THR E  1 70  ? 29.772  25.122  44.252  1.00 22.26  ? 62  THR E O   1 
ATOM   7287  C CB  . THR E  1 70  ? 30.769  22.488  45.320  1.00 18.94  ? 62  THR E CB  1 
ATOM   7288  O OG1 . THR E  1 70  ? 29.439  22.186  45.740  1.00 22.71  ? 62  THR E OG1 1 
ATOM   7289  C CG2 . THR E  1 70  ? 31.735  21.425  45.864  1.00 15.51  ? 62  THR E CG2 1 
ATOM   7290  N N   . LEU E  1 71  ? 29.348  25.436  46.436  1.00 19.29  ? 63  LEU E N   1 
ATOM   7291  C CA  . LEU E  1 71  ? 28.309  26.435  46.177  1.00 19.29  ? 63  LEU E CA  1 
ATOM   7292  C C   . LEU E  1 71  ? 28.875  27.863  46.202  1.00 17.39  ? 63  LEU E C   1 
ATOM   7293  O O   . LEU E  1 71  ? 28.200  28.820  45.838  1.00 15.73  ? 63  LEU E O   1 
ATOM   7294  C CB  . LEU E  1 71  ? 27.142  26.288  47.166  1.00 17.82  ? 63  LEU E CB  1 
ATOM   7295  C CG  . LEU E  1 71  ? 26.541  24.880  47.288  1.00 23.23  ? 63  LEU E CG  1 
ATOM   7296  C CD1 . LEU E  1 71  ? 25.250  24.842  48.126  1.00 10.78  ? 63  LEU E CD1 1 
ATOM   7297  C CD2 . LEU E  1 71  ? 26.313  24.260  45.912  1.00 18.40  ? 63  LEU E CD2 1 
ATOM   7298  N N   . ALA E  1 72  ? 30.124  27.991  46.626  1.00 20.37  ? 64  ALA E N   1 
ATOM   7299  C CA  . ALA E  1 72  ? 30.745  29.296  46.807  1.00 18.12  ? 64  ALA E CA  1 
ATOM   7300  C C   . ALA E  1 72  ? 30.954  29.992  45.483  1.00 19.58  ? 64  ALA E C   1 
ATOM   7301  O O   . ALA E  1 72  ? 31.271  29.363  44.483  1.00 21.37  ? 64  ALA E O   1 
ATOM   7302  C CB  . ALA E  1 72  ? 32.075  29.152  47.523  1.00 19.59  ? 64  ALA E CB  1 
ATOM   7303  N N   . TRP E  1 73  ? 30.790  31.302  45.482  1.00 20.67  ? 65  TRP E N   1 
ATOM   7304  C CA  . TRP E  1 73  ? 31.068  32.071  44.294  1.00 16.97  ? 65  TRP E CA  1 
ATOM   7305  C C   . TRP E  1 73  ? 31.872  33.310  44.665  1.00 19.10  ? 65  TRP E C   1 
ATOM   7306  O O   . TRP E  1 73  ? 32.161  33.538  45.831  1.00 20.94  ? 65  TRP E O   1 
ATOM   7307  C CB  . TRP E  1 73  ? 29.767  32.424  43.569  1.00 17.71  ? 65  TRP E CB  1 
ATOM   7308  C CG  . TRP E  1 73  ? 28.876  33.382  44.295  1.00 19.72  ? 65  TRP E CG  1 
ATOM   7309  C CD1 . TRP E  1 73  ? 28.797  34.730  44.099  1.00 20.78  ? 65  TRP E CD1 1 
ATOM   7310  C CD2 . TRP E  1 73  ? 27.909  33.066  45.309  1.00 17.00  ? 65  TRP E CD2 1 
ATOM   7311  N NE1 . TRP E  1 73  ? 27.854  35.274  44.934  1.00 22.59  ? 65  TRP E NE1 1 
ATOM   7312  C CE2 . TRP E  1 73  ? 27.295  34.277  45.689  1.00 19.83  ? 65  TRP E CE2 1 
ATOM   7313  C CE3 . TRP E  1 73  ? 27.507  31.883  45.931  1.00 13.45  ? 65  TRP E CE3 1 
ATOM   7314  C CZ2 . TRP E  1 73  ? 26.309  34.341  46.671  1.00 18.11  ? 65  TRP E CZ2 1 
ATOM   7315  C CZ3 . TRP E  1 73  ? 26.524  31.947  46.902  1.00 19.19  ? 65  TRP E CZ3 1 
ATOM   7316  C CH2 . TRP E  1 73  ? 25.937  33.170  47.267  1.00 17.82  ? 65  TRP E CH2 1 
ATOM   7317  N N   . ASN E  1 74  ? 32.252  34.102  43.674  1.00 26.13  ? 66  ASN E N   1 
ATOM   7318  C CA  . ASN E  1 74  ? 33.035  35.295  43.947  1.00 28.19  ? 66  ASN E CA  1 
ATOM   7319  C C   . ASN E  1 74  ? 32.145  36.519  44.075  1.00 29.62  ? 66  ASN E C   1 
ATOM   7320  O O   . ASN E  1 74  ? 31.611  37.015  43.078  1.00 30.50  ? 66  ASN E O   1 
ATOM   7321  C CB  . ASN E  1 74  ? 34.102  35.510  42.878  1.00 27.35  ? 66  ASN E CB  1 
ATOM   7322  C CG  . ASN E  1 74  ? 34.960  36.708  43.164  1.00 37.63  ? 66  ASN E CG  1 
ATOM   7323  O OD1 . ASN E  1 74  ? 35.176  37.046  44.324  1.00 37.53  ? 66  ASN E OD1 1 
ATOM   7324  N ND2 . ASN E  1 74  ? 35.425  37.389  42.108  1.00 52.53  ? 66  ASN E ND2 1 
ATOM   7325  N N   . SER E  1 75  ? 32.014  37.003  45.308  1.00 25.57  ? 67  SER E N   1 
ATOM   7326  C CA  . SER E  1 75  ? 31.088  38.076  45.649  1.00 26.86  ? 67  SER E CA  1 
ATOM   7327  C C   . SER E  1 75  ? 31.669  39.487  45.567  1.00 30.89  ? 67  SER E C   1 
ATOM   7328  O O   . SER E  1 75  ? 31.091  40.428  46.112  1.00 33.11  ? 67  SER E O   1 
ATOM   7329  C CB  . SER E  1 75  ? 30.532  37.846  47.056  1.00 29.31  ? 67  SER E CB  1 
ATOM   7330  O OG  . SER E  1 75  ? 31.575  37.516  47.951  1.00 30.58  ? 67  SER E OG  1 
ATOM   7331  N N   . SER E  1 76  ? 32.798  39.635  44.885  1.00 33.42  ? 68  SER E N   1 
ATOM   7332  C CA  . SER E  1 76  ? 33.427  40.945  44.715  1.00 35.18  ? 68  SER E CA  1 
ATOM   7333  C C   . SER E  1 76  ? 32.481  42.019  44.171  1.00 38.41  ? 68  SER E C   1 
ATOM   7334  O O   . SER E  1 76  ? 32.405  43.116  44.731  1.00 40.54  ? 68  SER E O   1 
ATOM   7335  C CB  . SER E  1 76  ? 34.669  40.837  43.831  1.00 43.44  ? 68  SER E CB  1 
ATOM   7336  O OG  . SER E  1 76  ? 35.658  40.043  44.461  1.00 47.47  ? 68  SER E OG  1 
ATOM   7337  N N   . HIS E  1 77  ? 31.765  41.715  43.089  1.00 33.83  ? 69  HIS E N   1 
ATOM   7338  C CA  . HIS E  1 77  ? 30.730  42.633  42.609  1.00 38.09  ? 69  HIS E CA  1 
ATOM   7339  C C   . HIS E  1 77  ? 29.373  41.962  42.404  1.00 34.82  ? 69  HIS E C   1 
ATOM   7340  O O   . HIS E  1 77  ? 28.624  42.311  41.492  1.00 32.33  ? 69  HIS E O   1 
ATOM   7341  C CB  . HIS E  1 77  ? 31.182  43.369  41.351  1.00 41.91  ? 69  HIS E CB  1 
ATOM   7342  C CG  . HIS E  1 77  ? 32.403  44.209  41.556  1.00 48.59  ? 69  HIS E CG  1 
ATOM   7343  N ND1 . HIS E  1 77  ? 33.680  43.686  41.532  1.00 49.12  ? 69  HIS E ND1 1 
ATOM   7344  C CD2 . HIS E  1 77  ? 32.544  45.534  41.800  1.00 47.83  ? 69  HIS E CD2 1 
ATOM   7345  C CE1 . HIS E  1 77  ? 34.554  44.652  41.748  1.00 42.95  ? 69  HIS E CE1 1 
ATOM   7346  N NE2 . HIS E  1 77  ? 33.891  45.784  41.908  1.00 51.47  ? 69  HIS E NE2 1 
ATOM   7347  N N   . SER E  1 78  ? 29.065  41.012  43.285  1.00 38.83  ? 70  SER E N   1 
ATOM   7348  C CA  . SER E  1 78  ? 27.797  40.287  43.280  1.00 35.58  ? 70  SER E CA  1 
ATOM   7349  C C   . SER E  1 78  ? 27.289  40.130  44.731  1.00 32.53  ? 70  SER E C   1 
ATOM   7350  O O   . SER E  1 78  ? 28.032  40.399  45.667  1.00 39.91  ? 70  SER E O   1 
ATOM   7351  C CB  . SER E  1 78  ? 28.005  38.929  42.616  1.00 30.34  ? 70  SER E CB  1 
ATOM   7352  O OG  . SER E  1 78  ? 28.925  38.159  43.361  1.00 33.25  ? 70  SER E OG  1 
ATOM   7353  N N   . PRO E  1 79  ? 26.020  39.717  44.922  1.00 32.58  ? 71  PRO E N   1 
ATOM   7354  C CA  . PRO E  1 79  ? 25.436  39.503  46.261  1.00 32.02  ? 71  PRO E CA  1 
ATOM   7355  C C   . PRO E  1 79  ? 26.199  38.529  47.167  1.00 26.69  ? 71  PRO E C   1 
ATOM   7356  O O   . PRO E  1 79  ? 26.697  37.526  46.669  1.00 25.42  ? 71  PRO E O   1 
ATOM   7357  C CB  . PRO E  1 79  ? 24.063  38.917  45.936  1.00 30.24  ? 71  PRO E CB  1 
ATOM   7358  C CG  . PRO E  1 79  ? 23.709  39.520  44.625  1.00 27.39  ? 71  PRO E CG  1 
ATOM   7359  C CD  . PRO E  1 79  ? 24.996  39.609  43.864  1.00 32.49  ? 71  PRO E CD  1 
ATOM   7360  N N   . ASP E  1 80  ? 26.266  38.817  48.470  1.00 30.21  ? 72  ASP E N   1 
ATOM   7361  C CA  . ASP E  1 80  ? 26.982  37.966  49.440  1.00 27.69  ? 72  ASP E CA  1 
ATOM   7362  C C   . ASP E  1 80  ? 26.214  36.687  49.707  1.00 28.20  ? 72  ASP E C   1 
ATOM   7363  O O   . ASP E  1 80  ? 26.803  35.616  49.864  1.00 30.11  ? 72  ASP E O   1 
ATOM   7364  C CB  . ASP E  1 80  ? 27.164  38.657  50.804  1.00 36.17  ? 72  ASP E CB  1 
ATOM   7365  C CG  . ASP E  1 80  ? 27.465  40.135  50.692  1.00 44.22  ? 72  ASP E CG  1 
ATOM   7366  O OD1 . ASP E  1 80  ? 28.604  40.460  50.303  1.00 42.35  ? 72  ASP E OD1 1 
ATOM   7367  O OD2 . ASP E  1 80  ? 26.574  40.963  51.022  1.00 43.56  ? 72  ASP E OD2 1 
ATOM   7368  N N   . GLN E  1 81  ? 24.894  36.815  49.813  1.00 26.40  ? 73  GLN E N   1 
ATOM   7369  C CA  . GLN E  1 81  ? 24.033  35.664  50.001  1.00 21.28  ? 73  GLN E CA  1 
ATOM   7370  C C   . GLN E  1 81  ? 22.719  35.820  49.243  1.00 21.00  ? 73  GLN E C   1 
ATOM   7371  O O   . GLN E  1 81  ? 22.334  36.934  48.863  1.00 18.74  ? 73  GLN E O   1 
ATOM   7372  C CB  . GLN E  1 81  ? 23.780  35.428  51.491  1.00 22.62  ? 73  GLN E CB  1 
ATOM   7373  C CG  . GLN E  1 81  ? 23.714  36.702  52.328  1.00 28.25  ? 73  GLN E CG  1 
ATOM   7374  C CD  . GLN E  1 81  ? 23.366  36.438  53.803  1.00 35.07  ? 73  GLN E CD  1 
ATOM   7375  O OE1 . GLN E  1 81  ? 23.631  35.360  54.341  1.00 32.12  ? 73  GLN E OE1 1 
ATOM   7376  N NE2 . GLN E  1 81  ? 22.762  37.432  54.453  1.00 38.81  ? 73  GLN E NE2 1 
ATOM   7377  N N   . VAL E  1 82  ? 22.047  34.691  49.013  1.00 20.62  ? 74  VAL E N   1 
ATOM   7378  C CA  . VAL E  1 82  ? 20.688  34.679  48.475  1.00 16.76  ? 74  VAL E CA  1 
ATOM   7379  C C   . VAL E  1 82  ? 19.845  33.591  49.154  1.00 13.20  ? 74  VAL E C   1 
ATOM   7380  O O   . VAL E  1 82  ? 20.364  32.731  49.860  1.00 11.16  ? 74  VAL E O   1 
ATOM   7381  C CB  . VAL E  1 82  ? 20.664  34.411  46.951  1.00 14.79  ? 74  VAL E CB  1 
ATOM   7382  C CG1 . VAL E  1 82  ? 21.378  35.513  46.171  1.00 12.44  ? 74  VAL E CG1 1 
ATOM   7383  C CG2 . VAL E  1 82  ? 21.252  33.059  46.666  1.00 13.04  ? 74  VAL E CG2 1 
ATOM   7384  N N   . SER E  1 83  ? 18.540  33.627  48.913  1.00 14.41  ? 75  SER E N   1 
ATOM   7385  C CA  . SER E  1 83  ? 17.620  32.637  49.472  1.00 14.42  ? 75  SER E CA  1 
ATOM   7386  C C   . SER E  1 83  ? 17.319  31.542  48.454  1.00 12.07  ? 75  SER E C   1 
ATOM   7387  O O   . SER E  1 83  ? 17.161  31.816  47.265  1.00 12.12  ? 75  SER E O   1 
ATOM   7388  C CB  . SER E  1 83  ? 16.319  33.311  49.920  1.00 13.03  ? 75  SER E CB  1 
ATOM   7389  O OG  . SER E  1 83  ? 16.587  34.345  50.865  1.00 14.95  ? 75  SER E OG  1 
ATOM   7390  N N   . VAL E  1 84  ? 17.233  30.303  48.922  1.00 8.57   ? 76  VAL E N   1 
ATOM   7391  C CA  . VAL E  1 84  ? 17.062  29.161  48.037  1.00 9.42   ? 76  VAL E CA  1 
ATOM   7392  C C   . VAL E  1 84  ? 16.018  28.194  48.612  1.00 10.71  ? 76  VAL E C   1 
ATOM   7393  O O   . VAL E  1 84  ? 16.051  27.892  49.804  1.00 11.06  ? 76  VAL E O   1 
ATOM   7394  C CB  . VAL E  1 84  ? 18.416  28.428  47.842  1.00 9.01   ? 76  VAL E CB  1 
ATOM   7395  C CG1 . VAL E  1 84  ? 18.261  27.212  46.954  1.00 7.38   ? 76  VAL E CG1 1 
ATOM   7396  C CG2 . VAL E  1 84  ? 19.432  29.366  47.262  1.00 9.97   ? 76  VAL E CG2 1 
ATOM   7397  N N   . PRO E  1 85  ? 15.073  27.720  47.773  1.00 12.11  ? 77  PRO E N   1 
ATOM   7398  C CA  . PRO E  1 85  ? 14.102  26.706  48.211  1.00 10.33  ? 77  PRO E CA  1 
ATOM   7399  C C   . PRO E  1 85  ? 14.830  25.431  48.647  1.00 10.12  ? 77  PRO E C   1 
ATOM   7400  O O   . PRO E  1 85  ? 15.683  24.997  47.898  1.00 9.54   ? 77  PRO E O   1 
ATOM   7401  C CB  . PRO E  1 85  ? 13.297  26.437  46.938  1.00 5.93   ? 77  PRO E CB  1 
ATOM   7402  C CG  . PRO E  1 85  ? 13.404  27.684  46.162  1.00 7.27   ? 77  PRO E CG  1 
ATOM   7403  C CD  . PRO E  1 85  ? 14.802  28.174  46.396  1.00 10.15  ? 77  PRO E CD  1 
ATOM   7404  N N   . ILE E  1 86  ? 14.515  24.845  49.803  1.00 9.52   ? 78  ILE E N   1 
ATOM   7405  C CA  . ILE E  1 86  ? 15.306  23.714  50.282  1.00 9.02   ? 78  ILE E CA  1 
ATOM   7406  C C   . ILE E  1 86  ? 15.222  22.490  49.384  1.00 12.44  ? 78  ILE E C   1 
ATOM   7407  O O   . ILE E  1 86  ? 16.016  21.559  49.525  1.00 16.12  ? 78  ILE E O   1 
ATOM   7408  C CB  . ILE E  1 86  ? 14.964  23.277  51.719  1.00 8.56   ? 78  ILE E CB  1 
ATOM   7409  C CG1 . ILE E  1 86  ? 13.473  22.988  51.856  1.00 11.92  ? 78  ILE E CG1 1 
ATOM   7410  C CG2 . ILE E  1 86  ? 15.451  24.301  52.734  1.00 6.95   ? 78  ILE E CG2 1 
ATOM   7411  C CD1 . ILE E  1 86  ? 13.085  22.430  53.223  1.00 8.49   ? 78  ILE E CD1 1 
ATOM   7412  N N   . SER E  1 87  ? 14.271  22.482  48.460  1.00 12.15  ? 79  SER E N   1 
ATOM   7413  C CA  . SER E  1 87  ? 14.162  21.377  47.513  1.00 12.46  ? 79  SER E CA  1 
ATOM   7414  C C   . SER E  1 87  ? 15.254  21.438  46.427  1.00 11.44  ? 79  SER E C   1 
ATOM   7415  O O   . SER E  1 87  ? 15.391  20.531  45.616  1.00 12.92  ? 79  SER E O   1 
ATOM   7416  C CB  . SER E  1 87  ? 12.762  21.342  46.895  1.00 11.81  ? 79  SER E CB  1 
ATOM   7417  O OG  . SER E  1 87  ? 12.544  22.457  46.050  1.00 15.01  ? 79  SER E OG  1 
ATOM   7418  N N   . SER E  1 88  ? 16.034  22.508  46.431  1.00 8.86   ? 80  SER E N   1 
ATOM   7419  C CA  . SER E  1 88  ? 17.145  22.642  45.514  1.00 11.45  ? 80  SER E CA  1 
ATOM   7420  C C   . SER E  1 88  ? 18.460  22.252  46.184  1.00 13.84  ? 80  SER E C   1 
ATOM   7421  O O   . SER E  1 88  ? 19.516  22.225  45.534  1.00 17.31  ? 80  SER E O   1 
ATOM   7422  C CB  . SER E  1 88  ? 17.235  24.081  44.999  1.00 11.24  ? 80  SER E CB  1 
ATOM   7423  O OG  . SER E  1 88  ? 16.057  24.454  44.301  1.00 14.01  ? 80  SER E OG  1 
ATOM   7424  N N   . LEU E  1 89  ? 18.390  21.937  47.473  1.00 10.00  ? 81  LEU E N   1 
ATOM   7425  C CA  . LEU E  1 89  ? 19.580  21.781  48.301  1.00 10.76  ? 81  LEU E CA  1 
ATOM   7426  C C   . LEU E  1 89  ? 19.562  20.527  49.163  1.00 13.38  ? 81  LEU E C   1 
ATOM   7427  O O   . LEU E  1 89  ? 18.492  20.065  49.604  1.00 14.00  ? 81  LEU E O   1 
ATOM   7428  C CB  . LEU E  1 89  ? 19.735  22.990  49.227  1.00 11.93  ? 81  LEU E CB  1 
ATOM   7429  C CG  . LEU E  1 89  ? 20.146  24.318  48.591  1.00 14.32  ? 81  LEU E CG  1 
ATOM   7430  C CD1 . LEU E  1 89  ? 20.268  25.406  49.660  1.00 12.57  ? 81  LEU E CD1 1 
ATOM   7431  C CD2 . LEU E  1 89  ? 21.442  24.166  47.793  1.00 11.19  ? 81  LEU E CD2 1 
ATOM   7432  N N   . TRP E  1 90  ? 20.747  19.985  49.425  1.00 9.86   ? 82  TRP E N   1 
ATOM   7433  C CA  . TRP E  1 90  ? 20.857  18.952  50.432  1.00 12.36  ? 82  TRP E CA  1 
ATOM   7434  C C   . TRP E  1 90  ? 20.578  19.603  51.783  1.00 12.64  ? 82  TRP E C   1 
ATOM   7435  O O   . TRP E  1 90  ? 21.059  20.698  52.040  1.00 11.42  ? 82  TRP E O   1 
ATOM   7436  C CB  . TRP E  1 90  ? 22.239  18.308  50.433  1.00 9.44   ? 82  TRP E CB  1 
ATOM   7437  C CG  . TRP E  1 90  ? 22.398  17.284  51.513  1.00 10.33  ? 82  TRP E CG  1 
ATOM   7438  C CD1 . TRP E  1 90  ? 22.015  15.974  51.464  1.00 11.73  ? 82  TRP E CD1 1 
ATOM   7439  C CD2 . TRP E  1 90  ? 22.947  17.489  52.819  1.00 13.37  ? 82  TRP E CD2 1 
ATOM   7440  N NE1 . TRP E  1 90  ? 22.299  15.346  52.653  1.00 12.06  ? 82  TRP E NE1 1 
ATOM   7441  C CE2 . TRP E  1 90  ? 22.873  16.254  53.504  1.00 14.67  ? 82  TRP E CE2 1 
ATOM   7442  C CE3 . TRP E  1 90  ? 23.495  18.595  53.481  1.00 15.74  ? 82  TRP E CE3 1 
ATOM   7443  C CZ2 . TRP E  1 90  ? 23.337  16.096  54.816  1.00 11.16  ? 82  TRP E CZ2 1 
ATOM   7444  C CZ3 . TRP E  1 90  ? 23.966  18.427  54.791  1.00 13.25  ? 82  TRP E CZ3 1 
ATOM   7445  C CH2 . TRP E  1 90  ? 23.886  17.189  55.433  1.00 9.05   ? 82  TRP E CH2 1 
ATOM   7446  N N   . VAL E  1 91  ? 19.773  18.935  52.612  1.00 11.32  ? 83  VAL E N   1 
ATOM   7447  C CA  . VAL E  1 91  ? 19.570  19.315  54.018  1.00 14.97  ? 83  VAL E CA  1 
ATOM   7448  C C   . VAL E  1 91  ? 19.804  18.088  54.895  1.00 13.31  ? 83  VAL E C   1 
ATOM   7449  O O   . VAL E  1 91  ? 19.542  16.969  54.461  1.00 17.25  ? 83  VAL E O   1 
ATOM   7450  C CB  . VAL E  1 91  ? 18.149  19.878  54.308  1.00 11.13  ? 83  VAL E CB  1 
ATOM   7451  C CG1 . VAL E  1 91  ? 17.981  21.274  53.689  1.00 8.28   ? 83  VAL E CG1 1 
ATOM   7452  C CG2 . VAL E  1 91  ? 17.077  18.893  53.838  1.00 8.65   ? 83  VAL E CG2 1 
ATOM   7453  N N   . PRO E  1 92  ? 20.337  18.284  56.115  1.00 12.54  ? 84  PRO E N   1 
ATOM   7454  C CA  . PRO E  1 92  ? 20.585  17.086  56.927  1.00 13.87  ? 84  PRO E CA  1 
ATOM   7455  C C   . PRO E  1 92  ? 19.288  16.457  57.407  1.00 12.78  ? 84  PRO E C   1 
ATOM   7456  O O   . PRO E  1 92  ? 18.383  17.188  57.800  1.00 13.23  ? 84  PRO E O   1 
ATOM   7457  C CB  . PRO E  1 92  ? 21.422  17.604  58.101  1.00 13.04  ? 84  PRO E CB  1 
ATOM   7458  C CG  . PRO E  1 92  ? 21.322  19.104  58.048  1.00 15.69  ? 84  PRO E CG  1 
ATOM   7459  C CD  . PRO E  1 92  ? 21.017  19.479  56.646  1.00 12.46  ? 84  PRO E CD  1 
ATOM   7460  N N   . ASP E  1 93  ? 19.203  15.128  57.346  1.00 9.25   ? 85  ASP E N   1 
ATOM   7461  C CA  . ASP E  1 93  ? 18.011  14.399  57.768  1.00 14.32  ? 85  ASP E CA  1 
ATOM   7462  C C   . ASP E  1 93  ? 17.884  14.256  59.299  1.00 17.60  ? 85  ASP E C   1 
ATOM   7463  O O   . ASP E  1 93  ? 17.880  13.141  59.840  1.00 15.47  ? 85  ASP E O   1 
ATOM   7464  C CB  . ASP E  1 93  ? 17.997  13.022  57.117  1.00 11.48  ? 85  ASP E CB  1 
ATOM   7465  C CG  . ASP E  1 93  ? 19.218  12.231  57.457  1.00 15.95  ? 85  ASP E CG  1 
ATOM   7466  O OD1 . ASP E  1 93  ? 20.219  12.884  57.801  1.00 19.33  ? 85  ASP E OD1 1 
ATOM   7467  O OD2 . ASP E  1 93  ? 19.187  10.980  57.400  1.00 18.58  ? 85  ASP E OD2 1 
ATOM   7468  N N   . LEU E  1 94  ? 17.771  15.389  59.987  1.00 15.97  ? 86  LEU E N   1 
ATOM   7469  C CA  . LEU E  1 94  ? 17.641  15.404  61.438  1.00 14.89  ? 86  LEU E CA  1 
ATOM   7470  C C   . LEU E  1 94  ? 16.317  14.809  61.891  1.00 14.05  ? 86  LEU E C   1 
ATOM   7471  O O   . LEU E  1 94  ? 15.297  14.964  61.230  1.00 19.48  ? 86  LEU E O   1 
ATOM   7472  C CB  . LEU E  1 94  ? 17.772  16.829  61.952  1.00 13.11  ? 86  LEU E CB  1 
ATOM   7473  C CG  . LEU E  1 94  ? 19.126  17.450  61.629  1.00 13.95  ? 86  LEU E CG  1 
ATOM   7474  C CD1 . LEU E  1 94  ? 19.194  18.877  62.152  1.00 13.01  ? 86  LEU E CD1 1 
ATOM   7475  C CD2 . LEU E  1 94  ? 20.258  16.584  62.182  1.00 12.71  ? 86  LEU E CD2 1 
ATOM   7476  N N   . ALA E  1 95  ? 16.347  14.098  63.008  1.00 15.86  ? 87  ALA E N   1 
ATOM   7477  C CA  . ALA E  1 95  ? 15.127  13.574  63.616  1.00 18.47  ? 87  ALA E CA  1 
ATOM   7478  C C   . ALA E  1 95  ? 15.245  13.675  65.123  1.00 12.54  ? 87  ALA E C   1 
ATOM   7479  O O   . ALA E  1 95  ? 16.327  13.497  65.666  1.00 14.74  ? 87  ALA E O   1 
ATOM   7480  C CB  . ALA E  1 95  ? 14.891  12.125  63.191  1.00 14.02  ? 87  ALA E CB  1 
ATOM   7481  N N   . ALA E  1 96  ? 14.138  13.985  65.788  1.00 16.42  ? 88  ALA E N   1 
ATOM   7482  C CA  . ALA E  1 96  ? 14.056  13.929  67.257  1.00 16.52  ? 88  ALA E CA  1 
ATOM   7483  C C   . ALA E  1 96  ? 13.698  12.522  67.708  1.00 16.05  ? 88  ALA E C   1 
ATOM   7484  O O   . ALA E  1 96  ? 12.628  12.016  67.366  1.00 16.95  ? 88  ALA E O   1 
ATOM   7485  C CB  . ALA E  1 96  ? 13.018  14.899  67.766  1.00 13.97  ? 88  ALA E CB  1 
ATOM   7486  N N   . TYR E  1 97  ? 14.588  11.891  68.471  1.00 18.83  ? 89  TYR E N   1 
ATOM   7487  C CA  . TYR E  1 97  ? 14.372  10.517  68.940  1.00 21.94  ? 89  TYR E CA  1 
ATOM   7488  C C   . TYR E  1 97  ? 13.103  10.373  69.796  1.00 22.24  ? 89  TYR E C   1 
ATOM   7489  O O   . TYR E  1 97  ? 12.394  9.370   69.688  1.00 25.56  ? 89  TYR E O   1 
ATOM   7490  C CB  . TYR E  1 97  ? 15.583  10.000  69.733  1.00 25.01  ? 89  TYR E CB  1 
ATOM   7491  C CG  . TYR E  1 97  ? 16.876  9.933   68.953  1.00 31.34  ? 89  TYR E CG  1 
ATOM   7492  C CD1 . TYR E  1 97  ? 17.501  8.720   68.692  1.00 39.76  ? 89  TYR E CD1 1 
ATOM   7493  C CD2 . TYR E  1 97  ? 17.479  11.088  68.476  1.00 38.84  ? 89  TYR E CD2 1 
ATOM   7494  C CE1 . TYR E  1 97  ? 18.693  8.667   67.968  1.00 41.17  ? 89  TYR E CE1 1 
ATOM   7495  C CE2 . TYR E  1 97  ? 18.658  11.049  67.748  1.00 38.01  ? 89  TYR E CE2 1 
ATOM   7496  C CZ  . TYR E  1 97  ? 19.263  9.844   67.502  1.00 40.54  ? 89  TYR E CZ  1 
ATOM   7497  O OH  . TYR E  1 97  ? 20.432  9.839   66.782  1.00 44.56  ? 89  TYR E OH  1 
ATOM   7498  N N   . ASN E  1 98  ? 12.806  11.361  70.639  1.00 14.40  ? 90  ASN E N   1 
ATOM   7499  C CA  . ASN E  1 98  ? 11.670  11.219  71.550  1.00 21.17  ? 90  ASN E CA  1 
ATOM   7500  C C   . ASN E  1 98  ? 10.419  11.965  71.124  1.00 23.98  ? 90  ASN E C   1 
ATOM   7501  O O   . ASN E  1 98  ? 9.532   12.204  71.944  1.00 22.54  ? 90  ASN E O   1 
ATOM   7502  C CB  . ASN E  1 98  ? 12.041  11.625  72.981  1.00 20.79  ? 90  ASN E CB  1 
ATOM   7503  C CG  . ASN E  1 98  ? 12.691  12.997  73.050  1.00 28.42  ? 90  ASN E CG  1 
ATOM   7504  O OD1 . ASN E  1 98  ? 13.620  13.309  72.285  1.00 27.24  ? 90  ASN E OD1 1 
ATOM   7505  N ND2 . ASN E  1 98  ? 12.203  13.831  73.966  1.00 25.03  ? 90  ASN E ND2 1 
ATOM   7506  N N   . ALA E  1 99  ? 10.349  12.333  69.849  1.00 23.05  ? 91  ALA E N   1 
ATOM   7507  C CA  . ALA E  1 99  ? 9.217   13.092  69.333  1.00 17.81  ? 91  ALA E CA  1 
ATOM   7508  C C   . ALA E  1 99  ? 8.064   12.158  69.093  1.00 14.57  ? 91  ALA E C   1 
ATOM   7509  O O   . ALA E  1 99  ? 8.265   11.028  68.683  1.00 16.25  ? 91  ALA E O   1 
ATOM   7510  C CB  . ALA E  1 99  ? 9.593   13.791  68.045  1.00 19.03  ? 91  ALA E CB  1 
ATOM   7511  N N   . ILE E  1 100 ? 6.852   12.632  69.334  1.00 16.92  ? 92  ILE E N   1 
ATOM   7512  C CA  . ILE E  1 100 ? 5.693   11.767  69.206  1.00 18.28  ? 92  ILE E CA  1 
ATOM   7513  C C   . ILE E  1 100 ? 4.676   12.293  68.204  1.00 16.10  ? 92  ILE E C   1 
ATOM   7514  O O   . ILE E  1 100 ? 3.536   11.836  68.165  1.00 19.68  ? 92  ILE E O   1 
ATOM   7515  C CB  . ILE E  1 100 ? 5.036   11.511  70.577  1.00 20.56  ? 92  ILE E CB  1 
ATOM   7516  C CG1 . ILE E  1 100 ? 4.686   12.837  71.257  1.00 21.56  ? 92  ILE E CG1 1 
ATOM   7517  C CG2 . ILE E  1 100 ? 5.969   10.692  71.458  1.00 15.24  ? 92  ILE E CG2 1 
ATOM   7518  C CD1 . ILE E  1 100 ? 3.927   12.672  72.551  1.00 22.09  ? 92  ILE E CD1 1 
ATOM   7519  N N   . SER E  1 101 ? 5.107   13.254  67.395  1.00 17.65  ? 93  SER E N   1 
ATOM   7520  C CA  . SER E  1 101 ? 4.318   13.776  66.278  1.00 20.34  ? 93  SER E CA  1 
ATOM   7521  C C   . SER E  1 101 ? 5.279   14.316  65.226  1.00 16.74  ? 93  SER E C   1 
ATOM   7522  O O   . SER E  1 101 ? 6.431   14.602  65.536  1.00 13.28  ? 93  SER E O   1 
ATOM   7523  C CB  . SER E  1 101 ? 3.388   14.901  66.737  1.00 18.60  ? 93  SER E CB  1 
ATOM   7524  O OG  . SER E  1 101 ? 4.124   16.025  67.210  1.00 16.21  ? 93  SER E OG  1 
ATOM   7525  N N   . LYS E  1 102 ? 4.805   14.450  63.988  1.00 22.48  ? 94  LYS E N   1 
ATOM   7526  C CA  . LYS E  1 102 ? 5.607   15.050  62.914  1.00 21.45  ? 94  LYS E CA  1 
ATOM   7527  C C   . LYS E  1 102 ? 5.964   16.489  63.259  1.00 19.14  ? 94  LYS E C   1 
ATOM   7528  O O   . LYS E  1 102 ? 5.175   17.204  63.883  1.00 14.91  ? 94  LYS E O   1 
ATOM   7529  C CB  . LYS E  1 102 ? 4.835   15.091  61.594  1.00 22.32  ? 94  LYS E CB  1 
ATOM   7530  C CG  . LYS E  1 102 ? 4.436   13.769  60.987  1.00 23.60  ? 94  LYS E CG  1 
ATOM   7531  C CD  . LYS E  1 102 ? 3.447   14.044  59.858  1.00 29.54  ? 94  LYS E CD  1 
ATOM   7532  C CE  . LYS E  1 102 ? 2.947   12.773  59.185  1.00 35.18  ? 94  LYS E CE  1 
ATOM   7533  N NZ  . LYS E  1 102 ? 1.746   13.018  58.326  1.00 44.57  ? 94  LYS E NZ  1 
ATOM   7534  N N   . PRO E  1 103 ? 7.156   16.924  62.844  1.00 18.07  ? 95  PRO E N   1 
ATOM   7535  C CA  . PRO E  1 103 ? 7.468   18.352  62.952  1.00 17.28  ? 95  PRO E CA  1 
ATOM   7536  C C   . PRO E  1 103 ? 6.561   19.150  62.023  1.00 20.31  ? 95  PRO E C   1 
ATOM   7537  O O   . PRO E  1 103 ? 6.631   18.963  60.802  1.00 27.60  ? 95  PRO E O   1 
ATOM   7538  C CB  . PRO E  1 103 ? 8.925   18.435  62.474  1.00 17.48  ? 95  PRO E CB  1 
ATOM   7539  C CG  . PRO E  1 103 ? 9.171   17.163  61.693  1.00 14.61  ? 95  PRO E CG  1 
ATOM   7540  C CD  . PRO E  1 103 ? 8.289   16.129  62.337  1.00 17.94  ? 95  PRO E CD  1 
ATOM   7541  N N   . GLU E  1 104 ? 5.713   20.005  62.583  1.00 15.84  ? 96  GLU E N   1 
ATOM   7542  C CA  . GLU E  1 104 ? 4.901   20.915  61.787  1.00 17.18  ? 96  GLU E CA  1 
ATOM   7543  C C   . GLU E  1 104 ? 5.680   22.212  61.557  1.00 15.32  ? 96  GLU E C   1 
ATOM   7544  O O   . GLU E  1 104 ? 5.912   22.962  62.488  1.00 15.74  ? 96  GLU E O   1 
ATOM   7545  C CB  . GLU E  1 104 ? 3.574   21.202  62.498  1.00 26.25  ? 96  GLU E CB  1 
ATOM   7546  C CG  . GLU E  1 104 ? 2.737   22.314  61.871  1.00 33.67  ? 96  GLU E CG  1 
ATOM   7547  C CD  . GLU E  1 104 ? 1.349   22.437  62.495  1.00 51.57  ? 96  GLU E CD  1 
ATOM   7548  O OE1 . GLU E  1 104 ? 1.009   21.600  63.370  1.00 60.46  ? 96  GLU E OE1 1 
ATOM   7549  O OE2 . GLU E  1 104 ? 0.603   23.372  62.103  1.00 47.18  ? 96  GLU E OE2 1 
ATOM   7550  N N   . VAL E  1 105 ? 6.101   22.460  60.317  1.00 16.27  ? 97  VAL E N   1 
ATOM   7551  C CA  . VAL E  1 105 ? 6.938   23.619  59.991  1.00 15.24  ? 97  VAL E CA  1 
ATOM   7552  C C   . VAL E  1 105 ? 6.028   24.817  59.732  1.00 15.31  ? 97  VAL E C   1 
ATOM   7553  O O   . VAL E  1 105 ? 5.035   24.692  59.020  1.00 18.93  ? 97  VAL E O   1 
ATOM   7554  C CB  . VAL E  1 105 ? 7.848   23.339  58.757  1.00 11.34  ? 97  VAL E CB  1 
ATOM   7555  C CG1 . VAL E  1 105 ? 8.609   24.568  58.356  1.00 11.82  ? 97  VAL E CG1 1 
ATOM   7556  C CG2 . VAL E  1 105 ? 8.799   22.212  59.048  1.00 9.13   ? 97  VAL E CG2 1 
ATOM   7557  N N   . LEU E  1 106 ? 6.343   25.963  60.329  1.00 13.76  ? 98  LEU E N   1 
ATOM   7558  C CA  . LEU E  1 106 ? 5.435   27.109  60.292  1.00 13.23  ? 98  LEU E CA  1 
ATOM   7559  C C   . LEU E  1 106 ? 5.924   28.232  59.377  1.00 15.75  ? 98  LEU E C   1 
ATOM   7560  O O   . LEU E  1 106 ? 5.159   29.120  59.018  1.00 16.70  ? 98  LEU E O   1 
ATOM   7561  C CB  . LEU E  1 106 ? 5.216   27.659  61.704  1.00 13.62  ? 98  LEU E CB  1 
ATOM   7562  C CG  . LEU E  1 106 ? 4.775   26.691  62.804  1.00 17.77  ? 98  LEU E CG  1 
ATOM   7563  C CD1 . LEU E  1 106 ? 4.887   27.396  64.129  1.00 18.86  ? 98  LEU E CD1 1 
ATOM   7564  C CD2 . LEU E  1 106 ? 3.357   26.139  62.594  1.00 16.52  ? 98  LEU E CD2 1 
ATOM   7565  N N   . THR E  1 107 ? 7.198   28.180  58.997  1.00 15.17  ? 99  THR E N   1 
ATOM   7566  C CA  . THR E  1 107 ? 7.818   29.235  58.209  1.00 14.99  ? 99  THR E CA  1 
ATOM   7567  C C   . THR E  1 107 ? 7.981   28.839  56.738  1.00 15.20  ? 99  THR E C   1 
ATOM   7568  O O   . THR E  1 107 ? 7.875   27.660  56.404  1.00 15.28  ? 99  THR E O   1 
ATOM   7569  C CB  . THR E  1 107 ? 9.188   29.564  58.792  1.00 17.24  ? 99  THR E CB  1 
ATOM   7570  O OG1 . THR E  1 107 ? 9.735   28.385  59.384  1.00 15.50  ? 99  THR E OG1 1 
ATOM   7571  C CG2 . THR E  1 107 ? 9.048   30.616  59.853  1.00 19.07  ? 99  THR E CG2 1 
ATOM   7572  N N   . PRO E  1 108 ? 8.225   29.821  55.847  1.00 14.35  ? 100 PRO E N   1 
ATOM   7573  C CA  . PRO E  1 108 ? 8.501   29.414  54.460  1.00 13.97  ? 100 PRO E CA  1 
ATOM   7574  C C   . PRO E  1 108 ? 9.816   28.657  54.393  1.00 12.74  ? 100 PRO E C   1 
ATOM   7575  O O   . PRO E  1 108 ? 10.795  29.038  55.040  1.00 17.27  ? 100 PRO E O   1 
ATOM   7576  C CB  . PRO E  1 108 ? 8.614   30.750  53.716  1.00 9.70   ? 100 PRO E CB  1 
ATOM   7577  C CG  . PRO E  1 108 ? 7.859   31.735  54.591  1.00 12.14  ? 100 PRO E CG  1 
ATOM   7578  C CD  . PRO E  1 108 ? 8.178   31.286  55.984  1.00 11.58  ? 100 PRO E CD  1 
ATOM   7579  N N   . GLN E  1 109 ? 9.840   27.582  53.626  1.00 12.33  ? 101 GLN E N   1 
ATOM   7580  C CA  . GLN E  1 109 ? 11.017  26.723  53.574  1.00 11.55  ? 101 GLN E CA  1 
ATOM   7581  C C   . GLN E  1 109 ? 12.084  27.179  52.589  1.00 10.44  ? 101 GLN E C   1 
ATOM   7582  O O   . GLN E  1 109 ? 12.229  26.604  51.517  1.00 13.94  ? 101 GLN E O   1 
ATOM   7583  C CB  . GLN E  1 109 ? 10.578  25.299  53.268  1.00 15.24  ? 101 GLN E CB  1 
ATOM   7584  C CG  . GLN E  1 109 ? 9.413   24.840  54.158  1.00 13.96  ? 101 GLN E CG  1 
ATOM   7585  C CD  . GLN E  1 109 ? 9.560   23.392  54.578  1.00 20.42  ? 101 GLN E CD  1 
ATOM   7586  O OE1 . GLN E  1 109 ? 8.807   22.538  54.119  1.00 26.80  ? 101 GLN E OE1 1 
ATOM   7587  N NE2 . GLN E  1 109 ? 10.551  23.102  55.442  1.00 12.19  ? 101 GLN E NE2 1 
ATOM   7588  N N   . LEU E  1 110 ? 12.831  28.209  52.973  1.00 11.21  ? 102 LEU E N   1 
ATOM   7589  C CA  . LEU E  1 110 ? 13.971  28.719  52.215  1.00 9.60   ? 102 LEU E CA  1 
ATOM   7590  C C   . LEU E  1 110 ? 15.267  28.560  53.014  1.00 12.07  ? 102 LEU E C   1 
ATOM   7591  O O   . LEU E  1 110 ? 15.261  28.613  54.231  1.00 11.69  ? 102 LEU E O   1 
ATOM   7592  C CB  . LEU E  1 110 ? 13.771  30.205  51.928  1.00 9.70   ? 102 LEU E CB  1 
ATOM   7593  C CG  . LEU E  1 110 ? 12.483  30.603  51.199  1.00 12.35  ? 102 LEU E CG  1 
ATOM   7594  C CD1 . LEU E  1 110 ? 12.478  32.085  50.965  1.00 11.34  ? 102 LEU E CD1 1 
ATOM   7595  C CD2 . LEU E  1 110 ? 12.361  29.887  49.867  1.00 14.61  ? 102 LEU E CD2 1 
ATOM   7596  N N   . ALA E  1 111 ? 16.391  28.352  52.344  1.00 14.47  ? 103 ALA E N   1 
ATOM   7597  C CA  . ALA E  1 111 ? 17.665  28.401  53.049  1.00 12.43  ? 103 ALA E CA  1 
ATOM   7598  C C   . ALA E  1 111 ? 18.325  29.684  52.619  1.00 11.39  ? 103 ALA E C   1 
ATOM   7599  O O   . ALA E  1 111 ? 17.847  30.329  51.693  1.00 12.57  ? 103 ALA E O   1 
ATOM   7600  C CB  . ALA E  1 111 ? 18.536  27.206  52.707  1.00 9.84   ? 103 ALA E CB  1 
ATOM   7601  N N   . ARG E  1 112 ? 19.386  30.085  53.307  1.00 12.76  ? 104 ARG E N   1 
ATOM   7602  C CA  . ARG E  1 112 ? 20.234  31.157  52.794  1.00 13.08  ? 104 ARG E CA  1 
ATOM   7603  C C   . ARG E  1 112 ? 21.536  30.498  52.396  1.00 12.33  ? 104 ARG E C   1 
ATOM   7604  O O   . ARG E  1 112 ? 21.992  29.576  53.057  1.00 16.90  ? 104 ARG E O   1 
ATOM   7605  C CB  . ARG E  1 112 ? 20.465  32.252  53.842  1.00 14.59  ? 104 ARG E CB  1 
ATOM   7606  C CG  . ARG E  1 112 ? 19.188  32.930  54.320  1.00 14.17  ? 104 ARG E CG  1 
ATOM   7607  C CD  . ARG E  1 112 ? 18.667  33.952  53.314  1.00 11.37  ? 104 ARG E CD  1 
ATOM   7608  N NE  . ARG E  1 112 ? 19.609  35.048  53.104  1.00 12.40  ? 104 ARG E NE  1 
ATOM   7609  C CZ  . ARG E  1 112 ? 19.373  36.096  52.314  1.00 16.85  ? 104 ARG E CZ  1 
ATOM   7610  N NH1 . ARG E  1 112 ? 18.226  36.189  51.652  1.00 16.27  ? 104 ARG E NH1 1 
ATOM   7611  N NH2 . ARG E  1 112 ? 20.282  37.050  52.176  1.00 15.35  ? 104 ARG E NH2 1 
ATOM   7612  N N   . VAL E  1 113 ? 22.120  30.918  51.288  1.00 14.96  ? 105 VAL E N   1 
ATOM   7613  C CA  . VAL E  1 113 ? 23.418  30.386  50.918  1.00 14.38  ? 105 VAL E CA  1 
ATOM   7614  C C   . VAL E  1 113 ? 24.372  31.549  50.880  1.00 14.34  ? 105 VAL E C   1 
ATOM   7615  O O   . VAL E  1 113 ? 24.060  32.579  50.291  1.00 14.03  ? 105 VAL E O   1 
ATOM   7616  C CB  . VAL E  1 113 ? 23.383  29.673  49.560  1.00 10.27  ? 105 VAL E CB  1 
ATOM   7617  C CG1 . VAL E  1 113 ? 24.693  28.959  49.313  1.00 10.70  ? 105 VAL E CG1 1 
ATOM   7618  C CG2 . VAL E  1 113 ? 22.259  28.684  49.536  1.00 8.73   ? 105 VAL E CG2 1 
ATOM   7619  N N   . VAL E  1 114 ? 25.515  31.404  51.541  1.00 15.46  ? 106 VAL E N   1 
ATOM   7620  C CA  . VAL E  1 114 ? 26.502  32.481  51.554  1.00 22.25  ? 106 VAL E CA  1 
ATOM   7621  C C   . VAL E  1 114 ? 27.598  32.246  50.510  1.00 23.31  ? 106 VAL E C   1 
ATOM   7622  O O   . VAL E  1 114 ? 27.987  31.101  50.250  1.00 16.82  ? 106 VAL E O   1 
ATOM   7623  C CB  . VAL E  1 114 ? 27.131  32.692  52.955  1.00 23.30  ? 106 VAL E CB  1 
ATOM   7624  C CG1 . VAL E  1 114 ? 27.563  34.144  53.126  1.00 18.84  ? 106 VAL E CG1 1 
ATOM   7625  C CG2 . VAL E  1 114 ? 26.139  32.319  54.033  1.00 19.46  ? 106 VAL E CG2 1 
ATOM   7626  N N   . SER E  1 115 ? 28.099  33.346  49.940  1.00 23.40  ? 107 SER E N   1 
ATOM   7627  C CA  . SER E  1 115 ? 29.074  33.315  48.856  1.00 18.54  ? 107 SER E CA  1 
ATOM   7628  C C   . SER E  1 115 ? 30.306  32.481  49.160  1.00 22.86  ? 107 SER E C   1 
ATOM   7629  O O   . SER E  1 115 ? 31.059  32.137  48.241  1.00 26.26  ? 107 SER E O   1 
ATOM   7630  C CB  . SER E  1 115 ? 29.508  34.726  48.486  1.00 21.49  ? 107 SER E CB  1 
ATOM   7631  O OG  . SER E  1 115 ? 30.289  35.287  49.524  1.00 24.39  ? 107 SER E OG  1 
ATOM   7632  N N   . ASP E  1 116 ? 30.517  32.153  50.432  1.00 16.59  ? 108 ASP E N   1 
ATOM   7633  C CA  . ASP E  1 116 ? 31.644  31.312  50.815  1.00 17.38  ? 108 ASP E CA  1 
ATOM   7634  C C   . ASP E  1 116 ? 31.267  29.844  50.978  1.00 22.34  ? 108 ASP E C   1 
ATOM   7635  O O   . ASP E  1 116 ? 32.097  29.032  51.390  1.00 29.24  ? 108 ASP E O   1 
ATOM   7636  C CB  . ASP E  1 116 ? 32.295  31.828  52.102  1.00 24.35  ? 108 ASP E CB  1 
ATOM   7637  C CG  . ASP E  1 116 ? 31.298  31.994  53.246  1.00 30.98  ? 108 ASP E CG  1 
ATOM   7638  O OD1 . ASP E  1 116 ? 30.464  31.082  53.473  1.00 27.73  ? 108 ASP E OD1 1 
ATOM   7639  O OD2 . ASP E  1 116 ? 31.346  33.048  53.920  1.00 31.26  ? 108 ASP E OD2 1 
ATOM   7640  N N   . GLY E  1 117 ? 30.015  29.504  50.682  1.00 24.22  ? 109 GLY E N   1 
ATOM   7641  C CA  . GLY E  1 117 ? 29.553  28.129  50.799  1.00 22.36  ? 109 GLY E CA  1 
ATOM   7642  C C   . GLY E  1 117 ? 28.756  27.773  52.054  1.00 17.96  ? 109 GLY E C   1 
ATOM   7643  O O   . GLY E  1 117 ? 28.346  26.616  52.225  1.00 18.37  ? 109 GLY E O   1 
ATOM   7644  N N   . GLU E  1 118 ? 28.540  28.736  52.944  1.00 19.27  ? 110 GLU E N   1 
ATOM   7645  C CA  . GLU E  1 118 ? 27.755  28.454  54.155  1.00 20.10  ? 110 GLU E CA  1 
ATOM   7646  C C   . GLU E  1 118 ? 26.283  28.375  53.794  1.00 16.92  ? 110 GLU E C   1 
ATOM   7647  O O   . GLU E  1 118 ? 25.772  29.190  53.011  1.00 16.27  ? 110 GLU E O   1 
ATOM   7648  C CB  . GLU E  1 118 ? 27.958  29.515  55.238  1.00 14.15  ? 110 GLU E CB  1 
ATOM   7649  C CG  . GLU E  1 118 ? 27.954  28.948  56.643  1.00 19.31  ? 110 GLU E CG  1 
ATOM   7650  C CD  . GLU E  1 118 ? 27.451  29.926  57.723  1.00 23.55  ? 110 GLU E CD  1 
ATOM   7651  O OE1 . GLU E  1 118 ? 27.580  31.163  57.565  1.00 22.73  ? 110 GLU E OE1 1 
ATOM   7652  O OE2 . GLU E  1 118 ? 26.917  29.442  58.745  1.00 25.98  ? 110 GLU E OE2 1 
ATOM   7653  N N   . VAL E  1 119 ? 25.611  27.378  54.347  1.00 12.37  ? 111 VAL E N   1 
ATOM   7654  C CA  . VAL E  1 119 ? 24.175  27.240  54.177  1.00 14.40  ? 111 VAL E CA  1 
ATOM   7655  C C   . VAL E  1 119 ? 23.512  27.367  55.558  1.00 19.28  ? 111 VAL E C   1 
ATOM   7656  O O   . VAL E  1 119 ? 23.869  26.646  56.501  1.00 20.13  ? 111 VAL E O   1 
ATOM   7657  C CB  . VAL E  1 119 ? 23.822  25.880  53.516  1.00 15.20  ? 111 VAL E CB  1 
ATOM   7658  C CG1 . VAL E  1 119 ? 22.338  25.782  53.195  1.00 11.98  ? 111 VAL E CG1 1 
ATOM   7659  C CG2 . VAL E  1 119 ? 24.644  25.684  52.261  1.00 12.42  ? 111 VAL E CG2 1 
ATOM   7660  N N   . LEU E  1 120 ? 22.568  28.294  55.688  1.00 15.91  ? 112 LEU E N   1 
ATOM   7661  C CA  . LEU E  1 120 ? 21.815  28.442  56.931  1.00 17.19  ? 112 LEU E CA  1 
ATOM   7662  C C   . LEU E  1 120 ? 20.348  28.129  56.664  1.00 15.29  ? 112 LEU E C   1 
ATOM   7663  O O   . LEU E  1 120 ? 19.734  28.752  55.814  1.00 18.40  ? 112 LEU E O   1 
ATOM   7664  C CB  . LEU E  1 120 ? 21.971  29.862  57.487  1.00 16.84  ? 112 LEU E CB  1 
ATOM   7665  C CG  . LEU E  1 120 ? 23.348  30.491  57.203  1.00 23.00  ? 112 LEU E CG  1 
ATOM   7666  C CD1 . LEU E  1 120 ? 23.326  31.378  55.951  1.00 15.37  ? 112 LEU E CD1 1 
ATOM   7667  C CD2 . LEU E  1 120 ? 23.898  31.261  58.405  1.00 17.71  ? 112 LEU E CD2 1 
ATOM   7668  N N   . TYR E  1 121 ? 19.802  27.140  57.362  1.00 15.62  ? 113 TYR E N   1 
ATOM   7669  C CA  . TYR E  1 121 ? 18.365  26.846  57.314  1.00 14.00  ? 113 TYR E CA  1 
ATOM   7670  C C   . TYR E  1 121 ? 17.776  26.845  58.725  1.00 15.51  ? 113 TYR E C   1 
ATOM   7671  O O   . TYR E  1 121 ? 18.157  26.023  59.553  1.00 15.74  ? 113 TYR E O   1 
ATOM   7672  C CB  . TYR E  1 121 ? 18.120  25.490  56.661  1.00 12.57  ? 113 TYR E CB  1 
ATOM   7673  C CG  . TYR E  1 121 ? 16.670  25.072  56.636  1.00 11.19  ? 113 TYR E CG  1 
ATOM   7674  C CD1 . TYR E  1 121 ? 15.695  25.910  56.101  1.00 9.80   ? 113 TYR E CD1 1 
ATOM   7675  C CD2 . TYR E  1 121 ? 16.274  23.826  57.122  1.00 9.70   ? 113 TYR E CD2 1 
ATOM   7676  C CE1 . TYR E  1 121 ? 14.375  25.535  56.067  1.00 7.96   ? 113 TYR E CE1 1 
ATOM   7677  C CE2 . TYR E  1 121 ? 14.942  23.440  57.095  1.00 8.24   ? 113 TYR E CE2 1 
ATOM   7678  C CZ  . TYR E  1 121 ? 13.998  24.301  56.567  1.00 10.63  ? 113 TYR E CZ  1 
ATOM   7679  O OH  . TYR E  1 121 ? 12.664  23.924  56.524  1.00 14.66  ? 113 TYR E OH  1 
ATOM   7680  N N   . MET E  1 122 ? 16.852  27.764  58.993  1.00 18.68  ? 114 MET E N   1 
ATOM   7681  C CA  . MET E  1 122 ? 16.298  27.937  60.336  1.00 16.33  ? 114 MET E CA  1 
ATOM   7682  C C   . MET E  1 122 ? 14.768  27.958  60.340  1.00 15.29  ? 114 MET E C   1 
ATOM   7683  O O   . MET E  1 122 ? 14.161  29.024  60.450  1.00 18.46  ? 114 MET E O   1 
ATOM   7684  C CB  . MET E  1 122 ? 16.827  29.236  60.955  1.00 20.34  ? 114 MET E CB  1 
ATOM   7685  C CG  . MET E  1 122 ? 16.515  29.389  62.457  1.00 31.54  ? 114 MET E CG  1 
ATOM   7686  S SD  . MET E  1 122 ? 16.819  31.031  63.182  1.00 51.20  ? 114 MET E SD  1 
ATOM   7687  C CE  . MET E  1 122 ? 15.251  31.835  62.906  1.00 29.28  ? 114 MET E CE  1 
ATOM   7688  N N   . PRO E  1 123 ? 14.131  26.786  60.229  1.00 11.66  ? 115 PRO E N   1 
ATOM   7689  C CA  . PRO E  1 123 ? 12.660  26.742  60.240  1.00 14.47  ? 115 PRO E CA  1 
ATOM   7690  C C   . PRO E  1 123 ? 12.070  26.826  61.654  1.00 18.18  ? 115 PRO E C   1 
ATOM   7691  O O   . PRO E  1 123 ? 12.704  26.401  62.629  1.00 14.63  ? 115 PRO E O   1 
ATOM   7692  C CB  . PRO E  1 123 ? 12.351  25.364  59.658  1.00 10.72  ? 115 PRO E CB  1 
ATOM   7693  C CG  . PRO E  1 123 ? 13.494  24.529  60.117  1.00 13.46  ? 115 PRO E CG  1 
ATOM   7694  C CD  . PRO E  1 123 ? 14.720  25.441  60.178  1.00 11.38  ? 115 PRO E CD  1 
ATOM   7695  N N   . SER E  1 124 ? 10.861  27.376  61.754  1.00 19.53  ? 116 SER E N   1 
ATOM   7696  C CA  . SER E  1 124 ? 10.123  27.384  63.011  1.00 18.65  ? 116 SER E CA  1 
ATOM   7697  C C   . SER E  1 124 ? 9.271   26.129  63.085  1.00 16.27  ? 116 SER E C   1 
ATOM   7698  O O   . SER E  1 124 ? 8.528   25.817  62.144  1.00 13.67  ? 116 SER E O   1 
ATOM   7699  C CB  . SER E  1 124 ? 9.236   28.620  63.112  1.00 20.52  ? 116 SER E CB  1 
ATOM   7700  O OG  . SER E  1 124 ? 8.490   28.607  64.321  1.00 25.12  ? 116 SER E OG  1 
ATOM   7701  N N   . ILE E  1 125 ? 9.384   25.405  64.195  1.00 12.79  ? 117 ILE E N   1 
ATOM   7702  C CA  . ILE E  1 125 ? 8.708   24.122  64.314  1.00 12.66  ? 117 ILE E CA  1 
ATOM   7703  C C   . ILE E  1 125 ? 7.846   23.981  65.568  1.00 15.91  ? 117 ILE E C   1 
ATOM   7704  O O   . ILE E  1 125 ? 8.277   24.273  66.671  1.00 18.30  ? 117 ILE E O   1 
ATOM   7705  C CB  . ILE E  1 125 ? 9.722   22.963  64.227  1.00 13.23  ? 117 ILE E CB  1 
ATOM   7706  C CG1 . ILE E  1 125 ? 10.540  23.092  62.942  1.00 13.58  ? 117 ILE E CG1 1 
ATOM   7707  C CG2 . ILE E  1 125 ? 9.026   21.603  64.257  1.00 12.84  ? 117 ILE E CG2 1 
ATOM   7708  C CD1 . ILE E  1 125 ? 11.438  21.930  62.683  1.00 14.01  ? 117 ILE E CD1 1 
ATOM   7709  N N   . ARG E  1 126 ? 6.607   23.546  65.384  1.00 17.75  ? 118 ARG E N   1 
ATOM   7710  C CA  . ARG E  1 126 ? 5.808   23.084  66.496  1.00 16.14  ? 118 ARG E CA  1 
ATOM   7711  C C   . ARG E  1 126 ? 5.815   21.565  66.495  1.00 17.64  ? 118 ARG E C   1 
ATOM   7712  O O   . ARG E  1 126 ? 5.327   20.939  65.559  1.00 16.92  ? 118 ARG E O   1 
ATOM   7713  C CB  . ARG E  1 126 ? 4.372   23.599  66.406  1.00 17.85  ? 118 ARG E CB  1 
ATOM   7714  C CG  . ARG E  1 126 ? 3.462   23.081  67.532  1.00 15.89  ? 118 ARG E CG  1 
ATOM   7715  C CD  . ARG E  1 126 ? 2.101   23.744  67.493  1.00 17.90  ? 118 ARG E CD  1 
ATOM   7716  N NE  . ARG E  1 126 ? 1.162   23.180  68.459  1.00 26.42  ? 118 ARG E NE  1 
ATOM   7717  C CZ  . ARG E  1 126 ? -0.083  23.619  68.628  1.00 29.33  ? 118 ARG E CZ  1 
ATOM   7718  N NH1 . ARG E  1 126 ? -0.528  24.637  67.899  1.00 27.59  ? 118 ARG E NH1 1 
ATOM   7719  N NH2 . ARG E  1 126 ? -0.880  23.058  69.532  1.00 29.48  ? 118 ARG E NH2 1 
ATOM   7720  N N   . GLN E  1 127 ? 6.374   20.975  67.543  1.00 18.29  ? 119 GLN E N   1 
ATOM   7721  C CA  . GLN E  1 127 ? 6.352   19.526  67.687  1.00 20.93  ? 119 GLN E CA  1 
ATOM   7722  C C   . GLN E  1 127 ? 5.995   19.102  69.121  1.00 21.75  ? 119 GLN E C   1 
ATOM   7723  O O   . GLN E  1 127 ? 6.058   19.903  70.045  1.00 19.13  ? 119 GLN E O   1 
ATOM   7724  C CB  . GLN E  1 127 ? 7.692   18.919  67.261  1.00 15.12  ? 119 GLN E CB  1 
ATOM   7725  C CG  . GLN E  1 127 ? 7.599   17.449  66.928  1.00 15.66  ? 119 GLN E CG  1 
ATOM   7726  C CD  . GLN E  1 127 ? 8.829   16.910  66.247  1.00 17.81  ? 119 GLN E CD  1 
ATOM   7727  O OE1 . GLN E  1 127 ? 9.897   17.529  66.262  1.00 19.63  ? 119 GLN E OE1 1 
ATOM   7728  N NE2 . GLN E  1 127 ? 8.686   15.747  65.628  1.00 19.44  ? 119 GLN E NE2 1 
ATOM   7729  N N   . ARG E  1 128 ? 5.604   17.841  69.283  1.00 22.44  ? 120 ARG E N   1 
ATOM   7730  C CA  . ARG E  1 128 ? 5.302   17.278  70.588  1.00 22.35  ? 120 ARG E CA  1 
ATOM   7731  C C   . ARG E  1 128 ? 6.326   16.222  70.977  1.00 20.76  ? 120 ARG E C   1 
ATOM   7732  O O   . ARG E  1 128 ? 6.740   15.404  70.163  1.00 18.33  ? 120 ARG E O   1 
ATOM   7733  C CB  . ARG E  1 128 ? 3.894   16.678  70.617  1.00 21.61  ? 120 ARG E CB  1 
ATOM   7734  C CG  . ARG E  1 128 ? 2.798   17.705  70.426  1.00 25.15  ? 120 ARG E CG  1 
ATOM   7735  C CD  . ARG E  1 128 ? 1.427   17.086  70.576  1.00 38.71  ? 120 ARG E CD  1 
ATOM   7736  N NE  . ARG E  1 128 ? 1.404   16.048  71.604  1.00 46.14  ? 120 ARG E NE  1 
ATOM   7737  C CZ  . ARG E  1 128 ? 1.328   16.272  72.915  1.00 44.45  ? 120 ARG E CZ  1 
ATOM   7738  N NH1 . ARG E  1 128 ? 1.276   17.511  73.399  1.00 42.17  ? 120 ARG E NH1 1 
ATOM   7739  N NH2 . ARG E  1 128 ? 1.311   15.245  73.751  1.00 41.91  ? 120 ARG E NH2 1 
ATOM   7740  N N   . PHE E  1 129 ? 6.718   16.228  72.240  1.00 25.14  ? 121 PHE E N   1 
ATOM   7741  C CA  . PHE E  1 129 ? 7.710   15.279  72.700  1.00 21.03  ? 121 PHE E CA  1 
ATOM   7742  C C   . PHE E  1 129 ? 7.250   14.455  73.886  1.00 24.20  ? 121 PHE E C   1 
ATOM   7743  O O   . PHE E  1 129 ? 6.292   14.789  74.578  1.00 22.72  ? 121 PHE E O   1 
ATOM   7744  C CB  . PHE E  1 129 ? 9.010   15.994  73.023  1.00 19.31  ? 121 PHE E CB  1 
ATOM   7745  C CG  . PHE E  1 129 ? 9.604   16.704  71.850  1.00 22.99  ? 121 PHE E CG  1 
ATOM   7746  C CD1 . PHE E  1 129 ? 9.185   17.979  71.510  1.00 22.35  ? 121 PHE E CD1 1 
ATOM   7747  C CD2 . PHE E  1 129 ? 10.571  16.091  71.074  1.00 23.15  ? 121 PHE E CD2 1 
ATOM   7748  C CE1 . PHE E  1 129 ? 9.727   18.638  70.428  1.00 20.94  ? 121 PHE E CE1 1 
ATOM   7749  C CE2 . PHE E  1 129 ? 11.126  16.747  69.992  1.00 22.62  ? 121 PHE E CE2 1 
ATOM   7750  C CZ  . PHE E  1 129 ? 10.706  18.023  69.668  1.00 23.10  ? 121 PHE E CZ  1 
ATOM   7751  N N   . SER E  1 130 ? 7.947   13.348  74.080  1.00 26.13  ? 122 SER E N   1 
ATOM   7752  C CA  . SER E  1 130 ? 7.736   12.469  75.204  1.00 23.69  ? 122 SER E CA  1 
ATOM   7753  C C   . SER E  1 130 ? 8.922   12.657  76.138  1.00 29.80  ? 122 SER E C   1 
ATOM   7754  O O   . SER E  1 130 ? 10.012  12.121  75.897  1.00 31.99  ? 122 SER E O   1 
ATOM   7755  C CB  . SER E  1 130 ? 7.657   11.034  74.708  1.00 17.71  ? 122 SER E CB  1 
ATOM   7756  O OG  . SER E  1 130 ? 7.957   10.123  75.736  1.00 22.28  ? 122 SER E OG  1 
ATOM   7757  N N   . CYS E  1 131 ? 8.726   13.465  77.184  1.00 28.94  ? 123 CYS E N   1 
ATOM   7758  C CA  . CYS E  1 131 ? 9.807   13.880  78.091  1.00 35.71  ? 123 CYS E CA  1 
ATOM   7759  C C   . CYS E  1 131 ? 9.371   14.056  79.556  1.00 35.89  ? 123 CYS E C   1 
ATOM   7760  O O   . CYS E  1 131 ? 8.181   14.193  79.842  1.00 30.58  ? 123 CYS E O   1 
ATOM   7761  C CB  . CYS E  1 131 ? 10.462  15.167  77.584  1.00 41.37  ? 123 CYS E CB  1 
ATOM   7762  S SG  . CYS E  1 131 ? 9.431   16.643  77.743  1.00 46.68  ? 123 CYS E SG  1 
ATOM   7763  N N   . ASP E  1 132 ? 10.338  14.048  80.477  1.00 34.06  ? 124 ASP E N   1 
ATOM   7764  C CA  . ASP E  1 132 ? 10.055  14.158  81.902  1.00 33.51  ? 124 ASP E CA  1 
ATOM   7765  C C   . ASP E  1 132 ? 9.562   15.544  82.285  1.00 34.78  ? 124 ASP E C   1 
ATOM   7766  O O   . ASP E  1 132 ? 10.340  16.494  82.343  1.00 32.25  ? 124 ASP E O   1 
ATOM   7767  C CB  . ASP E  1 132 ? 11.278  13.815  82.753  1.00 35.97  ? 124 ASP E CB  1 
ATOM   7768  C CG  . ASP E  1 132 ? 10.982  13.898  84.246  1.00 39.19  ? 124 ASP E CG  1 
ATOM   7769  O OD1 . ASP E  1 132 ? 10.786  12.841  84.880  1.00 33.71  ? 124 ASP E OD1 1 
ATOM   7770  O OD2 . ASP E  1 132 ? 10.921  15.026  84.781  1.00 44.52  ? 124 ASP E OD2 1 
ATOM   7771  N N   . VAL E  1 133 ? 8.269   15.631  82.582  1.00 34.58  ? 125 VAL E N   1 
ATOM   7772  C CA  . VAL E  1 133 ? 7.633   16.877  82.978  1.00 33.40  ? 125 VAL E CA  1 
ATOM   7773  C C   . VAL E  1 133 ? 7.400   16.922  84.486  1.00 40.17  ? 125 VAL E C   1 
ATOM   7774  O O   . VAL E  1 133 ? 6.831   17.883  84.998  1.00 36.44  ? 125 VAL E O   1 
ATOM   7775  C CB  . VAL E  1 133 ? 6.278   17.014  82.302  1.00 34.15  ? 125 VAL E CB  1 
ATOM   7776  C CG1 . VAL E  1 133 ? 5.877   18.473  82.210  1.00 40.81  ? 125 VAL E CG1 1 
ATOM   7777  C CG2 . VAL E  1 133 ? 6.337   16.403  80.925  1.00 42.18  ? 125 VAL E CG2 1 
ATOM   7778  N N   . SER E  1 134 ? 7.834   15.875  85.191  1.00 43.69  ? 126 SER E N   1 
ATOM   7779  C CA  . SER E  1 134 ? 7.680   15.805  86.645  1.00 43.97  ? 126 SER E CA  1 
ATOM   7780  C C   . SER E  1 134 ? 8.353   16.987  87.341  1.00 39.94  ? 126 SER E C   1 
ATOM   7781  O O   . SER E  1 134 ? 9.520   17.294  87.084  1.00 33.84  ? 126 SER E O   1 
ATOM   7782  C CB  . SER E  1 134 ? 8.266   14.503  87.190  1.00 37.35  ? 126 SER E CB  1 
ATOM   7783  O OG  . SER E  1 134 ? 9.665   14.630  87.354  1.00 35.42  ? 126 SER E OG  1 
ATOM   7784  N N   . GLY E  1 135 ? 7.607   17.651  88.219  1.00 37.11  ? 127 GLY E N   1 
ATOM   7785  C CA  . GLY E  1 135 ? 8.169   18.728  89.009  1.00 36.04  ? 127 GLY E CA  1 
ATOM   7786  C C   . GLY E  1 135 ? 8.050   20.076  88.341  1.00 37.59  ? 127 GLY E C   1 
ATOM   7787  O O   . GLY E  1 135 ? 8.767   21.013  88.689  1.00 39.39  ? 127 GLY E O   1 
ATOM   7788  N N   . VAL E  1 136 ? 7.128   20.174  87.391  1.00 36.67  ? 128 VAL E N   1 
ATOM   7789  C CA  . VAL E  1 136 ? 6.927   21.386  86.612  1.00 29.91  ? 128 VAL E CA  1 
ATOM   7790  C C   . VAL E  1 136 ? 6.267   22.491  87.443  1.00 40.32  ? 128 VAL E C   1 
ATOM   7791  O O   . VAL E  1 136 ? 6.614   23.666  87.303  1.00 39.99  ? 128 VAL E O   1 
ATOM   7792  C CB  . VAL E  1 136 ? 6.092   21.078  85.338  1.00 35.79  ? 128 VAL E CB  1 
ATOM   7793  C CG1 . VAL E  1 136 ? 4.769   20.428  85.705  1.00 36.61  ? 128 VAL E CG1 1 
ATOM   7794  C CG2 . VAL E  1 136 ? 5.870   22.324  84.498  1.00 32.40  ? 128 VAL E CG2 1 
ATOM   7795  N N   . ASP E  1 137 ? 5.332   22.106  88.315  1.00 43.77  ? 129 ASP E N   1 
ATOM   7796  C CA  . ASP E  1 137 ? 4.599   23.053  89.157  1.00 38.13  ? 129 ASP E CA  1 
ATOM   7797  C C   . ASP E  1 137 ? 5.446   23.608  90.289  1.00 39.03  ? 129 ASP E C   1 
ATOM   7798  O O   . ASP E  1 137 ? 5.117   24.646  90.865  1.00 46.71  ? 129 ASP E O   1 
ATOM   7799  C CB  . ASP E  1 137 ? 3.344   22.406  89.747  1.00 41.02  ? 129 ASP E CB  1 
ATOM   7800  C CG  . ASP E  1 137 ? 2.163   22.466  88.806  1.00 53.15  ? 129 ASP E CG  1 
ATOM   7801  O OD1 . ASP E  1 137 ? 2.278   23.171  87.783  1.00 55.94  ? 129 ASP E OD1 1 
ATOM   7802  O OD2 . ASP E  1 137 ? 1.122   21.823  89.089  1.00 56.46  ? 129 ASP E OD2 1 
ATOM   7803  N N   . THR E  1 138 ? 6.553   22.905  90.535  1.00 33.95  ? 130 THR E N   1 
ATOM   7804  C CA  . THR E  1 138 ? 7.589   23.246  91.510  1.00 34.93  ? 130 THR E CA  1 
ATOM   7805  C C   . THR E  1 138 ? 8.484   24.401  91.059  1.00 37.71  ? 130 THR E C   1 
ATOM   7806  O O   . THR E  1 138 ? 8.500   24.771  89.884  1.00 35.44  ? 130 THR E O   1 
ATOM   7807  C CB  . THR E  1 138 ? 8.473   22.028  91.839  1.00 26.54  ? 130 THR E CB  1 
ATOM   7808  O OG1 . THR E  1 138 ? 9.484   21.882  90.834  1.00 39.10  ? 130 THR E OG1 1 
ATOM   7809  C CG2 . THR E  1 138 ? 7.634   20.761  91.897  1.00 20.09  ? 130 THR E CG2 1 
ATOM   7810  N N   . GLU E  1 139 ? 9.213   24.972  92.013  1.00 42.95  ? 131 GLU E N   1 
ATOM   7811  C CA  . GLU E  1 139 ? 9.913   26.234  91.830  1.00 48.99  ? 131 GLU E CA  1 
ATOM   7812  C C   . GLU E  1 139 ? 11.193  25.971  91.058  1.00 45.56  ? 131 GLU E C   1 
ATOM   7813  O O   . GLU E  1 139 ? 11.748  26.867  90.414  1.00 41.96  ? 131 GLU E O   1 
ATOM   7814  C CB  . GLU E  1 139 ? 10.224  26.862  93.191  1.00 49.38  ? 131 GLU E CB  1 
ATOM   7815  C CG  . GLU E  1 139 ? 10.472  28.363  93.158  1.00 56.87  ? 131 GLU E CG  1 
ATOM   7816  C CD  . GLU E  1 139 ? 11.103  28.876  94.445  1.00 69.90  ? 131 GLU E CD  1 
ATOM   7817  O OE1 . GLU E  1 139 ? 11.982  28.177  94.998  1.00 66.74  ? 131 GLU E OE1 1 
ATOM   7818  O OE2 . GLU E  1 139 ? 10.717  29.974  94.906  1.00 70.45  ? 131 GLU E OE2 1 
ATOM   7819  N N   . SER E  1 140 ? 11.652  24.726  91.139  1.00 42.85  ? 132 SER E N   1 
ATOM   7820  C CA  . SER E  1 140 ? 12.821  24.277  90.390  1.00 45.87  ? 132 SER E CA  1 
ATOM   7821  C C   . SER E  1 140 ? 12.449  23.715  89.007  1.00 38.97  ? 132 SER E C   1 
ATOM   7822  O O   . SER E  1 140 ? 13.299  23.600  88.139  1.00 32.39  ? 132 SER E O   1 
ATOM   7823  C CB  . SER E  1 140 ? 13.636  23.267  91.206  1.00 42.99  ? 132 SER E CB  1 
ATOM   7824  O OG  . SER E  1 140 ? 14.759  23.895  91.807  1.00 49.71  ? 132 SER E OG  1 
ATOM   7825  N N   . GLY E  1 141 ? 11.180  23.361  88.815  1.00 39.32  ? 133 GLY E N   1 
ATOM   7826  C CA  . GLY E  1 141 ? 10.658  23.078  87.490  1.00 34.06  ? 133 GLY E CA  1 
ATOM   7827  C C   . GLY E  1 141 ? 11.076  21.752  86.886  1.00 35.78  ? 133 GLY E C   1 
ATOM   7828  O O   . GLY E  1 141 ? 11.868  21.020  87.470  1.00 37.46  ? 133 GLY E O   1 
ATOM   7829  N N   . ALA E  1 142 ? 10.539  21.443  85.706  1.00 35.16  ? 134 ALA E N   1 
ATOM   7830  C CA  . ALA E  1 142 ? 10.889  20.212  85.001  1.00 36.19  ? 134 ALA E CA  1 
ATOM   7831  C C   . ALA E  1 142 ? 12.211  20.352  84.247  1.00 32.59  ? 134 ALA E C   1 
ATOM   7832  O O   . ALA E  1 142 ? 12.669  21.461  83.981  1.00 33.38  ? 134 ALA E O   1 
ATOM   7833  C CB  . ALA E  1 142 ? 9.782   19.821  84.047  1.00 35.31  ? 134 ALA E CB  1 
ATOM   7834  N N   . THR E  1 143 ? 12.843  19.229  83.940  1.00 29.29  ? 135 THR E N   1 
ATOM   7835  C CA  . THR E  1 143 ? 13.937  19.242  82.977  1.00 35.39  ? 135 THR E CA  1 
ATOM   7836  C C   . THR E  1 143 ? 13.617  18.268  81.850  1.00 38.15  ? 135 THR E C   1 
ATOM   7837  O O   . THR E  1 143 ? 13.604  17.042  82.036  1.00 33.82  ? 135 THR E O   1 
ATOM   7838  C CB  . THR E  1 143 ? 15.318  18.953  83.599  1.00 35.16  ? 135 THR E CB  1 
ATOM   7839  O OG1 . THR E  1 143 ? 15.770  20.119  84.301  1.00 40.36  ? 135 THR E OG1 1 
ATOM   7840  C CG2 . THR E  1 143 ? 16.337  18.629  82.500  1.00 38.76  ? 135 THR E CG2 1 
ATOM   7841  N N   . CYS E  1 144 ? 13.308  18.826  80.686  1.00 33.31  ? 136 CYS E N   1 
ATOM   7842  C CA  . CYS E  1 144 ? 12.877  18.024  79.556  1.00 34.11  ? 136 CYS E CA  1 
ATOM   7843  C C   . CYS E  1 144 ? 14.024  17.893  78.576  1.00 36.45  ? 136 CYS E C   1 
ATOM   7844  O O   . CYS E  1 144 ? 14.596  18.887  78.130  1.00 31.16  ? 136 CYS E O   1 
ATOM   7845  C CB  . CYS E  1 144 ? 11.669  18.665  78.871  1.00 32.81  ? 136 CYS E CB  1 
ATOM   7846  S SG  . CYS E  1 144 ? 10.070  18.051  79.451  1.00 64.75  ? 136 CYS E SG  1 
ATOM   7847  N N   . ARG E  1 145 ? 14.360  16.653  78.251  1.00 35.24  ? 137 ARG E N   1 
ATOM   7848  C CA  . ARG E  1 145 ? 15.492  16.383  77.386  1.00 32.28  ? 137 ARG E CA  1 
ATOM   7849  C C   . ARG E  1 145 ? 15.040  15.912  76.010  1.00 29.88  ? 137 ARG E C   1 
ATOM   7850  O O   . ARG E  1 145 ? 14.273  14.959  75.890  1.00 33.74  ? 137 ARG E O   1 
ATOM   7851  C CB  . ARG E  1 145 ? 16.431  15.372  78.047  1.00 42.21  ? 137 ARG E CB  1 
ATOM   7852  C CG  . ARG E  1 145 ? 17.158  15.927  79.268  1.00 43.59  ? 137 ARG E CG  1 
ATOM   7853  C CD  . ARG E  1 145 ? 18.017  14.869  79.949  1.00 52.97  ? 137 ARG E CD  1 
ATOM   7854  N NE  . ARG E  1 145 ? 17.343  14.263  81.096  1.00 57.36  ? 137 ARG E NE  1 
ATOM   7855  C CZ  . ARG E  1 145 ? 17.458  14.709  82.344  1.00 67.93  ? 137 ARG E CZ  1 
ATOM   7856  N NH1 . ARG E  1 145 ? 18.225  15.767  82.590  1.00 58.02  ? 137 ARG E NH1 1 
ATOM   7857  N NH2 . ARG E  1 145 ? 16.812  14.102  83.342  1.00 61.56  ? 137 ARG E NH2 1 
ATOM   7858  N N   . ILE E  1 146 ? 15.517  16.614  74.984  1.00 28.71  ? 138 ILE E N   1 
ATOM   7859  C CA  . ILE E  1 146 ? 15.181  16.356  73.589  1.00 23.32  ? 138 ILE E CA  1 
ATOM   7860  C C   . ILE E  1 146 ? 16.447  15.944  72.859  1.00 24.71  ? 138 ILE E C   1 
ATOM   7861  O O   . ILE E  1 146 ? 17.480  16.589  73.008  1.00 26.62  ? 138 ILE E O   1 
ATOM   7862  C CB  . ILE E  1 146 ? 14.651  17.627  72.930  1.00 21.83  ? 138 ILE E CB  1 
ATOM   7863  C CG1 . ILE E  1 146 ? 13.190  17.842  73.296  1.00 19.67  ? 138 ILE E CG1 1 
ATOM   7864  C CG2 . ILE E  1 146 ? 14.800  17.563  71.412  1.00 27.81  ? 138 ILE E CG2 1 
ATOM   7865  C CD1 . ILE E  1 146 ? 12.693  19.209  72.933  1.00 16.24  ? 138 ILE E CD1 1 
ATOM   7866  N N   . LYS E  1 147 ? 16.374  14.870  72.080  1.00 22.17  ? 139 LYS E N   1 
ATOM   7867  C CA  . LYS E  1 147 ? 17.547  14.368  71.370  1.00 24.91  ? 139 LYS E CA  1 
ATOM   7868  C C   . LYS E  1 147 ? 17.408  14.428  69.837  1.00 24.69  ? 139 LYS E C   1 
ATOM   7869  O O   . LYS E  1 147 ? 16.549  13.758  69.251  1.00 17.98  ? 139 LYS E O   1 
ATOM   7870  C CB  . LYS E  1 147 ? 17.866  12.948  71.832  1.00 27.03  ? 139 LYS E CB  1 
ATOM   7871  C CG  . LYS E  1 147 ? 18.878  12.900  72.950  1.00 30.38  ? 139 LYS E CG  1 
ATOM   7872  C CD  . LYS E  1 147 ? 19.117  11.467  73.401  1.00 46.87  ? 139 LYS E CD  1 
ATOM   7873  C CE  . LYS E  1 147 ? 20.420  11.341  74.182  1.00 55.51  ? 139 LYS E CE  1 
ATOM   7874  N NZ  . LYS E  1 147 ? 21.644  11.508  73.329  1.00 50.54  ? 139 LYS E NZ  1 
ATOM   7875  N N   . ILE E  1 148 ? 18.256  15.237  69.200  1.00 26.22  ? 140 ILE E N   1 
ATOM   7876  C CA  . ILE E  1 148 ? 18.218  15.418  67.748  1.00 23.31  ? 140 ILE E CA  1 
ATOM   7877  C C   . ILE E  1 148 ? 19.536  15.007  67.100  1.00 28.32  ? 140 ILE E C   1 
ATOM   7878  O O   . ILE E  1 148 ? 20.599  15.427  67.542  1.00 32.26  ? 140 ILE E O   1 
ATOM   7879  C CB  . ILE E  1 148 ? 17.899  16.888  67.356  1.00 21.81  ? 140 ILE E CB  1 
ATOM   7880  C CG1 . ILE E  1 148 ? 16.422  17.201  67.594  1.00 24.46  ? 140 ILE E CG1 1 
ATOM   7881  C CG2 . ILE E  1 148 ? 18.229  17.143  65.886  1.00 25.42  ? 140 ILE E CG2 1 
ATOM   7882  C CD1 . ILE E  1 148 ? 15.851  18.321  66.713  1.00 25.97  ? 140 ILE E CD1 1 
ATOM   7883  N N   . GLY E  1 149 ? 19.463  14.192  66.049  1.00 28.22  ? 141 GLY E N   1 
ATOM   7884  C CA  . GLY E  1 149 ? 20.641  13.806  65.288  1.00 22.48  ? 141 GLY E CA  1 
ATOM   7885  C C   . GLY E  1 149 ? 20.286  13.276  63.912  1.00 19.56  ? 141 GLY E C   1 
ATOM   7886  O O   . GLY E  1 149 ? 19.118  13.226  63.546  1.00 17.62  ? 141 GLY E O   1 
ATOM   7887  N N   . SER E  1 150 ? 21.293  12.882  63.137  1.00 27.77  ? 142 SER E N   1 
ATOM   7888  C CA  . SER E  1 150 ? 21.045  12.340  61.803  1.00 17.52  ? 142 SER E CA  1 
ATOM   7889  C C   . SER E  1 150 ? 20.286  11.037  61.930  1.00 16.94  ? 142 SER E C   1 
ATOM   7890  O O   . SER E  1 150 ? 20.625  10.201  62.753  1.00 20.92  ? 142 SER E O   1 
ATOM   7891  C CB  . SER E  1 150 ? 22.359  12.119  61.053  1.00 24.30  ? 142 SER E CB  1 
ATOM   7892  O OG  . SER E  1 150 ? 22.152  11.538  59.768  1.00 25.45  ? 142 SER E OG  1 
ATOM   7893  N N   . TRP E  1 151 ? 19.249  10.872  61.122  1.00 17.82  ? 143 TRP E N   1 
ATOM   7894  C CA  . TRP E  1 151 ? 18.455  9.662   61.173  1.00 14.51  ? 143 TRP E CA  1 
ATOM   7895  C C   . TRP E  1 151 ? 19.069  8.474   60.413  1.00 19.23  ? 143 TRP E C   1 
ATOM   7896  O O   . TRP E  1 151 ? 18.844  7.329   60.781  1.00 21.72  ? 143 TRP E O   1 
ATOM   7897  C CB  . TRP E  1 151 ? 17.039  9.930   60.687  1.00 13.27  ? 143 TRP E CB  1 
ATOM   7898  C CG  . TRP E  1 151 ? 16.153  8.727   60.808  1.00 16.88  ? 143 TRP E CG  1 
ATOM   7899  C CD1 . TRP E  1 151 ? 15.520  8.081   59.799  1.00 16.01  ? 143 TRP E CD1 1 
ATOM   7900  C CD2 . TRP E  1 151 ? 15.825  8.012   62.014  1.00 19.63  ? 143 TRP E CD2 1 
ATOM   7901  N NE1 . TRP E  1 151 ? 14.811  7.012   60.290  1.00 19.07  ? 143 TRP E NE1 1 
ATOM   7902  C CE2 . TRP E  1 151 ? 14.988  6.941   61.646  1.00 18.63  ? 143 TRP E CE2 1 
ATOM   7903  C CE3 . TRP E  1 151 ? 16.155  8.179   63.368  1.00 18.96  ? 143 TRP E CE3 1 
ATOM   7904  C CZ2 . TRP E  1 151 ? 14.462  6.043   62.581  1.00 20.87  ? 143 TRP E CZ2 1 
ATOM   7905  C CZ3 . TRP E  1 151 ? 15.638  7.280   64.301  1.00 23.40  ? 143 TRP E CZ3 1 
ATOM   7906  C CH2 . TRP E  1 151 ? 14.799  6.228   63.902  1.00 23.16  ? 143 TRP E CH2 1 
ATOM   7907  N N   . THR E  1 152 ? 19.836  8.728   59.357  1.00 17.31  ? 144 THR E N   1 
ATOM   7908  C CA  . THR E  1 152 ? 20.371  7.620   58.569  1.00 16.12  ? 144 THR E CA  1 
ATOM   7909  C C   . THR E  1 152 ? 21.891  7.649   58.440  1.00 17.92  ? 144 THR E C   1 
ATOM   7910  O O   . THR E  1 152 ? 22.508  6.636   58.133  1.00 18.69  ? 144 THR E O   1 
ATOM   7911  C CB  . THR E  1 152 ? 19.663  7.463   57.169  1.00 17.12  ? 144 THR E CB  1 
ATOM   7912  O OG1 . THR E  1 152 ? 19.980  8.560   56.299  1.00 16.04  ? 144 THR E OG1 1 
ATOM   7913  C CG2 . THR E  1 152 ? 18.149  7.390   57.340  1.00 17.85  ? 144 THR E CG2 1 
ATOM   7914  N N   . HIS E  1 153 ? 22.505  8.795   58.703  1.00 20.86  ? 145 HIS E N   1 
ATOM   7915  C CA  . HIS E  1 153 ? 23.957  8.895   58.549  1.00 25.72  ? 145 HIS E CA  1 
ATOM   7916  C C   . HIS E  1 153 ? 24.727  8.769   59.864  1.00 31.13  ? 145 HIS E C   1 
ATOM   7917  O O   . HIS E  1 153 ? 24.661  9.650   60.719  1.00 28.85  ? 145 HIS E O   1 
ATOM   7918  C CB  . HIS E  1 153 ? 24.345  10.198  57.846  1.00 25.24  ? 145 HIS E CB  1 
ATOM   7919  C CG  . HIS E  1 153 ? 23.780  10.332  56.467  1.00 24.59  ? 145 HIS E CG  1 
ATOM   7920  N ND1 . HIS E  1 153 ? 22.718  11.162  56.173  1.00 23.57  ? 145 HIS E ND1 1 
ATOM   7921  C CD2 . HIS E  1 153 ? 24.124  9.733   55.303  1.00 20.93  ? 145 HIS E CD2 1 
ATOM   7922  C CE1 . HIS E  1 153 ? 22.435  11.069  54.887  1.00 25.00  ? 145 HIS E CE1 1 
ATOM   7923  N NE2 . HIS E  1 153 ? 23.276  10.212  54.335  1.00 22.14  ? 145 HIS E NE2 1 
ATOM   7924  N N   . HIS E  1 154 ? 25.473  7.679   60.010  1.00 34.95  ? 146 HIS E N   1 
ATOM   7925  C CA  . HIS E  1 154 ? 26.273  7.473   61.207  1.00 35.44  ? 146 HIS E CA  1 
ATOM   7926  C C   . HIS E  1 154 ? 27.413  8.496   61.316  1.00 37.86  ? 146 HIS E C   1 
ATOM   7927  O O   . HIS E  1 154 ? 27.650  9.274   60.386  1.00 30.83  ? 146 HIS E O   1 
ATOM   7928  C CB  . HIS E  1 154 ? 26.761  6.021   61.311  1.00 37.81  ? 146 HIS E CB  1 
ATOM   7929  C CG  . HIS E  1 154 ? 27.253  5.440   60.019  1.00 48.43  ? 146 HIS E CG  1 
ATOM   7930  N ND1 . HIS E  1 154 ? 28.478  5.765   59.471  1.00 53.29  ? 146 HIS E ND1 1 
ATOM   7931  C CD2 . HIS E  1 154 ? 26.696  4.537   59.176  1.00 53.04  ? 146 HIS E CD2 1 
ATOM   7932  C CE1 . HIS E  1 154 ? 28.647  5.102   58.339  1.00 45.22  ? 146 HIS E CE1 1 
ATOM   7933  N NE2 . HIS E  1 154 ? 27.578  4.351   58.135  1.00 52.62  ? 146 HIS E NE2 1 
ATOM   7934  N N   . SER E  1 155 ? 28.084  8.496   62.470  1.00 44.24  ? 147 SER E N   1 
ATOM   7935  C CA  . SER E  1 155 ? 29.098  9.497   62.839  1.00 36.28  ? 147 SER E CA  1 
ATOM   7936  C C   . SER E  1 155 ? 30.146  9.759   61.771  1.00 37.08  ? 147 SER E C   1 
ATOM   7937  O O   . SER E  1 155 ? 30.604  10.893  61.608  1.00 36.97  ? 147 SER E O   1 
ATOM   7938  C CB  . SER E  1 155 ? 29.817  9.070   64.123  1.00 44.14  ? 147 SER E CB  1 
ATOM   7939  O OG  . SER E  1 155 ? 30.630  7.923   63.898  1.00 43.63  ? 147 SER E OG  1 
ATOM   7940  N N   . ARG E  1 156 ? 30.534  8.700   61.063  1.00 39.13  ? 148 ARG E N   1 
ATOM   7941  C CA  . ARG E  1 156 ? 31.558  8.773   60.029  1.00 31.70  ? 148 ARG E CA  1 
ATOM   7942  C C   . ARG E  1 156 ? 31.136  9.697   58.886  1.00 38.77  ? 148 ARG E C   1 
ATOM   7943  O O   . ARG E  1 156 ? 31.984  10.264  58.196  1.00 40.69  ? 148 ARG E O   1 
ATOM   7944  C CB  . ARG E  1 156 ? 31.835  7.368   59.493  1.00 39.13  ? 148 ARG E CB  1 
ATOM   7945  C CG  . ARG E  1 156 ? 32.943  7.283   58.458  1.00 50.96  ? 148 ARG E CG  1 
ATOM   7946  C CD  . ARG E  1 156 ? 34.307  7.220   59.125  1.00 57.72  ? 148 ARG E CD  1 
ATOM   7947  N NE  . ARG E  1 156 ? 34.380  6.132   60.099  1.00 61.23  ? 148 ARG E NE  1 
ATOM   7948  C CZ  . ARG E  1 156 ? 34.621  4.866   59.778  1.00 62.22  ? 148 ARG E CZ  1 
ATOM   7949  N NH1 . ARG E  1 156 ? 34.801  4.542   58.512  1.00 67.46  ? 148 ARG E NH1 1 
ATOM   7950  N NH2 . ARG E  1 156 ? 34.680  3.926   60.712  1.00 63.16  ? 148 ARG E NH2 1 
ATOM   7951  N N   . GLU E  1 157 ? 29.824  9.859   58.700  1.00 37.97  ? 149 GLU E N   1 
ATOM   7952  C CA  . GLU E  1 157 ? 29.281  10.615  57.565  1.00 29.04  ? 149 GLU E CA  1 
ATOM   7953  C C   . GLU E  1 157 ? 28.774  12.023  57.915  1.00 25.95  ? 149 GLU E C   1 
ATOM   7954  O O   . GLU E  1 157 ? 28.926  12.960  57.125  1.00 24.11  ? 149 GLU E O   1 
ATOM   7955  C CB  . GLU E  1 157 ? 28.204  9.779   56.869  1.00 23.94  ? 149 GLU E CB  1 
ATOM   7956  C CG  . GLU E  1 157 ? 28.719  8.390   56.533  1.00 28.39  ? 149 GLU E CG  1 
ATOM   7957  C CD  . GLU E  1 157 ? 27.733  7.543   55.762  1.00 32.74  ? 149 GLU E CD  1 
ATOM   7958  O OE1 . GLU E  1 157 ? 26.522  7.620   56.055  1.00 28.23  ? 149 GLU E OE1 1 
ATOM   7959  O OE2 . GLU E  1 157 ? 28.177  6.792   54.859  1.00 37.54  ? 149 GLU E OE2 1 
ATOM   7960  N N   . ILE E  1 158 ? 28.191  12.167  59.103  1.00 24.41  ? 150 ILE E N   1 
ATOM   7961  C CA  . ILE E  1 158 ? 27.680  13.448  59.584  1.00 24.38  ? 150 ILE E CA  1 
ATOM   7962  C C   . ILE E  1 158 ? 27.993  13.627  61.070  1.00 27.44  ? 150 ILE E C   1 
ATOM   7963  O O   . ILE E  1 158 ? 27.717  12.732  61.875  1.00 28.00  ? 150 ILE E O   1 
ATOM   7964  C CB  . ILE E  1 158 ? 26.124  13.542  59.420  1.00 28.24  ? 150 ILE E CB  1 
ATOM   7965  C CG1 . ILE E  1 158 ? 25.709  13.445  57.951  1.00 21.90  ? 150 ILE E CG1 1 
ATOM   7966  C CG2 . ILE E  1 158 ? 25.574  14.829  60.042  1.00 21.58  ? 150 ILE E CG2 1 
ATOM   7967  C CD1 . ILE E  1 158 ? 24.247  13.751  57.714  1.00 20.47  ? 150 ILE E CD1 1 
ATOM   7968  N N   . SER E  1 159 ? 28.562  14.775  61.439  1.00 27.23  ? 151 SER E N   1 
ATOM   7969  C CA  . SER E  1 159 ? 28.661  15.155  62.851  1.00 27.37  ? 151 SER E CA  1 
ATOM   7970  C C   . SER E  1 159 ? 27.704  16.298  63.128  1.00 26.76  ? 151 SER E C   1 
ATOM   7971  O O   . SER E  1 159 ? 27.606  17.225  62.327  1.00 28.62  ? 151 SER E O   1 
ATOM   7972  C CB  . SER E  1 159 ? 30.071  15.616  63.239  1.00 22.53  ? 151 SER E CB  1 
ATOM   7973  O OG  . SER E  1 159 ? 31.040  15.292  62.266  1.00 31.22  ? 151 SER E OG  1 
ATOM   7974  N N   . VAL E  1 160 ? 27.008  16.251  64.261  1.00 26.10  ? 152 VAL E N   1 
ATOM   7975  C CA  . VAL E  1 160 ? 26.241  17.414  64.703  1.00 29.08  ? 152 VAL E CA  1 
ATOM   7976  C C   . VAL E  1 160 ? 26.886  18.056  65.939  1.00 30.06  ? 152 VAL E C   1 
ATOM   7977  O O   . VAL E  1 160 ? 27.379  17.366  66.827  1.00 35.47  ? 152 VAL E O   1 
ATOM   7978  C CB  . VAL E  1 160 ? 24.739  17.089  64.929  1.00 24.98  ? 152 VAL E CB  1 
ATOM   7979  C CG1 . VAL E  1 160 ? 24.289  15.970  64.000  1.00 22.57  ? 152 VAL E CG1 1 
ATOM   7980  C CG2 . VAL E  1 160 ? 24.486  16.698  66.357  1.00 31.24  ? 152 VAL E CG2 1 
ATOM   7981  N N   . ASP E  1 161 ? 26.905  19.385  65.961  1.00 30.06  ? 153 ASP E N   1 
ATOM   7982  C CA  . ASP E  1 161 ? 27.573  20.159  66.997  1.00 32.08  ? 153 ASP E CA  1 
ATOM   7983  C C   . ASP E  1 161 ? 26.693  21.323  67.433  1.00 43.85  ? 153 ASP E C   1 
ATOM   7984  O O   . ASP E  1 161 ? 26.076  21.977  66.588  1.00 39.63  ? 153 ASP E O   1 
ATOM   7985  C CB  . ASP E  1 161 ? 28.892  20.719  66.470  1.00 33.85  ? 153 ASP E CB  1 
ATOM   7986  C CG  . ASP E  1 161 ? 30.025  19.707  66.527  1.00 57.21  ? 153 ASP E CG  1 
ATOM   7987  O OD1 . ASP E  1 161 ? 29.765  18.491  66.374  1.00 52.50  ? 153 ASP E OD1 1 
ATOM   7988  O OD2 . ASP E  1 161 ? 31.186  20.131  66.732  1.00 67.15  ? 153 ASP E OD2 1 
ATOM   7989  N N   . PRO E  1 162 ? 26.636  21.593  68.752  1.00 45.26  ? 154 PRO E N   1 
ATOM   7990  C CA  . PRO E  1 162 ? 25.893  22.728  69.325  1.00 42.49  ? 154 PRO E CA  1 
ATOM   7991  C C   . PRO E  1 162 ? 26.597  24.083  69.147  1.00 45.21  ? 154 PRO E C   1 
ATOM   7992  O O   . PRO E  1 162 ? 27.779  24.122  68.809  1.00 45.00  ? 154 PRO E O   1 
ATOM   7993  C CB  . PRO E  1 162 ? 25.824  22.375  70.810  1.00 41.90  ? 154 PRO E CB  1 
ATOM   7994  C CG  . PRO E  1 162 ? 27.043  21.546  71.044  1.00 45.29  ? 154 PRO E CG  1 
ATOM   7995  C CD  . PRO E  1 162 ? 27.210  20.727  69.799  1.00 40.91  ? 154 PRO E CD  1 
ATOM   7996  N N   . THR E  1 163 ? 25.869  25.175  69.373  1.00 46.38  ? 155 THR E N   1 
ATOM   7997  C CA  . THR E  1 163 ? 26.445  26.517  69.307  1.00 46.27  ? 155 THR E CA  1 
ATOM   7998  C C   . THR E  1 163 ? 25.642  27.532  70.133  1.00 56.43  ? 155 THR E C   1 
ATOM   7999  O O   . THR E  1 163 ? 25.955  27.807  71.301  1.00 53.03  ? 155 THR E O   1 
ATOM   8000  C CB  . THR E  1 163 ? 26.556  27.012  67.852  1.00 49.99  ? 155 THR E CB  1 
ATOM   8001  O OG1 . THR E  1 163 ? 26.884  28.408  67.843  1.00 53.59  ? 155 THR E OG1 1 
ATOM   8002  C CG2 . THR E  1 163 ? 25.242  26.800  67.108  1.00 43.63  ? 155 THR E CG2 1 
ATOM   8003  N N   . SER E  1 167 ? 22.379  28.817  77.416  1.00 39.10  ? 159 SER E N   1 
ATOM   8004  C CA  . SER E  1 167 ? 21.551  30.016  77.309  1.00 51.79  ? 159 SER E CA  1 
ATOM   8005  C C   . SER E  1 167 ? 20.236  29.880  78.093  1.00 50.62  ? 159 SER E C   1 
ATOM   8006  O O   . SER E  1 167 ? 19.899  28.800  78.583  1.00 44.27  ? 159 SER E O   1 
ATOM   8007  C CB  . SER E  1 167 ? 21.267  30.337  75.833  1.00 56.00  ? 159 SER E CB  1 
ATOM   8008  O OG  . SER E  1 167 ? 20.787  31.662  75.660  1.00 59.75  ? 159 SER E OG  1 
ATOM   8009  N N   . ASP E  1 168 ? 19.503  30.986  78.216  1.00 55.38  ? 160 ASP E N   1 
ATOM   8010  C CA  . ASP E  1 168 ? 18.167  30.962  78.811  1.00 54.91  ? 160 ASP E CA  1 
ATOM   8011  C C   . ASP E  1 168 ? 17.092  31.307  77.768  1.00 54.90  ? 160 ASP E C   1 
ATOM   8012  O O   . ASP E  1 168 ? 15.893  31.335  78.074  1.00 56.96  ? 160 ASP E O   1 
ATOM   8013  C CB  . ASP E  1 168 ? 18.077  31.898  80.029  1.00 61.46  ? 160 ASP E CB  1 
ATOM   8014  C CG  . ASP E  1 168 ? 18.002  33.377  79.642  1.00 68.18  ? 160 ASP E CG  1 
ATOM   8015  O OD1 . ASP E  1 168 ? 18.607  33.763  78.613  1.00 70.14  ? 160 ASP E OD1 1 
ATOM   8016  O OD2 . ASP E  1 168 ? 17.336  34.151  80.375  1.00 56.85  ? 160 ASP E OD2 1 
ATOM   8017  N N   . ASP E  1 169 ? 17.541  31.555  76.538  1.00 52.22  ? 161 ASP E N   1 
ATOM   8018  C CA  . ASP E  1 169 ? 16.667  31.888  75.411  1.00 52.57  ? 161 ASP E CA  1 
ATOM   8019  C C   . ASP E  1 169 ? 15.713  33.032  75.742  1.00 49.55  ? 161 ASP E C   1 
ATOM   8020  O O   . ASP E  1 169 ? 14.566  33.047  75.306  1.00 51.95  ? 161 ASP E O   1 
ATOM   8021  C CB  . ASP E  1 169 ? 15.913  30.649  74.889  1.00 37.63  ? 161 ASP E CB  1 
ATOM   8022  C CG  . ASP E  1 169 ? 16.808  29.709  74.050  1.00 51.78  ? 161 ASP E CG  1 
ATOM   8023  O OD1 . ASP E  1 169 ? 17.856  30.162  73.514  1.00 55.96  ? 161 ASP E OD1 1 
ATOM   8024  O OD2 . ASP E  1 169 ? 16.458  28.509  73.914  1.00 38.25  ? 161 ASP E OD2 1 
ATOM   8025  N N   . SER E  1 170 ? 16.205  33.994  76.512  1.00 54.99  ? 162 SER E N   1 
ATOM   8026  C CA  . SER E  1 170 ? 15.399  35.141  76.919  1.00 62.48  ? 162 SER E CA  1 
ATOM   8027  C C   . SER E  1 170 ? 15.019  35.967  75.692  1.00 57.53  ? 162 SER E C   1 
ATOM   8028  O O   . SER E  1 170 ? 13.987  36.640  75.669  1.00 58.12  ? 162 SER E O   1 
ATOM   8029  C CB  . SER E  1 170 ? 16.171  35.998  77.936  1.00 59.48  ? 162 SER E CB  1 
ATOM   8030  O OG  . SER E  1 170 ? 15.385  37.066  78.442  1.00 65.15  ? 162 SER E OG  1 
ATOM   8031  N N   . GLU E  1 171 ? 15.858  35.891  74.666  1.00 58.41  ? 163 GLU E N   1 
ATOM   8032  C CA  . GLU E  1 171 ? 15.703  36.714  73.477  1.00 54.64  ? 163 GLU E CA  1 
ATOM   8033  C C   . GLU E  1 171 ? 14.418  36.435  72.720  1.00 52.80  ? 163 GLU E C   1 
ATOM   8034  O O   . GLU E  1 171 ? 13.703  37.353  72.325  1.00 54.60  ? 163 GLU E O   1 
ATOM   8035  C CB  . GLU E  1 171 ? 16.880  36.473  72.543  1.00 49.82  ? 163 GLU E CB  1 
ATOM   8036  C CG  . GLU E  1 171 ? 18.078  37.337  72.827  1.00 63.35  ? 163 GLU E CG  1 
ATOM   8037  C CD  . GLU E  1 171 ? 18.177  38.494  71.865  1.00 66.97  ? 163 GLU E CD  1 
ATOM   8038  O OE1 . GLU E  1 171 ? 19.284  38.712  71.325  1.00 67.14  ? 163 GLU E OE1 1 
ATOM   8039  O OE2 . GLU E  1 171 ? 17.149  39.177  71.651  1.00 65.46  ? 163 GLU E OE2 1 
ATOM   8040  N N   . TYR E  1 172 ? 14.132  35.159  72.518  1.00 47.16  ? 164 TYR E N   1 
ATOM   8041  C CA  . TYR E  1 172 ? 13.145  34.771  71.530  1.00 43.41  ? 164 TYR E CA  1 
ATOM   8042  C C   . TYR E  1 172 ? 11.857  34.265  72.173  1.00 37.94  ? 164 TYR E C   1 
ATOM   8043  O O   . TYR E  1 172 ? 10.811  34.188  71.515  1.00 32.84  ? 164 TYR E O   1 
ATOM   8044  C CB  . TYR E  1 172 ? 13.729  33.693  70.604  1.00 45.03  ? 164 TYR E CB  1 
ATOM   8045  C CG  . TYR E  1 172 ? 15.165  33.933  70.143  1.00 52.23  ? 164 TYR E CG  1 
ATOM   8046  C CD1 . TYR E  1 172 ? 15.439  34.675  69.003  1.00 50.17  ? 164 TYR E CD1 1 
ATOM   8047  C CD2 . TYR E  1 172 ? 16.244  33.390  70.834  1.00 58.32  ? 164 TYR E CD2 1 
ATOM   8048  C CE1 . TYR E  1 172 ? 16.742  34.890  68.572  1.00 48.75  ? 164 TYR E CE1 1 
ATOM   8049  C CE2 . TYR E  1 172 ? 17.555  33.602  70.404  1.00 62.20  ? 164 TYR E CE2 1 
ATOM   8050  C CZ  . TYR E  1 172 ? 17.792  34.355  69.272  1.00 56.29  ? 164 TYR E CZ  1 
ATOM   8051  O OH  . TYR E  1 172 ? 19.082  34.574  68.840  1.00 58.32  ? 164 TYR E OH  1 
ATOM   8052  N N   . PHE E  1 173 ? 11.933  33.935  73.460  1.00 36.51  ? 165 PHE E N   1 
ATOM   8053  C CA  . PHE E  1 173 ? 10.842  33.238  74.135  1.00 28.35  ? 165 PHE E CA  1 
ATOM   8054  C C   . PHE E  1 173 ? 9.641   34.128  74.440  1.00 32.76  ? 165 PHE E C   1 
ATOM   8055  O O   . PHE E  1 173 ? 9.801   35.290  74.816  1.00 36.43  ? 165 PHE E O   1 
ATOM   8056  C CB  . PHE E  1 173 ? 11.338  32.562  75.404  1.00 27.16  ? 165 PHE E CB  1 
ATOM   8057  C CG  . PHE E  1 173 ? 10.419  31.503  75.908  1.00 23.45  ? 165 PHE E CG  1 
ATOM   8058  C CD1 . PHE E  1 173 ? 10.429  30.240  75.342  1.00 24.53  ? 165 PHE E CD1 1 
ATOM   8059  C CD2 . PHE E  1 173 ? 9.534   31.768  76.934  1.00 22.01  ? 165 PHE E CD2 1 
ATOM   8060  C CE1 . PHE E  1 173 ? 9.569   29.241  75.806  1.00 29.98  ? 165 PHE E CE1 1 
ATOM   8061  C CE2 . PHE E  1 173 ? 8.669   30.782  77.410  1.00 25.00  ? 165 PHE E CE2 1 
ATOM   8062  C CZ  . PHE E  1 173 ? 8.684   29.515  76.845  1.00 26.52  ? 165 PHE E CZ  1 
ATOM   8063  N N   . SER E  1 174 ? 8.443   33.566  74.282  1.00 28.19  ? 166 SER E N   1 
ATOM   8064  C CA  . SER E  1 174 ? 7.196   34.325  74.383  1.00 31.61  ? 166 SER E CA  1 
ATOM   8065  C C   . SER E  1 174 ? 6.859   34.779  75.805  1.00 33.18  ? 166 SER E C   1 
ATOM   8066  O O   . SER E  1 174 ? 6.771   33.968  76.733  1.00 33.36  ? 166 SER E O   1 
ATOM   8067  C CB  . SER E  1 174 ? 6.024   33.508  73.825  1.00 31.11  ? 166 SER E CB  1 
ATOM   8068  O OG  . SER E  1 174 ? 4.860   34.306  73.667  1.00 27.99  ? 166 SER E OG  1 
ATOM   8069  N N   . GLN E  1 175 ? 6.639   36.079  75.960  1.00 33.53  ? 167 GLN E N   1 
ATOM   8070  C CA  . GLN E  1 175 ? 6.238   36.640  77.240  1.00 32.01  ? 167 GLN E CA  1 
ATOM   8071  C C   . GLN E  1 175 ? 4.818   36.200  77.618  1.00 32.18  ? 167 GLN E C   1 
ATOM   8072  O O   . GLN E  1 175 ? 4.397   36.328  78.762  1.00 38.21  ? 167 GLN E O   1 
ATOM   8073  C CB  . GLN E  1 175 ? 6.321   38.160  77.171  1.00 32.78  ? 167 GLN E CB  1 
ATOM   8074  C CG  . GLN E  1 175 ? 5.406   38.757  76.123  1.00 45.61  ? 167 GLN E CG  1 
ATOM   8075  C CD  . GLN E  1 175 ? 5.965   40.030  75.499  1.00 55.73  ? 167 GLN E CD  1 
ATOM   8076  O OE1 . GLN E  1 175 ? 5.869   41.115  76.078  1.00 59.46  ? 167 GLN E OE1 1 
ATOM   8077  N NE2 . GLN E  1 175 ? 6.549   39.901  74.305  1.00 56.02  ? 167 GLN E NE2 1 
ATOM   8078  N N   . TYR E  1 176 ? 4.091   35.658  76.653  1.00 30.96  ? 168 TYR E N   1 
ATOM   8079  C CA  . TYR E  1 176 ? 2.694   35.317  76.851  1.00 28.64  ? 168 TYR E CA  1 
ATOM   8080  C C   . TYR E  1 176 ? 2.497   33.835  77.136  1.00 30.05  ? 168 TYR E C   1 
ATOM   8081  O O   . TYR E  1 176 ? 1.373   33.365  77.319  1.00 30.34  ? 168 TYR E O   1 
ATOM   8082  C CB  . TYR E  1 176 ? 1.892   35.731  75.621  1.00 34.81  ? 168 TYR E CB  1 
ATOM   8083  C CG  . TYR E  1 176 ? 2.048   37.195  75.301  1.00 37.27  ? 168 TYR E CG  1 
ATOM   8084  C CD1 . TYR E  1 176 ? 1.879   38.166  76.289  1.00 39.29  ? 168 TYR E CD1 1 
ATOM   8085  C CD2 . TYR E  1 176 ? 2.393   37.606  74.027  1.00 35.93  ? 168 TYR E CD2 1 
ATOM   8086  C CE1 . TYR E  1 176 ? 2.029   39.510  75.999  1.00 44.54  ? 168 TYR E CE1 1 
ATOM   8087  C CE2 . TYR E  1 176 ? 2.551   38.938  73.724  1.00 40.96  ? 168 TYR E CE2 1 
ATOM   8088  C CZ  . TYR E  1 176 ? 2.369   39.889  74.707  1.00 52.42  ? 168 TYR E CZ  1 
ATOM   8089  O OH  . TYR E  1 176 ? 2.527   41.218  74.381  1.00 58.66  ? 168 TYR E OH  1 
ATOM   8090  N N   . SER E  1 177 ? 3.591   33.092  77.176  1.00 27.29  ? 169 SER E N   1 
ATOM   8091  C CA  . SER E  1 177 ? 3.491   31.690  77.521  1.00 25.50  ? 169 SER E CA  1 
ATOM   8092  C C   . SER E  1 177 ? 3.081   31.538  78.977  1.00 26.76  ? 169 SER E C   1 
ATOM   8093  O O   . SER E  1 177 ? 3.543   32.281  79.846  1.00 25.84  ? 169 SER E O   1 
ATOM   8094  C CB  . SER E  1 177 ? 4.828   30.984  77.302  1.00 26.48  ? 169 SER E CB  1 
ATOM   8095  O OG  . SER E  1 177 ? 4.755   29.624  77.714  1.00 25.98  ? 169 SER E OG  1 
ATOM   8096  N N   . ARG E  1 178 ? 2.337   30.492  79.278  1.00 26.35  ? 170 ARG E N   1 
ATOM   8097  C CA  . ARG E  1 178 ? 1.995   30.243  80.660  1.00 21.36  ? 170 ARG E CA  1 
ATOM   8098  C C   . ARG E  1 178 ? 3.312   30.039  81.398  1.00 25.04  ? 170 ARG E C   1 
ATOM   8099  O O   . ARG E  1 178 ? 3.395   30.247  82.609  1.00 30.40  ? 170 ARG E O   1 
ATOM   8100  C CB  . ARG E  1 178 ? 1.116   28.999  80.785  1.00 15.97  ? 170 ARG E CB  1 
ATOM   8101  C CG  . ARG E  1 178 ? -0.295  29.283  81.275  1.00 29.79  ? 170 ARG E CG  1 
ATOM   8102  C CD  . ARG E  1 178 ? -0.843  30.565  80.669  1.00 32.86  ? 170 ARG E CD  1 
ATOM   8103  N NE  . ARG E  1 178 ? -1.786  31.232  81.561  1.00 40.39  ? 170 ARG E NE  1 
ATOM   8104  C CZ  . ARG E  1 178 ? -1.752  32.529  81.849  1.00 50.36  ? 170 ARG E CZ  1 
ATOM   8105  N NH1 . ARG E  1 178 ? -0.820  33.305  81.314  1.00 50.03  ? 170 ARG E NH1 1 
ATOM   8106  N NH2 . ARG E  1 178 ? -2.651  33.051  82.672  1.00 46.65  ? 170 ARG E NH2 1 
ATOM   8107  N N   . PHE E  1 179 ? 4.335   29.608  80.664  1.00 23.41  ? 171 PHE E N   1 
ATOM   8108  C CA  . PHE E  1 179 ? 5.538   29.070  81.278  1.00 26.38  ? 171 PHE E CA  1 
ATOM   8109  C C   . PHE E  1 179 ? 6.684   30.048  81.142  1.00 23.80  ? 171 PHE E C   1 
ATOM   8110  O O   . PHE E  1 179 ? 6.535   31.104  80.529  1.00 24.43  ? 171 PHE E O   1 
ATOM   8111  C CB  . PHE E  1 179 ? 5.902   27.711  80.682  1.00 25.04  ? 171 PHE E CB  1 
ATOM   8112  C CG  . PHE E  1 179 ? 4.802   26.698  80.782  1.00 23.08  ? 171 PHE E CG  1 
ATOM   8113  C CD1 . PHE E  1 179 ? 3.748   26.700  79.872  1.00 25.99  ? 171 PHE E CD1 1 
ATOM   8114  C CD2 . PHE E  1 179 ? 4.822   25.735  81.774  1.00 27.42  ? 171 PHE E CD2 1 
ATOM   8115  C CE1 . PHE E  1 179 ? 2.727   25.768  79.957  1.00 25.40  ? 171 PHE E CE1 1 
ATOM   8116  C CE2 . PHE E  1 179 ? 3.802   24.799  81.873  1.00 30.72  ? 171 PHE E CE2 1 
ATOM   8117  C CZ  . PHE E  1 179 ? 2.750   24.817  80.962  1.00 28.71  ? 171 PHE E CZ  1 
ATOM   8118  N N   . GLU E  1 180 ? 7.817   29.698  81.739  1.00 21.02  ? 172 GLU E N   1 
ATOM   8119  C CA  . GLU E  1 180 ? 9.004   30.526  81.661  1.00 24.29  ? 172 GLU E CA  1 
ATOM   8120  C C   . GLU E  1 180 ? 10.187  29.587  81.744  1.00 27.28  ? 172 GLU E C   1 
ATOM   8121  O O   . GLU E  1 180 ? 10.063  28.484  82.281  1.00 24.85  ? 172 GLU E O   1 
ATOM   8122  C CB  . GLU E  1 180 ? 9.036   31.549  82.797  1.00 26.46  ? 172 GLU E CB  1 
ATOM   8123  C CG  . GLU E  1 180 ? 9.503   30.995  84.138  1.00 31.97  ? 172 GLU E CG  1 
ATOM   8124  C CD  . GLU E  1 180 ? 9.081   31.861  85.317  1.00 44.86  ? 172 GLU E CD  1 
ATOM   8125  O OE1 . GLU E  1 180 ? 8.527   32.963  85.091  1.00 43.48  ? 172 GLU E OE1 1 
ATOM   8126  O OE2 . GLU E  1 180 ? 9.291   31.432  86.475  1.00 50.04  ? 172 GLU E OE2 1 
ATOM   8127  N N   . ILE E  1 181 ? 11.322  30.017  81.202  1.00 24.82  ? 173 ILE E N   1 
ATOM   8128  C CA  . ILE E  1 181 ? 12.472  29.135  81.054  1.00 25.64  ? 173 ILE E CA  1 
ATOM   8129  C C   . ILE E  1 181 ? 13.533  29.456  82.087  1.00 27.34  ? 173 ILE E C   1 
ATOM   8130  O O   . ILE E  1 181 ? 13.998  30.587  82.198  1.00 33.74  ? 173 ILE E O   1 
ATOM   8131  C CB  . ILE E  1 181 ? 13.087  29.226  79.618  1.00 30.51  ? 173 ILE E CB  1 
ATOM   8132  C CG1 . ILE E  1 181 ? 12.133  28.635  78.584  1.00 27.84  ? 173 ILE E CG1 1 
ATOM   8133  C CG2 . ILE E  1 181 ? 14.413  28.494  79.529  1.00 26.93  ? 173 ILE E CG2 1 
ATOM   8134  C CD1 . ILE E  1 181 ? 12.747  28.506  77.206  1.00 29.48  ? 173 ILE E CD1 1 
ATOM   8135  N N   . LEU E  1 182 ? 13.926  28.445  82.839  1.00 26.81  ? 174 LEU E N   1 
ATOM   8136  C CA  . LEU E  1 182 ? 14.968  28.618  83.833  1.00 33.67  ? 174 LEU E CA  1 
ATOM   8137  C C   . LEU E  1 182 ? 16.351  28.558  83.200  1.00 31.17  ? 174 LEU E C   1 
ATOM   8138  O O   . LEU E  1 182 ? 17.193  29.417  83.459  1.00 34.81  ? 174 LEU E O   1 
ATOM   8139  C CB  . LEU E  1 182 ? 14.833  27.559  84.934  1.00 35.79  ? 174 LEU E CB  1 
ATOM   8140  C CG  . LEU E  1 182 ? 13.419  27.430  85.505  1.00 33.13  ? 174 LEU E CG  1 
ATOM   8141  C CD1 . LEU E  1 182 ? 13.370  26.440  86.648  1.00 35.55  ? 174 LEU E CD1 1 
ATOM   8142  C CD2 . LEU E  1 182 ? 12.910  28.789  85.938  1.00 32.70  ? 174 LEU E CD2 1 
ATOM   8143  N N   . ASP E  1 183 ? 16.577  27.550  82.361  1.00 36.29  ? 175 ASP E N   1 
ATOM   8144  C CA  . ASP E  1 183 ? 17.889  27.331  81.756  1.00 38.39  ? 175 ASP E CA  1 
ATOM   8145  C C   . ASP E  1 183 ? 17.820  26.352  80.583  1.00 39.88  ? 175 ASP E C   1 
ATOM   8146  O O   . ASP E  1 183 ? 17.137  25.326  80.666  1.00 37.07  ? 175 ASP E O   1 
ATOM   8147  C CB  . ASP E  1 183 ? 18.850  26.786  82.816  1.00 37.34  ? 175 ASP E CB  1 
ATOM   8148  C CG  . ASP E  1 183 ? 20.229  26.500  82.269  1.00 35.23  ? 175 ASP E CG  1 
ATOM   8149  O OD1 . ASP E  1 183 ? 20.789  27.370  81.568  1.00 40.81  ? 175 ASP E OD1 1 
ATOM   8150  O OD2 . ASP E  1 183 ? 20.753  25.401  82.546  1.00 32.98  ? 175 ASP E OD2 1 
ATOM   8151  N N   . VAL E  1 184 ? 18.529  26.667  79.497  1.00 34.58  ? 176 VAL E N   1 
ATOM   8152  C CA  . VAL E  1 184 ? 18.674  25.727  78.392  1.00 30.94  ? 176 VAL E CA  1 
ATOM   8153  C C   . VAL E  1 184 ? 20.135  25.363  78.156  1.00 35.22  ? 176 VAL E C   1 
ATOM   8154  O O   . VAL E  1 184 ? 20.973  26.234  77.928  1.00 38.67  ? 176 VAL E O   1 
ATOM   8155  C CB  . VAL E  1 184 ? 18.103  26.263  77.064  1.00 33.46  ? 176 VAL E CB  1 
ATOM   8156  C CG1 . VAL E  1 184 ? 18.094  25.142  76.023  1.00 34.29  ? 176 VAL E CG1 1 
ATOM   8157  C CG2 . VAL E  1 184 ? 16.704  26.816  77.245  1.00 29.53  ? 176 VAL E CG2 1 
ATOM   8158  N N   . THR E  1 185 ? 20.435  24.071  78.201  1.00 33.01  ? 177 THR E N   1 
ATOM   8159  C CA  . THR E  1 185 ? 21.780  23.591  77.920  1.00 36.52  ? 177 THR E CA  1 
ATOM   8160  C C   . THR E  1 185 ? 21.801  22.683  76.691  1.00 32.96  ? 177 THR E C   1 
ATOM   8161  O O   . THR E  1 185 ? 20.866  21.912  76.466  1.00 32.57  ? 177 THR E O   1 
ATOM   8162  C CB  . THR E  1 185 ? 22.347  22.816  79.122  1.00 37.06  ? 177 THR E CB  1 
ATOM   8163  O OG1 . THR E  1 185 ? 21.568  21.632  79.341  1.00 33.89  ? 177 THR E OG1 1 
ATOM   8164  C CG2 . THR E  1 185 ? 22.315  23.684  80.361  1.00 27.60  ? 177 THR E CG2 1 
ATOM   8165  N N   . GLN E  1 186 ? 22.865  22.770  75.901  1.00 32.61  ? 178 GLN E N   1 
ATOM   8166  C CA  . GLN E  1 186 ? 23.007  21.914  74.720  1.00 37.20  ? 178 GLN E CA  1 
ATOM   8167  C C   . GLN E  1 186 ? 24.353  21.200  74.748  1.00 37.90  ? 178 GLN E C   1 
ATOM   8168  O O   . GLN E  1 186 ? 25.393  21.856  74.702  1.00 38.93  ? 178 GLN E O   1 
ATOM   8169  C CB  . GLN E  1 186 ? 22.879  22.740  73.432  1.00 32.71  ? 178 GLN E CB  1 
ATOM   8170  C CG  . GLN E  1 186 ? 21.579  23.545  73.301  1.00 38.11  ? 178 GLN E CG  1 
ATOM   8171  C CD  . GLN E  1 186 ? 21.381  24.140  71.907  1.00 45.91  ? 178 GLN E CD  1 
ATOM   8172  O OE1 . GLN E  1 186 ? 21.781  23.542  70.906  1.00 45.03  ? 178 GLN E OE1 1 
ATOM   8173  N NE2 . GLN E  1 186 ? 20.768  25.324  71.839  1.00 37.84  ? 178 GLN E NE2 1 
ATOM   8174  N N   . LYS E  1 187 ? 24.341  19.869  74.831  1.00 36.99  ? 179 LYS E N   1 
ATOM   8175  C CA  . LYS E  1 187 ? 25.595  19.096  74.853  1.00 46.89  ? 179 LYS E CA  1 
ATOM   8176  C C   . LYS E  1 187 ? 25.649  17.967  73.805  1.00 43.53  ? 179 LYS E C   1 
ATOM   8177  O O   . LYS E  1 187 ? 24.614  17.414  73.433  1.00 41.70  ? 179 LYS E O   1 
ATOM   8178  C CB  . LYS E  1 187 ? 25.863  18.516  76.253  1.00 47.51  ? 179 LYS E CB  1 
ATOM   8179  C CG  . LYS E  1 187 ? 25.052  17.263  76.573  1.00 47.68  ? 179 LYS E CG  1 
ATOM   8180  C CD  . LYS E  1 187 ? 25.805  16.284  77.470  1.00 48.47  ? 179 LYS E CD  1 
ATOM   8181  C CE  . LYS E  1 187 ? 24.992  15.005  77.653  1.00 56.93  ? 179 LYS E CE  1 
ATOM   8182  N NZ  . LYS E  1 187 ? 25.751  13.894  78.291  1.00 60.35  ? 179 LYS E NZ  1 
ATOM   8183  N N   . LYS E  1 188 ? 26.855  17.636  73.336  1.00 43.07  ? 180 LYS E N   1 
ATOM   8184  C CA  . LYS E  1 188 ? 27.071  16.477  72.459  1.00 35.88  ? 180 LYS E CA  1 
ATOM   8185  C C   . LYS E  1 188 ? 26.839  15.178  73.218  1.00 40.62  ? 180 LYS E C   1 
ATOM   8186  O O   . LYS E  1 188 ? 26.860  15.155  74.447  1.00 56.54  ? 180 LYS E O   1 
ATOM   8187  C CB  . LYS E  1 188 ? 28.495  16.460  71.888  1.00 42.65  ? 180 LYS E CB  1 
ATOM   8188  C CG  . LYS E  1 188 ? 28.745  17.370  70.698  1.00 43.02  ? 180 LYS E CG  1 
ATOM   8189  C CD  . LYS E  1 188 ? 30.033  16.974  69.960  1.00 54.54  ? 180 LYS E CD  1 
ATOM   8190  C CE  . LYS E  1 188 ? 29.820  15.838  68.933  1.00 51.45  ? 180 LYS E CE  1 
ATOM   8191  N NZ  . LYS E  1 188 ? 29.515  14.490  69.530  1.00 44.42  ? 180 LYS E NZ  1 
ATOM   8192  N N   . ASN E  1 189 ? 26.485  14.148  72.464  1.00 39.83  ? 181 ASN E N   1 
ATOM   8193  C CA  . ASN E  1 189 ? 26.309  12.805  72.980  1.00 44.93  ? 181 ASN E CA  1 
ATOM   8194  C C   . ASN E  1 189 ? 26.396  11.851  71.805  1.00 51.54  ? 181 ASN E C   1 
ATOM   8195  O O   . ASN E  1 189 ? 26.226  12.262  70.657  1.00 50.44  ? 181 ASN E O   1 
ATOM   8196  C CB  . ASN E  1 189 ? 24.958  12.666  73.680  1.00 47.71  ? 181 ASN E CB  1 
ATOM   8197  C CG  . ASN E  1 189 ? 24.948  11.557  74.712  1.00 57.71  ? 181 ASN E CG  1 
ATOM   8198  O OD1 . ASN E  1 189 ? 24.713  10.393  74.388  1.00 57.28  ? 181 ASN E OD1 1 
ATOM   8199  N ND2 . ASN E  1 189 ? 25.205  11.912  75.966  1.00 57.98  ? 181 ASN E ND2 1 
ATOM   8200  N N   . SER E  1 190 ? 26.646  10.579  72.077  1.00 54.37  ? 182 SER E N   1 
ATOM   8201  C CA  . SER E  1 190 ? 26.592  9.580   71.009  1.00 49.77  ? 182 SER E CA  1 
ATOM   8202  C C   . SER E  1 190 ? 25.700  8.412   71.405  1.00 54.44  ? 182 SER E C   1 
ATOM   8203  O O   . SER E  1 190 ? 25.564  8.096   72.587  1.00 65.54  ? 182 SER E O   1 
ATOM   8204  C CB  . SER E  1 190 ? 27.993  9.081   70.621  1.00 48.21  ? 182 SER E CB  1 
ATOM   8205  O OG  . SER E  1 190 ? 28.603  9.918   69.649  1.00 45.02  ? 182 SER E OG  1 
ATOM   8206  N N   . VAL E  1 191 ? 25.087  7.782   70.410  1.00 48.53  ? 183 VAL E N   1 
ATOM   8207  C CA  . VAL E  1 191 ? 24.247  6.616   70.643  1.00 47.92  ? 183 VAL E CA  1 
ATOM   8208  C C   . VAL E  1 191 ? 24.615  5.469   69.684  1.00 57.77  ? 183 VAL E C   1 
ATOM   8209  O O   . VAL E  1 191 ? 24.944  5.700   68.512  1.00 52.47  ? 183 VAL E O   1 
ATOM   8210  C CB  . VAL E  1 191 ? 22.725  6.971   70.582  1.00 50.32  ? 183 VAL E CB  1 
ATOM   8211  C CG1 . VAL E  1 191 ? 22.500  8.398   70.079  1.00 43.31  ? 183 VAL E CG1 1 
ATOM   8212  C CG2 . VAL E  1 191 ? 21.964  5.979   69.734  1.00 50.02  ? 183 VAL E CG2 1 
ATOM   8213  N N   . THR E  1 192 ? 24.585  4.239   70.200  1.00 63.13  ? 184 THR E N   1 
ATOM   8214  C CA  . THR E  1 192 ? 24.922  3.057   69.409  1.00 56.83  ? 184 THR E CA  1 
ATOM   8215  C C   . THR E  1 192 ? 23.945  1.913   69.683  1.00 54.84  ? 184 THR E C   1 
ATOM   8216  O O   . THR E  1 192 ? 22.811  2.140   70.111  1.00 50.80  ? 184 THR E O   1 
ATOM   8217  C CB  . THR E  1 192 ? 26.362  2.585   69.699  1.00 52.16  ? 184 THR E CB  1 
ATOM   8218  O OG1 . THR E  1 192 ? 27.252  3.705   69.656  1.00 44.94  ? 184 THR E OG1 1 
ATOM   8219  C CG2 . THR E  1 192 ? 26.807  1.544   68.682  1.00 47.73  ? 184 THR E CG2 1 
ATOM   8220  N N   . GLU E  1 198 ? 27.941  0.696   64.575  1.00 54.95  ? 190 GLU E N   1 
ATOM   8221  C CA  . GLU E  1 198 ? 28.325  2.066   64.227  1.00 59.95  ? 190 GLU E CA  1 
ATOM   8222  C C   . GLU E  1 198 ? 27.420  3.098   64.923  1.00 51.91  ? 190 GLU E C   1 
ATOM   8223  O O   . GLU E  1 198 ? 26.235  2.835   65.138  1.00 50.28  ? 190 GLU E O   1 
ATOM   8224  C CB  . GLU E  1 198 ? 28.315  2.243   62.706  1.00 64.08  ? 190 GLU E CB  1 
ATOM   8225  C CG  . GLU E  1 198 ? 28.901  3.556   62.197  1.00 64.23  ? 190 GLU E CG  1 
ATOM   8226  C CD  . GLU E  1 198 ? 30.386  3.723   62.472  1.00 63.83  ? 190 GLU E CD  1 
ATOM   8227  O OE1 . GLU E  1 198 ? 31.153  2.759   62.239  1.00 67.76  ? 190 GLU E OE1 1 
ATOM   8228  O OE2 . GLU E  1 198 ? 30.776  4.831   62.913  1.00 57.29  ? 190 GLU E OE2 1 
ATOM   8229  N N   . ALA E  1 199 ? 27.981  4.262   65.266  1.00 48.82  ? 191 ALA E N   1 
ATOM   8230  C CA  . ALA E  1 199 ? 27.325  5.222   66.167  1.00 46.48  ? 191 ALA E CA  1 
ATOM   8231  C C   . ALA E  1 199 ? 26.797  6.498   65.519  1.00 45.24  ? 191 ALA E C   1 
ATOM   8232  O O   . ALA E  1 199 ? 27.304  6.953   64.493  1.00 40.65  ? 191 ALA E O   1 
ATOM   8233  C CB  . ALA E  1 199 ? 28.263  5.594   67.310  1.00 51.76  ? 191 ALA E CB  1 
ATOM   8234  N N   . TYR E  1 200 ? 25.799  7.096   66.165  1.00 41.56  ? 192 TYR E N   1 
ATOM   8235  C CA  . TYR E  1 200 ? 25.181  8.316   65.660  1.00 37.36  ? 192 TYR E CA  1 
ATOM   8236  C C   . TYR E  1 200 ? 25.472  9.496   66.565  1.00 38.17  ? 192 TYR E C   1 
ATOM   8237  O O   . TYR E  1 200 ? 25.394  9.377   67.777  1.00 43.83  ? 192 TYR E O   1 
ATOM   8238  C CB  . TYR E  1 200 ? 23.674  8.117   65.511  1.00 31.40  ? 192 TYR E CB  1 
ATOM   8239  C CG  . TYR E  1 200 ? 23.346  7.022   64.529  1.00 32.24  ? 192 TYR E CG  1 
ATOM   8240  C CD1 . TYR E  1 200 ? 23.352  5.693   64.923  1.00 32.47  ? 192 TYR E CD1 1 
ATOM   8241  C CD2 . TYR E  1 200 ? 23.072  7.313   63.195  1.00 32.28  ? 192 TYR E CD2 1 
ATOM   8242  C CE1 . TYR E  1 200 ? 23.079  4.682   64.035  1.00 31.89  ? 192 TYR E CE1 1 
ATOM   8243  C CE2 . TYR E  1 200 ? 22.788  6.301   62.287  1.00 31.03  ? 192 TYR E CE2 1 
ATOM   8244  C CZ  . TYR E  1 200 ? 22.795  4.985   62.718  1.00 37.71  ? 192 TYR E CZ  1 
ATOM   8245  O OH  . TYR E  1 200 ? 22.521  3.962   61.842  1.00 33.78  ? 192 TYR E OH  1 
ATOM   8246  N N   . GLU E  1 201 ? 25.829  10.630  65.976  1.00 36.11  ? 193 GLU E N   1 
ATOM   8247  C CA  . GLU E  1 201 ? 25.983  11.853  66.747  1.00 34.04  ? 193 GLU E CA  1 
ATOM   8248  C C   . GLU E  1 201 ? 24.638  12.546  66.922  1.00 36.94  ? 193 GLU E C   1 
ATOM   8249  O O   . GLU E  1 201 ? 23.823  12.599  66.001  1.00 39.64  ? 193 GLU E O   1 
ATOM   8250  C CB  . GLU E  1 201 ? 26.969  12.806  66.077  1.00 31.59  ? 193 GLU E CB  1 
ATOM   8251  C CG  . GLU E  1 201 ? 28.369  12.259  65.963  1.00 34.96  ? 193 GLU E CG  1 
ATOM   8252  C CD  . GLU E  1 201 ? 29.412  13.355  65.933  1.00 44.26  ? 193 GLU E CD  1 
ATOM   8253  O OE1 . GLU E  1 201 ? 29.034  14.535  66.114  1.00 43.71  ? 193 GLU E OE1 1 
ATOM   8254  O OE2 . GLU E  1 201 ? 30.609  13.038  65.738  1.00 51.35  ? 193 GLU E OE2 1 
ATOM   8255  N N   . ASP E  1 202 ? 24.408  13.074  68.115  1.00 39.81  ? 194 ASP E N   1 
ATOM   8256  C CA  . ASP E  1 202 ? 23.204  13.843  68.394  1.00 41.24  ? 194 ASP E CA  1 
ATOM   8257  C C   . ASP E  1 202 ? 23.509  14.998  69.340  1.00 35.30  ? 194 ASP E C   1 
ATOM   8258  O O   . ASP E  1 202 ? 24.569  15.044  69.960  1.00 37.49  ? 194 ASP E O   1 
ATOM   8259  C CB  . ASP E  1 202 ? 22.107  12.956  68.993  1.00 37.05  ? 194 ASP E CB  1 
ATOM   8260  C CG  . ASP E  1 202 ? 22.390  12.562  70.433  1.00 45.12  ? 194 ASP E CG  1 
ATOM   8261  O OD1 . ASP E  1 202 ? 22.090  13.356  71.356  1.00 42.53  ? 194 ASP E OD1 1 
ATOM   8262  O OD2 . ASP E  1 202 ? 22.899  11.441  70.645  1.00 54.21  ? 194 ASP E OD2 1 
ATOM   8263  N N   . VAL E  1 203 ? 22.583  15.941  69.432  1.00 31.22  ? 195 VAL E N   1 
ATOM   8264  C CA  . VAL E  1 203 ? 22.668  16.977  70.444  1.00 32.21  ? 195 VAL E CA  1 
ATOM   8265  C C   . VAL E  1 203 ? 21.523  16.790  71.413  1.00 26.72  ? 195 VAL E C   1 
ATOM   8266  O O   . VAL E  1 203 ? 20.364  16.778  71.015  1.00 27.07  ? 195 VAL E O   1 
ATOM   8267  C CB  . VAL E  1 203 ? 22.619  18.386  69.841  1.00 29.42  ? 195 VAL E CB  1 
ATOM   8268  C CG1 . VAL E  1 203 ? 22.210  19.379  70.874  1.00 25.00  ? 195 VAL E CG1 1 
ATOM   8269  C CG2 . VAL E  1 203 ? 23.977  18.759  69.270  1.00 37.31  ? 195 VAL E CG2 1 
ATOM   8270  N N   . GLU E  1 204 ? 21.861  16.594  72.681  1.00 31.92  ? 196 GLU E N   1 
ATOM   8271  C CA  . GLU E  1 204 ? 20.872  16.645  73.749  1.00 34.46  ? 196 GLU E CA  1 
ATOM   8272  C C   . GLU E  1 204 ? 20.614  18.098  74.102  1.00 25.78  ? 196 GLU E C   1 
ATOM   8273  O O   . GLU E  1 204 ? 21.534  18.837  74.470  1.00 24.40  ? 196 GLU E O   1 
ATOM   8274  C CB  . GLU E  1 204 ? 21.372  15.910  74.981  1.00 35.01  ? 196 GLU E CB  1 
ATOM   8275  C CG  . GLU E  1 204 ? 20.389  14.938  75.558  1.00 35.02  ? 196 GLU E CG  1 
ATOM   8276  C CD  . GLU E  1 204 ? 20.985  14.189  76.726  1.00 57.04  ? 196 GLU E CD  1 
ATOM   8277  O OE1 . GLU E  1 204 ? 21.612  13.131  76.490  1.00 59.41  ? 196 GLU E OE1 1 
ATOM   8278  O OE2 . GLU E  1 204 ? 20.844  14.669  77.876  1.00 64.99  ? 196 GLU E OE2 1 
ATOM   8279  N N   . VAL E  1 205 ? 19.365  18.511  73.941  1.00 28.60  ? 197 VAL E N   1 
ATOM   8280  C CA  . VAL E  1 205 ? 18.918  19.817  74.404  1.00 31.91  ? 197 VAL E CA  1 
ATOM   8281  C C   . VAL E  1 205 ? 18.133  19.607  75.685  1.00 25.94  ? 197 VAL E C   1 
ATOM   8282  O O   . VAL E  1 205 ? 17.194  18.815  75.716  1.00 27.31  ? 197 VAL E O   1 
ATOM   8283  C CB  . VAL E  1 205 ? 18.055  20.531  73.340  1.00 27.91  ? 197 VAL E CB  1 
ATOM   8284  C CG1 . VAL E  1 205 ? 17.347  21.746  73.923  1.00 22.19  ? 197 VAL E CG1 1 
ATOM   8285  C CG2 . VAL E  1 205 ? 18.929  20.936  72.176  1.00 31.17  ? 197 VAL E CG2 1 
ATOM   8286  N N   . SER E  1 206 ? 18.551  20.281  76.754  1.00 33.17  ? 198 SER E N   1 
ATOM   8287  C CA  . SER E  1 206 ? 17.875  20.164  78.049  1.00 29.80  ? 198 SER E CA  1 
ATOM   8288  C C   . SER E  1 206 ? 17.147  21.443  78.389  1.00 30.21  ? 198 SER E C   1 
ATOM   8289  O O   . SER E  1 206 ? 17.770  22.482  78.614  1.00 30.59  ? 198 SER E O   1 
ATOM   8290  C CB  . SER E  1 206 ? 18.861  19.820  79.158  1.00 23.94  ? 198 SER E CB  1 
ATOM   8291  O OG  . SER E  1 206 ? 19.231  18.458  79.073  1.00 35.72  ? 198 SER E OG  1 
ATOM   8292  N N   . LEU E  1 207 ? 15.822  21.355  78.413  1.00 29.32  ? 199 LEU E N   1 
ATOM   8293  C CA  . LEU E  1 207 ? 14.974  22.497  78.712  1.00 25.53  ? 199 LEU E CA  1 
ATOM   8294  C C   . LEU E  1 207 ? 14.489  22.435  80.149  1.00 30.99  ? 199 LEU E C   1 
ATOM   8295  O O   . LEU E  1 207 ? 13.853  21.464  80.578  1.00 28.23  ? 199 LEU E O   1 
ATOM   8296  C CB  . LEU E  1 207 ? 13.789  22.545  77.751  1.00 26.87  ? 199 LEU E CB  1 
ATOM   8297  C CG  . LEU E  1 207 ? 12.821  23.713  77.911  1.00 29.74  ? 199 LEU E CG  1 
ATOM   8298  C CD1 . LEU E  1 207 ? 13.578  25.035  78.075  1.00 28.15  ? 199 LEU E CD1 1 
ATOM   8299  C CD2 . LEU E  1 207 ? 11.854  23.759  76.723  1.00 25.10  ? 199 LEU E CD2 1 
ATOM   8300  N N   . ASN E  1 208 ? 14.801  23.487  80.892  1.00 33.67  ? 200 ASN E N   1 
ATOM   8301  C CA  . ASN E  1 208 ? 14.433  23.570  82.290  1.00 32.23  ? 200 ASN E CA  1 
ATOM   8302  C C   . ASN E  1 208 ? 13.457  24.729  82.549  1.00 30.86  ? 200 ASN E C   1 
ATOM   8303  O O   . ASN E  1 208 ? 13.813  25.897  82.427  1.00 31.86  ? 200 ASN E O   1 
ATOM   8304  C CB  . ASN E  1 208 ? 15.694  23.674  83.145  1.00 33.12  ? 200 ASN E CB  1 
ATOM   8305  C CG  . ASN E  1 208 ? 15.389  23.946  84.586  1.00 36.07  ? 200 ASN E CG  1 
ATOM   8306  O OD1 . ASN E  1 208 ? 16.068  24.738  85.232  1.00 41.55  ? 200 ASN E OD1 1 
ATOM   8307  N ND2 . ASN E  1 208 ? 14.341  23.310  85.101  1.00 35.36  ? 200 ASN E ND2 1 
ATOM   8308  N N   . PHE E  1 209 ? 12.225  24.393  82.920  1.00 30.79  ? 201 PHE E N   1 
ATOM   8309  C CA  . PHE E  1 209 ? 11.122  25.350  82.869  1.00 31.59  ? 201 PHE E CA  1 
ATOM   8310  C C   . PHE E  1 209 ? 10.027  25.036  83.889  1.00 27.84  ? 201 PHE E C   1 
ATOM   8311  O O   . PHE E  1 209 ? 9.818   23.867  84.245  1.00 26.75  ? 201 PHE E O   1 
ATOM   8312  C CB  . PHE E  1 209 ? 10.505  25.330  81.464  1.00 25.14  ? 201 PHE E CB  1 
ATOM   8313  C CG  . PHE E  1 209 ? 9.704   24.088  81.174  1.00 21.46  ? 201 PHE E CG  1 
ATOM   8314  C CD1 . PHE E  1 209 ? 10.337  22.868  80.971  1.00 22.94  ? 201 PHE E CD1 1 
ATOM   8315  C CD2 . PHE E  1 209 ? 8.319   24.135  81.119  1.00 25.76  ? 201 PHE E CD2 1 
ATOM   8316  C CE1 . PHE E  1 209 ? 9.606   21.716  80.718  1.00 21.93  ? 201 PHE E CE1 1 
ATOM   8317  C CE2 . PHE E  1 209 ? 7.574   22.986  80.858  1.00 25.90  ? 201 PHE E CE2 1 
ATOM   8318  C CZ  . PHE E  1 209 ? 8.220   21.772  80.658  1.00 20.18  ? 201 PHE E CZ  1 
ATOM   8319  N N   . ARG E  1 210 ? 9.308   26.073  84.320  1.00 24.34  ? 202 ARG E N   1 
ATOM   8320  C CA  . ARG E  1 210 ? 8.248   25.915  85.317  1.00 26.79  ? 202 ARG E CA  1 
ATOM   8321  C C   . ARG E  1 210 ? 6.986   26.694  84.979  1.00 28.20  ? 202 ARG E C   1 
ATOM   8322  O O   . ARG E  1 210 ? 6.997   27.556  84.110  1.00 31.51  ? 202 ARG E O   1 
ATOM   8323  C CB  . ARG E  1 210 ? 8.740   26.366  86.692  1.00 29.01  ? 202 ARG E CB  1 
ATOM   8324  C CG  . ARG E  1 210 ? 8.873   27.873  86.834  1.00 29.69  ? 202 ARG E CG  1 
ATOM   8325  C CD  . ARG E  1 210 ? 8.994   28.281  88.301  1.00 39.85  ? 202 ARG E CD  1 
ATOM   8326  N NE  . ARG E  1 210 ? 9.377   29.682  88.427  1.00 40.57  ? 202 ARG E NE  1 
ATOM   8327  C CZ  . ARG E  1 210 ? 10.601  30.087  88.736  1.00 39.70  ? 202 ARG E CZ  1 
ATOM   8328  N NH1 . ARG E  1 210 ? 11.555  29.194  88.971  1.00 41.35  ? 202 ARG E NH1 1 
ATOM   8329  N NH2 . ARG E  1 210 ? 10.871  31.383  88.808  1.00 33.99  ? 202 ARG E NH2 1 
ATOM   8330  N N   . LYS E  1 211 ? 5.901   26.386  85.689  1.00 33.21  ? 203 LYS E N   1 
ATOM   8331  C CA  . LYS E  1 211 ? 4.651   27.140  85.604  1.00 30.22  ? 203 LYS E CA  1 
ATOM   8332  C C   . LYS E  1 211 ? 4.882   28.569  86.085  1.00 29.40  ? 203 LYS E C   1 
ATOM   8333  O O   . LYS E  1 211 ? 5.728   28.805  86.944  1.00 27.89  ? 203 LYS E O   1 
ATOM   8334  C CB  . LYS E  1 211 ? 3.580   26.475  86.483  1.00 33.89  ? 203 LYS E CB  1 
ATOM   8335  C CG  . LYS E  1 211 ? 2.147   26.466  85.918  1.00 36.09  ? 203 LYS E CG  1 
ATOM   8336  C CD  . LYS E  1 211 ? 1.748   25.057  85.434  1.00 43.12  ? 203 LYS E CD  1 
ATOM   8337  C CE  . LYS E  1 211 ? 0.322   24.975  84.863  1.00 43.74  ? 203 LYS E CE  1 
ATOM   8338  N NZ  . LYS E  1 211 ? 0.057   23.638  84.228  1.00 32.37  ? 203 LYS E NZ  1 
ATOM   8339  N N   . LYS E  1 212 ? 4.138   29.518  85.521  1.00 37.50  ? 204 LYS E N   1 
ATOM   8340  C CA  . LYS E  1 212 ? 4.147   30.906  85.996  1.00 38.27  ? 204 LYS E CA  1 
ATOM   8341  C C   . LYS E  1 212 ? 2.955   31.162  86.911  1.00 45.60  ? 204 LYS E C   1 
ATOM   8342  O O   . LYS E  1 212 ? 1.805   31.055  86.473  1.00 53.56  ? 204 LYS E O   1 
ATOM   8343  C CB  . LYS E  1 212 ? 4.099   31.881  84.819  1.00 35.84  ? 204 LYS E CB  1 
ATOM   8344  C CG  . LYS E  1 212 ? 5.370   31.933  83.999  1.00 30.16  ? 204 LYS E CG  1 
ATOM   8345  C CD  . LYS E  1 212 ? 5.593   33.327  83.423  1.00 28.31  ? 204 LYS E CD  1 
ATOM   8346  C CE  . LYS E  1 212 ? 4.480   33.739  82.477  1.00 27.05  ? 204 LYS E CE  1 
ATOM   8347  N NZ  . LYS E  1 212 ? 4.816   34.983  81.716  1.00 28.06  ? 204 LYS E NZ  1 
ATOM   8348  N N   . GLY E  1 213 ? 3.224   31.504  88.172  1.00 48.49  ? 205 GLY E N   1 
ATOM   8349  C CA  . GLY E  1 213 ? 2.176   31.675  89.169  1.00 35.71  ? 205 GLY E CA  1 
ATOM   8350  C C   . GLY E  1 213 ? 2.219   30.573  90.219  1.00 46.06  ? 205 GLY E C   1 
ATOM   8351  O O   . GLY E  1 213 ? 1.211   30.250  90.858  1.00 45.17  ? 205 GLY E O   1 
ATOM   8352  N N   . ASP F  1 1   ? -1.061  46.643  13.298  1.00 50.89  ? -7  ASP F N   1 
ATOM   8353  C CA  . ASP F  1 1   ? -1.657  46.830  11.979  1.00 53.10  ? -7  ASP F CA  1 
ATOM   8354  C C   . ASP F  1 1   ? -0.575  47.046  10.920  1.00 61.51  ? -7  ASP F C   1 
ATOM   8355  O O   . ASP F  1 1   ? -0.059  46.092  10.331  1.00 58.01  ? -7  ASP F O   1 
ATOM   8356  C CB  . ASP F  1 1   ? -2.654  47.998  11.999  1.00 50.94  ? -7  ASP F CB  1 
ATOM   8357  C CG  . ASP F  1 1   ? -2.177  49.165  12.853  1.00 61.71  ? -7  ASP F CG  1 
ATOM   8358  O OD1 . ASP F  1 1   ? -1.559  50.096  12.291  1.00 63.43  ? -7  ASP F OD1 1 
ATOM   8359  O OD2 . ASP F  1 1   ? -2.420  49.154  14.085  1.00 60.18  ? -7  ASP F OD2 1 
ATOM   8360  N N   . TYR F  1 2   ? -0.246  48.312  10.688  1.00 68.76  ? -6  TYR F N   1 
ATOM   8361  C CA  . TYR F  1 2   ? 0.849   48.715  9.813   1.00 69.58  ? -6  TYR F CA  1 
ATOM   8362  C C   . TYR F  1 2   ? 1.774   49.538  10.703  1.00 69.00  ? -6  TYR F C   1 
ATOM   8363  O O   . TYR F  1 2   ? 3.004   49.472  10.593  1.00 70.31  ? -6  TYR F O   1 
ATOM   8364  C CB  . TYR F  1 2   ? 0.284   49.504  8.617   1.00 70.40  ? -6  TYR F CB  1 
ATOM   8365  C CG  . TYR F  1 2   ? 1.122   50.642  8.052   1.00 74.83  ? -6  TYR F CG  1 
ATOM   8366  C CD1 . TYR F  1 2   ? 2.281   50.394  7.319   1.00 76.50  ? -6  TYR F CD1 1 
ATOM   8367  C CD2 . TYR F  1 2   ? 0.713   51.966  8.198   1.00 76.34  ? -6  TYR F CD2 1 
ATOM   8368  C CE1 . TYR F  1 2   ? 3.031   51.438  6.783   1.00 73.43  ? -6  TYR F CE1 1 
ATOM   8369  C CE2 . TYR F  1 2   ? 1.456   53.016  7.665   1.00 79.07  ? -6  TYR F CE2 1 
ATOM   8370  C CZ  . TYR F  1 2   ? 2.614   52.743  6.958   1.00 79.88  ? -6  TYR F CZ  1 
ATOM   8371  O OH  . TYR F  1 2   ? 3.356   53.774  6.425   1.00 72.83  ? -6  TYR F OH  1 
ATOM   8372  N N   . LYS F  1 3   ? 1.149   50.277  11.618  1.00 64.36  ? -5  LYS F N   1 
ATOM   8373  C CA  . LYS F  1 3   ? 1.839   50.995  12.679  1.00 60.84  ? -5  LYS F CA  1 
ATOM   8374  C C   . LYS F  1 3   ? 2.522   50.006  13.623  1.00 64.36  ? -5  LYS F C   1 
ATOM   8375  O O   . LYS F  1 3   ? 3.752   49.965  13.703  1.00 67.20  ? -5  LYS F O   1 
ATOM   8376  C CB  . LYS F  1 3   ? 0.834   51.871  13.443  1.00 65.10  ? -5  LYS F CB  1 
ATOM   8377  C CG  . LYS F  1 3   ? 1.331   52.454  14.764  1.00 64.88  ? -5  LYS F CG  1 
ATOM   8378  C CD  . LYS F  1 3   ? 0.191   53.153  15.504  1.00 65.94  ? -5  LYS F CD  1 
ATOM   8379  C CE  . LYS F  1 3   ? 0.502   53.357  16.988  1.00 69.52  ? -5  LYS F CE  1 
ATOM   8380  N NZ  . LYS F  1 3   ? 1.609   54.330  17.237  1.00 61.19  ? -5  LYS F NZ  1 
ATOM   8381  N N   . ASP F  1 4   ? 1.716   49.192  14.310  1.00 70.75  ? -4  ASP F N   1 
ATOM   8382  C CA  . ASP F  1 4   ? 2.203   48.262  15.339  1.00 62.76  ? -4  ASP F CA  1 
ATOM   8383  C C   . ASP F  1 4   ? 2.919   47.002  14.813  1.00 51.87  ? -4  ASP F C   1 
ATOM   8384  O O   . ASP F  1 4   ? 3.125   46.048  15.565  1.00 42.04  ? -4  ASP F O   1 
ATOM   8385  C CB  . ASP F  1 4   ? 1.057   47.849  16.274  1.00 54.48  ? -4  ASP F CB  1 
ATOM   8386  C CG  . ASP F  1 4   ? 0.665   48.948  17.253  1.00 61.29  ? -4  ASP F CG  1 
ATOM   8387  O OD1 . ASP F  1 4   ? 1.391   49.144  18.258  1.00 60.95  ? -4  ASP F OD1 1 
ATOM   8388  O OD2 . ASP F  1 4   ? -0.381  49.598  17.029  1.00 57.98  ? -4  ASP F OD2 1 
ATOM   8389  N N   . ASP F  1 5   ? 3.308   47.005  13.539  1.00 53.32  ? -3  ASP F N   1 
ATOM   8390  C CA  . ASP F  1 5   ? 4.035   45.873  12.948  1.00 52.95  ? -3  ASP F CA  1 
ATOM   8391  C C   . ASP F  1 5   ? 5.347   45.528  13.686  1.00 45.13  ? -3  ASP F C   1 
ATOM   8392  O O   . ASP F  1 5   ? 5.774   44.365  13.693  1.00 34.53  ? -3  ASP F O   1 
ATOM   8393  C CB  . ASP F  1 5   ? 4.322   46.121  11.452  1.00 58.84  ? -3  ASP F CB  1 
ATOM   8394  C CG  . ASP F  1 5   ? 3.779   45.009  10.547  1.00 57.48  ? -3  ASP F CG  1 
ATOM   8395  O OD1 . ASP F  1 5   ? 2.567   44.704  10.657  1.00 53.53  ? -3  ASP F OD1 1 
ATOM   8396  O OD2 . ASP F  1 5   ? 4.561   44.445  9.734   1.00 45.62  ? -3  ASP F OD2 1 
ATOM   8397  N N   . ASP F  1 6   ? 5.977   46.528  14.307  1.00 40.74  ? -2  ASP F N   1 
ATOM   8398  C CA  . ASP F  1 6   ? 7.284   46.327  14.946  1.00 40.96  ? -2  ASP F CA  1 
ATOM   8399  C C   . ASP F  1 6   ? 7.233   46.220  16.481  1.00 41.09  ? -2  ASP F C   1 
ATOM   8400  O O   . ASP F  1 6   ? 8.257   46.335  17.159  1.00 45.16  ? -2  ASP F O   1 
ATOM   8401  C CB  . ASP F  1 6   ? 8.275   47.413  14.500  1.00 42.36  ? -2  ASP F CB  1 
ATOM   8402  C CG  . ASP F  1 6   ? 8.527   47.392  12.999  1.00 40.50  ? -2  ASP F CG  1 
ATOM   8403  O OD1 . ASP F  1 6   ? 8.576   46.280  12.428  1.00 32.98  ? -2  ASP F OD1 1 
ATOM   8404  O OD2 . ASP F  1 6   ? 8.664   48.482  12.391  1.00 42.35  ? -2  ASP F OD2 1 
ATOM   8405  N N   . ASP F  1 7   ? 6.033   46.009  17.012  1.00 35.70  ? -1  ASP F N   1 
ATOM   8406  C CA  . ASP F  1 7   ? 5.824   45.710  18.421  1.00 35.10  ? -1  ASP F CA  1 
ATOM   8407  C C   . ASP F  1 7   ? 6.377   44.308  18.639  1.00 29.05  ? -1  ASP F C   1 
ATOM   8408  O O   . ASP F  1 7   ? 5.770   43.332  18.194  1.00 29.45  ? -1  ASP F O   1 
ATOM   8409  C CB  . ASP F  1 7   ? 4.310   45.737  18.687  1.00 49.12  ? -1  ASP F CB  1 
ATOM   8410  C CG  . ASP F  1 7   ? 3.946   45.676  20.166  1.00 42.95  ? -1  ASP F CG  1 
ATOM   8411  O OD1 . ASP F  1 7   ? 4.593   44.923  20.927  1.00 44.02  ? -1  ASP F OD1 1 
ATOM   8412  O OD2 . ASP F  1 7   ? 2.981   46.376  20.555  1.00 45.09  ? -1  ASP F OD2 1 
ATOM   8413  N N   . LYS F  1 8   ? 7.529   44.192  19.296  1.00 25.31  ? 0   LYS F N   1 
ATOM   8414  C CA  . LYS F  1 8   ? 8.207   42.894  19.353  1.00 22.75  ? 0   LYS F CA  1 
ATOM   8415  C C   . LYS F  1 8   ? 7.486   41.867  20.216  1.00 26.48  ? 0   LYS F C   1 
ATOM   8416  O O   . LYS F  1 8   ? 7.476   40.677  19.898  1.00 25.54  ? 0   LYS F O   1 
ATOM   8417  C CB  . LYS F  1 8   ? 9.652   43.019  19.821  1.00 23.50  ? 0   LYS F CB  1 
ATOM   8418  C CG  . LYS F  1 8   ? 10.407  41.706  19.683  1.00 19.31  ? 0   LYS F CG  1 
ATOM   8419  C CD  . LYS F  1 8   ? 11.718  41.702  20.424  1.00 14.44  ? 0   LYS F CD  1 
ATOM   8420  C CE  . LYS F  1 8   ? 12.362  40.332  20.330  1.00 14.76  ? 0   LYS F CE  1 
ATOM   8421  N NZ  . LYS F  1 8   ? 13.513  40.173  21.272  1.00 19.28  ? 0   LYS F NZ  1 
ATOM   8422  N N   . LEU F  1 9   ? 6.890   42.321  21.312  1.00 26.51  ? 1   LEU F N   1 
ATOM   8423  C CA  . LEU F  1 9   ? 6.162   41.418  22.188  1.00 22.42  ? 1   LEU F CA  1 
ATOM   8424  C C   . LEU F  1 9   ? 4.911   40.898  21.481  1.00 24.66  ? 1   LEU F C   1 
ATOM   8425  O O   . LEU F  1 9   ? 4.537   39.724  21.630  1.00 18.69  ? 1   LEU F O   1 
ATOM   8426  C CB  . LEU F  1 9   ? 5.800   42.124  23.492  1.00 26.45  ? 1   LEU F CB  1 
ATOM   8427  C CG  . LEU F  1 9   ? 5.080   41.258  24.523  1.00 21.43  ? 1   LEU F CG  1 
ATOM   8428  C CD1 . LEU F  1 9   ? 5.987   40.096  24.871  1.00 19.36  ? 1   LEU F CD1 1 
ATOM   8429  C CD2 . LEU F  1 9   ? 4.721   42.079  25.742  1.00 12.09  ? 1   LEU F CD2 1 
ATOM   8430  N N   . ASP F  1 10  ? 4.285   41.781  20.701  1.00 27.69  ? 2   ASP F N   1 
ATOM   8431  C CA  . ASP F  1 10  ? 3.059   41.464  19.966  1.00 28.36  ? 2   ASP F CA  1 
ATOM   8432  C C   . ASP F  1 10  ? 3.303   40.424  18.863  1.00 24.66  ? 2   ASP F C   1 
ATOM   8433  O O   . ASP F  1 10  ? 2.414   39.636  18.531  1.00 24.01  ? 2   ASP F O   1 
ATOM   8434  C CB  . ASP F  1 10  ? 2.443   42.739  19.365  1.00 35.56  ? 2   ASP F CB  1 
ATOM   8435  C CG  . ASP F  1 10  ? 1.166   43.191  20.087  1.00 43.92  ? 2   ASP F CG  1 
ATOM   8436  O OD1 . ASP F  1 10  ? 0.361   42.329  20.523  1.00 45.17  ? 2   ASP F OD1 1 
ATOM   8437  O OD2 . ASP F  1 10  ? 0.963   44.423  20.196  1.00 40.47  ? 2   ASP F OD2 1 
ATOM   8438  N N   . ARG F  1 11  ? 4.508   40.419  18.297  1.00 24.31  ? 3   ARG F N   1 
ATOM   8439  C CA  . ARG F  1 11  ? 4.836   39.453  17.251  1.00 19.59  ? 3   ARG F CA  1 
ATOM   8440  C C   . ARG F  1 11  ? 5.100   38.082  17.862  1.00 15.22  ? 3   ARG F C   1 
ATOM   8441  O O   . ARG F  1 11  ? 4.821   37.057  17.245  1.00 10.56  ? 3   ARG F O   1 
ATOM   8442  C CB  . ARG F  1 11  ? 6.048   39.910  16.426  1.00 17.97  ? 3   ARG F CB  1 
ATOM   8443  C CG  . ARG F  1 11  ? 5.869   41.236  15.703  1.00 18.74  ? 3   ARG F CG  1 
ATOM   8444  C CD  . ARG F  1 11  ? 7.079   41.558  14.805  1.00 23.57  ? 3   ARG F CD  1 
ATOM   8445  N NE  . ARG F  1 11  ? 7.210   40.629  13.683  1.00 21.51  ? 3   ARG F NE  1 
ATOM   8446  C CZ  . ARG F  1 11  ? 6.750   40.863  12.458  1.00 18.72  ? 3   ARG F CZ  1 
ATOM   8447  N NH1 . ARG F  1 11  ? 6.131   41.999  12.177  1.00 21.63  ? 3   ARG F NH1 1 
ATOM   8448  N NH2 . ARG F  1 11  ? 6.907   39.956  11.514  1.00 17.28  ? 3   ARG F NH2 1 
ATOM   8449  N N   . ALA F  1 12  ? 5.629   38.076  19.085  1.00 19.49  ? 4   ALA F N   1 
ATOM   8450  C CA  . ALA F  1 12  ? 5.991   36.836  19.763  1.00 11.27  ? 4   ALA F CA  1 
ATOM   8451  C C   . ALA F  1 12  ? 4.731   36.163  20.225  1.00 12.73  ? 4   ALA F C   1 
ATOM   8452  O O   . ALA F  1 12  ? 4.619   34.938  20.162  1.00 10.24  ? 4   ALA F O   1 
ATOM   8453  C CB  . ALA F  1 12  ? 6.919   37.107  20.932  1.00 12.33  ? 4   ALA F CB  1 
ATOM   8454  N N   . ASP F  1 13  ? 3.775   36.974  20.675  1.00 13.04  ? 5   ASP F N   1 
ATOM   8455  C CA  . ASP F  1 13  ? 2.472   36.450  21.056  1.00 14.20  ? 5   ASP F CA  1 
ATOM   8456  C C   . ASP F  1 13  ? 1.749   35.800  19.879  1.00 14.65  ? 5   ASP F C   1 
ATOM   8457  O O   . ASP F  1 13  ? 1.190   34.713  20.020  1.00 16.46  ? 5   ASP F O   1 
ATOM   8458  C CB  . ASP F  1 13  ? 1.589   37.527  21.687  1.00 15.20  ? 5   ASP F CB  1 
ATOM   8459  C CG  . ASP F  1 13  ? 2.015   37.881  23.092  1.00 16.95  ? 5   ASP F CG  1 
ATOM   8460  O OD1 . ASP F  1 13  ? 2.848   37.151  23.680  1.00 15.82  ? 5   ASP F OD1 1 
ATOM   8461  O OD2 . ASP F  1 13  ? 1.514   38.892  23.610  1.00 15.97  ? 5   ASP F OD2 1 
ATOM   8462  N N   . ILE F  1 14  ? 1.739   36.471  18.731  1.00 12.95  ? 6   ILE F N   1 
ATOM   8463  C CA  . ILE F  1 14  ? 1.128   35.914  17.526  1.00 11.27  ? 6   ILE F CA  1 
ATOM   8464  C C   . ILE F  1 14  ? 1.785   34.583  17.167  1.00 11.89  ? 6   ILE F C   1 
ATOM   8465  O O   . ILE F  1 14  ? 1.098   33.598  16.875  1.00 9.93   ? 6   ILE F O   1 
ATOM   8466  C CB  . ILE F  1 14  ? 1.217   36.908  16.343  1.00 14.37  ? 6   ILE F CB  1 
ATOM   8467  C CG1 . ILE F  1 14  ? 0.252   38.070  16.573  1.00 15.46  ? 6   ILE F CG1 1 
ATOM   8468  C CG2 . ILE F  1 14  ? 0.892   36.223  15.035  1.00 11.44  ? 6   ILE F CG2 1 
ATOM   8469  C CD1 . ILE F  1 14  ? 0.578   39.302  15.792  1.00 20.71  ? 6   ILE F CD1 1 
ATOM   8470  N N   . LEU F  1 15  ? 3.116   34.557  17.219  1.00 10.96  ? 7   LEU F N   1 
ATOM   8471  C CA  . LEU F  1 15  ? 3.891   33.343  16.965  1.00 10.08  ? 7   LEU F CA  1 
ATOM   8472  C C   . LEU F  1 15  ? 3.462   32.216  17.897  1.00 12.57  ? 7   LEU F C   1 
ATOM   8473  O O   . LEU F  1 15  ? 3.267   31.070  17.467  1.00 12.26  ? 7   LEU F O   1 
ATOM   8474  C CB  . LEU F  1 15  ? 5.377   33.626  17.164  1.00 9.60   ? 7   LEU F CB  1 
ATOM   8475  C CG  . LEU F  1 15  ? 6.355   32.599  16.610  1.00 18.83  ? 7   LEU F CG  1 
ATOM   8476  C CD1 . LEU F  1 15  ? 6.217   32.493  15.086  1.00 14.96  ? 7   LEU F CD1 1 
ATOM   8477  C CD2 . LEU F  1 15  ? 7.771   32.984  17.003  1.00 13.50  ? 7   LEU F CD2 1 
ATOM   8478  N N   . TYR F  1 16  ? 3.317   32.560  19.177  1.00 10.71  ? 8   TYR F N   1 
ATOM   8479  C CA  . TYR F  1 16  ? 2.897   31.619  20.198  1.00 9.62   ? 8   TYR F CA  1 
ATOM   8480  C C   . TYR F  1 16  ? 1.463   31.123  19.926  1.00 11.63  ? 8   TYR F C   1 
ATOM   8481  O O   . TYR F  1 16  ? 1.200   29.919  19.968  1.00 11.17  ? 8   TYR F O   1 
ATOM   8482  C CB  . TYR F  1 16  ? 3.059   32.262  21.589  1.00 11.70  ? 8   TYR F CB  1 
ATOM   8483  C CG  . TYR F  1 16  ? 2.293   31.587  22.718  1.00 14.22  ? 8   TYR F CG  1 
ATOM   8484  C CD1 . TYR F  1 16  ? 2.749   30.398  23.294  1.00 12.44  ? 8   TYR F CD1 1 
ATOM   8485  C CD2 . TYR F  1 16  ? 1.113   32.147  23.213  1.00 13.47  ? 8   TYR F CD2 1 
ATOM   8486  C CE1 . TYR F  1 16  ? 2.052   29.785  24.321  1.00 15.10  ? 8   TYR F CE1 1 
ATOM   8487  C CE2 . TYR F  1 16  ? 0.414   31.549  24.236  1.00 15.69  ? 8   TYR F CE2 1 
ATOM   8488  C CZ  . TYR F  1 16  ? 0.881   30.367  24.793  1.00 19.31  ? 8   TYR F CZ  1 
ATOM   8489  O OH  . TYR F  1 16  ? 0.165   29.774  25.820  1.00 19.37  ? 8   TYR F OH  1 
ATOM   8490  N N   . ASN F  1 17  ? 0.551   32.046  19.617  1.00 9.71   ? 9   ASN F N   1 
ATOM   8491  C CA  . ASN F  1 17  ? -0.802  31.674  19.229  1.00 8.67   ? 9   ASN F CA  1 
ATOM   8492  C C   . ASN F  1 17  ? -0.817  30.746  18.039  1.00 10.67  ? 9   ASN F C   1 
ATOM   8493  O O   . ASN F  1 17  ? -1.510  29.734  18.056  1.00 9.86   ? 9   ASN F O   1 
ATOM   8494  C CB  . ASN F  1 17  ? -1.662  32.903  18.962  1.00 8.00   ? 9   ASN F CB  1 
ATOM   8495  C CG  . ASN F  1 17  ? -1.751  33.789  20.159  1.00 12.51  ? 9   ASN F CG  1 
ATOM   8496  O OD1 . ASN F  1 17  ? -1.531  33.328  21.273  1.00 18.40  ? 9   ASN F OD1 1 
ATOM   8497  N ND2 . ASN F  1 17  ? -2.069  35.060  19.958  1.00 12.88  ? 9   ASN F ND2 1 
ATOM   8498  N N   . ILE F  1 18  ? -0.032  31.087  17.013  1.00 14.90  ? 10  ILE F N   1 
ATOM   8499  C CA  . ILE F  1 18  ? 0.069   30.259  15.813  1.00 11.79  ? 10  ILE F CA  1 
ATOM   8500  C C   . ILE F  1 18  ? 0.626   28.876  16.165  1.00 11.80  ? 10  ILE F C   1 
ATOM   8501  O O   . ILE F  1 18  ? 0.081   27.849  15.738  1.00 11.36  ? 10  ILE F O   1 
ATOM   8502  C CB  . ILE F  1 18  ? 0.890   30.946  14.688  1.00 13.72  ? 10  ILE F CB  1 
ATOM   8503  C CG1 . ILE F  1 18  ? 0.176   32.212  14.214  1.00 12.59  ? 10  ILE F CG1 1 
ATOM   8504  C CG2 . ILE F  1 18  ? 1.108   29.999  13.509  1.00 10.83  ? 10  ILE F CG2 1 
ATOM   8505  C CD1 . ILE F  1 18  ? 0.951   33.013  13.201  1.00 13.23  ? 10  ILE F CD1 1 
ATOM   8506  N N   . ARG F  1 19  ? 1.678   28.827  16.973  1.00 9.46   ? 11  ARG F N   1 
ATOM   8507  C CA  . ARG F  1 19  ? 2.185   27.520  17.379  1.00 11.04  ? 11  ARG F CA  1 
ATOM   8508  C C   . ARG F  1 19  ? 1.181   26.687  18.194  1.00 11.80  ? 11  ARG F C   1 
ATOM   8509  O O   . ARG F  1 19  ? 1.115   25.463  18.071  1.00 13.14  ? 11  ARG F O   1 
ATOM   8510  C CB  . ARG F  1 19  ? 3.528   27.652  18.076  1.00 11.81  ? 11  ARG F CB  1 
ATOM   8511  C CG  . ARG F  1 19  ? 4.672   27.600  17.081  1.00 16.14  ? 11  ARG F CG  1 
ATOM   8512  C CD  . ARG F  1 19  ? 5.943   28.213  17.609  1.00 17.27  ? 11  ARG F CD  1 
ATOM   8513  N NE  . ARG F  1 19  ? 6.991   28.082  16.608  1.00 24.67  ? 11  ARG F NE  1 
ATOM   8514  C CZ  . ARG F  1 19  ? 8.176   28.676  16.678  1.00 24.06  ? 11  ARG F CZ  1 
ATOM   8515  N NH1 . ARG F  1 19  ? 8.470   29.469  17.702  1.00 26.54  ? 11  ARG F NH1 1 
ATOM   8516  N NH2 . ARG F  1 19  ? 9.058   28.481  15.712  1.00 21.77  ? 11  ARG F NH2 1 
ATOM   8517  N N   . GLN F  1 20  ? 0.374   27.354  19.001  1.00 12.68  ? 12  GLN F N   1 
ATOM   8518  C CA  . GLN F  1 20  ? -0.627  26.655  19.777  1.00 10.88  ? 12  GLN F CA  1 
ATOM   8519  C C   . GLN F  1 20  ? -1.772  26.093  18.919  1.00 13.18  ? 12  GLN F C   1 
ATOM   8520  O O   . GLN F  1 20  ? -2.202  24.963  19.120  1.00 17.52  ? 12  GLN F O   1 
ATOM   8521  C CB  . GLN F  1 20  ? -1.140  27.580  20.862  1.00 13.09  ? 12  GLN F CB  1 
ATOM   8522  C CG  . GLN F  1 20  ? -0.111  27.839  21.943  1.00 15.68  ? 12  GLN F CG  1 
ATOM   8523  C CD  . GLN F  1 20  ? -0.690  27.640  23.325  1.00 30.15  ? 12  GLN F CD  1 
ATOM   8524  O OE1 . GLN F  1 20  ? -1.610  28.360  23.737  1.00 34.70  ? 12  GLN F OE1 1 
ATOM   8525  N NE2 . GLN F  1 20  ? -0.179  26.636  24.044  1.00 27.68  ? 12  GLN F NE2 1 
ATOM   8526  N N   . THR F  1 21  ? -2.258  26.867  17.955  1.00 13.09  ? 13  THR F N   1 
ATOM   8527  C CA  . THR F  1 21  ? -3.358  26.417  17.096  1.00 14.39  ? 13  THR F CA  1 
ATOM   8528  C C   . THR F  1 21  ? -2.928  25.404  16.024  1.00 12.88  ? 13  THR F C   1 
ATOM   8529  O O   . THR F  1 21  ? -3.637  24.432  15.744  1.00 11.79  ? 13  THR F O   1 
ATOM   8530  C CB  . THR F  1 21  ? -4.012  27.603  16.383  1.00 14.15  ? 13  THR F CB  1 
ATOM   8531  O OG1 . THR F  1 21  ? -4.570  28.500  17.353  1.00 12.37  ? 13  THR F OG1 1 
ATOM   8532  C CG2 . THR F  1 21  ? -5.090  27.130  15.403  1.00 12.22  ? 13  THR F CG2 1 
ATOM   8533  N N   . SER F  1 22  ? -1.754  25.632  15.447  1.00 13.11  ? 14  SER F N   1 
ATOM   8534  C CA  . SER F  1 22  ? -1.297  24.883  14.274  1.00 11.39  ? 14  SER F CA  1 
ATOM   8535  C C   . SER F  1 22  ? -1.130  23.380  14.469  1.00 10.69  ? 14  SER F C   1 
ATOM   8536  O O   . SER F  1 22  ? -0.577  22.913  15.473  1.00 10.80  ? 14  SER F O   1 
ATOM   8537  C CB  . SER F  1 22  ? 0.010   25.466  13.751  1.00 9.36   ? 14  SER F CB  1 
ATOM   8538  O OG  . SER F  1 22  ? 0.591   24.594  12.804  1.00 11.76  ? 14  SER F OG  1 
ATOM   8539  N N   . ARG F  1 23  ? -1.625  22.636  13.487  1.00 9.14   ? 15  ARG F N   1 
ATOM   8540  C CA  . ARG F  1 23  ? -1.463  21.197  13.438  1.00 9.25   ? 15  ARG F CA  1 
ATOM   8541  C C   . ARG F  1 23  ? -0.736  20.862  12.136  1.00 12.65  ? 15  ARG F C   1 
ATOM   8542  O O   . ARG F  1 23  ? -1.360  20.582  11.100  1.00 13.29  ? 15  ARG F O   1 
ATOM   8543  C CB  . ARG F  1 23  ? -2.819  20.512  13.506  1.00 8.68   ? 15  ARG F CB  1 
ATOM   8544  C CG  . ARG F  1 23  ? -3.864  21.328  14.229  1.00 12.35  ? 15  ARG F CG  1 
ATOM   8545  C CD  . ARG F  1 23  ? -5.160  20.550  14.430  1.00 21.37  ? 15  ARG F CD  1 
ATOM   8546  N NE  . ARG F  1 23  ? -5.031  19.555  15.491  1.00 28.17  ? 15  ARG F NE  1 
ATOM   8547  C CZ  . ARG F  1 23  ? -5.982  19.269  16.374  1.00 21.00  ? 15  ARG F CZ  1 
ATOM   8548  N NH1 . ARG F  1 23  ? -7.150  19.893  16.330  1.00 13.77  ? 15  ARG F NH1 1 
ATOM   8549  N NH2 . ARG F  1 23  ? -5.757  18.350  17.303  1.00 25.67  ? 15  ARG F NH2 1 
ATOM   8550  N N   . PRO F  1 24  ? 0.598   20.901  12.188  1.00 12.15  ? 16  PRO F N   1 
ATOM   8551  C CA  . PRO F  1 24  ? 1.534   20.728  11.071  1.00 13.23  ? 16  PRO F CA  1 
ATOM   8552  C C   . PRO F  1 24  ? 1.277   19.516  10.178  1.00 12.61  ? 16  PRO F C   1 
ATOM   8553  O O   . PRO F  1 24  ? 1.654   19.544  9.012   1.00 20.58  ? 16  PRO F O   1 
ATOM   8554  C CB  . PRO F  1 24  ? 2.880   20.548  11.791  1.00 16.47  ? 16  PRO F CB  1 
ATOM   8555  C CG  . PRO F  1 24  ? 2.717   21.324  13.048  1.00 8.97   ? 16  PRO F CG  1 
ATOM   8556  C CD  . PRO F  1 24  ? 1.306   21.068  13.468  1.00 8.55   ? 16  PRO F CD  1 
ATOM   8557  N N   . ASP F  1 25  ? 0.655   18.473  10.707  1.00 10.67  ? 17  ASP F N   1 
ATOM   8558  C CA  . ASP F  1 25  ? 0.556   17.225  9.988   1.00 8.90   ? 17  ASP F CA  1 
ATOM   8559  C C   . ASP F  1 25  ? -0.869  16.918  9.596   1.00 10.06  ? 17  ASP F C   1 
ATOM   8560  O O   . ASP F  1 25  ? -1.160  15.818  9.112   1.00 13.01  ? 17  ASP F O   1 
ATOM   8561  C CB  . ASP F  1 25  ? 1.150   16.076  10.809  1.00 9.57   ? 17  ASP F CB  1 
ATOM   8562  C CG  . ASP F  1 25  ? 2.647   16.242  11.052  1.00 14.90  ? 17  ASP F CG  1 
ATOM   8563  O OD1 . ASP F  1 25  ? 3.275   17.025  10.310  1.00 26.38  ? 17  ASP F OD1 1 
ATOM   8564  O OD2 . ASP F  1 25  ? 3.208   15.597  11.972  1.00 11.85  ? 17  ASP F OD2 1 
ATOM   8565  N N   . VAL F  1 26  ? -1.761  17.883  9.787   1.00 8.06   ? 18  VAL F N   1 
ATOM   8566  C CA  . VAL F  1 26  ? -3.147  17.688  9.365   1.00 13.46  ? 18  VAL F CA  1 
ATOM   8567  C C   . VAL F  1 26  ? -3.595  18.783  8.399   1.00 10.22  ? 18  VAL F C   1 
ATOM   8568  O O   . VAL F  1 26  ? -3.395  19.969  8.674   1.00 9.51   ? 18  VAL F O   1 
ATOM   8569  C CB  . VAL F  1 26  ? -4.151  17.619  10.572  1.00 11.68  ? 18  VAL F CB  1 
ATOM   8570  C CG1 . VAL F  1 26  ? -5.550  17.283  10.073  1.00 12.29  ? 18  VAL F CG1 1 
ATOM   8571  C CG2 . VAL F  1 26  ? -3.731  16.586  11.597  1.00 7.10   ? 18  VAL F CG2 1 
ATOM   8572  N N   . ILE F  1 27  ? -4.211  18.389  7.284   1.00 10.15  ? 19  ILE F N   1 
ATOM   8573  C CA  . ILE F  1 27  ? -4.693  19.360  6.287   1.00 15.57  ? 19  ILE F CA  1 
ATOM   8574  C C   . ILE F  1 27  ? -5.760  20.293  6.875   1.00 15.48  ? 19  ILE F C   1 
ATOM   8575  O O   . ILE F  1 27  ? -6.650  19.851  7.586   1.00 13.89  ? 19  ILE F O   1 
ATOM   8576  C CB  . ILE F  1 27  ? -5.240  18.680  4.987   1.00 17.08  ? 19  ILE F CB  1 
ATOM   8577  C CG1 . ILE F  1 27  ? -6.563  17.958  5.261   1.00 18.20  ? 19  ILE F CG1 1 
ATOM   8578  C CG2 . ILE F  1 27  ? -4.207  17.713  4.367   1.00 12.43  ? 19  ILE F CG2 1 
ATOM   8579  C CD1 . ILE F  1 27  ? -6.994  17.055  4.125   1.00 20.25  ? 19  ILE F CD1 1 
ATOM   8580  N N   . PRO F  1 28  ? -5.654  21.599  6.592   1.00 15.86  ? 20  PRO F N   1 
ATOM   8581  C CA  . PRO F  1 28  ? -6.555  22.639  7.113   1.00 15.77  ? 20  PRO F CA  1 
ATOM   8582  C C   . PRO F  1 28  ? -7.883  22.778  6.356   1.00 18.59  ? 20  PRO F C   1 
ATOM   8583  O O   . PRO F  1 28  ? -8.229  23.886  5.935   1.00 19.53  ? 20  PRO F O   1 
ATOM   8584  C CB  . PRO F  1 28  ? -5.731  23.921  6.957   1.00 12.75  ? 20  PRO F CB  1 
ATOM   8585  C CG  . PRO F  1 28  ? -4.833  23.649  5.852   1.00 14.54  ? 20  PRO F CG  1 
ATOM   8586  C CD  . PRO F  1 28  ? -4.555  22.169  5.806   1.00 11.74  ? 20  PRO F CD  1 
ATOM   8587  N N   . THR F  1 29  ? -8.608  21.671  6.203   1.00 23.06  ? 21  THR F N   1 
ATOM   8588  C CA  . THR F  1 29  ? -9.902  21.657  5.516   1.00 28.94  ? 21  THR F CA  1 
ATOM   8589  C C   . THR F  1 29  ? -10.967 22.298  6.384   1.00 32.45  ? 21  THR F C   1 
ATOM   8590  O O   . THR F  1 29  ? -11.005 22.084  7.598   1.00 30.03  ? 21  THR F O   1 
ATOM   8591  C CB  . THR F  1 29  ? -10.372 20.232  5.198   1.00 25.35  ? 21  THR F CB  1 
ATOM   8592  O OG1 . THR F  1 29  ? -10.383 19.458  6.404   1.00 17.93  ? 21  THR F OG1 1 
ATOM   8593  C CG2 . THR F  1 29  ? -9.451  19.579  4.198   1.00 23.43  ? 21  THR F CG2 1 
ATOM   8594  N N   . GLN F  1 30  ? -11.850 23.057  5.746   1.00 39.13  ? 22  GLN F N   1 
ATOM   8595  C CA  . GLN F  1 30  ? -12.764 23.936  6.460   1.00 49.64  ? 22  GLN F CA  1 
ATOM   8596  C C   . GLN F  1 30  ? -14.225 23.678  6.090   1.00 55.75  ? 22  GLN F C   1 
ATOM   8597  O O   . GLN F  1 30  ? -14.722 24.216  5.103   1.00 59.26  ? 22  GLN F O   1 
ATOM   8598  C CB  . GLN F  1 30  ? -12.377 25.396  6.186   1.00 47.20  ? 22  GLN F CB  1 
ATOM   8599  C CG  . GLN F  1 30  ? -10.902 25.692  6.490   1.00 47.24  ? 22  GLN F CG  1 
ATOM   8600  C CD  . GLN F  1 30  ? -10.414 27.012  5.906   1.00 47.35  ? 22  GLN F CD  1 
ATOM   8601  O OE1 . GLN F  1 30  ? -9.392  27.556  6.342   1.00 36.18  ? 22  GLN F OE1 1 
ATOM   8602  N NE2 . GLN F  1 30  ? -11.138 27.529  4.913   1.00 47.70  ? 22  GLN F NE2 1 
ATOM   8603  N N   . ARG F  1 31  ? -14.898 22.853  6.893   1.00 51.85  ? 23  ARG F N   1 
ATOM   8604  C CA  . ARG F  1 31  ? -16.308 22.500  6.678   1.00 59.79  ? 23  ARG F CA  1 
ATOM   8605  C C   . ARG F  1 31  ? -16.563 21.809  5.329   1.00 55.62  ? 23  ARG F C   1 
ATOM   8606  O O   . ARG F  1 31  ? -17.495 22.146  4.592   1.00 42.22  ? 23  ARG F O   1 
ATOM   8607  C CB  . ARG F  1 31  ? -17.217 23.718  6.885   1.00 67.54  ? 23  ARG F CB  1 
ATOM   8608  C CG  . ARG F  1 31  ? -17.205 24.248  8.324   1.00 68.20  ? 23  ARG F CG  1 
ATOM   8609  C CD  . ARG F  1 31  ? -17.168 25.772  8.364   1.00 71.75  ? 23  ARG F CD  1 
ATOM   8610  N NE  . ARG F  1 31  ? -18.409 26.354  8.871   1.00 74.37  ? 23  ARG F NE  1 
ATOM   8611  C CZ  . ARG F  1 31  ? -18.663 27.660  8.899   1.00 79.53  ? 23  ARG F CZ  1 
ATOM   8612  N NH1 . ARG F  1 31  ? -17.762 28.523  8.442   1.00 69.03  ? 23  ARG F NH1 1 
ATOM   8613  N NH2 . ARG F  1 31  ? -19.818 28.105  9.379   1.00 77.24  ? 23  ARG F NH2 1 
ATOM   8614  N N   . ASP F  1 32  ? -15.693 20.849  5.026   1.00 55.12  ? 24  ASP F N   1 
ATOM   8615  C CA  . ASP F  1 32  ? -15.833 19.921  3.895   1.00 52.41  ? 24  ASP F CA  1 
ATOM   8616  C C   . ASP F  1 32  ? -15.677 20.470  2.466   1.00 54.07  ? 24  ASP F C   1 
ATOM   8617  O O   . ASP F  1 32  ? -16.277 19.965  1.506   1.00 50.47  ? 24  ASP F O   1 
ATOM   8618  C CB  . ASP F  1 32  ? -17.079 19.046  4.031   1.00 51.01  ? 24  ASP F CB  1 
ATOM   8619  C CG  . ASP F  1 32  ? -16.741 17.573  3.962   1.00 55.73  ? 24  ASP F CG  1 
ATOM   8620  O OD1 . ASP F  1 32  ? -16.905 16.970  2.877   1.00 69.35  ? 24  ASP F OD1 1 
ATOM   8621  O OD2 . ASP F  1 32  ? -16.270 17.030  4.985   1.00 49.00  ? 24  ASP F OD2 1 
ATOM   8622  N N   . ARG F  1 33  ? -14.856 21.501  2.337   1.00 53.18  ? 25  ARG F N   1 
ATOM   8623  C CA  . ARG F  1 33  ? -14.292 21.858  1.054   1.00 43.90  ? 25  ARG F CA  1 
ATOM   8624  C C   . ARG F  1 33  ? -12.816 21.475  1.159   1.00 40.32  ? 25  ARG F C   1 
ATOM   8625  O O   . ARG F  1 33  ? -12.169 21.754  2.172   1.00 42.78  ? 25  ARG F O   1 
ATOM   8626  C CB  . ARG F  1 33  ? -14.443 23.359  0.791   1.00 47.80  ? 25  ARG F CB  1 
ATOM   8627  C CG  . ARG F  1 33  ? -15.557 24.044  1.584   1.00 51.20  ? 25  ARG F CG  1 
ATOM   8628  C CD  . ARG F  1 33  ? -15.462 25.573  1.482   1.00 60.87  ? 25  ARG F CD  1 
ATOM   8629  N NE  . ARG F  1 33  ? -16.147 26.260  2.582   1.00 74.42  ? 25  ARG F NE  1 
ATOM   8630  C CZ  . ARG F  1 33  ? -15.543 26.715  3.681   1.00 76.13  ? 25  ARG F CZ  1 
ATOM   8631  N NH1 . ARG F  1 33  ? -14.230 26.562  3.833   1.00 67.05  ? 25  ARG F NH1 1 
ATOM   8632  N NH2 . ARG F  1 33  ? -16.246 27.325  4.634   1.00 58.72  ? 25  ARG F NH2 1 
ATOM   8633  N N   . PRO F  1 34  ? -12.280 20.808  0.132   1.00 38.20  ? 26  PRO F N   1 
ATOM   8634  C CA  . PRO F  1 34  ? -10.843 20.532  0.058   1.00 32.74  ? 26  PRO F CA  1 
ATOM   8635  C C   . PRO F  1 34  ? -10.000 21.787  0.275   1.00 28.81  ? 26  PRO F C   1 
ATOM   8636  O O   . PRO F  1 34  ? -10.489 22.890  0.042   1.00 29.03  ? 26  PRO F O   1 
ATOM   8637  C CB  . PRO F  1 34  ? -10.664 20.044  -1.388  1.00 31.41  ? 26  PRO F CB  1 
ATOM   8638  C CG  . PRO F  1 34  ? -11.948 20.352  -2.076  1.00 26.09  ? 26  PRO F CG  1 
ATOM   8639  C CD  . PRO F  1 34  ? -12.989 20.271  -1.036  1.00 31.78  ? 26  PRO F CD  1 
ATOM   8640  N N   . VAL F  1 35  ? -8.754  21.627  0.706   1.00 26.68  ? 27  VAL F N   1 
ATOM   8641  C CA  . VAL F  1 35  ? -7.864  22.775  0.814   1.00 27.12  ? 27  VAL F CA  1 
ATOM   8642  C C   . VAL F  1 35  ? -7.610  23.335  -0.582  1.00 26.94  ? 27  VAL F C   1 
ATOM   8643  O O   . VAL F  1 35  ? -7.307  22.591  -1.526  1.00 23.73  ? 27  VAL F O   1 
ATOM   8644  C CB  . VAL F  1 35  ? -6.518  22.415  1.484   1.00 25.92  ? 27  VAL F CB  1 
ATOM   8645  C CG1 . VAL F  1 35  ? -5.805  23.678  1.947   1.00 18.77  ? 27  VAL F CG1 1 
ATOM   8646  C CG2 . VAL F  1 35  ? -6.745  21.504  2.664   1.00 24.27  ? 27  VAL F CG2 1 
ATOM   8647  N N   . ALA F  1 36  ? -7.758  24.646  -0.718  1.00 26.48  ? 28  ALA F N   1 
ATOM   8648  C CA  . ALA F  1 36  ? -7.526  25.290  -2.000  1.00 21.80  ? 28  ALA F CA  1 
ATOM   8649  C C   . ALA F  1 36  ? -6.168  25.955  -2.015  1.00 22.78  ? 28  ALA F C   1 
ATOM   8650  O O   . ALA F  1 36  ? -6.017  27.097  -1.573  1.00 20.16  ? 28  ALA F O   1 
ATOM   8651  C CB  . ALA F  1 36  ? -8.605  26.298  -2.298  1.00 19.95  ? 28  ALA F CB  1 
ATOM   8652  N N   . VAL F  1 37  ? -5.186  25.231  -2.542  1.00 26.79  ? 29  VAL F N   1 
ATOM   8653  C CA  . VAL F  1 37  ? -3.825  25.741  -2.664  1.00 30.32  ? 29  VAL F CA  1 
ATOM   8654  C C   . VAL F  1 37  ? -3.534  26.369  -4.030  1.00 30.20  ? 29  VAL F C   1 
ATOM   8655  O O   . VAL F  1 37  ? -3.652  25.702  -5.055  1.00 26.64  ? 29  VAL F O   1 
ATOM   8656  C CB  . VAL F  1 37  ? -2.810  24.618  -2.443  1.00 31.67  ? 29  VAL F CB  1 
ATOM   8657  C CG1 . VAL F  1 37  ? -1.391  25.165  -2.564  1.00 26.38  ? 29  VAL F CG1 1 
ATOM   8658  C CG2 . VAL F  1 37  ? -3.049  23.936  -1.088  1.00 26.12  ? 29  VAL F CG2 1 
ATOM   8659  N N   . SER F  1 38  ? -3.144  27.645  -4.023  1.00 30.40  ? 30  SER F N   1 
ATOM   8660  C CA  . SER F  1 38  ? -2.717  28.362  -5.227  1.00 28.20  ? 30  SER F CA  1 
ATOM   8661  C C   . SER F  1 38  ? -1.228  28.209  -5.505  1.00 30.90  ? 30  SER F C   1 
ATOM   8662  O O   . SER F  1 38  ? -0.397  28.648  -4.716  1.00 30.56  ? 30  SER F O   1 
ATOM   8663  C CB  . SER F  1 38  ? -3.028  29.850  -5.108  1.00 22.43  ? 30  SER F CB  1 
ATOM   8664  O OG  . SER F  1 38  ? -4.411  30.078  -5.278  1.00 37.72  ? 30  SER F OG  1 
ATOM   8665  N N   . VAL F  1 39  ? -0.893  27.605  -6.640  1.00 32.91  ? 31  VAL F N   1 
ATOM   8666  C CA  . VAL F  1 39  ? 0.497   27.477  -7.049  1.00 30.03  ? 31  VAL F CA  1 
ATOM   8667  C C   . VAL F  1 39  ? 0.764   28.370  -8.246  1.00 38.97  ? 31  VAL F C   1 
ATOM   8668  O O   . VAL F  1 39  ? -0.162  28.802  -8.934  1.00 42.32  ? 31  VAL F O   1 
ATOM   8669  C CB  . VAL F  1 39  ? 0.831   26.045  -7.454  1.00 27.96  ? 31  VAL F CB  1 
ATOM   8670  C CG1 . VAL F  1 39  ? 2.205   25.661  -6.940  1.00 28.94  ? 31  VAL F CG1 1 
ATOM   8671  C CG2 . VAL F  1 39  ? -0.223  25.097  -6.929  1.00 27.96  ? 31  VAL F CG2 1 
ATOM   8672  N N   . SER F  1 40  ? 2.008   28.794  -8.335  1.00 35.33  ? 32  SER F N   1 
ATOM   8673  C CA  . SER F  1 40  ? 2.518   29.439  -9.506  1.00 36.96  ? 32  SER F CA  1 
ATOM   8674  C C   . SER F  1 40  ? 3.990   29.136  -9.497  1.00 35.78  ? 32  SER F C   1 
ATOM   8675  O O   . SER F  1 40  ? 4.629   29.125  -8.444  1.00 34.41  ? 32  SER F O   1 
ATOM   8676  C CB  . SER F  1 40  ? 2.284   30.948  -9.437  1.00 40.27  ? 32  SER F CB  1 
ATOM   8677  O OG  . SER F  1 40  ? 3.264   31.650  -10.182 1.00 45.02  ? 32  SER F OG  1 
ATOM   8678  N N   . LEU F  1 41  ? 4.535   28.918  -10.675 1.00 33.57  ? 33  LEU F N   1 
ATOM   8679  C CA  . LEU F  1 41  ? 5.980   28.976  -10.855 1.00 31.49  ? 33  LEU F CA  1 
ATOM   8680  C C   . LEU F  1 41  ? 6.382   30.314  -11.470 1.00 33.21  ? 33  LEU F C   1 
ATOM   8681  O O   . LEU F  1 41  ? 5.720   30.834  -12.366 1.00 37.38  ? 33  LEU F O   1 
ATOM   8682  C CB  . LEU F  1 41  ? 6.493   27.812  -11.699 1.00 30.35  ? 33  LEU F CB  1 
ATOM   8683  C CG  . LEU F  1 41  ? 6.082   26.408  -11.250 1.00 29.99  ? 33  LEU F CG  1 
ATOM   8684  C CD1 . LEU F  1 41  ? 6.944   25.333  -11.923 1.00 21.46  ? 33  LEU F CD1 1 
ATOM   8685  C CD2 . LEU F  1 41  ? 6.126   26.281  -9.732  1.00 31.69  ? 33  LEU F CD2 1 
ATOM   8686  N N   . LYS F  1 42  ? 7.446   30.895  -10.943 1.00 30.72  ? 34  LYS F N   1 
ATOM   8687  C CA  . LYS F  1 42  ? 7.964   32.138  -11.476 1.00 34.14  ? 34  LYS F CA  1 
ATOM   8688  C C   . LYS F  1 42  ? 9.397   31.849  -11.844 1.00 31.63  ? 34  LYS F C   1 
ATOM   8689  O O   . LYS F  1 42  ? 10.272  31.739  -10.980 1.00 26.90  ? 34  LYS F O   1 
ATOM   8690  C CB  . LYS F  1 42  ? 7.876   33.278  -10.455 1.00 34.55  ? 34  LYS F CB  1 
ATOM   8691  C CG  . LYS F  1 42  ? 6.789   34.297  -10.755 1.00 39.90  ? 34  LYS F CG  1 
ATOM   8692  C CD  . LYS F  1 42  ? 5.393   33.746  -10.504 1.00 52.88  ? 34  LYS F CD  1 
ATOM   8693  C CE  . LYS F  1 42  ? 4.318   34.602  -11.175 1.00 56.86  ? 34  LYS F CE  1 
ATOM   8694  N NZ  . LYS F  1 42  ? 4.331   34.424  -12.661 1.00 61.74  ? 34  LYS F NZ  1 
ATOM   8695  N N   . PHE F  1 43  ? 9.628   31.694  -13.140 1.00 35.21  ? 35  PHE F N   1 
ATOM   8696  C CA  . PHE F  1 43  ? 10.934  31.293  -13.618 1.00 27.53  ? 35  PHE F CA  1 
ATOM   8697  C C   . PHE F  1 43  ? 11.966  32.402  -13.485 1.00 26.73  ? 35  PHE F C   1 
ATOM   8698  O O   . PHE F  1 43  ? 11.676  33.572  -13.736 1.00 31.62  ? 35  PHE F O   1 
ATOM   8699  C CB  . PHE F  1 43  ? 10.824  30.751  -15.033 1.00 30.47  ? 35  PHE F CB  1 
ATOM   8700  C CG  . PHE F  1 43  ? 10.121  29.429  -15.104 1.00 24.46  ? 35  PHE F CG  1 
ATOM   8701  C CD1 . PHE F  1 43  ? 8.774   29.360  -15.413 1.00 24.19  ? 35  PHE F CD1 1 
ATOM   8702  C CD2 . PHE F  1 43  ? 10.805  28.254  -14.824 1.00 21.45  ? 35  PHE F CD2 1 
ATOM   8703  C CE1 . PHE F  1 43  ? 8.120   28.131  -15.464 1.00 30.96  ? 35  PHE F CE1 1 
ATOM   8704  C CE2 . PHE F  1 43  ? 10.159  27.021  -14.873 1.00 25.90  ? 35  PHE F CE2 1 
ATOM   8705  C CZ  . PHE F  1 43  ? 8.815   26.957  -15.195 1.00 24.17  ? 35  PHE F CZ  1 
ATOM   8706  N N   . ILE F  1 44  ? 13.161  32.019  -13.047 1.00 24.62  ? 36  ILE F N   1 
ATOM   8707  C CA  . ILE F  1 44  ? 14.231  32.965  -12.768 1.00 29.98  ? 36  ILE F CA  1 
ATOM   8708  C C   . ILE F  1 44  ? 15.405  32.728  -13.701 1.00 28.95  ? 36  ILE F C   1 
ATOM   8709  O O   . ILE F  1 44  ? 16.024  33.670  -14.188 1.00 33.14  ? 36  ILE F O   1 
ATOM   8710  C CB  . ILE F  1 44  ? 14.764  32.819  -11.316 1.00 33.89  ? 36  ILE F CB  1 
ATOM   8711  C CG1 . ILE F  1 44  ? 13.612  32.723  -10.302 1.00 28.68  ? 36  ILE F CG1 1 
ATOM   8712  C CG2 . ILE F  1 44  ? 15.716  33.972  -10.979 1.00 32.86  ? 36  ILE F CG2 1 
ATOM   8713  C CD1 . ILE F  1 44  ? 12.866  34.021  -10.090 1.00 27.46  ? 36  ILE F CD1 1 
ATOM   8714  N N   . ASN F  1 45  ? 15.707  31.459  -13.948 1.00 24.91  ? 37  ASN F N   1 
ATOM   8715  C CA  . ASN F  1 45  ? 16.909  31.100  -14.674 1.00 25.74  ? 37  ASN F CA  1 
ATOM   8716  C C   . ASN F  1 45  ? 16.789  29.707  -15.273 1.00 28.39  ? 37  ASN F C   1 
ATOM   8717  O O   . ASN F  1 45  ? 16.143  28.839  -14.701 1.00 26.24  ? 37  ASN F O   1 
ATOM   8718  C CB  . ASN F  1 45  ? 18.103  31.155  -13.722 1.00 30.11  ? 37  ASN F CB  1 
ATOM   8719  C CG  . ASN F  1 45  ? 19.413  31.542  -14.418 1.00 38.62  ? 37  ASN F CG  1 
ATOM   8720  O OD1 . ASN F  1 45  ? 19.536  31.480  -15.652 1.00 33.70  ? 37  ASN F OD1 1 
ATOM   8721  N ND2 . ASN F  1 45  ? 20.404  31.936  -13.615 1.00 30.26  ? 37  ASN F ND2 1 
ATOM   8722  N N   . ILE F  1 46  ? 17.403  29.494  -16.432 1.00 29.38  ? 38  ILE F N   1 
ATOM   8723  C CA  . ILE F  1 46  ? 17.451  28.164  -17.027 1.00 26.16  ? 38  ILE F CA  1 
ATOM   8724  C C   . ILE F  1 46  ? 18.895  27.835  -17.360 1.00 35.50  ? 38  ILE F C   1 
ATOM   8725  O O   . ILE F  1 46  ? 19.499  28.470  -18.226 1.00 49.91  ? 38  ILE F O   1 
ATOM   8726  C CB  . ILE F  1 46  ? 16.590  28.093  -18.306 1.00 30.37  ? 38  ILE F CB  1 
ATOM   8727  C CG1 . ILE F  1 46  ? 15.118  28.349  -17.969 1.00 28.93  ? 38  ILE F CG1 1 
ATOM   8728  C CG2 . ILE F  1 46  ? 16.764  26.746  -19.013 1.00 27.53  ? 38  ILE F CG2 1 
ATOM   8729  C CD1 . ILE F  1 46  ? 14.274  28.753  -19.147 1.00 27.71  ? 38  ILE F CD1 1 
ATOM   8730  N N   . LEU F  1 47  ? 19.430  26.768  -16.757 1.00 28.91  ? 39  LEU F N   1 
ATOM   8731  C CA  . LEU F  1 47  ? 20.806  26.311  -17.040 1.00 39.21  ? 39  LEU F CA  1 
ATOM   8732  C C   . LEU F  1 47  ? 20.978  24.788  -17.264 1.00 43.07  ? 39  LEU F C   1 
ATOM   8733  O O   . LEU F  1 47  ? 20.169  23.990  -16.791 1.00 46.13  ? 39  LEU F O   1 
ATOM   8734  C CB  . LEU F  1 47  ? 21.757  26.783  -15.936 1.00 47.95  ? 39  LEU F CB  1 
ATOM   8735  C CG  . LEU F  1 47  ? 22.982  27.579  -16.390 1.00 53.14  ? 39  LEU F CG  1 
ATOM   8736  C CD1 . LEU F  1 47  ? 23.451  27.111  -17.759 1.00 41.17  ? 39  LEU F CD1 1 
ATOM   8737  C CD2 . LEU F  1 47  ? 22.680  29.070  -16.403 1.00 40.63  ? 39  LEU F CD2 1 
ATOM   8738  N N   . GLU F  1 48  ? 22.037  24.404  -17.987 1.00 37.80  ? 40  GLU F N   1 
ATOM   8739  C CA  . GLU F  1 48  ? 22.365  22.994  -18.268 1.00 35.47  ? 40  GLU F CA  1 
ATOM   8740  C C   . GLU F  1 48  ? 21.366  22.170  -19.105 1.00 36.96  ? 40  GLU F C   1 
ATOM   8741  O O   . GLU F  1 48  ? 21.001  21.058  -18.720 1.00 47.05  ? 40  GLU F O   1 
ATOM   8742  C CB  . GLU F  1 48  ? 22.668  22.256  -16.959 1.00 43.30  ? 40  GLU F CB  1 
ATOM   8743  C CG  . GLU F  1 48  ? 24.148  22.179  -16.619 1.00 49.19  ? 40  GLU F CG  1 
ATOM   8744  C CD  . GLU F  1 48  ? 24.419  21.337  -15.388 1.00 64.27  ? 40  GLU F CD  1 
ATOM   8745  O OE1 . GLU F  1 48  ? 23.449  20.831  -14.786 1.00 56.98  ? 40  GLU F OE1 1 
ATOM   8746  O OE2 . GLU F  1 48  ? 25.603  21.181  -15.022 1.00 61.13  ? 40  GLU F OE2 1 
ATOM   8747  N N   . VAL F  1 49  ? 20.921  22.716  -20.234 1.00 43.10  ? 41  VAL F N   1 
ATOM   8748  C CA  . VAL F  1 49  ? 19.877  22.098  -21.038 1.00 40.18  ? 41  VAL F CA  1 
ATOM   8749  C C   . VAL F  1 49  ? 20.504  21.022  -21.928 1.00 35.88  ? 41  VAL F C   1 
ATOM   8750  O O   . VAL F  1 49  ? 21.643  21.166  -22.351 1.00 37.20  ? 41  VAL F O   1 
ATOM   8751  C CB  . VAL F  1 49  ? 19.153  23.168  -21.855 1.00 38.38  ? 41  VAL F CB  1 
ATOM   8752  C CG1 . VAL F  1 49  ? 18.492  22.572  -23.040 1.00 35.40  ? 41  VAL F CG1 1 
ATOM   8753  C CG2 . VAL F  1 49  ? 18.142  23.890  -20.987 1.00 35.97  ? 41  VAL F CG2 1 
ATOM   8754  N N   . ASN F  1 50  ? 19.785  19.935  -22.187 1.00 37.79  ? 42  ASN F N   1 
ATOM   8755  C CA  . ASN F  1 50  ? 20.363  18.792  -22.898 1.00 37.61  ? 42  ASN F CA  1 
ATOM   8756  C C   . ASN F  1 50  ? 19.370  18.180  -23.890 1.00 43.19  ? 42  ASN F C   1 
ATOM   8757  O O   . ASN F  1 50  ? 18.494  17.396  -23.495 1.00 35.80  ? 42  ASN F O   1 
ATOM   8758  C CB  . ASN F  1 50  ? 20.800  17.743  -21.871 1.00 37.73  ? 42  ASN F CB  1 
ATOM   8759  C CG  . ASN F  1 50  ? 21.732  16.697  -22.439 1.00 35.43  ? 42  ASN F CG  1 
ATOM   8760  O OD1 . ASN F  1 50  ? 21.546  16.205  -23.552 1.00 43.95  ? 42  ASN F OD1 1 
ATOM   8761  N ND2 . ASN F  1 50  ? 22.739  16.330  -21.654 1.00 28.75  ? 42  ASN F ND2 1 
ATOM   8762  N N   . GLU F  1 51  ? 19.506  18.527  -25.173 1.00 44.73  ? 43  GLU F N   1 
ATOM   8763  C CA  . GLU F  1 51  ? 18.544  18.069  -26.183 1.00 44.77  ? 43  GLU F CA  1 
ATOM   8764  C C   . GLU F  1 51  ? 18.707  16.581  -26.492 1.00 40.73  ? 43  GLU F C   1 
ATOM   8765  O O   . GLU F  1 51  ? 17.758  15.912  -26.930 1.00 33.49  ? 43  GLU F O   1 
ATOM   8766  C CB  . GLU F  1 51  ? 18.628  18.893  -27.474 1.00 50.17  ? 43  GLU F CB  1 
ATOM   8767  C CG  . GLU F  1 51  ? 17.411  18.700  -28.388 1.00 55.57  ? 43  GLU F CG  1 
ATOM   8768  C CD  . GLU F  1 51  ? 17.659  19.096  -29.842 1.00 54.21  ? 43  GLU F CD  1 
ATOM   8769  O OE1 . GLU F  1 51  ? 18.732  19.669  -30.141 1.00 51.96  ? 43  GLU F OE1 1 
ATOM   8770  O OE2 . GLU F  1 51  ? 16.770  18.825  -30.684 1.00 50.45  ? 43  GLU F OE2 1 
ATOM   8771  N N   . ILE F  1 52  ? 19.908  16.065  -26.251 1.00 37.40  ? 44  ILE F N   1 
ATOM   8772  C CA  . ILE F  1 52  ? 20.171  14.660  -26.518 1.00 40.38  ? 44  ILE F CA  1 
ATOM   8773  C C   . ILE F  1 52  ? 19.380  13.780  -25.560 1.00 38.18  ? 44  ILE F C   1 
ATOM   8774  O O   . ILE F  1 52  ? 18.692  12.853  -25.985 1.00 40.27  ? 44  ILE F O   1 
ATOM   8775  C CB  . ILE F  1 52  ? 21.677  14.305  -26.431 1.00 48.22  ? 44  ILE F CB  1 
ATOM   8776  C CG1 . ILE F  1 52  ? 22.534  15.307  -27.221 1.00 49.77  ? 44  ILE F CG1 1 
ATOM   8777  C CG2 . ILE F  1 52  ? 21.906  12.887  -26.938 1.00 40.82  ? 44  ILE F CG2 1 
ATOM   8778  C CD1 . ILE F  1 52  ? 23.355  16.271  -26.358 1.00 48.36  ? 44  ILE F CD1 1 
ATOM   8779  N N   . THR F  1 53  ? 19.465  14.091  -24.269 1.00 43.45  ? 45  THR F N   1 
ATOM   8780  C CA  . THR F  1 53  ? 18.842  13.267  -23.226 1.00 47.11  ? 45  THR F CA  1 
ATOM   8781  C C   . THR F  1 53  ? 17.498  13.815  -22.714 1.00 39.78  ? 45  THR F C   1 
ATOM   8782  O O   . THR F  1 53  ? 16.829  13.171  -21.897 1.00 34.62  ? 45  THR F O   1 
ATOM   8783  C CB  . THR F  1 53  ? 19.794  13.059  -22.024 1.00 37.08  ? 45  THR F CB  1 
ATOM   8784  O OG1 . THR F  1 53  ? 19.359  11.928  -21.263 1.00 38.42  ? 45  THR F OG1 1 
ATOM   8785  C CG2 . THR F  1 53  ? 19.809  14.284  -21.142 1.00 29.27  ? 45  THR F CG2 1 
ATOM   8786  N N   . ASN F  1 54  ? 17.114  14.991  -23.207 1.00 36.91  ? 46  ASN F N   1 
ATOM   8787  C CA  . ASN F  1 54  ? 15.863  15.634  -22.814 1.00 40.14  ? 46  ASN F CA  1 
ATOM   8788  C C   . ASN F  1 54  ? 15.743  15.830  -21.306 1.00 34.66  ? 46  ASN F C   1 
ATOM   8789  O O   . ASN F  1 54  ? 14.879  15.249  -20.649 1.00 36.94  ? 46  ASN F O   1 
ATOM   8790  C CB  . ASN F  1 54  ? 14.654  14.890  -23.391 1.00 43.24  ? 46  ASN F CB  1 
ATOM   8791  C CG  . ASN F  1 54  ? 14.195  15.473  -24.727 1.00 45.23  ? 46  ASN F CG  1 
ATOM   8792  O OD1 . ASN F  1 54  ? 14.200  16.692  -24.927 1.00 38.91  ? 46  ASN F OD1 1 
ATOM   8793  N ND2 . ASN F  1 54  ? 13.798  14.600  -25.643 1.00 43.60  ? 46  ASN F ND2 1 
ATOM   8794  N N   . GLU F  1 55  ? 16.647  16.648  -20.780 1.00 32.38  ? 47  GLU F N   1 
ATOM   8795  C CA  . GLU F  1 55  ? 16.704  16.993  -19.374 1.00 31.21  ? 47  GLU F CA  1 
ATOM   8796  C C   . GLU F  1 55  ? 17.024  18.480  -19.263 1.00 34.98  ? 47  GLU F C   1 
ATOM   8797  O O   . GLU F  1 55  ? 17.842  19.008  -20.015 1.00 38.43  ? 47  GLU F O   1 
ATOM   8798  C CB  . GLU F  1 55  ? 17.770  16.162  -18.645 1.00 23.72  ? 47  GLU F CB  1 
ATOM   8799  C CG  . GLU F  1 55  ? 17.418  14.689  -18.481 1.00 27.86  ? 47  GLU F CG  1 
ATOM   8800  C CD  . GLU F  1 55  ? 18.561  13.862  -17.899 1.00 36.38  ? 47  GLU F CD  1 
ATOM   8801  O OE1 . GLU F  1 55  ? 19.494  14.458  -17.312 1.00 37.52  ? 47  GLU F OE1 1 
ATOM   8802  O OE2 . GLU F  1 55  ? 18.525  12.613  -18.036 1.00 32.62  ? 47  GLU F OE2 1 
ATOM   8803  N N   . VAL F  1 56  ? 16.360  19.150  -18.331 1.00 31.91  ? 48  VAL F N   1 
ATOM   8804  C CA  . VAL F  1 56  ? 16.576  20.560  -18.081 1.00 31.40  ? 48  VAL F CA  1 
ATOM   8805  C C   . VAL F  1 56  ? 16.921  20.722  -16.599 1.00 38.66  ? 48  VAL F C   1 
ATOM   8806  O O   . VAL F  1 56  ? 16.790  19.782  -15.818 1.00 36.04  ? 48  VAL F O   1 
ATOM   8807  C CB  . VAL F  1 56  ? 15.310  21.374  -18.419 1.00 36.80  ? 48  VAL F CB  1 
ATOM   8808  C CG1 . VAL F  1 56  ? 14.277  21.209  -17.325 1.00 35.44  ? 48  VAL F CG1 1 
ATOM   8809  C CG2 . VAL F  1 56  ? 15.640  22.851  -18.609 1.00 36.20  ? 48  VAL F CG2 1 
ATOM   8810  N N   . ASP F  1 57  ? 17.359  21.915  -16.217 1.00 39.08  ? 49  ASP F N   1 
ATOM   8811  C CA  . ASP F  1 57  ? 17.833  22.180  -14.872 1.00 30.35  ? 49  ASP F CA  1 
ATOM   8812  C C   . ASP F  1 57  ? 17.451  23.626  -14.629 1.00 30.07  ? 49  ASP F C   1 
ATOM   8813  O O   . ASP F  1 57  ? 18.182  24.528  -15.004 1.00 38.96  ? 49  ASP F O   1 
ATOM   8814  C CB  . ASP F  1 57  ? 19.356  21.978  -14.842 1.00 36.96  ? 49  ASP F CB  1 
ATOM   8815  C CG  . ASP F  1 57  ? 19.964  22.098  -13.443 1.00 40.37  ? 49  ASP F CG  1 
ATOM   8816  O OD1 . ASP F  1 57  ? 19.726  23.120  -12.773 1.00 36.80  ? 49  ASP F OD1 1 
ATOM   8817  O OD2 . ASP F  1 57  ? 20.719  21.184  -13.026 1.00 40.58  ? 49  ASP F OD2 1 
ATOM   8818  N N   . VAL F  1 58  ? 16.284  23.854  -14.038 1.00 28.60  ? 50  VAL F N   1 
ATOM   8819  C CA  . VAL F  1 58  ? 15.772  25.214  -13.870 1.00 27.89  ? 50  VAL F CA  1 
ATOM   8820  C C   . VAL F  1 58  ? 15.854  25.746  -12.428 1.00 25.15  ? 50  VAL F C   1 
ATOM   8821  O O   . VAL F  1 58  ? 16.126  25.001  -11.489 1.00 22.85  ? 50  VAL F O   1 
ATOM   8822  C CB  . VAL F  1 58  ? 14.306  25.327  -14.354 1.00 27.06  ? 50  VAL F CB  1 
ATOM   8823  C CG1 . VAL F  1 58  ? 14.183  24.824  -15.769 1.00 35.20  ? 50  VAL F CG1 1 
ATOM   8824  C CG2 . VAL F  1 58  ? 13.403  24.530  -13.458 1.00 27.98  ? 50  VAL F CG2 1 
ATOM   8825  N N   . VAL F  1 59  ? 15.624  27.050  -12.293 1.00 19.08  ? 51  VAL F N   1 
ATOM   8826  C CA  . VAL F  1 59  ? 15.617  27.753  -11.032 1.00 16.34  ? 51  VAL F CA  1 
ATOM   8827  C C   . VAL F  1 59  ? 14.388  28.634  -11.034 1.00 21.64  ? 51  VAL F C   1 
ATOM   8828  O O   . VAL F  1 59  ? 14.282  29.542  -11.852 1.00 18.59  ? 51  VAL F O   1 
ATOM   8829  C CB  . VAL F  1 59  ? 16.850  28.638  -10.859 1.00 16.85  ? 51  VAL F CB  1 
ATOM   8830  C CG1 . VAL F  1 59  ? 16.640  29.637  -9.727  1.00 16.63  ? 51  VAL F CG1 1 
ATOM   8831  C CG2 . VAL F  1 59  ? 18.073  27.791  -10.597 1.00 17.92  ? 51  VAL F CG2 1 
ATOM   8832  N N   . PHE F  1 60  ? 13.459  28.363  -10.113 1.00 28.28  ? 52  PHE F N   1 
ATOM   8833  C CA  . PHE F  1 60  ? 12.170  29.070  -10.065 1.00 26.70  ? 52  PHE F CA  1 
ATOM   8834  C C   . PHE F  1 60  ? 11.677  29.412  -8.651  1.00 28.18  ? 52  PHE F C   1 
ATOM   8835  O O   . PHE F  1 60  ? 11.977  28.710  -7.682  1.00 26.60  ? 52  PHE F O   1 
ATOM   8836  C CB  . PHE F  1 60  ? 11.100  28.259  -10.787 1.00 19.00  ? 52  PHE F CB  1 
ATOM   8837  C CG  . PHE F  1 60  ? 10.919  26.882  -10.240 1.00 18.58  ? 52  PHE F CG  1 
ATOM   8838  C CD1 . PHE F  1 60  ? 9.856   26.591  -9.396  1.00 25.96  ? 52  PHE F CD1 1 
ATOM   8839  C CD2 . PHE F  1 60  ? 11.800  25.872  -10.567 1.00 18.99  ? 52  PHE F CD2 1 
ATOM   8840  C CE1 . PHE F  1 60  ? 9.675   25.313  -8.896  1.00 22.84  ? 52  PHE F CE1 1 
ATOM   8841  C CE2 . PHE F  1 60  ? 11.634  24.590  -10.067 1.00 25.20  ? 52  PHE F CE2 1 
ATOM   8842  C CZ  . PHE F  1 60  ? 10.572  24.307  -9.229  1.00 21.44  ? 52  PHE F CZ  1 
ATOM   8843  N N   . TRP F  1 61  ? 10.924  30.502  -8.542  1.00 27.40  ? 53  TRP F N   1 
ATOM   8844  C CA  . TRP F  1 61  ? 10.227  30.816  -7.305  1.00 23.81  ? 53  TRP F CA  1 
ATOM   8845  C C   . TRP F  1 61  ? 8.854   30.175  -7.332  1.00 25.75  ? 53  TRP F C   1 
ATOM   8846  O O   . TRP F  1 61  ? 8.028   30.496  -8.184  1.00 24.91  ? 53  TRP F O   1 
ATOM   8847  C CB  . TRP F  1 61  ? 10.099  32.321  -7.114  1.00 24.47  ? 53  TRP F CB  1 
ATOM   8848  C CG  . TRP F  1 61  ? 11.428  32.986  -6.932  1.00 29.20  ? 53  TRP F CG  1 
ATOM   8849  C CD1 . TRP F  1 61  ? 12.646  32.370  -6.831  1.00 28.23  ? 53  TRP F CD1 1 
ATOM   8850  C CD2 . TRP F  1 61  ? 11.679  34.396  -6.826  1.00 30.73  ? 53  TRP F CD2 1 
ATOM   8851  N NE1 . TRP F  1 61  ? 13.639  33.310  -6.671  1.00 34.87  ? 53  TRP F NE1 1 
ATOM   8852  C CE2 . TRP F  1 61  ? 13.074  34.560  -6.670  1.00 30.96  ? 53  TRP F CE2 1 
ATOM   8853  C CE3 . TRP F  1 61  ? 10.861  35.534  -6.855  1.00 34.41  ? 53  TRP F CE3 1 
ATOM   8854  C CZ2 . TRP F  1 61  ? 13.670  35.814  -6.547  1.00 28.58  ? 53  TRP F CZ2 1 
ATOM   8855  C CZ3 . TRP F  1 61  ? 11.452  36.779  -6.724  1.00 38.22  ? 53  TRP F CZ3 1 
ATOM   8856  C CH2 . TRP F  1 61  ? 12.846  36.908  -6.573  1.00 36.67  ? 53  TRP F CH2 1 
ATOM   8857  N N   . GLN F  1 62  ? 8.626   29.250  -6.404  1.00 24.97  ? 54  GLN F N   1 
ATOM   8858  C CA  . GLN F  1 62  ? 7.338   28.586  -6.286  1.00 24.73  ? 54  GLN F CA  1 
ATOM   8859  C C   . GLN F  1 62  ? 6.438   29.385  -5.350  1.00 24.63  ? 54  GLN F C   1 
ATOM   8860  O O   . GLN F  1 62  ? 6.600   29.348  -4.137  1.00 21.23  ? 54  GLN F O   1 
ATOM   8861  C CB  . GLN F  1 62  ? 7.532   27.170  -5.759  1.00 23.69  ? 54  GLN F CB  1 
ATOM   8862  C CG  . GLN F  1 62  ? 6.403   26.231  -6.100  1.00 26.07  ? 54  GLN F CG  1 
ATOM   8863  C CD  . GLN F  1 62  ? 6.368   25.029  -5.189  1.00 29.29  ? 54  GLN F CD  1 
ATOM   8864  O OE1 . GLN F  1 62  ? 6.936   23.979  -5.497  1.00 29.29  ? 54  GLN F OE1 1 
ATOM   8865  N NE2 . GLN F  1 62  ? 5.705   25.178  -4.048  1.00 26.82  ? 54  GLN F NE2 1 
ATOM   8866  N N   . GLN F  1 63  ? 5.504   30.141  -5.913  1.00 30.95  ? 55  GLN F N   1 
ATOM   8867  C CA  . GLN F  1 63  ? 4.580   30.893  -5.080  1.00 28.73  ? 55  GLN F CA  1 
ATOM   8868  C C   . GLN F  1 63  ? 3.405   29.998  -4.715  1.00 28.10  ? 55  GLN F C   1 
ATOM   8869  O O   . GLN F  1 63  ? 2.682   29.521  -5.594  1.00 29.09  ? 55  GLN F O   1 
ATOM   8870  C CB  . GLN F  1 63  ? 4.108   32.159  -5.783  1.00 29.49  ? 55  GLN F CB  1 
ATOM   8871  C CG  . GLN F  1 63  ? 3.864   33.320  -4.828  1.00 42.75  ? 55  GLN F CG  1 
ATOM   8872  C CD  . GLN F  1 63  ? 3.354   34.558  -5.537  1.00 50.82  ? 55  GLN F CD  1 
ATOM   8873  O OE1 . GLN F  1 63  ? 4.063   35.162  -6.357  1.00 50.61  ? 55  GLN F OE1 1 
ATOM   8874  N NE2 . GLN F  1 63  ? 2.112   34.942  -5.232  1.00 45.35  ? 55  GLN F NE2 1 
ATOM   8875  N N   . THR F  1 64  ? 3.246   29.757  -3.414  1.00 22.91  ? 56  THR F N   1 
ATOM   8876  C CA  . THR F  1 64  ? 2.222   28.860  -2.888  1.00 20.32  ? 56  THR F CA  1 
ATOM   8877  C C   . THR F  1 64  ? 1.452   29.571  -1.786  1.00 23.29  ? 56  THR F C   1 
ATOM   8878  O O   . THR F  1 64  ? 2.035   30.038  -0.801  1.00 22.16  ? 56  THR F O   1 
ATOM   8879  C CB  . THR F  1 64  ? 2.852   27.595  -2.314  1.00 15.76  ? 56  THR F CB  1 
ATOM   8880  O OG1 . THR F  1 64  ? 4.021   27.281  -3.068  1.00 28.50  ? 56  THR F OG1 1 
ATOM   8881  C CG2 . THR F  1 64  ? 1.910   26.434  -2.405  1.00 16.92  ? 56  THR F CG2 1 
ATOM   8882  N N   . THR F  1 65  ? 0.145   29.694  -1.964  1.00 19.68  ? 57  THR F N   1 
ATOM   8883  C CA  . THR F  1 65  ? -0.674  30.277  -0.928  1.00 17.57  ? 57  THR F CA  1 
ATOM   8884  C C   . THR F  1 65  ? -1.926  29.449  -0.726  1.00 22.81  ? 57  THR F C   1 
ATOM   8885  O O   . THR F  1 65  ? -2.402  28.786  -1.646  1.00 21.50  ? 57  THR F O   1 
ATOM   8886  C CB  . THR F  1 65  ? -1.063  31.727  -1.222  1.00 20.54  ? 57  THR F CB  1 
ATOM   8887  O OG1 . THR F  1 65  ? -1.976  31.761  -2.323  1.00 33.94  ? 57  THR F OG1 1 
ATOM   8888  C CG2 . THR F  1 65  ? 0.164   32.555  -1.547  1.00 22.64  ? 57  THR F CG2 1 
ATOM   8889  N N   . TRP F  1 66  ? -2.429  29.481  0.505   1.00 21.29  ? 58  TRP F N   1 
ATOM   8890  C CA  . TRP F  1 66  ? -3.643  28.793  0.891   1.00 18.26  ? 58  TRP F CA  1 
ATOM   8891  C C   . TRP F  1 66  ? -4.095  29.510  2.133   1.00 20.26  ? 58  TRP F C   1 
ATOM   8892  O O   . TRP F  1 66  ? -3.370  30.354  2.659   1.00 20.03  ? 58  TRP F O   1 
ATOM   8893  C CB  . TRP F  1 66  ? -3.352  27.332  1.215   1.00 19.73  ? 58  TRP F CB  1 
ATOM   8894  C CG  . TRP F  1 66  ? -2.362  27.150  2.351   1.00 25.05  ? 58  TRP F CG  1 
ATOM   8895  C CD1 . TRP F  1 66  ? -2.646  27.072  3.690   1.00 20.78  ? 58  TRP F CD1 1 
ATOM   8896  C CD2 . TRP F  1 66  ? -0.934  27.021  2.240   1.00 24.37  ? 58  TRP F CD2 1 
ATOM   8897  N NE1 . TRP F  1 66  ? -1.488  26.907  4.415   1.00 17.82  ? 58  TRP F NE1 1 
ATOM   8898  C CE2 . TRP F  1 66  ? -0.425  26.868  3.553   1.00 20.73  ? 58  TRP F CE2 1 
ATOM   8899  C CE3 . TRP F  1 66  ? -0.038  27.019  1.162   1.00 18.42  ? 58  TRP F CE3 1 
ATOM   8900  C CZ2 . TRP F  1 66  ? 0.937   26.713  3.810   1.00 17.85  ? 58  TRP F CZ2 1 
ATOM   8901  C CZ3 . TRP F  1 66  ? 1.306   26.868  1.420   1.00 16.18  ? 58  TRP F CZ3 1 
ATOM   8902  C CH2 . TRP F  1 66  ? 1.785   26.717  2.732   1.00 18.30  ? 58  TRP F CH2 1 
ATOM   8903  N N   . SER F  1 67  ? -5.283  29.182  2.621   1.00 23.46  ? 59  SER F N   1 
ATOM   8904  C CA  . SER F  1 67  ? -5.726  29.765  3.881   1.00 25.31  ? 59  SER F CA  1 
ATOM   8905  C C   . SER F  1 67  ? -5.969  28.680  4.924   1.00 21.50  ? 59  SER F C   1 
ATOM   8906  O O   . SER F  1 67  ? -6.340  27.560  4.579   1.00 22.06  ? 59  SER F O   1 
ATOM   8907  C CB  . SER F  1 67  ? -7.000  30.576  3.679   1.00 20.11  ? 59  SER F CB  1 
ATOM   8908  O OG  . SER F  1 67  ? -8.102  29.697  3.577   1.00 21.32  ? 59  SER F OG  1 
ATOM   8909  N N   . ASP F  1 68  ? -5.741  29.028  6.190   1.00 19.98  ? 60  ASP F N   1 
ATOM   8910  C CA  . ASP F  1 68  ? -6.180  28.237  7.351   1.00 22.37  ? 60  ASP F CA  1 
ATOM   8911  C C   . ASP F  1 68  ? -6.819  29.217  8.347   1.00 20.28  ? 60  ASP F C   1 
ATOM   8912  O O   . ASP F  1 68  ? -6.121  29.891  9.099   1.00 19.18  ? 60  ASP F O   1 
ATOM   8913  C CB  . ASP F  1 68  ? -4.983  27.516  7.990   1.00 21.55  ? 60  ASP F CB  1 
ATOM   8914  C CG  . ASP F  1 68  ? -5.367  26.629  9.187   1.00 24.48  ? 60  ASP F CG  1 
ATOM   8915  O OD1 . ASP F  1 68  ? -6.482  26.777  9.747   1.00 25.36  ? 60  ASP F OD1 1 
ATOM   8916  O OD2 . ASP F  1 68  ? -4.527  25.775  9.574   1.00 21.17  ? 60  ASP F OD2 1 
ATOM   8917  N N   . ARG F  1 69  ? -8.142  29.305  8.346   1.00 23.78  ? 61  ARG F N   1 
ATOM   8918  C CA  . ARG F  1 69  ? -8.827  30.317  9.150   1.00 23.16  ? 61  ARG F CA  1 
ATOM   8919  C C   . ARG F  1 69  ? -8.590  30.207  10.660  1.00 19.48  ? 61  ARG F C   1 
ATOM   8920  O O   . ARG F  1 69  ? -8.652  31.214  11.371  1.00 14.70  ? 61  ARG F O   1 
ATOM   8921  C CB  . ARG F  1 69  ? -10.327 30.343  8.847   1.00 24.80  ? 61  ARG F CB  1 
ATOM   8922  C CG  . ARG F  1 69  ? -10.735 31.340  7.770   1.00 36.19  ? 61  ARG F CG  1 
ATOM   8923  C CD  . ARG F  1 69  ? -10.463 32.785  8.189   1.00 37.51  ? 61  ARG F CD  1 
ATOM   8924  N NE  . ARG F  1 69  ? -11.088 33.742  7.275   1.00 47.16  ? 61  ARG F NE  1 
ATOM   8925  C CZ  . ARG F  1 69  ? -10.952 35.065  7.347   1.00 45.23  ? 61  ARG F CZ  1 
ATOM   8926  N NH1 . ARG F  1 69  ? -10.196 35.615  8.290   1.00 40.99  ? 61  ARG F NH1 1 
ATOM   8927  N NH2 . ARG F  1 69  ? -11.571 35.844  6.464   1.00 51.44  ? 61  ARG F NH2 1 
ATOM   8928  N N   . THR F  1 70  ? -8.294  29.003  11.149  1.00 18.91  ? 62  THR F N   1 
ATOM   8929  C CA  . THR F  1 70  ? -8.099  28.818  12.589  1.00 19.27  ? 62  THR F CA  1 
ATOM   8930  C C   . THR F  1 70  ? -6.889  29.605  13.100  1.00 20.02  ? 62  THR F C   1 
ATOM   8931  O O   . THR F  1 70  ? -6.748  29.808  14.316  1.00 22.77  ? 62  THR F O   1 
ATOM   8932  C CB  . THR F  1 70  ? -7.951  27.325  13.005  1.00 19.40  ? 62  THR F CB  1 
ATOM   8933  O OG1 . THR F  1 70  ? -6.713  26.806  12.519  1.00 20.26  ? 62  THR F OG1 1 
ATOM   8934  C CG2 . THR F  1 70  ? -9.101  26.472  12.488  1.00 11.97  ? 62  THR F CG2 1 
ATOM   8935  N N   . LEU F  1 71  ? -6.039  30.048  12.167  1.00 15.19  ? 63  LEU F N   1 
ATOM   8936  C CA  . LEU F  1 71  ? -4.817  30.793  12.471  1.00 14.87  ? 63  LEU F CA  1 
ATOM   8937  C C   . LEU F  1 71  ? -5.016  32.302  12.528  1.00 18.43  ? 63  LEU F C   1 
ATOM   8938  O O   . LEU F  1 71  ? -4.102  33.044  12.894  1.00 21.91  ? 63  LEU F O   1 
ATOM   8939  C CB  . LEU F  1 71  ? -3.752  30.512  11.417  1.00 18.53  ? 63  LEU F CB  1 
ATOM   8940  C CG  . LEU F  1 71  ? -3.108  29.131  11.344  1.00 19.33  ? 63  LEU F CG  1 
ATOM   8941  C CD1 . LEU F  1 71  ? -2.060  29.122  10.253  1.00 10.58  ? 63  LEU F CD1 1 
ATOM   8942  C CD2 . LEU F  1 71  ? -2.515  28.743  12.696  1.00 14.88  ? 63  LEU F CD2 1 
ATOM   8943  N N   . ALA F  1 72  ? -6.200  32.765  12.157  1.00 16.51  ? 64  ALA F N   1 
ATOM   8944  C CA  . ALA F  1 72  ? -6.445  34.197  12.097  1.00 17.97  ? 64  ALA F CA  1 
ATOM   8945  C C   . ALA F  1 72  ? -6.560  34.848  13.484  1.00 19.29  ? 64  ALA F C   1 
ATOM   8946  O O   . ALA F  1 72  ? -6.905  34.198  14.475  1.00 13.94  ? 64  ALA F O   1 
ATOM   8947  C CB  . ALA F  1 72  ? -7.686  34.486  11.249  1.00 17.87  ? 64  ALA F CB  1 
ATOM   8948  N N   . TRP F  1 73  ? -6.258  36.141  13.533  1.00 19.50  ? 65  TRP F N   1 
ATOM   8949  C CA  . TRP F  1 73  ? -6.386  36.910  14.755  1.00 18.85  ? 65  TRP F CA  1 
ATOM   8950  C C   . TRP F  1 73  ? -6.831  38.333  14.455  1.00 21.56  ? 65  TRP F C   1 
ATOM   8951  O O   . TRP F  1 73  ? -6.951  38.729  13.311  1.00 23.59  ? 65  TRP F O   1 
ATOM   8952  C CB  . TRP F  1 73  ? -5.074  36.923  15.535  1.00 21.57  ? 65  TRP F CB  1 
ATOM   8953  C CG  . TRP F  1 73  ? -3.988  37.705  14.887  1.00 18.26  ? 65  TRP F CG  1 
ATOM   8954  C CD1 . TRP F  1 73  ? -3.661  39.001  15.134  1.00 22.17  ? 65  TRP F CD1 1 
ATOM   8955  C CD2 . TRP F  1 73  ? -3.074  37.243  13.888  1.00 18.83  ? 65  TRP F CD2 1 
ATOM   8956  N NE1 . TRP F  1 73  ? -2.600  39.382  14.349  1.00 18.98  ? 65  TRP F NE1 1 
ATOM   8957  C CE2 . TRP F  1 73  ? -2.221  38.322  13.572  1.00 17.45  ? 65  TRP F CE2 1 
ATOM   8958  C CE3 . TRP F  1 73  ? -2.893  36.022  13.228  1.00 17.30  ? 65  TRP F CE3 1 
ATOM   8959  C CZ2 . TRP F  1 73  ? -1.211  38.224  12.626  1.00 15.13  ? 65  TRP F CZ2 1 
ATOM   8960  C CZ3 . TRP F  1 73  ? -1.881  35.922  12.295  1.00 19.51  ? 65  TRP F CZ3 1 
ATOM   8961  C CH2 . TRP F  1 73  ? -1.056  37.021  11.996  1.00 18.11  ? 65  TRP F CH2 1 
ATOM   8962  N N   . ASN F  1 74  ? -6.968  39.152  15.494  1.00 29.02  ? 66  ASN F N   1 
ATOM   8963  C CA  . ASN F  1 74  ? -7.251  40.571  15.284  1.00 27.99  ? 66  ASN F CA  1 
ATOM   8964  C C   . ASN F  1 74  ? -5.955  41.384  15.218  1.00 29.64  ? 66  ASN F C   1 
ATOM   8965  O O   . ASN F  1 74  ? -5.179  41.414  16.174  1.00 27.52  ? 66  ASN F O   1 
ATOM   8966  C CB  . ASN F  1 74  ? -8.158  41.109  16.390  1.00 32.02  ? 66  ASN F CB  1 
ATOM   8967  C CG  . ASN F  1 74  ? -9.033  42.255  15.921  1.00 38.18  ? 66  ASN F CG  1 
ATOM   8968  O OD1 . ASN F  1 74  ? -8.591  43.118  15.163  1.00 35.07  ? 66  ASN F OD1 1 
ATOM   8969  N ND2 . ASN F  1 74  ? -10.283 42.268  16.369  1.00 50.90  ? 66  ASN F ND2 1 
ATOM   8970  N N   . SER F  1 75  ? -5.727  42.031  14.077  1.00 30.82  ? 67  SER F N   1 
ATOM   8971  C CA  . SER F  1 75  ? -4.469  42.733  13.807  1.00 30.88  ? 67  SER F CA  1 
ATOM   8972  C C   . SER F  1 75  ? -4.519  44.266  13.843  1.00 29.90  ? 67  SER F C   1 
ATOM   8973  O O   . SER F  1 75  ? -3.560  44.923  13.439  1.00 40.67  ? 67  SER F O   1 
ATOM   8974  C CB  . SER F  1 75  ? -3.885  42.270  12.469  1.00 28.32  ? 67  SER F CB  1 
ATOM   8975  O OG  . SER F  1 75  ? -4.865  42.304  11.446  1.00 36.04  ? 67  SER F OG  1 
ATOM   8976  N N   . SER F  1 76  ? -5.623  44.835  14.315  1.00 34.09  ? 68  SER F N   1 
ATOM   8977  C CA  . SER F  1 76  ? -5.818  46.285  14.250  1.00 34.88  ? 68  SER F CA  1 
ATOM   8978  C C   . SER F  1 76  ? -4.778  47.076  15.046  1.00 40.88  ? 68  SER F C   1 
ATOM   8979  O O   . SER F  1 76  ? -4.296  48.116  14.596  1.00 47.19  ? 68  SER F O   1 
ATOM   8980  C CB  . SER F  1 76  ? -7.227  46.654  14.722  1.00 34.40  ? 68  SER F CB  1 
ATOM   8981  O OG  . SER F  1 76  ? -8.138  45.595  14.485  1.00 31.24  ? 68  SER F OG  1 
ATOM   8982  N N   . HIS F  1 77  ? -4.441  46.574  16.227  1.00 35.77  ? 69  HIS F N   1 
ATOM   8983  C CA  . HIS F  1 77  ? -3.477  47.215  17.118  1.00 40.01  ? 69  HIS F CA  1 
ATOM   8984  C C   . HIS F  1 77  ? -2.185  46.405  17.158  1.00 42.94  ? 69  HIS F C   1 
ATOM   8985  O O   . HIS F  1 77  ? -1.242  46.738  17.876  1.00 51.18  ? 69  HIS F O   1 
ATOM   8986  C CB  . HIS F  1 77  ? -4.057  47.356  18.527  1.00 44.73  ? 69  HIS F CB  1 
ATOM   8987  C CG  . HIS F  1 77  ? -4.937  48.553  18.701  1.00 46.32  ? 69  HIS F CG  1 
ATOM   8988  N ND1 . HIS F  1 77  ? -6.307  48.498  18.555  1.00 43.88  ? 69  HIS F ND1 1 
ATOM   8989  C CD2 . HIS F  1 77  ? -4.644  49.839  19.009  1.00 47.68  ? 69  HIS F CD2 1 
ATOM   8990  C CE1 . HIS F  1 77  ? -6.819  49.697  18.765  1.00 43.43  ? 69  HIS F CE1 1 
ATOM   8991  N NE2 . HIS F  1 77  ? -5.831  50.529  19.043  1.00 47.37  ? 69  HIS F NE2 1 
ATOM   8992  N N   . SER F  1 78  ? -2.170  45.328  16.382  1.00 37.72  ? 70  SER F N   1 
ATOM   8993  C CA  . SER F  1 78  ? -1.129  44.315  16.425  1.00 38.33  ? 70  SER F CA  1 
ATOM   8994  C C   . SER F  1 78  ? -0.723  43.972  14.992  1.00 36.31  ? 70  SER F C   1 
ATOM   8995  O O   . SER F  1 78  ? -1.494  44.185  14.070  1.00 36.69  ? 70  SER F O   1 
ATOM   8996  C CB  . SER F  1 78  ? -1.639  43.066  17.161  1.00 40.75  ? 70  SER F CB  1 
ATOM   8997  O OG  . SER F  1 78  ? -2.495  42.290  16.340  1.00 38.78  ? 70  SER F OG  1 
ATOM   8998  N N   . PRO F  1 79  ? 0.495   43.447  14.807  1.00 33.66  ? 71  PRO F N   1 
ATOM   8999  C CA  . PRO F  1 79  ? 1.062   43.088  13.507  1.00 32.05  ? 71  PRO F CA  1 
ATOM   9000  C C   . PRO F  1 79  ? 0.116   42.374  12.549  1.00 29.49  ? 71  PRO F C   1 
ATOM   9001  O O   . PRO F  1 79  ? -0.622  41.484  12.937  1.00 29.02  ? 71  PRO F O   1 
ATOM   9002  C CB  . PRO F  1 79  ? 2.199   42.158  13.893  1.00 29.09  ? 71  PRO F CB  1 
ATOM   9003  C CG  . PRO F  1 79  ? 2.688   42.745  15.159  1.00 36.85  ? 71  PRO F CG  1 
ATOM   9004  C CD  . PRO F  1 79  ? 1.468   43.223  15.890  1.00 36.89  ? 71  PRO F CD  1 
ATOM   9005  N N   . ASP F  1 80  ? 0.179   42.776  11.287  1.00 31.43  ? 72  ASP F N   1 
ATOM   9006  C CA  . ASP F  1 80  ? -0.676  42.274  10.226  1.00 29.68  ? 72  ASP F CA  1 
ATOM   9007  C C   . ASP F  1 80  ? -0.216  40.902  9.748   1.00 25.86  ? 72  ASP F C   1 
ATOM   9008  O O   . ASP F  1 80  ? -0.983  40.133  9.148   1.00 22.20  ? 72  ASP F O   1 
ATOM   9009  C CB  . ASP F  1 80  ? -0.569  43.242  9.049   1.00 33.71  ? 72  ASP F CB  1 
ATOM   9010  C CG  . ASP F  1 80  ? -1.909  43.681  8.527   1.00 45.82  ? 72  ASP F CG  1 
ATOM   9011  O OD1 . ASP F  1 80  ? -2.809  42.819  8.405   1.00 54.65  ? 72  ASP F OD1 1 
ATOM   9012  O OD2 . ASP F  1 80  ? -2.060  44.888  8.230   1.00 55.07  ? 72  ASP F OD2 1 
ATOM   9013  N N   . GLN F  1 81  ? 1.053   40.613  10.007  1.00 23.15  ? 73  GLN F N   1 
ATOM   9014  C CA  . GLN F  1 81  ? 1.740   39.506  9.374   1.00 17.69  ? 73  GLN F CA  1 
ATOM   9015  C C   . GLN F  1 81  ? 3.022   39.194  10.118  1.00 18.39  ? 73  GLN F C   1 
ATOM   9016  O O   . GLN F  1 81  ? 3.645   40.078  10.707  1.00 20.32  ? 73  GLN F O   1 
ATOM   9017  C CB  . GLN F  1 81  ? 2.087   39.880  7.939   1.00 19.94  ? 73  GLN F CB  1 
ATOM   9018  C CG  . GLN F  1 81  ? 1.040   39.479  6.932   1.00 30.02  ? 73  GLN F CG  1 
ATOM   9019  C CD  . GLN F  1 81  ? 1.211   40.167  5.582   1.00 33.03  ? 73  GLN F CD  1 
ATOM   9020  O OE1 . GLN F  1 81  ? 0.316   40.899  5.124   1.00 26.75  ? 73  GLN F OE1 1 
ATOM   9021  N NE2 . GLN F  1 81  ? 2.349   39.922  4.931   1.00 28.35  ? 73  GLN F NE2 1 
ATOM   9022  N N   . VAL F  1 82  ? 3.419   37.930  10.088  1.00 14.84  ? 74  VAL F N   1 
ATOM   9023  C CA  . VAL F  1 82  ? 4.647   37.517  10.730  1.00 15.69  ? 74  VAL F CA  1 
ATOM   9024  C C   . VAL F  1 82  ? 5.271   36.424  9.895   1.00 14.67  ? 74  VAL F C   1 
ATOM   9025  O O   . VAL F  1 82  ? 4.604   35.797  9.075   1.00 13.31  ? 74  VAL F O   1 
ATOM   9026  C CB  . VAL F  1 82  ? 4.410   36.955  12.175  1.00 17.10  ? 74  VAL F CB  1 
ATOM   9027  C CG1 . VAL F  1 82  ? 3.968   38.039  13.124  1.00 13.34  ? 74  VAL F CG1 1 
ATOM   9028  C CG2 . VAL F  1 82  ? 3.407   35.812  12.157  1.00 14.46  ? 74  VAL F CG2 1 
ATOM   9029  N N   . SER F  1 83  ? 6.555   36.189  10.121  1.00 15.37  ? 75  SER F N   1 
ATOM   9030  C CA  . SER F  1 83  ? 7.221   35.045  9.528   1.00 17.26  ? 75  SER F CA  1 
ATOM   9031  C C   . SER F  1 83  ? 7.245   33.893  10.514  1.00 15.16  ? 75  SER F C   1 
ATOM   9032  O O   . SER F  1 83  ? 7.559   34.070  11.681  1.00 16.15  ? 75  SER F O   1 
ATOM   9033  C CB  . SER F  1 83  ? 8.645   35.400  9.104   1.00 15.07  ? 75  SER F CB  1 
ATOM   9034  O OG  . SER F  1 83  ? 8.618   36.383  8.086   1.00 20.43  ? 75  SER F OG  1 
ATOM   9035  N N   . VAL F  1 84  ? 6.912   32.710  10.021  1.00 15.90  ? 76  VAL F N   1 
ATOM   9036  C CA  . VAL F  1 84  ? 6.908   31.503  10.819  1.00 14.91  ? 76  VAL F CA  1 
ATOM   9037  C C   . VAL F  1 84  ? 7.763   30.450  10.114  1.00 15.64  ? 76  VAL F C   1 
ATOM   9038  O O   . VAL F  1 84  ? 7.615   30.242  8.915   1.00 14.84  ? 76  VAL F O   1 
ATOM   9039  C CB  . VAL F  1 84  ? 5.476   30.967  10.923  1.00 15.64  ? 76  VAL F CB  1 
ATOM   9040  C CG1 . VAL F  1 84  ? 5.431   29.718  11.790  1.00 12.44  ? 76  VAL F CG1 1 
ATOM   9041  C CG2 . VAL F  1 84  ? 4.536   32.056  11.444  1.00 15.59  ? 76  VAL F CG2 1 
ATOM   9042  N N   . PRO F  1 85  ? 8.681   29.798  10.848  1.00 16.51  ? 77  PRO F N   1 
ATOM   9043  C CA  . PRO F  1 85  ? 9.407   28.671  10.259  1.00 12.13  ? 77  PRO F CA  1 
ATOM   9044  C C   . PRO F  1 85  ? 8.401   27.600  9.828   1.00 17.92  ? 77  PRO F C   1 
ATOM   9045  O O   . PRO F  1 85  ? 7.462   27.313  10.578  1.00 16.51  ? 77  PRO F O   1 
ATOM   9046  C CB  . PRO F  1 85  ? 10.260  28.163  11.420  1.00 10.88  ? 77  PRO F CB  1 
ATOM   9047  C CG  . PRO F  1 85  ? 10.421  29.348  12.323  1.00 14.94  ? 77  PRO F CG  1 
ATOM   9048  C CD  . PRO F  1 85  ? 9.120   30.086  12.226  1.00 16.47  ? 77  PRO F CD  1 
ATOM   9049  N N   . ILE F  1 86  ? 8.580   27.026  8.639   1.00 17.03  ? 78  ILE F N   1 
ATOM   9050  C CA  . ILE F  1 86  ? 7.579   26.116  8.088   1.00 14.61  ? 78  ILE F CA  1 
ATOM   9051  C C   . ILE F  1 86  ? 7.463   24.783  8.817   1.00 12.38  ? 78  ILE F C   1 
ATOM   9052  O O   . ILE F  1 86  ? 6.553   24.012  8.561   1.00 18.81  ? 78  ILE F O   1 
ATOM   9053  C CB  . ILE F  1 86  ? 7.798   25.857  6.583   1.00 15.24  ? 78  ILE F CB  1 
ATOM   9054  C CG1 . ILE F  1 86  ? 9.152   25.174  6.340   1.00 13.82  ? 78  ILE F CG1 1 
ATOM   9055  C CG2 . ILE F  1 86  ? 7.667   27.164  5.810   1.00 13.13  ? 78  ILE F CG2 1 
ATOM   9056  C CD1 . ILE F  1 86  ? 9.295   24.557  4.962   1.00 10.19  ? 78  ILE F CD1 1 
ATOM   9057  N N   . SER F  1 87  ? 8.373   24.498  9.728   1.00 11.54  ? 79  SER F N   1 
ATOM   9058  C CA  . SER F  1 87  ? 8.239   23.276  10.507  1.00 14.78  ? 79  SER F CA  1 
ATOM   9059  C C   . SER F  1 87  ? 7.135   23.405  11.582  1.00 12.39  ? 79  SER F C   1 
ATOM   9060  O O   . SER F  1 87  ? 6.669   22.402  12.120  1.00 9.56   ? 79  SER F O   1 
ATOM   9061  C CB  . SER F  1 87  ? 9.586   22.872  11.108  1.00 13.37  ? 79  SER F CB  1 
ATOM   9062  O OG  . SER F  1 87  ? 10.251  24.005  11.630  1.00 18.91  ? 79  SER F OG  1 
ATOM   9063  N N   . SER F  1 88  ? 6.717   24.643  11.855  1.00 11.73  ? 80  SER F N   1 
ATOM   9064  C CA  . SER F  1 88  ? 5.595   24.949  12.746  1.00 10.69  ? 80  SER F CA  1 
ATOM   9065  C C   . SER F  1 88  ? 4.239   24.993  12.015  1.00 14.84  ? 80  SER F C   1 
ATOM   9066  O O   . SER F  1 88  ? 3.190   25.137  12.645  1.00 9.66   ? 80  SER F O   1 
ATOM   9067  C CB  . SER F  1 88  ? 5.813   26.300  13.442  1.00 13.79  ? 80  SER F CB  1 
ATOM   9068  O OG  . SER F  1 88  ? 6.917   26.282  14.336  1.00 15.91  ? 80  SER F OG  1 
ATOM   9069  N N   . LEU F  1 89  ? 4.253   24.876  10.688  1.00 15.86  ? 81  LEU F N   1 
ATOM   9070  C CA  . LEU F  1 89  ? 3.018   24.989  9.925   1.00 12.63  ? 81  LEU F CA  1 
ATOM   9071  C C   . LEU F  1 89  ? 2.767   23.757  9.094   1.00 11.55  ? 81  LEU F C   1 
ATOM   9072  O O   . LEU F  1 89  ? 3.680   23.009  8.808   1.00 13.00  ? 81  LEU F O   1 
ATOM   9073  C CB  . LEU F  1 89  ? 3.059   26.201  9.003   1.00 14.41  ? 81  LEU F CB  1 
ATOM   9074  C CG  . LEU F  1 89  ? 3.009   27.592  9.618   1.00 13.48  ? 81  LEU F CG  1 
ATOM   9075  C CD1 . LEU F  1 89  ? 3.401   28.577  8.528   1.00 15.18  ? 81  LEU F CD1 1 
ATOM   9076  C CD2 . LEU F  1 89  ? 1.629   27.906  10.154  1.00 10.40  ? 81  LEU F CD2 1 
ATOM   9077  N N   . TRP F  1 90  ? 1.510   23.544  8.724   1.00 14.80  ? 82  TRP F N   1 
ATOM   9078  C CA  . TRP F  1 90  ? 1.201   22.579  7.686   1.00 14.94  ? 82  TRP F CA  1 
ATOM   9079  C C   . TRP F  1 90  ? 1.566   23.220  6.363   1.00 16.03  ? 82  TRP F C   1 
ATOM   9080  O O   . TRP F  1 90  ? 1.378   24.424  6.156   1.00 13.18  ? 82  TRP F O   1 
ATOM   9081  C CB  . TRP F  1 90  ? -0.276  22.201  7.675   1.00 10.34  ? 82  TRP F CB  1 
ATOM   9082  C CG  . TRP F  1 90  ? -0.643  21.275  6.540   1.00 12.85  ? 82  TRP F CG  1 
ATOM   9083  C CD1 . TRP F  1 90  ? -0.539  19.909  6.525   1.00 11.36  ? 82  TRP F CD1 1 
ATOM   9084  C CD2 . TRP F  1 90  ? -1.164  21.650  5.255   1.00 13.33  ? 82  TRP F CD2 1 
ATOM   9085  N NE1 . TRP F  1 90  ? -0.976  19.412  5.320   1.00 10.59  ? 82  TRP F NE1 1 
ATOM   9086  C CE2 . TRP F  1 90  ? -1.359  20.457  4.518   1.00 13.05  ? 82  TRP F CE2 1 
ATOM   9087  C CE3 . TRP F  1 90  ? -1.486  22.877  4.653   1.00 14.82  ? 82  TRP F CE3 1 
ATOM   9088  C CZ2 . TRP F  1 90  ? -1.859  20.455  3.200   1.00 11.47  ? 82  TRP F CZ2 1 
ATOM   9089  C CZ3 . TRP F  1 90  ? -2.000  22.872  3.349   1.00 13.09  ? 82  TRP F CZ3 1 
ATOM   9090  C CH2 . TRP F  1 90  ? -2.172  21.664  2.639   1.00 8.87   ? 82  TRP F CH2 1 
ATOM   9091  N N   . VAL F  1 91  ? 2.071   22.396  5.463   1.00 15.43  ? 83  VAL F N   1 
ATOM   9092  C CA  . VAL F  1 91  ? 2.585   22.880  4.203   1.00 16.42  ? 83  VAL F CA  1 
ATOM   9093  C C   . VAL F  1 91  ? 2.323   21.773  3.185   1.00 15.05  ? 83  VAL F C   1 
ATOM   9094  O O   . VAL F  1 91  ? 2.643   20.607  3.432   1.00 15.38  ? 83  VAL F O   1 
ATOM   9095  C CB  . VAL F  1 91  ? 4.073   23.303  4.361   1.00 17.10  ? 83  VAL F CB  1 
ATOM   9096  C CG1 . VAL F  1 91  ? 5.024   22.245  3.836   1.00 18.89  ? 83  VAL F CG1 1 
ATOM   9097  C CG2 . VAL F  1 91  ? 4.334   24.682  3.740   1.00 15.70  ? 83  VAL F CG2 1 
ATOM   9098  N N   . PRO F  1 92  ? 1.653   22.122  2.072   1.00 14.50  ? 84  PRO F N   1 
ATOM   9099  C CA  . PRO F  1 92  ? 1.123   21.090  1.169   1.00 14.60  ? 84  PRO F CA  1 
ATOM   9100  C C   . PRO F  1 92  ? 2.219   20.233  0.549   1.00 15.77  ? 84  PRO F C   1 
ATOM   9101  O O   . PRO F  1 92  ? 3.247   20.764  0.147   1.00 14.09  ? 84  PRO F O   1 
ATOM   9102  C CB  . PRO F  1 92  ? 0.385   21.895  0.095   1.00 13.25  ? 84  PRO F CB  1 
ATOM   9103  C CG  . PRO F  1 92  ? 0.881   23.294  0.237   1.00 18.66  ? 84  PRO F CG  1 
ATOM   9104  C CD  . PRO F  1 92  ? 1.264   23.479  1.661   1.00 12.50  ? 84  PRO F CD  1 
ATOM   9105  N N   . ASP F  1 93  ? 2.002   18.920  0.500   1.00 16.26  ? 85  ASP F N   1 
ATOM   9106  C CA  . ASP F  1 93  ? 2.972   17.993  -0.092  1.00 17.36  ? 85  ASP F CA  1 
ATOM   9107  C C   . ASP F  1 93  ? 2.997   18.037  -1.629  1.00 15.65  ? 85  ASP F C   1 
ATOM   9108  O O   . ASP F  1 93  ? 2.798   17.020  -2.284  1.00 17.34  ? 85  ASP F O   1 
ATOM   9109  C CB  . ASP F  1 93  ? 2.722   16.553  0.396   1.00 13.50  ? 85  ASP F CB  1 
ATOM   9110  C CG  . ASP F  1 93  ? 1.278   16.099  0.176   1.00 20.94  ? 85  ASP F CG  1 
ATOM   9111  O OD1 . ASP F  1 93  ? 0.369   16.959  0.281   1.00 20.13  ? 85  ASP F OD1 1 
ATOM   9112  O OD2 . ASP F  1 93  ? 1.051   14.890  -0.106  1.00 20.62  ? 85  ASP F OD2 1 
ATOM   9113  N N   . LEU F  1 94  ? 3.253   19.211  -2.193  1.00 13.95  ? 86  LEU F N   1 
ATOM   9114  C CA  . LEU F  1 94  ? 3.350   19.357  -3.641  1.00 19.65  ? 86  LEU F CA  1 
ATOM   9115  C C   . LEU F  1 94  ? 4.516   18.539  -4.194  1.00 22.21  ? 86  LEU F C   1 
ATOM   9116  O O   . LEU F  1 94  ? 5.607   18.568  -3.641  1.00 26.41  ? 86  LEU F O   1 
ATOM   9117  C CB  . LEU F  1 94  ? 3.498   20.835  -4.016  1.00 16.61  ? 86  LEU F CB  1 
ATOM   9118  C CG  . LEU F  1 94  ? 2.265   21.692  -3.707  1.00 15.75  ? 86  LEU F CG  1 
ATOM   9119  C CD1 . LEU F  1 94  ? 2.443   23.117  -4.167  1.00 15.48  ? 86  LEU F CD1 1 
ATOM   9120  C CD2 . LEU F  1 94  ? 0.998   21.085  -4.315  1.00 20.68  ? 86  LEU F CD2 1 
ATOM   9121  N N   . ALA F  1 95  ? 4.283   17.783  -5.262  1.00 19.99  ? 87  ALA F N   1 
ATOM   9122  C CA  . ALA F  1 95  ? 5.372   17.043  -5.912  1.00 23.55  ? 87  ALA F CA  1 
ATOM   9123  C C   . ALA F  1 95  ? 5.408   17.275  -7.438  1.00 20.88  ? 87  ALA F C   1 
ATOM   9124  O O   . ALA F  1 95  ? 4.375   17.275  -8.094  1.00 21.89  ? 87  ALA F O   1 
ATOM   9125  C CB  . ALA F  1 95  ? 5.290   15.541  -5.577  1.00 14.57  ? 87  ALA F CB  1 
ATOM   9126  N N   . ALA F  1 96  ? 6.593   17.493  -7.998  1.00 22.94  ? 88  ALA F N   1 
ATOM   9127  C CA  . ALA F  1 96  ? 6.726   17.641  -9.454  1.00 24.05  ? 88  ALA F CA  1 
ATOM   9128  C C   . ALA F  1 96  ? 6.931   16.282  -10.115 1.00 21.07  ? 88  ALA F C   1 
ATOM   9129  O O   . ALA F  1 96  ? 7.950   15.628  -9.888  1.00 21.44  ? 88  ALA F O   1 
ATOM   9130  C CB  . ALA F  1 96  ? 7.875   18.562  -9.789  1.00 19.53  ? 88  ALA F CB  1 
ATOM   9131  N N   . TYR F  1 97  ? 5.975   15.865  -10.940 1.00 18.89  ? 89  TYR F N   1 
ATOM   9132  C CA  . TYR F  1 97  ? 5.956   14.490  -11.434 1.00 22.00  ? 89  TYR F CA  1 
ATOM   9133  C C   . TYR F  1 97  ? 7.103   14.167  -12.422 1.00 24.60  ? 89  TYR F C   1 
ATOM   9134  O O   . TYR F  1 97  ? 7.565   13.026  -12.496 1.00 20.49  ? 89  TYR F O   1 
ATOM   9135  C CB  . TYR F  1 97  ? 4.605   14.128  -12.074 1.00 24.09  ? 89  TYR F CB  1 
ATOM   9136  C CG  . TYR F  1 97  ? 3.356   14.341  -11.234 1.00 31.84  ? 89  TYR F CG  1 
ATOM   9137  C CD1 . TYR F  1 97  ? 2.102   14.007  -11.731 1.00 40.38  ? 89  TYR F CD1 1 
ATOM   9138  C CD2 . TYR F  1 97  ? 3.422   14.874  -9.957  1.00 36.56  ? 89  TYR F CD2 1 
ATOM   9139  C CE1 . TYR F  1 97  ? 0.955   14.198  -10.977 1.00 39.34  ? 89  TYR F CE1 1 
ATOM   9140  C CE2 . TYR F  1 97  ? 2.285   15.075  -9.197  1.00 32.86  ? 89  TYR F CE2 1 
ATOM   9141  C CZ  . TYR F  1 97  ? 1.055   14.738  -9.708  1.00 40.70  ? 89  TYR F CZ  1 
ATOM   9142  O OH  . TYR F  1 97  ? -0.068  14.948  -8.926  1.00 40.89  ? 89  TYR F OH  1 
ATOM   9143  N N   . ASN F  1 98  ? 7.558   15.149  -13.193 1.00 20.73  ? 90  ASN F N   1 
ATOM   9144  C CA  . ASN F  1 98  ? 8.649   14.870  -14.127 1.00 29.32  ? 90  ASN F CA  1 
ATOM   9145  C C   . ASN F  1 98  ? 10.033  15.254  -13.594 1.00 27.02  ? 90  ASN F C   1 
ATOM   9146  O O   . ASN F  1 98  ? 11.024  15.184  -14.314 1.00 29.29  ? 90  ASN F O   1 
ATOM   9147  C CB  . ASN F  1 98  ? 8.385   15.485  -15.508 1.00 24.97  ? 90  ASN F CB  1 
ATOM   9148  C CG  . ASN F  1 98  ? 7.946   16.926  -15.427 1.00 31.91  ? 90  ASN F CG  1 
ATOM   9149  O OD1 . ASN F  1 98  ? 7.408   17.371  -14.409 1.00 30.86  ? 90  ASN F OD1 1 
ATOM   9150  N ND2 . ASN F  1 98  ? 8.160   17.666  -16.506 1.00 35.25  ? 90  ASN F ND2 1 
ATOM   9151  N N   . ALA F  1 99  ? 10.094  15.648  -12.327 1.00 24.77  ? 91  ALA F N   1 
ATOM   9152  C CA  . ALA F  1 99  ? 11.364  15.968  -11.684 1.00 24.44  ? 91  ALA F CA  1 
ATOM   9153  C C   . ALA F  1 99  ? 12.251  14.742  -11.655 1.00 23.08  ? 91  ALA F C   1 
ATOM   9154  O O   . ALA F  1 99  ? 11.757  13.619  -11.636 1.00 24.14  ? 91  ALA F O   1 
ATOM   9155  C CB  . ALA F  1 99  ? 11.141  16.488  -10.285 1.00 20.99  ? 91  ALA F CB  1 
ATOM   9156  N N   . ILE F  1 100 ? 13.562  14.959  -11.684 1.00 23.07  ? 92  ILE F N   1 
ATOM   9157  C CA  . ILE F  1 100 ? 14.504  13.849  -11.717 1.00 27.00  ? 92  ILE F CA  1 
ATOM   9158  C C   . ILE F  1 100 ? 15.639  14.020  -10.712 1.00 30.44  ? 92  ILE F C   1 
ATOM   9159  O O   . ILE F  1 100 ? 16.469  13.130  -10.553 1.00 30.98  ? 92  ILE F O   1 
ATOM   9160  C CB  . ILE F  1 100 ? 15.072  13.625  -13.123 1.00 24.55  ? 92  ILE F CB  1 
ATOM   9161  C CG1 . ILE F  1 100 ? 15.787  14.893  -13.614 1.00 32.87  ? 92  ILE F CG1 1 
ATOM   9162  C CG2 . ILE F  1 100 ? 13.964  13.183  -14.065 1.00 17.15  ? 92  ILE F CG2 1 
ATOM   9163  C CD1 . ILE F  1 100 ? 16.386  14.778  -15.004 1.00 28.66  ? 92  ILE F CD1 1 
ATOM   9164  N N   . SER F  1 101 ? 15.667  15.169  -10.045 1.00 23.13  ? 93  SER F N   1 
ATOM   9165  C CA  . SER F  1 101 ? 16.503  15.362  -8.877  1.00 20.61  ? 93  SER F CA  1 
ATOM   9166  C C   . SER F  1 101 ? 15.587  15.843  -7.752  1.00 28.18  ? 93  SER F C   1 
ATOM   9167  O O   . SER F  1 101 ? 14.501  16.386  -8.025  1.00 22.27  ? 93  SER F O   1 
ATOM   9168  C CB  . SER F  1 101 ? 17.564  16.413  -9.162  1.00 19.64  ? 93  SER F CB  1 
ATOM   9169  O OG  . SER F  1 101 ? 16.985  17.703  -9.267  1.00 22.24  ? 93  SER F OG  1 
ATOM   9170  N N   . LYS F  1 102 ? 15.995  15.644  -6.496  1.00 24.75  ? 94  LYS F N   1 
ATOM   9171  C CA  . LYS F  1 102 ? 15.190  16.157  -5.379  1.00 26.48  ? 94  LYS F CA  1 
ATOM   9172  C C   . LYS F  1 102 ? 15.238  17.680  -5.409  1.00 22.72  ? 94  LYS F C   1 
ATOM   9173  O O   . LYS F  1 102 ? 16.239  18.256  -5.807  1.00 20.51  ? 94  LYS F O   1 
ATOM   9174  C CB  . LYS F  1 102 ? 15.631  15.593  -4.017  1.00 27.95  ? 94  LYS F CB  1 
ATOM   9175  C CG  . LYS F  1 102 ? 17.060  15.948  -3.581  1.00 34.95  ? 94  LYS F CG  1 
ATOM   9176  C CD  . LYS F  1 102 ? 17.704  14.810  -2.773  1.00 29.05  ? 94  LYS F CD  1 
ATOM   9177  C CE  . LYS F  1 102 ? 16.897  14.475  -1.518  1.00 31.47  ? 94  LYS F CE  1 
ATOM   9178  N NZ  . LYS F  1 102 ? 17.251  13.146  -0.935  1.00 24.01  ? 94  LYS F NZ  1 
ATOM   9179  N N   . PRO F  1 103 ? 14.134  18.335  -5.034  1.00 23.82  ? 95  PRO F N   1 
ATOM   9180  C CA  . PRO F  1 103 ? 14.167  19.797  -5.134  1.00 22.58  ? 95  PRO F CA  1 
ATOM   9181  C C   . PRO F  1 103 ? 15.249  20.327  -4.222  1.00 24.25  ? 95  PRO F C   1 
ATOM   9182  O O   . PRO F  1 103 ? 15.497  19.747  -3.176  1.00 32.12  ? 95  PRO F O   1 
ATOM   9183  C CB  . PRO F  1 103 ? 12.787  20.221  -4.628  1.00 15.77  ? 95  PRO F CB  1 
ATOM   9184  C CG  . PRO F  1 103 ? 12.256  19.033  -3.897  1.00 18.37  ? 95  PRO F CG  1 
ATOM   9185  C CD  . PRO F  1 103 ? 12.844  17.830  -4.535  1.00 14.82  ? 95  PRO F CD  1 
ATOM   9186  N N   . GLU F  1 104 ? 15.927  21.380  -4.633  1.00 21.04  ? 96  GLU F N   1 
ATOM   9187  C CA  . GLU F  1 104 ? 16.944  21.966  -3.794  1.00 19.39  ? 96  GLU F CA  1 
ATOM   9188  C C   . GLU F  1 104 ? 16.457  23.361  -3.474  1.00 20.15  ? 96  GLU F C   1 
ATOM   9189  O O   . GLU F  1 104 ? 16.271  24.179  -4.375  1.00 21.06  ? 96  GLU F O   1 
ATOM   9190  C CB  . GLU F  1 104 ? 18.288  21.978  -4.521  1.00 21.75  ? 96  GLU F CB  1 
ATOM   9191  C CG  . GLU F  1 104 ? 19.345  22.862  -3.899  1.00 28.25  ? 96  GLU F CG  1 
ATOM   9192  C CD  . GLU F  1 104 ? 20.656  22.836  -4.679  1.00 41.60  ? 96  GLU F CD  1 
ATOM   9193  O OE1 . GLU F  1 104 ? 20.838  21.906  -5.501  1.00 41.26  ? 96  GLU F OE1 1 
ATOM   9194  O OE2 . GLU F  1 104 ? 21.497  23.746  -4.469  1.00 40.61  ? 96  GLU F OE2 1 
ATOM   9195  N N   . VAL F  1 105 ? 16.199  23.617  -2.195  1.00 16.87  ? 97  VAL F N   1 
ATOM   9196  C CA  . VAL F  1 105 ? 15.649  24.899  -1.794  1.00 17.12  ? 97  VAL F CA  1 
ATOM   9197  C C   . VAL F  1 105 ? 16.800  25.815  -1.460  1.00 18.11  ? 97  VAL F C   1 
ATOM   9198  O O   . VAL F  1 105 ? 17.678  25.454  -0.673  1.00 17.47  ? 97  VAL F O   1 
ATOM   9199  C CB  . VAL F  1 105 ? 14.671  24.757  -0.609  1.00 18.13  ? 97  VAL F CB  1 
ATOM   9200  C CG1 . VAL F  1 105 ? 14.448  26.100  0.075   1.00 12.55  ? 97  VAL F CG1 1 
ATOM   9201  C CG2 . VAL F  1 105 ? 13.380  24.160  -1.098  1.00 12.72  ? 97  VAL F CG2 1 
ATOM   9202  N N   . LEU F  1 106 ? 16.804  26.989  -2.086  1.00 18.18  ? 98  LEU F N   1 
ATOM   9203  C CA  . LEU F  1 106 ? 17.970  27.866  -2.070  1.00 18.09  ? 98  LEU F CA  1 
ATOM   9204  C C   . LEU F  1 106 ? 17.810  28.996  -1.076  1.00 20.18  ? 98  LEU F C   1 
ATOM   9205  O O   . LEU F  1 106 ? 18.740  29.759  -0.834  1.00 23.85  ? 98  LEU F O   1 
ATOM   9206  C CB  . LEU F  1 106 ? 18.191  28.464  -3.458  1.00 19.05  ? 98  LEU F CB  1 
ATOM   9207  C CG  . LEU F  1 106 ? 18.449  27.492  -4.610  1.00 24.62  ? 98  LEU F CG  1 
ATOM   9208  C CD1 . LEU F  1 106 ? 18.698  28.249  -5.906  1.00 23.57  ? 98  LEU F CD1 1 
ATOM   9209  C CD2 . LEU F  1 106 ? 19.617  26.568  -4.293  1.00 23.55  ? 98  LEU F CD2 1 
ATOM   9210  N N   . THR F  1 107 ? 16.608  29.111  -0.516  1.00 21.05  ? 99  THR F N   1 
ATOM   9211  C CA  . THR F  1 107 ? 16.238  30.238  0.338   1.00 19.05  ? 99  THR F CA  1 
ATOM   9212  C C   . THR F  1 107 ? 15.826  29.778  1.732   1.00 17.58  ? 99  THR F C   1 
ATOM   9213  O O   . THR F  1 107 ? 15.240  28.707  1.894   1.00 13.46  ? 99  THR F O   1 
ATOM   9214  C CB  . THR F  1 107 ? 15.092  31.061  -0.279  1.00 20.55  ? 99  THR F CB  1 
ATOM   9215  O OG1 . THR F  1 107 ? 14.832  32.210  0.536   1.00 21.39  ? 99  THR F OG1 1 
ATOM   9216  C CG2 . THR F  1 107 ? 13.828  30.221  -0.381  1.00 20.34  ? 99  THR F CG2 1 
ATOM   9217  N N   . PRO F  1 108 ? 16.148  30.585  2.739   1.00 14.93  ? 100 PRO F N   1 
ATOM   9218  C CA  . PRO F  1 108 ? 15.977  30.175  4.128   1.00 17.24  ? 100 PRO F CA  1 
ATOM   9219  C C   . PRO F  1 108 ? 14.507  29.953  4.360   1.00 13.30  ? 100 PRO F C   1 
ATOM   9220  O O   . PRO F  1 108 ? 13.682  30.766  3.943   1.00 17.09  ? 100 PRO F O   1 
ATOM   9221  C CB  . PRO F  1 108 ? 16.457  31.396  4.911   1.00 13.09  ? 100 PRO F CB  1 
ATOM   9222  C CG  . PRO F  1 108 ? 16.180  32.546  4.006   1.00 18.18  ? 100 PRO F CG  1 
ATOM   9223  C CD  . PRO F  1 108 ? 16.404  32.031  2.612   1.00 15.87  ? 100 PRO F CD  1 
ATOM   9224  N N   . GLN F  1 109 ? 14.159  28.861  5.023   1.00 13.07  ? 101 GLN F N   1 
ATOM   9225  C CA  . GLN F  1 109 ? 12.754  28.544  5.145   1.00 12.39  ? 101 GLN F CA  1 
ATOM   9226  C C   . GLN F  1 109 ? 12.028  29.643  5.905   1.00 12.06  ? 101 GLN F C   1 
ATOM   9227  O O   . GLN F  1 109 ? 12.452  30.073  6.977   1.00 13.52  ? 101 GLN F O   1 
ATOM   9228  C CB  . GLN F  1 109 ? 12.567  27.202  5.857   1.00 11.09  ? 101 GLN F CB  1 
ATOM   9229  C CG  . GLN F  1 109 ? 13.497  26.105  5.365   1.00 9.58   ? 101 GLN F CG  1 
ATOM   9230  C CD  . GLN F  1 109 ? 12.860  25.234  4.300   1.00 18.13  ? 101 GLN F CD  1 
ATOM   9231  O OE1 . GLN F  1 109 ? 12.054  25.705  3.498   1.00 17.22  ? 101 GLN F OE1 1 
ATOM   9232  N NE2 . GLN F  1 109 ? 13.219  23.956  4.288   1.00 18.84  ? 101 GLN F NE2 1 
ATOM   9233  N N   . LEU F  1 110 ? 10.915  30.073  5.328   1.00 13.81  ? 102 LEU F N   1 
ATOM   9234  C CA  . LEU F  1 110 ? 9.927   30.893  6.004   1.00 13.31  ? 102 LEU F CA  1 
ATOM   9235  C C   . LEU F  1 110 ? 8.563   30.716  5.342   1.00 16.91  ? 102 LEU F C   1 
ATOM   9236  O O   . LEU F  1 110 ? 8.476   30.400  4.155   1.00 15.55  ? 102 LEU F O   1 
ATOM   9237  C CB  . LEU F  1 110 ? 10.341  32.366  5.974   1.00 12.43  ? 102 LEU F CB  1 
ATOM   9238  C CG  . LEU F  1 110 ? 11.358  32.806  7.029   1.00 13.29  ? 102 LEU F CG  1 
ATOM   9239  C CD1 . LEU F  1 110 ? 11.411  34.323  7.125   1.00 10.89  ? 102 LEU F CD1 1 
ATOM   9240  C CD2 . LEU F  1 110 ? 11.030  32.190  8.381   1.00 15.78  ? 102 LEU F CD2 1 
ATOM   9241  N N   . ALA F  1 111 ? 7.504   30.943  6.109   1.00 17.12  ? 103 ALA F N   1 
ATOM   9242  C CA  . ALA F  1 111 ? 6.167   31.148  5.556   1.00 15.00  ? 103 ALA F CA  1 
ATOM   9243  C C   . ALA F  1 111 ? 5.462   32.288  6.288   1.00 12.49  ? 103 ALA F C   1 
ATOM   9244  O O   . ALA F  1 111 ? 5.462   32.332  7.519   1.00 14.06  ? 103 ALA F O   1 
ATOM   9245  C CB  . ALA F  1 111 ? 5.352   29.868  5.649   1.00 12.20  ? 103 ALA F CB  1 
ATOM   9246  N N   . ARG F  1 112 ? 4.870   33.213  5.537   1.00 9.75   ? 104 ARG F N   1 
ATOM   9247  C CA  . ARG F  1 112 ? 4.276   34.385  6.137   1.00 11.72  ? 104 ARG F CA  1 
ATOM   9248  C C   . ARG F  1 112 ? 2.879   33.968  6.459   1.00 18.40  ? 104 ARG F C   1 
ATOM   9249  O O   . ARG F  1 112 ? 2.254   33.241  5.679   1.00 18.75  ? 104 ARG F O   1 
ATOM   9250  C CB  . ARG F  1 112 ? 4.258   35.588  5.189   1.00 16.63  ? 104 ARG F CB  1 
ATOM   9251  C CG  . ARG F  1 112 ? 5.641   36.175  4.874   1.00 17.66  ? 104 ARG F CG  1 
ATOM   9252  C CD  . ARG F  1 112 ? 6.232   36.987  6.038   1.00 13.37  ? 104 ARG F CD  1 
ATOM   9253  N NE  . ARG F  1 112 ? 5.611   38.306  6.168   1.00 16.62  ? 104 ARG F NE  1 
ATOM   9254  C CZ  . ARG F  1 112 ? 6.030   39.257  7.001   1.00 20.29  ? 104 ARG F CZ  1 
ATOM   9255  N NH1 . ARG F  1 112 ? 7.075   39.041  7.794   1.00 20.73  ? 104 ARG F NH1 1 
ATOM   9256  N NH2 . ARG F  1 112 ? 5.410   40.429  7.044   1.00 20.72  ? 104 ARG F NH2 1 
ATOM   9257  N N   . VAL F  1 113 ? 2.403   34.384  7.629   1.00 18.70  ? 105 VAL F N   1 
ATOM   9258  C CA  . VAL F  1 113 ? 1.026   34.149  8.014   1.00 15.48  ? 105 VAL F CA  1 
ATOM   9259  C C   . VAL F  1 113 ? 0.377   35.513  8.164   1.00 17.97  ? 105 VAL F C   1 
ATOM   9260  O O   . VAL F  1 113 ? 0.970   36.437  8.720   1.00 18.02  ? 105 VAL F O   1 
ATOM   9261  C CB  . VAL F  1 113 ? 0.938   33.329  9.309   1.00 21.02  ? 105 VAL F CB  1 
ATOM   9262  C CG1 . VAL F  1 113 ? -0.504  33.240  9.781   1.00 19.98  ? 105 VAL F CG1 1 
ATOM   9263  C CG2 . VAL F  1 113 ? 1.536   31.934  9.104   1.00 13.15  ? 105 VAL F CG2 1 
ATOM   9264  N N   . VAL F  1 114 ? -0.822  35.657  7.619   1.00 20.39  ? 106 VAL F N   1 
ATOM   9265  C CA  . VAL F  1 114 ? -1.493  36.945  7.614   1.00 19.80  ? 106 VAL F CA  1 
ATOM   9266  C C   . VAL F  1 114 ? -2.631  36.890  8.612   1.00 20.75  ? 106 VAL F C   1 
ATOM   9267  O O   . VAL F  1 114 ? -3.287  35.860  8.747   1.00 20.95  ? 106 VAL F O   1 
ATOM   9268  C CB  . VAL F  1 114 ? -2.029  37.266  6.210   1.00 22.34  ? 106 VAL F CB  1 
ATOM   9269  C CG1 . VAL F  1 114 ? -2.548  38.682  6.137   1.00 23.61  ? 106 VAL F CG1 1 
ATOM   9270  C CG2 . VAL F  1 114 ? -0.936  37.070  5.186   1.00 23.95  ? 106 VAL F CG2 1 
ATOM   9271  N N   . SER F  1 115 ? -2.881  37.995  9.306   1.00 21.22  ? 107 SER F N   1 
ATOM   9272  C CA  . SER F  1 115 ? -3.892  38.019  10.367  1.00 22.38  ? 107 SER F CA  1 
ATOM   9273  C C   . SER F  1 115 ? -5.265  37.467  9.978   1.00 21.92  ? 107 SER F C   1 
ATOM   9274  O O   . SER F  1 115 ? -6.122  37.260  10.850  1.00 23.54  ? 107 SER F O   1 
ATOM   9275  C CB  . SER F  1 115 ? -4.044  39.424  10.951  1.00 20.18  ? 107 SER F CB  1 
ATOM   9276  O OG  . SER F  1 115 ? -4.700  40.284  10.043  1.00 23.82  ? 107 SER F OG  1 
ATOM   9277  N N   . ASP F  1 116 ? -5.472  37.218  8.687   1.00 16.41  ? 108 ASP F N   1 
ATOM   9278  C CA  . ASP F  1 116 ? -6.739  36.664  8.222   1.00 21.42  ? 108 ASP F CA  1 
ATOM   9279  C C   . ASP F  1 116 ? -6.676  35.169  7.885   1.00 21.88  ? 108 ASP F C   1 
ATOM   9280  O O   . ASP F  1 116 ? -7.645  34.606  7.380   1.00 27.75  ? 108 ASP F O   1 
ATOM   9281  C CB  . ASP F  1 116 ? -7.283  37.466  7.031   1.00 22.57  ? 108 ASP F CB  1 
ATOM   9282  C CG  . ASP F  1 116 ? -6.351  37.435  5.819   1.00 29.34  ? 108 ASP F CG  1 
ATOM   9283  O OD1 . ASP F  1 116 ? -6.697  38.062  4.793   1.00 28.43  ? 108 ASP F OD1 1 
ATOM   9284  O OD2 . ASP F  1 116 ? -5.277  36.788  5.884   1.00 28.10  ? 108 ASP F OD2 1 
ATOM   9285  N N   . GLY F  1 117 ? -5.537  34.536  8.146   1.00 19.55  ? 109 GLY F N   1 
ATOM   9286  C CA  . GLY F  1 117 ? -5.415  33.097  7.979   1.00 18.87  ? 109 GLY F CA  1 
ATOM   9287  C C   . GLY F  1 117 ? -4.762  32.633  6.687   1.00 22.35  ? 109 GLY F C   1 
ATOM   9288  O O   . GLY F  1 117 ? -4.538  31.430  6.472   1.00 18.77  ? 109 GLY F O   1 
ATOM   9289  N N   . GLU F  1 118 ? -4.454  33.575  5.807   1.00 21.19  ? 110 GLU F N   1 
ATOM   9290  C CA  . GLU F  1 118 ? -3.830  33.190  4.555   1.00 23.99  ? 110 GLU F CA  1 
ATOM   9291  C C   . GLU F  1 118 ? -2.370  32.874  4.851   1.00 20.82  ? 110 GLU F C   1 
ATOM   9292  O O   . GLU F  1 118 ? -1.708  33.622  5.577   1.00 18.91  ? 110 GLU F O   1 
ATOM   9293  C CB  . GLU F  1 118 ? -3.954  34.314  3.529   1.00 27.04  ? 110 GLU F CB  1 
ATOM   9294  C CG  . GLU F  1 118 ? -3.533  33.938  2.118   1.00 26.51  ? 110 GLU F CG  1 
ATOM   9295  C CD  . GLU F  1 118 ? -3.087  35.150  1.307   1.00 36.73  ? 110 GLU F CD  1 
ATOM   9296  O OE1 . GLU F  1 118 ? -3.553  36.278  1.604   1.00 37.33  ? 110 GLU F OE1 1 
ATOM   9297  O OE2 . GLU F  1 118 ? -2.254  34.977  0.384   1.00 41.80  ? 110 GLU F OE2 1 
ATOM   9298  N N   . VAL F  1 119 ? -1.886  31.750  4.326   1.00 16.80  ? 111 VAL F N   1 
ATOM   9299  C CA  . VAL F  1 119 ? -0.477  31.390  4.454   1.00 16.99  ? 111 VAL F CA  1 
ATOM   9300  C C   . VAL F  1 119 ? 0.272   31.523  3.122   1.00 20.76  ? 111 VAL F C   1 
ATOM   9301  O O   . VAL F  1 119 ? -0.163  31.023  2.088   1.00 22.27  ? 111 VAL F O   1 
ATOM   9302  C CB  . VAL F  1 119 ? -0.296  29.952  4.954   1.00 14.49  ? 111 VAL F CB  1 
ATOM   9303  C CG1 . VAL F  1 119 ? 1.163   29.697  5.238   1.00 14.00  ? 111 VAL F CG1 1 
ATOM   9304  C CG2 . VAL F  1 119 ? -1.119  29.713  6.185   1.00 18.65  ? 111 VAL F CG2 1 
ATOM   9305  N N   . LEU F  1 120 ? 1.423   32.171  3.159   1.00 20.51  ? 112 LEU F N   1 
ATOM   9306  C CA  . LEU F  1 120 ? 2.228   32.366  1.963   1.00 18.34  ? 112 LEU F CA  1 
ATOM   9307  C C   . LEU F  1 120 ? 3.584   31.684  2.125   1.00 15.57  ? 112 LEU F C   1 
ATOM   9308  O O   . LEU F  1 120 ? 4.336   32.004  3.039   1.00 15.94  ? 112 LEU F O   1 
ATOM   9309  C CB  . LEU F  1 120 ? 2.440   33.860  1.731   1.00 20.58  ? 112 LEU F CB  1 
ATOM   9310  C CG  . LEU F  1 120 ? 1.199   34.697  1.416   1.00 22.42  ? 112 LEU F CG  1 
ATOM   9311  C CD1 . LEU F  1 120 ? 0.310   34.900  2.619   1.00 22.03  ? 112 LEU F CD1 1 
ATOM   9312  C CD2 . LEU F  1 120 ? 1.615   36.042  0.860   1.00 27.87  ? 112 LEU F CD2 1 
ATOM   9313  N N   . TYR F  1 121 ? 3.891   30.733  1.254   1.00 15.18  ? 113 TYR F N   1 
ATOM   9314  C CA  . TYR F  1 121 ? 5.215   30.133  1.255   1.00 15.48  ? 113 TYR F CA  1 
ATOM   9315  C C   . TYR F  1 121 ? 5.769   30.150  -0.159  1.00 16.94  ? 113 TYR F C   1 
ATOM   9316  O O   . TYR F  1 121 ? 5.213   29.508  -1.046  1.00 17.36  ? 113 TYR F O   1 
ATOM   9317  C CB  . TYR F  1 121 ? 5.180   28.708  1.810   1.00 12.23  ? 113 TYR F CB  1 
ATOM   9318  C CG  . TYR F  1 121 ? 6.525   28.013  1.795   1.00 12.80  ? 113 TYR F CG  1 
ATOM   9319  C CD1 . TYR F  1 121 ? 7.626   28.577  2.428   1.00 15.06  ? 113 TYR F CD1 1 
ATOM   9320  C CD2 . TYR F  1 121 ? 6.696   26.792  1.147   1.00 11.20  ? 113 TYR F CD2 1 
ATOM   9321  C CE1 . TYR F  1 121 ? 8.869   27.944  2.419   1.00 14.82  ? 113 TYR F CE1 1 
ATOM   9322  C CE2 . TYR F  1 121 ? 7.926   26.146  1.133   1.00 11.09  ? 113 TYR F CE2 1 
ATOM   9323  C CZ  . TYR F  1 121 ? 9.015   26.727  1.768   1.00 16.16  ? 113 TYR F CZ  1 
ATOM   9324  O OH  . TYR F  1 121 ? 10.252  26.094  1.752   1.00 16.70  ? 113 TYR F OH  1 
ATOM   9325  N N   . MET F  1 122 ? 6.856   30.894  -0.363  1.00 19.36  ? 114 MET F N   1 
ATOM   9326  C CA  . MET F  1 122 ? 7.481   31.017  -1.688  1.00 19.28  ? 114 MET F CA  1 
ATOM   9327  C C   . MET F  1 122 ? 8.973   30.698  -1.669  1.00 15.74  ? 114 MET F C   1 
ATOM   9328  O O   . MET F  1 122 ? 9.820   31.591  -1.557  1.00 14.92  ? 114 MET F O   1 
ATOM   9329  C CB  . MET F  1 122 ? 7.247   32.409  -2.284  1.00 21.66  ? 114 MET F CB  1 
ATOM   9330  C CG  . MET F  1 122 ? 7.546   32.492  -3.795  1.00 31.50  ? 114 MET F CG  1 
ATOM   9331  S SD  . MET F  1 122 ? 7.547   34.172  -4.509  1.00 42.70  ? 114 MET F SD  1 
ATOM   9332  C CE  . MET F  1 122 ? 9.092   34.855  -3.915  1.00 28.27  ? 114 MET F CE  1 
ATOM   9333  N N   . PRO F  1 123 ? 9.303   29.411  -1.766  1.00 13.55  ? 115 PRO F N   1 
ATOM   9334  C CA  . PRO F  1 123 ? 10.703  28.986  -1.819  1.00 16.50  ? 115 PRO F CA  1 
ATOM   9335  C C   . PRO F  1 123 ? 11.303  29.143  -3.225  1.00 22.51  ? 115 PRO F C   1 
ATOM   9336  O O   . PRO F  1 123 ? 10.569  29.150  -4.216  1.00 22.75  ? 115 PRO F O   1 
ATOM   9337  C CB  . PRO F  1 123 ? 10.624  27.506  -1.439  1.00 14.88  ? 115 PRO F CB  1 
ATOM   9338  C CG  . PRO F  1 123 ? 9.284   27.079  -1.934  1.00 13.37  ? 115 PRO F CG  1 
ATOM   9339  C CD  . PRO F  1 123 ? 8.375   28.271  -1.709  1.00 14.70  ? 115 PRO F CD  1 
ATOM   9340  N N   . SER F  1 124 ? 12.625  29.266  -3.305  1.00 22.07  ? 116 SER F N   1 
ATOM   9341  C CA  . SER F  1 124 ? 13.318  29.324  -4.583  1.00 19.63  ? 116 SER F CA  1 
ATOM   9342  C C   . SER F  1 124 ? 13.958  27.977  -4.817  1.00 20.36  ? 116 SER F C   1 
ATOM   9343  O O   . SER F  1 124 ? 14.786  27.528  -4.027  1.00 23.67  ? 116 SER F O   1 
ATOM   9344  C CB  . SER F  1 124 ? 14.392  30.403  -4.558  1.00 21.98  ? 116 SER F CB  1 
ATOM   9345  O OG  . SER F  1 124 ? 14.866  30.664  -5.863  1.00 23.02  ? 116 SER F OG  1 
ATOM   9346  N N   . ILE F  1 125 ? 13.572  27.328  -5.905  1.00 22.05  ? 117 ILE F N   1 
ATOM   9347  C CA  . ILE F  1 125 ? 14.005  25.964  -6.171  1.00 20.17  ? 117 ILE F CA  1 
ATOM   9348  C C   . ILE F  1 125 ? 14.887  25.810  -7.419  1.00 23.05  ? 117 ILE F C   1 
ATOM   9349  O O   . ILE F  1 125 ? 14.562  26.316  -8.485  1.00 19.35  ? 117 ILE F O   1 
ATOM   9350  C CB  . ILE F  1 125 ? 12.784  25.076  -6.325  1.00 15.95  ? 117 ILE F CB  1 
ATOM   9351  C CG1 . ILE F  1 125 ? 11.914  25.197  -5.069  1.00 23.87  ? 117 ILE F CG1 1 
ATOM   9352  C CG2 . ILE F  1 125 ? 13.191  23.644  -6.592  1.00 18.73  ? 117 ILE F CG2 1 
ATOM   9353  C CD1 . ILE F  1 125 ? 10.831  24.123  -4.952  1.00 23.94  ? 117 ILE F CD1 1 
ATOM   9354  N N   . ARG F  1 126 ? 16.013  25.122  -7.266  1.00 24.05  ? 118 ARG F N   1 
ATOM   9355  C CA  . ARG F  1 126 ? 16.768  24.627  -8.400  1.00 19.59  ? 118 ARG F CA  1 
ATOM   9356  C C   . ARG F  1 126 ? 16.520  23.133  -8.492  1.00 23.40  ? 118 ARG F C   1 
ATOM   9357  O O   . ARG F  1 126 ? 16.826  22.397  -7.560  1.00 25.09  ? 118 ARG F O   1 
ATOM   9358  C CB  . ARG F  1 126 ? 18.264  24.873  -8.221  1.00 23.84  ? 118 ARG F CB  1 
ATOM   9359  C CG  . ARG F  1 126 ? 19.079  24.617  -9.502  1.00 25.86  ? 118 ARG F CG  1 
ATOM   9360  C CD  . ARG F  1 126 ? 20.214  23.610  -9.324  1.00 32.69  ? 118 ARG F CD  1 
ATOM   9361  N NE  . ARG F  1 126 ? 19.766  22.209  -9.365  1.00 36.37  ? 118 ARG F NE  1 
ATOM   9362  C CZ  . ARG F  1 126 ? 20.577  21.169  -9.571  1.00 35.88  ? 118 ARG F CZ  1 
ATOM   9363  N NH1 . ARG F  1 126 ? 21.874  21.366  -9.770  1.00 45.58  ? 118 ARG F NH1 1 
ATOM   9364  N NH2 . ARG F  1 126 ? 20.099  19.933  -9.592  1.00 31.88  ? 118 ARG F NH2 1 
ATOM   9365  N N   . GLN F  1 127 ? 15.989  22.675  -9.618  1.00 25.37  ? 119 GLN F N   1 
ATOM   9366  C CA  . GLN F  1 127 ? 15.677  21.261  -9.771  1.00 23.78  ? 119 GLN F CA  1 
ATOM   9367  C C   . GLN F  1 127 ? 15.798  20.799  -11.231 1.00 27.47  ? 119 GLN F C   1 
ATOM   9368  O O   . GLN F  1 127 ? 15.506  21.552  -12.153 1.00 24.27  ? 119 GLN F O   1 
ATOM   9369  C CB  . GLN F  1 127 ? 14.266  21.017  -9.254  1.00 22.41  ? 119 GLN F CB  1 
ATOM   9370  C CG  . GLN F  1 127 ? 13.863  19.570  -9.188  1.00 26.71  ? 119 GLN F CG  1 
ATOM   9371  C CD  . GLN F  1 127 ? 12.518  19.405  -8.521  1.00 29.27  ? 119 GLN F CD  1 
ATOM   9372  O OE1 . GLN F  1 127 ? 11.695  20.320  -8.535  1.00 28.57  ? 119 GLN F OE1 1 
ATOM   9373  N NE2 . GLN F  1 127 ? 12.294  18.247  -7.911  1.00 29.74  ? 119 GLN F NE2 1 
ATOM   9374  N N   . ARG F  1 128 ? 16.229  19.558  -11.433 1.00 26.54  ? 120 ARG F N   1 
ATOM   9375  C CA  . ARG F  1 128 ? 16.330  18.996  -12.771 1.00 27.30  ? 120 ARG F CA  1 
ATOM   9376  C C   . ARG F  1 128 ? 15.030  18.303  -13.192 1.00 30.41  ? 120 ARG F C   1 
ATOM   9377  O O   . ARG F  1 128 ? 14.454  17.525  -12.431 1.00 29.17  ? 120 ARG F O   1 
ATOM   9378  C CB  . ARG F  1 128 ? 17.518  18.026  -12.873 1.00 31.30  ? 120 ARG F CB  1 
ATOM   9379  C CG  . ARG F  1 128 ? 18.797  18.646  -13.461 1.00 37.63  ? 120 ARG F CG  1 
ATOM   9380  C CD  . ARG F  1 128 ? 19.641  17.615  -14.239 1.00 52.41  ? 120 ARG F CD  1 
ATOM   9381  N NE  . ARG F  1 128 ? 20.693  16.999  -13.421 1.00 70.20  ? 120 ARG F NE  1 
ATOM   9382  C CZ  . ARG F  1 128 ? 21.426  15.946  -13.792 1.00 71.46  ? 120 ARG F CZ  1 
ATOM   9383  N NH1 . ARG F  1 128 ? 21.227  15.364  -14.970 1.00 55.45  ? 120 ARG F NH1 1 
ATOM   9384  N NH2 . ARG F  1 128 ? 22.361  15.466  -12.978 1.00 69.74  ? 120 ARG F NH2 1 
ATOM   9385  N N   . PHE F  1 129 ? 14.575  18.585  -14.411 1.00 36.31  ? 121 PHE F N   1 
ATOM   9386  C CA  . PHE F  1 129 ? 13.361  17.968  -14.956 1.00 32.80  ? 121 PHE F CA  1 
ATOM   9387  C C   . PHE F  1 129 ? 13.625  17.163  -16.219 1.00 32.13  ? 121 PHE F C   1 
ATOM   9388  O O   . PHE F  1 129 ? 14.593  17.407  -16.929 1.00 30.56  ? 121 PHE F O   1 
ATOM   9389  C CB  . PHE F  1 129 ? 12.306  19.028  -15.253 1.00 26.52  ? 121 PHE F CB  1 
ATOM   9390  C CG  . PHE F  1 129 ? 11.783  19.688  -14.038 1.00 29.35  ? 121 PHE F CG  1 
ATOM   9391  C CD1 . PHE F  1 129 ? 12.237  20.943  -13.662 1.00 28.44  ? 121 PHE F CD1 1 
ATOM   9392  C CD2 . PHE F  1 129 ? 10.854  19.037  -13.235 1.00 30.80  ? 121 PHE F CD2 1 
ATOM   9393  C CE1 . PHE F  1 129 ? 11.749  21.548  -12.517 1.00 29.11  ? 121 PHE F CE1 1 
ATOM   9394  C CE2 . PHE F  1 129 ? 10.367  19.630  -12.096 1.00 22.75  ? 121 PHE F CE2 1 
ATOM   9395  C CZ  . PHE F  1 129 ? 10.810  20.886  -11.735 1.00 25.50  ? 121 PHE F CZ  1 
ATOM   9396  N N   . SER F  1 130 ? 12.747  16.204  -16.489 1.00 33.59  ? 122 SER F N   1 
ATOM   9397  C CA  . SER F  1 130 ? 12.810  15.415  -17.712 1.00 35.73  ? 122 SER F CA  1 
ATOM   9398  C C   . SER F  1 130 ? 11.652  15.819  -18.619 1.00 34.23  ? 122 SER F C   1 
ATOM   9399  O O   . SER F  1 130 ? 10.492  15.612  -18.271 1.00 35.67  ? 122 SER F O   1 
ATOM   9400  C CB  . SER F  1 130 ? 12.746  13.922  -17.386 1.00 29.72  ? 122 SER F CB  1 
ATOM   9401  O OG  . SER F  1 130 ? 11.521  13.356  -17.807 1.00 29.53  ? 122 SER F OG  1 
ATOM   9402  N N   . CYS F  1 131 ? 11.969  16.388  -19.782 1.00 42.10  ? 123 CYS F N   1 
ATOM   9403  C CA  . CYS F  1 131 ? 10.948  16.983  -20.655 1.00 47.57  ? 123 CYS F CA  1 
ATOM   9404  C C   . CYS F  1 131 ? 11.381  17.195  -22.118 1.00 46.64  ? 123 CYS F C   1 
ATOM   9405  O O   . CYS F  1 131 ? 12.523  16.916  -22.493 1.00 42.12  ? 123 CYS F O   1 
ATOM   9406  C CB  . CYS F  1 131 ? 10.512  18.314  -20.064 1.00 44.01  ? 123 CYS F CB  1 
ATOM   9407  S SG  . CYS F  1 131 ? 11.928  19.323  -19.632 1.00 64.63  ? 123 CYS F SG  1 
ATOM   9408  N N   . ASP F  1 132 ? 10.458  17.709  -22.932 1.00 47.82  ? 124 ASP F N   1 
ATOM   9409  C CA  . ASP F  1 132 ? 10.711  17.948  -24.358 1.00 45.92  ? 124 ASP F CA  1 
ATOM   9410  C C   . ASP F  1 132 ? 11.628  19.144  -24.631 1.00 43.09  ? 124 ASP F C   1 
ATOM   9411  O O   . ASP F  1 132 ? 11.201  20.301  -24.601 1.00 41.26  ? 124 ASP F O   1 
ATOM   9412  C CB  . ASP F  1 132 ? 9.393   18.136  -25.114 1.00 45.42  ? 124 ASP F CB  1 
ATOM   9413  C CG  . ASP F  1 132 ? 9.603   18.453  -26.578 1.00 40.07  ? 124 ASP F CG  1 
ATOM   9414  O OD1 . ASP F  1 132 ? 9.753   17.499  -27.372 1.00 35.95  ? 124 ASP F OD1 1 
ATOM   9415  O OD2 . ASP F  1 132 ? 9.622   19.656  -26.925 1.00 39.85  ? 124 ASP F OD2 1 
ATOM   9416  N N   . VAL F  1 133 ? 12.889  18.860  -24.919 1.00 42.50  ? 125 VAL F N   1 
ATOM   9417  C CA  . VAL F  1 133 ? 13.838  19.923  -25.210 1.00 50.35  ? 125 VAL F CA  1 
ATOM   9418  C C   . VAL F  1 133 ? 14.050  20.141  -26.727 1.00 48.17  ? 125 VAL F C   1 
ATOM   9419  O O   . VAL F  1 133 ? 14.589  21.170  -27.137 1.00 47.68  ? 125 VAL F O   1 
ATOM   9420  C CB  . VAL F  1 133 ? 15.191  19.678  -24.493 1.00 48.25  ? 125 VAL F CB  1 
ATOM   9421  C CG1 . VAL F  1 133 ? 15.996  20.937  -24.471 1.00 40.41  ? 125 VAL F CG1 1 
ATOM   9422  C CG2 . VAL F  1 133 ? 14.954  19.219  -23.073 1.00 45.98  ? 125 VAL F CG2 1 
ATOM   9423  N N   . SER F  1 134 ? 13.612  19.193  -27.557 1.00 46.03  ? 126 SER F N   1 
ATOM   9424  C CA  . SER F  1 134 ? 13.775  19.326  -29.012 1.00 47.98  ? 126 SER F CA  1 
ATOM   9425  C C   . SER F  1 134 ? 13.156  20.624  -29.551 1.00 43.60  ? 126 SER F C   1 
ATOM   9426  O O   . SER F  1 134 ? 12.006  20.955  -29.254 1.00 39.44  ? 126 SER F O   1 
ATOM   9427  C CB  . SER F  1 134 ? 13.215  18.103  -29.759 1.00 46.63  ? 126 SER F CB  1 
ATOM   9428  O OG  . SER F  1 134 ? 11.818  18.223  -30.001 1.00 43.55  ? 126 SER F OG  1 
ATOM   9429  N N   . GLY F  1 135 ? 13.939  21.360  -30.332 1.00 39.63  ? 127 GLY F N   1 
ATOM   9430  C CA  . GLY F  1 135 ? 13.482  22.612  -30.905 1.00 43.23  ? 127 GLY F CA  1 
ATOM   9431  C C   . GLY F  1 135 ? 14.050  23.806  -30.173 1.00 45.26  ? 127 GLY F C   1 
ATOM   9432  O O   . GLY F  1 135 ? 13.696  24.949  -30.451 1.00 46.51  ? 127 GLY F O   1 
ATOM   9433  N N   . VAL F  1 136 ? 14.951  23.523  -29.239 1.00 52.80  ? 128 VAL F N   1 
ATOM   9434  C CA  . VAL F  1 136 ? 15.534  24.527  -28.350 1.00 47.21  ? 128 VAL F CA  1 
ATOM   9435  C C   . VAL F  1 136 ? 16.444  25.522  -29.079 1.00 49.16  ? 128 VAL F C   1 
ATOM   9436  O O   . VAL F  1 136 ? 16.537  26.695  -28.695 1.00 43.00  ? 128 VAL F O   1 
ATOM   9437  C CB  . VAL F  1 136 ? 16.308  23.834  -27.192 1.00 48.92  ? 128 VAL F CB  1 
ATOM   9438  C CG1 . VAL F  1 136 ? 17.447  22.956  -27.736 1.00 43.98  ? 128 VAL F CG1 1 
ATOM   9439  C CG2 . VAL F  1 136 ? 16.805  24.850  -26.154 1.00 41.12  ? 128 VAL F CG2 1 
ATOM   9440  N N   . ASP F  1 137 ? 17.099  25.052  -30.139 1.00 55.11  ? 129 ASP F N   1 
ATOM   9441  C CA  . ASP F  1 137 ? 18.034  25.882  -30.893 1.00 52.53  ? 129 ASP F CA  1 
ATOM   9442  C C   . ASP F  1 137 ? 17.353  26.723  -31.977 1.00 51.06  ? 129 ASP F C   1 
ATOM   9443  O O   . ASP F  1 137 ? 17.931  27.697  -32.462 1.00 52.71  ? 129 ASP F O   1 
ATOM   9444  C CB  . ASP F  1 137 ? 19.143  25.020  -31.497 1.00 55.12  ? 129 ASP F CB  1 
ATOM   9445  C CG  . ASP F  1 137 ? 19.992  24.329  -30.436 1.00 59.12  ? 129 ASP F CG  1 
ATOM   9446  O OD1 . ASP F  1 137 ? 20.375  24.996  -29.454 1.00 55.92  ? 129 ASP F OD1 1 
ATOM   9447  O OD2 . ASP F  1 137 ? 20.274  23.118  -30.582 1.00 63.95  ? 129 ASP F OD2 1 
ATOM   9448  N N   . THR F  1 138 ? 16.133  26.282  -32.291 1.00 50.10  ? 130 THR F N   1 
ATOM   9449  C CA  . THR F  1 138 ? 15.174  26.892  -33.209 1.00 50.51  ? 130 THR F CA  1 
ATOM   9450  C C   . THR F  1 138 ? 14.359  28.027  -32.584 1.00 51.06  ? 130 THR F C   1 
ATOM   9451  O O   . THR F  1 138 ? 14.448  28.295  -31.386 1.00 54.10  ? 130 THR F O   1 
ATOM   9452  C CB  . THR F  1 138 ? 14.204  25.843  -33.785 1.00 49.48  ? 130 THR F CB  1 
ATOM   9453  O OG1 . THR F  1 138 ? 13.136  25.615  -32.857 1.00 51.58  ? 130 THR F OG1 1 
ATOM   9454  C CG2 . THR F  1 138 ? 14.931  24.533  -34.047 1.00 39.08  ? 130 THR F CG2 1 
ATOM   9455  N N   . GLU F  1 139 ? 13.579  28.693  -33.429 1.00 48.68  ? 131 GLU F N   1 
ATOM   9456  C CA  . GLU F  1 139 ? 12.931  29.962  -33.117 1.00 49.70  ? 131 GLU F CA  1 
ATOM   9457  C C   . GLU F  1 139 ? 11.536  29.765  -32.552 1.00 54.26  ? 131 GLU F C   1 
ATOM   9458  O O   . GLU F  1 139 ? 11.027  30.619  -31.817 1.00 52.17  ? 131 GLU F O   1 
ATOM   9459  C CB  . GLU F  1 139 ? 12.862  30.857  -34.351 1.00 52.10  ? 131 GLU F CB  1 
ATOM   9460  C CG  . GLU F  1 139 ? 14.078  31.750  -34.544 1.00 66.30  ? 131 GLU F CG  1 
ATOM   9461  C CD  . GLU F  1 139 ? 13.696  33.183  -34.907 1.00 77.82  ? 131 GLU F CD  1 
ATOM   9462  O OE1 . GLU F  1 139 ? 12.674  33.688  -34.375 1.00 62.77  ? 131 GLU F OE1 1 
ATOM   9463  O OE2 . GLU F  1 139 ? 14.416  33.799  -35.728 1.00 72.44  ? 131 GLU F OE2 1 
ATOM   9464  N N   . SER F  1 140 ? 10.910  28.646  -32.909 1.00 52.41  ? 132 SER F N   1 
ATOM   9465  C CA  . SER F  1 140 ? 9.627   28.286  -32.318 1.00 49.85  ? 132 SER F CA  1 
ATOM   9466  C C   . SER F  1 140 ? 9.883   27.864  -30.873 1.00 52.49  ? 132 SER F C   1 
ATOM   9467  O O   . SER F  1 140 ? 9.041   28.057  -29.993 1.00 45.83  ? 132 SER F O   1 
ATOM   9468  C CB  . SER F  1 140 ? 8.928   27.176  -33.119 1.00 43.12  ? 132 SER F CB  1 
ATOM   9469  O OG  . SER F  1 140 ? 9.759   26.040  -33.287 1.00 46.73  ? 132 SER F OG  1 
ATOM   9470  N N   . GLY F  1 141 ? 11.067  27.299  -30.642 1.00 52.49  ? 133 GLY F N   1 
ATOM   9471  C CA  . GLY F  1 141 ? 11.516  26.953  -29.309 1.00 46.07  ? 133 GLY F CA  1 
ATOM   9472  C C   . GLY F  1 141 ? 10.879  25.691  -28.761 1.00 48.84  ? 133 GLY F C   1 
ATOM   9473  O O   . GLY F  1 141 ? 9.737   25.359  -29.091 1.00 49.42  ? 133 GLY F O   1 
ATOM   9474  N N   . ALA F  1 142 ? 11.627  24.991  -27.912 1.00 47.94  ? 134 ALA F N   1 
ATOM   9475  C CA  . ALA F  1 142 ? 11.125  23.823  -27.198 1.00 46.93  ? 134 ALA F CA  1 
ATOM   9476  C C   . ALA F  1 142 ? 10.055  24.224  -26.188 1.00 40.52  ? 134 ALA F C   1 
ATOM   9477  O O   . ALA F  1 142 ? 10.031  25.359  -25.710 1.00 40.56  ? 134 ALA F O   1 
ATOM   9478  C CB  . ALA F  1 142 ? 12.264  23.122  -26.489 1.00 45.09  ? 134 ALA F CB  1 
ATOM   9479  N N   . THR F  1 143 ? 9.165   23.294  -25.872 1.00 36.30  ? 135 THR F N   1 
ATOM   9480  C CA  . THR F  1 143 ? 8.205   23.529  -24.805 1.00 46.30  ? 135 THR F CA  1 
ATOM   9481  C C   . THR F  1 143 ? 8.245   22.398  -23.787 1.00 49.85  ? 135 THR F C   1 
ATOM   9482  O O   . THR F  1 143 ? 7.664   21.325  -23.999 1.00 46.37  ? 135 THR F O   1 
ATOM   9483  C CB  . THR F  1 143 ? 6.768   23.687  -25.332 1.00 49.27  ? 135 THR F CB  1 
ATOM   9484  O OG1 . THR F  1 143 ? 6.700   24.816  -26.211 1.00 52.90  ? 135 THR F OG1 1 
ATOM   9485  C CG2 . THR F  1 143 ? 5.802   23.910  -24.171 1.00 45.39  ? 135 THR F CG2 1 
ATOM   9486  N N   . CYS F  1 144 ? 8.943   22.630  -22.682 1.00 43.64  ? 136 CYS F N   1 
ATOM   9487  C CA  . CYS F  1 144 ? 8.932   21.648  -21.610 1.00 52.65  ? 136 CYS F CA  1 
ATOM   9488  C C   . CYS F  1 144 ? 7.743   21.882  -20.674 1.00 45.66  ? 136 CYS F C   1 
ATOM   9489  O O   . CYS F  1 144 ? 7.480   23.007  -20.240 1.00 43.05  ? 136 CYS F O   1 
ATOM   9490  C CB  . CYS F  1 144 ? 10.247  21.638  -20.827 1.00 47.83  ? 136 CYS F CB  1 
ATOM   9491  S SG  . CYS F  1 144 ? 10.098  20.775  -19.232 1.00 68.13  ? 136 CYS F SG  1 
ATOM   9492  N N   . ARG F  1 145 ? 7.023   20.807  -20.380 1.00 41.58  ? 137 ARG F N   1 
ATOM   9493  C CA  . ARG F  1 145 ? 5.868   20.889  -19.505 1.00 45.87  ? 137 ARG F CA  1 
ATOM   9494  C C   . ARG F  1 145 ? 6.131   20.186  -18.172 1.00 42.07  ? 137 ARG F C   1 
ATOM   9495  O O   . ARG F  1 145 ? 6.422   18.982  -18.137 1.00 37.28  ? 137 ARG F O   1 
ATOM   9496  C CB  . ARG F  1 145 ? 4.634   20.314  -20.212 1.00 47.61  ? 137 ARG F CB  1 
ATOM   9497  C CG  . ARG F  1 145 ? 4.300   21.056  -21.495 1.00 49.39  ? 137 ARG F CG  1 
ATOM   9498  C CD  . ARG F  1 145 ? 3.163   20.426  -22.286 1.00 54.45  ? 137 ARG F CD  1 
ATOM   9499  N NE  . ARG F  1 145 ? 3.014   21.066  -23.598 1.00 60.72  ? 137 ARG F NE  1 
ATOM   9500  C CZ  . ARG F  1 145 ? 2.208   22.096  -23.849 1.00 58.53  ? 137 ARG F CZ  1 
ATOM   9501  N NH1 . ARG F  1 145 ? 1.461   22.609  -22.883 1.00 64.33  ? 137 ARG F NH1 1 
ATOM   9502  N NH2 . ARG F  1 145 ? 2.142   22.614  -25.067 1.00 52.07  ? 137 ARG F NH2 1 
ATOM   9503  N N   . ILE F  1 146 ? 6.047   20.964  -17.090 1.00 43.34  ? 138 ILE F N   1 
ATOM   9504  C CA  . ILE F  1 146 ? 6.132   20.454  -15.714 1.00 43.76  ? 138 ILE F CA  1 
ATOM   9505  C C   . ILE F  1 146 ? 4.757   20.389  -15.048 1.00 33.29  ? 138 ILE F C   1 
ATOM   9506  O O   . ILE F  1 146 ? 4.003   21.365  -15.047 1.00 25.72  ? 138 ILE F O   1 
ATOM   9507  C CB  . ILE F  1 146 ? 6.998   21.358  -14.830 1.00 38.40  ? 138 ILE F CB  1 
ATOM   9508  C CG1 . ILE F  1 146 ? 8.421   21.444  -15.359 1.00 28.34  ? 138 ILE F CG1 1 
ATOM   9509  C CG2 . ILE F  1 146 ? 7.006   20.846  -13.397 1.00 33.29  ? 138 ILE F CG2 1 
ATOM   9510  C CD1 . ILE F  1 146 ? 9.227   22.472  -14.626 1.00 28.88  ? 138 ILE F CD1 1 
ATOM   9511  N N   . LYS F  1 147 ? 4.445   19.239  -14.466 1.00 38.14  ? 139 LYS F N   1 
ATOM   9512  C CA  . LYS F  1 147 ? 3.156   19.033  -13.813 1.00 38.60  ? 139 LYS F CA  1 
ATOM   9513  C C   . LYS F  1 147 ? 3.328   18.915  -12.292 1.00 36.21  ? 139 LYS F C   1 
ATOM   9514  O O   . LYS F  1 147 ? 3.903   17.937  -11.795 1.00 34.62  ? 139 LYS F O   1 
ATOM   9515  C CB  . LYS F  1 147 ? 2.506   17.781  -14.396 1.00 38.71  ? 139 LYS F CB  1 
ATOM   9516  C CG  . LYS F  1 147 ? 3.172   17.357  -15.707 1.00 56.43  ? 139 LYS F CG  1 
ATOM   9517  C CD  . LYS F  1 147 ? 2.450   16.208  -16.399 1.00 73.48  ? 139 LYS F CD  1 
ATOM   9518  C CE  . LYS F  1 147 ? 3.077   15.893  -17.761 1.00 60.92  ? 139 LYS F CE  1 
ATOM   9519  N NZ  . LYS F  1 147 ? 4.532   15.595  -17.651 1.00 45.90  ? 139 LYS F NZ  1 
ATOM   9520  N N   . ILE F  1 148 ? 2.851   19.917  -11.553 1.00 31.98  ? 140 ILE F N   1 
ATOM   9521  C CA  . ILE F  1 148 ? 2.985   19.907  -10.089 1.00 33.75  ? 140 ILE F CA  1 
ATOM   9522  C C   . ILE F  1 148 ? 1.676   19.595  -9.347  1.00 30.90  ? 140 ILE F C   1 
ATOM   9523  O O   . ILE F  1 148 ? 0.711   20.347  -9.445  1.00 33.70  ? 140 ILE F O   1 
ATOM   9524  C CB  . ILE F  1 148 ? 3.528   21.246  -9.556  1.00 28.16  ? 140 ILE F CB  1 
ATOM   9525  C CG1 . ILE F  1 148 ? 4.979   21.446  -9.960  1.00 29.33  ? 140 ILE F CG1 1 
ATOM   9526  C CG2 . ILE F  1 148 ? 3.446   21.281  -8.050  1.00 27.68  ? 140 ILE F CG2 1 
ATOM   9527  C CD1 . ILE F  1 148 ? 5.621   22.641  -9.298  1.00 30.31  ? 140 ILE F CD1 1 
ATOM   9528  N N   . GLY F  1 149 ? 1.654   18.500  -8.592  1.00 28.49  ? 141 GLY F N   1 
ATOM   9529  C CA  . GLY F  1 149 ? 0.471   18.126  -7.832  1.00 28.06  ? 141 GLY F CA  1 
ATOM   9530  C C   . GLY F  1 149 ? 0.717   17.685  -6.395  1.00 28.70  ? 141 GLY F C   1 
ATOM   9531  O O   . GLY F  1 149 ? 1.859   17.482  -5.962  1.00 25.10  ? 141 GLY F O   1 
ATOM   9532  N N   . SER F  1 150 ? -0.360  17.536  -5.633  1.00 25.14  ? 142 SER F N   1 
ATOM   9533  C CA  . SER F  1 150 ? -0.227  16.931  -4.321  1.00 17.70  ? 142 SER F CA  1 
ATOM   9534  C C   . SER F  1 150 ? 0.168   15.465  -4.483  1.00 20.86  ? 142 SER F C   1 
ATOM   9535  O O   . SER F  1 150 ? -0.358  14.754  -5.344  1.00 23.27  ? 142 SER F O   1 
ATOM   9536  C CB  . SER F  1 150 ? -1.522  17.049  -3.528  1.00 21.98  ? 142 SER F CB  1 
ATOM   9537  O OG  . SER F  1 150 ? -1.400  16.404  -2.269  1.00 25.48  ? 142 SER F OG  1 
ATOM   9538  N N   . TRP F  1 151 ? 1.102   15.009  -3.660  1.00 18.12  ? 143 TRP F N   1 
ATOM   9539  C CA  . TRP F  1 151 ? 1.555   13.631  -3.753  1.00 17.02  ? 143 TRP F CA  1 
ATOM   9540  C C   . TRP F  1 151 ? 0.587   12.629  -3.116  1.00 20.83  ? 143 TRP F C   1 
ATOM   9541  O O   . TRP F  1 151 ? 0.319   11.584  -3.699  1.00 19.30  ? 143 TRP F O   1 
ATOM   9542  C CB  . TRP F  1 151 ? 2.962   13.483  -3.174  1.00 13.62  ? 143 TRP F CB  1 
ATOM   9543  C CG  . TRP F  1 151 ? 3.540   12.136  -3.372  1.00 16.55  ? 143 TRP F CG  1 
ATOM   9544  C CD1 . TRP F  1 151 ? 3.996   11.284  -2.407  1.00 18.19  ? 143 TRP F CD1 1 
ATOM   9545  C CD2 . TRP F  1 151 ? 3.739   11.466  -4.622  1.00 22.55  ? 143 TRP F CD2 1 
ATOM   9546  N NE1 . TRP F  1 151 ? 4.474   10.127  -2.978  1.00 17.09  ? 143 TRP F NE1 1 
ATOM   9547  C CE2 . TRP F  1 151 ? 4.320   10.211  -4.337  1.00 17.94  ? 143 TRP F CE2 1 
ATOM   9548  C CE3 . TRP F  1 151 ? 3.483   11.804  -5.956  1.00 23.11  ? 143 TRP F CE3 1 
ATOM   9549  C CZ2 . TRP F  1 151 ? 4.640   9.298   -5.332  1.00 21.48  ? 143 TRP F CZ2 1 
ATOM   9550  C CZ3 . TRP F  1 151 ? 3.807   10.895  -6.945  1.00 24.44  ? 143 TRP F CZ3 1 
ATOM   9551  C CH2 . TRP F  1 151 ? 4.380   9.656   -6.628  1.00 25.26  ? 143 TRP F CH2 1 
ATOM   9552  N N   . THR F  1 152 ? 0.049   12.945  -1.934  1.00 21.43  ? 144 THR F N   1 
ATOM   9553  C CA  . THR F  1 152 ? -0.730  11.951  -1.182  1.00 16.73  ? 144 THR F CA  1 
ATOM   9554  C C   . THR F  1 152 ? -2.227  12.252  -1.085  1.00 14.94  ? 144 THR F C   1 
ATOM   9555  O O   . THR F  1 152 ? -3.048  11.356  -0.947  1.00 17.16  ? 144 THR F O   1 
ATOM   9556  C CB  . THR F  1 152 ? -0.114  11.705  0.217   1.00 15.14  ? 144 THR F CB  1 
ATOM   9557  O OG1 . THR F  1 152 ? -0.148  12.911  0.995   1.00 17.21  ? 144 THR F OG1 1 
ATOM   9558  C CG2 . THR F  1 152 ? 1.329   11.261  0.071   1.00 14.91  ? 144 THR F CG2 1 
ATOM   9559  N N   . HIS F  1 153 ? -2.585  13.517  -1.189  1.00 16.49  ? 145 HIS F N   1 
ATOM   9560  C CA  . HIS F  1 153 ? -3.969  13.910  -1.029  1.00 19.30  ? 145 HIS F CA  1 
ATOM   9561  C C   . HIS F  1 153 ? -4.692  14.048  -2.362  1.00 23.06  ? 145 HIS F C   1 
ATOM   9562  O O   . HIS F  1 153 ? -4.331  14.890  -3.181  1.00 26.28  ? 145 HIS F O   1 
ATOM   9563  C CB  . HIS F  1 153 ? -4.027  15.219  -0.241  1.00 22.74  ? 145 HIS F CB  1 
ATOM   9564  C CG  . HIS F  1 153 ? -3.354  15.130  1.092   1.00 22.87  ? 145 HIS F CG  1 
ATOM   9565  N ND1 . HIS F  1 153 ? -1.994  15.295  1.250   1.00 18.77  ? 145 HIS F ND1 1 
ATOM   9566  C CD2 . HIS F  1 153 ? -3.842  14.833  2.321   1.00 24.85  ? 145 HIS F CD2 1 
ATOM   9567  C CE1 . HIS F  1 153 ? -1.680  15.125  2.521   1.00 24.46  ? 145 HIS F CE1 1 
ATOM   9568  N NE2 . HIS F  1 153 ? -2.785  14.849  3.195   1.00 22.83  ? 145 HIS F NE2 1 
ATOM   9569  N N   . HIS F  1 154 ? -5.713  13.221  -2.579  1.00 25.12  ? 146 HIS F N   1 
ATOM   9570  C CA  . HIS F  1 154 ? -6.509  13.316  -3.801  1.00 25.86  ? 146 HIS F CA  1 
ATOM   9571  C C   . HIS F  1 154 ? -7.393  14.561  -3.830  1.00 27.51  ? 146 HIS F C   1 
ATOM   9572  O O   . HIS F  1 154 ? -7.303  15.416  -2.949  1.00 25.30  ? 146 HIS F O   1 
ATOM   9573  C CB  . HIS F  1 154 ? -7.310  12.036  -4.079  1.00 30.19  ? 146 HIS F CB  1 
ATOM   9574  C CG  . HIS F  1 154 ? -7.969  11.442  -2.871  1.00 34.64  ? 146 HIS F CG  1 
ATOM   9575  N ND1 . HIS F  1 154 ? -8.941  12.102  -2.148  1.00 41.29  ? 146 HIS F ND1 1 
ATOM   9576  C CD2 . HIS F  1 154 ? -7.815  10.233  -2.278  1.00 37.46  ? 146 HIS F CD2 1 
ATOM   9577  C CE1 . HIS F  1 154 ? -9.348  11.332  -1.153  1.00 39.15  ? 146 HIS F CE1 1 
ATOM   9578  N NE2 . HIS F  1 154 ? -8.677  10.195  -1.205  1.00 41.16  ? 146 HIS F NE2 1 
ATOM   9579  N N   . SER F  1 155 ? -8.231  14.664  -4.856  1.00 29.75  ? 147 SER F N   1 
ATOM   9580  C CA  . SER F  1 155 ? -8.993  15.884  -5.137  1.00 29.15  ? 147 SER F CA  1 
ATOM   9581  C C   . SER F  1 155 ? -10.014 16.256  -4.065  1.00 29.78  ? 147 SER F C   1 
ATOM   9582  O O   . SER F  1 155 ? -10.318 17.434  -3.877  1.00 27.91  ? 147 SER F O   1 
ATOM   9583  C CB  . SER F  1 155 ? -9.701  15.763  -6.488  1.00 37.50  ? 147 SER F CB  1 
ATOM   9584  O OG  . SER F  1 155 ? -10.688 14.737  -6.451  1.00 44.61  ? 147 SER F OG  1 
ATOM   9585  N N   . ARG F  1 156 ? -10.559 15.261  -3.375  1.00 27.31  ? 148 ARG F N   1 
ATOM   9586  C CA  . ARG F  1 156 ? -11.444 15.545  -2.257  1.00 28.58  ? 148 ARG F CA  1 
ATOM   9587  C C   . ARG F  1 156 ? -10.713 16.315  -1.139  1.00 31.47  ? 148 ARG F C   1 
ATOM   9588  O O   . ARG F  1 156 ? -11.310 17.166  -0.486  1.00 33.39  ? 148 ARG F O   1 
ATOM   9589  C CB  . ARG F  1 156 ? -12.061 14.253  -1.698  1.00 42.67  ? 148 ARG F CB  1 
ATOM   9590  C CG  . ARG F  1 156 ? -12.948 13.449  -2.670  1.00 43.11  ? 148 ARG F CG  1 
ATOM   9591  C CD  . ARG F  1 156 ? -13.667 12.303  -1.936  1.00 46.95  ? 148 ARG F CD  1 
ATOM   9592  N NE  . ARG F  1 156 ? -14.154 11.265  -2.841  1.00 49.37  ? 148 ARG F NE  1 
ATOM   9593  C CZ  . ARG F  1 156 ? -15.377 11.228  -3.373  1.00 61.08  ? 148 ARG F CZ  1 
ATOM   9594  N NH1 . ARG F  1 156 ? -16.266 12.180  -3.096  1.00 48.98  ? 148 ARG F NH1 1 
ATOM   9595  N NH2 . ARG F  1 156 ? -15.713 10.231  -4.190  1.00 57.09  ? 148 ARG F NH2 1 
ATOM   9596  N N   . GLU F  1 157 ? -9.428  16.016  -0.925  1.00 29.45  ? 149 GLU F N   1 
ATOM   9597  C CA  . GLU F  1 157 ? -8.629  16.661  0.130   1.00 22.92  ? 149 GLU F CA  1 
ATOM   9598  C C   . GLU F  1 157 ? -7.935  17.960  -0.295  1.00 26.17  ? 149 GLU F C   1 
ATOM   9599  O O   . GLU F  1 157 ? -7.991  18.956  0.438   1.00 25.71  ? 149 GLU F O   1 
ATOM   9600  C CB  . GLU F  1 157 ? -7.590  15.689  0.723   1.00 19.00  ? 149 GLU F CB  1 
ATOM   9601  C CG  . GLU F  1 157 ? -7.754  14.246  0.279   1.00 24.97  ? 149 GLU F CG  1 
ATOM   9602  C CD  . GLU F  1 157 ? -7.535  13.240  1.397   1.00 28.46  ? 149 GLU F CD  1 
ATOM   9603  O OE1 . GLU F  1 157 ? -8.473  13.018  2.204   1.00 33.19  ? 149 GLU F OE1 1 
ATOM   9604  O OE2 . GLU F  1 157 ? -6.431  12.658  1.461   1.00 24.52  ? 149 GLU F OE2 1 
ATOM   9605  N N   . ILE F  1 158 ? -7.273  17.948  -1.458  1.00 27.90  ? 150 ILE F N   1 
ATOM   9606  C CA  . ILE F  1 158 ? -6.517  19.120  -1.935  1.00 26.35  ? 150 ILE F CA  1 
ATOM   9607  C C   . ILE F  1 158 ? -6.768  19.504  -3.395  1.00 28.85  ? 150 ILE F C   1 
ATOM   9608  O O   . ILE F  1 158 ? -6.670  18.671  -4.303  1.00 27.48  ? 150 ILE F O   1 
ATOM   9609  C CB  . ILE F  1 158 ? -4.986  18.960  -1.738  1.00 23.81  ? 150 ILE F CB  1 
ATOM   9610  C CG1 . ILE F  1 158 ? -4.643  18.763  -0.260  1.00 26.53  ? 150 ILE F CG1 1 
ATOM   9611  C CG2 . ILE F  1 158 ? -4.261  20.190  -2.247  1.00 24.97  ? 150 ILE F CG2 1 
ATOM   9612  C CD1 . ILE F  1 158 ? -3.176  18.823  0.034   1.00 18.18  ? 150 ILE F CD1 1 
ATOM   9613  N N   . SER F  1 159 ? -7.080  20.780  -3.614  1.00 29.48  ? 151 SER F N   1 
ATOM   9614  C CA  . SER F  1 159 ? -7.220  21.301  -4.967  1.00 33.11  ? 151 SER F CA  1 
ATOM   9615  C C   . SER F  1 159 ? -6.182  22.395  -5.282  1.00 36.25  ? 151 SER F C   1 
ATOM   9616  O O   . SER F  1 159 ? -5.991  23.332  -4.500  1.00 31.14  ? 151 SER F O   1 
ATOM   9617  C CB  . SER F  1 159 ? -8.653  21.796  -5.220  1.00 35.88  ? 151 SER F CB  1 
ATOM   9618  O OG  . SER F  1 159 ? -8.881  23.087  -4.684  1.00 36.46  ? 151 SER F OG  1 
ATOM   9619  N N   . VAL F  1 160 ? -5.513  22.248  -6.430  1.00 40.09  ? 152 VAL F N   1 
ATOM   9620  C CA  . VAL F  1 160 ? -4.507  23.200  -6.915  1.00 37.68  ? 152 VAL F CA  1 
ATOM   9621  C C   . VAL F  1 160 ? -5.045  24.114  -8.023  1.00 38.39  ? 152 VAL F C   1 
ATOM   9622  O O   . VAL F  1 160 ? -5.862  23.715  -8.848  1.00 44.31  ? 152 VAL F O   1 
ATOM   9623  C CB  . VAL F  1 160 ? -3.300  22.471  -7.487  1.00 36.74  ? 152 VAL F CB  1 
ATOM   9624  C CG1 . VAL F  1 160 ? -2.574  21.695  -6.400  1.00 39.84  ? 152 VAL F CG1 1 
ATOM   9625  C CG2 . VAL F  1 160 ? -3.767  21.543  -8.572  1.00 38.95  ? 152 VAL F CG2 1 
ATOM   9626  N N   . ASP F  1 161 ? -4.578  25.352  -8.031  1.00 35.25  ? 153 ASP F N   1 
ATOM   9627  C CA  . ASP F  1 161 ? -5.041  26.349  -8.985  1.00 44.81  ? 153 ASP F CA  1 
ATOM   9628  C C   . ASP F  1 161 ? -3.892  27.314  -9.270  1.00 48.95  ? 153 ASP F C   1 
ATOM   9629  O O   . ASP F  1 161 ? -3.214  27.760  -8.347  1.00 47.57  ? 153 ASP F O   1 
ATOM   9630  C CB  . ASP F  1 161 ? -6.231  27.128  -8.412  1.00 44.84  ? 153 ASP F CB  1 
ATOM   9631  C CG  . ASP F  1 161 ? -7.286  26.224  -7.786  1.00 52.57  ? 153 ASP F CG  1 
ATOM   9632  O OD1 . ASP F  1 161 ? -7.950  25.491  -8.556  1.00 58.11  ? 153 ASP F OD1 1 
ATOM   9633  O OD2 . ASP F  1 161 ? -7.453  26.252  -6.534  1.00 42.50  ? 153 ASP F OD2 1 
ATOM   9634  N N   . PRO F  1 162 ? -3.657  27.632  -10.549 1.00 44.41  ? 154 PRO F N   1 
ATOM   9635  C CA  . PRO F  1 162 ? -2.587  28.570  -10.911 1.00 43.23  ? 154 PRO F CA  1 
ATOM   9636  C C   . PRO F  1 162 ? -2.932  30.024  -10.587 1.00 46.70  ? 154 PRO F C   1 
ATOM   9637  O O   . PRO F  1 162 ? -4.013  30.288  -10.066 1.00 42.94  ? 154 PRO F O   1 
ATOM   9638  C CB  . PRO F  1 162 ? -2.452  28.378  -12.420 1.00 55.84  ? 154 PRO F CB  1 
ATOM   9639  C CG  . PRO F  1 162 ? -3.779  27.840  -12.853 1.00 53.72  ? 154 PRO F CG  1 
ATOM   9640  C CD  . PRO F  1 162 ? -4.268  26.993  -11.723 1.00 43.76  ? 154 PRO F CD  1 
ATOM   9641  N N   . THR F  1 163 ? -2.017  30.939  -10.910 1.00 54.78  ? 155 THR F N   1 
ATOM   9642  C CA  . THR F  1 163 ? -2.140  32.369  -10.583 1.00 56.85  ? 155 THR F CA  1 
ATOM   9643  C C   . THR F  1 163 ? -2.571  32.617  -9.144  1.00 45.70  ? 155 THR F C   1 
ATOM   9644  O O   . THR F  1 163 ? -1.803  32.379  -8.219  1.00 48.40  ? 155 THR F O   1 
ATOM   9645  C CB  . THR F  1 163 ? -3.079  33.133  -11.549 1.00 57.14  ? 155 THR F CB  1 
ATOM   9646  O OG1 . THR F  1 163 ? -2.380  34.248  -12.116 1.00 57.00  ? 155 THR F OG1 1 
ATOM   9647  C CG2 . THR F  1 163 ? -4.313  33.652  -10.821 1.00 58.67  ? 155 THR F CG2 1 
ATOM   9648  N N   . GLU F  1 165 ? -0.741  32.827  -13.968 1.00 64.42  ? 157 GLU F N   1 
ATOM   9649  C CA  . GLU F  1 165 ? -1.555  32.629  -15.163 1.00 77.39  ? 157 GLU F CA  1 
ATOM   9650  C C   . GLU F  1 165 ? -0.732  32.843  -16.421 1.00 79.78  ? 157 GLU F C   1 
ATOM   9651  O O   . GLU F  1 165 ? 0.071   31.990  -16.810 1.00 73.90  ? 157 GLU F O   1 
ATOM   9652  C CB  . GLU F  1 165 ? -2.749  33.594  -15.187 1.00 83.52  ? 157 GLU F CB  1 
ATOM   9653  C CG  . GLU F  1 165 ? -4.102  32.987  -14.806 1.00 78.01  ? 157 GLU F CG  1 
ATOM   9654  C CD  . GLU F  1 165 ? -4.549  31.871  -15.735 1.00 81.93  ? 157 GLU F CD  1 
ATOM   9655  O OE1 . GLU F  1 165 ? -4.006  31.762  -16.857 1.00 76.17  ? 157 GLU F OE1 1 
ATOM   9656  O OE2 . GLU F  1 165 ? -5.450  31.101  -15.336 1.00 78.55  ? 157 GLU F OE2 1 
ATOM   9657  N N   . ASN F  1 166 ? -0.951  33.994  -17.054 1.00 83.80  ? 158 ASN F N   1 
ATOM   9658  C CA  . ASN F  1 166 ? -0.230  34.366  -18.266 1.00 86.15  ? 158 ASN F CA  1 
ATOM   9659  C C   . ASN F  1 166 ? 0.804   35.457  -17.997 1.00 88.93  ? 158 ASN F C   1 
ATOM   9660  O O   . ASN F  1 166 ? 0.516   36.465  -17.339 1.00 88.19  ? 158 ASN F O   1 
ATOM   9661  C CB  . ASN F  1 166 ? -1.196  34.800  -19.379 1.00 83.24  ? 158 ASN F CB  1 
ATOM   9662  C CG  . ASN F  1 166 ? -0.565  34.720  -20.768 1.00 83.74  ? 158 ASN F CG  1 
ATOM   9663  O OD1 . ASN F  1 166 ? -0.346  33.628  -21.298 1.00 79.15  ? 158 ASN F OD1 1 
ATOM   9664  N ND2 . ASN F  1 166 ? -0.277  35.878  -21.362 1.00 74.01  ? 158 ASN F ND2 1 
ATOM   9665  N N   . SER F  1 167 ? 2.047   35.126  -18.339 1.00 85.74  ? 159 SER F N   1 
ATOM   9666  C CA  . SER F  1 167 ? 3.208   35.994  -18.183 1.00 81.60  ? 159 SER F CA  1 
ATOM   9667  C C   . SER F  1 167 ? 4.358   35.375  -18.975 1.00 72.92  ? 159 SER F C   1 
ATOM   9668  O O   . SER F  1 167 ? 4.264   34.219  -19.387 1.00 70.21  ? 159 SER F O   1 
ATOM   9669  C CB  . SER F  1 167 ? 3.589   36.130  -16.709 1.00 79.61  ? 159 SER F CB  1 
ATOM   9670  O OG  . SER F  1 167 ? 4.556   37.149  -16.523 1.00 73.30  ? 159 SER F OG  1 
ATOM   9671  N N   . ASP F  1 168 ? 5.445   36.114  -19.180 1.00 72.64  ? 160 ASP F N   1 
ATOM   9672  C CA  . ASP F  1 168 ? 6.630   35.507  -19.777 1.00 70.96  ? 160 ASP F CA  1 
ATOM   9673  C C   . ASP F  1 168 ? 7.789   35.684  -18.805 1.00 68.32  ? 160 ASP F C   1 
ATOM   9674  O O   . ASP F  1 168 ? 8.963   35.557  -19.170 1.00 65.90  ? 160 ASP F O   1 
ATOM   9675  C CB  . ASP F  1 168 ? 6.950   36.113  -21.150 1.00 70.66  ? 160 ASP F CB  1 
ATOM   9676  C CG  . ASP F  1 168 ? 7.101   37.620  -21.106 1.00 71.26  ? 160 ASP F CG  1 
ATOM   9677  O OD1 . ASP F  1 168 ? 6.363   38.273  -20.334 1.00 70.08  ? 160 ASP F OD1 1 
ATOM   9678  O OD2 . ASP F  1 168 ? 7.961   38.145  -21.845 1.00 66.78  ? 160 ASP F OD2 1 
ATOM   9679  N N   . ASP F  1 169 ? 7.420   35.981  -17.560 1.00 66.15  ? 161 ASP F N   1 
ATOM   9680  C CA  . ASP F  1 169 ? 8.358   36.195  -16.466 1.00 64.44  ? 161 ASP F CA  1 
ATOM   9681  C C   . ASP F  1 169 ? 9.450   37.205  -16.814 1.00 60.41  ? 161 ASP F C   1 
ATOM   9682  O O   . ASP F  1 169 ? 10.611  37.027  -16.446 1.00 57.28  ? 161 ASP F O   1 
ATOM   9683  C CB  . ASP F  1 169 ? 8.941   34.861  -15.980 1.00 61.50  ? 161 ASP F CB  1 
ATOM   9684  C CG  . ASP F  1 169 ? 7.894   33.980  -15.299 1.00 57.81  ? 161 ASP F CG  1 
ATOM   9685  O OD1 . ASP F  1 169 ? 8.040   32.733  -15.320 1.00 44.95  ? 161 ASP F OD1 1 
ATOM   9686  O OD2 . ASP F  1 169 ? 6.919   34.545  -14.746 1.00 63.39  ? 161 ASP F OD2 1 
ATOM   9687  N N   . SER F  1 170 ? 9.057   38.265  -17.521 1.00 70.05  ? 162 SER F N   1 
ATOM   9688  C CA  . SER F  1 170 ? 9.965   39.357  -17.873 1.00 69.43  ? 162 SER F CA  1 
ATOM   9689  C C   . SER F  1 170 ? 10.528  39.966  -16.603 1.00 69.54  ? 162 SER F C   1 
ATOM   9690  O O   . SER F  1 170 ? 11.688  40.384  -16.549 1.00 67.62  ? 162 SER F O   1 
ATOM   9691  C CB  . SER F  1 170 ? 9.224   40.453  -18.645 1.00 59.55  ? 162 SER F CB  1 
ATOM   9692  O OG  . SER F  1 170 ? 8.597   39.945  -19.804 1.00 68.82  ? 162 SER F OG  1 
ATOM   9693  N N   . GLU F  1 171 ? 9.688   40.003  -15.578 1.00 59.25  ? 163 GLU F N   1 
ATOM   9694  C CA  . GLU F  1 171 ? 10.009  40.715  -14.360 1.00 59.72  ? 163 GLU F CA  1 
ATOM   9695  C C   . GLU F  1 171 ? 11.026  39.963  -13.515 1.00 59.04  ? 163 GLU F C   1 
ATOM   9696  O O   . GLU F  1 171 ? 11.688  40.551  -12.661 1.00 63.33  ? 163 GLU F O   1 
ATOM   9697  C CB  . GLU F  1 171 ? 8.726   40.960  -13.570 1.00 62.09  ? 163 GLU F CB  1 
ATOM   9698  C CG  . GLU F  1 171 ? 7.509   40.274  -14.188 1.00 68.10  ? 163 GLU F CG  1 
ATOM   9699  C CD  . GLU F  1 171 ? 6.235   40.532  -13.409 1.00 70.18  ? 163 GLU F CD  1 
ATOM   9700  O OE1 . GLU F  1 171 ? 5.273   39.745  -13.566 1.00 69.52  ? 163 GLU F OE1 1 
ATOM   9701  O OE2 . GLU F  1 171 ? 6.201   41.521  -12.643 1.00 64.03  ? 163 GLU F OE2 1 
ATOM   9702  N N   . TYR F  1 172 ? 11.164  38.665  -13.755 1.00 52.63  ? 164 TYR F N   1 
ATOM   9703  C CA  . TYR F  1 172 ? 11.927  37.832  -12.837 1.00 45.68  ? 164 TYR F CA  1 
ATOM   9704  C C   . TYR F  1 172 ? 13.084  37.080  -13.484 1.00 40.44  ? 164 TYR F C   1 
ATOM   9705  O O   . TYR F  1 172 ? 14.065  36.742  -12.816 1.00 36.33  ? 164 TYR F O   1 
ATOM   9706  C CB  . TYR F  1 172 ? 10.983  36.868  -12.108 1.00 48.31  ? 164 TYR F CB  1 
ATOM   9707  C CG  . TYR F  1 172 ? 9.918   37.589  -11.303 1.00 58.96  ? 164 TYR F CG  1 
ATOM   9708  C CD1 . TYR F  1 172 ? 8.629   37.073  -11.188 1.00 61.31  ? 164 TYR F CD1 1 
ATOM   9709  C CD2 . TYR F  1 172 ? 10.202  38.791  -10.663 1.00 54.33  ? 164 TYR F CD2 1 
ATOM   9710  C CE1 . TYR F  1 172 ? 7.655   37.734  -10.462 1.00 44.66  ? 164 TYR F CE1 1 
ATOM   9711  C CE2 . TYR F  1 172 ? 9.239   39.457  -9.943  1.00 54.20  ? 164 TYR F CE2 1 
ATOM   9712  C CZ  . TYR F  1 172 ? 7.970   38.928  -9.845  1.00 51.89  ? 164 TYR F CZ  1 
ATOM   9713  O OH  . TYR F  1 172 ? 7.021   39.610  -9.123  1.00 62.51  ? 164 TYR F OH  1 
ATOM   9714  N N   . PHE F  1 173 ? 12.977  36.828  -14.784 1.00 40.31  ? 165 PHE F N   1 
ATOM   9715  C CA  . PHE F  1 173 ? 14.003  36.063  -15.491 1.00 37.68  ? 165 PHE F CA  1 
ATOM   9716  C C   . PHE F  1 173 ? 15.354  36.792  -15.590 1.00 38.43  ? 165 PHE F C   1 
ATOM   9717  O O   . PHE F  1 173 ? 15.417  38.002  -15.842 1.00 37.39  ? 165 PHE F O   1 
ATOM   9718  C CB  . PHE F  1 173 ? 13.505  35.650  -16.879 1.00 38.22  ? 165 PHE F CB  1 
ATOM   9719  C CG  . PHE F  1 173 ? 14.098  34.362  -17.376 1.00 37.03  ? 165 PHE F CG  1 
ATOM   9720  C CD1 . PHE F  1 173 ? 13.784  33.157  -16.758 1.00 27.37  ? 165 PHE F CD1 1 
ATOM   9721  C CD2 . PHE F  1 173 ? 14.970  34.353  -18.463 1.00 36.24  ? 165 PHE F CD2 1 
ATOM   9722  C CE1 . PHE F  1 173 ? 14.328  31.958  -17.212 1.00 33.10  ? 165 PHE F CE1 1 
ATOM   9723  C CE2 . PHE F  1 173 ? 15.519  33.159  -18.928 1.00 34.25  ? 165 PHE F CE2 1 
ATOM   9724  C CZ  . PHE F  1 173 ? 15.200  31.958  -18.300 1.00 33.95  ? 165 PHE F CZ  1 
ATOM   9725  N N   . SER F  1 174 ? 16.430  36.039  -15.386 1.00 32.34  ? 166 SER F N   1 
ATOM   9726  C CA  . SER F  1 174 ? 17.784  36.577  -15.458 1.00 34.18  ? 166 SER F CA  1 
ATOM   9727  C C   . SER F  1 174 ? 18.192  36.934  -16.892 1.00 39.85  ? 166 SER F C   1 
ATOM   9728  O O   . SER F  1 174 ? 18.169  36.088  -17.798 1.00 33.67  ? 166 SER F O   1 
ATOM   9729  C CB  . SER F  1 174 ? 18.769  35.560  -14.898 1.00 29.92  ? 166 SER F CB  1 
ATOM   9730  O OG  . SER F  1 174 ? 20.070  36.093  -14.883 1.00 31.87  ? 166 SER F OG  1 
ATOM   9731  N N   . GLN F  1 175 ? 18.575  38.188  -17.093 1.00 37.97  ? 167 GLN F N   1 
ATOM   9732  C CA  . GLN F  1 175 ? 18.999  38.632  -18.411 1.00 39.25  ? 167 GLN F CA  1 
ATOM   9733  C C   . GLN F  1 175 ? 20.276  37.919  -18.844 1.00 39.29  ? 167 GLN F C   1 
ATOM   9734  O O   . GLN F  1 175 ? 20.463  37.623  -20.028 1.00 39.69  ? 167 GLN F O   1 
ATOM   9735  C CB  . GLN F  1 175 ? 19.176  40.145  -18.434 1.00 38.20  ? 167 GLN F CB  1 
ATOM   9736  C CG  . GLN F  1 175 ? 20.137  40.665  -17.406 1.00 37.61  ? 167 GLN F CG  1 
ATOM   9737  C CD  . GLN F  1 175 ? 19.702  41.998  -16.851 1.00 49.89  ? 167 GLN F CD  1 
ATOM   9738  O OE1 . GLN F  1 175 ? 20.390  43.011  -17.017 1.00 48.92  ? 167 GLN F OE1 1 
ATOM   9739  N NE2 . GLN F  1 175 ? 18.549  42.009  -16.179 1.00 51.30  ? 167 GLN F NE2 1 
ATOM   9740  N N   . TYR F  1 176 ? 21.124  37.599  -17.871 1.00 34.75  ? 168 TYR F N   1 
ATOM   9741  C CA  . TYR F  1 176 ? 22.400  36.943  -18.133 1.00 33.32  ? 168 TYR F CA  1 
ATOM   9742  C C   . TYR F  1 176 ? 22.260  35.443  -18.369 1.00 36.24  ? 168 TYR F C   1 
ATOM   9743  O O   . TYR F  1 176 ? 23.250  34.715  -18.449 1.00 37.80  ? 168 TYR F O   1 
ATOM   9744  C CB  . TYR F  1 176 ? 23.359  37.230  -16.987 1.00 35.77  ? 168 TYR F CB  1 
ATOM   9745  C CG  . TYR F  1 176 ? 23.297  38.678  -16.601 1.00 42.28  ? 168 TYR F CG  1 
ATOM   9746  C CD1 . TYR F  1 176 ? 23.658  39.669  -17.509 1.00 47.81  ? 168 TYR F CD1 1 
ATOM   9747  C CD2 . TYR F  1 176 ? 22.842  39.065  -15.357 1.00 33.25  ? 168 TYR F CD2 1 
ATOM   9748  C CE1 . TYR F  1 176 ? 23.585  41.005  -17.173 1.00 47.06  ? 168 TYR F CE1 1 
ATOM   9749  C CE2 . TYR F  1 176 ? 22.764  40.396  -15.015 1.00 39.66  ? 168 TYR F CE2 1 
ATOM   9750  C CZ  . TYR F  1 176 ? 23.137  41.362  -15.924 1.00 41.12  ? 168 TYR F CZ  1 
ATOM   9751  O OH  . TYR F  1 176 ? 23.064  42.690  -15.580 1.00 51.37  ? 168 TYR F OH  1 
ATOM   9752  N N   . SER F  1 177 ? 21.025  34.981  -18.490 1.00 35.01  ? 169 SER F N   1 
ATOM   9753  C CA  . SER F  1 177 ? 20.792  33.584  -18.785 1.00 32.76  ? 169 SER F CA  1 
ATOM   9754  C C   . SER F  1 177 ? 21.071  33.306  -20.247 1.00 37.16  ? 169 SER F C   1 
ATOM   9755  O O   . SER F  1 177 ? 20.655  34.057  -21.133 1.00 36.98  ? 169 SER F O   1 
ATOM   9756  C CB  . SER F  1 177 ? 19.353  33.191  -18.461 1.00 35.34  ? 169 SER F CB  1 
ATOM   9757  O OG  . SER F  1 177 ? 19.037  31.933  -19.034 1.00 34.09  ? 169 SER F OG  1 
ATOM   9758  N N   . ARG F  1 178 ? 21.649  32.157  -20.535 1.00 36.01  ? 170 ARG F N   1 
ATOM   9759  C CA  . ARG F  1 178 ? 21.987  31.866  -21.910 1.00 29.74  ? 170 ARG F CA  1 
ATOM   9760  C C   . ARG F  1 178 ? 20.683  31.915  -22.691 1.00 33.49  ? 170 ARG F C   1 
ATOM   9761  O O   . ARG F  1 178 ? 20.683  32.132  -23.903 1.00 40.66  ? 170 ARG F O   1 
ATOM   9762  C CB  . ARG F  1 178 ? 22.628  30.484  -22.029 1.00 37.02  ? 170 ARG F CB  1 
ATOM   9763  C CG  . ARG F  1 178 ? 23.894  30.457  -22.869 1.00 41.55  ? 170 ARG F CG  1 
ATOM   9764  C CD  . ARG F  1 178 ? 24.734  29.228  -22.563 1.00 52.50  ? 170 ARG F CD  1 
ATOM   9765  N NE  . ARG F  1 178 ? 24.810  28.320  -23.704 1.00 63.36  ? 170 ARG F NE  1 
ATOM   9766  C CZ  . ARG F  1 178 ? 24.843  26.995  -23.602 1.00 68.93  ? 170 ARG F CZ  1 
ATOM   9767  N NH1 . ARG F  1 178 ? 24.808  26.418  -22.409 1.00 67.09  ? 170 ARG F NH1 1 
ATOM   9768  N NH2 . ARG F  1 178 ? 24.912  26.246  -24.695 1.00 69.20  ? 170 ARG F NH2 1 
ATOM   9769  N N   . PHE F  1 179 ? 19.573  31.692  -21.994 1.00 33.18  ? 171 PHE F N   1 
ATOM   9770  C CA  . PHE F  1 179 ? 18.304  31.438  -22.660 1.00 34.17  ? 171 PHE F CA  1 
ATOM   9771  C C   . PHE F  1 179 ? 17.359  32.615  -22.489 1.00 35.74  ? 171 PHE F C   1 
ATOM   9772  O O   . PHE F  1 179 ? 17.642  33.571  -21.755 1.00 34.36  ? 171 PHE F O   1 
ATOM   9773  C CB  . PHE F  1 179 ? 17.630  30.174  -22.126 1.00 32.75  ? 171 PHE F CB  1 
ATOM   9774  C CG  . PHE F  1 179 ? 18.412  28.915  -22.353 1.00 32.07  ? 171 PHE F CG  1 
ATOM   9775  C CD1 . PHE F  1 179 ? 19.423  28.538  -21.479 1.00 33.89  ? 171 PHE F CD1 1 
ATOM   9776  C CD2 . PHE F  1 179 ? 18.114  28.085  -23.418 1.00 33.52  ? 171 PHE F CD2 1 
ATOM   9777  C CE1 . PHE F  1 179 ? 20.144  27.366  -21.679 1.00 36.95  ? 171 PHE F CE1 1 
ATOM   9778  C CE2 . PHE F  1 179 ? 18.828  26.908  -23.623 1.00 38.17  ? 171 PHE F CE2 1 
ATOM   9779  C CZ  . PHE F  1 179 ? 19.846  26.550  -22.751 1.00 36.82  ? 171 PHE F CZ  1 
ATOM   9780  N N   . GLU F  1 180 ? 16.234  32.538  -23.188 1.00 32.66  ? 172 GLU F N   1 
ATOM   9781  C CA  . GLU F  1 180 ? 15.203  33.550  -23.075 1.00 37.84  ? 172 GLU F CA  1 
ATOM   9782  C C   . GLU F  1 180 ? 13.848  32.867  -23.056 1.00 35.12  ? 172 GLU F C   1 
ATOM   9783  O O   . GLU F  1 180 ? 13.677  31.782  -23.618 1.00 32.35  ? 172 GLU F O   1 
ATOM   9784  C CB  . GLU F  1 180 ? 15.300  34.570  -24.216 1.00 41.65  ? 172 GLU F CB  1 
ATOM   9785  C CG  . GLU F  1 180 ? 15.242  33.982  -25.629 1.00 45.71  ? 172 GLU F CG  1 
ATOM   9786  C CD  . GLU F  1 180 ? 15.653  34.991  -26.713 1.00 47.15  ? 172 GLU F CD  1 
ATOM   9787  O OE1 . GLU F  1 180 ? 15.886  36.175  -26.379 1.00 44.83  ? 172 GLU F OE1 1 
ATOM   9788  O OE2 . GLU F  1 180 ? 15.756  34.598  -27.899 1.00 47.01  ? 172 GLU F OE2 1 
ATOM   9789  N N   . ILE F  1 181 ? 12.890  33.492  -22.388 1.00 27.83  ? 173 ILE F N   1 
ATOM   9790  C CA  . ILE F  1 181 ? 11.564  32.916  -22.320 1.00 36.55  ? 173 ILE F CA  1 
ATOM   9791  C C   . ILE F  1 181 ? 10.675  33.558  -23.369 1.00 37.30  ? 173 ILE F C   1 
ATOM   9792  O O   . ILE F  1 181 ? 10.650  34.782  -23.509 1.00 37.10  ? 173 ILE F O   1 
ATOM   9793  C CB  . ILE F  1 181 ? 10.940  33.073  -20.909 1.00 39.25  ? 173 ILE F CB  1 
ATOM   9794  C CG1 . ILE F  1 181 ? 11.685  32.194  -19.905 1.00 37.34  ? 173 ILE F CG1 1 
ATOM   9795  C CG2 . ILE F  1 181 ? 9.466   32.705  -20.920 1.00 35.72  ? 173 ILE F CG2 1 
ATOM   9796  C CD1 . ILE F  1 181 ? 11.044  32.150  -18.553 1.00 37.88  ? 173 ILE F CD1 1 
ATOM   9797  N N   . LEU F  1 182 ? 9.956   32.724  -24.112 1.00 34.68  ? 174 LEU F N   1 
ATOM   9798  C CA  . LEU F  1 182 ? 8.964   33.224  -25.052 1.00 41.91  ? 174 LEU F CA  1 
ATOM   9799  C C   . LEU F  1 182 ? 7.609   33.361  -24.355 1.00 47.43  ? 174 LEU F C   1 
ATOM   9800  O O   . LEU F  1 182 ? 6.985   34.423  -24.408 1.00 51.86  ? 174 LEU F O   1 
ATOM   9801  C CB  . LEU F  1 182 ? 8.871   32.308  -26.281 1.00 47.20  ? 174 LEU F CB  1 
ATOM   9802  C CG  . LEU F  1 182 ? 10.222  31.865  -26.862 1.00 40.61  ? 174 LEU F CG  1 
ATOM   9803  C CD1 . LEU F  1 182 ? 10.075  30.946  -28.066 1.00 42.39  ? 174 LEU F CD1 1 
ATOM   9804  C CD2 . LEU F  1 182 ? 11.087  33.063  -27.207 1.00 42.70  ? 174 LEU F CD2 1 
ATOM   9805  N N   . ASP F  1 183 ? 7.167   32.297  -23.684 1.00 51.06  ? 175 ASP F N   1 
ATOM   9806  C CA  . ASP F  1 183 ? 5.866   32.304  -23.009 1.00 51.37  ? 175 ASP F CA  1 
ATOM   9807  C C   . ASP F  1 183 ? 5.707   31.175  -21.979 1.00 48.07  ? 175 ASP F C   1 
ATOM   9808  O O   . ASP F  1 183 ? 6.207   30.063  -22.177 1.00 43.03  ? 175 ASP F O   1 
ATOM   9809  C CB  . ASP F  1 183 ? 4.736   32.228  -24.047 1.00 49.93  ? 175 ASP F CB  1 
ATOM   9810  C CG  . ASP F  1 183 ? 3.355   32.343  -23.423 1.00 63.03  ? 175 ASP F CG  1 
ATOM   9811  O OD1 . ASP F  1 183 ? 3.121   33.291  -22.640 1.00 68.05  ? 175 ASP F OD1 1 
ATOM   9812  O OD2 . ASP F  1 183 ? 2.501   31.478  -23.710 1.00 61.21  ? 175 ASP F OD2 1 
ATOM   9813  N N   . VAL F  1 184 ? 5.011   31.480  -20.881 1.00 55.28  ? 176 VAL F N   1 
ATOM   9814  C CA  . VAL F  1 184 ? 4.632   30.486  -19.869 1.00 54.26  ? 176 VAL F CA  1 
ATOM   9815  C C   . VAL F  1 184 ? 3.122   30.400  -19.692 1.00 52.35  ? 176 VAL F C   1 
ATOM   9816  O O   . VAL F  1 184 ? 2.452   31.416  -19.504 1.00 58.84  ? 176 VAL F O   1 
ATOM   9817  C CB  . VAL F  1 184 ? 5.232   30.791  -18.473 1.00 48.77  ? 176 VAL F CB  1 
ATOM   9818  C CG1 . VAL F  1 184 ? 6.476   29.983  -18.241 1.00 36.78  ? 176 VAL F CG1 1 
ATOM   9819  C CG2 . VAL F  1 184 ? 5.496   32.279  -18.294 1.00 54.01  ? 176 VAL F CG2 1 
ATOM   9820  N N   . THR F  1 185 ? 2.596   29.181  -19.737 1.00 50.71  ? 177 THR F N   1 
ATOM   9821  C CA  . THR F  1 185 ? 1.175   28.945  -19.509 1.00 52.45  ? 177 THR F CA  1 
ATOM   9822  C C   . THR F  1 185 ? 0.965   27.878  -18.432 1.00 55.29  ? 177 THR F C   1 
ATOM   9823  O O   . THR F  1 185 ? 1.482   26.767  -18.536 1.00 52.97  ? 177 THR F O   1 
ATOM   9824  C CB  . THR F  1 185 ? 0.451   28.518  -20.809 1.00 49.96  ? 177 THR F CB  1 
ATOM   9825  O OG1 . THR F  1 185 ? 0.951   27.250  -21.252 1.00 48.95  ? 177 THR F OG1 1 
ATOM   9826  C CG2 . THR F  1 185 ? 0.662   29.549  -21.903 1.00 46.54  ? 177 THR F CG2 1 
ATOM   9827  N N   . GLN F  1 186 ? 0.211   28.221  -17.393 1.00 60.94  ? 178 GLN F N   1 
ATOM   9828  C CA  . GLN F  1 186 ? -0.092  27.270  -16.331 1.00 53.04  ? 178 GLN F CA  1 
ATOM   9829  C C   . GLN F  1 186 ? -1.581  26.969  -16.334 1.00 52.27  ? 178 GLN F C   1 
ATOM   9830  O O   . GLN F  1 186 ? -2.389  27.882  -16.470 1.00 60.03  ? 178 GLN F O   1 
ATOM   9831  C CB  . GLN F  1 186 ? 0.344   27.828  -14.977 1.00 52.06  ? 178 GLN F CB  1 
ATOM   9832  C CG  . GLN F  1 186 ? 0.739   29.304  -15.003 1.00 60.68  ? 178 GLN F CG  1 
ATOM   9833  C CD  . GLN F  1 186 ? 1.805   29.646  -13.965 1.00 63.04  ? 178 GLN F CD  1 
ATOM   9834  O OE1 . GLN F  1 186 ? 2.780   28.910  -13.794 1.00 46.39  ? 178 GLN F OE1 1 
ATOM   9835  N NE2 . GLN F  1 186 ? 1.620   30.765  -13.265 1.00 62.80  ? 178 GLN F NE2 1 
ATOM   9836  N N   . LYS F  1 187 ? -1.944  25.694  -16.200 1.00 49.77  ? 179 LYS F N   1 
ATOM   9837  C CA  . LYS F  1 187 ? -3.356  25.302  -16.213 1.00 50.44  ? 179 LYS F CA  1 
ATOM   9838  C C   . LYS F  1 187 ? -3.684  24.005  -15.457 1.00 50.30  ? 179 LYS F C   1 
ATOM   9839  O O   . LYS F  1 187 ? -2.809  23.176  -15.218 1.00 47.02  ? 179 LYS F O   1 
ATOM   9840  C CB  . LYS F  1 187 ? -3.881  25.233  -17.652 1.00 50.69  ? 179 LYS F CB  1 
ATOM   9841  C CG  . LYS F  1 187 ? -2.968  24.526  -18.630 1.00 49.98  ? 179 LYS F CG  1 
ATOM   9842  C CD  . LYS F  1 187 ? -3.060  23.011  -18.503 1.00 51.58  ? 179 LYS F CD  1 
ATOM   9843  C CE  . LYS F  1 187 ? -2.429  22.341  -19.710 1.00 45.96  ? 179 LYS F CE  1 
ATOM   9844  N NZ  . LYS F  1 187 ? -3.011  22.927  -20.942 1.00 35.13  ? 179 LYS F NZ  1 
ATOM   9845  N N   . LYS F  1 188 ? -4.959  23.837  -15.104 1.00 53.01  ? 180 LYS F N   1 
ATOM   9846  C CA  . LYS F  1 188 ? -5.419  22.688  -14.323 1.00 41.38  ? 180 LYS F CA  1 
ATOM   9847  C C   . LYS F  1 188 ? -5.491  21.382  -15.114 1.00 42.42  ? 180 LYS F C   1 
ATOM   9848  O O   . LYS F  1 188 ? -6.011  21.342  -16.221 1.00 53.62  ? 180 LYS F O   1 
ATOM   9849  C CB  . LYS F  1 188 ? -6.786  22.989  -13.705 1.00 51.11  ? 180 LYS F CB  1 
ATOM   9850  C CG  . LYS F  1 188 ? -6.756  23.372  -12.233 1.00 56.60  ? 180 LYS F CG  1 
ATOM   9851  C CD  . LYS F  1 188 ? -6.693  22.131  -11.344 1.00 52.46  ? 180 LYS F CD  1 
ATOM   9852  C CE  . LYS F  1 188 ? -7.992  21.338  -11.392 1.00 51.48  ? 180 LYS F CE  1 
ATOM   9853  N NZ  . LYS F  1 188 ? -9.134  22.106  -10.821 1.00 65.56  ? 180 LYS F NZ  1 
ATOM   9854  N N   . ASN F  1 189 ? -4.952  20.321  -14.512 1.00 48.79  ? 181 ASN F N   1 
ATOM   9855  C CA  . ASN F  1 189 ? -5.011  18.963  -15.056 1.00 46.96  ? 181 ASN F CA  1 
ATOM   9856  C C   . ASN F  1 189 ? -5.346  17.941  -13.964 1.00 49.97  ? 181 ASN F C   1 
ATOM   9857  O O   . ASN F  1 189 ? -5.004  18.141  -12.798 1.00 48.44  ? 181 ASN F O   1 
ATOM   9858  C CB  . ASN F  1 189 ? -3.692  18.598  -15.738 1.00 47.75  ? 181 ASN F CB  1 
ATOM   9859  C CG  . ASN F  1 189 ? -3.791  17.323  -16.553 1.00 60.25  ? 181 ASN F CG  1 
ATOM   9860  O OD1 . ASN F  1 189 ? -4.842  17.011  -17.113 1.00 66.91  ? 181 ASN F OD1 1 
ATOM   9861  N ND2 . ASN F  1 189 ? -2.694  16.579  -16.622 1.00 55.61  ? 181 ASN F ND2 1 
ATOM   9862  N N   . SER F  1 190 ? -6.019  16.854  -14.338 1.00 43.71  ? 182 SER F N   1 
ATOM   9863  C CA  . SER F  1 190 ? -6.474  15.856  -13.364 1.00 50.03  ? 182 SER F CA  1 
ATOM   9864  C C   . SER F  1 190 ? -6.148  14.395  -13.710 1.00 59.61  ? 182 SER F C   1 
ATOM   9865  O O   . SER F  1 190 ? -6.997  13.686  -14.250 1.00 61.76  ? 182 SER F O   1 
ATOM   9866  C CB  . SER F  1 190 ? -7.979  16.005  -13.118 1.00 45.89  ? 182 SER F CB  1 
ATOM   9867  O OG  . SER F  1 190 ? -8.370  15.341  -11.929 1.00 49.93  ? 182 SER F OG  1 
ATOM   9868  N N   . VAL F  1 191 ? -4.934  13.945  -13.408 1.00 55.59  ? 183 VAL F N   1 
ATOM   9869  C CA  . VAL F  1 191 ? -4.540  12.551  -13.649 1.00 52.22  ? 183 VAL F CA  1 
ATOM   9870  C C   . VAL F  1 191 ? -5.157  11.538  -12.671 1.00 56.35  ? 183 VAL F C   1 
ATOM   9871  O O   . VAL F  1 191 ? -5.424  11.870  -11.516 1.00 58.10  ? 183 VAL F O   1 
ATOM   9872  C CB  . VAL F  1 191 ? -3.008  12.390  -13.628 1.00 58.75  ? 183 VAL F CB  1 
ATOM   9873  C CG1 . VAL F  1 191 ? -2.354  13.424  -14.532 1.00 58.89  ? 183 VAL F CG1 1 
ATOM   9874  C CG2 . VAL F  1 191 ? -2.481  12.506  -12.206 1.00 53.00  ? 183 VAL F CG2 1 
ATOM   9875  N N   . THR F  1 192 ? -5.369  10.304  -13.133 1.00 61.16  ? 184 THR F N   1 
ATOM   9876  C CA  . THR F  1 192 ? -5.796  9.209   -12.250 1.00 67.20  ? 184 THR F CA  1 
ATOM   9877  C C   . THR F  1 192 ? -4.883  7.986   -12.383 1.00 65.69  ? 184 THR F C   1 
ATOM   9878  O O   . THR F  1 192 ? -5.294  6.855   -12.097 1.00 64.88  ? 184 THR F O   1 
ATOM   9879  C CB  . THR F  1 192 ? -7.257  8.760   -12.502 1.00 62.84  ? 184 THR F CB  1 
ATOM   9880  O OG1 . THR F  1 192 ? -7.394  8.314   -13.857 1.00 72.52  ? 184 THR F OG1 1 
ATOM   9881  C CG2 . THR F  1 192 ? -8.246  9.890   -12.229 1.00 49.77  ? 184 THR F CG2 1 
ATOM   9882  N N   . CYS F  1 196 ? -6.183  2.785   -8.383  1.00 45.53  ? 188 CYS F N   1 
ATOM   9883  C CA  . CYS F  1 196 ? -7.085  3.514   -7.495  1.00 58.01  ? 188 CYS F CA  1 
ATOM   9884  C C   . CYS F  1 196 ? -7.852  4.614   -8.236  1.00 64.41  ? 188 CYS F C   1 
ATOM   9885  O O   . CYS F  1 196 ? -7.280  5.292   -9.092  1.00 64.26  ? 188 CYS F O   1 
ATOM   9886  C CB  . CYS F  1 196 ? -6.314  4.090   -6.304  1.00 64.96  ? 188 CYS F CB  1 
ATOM   9887  S SG  . CYS F  1 196 ? -4.696  4.802   -6.713  1.00 90.94  ? 188 CYS F SG  1 
ATOM   9888  N N   . PRO F  1 197 ? -9.153  4.795   -7.895  1.00 75.54  ? 189 PRO F N   1 
ATOM   9889  C CA  . PRO F  1 197 ? -10.112 5.636   -8.632  1.00 65.06  ? 189 PRO F CA  1 
ATOM   9890  C C   . PRO F  1 197 ? -10.302 7.081   -8.127  1.00 66.53  ? 189 PRO F C   1 
ATOM   9891  O O   . PRO F  1 197 ? -11.315 7.702   -8.463  1.00 62.24  ? 189 PRO F O   1 
ATOM   9892  C CB  . PRO F  1 197 ? -11.422 4.873   -8.438  1.00 63.70  ? 189 PRO F CB  1 
ATOM   9893  C CG  . PRO F  1 197 ? -11.309 4.363   -7.023  1.00 62.99  ? 189 PRO F CG  1 
ATOM   9894  C CD  . PRO F  1 197 ? -9.826  4.065   -6.798  1.00 67.56  ? 189 PRO F CD  1 
ATOM   9895  N N   . GLU F  1 198 ? -9.373  7.606   -7.333  1.00 61.62  ? 190 GLU F N   1 
ATOM   9896  C CA  . GLU F  1 198 ? -9.435  9.013   -6.959  1.00 49.07  ? 190 GLU F CA  1 
ATOM   9897  C C   . GLU F  1 198 ? -8.488  9.801   -7.849  1.00 51.25  ? 190 GLU F C   1 
ATOM   9898  O O   . GLU F  1 198 ? -7.460  9.281   -8.278  1.00 54.34  ? 190 GLU F O   1 
ATOM   9899  C CB  . GLU F  1 198 ? -9.091  9.216   -5.481  1.00 53.46  ? 190 GLU F CB  1 
ATOM   9900  C CG  . GLU F  1 198 ? -10.311 9.329   -4.562  1.00 51.32  ? 190 GLU F CG  1 
ATOM   9901  C CD  . GLU F  1 198 ? -11.295 10.414  -5.004  1.00 56.02  ? 190 GLU F CD  1 
ATOM   9902  O OE1 . GLU F  1 198 ? -10.850 11.520  -5.402  1.00 47.61  ? 190 GLU F OE1 1 
ATOM   9903  O OE2 . GLU F  1 198 ? -12.521 10.152  -4.961  1.00 57.66  ? 190 GLU F OE2 1 
ATOM   9904  N N   . ALA F  1 199 ? -8.846  11.043  -8.149  1.00 48.63  ? 191 ALA F N   1 
ATOM   9905  C CA  . ALA F  1 199 ? -8.032  11.872  -9.026  1.00 40.23  ? 191 ALA F CA  1 
ATOM   9906  C C   . ALA F  1 199 ? -7.163  12.831  -8.217  1.00 40.39  ? 191 ALA F C   1 
ATOM   9907  O O   . ALA F  1 199 ? -7.541  13.257  -7.116  1.00 27.53  ? 191 ALA F O   1 
ATOM   9908  C CB  . ALA F  1 199 ? -8.915  12.641  -9.995  1.00 38.34  ? 191 ALA F CB  1 
ATOM   9909  N N   . TYR F  1 200 ? -5.998  13.168  -8.772  1.00 40.54  ? 192 TYR F N   1 
ATOM   9910  C CA  . TYR F  1 200 ? -5.087  14.106  -8.128  1.00 33.20  ? 192 TYR F CA  1 
ATOM   9911  C C   . TYR F  1 200 ? -5.017  15.402  -8.909  1.00 37.11  ? 192 TYR F C   1 
ATOM   9912  O O   . TYR F  1 200 ? -4.427  15.456  -9.988  1.00 44.34  ? 192 TYR F O   1 
ATOM   9913  C CB  . TYR F  1 200 ? -3.692  13.499  -7.959  1.00 27.38  ? 192 TYR F CB  1 
ATOM   9914  C CG  . TYR F  1 200 ? -3.698  12.243  -7.127  1.00 27.77  ? 192 TYR F CG  1 
ATOM   9915  C CD1 . TYR F  1 200 ? -4.030  11.017  -7.688  1.00 31.43  ? 192 TYR F CD1 1 
ATOM   9916  C CD2 . TYR F  1 200 ? -3.387  12.281  -5.774  1.00 28.15  ? 192 TYR F CD2 1 
ATOM   9917  C CE1 . TYR F  1 200 ? -4.052  9.863   -6.929  1.00 32.45  ? 192 TYR F CE1 1 
ATOM   9918  C CE2 . TYR F  1 200 ? -3.406  11.128  -4.999  1.00 26.78  ? 192 TYR F CE2 1 
ATOM   9919  C CZ  . TYR F  1 200 ? -3.739  9.923   -5.583  1.00 34.67  ? 192 TYR F CZ  1 
ATOM   9920  O OH  . TYR F  1 200 ? -3.762  8.770   -4.830  1.00 34.80  ? 192 TYR F OH  1 
ATOM   9921  N N   . GLU F  1 201 ? -5.643  16.440  -8.361  1.00 36.11  ? 193 GLU F N   1 
ATOM   9922  C CA  . GLU F  1 201 ? -5.574  17.774  -8.939  1.00 36.72  ? 193 GLU F CA  1 
ATOM   9923  C C   . GLU F  1 201 ? -4.123  18.243  -9.041  1.00 38.81  ? 193 GLU F C   1 
ATOM   9924  O O   . GLU F  1 201 ? -3.444  18.407  -8.026  1.00 44.05  ? 193 GLU F O   1 
ATOM   9925  C CB  . GLU F  1 201 ? -6.386  18.766  -8.102  1.00 32.20  ? 193 GLU F CB  1 
ATOM   9926  C CG  . GLU F  1 201 ? -7.882  18.504  -8.070  1.00 34.60  ? 193 GLU F CG  1 
ATOM   9927  C CD  . GLU F  1 201 ? -8.694  19.783  -8.183  1.00 43.34  ? 193 GLU F CD  1 
ATOM   9928  O OE1 . GLU F  1 201 ? -8.084  20.872  -8.176  1.00 39.43  ? 193 GLU F OE1 1 
ATOM   9929  O OE2 . GLU F  1 201 ? -9.941  19.707  -8.287  1.00 52.42  ? 193 GLU F OE2 1 
ATOM   9930  N N   . ASP F  1 202 ? -3.648  18.455  -10.264 1.00 38.97  ? 194 ASP F N   1 
ATOM   9931  C CA  . ASP F  1 202 ? -2.315  19.019  -10.467 1.00 41.54  ? 194 ASP F CA  1 
ATOM   9932  C C   . ASP F  1 202 ? -2.380  20.251  -11.385 1.00 43.87  ? 194 ASP F C   1 
ATOM   9933  O O   . ASP F  1 202 ? -3.353  20.435  -12.110 1.00 46.84  ? 194 ASP F O   1 
ATOM   9934  C CB  . ASP F  1 202 ? -1.376  17.974  -11.060 1.00 39.48  ? 194 ASP F CB  1 
ATOM   9935  C CG  . ASP F  1 202 ? -1.317  18.046  -12.575 1.00 45.51  ? 194 ASP F CG  1 
ATOM   9936  O OD1 . ASP F  1 202 ? -0.593  18.916  -13.109 1.00 47.56  ? 194 ASP F OD1 1 
ATOM   9937  O OD2 . ASP F  1 202 ? -1.990  17.232  -13.238 1.00 51.25  ? 194 ASP F OD2 1 
ATOM   9938  N N   . VAL F  1 203 ? -1.349  21.092  -11.344 1.00 36.98  ? 195 VAL F N   1 
ATOM   9939  C CA  . VAL F  1 203 ? -1.204  22.188  -12.304 1.00 41.87  ? 195 VAL F CA  1 
ATOM   9940  C C   . VAL F  1 203 ? -0.113  21.852  -13.327 1.00 43.04  ? 195 VAL F C   1 
ATOM   9941  O O   . VAL F  1 203 ? 0.969   21.381  -12.959 1.00 40.97  ? 195 VAL F O   1 
ATOM   9942  C CB  . VAL F  1 203 ? -0.878  23.531  -11.605 1.00 34.96  ? 195 VAL F CB  1 
ATOM   9943  C CG1 . VAL F  1 203 ? -0.514  24.593  -12.618 1.00 35.23  ? 195 VAL F CG1 1 
ATOM   9944  C CG2 . VAL F  1 203 ? -2.059  23.991  -10.777 1.00 45.62  ? 195 VAL F CG2 1 
ATOM   9945  N N   . GLU F  1 204 ? -0.410  22.068  -14.608 1.00 48.04  ? 196 GLU F N   1 
ATOM   9946  C CA  . GLU F  1 204 ? 0.558   21.840  -15.686 1.00 47.85  ? 196 GLU F CA  1 
ATOM   9947  C C   . GLU F  1 204 ? 1.139   23.164  -16.187 1.00 44.27  ? 196 GLU F C   1 
ATOM   9948  O O   . GLU F  1 204 ? 0.413   24.023  -16.695 1.00 41.82  ? 196 GLU F O   1 
ATOM   9949  C CB  . GLU F  1 204 ? -0.080  21.056  -16.838 1.00 47.99  ? 196 GLU F CB  1 
ATOM   9950  C CG  . GLU F  1 204 ? 0.899   20.591  -17.908 1.00 48.71  ? 196 GLU F CG  1 
ATOM   9951  C CD  . GLU F  1 204 ? 0.619   19.167  -18.376 1.00 61.32  ? 196 GLU F CD  1 
ATOM   9952  O OE1 . GLU F  1 204 ? 0.225   18.317  -17.532 1.00 61.98  ? 196 GLU F OE1 1 
ATOM   9953  O OE2 . GLU F  1 204 ? 0.788   18.904  -19.589 1.00 45.19  ? 196 GLU F OE2 1 
ATOM   9954  N N   . VAL F  1 205 ? 2.449   23.324  -16.012 1.00 43.82  ? 197 VAL F N   1 
ATOM   9955  C CA  . VAL F  1 205 ? 3.148   24.543  -16.416 1.00 42.60  ? 197 VAL F CA  1 
ATOM   9956  C C   . VAL F  1 205 ? 3.962   24.308  -17.684 1.00 38.42  ? 197 VAL F C   1 
ATOM   9957  O O   . VAL F  1 205 ? 4.912   23.522  -17.696 1.00 38.22  ? 197 VAL F O   1 
ATOM   9958  C CB  . VAL F  1 205 ? 4.070   25.082  -15.292 1.00 39.95  ? 197 VAL F CB  1 
ATOM   9959  C CG1 . VAL F  1 205 ? 5.051   26.121  -15.839 1.00 36.67  ? 197 VAL F CG1 1 
ATOM   9960  C CG2 . VAL F  1 205 ? 3.246   25.674  -14.166 1.00 37.61  ? 197 VAL F CG2 1 
ATOM   9961  N N   . SER F  1 206 ? 3.571   24.987  -18.755 1.00 47.11  ? 198 SER F N   1 
ATOM   9962  C CA  . SER F  1 206 ? 4.251   24.856  -20.036 1.00 40.88  ? 198 SER F CA  1 
ATOM   9963  C C   . SER F  1 206 ? 5.195   26.019  -20.230 1.00 36.86  ? 198 SER F C   1 
ATOM   9964  O O   . SER F  1 206 ? 4.777   27.171  -20.334 1.00 41.65  ? 198 SER F O   1 
ATOM   9965  C CB  . SER F  1 206 ? 3.244   24.786  -21.178 1.00 42.63  ? 198 SER F CB  1 
ATOM   9966  O OG  . SER F  1 206 ? 2.510   23.574  -21.122 1.00 46.50  ? 198 SER F OG  1 
ATOM   9967  N N   . LEU F  1 207 ? 6.479   25.706  -20.252 1.00 32.57  ? 199 LEU F N   1 
ATOM   9968  C CA  . LEU F  1 207 ? 7.502   26.710  -20.452 1.00 38.50  ? 199 LEU F CA  1 
ATOM   9969  C C   . LEU F  1 207 ? 8.093   26.572  -21.856 1.00 42.99  ? 199 LEU F C   1 
ATOM   9970  O O   . LEU F  1 207 ? 8.728   25.560  -22.200 1.00 37.92  ? 199 LEU F O   1 
ATOM   9971  C CB  . LEU F  1 207 ? 8.584   26.569  -19.380 1.00 39.79  ? 199 LEU F CB  1 
ATOM   9972  C CG  . LEU F  1 207 ? 9.842   27.436  -19.461 1.00 38.30  ? 199 LEU F CG  1 
ATOM   9973  C CD1 . LEU F  1 207 ? 9.552   28.869  -19.081 1.00 36.94  ? 199 LEU F CD1 1 
ATOM   9974  C CD2 . LEU F  1 207 ? 10.920  26.872  -18.560 1.00 33.91  ? 199 LEU F CD2 1 
ATOM   9975  N N   . ASN F  1 208 ? 7.850   27.591  -22.672 1.00 39.31  ? 200 ASN F N   1 
ATOM   9976  C CA  . ASN F  1 208 ? 8.397   27.637  -24.018 1.00 40.47  ? 200 ASN F CA  1 
ATOM   9977  C C   . ASN F  1 208 ? 9.536   28.651  -24.110 1.00 39.71  ? 200 ASN F C   1 
ATOM   9978  O O   . ASN F  1 208 ? 9.342   29.859  -23.894 1.00 34.28  ? 200 ASN F O   1 
ATOM   9979  C CB  . ASN F  1 208 ? 7.293   27.940  -25.028 1.00 45.91  ? 200 ASN F CB  1 
ATOM   9980  C CG  . ASN F  1 208 ? 7.832   28.264  -26.392 1.00 36.91  ? 200 ASN F CG  1 
ATOM   9981  O OD1 . ASN F  1 208 ? 7.692   29.388  -26.876 1.00 32.87  ? 200 ASN F OD1 1 
ATOM   9982  N ND2 . ASN F  1 208 ? 8.468   27.287  -27.019 1.00 41.10  ? 200 ASN F ND2 1 
ATOM   9983  N N   . PHE F  1 209 ? 10.724  28.140  -24.425 1.00 35.92  ? 201 PHE F N   1 
ATOM   9984  C CA  . PHE F  1 209 ? 11.961  28.920  -24.366 1.00 40.30  ? 201 PHE F CA  1 
ATOM   9985  C C   . PHE F  1 209 ? 12.878  28.594  -25.543 1.00 38.29  ? 201 PHE F C   1 
ATOM   9986  O O   . PHE F  1 209 ? 12.780  27.511  -26.120 1.00 38.74  ? 201 PHE F O   1 
ATOM   9987  C CB  . PHE F  1 209 ? 12.697  28.646  -23.044 1.00 33.27  ? 201 PHE F CB  1 
ATOM   9988  C CG  . PHE F  1 209 ? 13.244  27.231  -22.912 1.00 25.95  ? 201 PHE F CG  1 
ATOM   9989  C CD1 . PHE F  1 209 ? 12.395  26.124  -22.892 1.00 28.29  ? 201 PHE F CD1 1 
ATOM   9990  C CD2 . PHE F  1 209 ? 14.602  27.017  -22.765 1.00 24.21  ? 201 PHE F CD2 1 
ATOM   9991  C CE1 . PHE F  1 209 ? 12.893  24.824  -22.753 1.00 19.31  ? 201 PHE F CE1 1 
ATOM   9992  C CE2 . PHE F  1 209 ? 15.109  25.719  -22.624 1.00 26.68  ? 201 PHE F CE2 1 
ATOM   9993  C CZ  . PHE F  1 209 ? 14.249  24.623  -22.614 1.00 19.66  ? 201 PHE F CZ  1 
ATOM   9994  N N   . ARG F  1 210 ? 13.765  29.524  -25.895 1.00 36.68  ? 202 ARG F N   1 
ATOM   9995  C CA  . ARG F  1 210 ? 14.782  29.251  -26.917 1.00 47.08  ? 202 ARG F CA  1 
ATOM   9996  C C   . ARG F  1 210 ? 16.175  29.752  -26.524 1.00 42.17  ? 202 ARG F C   1 
ATOM   9997  O O   . ARG F  1 210 ? 16.320  30.556  -25.597 1.00 33.54  ? 202 ARG F O   1 
ATOM   9998  C CB  . ARG F  1 210 ? 14.379  29.814  -28.296 1.00 41.31  ? 202 ARG F CB  1 
ATOM   9999  C CG  . ARG F  1 210 ? 14.218  31.323  -28.340 1.00 39.27  ? 202 ARG F CG  1 
ATOM   10000 C CD  . ARG F  1 210 ? 14.573  31.887  -29.711 1.00 49.16  ? 202 ARG F CD  1 
ATOM   10001 N NE  . ARG F  1 210 ? 14.454  33.343  -29.756 1.00 41.91  ? 202 ARG F NE  1 
ATOM   10002 C CZ  . ARG F  1 210 ? 13.444  33.985  -30.328 1.00 41.03  ? 202 ARG F CZ  1 
ATOM   10003 N NH1 . ARG F  1 210 ? 12.481  33.292  -30.918 1.00 42.39  ? 202 ARG F NH1 1 
ATOM   10004 N NH2 . ARG F  1 210 ? 13.403  35.312  -30.320 1.00 40.35  ? 202 ARG F NH2 1 
ATOM   10005 N N   . LYS F  1 211 ? 17.189  29.267  -27.245 1.00 43.87  ? 203 LYS F N   1 
ATOM   10006 C CA  . LYS F  1 211 ? 18.572  29.713  -27.074 1.00 38.71  ? 203 LYS F CA  1 
ATOM   10007 C C   . LYS F  1 211 ? 18.747  31.118  -27.653 1.00 38.25  ? 203 LYS F C   1 
ATOM   10008 O O   . LYS F  1 211 ? 17.952  31.543  -28.489 1.00 39.39  ? 203 LYS F O   1 
ATOM   10009 C CB  . LYS F  1 211 ? 19.525  28.722  -27.755 1.00 42.46  ? 203 LYS F CB  1 
ATOM   10010 C CG  . LYS F  1 211 ? 20.738  28.312  -26.917 1.00 48.70  ? 203 LYS F CG  1 
ATOM   10011 C CD  . LYS F  1 211 ? 21.252  26.927  -27.314 1.00 56.82  ? 203 LYS F CD  1 
ATOM   10012 C CE  . LYS F  1 211 ? 22.264  26.360  -26.307 1.00 64.74  ? 203 LYS F CE  1 
ATOM   10013 N NZ  . LYS F  1 211 ? 22.576  24.909  -26.528 1.00 52.34  ? 203 LYS F NZ  1 
ATOM   10014 N N   . LYS F  1 212 ? 19.777  31.836  -27.203 1.00 44.26  ? 204 LYS F N   1 
ATOM   10015 C CA  . LYS F  1 212 ? 20.071  33.194  -27.689 1.00 45.94  ? 204 LYS F CA  1 
ATOM   10016 C C   . LYS F  1 212 ? 21.342  33.257  -28.539 1.00 53.21  ? 204 LYS F C   1 
ATOM   10017 O O   . LYS F  1 212 ? 22.448  33.251  -27.999 1.00 60.80  ? 204 LYS F O   1 
ATOM   10018 C CB  . LYS F  1 212 ? 20.201  34.172  -26.516 1.00 43.02  ? 204 LYS F CB  1 
ATOM   10019 C CG  . LYS F  1 212 ? 18.873  34.648  -25.965 1.00 44.17  ? 204 LYS F CG  1 
ATOM   10020 C CD  . LYS F  1 212 ? 18.934  34.950  -24.469 1.00 43.20  ? 204 LYS F CD  1 
ATOM   10021 C CE  . LYS F  1 212 ? 19.884  36.080  -24.127 1.00 37.15  ? 204 LYS F CE  1 
ATOM   10022 N NZ  . LYS F  1 212 ? 19.809  36.392  -22.667 1.00 43.86  ? 204 LYS F NZ  1 
ATOM   10023 N N   . GLY F  1 213 ? 21.183  33.330  -29.862 1.00 52.36  ? 205 GLY F N   1 
ATOM   10024 C CA  . GLY F  1 213 ? 22.317  33.356  -30.774 1.00 46.58  ? 205 GLY F CA  1 
ATOM   10025 C C   . GLY F  1 213 ? 22.465  32.081  -31.587 1.00 57.42  ? 205 GLY F C   1 
ATOM   10026 O O   . GLY F  1 213 ? 21.962  31.972  -32.709 1.00 58.13  ? 205 GLY F O   1 
ATOM   10027 N N   . ASP G  1 1   ? -17.218 7.055   5.383   1.00 48.17  ? -7  ASP G N   1 
ATOM   10028 C CA  . ASP G  1 1   ? -17.756 7.427   4.077   1.00 60.80  ? -7  ASP G CA  1 
ATOM   10029 C C   . ASP G  1 1   ? -17.039 8.649   3.511   1.00 60.61  ? -7  ASP G C   1 
ATOM   10030 O O   . ASP G  1 1   ? -16.443 9.429   4.261   1.00 52.76  ? -7  ASP G O   1 
ATOM   10031 C CB  . ASP G  1 1   ? -19.272 7.677   4.153   1.00 64.66  ? -7  ASP G CB  1 
ATOM   10032 C CG  . ASP G  1 1   ? -20.096 6.409   3.903   1.00 73.44  ? -7  ASP G CG  1 
ATOM   10033 O OD1 . ASP G  1 1   ? -20.266 5.606   4.850   1.00 66.73  ? -7  ASP G OD1 1 
ATOM   10034 O OD2 . ASP G  1 1   ? -20.581 6.222   2.761   1.00 70.35  ? -7  ASP G OD2 1 
ATOM   10035 N N   . TYR G  1 2   ? -17.109 8.788   2.184   1.00 61.87  ? -6  TYR G N   1 
ATOM   10036 C CA  . TYR G  1 2   ? -16.512 9.891   1.422   1.00 57.19  ? -6  TYR G CA  1 
ATOM   10037 C C   . TYR G  1 2   ? -16.805 11.283  1.988   1.00 57.97  ? -6  TYR G C   1 
ATOM   10038 O O   . TYR G  1 2   ? -15.936 12.156  1.998   1.00 54.02  ? -6  TYR G O   1 
ATOM   10039 C CB  . TYR G  1 2   ? -17.022 9.857   -0.026  1.00 59.86  ? -6  TYR G CB  1 
ATOM   10040 C CG  . TYR G  1 2   ? -17.130 8.474   -0.624  1.00 70.69  ? -6  TYR G CG  1 
ATOM   10041 C CD1 . TYR G  1 2   ? -16.133 7.979   -1.462  1.00 79.11  ? -6  TYR G CD1 1 
ATOM   10042 C CD2 . TYR G  1 2   ? -18.233 7.661   -0.363  1.00 74.55  ? -6  TYR G CD2 1 
ATOM   10043 C CE1 . TYR G  1 2   ? -16.226 6.707   -2.022  1.00 82.74  ? -6  TYR G CE1 1 
ATOM   10044 C CE2 . TYR G  1 2   ? -18.333 6.388   -0.912  1.00 85.51  ? -6  TYR G CE2 1 
ATOM   10045 C CZ  . TYR G  1 2   ? -17.326 5.917   -1.742  1.00 81.42  ? -6  TYR G CZ  1 
ATOM   10046 O OH  . TYR G  1 2   ? -17.419 4.658   -2.292  1.00 59.51  ? -6  TYR G OH  1 
ATOM   10047 N N   . LYS G  1 3   ? -18.038 11.491  2.444   1.00 61.92  ? -5  LYS G N   1 
ATOM   10048 C CA  . LYS G  1 3   ? -18.496 12.818  2.858   1.00 59.25  ? -5  LYS G CA  1 
ATOM   10049 C C   . LYS G  1 3   ? -17.956 13.255  4.219   1.00 53.61  ? -5  LYS G C   1 
ATOM   10050 O O   . LYS G  1 3   ? -18.325 14.318  4.732   1.00 47.68  ? -5  LYS G O   1 
ATOM   10051 C CB  . LYS G  1 3   ? -20.028 12.879  2.824   1.00 57.45  ? -5  LYS G CB  1 
ATOM   10052 C CG  . LYS G  1 3   ? -20.582 12.835  1.406   1.00 62.20  ? -5  LYS G CG  1 
ATOM   10053 C CD  . LYS G  1 3   ? -21.988 12.267  1.334   1.00 62.11  ? -5  LYS G CD  1 
ATOM   10054 C CE  . LYS G  1 3   ? -22.406 12.090  -0.127  1.00 62.30  ? -5  LYS G CE  1 
ATOM   10055 N NZ  . LYS G  1 3   ? -23.715 11.388  -0.285  1.00 53.54  ? -5  LYS G NZ  1 
ATOM   10056 N N   . ASP G  1 4   ? -17.070 12.439  4.786   1.00 49.75  ? -4  ASP G N   1 
ATOM   10057 C CA  . ASP G  1 4   ? -16.485 12.718  6.095   1.00 46.35  ? -4  ASP G CA  1 
ATOM   10058 C C   . ASP G  1 4   ? -14.994 13.074  6.030   1.00 35.19  ? -4  ASP G C   1 
ATOM   10059 O O   . ASP G  1 4   ? -14.432 13.554  7.011   1.00 32.11  ? -4  ASP G O   1 
ATOM   10060 C CB  . ASP G  1 4   ? -16.709 11.530  7.035   1.00 44.17  ? -4  ASP G CB  1 
ATOM   10061 C CG  . ASP G  1 4   ? -18.186 11.308  7.366   1.00 49.71  ? -4  ASP G CG  1 
ATOM   10062 O OD1 . ASP G  1 4   ? -18.851 12.267  7.819   1.00 47.82  ? -4  ASP G OD1 1 
ATOM   10063 O OD2 . ASP G  1 4   ? -18.683 10.171  7.168   1.00 52.67  ? -4  ASP G OD2 1 
ATOM   10064 N N   . ASP G  1 5   ? -14.382 12.858  4.865   1.00 41.43  ? -3  ASP G N   1 
ATOM   10065 C CA  . ASP G  1 5   ? -12.938 13.059  4.631   1.00 35.75  ? -3  ASP G CA  1 
ATOM   10066 C C   . ASP G  1 5   ? -12.362 14.406  5.048   1.00 27.84  ? -3  ASP G C   1 
ATOM   10067 O O   . ASP G  1 5   ? -11.197 14.494  5.435   1.00 24.65  ? -3  ASP G O   1 
ATOM   10068 C CB  . ASP G  1 5   ? -12.597 12.853  3.152   1.00 30.13  ? -3  ASP G CB  1 
ATOM   10069 C CG  . ASP G  1 5   ? -12.799 11.429  2.699   1.00 39.35  ? -3  ASP G CG  1 
ATOM   10070 O OD1 . ASP G  1 5   ? -12.880 10.524  3.566   1.00 33.78  ? -3  ASP G OD1 1 
ATOM   10071 O OD2 . ASP G  1 5   ? -12.868 11.219  1.467   1.00 48.04  ? -3  ASP G OD2 1 
ATOM   10072 N N   . ASP G  1 6   ? -13.166 15.455  4.951   1.00 28.28  ? -2  ASP G N   1 
ATOM   10073 C CA  . ASP G  1 6   ? -12.650 16.793  5.187   1.00 28.85  ? -2  ASP G CA  1 
ATOM   10074 C C   . ASP G  1 6   ? -13.015 17.396  6.547   1.00 26.85  ? -2  ASP G C   1 
ATOM   10075 O O   . ASP G  1 6   ? -12.944 18.607  6.728   1.00 32.01  ? -2  ASP G O   1 
ATOM   10076 C CB  . ASP G  1 6   ? -13.029 17.733  4.032   1.00 33.75  ? -2  ASP G CB  1 
ATOM   10077 C CG  . ASP G  1 6   ? -12.342 17.355  2.707   1.00 34.76  ? -2  ASP G CG  1 
ATOM   10078 O OD1 . ASP G  1 6   ? -12.020 16.165  2.487   1.00 24.49  ? -2  ASP G OD1 1 
ATOM   10079 O OD2 . ASP G  1 6   ? -12.133 18.262  1.876   1.00 37.69  ? -2  ASP G OD2 1 
ATOM   10080 N N   . ASP G  1 7   ? -13.392 16.564  7.510   1.00 25.63  ? -1  ASP G N   1 
ATOM   10081 C CA  . ASP G  1 7   ? -13.463 17.058  8.875   1.00 23.91  ? -1  ASP G CA  1 
ATOM   10082 C C   . ASP G  1 7   ? -12.090 17.021  9.519   1.00 16.87  ? -1  ASP G C   1 
ATOM   10083 O O   . ASP G  1 7   ? -11.550 15.946  9.780   1.00 18.25  ? -1  ASP G O   1 
ATOM   10084 C CB  . ASP G  1 7   ? -14.440 16.272  9.746   1.00 26.56  ? -1  ASP G CB  1 
ATOM   10085 C CG  . ASP G  1 7   ? -14.471 16.799  11.177  1.00 25.06  ? -1  ASP G CG  1 
ATOM   10086 O OD1 . ASP G  1 7   ? -14.544 18.031  11.370  1.00 26.14  ? -1  ASP G OD1 1 
ATOM   10087 O OD2 . ASP G  1 7   ? -14.372 15.994  12.116  1.00 29.74  ? -1  ASP G OD2 1 
ATOM   10088 N N   . LYS G  1 8   ? -11.545 18.199  9.789   1.00 13.69  ? 0   LYS G N   1 
ATOM   10089 C CA  . LYS G  1 8   ? -10.195 18.341  10.322  1.00 16.00  ? 0   LYS G CA  1 
ATOM   10090 C C   . LYS G  1 8   ? -10.016 17.630  11.669  1.00 18.98  ? 0   LYS G C   1 
ATOM   10091 O O   . LYS G  1 8   ? -9.001  16.951  11.913  1.00 13.92  ? 0   LYS G O   1 
ATOM   10092 C CB  . LYS G  1 8   ? -9.858  19.827  10.465  1.00 16.22  ? 0   LYS G CB  1 
ATOM   10093 C CG  . LYS G  1 8   ? -8.378  20.130  10.532  1.00 15.64  ? 0   LYS G CG  1 
ATOM   10094 C CD  . LYS G  1 8   ? -8.111  21.629  10.517  1.00 13.77  ? 0   LYS G CD  1 
ATOM   10095 C CE  . LYS G  1 8   ? -6.680  21.913  10.952  1.00 13.55  ? 0   LYS G CE  1 
ATOM   10096 N NZ  . LYS G  1 8   ? -6.358  23.368  10.955  1.00 26.00  ? 0   LYS G NZ  1 
ATOM   10097 N N   . LEU G  1 9   ? -11.009 17.785  12.541  1.00 18.24  ? 1   LEU G N   1 
ATOM   10098 C CA  . LEU G  1 9   ? -10.935 17.194  13.869  1.00 16.02  ? 1   LEU G CA  1 
ATOM   10099 C C   . LEU G  1 9   ? -10.897 15.671  13.826  1.00 15.40  ? 1   LEU G C   1 
ATOM   10100 O O   . LEU G  1 9   ? -10.084 15.054  14.510  1.00 18.57  ? 1   LEU G O   1 
ATOM   10101 C CB  . LEU G  1 9   ? -12.086 17.681  14.749  1.00 21.44  ? 1   LEU G CB  1 
ATOM   10102 C CG  . LEU G  1 9   ? -11.892 17.359  16.221  1.00 13.29  ? 1   LEU G CG  1 
ATOM   10103 C CD1 . LEU G  1 9   ? -10.703 18.155  16.754  1.00 14.27  ? 1   LEU G CD1 1 
ATOM   10104 C CD2 . LEU G  1 9   ? -13.160 17.652  16.979  1.00 15.54  ? 1   LEU G CD2 1 
ATOM   10105 N N   . ASP G  1 10  ? -11.766 15.059  13.034  1.00 14.46  ? 2   ASP G N   1 
ATOM   10106 C CA  . ASP G  1 10  ? -11.701 13.612  12.864  1.00 17.85  ? 2   ASP G CA  1 
ATOM   10107 C C   . ASP G  1 10  ? -10.313 13.196  12.376  1.00 17.50  ? 2   ASP G C   1 
ATOM   10108 O O   . ASP G  1 10  ? -9.774  12.182  12.820  1.00 15.89  ? 2   ASP G O   1 
ATOM   10109 C CB  . ASP G  1 10  ? -12.782 13.096  11.900  1.00 26.52  ? 2   ASP G CB  1 
ATOM   10110 C CG  . ASP G  1 10  ? -14.205 13.193  12.476  1.00 26.37  ? 2   ASP G CG  1 
ATOM   10111 O OD1 . ASP G  1 10  ? -14.358 13.433  13.695  1.00 24.73  ? 2   ASP G OD1 1 
ATOM   10112 O OD2 . ASP G  1 10  ? -15.174 13.035  11.693  1.00 27.51  ? 2   ASP G OD2 1 
ATOM   10113 N N   . ARG G  1 11  ? -9.731  13.990  11.472  1.00 19.33  ? 3   ARG G N   1 
ATOM   10114 C CA  . ARG G  1 11  ? -8.400  13.694  10.926  1.00 16.70  ? 3   ARG G CA  1 
ATOM   10115 C C   . ARG G  1 11  ? -7.325  13.795  11.997  1.00 13.64  ? 3   ARG G C   1 
ATOM   10116 O O   . ARG G  1 11  ? -6.468  12.913  12.096  1.00 11.30  ? 3   ARG G O   1 
ATOM   10117 C CB  . ARG G  1 11  ? -8.056  14.607  9.738   1.00 15.92  ? 3   ARG G CB  1 
ATOM   10118 C CG  . ARG G  1 11  ? -8.974  14.427  8.531   1.00 17.44  ? 3   ARG G CG  1 
ATOM   10119 C CD  . ARG G  1 11  ? -8.494  15.200  7.321   1.00 17.12  ? 3   ARG G CD  1 
ATOM   10120 N NE  . ARG G  1 11  ? -7.418  14.507  6.618   1.00 18.87  ? 3   ARG G NE  1 
ATOM   10121 C CZ  . ARG G  1 11  ? -7.592  13.759  5.529   1.00 23.73  ? 3   ARG G CZ  1 
ATOM   10122 N NH1 . ARG G  1 11  ? -8.808  13.593  5.010   1.00 24.33  ? 3   ARG G NH1 1 
ATOM   10123 N NH2 . ARG G  1 11  ? -6.549  13.170  4.956   1.00 17.82  ? 3   ARG G NH2 1 
ATOM   10124 N N   . ALA G  1 12  ? -7.379  14.859  12.803  1.00 12.37  ? 4   ALA G N   1 
ATOM   10125 C CA  . ALA G  1 12  ? -6.453  15.010  13.918  1.00 11.02  ? 4   ALA G CA  1 
ATOM   10126 C C   . ALA G  1 12  ? -6.535  13.798  14.837  1.00 12.51  ? 4   ALA G C   1 
ATOM   10127 O O   . ALA G  1 12  ? -5.520  13.289  15.322  1.00 11.19  ? 4   ALA G O   1 
ATOM   10128 C CB  . ALA G  1 12  ? -6.746  16.278  14.698  1.00 11.99  ? 4   ALA G CB  1 
ATOM   10129 N N   . ASP G  1 13  ? -7.754  13.324  15.057  1.00 13.75  ? 5   ASP G N   1 
ATOM   10130 C CA  . ASP G  1 13  ? -7.973  12.251  16.013  1.00 13.71  ? 5   ASP G CA  1 
ATOM   10131 C C   . ASP G  1 13  ? -7.487  10.909  15.496  1.00 13.12  ? 5   ASP G C   1 
ATOM   10132 O O   . ASP G  1 13  ? -6.907  10.128  16.244  1.00 14.34  ? 5   ASP G O   1 
ATOM   10133 C CB  . ASP G  1 13  ? -9.428  12.226  16.466  1.00 10.37  ? 5   ASP G CB  1 
ATOM   10134 C CG  . ASP G  1 13  ? -9.768  13.437  17.303  1.00 15.40  ? 5   ASP G CG  1 
ATOM   10135 O OD1 . ASP G  1 13  ? -8.817  14.179  17.639  1.00 14.34  ? 5   ASP G OD1 1 
ATOM   10136 O OD2 . ASP G  1 13  ? -10.956 13.661  17.639  1.00 24.99  ? 5   ASP G OD2 1 
ATOM   10137 N N   . ILE G  1 14  ? -7.710  10.650  14.215  1.00 11.97  ? 6   ILE G N   1 
ATOM   10138 C CA  . ILE G  1 14  ? -7.098  9.502   13.569  1.00 11.29  ? 6   ILE G CA  1 
ATOM   10139 C C   . ILE G  1 14  ? -5.568  9.561   13.693  1.00 11.14  ? 6   ILE G C   1 
ATOM   10140 O O   . ILE G  1 14  ? -4.944  8.577   14.109  1.00 9.35   ? 6   ILE G O   1 
ATOM   10141 C CB  . ILE G  1 14  ? -7.538  9.400   12.098  1.00 15.08  ? 6   ILE G CB  1 
ATOM   10142 C CG1 . ILE G  1 14  ? -9.022  9.007   12.038  1.00 14.50  ? 6   ILE G CG1 1 
ATOM   10143 C CG2 . ILE G  1 14  ? -6.664  8.399   11.347  1.00 8.76   ? 6   ILE G CG2 1 
ATOM   10144 C CD1 . ILE G  1 14  ? -9.809  9.683   10.949  1.00 15.13  ? 6   ILE G CD1 1 
ATOM   10145 N N   . LEU G  1 15  ? -4.974  10.713  13.363  1.00 10.49  ? 7   LEU G N   1 
ATOM   10146 C CA  . LEU G  1 15  ? -3.518  10.893  13.481  1.00 9.55   ? 7   LEU G CA  1 
ATOM   10147 C C   . LEU G  1 15  ? -3.028  10.564  14.890  1.00 11.10  ? 7   LEU G C   1 
ATOM   10148 O O   . LEU G  1 15  ? -2.085  9.784   15.065  1.00 10.28  ? 7   LEU G O   1 
ATOM   10149 C CB  . LEU G  1 15  ? -3.098  12.317  13.100  1.00 9.62   ? 7   LEU G CB  1 
ATOM   10150 C CG  . LEU G  1 15  ? -1.617  12.498  12.729  1.00 12.58  ? 7   LEU G CG  1 
ATOM   10151 C CD1 . LEU G  1 15  ? -1.238  11.516  11.639  1.00 10.24  ? 7   LEU G CD1 1 
ATOM   10152 C CD2 . LEU G  1 15  ? -1.305  13.911  12.274  1.00 8.49   ? 7   LEU G CD2 1 
ATOM   10153 N N   . TYR G  1 16  ? -3.687  11.155  15.886  1.00 8.98   ? 8   TYR G N   1 
ATOM   10154 C CA  . TYR G  1 16  ? -3.433  10.849  17.288  1.00 9.69   ? 8   TYR G CA  1 
ATOM   10155 C C   . TYR G  1 16  ? -3.566  9.340   17.598  1.00 9.77   ? 8   TYR G C   1 
ATOM   10156 O O   . TYR G  1 16  ? -2.668  8.748   18.187  1.00 10.08  ? 8   TYR G O   1 
ATOM   10157 C CB  . TYR G  1 16  ? -4.336  11.725  18.181  1.00 13.21  ? 8   TYR G CB  1 
ATOM   10158 C CG  . TYR G  1 16  ? -4.391  11.359  19.650  1.00 14.23  ? 8   TYR G CG  1 
ATOM   10159 C CD1 . TYR G  1 16  ? -3.296  11.559  20.490  1.00 15.33  ? 8   TYR G CD1 1 
ATOM   10160 C CD2 . TYR G  1 16  ? -5.555  10.840  20.210  1.00 15.00  ? 8   TYR G CD2 1 
ATOM   10161 C CE1 . TYR G  1 16  ? -3.354  11.226  21.839  1.00 13.62  ? 8   TYR G CE1 1 
ATOM   10162 C CE2 . TYR G  1 16  ? -5.626  10.518  21.563  1.00 12.50  ? 8   TYR G CE2 1 
ATOM   10163 C CZ  . TYR G  1 16  ? -4.527  10.708  22.366  1.00 15.25  ? 8   TYR G CZ  1 
ATOM   10164 O OH  . TYR G  1 16  ? -4.607  10.370  23.703  1.00 19.65  ? 8   TYR G OH  1 
ATOM   10165 N N   . ASN G  1 17  ? -4.658  8.712   17.178  1.00 8.96   ? 9   ASN G N   1 
ATOM   10166 C CA  . ASN G  1 17  ? -4.849  7.286   17.444  1.00 10.49  ? 9   ASN G CA  1 
ATOM   10167 C C   . ASN G  1 17  ? -3.745  6.428   16.859  1.00 11.66  ? 9   ASN G C   1 
ATOM   10168 O O   . ASN G  1 17  ? -3.206  5.561   17.542  1.00 13.71  ? 9   ASN G O   1 
ATOM   10169 C CB  . ASN G  1 17  ? -6.215  6.804   16.950  1.00 10.44  ? 9   ASN G CB  1 
ATOM   10170 C CG  . ASN G  1 17  ? -7.344  7.509   17.633  1.00 12.01  ? 9   ASN G CG  1 
ATOM   10171 O OD1 . ASN G  1 17  ? -7.183  8.000   18.752  1.00 18.06  ? 9   ASN G OD1 1 
ATOM   10172 N ND2 . ASN G  1 17  ? -8.495  7.573   16.980  1.00 13.38  ? 9   ASN G ND2 1 
ATOM   10173 N N   . ILE G  1 18  ? -3.413  6.687   15.594  1.00 12.74  ? 10  ILE G N   1 
ATOM   10174 C CA  . ILE G  1 18  ? -2.268  6.067   14.916  1.00 10.39  ? 10  ILE G CA  1 
ATOM   10175 C C   . ILE G  1 18  ? -0.967  6.268   15.686  1.00 8.28   ? 10  ILE G C   1 
ATOM   10176 O O   . ILE G  1 18  ? -0.254  5.319   15.970  1.00 9.86   ? 10  ILE G O   1 
ATOM   10177 C CB  . ILE G  1 18  ? -2.102  6.623   13.471  1.00 8.68   ? 10  ILE G CB  1 
ATOM   10178 C CG1 . ILE G  1 18  ? -3.235  6.145   12.576  1.00 7.11   ? 10  ILE G CG1 1 
ATOM   10179 C CG2 . ILE G  1 18  ? -0.788  6.198   12.870  1.00 7.61   ? 10  ILE G CG2 1 
ATOM   10180 C CD1 . ILE G  1 18  ? -3.246  6.813   11.258  1.00 8.64   ? 10  ILE G CD1 1 
ATOM   10181 N N   . ARG G  1 19  ? -0.648  7.503   16.033  1.00 8.48   ? 11  ARG G N   1 
ATOM   10182 C CA  . ARG G  1 19  ? 0.597   7.740   16.754  1.00 10.18  ? 11  ARG G CA  1 
ATOM   10183 C C   . ARG G  1 19  ? 0.669   7.034   18.126  1.00 12.53  ? 11  ARG G C   1 
ATOM   10184 O O   . ARG G  1 19  ? 1.746   6.593   18.527  1.00 13.27  ? 11  ARG G O   1 
ATOM   10185 C CB  . ARG G  1 19  ? 0.886   9.237   16.841  1.00 8.67   ? 11  ARG G CB  1 
ATOM   10186 C CG  . ARG G  1 19  ? 1.300   9.807   15.504  1.00 10.86  ? 11  ARG G CG  1 
ATOM   10187 C CD  . ARG G  1 19  ? 1.200   11.324  15.413  1.00 15.02  ? 11  ARG G CD  1 
ATOM   10188 N NE  . ARG G  1 19  ? 2.099   11.821  14.368  1.00 14.25  ? 11  ARG G NE  1 
ATOM   10189 C CZ  . ARG G  1 19  ? 2.158   13.080  13.944  1.00 11.63  ? 11  ARG G CZ  1 
ATOM   10190 N NH1 . ARG G  1 19  ? 1.346   13.997  14.456  1.00 14.15  ? 11  ARG G NH1 1 
ATOM   10191 N NH2 . ARG G  1 19  ? 3.038   13.418  13.008  1.00 10.02  ? 11  ARG G NH2 1 
ATOM   10192 N N   . GLN G  1 20  ? -0.472  6.903   18.816  1.00 11.64  ? 12  GLN G N   1 
ATOM   10193 C CA  . GLN G  1 20  ? -0.555  6.151   20.081  1.00 12.58  ? 12  GLN G CA  1 
ATOM   10194 C C   . GLN G  1 20  ? -0.396  4.637   19.896  1.00 12.85  ? 12  GLN G C   1 
ATOM   10195 O O   . GLN G  1 20  ? 0.313   3.983   20.651  1.00 15.56  ? 12  GLN G O   1 
ATOM   10196 C CB  . GLN G  1 20  ? -1.894  6.392   20.777  1.00 12.22  ? 12  GLN G CB  1 
ATOM   10197 C CG  . GLN G  1 20  ? -2.216  7.827   21.093  1.00 14.24  ? 12  GLN G CG  1 
ATOM   10198 C CD  . GLN G  1 20  ? -1.492  8.316   22.310  1.00 23.11  ? 12  GLN G CD  1 
ATOM   10199 O OE1 . GLN G  1 20  ? -0.489  9.028   22.207  1.00 29.95  ? 12  GLN G OE1 1 
ATOM   10200 N NE2 . GLN G  1 20  ? -1.990  7.933   23.487  1.00 24.03  ? 12  GLN G NE2 1 
ATOM   10201 N N   . THR G  1 21  ? -1.078  4.080   18.904  1.00 10.77  ? 13  THR G N   1 
ATOM   10202 C CA  . THR G  1 21  ? -1.088  2.635   18.711  1.00 14.07  ? 13  THR G CA  1 
ATOM   10203 C C   . THR G  1 21  ? 0.193   2.100   18.058  1.00 14.38  ? 13  THR G C   1 
ATOM   10204 O O   . THR G  1 21  ? 0.625   0.990   18.348  1.00 16.47  ? 13  THR G O   1 
ATOM   10205 C CB  . THR G  1 21  ? -2.310  2.199   17.874  1.00 15.39  ? 13  THR G CB  1 
ATOM   10206 O OG1 . THR G  1 21  ? -3.506  2.648   18.518  1.00 26.68  ? 13  THR G OG1 1 
ATOM   10207 C CG2 . THR G  1 21  ? -2.367  0.692   17.754  1.00 15.13  ? 13  THR G CG2 1 
ATOM   10208 N N   . SER G  1 22  ? 0.794   2.909   17.192  1.00 16.25  ? 14  SER G N   1 
ATOM   10209 C CA  . SER G  1 22  ? 1.912   2.503   16.349  1.00 11.58  ? 14  SER G CA  1 
ATOM   10210 C C   . SER G  1 22  ? 3.231   2.330   17.062  1.00 15.45  ? 14  SER G C   1 
ATOM   10211 O O   . SER G  1 22  ? 3.705   3.240   17.749  1.00 18.52  ? 14  SER G O   1 
ATOM   10212 C CB  . SER G  1 22  ? 2.145   3.539   15.269  1.00 12.73  ? 14  SER G CB  1 
ATOM   10213 O OG  . SER G  1 22  ? 3.515   3.525   14.888  1.00 18.04  ? 14  SER G OG  1 
ATOM   10214 N N   . ARG G  1 23  ? 3.838   1.168   16.857  1.00 17.30  ? 15  ARG G N   1 
ATOM   10215 C CA  . ARG G  1 23  ? 5.192   0.905   17.316  1.00 15.68  ? 15  ARG G CA  1 
ATOM   10216 C C   . ARG G  1 23  ? 6.083   0.923   16.069  1.00 16.19  ? 15  ARG G C   1 
ATOM   10217 O O   . ARG G  1 23  ? 6.126   -0.053  15.327  1.00 13.53  ? 15  ARG G O   1 
ATOM   10218 C CB  . ARG G  1 23  ? 5.246   -0.463  18.003  1.00 15.60  ? 15  ARG G CB  1 
ATOM   10219 C CG  . ARG G  1 23  ? 3.899   -0.947  18.540  1.00 17.48  ? 15  ARG G CG  1 
ATOM   10220 C CD  . ARG G  1 23  ? 4.019   -2.111  19.534  1.00 16.64  ? 15  ARG G CD  1 
ATOM   10221 N NE  . ARG G  1 23  ? 4.499   -1.632  20.830  1.00 29.75  ? 15  ARG G NE  1 
ATOM   10222 C CZ  . ARG G  1 23  ? 4.026   -2.007  22.023  1.00 27.56  ? 15  ARG G CZ  1 
ATOM   10223 N NH1 . ARG G  1 23  ? 3.036   -2.893  22.134  1.00 16.48  ? 15  ARG G NH1 1 
ATOM   10224 N NH2 . ARG G  1 23  ? 4.554   -1.479  23.122  1.00 26.44  ? 15  ARG G NH2 1 
ATOM   10225 N N   . PRO G  1 24  ? 6.776   2.045   15.819  1.00 14.33  ? 16  PRO G N   1 
ATOM   10226 C CA  . PRO G  1 24  ? 7.505   2.233   14.559  1.00 14.89  ? 16  PRO G CA  1 
ATOM   10227 C C   . PRO G  1 24  ? 8.735   1.334   14.376  1.00 17.56  ? 16  PRO G C   1 
ATOM   10228 O O   . PRO G  1 24  ? 9.323   1.309   13.288  1.00 21.43  ? 16  PRO G O   1 
ATOM   10229 C CB  . PRO G  1 24  ? 7.944   3.702   14.627  1.00 15.25  ? 16  PRO G CB  1 
ATOM   10230 C CG  . PRO G  1 24  ? 7.071   4.328   15.621  1.00 9.92   ? 16  PRO G CG  1 
ATOM   10231 C CD  . PRO G  1 24  ? 6.800   3.265   16.637  1.00 13.46  ? 16  PRO G CD  1 
ATOM   10232 N N   . ASP G  1 25  ? 9.115   0.596   15.411  1.00 14.36  ? 17  ASP G N   1 
ATOM   10233 C CA  . ASP G  1 25  ? 10.322  -0.202  15.351  1.00 8.04   ? 17  ASP G CA  1 
ATOM   10234 C C   . ASP G  1 25  ? 10.040  -1.669  15.563  1.00 11.32  ? 17  ASP G C   1 
ATOM   10235 O O   . ASP G  1 25  ? 10.956  -2.458  15.734  1.00 18.16  ? 17  ASP G O   1 
ATOM   10236 C CB  . ASP G  1 25  ? 11.332  0.290   16.383  1.00 10.97  ? 17  ASP G CB  1 
ATOM   10237 C CG  . ASP G  1 25  ? 11.738  1.749   16.163  1.00 19.62  ? 17  ASP G CG  1 
ATOM   10238 O OD1 . ASP G  1 25  ? 11.837  2.171   14.982  1.00 24.14  ? 17  ASP G OD1 1 
ATOM   10239 O OD2 . ASP G  1 25  ? 11.966  2.472   17.166  1.00 17.69  ? 17  ASP G OD2 1 
ATOM   10240 N N   . VAL G  1 26  ? 8.772   -2.051  15.556  1.00 13.65  ? 18  VAL G N   1 
ATOM   10241 C CA  . VAL G  1 26  ? 8.426   -3.453  15.746  1.00 13.45  ? 18  VAL G CA  1 
ATOM   10242 C C   . VAL G  1 26  ? 7.552   -3.974  14.605  1.00 14.57  ? 18  VAL G C   1 
ATOM   10243 O O   . VAL G  1 26  ? 6.691   -3.256  14.093  1.00 15.03  ? 18  VAL G O   1 
ATOM   10244 C CB  . VAL G  1 26  ? 7.747   -3.660  17.104  1.00 15.35  ? 18  VAL G CB  1 
ATOM   10245 C CG1 . VAL G  1 26  ? 7.313   -5.112  17.282  1.00 16.29  ? 18  VAL G CG1 1 
ATOM   10246 C CG2 . VAL G  1 26  ? 8.692   -3.244  18.218  1.00 13.25  ? 18  VAL G CG2 1 
ATOM   10247 N N   . ILE G  1 27  ? 7.778   -5.210  14.177  1.00 16.17  ? 19  ILE G N   1 
ATOM   10248 C CA  . ILE G  1 27  ? 7.029   -5.694  13.032  1.00 16.97  ? 19  ILE G CA  1 
ATOM   10249 C C   . ILE G  1 27  ? 5.571   -5.956  13.373  1.00 17.02  ? 19  ILE G C   1 
ATOM   10250 O O   . ILE G  1 27  ? 5.247   -6.520  14.408  1.00 15.55  ? 19  ILE G O   1 
ATOM   10251 C CB  . ILE G  1 27  ? 7.678   -6.906  12.357  1.00 16.64  ? 19  ILE G CB  1 
ATOM   10252 C CG1 . ILE G  1 27  ? 7.961   -8.008  13.368  1.00 16.68  ? 19  ILE G CG1 1 
ATOM   10253 C CG2 . ILE G  1 27  ? 8.969   -6.486  11.636  1.00 17.71  ? 19  ILE G CG2 1 
ATOM   10254 C CD1 . ILE G  1 27  ? 8.596   -9.240  12.727  1.00 21.83  ? 19  ILE G CD1 1 
ATOM   10255 N N   . PRO G  1 28  ? 4.677   -5.507  12.500  1.00 18.38  ? 20  PRO G N   1 
ATOM   10256 C CA  . PRO G  1 28  ? 3.252   -5.763  12.708  1.00 15.15  ? 20  PRO G CA  1 
ATOM   10257 C C   . PRO G  1 28  ? 2.872   -7.193  12.338  1.00 20.96  ? 20  PRO G C   1 
ATOM   10258 O O   . PRO G  1 28  ? 2.149   -7.400  11.365  1.00 25.74  ? 20  PRO G O   1 
ATOM   10259 C CB  . PRO G  1 28  ? 2.577   -4.758  11.777  1.00 14.23  ? 20  PRO G CB  1 
ATOM   10260 C CG  . PRO G  1 28  ? 3.601   -4.434  10.752  1.00 19.71  ? 20  PRO G CG  1 
ATOM   10261 C CD  . PRO G  1 28  ? 4.940   -4.584  11.384  1.00 14.83  ? 20  PRO G CD  1 
ATOM   10262 N N   . THR G  1 29  ? 3.360   -8.164  13.111  1.00 24.26  ? 21  THR G N   1 
ATOM   10263 C CA  . THR G  1 29  ? 3.003   -9.571  12.920  1.00 26.06  ? 21  THR G CA  1 
ATOM   10264 C C   . THR G  1 29  ? 1.683   -9.866  13.600  1.00 30.77  ? 21  THR G C   1 
ATOM   10265 O O   . THR G  1 29  ? 1.477   -9.523  14.771  1.00 33.25  ? 21  THR G O   1 
ATOM   10266 C CB  . THR G  1 29  ? 4.083   -10.543 13.471  1.00 27.51  ? 21  THR G CB  1 
ATOM   10267 O OG1 . THR G  1 29  ? 4.531   -10.099 14.753  1.00 25.54  ? 21  THR G OG1 1 
ATOM   10268 C CG2 . THR G  1 29  ? 5.282   -10.616 12.538  1.00 28.89  ? 21  THR G CG2 1 
ATOM   10269 N N   . GLN G  1 30  ? 0.785   -10.502 12.857  1.00 45.90  ? 22  GLN G N   1 
ATOM   10270 C CA  . GLN G  1 30  ? -0.557  -10.796 13.350  1.00 49.43  ? 22  GLN G CA  1 
ATOM   10271 C C   . GLN G  1 30  ? -0.746  -12.295 13.540  1.00 56.93  ? 22  GLN G C   1 
ATOM   10272 O O   . GLN G  1 30  ? -0.747  -13.054 12.569  1.00 61.30  ? 22  GLN G O   1 
ATOM   10273 C CB  . GLN G  1 30  ? -1.603  -10.275 12.366  1.00 47.19  ? 22  GLN G CB  1 
ATOM   10274 C CG  . GLN G  1 30  ? -1.309  -8.886  11.816  1.00 41.24  ? 22  GLN G CG  1 
ATOM   10275 C CD  . GLN G  1 30  ? -2.340  -8.444  10.792  1.00 48.97  ? 22  GLN G CD  1 
ATOM   10276 O OE1 . GLN G  1 30  ? -3.203  -9.226  10.387  1.00 53.64  ? 22  GLN G OE1 1 
ATOM   10277 N NE2 . GLN G  1 30  ? -2.257  -7.185  10.368  1.00 41.16  ? 22  GLN G NE2 1 
ATOM   10278 N N   . ARG G  1 31  ? -0.902  -12.706 14.796  1.00 58.47  ? 23  ARG G N   1 
ATOM   10279 C CA  . ARG G  1 31  ? -1.155  -14.103 15.171  1.00 66.01  ? 23  ARG G CA  1 
ATOM   10280 C C   . ARG G  1 31  ? -0.085  -15.073 14.665  1.00 60.98  ? 23  ARG G C   1 
ATOM   10281 O O   . ARG G  1 31  ? -0.391  -16.082 14.021  1.00 61.16  ? 23  ARG G O   1 
ATOM   10282 C CB  . ARG G  1 31  ? -2.552  -14.560 14.727  1.00 62.06  ? 23  ARG G CB  1 
ATOM   10283 C CG  . ARG G  1 31  ? -3.112  -15.720 15.553  1.00 62.23  ? 23  ARG G CG  1 
ATOM   10284 C CD  . ARG G  1 31  ? -4.407  -16.238 14.953  1.00 69.38  ? 23  ARG G CD  1 
ATOM   10285 N NE  . ARG G  1 31  ? -5.343  -15.153 14.663  1.00 73.56  ? 23  ARG G NE  1 
ATOM   10286 C CZ  . ARG G  1 31  ? -6.296  -14.740 15.494  1.00 65.16  ? 23  ARG G CZ  1 
ATOM   10287 N NH1 . ARG G  1 31  ? -6.447  -15.321 16.675  1.00 50.19  ? 23  ARG G NH1 1 
ATOM   10288 N NH2 . ARG G  1 31  ? -7.100  -13.747 15.140  1.00 68.24  ? 23  ARG G NH2 1 
ATOM   10289 N N   . ASP G  1 32  ? 1.168   -14.753 14.956  1.00 49.99  ? 24  ASP G N   1 
ATOM   10290 C CA  . ASP G  1 32  ? 2.284   -15.632 14.612  1.00 58.23  ? 24  ASP G CA  1 
ATOM   10291 C C   . ASP G  1 32  ? 2.416   -16.042 13.133  1.00 55.56  ? 24  ASP G C   1 
ATOM   10292 O O   . ASP G  1 32  ? 2.633   -17.213 12.819  1.00 55.45  ? 24  ASP G O   1 
ATOM   10293 C CB  . ASP G  1 32  ? 2.309   -16.852 15.534  1.00 57.57  ? 24  ASP G CB  1 
ATOM   10294 C CG  . ASP G  1 32  ? 3.016   -16.564 16.842  1.00 58.51  ? 24  ASP G CG  1 
ATOM   10295 O OD1 . ASP G  1 32  ? 4.249   -16.786 16.899  1.00 53.39  ? 24  ASP G OD1 1 
ATOM   10296 O OD2 . ASP G  1 32  ? 2.349   -16.095 17.796  1.00 54.24  ? 24  ASP G OD2 1 
ATOM   10297 N N   . ARG G  1 33  ? 2.297   -15.065 12.239  1.00 51.66  ? 25  ARG G N   1 
ATOM   10298 C CA  . ARG G  1 33  ? 2.592   -15.262 10.825  1.00 48.93  ? 25  ARG G CA  1 
ATOM   10299 C C   . ARG G  1 33  ? 3.336   -14.049 10.251  1.00 42.48  ? 25  ARG G C   1 
ATOM   10300 O O   . ARG G  1 33  ? 3.173   -12.928 10.732  1.00 41.11  ? 25  ARG G O   1 
ATOM   10301 C CB  . ARG G  1 33  ? 1.311   -15.545 10.036  1.00 52.45  ? 25  ARG G CB  1 
ATOM   10302 C CG  . ARG G  1 33  ? 0.768   -16.964 10.203  1.00 62.49  ? 25  ARG G CG  1 
ATOM   10303 C CD  . ARG G  1 33  ? -0.550  -17.128 9.461   1.00 64.33  ? 25  ARG G CD  1 
ATOM   10304 N NE  . ARG G  1 33  ? -1.307  -15.879 9.474   1.00 67.08  ? 25  ARG G NE  1 
ATOM   10305 C CZ  . ARG G  1 33  ? -1.997  -15.425 10.519  1.00 69.98  ? 25  ARG G CZ  1 
ATOM   10306 N NH1 . ARG G  1 33  ? -2.037  -16.118 11.653  1.00 64.89  ? 25  ARG G NH1 1 
ATOM   10307 N NH2 . ARG G  1 33  ? -2.643  -14.269 10.430  1.00 67.15  ? 25  ARG G NH2 1 
ATOM   10308 N N   . PRO G  1 34  ? 4.174   -14.277 9.229   1.00 41.06  ? 26  PRO G N   1 
ATOM   10309 C CA  . PRO G  1 34  ? 4.975   -13.219 8.605   1.00 38.14  ? 26  PRO G CA  1 
ATOM   10310 C C   . PRO G  1 34  ? 4.148   -12.016 8.211   1.00 25.65  ? 26  PRO G C   1 
ATOM   10311 O O   . PRO G  1 34  ? 2.969   -12.162 7.936   1.00 29.84  ? 26  PRO G O   1 
ATOM   10312 C CB  . PRO G  1 34  ? 5.507   -13.899 7.341   1.00 35.80  ? 26  PRO G CB  1 
ATOM   10313 C CG  . PRO G  1 34  ? 5.631   -15.323 7.730   1.00 36.26  ? 26  PRO G CG  1 
ATOM   10314 C CD  . PRO G  1 34  ? 4.472   -15.600 8.650   1.00 39.61  ? 26  PRO G CD  1 
ATOM   10315 N N   . VAL G  1 35  ? 4.760   -10.842 8.206   1.00 27.24  ? 27  VAL G N   1 
ATOM   10316 C CA  . VAL G  1 35  ? 4.102   -9.661  7.674   1.00 26.35  ? 27  VAL G CA  1 
ATOM   10317 C C   . VAL G  1 35  ? 4.203   -9.741  6.165   1.00 30.51  ? 27  VAL G C   1 
ATOM   10318 O O   . VAL G  1 35  ? 5.281   -10.005 5.621   1.00 26.88  ? 27  VAL G O   1 
ATOM   10319 C CB  . VAL G  1 35  ? 4.783   -8.351  8.117   1.00 23.09  ? 27  VAL G CB  1 
ATOM   10320 C CG1 . VAL G  1 35  ? 3.796   -7.206  8.030   1.00 19.27  ? 27  VAL G CG1 1 
ATOM   10321 C CG2 . VAL G  1 35  ? 5.331   -8.473  9.515   1.00 23.34  ? 27  VAL G CG2 1 
ATOM   10322 N N   . ALA G  1 36  ? 3.085   -9.504  5.493   1.00 25.00  ? 28  ALA G N   1 
ATOM   10323 C CA  . ALA G  1 36  ? 3.035   -9.640  4.055   1.00 20.52  ? 28  ALA G CA  1 
ATOM   10324 C C   . ALA G  1 36  ? 3.241   -8.294  3.410   1.00 24.72  ? 28  ALA G C   1 
ATOM   10325 O O   . ALA G  1 36  ? 2.306   -7.502  3.270   1.00 23.16  ? 28  ALA G O   1 
ATOM   10326 C CB  . ALA G  1 36  ? 1.706   -10.225 3.627   1.00 22.04  ? 28  ALA G CB  1 
ATOM   10327 N N   . VAL G  1 37  ? 4.470   -8.025  3.004   1.00 24.39  ? 29  VAL G N   1 
ATOM   10328 C CA  . VAL G  1 37  ? 4.724   -6.788  2.294   1.00 24.81  ? 29  VAL G CA  1 
ATOM   10329 C C   . VAL G  1 37  ? 4.568   -7.031  0.792   1.00 29.45  ? 29  VAL G C   1 
ATOM   10330 O O   . VAL G  1 37  ? 5.031   -8.042  0.271   1.00 29.65  ? 29  VAL G O   1 
ATOM   10331 C CB  . VAL G  1 37  ? 6.105   -6.201  2.643   1.00 18.45  ? 29  VAL G CB  1 
ATOM   10332 C CG1 . VAL G  1 37  ? 6.435   -5.042  1.733   1.00 22.73  ? 29  VAL G CG1 1 
ATOM   10333 C CG2 . VAL G  1 37  ? 6.120   -5.742  4.081   1.00 22.05  ? 29  VAL G CG2 1 
ATOM   10334 N N   . SER G  1 38  ? 3.876   -6.115  0.122   1.00 22.21  ? 30  SER G N   1 
ATOM   10335 C CA  . SER G  1 38  ? 3.738   -6.144  -1.319  1.00 24.76  ? 30  SER G CA  1 
ATOM   10336 C C   . SER G  1 38  ? 4.581   -5.041  -1.942  1.00 31.82  ? 30  SER G C   1 
ATOM   10337 O O   . SER G  1 38  ? 4.439   -3.866  -1.593  1.00 30.76  ? 30  SER G O   1 
ATOM   10338 C CB  . SER G  1 38  ? 2.276   -5.948  -1.721  1.00 25.44  ? 30  SER G CB  1 
ATOM   10339 O OG  . SER G  1 38  ? 1.509   -7.112  -1.469  1.00 32.12  ? 30  SER G OG  1 
ATOM   10340 N N   . VAL G  1 39  ? 5.462   -5.414  -2.866  1.00 29.18  ? 31  VAL G N   1 
ATOM   10341 C CA  . VAL G  1 39  ? 6.215   -4.422  -3.613  1.00 29.81  ? 31  VAL G CA  1 
ATOM   10342 C C   . VAL G  1 39  ? 5.955   -4.568  -5.106  1.00 37.46  ? 31  VAL G C   1 
ATOM   10343 O O   . VAL G  1 39  ? 5.785   -5.678  -5.613  1.00 37.61  ? 31  VAL G O   1 
ATOM   10344 C CB  . VAL G  1 39  ? 7.733   -4.529  -3.366  1.00 36.84  ? 31  VAL G CB  1 
ATOM   10345 C CG1 . VAL G  1 39  ? 8.394   -3.187  -3.628  1.00 31.65  ? 31  VAL G CG1 1 
ATOM   10346 C CG2 . VAL G  1 39  ? 8.024   -4.998  -1.945  1.00 36.75  ? 31  VAL G CG2 1 
ATOM   10347 N N   . SER G  1 40  ? 5.927   -3.437  -5.801  1.00 35.70  ? 32  SER G N   1 
ATOM   10348 C CA  . SER G  1 40  ? 5.760   -3.414  -7.245  1.00 39.17  ? 32  SER G CA  1 
ATOM   10349 C C   . SER G  1 40  ? 6.316   -2.099  -7.783  1.00 36.94  ? 32  SER G C   1 
ATOM   10350 O O   . SER G  1 40  ? 5.978   -1.027  -7.285  1.00 37.13  ? 32  SER G O   1 
ATOM   10351 C CB  . SER G  1 40  ? 4.285   -3.567  -7.622  1.00 43.01  ? 32  SER G CB  1 
ATOM   10352 O OG  . SER G  1 40  ? 3.750   -2.347  -8.106  1.00 44.07  ? 32  SER G OG  1 
ATOM   10353 N N   . LEU G  1 41  ? 7.172   -2.180  -8.796  1.00 35.45  ? 33  LEU G N   1 
ATOM   10354 C CA  . LEU G  1 41  ? 7.837   -0.993  -9.307  1.00 27.71  ? 33  LEU G CA  1 
ATOM   10355 C C   . LEU G  1 41  ? 7.131   -0.408  -10.523 1.00 32.07  ? 33  LEU G C   1 
ATOM   10356 O O   . LEU G  1 41  ? 6.753   -1.123  -11.444 1.00 34.99  ? 33  LEU G O   1 
ATOM   10357 C CB  . LEU G  1 41  ? 9.290   -1.303  -9.649  1.00 30.15  ? 33  LEU G CB  1 
ATOM   10358 C CG  . LEU G  1 41  ? 10.199  -1.764  -8.510  1.00 31.58  ? 33  LEU G CG  1 
ATOM   10359 C CD1 . LEU G  1 41  ? 11.641  -1.863  -8.981  1.00 34.08  ? 33  LEU G CD1 1 
ATOM   10360 C CD2 . LEU G  1 41  ? 10.094  -0.809  -7.342  1.00 33.11  ? 33  LEU G CD2 1 
ATOM   10361 N N   . LYS G  1 42  ? 6.936   0.904   -10.497 1.00 34.07  ? 34  LYS G N   1 
ATOM   10362 C CA  . LYS G  1 42  ? 6.476   1.637   -11.660 1.00 30.44  ? 34  LYS G CA  1 
ATOM   10363 C C   . LYS G  1 42  ? 7.668   2.418   -12.179 1.00 31.20  ? 34  LYS G C   1 
ATOM   10364 O O   . LYS G  1 42  ? 8.101   3.400   -11.574 1.00 30.37  ? 34  LYS G O   1 
ATOM   10365 C CB  . LYS G  1 42  ? 5.328   2.595   -11.319 1.00 32.09  ? 34  LYS G CB  1 
ATOM   10366 C CG  . LYS G  1 42  ? 4.106   1.944   -10.693 1.00 37.04  ? 34  LYS G CG  1 
ATOM   10367 C CD  . LYS G  1 42  ? 3.640   0.710   -11.457 1.00 44.19  ? 34  LYS G CD  1 
ATOM   10368 C CE  . LYS G  1 42  ? 2.364   0.122   -10.840 1.00 51.00  ? 34  LYS G CE  1 
ATOM   10369 N NZ  . LYS G  1 42  ? 2.047   -1.248  -11.356 1.00 53.60  ? 34  LYS G NZ  1 
ATOM   10370 N N   . PHE G  1 43  ? 8.218   1.966   -13.295 1.00 32.47  ? 35  PHE G N   1 
ATOM   10371 C CA  . PHE G  1 43  ? 9.364   2.637   -13.851 1.00 25.84  ? 35  PHE G CA  1 
ATOM   10372 C C   . PHE G  1 43  ? 8.921   3.920   -14.501 1.00 26.34  ? 35  PHE G C   1 
ATOM   10373 O O   . PHE G  1 43  ? 7.997   3.921   -15.300 1.00 32.85  ? 35  PHE G O   1 
ATOM   10374 C CB  . PHE G  1 43  ? 10.070  1.728   -14.827 1.00 27.04  ? 35  PHE G CB  1 
ATOM   10375 C CG  . PHE G  1 43  ? 10.985  0.744   -14.167 1.00 22.39  ? 35  PHE G CG  1 
ATOM   10376 C CD1 . PHE G  1 43  ? 10.635  -0.585  -14.065 1.00 24.16  ? 35  PHE G CD1 1 
ATOM   10377 C CD2 . PHE G  1 43  ? 12.193  1.159   -13.638 1.00 19.57  ? 35  PHE G CD2 1 
ATOM   10378 C CE1 . PHE G  1 43  ? 11.476  -1.492  -13.462 1.00 25.35  ? 35  PHE G CE1 1 
ATOM   10379 C CE2 . PHE G  1 43  ? 13.037  0.265   -13.036 1.00 20.35  ? 35  PHE G CE2 1 
ATOM   10380 C CZ  . PHE G  1 43  ? 12.679  -1.072  -12.950 1.00 26.21  ? 35  PHE G CZ  1 
ATOM   10381 N N   . ILE G  1 44  ? 9.564   5.019   -14.126 1.00 27.44  ? 36  ILE G N   1 
ATOM   10382 C CA  . ILE G  1 44  ? 9.179   6.338   -14.616 1.00 28.34  ? 36  ILE G CA  1 
ATOM   10383 C C   . ILE G  1 44  ? 10.203  6.855   -15.626 1.00 28.10  ? 36  ILE G C   1 
ATOM   10384 O O   . ILE G  1 44  ? 9.849   7.513   -16.599 1.00 30.62  ? 36  ILE G O   1 
ATOM   10385 C CB  . ILE G  1 44  ? 9.044   7.367   -13.451 1.00 30.87  ? 36  ILE G CB  1 
ATOM   10386 C CG1 . ILE G  1 44  ? 8.221   6.795   -12.281 1.00 28.81  ? 36  ILE G CG1 1 
ATOM   10387 C CG2 . ILE G  1 44  ? 8.484   8.696   -13.953 1.00 27.70  ? 36  ILE G CG2 1 
ATOM   10388 C CD1 . ILE G  1 44  ? 6.884   6.187   -12.654 1.00 24.16  ? 36  ILE G CD1 1 
ATOM   10389 N N   . ASN G  1 45  ? 11.476  6.551   -15.403 1.00 24.09  ? 37  ASN G N   1 
ATOM   10390 C CA  . ASN G  1 45  ? 12.514  7.092   -16.262 1.00 27.87  ? 37  ASN G CA  1 
ATOM   10391 C C   . ASN G  1 45  ? 13.832  6.328   -16.229 1.00 27.88  ? 37  ASN G C   1 
ATOM   10392 O O   . ASN G  1 45  ? 14.251  5.838   -15.182 1.00 23.54  ? 37  ASN G O   1 
ATOM   10393 C CB  . ASN G  1 45  ? 12.759  8.565   -15.934 1.00 24.21  ? 37  ASN G CB  1 
ATOM   10394 C CG  . ASN G  1 45  ? 13.062  9.380   -17.168 1.00 32.44  ? 37  ASN G CG  1 
ATOM   10395 O OD1 . ASN G  1 45  ? 13.688  8.876   -18.111 1.00 27.62  ? 37  ASN G OD1 1 
ATOM   10396 N ND2 . ASN G  1 45  ? 12.606  10.638  -17.188 1.00 24.78  ? 37  ASN G ND2 1 
ATOM   10397 N N   . ILE G  1 46  ? 14.482  6.216   -17.384 1.00 25.02  ? 38  ILE G N   1 
ATOM   10398 C CA  . ILE G  1 46  ? 15.863  5.739   -17.402 1.00 28.83  ? 38  ILE G CA  1 
ATOM   10399 C C   . ILE G  1 46  ? 16.762  6.860   -17.888 1.00 26.23  ? 38  ILE G C   1 
ATOM   10400 O O   . ILE G  1 46  ? 16.578  7.378   -18.984 1.00 37.24  ? 38  ILE G O   1 
ATOM   10401 C CB  . ILE G  1 46  ? 16.042  4.484   -18.244 1.00 29.23  ? 38  ILE G CB  1 
ATOM   10402 C CG1 . ILE G  1 46  ? 14.967  3.468   -17.881 1.00 28.33  ? 38  ILE G CG1 1 
ATOM   10403 C CG2 . ILE G  1 46  ? 17.410  3.882   -17.994 1.00 29.83  ? 38  ILE G CG2 1 
ATOM   10404 C CD1 . ILE G  1 46  ? 15.105  2.184   -18.610 1.00 27.10  ? 38  ILE G CD1 1 
ATOM   10405 N N   . LEU G  1 47  ? 17.714  7.253   -17.053 1.00 27.14  ? 39  LEU G N   1 
ATOM   10406 C CA  . LEU G  1 47  ? 18.448  8.497   -17.264 1.00 33.37  ? 39  LEU G CA  1 
ATOM   10407 C C   . LEU G  1 47  ? 19.829  8.292   -17.899 1.00 40.19  ? 39  LEU G C   1 
ATOM   10408 O O   . LEU G  1 47  ? 20.173  8.928   -18.901 1.00 44.85  ? 39  LEU G O   1 
ATOM   10409 C CB  . LEU G  1 47  ? 18.594  9.251   -15.941 1.00 26.10  ? 39  LEU G CB  1 
ATOM   10410 C CG  . LEU G  1 47  ? 17.302  9.764   -15.317 1.00 26.06  ? 39  LEU G CG  1 
ATOM   10411 C CD1 . LEU G  1 47  ? 17.601  10.532  -14.035 1.00 22.82  ? 39  LEU G CD1 1 
ATOM   10412 C CD2 . LEU G  1 47  ? 16.546  10.629  -16.304 1.00 26.01  ? 39  LEU G CD2 1 
ATOM   10413 N N   . GLU G  1 48  ? 20.618  7.408   -17.307 1.00 32.17  ? 40  GLU G N   1 
ATOM   10414 C CA  . GLU G  1 48  ? 21.978  7.206   -17.750 1.00 29.23  ? 40  GLU G CA  1 
ATOM   10415 C C   . GLU G  1 48  ? 22.250  5.714   -17.840 1.00 35.60  ? 40  GLU G C   1 
ATOM   10416 O O   . GLU G  1 48  ? 21.991  4.959   -16.901 1.00 35.41  ? 40  GLU G O   1 
ATOM   10417 C CB  . GLU G  1 48  ? 22.949  7.899   -16.783 1.00 37.95  ? 40  GLU G CB  1 
ATOM   10418 C CG  . GLU G  1 48  ? 24.442  7.640   -17.020 1.00 40.05  ? 40  GLU G CG  1 
ATOM   10419 C CD  . GLU G  1 48  ? 25.284  8.920   -16.930 1.00 47.88  ? 40  GLU G CD  1 
ATOM   10420 O OE1 . GLU G  1 48  ? 26.520  8.824   -16.722 1.00 37.78  ? 40  GLU G OE1 1 
ATOM   10421 O OE2 . GLU G  1 48  ? 24.708  10.024  -17.080 1.00 48.34  ? 40  GLU G OE2 1 
ATOM   10422 N N   . VAL G  1 49  ? 22.740  5.279   -18.992 1.00 37.16  ? 41  VAL G N   1 
ATOM   10423 C CA  . VAL G  1 49  ? 23.181  3.904   -19.129 1.00 33.95  ? 41  VAL G CA  1 
ATOM   10424 C C   . VAL G  1 49  ? 24.671  3.876   -19.444 1.00 37.46  ? 41  VAL G C   1 
ATOM   10425 O O   . VAL G  1 49  ? 25.182  4.692   -20.230 1.00 31.32  ? 41  VAL G O   1 
ATOM   10426 C CB  . VAL G  1 49  ? 22.360  3.135   -20.185 1.00 34.75  ? 41  VAL G CB  1 
ATOM   10427 C CG1 . VAL G  1 49  ? 23.036  1.840   -20.548 1.00 38.71  ? 41  VAL G CG1 1 
ATOM   10428 C CG2 . VAL G  1 49  ? 20.973  2.847   -19.657 1.00 38.49  ? 41  VAL G CG2 1 
ATOM   10429 N N   . ASN G  1 50  ? 25.366  2.952   -18.789 1.00 35.43  ? 42  ASN G N   1 
ATOM   10430 C CA  . ASN G  1 50  ? 26.788  2.772   -19.002 1.00 40.20  ? 42  ASN G CA  1 
ATOM   10431 C C   . ASN G  1 50  ? 27.103  1.325   -19.380 1.00 44.40  ? 42  ASN G C   1 
ATOM   10432 O O   . ASN G  1 50  ? 27.007  0.418   -18.544 1.00 34.74  ? 42  ASN G O   1 
ATOM   10433 C CB  . ASN G  1 50  ? 27.555  3.192   -17.755 1.00 40.33  ? 42  ASN G CB  1 
ATOM   10434 C CG  . ASN G  1 50  ? 29.004  3.491   -18.043 1.00 49.85  ? 42  ASN G CG  1 
ATOM   10435 O OD1 . ASN G  1 50  ? 29.715  2.666   -18.619 1.00 48.72  ? 42  ASN G OD1 1 
ATOM   10436 N ND2 . ASN G  1 50  ? 29.455  4.682   -17.652 1.00 53.90  ? 42  ASN G ND2 1 
ATOM   10437 N N   . GLU G  1 51  ? 27.463  1.114   -20.648 1.00 48.57  ? 43  GLU G N   1 
ATOM   10438 C CA  . GLU G  1 51  ? 27.722  -0.230  -21.153 1.00 44.06  ? 43  GLU G CA  1 
ATOM   10439 C C   . GLU G  1 51  ? 29.125  -0.654  -20.757 1.00 41.72  ? 43  GLU G C   1 
ATOM   10440 O O   . GLU G  1 51  ? 29.444  -1.847  -20.744 1.00 35.81  ? 43  GLU G O   1 
ATOM   10441 C CB  . GLU G  1 51  ? 27.517  -0.307  -22.672 1.00 56.23  ? 43  GLU G CB  1 
ATOM   10442 C CG  . GLU G  1 51  ? 27.183  -1.722  -23.186 1.00 59.02  ? 43  GLU G CG  1 
ATOM   10443 C CD  . GLU G  1 51  ? 26.517  -1.728  -24.566 1.00 61.68  ? 43  GLU G CD  1 
ATOM   10444 O OE1 . GLU G  1 51  ? 26.155  -0.636  -25.069 1.00 56.46  ? 43  GLU G OE1 1 
ATOM   10445 O OE2 . GLU G  1 51  ? 26.352  -2.833  -25.142 1.00 60.05  ? 43  GLU G OE2 1 
ATOM   10446 N N   . ILE G  1 52  ? 29.938  0.340   -20.396 1.00 42.88  ? 44  ILE G N   1 
ATOM   10447 C CA  . ILE G  1 52  ? 31.319  0.133   -19.951 1.00 46.22  ? 44  ILE G CA  1 
ATOM   10448 C C   . ILE G  1 52  ? 31.445  -0.306  -18.470 1.00 44.94  ? 44  ILE G C   1 
ATOM   10449 O O   . ILE G  1 52  ? 32.119  -1.296  -18.168 1.00 39.37  ? 44  ILE G O   1 
ATOM   10450 C CB  . ILE G  1 52  ? 32.184  1.397   -20.228 1.00 48.38  ? 44  ILE G CB  1 
ATOM   10451 C CG1 . ILE G  1 52  ? 32.175  1.741   -21.723 1.00 52.65  ? 44  ILE G CG1 1 
ATOM   10452 C CG2 . ILE G  1 52  ? 33.605  1.205   -19.734 1.00 51.63  ? 44  ILE G CG2 1 
ATOM   10453 C CD1 . ILE G  1 52  ? 32.593  0.589   -22.643 1.00 44.76  ? 44  ILE G CD1 1 
ATOM   10454 N N   . THR G  1 53  ? 30.800  0.419   -17.551 1.00 48.70  ? 45  THR G N   1 
ATOM   10455 C CA  . THR G  1 53  ? 30.808  0.031   -16.129 1.00 45.80  ? 45  THR G CA  1 
ATOM   10456 C C   . THR G  1 53  ? 29.667  -0.905  -15.739 1.00 42.47  ? 45  THR G C   1 
ATOM   10457 O O   . THR G  1 53  ? 29.674  -1.460  -14.636 1.00 45.00  ? 45  THR G O   1 
ATOM   10458 C CB  . THR G  1 53  ? 30.772  1.238   -15.168 1.00 43.40  ? 45  THR G CB  1 
ATOM   10459 O OG1 . THR G  1 53  ? 29.739  2.143   -15.571 1.00 44.29  ? 45  THR G OG1 1 
ATOM   10460 C CG2 . THR G  1 53  ? 32.115  1.958   -15.133 1.00 46.38  ? 45  THR G CG2 1 
ATOM   10461 N N   . ASN G  1 54  ? 28.700  -1.072  -16.643 1.00 41.31  ? 46  ASN G N   1 
ATOM   10462 C CA  . ASN G  1 54  ? 27.535  -1.932  -16.420 1.00 38.70  ? 46  ASN G CA  1 
ATOM   10463 C C   . ASN G  1 54  ? 26.619  -1.414  -15.296 1.00 37.12  ? 46  ASN G C   1 
ATOM   10464 O O   . ASN G  1 54  ? 26.233  -2.142  -14.386 1.00 33.35  ? 46  ASN G O   1 
ATOM   10465 C CB  . ASN G  1 54  ? 27.952  -3.399  -16.214 1.00 36.08  ? 46  ASN G CB  1 
ATOM   10466 C CG  . ASN G  1 54  ? 27.681  -4.256  -17.439 1.00 36.07  ? 46  ASN G CG  1 
ATOM   10467 O OD1 . ASN G  1 54  ? 26.940  -3.848  -18.329 1.00 43.95  ? 46  ASN G OD1 1 
ATOM   10468 N ND2 . ASN G  1 54  ? 28.264  -5.449  -17.483 1.00 31.05  ? 46  ASN G ND2 1 
ATOM   10469 N N   . GLU G  1 55  ? 26.278  -0.135  -15.395 1.00 37.21  ? 47  GLU G N   1 
ATOM   10470 C CA  . GLU G  1 55  ? 25.515  0.561   -14.380 1.00 34.45  ? 47  GLU G CA  1 
ATOM   10471 C C   . GLU G  1 55  ? 24.319  1.221   -15.043 1.00 34.27  ? 47  GLU G C   1 
ATOM   10472 O O   . GLU G  1 55  ? 24.380  1.566   -16.218 1.00 33.76  ? 47  GLU G O   1 
ATOM   10473 C CB  . GLU G  1 55  ? 26.393  1.620   -13.693 1.00 37.17  ? 47  GLU G CB  1 
ATOM   10474 C CG  . GLU G  1 55  ? 27.643  1.049   -12.992 1.00 42.12  ? 47  GLU G CG  1 
ATOM   10475 C CD  . GLU G  1 55  ? 28.553  2.126   -12.395 1.00 48.31  ? 47  GLU G CD  1 
ATOM   10476 O OE1 . GLU G  1 55  ? 28.161  3.316   -12.419 1.00 53.49  ? 47  GLU G OE1 1 
ATOM   10477 O OE2 . GLU G  1 55  ? 29.658  1.781   -11.904 1.00 41.12  ? 47  GLU G OE2 1 
ATOM   10478 N N   . VAL G  1 56  ? 23.223  1.379   -14.303 1.00 35.57  ? 48  VAL G N   1 
ATOM   10479 C CA  . VAL G  1 56  ? 22.047  2.084   -14.818 1.00 29.71  ? 48  VAL G CA  1 
ATOM   10480 C C   . VAL G  1 56  ? 21.660  3.204   -13.860 1.00 25.82  ? 48  VAL G C   1 
ATOM   10481 O O   . VAL G  1 56  ? 22.026  3.169   -12.699 1.00 27.36  ? 48  VAL G O   1 
ATOM   10482 C CB  . VAL G  1 56  ? 20.851  1.135   -14.992 1.00 29.93  ? 48  VAL G CB  1 
ATOM   10483 C CG1 . VAL G  1 56  ? 19.903  1.661   -16.048 1.00 26.58  ? 48  VAL G CG1 1 
ATOM   10484 C CG2 . VAL G  1 56  ? 21.326  -0.230  -15.371 1.00 28.33  ? 48  VAL G CG2 1 
ATOM   10485 N N   . ASP G  1 57  ? 20.951  4.210   -14.354 1.00 27.70  ? 49  ASP G N   1 
ATOM   10486 C CA  . ASP G  1 57  ? 20.455  5.282   -13.507 1.00 26.38  ? 49  ASP G CA  1 
ATOM   10487 C C   . ASP G  1 57  ? 18.943  5.459   -13.730 1.00 29.64  ? 49  ASP G C   1 
ATOM   10488 O O   . ASP G  1 57  ? 18.503  5.896   -14.795 1.00 32.45  ? 49  ASP G O   1 
ATOM   10489 C CB  . ASP G  1 57  ? 21.220  6.588   -13.758 1.00 26.27  ? 49  ASP G CB  1 
ATOM   10490 C CG  . ASP G  1 57  ? 21.124  7.564   -12.577 1.00 35.31  ? 49  ASP G CG  1 
ATOM   10491 O OD1 . ASP G  1 57  ? 21.369  7.145   -11.428 1.00 32.49  ? 49  ASP G OD1 1 
ATOM   10492 O OD2 . ASP G  1 57  ? 20.795  8.753   -12.788 1.00 37.60  ? 49  ASP G OD2 1 
ATOM   10493 N N   . VAL G  1 58  ? 18.160  5.130   -12.708 1.00 25.50  ? 50  VAL G N   1 
ATOM   10494 C CA  . VAL G  1 58  ? 16.714  4.987   -12.843 1.00 26.36  ? 50  VAL G CA  1 
ATOM   10495 C C   . VAL G  1 58  ? 15.902  5.821   -11.832 1.00 25.07  ? 50  VAL G C   1 
ATOM   10496 O O   . VAL G  1 58  ? 16.301  5.989   -10.681 1.00 26.20  ? 50  VAL G O   1 
ATOM   10497 C CB  . VAL G  1 58  ? 16.336  3.496   -12.688 1.00 25.47  ? 50  VAL G CB  1 
ATOM   10498 C CG1 . VAL G  1 58  ? 14.842  3.310   -12.510 1.00 23.77  ? 50  VAL G CG1 1 
ATOM   10499 C CG2 . VAL G  1 58  ? 16.855  2.695   -13.883 1.00 30.33  ? 50  VAL G CG2 1 
ATOM   10500 N N   . VAL G  1 59  ? 14.778  6.356   -12.296 1.00 22.22  ? 51  VAL G N   1 
ATOM   10501 C CA  . VAL G  1 59  ? 13.733  6.894   -11.446 1.00 20.22  ? 51  VAL G CA  1 
ATOM   10502 C C   . VAL G  1 59  ? 12.550  5.915   -11.430 1.00 23.45  ? 51  VAL G C   1 
ATOM   10503 O O   . VAL G  1 59  ? 12.128  5.420   -12.474 1.00 23.16  ? 51  VAL G O   1 
ATOM   10504 C CB  . VAL G  1 59  ? 13.284  8.260   -11.962 1.00 20.37  ? 51  VAL G CB  1 
ATOM   10505 C CG1 . VAL G  1 59  ? 12.114  8.797   -11.149 1.00 21.71  ? 51  VAL G CG1 1 
ATOM   10506 C CG2 . VAL G  1 59  ? 14.462  9.219   -11.938 1.00 20.95  ? 51  VAL G CG2 1 
ATOM   10507 N N   . PHE G  1 60  ? 12.022  5.604   -10.252 1.00 25.20  ? 52  PHE G N   1 
ATOM   10508 C CA  . PHE G  1 60  ? 10.898  4.670   -10.197 1.00 26.07  ? 52  PHE G CA  1 
ATOM   10509 C C   . PHE G  1 60  ? 9.998   4.898   -9.001  1.00 28.67  ? 52  PHE G C   1 
ATOM   10510 O O   . PHE G  1 60  ? 10.460  5.308   -7.935  1.00 29.84  ? 52  PHE G O   1 
ATOM   10511 C CB  . PHE G  1 60  ? 11.379  3.214   -10.235 1.00 24.30  ? 52  PHE G CB  1 
ATOM   10512 C CG  . PHE G  1 60  ? 12.305  2.847   -9.112  1.00 25.14  ? 52  PHE G CG  1 
ATOM   10513 C CD1 . PHE G  1 60  ? 11.831  2.174   -7.990  1.00 30.77  ? 52  PHE G CD1 1 
ATOM   10514 C CD2 . PHE G  1 60  ? 13.645  3.165   -9.170  1.00 20.40  ? 52  PHE G CD2 1 
ATOM   10515 C CE1 . PHE G  1 60  ? 12.683  1.828   -6.945  1.00 25.05  ? 52  PHE G CE1 1 
ATOM   10516 C CE2 . PHE G  1 60  ? 14.501  2.822   -8.134  1.00 23.47  ? 52  PHE G CE2 1 
ATOM   10517 C CZ  . PHE G  1 60  ? 14.019  2.158   -7.020  1.00 22.80  ? 52  PHE G CZ  1 
ATOM   10518 N N   . TRP G  1 61  ? 8.706   4.641   -9.190  1.00 29.79  ? 53  TRP G N   1 
ATOM   10519 C CA  . TRP G  1 61  ? 7.734   4.723   -8.108  1.00 23.99  ? 53  TRP G CA  1 
ATOM   10520 C C   . TRP G  1 61  ? 7.684   3.377   -7.414  1.00 27.45  ? 53  TRP G C   1 
ATOM   10521 O O   . TRP G  1 61  ? 7.244   2.395   -8.006  1.00 30.90  ? 53  TRP G O   1 
ATOM   10522 C CB  . TRP G  1 61  ? 6.351   5.076   -8.657  1.00 25.35  ? 53  TRP G CB  1 
ATOM   10523 C CG  . TRP G  1 61  ? 6.236   6.496   -9.140  1.00 25.09  ? 53  TRP G CG  1 
ATOM   10524 C CD1 . TRP G  1 61  ? 7.174   7.488   -9.019  1.00 29.56  ? 53  TRP G CD1 1 
ATOM   10525 C CD2 . TRP G  1 61  ? 5.114   7.088   -9.809  1.00 25.72  ? 53  TRP G CD2 1 
ATOM   10526 N NE1 . TRP G  1 61  ? 6.705   8.663   -9.580  1.00 30.25  ? 53  TRP G NE1 1 
ATOM   10527 C CE2 . TRP G  1 61  ? 5.446   8.444   -10.069 1.00 26.21  ? 53  TRP G CE2 1 
ATOM   10528 C CE3 . TRP G  1 61  ? 3.869   6.604   -10.224 1.00 26.21  ? 53  TRP G CE3 1 
ATOM   10529 C CZ2 . TRP G  1 61  ? 4.576   9.313   -10.723 1.00 21.87  ? 53  TRP G CZ2 1 
ATOM   10530 C CZ3 . TRP G  1 61  ? 3.005   7.470   -10.869 1.00 29.05  ? 53  TRP G CZ3 1 
ATOM   10531 C CH2 . TRP G  1 61  ? 3.362   8.810   -11.113 1.00 30.38  ? 53  TRP G CH2 1 
ATOM   10532 N N   . GLN G  1 62  ? 8.146   3.318   -6.168  1.00 22.47  ? 54  GLN G N   1 
ATOM   10533 C CA  . GLN G  1 62  ? 8.167   2.048   -5.456  1.00 22.36  ? 54  GLN G CA  1 
ATOM   10534 C C   . GLN G  1 62  ? 6.909   1.812   -4.603  1.00 25.67  ? 54  GLN G C   1 
ATOM   10535 O O   . GLN G  1 62  ? 6.870   2.137   -3.414  1.00 27.77  ? 54  GLN G O   1 
ATOM   10536 C CB  . GLN G  1 62  ? 9.422   1.928   -4.603  1.00 19.17  ? 54  GLN G CB  1 
ATOM   10537 C CG  . GLN G  1 62  ? 9.511   0.598   -3.877  1.00 26.41  ? 54  GLN G CG  1 
ATOM   10538 C CD  . GLN G  1 62  ? 10.511  0.617   -2.742  1.00 32.71  ? 54  GLN G CD  1 
ATOM   10539 O OE1 . GLN G  1 62  ? 10.130  0.644   -1.572  1.00 33.01  ? 54  GLN G OE1 1 
ATOM   10540 N NE2 . GLN G  1 62  ? 11.797  0.596   -3.079  1.00 29.80  ? 54  GLN G NE2 1 
ATOM   10541 N N   . GLN G  1 63  ? 5.893   1.224   -5.218  1.00 21.71  ? 55  GLN G N   1 
ATOM   10542 C CA  . GLN G  1 63  ? 4.632   0.948   -4.558  1.00 22.25  ? 55  GLN G CA  1 
ATOM   10543 C C   . GLN G  1 63  ? 4.740   -0.170  -3.512  1.00 24.82  ? 55  GLN G C   1 
ATOM   10544 O O   . GLN G  1 63  ? 4.981   -1.328  -3.844  1.00 27.82  ? 55  GLN G O   1 
ATOM   10545 C CB  . GLN G  1 63  ? 3.593   0.603   -5.617  1.00 32.53  ? 55  GLN G CB  1 
ATOM   10546 C CG  . GLN G  1 63  ? 2.165   0.559   -5.133  1.00 41.66  ? 55  GLN G CG  1 
ATOM   10547 C CD  . GLN G  1 63  ? 1.208   0.207   -6.254  1.00 49.42  ? 55  GLN G CD  1 
ATOM   10548 O OE1 . GLN G  1 63  ? 1.545   0.350   -7.438  1.00 46.12  ? 55  GLN G OE1 1 
ATOM   10549 N NE2 . GLN G  1 63  ? 0.010   -0.265  -5.891  1.00 40.76  ? 55  GLN G NE2 1 
ATOM   10550 N N   . THR G  1 64  ? 4.556   0.193   -2.243  1.00 22.51  ? 56  THR G N   1 
ATOM   10551 C CA  . THR G  1 64  ? 4.694   -0.736  -1.127  1.00 21.13  ? 56  THR G CA  1 
ATOM   10552 C C   . THR G  1 64  ? 3.425   -0.740  -0.264  1.00 19.67  ? 56  THR G C   1 
ATOM   10553 O O   . THR G  1 64  ? 2.918   0.314   0.122   1.00 15.70  ? 56  THR G O   1 
ATOM   10554 C CB  . THR G  1 64  ? 5.891   -0.348  -0.228  1.00 20.91  ? 56  THR G CB  1 
ATOM   10555 O OG1 . THR G  1 64  ? 6.891   0.312   -1.013  1.00 27.21  ? 56  THR G OG1 1 
ATOM   10556 C CG2 . THR G  1 64  ? 6.494   -1.575  0.425   1.00 17.48  ? 56  THR G CG2 1 
ATOM   10557 N N   . THR G  1 65  ? 2.904   -1.925  0.026   1.00 15.53  ? 57  THR G N   1 
ATOM   10558 C CA  . THR G  1 65  ? 1.725   -2.033  0.864   1.00 16.51  ? 57  THR G CA  1 
ATOM   10559 C C   . THR G  1 65  ? 1.851   -3.171  1.846   1.00 19.46  ? 57  THR G C   1 
ATOM   10560 O O   . THR G  1 65  ? 2.461   -4.199  1.541   1.00 20.66  ? 57  THR G O   1 
ATOM   10561 C CB  . THR G  1 65  ? 0.410   -2.266  0.076   1.00 17.52  ? 57  THR G CB  1 
ATOM   10562 O OG1 . THR G  1 65  ? 0.430   -3.556  -0.551  1.00 24.50  ? 57  THR G OG1 1 
ATOM   10563 C CG2 . THR G  1 65  ? 0.185   -1.193  -0.942  1.00 16.98  ? 57  THR G CG2 1 
ATOM   10564 N N   . TRP G  1 66  ? 1.258   -2.978  3.023   1.00 15.76  ? 58  TRP G N   1 
ATOM   10565 C CA  . TRP G  1 66  ? 1.159   -4.039  4.004   1.00 16.73  ? 58  TRP G CA  1 
ATOM   10566 C C   . TRP G  1 66  ? -0.015  -3.734  4.893   1.00 22.04  ? 58  TRP G C   1 
ATOM   10567 O O   . TRP G  1 66  ? -0.664  -2.686  4.747   1.00 21.48  ? 58  TRP G O   1 
ATOM   10568 C CB  . TRP G  1 66  ? 2.446   -4.164  4.821   1.00 15.01  ? 58  TRP G CB  1 
ATOM   10569 C CG  . TRP G  1 66  ? 2.785   -2.944  5.612   1.00 17.65  ? 58  TRP G CG  1 
ATOM   10570 C CD1 . TRP G  1 66  ? 2.532   -2.736  6.933   1.00 16.52  ? 58  TRP G CD1 1 
ATOM   10571 C CD2 . TRP G  1 66  ? 3.457   -1.761  5.142   1.00 18.41  ? 58  TRP G CD2 1 
ATOM   10572 N NE1 . TRP G  1 66  ? 3.000   -1.503  7.314   1.00 15.92  ? 58  TRP G NE1 1 
ATOM   10573 C CE2 . TRP G  1 66  ? 3.562   -0.881  6.234   1.00 13.59  ? 58  TRP G CE2 1 
ATOM   10574 C CE3 . TRP G  1 66  ? 3.975   -1.362  3.905   1.00 16.90  ? 58  TRP G CE3 1 
ATOM   10575 C CZ2 . TRP G  1 66  ? 4.165   0.368   6.132   1.00 13.99  ? 58  TRP G CZ2 1 
ATOM   10576 C CZ3 . TRP G  1 66  ? 4.564   -0.115  3.807   1.00 14.24  ? 58  TRP G CZ3 1 
ATOM   10577 C CH2 . TRP G  1 66  ? 4.657   0.734   4.916   1.00 12.73  ? 58  TRP G CH2 1 
ATOM   10578 N N   . SER G  1 67  ? -0.297  -4.649  5.812   1.00 21.71  ? 59  SER G N   1 
ATOM   10579 C CA  . SER G  1 67  ? -1.427  -4.468  6.706   1.00 23.62  ? 59  SER G CA  1 
ATOM   10580 C C   . SER G  1 67  ? -1.012  -4.472  8.173   1.00 23.99  ? 59  SER G C   1 
ATOM   10581 O O   . SER G  1 67  ? -0.205  -5.316  8.602   1.00 21.91  ? 59  SER G O   1 
ATOM   10582 C CB  . SER G  1 67  ? -2.505  -5.524  6.428   1.00 26.06  ? 59  SER G CB  1 
ATOM   10583 O OG  . SER G  1 67  ? -2.957  -6.135  7.627   1.00 33.04  ? 59  SER G OG  1 
ATOM   10584 N N   . ASP G  1 68  ? -1.558  -3.504  8.916   1.00 19.97  ? 60  ASP G N   1 
ATOM   10585 C CA  . ASP G  1 68  ? -1.454  -3.443  10.376  1.00 23.09  ? 60  ASP G CA  1 
ATOM   10586 C C   . ASP G  1 68  ? -2.854  -3.198  10.978  1.00 25.58  ? 60  ASP G C   1 
ATOM   10587 O O   . ASP G  1 68  ? -3.300  -2.049  11.086  1.00 23.05  ? 60  ASP G O   1 
ATOM   10588 C CB  . ASP G  1 68  ? -0.492  -2.325  10.799  1.00 20.04  ? 60  ASP G CB  1 
ATOM   10589 C CG  . ASP G  1 68  ? -0.172  -2.345  12.311  1.00 26.37  ? 60  ASP G CG  1 
ATOM   10590 O OD1 . ASP G  1 68  ? -0.812  -3.112  13.078  1.00 26.15  ? 60  ASP G OD1 1 
ATOM   10591 O OD2 . ASP G  1 68  ? 0.725   -1.577  12.734  1.00 25.88  ? 60  ASP G OD2 1 
ATOM   10592 N N   . ARG G  1 69  ? -3.551  -4.264  11.367  1.00 22.02  ? 61  ARG G N   1 
ATOM   10593 C CA  . ARG G  1 69  ? -4.950  -4.121  11.760  1.00 22.92  ? 61  ARG G CA  1 
ATOM   10594 C C   . ARG G  1 69  ? -5.108  -3.316  13.045  1.00 21.88  ? 61  ARG G C   1 
ATOM   10595 O O   . ARG G  1 69  ? -6.164  -2.735  13.292  1.00 15.43  ? 61  ARG G O   1 
ATOM   10596 C CB  . ARG G  1 69  ? -5.644  -5.477  11.889  1.00 27.02  ? 61  ARG G CB  1 
ATOM   10597 C CG  . ARG G  1 69  ? -6.045  -6.088  10.561  1.00 36.98  ? 61  ARG G CG  1 
ATOM   10598 C CD  . ARG G  1 69  ? -6.615  -7.487  10.748  1.00 53.84  ? 61  ARG G CD  1 
ATOM   10599 N NE  . ARG G  1 69  ? -6.648  -8.231  9.489   1.00 68.24  ? 61  ARG G NE  1 
ATOM   10600 C CZ  . ARG G  1 69  ? -6.919  -9.531  9.388   1.00 76.75  ? 61  ARG G CZ  1 
ATOM   10601 N NH1 . ARG G  1 69  ? -7.185  -10.245 10.477  1.00 65.54  ? 61  ARG G NH1 1 
ATOM   10602 N NH2 . ARG G  1 69  ? -6.922  -10.120 8.195   1.00 81.22  ? 61  ARG G NH2 1 
ATOM   10603 N N   . THR G  1 70  ? -4.048  -3.260  13.848  1.00 20.35  ? 62  THR G N   1 
ATOM   10604 C CA  . THR G  1 70  ? -4.101  -2.506  15.094  1.00 17.48  ? 62  THR G CA  1 
ATOM   10605 C C   . THR G  1 70  ? -4.272  -0.997  14.854  1.00 16.35  ? 62  THR G C   1 
ATOM   10606 O O   . THR G  1 70  ? -4.603  -0.249  15.764  1.00 16.51  ? 62  THR G O   1 
ATOM   10607 C CB  . THR G  1 70  ? -2.880  -2.792  16.012  1.00 15.71  ? 62  THR G CB  1 
ATOM   10608 O OG1 . THR G  1 70  ? -1.699  -2.190  15.467  1.00 22.06  ? 62  THR G OG1 1 
ATOM   10609 C CG2 . THR G  1 70  ? -2.669  -4.289  16.184  1.00 11.42  ? 62  THR G CG2 1 
ATOM   10610 N N   . LEU G  1 71  ? -4.060  -0.553  13.627  1.00 14.78  ? 63  LEU G N   1 
ATOM   10611 C CA  . LEU G  1 71  ? -4.285  0.843   13.297  1.00 15.59  ? 63  LEU G CA  1 
ATOM   10612 C C   . LEU G  1 71  ? -5.699  1.059   12.735  1.00 18.20  ? 63  LEU G C   1 
ATOM   10613 O O   . LEU G  1 71  ? -6.077  2.191   12.376  1.00 15.47  ? 63  LEU G O   1 
ATOM   10614 C CB  . LEU G  1 71  ? -3.233  1.328   12.295  1.00 16.53  ? 63  LEU G CB  1 
ATOM   10615 C CG  . LEU G  1 71  ? -1.764  1.082   12.660  1.00 21.65  ? 63  LEU G CG  1 
ATOM   10616 C CD1 . LEU G  1 71  ? -0.812  1.641   11.579  1.00 11.38  ? 63  LEU G CD1 1 
ATOM   10617 C CD2 . LEU G  1 71  ? -1.415  1.632   14.048  1.00 14.66  ? 63  LEU G CD2 1 
ATOM   10618 N N   . ALA G  1 72  ? -6.476  -0.022  12.656  1.00 14.67  ? 64  ALA G N   1 
ATOM   10619 C CA  . ALA G  1 72  ? -7.806  0.056   12.056  1.00 13.97  ? 64  ALA G CA  1 
ATOM   10620 C C   . ALA G  1 72  ? -8.716  0.922   12.897  1.00 16.97  ? 64  ALA G C   1 
ATOM   10621 O O   . ALA G  1 72  ? -8.610  0.925   14.119  1.00 16.32  ? 64  ALA G O   1 
ATOM   10622 C CB  . ALA G  1 72  ? -8.411  -1.318  11.906  1.00 9.90   ? 64  ALA G CB  1 
ATOM   10623 N N   . TRP G  1 73  ? -9.609  1.656   12.244  1.00 14.39  ? 65  TRP G N   1 
ATOM   10624 C CA  . TRP G  1 73  ? -10.696 2.291   12.961  1.00 17.92  ? 65  TRP G CA  1 
ATOM   10625 C C   . TRP G  1 73  ? -12.019 2.092   12.230  1.00 20.88  ? 65  TRP G C   1 
ATOM   10626 O O   . TRP G  1 73  ? -12.052 1.539   11.146  1.00 20.27  ? 65  TRP G O   1 
ATOM   10627 C CB  . TRP G  1 73  ? -10.417 3.771   13.233  1.00 15.55  ? 65  TRP G CB  1 
ATOM   10628 C CG  . TRP G  1 73  ? -10.437 4.639   12.019  1.00 19.54  ? 65  TRP G CG  1 
ATOM   10629 C CD1 . TRP G  1 73  ? -11.491 5.356   11.549  1.00 21.46  ? 65  TRP G CD1 1 
ATOM   10630 C CD2 . TRP G  1 73  ? -9.340  4.903   11.126  1.00 19.25  ? 65  TRP G CD2 1 
ATOM   10631 N NE1 . TRP G  1 73  ? -11.128 6.041   10.411  1.00 19.43  ? 65  TRP G NE1 1 
ATOM   10632 C CE2 . TRP G  1 73  ? -9.812  5.784   10.137  1.00 18.24  ? 65  TRP G CE2 1 
ATOM   10633 C CE3 . TRP G  1 73  ? -8.007  4.474   11.069  1.00 15.81  ? 65  TRP G CE3 1 
ATOM   10634 C CZ2 . TRP G  1 73  ? -8.999  6.246   9.102   1.00 21.41  ? 65  TRP G CZ2 1 
ATOM   10635 C CZ3 . TRP G  1 73  ? -7.209  4.928   10.044  1.00 14.99  ? 65  TRP G CZ3 1 
ATOM   10636 C CH2 . TRP G  1 73  ? -7.706  5.801   9.069   1.00 18.78  ? 65  TRP G CH2 1 
ATOM   10637 N N   . ASN G  1 74  ? -13.113 2.514   12.853  1.00 25.65  ? 66  ASN G N   1 
ATOM   10638 C CA  . ASN G  1 74  ? -14.412 2.444   12.220  1.00 26.20  ? 66  ASN G CA  1 
ATOM   10639 C C   . ASN G  1 74  ? -14.667 3.773   11.514  1.00 29.34  ? 66  ASN G C   1 
ATOM   10640 O O   . ASN G  1 74  ? -14.823 4.816   12.158  1.00 25.36  ? 66  ASN G O   1 
ATOM   10641 C CB  . ASN G  1 74  ? -15.493 2.133   13.261  1.00 25.56  ? 66  ASN G CB  1 
ATOM   10642 C CG  . ASN G  1 74  ? -16.857 1.878   12.643  1.00 35.55  ? 66  ASN G CG  1 
ATOM   10643 O OD1 . ASN G  1 74  ? -17.239 2.500   11.654  1.00 32.51  ? 66  ASN G OD1 1 
ATOM   10644 N ND2 . ASN G  1 74  ? -17.606 0.955   13.238  1.00 52.07  ? 66  ASN G ND2 1 
ATOM   10645 N N   . SER G  1 75  ? -14.714 3.724   10.186  1.00 24.67  ? 67  SER G N   1 
ATOM   10646 C CA  . SER G  1 75  ? -14.841 4.934   9.382   1.00 28.65  ? 67  SER G CA  1 
ATOM   10647 C C   . SER G  1 75  ? -16.254 5.172   8.848   1.00 32.62  ? 67  SER G C   1 
ATOM   10648 O O   . SER G  1 75  ? -16.427 5.721   7.757   1.00 34.72  ? 67  SER G O   1 
ATOM   10649 C CB  . SER G  1 75  ? -13.837 4.910   8.219   1.00 33.80  ? 67  SER G CB  1 
ATOM   10650 O OG  . SER G  1 75  ? -13.944 3.718   7.449   1.00 28.46  ? 67  SER G OG  1 
ATOM   10651 N N   . SER G  1 76  ? -17.267 4.758   9.601   1.00 31.26  ? 68  SER G N   1 
ATOM   10652 C CA  . SER G  1 76  ? -18.643 5.003   9.182   1.00 24.23  ? 68  SER G CA  1 
ATOM   10653 C C   . SER G  1 76  ? -18.992 6.495   9.124   1.00 26.58  ? 68  SER G C   1 
ATOM   10654 O O   . SER G  1 76  ? -19.624 6.954   8.173   1.00 26.80  ? 68  SER G O   1 
ATOM   10655 C CB  . SER G  1 76  ? -19.620 4.274   10.107  1.00 26.32  ? 68  SER G CB  1 
ATOM   10656 O OG  . SER G  1 76  ? -19.267 2.908   10.247  1.00 33.37  ? 68  SER G OG  1 
ATOM   10657 N N   . HIS G  1 77  ? -18.501 7.253   10.059  1.00 26.46  ? 69  HIS G N   1 
ATOM   10658 C CA  . HIS G  1 77  ? -18.823 8.642   10.070  1.00 29.93  ? 69  HIS G CA  1 
ATOM   10659 C C   . HIS G  1 77  ? -17.595 9.434   10.292  1.00 33.78  ? 69  HIS G C   1 
ATOM   10660 O O   . HIS G  1 77  ? -17.645 10.463  10.884  1.00 37.40  ? 69  HIS G O   1 
ATOM   10661 C CB  . HIS G  1 77  ? -19.872 8.952   11.141  1.00 30.09  ? 69  HIS G CB  1 
ATOM   10662 C CG  . HIS G  1 77  ? -21.083 8.093   11.049  1.00 32.95  ? 69  HIS G CG  1 
ATOM   10663 N ND1 . HIS G  1 77  ? -22.160 8.415   10.265  1.00 30.90  ? 69  HIS G ND1 1 
ATOM   10664 C CD2 . HIS G  1 77  ? -21.357 6.891   11.589  1.00 28.20  ? 69  HIS G CD2 1 
ATOM   10665 C CE1 . HIS G  1 77  ? -23.046 7.453   10.325  1.00 25.93  ? 69  HIS G CE1 1 
ATOM   10666 N NE2 . HIS G  1 77  ? -22.583 6.516   11.124  1.00 31.53  ? 69  HIS G NE2 1 
ATOM   10667 N N   . SER G  1 78  ? -16.484 8.946   9.780   1.00 36.24  ? 70  SER G N   1 
ATOM   10668 C CA  . SER G  1 78  ? -15.190 9.615   9.830   1.00 38.61  ? 70  SER G CA  1 
ATOM   10669 C C   . SER G  1 78  ? -14.445 9.293   8.512   1.00 34.95  ? 70  SER G C   1 
ATOM   10670 O O   . SER G  1 78  ? -14.885 8.412   7.781   1.00 33.32  ? 70  SER G O   1 
ATOM   10671 C CB  . SER G  1 78  ? -14.425 9.129   11.059  1.00 31.51  ? 70  SER G CB  1 
ATOM   10672 O OG  . SER G  1 78  ? -14.225 7.728   11.012  1.00 31.24  ? 70  SER G OG  1 
ATOM   10673 N N   . PRO G  1 79  ? -13.345 10.017  8.193   1.00 32.21  ? 71  PRO G N   1 
ATOM   10674 C CA  . PRO G  1 79  ? -12.557 9.807   6.967   1.00 26.85  ? 71  PRO G CA  1 
ATOM   10675 C C   . PRO G  1 79  ? -12.032 8.384   6.786   1.00 25.44  ? 71  PRO G C   1 
ATOM   10676 O O   . PRO G  1 79  ? -11.625 7.765   7.760   1.00 24.49  ? 71  PRO G O   1 
ATOM   10677 C CB  . PRO G  1 79  ? -11.369 10.743  7.170   1.00 22.52  ? 71  PRO G CB  1 
ATOM   10678 C CG  . PRO G  1 79  ? -11.899 11.835  7.950   1.00 26.78  ? 71  PRO G CG  1 
ATOM   10679 C CD  . PRO G  1 79  ? -12.849 11.190  8.934   1.00 31.86  ? 71  PRO G CD  1 
ATOM   10680 N N   . ASP G  1 80  ? -12.014 7.885   5.551   1.00 29.30  ? 72  ASP G N   1 
ATOM   10681 C CA  . ASP G  1 80  ? -11.618 6.496   5.297   1.00 27.12  ? 72  ASP G CA  1 
ATOM   10682 C C   . ASP G  1 80  ? -10.107 6.303   5.264   1.00 24.67  ? 72  ASP G C   1 
ATOM   10683 O O   . ASP G  1 80  ? -9.603  5.192   5.466   1.00 23.48  ? 72  ASP G O   1 
ATOM   10684 C CB  . ASP G  1 80  ? -12.242 5.975   4.001   1.00 29.62  ? 72  ASP G CB  1 
ATOM   10685 C CG  . ASP G  1 80  ? -13.719 6.301   3.897   1.00 40.15  ? 72  ASP G CG  1 
ATOM   10686 O OD1 . ASP G  1 80  ? -14.521 5.722   4.672   1.00 35.93  ? 72  ASP G OD1 1 
ATOM   10687 O OD2 . ASP G  1 80  ? -14.072 7.143   3.040   1.00 50.13  ? 72  ASP G OD2 1 
ATOM   10688 N N   . GLN G  1 81  ? -9.382  7.385   5.011   1.00 24.25  ? 73  GLN G N   1 
ATOM   10689 C CA  . GLN G  1 81  ? -7.929  7.326   5.026   1.00 21.21  ? 73  GLN G CA  1 
ATOM   10690 C C   . GLN G  1 81  ? -7.288  8.667   5.394   1.00 20.62  ? 73  GLN G C   1 
ATOM   10691 O O   . GLN G  1 81  ? -7.901  9.728   5.238   1.00 19.68  ? 73  GLN G O   1 
ATOM   10692 C CB  . GLN G  1 81  ? -7.407  6.805   3.684   1.00 22.63  ? 73  GLN G CB  1 
ATOM   10693 C CG  . GLN G  1 81  ? -7.941  7.553   2.477   1.00 31.81  ? 73  GLN G CG  1 
ATOM   10694 C CD  . GLN G  1 81  ? -7.968  6.706   1.214   1.00 37.73  ? 73  GLN G CD  1 
ATOM   10695 O OE1 . GLN G  1 81  ? -7.062  5.896   0.963   1.00 28.07  ? 73  GLN G OE1 1 
ATOM   10696 N NE2 . GLN G  1 81  ? -9.025  6.878   0.416   1.00 35.20  ? 73  GLN G NE2 1 
ATOM   10697 N N   . VAL G  1 82  ? -6.067  8.606   5.923   1.00 20.38  ? 74  VAL G N   1 
ATOM   10698 C CA  . VAL G  1 82  ? -5.258  9.812   6.124   1.00 22.16  ? 74  VAL G CA  1 
ATOM   10699 C C   . VAL G  1 82  ? -3.805  9.628   5.657   1.00 15.38  ? 74  VAL G C   1 
ATOM   10700 O O   . VAL G  1 82  ? -3.312  8.505   5.536   1.00 12.56  ? 74  VAL G O   1 
ATOM   10701 C CB  . VAL G  1 82  ? -5.253  10.289  7.618   1.00 17.83  ? 74  VAL G CB  1 
ATOM   10702 C CG1 . VAL G  1 82  ? -6.647  10.687  8.072   1.00 13.74  ? 74  VAL G CG1 1 
ATOM   10703 C CG2 . VAL G  1 82  ? -4.660  9.231   8.514   1.00 11.82  ? 74  VAL G CG2 1 
ATOM   10704 N N   . SER G  1 83  ? -3.132  10.745  5.403   1.00 16.16  ? 75  SER G N   1 
ATOM   10705 C CA  . SER G  1 83  ? -1.677  10.757  5.241   1.00 16.77  ? 75  SER G CA  1 
ATOM   10706 C C   . SER G  1 83  ? -1.029  10.883  6.624   1.00 19.40  ? 75  SER G C   1 
ATOM   10707 O O   . SER G  1 83  ? -1.562  11.564  7.510   1.00 18.26  ? 75  SER G O   1 
ATOM   10708 C CB  . SER G  1 83  ? -1.248  11.932  4.369   1.00 17.65  ? 75  SER G CB  1 
ATOM   10709 O OG  . SER G  1 83  ? -2.167  12.139  3.301   1.00 21.04  ? 75  SER G OG  1 
ATOM   10710 N N   . VAL G  1 84  ? 0.086   10.191  6.839   1.00 14.05  ? 76  VAL G N   1 
ATOM   10711 C CA  . VAL G  1 84  ? 0.833   10.332  8.087   1.00 13.92  ? 76  VAL G CA  1 
ATOM   10712 C C   . VAL G  1 84  ? 2.321   10.197  7.771   1.00 13.57  ? 76  VAL G C   1 
ATOM   10713 O O   . VAL G  1 84  ? 2.693   9.450   6.870   1.00 12.60  ? 76  VAL G O   1 
ATOM   10714 C CB  . VAL G  1 84  ? 0.356   9.338   9.225   1.00 12.51  ? 76  VAL G CB  1 
ATOM   10715 C CG1 . VAL G  1 84  ? -0.979  8.694   8.895   1.00 11.42  ? 76  VAL G CG1 1 
ATOM   10716 C CG2 . VAL G  1 84  ? 1.380   8.273   9.520   1.00 9.60   ? 76  VAL G CG2 1 
ATOM   10717 N N   . PRO G  1 85  ? 3.174   10.958  8.478   1.00 13.98  ? 77  PRO G N   1 
ATOM   10718 C CA  . PRO G  1 85  ? 4.616   10.992  8.186   1.00 10.47  ? 77  PRO G CA  1 
ATOM   10719 C C   . PRO G  1 85  ? 5.281   9.666   8.479   1.00 13.10  ? 77  PRO G C   1 
ATOM   10720 O O   . PRO G  1 85  ? 5.103   9.179   9.588   1.00 9.44   ? 77  PRO G O   1 
ATOM   10721 C CB  . PRO G  1 85  ? 5.139   12.038  9.163   1.00 7.52   ? 77  PRO G CB  1 
ATOM   10722 C CG  . PRO G  1 85  ? 3.965   12.907  9.439   1.00 10.48  ? 77  PRO G CG  1 
ATOM   10723 C CD  . PRO G  1 85  ? 2.795   11.968  9.478   1.00 10.57  ? 77  PRO G CD  1 
ATOM   10724 N N   . ILE G  1 86  ? 6.055   9.109   7.539   1.00 16.85  ? 78  ILE G N   1 
ATOM   10725 C CA  . ILE G  1 86  ? 6.628   7.772   7.762   1.00 14.70  ? 78  ILE G CA  1 
ATOM   10726 C C   . ILE G  1 86  ? 7.416   7.617   9.066   1.00 11.37  ? 78  ILE G C   1 
ATOM   10727 O O   . ILE G  1 86  ? 7.519   6.515   9.595   1.00 13.27  ? 78  ILE G O   1 
ATOM   10728 C CB  . ILE G  1 86  ? 7.379   7.171   6.522   1.00 17.29  ? 78  ILE G CB  1 
ATOM   10729 C CG1 . ILE G  1 86  ? 8.582   8.017   6.106   1.00 19.84  ? 78  ILE G CG1 1 
ATOM   10730 C CG2 . ILE G  1 86  ? 6.406   6.948   5.360   1.00 12.35  ? 78  ILE G CG2 1 
ATOM   10731 C CD1 . ILE G  1 86  ? 9.863   7.648   6.834   1.00 20.98  ? 78  ILE G CD1 1 
ATOM   10732 N N   . SER G  1 87  ? 7.923   8.718   9.611   1.00 10.25  ? 79  SER G N   1 
ATOM   10733 C CA  . SER G  1 87  ? 8.560   8.672   10.928  1.00 11.81  ? 79  SER G CA  1 
ATOM   10734 C C   . SER G  1 87  ? 7.608   8.258   12.085  1.00 16.58  ? 79  SER G C   1 
ATOM   10735 O O   . SER G  1 87  ? 8.073   7.830   13.146  1.00 14.44  ? 79  SER G O   1 
ATOM   10736 C CB  . SER G  1 87  ? 9.281   9.995   11.246  1.00 13.59  ? 79  SER G CB  1 
ATOM   10737 O OG  . SER G  1 87  ? 8.436   11.128  11.094  1.00 19.16  ? 79  SER G OG  1 
ATOM   10738 N N   . SER G  1 88  ? 6.291   8.362   11.878  1.00 12.75  ? 80  SER G N   1 
ATOM   10739 C CA  . SER G  1 88  ? 5.323   7.889   12.871  1.00 9.95   ? 80  SER G CA  1 
ATOM   10740 C C   . SER G  1 88  ? 4.946   6.419   12.734  1.00 12.62  ? 80  SER G C   1 
ATOM   10741 O O   . SER G  1 88  ? 4.258   5.871   13.603  1.00 12.89  ? 80  SER G O   1 
ATOM   10742 C CB  . SER G  1 88  ? 4.038   8.716   12.828  1.00 10.26  ? 80  SER G CB  1 
ATOM   10743 O OG  . SER G  1 88  ? 4.267   10.065  13.199  1.00 16.44  ? 80  SER G OG  1 
ATOM   10744 N N   . LEU G  1 89  ? 5.362   5.774   11.649  1.00 11.30  ? 81  LEU G N   1 
ATOM   10745 C CA  . LEU G  1 89  ? 4.883   4.423   11.380  1.00 9.92   ? 81  LEU G CA  1 
ATOM   10746 C C   . LEU G  1 89  ? 6.019   3.473   11.156  1.00 11.12  ? 81  LEU G C   1 
ATOM   10747 O O   . LEU G  1 89  ? 7.084   3.883   10.711  1.00 13.90  ? 81  LEU G O   1 
ATOM   10748 C CB  . LEU G  1 89  ? 4.039   4.401   10.119  1.00 13.31  ? 81  LEU G CB  1 
ATOM   10749 C CG  . LEU G  1 89  ? 2.649   5.004   10.008  1.00 11.37  ? 81  LEU G CG  1 
ATOM   10750 C CD1 . LEU G  1 89  ? 2.292   4.981   8.535   1.00 16.62  ? 81  LEU G CD1 1 
ATOM   10751 C CD2 . LEU G  1 89  ? 1.664   4.191   10.792  1.00 10.47  ? 81  LEU G CD2 1 
ATOM   10752 N N   . TRP G  1 90  ? 5.778   2.197   11.439  1.00 11.44  ? 82  TRP G N   1 
ATOM   10753 C CA  . TRP G  1 90  ? 6.673   1.137   11.002  1.00 13.51  ? 82  TRP G CA  1 
ATOM   10754 C C   . TRP G  1 90  ? 6.639   1.025   9.485   1.00 13.83  ? 82  TRP G C   1 
ATOM   10755 O O   . TRP G  1 90  ? 5.580   1.129   8.872   1.00 9.85   ? 82  TRP G O   1 
ATOM   10756 C CB  . TRP G  1 90  ? 6.284   -0.206  11.597  1.00 11.65  ? 82  TRP G CB  1 
ATOM   10757 C CG  . TRP G  1 90  ? 7.209   -1.317  11.187  1.00 17.75  ? 82  TRP G CG  1 
ATOM   10758 C CD1 . TRP G  1 90  ? 8.382   -1.680  11.799  1.00 16.34  ? 82  TRP G CD1 1 
ATOM   10759 C CD2 . TRP G  1 90  ? 7.052   -2.200  10.067  1.00 16.86  ? 82  TRP G CD2 1 
ATOM   10760 N NE1 . TRP G  1 90  ? 8.953   -2.747  11.133  1.00 19.26  ? 82  TRP G NE1 1 
ATOM   10761 C CE2 . TRP G  1 90  ? 8.161   -3.081  10.066  1.00 16.71  ? 82  TRP G CE2 1 
ATOM   10762 C CE3 . TRP G  1 90  ? 6.076   -2.344  9.076   1.00 16.74  ? 82  TRP G CE3 1 
ATOM   10763 C CZ2 . TRP G  1 90  ? 8.314   -4.094  9.116   1.00 14.78  ? 82  TRP G CZ2 1 
ATOM   10764 C CZ3 . TRP G  1 90  ? 6.237   -3.351  8.126   1.00 19.42  ? 82  TRP G CZ3 1 
ATOM   10765 C CH2 . TRP G  1 90  ? 7.349   -4.212  8.155   1.00 14.86  ? 82  TRP G CH2 1 
ATOM   10766 N N   . VAL G  1 91  ? 7.814   0.795   8.906   1.00 14.28  ? 83  VAL G N   1 
ATOM   10767 C CA  . VAL G  1 91  ? 8.008   0.709   7.460   1.00 15.08  ? 83  VAL G CA  1 
ATOM   10768 C C   . VAL G  1 91  ? 8.995   -0.419  7.199   1.00 16.08  ? 83  VAL G C   1 
ATOM   10769 O O   . VAL G  1 91  ? 10.036  -0.497  7.867   1.00 17.34  ? 83  VAL G O   1 
ATOM   10770 C CB  . VAL G  1 91  ? 8.578   2.027   6.908   1.00 12.00  ? 83  VAL G CB  1 
ATOM   10771 C CG1 . VAL G  1 91  ? 9.135   1.836   5.537   1.00 17.51  ? 83  VAL G CG1 1 
ATOM   10772 C CG2 . VAL G  1 91  ? 7.495   3.089   6.880   1.00 14.81  ? 83  VAL G CG2 1 
ATOM   10773 N N   . PRO G  1 92  ? 8.667   -1.317  6.252   1.00 13.37  ? 84  PRO G N   1 
ATOM   10774 C CA  . PRO G  1 92  ? 9.562   -2.426  5.877   1.00 17.39  ? 84  PRO G CA  1 
ATOM   10775 C C   . PRO G  1 92  ? 10.980  -1.944  5.518   1.00 16.69  ? 84  PRO G C   1 
ATOM   10776 O O   . PRO G  1 92  ? 11.141  -0.947  4.792   1.00 13.21  ? 84  PRO G O   1 
ATOM   10777 C CB  . PRO G  1 92  ? 8.874   -3.031  4.641   1.00 18.28  ? 84  PRO G CB  1 
ATOM   10778 C CG  . PRO G  1 92  ? 7.946   -1.960  4.147   1.00 16.28  ? 84  PRO G CG  1 
ATOM   10779 C CD  . PRO G  1 92  ? 7.476   -1.268  5.396   1.00 12.80  ? 84  PRO G CD  1 
ATOM   10780 N N   . ASP G  1 93  ? 11.988  -2.639  6.042   1.00 16.02  ? 85  ASP G N   1 
ATOM   10781 C CA  . ASP G  1 93  ? 13.389  -2.295  5.786   1.00 19.60  ? 85  ASP G CA  1 
ATOM   10782 C C   . ASP G  1 93  ? 13.908  -2.929  4.484   1.00 25.75  ? 85  ASP G C   1 
ATOM   10783 O O   . ASP G  1 93  ? 14.727  -3.849  4.508   1.00 23.96  ? 85  ASP G O   1 
ATOM   10784 C CB  . ASP G  1 93  ? 14.283  -2.669  6.981   1.00 19.33  ? 85  ASP G CB  1 
ATOM   10785 C CG  . ASP G  1 93  ? 14.245  -4.160  7.317   1.00 25.08  ? 85  ASP G CG  1 
ATOM   10786 O OD1 . ASP G  1 93  ? 13.151  -4.757  7.295   1.00 29.71  ? 85  ASP G OD1 1 
ATOM   10787 O OD2 . ASP G  1 93  ? 15.315  -4.742  7.603   1.00 26.15  ? 85  ASP G OD2 1 
ATOM   10788 N N   . LEU G  1 94  ? 13.423  -2.424  3.351   1.00 22.61  ? 86  LEU G N   1 
ATOM   10789 C CA  . LEU G  1 94  ? 13.749  -2.999  2.058   1.00 24.25  ? 86  LEU G CA  1 
ATOM   10790 C C   . LEU G  1 94  ? 15.095  -2.498  1.575   1.00 25.45  ? 86  LEU G C   1 
ATOM   10791 O O   . LEU G  1 94  ? 15.457  -1.351  1.815   1.00 30.47  ? 86  LEU G O   1 
ATOM   10792 C CB  . LEU G  1 94  ? 12.659  -2.670  1.036   1.00 22.97  ? 86  LEU G CB  1 
ATOM   10793 C CG  . LEU G  1 94  ? 11.278  -3.226  1.387   1.00 21.82  ? 86  LEU G CG  1 
ATOM   10794 C CD1 . LEU G  1 94  ? 10.252  -2.864  0.338   1.00 21.80  ? 86  LEU G CD1 1 
ATOM   10795 C CD2 . LEU G  1 94  ? 11.354  -4.725  1.558   1.00 23.34  ? 86  LEU G CD2 1 
ATOM   10796 N N   . ALA G  1 95  ? 15.847  -3.363  0.907   1.00 27.70  ? 87  ALA G N   1 
ATOM   10797 C CA  . ALA G  1 95  ? 17.085  -2.929  0.255   1.00 30.85  ? 87  ALA G CA  1 
ATOM   10798 C C   . ALA G  1 95  ? 17.219  -3.554  -1.125  1.00 27.24  ? 87  ALA G C   1 
ATOM   10799 O O   . ALA G  1 95  ? 16.734  -4.659  -1.363  1.00 28.58  ? 87  ALA G O   1 
ATOM   10800 C CB  . ALA G  1 95  ? 18.313  -3.262  1.121   1.00 23.57  ? 87  ALA G CB  1 
ATOM   10801 N N   . ALA G  1 96  ? 17.881  -2.847  -2.033  1.00 33.40  ? 88  ALA G N   1 
ATOM   10802 C CA  . ALA G  1 96  ? 18.177  -3.394  -3.356  1.00 24.64  ? 88  ALA G CA  1 
ATOM   10803 C C   . ALA G  1 96  ? 19.552  -4.028  -3.361  1.00 24.47  ? 88  ALA G C   1 
ATOM   10804 O O   . ALA G  1 96  ? 20.559  -3.335  -3.232  1.00 30.03  ? 88  ALA G O   1 
ATOM   10805 C CB  . ALA G  1 96  ? 18.092  -2.316  -4.403  1.00 21.00  ? 88  ALA G CB  1 
ATOM   10806 N N   . TYR G  1 97  ? 19.593  -5.344  -3.530  1.00 30.71  ? 89  TYR G N   1 
ATOM   10807 C CA  . TYR G  1 97  ? 20.845  -6.109  -3.444  1.00 32.55  ? 89  TYR G CA  1 
ATOM   10808 C C   . TYR G  1 97  ? 21.942  -5.658  -4.414  1.00 25.86  ? 89  TYR G C   1 
ATOM   10809 O O   . TYR G  1 97  ? 23.130  -5.726  -4.093  1.00 26.35  ? 89  TYR G O   1 
ATOM   10810 C CB  . TYR G  1 97  ? 20.588  -7.611  -3.633  1.00 36.58  ? 89  TYR G CB  1 
ATOM   10811 C CG  . TYR G  1 97  ? 19.658  -8.252  -2.618  1.00 35.43  ? 89  TYR G CG  1 
ATOM   10812 C CD1 . TYR G  1 97  ? 19.202  -7.552  -1.507  1.00 36.18  ? 89  TYR G CD1 1 
ATOM   10813 C CD2 . TYR G  1 97  ? 19.244  -9.570  -2.773  1.00 43.77  ? 89  TYR G CD2 1 
ATOM   10814 C CE1 . TYR G  1 97  ? 18.351  -8.144  -0.585  1.00 44.00  ? 89  TYR G CE1 1 
ATOM   10815 C CE2 . TYR G  1 97  ? 18.394  -10.171 -1.856  1.00 48.52  ? 89  TYR G CE2 1 
ATOM   10816 C CZ  . TYR G  1 97  ? 17.954  -9.457  -0.763  1.00 45.80  ? 89  TYR G CZ  1 
ATOM   10817 O OH  . TYR G  1 97  ? 17.110  -10.058 0.149   1.00 46.88  ? 89  TYR G OH  1 
ATOM   10818 N N   . ASN G  1 98  ? 21.552  -5.223  -5.607  1.00 30.71  ? 90  ASN G N   1 
ATOM   10819 C CA  . ASN G  1 98  ? 22.531  -4.740  -6.584  1.00 27.41  ? 90  ASN G CA  1 
ATOM   10820 C C   . ASN G  1 98  ? 22.433  -3.243  -6.800  1.00 28.06  ? 90  ASN G C   1 
ATOM   10821 O O   . ASN G  1 98  ? 22.613  -2.748  -7.915  1.00 21.83  ? 90  ASN G O   1 
ATOM   10822 C CB  . ASN G  1 98  ? 22.409  -5.474  -7.917  1.00 28.08  ? 90  ASN G CB  1 
ATOM   10823 C CG  . ASN G  1 98  ? 21.004  -5.465  -8.462  1.00 30.70  ? 90  ASN G CG  1 
ATOM   10824 O OD1 . ASN G  1 98  ? 20.228  -6.382  -8.206  1.00 38.83  ? 90  ASN G OD1 1 
ATOM   10825 N ND2 . ASN G  1 98  ? 20.667  -4.433  -9.223  1.00 30.43  ? 90  ASN G ND2 1 
ATOM   10826 N N   . ALA G  1 99  ? 22.134  -2.525  -5.722  1.00 28.14  ? 91  ALA G N   1 
ATOM   10827 C CA  . ALA G  1 99  ? 22.136  -1.079  -5.782  1.00 24.61  ? 91  ALA G CA  1 
ATOM   10828 C C   . ALA G  1 99  ? 23.543  -0.598  -5.465  1.00 22.06  ? 91  ALA G C   1 
ATOM   10829 O O   . ALA G  1 99  ? 24.268  -1.224  -4.679  1.00 16.55  ? 91  ALA G O   1 
ATOM   10830 C CB  . ALA G  1 99  ? 21.136  -0.505  -4.808  1.00 20.57  ? 91  ALA G CB  1 
ATOM   10831 N N   . ILE G  1 100 ? 23.941  0.499   -6.093  1.00 18.61  ? 92  ILE G N   1 
ATOM   10832 C CA  . ILE G  1 100 ? 25.266  1.037   -5.849  1.00 23.02  ? 92  ILE G CA  1 
ATOM   10833 C C   . ILE G  1 100 ? 25.239  2.518   -5.487  1.00 23.36  ? 92  ILE G C   1 
ATOM   10834 O O   . ILE G  1 100 ? 26.269  3.185   -5.533  1.00 30.56  ? 92  ILE G O   1 
ATOM   10835 C CB  . ILE G  1 100 ? 26.195  0.792   -7.041  1.00 20.92  ? 92  ILE G CB  1 
ATOM   10836 C CG1 . ILE G  1 100 ? 25.650  1.505   -8.276  1.00 22.70  ? 92  ILE G CG1 1 
ATOM   10837 C CG2 . ILE G  1 100 ? 26.352  -0.715  -7.296  1.00 19.01  ? 92  ILE G CG2 1 
ATOM   10838 C CD1 . ILE G  1 100 ? 26.345  1.114   -9.546  1.00 30.15  ? 92  ILE G CD1 1 
ATOM   10839 N N   . SER G  1 101 ? 24.064  3.029   -5.135  1.00 16.43  ? 93  SER G N   1 
ATOM   10840 C CA  . SER G  1 101 ? 23.978  4.317   -4.452  1.00 24.52  ? 93  SER G CA  1 
ATOM   10841 C C   . SER G  1 101 ? 22.819  4.307   -3.436  1.00 24.29  ? 93  SER G C   1 
ATOM   10842 O O   . SER G  1 101 ? 22.013  3.376   -3.434  1.00 20.52  ? 93  SER G O   1 
ATOM   10843 C CB  . SER G  1 101 ? 23.836  5.461   -5.450  1.00 18.60  ? 93  SER G CB  1 
ATOM   10844 O OG  . SER G  1 101 ? 22.548  5.455   -6.030  1.00 23.59  ? 93  SER G OG  1 
ATOM   10845 N N   . LYS G  1 102 ? 22.755  5.310   -2.557  1.00 25.12  ? 94  LYS G N   1 
ATOM   10846 C CA  . LYS G  1 102 ? 21.617  5.440   -1.639  1.00 22.16  ? 94  LYS G CA  1 
ATOM   10847 C C   . LYS G  1 102 ? 20.393  5.760   -2.463  1.00 23.10  ? 94  LYS G C   1 
ATOM   10848 O O   . LYS G  1 102 ? 20.510  6.376   -3.520  1.00 23.04  ? 94  LYS G O   1 
ATOM   10849 C CB  . LYS G  1 102 ? 21.808  6.582   -0.632  1.00 21.30  ? 94  LYS G CB  1 
ATOM   10850 C CG  . LYS G  1 102 ? 23.054  6.529   0.201   1.00 21.44  ? 94  LYS G CG  1 
ATOM   10851 C CD  . LYS G  1 102 ? 22.867  7.246   1.519   1.00 26.29  ? 94  LYS G CD  1 
ATOM   10852 C CE  . LYS G  1 102 ? 21.915  6.468   2.447   1.00 43.04  ? 94  LYS G CE  1 
ATOM   10853 N NZ  . LYS G  1 102 ? 22.342  6.462   3.897   1.00 35.70  ? 94  LYS G NZ  1 
ATOM   10854 N N   . PRO G  1 103 ? 19.209  5.356   -1.984  1.00 22.40  ? 95  PRO G N   1 
ATOM   10855 C CA  . PRO G  1 103 ? 17.991  5.816   -2.657  1.00 21.25  ? 95  PRO G CA  1 
ATOM   10856 C C   . PRO G  1 103 ? 17.865  7.323   -2.508  1.00 22.58  ? 95  PRO G C   1 
ATOM   10857 O O   . PRO G  1 103 ? 17.986  7.827   -1.392  1.00 22.65  ? 95  PRO G O   1 
ATOM   10858 C CB  . PRO G  1 103 ? 16.872  5.124   -1.878  1.00 19.42  ? 95  PRO G CB  1 
ATOM   10859 C CG  . PRO G  1 103 ? 17.515  3.960   -1.204  1.00 25.00  ? 95  PRO G CG  1 
ATOM   10860 C CD  . PRO G  1 103 ? 18.931  4.381   -0.919  1.00 23.90  ? 95  PRO G CD  1 
ATOM   10861 N N   . GLU G  1 104 ? 17.670  8.027   -3.620  1.00 20.69  ? 96  GLU G N   1 
ATOM   10862 C CA  . GLU G  1 104 ? 17.374  9.452   -3.604  1.00 16.84  ? 96  GLU G CA  1 
ATOM   10863 C C   . GLU G  1 104 ? 15.854  9.554   -3.653  1.00 23.91  ? 96  GLU G C   1 
ATOM   10864 O O   . GLU G  1 104 ? 15.251  9.500   -4.734  1.00 25.27  ? 96  GLU G O   1 
ATOM   10865 C CB  . GLU G  1 104 ? 18.018  10.153  -4.815  1.00 23.48  ? 96  GLU G CB  1 
ATOM   10866 C CG  . GLU G  1 104 ? 18.130  11.697  -4.737  1.00 29.97  ? 96  GLU G CG  1 
ATOM   10867 C CD  . GLU G  1 104 ? 18.853  12.328  -5.952  1.00 48.31  ? 96  GLU G CD  1 
ATOM   10868 O OE1 . GLU G  1 104 ? 20.012  11.934  -6.247  1.00 51.15  ? 96  GLU G OE1 1 
ATOM   10869 O OE2 . GLU G  1 104 ? 18.263  13.226  -6.611  1.00 39.92  ? 96  GLU G OE2 1 
ATOM   10870 N N   . VAL G  1 105 ? 15.233  9.651   -2.475  1.00 23.60  ? 97  VAL G N   1 
ATOM   10871 C CA  . VAL G  1 105 ? 13.779  9.765   -2.361  1.00 16.05  ? 97  VAL G CA  1 
ATOM   10872 C C   . VAL G  1 105 ? 13.307  11.148  -2.820  1.00 21.81  ? 97  VAL G C   1 
ATOM   10873 O O   . VAL G  1 105 ? 13.577  12.159  -2.162  1.00 21.70  ? 97  VAL G O   1 
ATOM   10874 C CB  . VAL G  1 105 ? 13.316  9.492   -0.923  1.00 18.08  ? 97  VAL G CB  1 
ATOM   10875 C CG1 . VAL G  1 105 ? 11.843  9.795   -0.770  1.00 18.92  ? 97  VAL G CG1 1 
ATOM   10876 C CG2 . VAL G  1 105 ? 13.612  8.045   -0.542  1.00 17.62  ? 97  VAL G CG2 1 
ATOM   10877 N N   . LEU G  1 106 ? 12.599  11.175  -3.953  1.00 23.04  ? 98  LEU G N   1 
ATOM   10878 C CA  . LEU G  1 106 ? 12.250  12.414  -4.658  1.00 20.35  ? 98  LEU G CA  1 
ATOM   10879 C C   . LEU G  1 106 ? 10.928  13.033  -4.194  1.00 21.89  ? 98  LEU G C   1 
ATOM   10880 O O   . LEU G  1 106 ? 10.686  14.222  -4.408  1.00 17.79  ? 98  LEU G O   1 
ATOM   10881 C CB  . LEU G  1 106 ? 12.164  12.155  -6.172  1.00 18.89  ? 98  LEU G CB  1 
ATOM   10882 C CG  . LEU G  1 106 ? 13.400  11.664  -6.945  1.00 28.25  ? 98  LEU G CG  1 
ATOM   10883 C CD1 . LEU G  1 106 ? 13.020  10.681  -8.066  1.00 24.10  ? 98  LEU G CD1 1 
ATOM   10884 C CD2 . LEU G  1 106 ? 14.194  12.834  -7.523  1.00 25.06  ? 98  LEU G CD2 1 
ATOM   10885 N N   . THR G  1 107 ? 10.060  12.220  -3.596  1.00 22.05  ? 99  THR G N   1 
ATOM   10886 C CA  . THR G  1 107 ? 8.735   12.687  -3.177  1.00 20.18  ? 99  THR G CA  1 
ATOM   10887 C C   . THR G  1 107 ? 8.660   13.016  -1.672  1.00 20.80  ? 99  THR G C   1 
ATOM   10888 O O   . THR G  1 107 ? 9.610   12.729  -0.923  1.00 16.24  ? 99  THR G O   1 
ATOM   10889 C CB  . THR G  1 107 ? 7.648   11.680  -3.583  1.00 17.60  ? 99  THR G CB  1 
ATOM   10890 O OG1 . THR G  1 107 ? 8.159   10.350  -3.473  1.00 20.08  ? 99  THR G OG1 1 
ATOM   10891 C CG2 . THR G  1 107 ? 7.250   11.921  -5.017  1.00 24.16  ? 99  THR G CG2 1 
ATOM   10892 N N   . PRO G  1 108 ? 7.560   13.673  -1.234  1.00 18.50  ? 100 PRO G N   1 
ATOM   10893 C CA  . PRO G  1 108 ? 7.360   13.864  0.206   1.00 15.84  ? 100 PRO G CA  1 
ATOM   10894 C C   . PRO G  1 108 ? 7.219   12.526  0.896   1.00 14.40  ? 100 PRO G C   1 
ATOM   10895 O O   . PRO G  1 108 ? 6.587   11.619  0.365   1.00 14.53  ? 100 PRO G O   1 
ATOM   10896 C CB  . PRO G  1 108 ? 6.053   14.638  0.272   1.00 17.75  ? 100 PRO G CB  1 
ATOM   10897 C CG  . PRO G  1 108 ? 6.025   15.403  -1.038  1.00 17.81  ? 100 PRO G CG  1 
ATOM   10898 C CD  . PRO G  1 108 ? 6.596   14.462  -2.023  1.00 19.16  ? 100 PRO G CD  1 
ATOM   10899 N N   . GLN G  1 109 ? 7.831   12.410  2.067   1.00 19.09  ? 101 GLN G N   1 
ATOM   10900 C CA  . GLN G  1 109 ? 7.880   11.157  2.817   1.00 20.01  ? 101 GLN G CA  1 
ATOM   10901 C C   . GLN G  1 109 ? 6.617   10.812  3.621   1.00 16.14  ? 101 GLN G C   1 
ATOM   10902 O O   . GLN G  1 109 ? 6.714   10.495  4.807   1.00 19.48  ? 101 GLN G O   1 
ATOM   10903 C CB  . GLN G  1 109 ? 9.066   11.214  3.767   1.00 19.32  ? 101 GLN G CB  1 
ATOM   10904 C CG  . GLN G  1 109 ? 10.377  11.483  3.064   1.00 19.65  ? 101 GLN G CG  1 
ATOM   10905 C CD  . GLN G  1 109 ? 11.091  10.198  2.731   1.00 25.31  ? 101 GLN G CD  1 
ATOM   10906 O OE1 . GLN G  1 109 ? 10.514  9.291   2.114   1.00 21.10  ? 101 GLN G OE1 1 
ATOM   10907 N NE2 . GLN G  1 109 ? 12.346  10.091  3.166   1.00 25.94  ? 101 GLN G NE2 1 
ATOM   10908 N N   . LEU G  1 110 ? 5.452   10.837  2.973   1.00 13.46  ? 102 LEU G N   1 
ATOM   10909 C CA  . LEU G  1 110 ? 4.179   10.542  3.642   1.00 15.97  ? 102 LEU G CA  1 
ATOM   10910 C C   . LEU G  1 110 ? 3.575   9.221   3.185   1.00 14.24  ? 102 LEU G C   1 
ATOM   10911 O O   . LEU G  1 110 ? 3.593   8.911   1.998   1.00 14.88  ? 102 LEU G O   1 
ATOM   10912 C CB  . LEU G  1 110 ? 3.171   11.658  3.388   1.00 10.10  ? 102 LEU G CB  1 
ATOM   10913 C CG  . LEU G  1 110 ? 3.574   13.013  3.925   1.00 9.52   ? 102 LEU G CG  1 
ATOM   10914 C CD1 . LEU G  1 110 ? 2.767   14.062  3.253   1.00 8.62   ? 102 LEU G CD1 1 
ATOM   10915 C CD2 . LEU G  1 110 ? 3.300   13.026  5.413   1.00 12.06  ? 102 LEU G CD2 1 
ATOM   10916 N N   . ALA G  1 111 ? 3.040   8.451   4.131   1.00 12.13  ? 103 ALA G N   1 
ATOM   10917 C CA  . ALA G  1 111 ? 2.305   7.231   3.802   1.00 12.81  ? 103 ALA G CA  1 
ATOM   10918 C C   . ALA G  1 111 ? 0.804   7.496   3.849   1.00 12.62  ? 103 ALA G C   1 
ATOM   10919 O O   . ALA G  1 111 ? 0.375   8.560   4.261   1.00 12.61  ? 103 ALA G O   1 
ATOM   10920 C CB  . ALA G  1 111 ? 2.678   6.094   4.744   1.00 9.16   ? 103 ALA G CB  1 
ATOM   10921 N N   . ARG G  1 112 ? 0.011   6.545   3.381   1.00 15.98  ? 104 ARG G N   1 
ATOM   10922 C CA  . ARG G  1 112 ? -1.429  6.631   3.553   1.00 16.42  ? 104 ARG G CA  1 
ATOM   10923 C C   . ARG G  1 112 ? -1.828  5.470   4.429   1.00 19.22  ? 104 ARG G C   1 
ATOM   10924 O O   . ARG G  1 112 ? -1.443  4.321   4.168   1.00 18.61  ? 104 ARG G O   1 
ATOM   10925 C CB  . ARG G  1 112 ? -2.192  6.564   2.226   1.00 15.68  ? 104 ARG G CB  1 
ATOM   10926 C CG  . ARG G  1 112 ? -2.021  7.773   1.332   1.00 17.92  ? 104 ARG G CG  1 
ATOM   10927 C CD  . ARG G  1 112 ? -2.689  9.014   1.884   1.00 13.67  ? 104 ARG G CD  1 
ATOM   10928 N NE  . ARG G  1 112 ? -4.131  9.012   1.661   1.00 19.97  ? 104 ARG G NE  1 
ATOM   10929 C CZ  . ARG G  1 112 ? -4.900  10.097  1.755   1.00 23.25  ? 104 ARG G CZ  1 
ATOM   10930 N NH1 . ARG G  1 112 ? -4.362  11.276  2.061   1.00 19.03  ? 104 ARG G NH1 1 
ATOM   10931 N NH2 . ARG G  1 112 ? -6.206  10.015  1.535   1.00 21.76  ? 104 ARG G NH2 1 
ATOM   10932 N N   . VAL G  1 113 ? -2.578  5.776   5.484   1.00 17.70  ? 105 VAL G N   1 
ATOM   10933 C CA  . VAL G  1 113 ? -3.144  4.744   6.333   1.00 16.21  ? 105 VAL G CA  1 
ATOM   10934 C C   . VAL G  1 113 ? -4.648  4.680   6.064   1.00 17.23  ? 105 VAL G C   1 
ATOM   10935 O O   . VAL G  1 113 ? -5.333  5.704   6.079   1.00 15.61  ? 105 VAL G O   1 
ATOM   10936 C CB  . VAL G  1 113 ? -2.825  5.024   7.801   1.00 14.08  ? 105 VAL G CB  1 
ATOM   10937 C CG1 . VAL G  1 113 ? -3.334  3.908   8.693   1.00 11.79  ? 105 VAL G CG1 1 
ATOM   10938 C CG2 . VAL G  1 113 ? -1.318  5.196   7.958   1.00 14.35  ? 105 VAL G CG2 1 
ATOM   10939 N N   . VAL G  1 114 ? -5.138  3.480   5.768   1.00 15.22  ? 106 VAL G N   1 
ATOM   10940 C CA  . VAL G  1 114 ? -6.546  3.275   5.453   1.00 18.55  ? 106 VAL G CA  1 
ATOM   10941 C C   . VAL G  1 114 ? -7.274  2.697   6.670   1.00 18.75  ? 106 VAL G C   1 
ATOM   10942 O O   . VAL G  1 114 ? -6.667  1.993   7.484   1.00 17.11  ? 106 VAL G O   1 
ATOM   10943 C CB  . VAL G  1 114 ? -6.695  2.331   4.238   1.00 24.97  ? 106 VAL G CB  1 
ATOM   10944 C CG1 . VAL G  1 114 ? -8.088  2.424   3.644   1.00 16.17  ? 106 VAL G CG1 1 
ATOM   10945 C CG2 . VAL G  1 114 ? -5.652  2.672   3.189   1.00 17.90  ? 106 VAL G CG2 1 
ATOM   10946 N N   . SER G  1 115 ? -8.571  2.981   6.789   1.00 20.56  ? 107 SER G N   1 
ATOM   10947 C CA  . SER G  1 115 ? -9.326  2.651   8.006   1.00 16.43  ? 107 SER G CA  1 
ATOM   10948 C C   . SER G  1 115 ? -9.372  1.163   8.332   1.00 16.13  ? 107 SER G C   1 
ATOM   10949 O O   . SER G  1 115 ? -9.601  0.789   9.484   1.00 15.86  ? 107 SER G O   1 
ATOM   10950 C CB  . SER G  1 115 ? -10.739 3.227   7.963   1.00 17.09  ? 107 SER G CB  1 
ATOM   10951 O OG  . SER G  1 115 ? -11.619 2.374   7.261   1.00 23.45  ? 107 SER G OG  1 
ATOM   10952 N N   . ASP G  1 116 ? -9.135  0.315   7.334   1.00 17.25  ? 108 ASP G N   1 
ATOM   10953 C CA  . ASP G  1 116 ? -9.113  -1.127  7.567   1.00 15.33  ? 108 ASP G CA  1 
ATOM   10954 C C   . ASP G  1 116 ? -7.752  -1.635  8.035   1.00 20.97  ? 108 ASP G C   1 
ATOM   10955 O O   . ASP G  1 116 ? -7.555  -2.844  8.156   1.00 23.08  ? 108 ASP G O   1 
ATOM   10956 C CB  . ASP G  1 116 ? -9.518  -1.884  6.316   1.00 14.96  ? 108 ASP G CB  1 
ATOM   10957 C CG  . ASP G  1 116 ? -8.422  -1.886  5.268   1.00 31.70  ? 108 ASP G CG  1 
ATOM   10958 O OD1 . ASP G  1 116 ? -8.419  -0.993  4.388   1.00 31.16  ? 108 ASP G OD1 1 
ATOM   10959 O OD2 . ASP G  1 116 ? -7.548  -2.777  5.330   1.00 43.40  ? 108 ASP G OD2 1 
ATOM   10960 N N   . GLY G  1 117 ? -6.815  -0.720  8.288   1.00 18.66  ? 109 GLY G N   1 
ATOM   10961 C CA  . GLY G  1 117 ? -5.496  -1.090  8.783   1.00 21.32  ? 109 GLY G CA  1 
ATOM   10962 C C   . GLY G  1 117 ? -4.438  -1.319  7.703   1.00 24.16  ? 109 GLY G C   1 
ATOM   10963 O O   . GLY G  1 117 ? -3.504  -2.118  7.861   1.00 20.63  ? 109 GLY G O   1 
ATOM   10964 N N   . GLU G  1 118 ? -4.570  -0.608  6.598   1.00 20.30  ? 110 GLU G N   1 
ATOM   10965 C CA  . GLU G  1 118 ? -3.687  -0.851  5.490   1.00 23.04  ? 110 GLU G CA  1 
ATOM   10966 C C   . GLU G  1 118 ? -2.832  0.369   5.227   1.00 24.03  ? 110 GLU G C   1 
ATOM   10967 O O   . GLU G  1 118 ? -3.332  1.504   5.166   1.00 21.46  ? 110 GLU G O   1 
ATOM   10968 C CB  . GLU G  1 118 ? -4.487  -1.218  4.253   1.00 23.06  ? 110 GLU G CB  1 
ATOM   10969 C CG  . GLU G  1 118 ? -3.756  -2.171  3.350   1.00 30.53  ? 110 GLU G CG  1 
ATOM   10970 C CD  . GLU G  1 118 ? -3.887  -1.801  1.881   1.00 32.80  ? 110 GLU G CD  1 
ATOM   10971 O OE1 . GLU G  1 118 ? -4.960  -1.307  1.482   1.00 35.57  ? 110 GLU G OE1 1 
ATOM   10972 O OE2 . GLU G  1 118 ? -2.910  -1.998  1.127   1.00 29.39  ? 110 GLU G OE2 1 
ATOM   10973 N N   . VAL G  1 119 ? -1.536  0.126   5.074   1.00 16.68  ? 111 VAL G N   1 
ATOM   10974 C CA  . VAL G  1 119 ? -0.584  1.200   4.881   1.00 13.63  ? 111 VAL G CA  1 
ATOM   10975 C C   . VAL G  1 119 ? -0.036  1.146   3.463   1.00 19.51  ? 111 VAL G C   1 
ATOM   10976 O O   . VAL G  1 119 ? 0.370   0.083   2.983   1.00 15.71  ? 111 VAL G O   1 
ATOM   10977 C CB  . VAL G  1 119 ? 0.582   1.081   5.886   1.00 18.17  ? 111 VAL G CB  1 
ATOM   10978 C CG1 . VAL G  1 119 ? 1.499   2.277   5.773   1.00 15.19  ? 111 VAL G CG1 1 
ATOM   10979 C CG2 . VAL G  1 119 ? 0.043   0.933   7.334   1.00 22.08  ? 111 VAL G CG2 1 
ATOM   10980 N N   . LEU G  1 120 ? -0.042  2.299   2.795   1.00 22.57  ? 112 LEU G N   1 
ATOM   10981 C CA  . LEU G  1 120 ? 0.515   2.439   1.457   1.00 18.92  ? 112 LEU G CA  1 
ATOM   10982 C C   . LEU G  1 120 ? 1.607   3.494   1.506   1.00 17.15  ? 112 LEU G C   1 
ATOM   10983 O O   . LEU G  1 120 ? 1.376   4.617   1.949   1.00 17.77  ? 112 LEU G O   1 
ATOM   10984 C CB  . LEU G  1 120 ? -0.556  2.883   0.457   1.00 18.94  ? 112 LEU G CB  1 
ATOM   10985 C CG  . LEU G  1 120 ? -2.014  2.471   0.697   1.00 23.22  ? 112 LEU G CG  1 
ATOM   10986 C CD1 . LEU G  1 120 ? -2.951  3.103   -0.330  1.00 20.86  ? 112 LEU G CD1 1 
ATOM   10987 C CD2 . LEU G  1 120 ? -2.141  0.965   0.664   1.00 24.53  ? 112 LEU G CD2 1 
ATOM   10988 N N   . TYR G  1 121 ? 2.795   3.125   1.049   1.00 15.82  ? 113 TYR G N   1 
ATOM   10989 C CA  . TYR G  1 121 ? 3.898   4.062   0.896   1.00 15.39  ? 113 TYR G CA  1 
ATOM   10990 C C   . TYR G  1 121 ? 4.447   3.929   -0.530  1.00 17.27  ? 113 TYR G C   1 
ATOM   10991 O O   . TYR G  1 121 ? 4.925   2.860   -0.917  1.00 18.87  ? 113 TYR G O   1 
ATOM   10992 C CB  . TYR G  1 121 ? 4.987   3.779   1.946   1.00 11.74  ? 113 TYR G CB  1 
ATOM   10993 C CG  . TYR G  1 121 ? 6.151   4.732   1.893   1.00 10.88  ? 113 TYR G CG  1 
ATOM   10994 C CD1 . TYR G  1 121 ? 5.944   6.096   1.752   1.00 10.50  ? 113 TYR G CD1 1 
ATOM   10995 C CD2 . TYR G  1 121 ? 7.462   4.270   1.982   1.00 11.91  ? 113 TYR G CD2 1 
ATOM   10996 C CE1 . TYR G  1 121 ? 7.011   6.974   1.699   1.00 12.53  ? 113 TYR G CE1 1 
ATOM   10997 C CE2 . TYR G  1 121 ? 8.530   5.137   1.928   1.00 9.17   ? 113 TYR G CE2 1 
ATOM   10998 C CZ  . TYR G  1 121 ? 8.300   6.491   1.788   1.00 11.05  ? 113 TYR G CZ  1 
ATOM   10999 O OH  . TYR G  1 121 ? 9.361   7.373   1.735   1.00 11.48  ? 113 TYR G OH  1 
ATOM   11000 N N   . MET G  1 122 ? 4.334   4.998   -1.318  1.00 18.30  ? 114 MET G N   1 
ATOM   11001 C CA  . MET G  1 122 ? 4.873   5.023   -2.680  1.00 16.64  ? 114 MET G CA  1 
ATOM   11002 C C   . MET G  1 122 ? 5.799   6.204   -2.885  1.00 14.73  ? 114 MET G C   1 
ATOM   11003 O O   . MET G  1 122 ? 5.400   7.224   -3.440  1.00 14.25  ? 114 MET G O   1 
ATOM   11004 C CB  . MET G  1 122 ? 3.775   5.062   -3.755  1.00 21.57  ? 114 MET G CB  1 
ATOM   11005 C CG  . MET G  1 122 ? 4.365   5.028   -5.191  1.00 31.46  ? 114 MET G CG  1 
ATOM   11006 S SD  . MET G  1 122 ? 3.248   4.916   -6.611  1.00 45.45  ? 114 MET G SD  1 
ATOM   11007 C CE  . MET G  1 122 ? 2.425   6.513   -6.612  1.00 26.74  ? 114 MET G CE  1 
ATOM   11008 N N   . PRO G  1 123 ? 7.045   6.069   -2.435  1.00 13.47  ? 115 PRO G N   1 
ATOM   11009 C CA  . PRO G  1 123 ? 8.042   7.096   -2.703  1.00 17.82  ? 115 PRO G CA  1 
ATOM   11010 C C   . PRO G  1 123 ? 8.522   7.032   -4.156  1.00 21.48  ? 115 PRO G C   1 
ATOM   11011 O O   . PRO G  1 123 ? 8.664   5.936   -4.710  1.00 23.25  ? 115 PRO G O   1 
ATOM   11012 C CB  . PRO G  1 123 ? 9.185   6.696   -1.771  1.00 13.14  ? 115 PRO G CB  1 
ATOM   11013 C CG  . PRO G  1 123 ? 9.094   5.235   -1.709  1.00 12.66  ? 115 PRO G CG  1 
ATOM   11014 C CD  . PRO G  1 123 ? 7.615   4.938   -1.687  1.00 14.93  ? 115 PRO G CD  1 
ATOM   11015 N N   . SER G  1 124 ? 8.751   8.189   -4.768  1.00 17.94  ? 116 SER G N   1 
ATOM   11016 C CA  . SER G  1 124 ? 9.474   8.240   -6.035  1.00 23.62  ? 116 SER G CA  1 
ATOM   11017 C C   . SER G  1 124 ? 10.969  8.257   -5.723  1.00 26.67  ? 116 SER G C   1 
ATOM   11018 O O   . SER G  1 124 ? 11.441  9.023   -4.869  1.00 23.87  ? 116 SER G O   1 
ATOM   11019 C CB  . SER G  1 124 ? 9.089   9.474   -6.842  1.00 23.14  ? 116 SER G CB  1 
ATOM   11020 O OG  . SER G  1 124 ? 9.757   9.495   -8.089  1.00 28.29  ? 116 SER G OG  1 
ATOM   11021 N N   . ILE G  1 125 ? 11.713  7.408   -6.419  1.00 25.06  ? 117 ILE G N   1 
ATOM   11022 C CA  . ILE G  1 125 ? 13.096  7.140   -6.057  1.00 26.20  ? 117 ILE G CA  1 
ATOM   11023 C C   . ILE G  1 125 ? 14.039  7.213   -7.248  1.00 24.33  ? 117 ILE G C   1 
ATOM   11024 O O   . ILE G  1 125 ? 13.709  6.732   -8.334  1.00 21.78  ? 117 ILE G O   1 
ATOM   11025 C CB  . ILE G  1 125 ? 13.196  5.742   -5.431  1.00 27.25  ? 117 ILE G CB  1 
ATOM   11026 C CG1 . ILE G  1 125 ? 12.553  5.758   -4.046  1.00 14.35  ? 117 ILE G CG1 1 
ATOM   11027 C CG2 . ILE G  1 125 ? 14.652  5.246   -5.410  1.00 22.35  ? 117 ILE G CG2 1 
ATOM   11028 C CD1 . ILE G  1 125 ? 12.634  4.439   -3.363  1.00 19.51  ? 117 ILE G CD1 1 
ATOM   11029 N N   . ARG G  1 126 ? 15.205  7.825   -7.039  1.00 27.37  ? 118 ARG G N   1 
ATOM   11030 C CA  . ARG G  1 126 ? 16.279  7.817   -8.038  1.00 23.15  ? 118 ARG G CA  1 
ATOM   11031 C C   . ARG G  1 126 ? 17.491  7.053   -7.521  1.00 20.00  ? 118 ARG G C   1 
ATOM   11032 O O   . ARG G  1 126 ? 18.093  7.415   -6.510  1.00 18.93  ? 118 ARG G O   1 
ATOM   11033 C CB  . ARG G  1 126 ? 16.681  9.235   -8.438  1.00 25.54  ? 118 ARG G CB  1 
ATOM   11034 C CG  . ARG G  1 126 ? 17.685  9.283   -9.567  1.00 25.12  ? 118 ARG G CG  1 
ATOM   11035 C CD  . ARG G  1 126 ? 18.093  10.695  -9.905  1.00 25.67  ? 118 ARG G CD  1 
ATOM   11036 N NE  . ARG G  1 126 ? 19.317  10.699  -10.702 1.00 41.81  ? 118 ARG G NE  1 
ATOM   11037 C CZ  . ARG G  1 126 ? 19.744  11.710  -11.461 1.00 44.93  ? 118 ARG G CZ  1 
ATOM   11038 N NH1 . ARG G  1 126 ? 19.044  12.844  -11.557 1.00 35.82  ? 118 ARG G NH1 1 
ATOM   11039 N NH2 . ARG G  1 126 ? 20.886  11.581  -12.133 1.00 41.44  ? 118 ARG G NH2 1 
ATOM   11040 N N   . GLN G  1 127 ? 17.851  5.988   -8.221  1.00 22.01  ? 119 GLN G N   1 
ATOM   11041 C CA  . GLN G  1 127 ? 18.934  5.139   -7.755  1.00 21.46  ? 119 GLN G CA  1 
ATOM   11042 C C   . GLN G  1 127 ? 19.735  4.499   -8.902  1.00 23.19  ? 119 GLN G C   1 
ATOM   11043 O O   . GLN G  1 127 ? 19.204  4.324   -10.006 1.00 16.48  ? 119 GLN G O   1 
ATOM   11044 C CB  . GLN G  1 127 ? 18.354  4.071   -6.837  1.00 20.44  ? 119 GLN G CB  1 
ATOM   11045 C CG  . GLN G  1 127 ? 19.383  3.417   -5.971  1.00 26.51  ? 119 GLN G CG  1 
ATOM   11046 C CD  . GLN G  1 127 ? 18.754  2.574   -4.924  1.00 22.95  ? 119 GLN G CD  1 
ATOM   11047 O OE1 . GLN G  1 127 ? 17.827  1.819   -5.204  1.00 24.86  ? 119 GLN G OE1 1 
ATOM   11048 N NE2 . GLN G  1 127 ? 19.227  2.709   -3.695  1.00 24.46  ? 119 GLN G NE2 1 
ATOM   11049 N N   . ARG G  1 128 ? 21.003  4.159   -8.630  1.00 24.94  ? 120 ARG G N   1 
ATOM   11050 C CA  . ARG G  1 128 ? 21.888  3.522   -9.616  1.00 20.60  ? 120 ARG G CA  1 
ATOM   11051 C C   . ARG G  1 128 ? 22.114  2.057   -9.310  1.00 20.57  ? 120 ARG G C   1 
ATOM   11052 O O   . ARG G  1 128 ? 22.316  1.688   -8.160  1.00 27.05  ? 120 ARG G O   1 
ATOM   11053 C CB  . ARG G  1 128 ? 23.247  4.218   -9.677  1.00 23.87  ? 120 ARG G CB  1 
ATOM   11054 C CG  . ARG G  1 128 ? 23.187  5.733   -9.600  1.00 29.45  ? 120 ARG G CG  1 
ATOM   11055 C CD  . ARG G  1 128 ? 24.569  6.374   -9.732  1.00 38.45  ? 120 ARG G CD  1 
ATOM   11056 N NE  . ARG G  1 128 ? 24.698  7.520   -8.834  1.00 49.27  ? 120 ARG G NE  1 
ATOM   11057 C CZ  . ARG G  1 128 ? 24.420  8.778   -9.170  1.00 59.68  ? 120 ARG G CZ  1 
ATOM   11058 N NH1 . ARG G  1 128 ? 24.009  9.070   -10.402 1.00 48.33  ? 120 ARG G NH1 1 
ATOM   11059 N NH2 . ARG G  1 128 ? 24.562  9.748   -8.272  1.00 57.30  ? 120 ARG G NH2 1 
ATOM   11060 N N   . PHE G  1 129 ? 22.112  1.223   -10.342 1.00 22.88  ? 121 PHE G N   1 
ATOM   11061 C CA  . PHE G  1 129 ? 22.236  -0.223  -10.158 1.00 24.61  ? 121 PHE G CA  1 
ATOM   11062 C C   . PHE G  1 129 ? 23.344  -0.824  -11.012 1.00 27.55  ? 121 PHE G C   1 
ATOM   11063 O O   . PHE G  1 129 ? 23.771  -0.223  -11.988 1.00 33.68  ? 121 PHE G O   1 
ATOM   11064 C CB  . PHE G  1 129 ? 20.904  -0.909  -10.480 1.00 26.24  ? 121 PHE G CB  1 
ATOM   11065 C CG  . PHE G  1 129 ? 19.767  -0.477  -9.587  1.00 26.01  ? 121 PHE G CG  1 
ATOM   11066 C CD1 . PHE G  1 129 ? 19.055  0.679   -9.857  1.00 21.80  ? 121 PHE G CD1 1 
ATOM   11067 C CD2 . PHE G  1 129 ? 19.420  -1.224  -8.474  1.00 24.46  ? 121 PHE G CD2 1 
ATOM   11068 C CE1 . PHE G  1 129 ? 18.022  1.077   -9.043  1.00 19.60  ? 121 PHE G CE1 1 
ATOM   11069 C CE2 . PHE G  1 129 ? 18.378  -0.828  -7.657  1.00 23.80  ? 121 PHE G CE2 1 
ATOM   11070 C CZ  . PHE G  1 129 ? 17.678  0.321   -7.944  1.00 22.08  ? 121 PHE G CZ  1 
ATOM   11071 N N   . SER G  1 130 ? 23.803  -2.013  -10.641 1.00 28.28  ? 122 SER G N   1 
ATOM   11072 C CA  . SER G  1 130 ? 24.776  -2.745  -11.440 1.00 31.05  ? 122 SER G CA  1 
ATOM   11073 C C   . SER G  1 130 ? 24.131  -4.017  -11.962 1.00 39.02  ? 122 SER G C   1 
ATOM   11074 O O   . SER G  1 130 ? 23.717  -4.881  -11.176 1.00 41.85  ? 122 SER G O   1 
ATOM   11075 C CB  . SER G  1 130 ? 25.981  -3.137  -10.597 1.00 37.55  ? 122 SER G CB  1 
ATOM   11076 O OG  . SER G  1 130 ? 25.844  -4.479  -10.149 1.00 41.36  ? 122 SER G OG  1 
ATOM   11077 N N   . CYS G  1 131 ? 24.073  -4.144  -13.284 1.00 41.92  ? 123 CYS G N   1 
ATOM   11078 C CA  . CYS G  1 131 ? 23.418  -5.284  -13.921 1.00 50.91  ? 123 CYS G CA  1 
ATOM   11079 C C   . CYS G  1 131 ? 23.782  -5.445  -15.410 1.00 48.90  ? 123 CYS G C   1 
ATOM   11080 O O   . CYS G  1 131 ? 24.623  -4.721  -15.949 1.00 39.23  ? 123 CYS G O   1 
ATOM   11081 C CB  . CYS G  1 131 ? 21.908  -5.133  -13.789 1.00 49.43  ? 123 CYS G CB  1 
ATOM   11082 S SG  . CYS G  1 131 ? 21.331  -3.556  -14.475 1.00 56.38  ? 123 CYS G SG  1 
ATOM   11083 N N   . ASP G  1 132 ? 23.122  -6.400  -16.061 1.00 44.01  ? 124 ASP G N   1 
ATOM   11084 C CA  . ASP G  1 132 ? 23.361  -6.695  -17.463 1.00 45.73  ? 124 ASP G CA  1 
ATOM   11085 C C   . ASP G  1 132 ? 22.892  -5.557  -18.353 1.00 44.00  ? 124 ASP G C   1 
ATOM   11086 O O   . ASP G  1 132 ? 21.740  -5.135  -18.290 1.00 47.20  ? 124 ASP G O   1 
ATOM   11087 C CB  . ASP G  1 132 ? 22.643  -7.983  -17.861 1.00 53.49  ? 124 ASP G CB  1 
ATOM   11088 C CG  . ASP G  1 132 ? 23.366  -8.730  -18.955 1.00 48.67  ? 124 ASP G CG  1 
ATOM   11089 O OD1 . ASP G  1 132 ? 23.930  -8.059  -19.843 1.00 45.40  ? 124 ASP G OD1 1 
ATOM   11090 O OD2 . ASP G  1 132 ? 23.385  -9.982  -18.911 1.00 49.42  ? 124 ASP G OD2 1 
ATOM   11091 N N   . VAL G  1 133 ? 23.794  -5.061  -19.187 1.00 40.30  ? 125 VAL G N   1 
ATOM   11092 C CA  . VAL G  1 133 ? 23.474  -3.948  -20.061 1.00 41.58  ? 125 VAL G CA  1 
ATOM   11093 C C   . VAL G  1 133 ? 23.770  -4.309  -21.523 1.00 48.08  ? 125 VAL G C   1 
ATOM   11094 O O   . VAL G  1 133 ? 23.185  -3.739  -22.441 1.00 47.37  ? 125 VAL G O   1 
ATOM   11095 C CB  . VAL G  1 133 ? 24.227  -2.674  -19.624 1.00 41.68  ? 125 VAL G CB  1 
ATOM   11096 C CG1 . VAL G  1 133 ? 23.847  -1.498  -20.491 1.00 40.80  ? 125 VAL G CG1 1 
ATOM   11097 C CG2 . VAL G  1 133 ? 23.924  -2.364  -18.175 1.00 40.40  ? 125 VAL G CG2 1 
ATOM   11098 N N   . SER G  1 134 ? 24.671  -5.266  -21.734 1.00 47.75  ? 126 SER G N   1 
ATOM   11099 C CA  . SER G  1 134 ? 24.930  -5.780  -23.072 1.00 47.62  ? 126 SER G CA  1 
ATOM   11100 C C   . SER G  1 134 ? 23.613  -6.200  -23.729 1.00 51.10  ? 126 SER G C   1 
ATOM   11101 O O   . SER G  1 134 ? 22.858  -7.007  -23.180 1.00 48.59  ? 126 SER G O   1 
ATOM   11102 C CB  . SER G  1 134 ? 25.910  -6.957  -23.027 1.00 52.16  ? 126 SER G CB  1 
ATOM   11103 O OG  . SER G  1 134 ? 25.379  -8.052  -22.297 1.00 56.80  ? 126 SER G OG  1 
ATOM   11104 N N   . GLY G  1 135 ? 23.335  -5.627  -24.894 1.00 45.13  ? 127 GLY G N   1 
ATOM   11105 C CA  . GLY G  1 135 ? 22.063  -5.840  -25.555 1.00 40.97  ? 127 GLY G CA  1 
ATOM   11106 C C   . GLY G  1 135 ? 21.305  -4.534  -25.685 1.00 43.47  ? 127 GLY G C   1 
ATOM   11107 O O   . GLY G  1 135 ? 20.372  -4.426  -26.472 1.00 41.19  ? 127 GLY G O   1 
ATOM   11108 N N   . VAL G  1 136 ? 21.723  -3.531  -24.922 1.00 43.54  ? 128 VAL G N   1 
ATOM   11109 C CA  . VAL G  1 136 ? 20.978  -2.282  -24.828 1.00 42.81  ? 128 VAL G CA  1 
ATOM   11110 C C   . VAL G  1 136 ? 20.814  -1.582  -26.180 1.00 39.90  ? 128 VAL G C   1 
ATOM   11111 O O   . VAL G  1 136 ? 19.753  -1.043  -26.487 1.00 39.71  ? 128 VAL G O   1 
ATOM   11112 C CB  . VAL G  1 136 ? 21.606  -1.323  -23.773 1.00 44.55  ? 128 VAL G CB  1 
ATOM   11113 C CG1 . VAL G  1 136 ? 23.071  -1.064  -24.081 1.00 48.66  ? 128 VAL G CG1 1 
ATOM   11114 C CG2 . VAL G  1 136 ? 20.823  -0.012  -23.673 1.00 38.06  ? 128 VAL G CG2 1 
ATOM   11115 N N   . ASP G  1 137 ? 21.861  -1.621  -26.992 1.00 46.89  ? 129 ASP G N   1 
ATOM   11116 C CA  . ASP G  1 137 ? 21.883  -0.895  -28.258 1.00 47.82  ? 129 ASP G CA  1 
ATOM   11117 C C   . ASP G  1 137 ? 21.182  -1.651  -29.389 1.00 50.69  ? 129 ASP G C   1 
ATOM   11118 O O   . ASP G  1 137 ? 20.965  -1.098  -30.474 1.00 47.48  ? 129 ASP G O   1 
ATOM   11119 C CB  . ASP G  1 137 ? 23.327  -0.595  -28.663 1.00 44.94  ? 129 ASP G CB  1 
ATOM   11120 C CG  . ASP G  1 137 ? 23.535  0.859   -29.035 1.00 54.53  ? 129 ASP G CG  1 
ATOM   11121 O OD1 . ASP G  1 137 ? 22.535  1.544   -29.343 1.00 52.01  ? 129 ASP G OD1 1 
ATOM   11122 O OD2 . ASP G  1 137 ? 24.699  1.318   -29.019 1.00 61.52  ? 129 ASP G OD2 1 
ATOM   11123 N N   . THR G  1 138 ? 20.796  -2.890  -29.086 1.00 43.62  ? 130 THR G N   1 
ATOM   11124 C CA  . THR G  1 138 ? 20.185  -3.816  -30.038 1.00 37.00  ? 130 THR G CA  1 
ATOM   11125 C C   . THR G  1 138 ? 18.714  -4.074  -29.708 1.00 39.87  ? 130 THR G C   1 
ATOM   11126 O O   . THR G  1 138 ? 18.314  -4.070  -28.544 1.00 45.75  ? 130 THR G O   1 
ATOM   11127 C CB  . THR G  1 138 ? 20.936  -5.160  -30.079 1.00 39.90  ? 130 THR G CB  1 
ATOM   11128 O OG1 . THR G  1 138 ? 20.489  -5.993  -29.002 1.00 45.59  ? 130 THR G OG1 1 
ATOM   11129 C CG2 . THR G  1 138 ? 22.435  -4.936  -29.954 1.00 37.07  ? 130 THR G CG2 1 
ATOM   11130 N N   . GLU G  1 139 ? 17.923  -4.376  -30.727 1.00 41.51  ? 131 GLU G N   1 
ATOM   11131 C CA  . GLU G  1 139 ? 16.477  -4.279  -30.620 1.00 46.53  ? 131 GLU G CA  1 
ATOM   11132 C C   . GLU G  1 139 ? 15.911  -5.156  -29.509 1.00 47.06  ? 131 GLU G C   1 
ATOM   11133 O O   . GLU G  1 139 ? 14.975  -4.754  -28.819 1.00 39.72  ? 131 GLU G O   1 
ATOM   11134 C CB  . GLU G  1 139 ? 15.819  -4.639  -31.955 1.00 45.98  ? 131 GLU G CB  1 
ATOM   11135 C CG  . GLU G  1 139 ? 14.391  -4.140  -32.097 1.00 49.15  ? 131 GLU G CG  1 
ATOM   11136 C CD  . GLU G  1 139 ? 13.626  -4.867  -33.186 1.00 49.73  ? 131 GLU G CD  1 
ATOM   11137 O OE1 . GLU G  1 139 ? 13.897  -6.066  -33.405 1.00 46.48  ? 131 GLU G OE1 1 
ATOM   11138 O OE2 . GLU G  1 139 ? 12.753  -4.239  -33.822 1.00 39.30  ? 131 GLU G OE2 1 
ATOM   11139 N N   . SER G  1 140 ? 16.464  -6.350  -29.335 1.00 42.25  ? 132 SER G N   1 
ATOM   11140 C CA  . SER G  1 140 ? 15.924  -7.268  -28.348 1.00 42.87  ? 132 SER G CA  1 
ATOM   11141 C C   . SER G  1 140 ? 16.214  -6.641  -26.984 1.00 48.34  ? 132 SER G C   1 
ATOM   11142 O O   . SER G  1 140 ? 15.570  -6.960  -25.987 1.00 40.24  ? 132 SER G O   1 
ATOM   11143 C CB  . SER G  1 140 ? 16.555  -8.657  -28.482 1.00 47.29  ? 132 SER G CB  1 
ATOM   11144 O OG  . SER G  1 140 ? 17.972  -8.589  -28.497 1.00 45.93  ? 132 SER G OG  1 
ATOM   11145 N N   . GLY G  1 141 ? 17.191  -5.735  -26.963 1.00 44.42  ? 133 GLY G N   1 
ATOM   11146 C CA  . GLY G  1 141 ? 17.440  -4.890  -25.814 1.00 37.32  ? 133 GLY G CA  1 
ATOM   11147 C C   . GLY G  1 141 ? 18.237  -5.543  -24.705 1.00 42.49  ? 133 GLY G C   1 
ATOM   11148 O O   . GLY G  1 141 ? 18.661  -6.691  -24.817 1.00 42.85  ? 133 GLY G O   1 
ATOM   11149 N N   . ALA G  1 142 ? 18.451  -4.788  -23.628 1.00 47.21  ? 134 ALA G N   1 
ATOM   11150 C CA  . ALA G  1 142 ? 19.116  -5.302  -22.437 1.00 44.88  ? 134 ALA G CA  1 
ATOM   11151 C C   . ALA G  1 142 ? 18.067  -5.714  -21.423 1.00 37.76  ? 134 ALA G C   1 
ATOM   11152 O O   . ALA G  1 142 ? 16.931  -5.253  -21.475 1.00 35.25  ? 134 ALA G O   1 
ATOM   11153 C CB  . ALA G  1 142 ? 20.034  -4.255  -21.845 1.00 39.00  ? 134 ALA G CB  1 
ATOM   11154 N N   . THR G  1 143 ? 18.452  -6.593  -20.510 1.00 40.37  ? 135 THR G N   1 
ATOM   11155 C CA  . THR G  1 143 ? 17.558  -7.004  -19.431 1.00 44.36  ? 135 THR G CA  1 
ATOM   11156 C C   . THR G  1 143 ? 18.176  -6.685  -18.078 1.00 43.45  ? 135 THR G C   1 
ATOM   11157 O O   . THR G  1 143 ? 18.954  -7.474  -17.530 1.00 35.66  ? 135 THR G O   1 
ATOM   11158 C CB  . THR G  1 143 ? 17.235  -8.493  -19.489 1.00 37.82  ? 135 THR G CB  1 
ATOM   11159 O OG1 . THR G  1 143 ? 16.600  -8.783  -20.739 1.00 49.29  ? 135 THR G OG1 1 
ATOM   11160 C CG2 . THR G  1 143 ? 16.305  -8.878  -18.338 1.00 40.52  ? 135 THR G CG2 1 
ATOM   11161 N N   . CYS G  1 144 ? 17.837  -5.513  -17.557 1.00 39.04  ? 136 CYS G N   1 
ATOM   11162 C CA  . CYS G  1 144 ? 18.364  -5.085  -16.281 1.00 42.58  ? 136 CYS G CA  1 
ATOM   11163 C C   . CYS G  1 144 ? 17.562  -5.720  -15.142 1.00 43.52  ? 136 CYS G C   1 
ATOM   11164 O O   . CYS G  1 144 ? 16.343  -5.579  -15.069 1.00 39.63  ? 136 CYS G O   1 
ATOM   11165 C CB  . CYS G  1 144 ? 18.358  -3.565  -16.184 1.00 44.80  ? 136 CYS G CB  1 
ATOM   11166 S SG  . CYS G  1 144 ? 18.984  -2.983  -14.589 1.00 78.44  ? 136 CYS G SG  1 
ATOM   11167 N N   . ARG G  1 145 ? 18.269  -6.403  -14.249 1.00 41.20  ? 137 ARG G N   1 
ATOM   11168 C CA  . ARG G  1 145 ? 17.659  -7.334  -13.311 1.00 41.19  ? 137 ARG G CA  1 
ATOM   11169 C C   . ARG G  1 145 ? 17.943  -6.924  -11.840 1.00 45.01  ? 137 ARG G C   1 
ATOM   11170 O O   . ARG G  1 145 ? 19.054  -7.127  -11.336 1.00 46.14  ? 137 ARG G O   1 
ATOM   11171 C CB  . ARG G  1 145 ? 18.197  -8.736  -13.635 1.00 39.28  ? 137 ARG G CB  1 
ATOM   11172 C CG  . ARG G  1 145 ? 17.345  -9.905  -13.191 1.00 55.37  ? 137 ARG G CG  1 
ATOM   11173 C CD  . ARG G  1 145 ? 17.934  -10.590 -11.951 1.00 64.73  ? 137 ARG G CD  1 
ATOM   11174 N NE  . ARG G  1 145 ? 19.113  -11.410 -12.240 1.00 65.62  ? 137 ARG G NE  1 
ATOM   11175 C CZ  . ARG G  1 145 ? 20.309  -11.236 -11.681 1.00 65.47  ? 137 ARG G CZ  1 
ATOM   11176 N NH1 . ARG G  1 145 ? 20.506  -10.263 -10.796 1.00 66.53  ? 137 ARG G NH1 1 
ATOM   11177 N NH2 . ARG G  1 145 ? 21.313  -12.039 -12.007 1.00 63.07  ? 137 ARG G NH2 1 
ATOM   11178 N N   . ILE G  1 146 ? 16.943  -6.346  -11.164 1.00 38.02  ? 138 ILE G N   1 
ATOM   11179 C CA  . ILE G  1 146 ? 17.122  -5.804  -9.804  1.00 38.05  ? 138 ILE G CA  1 
ATOM   11180 C C   . ILE G  1 146 ? 16.339  -6.546  -8.699  1.00 30.34  ? 138 ILE G C   1 
ATOM   11181 O O   . ILE G  1 146 ? 15.174  -6.899  -8.872  1.00 30.39  ? 138 ILE G O   1 
ATOM   11182 C CB  . ILE G  1 146 ? 16.834  -4.267  -9.737  1.00 36.00  ? 138 ILE G CB  1 
ATOM   11183 C CG1 . ILE G  1 146 ? 15.767  -3.947  -8.690  1.00 35.78  ? 138 ILE G CG1 1 
ATOM   11184 C CG2 . ILE G  1 146 ? 16.436  -3.699  -11.097 1.00 25.49  ? 138 ILE G CG2 1 
ATOM   11185 C CD1 . ILE G  1 146 ? 15.321  -2.502  -8.707  1.00 37.87  ? 138 ILE G CD1 1 
ATOM   11186 N N   . LYS G  1 147 ? 16.992  -6.790  -7.567  1.00 30.00  ? 139 LYS G N   1 
ATOM   11187 C CA  . LYS G  1 147 ? 16.357  -7.535  -6.478  1.00 37.47  ? 139 LYS G CA  1 
ATOM   11188 C C   . LYS G  1 147 ? 16.085  -6.671  -5.238  1.00 36.54  ? 139 LYS G C   1 
ATOM   11189 O O   . LYS G  1 147 ? 16.990  -6.026  -4.708  1.00 35.42  ? 139 LYS G O   1 
ATOM   11190 C CB  . LYS G  1 147 ? 17.155  -8.796  -6.118  1.00 36.98  ? 139 LYS G CB  1 
ATOM   11191 C CG  . LYS G  1 147 ? 17.213  -9.821  -7.254  1.00 55.11  ? 139 LYS G CG  1 
ATOM   11192 C CD  . LYS G  1 147 ? 17.966  -11.107 -6.880  1.00 65.63  ? 139 LYS G CD  1 
ATOM   11193 C CE  . LYS G  1 147 ? 18.706  -11.669 -8.106  1.00 76.53  ? 139 LYS G CE  1 
ATOM   11194 N NZ  . LYS G  1 147 ? 19.042  -13.122 -8.014  1.00 67.61  ? 139 LYS G NZ  1 
ATOM   11195 N N   . ILE G  1 148 ? 14.825  -6.662  -4.801  1.00 32.25  ? 140 ILE G N   1 
ATOM   11196 C CA  . ILE G  1 148 ? 14.389  -5.898  -3.639  1.00 34.39  ? 140 ILE G CA  1 
ATOM   11197 C C   . ILE G  1 148 ? 13.874  -6.828  -2.546  1.00 36.96  ? 140 ILE G C   1 
ATOM   11198 O O   . ILE G  1 148 ? 13.009  -7.665  -2.802  1.00 36.83  ? 140 ILE G O   1 
ATOM   11199 C CB  . ILE G  1 148 ? 13.275  -4.901  -4.007  1.00 27.07  ? 140 ILE G CB  1 
ATOM   11200 C CG1 . ILE G  1 148 ? 13.746  -3.984  -5.133  1.00 32.57  ? 140 ILE G CG1 1 
ATOM   11201 C CG2 . ILE G  1 148 ? 12.898  -4.081  -2.810  1.00 26.67  ? 140 ILE G CG2 1 
ATOM   11202 C CD1 . ILE G  1 148 ? 12.986  -2.688  -5.239  1.00 32.73  ? 140 ILE G CD1 1 
ATOM   11203 N N   . GLY G  1 149 ? 14.408  -6.677  -1.334  1.00 33.77  ? 141 GLY G N   1 
ATOM   11204 C CA  . GLY G  1 149 ? 13.999  -7.495  -0.204  1.00 35.81  ? 141 GLY G CA  1 
ATOM   11205 C C   . GLY G  1 149 ? 14.178  -6.875  1.177   1.00 32.76  ? 141 GLY G C   1 
ATOM   11206 O O   . GLY G  1 149 ? 14.775  -5.804  1.338   1.00 25.80  ? 141 GLY G O   1 
ATOM   11207 N N   . SER G  1 150 ? 13.645  -7.561  2.185   1.00 32.16  ? 142 SER G N   1 
ATOM   11208 C CA  . SER G  1 150 ? 13.849  -7.158  3.573   1.00 31.20  ? 142 SER G CA  1 
ATOM   11209 C C   . SER G  1 150 ? 15.303  -7.365  3.974   1.00 30.38  ? 142 SER G C   1 
ATOM   11210 O O   . SER G  1 150 ? 15.820  -8.476  3.881   1.00 38.88  ? 142 SER G O   1 
ATOM   11211 C CB  . SER G  1 150 ? 12.952  -7.964  4.514   1.00 28.17  ? 142 SER G CB  1 
ATOM   11212 O OG  . SER G  1 150 ? 13.366  -7.780  5.863   1.00 28.97  ? 142 SER G OG  1 
ATOM   11213 N N   . TRP G  1 151 ? 15.966  -6.312  4.432   1.00 27.04  ? 143 TRP G N   1 
ATOM   11214 C CA  . TRP G  1 151 ? 17.370  -6.440  4.797   1.00 24.32  ? 143 TRP G CA  1 
ATOM   11215 C C   . TRP G  1 151 ? 17.616  -7.315  6.037   1.00 27.65  ? 143 TRP G C   1 
ATOM   11216 O O   . TRP G  1 151 ? 18.422  -8.233  5.982   1.00 28.01  ? 143 TRP G O   1 
ATOM   11217 C CB  . TRP G  1 151 ? 18.016  -5.070  4.948   1.00 22.49  ? 143 TRP G CB  1 
ATOM   11218 C CG  . TRP G  1 151 ? 19.497  -5.123  5.123   1.00 29.07  ? 143 TRP G CG  1 
ATOM   11219 C CD1 . TRP G  1 151 ? 20.214  -4.628  6.171   1.00 28.11  ? 143 TRP G CD1 1 
ATOM   11220 C CD2 . TRP G  1 151 ? 20.452  -5.689  4.219   1.00 31.34  ? 143 TRP G CD2 1 
ATOM   11221 N NE1 . TRP G  1 151 ? 21.557  -4.849  5.979   1.00 25.42  ? 143 TRP G NE1 1 
ATOM   11222 C CE2 . TRP G  1 151 ? 21.729  -5.500  4.788   1.00 33.33  ? 143 TRP G CE2 1 
ATOM   11223 C CE3 . TRP G  1 151 ? 20.354  -6.338  2.985   1.00 25.88  ? 143 TRP G CE3 1 
ATOM   11224 C CZ2 . TRP G  1 151 ? 22.894  -5.937  4.165   1.00 32.23  ? 143 TRP G CZ2 1 
ATOM   11225 C CZ3 . TRP G  1 151 ? 21.507  -6.769  2.372   1.00 30.73  ? 143 TRP G CZ3 1 
ATOM   11226 C CH2 . TRP G  1 151 ? 22.762  -6.570  2.962   1.00 32.40  ? 143 TRP G CH2 1 
ATOM   11227 N N   . THR G  1 152 ? 16.913  -7.062  7.142   1.00 27.59  ? 144 THR G N   1 
ATOM   11228 C CA  . THR G  1 152 ? 17.232  -7.769  8.390   1.00 26.31  ? 144 THR G CA  1 
ATOM   11229 C C   . THR G  1 152 ? 16.273  -8.888  8.788   1.00 21.43  ? 144 THR G C   1 
ATOM   11230 O O   . THR G  1 152 ? 16.619  -9.755  9.587   1.00 22.52  ? 144 THR G O   1 
ATOM   11231 C CB  . THR G  1 152 ? 17.430  -6.792  9.586   1.00 29.03  ? 144 THR G CB  1 
ATOM   11232 O OG1 . THR G  1 152 ? 16.179  -6.189  9.962   1.00 25.18  ? 144 THR G OG1 1 
ATOM   11233 C CG2 . THR G  1 152 ? 18.454  -5.715  9.221   1.00 22.18  ? 144 THR G CG2 1 
ATOM   11234 N N   . HIS G  1 153 ? 15.076  -8.878  8.227   1.00 21.64  ? 145 HIS G N   1 
ATOM   11235 C CA  . HIS G  1 153 ? 14.087  -9.873  8.607   1.00 29.03  ? 145 HIS G CA  1 
ATOM   11236 C C   . HIS G  1 153 ? 14.038  -11.031 7.624   1.00 27.75  ? 145 HIS G C   1 
ATOM   11237 O O   . HIS G  1 153 ? 13.778  -10.832 6.443   1.00 28.39  ? 145 HIS G O   1 
ATOM   11238 C CB  . HIS G  1 153 ? 12.701  -9.226  8.752   1.00 25.71  ? 145 HIS G CB  1 
ATOM   11239 C CG  . HIS G  1 153 ? 12.664  -8.120  9.757   1.00 25.88  ? 145 HIS G CG  1 
ATOM   11240 N ND1 . HIS G  1 153 ? 12.918  -6.803  9.425   1.00 25.20  ? 145 HIS G ND1 1 
ATOM   11241 C CD2 . HIS G  1 153 ? 12.430  -8.131  11.091  1.00 24.75  ? 145 HIS G CD2 1 
ATOM   11242 C CE1 . HIS G  1 153 ? 12.834  -6.057  10.509  1.00 27.54  ? 145 HIS G CE1 1 
ATOM   11243 N NE2 . HIS G  1 153 ? 12.534  -6.838  11.536  1.00 24.19  ? 145 HIS G NE2 1 
ATOM   11244 N N   . HIS G  1 154 ? 14.288  -12.240 8.117   1.00 30.62  ? 146 HIS G N   1 
ATOM   11245 C CA  . HIS G  1 154 ? 14.131  -13.435 7.302   1.00 31.00  ? 146 HIS G CA  1 
ATOM   11246 C C   . HIS G  1 154 ? 12.658  -13.716 6.996   1.00 36.43  ? 146 HIS G C   1 
ATOM   11247 O O   . HIS G  1 154 ? 11.767  -13.024 7.490   1.00 30.42  ? 146 HIS G O   1 
ATOM   11248 C CB  . HIS G  1 154 ? 14.825  -14.651 7.931   1.00 35.23  ? 146 HIS G CB  1 
ATOM   11249 C CG  . HIS G  1 154 ? 14.657  -14.758 9.416   1.00 41.93  ? 146 HIS G CG  1 
ATOM   11250 N ND1 . HIS G  1 154 ? 15.527  -14.164 10.306  1.00 48.68  ? 146 HIS G ND1 1 
ATOM   11251 C CD2 . HIS G  1 154 ? 13.733  -15.405 10.167  1.00 46.51  ? 146 HIS G CD2 1 
ATOM   11252 C CE1 . HIS G  1 154 ? 15.138  -14.428 11.543  1.00 46.20  ? 146 HIS G CE1 1 
ATOM   11253 N NE2 . HIS G  1 154 ? 14.054  -15.182 11.487  1.00 48.28  ? 146 HIS G NE2 1 
ATOM   11254 N N   . SER G  1 155 ? 12.415  -14.729 6.169   1.00 44.19  ? 147 SER G N   1 
ATOM   11255 C CA  . SER G  1 155 ? 11.077  -15.037 5.650   1.00 42.80  ? 147 SER G CA  1 
ATOM   11256 C C   . SER G  1 155 ? 10.013  -15.335 6.721   1.00 34.23  ? 147 SER G C   1 
ATOM   11257 O O   . SER G  1 155 ? 8.822   -15.106 6.494   1.00 31.45  ? 147 SER G O   1 
ATOM   11258 C CB  . SER G  1 155 ? 11.152  -16.201 4.648   1.00 41.04  ? 147 SER G CB  1 
ATOM   11259 O OG  . SER G  1 155 ? 11.611  -17.399 5.264   1.00 40.72  ? 147 SER G OG  1 
ATOM   11260 N N   . ARG G  1 156 ? 10.440  -15.854 7.870   1.00 36.22  ? 148 ARG G N   1 
ATOM   11261 C CA  . ARG G  1 156 ? 9.517   -16.154 8.965   1.00 40.13  ? 148 ARG G CA  1 
ATOM   11262 C C   . ARG G  1 156 ? 8.873   -14.897 9.566   1.00 35.56  ? 148 ARG G C   1 
ATOM   11263 O O   . ARG G  1 156 ? 7.773   -14.959 10.099  1.00 37.24  ? 148 ARG G O   1 
ATOM   11264 C CB  . ARG G  1 156 ? 10.208  -16.988 10.050  1.00 40.44  ? 148 ARG G CB  1 
ATOM   11265 C CG  . ARG G  1 156 ? 10.373  -18.451 9.675   1.00 35.70  ? 148 ARG G CG  1 
ATOM   11266 C CD  . ARG G  1 156 ? 10.709  -19.323 10.878  1.00 53.83  ? 148 ARG G CD  1 
ATOM   11267 N NE  . ARG G  1 156 ? 10.365  -20.724 10.635  1.00 56.83  ? 148 ARG G NE  1 
ATOM   11268 C CZ  . ARG G  1 156 ? 9.142   -21.230 10.788  1.00 64.09  ? 148 ARG G CZ  1 
ATOM   11269 N NH1 . ARG G  1 156 ? 8.145   -20.452 11.192  1.00 64.44  ? 148 ARG G NH1 1 
ATOM   11270 N NH2 . ARG G  1 156 ? 8.913   -22.515 10.541  1.00 62.89  ? 148 ARG G NH2 1 
ATOM   11271 N N   . GLU G  1 157 ? 9.560   -13.763 9.443   1.00 32.66  ? 149 GLU G N   1 
ATOM   11272 C CA  . GLU G  1 157 ? 9.098   -12.478 9.964   1.00 29.38  ? 149 GLU G CA  1 
ATOM   11273 C C   . GLU G  1 157 ? 8.489   -11.575 8.880   1.00 30.14  ? 149 GLU G C   1 
ATOM   11274 O O   . GLU G  1 157 ? 7.441   -10.970 9.094   1.00 28.51  ? 149 GLU G O   1 
ATOM   11275 C CB  . GLU G  1 157 ? 10.264  -11.777 10.673  1.00 26.96  ? 149 GLU G CB  1 
ATOM   11276 C CG  . GLU G  1 157 ? 11.203  -12.789 11.340  1.00 35.50  ? 149 GLU G CG  1 
ATOM   11277 C CD  . GLU G  1 157 ? 12.270  -12.173 12.235  1.00 35.49  ? 149 GLU G CD  1 
ATOM   11278 O OE1 . GLU G  1 157 ? 12.589  -12.784 13.278  1.00 37.12  ? 149 GLU G OE1 1 
ATOM   11279 O OE2 . GLU G  1 157 ? 12.805  -11.099 11.897  1.00 36.73  ? 149 GLU G OE2 1 
ATOM   11280 N N   . ILE G  1 158 ? 9.151   -11.482 7.724   1.00 33.05  ? 150 ILE G N   1 
ATOM   11281 C CA  . ILE G  1 158 ? 8.647   -10.694 6.592   1.00 29.80  ? 150 ILE G CA  1 
ATOM   11282 C C   . ILE G  1 158 ? 8.650   -11.463 5.266   1.00 37.54  ? 150 ILE G C   1 
ATOM   11283 O O   . ILE G  1 158 ? 9.655   -12.064 4.870   1.00 36.39  ? 150 ILE G O   1 
ATOM   11284 C CB  . ILE G  1 158 ? 9.452   -9.392  6.379   1.00 27.90  ? 150 ILE G CB  1 
ATOM   11285 C CG1 . ILE G  1 158 ? 9.206   -8.411  7.528   1.00 26.54  ? 150 ILE G CG1 1 
ATOM   11286 C CG2 . ILE G  1 158 ? 9.101   -8.746  5.021   1.00 22.73  ? 150 ILE G CG2 1 
ATOM   11287 C CD1 . ILE G  1 158 ? 9.543   -6.971  7.183   1.00 21.53  ? 150 ILE G CD1 1 
ATOM   11288 N N   . SER G  1 159 ? 7.515   -11.431 4.580   1.00 36.15  ? 151 SER G N   1 
ATOM   11289 C CA  . SER G  1 159 ? 7.421   -12.011 3.257   1.00 31.81  ? 151 SER G CA  1 
ATOM   11290 C C   . SER G  1 159 ? 7.229   -10.915 2.210   1.00 35.61  ? 151 SER G C   1 
ATOM   11291 O O   . SER G  1 159 ? 6.392   -10.021 2.367   1.00 32.92  ? 151 SER G O   1 
ATOM   11292 C CB  . SER G  1 159 ? 6.271   -13.014 3.197   1.00 36.66  ? 151 SER G CB  1 
ATOM   11293 O OG  . SER G  1 159 ? 5.044   -12.361 2.931   1.00 32.87  ? 151 SER G OG  1 
ATOM   11294 N N   . VAL G  1 160 ? 8.014   -10.994 1.139   1.00 43.39  ? 152 VAL G N   1 
ATOM   11295 C CA  . VAL G  1 160 ? 7.946   -10.023 0.048   1.00 41.80  ? 152 VAL G CA  1 
ATOM   11296 C C   . VAL G  1 160 ? 7.331   -10.634 -1.215  1.00 39.69  ? 152 VAL G C   1 
ATOM   11297 O O   . VAL G  1 160 ? 7.765   -11.686 -1.686  1.00 42.76  ? 152 VAL G O   1 
ATOM   11298 C CB  . VAL G  1 160 ? 9.334   -9.450  -0.281  1.00 39.35  ? 152 VAL G CB  1 
ATOM   11299 C CG1 . VAL G  1 160 ? 9.216   -8.409  -1.362  1.00 39.97  ? 152 VAL G CG1 1 
ATOM   11300 C CG2 . VAL G  1 160 ? 9.977   -8.852  0.975   1.00 31.84  ? 152 VAL G CG2 1 
ATOM   11301 N N   . ASP G  1 161 ? 6.315   -9.962  -1.749  1.00 35.81  ? 153 ASP G N   1 
ATOM   11302 C CA  . ASP G  1 161 ? 5.530   -10.475 -2.865  1.00 40.40  ? 153 ASP G CA  1 
ATOM   11303 C C   . ASP G  1 161 ? 5.248   -9.372  -3.884  1.00 43.44  ? 153 ASP G C   1 
ATOM   11304 O O   . ASP G  1 161 ? 5.038   -8.218  -3.519  1.00 37.67  ? 153 ASP G O   1 
ATOM   11305 C CB  . ASP G  1 161 ? 4.212   -11.057 -2.352  1.00 35.13  ? 153 ASP G CB  1 
ATOM   11306 C CG  . ASP G  1 161 ? 4.405   -11.945 -1.136  1.00 50.50  ? 153 ASP G CG  1 
ATOM   11307 O OD1 . ASP G  1 161 ? 3.761   -11.692 -0.081  1.00 43.71  ? 153 ASP G OD1 1 
ATOM   11308 O OD2 . ASP G  1 161 ? 5.213   -12.896 -1.240  1.00 53.22  ? 153 ASP G OD2 1 
ATOM   11309 N N   . PRO G  1 162 ? 5.256   -9.715  -5.180  1.00 48.56  ? 154 PRO G N   1 
ATOM   11310 C CA  . PRO G  1 162 ? 4.867   -8.667  -6.123  1.00 47.00  ? 154 PRO G CA  1 
ATOM   11311 C C   . PRO G  1 162 ? 3.350   -8.584  -6.143  1.00 47.48  ? 154 PRO G C   1 
ATOM   11312 O O   . PRO G  1 162 ? 2.690   -9.473  -5.593  1.00 39.35  ? 154 PRO G O   1 
ATOM   11313 C CB  . PRO G  1 162 ? 5.402   -9.189  -7.456  1.00 44.67  ? 154 PRO G CB  1 
ATOM   11314 C CG  . PRO G  1 162 ? 5.347   -10.664 -7.313  1.00 48.02  ? 154 PRO G CG  1 
ATOM   11315 C CD  . PRO G  1 162 ? 5.588   -10.981 -5.857  1.00 38.39  ? 154 PRO G CD  1 
ATOM   11316 N N   . THR G  1 163 ? 2.818   -7.504  -6.709  1.00 46.19  ? 155 THR G N   1 
ATOM   11317 C CA  . THR G  1 163 ? 1.386   -7.378  -6.942  1.00 62.98  ? 155 THR G CA  1 
ATOM   11318 C C   . THR G  1 163 ? 1.048   -7.766  -8.379  1.00 73.25  ? 155 THR G C   1 
ATOM   11319 O O   . THR G  1 163 ? 0.083   -8.490  -8.626  1.00 79.17  ? 155 THR G O   1 
ATOM   11320 C CB  . THR G  1 163 ? 0.894   -5.944  -6.676  1.00 52.58  ? 155 THR G CB  1 
ATOM   11321 O OG1 . THR G  1 163 ? 1.850   -5.250  -5.865  1.00 45.44  ? 155 THR G OG1 1 
ATOM   11322 C CG2 . THR G  1 163 ? -0.449  -5.966  -5.963  1.00 45.69  ? 155 THR G CG2 1 
ATOM   11323 N N   . THR G  1 164 ? 1.853   -7.282  -9.321  1.00 71.21  ? 156 THR G N   1 
ATOM   11324 C CA  . THR G  1 164 ? 1.674   -7.616  -10.731 1.00 77.48  ? 156 THR G CA  1 
ATOM   11325 C C   . THR G  1 164 ? 2.949   -8.194  -11.340 1.00 80.29  ? 156 THR G C   1 
ATOM   11326 O O   . THR G  1 164 ? 4.018   -7.589  -11.263 1.00 75.96  ? 156 THR G O   1 
ATOM   11327 C CB  . THR G  1 164 ? 1.239   -6.387  -11.551 1.00 78.46  ? 156 THR G CB  1 
ATOM   11328 O OG1 . THR G  1 164 ? 2.390   -5.608  -11.898 1.00 66.10  ? 156 THR G OG1 1 
ATOM   11329 C CG2 . THR G  1 164 ? 0.273   -5.527  -10.749 1.00 69.22  ? 156 THR G CG2 1 
ATOM   11330 N N   . GLU G  1 165 ? 2.831   -9.377  -11.932 1.00 79.32  ? 157 GLU G N   1 
ATOM   11331 C CA  . GLU G  1 165 ? 3.955   -10.034 -12.594 1.00 71.23  ? 157 GLU G CA  1 
ATOM   11332 C C   . GLU G  1 165 ? 4.508   -9.302  -13.824 1.00 72.84  ? 157 GLU G C   1 
ATOM   11333 O O   . GLU G  1 165 ? 5.719   -9.267  -14.039 1.00 69.02  ? 157 GLU G O   1 
ATOM   11334 C CB  . GLU G  1 165 ? 3.579   -11.470 -12.973 1.00 71.61  ? 157 GLU G CB  1 
ATOM   11335 C CG  . GLU G  1 165 ? 4.409   -12.534 -12.274 1.00 70.98  ? 157 GLU G CG  1 
ATOM   11336 C CD  . GLU G  1 165 ? 3.935   -12.807 -10.860 1.00 70.36  ? 157 GLU G CD  1 
ATOM   11337 O OE1 . GLU G  1 165 ? 4.673   -13.469 -10.101 1.00 65.29  ? 157 GLU G OE1 1 
ATOM   11338 O OE2 . GLU G  1 165 ? 2.824   -12.358 -10.507 1.00 75.86  ? 157 GLU G OE2 1 
ATOM   11339 N N   . ASN G  1 166 ? 3.615   -8.741  -14.634 1.00 79.17  ? 158 ASN G N   1 
ATOM   11340 C CA  . ASN G  1 166 ? 3.949   -8.313  -15.974 1.00 76.87  ? 158 ASN G CA  1 
ATOM   11341 C C   . ASN G  1 166 ? 3.354   -6.938  -16.220 1.00 75.11  ? 158 ASN G C   1 
ATOM   11342 O O   . ASN G  1 166 ? 2.308   -6.592  -15.670 1.00 79.60  ? 158 ASN G O   1 
ATOM   11343 C CB  . ASN G  1 166 ? 3.422   -9.310  -17.007 1.00 74.17  ? 158 ASN G CB  1 
ATOM   11344 C CG  . ASN G  1 166 ? 4.247   -9.323  -18.278 1.00 76.73  ? 158 ASN G CG  1 
ATOM   11345 O OD1 . ASN G  1 166 ? 4.008   -8.537  -19.195 1.00 75.70  ? 158 ASN G OD1 1 
ATOM   11346 N ND2 . ASN G  1 166 ? 5.226   -10.218 -18.340 1.00 66.76  ? 158 ASN G ND2 1 
ATOM   11347 N N   . SER G  1 167 ? 4.022   -6.161  -17.057 1.00 71.86  ? 159 SER G N   1 
ATOM   11348 C CA  . SER G  1 167 ? 3.508   -4.856  -17.492 1.00 74.47  ? 159 SER G CA  1 
ATOM   11349 C C   . SER G  1 167 ? 4.486   -4.161  -18.441 1.00 68.39  ? 159 SER G C   1 
ATOM   11350 O O   . SER G  1 167 ? 5.619   -4.611  -18.621 1.00 60.70  ? 159 SER G O   1 
ATOM   11351 C CB  . SER G  1 167 ? 3.192   -3.943  -16.295 1.00 65.38  ? 159 SER G CB  1 
ATOM   11352 O OG  . SER G  1 167 ? 2.529   -2.761  -16.714 1.00 62.31  ? 159 SER G OG  1 
ATOM   11353 N N   . SER G  1 170 ? 5.470   1.447   -16.958 1.00 39.46  ? 162 SER G N   1 
ATOM   11354 C CA  . SER G  1 170 ? 4.975   1.297   -18.322 1.00 38.77  ? 162 SER G CA  1 
ATOM   11355 C C   . SER G  1 170 ? 4.095   2.465   -18.747 1.00 40.50  ? 162 SER G C   1 
ATOM   11356 O O   . SER G  1 170 ? 4.457   3.207   -19.655 1.00 45.82  ? 162 SER G O   1 
ATOM   11357 C CB  . SER G  1 170 ? 4.223   -0.027  -18.490 1.00 54.36  ? 162 SER G CB  1 
ATOM   11358 O OG  . SER G  1 170 ? 5.122   -1.113  -18.653 1.00 52.26  ? 162 SER G OG  1 
ATOM   11359 N N   . GLU G  1 171 ? 2.941   2.628   -18.101 1.00 39.02  ? 163 GLU G N   1 
ATOM   11360 C CA  . GLU G  1 171 ? 2.019   3.714   -18.458 1.00 40.68  ? 163 GLU G CA  1 
ATOM   11361 C C   . GLU G  1 171 ? 2.313   5.021   -17.724 1.00 40.79  ? 163 GLU G C   1 
ATOM   11362 O O   . GLU G  1 171 ? 1.607   6.020   -17.900 1.00 36.60  ? 163 GLU G O   1 
ATOM   11363 C CB  . GLU G  1 171 ? 0.572   3.309   -18.210 1.00 43.90  ? 163 GLU G CB  1 
ATOM   11364 C CG  . GLU G  1 171 ? 0.285   2.945   -16.774 1.00 46.64  ? 163 GLU G CG  1 
ATOM   11365 C CD  . GLU G  1 171 ? -1.195  2.803   -16.504 1.00 54.49  ? 163 GLU G CD  1 
ATOM   11366 O OE1 . GLU G  1 171 ? -1.606  1.731   -16.006 1.00 55.24  ? 163 GLU G OE1 1 
ATOM   11367 O OE2 . GLU G  1 171 ? -1.944  3.767   -16.789 1.00 54.74  ? 163 GLU G OE2 1 
ATOM   11368 N N   . TYR G  1 172 ? 3.348   5.003   -16.892 1.00 38.55  ? 164 TYR G N   1 
ATOM   11369 C CA  . TYR G  1 172 ? 3.844   6.221   -16.273 1.00 37.04  ? 164 TYR G CA  1 
ATOM   11370 C C   . TYR G  1 172 ? 5.246   6.523   -16.809 1.00 36.33  ? 164 TYR G C   1 
ATOM   11371 O O   . TYR G  1 172 ? 5.837   7.560   -16.486 1.00 27.99  ? 164 TYR G O   1 
ATOM   11372 C CB  . TYR G  1 172 ? 3.854   6.085   -14.744 1.00 40.93  ? 164 TYR G CB  1 
ATOM   11373 C CG  . TYR G  1 172 ? 2.603   5.435   -14.190 1.00 41.99  ? 164 TYR G CG  1 
ATOM   11374 C CD1 . TYR G  1 172 ? 1.383   6.113   -14.185 1.00 41.81  ? 164 TYR G CD1 1 
ATOM   11375 C CD2 . TYR G  1 172 ? 2.636   4.135   -13.687 1.00 41.94  ? 164 TYR G CD2 1 
ATOM   11376 C CE1 . TYR G  1 172 ? 0.229   5.514   -13.691 1.00 42.89  ? 164 TYR G CE1 1 
ATOM   11377 C CE2 . TYR G  1 172 ? 1.491   3.527   -13.186 1.00 41.27  ? 164 TYR G CE2 1 
ATOM   11378 C CZ  . TYR G  1 172 ? 0.290   4.220   -13.191 1.00 45.53  ? 164 TYR G CZ  1 
ATOM   11379 O OH  . TYR G  1 172 ? -0.846  3.613   -12.697 1.00 47.33  ? 164 TYR G OH  1 
ATOM   11380 N N   . PHE G  1 173 ? 5.765   5.618   -17.645 1.00 41.59  ? 165 PHE G N   1 
ATOM   11381 C CA  . PHE G  1 173 ? 7.126   5.749   -18.172 1.00 30.17  ? 165 PHE G CA  1 
ATOM   11382 C C   . PHE G  1 173 ? 7.274   6.916   -19.119 1.00 24.52  ? 165 PHE G C   1 
ATOM   11383 O O   . PHE G  1 173 ? 6.409   7.176   -19.933 1.00 32.51  ? 165 PHE G O   1 
ATOM   11384 C CB  . PHE G  1 173 ? 7.612   4.478   -18.842 1.00 28.34  ? 165 PHE G CB  1 
ATOM   11385 C CG  . PHE G  1 173 ? 9.057   4.539   -19.226 1.00 38.70  ? 165 PHE G CG  1 
ATOM   11386 C CD1 . PHE G  1 173 ? 10.048  4.414   -18.258 1.00 33.03  ? 165 PHE G CD1 1 
ATOM   11387 C CD2 . PHE G  1 173 ? 9.433   4.758   -20.548 1.00 37.07  ? 165 PHE G CD2 1 
ATOM   11388 C CE1 . PHE G  1 173 ? 11.392  4.486   -18.603 1.00 35.76  ? 165 PHE G CE1 1 
ATOM   11389 C CE2 . PHE G  1 173 ? 10.771  4.828   -20.902 1.00 34.94  ? 165 PHE G CE2 1 
ATOM   11390 C CZ  . PHE G  1 173 ? 11.756  4.693   -19.930 1.00 36.76  ? 165 PHE G CZ  1 
ATOM   11391 N N   . SER G  1 174 ? 8.379   7.631   -18.993 1.00 28.21  ? 166 SER G N   1 
ATOM   11392 C CA  . SER G  1 174 ? 8.533   8.895   -19.694 1.00 30.75  ? 166 SER G CA  1 
ATOM   11393 C C   . SER G  1 174 ? 8.756   8.666   -21.180 1.00 33.60  ? 166 SER G C   1 
ATOM   11394 O O   . SER G  1 174 ? 9.588   7.844   -21.582 1.00 32.37  ? 166 SER G O   1 
ATOM   11395 C CB  . SER G  1 174 ? 9.694   9.698   -19.105 1.00 25.79  ? 166 SER G CB  1 
ATOM   11396 O OG  . SER G  1 174 ? 9.667   11.035  -19.567 1.00 26.25  ? 166 SER G OG  1 
ATOM   11397 N N   . GLN G  1 175 ? 8.004   9.396   -21.992 1.00 32.64  ? 167 GLN G N   1 
ATOM   11398 C CA  . GLN G  1 175 ? 8.176   9.331   -23.435 1.00 37.43  ? 167 GLN G CA  1 
ATOM   11399 C C   . GLN G  1 175 ? 9.512   9.977   -23.832 1.00 36.08  ? 167 GLN G C   1 
ATOM   11400 O O   . GLN G  1 175 ? 10.170  9.539   -24.781 1.00 37.20  ? 167 GLN G O   1 
ATOM   11401 C CB  . GLN G  1 175 ? 6.978   9.983   -24.160 1.00 31.30  ? 167 GLN G CB  1 
ATOM   11402 C CG  . GLN G  1 175 ? 6.803   11.484  -23.915 1.00 36.11  ? 167 GLN G CG  1 
ATOM   11403 C CD  . GLN G  1 175 ? 5.402   11.982  -24.249 1.00 39.72  ? 167 GLN G CD  1 
ATOM   11404 O OE1 . GLN G  1 175 ? 5.087   12.256  -25.402 1.00 40.17  ? 167 GLN G OE1 1 
ATOM   11405 N NE2 . GLN G  1 175 ? 4.557   12.104  -23.231 1.00 39.93  ? 167 GLN G NE2 1 
ATOM   11406 N N   . TYR G  1 176 ? 9.921   10.989  -23.070 1.00 31.93  ? 168 TYR G N   1 
ATOM   11407 C CA  . TYR G  1 176 ? 11.066  11.826  -23.418 1.00 31.05  ? 168 TYR G CA  1 
ATOM   11408 C C   . TYR G  1 176 ? 12.415  11.220  -23.031 1.00 29.25  ? 168 TYR G C   1 
ATOM   11409 O O   . TYR G  1 176 ? 13.447  11.885  -23.106 1.00 30.03  ? 168 TYR G O   1 
ATOM   11410 C CB  . TYR G  1 176 ? 10.919  13.210  -22.780 1.00 35.73  ? 168 TYR G CB  1 
ATOM   11411 C CG  . TYR G  1 176 ? 9.651   13.934  -23.162 1.00 39.55  ? 168 TYR G CG  1 
ATOM   11412 C CD1 . TYR G  1 176 ? 8.662   14.170  -22.220 1.00 36.65  ? 168 TYR G CD1 1 
ATOM   11413 C CD2 . TYR G  1 176 ? 9.437   14.381  -24.467 1.00 38.22  ? 168 TYR G CD2 1 
ATOM   11414 C CE1 . TYR G  1 176 ? 7.497   14.832  -22.554 1.00 37.81  ? 168 TYR G CE1 1 
ATOM   11415 C CE2 . TYR G  1 176 ? 8.273   15.039  -24.813 1.00 37.09  ? 168 TYR G CE2 1 
ATOM   11416 C CZ  . TYR G  1 176 ? 7.307   15.264  -23.847 1.00 41.41  ? 168 TYR G CZ  1 
ATOM   11417 O OH  . TYR G  1 176 ? 6.142   15.921  -24.154 1.00 39.43  ? 168 TYR G OH  1 
ATOM   11418 N N   . SER G  1 177 ? 12.403  9.964   -22.610 1.00 23.80  ? 169 SER G N   1 
ATOM   11419 C CA  . SER G  1 177 ? 13.630  9.254   -22.312 1.00 27.19  ? 169 SER G CA  1 
ATOM   11420 C C   . SER G  1 177 ? 14.338  8.843   -23.612 1.00 40.31  ? 169 SER G C   1 
ATOM   11421 O O   . SER G  1 177 ? 13.683  8.599   -24.629 1.00 39.40  ? 169 SER G O   1 
ATOM   11422 C CB  . SER G  1 177 ? 13.305  8.008   -21.496 1.00 30.95  ? 169 SER G CB  1 
ATOM   11423 O OG  . SER G  1 177 ? 14.476  7.299   -21.133 1.00 31.15  ? 169 SER G OG  1 
ATOM   11424 N N   . ARG G  1 178 ? 15.669  8.754   -23.580 1.00 35.30  ? 170 ARG G N   1 
ATOM   11425 C CA  . ARG G  1 178 ? 16.416  8.181   -24.697 1.00 29.86  ? 170 ARG G CA  1 
ATOM   11426 C C   . ARG G  1 178 ? 16.061  6.704   -24.880 1.00 32.66  ? 170 ARG G C   1 
ATOM   11427 O O   . ARG G  1 178 ? 16.448  6.079   -25.865 1.00 39.64  ? 170 ARG G O   1 
ATOM   11428 C CB  . ARG G  1 178 ? 17.931  8.298   -24.485 1.00 30.01  ? 170 ARG G CB  1 
ATOM   11429 C CG  . ARG G  1 178 ? 18.515  9.690   -24.604 1.00 33.13  ? 170 ARG G CG  1 
ATOM   11430 C CD  . ARG G  1 178 ? 20.038  9.627   -24.632 1.00 38.43  ? 170 ARG G CD  1 
ATOM   11431 N NE  . ARG G  1 178 ? 20.515  8.932   -25.830 1.00 55.98  ? 170 ARG G NE  1 
ATOM   11432 C CZ  . ARG G  1 178 ? 21.694  9.137   -26.417 1.00 53.30  ? 170 ARG G CZ  1 
ATOM   11433 N NH1 . ARG G  1 178 ? 22.555  10.023  -25.926 1.00 45.18  ? 170 ARG G NH1 1 
ATOM   11434 N NH2 . ARG G  1 178 ? 22.011  8.447   -27.501 1.00 54.15  ? 170 ARG G NH2 1 
ATOM   11435 N N   . PHE G  1 179 ? 15.338  6.133   -23.932 1.00 28.68  ? 171 PHE G N   1 
ATOM   11436 C CA  . PHE G  1 179 ? 15.043  4.715   -23.998 1.00 32.60  ? 171 PHE G CA  1 
ATOM   11437 C C   . PHE G  1 179 ? 13.545  4.495   -23.996 1.00 34.80  ? 171 PHE G C   1 
ATOM   11438 O O   . PHE G  1 179 ? 12.760  5.446   -23.933 1.00 36.74  ? 171 PHE G O   1 
ATOM   11439 C CB  . PHE G  1 179 ? 15.678  3.962   -22.827 1.00 29.03  ? 171 PHE G CB  1 
ATOM   11440 C CG  . PHE G  1 179 ? 17.152  4.211   -22.660 1.00 30.77  ? 171 PHE G CG  1 
ATOM   11441 C CD1 . PHE G  1 179 ? 17.618  5.406   -22.127 1.00 31.57  ? 171 PHE G CD1 1 
ATOM   11442 C CD2 . PHE G  1 179 ? 18.073  3.237   -23.008 1.00 34.68  ? 171 PHE G CD2 1 
ATOM   11443 C CE1 . PHE G  1 179 ? 18.969  5.631   -21.964 1.00 32.24  ? 171 PHE G CE1 1 
ATOM   11444 C CE2 . PHE G  1 179 ? 19.429  3.456   -22.843 1.00 28.34  ? 171 PHE G CE2 1 
ATOM   11445 C CZ  . PHE G  1 179 ? 19.875  4.655   -22.325 1.00 29.66  ? 171 PHE G CZ  1 
ATOM   11446 N N   . GLU G  1 180 ? 13.160  3.229   -24.074 1.00 28.41  ? 172 GLU G N   1 
ATOM   11447 C CA  . GLU G  1 180 ? 11.767  2.844   -24.029 1.00 33.22  ? 172 GLU G CA  1 
ATOM   11448 C C   . GLU G  1 180 ? 11.714  1.420   -23.529 1.00 39.95  ? 172 GLU G C   1 
ATOM   11449 O O   . GLU G  1 180 ? 12.700  0.686   -23.632 1.00 42.21  ? 172 GLU G O   1 
ATOM   11450 C CB  . GLU G  1 180 ? 11.127  2.947   -25.404 1.00 39.82  ? 172 GLU G CB  1 
ATOM   11451 C CG  . GLU G  1 180 ? 11.863  2.181   -26.495 1.00 43.91  ? 172 GLU G CG  1 
ATOM   11452 C CD  . GLU G  1 180 ? 11.074  2.137   -27.791 1.00 48.90  ? 172 GLU G CD  1 
ATOM   11453 O OE1 . GLU G  1 180 ? 9.951   1.583   -27.786 1.00 46.96  ? 172 GLU G OE1 1 
ATOM   11454 O OE2 . GLU G  1 180 ? 11.568  2.668   -28.806 1.00 47.44  ? 172 GLU G OE2 1 
ATOM   11455 N N   . ILE G  1 181 ? 10.566  1.027   -22.992 1.00 36.95  ? 173 ILE G N   1 
ATOM   11456 C CA  . ILE G  1 181 ? 10.467  -0.230  -22.270 1.00 41.97  ? 173 ILE G CA  1 
ATOM   11457 C C   . ILE G  1 181 ? 9.872   -1.353  -23.107 1.00 35.42  ? 173 ILE G C   1 
ATOM   11458 O O   . ILE G  1 181 ? 8.875   -1.159  -23.803 1.00 31.47  ? 173 ILE G O   1 
ATOM   11459 C CB  . ILE G  1 181 ? 9.592   -0.066  -21.003 1.00 44.60  ? 173 ILE G CB  1 
ATOM   11460 C CG1 . ILE G  1 181 ? 9.879   1.271   -20.313 1.00 42.30  ? 173 ILE G CG1 1 
ATOM   11461 C CG2 . ILE G  1 181 ? 9.795   -1.250  -20.057 1.00 30.56  ? 173 ILE G CG2 1 
ATOM   11462 C CD1 . ILE G  1 181 ? 11.118  1.248   -19.463 1.00 43.46  ? 173 ILE G CD1 1 
ATOM   11463 N N   . LEU G  1 182 ? 10.685  -2.384  -23.316 1.00 35.94  ? 174 LEU G N   1 
ATOM   11464 C CA  . LEU G  1 182 ? 10.246  -3.584  -24.011 1.00 39.76  ? 174 LEU G CA  1 
ATOM   11465 C C   . LEU G  1 182 ? 9.291   -4.384  -23.150 1.00 42.58  ? 174 LEU G C   1 
ATOM   11466 O O   . LEU G  1 182 ? 8.251   -4.861  -23.604 1.00 38.43  ? 174 LEU G O   1 
ATOM   11467 C CB  . LEU G  1 182 ? 11.448  -4.447  -24.402 1.00 39.70  ? 174 LEU G CB  1 
ATOM   11468 C CG  . LEU G  1 182 ? 12.307  -3.928  -25.557 1.00 34.71  ? 174 LEU G CG  1 
ATOM   11469 C CD1 . LEU G  1 182 ? 13.054  -5.071  -26.227 1.00 42.23  ? 174 LEU G CD1 1 
ATOM   11470 C CD2 . LEU G  1 182 ? 11.454  -3.175  -26.567 1.00 32.60  ? 174 LEU G CD2 1 
ATOM   11471 N N   . ASP G  1 183 ? 9.679   -4.521  -21.887 1.00 45.56  ? 175 ASP G N   1 
ATOM   11472 C CA  . ASP G  1 183 ? 8.940   -5.320  -20.927 1.00 46.65  ? 175 ASP G CA  1 
ATOM   11473 C C   . ASP G  1 183 ? 9.339   -4.993  -19.493 1.00 52.91  ? 175 ASP G C   1 
ATOM   11474 O O   . ASP G  1 183 ? 10.380  -4.388  -19.238 1.00 51.07  ? 175 ASP G O   1 
ATOM   11475 C CB  . ASP G  1 183 ? 9.147   -6.811  -21.202 1.00 44.53  ? 175 ASP G CB  1 
ATOM   11476 C CG  . ASP G  1 183 ? 7.941   -7.646  -20.821 1.00 56.78  ? 175 ASP G CG  1 
ATOM   11477 O OD1 . ASP G  1 183 ? 6.873   -7.060  -20.544 1.00 64.66  ? 175 ASP G OD1 1 
ATOM   11478 O OD2 . ASP G  1 183 ? 8.060   -8.889  -20.799 1.00 56.64  ? 175 ASP G OD2 1 
ATOM   11479 N N   . VAL G  1 184 ? 8.494   -5.421  -18.568 1.00 54.14  ? 176 VAL G N   1 
ATOM   11480 C CA  . VAL G  1 184 ? 8.780   -5.418  -17.133 1.00 47.65  ? 176 VAL G CA  1 
ATOM   11481 C C   . VAL G  1 184 ? 8.104   -6.588  -16.443 1.00 45.61  ? 176 VAL G C   1 
ATOM   11482 O O   . VAL G  1 184 ? 6.878   -6.675  -16.430 1.00 53.91  ? 176 VAL G O   1 
ATOM   11483 C CB  . VAL G  1 184 ? 8.247   -4.154  -16.435 1.00 47.68  ? 176 VAL G CB  1 
ATOM   11484 C CG1 . VAL G  1 184 ? 8.829   -4.050  -15.029 1.00 41.18  ? 176 VAL G CG1 1 
ATOM   11485 C CG2 . VAL G  1 184 ? 8.563   -2.914  -17.230 1.00 38.08  ? 176 VAL G CG2 1 
ATOM   11486 N N   . THR G  1 185 ? 8.894   -7.485  -15.866 1.00 38.81  ? 177 THR G N   1 
ATOM   11487 C CA  . THR G  1 185 ? 8.329   -8.606  -15.129 1.00 45.13  ? 177 THR G CA  1 
ATOM   11488 C C   . THR G  1 185 ? 8.861   -8.671  -13.695 1.00 50.78  ? 177 THR G C   1 
ATOM   11489 O O   . THR G  1 185 ? 10.033  -8.388  -13.442 1.00 46.77  ? 177 THR G O   1 
ATOM   11490 C CB  . THR G  1 185 ? 8.581   -9.943  -15.834 1.00 35.38  ? 177 THR G CB  1 
ATOM   11491 O OG1 . THR G  1 185 ? 9.963   -10.278 -15.722 1.00 37.99  ? 177 THR G OG1 1 
ATOM   11492 C CG2 . THR G  1 185 ? 8.192   -9.858  -17.292 1.00 46.82  ? 177 THR G CG2 1 
ATOM   11493 N N   . GLN G  1 186 ? 7.989   -9.050  -12.760 1.00 53.42  ? 178 GLN G N   1 
ATOM   11494 C CA  . GLN G  1 186 ? 8.308   -9.009  -11.339 1.00 43.44  ? 178 GLN G CA  1 
ATOM   11495 C C   . GLN G  1 186 ? 7.879   -10.304 -10.661 1.00 53.70  ? 178 GLN G C   1 
ATOM   11496 O O   . GLN G  1 186 ? 6.684   -10.550 -10.518 1.00 62.18  ? 178 GLN G O   1 
ATOM   11497 C CB  . GLN G  1 186 ? 7.580   -7.826  -10.686 1.00 44.65  ? 178 GLN G CB  1 
ATOM   11498 C CG  . GLN G  1 186 ? 7.609   -6.535  -11.505 1.00 44.39  ? 178 GLN G CG  1 
ATOM   11499 C CD  . GLN G  1 186 ? 7.093   -5.319  -10.744 1.00 47.82  ? 178 GLN G CD  1 
ATOM   11500 O OE1 . GLN G  1 186 ? 7.765   -4.802  -9.851  1.00 40.62  ? 178 GLN G OE1 1 
ATOM   11501 N NE2 . GLN G  1 186 ? 5.899   -4.851  -11.107 1.00 57.21  ? 178 GLN G NE2 1 
ATOM   11502 N N   . LYS G  1 187 ? 8.836   -11.123 -10.224 1.00 47.24  ? 179 LYS G N   1 
ATOM   11503 C CA  . LYS G  1 187 ? 8.492   -12.410 -9.607  1.00 52.63  ? 179 LYS G CA  1 
ATOM   11504 C C   . LYS G  1 187 ? 8.996   -12.637 -8.171  1.00 53.25  ? 179 LYS G C   1 
ATOM   11505 O O   . LYS G  1 187 ? 9.980   -12.034 -7.748  1.00 52.73  ? 179 LYS G O   1 
ATOM   11506 C CB  . LYS G  1 187 ? 8.939   -13.563 -10.508 1.00 52.16  ? 179 LYS G CB  1 
ATOM   11507 C CG  . LYS G  1 187 ? 8.048   -13.742 -11.731 1.00 67.80  ? 179 LYS G CG  1 
ATOM   11508 C CD  . LYS G  1 187 ? 8.239   -15.102 -12.399 1.00 66.94  ? 179 LYS G CD  1 
ATOM   11509 C CE  . LYS G  1 187 ? 6.990   -15.504 -13.178 1.00 58.30  ? 179 LYS G CE  1 
ATOM   11510 N NZ  . LYS G  1 187 ? 6.554   -14.457 -14.153 1.00 64.48  ? 179 LYS G NZ  1 
ATOM   11511 N N   . LYS G  1 188 ? 8.311   -13.514 -7.431  1.00 50.76  ? 180 LYS G N   1 
ATOM   11512 C CA  . LYS G  1 188 ? 8.774   -13.952 -6.112  1.00 42.53  ? 180 LYS G CA  1 
ATOM   11513 C C   . LYS G  1 188 ? 10.087  -14.688 -6.264  1.00 40.46  ? 180 LYS G C   1 
ATOM   11514 O O   . LYS G  1 188 ? 10.417  -15.159 -7.344  1.00 50.03  ? 180 LYS G O   1 
ATOM   11515 C CB  . LYS G  1 188 ? 7.750   -14.870 -5.430  1.00 45.50  ? 180 LYS G CB  1 
ATOM   11516 C CG  . LYS G  1 188 ? 6.797   -14.172 -4.455  1.00 51.39  ? 180 LYS G CG  1 
ATOM   11517 C CD  . LYS G  1 188 ? 5.464   -14.929 -4.294  1.00 57.09  ? 180 LYS G CD  1 
ATOM   11518 C CE  . LYS G  1 188 ? 5.597   -16.204 -3.468  1.00 52.67  ? 180 LYS G CE  1 
ATOM   11519 N NZ  . LYS G  1 188 ? 5.632   -15.921 -2.003  1.00 49.05  ? 180 LYS G NZ  1 
ATOM   11520 N N   . ASN G  1 189 ? 10.825  -14.804 -5.171  1.00 43.99  ? 181 ASN G N   1 
ATOM   11521 C CA  . ASN G  1 189 ? 12.156  -15.384 -5.206  1.00 48.25  ? 181 ASN G CA  1 
ATOM   11522 C C   . ASN G  1 189 ? 12.661  -15.623 -3.788  1.00 49.95  ? 181 ASN G C   1 
ATOM   11523 O O   . ASN G  1 189 ? 12.082  -15.133 -2.817  1.00 49.79  ? 181 ASN G O   1 
ATOM   11524 C CB  . ASN G  1 189 ? 13.112  -14.449 -5.960  1.00 49.86  ? 181 ASN G CB  1 
ATOM   11525 C CG  . ASN G  1 189 ? 14.356  -15.155 -6.454  1.00 51.88  ? 181 ASN G CG  1 
ATOM   11526 O OD1 . ASN G  1 189 ? 15.433  -15.027 -5.870  1.00 54.77  ? 181 ASN G OD1 1 
ATOM   11527 N ND2 . ASN G  1 189 ? 14.215  -15.906 -7.541  1.00 52.91  ? 181 ASN G ND2 1 
ATOM   11528 N N   . SER G  1 190 ? 13.732  -16.402 -3.679  1.00 51.13  ? 182 SER G N   1 
ATOM   11529 C CA  . SER G  1 190 ? 14.347  -16.685 -2.390  1.00 51.52  ? 182 SER G CA  1 
ATOM   11530 C C   . SER G  1 190 ? 15.870  -16.658 -2.482  1.00 56.53  ? 182 SER G C   1 
ATOM   11531 O O   . SER G  1 190 ? 16.445  -16.966 -3.526  1.00 68.39  ? 182 SER G O   1 
ATOM   11532 C CB  . SER G  1 190 ? 13.877  -18.041 -1.858  1.00 53.66  ? 182 SER G CB  1 
ATOM   11533 O OG  . SER G  1 190 ? 14.440  -18.313 -0.587  1.00 53.19  ? 182 SER G OG  1 
ATOM   11534 N N   . VAL G  1 191 ? 16.514  -16.296 -1.379  1.00 58.80  ? 183 VAL G N   1 
ATOM   11535 C CA  . VAL G  1 191 ? 17.969  -16.324 -1.284  1.00 62.21  ? 183 VAL G CA  1 
ATOM   11536 C C   . VAL G  1 191 ? 18.379  -16.990 0.026   1.00 63.67  ? 183 VAL G C   1 
ATOM   11537 O O   . VAL G  1 191 ? 17.691  -16.846 1.036   1.00 58.73  ? 183 VAL G O   1 
ATOM   11538 C CB  . VAL G  1 191 ? 18.569  -14.908 -1.344  1.00 60.81  ? 183 VAL G CB  1 
ATOM   11539 C CG1 . VAL G  1 191 ? 18.130  -14.200 -2.617  1.00 52.24  ? 183 VAL G CG1 1 
ATOM   11540 C CG2 . VAL G  1 191 ? 18.166  -14.108 -0.115  1.00 54.13  ? 183 VAL G CG2 1 
ATOM   11541 N N   . THR G  1 192 ? 19.387  -17.842 -0.056  1.00 64.68  ? 184 THR G N   1 
ATOM   11542 C CA  . THR G  1 192 ? 20.001  -18.420 1.116   1.00 66.85  ? 184 THR G CA  1 
ATOM   11543 C C   . THR G  1 192 ? 21.493  -18.308 0.912   1.00 75.75  ? 184 THR G C   1 
ATOM   11544 O O   . THR G  1 192 ? 22.007  -18.702 -0.135  1.00 86.59  ? 184 THR G O   1 
ATOM   11545 C CB  . THR G  1 192 ? 19.617  -19.900 1.288   1.00 56.03  ? 184 THR G CB  1 
ATOM   11546 O OG1 . THR G  1 192 ? 20.581  -20.553 2.124   1.00 53.59  ? 184 THR G OG1 1 
ATOM   11547 C CG2 . THR G  1 192 ? 19.568  -20.599 -0.062  1.00 57.92  ? 184 THR G CG2 1 
ATOM   11548 N N   . TYR G  1 193 ? 22.202  -17.792 1.903   1.00 65.27  ? 185 TYR G N   1 
ATOM   11549 C CA  . TYR G  1 193 ? 23.668  -17.814 1.812   1.00 69.21  ? 185 TYR G CA  1 
ATOM   11550 C C   . TYR G  1 193 ? 24.298  -19.109 2.335   1.00 70.94  ? 185 TYR G C   1 
ATOM   11551 O O   . TYR G  1 193 ? 23.612  -19.986 2.861   1.00 63.59  ? 185 TYR G O   1 
ATOM   11552 C CB  . TYR G  1 193 ? 24.297  -16.583 2.490   1.00 70.35  ? 185 TYR G CB  1 
ATOM   11553 C CG  . TYR G  1 193 ? 24.481  -16.692 3.995   1.00 71.97  ? 185 TYR G CG  1 
ATOM   11554 C CD1 . TYR G  1 193 ? 25.635  -17.255 4.542   1.00 72.66  ? 185 TYR G CD1 1 
ATOM   11555 C CD2 . TYR G  1 193 ? 23.512  -16.215 4.869   1.00 76.57  ? 185 TYR G CD2 1 
ATOM   11556 C CE1 . TYR G  1 193 ? 25.805  -17.356 5.916   1.00 70.67  ? 185 TYR G CE1 1 
ATOM   11557 C CE2 . TYR G  1 193 ? 23.676  -16.303 6.247   1.00 78.73  ? 185 TYR G CE2 1 
ATOM   11558 C CZ  . TYR G  1 193 ? 24.823  -16.876 6.765   1.00 71.96  ? 185 TYR G CZ  1 
ATOM   11559 O OH  . TYR G  1 193 ? 24.979  -16.967 8.134   1.00 54.81  ? 185 TYR G OH  1 
ATOM   11560 N N   . PRO G  1 197 ? 21.470  -20.146 7.630   1.00 58.75  ? 189 PRO G N   1 
ATOM   11561 C CA  . PRO G  1 197 ? 20.514  -20.218 8.743   1.00 58.48  ? 189 PRO G CA  1 
ATOM   11562 C C   . PRO G  1 197 ? 19.083  -20.264 8.225   1.00 54.67  ? 189 PRO G C   1 
ATOM   11563 O O   . PRO G  1 197 ? 18.498  -21.347 8.161   1.00 53.62  ? 189 PRO G O   1 
ATOM   11564 C CB  . PRO G  1 197 ? 20.774  -18.920 9.522   1.00 62.57  ? 189 PRO G CB  1 
ATOM   11565 C CG  . PRO G  1 197 ? 21.625  -18.053 8.597   1.00 58.91  ? 189 PRO G CG  1 
ATOM   11566 C CD  . PRO G  1 197 ? 22.398  -19.013 7.768   1.00 55.14  ? 189 PRO G CD  1 
ATOM   11567 N N   . GLU G  1 198 ? 18.595  -19.086 7.817   1.00 54.79  ? 190 GLU G N   1 
ATOM   11568 C CA  . GLU G  1 198 ? 17.238  -18.835 7.320   1.00 55.67  ? 190 GLU G CA  1 
ATOM   11569 C C   . GLU G  1 198 ? 17.251  -17.970 6.042   1.00 56.40  ? 190 GLU G C   1 
ATOM   11570 O O   . GLU G  1 198 ? 18.251  -17.322 5.734   1.00 55.13  ? 190 GLU G O   1 
ATOM   11571 C CB  . GLU G  1 198 ? 16.386  -18.166 8.400   1.00 62.37  ? 190 GLU G CB  1 
ATOM   11572 C CG  . GLU G  1 198 ? 15.476  -19.123 9.154   1.00 67.26  ? 190 GLU G CG  1 
ATOM   11573 C CD  . GLU G  1 198 ? 14.301  -19.590 8.319   1.00 72.16  ? 190 GLU G CD  1 
ATOM   11574 O OE1 . GLU G  1 198 ? 13.822  -18.806 7.472   1.00 58.40  ? 190 GLU G OE1 1 
ATOM   11575 O OE2 . GLU G  1 198 ? 13.855  -20.741 8.508   1.00 68.41  ? 190 GLU G OE2 1 
ATOM   11576 N N   . ALA G  1 199 ? 16.142  -17.985 5.302   1.00 54.91  ? 191 ALA G N   1 
ATOM   11577 C CA  . ALA G  1 199 ? 16.058  -17.455 3.943   1.00 51.74  ? 191 ALA G CA  1 
ATOM   11578 C C   . ALA G  1 199 ? 15.389  -16.083 3.908   1.00 48.49  ? 191 ALA G C   1 
ATOM   11579 O O   . ALA G  1 199 ? 14.483  -15.812 4.694   1.00 48.99  ? 191 ALA G O   1 
ATOM   11580 C CB  . ALA G  1 199 ? 15.300  -18.428 3.059   1.00 49.76  ? 191 ALA G CB  1 
ATOM   11581 N N   . TYR G  1 200 ? 15.831  -15.226 2.990   1.00 46.89  ? 192 TYR G N   1 
ATOM   11582 C CA  . TYR G  1 200 ? 15.262  -13.888 2.849   1.00 38.14  ? 192 TYR G CA  1 
ATOM   11583 C C   . TYR G  1 200 ? 14.466  -13.805 1.560   1.00 44.06  ? 192 TYR G C   1 
ATOM   11584 O O   . TYR G  1 200 ? 15.034  -13.831 0.467   1.00 49.33  ? 192 TYR G O   1 
ATOM   11585 C CB  . TYR G  1 200 ? 16.360  -12.813 2.873   1.00 39.12  ? 192 TYR G CB  1 
ATOM   11586 C CG  . TYR G  1 200 ? 17.173  -12.800 4.156   1.00 43.28  ? 192 TYR G CG  1 
ATOM   11587 C CD1 . TYR G  1 200 ? 18.124  -13.785 4.410   1.00 43.32  ? 192 TYR G CD1 1 
ATOM   11588 C CD2 . TYR G  1 200 ? 16.986  -11.808 5.120   1.00 40.25  ? 192 TYR G CD2 1 
ATOM   11589 C CE1 . TYR G  1 200 ? 18.864  -13.790 5.585   1.00 41.99  ? 192 TYR G CE1 1 
ATOM   11590 C CE2 . TYR G  1 200 ? 17.730  -11.801 6.305   1.00 35.94  ? 192 TYR G CE2 1 
ATOM   11591 C CZ  . TYR G  1 200 ? 18.666  -12.798 6.532   1.00 41.19  ? 192 TYR G CZ  1 
ATOM   11592 O OH  . TYR G  1 200 ? 19.410  -12.811 7.700   1.00 36.54  ? 192 TYR G OH  1 
ATOM   11593 N N   . GLU G  1 201 ? 13.147  -13.729 1.695   1.00 40.03  ? 193 GLU G N   1 
ATOM   11594 C CA  . GLU G  1 201 ? 12.268  -13.539 0.552   1.00 37.69  ? 193 GLU G CA  1 
ATOM   11595 C C   . GLU G  1 201 ? 12.534  -12.194 -0.113  1.00 39.94  ? 193 GLU G C   1 
ATOM   11596 O O   . GLU G  1 201 ? 12.850  -11.212 0.548   1.00 43.51  ? 193 GLU G O   1 
ATOM   11597 C CB  . GLU G  1 201 ? 10.804  -13.610 0.983   1.00 36.20  ? 193 GLU G CB  1 
ATOM   11598 C CG  . GLU G  1 201 ? 10.344  -14.980 1.449   1.00 41.07  ? 193 GLU G CG  1 
ATOM   11599 C CD  . GLU G  1 201 ? 8.828   -15.129 1.383   1.00 52.64  ? 193 GLU G CD  1 
ATOM   11600 O OE1 . GLU G  1 201 ? 8.157   -14.153 0.975   1.00 51.01  ? 193 GLU G OE1 1 
ATOM   11601 O OE2 . GLU G  1 201 ? 8.308   -16.217 1.723   1.00 51.19  ? 193 GLU G OE2 1 
ATOM   11602 N N   . ASP G  1 202 ? 12.407  -12.157 -1.430  1.00 45.80  ? 194 ASP G N   1 
ATOM   11603 C CA  . ASP G  1 202 ? 12.597  -10.925 -2.179  1.00 46.31  ? 194 ASP G CA  1 
ATOM   11604 C C   . ASP G  1 202 ? 11.857  -11.045 -3.496  1.00 46.32  ? 194 ASP G C   1 
ATOM   11605 O O   . ASP G  1 202 ? 11.541  -12.151 -3.932  1.00 45.80  ? 194 ASP G O   1 
ATOM   11606 C CB  . ASP G  1 202 ? 14.081  -10.673 -2.456  1.00 45.72  ? 194 ASP G CB  1 
ATOM   11607 C CG  . ASP G  1 202 ? 14.634  -11.560 -3.571  1.00 52.57  ? 194 ASP G CG  1 
ATOM   11608 O OD1 . ASP G  1 202 ? 14.486  -11.205 -4.766  1.00 49.80  ? 194 ASP G OD1 1 
ATOM   11609 O OD2 . ASP G  1 202 ? 15.233  -12.611 -3.250  1.00 58.50  ? 194 ASP G OD2 1 
ATOM   11610 N N   . VAL G  1 203 ? 11.584  -9.908  -4.128  1.00 42.08  ? 195 VAL G N   1 
ATOM   11611 C CA  . VAL G  1 203 ? 10.970  -9.904  -5.446  1.00 45.69  ? 195 VAL G CA  1 
ATOM   11612 C C   . VAL G  1 203 ? 11.987  -9.447  -6.480  1.00 43.16  ? 195 VAL G C   1 
ATOM   11613 O O   . VAL G  1 203 ? 12.710  -8.479  -6.258  1.00 37.55  ? 195 VAL G O   1 
ATOM   11614 C CB  . VAL G  1 203 ? 9.698   -9.026  -5.501  1.00 48.50  ? 195 VAL G CB  1 
ATOM   11615 C CG1 . VAL G  1 203 ? 8.596   -9.666  -4.678  1.00 46.81  ? 195 VAL G CG1 1 
ATOM   11616 C CG2 . VAL G  1 203 ? 9.982   -7.614  -5.002  1.00 45.89  ? 195 VAL G CG2 1 
ATOM   11617 N N   . GLU G  1 204 ? 12.050  -10.168 -7.599  1.00 51.89  ? 196 GLU G N   1 
ATOM   11618 C CA  . GLU G  1 204 ? 13.014  -9.886  -8.661  1.00 40.39  ? 196 GLU G CA  1 
ATOM   11619 C C   . GLU G  1 204 ? 12.347  -9.104  -9.788  1.00 29.42  ? 196 GLU G C   1 
ATOM   11620 O O   . GLU G  1 204 ? 11.478  -9.614  -10.483 1.00 40.94  ? 196 GLU G O   1 
ATOM   11621 C CB  . GLU G  1 204 ? 13.598  -11.197 -9.179  1.00 42.89  ? 196 GLU G CB  1 
ATOM   11622 C CG  . GLU G  1 204 ? 14.920  -11.064 -9.917  1.00 56.65  ? 196 GLU G CG  1 
ATOM   11623 C CD  . GLU G  1 204 ? 15.392  -12.393 -10.508 1.00 69.67  ? 196 GLU G CD  1 
ATOM   11624 O OE1 . GLU G  1 204 ? 16.489  -12.859 -10.125 1.00 79.41  ? 196 GLU G OE1 1 
ATOM   11625 O OE2 . GLU G  1 204 ? 14.670  -12.969 -11.357 1.00 57.50  ? 196 GLU G OE2 1 
ATOM   11626 N N   . VAL G  1 205 ? 12.721  -7.846  -9.941  1.00 26.76  ? 197 VAL G N   1 
ATOM   11627 C CA  . VAL G  1 205 ? 12.191  -7.042  -11.031 1.00 33.70  ? 197 VAL G CA  1 
ATOM   11628 C C   . VAL G  1 205 ? 13.116  -7.171  -12.252 1.00 41.58  ? 197 VAL G C   1 
ATOM   11629 O O   . VAL G  1 205 ? 14.341  -7.015  -12.145 1.00 34.96  ? 197 VAL G O   1 
ATOM   11630 C CB  . VAL G  1 205 ? 12.039  -5.565  -10.620 1.00 33.16  ? 197 VAL G CB  1 
ATOM   11631 C CG1 . VAL G  1 205 ? 11.705  -4.703  -11.832 1.00 38.47  ? 197 VAL G CG1 1 
ATOM   11632 C CG2 . VAL G  1 205 ? 10.979  -5.422  -9.556  1.00 30.92  ? 197 VAL G CG2 1 
ATOM   11633 N N   . SER G  1 206 ? 12.527  -7.485  -13.404 1.00 44.42  ? 198 SER G N   1 
ATOM   11634 C CA  . SER G  1 206 ? 13.288  -7.712  -14.632 1.00 33.05  ? 198 SER G CA  1 
ATOM   11635 C C   . SER G  1 206 ? 12.873  -6.712  -15.681 1.00 35.09  ? 198 SER G C   1 
ATOM   11636 O O   . SER G  1 206 ? 11.845  -6.878  -16.333 1.00 38.57  ? 198 SER G O   1 
ATOM   11637 C CB  . SER G  1 206 ? 13.054  -9.120  -15.160 1.00 27.72  ? 198 SER G CB  1 
ATOM   11638 O OG  . SER G  1 206 ? 13.535  -10.082 -14.244 1.00 44.47  ? 198 SER G OG  1 
ATOM   11639 N N   . LEU G  1 207 ? 13.681  -5.671  -15.835 1.00 39.84  ? 199 LEU G N   1 
ATOM   11640 C CA  . LEU G  1 207 ? 13.406  -4.611  -16.791 1.00 34.73  ? 199 LEU G CA  1 
ATOM   11641 C C   . LEU G  1 207 ? 14.177  -4.851  -18.076 1.00 39.78  ? 199 LEU G C   1 
ATOM   11642 O O   . LEU G  1 207 ? 15.412  -4.804  -18.090 1.00 38.04  ? 199 LEU G O   1 
ATOM   11643 C CB  . LEU G  1 207 ? 13.768  -3.253  -16.194 1.00 35.11  ? 199 LEU G CB  1 
ATOM   11644 C CG  . LEU G  1 207 ? 13.805  -2.044  -17.117 1.00 31.63  ? 199 LEU G CG  1 
ATOM   11645 C CD1 . LEU G  1 207 ? 12.514  -1.925  -17.884 1.00 34.65  ? 199 LEU G CD1 1 
ATOM   11646 C CD2 . LEU G  1 207 ? 14.059  -0.791  -16.304 1.00 24.66  ? 199 LEU G CD2 1 
ATOM   11647 N N   . ASN G  1 208 ? 13.418  -5.133  -19.138 1.00 46.35  ? 200 ASN G N   1 
ATOM   11648 C CA  . ASN G  1 208 ? 13.922  -5.283  -20.497 1.00 37.66  ? 200 ASN G CA  1 
ATOM   11649 C C   . ASN G  1 208 ? 13.645  -4.001  -21.280 1.00 35.01  ? 200 ASN G C   1 
ATOM   11650 O O   . ASN G  1 208 ? 12.488  -3.639  -21.504 1.00 38.78  ? 200 ASN G O   1 
ATOM   11651 C CB  . ASN G  1 208 ? 13.245  -6.476  -21.177 1.00 40.96  ? 200 ASN G CB  1 
ATOM   11652 C CG  . ASN G  1 208 ? 13.933  -6.882  -22.476 1.00 43.79  ? 200 ASN G CG  1 
ATOM   11653 O OD1 . ASN G  1 208 ? 15.160  -6.809  -22.590 1.00 42.93  ? 200 ASN G OD1 1 
ATOM   11654 N ND2 . ASN G  1 208 ? 13.143  -7.317  -23.461 1.00 36.10  ? 200 ASN G ND2 1 
ATOM   11655 N N   . PHE G  1 209 ? 14.706  -3.317  -21.694 1.00 35.83  ? 201 PHE G N   1 
ATOM   11656 C CA  . PHE G  1 209 ? 14.588  -1.997  -22.320 1.00 37.60  ? 201 PHE G CA  1 
ATOM   11657 C C   . PHE G  1 209 ? 15.648  -1.842  -23.423 1.00 37.41  ? 201 PHE G C   1 
ATOM   11658 O O   . PHE G  1 209 ? 16.582  -2.645  -23.497 1.00 35.09  ? 201 PHE G O   1 
ATOM   11659 C CB  . PHE G  1 209 ? 14.758  -0.898  -21.255 1.00 33.53  ? 201 PHE G CB  1 
ATOM   11660 C CG  . PHE G  1 209 ? 16.176  -0.744  -20.766 1.00 27.39  ? 201 PHE G CG  1 
ATOM   11661 C CD1 . PHE G  1 209 ? 16.796  -1.766  -20.063 1.00 25.36  ? 201 PHE G CD1 1 
ATOM   11662 C CD2 . PHE G  1 209 ? 16.894  0.415   -21.036 1.00 26.24  ? 201 PHE G CD2 1 
ATOM   11663 C CE1 . PHE G  1 209 ? 18.103  -1.635  -19.637 1.00 29.81  ? 201 PHE G CE1 1 
ATOM   11664 C CE2 . PHE G  1 209 ? 18.198  0.559   -20.603 1.00 23.80  ? 201 PHE G CE2 1 
ATOM   11665 C CZ  . PHE G  1 209 ? 18.808  -0.465  -19.904 1.00 24.98  ? 201 PHE G CZ  1 
ATOM   11666 N N   . ARG G  1 210 ? 15.502  -0.831  -24.282 1.00 31.71  ? 202 ARG G N   1 
ATOM   11667 C CA  . ARG G  1 210 ? 16.442  -0.615  -25.394 1.00 41.63  ? 202 ARG G CA  1 
ATOM   11668 C C   . ARG G  1 210 ? 16.550  0.850   -25.849 1.00 42.78  ? 202 ARG G C   1 
ATOM   11669 O O   . ARG G  1 210 ? 15.661  1.654   -25.569 1.00 36.99  ? 202 ARG G O   1 
ATOM   11670 C CB  . ARG G  1 210 ? 16.072  -1.504  -26.584 1.00 47.21  ? 202 ARG G CB  1 
ATOM   11671 C CG  . ARG G  1 210 ? 15.020  -0.906  -27.503 1.00 44.89  ? 202 ARG G CG  1 
ATOM   11672 C CD  . ARG G  1 210 ? 14.431  -1.958  -28.428 1.00 35.75  ? 202 ARG G CD  1 
ATOM   11673 N NE  . ARG G  1 210 ? 13.407  -1.402  -29.308 1.00 36.40  ? 202 ARG G NE  1 
ATOM   11674 C CZ  . ARG G  1 210 ? 12.666  -2.124  -30.141 1.00 38.73  ? 202 ARG G CZ  1 
ATOM   11675 N NH1 . ARG G  1 210 ? 12.833  -3.438  -30.212 1.00 43.05  ? 202 ARG G NH1 1 
ATOM   11676 N NH2 . ARG G  1 210 ? 11.757  -1.534  -30.905 1.00 29.56  ? 202 ARG G NH2 1 
ATOM   11677 N N   . LYS G  1 211 ? 17.634  1.193   -26.551 1.00 41.65  ? 203 LYS G N   1 
ATOM   11678 C CA  . LYS G  1 211 ? 17.804  2.546   -27.069 1.00 40.15  ? 203 LYS G CA  1 
ATOM   11679 C C   . LYS G  1 211 ? 16.820  2.819   -28.209 1.00 44.13  ? 203 LYS G C   1 
ATOM   11680 O O   . LYS G  1 211 ? 16.448  1.907   -28.941 1.00 38.08  ? 203 LYS G O   1 
ATOM   11681 C CB  . LYS G  1 211 ? 19.243  2.787   -27.527 1.00 34.51  ? 203 LYS G CB  1 
ATOM   11682 C CG  . LYS G  1 211 ? 19.540  4.251   -27.834 1.00 43.57  ? 203 LYS G CG  1 
ATOM   11683 C CD  . LYS G  1 211 ? 20.844  4.430   -28.593 1.00 52.06  ? 203 LYS G CD  1 
ATOM   11684 C CE  . LYS G  1 211 ? 20.961  5.847   -29.130 1.00 55.90  ? 203 LYS G CE  1 
ATOM   11685 N NZ  . LYS G  1 211 ? 22.154  6.036   -30.001 1.00 64.13  ? 203 LYS G NZ  1 
ATOM   11686 N N   . LYS G  1 212 ? 16.397  4.075   -28.345 1.00 47.80  ? 204 LYS G N   1 
ATOM   11687 C CA  . LYS G  1 212 ? 15.370  4.455   -29.316 1.00 45.92  ? 204 LYS G CA  1 
ATOM   11688 C C   . LYS G  1 212 ? 15.914  4.697   -30.722 1.00 55.04  ? 204 LYS G C   1 
ATOM   11689 O O   . LYS G  1 212 ? 17.035  5.175   -30.906 1.00 47.60  ? 204 LYS G O   1 
ATOM   11690 C CB  . LYS G  1 212 ? 14.601  5.697   -28.842 1.00 39.85  ? 204 LYS G CB  1 
ATOM   11691 C CG  . LYS G  1 212 ? 13.265  5.394   -28.155 1.00 44.32  ? 204 LYS G CG  1 
ATOM   11692 C CD  . LYS G  1 212 ? 12.662  6.636   -27.487 1.00 36.84  ? 204 LYS G CD  1 
ATOM   11693 C CE  . LYS G  1 212 ? 11.313  6.319   -26.841 1.00 47.81  ? 204 LYS G CE  1 
ATOM   11694 N NZ  . LYS G  1 212 ? 11.077  7.019   -25.521 1.00 46.93  ? 204 LYS G NZ  1 
ATOM   11695 N N   . GLY G  1 213 ? 15.092  4.361   -31.709 1.00 59.96  ? 205 GLY G N   1 
ATOM   11696 C CA  . GLY G  1 213 ? 15.399  4.609   -33.102 1.00 63.07  ? 205 GLY G CA  1 
ATOM   11697 C C   . GLY G  1 213 ? 14.104  4.624   -33.888 1.00 74.07  ? 205 GLY G C   1 
ATOM   11698 O O   . GLY G  1 213 ? 13.027  4.435   -33.313 1.00 73.77  ? 205 GLY G O   1 
ATOM   11699 N N   . ASP H  1 1   ? 12.006  -20.404 21.475  1.00 43.32  ? -7  ASP H N   1 
ATOM   11700 C CA  . ASP H  1 1   ? 12.250  -20.953 20.148  1.00 56.03  ? -7  ASP H CA  1 
ATOM   11701 C C   . ASP H  1 1   ? 11.678  -20.070 19.034  1.00 64.39  ? -7  ASP H C   1 
ATOM   11702 O O   . ASP H  1 1   ? 11.231  -18.944 19.277  1.00 54.77  ? -7  ASP H O   1 
ATOM   11703 C CB  . ASP H  1 1   ? 11.708  -22.386 20.039  1.00 64.93  ? -7  ASP H CB  1 
ATOM   11704 C CG  . ASP H  1 1   ? 10.187  -22.460 20.183  1.00 70.11  ? -7  ASP H CG  1 
ATOM   11705 O OD1 . ASP H  1 1   ? 9.579   -23.369 19.573  1.00 68.98  ? -7  ASP H OD1 1 
ATOM   11706 O OD2 . ASP H  1 1   ? 9.602   -21.620 20.905  1.00 62.67  ? -7  ASP H OD2 1 
ATOM   11707 N N   . TYR H  1 2   ? 11.694  -20.601 17.812  1.00 70.24  ? -6  TYR H N   1 
ATOM   11708 C CA  . TYR H  1 2   ? 11.311  -19.847 16.620  1.00 66.79  ? -6  TYR H CA  1 
ATOM   11709 C C   . TYR H  1 2   ? 9.810   -19.948 16.345  1.00 59.55  ? -6  TYR H C   1 
ATOM   11710 O O   . TYR H  1 2   ? 9.300   -19.358 15.390  1.00 55.82  ? -6  TYR H O   1 
ATOM   11711 C CB  . TYR H  1 2   ? 12.099  -20.356 15.404  1.00 69.04  ? -6  TYR H CB  1 
ATOM   11712 C CG  . TYR H  1 2   ? 11.681  -21.746 14.979  1.00 72.30  ? -6  TYR H CG  1 
ATOM   11713 C CD1 . TYR H  1 2   ? 10.722  -21.931 13.988  1.00 70.49  ? -6  TYR H CD1 1 
ATOM   11714 C CD2 . TYR H  1 2   ? 12.222  -22.872 15.587  1.00 75.85  ? -6  TYR H CD2 1 
ATOM   11715 C CE1 . TYR H  1 2   ? 10.319  -23.195 13.610  1.00 71.81  ? -6  TYR H CE1 1 
ATOM   11716 C CE2 . TYR H  1 2   ? 11.827  -24.144 15.212  1.00 82.62  ? -6  TYR H CE2 1 
ATOM   11717 C CZ  . TYR H  1 2   ? 10.874  -24.298 14.222  1.00 81.04  ? -6  TYR H CZ  1 
ATOM   11718 O OH  . TYR H  1 2   ? 10.473  -25.559 13.840  1.00 86.29  ? -6  TYR H OH  1 
ATOM   11719 N N   . LYS H  1 3   ? 9.104   -20.708 17.173  1.00 65.26  ? -5  LYS H N   1 
ATOM   11720 C CA  . LYS H  1 3   ? 7.679   -20.926 16.952  1.00 67.51  ? -5  LYS H CA  1 
ATOM   11721 C C   . LYS H  1 3   ? 6.862   -19.761 17.507  1.00 61.91  ? -5  LYS H C   1 
ATOM   11722 O O   . LYS H  1 3   ? 5.736   -19.515 17.072  1.00 57.53  ? -5  LYS H O   1 
ATOM   11723 C CB  . LYS H  1 3   ? 7.226   -22.261 17.556  1.00 68.73  ? -5  LYS H CB  1 
ATOM   11724 C CG  . LYS H  1 3   ? 5.933   -22.822 16.959  1.00 71.25  ? -5  LYS H CG  1 
ATOM   11725 C CD  . LYS H  1 3   ? 6.061   -23.127 15.466  1.00 66.82  ? -5  LYS H CD  1 
ATOM   11726 C CE  . LYS H  1 3   ? 4.719   -23.577 14.887  1.00 67.99  ? -5  LYS H CE  1 
ATOM   11727 N NZ  . LYS H  1 3   ? 4.789   -23.963 13.447  1.00 52.93  ? -5  LYS H NZ  1 
ATOM   11728 N N   . ASP H  1 4   ? 7.438   -19.036 18.462  1.00 64.11  ? -4  ASP H N   1 
ATOM   11729 C CA  . ASP H  1 4   ? 6.777   -17.856 19.004  1.00 58.59  ? -4  ASP H CA  1 
ATOM   11730 C C   . ASP H  1 4   ? 7.548   -16.581 18.661  1.00 52.21  ? -4  ASP H C   1 
ATOM   11731 O O   . ASP H  1 4   ? 7.446   -15.584 19.379  1.00 48.73  ? -4  ASP H O   1 
ATOM   11732 C CB  . ASP H  1 4   ? 6.565   -17.988 20.522  1.00 53.41  ? -4  ASP H CB  1 
ATOM   11733 C CG  . ASP H  1 4   ? 5.406   -17.123 21.032  1.00 67.50  ? -4  ASP H CG  1 
ATOM   11734 O OD1 . ASP H  1 4   ? 4.739   -16.466 20.201  1.00 56.55  ? -4  ASP H OD1 1 
ATOM   11735 O OD2 . ASP H  1 4   ? 5.151   -17.106 22.262  1.00 71.93  ? -4  ASP H OD2 1 
ATOM   11736 N N   . ASP H  1 5   ? 8.308   -16.603 17.564  1.00 47.30  ? -3  ASP H N   1 
ATOM   11737 C CA  . ASP H  1 5   ? 9.064   -15.409 17.171  1.00 45.07  ? -3  ASP H CA  1 
ATOM   11738 C C   . ASP H  1 5   ? 8.291   -14.398 16.304  1.00 37.45  ? -3  ASP H C   1 
ATOM   11739 O O   . ASP H  1 5   ? 8.839   -13.399 15.868  1.00 35.59  ? -3  ASP H O   1 
ATOM   11740 C CB  . ASP H  1 5   ? 10.502  -15.728 16.662  1.00 48.70  ? -3  ASP H CB  1 
ATOM   11741 C CG  . ASP H  1 5   ? 10.583  -16.077 15.167  1.00 56.63  ? -3  ASP H CG  1 
ATOM   11742 O OD1 . ASP H  1 5   ? 9.617   -15.853 14.404  1.00 55.98  ? -3  ASP H OD1 1 
ATOM   11743 O OD2 . ASP H  1 5   ? 11.659  -16.570 14.749  1.00 54.62  ? -3  ASP H OD2 1 
ATOM   11744 N N   . ASP H  1 6   ? 7.010   -14.655 16.081  1.00 45.44  ? -2  ASP H N   1 
ATOM   11745 C CA  . ASP H  1 6   ? 6.144   -13.678 15.422  1.00 44.03  ? -2  ASP H CA  1 
ATOM   11746 C C   . ASP H  1 6   ? 5.100   -13.079 16.402  1.00 44.82  ? -2  ASP H C   1 
ATOM   11747 O O   . ASP H  1 6   ? 4.082   -12.514 15.989  1.00 41.95  ? -2  ASP H O   1 
ATOM   11748 C CB  . ASP H  1 6   ? 5.461   -14.293 14.189  1.00 43.99  ? -2  ASP H CB  1 
ATOM   11749 C CG  . ASP H  1 6   ? 6.329   -14.246 12.934  1.00 42.57  ? -2  ASP H CG  1 
ATOM   11750 O OD1 . ASP H  1 6   ? 5.797   -13.902 11.853  1.00 37.58  ? -2  ASP H OD1 1 
ATOM   11751 O OD2 . ASP H  1 6   ? 7.533   -14.565 13.022  1.00 43.01  ? -2  ASP H OD2 1 
ATOM   11752 N N   . ASP H  1 7   ? 5.354   -13.205 17.700  1.00 39.16  ? -1  ASP H N   1 
ATOM   11753 C CA  . ASP H  1 7   ? 4.511   -12.553 18.697  1.00 39.39  ? -1  ASP H CA  1 
ATOM   11754 C C   . ASP H  1 7   ? 4.908   -11.080 18.807  1.00 32.67  ? -1  ASP H C   1 
ATOM   11755 O O   . ASP H  1 7   ? 5.966   -10.758 19.362  1.00 31.74  ? -1  ASP H O   1 
ATOM   11756 C CB  . ASP H  1 7   ? 4.655   -13.241 20.059  1.00 39.93  ? -1  ASP H CB  1 
ATOM   11757 C CG  . ASP H  1 7   ? 3.487   -12.952 20.984  1.00 48.39  ? -1  ASP H CG  1 
ATOM   11758 O OD1 . ASP H  1 7   ? 3.449   -11.846 21.579  1.00 44.03  ? -1  ASP H OD1 1 
ATOM   11759 O OD2 . ASP H  1 7   ? 2.610   -13.838 21.120  1.00 53.82  ? -1  ASP H OD2 1 
ATOM   11760 N N   . LYS H  1 8   ? 4.071   -10.188 18.280  1.00 27.41  ? 0   LYS H N   1 
ATOM   11761 C CA  . LYS H  1 8   ? 4.401   -8.762  18.262  1.00 26.24  ? 0   LYS H CA  1 
ATOM   11762 C C   . LYS H  1 8   ? 4.693   -8.199  19.664  1.00 25.92  ? 0   LYS H C   1 
ATOM   11763 O O   . LYS H  1 8   ? 5.662   -7.451  19.857  1.00 19.73  ? 0   LYS H O   1 
ATOM   11764 C CB  . LYS H  1 8   ? 3.311   -7.950  17.558  1.00 17.89  ? 0   LYS H CB  1 
ATOM   11765 C CG  . LYS H  1 8   ? 3.713   -6.517  17.273  1.00 14.03  ? 0   LYS H CG  1 
ATOM   11766 C CD  . LYS H  1 8   ? 2.602   -5.752  16.569  1.00 14.77  ? 0   LYS H CD  1 
ATOM   11767 C CE  . LYS H  1 8   ? 3.057   -4.365  16.155  1.00 13.16  ? 0   LYS H CE  1 
ATOM   11768 N NZ  . LYS H  1 8   ? 1.951   -3.360  16.290  1.00 27.81  ? 0   LYS H NZ  1 
ATOM   11769 N N   . LEU H  1 9   ? 3.864   -8.582  20.636  1.00 24.75  ? 1   LEU H N   1 
ATOM   11770 C CA  . LEU H  1 9   ? 4.022   -8.125  22.010  1.00 22.90  ? 1   LEU H CA  1 
ATOM   11771 C C   . LEU H  1 9   ? 5.338   -8.614  22.625  1.00 24.53  ? 1   LEU H C   1 
ATOM   11772 O O   . LEU H  1 9   ? 6.053   -7.857  23.304  1.00 19.26  ? 1   LEU H O   1 
ATOM   11773 C CB  . LEU H  1 9   ? 2.839   -8.582  22.863  1.00 30.35  ? 1   LEU H CB  1 
ATOM   11774 C CG  . LEU H  1 9   ? 2.936   -8.140  24.325  1.00 22.82  ? 1   LEU H CG  1 
ATOM   11775 C CD1 . LEU H  1 9   ? 2.868   -6.625  24.374  1.00 18.35  ? 1   LEU H CD1 1 
ATOM   11776 C CD2 . LEU H  1 9   ? 1.859   -8.794  25.174  1.00 20.25  ? 1   LEU H CD2 1 
ATOM   11777 N N   . ASP H  1 10  ? 5.656   -9.881  22.393  1.00 26.09  ? 2   ASP H N   1 
ATOM   11778 C CA  . ASP H  1 10  ? 6.939   -10.402 22.839  1.00 28.10  ? 2   ASP H CA  1 
ATOM   11779 C C   . ASP H  1 10  ? 8.086   -9.632  22.184  1.00 27.24  ? 2   ASP H C   1 
ATOM   11780 O O   . ASP H  1 10  ? 9.113   -9.375  22.821  1.00 26.21  ? 2   ASP H O   1 
ATOM   11781 C CB  . ASP H  1 10  ? 7.058   -11.907 22.579  1.00 33.71  ? 2   ASP H CB  1 
ATOM   11782 C CG  . ASP H  1 10  ? 6.250   -12.739 23.571  1.00 46.33  ? 2   ASP H CG  1 
ATOM   11783 O OD1 . ASP H  1 10  ? 5.765   -12.165 24.575  1.00 47.03  ? 2   ASP H OD1 1 
ATOM   11784 O OD2 . ASP H  1 10  ? 6.109   -13.968 23.355  1.00 51.22  ? 2   ASP H OD2 1 
ATOM   11785 N N   . ARG H  1 11  ? 7.913   -9.231  20.927  1.00 21.57  ? 3   ARG H N   1 
ATOM   11786 C CA  . ARG H  1 11  ? 8.987   -8.491  20.283  1.00 20.71  ? 3   ARG H CA  1 
ATOM   11787 C C   . ARG H  1 11  ? 9.170   -7.128  20.945  1.00 16.13  ? 3   ARG H C   1 
ATOM   11788 O O   . ARG H  1 11  ? 10.278  -6.783  21.339  1.00 16.23  ? 3   ARG H O   1 
ATOM   11789 C CB  . ARG H  1 11  ? 8.784   -8.372  18.760  1.00 22.50  ? 3   ARG H CB  1 
ATOM   11790 C CG  . ARG H  1 11  ? 8.818   -9.702  18.029  1.00 21.07  ? 3   ARG H CG  1 
ATOM   11791 C CD  . ARG H  1 11  ? 8.670   -9.546  16.513  1.00 27.42  ? 3   ARG H CD  1 
ATOM   11792 N NE  . ARG H  1 11  ? 9.950   -9.234  15.886  1.00 22.54  ? 3   ARG H NE  1 
ATOM   11793 C CZ  . ARG H  1 11  ? 10.852  -10.145 15.544  1.00 22.69  ? 3   ARG H CZ  1 
ATOM   11794 N NH1 . ARG H  1 11  ? 10.619  -11.433 15.749  1.00 20.16  ? 3   ARG H NH1 1 
ATOM   11795 N NH2 . ARG H  1 11  ? 11.995  -9.763  15.004  1.00 29.19  ? 3   ARG H NH2 1 
ATOM   11796 N N   . ALA H  1 12  ? 8.081   -6.375  21.091  1.00 17.41  ? 4   ALA H N   1 
ATOM   11797 C CA  . ALA H  1 12  ? 8.135   -5.033  21.677  1.00 16.00  ? 4   ALA H CA  1 
ATOM   11798 C C   . ALA H  1 12  ? 8.732   -5.026  23.092  1.00 15.81  ? 4   ALA H C   1 
ATOM   11799 O O   . ALA H  1 12  ? 9.475   -4.104  23.452  1.00 11.14  ? 4   ALA H O   1 
ATOM   11800 C CB  . ALA H  1 12  ? 6.757   -4.394  21.668  1.00 14.23  ? 4   ALA H CB  1 
ATOM   11801 N N   . ASP H  1 13  ? 8.412   -6.056  23.879  1.00 15.36  ? 5   ASP H N   1 
ATOM   11802 C CA  . ASP H  1 13  ? 8.973   -6.199  25.222  1.00 16.70  ? 5   ASP H CA  1 
ATOM   11803 C C   . ASP H  1 13  ? 10.489  -6.405  25.174  1.00 18.64  ? 5   ASP H C   1 
ATOM   11804 O O   . ASP H  1 13  ? 11.209  -5.937  26.059  1.00 20.58  ? 5   ASP H O   1 
ATOM   11805 C CB  . ASP H  1 13  ? 8.334   -7.371  25.991  1.00 17.52  ? 5   ASP H CB  1 
ATOM   11806 C CG  . ASP H  1 13  ? 6.919   -7.076  26.475  1.00 24.83  ? 5   ASP H CG  1 
ATOM   11807 O OD1 . ASP H  1 13  ? 6.610   -5.919  26.854  1.00 23.55  ? 5   ASP H OD1 1 
ATOM   11808 O OD2 . ASP H  1 13  ? 6.106   -8.026  26.492  1.00 33.61  ? 5   ASP H OD2 1 
ATOM   11809 N N   . ILE H  1 14  ? 10.971  -7.136  24.170  1.00 14.88  ? 6   ILE H N   1 
ATOM   11810 C CA  . ILE H  1 14  ? 12.404  -7.350  24.028  1.00 16.74  ? 6   ILE H CA  1 
ATOM   11811 C C   . ILE H  1 14  ? 13.075  -6.028  23.678  1.00 15.83  ? 6   ILE H C   1 
ATOM   11812 O O   . ILE H  1 14  ? 14.061  -5.631  24.312  1.00 15.23  ? 6   ILE H O   1 
ATOM   11813 C CB  . ILE H  1 14  ? 12.736  -8.443  22.962  1.00 21.16  ? 6   ILE H CB  1 
ATOM   11814 C CG1 . ILE H  1 14  ? 12.350  -9.819  23.502  1.00 15.76  ? 6   ILE H CG1 1 
ATOM   11815 C CG2 . ILE H  1 14  ? 14.225  -8.436  22.596  1.00 12.68  ? 6   ILE H CG2 1 
ATOM   11816 C CD1 . ILE H  1 14  ? 12.476  -10.933 22.536  1.00 19.31  ? 6   ILE H CD1 1 
ATOM   11817 N N   . LEU H  1 15  ? 12.523  -5.344  22.683  1.00 12.40  ? 7   LEU H N   1 
ATOM   11818 C CA  . LEU H  1 15  ? 13.008  -4.019  22.310  1.00 15.07  ? 7   LEU H CA  1 
ATOM   11819 C C   . LEU H  1 15  ? 13.108  -3.103  23.519  1.00 14.97  ? 7   LEU H C   1 
ATOM   11820 O O   . LEU H  1 15  ? 14.125  -2.429  23.710  1.00 14.28  ? 7   LEU H O   1 
ATOM   11821 C CB  . LEU H  1 15  ? 12.101  -3.380  21.268  1.00 12.65  ? 7   LEU H CB  1 
ATOM   11822 C CG  . LEU H  1 15  ? 12.811  -2.349  20.408  1.00 17.55  ? 7   LEU H CG  1 
ATOM   11823 C CD1 . LEU H  1 15  ? 14.053  -2.998  19.877  1.00 18.11  ? 7   LEU H CD1 1 
ATOM   11824 C CD2 . LEU H  1 15  ? 11.931  -1.876  19.252  1.00 19.56  ? 7   LEU H CD2 1 
ATOM   11825 N N   . TYR H  1 16  ? 12.050  -3.093  24.331  1.00 14.31  ? 8   TYR H N   1 
ATOM   11826 C CA  . TYR H  1 16  ? 11.998  -2.290  25.547  1.00 11.69  ? 8   TYR H CA  1 
ATOM   11827 C C   . TYR H  1 16  ? 13.116  -2.677  26.502  1.00 13.71  ? 8   TYR H C   1 
ATOM   11828 O O   . TYR H  1 16  ? 13.886  -1.829  26.944  1.00 13.20  ? 8   TYR H O   1 
ATOM   11829 C CB  . TYR H  1 16  ? 10.645  -2.477  26.219  1.00 14.60  ? 8   TYR H CB  1 
ATOM   11830 C CG  . TYR H  1 16  ? 10.558  -2.009  27.653  1.00 13.00  ? 8   TYR H CG  1 
ATOM   11831 C CD1 . TYR H  1 16  ? 10.497  -0.654  27.963  1.00 14.79  ? 8   TYR H CD1 1 
ATOM   11832 C CD2 . TYR H  1 16  ? 10.505  -2.925  28.696  1.00 13.68  ? 8   TYR H CD2 1 
ATOM   11833 C CE1 . TYR H  1 16  ? 10.396  -0.216  29.290  1.00 17.29  ? 8   TYR H CE1 1 
ATOM   11834 C CE2 . TYR H  1 16  ? 10.396  -2.504  30.015  1.00 18.77  ? 8   TYR H CE2 1 
ATOM   11835 C CZ  . TYR H  1 16  ? 10.341  -1.147  30.311  1.00 17.92  ? 8   TYR H CZ  1 
ATOM   11836 O OH  . TYR H  1 16  ? 10.245  -0.738  31.626  1.00 15.34  ? 8   TYR H OH  1 
ATOM   11837 N N   . ASN H  1 17  ? 13.208  -3.967  26.805  1.00 13.41  ? 9   ASN H N   1 
ATOM   11838 C CA  . ASN H  1 17  ? 14.282  -4.469  27.641  1.00 12.96  ? 9   ASN H CA  1 
ATOM   11839 C C   . ASN H  1 17  ? 15.664  -4.116  27.120  1.00 18.16  ? 9   ASN H C   1 
ATOM   11840 O O   . ASN H  1 17  ? 16.497  -3.616  27.886  1.00 18.65  ? 9   ASN H O   1 
ATOM   11841 C CB  . ASN H  1 17  ? 14.158  -5.972  27.840  1.00 15.42  ? 9   ASN H CB  1 
ATOM   11842 C CG  . ASN H  1 17  ? 12.882  -6.354  28.547  1.00 18.55  ? 9   ASN H CG  1 
ATOM   11843 O OD1 . ASN H  1 17  ? 12.313  -7.409  28.278  1.00 21.05  ? 9   ASN H OD1 1 
ATOM   11844 N ND2 . ASN H  1 17  ? 12.416  -5.492  29.458  1.00 20.43  ? 9   ASN H ND2 1 
ATOM   11845 N N   . ILE H  1 18  ? 15.910  -4.359  25.828  1.00 15.41  ? 10  ILE H N   1 
ATOM   11846 C CA  . ILE H  1 18  ? 17.196  -3.991  25.243  1.00 15.36  ? 10  ILE H CA  1 
ATOM   11847 C C   . ILE H  1 18  ? 17.421  -2.496  25.433  1.00 15.62  ? 10  ILE H C   1 
ATOM   11848 O O   . ILE H  1 18  ? 18.511  -2.060  25.758  1.00 19.64  ? 10  ILE H O   1 
ATOM   11849 C CB  . ILE H  1 18  ? 17.319  -4.342  23.730  1.00 21.76  ? 10  ILE H CB  1 
ATOM   11850 C CG1 . ILE H  1 18  ? 17.193  -5.845  23.474  1.00 17.78  ? 10  ILE H CG1 1 
ATOM   11851 C CG2 . ILE H  1 18  ? 18.662  -3.874  23.164  1.00 19.00  ? 10  ILE H CG2 1 
ATOM   11852 C CD1 . ILE H  1 18  ? 17.247  -6.177  21.997  1.00 14.78  ? 10  ILE H CD1 1 
ATOM   11853 N N   . ARG H  1 19  ? 16.374  -1.708  25.261  1.00 16.49  ? 11  ARG H N   1 
ATOM   11854 C CA  . ARG H  1 19  ? 16.537  -0.266  25.309  1.00 14.25  ? 11  ARG H CA  1 
ATOM   11855 C C   . ARG H  1 19  ? 16.812  0.219   26.742  1.00 15.54  ? 11  ARG H C   1 
ATOM   11856 O O   . ARG H  1 19  ? 17.498  1.226   26.946  1.00 16.73  ? 11  ARG H O   1 
ATOM   11857 C CB  . ARG H  1 19  ? 15.336  0.424   24.643  1.00 12.93  ? 11  ARG H CB  1 
ATOM   11858 C CG  . ARG H  1 19  ? 15.708  1.356   23.497  1.00 17.98  ? 11  ARG H CG  1 
ATOM   11859 C CD  . ARG H  1 19  ? 15.157  0.934   22.132  1.00 19.25  ? 11  ARG H CD  1 
ATOM   11860 N NE  . ARG H  1 19  ? 13.812  1.437   21.850  1.00 22.00  ? 11  ARG H NE  1 
ATOM   11861 C CZ  . ARG H  1 19  ? 13.357  1.805   20.645  1.00 30.11  ? 11  ARG H CZ  1 
ATOM   11862 N NH1 . ARG H  1 19  ? 14.136  1.757   19.561  1.00 19.49  ? 11  ARG H NH1 1 
ATOM   11863 N NH2 . ARG H  1 19  ? 12.102  2.237   20.523  1.00 32.30  ? 11  ARG H NH2 1 
ATOM   11864 N N   . GLN H  1 20  ? 16.323  -0.525  27.734  1.00 17.61  ? 12  GLN H N   1 
ATOM   11865 C CA  . GLN H  1 20  ? 16.622  -0.220  29.146  1.00 19.67  ? 12  GLN H CA  1 
ATOM   11866 C C   . GLN H  1 20  ? 18.053  -0.606  29.577  1.00 19.25  ? 12  GLN H C   1 
ATOM   11867 O O   . GLN H  1 20  ? 18.751  0.186   30.191  1.00 26.68  ? 12  GLN H O   1 
ATOM   11868 C CB  . GLN H  1 20  ? 15.598  -0.868  30.087  1.00 19.10  ? 12  GLN H CB  1 
ATOM   11869 C CG  . GLN H  1 20  ? 14.181  -0.314  29.991  1.00 16.47  ? 12  GLN H CG  1 
ATOM   11870 C CD  . GLN H  1 20  ? 13.904  0.743   31.039  1.00 29.70  ? 12  GLN H CD  1 
ATOM   11871 O OE1 . GLN H  1 20  ? 13.418  0.434   32.133  1.00 30.36  ? 12  GLN H OE1 1 
ATOM   11872 N NE2 . GLN H  1 20  ? 14.210  2.005   30.713  1.00 27.11  ? 12  GLN H NE2 1 
ATOM   11873 N N   . THR H  1 21  ? 18.495  -1.812  29.247  1.00 19.16  ? 13  THR H N   1 
ATOM   11874 C CA  . THR H  1 21  ? 19.826  -2.267  29.651  1.00 19.88  ? 13  THR H CA  1 
ATOM   11875 C C   . THR H  1 21  ? 20.975  -1.599  28.886  1.00 18.19  ? 13  THR H C   1 
ATOM   11876 O O   . THR H  1 21  ? 22.019  -1.296  29.440  1.00 21.32  ? 13  THR H O   1 
ATOM   11877 C CB  . THR H  1 21  ? 19.959  -3.779  29.457  1.00 20.49  ? 13  THR H CB  1 
ATOM   11878 O OG1 . THR H  1 21  ? 18.829  -4.434  30.044  1.00 17.85  ? 13  THR H OG1 1 
ATOM   11879 C CG2 . THR H  1 21  ? 21.225  -4.280  30.101  1.00 20.68  ? 13  THR H CG2 1 
ATOM   11880 N N   . SER H  1 22  ? 20.773  -1.361  27.606  1.00 16.02  ? 14  SER H N   1 
ATOM   11881 C CA  . SER H  1 22  ? 21.860  -0.956  26.740  1.00 15.22  ? 14  SER H CA  1 
ATOM   11882 C C   . SER H  1 22  ? 22.342  0.466   26.985  1.00 19.48  ? 14  SER H C   1 
ATOM   11883 O O   . SER H  1 22  ? 21.536  1.383   27.122  1.00 23.70  ? 14  SER H O   1 
ATOM   11884 C CB  . SER H  1 22  ? 21.426  -1.127  25.283  1.00 17.51  ? 14  SER H CB  1 
ATOM   11885 O OG  . SER H  1 22  ? 21.686  0.041   24.522  1.00 25.99  ? 14  SER H OG  1 
ATOM   11886 N N   . ARG H  1 23  ? 23.659  0.647   27.039  1.00 19.46  ? 15  ARG H N   1 
ATOM   11887 C CA  . ARG H  1 23  ? 24.248  1.983   27.044  1.00 19.08  ? 15  ARG H CA  1 
ATOM   11888 C C   . ARG H  1 23  ? 24.966  2.227   25.723  1.00 20.28  ? 15  ARG H C   1 
ATOM   11889 O O   . ARG H  1 23  ? 26.088  1.751   25.524  1.00 18.30  ? 15  ARG H O   1 
ATOM   11890 C CB  . ARG H  1 23  ? 25.263  2.135   28.170  1.00 17.37  ? 15  ARG H CB  1 
ATOM   11891 C CG  . ARG H  1 23  ? 24.946  1.366   29.407  1.00 22.17  ? 15  ARG H CG  1 
ATOM   11892 C CD  . ARG H  1 23  ? 25.544  2.072   30.615  1.00 28.41  ? 15  ARG H CD  1 
ATOM   11893 N NE  . ARG H  1 23  ? 25.475  1.246   31.813  1.00 27.54  ? 15  ARG H NE  1 
ATOM   11894 C CZ  . ARG H  1 23  ? 25.072  1.679   33.001  1.00 26.97  ? 15  ARG H CZ  1 
ATOM   11895 N NH1 . ARG H  1 23  ? 24.696  2.947   33.164  1.00 22.66  ? 15  ARG H NH1 1 
ATOM   11896 N NH2 . ARG H  1 23  ? 25.055  0.835   34.025  1.00 21.99  ? 15  ARG H NH2 1 
ATOM   11897 N N   . PRO H  1 24  ? 24.344  3.004   24.827  1.00 23.00  ? 16  PRO H N   1 
ATOM   11898 C CA  . PRO H  1 24  ? 24.867  3.204   23.469  1.00 23.08  ? 16  PRO H CA  1 
ATOM   11899 C C   . PRO H  1 24  ? 26.266  3.804   23.416  1.00 18.55  ? 16  PRO H C   1 
ATOM   11900 O O   . PRO H  1 24  ? 26.881  3.725   22.366  1.00 30.07  ? 16  PRO H O   1 
ATOM   11901 C CB  . PRO H  1 24  ? 23.880  4.204   22.854  1.00 21.47  ? 16  PRO H CB  1 
ATOM   11902 C CG  . PRO H  1 24  ? 22.684  4.141   23.696  1.00 18.03  ? 16  PRO H CG  1 
ATOM   11903 C CD  . PRO H  1 24  ? 23.163  3.840   25.079  1.00 16.52  ? 16  PRO H CD  1 
ATOM   11904 N N   . ASP H  1 25  ? 26.757  4.386   24.503  1.00 16.66  ? 17  ASP H N   1 
ATOM   11905 C CA  . ASP H  1 25  ? 28.009  5.132   24.453  1.00 16.00  ? 17  ASP H CA  1 
ATOM   11906 C C   . ASP H  1 25  ? 29.168  4.533   25.252  1.00 20.69  ? 17  ASP H C   1 
ATOM   11907 O O   . ASP H  1 25  ? 30.306  5.001   25.143  1.00 20.57  ? 17  ASP H O   1 
ATOM   11908 C CB  . ASP H  1 25  ? 27.779  6.580   24.870  1.00 16.75  ? 17  ASP H CB  1 
ATOM   11909 C CG  . ASP H  1 25  ? 26.891  7.321   23.903  1.00 23.40  ? 17  ASP H CG  1 
ATOM   11910 O OD1 . ASP H  1 25  ? 26.650  6.785   22.803  1.00 26.46  ? 17  ASP H OD1 1 
ATOM   11911 O OD2 . ASP H  1 25  ? 26.438  8.440   24.225  1.00 24.64  ? 17  ASP H OD2 1 
ATOM   11912 N N   . VAL H  1 26  ? 28.900  3.511   26.057  1.00 16.14  ? 18  VAL H N   1 
ATOM   11913 C CA  . VAL H  1 26  ? 30.000  2.831   26.718  1.00 18.10  ? 18  VAL H CA  1 
ATOM   11914 C C   . VAL H  1 26  ? 30.231  1.416   26.180  1.00 18.86  ? 18  VAL H C   1 
ATOM   11915 O O   . VAL H  1 26  ? 29.282  0.665   25.964  1.00 20.61  ? 18  VAL H O   1 
ATOM   11916 C CB  . VAL H  1 26  ? 29.880  2.885   28.269  1.00 18.47  ? 18  VAL H CB  1 
ATOM   11917 C CG1 . VAL H  1 26  ? 28.618  3.615   28.683  1.00 21.36  ? 18  VAL H CG1 1 
ATOM   11918 C CG2 . VAL H  1 26  ? 29.983  1.501   28.898  1.00 15.34  ? 18  VAL H CG2 1 
ATOM   11919 N N   . ILE H  1 27  ? 31.499  1.077   25.941  1.00 18.05  ? 19  ILE H N   1 
ATOM   11920 C CA  . ILE H  1 27  ? 31.874  -0.246  25.446  1.00 18.85  ? 19  ILE H CA  1 
ATOM   11921 C C   . ILE H  1 27  ? 31.423  -1.400  26.361  1.00 18.25  ? 19  ILE H C   1 
ATOM   11922 O O   . ILE H  1 27  ? 31.657  -1.380  27.558  1.00 18.13  ? 19  ILE H O   1 
ATOM   11923 C CB  . ILE H  1 27  ? 33.403  -0.358  25.187  1.00 19.37  ? 19  ILE H CB  1 
ATOM   11924 C CG1 . ILE H  1 27  ? 34.203  -0.120  26.466  1.00 24.67  ? 19  ILE H CG1 1 
ATOM   11925 C CG2 . ILE H  1 27  ? 33.850  0.610   24.110  1.00 19.62  ? 19  ILE H CG2 1 
ATOM   11926 C CD1 . ILE H  1 27  ? 35.695  -0.311  26.284  1.00 19.76  ? 19  ILE H CD1 1 
ATOM   11927 N N   . PRO H  1 28  ? 30.780  -2.420  25.777  1.00 18.64  ? 20  PRO H N   1 
ATOM   11928 C CA  . PRO H  1 28  ? 30.247  -3.571  26.507  1.00 20.24  ? 20  PRO H CA  1 
ATOM   11929 C C   . PRO H  1 28  ? 31.316  -4.562  26.924  1.00 23.28  ? 20  PRO H C   1 
ATOM   11930 O O   . PRO H  1 28  ? 31.234  -5.727  26.548  1.00 26.35  ? 20  PRO H O   1 
ATOM   11931 C CB  . PRO H  1 28  ? 29.315  -4.224  25.486  1.00 20.56  ? 20  PRO H CB  1 
ATOM   11932 C CG  . PRO H  1 28  ? 29.892  -3.854  24.167  1.00 18.99  ? 20  PRO H CG  1 
ATOM   11933 C CD  . PRO H  1 28  ? 30.462  -2.484  24.339  1.00 21.12  ? 20  PRO H CD  1 
ATOM   11934 N N   . THR H  1 29  ? 32.299  -4.100  27.688  1.00 24.31  ? 21  THR H N   1 
ATOM   11935 C CA  . THR H  1 29  ? 33.333  -4.980  28.210  1.00 27.58  ? 21  THR H CA  1 
ATOM   11936 C C   . THR H  1 29  ? 32.741  -5.963  29.214  1.00 39.26  ? 21  THR H C   1 
ATOM   11937 O O   . THR H  1 29  ? 31.875  -5.606  30.014  1.00 41.35  ? 21  THR H O   1 
ATOM   11938 C CB  . THR H  1 29  ? 34.463  -4.184  28.888  1.00 32.91  ? 21  THR H CB  1 
ATOM   11939 O OG1 . THR H  1 29  ? 33.902  -3.246  29.815  1.00 29.61  ? 21  THR H OG1 1 
ATOM   11940 C CG2 . THR H  1 29  ? 35.284  -3.435  27.850  1.00 26.99  ? 21  THR H CG2 1 
ATOM   11941 N N   . GLN H  1 30  ? 32.984  -7.251  28.989  1.00 47.24  ? 22  GLN H N   1 
ATOM   11942 C CA  . GLN H  1 30  ? 32.151  -8.282  29.619  1.00 46.28  ? 22  GLN H CA  1 
ATOM   11943 C C   . GLN H  1 30  ? 32.736  -8.847  30.898  1.00 53.99  ? 22  GLN H C   1 
ATOM   11944 O O   . GLN H  1 30  ? 32.061  -8.948  31.922  1.00 53.60  ? 22  GLN H O   1 
ATOM   11945 C CB  . GLN H  1 30  ? 31.872  -9.416  28.629  1.00 50.81  ? 22  GLN H CB  1 
ATOM   11946 C CG  . GLN H  1 30  ? 30.405  -9.572  28.261  1.00 59.55  ? 22  GLN H CG  1 
ATOM   11947 C CD  . GLN H  1 30  ? 29.841  -8.341  27.580  1.00 56.39  ? 22  GLN H CD  1 
ATOM   11948 O OE1 . GLN H  1 30  ? 29.832  -7.251  28.151  1.00 56.19  ? 22  GLN H OE1 1 
ATOM   11949 N NE2 . GLN H  1 30  ? 29.367  -8.509  26.351  1.00 39.71  ? 22  GLN H NE2 1 
ATOM   11950 N N   . ARG H  1 31  ? 33.987  -9.290  30.847  1.00 61.60  ? 23  ARG H N   1 
ATOM   11951 C CA  . ARG H  1 31  ? 34.619  -9.826  32.050  1.00 61.87  ? 23  ARG H CA  1 
ATOM   11952 C C   . ARG H  1 31  ? 36.020  -9.269  32.262  1.00 65.32  ? 23  ARG H C   1 
ATOM   11953 O O   . ARG H  1 31  ? 37.007  -9.998  32.169  1.00 62.27  ? 23  ARG H O   1 
ATOM   11954 C CB  . ARG H  1 31  ? 34.667  -11.355 31.992  1.00 62.84  ? 23  ARG H CB  1 
ATOM   11955 C CG  . ARG H  1 31  ? 33.566  -12.041 32.784  1.00 56.13  ? 23  ARG H CG  1 
ATOM   11956 C CD  . ARG H  1 31  ? 33.402  -11.415 34.159  1.00 58.52  ? 23  ARG H CD  1 
ATOM   11957 N NE  . ARG H  1 31  ? 32.835  -12.353 35.124  1.00 68.76  ? 23  ARG H NE  1 
ATOM   11958 C CZ  . ARG H  1 31  ? 31.893  -12.038 36.007  1.00 60.80  ? 23  ARG H CZ  1 
ATOM   11959 N NH1 . ARG H  1 31  ? 31.408  -10.804 36.051  1.00 58.78  ? 23  ARG H NH1 1 
ATOM   11960 N NH2 . ARG H  1 31  ? 31.435  -12.956 36.847  1.00 58.15  ? 23  ARG H NH2 1 
ATOM   11961 N N   . ASP H  1 32  ? 36.102  -7.971  32.530  1.00 62.85  ? 24  ASP H N   1 
ATOM   11962 C CA  . ASP H  1 32  ? 37.388  -7.338  32.764  1.00 55.81  ? 24  ASP H CA  1 
ATOM   11963 C C   . ASP H  1 32  ? 38.243  -7.640  31.550  1.00 54.67  ? 24  ASP H C   1 
ATOM   11964 O O   . ASP H  1 32  ? 39.445  -7.880  31.659  1.00 57.71  ? 24  ASP H O   1 
ATOM   11965 C CB  . ASP H  1 32  ? 38.043  -7.894  34.028  1.00 63.58  ? 24  ASP H CB  1 
ATOM   11966 C CG  . ASP H  1 32  ? 38.565  -6.802  34.942  1.00 68.28  ? 24  ASP H CG  1 
ATOM   11967 O OD1 . ASP H  1 32  ? 39.590  -6.176  34.597  1.00 59.80  ? 24  ASP H OD1 1 
ATOM   11968 O OD2 . ASP H  1 32  ? 37.952  -6.570  36.004  1.00 62.36  ? 24  ASP H OD2 1 
ATOM   11969 N N   . ARG H  1 33  ? 37.602  -7.633  30.387  1.00 51.61  ? 25  ARG H N   1 
ATOM   11970 C CA  . ARG H  1 33  ? 38.267  -8.005  29.147  1.00 47.80  ? 25  ARG H CA  1 
ATOM   11971 C C   . ARG H  1 33  ? 37.797  -7.155  27.976  1.00 44.07  ? 25  ARG H C   1 
ATOM   11972 O O   . ARG H  1 33  ? 36.696  -6.605  27.992  1.00 41.15  ? 25  ARG H O   1 
ATOM   11973 C CB  . ARG H  1 33  ? 38.040  -9.488  28.843  1.00 45.57  ? 25  ARG H CB  1 
ATOM   11974 C CG  . ARG H  1 33  ? 39.151  -10.400 29.337  1.00 55.87  ? 25  ARG H CG  1 
ATOM   11975 C CD  . ARG H  1 33  ? 38.603  -11.509 30.219  1.00 69.35  ? 25  ARG H CD  1 
ATOM   11976 N NE  . ARG H  1 33  ? 39.663  -12.212 30.936  1.00 85.22  ? 25  ARG H NE  1 
ATOM   11977 C CZ  . ARG H  1 33  ? 39.471  -13.299 31.676  1.00 75.47  ? 25  ARG H CZ  1 
ATOM   11978 N NH1 . ARG H  1 33  ? 38.255  -13.813 31.800  1.00 73.96  ? 25  ARG H NH1 1 
ATOM   11979 N NH2 . ARG H  1 33  ? 40.494  -13.873 32.294  1.00 55.39  ? 25  ARG H NH2 1 
ATOM   11980 N N   . PRO H  1 34  ? 38.643  -7.058  26.959  1.00 43.16  ? 26  PRO H N   1 
ATOM   11981 C CA  . PRO H  1 34  ? 38.314  -6.301  25.739  1.00 38.24  ? 26  PRO H CA  1 
ATOM   11982 C C   . PRO H  1 34  ? 37.059  -6.794  25.039  1.00 31.15  ? 26  PRO H C   1 
ATOM   11983 O O   . PRO H  1 34  ? 36.677  -7.944  25.226  1.00 38.78  ? 26  PRO H O   1 
ATOM   11984 C CB  . PRO H  1 34  ? 39.517  -6.572  24.830  1.00 32.68  ? 26  PRO H CB  1 
ATOM   11985 C CG  . PRO H  1 34  ? 40.629  -6.815  25.757  1.00 31.81  ? 26  PRO H CG  1 
ATOM   11986 C CD  . PRO H  1 34  ? 40.040  -7.531  26.937  1.00 38.49  ? 26  PRO H CD  1 
ATOM   11987 N N   . VAL H  1 35  ? 36.425  -5.940  24.244  1.00 29.61  ? 27  VAL H N   1 
ATOM   11988 C CA  . VAL H  1 35  ? 35.321  -6.400  23.411  1.00 28.71  ? 27  VAL H CA  1 
ATOM   11989 C C   . VAL H  1 35  ? 35.887  -7.077  22.172  1.00 33.75  ? 27  VAL H C   1 
ATOM   11990 O O   . VAL H  1 35  ? 36.721  -6.509  21.465  1.00 29.18  ? 27  VAL H O   1 
ATOM   11991 C CB  . VAL H  1 35  ? 34.413  -5.257  22.953  1.00 27.38  ? 27  VAL H CB  1 
ATOM   11992 C CG1 . VAL H  1 35  ? 33.154  -5.827  22.307  1.00 25.83  ? 27  VAL H CG1 1 
ATOM   11993 C CG2 . VAL H  1 35  ? 34.052  -4.363  24.126  1.00 29.77  ? 27  VAL H CG2 1 
ATOM   11994 N N   . ALA H  1 36  ? 35.436  -8.296  21.915  1.00 35.63  ? 28  ALA H N   1 
ATOM   11995 C CA  . ALA H  1 36  ? 35.888  -9.029  20.750  1.00 25.53  ? 28  ALA H CA  1 
ATOM   11996 C C   . ALA H  1 36  ? 34.969  -8.746  19.577  1.00 25.74  ? 28  ALA H C   1 
ATOM   11997 O O   . ALA H  1 36  ? 34.012  -9.481  19.350  1.00 30.95  ? 28  ALA H O   1 
ATOM   11998 C CB  . ALA H  1 36  ? 35.921  -10.516 21.045  1.00 25.47  ? 28  ALA H CB  1 
ATOM   11999 N N   . VAL H  1 37  ? 35.257  -7.669  18.848  1.00 28.21  ? 29  VAL H N   1 
ATOM   12000 C CA  . VAL H  1 37  ? 34.598  -7.379  17.570  1.00 26.86  ? 29  VAL H CA  1 
ATOM   12001 C C   . VAL H  1 37  ? 35.176  -8.246  16.458  1.00 33.48  ? 29  VAL H C   1 
ATOM   12002 O O   . VAL H  1 37  ? 36.391  -8.251  16.244  1.00 33.98  ? 29  VAL H O   1 
ATOM   12003 C CB  . VAL H  1 37  ? 34.836  -5.922  17.121  1.00 22.06  ? 29  VAL H CB  1 
ATOM   12004 C CG1 . VAL H  1 37  ? 34.175  -5.672  15.772  1.00 20.86  ? 29  VAL H CG1 1 
ATOM   12005 C CG2 . VAL H  1 37  ? 34.348  -4.940  18.161  1.00 20.63  ? 29  VAL H CG2 1 
ATOM   12006 N N   . SER H  1 38  ? 34.309  -8.961  15.743  1.00 36.31  ? 30  SER H N   1 
ATOM   12007 C CA  . SER H  1 38  ? 34.706  -9.737  14.569  1.00 28.67  ? 30  SER H CA  1 
ATOM   12008 C C   . SER H  1 38  ? 34.288  -9.026  13.295  1.00 29.79  ? 30  SER H C   1 
ATOM   12009 O O   . SER H  1 38  ? 33.117  -9.050  12.950  1.00 33.38  ? 30  SER H O   1 
ATOM   12010 C CB  . SER H  1 38  ? 34.030  -11.108 14.570  1.00 27.18  ? 30  SER H CB  1 
ATOM   12011 O OG  . SER H  1 38  ? 34.054  -11.708 15.850  1.00 37.32  ? 30  SER H OG  1 
ATOM   12012 N N   . VAL H  1 39  ? 35.228  -8.403  12.589  1.00 32.12  ? 31  VAL H N   1 
ATOM   12013 C CA  . VAL H  1 39  ? 34.926  -7.833  11.278  1.00 29.79  ? 31  VAL H CA  1 
ATOM   12014 C C   . VAL H  1 39  ? 35.251  -8.866  10.197  1.00 41.22  ? 31  VAL H C   1 
ATOM   12015 O O   . VAL H  1 39  ? 36.043  -9.780  10.426  1.00 46.66  ? 31  VAL H O   1 
ATOM   12016 C CB  . VAL H  1 39  ? 35.718  -6.544  10.999  1.00 29.32  ? 31  VAL H CB  1 
ATOM   12017 C CG1 . VAL H  1 39  ? 34.918  -5.629  10.111  1.00 32.97  ? 31  VAL H CG1 1 
ATOM   12018 C CG2 . VAL H  1 39  ? 36.059  -5.834  12.278  1.00 26.23  ? 31  VAL H CG2 1 
ATOM   12019 N N   . SER H  1 40  ? 34.449  -8.830  9.152   1.00 39.47  ? 32  SER H N   1 
ATOM   12020 C CA  . SER H  1 40  ? 34.695  -9.602  7.972   1.00 33.76  ? 32  SER H CA  1 
ATOM   12021 C C   . SER H  1 40  ? 34.163  -8.746  6.859   1.00 36.49  ? 32  SER H C   1 
ATOM   12022 O O   . SER H  1 40  ? 33.079  -8.173  6.964   1.00 40.17  ? 32  SER H O   1 
ATOM   12023 C CB  . SER H  1 40  ? 33.943  -10.931 8.028   1.00 32.17  ? 32  SER H CB  1 
ATOM   12024 O OG  . SER H  1 40  ? 34.052  -11.631 6.800   1.00 47.68  ? 32  SER H OG  1 
ATOM   12025 N N   . LEU H  1 41  ? 34.914  -8.675  5.780   1.00 34.90  ? 33  LEU H N   1 
ATOM   12026 C CA  . LEU H  1 41  ? 34.383  -8.103  4.544   1.00 33.55  ? 33  LEU H CA  1 
ATOM   12027 C C   . LEU H  1 41  ? 34.014  -9.138  3.489   1.00 41.33  ? 33  LEU H C   1 
ATOM   12028 O O   . LEU H  1 41  ? 34.726  -10.127 3.281   1.00 44.39  ? 33  LEU H O   1 
ATOM   12029 C CB  . LEU H  1 41  ? 35.364  -7.114  3.928   1.00 28.93  ? 33  LEU H CB  1 
ATOM   12030 C CG  . LEU H  1 41  ? 35.843  -5.967  4.808   1.00 33.63  ? 33  LEU H CG  1 
ATOM   12031 C CD1 . LEU H  1 41  ? 36.549  -4.932  3.952   1.00 29.31  ? 33  LEU H CD1 1 
ATOM   12032 C CD2 . LEU H  1 41  ? 34.682  -5.341  5.562   1.00 33.42  ? 33  LEU H CD2 1 
ATOM   12033 N N   . LYS H  1 42  ? 32.891  -8.890  2.821   1.00 42.33  ? 34  LYS H N   1 
ATOM   12034 C CA  . LYS H  1 42  ? 32.480  -9.668  1.659   1.00 39.18  ? 34  LYS H CA  1 
ATOM   12035 C C   . LYS H  1 42  ? 32.113  -8.709  0.529   1.00 37.66  ? 34  LYS H C   1 
ATOM   12036 O O   . LYS H  1 42  ? 31.086  -8.028  0.585   1.00 31.62  ? 34  LYS H O   1 
ATOM   12037 C CB  . LYS H  1 42  ? 31.323  -10.610 2.004   1.00 36.97  ? 34  LYS H CB  1 
ATOM   12038 C CG  . LYS H  1 42  ? 31.607  -11.472 3.234   1.00 46.59  ? 34  LYS H CG  1 
ATOM   12039 C CD  . LYS H  1 42  ? 31.159  -12.913 3.054   1.00 50.26  ? 34  LYS H CD  1 
ATOM   12040 C CE  . LYS H  1 42  ? 31.773  -13.811 4.120   1.00 55.50  ? 34  LYS H CE  1 
ATOM   12041 N NZ  . LYS H  1 42  ? 33.269  -13.783 4.080   1.00 46.71  ? 34  LYS H NZ  1 
ATOM   12042 N N   . PHE H  1 43  ? 32.975  -8.656  -0.489  1.00 37.96  ? 35  PHE H N   1 
ATOM   12043 C CA  . PHE H  1 43  ? 32.842  -7.695  -1.581  1.00 32.51  ? 35  PHE H CA  1 
ATOM   12044 C C   . PHE H  1 43  ? 31.684  -7.995  -2.514  1.00 32.17  ? 35  PHE H C   1 
ATOM   12045 O O   . PHE H  1 43  ? 31.338  -9.155  -2.754  1.00 36.01  ? 35  PHE H O   1 
ATOM   12046 C CB  . PHE H  1 43  ? 34.144  -7.593  -2.366  1.00 26.33  ? 35  PHE H CB  1 
ATOM   12047 C CG  . PHE H  1 43  ? 35.264  -7.031  -1.568  1.00 23.44  ? 35  PHE H CG  1 
ATOM   12048 C CD1 . PHE H  1 43  ? 36.032  -7.851  -0.767  1.00 24.64  ? 35  PHE H CD1 1 
ATOM   12049 C CD2 . PHE H  1 43  ? 35.525  -5.676  -1.582  1.00 21.90  ? 35  PHE H CD2 1 
ATOM   12050 C CE1 . PHE H  1 43  ? 37.055  -7.330  -0.012  1.00 22.71  ? 35  PHE H CE1 1 
ATOM   12051 C CE2 . PHE H  1 43  ? 36.545  -5.154  -0.833  1.00 16.25  ? 35  PHE H CE2 1 
ATOM   12052 C CZ  . PHE H  1 43  ? 37.313  -5.981  -0.050  1.00 16.07  ? 35  PHE H CZ  1 
ATOM   12053 N N   . ILE H  1 44  ? 31.087  -6.929  -3.031  1.00 25.36  ? 36  ILE H N   1 
ATOM   12054 C CA  . ILE H  1 44  ? 29.934  -7.048  -3.896  1.00 31.62  ? 36  ILE H CA  1 
ATOM   12055 C C   . ILE H  1 44  ? 30.254  -6.457  -5.259  1.00 31.71  ? 36  ILE H C   1 
ATOM   12056 O O   . ILE H  1 44  ? 29.796  -6.958  -6.283  1.00 32.48  ? 36  ILE H O   1 
ATOM   12057 C CB  . ILE H  1 44  ? 28.714  -6.322  -3.296  1.00 30.47  ? 36  ILE H CB  1 
ATOM   12058 C CG1 . ILE H  1 44  ? 28.565  -6.672  -1.817  1.00 26.85  ? 36  ILE H CG1 1 
ATOM   12059 C CG2 . ILE H  1 44  ? 27.441  -6.694  -4.048  1.00 26.79  ? 36  ILE H CG2 1 
ATOM   12060 C CD1 . ILE H  1 44  ? 28.205  -8.106  -1.585  1.00 32.12  ? 36  ILE H CD1 1 
ATOM   12061 N N   . ASN H  1 45  ? 31.054  -5.397  -5.273  1.00 29.81  ? 37  ASN H N   1 
ATOM   12062 C CA  . ASN H  1 45  ? 31.324  -4.702  -6.517  1.00 27.34  ? 37  ASN H CA  1 
ATOM   12063 C C   . ASN H  1 45  ? 32.574  -3.844  -6.519  1.00 35.76  ? 37  ASN H C   1 
ATOM   12064 O O   . ASN H  1 45  ? 32.966  -3.298  -5.487  1.00 34.94  ? 37  ASN H O   1 
ATOM   12065 C CB  . ASN H  1 45  ? 30.136  -3.841  -6.907  1.00 25.95  ? 37  ASN H CB  1 
ATOM   12066 C CG  . ASN H  1 45  ? 29.776  -4.008  -8.344  1.00 34.88  ? 37  ASN H CG  1 
ATOM   12067 O OD1 . ASN H  1 45  ? 30.546  -4.584  -9.106  1.00 35.53  ? 37  ASN H OD1 1 
ATOM   12068 N ND2 . ASN H  1 45  ? 28.608  -3.505  -8.740  1.00 38.16  ? 37  ASN H ND2 1 
ATOM   12069 N N   . ILE H  1 46  ? 33.179  -3.727  -7.702  1.00 33.18  ? 38  ILE H N   1 
ATOM   12070 C CA  . ILE H  1 46  ? 34.329  -2.867  -7.939  1.00 27.45  ? 38  ILE H CA  1 
ATOM   12071 C C   . ILE H  1 46  ? 33.982  -1.992  -9.132  1.00 27.74  ? 38  ILE H C   1 
ATOM   12072 O O   . ILE H  1 46  ? 33.680  -2.501  -10.201 1.00 35.81  ? 38  ILE H O   1 
ATOM   12073 C CB  . ILE H  1 46  ? 35.569  -3.707  -8.247  1.00 32.16  ? 38  ILE H CB  1 
ATOM   12074 C CG1 . ILE H  1 46  ? 35.919  -4.582  -7.043  1.00 28.45  ? 38  ILE H CG1 1 
ATOM   12075 C CG2 . ILE H  1 46  ? 36.733  -2.821  -8.633  1.00 33.68  ? 38  ILE H CG2 1 
ATOM   12076 C CD1 . ILE H  1 46  ? 37.143  -5.426  -7.234  1.00 26.22  ? 38  ILE H CD1 1 
ATOM   12077 N N   . LEU H  1 47  ? 34.008  -0.680  -8.961  1.00 29.89  ? 39  LEU H N   1 
ATOM   12078 C CA  . LEU H  1 47  ? 33.295  0.185   -9.899  1.00 34.69  ? 39  LEU H CA  1 
ATOM   12079 C C   . LEU H  1 47  ? 34.164  1.129   -10.707 1.00 39.62  ? 39  LEU H C   1 
ATOM   12080 O O   . LEU H  1 47  ? 33.872  1.385   -11.873 1.00 52.09  ? 39  LEU H O   1 
ATOM   12081 C CB  . LEU H  1 47  ? 32.212  1.006   -9.183  1.00 36.45  ? 39  LEU H CB  1 
ATOM   12082 C CG  . LEU H  1 47  ? 31.011  0.308   -8.546  1.00 33.81  ? 39  LEU H CG  1 
ATOM   12083 C CD1 . LEU H  1 47  ? 31.343  -0.173  -7.145  1.00 36.83  ? 39  LEU H CD1 1 
ATOM   12084 C CD2 . LEU H  1 47  ? 29.829  1.248   -8.516  1.00 33.01  ? 39  LEU H CD2 1 
ATOM   12085 N N   . GLU H  1 48  ? 35.202  1.679   -10.089 1.00 35.55  ? 40  GLU H N   1 
ATOM   12086 C CA  . GLU H  1 48  ? 36.056  2.640   -10.773 1.00 37.55  ? 40  GLU H CA  1 
ATOM   12087 C C   . GLU H  1 48  ? 37.488  2.506   -10.301 1.00 43.31  ? 40  GLU H C   1 
ATOM   12088 O O   . GLU H  1 48  ? 37.861  3.059   -9.269  1.00 48.95  ? 40  GLU H O   1 
ATOM   12089 C CB  . GLU H  1 48  ? 35.576  4.074   -10.535 1.00 39.78  ? 40  GLU H CB  1 
ATOM   12090 C CG  . GLU H  1 48  ? 34.259  4.432   -11.205 1.00 44.53  ? 40  GLU H CG  1 
ATOM   12091 C CD  . GLU H  1 48  ? 33.436  5.410   -10.379 1.00 53.50  ? 40  GLU H CD  1 
ATOM   12092 O OE1 . GLU H  1 48  ? 33.687  5.516   -9.155  1.00 47.08  ? 40  GLU H OE1 1 
ATOM   12093 O OE2 . GLU H  1 48  ? 32.538  6.071   -10.949 1.00 60.07  ? 40  GLU H OE2 1 
ATOM   12094 N N   . VAL H  1 49  ? 38.291  1.772   -11.061 1.00 43.23  ? 41  VAL H N   1 
ATOM   12095 C CA  . VAL H  1 49  ? 39.700  1.628   -10.747 1.00 35.73  ? 41  VAL H CA  1 
ATOM   12096 C C   . VAL H  1 49  ? 40.484  2.637   -11.582 1.00 37.95  ? 41  VAL H C   1 
ATOM   12097 O O   . VAL H  1 49  ? 40.049  3.017   -12.668 1.00 38.05  ? 41  VAL H O   1 
ATOM   12098 C CB  . VAL H  1 49  ? 40.151  0.195   -11.001 1.00 32.87  ? 41  VAL H CB  1 
ATOM   12099 C CG1 . VAL H  1 49  ? 41.567  -0.015  -10.523 1.00 44.65  ? 41  VAL H CG1 1 
ATOM   12100 C CG2 . VAL H  1 49  ? 39.231  -0.741  -10.273 1.00 32.18  ? 41  VAL H CG2 1 
ATOM   12101 N N   . ASN H  1 50  ? 41.613  3.100   -11.054 1.00 36.82  ? 42  ASN H N   1 
ATOM   12102 C CA  . ASN H  1 50  ? 42.412  4.137   -11.701 1.00 37.55  ? 42  ASN H CA  1 
ATOM   12103 C C   . ASN H  1 50  ? 43.879  3.904   -11.342 1.00 47.29  ? 42  ASN H C   1 
ATOM   12104 O O   . ASN H  1 50  ? 44.335  4.351   -10.284 1.00 49.05  ? 42  ASN H O   1 
ATOM   12105 C CB  . ASN H  1 50  ? 41.928  5.517   -11.229 1.00 35.97  ? 42  ASN H CB  1 
ATOM   12106 C CG  . ASN H  1 50  ? 42.657  6.679   -11.897 1.00 36.70  ? 42  ASN H CG  1 
ATOM   12107 O OD1 . ASN H  1 50  ? 43.883  6.706   -11.963 1.00 43.97  ? 42  ASN H OD1 1 
ATOM   12108 N ND2 . ASN H  1 50  ? 41.896  7.661   -12.371 1.00 23.58  ? 42  ASN H ND2 1 
ATOM   12109 N N   . GLU H  1 51  ? 44.617  3.199   -12.205 1.00 44.39  ? 43  GLU H N   1 
ATOM   12110 C CA  . GLU H  1 51  ? 45.971  2.754   -11.851 1.00 42.58  ? 43  GLU H CA  1 
ATOM   12111 C C   . GLU H  1 51  ? 46.963  3.905   -11.800 1.00 42.44  ? 43  GLU H C   1 
ATOM   12112 O O   . GLU H  1 51  ? 48.061  3.770   -11.248 1.00 41.72  ? 43  GLU H O   1 
ATOM   12113 C CB  . GLU H  1 51  ? 46.476  1.666   -12.802 1.00 49.41  ? 43  GLU H CB  1 
ATOM   12114 C CG  . GLU H  1 51  ? 47.063  2.194   -14.107 1.00 60.54  ? 43  GLU H CG  1 
ATOM   12115 C CD  . GLU H  1 51  ? 48.004  1.202   -14.764 1.00 61.45  ? 43  GLU H CD  1 
ATOM   12116 O OE1 . GLU H  1 51  ? 47.857  -0.014  -14.494 1.00 62.87  ? 43  GLU H OE1 1 
ATOM   12117 O OE2 . GLU H  1 51  ? 48.891  1.642   -15.535 1.00 60.96  ? 43  GLU H OE2 1 
ATOM   12118 N N   . ILE H  1 52  ? 46.567  5.031   -12.386 1.00 36.65  ? 44  ILE H N   1 
ATOM   12119 C CA  . ILE H  1 52  ? 47.359  6.247   -12.353 1.00 38.68  ? 44  ILE H CA  1 
ATOM   12120 C C   . ILE H  1 52  ? 47.328  6.880   -10.970 1.00 42.29  ? 44  ILE H C   1 
ATOM   12121 O O   . ILE H  1 52  ? 48.376  7.142   -10.380 1.00 39.16  ? 44  ILE H O   1 
ATOM   12122 C CB  . ILE H  1 52  ? 46.839  7.275   -13.372 1.00 42.98  ? 44  ILE H CB  1 
ATOM   12123 C CG1 . ILE H  1 52  ? 46.919  6.706   -14.795 1.00 51.13  ? 44  ILE H CG1 1 
ATOM   12124 C CG2 . ILE H  1 52  ? 47.586  8.596   -13.232 1.00 38.85  ? 44  ILE H CG2 1 
ATOM   12125 C CD1 . ILE H  1 52  ? 48.239  6.009   -15.131 1.00 48.76  ? 44  ILE H CD1 1 
ATOM   12126 N N   . THR H  1 53  ? 46.121  7.123   -10.458 1.00 44.17  ? 45  THR H N   1 
ATOM   12127 C CA  . THR H  1 53  ? 45.948  7.776   -9.161  1.00 39.55  ? 45  THR H CA  1 
ATOM   12128 C C   . THR H  1 53  ? 45.901  6.768   -8.023  1.00 34.13  ? 45  THR H C   1 
ATOM   12129 O O   . THR H  1 53  ? 45.816  7.151   -6.863  1.00 42.70  ? 45  THR H O   1 
ATOM   12130 C CB  . THR H  1 53  ? 44.663  8.638   -9.099  1.00 38.13  ? 45  THR H CB  1 
ATOM   12131 O OG1 . THR H  1 53  ? 43.520  7.785   -8.959  1.00 38.51  ? 45  THR H OG1 1 
ATOM   12132 C CG2 . THR H  1 53  ? 44.513  9.509   -10.349 1.00 35.36  ? 45  THR H CG2 1 
ATOM   12133 N N   . ASN H  1 54  ? 45.957  5.486   -8.358  1.00 35.85  ? 46  ASN H N   1 
ATOM   12134 C CA  . ASN H  1 54  ? 45.946  4.423   -7.354  1.00 43.02  ? 46  ASN H CA  1 
ATOM   12135 C C   . ASN H  1 54  ? 44.753  4.512   -6.394  1.00 40.95  ? 46  ASN H C   1 
ATOM   12136 O O   . ASN H  1 54  ? 44.918  4.554   -5.171  1.00 37.46  ? 46  ASN H O   1 
ATOM   12137 C CB  . ASN H  1 54  ? 47.267  4.393   -6.582  1.00 41.23  ? 46  ASN H CB  1 
ATOM   12138 C CG  . ASN H  1 54  ? 48.215  3.313   -7.081  1.00 39.24  ? 46  ASN H CG  1 
ATOM   12139 O OD1 . ASN H  1 54  ? 47.799  2.208   -7.437  1.00 35.28  ? 46  ASN H OD1 1 
ATOM   12140 N ND2 . ASN H  1 54  ? 49.502  3.624   -7.089  1.00 45.19  ? 46  ASN H ND2 1 
ATOM   12141 N N   . GLU H  1 55  ? 43.555  4.548   -6.975  1.00 41.46  ? 47  GLU H N   1 
ATOM   12142 C CA  . GLU H  1 55  ? 42.310  4.641   -6.220  1.00 37.08  ? 47  GLU H CA  1 
ATOM   12143 C C   . GLU H  1 55  ? 41.343  3.544   -6.659  1.00 38.18  ? 47  GLU H C   1 
ATOM   12144 O O   . GLU H  1 55  ? 41.441  3.028   -7.778  1.00 44.65  ? 47  GLU H O   1 
ATOM   12145 C CB  . GLU H  1 55  ? 41.666  6.015   -6.422  1.00 32.25  ? 47  GLU H CB  1 
ATOM   12146 C CG  . GLU H  1 55  ? 42.543  7.189   -6.013  1.00 33.97  ? 47  GLU H CG  1 
ATOM   12147 C CD  . GLU H  1 55  ? 41.803  8.508   -6.077  1.00 37.92  ? 47  GLU H CD  1 
ATOM   12148 O OE1 . GLU H  1 55  ? 40.558  8.471   -6.021  1.00 40.16  ? 47  GLU H OE1 1 
ATOM   12149 O OE2 . GLU H  1 55  ? 42.454  9.574   -6.184  1.00 39.23  ? 47  GLU H OE2 1 
ATOM   12150 N N   . VAL H  1 56  ? 40.416  3.182   -5.781  1.00 30.63  ? 48  VAL H N   1 
ATOM   12151 C CA  . VAL H  1 56  ? 39.373  2.225   -6.141  1.00 33.44  ? 48  VAL H CA  1 
ATOM   12152 C C   . VAL H  1 56  ? 38.046  2.592   -5.506  1.00 36.33  ? 48  VAL H C   1 
ATOM   12153 O O   . VAL H  1 56  ? 38.006  3.229   -4.462  1.00 32.86  ? 48  VAL H O   1 
ATOM   12154 C CB  . VAL H  1 56  ? 39.725  0.804   -5.711  1.00 28.47  ? 48  VAL H CB  1 
ATOM   12155 C CG1 . VAL H  1 56  ? 40.524  0.107   -6.784  1.00 40.67  ? 48  VAL H CG1 1 
ATOM   12156 C CG2 . VAL H  1 56  ? 40.488  0.842   -4.438  1.00 31.63  ? 48  VAL H CG2 1 
ATOM   12157 N N   . ASP H  1 57  ? 36.958  2.181   -6.144  1.00 43.78  ? 49  ASP H N   1 
ATOM   12158 C CA  . ASP H  1 57  ? 35.622  2.457   -5.636  1.00 31.03  ? 49  ASP H CA  1 
ATOM   12159 C C   . ASP H  1 57  ? 34.893  1.139   -5.500  1.00 28.59  ? 49  ASP H C   1 
ATOM   12160 O O   . ASP H  1 57  ? 34.592  0.480   -6.491  1.00 33.07  ? 49  ASP H O   1 
ATOM   12161 C CB  . ASP H  1 57  ? 34.880  3.378   -6.598  1.00 37.71  ? 49  ASP H CB  1 
ATOM   12162 C CG  . ASP H  1 57  ? 33.759  4.139   -5.927  1.00 38.43  ? 49  ASP H CG  1 
ATOM   12163 O OD1 . ASP H  1 57  ? 33.035  3.527   -5.114  1.00 36.42  ? 49  ASP H OD1 1 
ATOM   12164 O OD2 . ASP H  1 57  ? 33.603  5.349   -6.213  1.00 43.81  ? 49  ASP H OD2 1 
ATOM   12165 N N   . VAL H  1 58  ? 34.617  0.742   -4.267  1.00 30.89  ? 50  VAL H N   1 
ATOM   12166 C CA  . VAL H  1 58  ? 34.047  -0.574  -4.029  1.00 32.08  ? 50  VAL H CA  1 
ATOM   12167 C C   . VAL H  1 58  ? 32.754  -0.550  -3.227  1.00 31.26  ? 50  VAL H C   1 
ATOM   12168 O O   . VAL H  1 58  ? 32.451  0.405   -2.522  1.00 30.35  ? 50  VAL H O   1 
ATOM   12169 C CB  . VAL H  1 58  ? 35.043  -1.480  -3.299  1.00 29.64  ? 50  VAL H CB  1 
ATOM   12170 C CG1 . VAL H  1 58  ? 36.233  -1.810  -4.208  1.00 29.14  ? 50  VAL H CG1 1 
ATOM   12171 C CG2 . VAL H  1 58  ? 35.499  -0.804  -2.024  1.00 30.75  ? 50  VAL H CG2 1 
ATOM   12172 N N   . VAL H  1 59  ? 31.992  -1.623  -3.366  1.00 28.14  ? 51  VAL H N   1 
ATOM   12173 C CA  . VAL H  1 59  ? 30.825  -1.849  -2.565  1.00 20.16  ? 51  VAL H CA  1 
ATOM   12174 C C   . VAL H  1 59  ? 31.093  -3.152  -1.837  1.00 27.04  ? 51  VAL H C   1 
ATOM   12175 O O   . VAL H  1 59  ? 31.499  -4.129  -2.457  1.00 31.41  ? 51  VAL H O   1 
ATOM   12176 C CB  . VAL H  1 59  ? 29.578  -1.985  -3.447  1.00 21.62  ? 51  VAL H CB  1 
ATOM   12177 C CG1 . VAL H  1 59  ? 28.376  -2.432  -2.625  1.00 26.63  ? 51  VAL H CG1 1 
ATOM   12178 C CG2 . VAL H  1 59  ? 29.284  -0.675  -4.136  1.00 22.85  ? 51  VAL H CG2 1 
ATOM   12179 N N   . PHE H  1 60  ? 30.894  -3.164  -0.521  1.00 25.15  ? 52  PHE H N   1 
ATOM   12180 C CA  . PHE H  1 60  ? 31.097  -4.368  0.276   1.00 22.84  ? 52  PHE H CA  1 
ATOM   12181 C C   . PHE H  1 60  ? 30.103  -4.437  1.419   1.00 28.55  ? 52  PHE H C   1 
ATOM   12182 O O   . PHE H  1 60  ? 29.539  -3.417  1.825   1.00 26.25  ? 52  PHE H O   1 
ATOM   12183 C CB  . PHE H  1 60  ? 32.518  -4.415  0.839   1.00 26.27  ? 52  PHE H CB  1 
ATOM   12184 C CG  . PHE H  1 60  ? 32.915  -3.174  1.584   1.00 23.38  ? 52  PHE H CG  1 
ATOM   12185 C CD1 . PHE H  1 60  ? 32.812  -3.115  2.959   1.00 26.08  ? 52  PHE H CD1 1 
ATOM   12186 C CD2 . PHE H  1 60  ? 33.388  -2.061  0.905   1.00 24.28  ? 52  PHE H CD2 1 
ATOM   12187 C CE1 . PHE H  1 60  ? 33.167  -1.966  3.648   1.00 24.24  ? 52  PHE H CE1 1 
ATOM   12188 C CE2 . PHE H  1 60  ? 33.745  -0.916  1.586   1.00 23.80  ? 52  PHE H CE2 1 
ATOM   12189 C CZ  . PHE H  1 60  ? 33.630  -0.867  2.961   1.00 18.95  ? 52  PHE H CZ  1 
ATOM   12190 N N   . TRP H  1 61  ? 29.893  -5.652  1.924   1.00 31.71  ? 53  TRP H N   1 
ATOM   12191 C CA  . TRP H  1 61  ? 29.079  -5.886  3.109   1.00 25.49  ? 53  TRP H CA  1 
ATOM   12192 C C   . TRP H  1 61  ? 29.999  -6.094  4.308   1.00 32.62  ? 53  TRP H C   1 
ATOM   12193 O O   . TRP H  1 61  ? 30.715  -7.097  4.376   1.00 30.46  ? 53  TRP H O   1 
ATOM   12194 C CB  . TRP H  1 61  ? 28.164  -7.097  2.910   1.00 25.26  ? 53  TRP H CB  1 
ATOM   12195 C CG  . TRP H  1 61  ? 27.120  -6.859  1.852   1.00 33.38  ? 53  TRP H CG  1 
ATOM   12196 C CD1 . TRP H  1 61  ? 26.915  -5.701  1.154   1.00 33.06  ? 53  TRP H CD1 1 
ATOM   12197 C CD2 . TRP H  1 61  ? 26.147  -7.796  1.360   1.00 33.86  ? 53  TRP H CD2 1 
ATOM   12198 N NE1 . TRP H  1 61  ? 25.880  -5.856  0.258   1.00 37.21  ? 53  TRP H NE1 1 
ATOM   12199 C CE2 . TRP H  1 61  ? 25.392  -7.133  0.365   1.00 33.65  ? 53  TRP H CE2 1 
ATOM   12200 C CE3 . TRP H  1 61  ? 25.848  -9.128  1.656   1.00 33.56  ? 53  TRP H CE3 1 
ATOM   12201 C CZ2 . TRP H  1 61  ? 24.359  -7.754  -0.323  1.00 31.36  ? 53  TRP H CZ2 1 
ATOM   12202 C CZ3 . TRP H  1 61  ? 24.818  -9.741  0.971   1.00 35.36  ? 53  TRP H CZ3 1 
ATOM   12203 C CH2 . TRP H  1 61  ? 24.086  -9.055  -0.006  1.00 38.62  ? 53  TRP H CH2 1 
ATOM   12204 N N   . GLN H  1 62  ? 29.977  -5.132  5.235   1.00 27.20  ? 54  GLN H N   1 
ATOM   12205 C CA  . GLN H  1 62  ? 30.866  -5.114  6.397   1.00 26.94  ? 54  GLN H CA  1 
ATOM   12206 C C   . GLN H  1 62  ? 30.277  -5.876  7.599   1.00 29.76  ? 54  GLN H C   1 
ATOM   12207 O O   . GLN H  1 62  ? 29.714  -5.297  8.522   1.00 34.46  ? 54  GLN H O   1 
ATOM   12208 C CB  . GLN H  1 62  ? 31.224  -3.662  6.754   1.00 28.72  ? 54  GLN H CB  1 
ATOM   12209 C CG  . GLN H  1 62  ? 32.102  -3.456  7.996   1.00 30.96  ? 54  GLN H CG  1 
ATOM   12210 C CD  . GLN H  1 62  ? 32.348  -1.977  8.296   1.00 33.47  ? 54  GLN H CD  1 
ATOM   12211 O OE1 . GLN H  1 62  ? 32.637  -1.191  7.396   1.00 37.01  ? 54  GLN H OE1 1 
ATOM   12212 N NE2 . GLN H  1 62  ? 32.224  -1.596  9.563   1.00 35.53  ? 54  GLN H NE2 1 
ATOM   12213 N N   . GLN H  1 63  ? 30.431  -7.190  7.569   1.00 29.51  ? 55  GLN H N   1 
ATOM   12214 C CA  . GLN H  1 63  ? 29.907  -8.087  8.584   1.00 26.74  ? 55  GLN H CA  1 
ATOM   12215 C C   . GLN H  1 63  ? 30.593  -7.921  9.940   1.00 27.76  ? 55  GLN H C   1 
ATOM   12216 O O   . GLN H  1 63  ? 31.706  -8.395  10.140  1.00 28.41  ? 55  GLN H O   1 
ATOM   12217 C CB  . GLN H  1 63  ? 30.073  -9.514  8.077   1.00 26.54  ? 55  GLN H CB  1 
ATOM   12218 C CG  . GLN H  1 63  ? 29.589  -10.595 8.986   1.00 34.59  ? 55  GLN H CG  1 
ATOM   12219 C CD  . GLN H  1 63  ? 29.180  -11.815 8.197   1.00 51.10  ? 55  GLN H CD  1 
ATOM   12220 O OE1 . GLN H  1 63  ? 29.486  -11.916 6.999   1.00 54.11  ? 55  GLN H OE1 1 
ATOM   12221 N NE2 . GLN H  1 63  ? 28.468  -12.741 8.845   1.00 37.46  ? 55  GLN H NE2 1 
ATOM   12222 N N   . THR H  1 64  ? 29.906  -7.265  10.876  1.00 29.62  ? 56  THR H N   1 
ATOM   12223 C CA  . THR H  1 64  ? 30.448  -6.971  12.206  1.00 22.00  ? 56  THR H CA  1 
ATOM   12224 C C   . THR H  1 64  ? 29.668  -7.709  13.291  1.00 25.03  ? 56  THR H C   1 
ATOM   12225 O O   . THR H  1 64  ? 28.442  -7.611  13.339  1.00 26.52  ? 56  THR H O   1 
ATOM   12226 C CB  . THR H  1 64  ? 30.326  -5.469  12.514  1.00 23.88  ? 56  THR H CB  1 
ATOM   12227 O OG1 . THR H  1 64  ? 30.483  -4.705  11.308  1.00 30.92  ? 56  THR H OG1 1 
ATOM   12228 C CG2 . THR H  1 64  ? 31.364  -5.038  13.541  1.00 24.67  ? 56  THR H CG2 1 
ATOM   12229 N N   . THR H  1 65  ? 30.350  -8.453  14.161  1.00 20.26  ? 57  THR H N   1 
ATOM   12230 C CA  . THR H  1 65  ? 29.650  -9.038  15.299  1.00 23.44  ? 57  THR H CA  1 
ATOM   12231 C C   . THR H  1 65  ? 30.409  -8.929  16.612  1.00 25.50  ? 57  THR H C   1 
ATOM   12232 O O   . THR H  1 65  ? 31.632  -8.846  16.642  1.00 20.89  ? 57  THR H O   1 
ATOM   12233 C CB  . THR H  1 65  ? 29.216  -10.522 15.112  1.00 29.28  ? 57  THR H CB  1 
ATOM   12234 O OG1 . THR H  1 65  ? 30.356  -11.386 15.219  1.00 37.83  ? 57  THR H OG1 1 
ATOM   12235 C CG2 . THR H  1 65  ? 28.464  -10.751 13.797  1.00 19.69  ? 57  THR H CG2 1 
ATOM   12236 N N   . TRP H  1 66  ? 29.641  -8.930  17.697  1.00 25.42  ? 58  TRP H N   1 
ATOM   12237 C CA  . TRP H  1 66  ? 30.182  -8.840  19.035  1.00 21.81  ? 58  TRP H CA  1 
ATOM   12238 C C   . TRP H  1 66  ? 29.145  -9.317  20.049  1.00 25.81  ? 58  TRP H C   1 
ATOM   12239 O O   . TRP H  1 66  ? 28.000  -9.625  19.706  1.00 27.22  ? 58  TRP H O   1 
ATOM   12240 C CB  . TRP H  1 66  ? 30.623  -7.413  19.341  1.00 18.97  ? 58  TRP H CB  1 
ATOM   12241 C CG  . TRP H  1 66  ? 29.507  -6.435  19.311  1.00 24.35  ? 58  TRP H CG  1 
ATOM   12242 C CD1 . TRP H  1 66  ? 28.716  -6.041  20.366  1.00 27.46  ? 58  TRP H CD1 1 
ATOM   12243 C CD2 . TRP H  1 66  ? 29.038  -5.719  18.172  1.00 23.44  ? 58  TRP H CD2 1 
ATOM   12244 N NE1 . TRP H  1 66  ? 27.785  -5.122  19.942  1.00 25.52  ? 58  TRP H NE1 1 
ATOM   12245 C CE2 . TRP H  1 66  ? 27.966  -4.902  18.601  1.00 21.33  ? 58  TRP H CE2 1 
ATOM   12246 C CE3 . TRP H  1 66  ? 29.419  -5.686  16.827  1.00 21.96  ? 58  TRP H CE3 1 
ATOM   12247 C CZ2 . TRP H  1 66  ? 27.280  -4.064  17.735  1.00 20.74  ? 58  TRP H CZ2 1 
ATOM   12248 C CZ3 . TRP H  1 66  ? 28.734  -4.857  15.969  1.00 24.40  ? 58  TRP H CZ3 1 
ATOM   12249 C CH2 . TRP H  1 66  ? 27.674  -4.052  16.425  1.00 24.88  ? 58  TRP H CH2 1 
ATOM   12250 N N   . SER H  1 67  ? 29.551  -9.375  21.307  1.00 23.52  ? 59  SER H N   1 
ATOM   12251 C CA  . SER H  1 67  ? 28.689  -9.913  22.330  1.00 24.43  ? 59  SER H CA  1 
ATOM   12252 C C   . SER H  1 67  ? 28.468  -8.907  23.454  1.00 28.29  ? 59  SER H C   1 
ATOM   12253 O O   . SER H  1 67  ? 29.426  -8.331  23.971  1.00 29.83  ? 59  SER H O   1 
ATOM   12254 C CB  . SER H  1 67  ? 29.292  -11.206 22.870  1.00 20.79  ? 59  SER H CB  1 
ATOM   12255 O OG  . SER H  1 67  ? 29.041  -11.343 24.252  1.00 31.75  ? 59  SER H OG  1 
ATOM   12256 N N   . ASP H  1 68  ? 27.204  -8.689  23.814  1.00 27.16  ? 60  ASP H N   1 
ATOM   12257 C CA  . ASP H  1 68  ? 26.868  -7.988  25.056  1.00 31.64  ? 60  ASP H CA  1 
ATOM   12258 C C   . ASP H  1 68  ? 25.834  -8.772  25.879  1.00 29.43  ? 60  ASP H C   1 
ATOM   12259 O O   . ASP H  1 68  ? 24.626  -8.549  25.779  1.00 28.14  ? 60  ASP H O   1 
ATOM   12260 C CB  . ASP H  1 68  ? 26.401  -6.555  24.794  1.00 24.00  ? 60  ASP H CB  1 
ATOM   12261 C CG  . ASP H  1 68  ? 26.029  -5.817  26.077  1.00 30.23  ? 60  ASP H CG  1 
ATOM   12262 O OD1 . ASP H  1 68  ? 26.427  -6.268  27.181  1.00 30.34  ? 60  ASP H OD1 1 
ATOM   12263 O OD2 . ASP H  1 68  ? 25.344  -4.774  25.981  1.00 33.06  ? 60  ASP H OD2 1 
ATOM   12264 N N   . ARG H  1 69  ? 26.338  -9.674  26.711  1.00 35.54  ? 61  ARG H N   1 
ATOM   12265 C CA  . ARG H  1 69  ? 25.509  -10.613 27.466  1.00 35.75  ? 61  ARG H CA  1 
ATOM   12266 C C   . ARG H  1 69  ? 24.437  -9.966  28.341  1.00 27.50  ? 61  ARG H C   1 
ATOM   12267 O O   . ARG H  1 69  ? 23.461  -10.615 28.684  1.00 27.71  ? 61  ARG H O   1 
ATOM   12268 C CB  . ARG H  1 69  ? 26.393  -11.549 28.303  1.00 37.27  ? 61  ARG H CB  1 
ATOM   12269 C CG  . ARG H  1 69  ? 26.310  -13.030 27.904  1.00 45.16  ? 61  ARG H CG  1 
ATOM   12270 C CD  . ARG H  1 69  ? 25.374  -13.790 28.842  1.00 48.92  ? 61  ARG H CD  1 
ATOM   12271 N NE  . ARG H  1 69  ? 25.539  -13.323 30.219  1.00 52.17  ? 61  ARG H NE  1 
ATOM   12272 C CZ  . ARG H  1 69  ? 26.353  -13.874 31.115  1.00 58.79  ? 61  ARG H CZ  1 
ATOM   12273 N NH1 . ARG H  1 69  ? 27.077  -14.943 30.798  1.00 54.11  ? 61  ARG H NH1 1 
ATOM   12274 N NH2 . ARG H  1 69  ? 26.433  -13.358 32.338  1.00 58.75  ? 61  ARG H NH2 1 
ATOM   12275 N N   . THR H  1 70  ? 24.616  -8.693  28.691  1.00 27.50  ? 62  THR H N   1 
ATOM   12276 C CA  . THR H  1 70  ? 23.607  -7.949  29.447  1.00 24.60  ? 62  THR H CA  1 
ATOM   12277 C C   . THR H  1 70  ? 22.276  -7.830  28.684  1.00 29.13  ? 62  THR H C   1 
ATOM   12278 O O   . THR H  1 70  ? 21.200  -7.654  29.291  1.00 23.29  ? 62  THR H O   1 
ATOM   12279 C CB  . THR H  1 70  ? 24.095  -6.531  29.815  1.00 22.37  ? 62  THR H CB  1 
ATOM   12280 O OG1 . THR H  1 70  ? 24.202  -5.736  28.630  1.00 28.78  ? 62  THR H OG1 1 
ATOM   12281 C CG2 . THR H  1 70  ? 25.444  -6.583  30.514  1.00 25.12  ? 62  THR H CG2 1 
ATOM   12282 N N   . LEU H  1 71  ? 22.365  -7.920  27.354  1.00 27.80  ? 63  LEU H N   1 
ATOM   12283 C CA  . LEU H  1 71  ? 21.196  -7.894  26.478  1.00 22.22  ? 63  LEU H CA  1 
ATOM   12284 C C   . LEU H  1 71  ? 20.533  -9.277  26.327  1.00 21.47  ? 63  LEU H C   1 
ATOM   12285 O O   . LEU H  1 71  ? 19.447  -9.392  25.756  1.00 22.61  ? 63  LEU H O   1 
ATOM   12286 C CB  . LEU H  1 71  ? 21.581  -7.341  25.102  1.00 20.35  ? 63  LEU H CB  1 
ATOM   12287 C CG  . LEU H  1 71  ? 22.282  -5.982  25.073  1.00 26.13  ? 63  LEU H CG  1 
ATOM   12288 C CD1 . LEU H  1 71  ? 22.713  -5.584  23.648  1.00 14.06  ? 63  LEU H CD1 1 
ATOM   12289 C CD2 . LEU H  1 71  ? 21.408  -4.891  25.700  1.00 20.02  ? 63  LEU H CD2 1 
ATOM   12290 N N   . ALA H  1 72  ? 21.181  -10.319 26.843  1.00 22.00  ? 64  ALA H N   1 
ATOM   12291 C CA  . ALA H  1 72  ? 20.678  -11.687 26.692  1.00 24.43  ? 64  ALA H CA  1 
ATOM   12292 C C   . ALA H  1 72  ? 19.314  -11.878 27.351  1.00 27.17  ? 64  ALA H C   1 
ATOM   12293 O O   . ALA H  1 72  ? 18.930  -11.116 28.235  1.00 28.94  ? 64  ALA H O   1 
ATOM   12294 C CB  . ALA H  1 72  ? 21.685  -12.699 27.249  1.00 23.09  ? 64  ALA H CB  1 
ATOM   12295 N N   . TRP H  1 73  ? 18.585  -12.904 26.922  1.00 31.67  ? 65  TRP H N   1 
ATOM   12296 C CA  . TRP H  1 73  ? 17.292  -13.209 27.516  1.00 22.72  ? 65  TRP H CA  1 
ATOM   12297 C C   . TRP H  1 73  ? 16.883  -14.654 27.255  1.00 27.39  ? 65  TRP H C   1 
ATOM   12298 O O   . TRP H  1 73  ? 17.278  -15.248 26.257  1.00 30.26  ? 65  TRP H O   1 
ATOM   12299 C CB  . TRP H  1 73  ? 16.222  -12.234 27.019  1.00 19.16  ? 65  TRP H CB  1 
ATOM   12300 C CG  . TRP H  1 73  ? 15.732  -12.472 25.634  1.00 16.66  ? 65  TRP H CG  1 
ATOM   12301 C CD1 . TRP H  1 73  ? 14.711  -13.290 25.259  1.00 20.55  ? 65  TRP H CD1 1 
ATOM   12302 C CD2 . TRP H  1 73  ? 16.211  -11.857 24.438  1.00 21.37  ? 65  TRP H CD2 1 
ATOM   12303 N NE1 . TRP H  1 73  ? 14.531  -13.239 23.903  1.00 19.15  ? 65  TRP H NE1 1 
ATOM   12304 C CE2 . TRP H  1 73  ? 15.442  -12.366 23.370  1.00 22.61  ? 65  TRP H CE2 1 
ATOM   12305 C CE3 . TRP H  1 73  ? 17.230  -10.936 24.158  1.00 23.73  ? 65  TRP H CE3 1 
ATOM   12306 C CZ2 . TRP H  1 73  ? 15.662  -11.989 22.040  1.00 22.37  ? 65  TRP H CZ2 1 
ATOM   12307 C CZ3 . TRP H  1 73  ? 17.444  -10.557 22.833  1.00 20.37  ? 65  TRP H CZ3 1 
ATOM   12308 C CH2 . TRP H  1 73  ? 16.660  -11.083 21.794  1.00 20.73  ? 65  TRP H CH2 1 
ATOM   12309 N N   . ASN H  1 74  ? 16.105  -15.209 28.177  1.00 29.72  ? 66  ASN H N   1 
ATOM   12310 C CA  . ASN H  1 74  ? 15.588  -16.565 28.080  1.00 31.35  ? 66  ASN H CA  1 
ATOM   12311 C C   . ASN H  1 74  ? 14.559  -16.674 26.965  1.00 32.03  ? 66  ASN H C   1 
ATOM   12312 O O   . ASN H  1 74  ? 13.411  -16.271 27.130  1.00 33.95  ? 66  ASN H O   1 
ATOM   12313 C CB  . ASN H  1 74  ? 14.952  -16.964 29.413  1.00 39.83  ? 66  ASN H CB  1 
ATOM   12314 C CG  . ASN H  1 74  ? 14.654  -18.441 29.502  1.00 47.34  ? 66  ASN H CG  1 
ATOM   12315 O OD1 . ASN H  1 74  ? 14.357  -19.089 28.498  1.00 54.20  ? 66  ASN H OD1 1 
ATOM   12316 N ND2 . ASN H  1 74  ? 14.716  -18.982 30.714  1.00 54.56  ? 66  ASN H ND2 1 
ATOM   12317 N N   . SER H  1 75  ? 14.977  -17.230 25.834  1.00 33.45  ? 67  SER H N   1 
ATOM   12318 C CA  . SER H  1 75  ? 14.130  -17.312 24.645  1.00 35.36  ? 67  SER H CA  1 
ATOM   12319 C C   . SER H  1 75  ? 13.310  -18.597 24.565  1.00 35.27  ? 67  SER H C   1 
ATOM   12320 O O   . SER H  1 75  ? 12.839  -18.962 23.492  1.00 37.83  ? 67  SER H O   1 
ATOM   12321 C CB  . SER H  1 75  ? 14.982  -17.166 23.374  1.00 37.75  ? 67  SER H CB  1 
ATOM   12322 O OG  . SER H  1 75  ? 16.187  -17.911 23.464  1.00 33.81  ? 67  SER H OG  1 
ATOM   12323 N N   . SER H  1 76  ? 13.137  -19.269 25.700  1.00 36.77  ? 68  SER H N   1 
ATOM   12324 C CA  . SER H  1 76  ? 12.458  -20.568 25.745  1.00 37.71  ? 68  SER H CA  1 
ATOM   12325 C C   . SER H  1 76  ? 11.051  -20.592 25.138  1.00 43.63  ? 68  SER H C   1 
ATOM   12326 O O   . SER H  1 76  ? 10.625  -21.619 24.609  1.00 49.25  ? 68  SER H O   1 
ATOM   12327 C CB  . SER H  1 76  ? 12.421  -21.108 27.176  1.00 43.75  ? 68  SER H CB  1 
ATOM   12328 O OG  . SER H  1 76  ? 13.735  -21.320 27.664  1.00 52.63  ? 68  SER H OG  1 
ATOM   12329 N N   . HIS H  1 77  ? 10.342  -19.480 25.239  1.00 41.56  ? 69  HIS H N   1 
ATOM   12330 C CA  . HIS H  1 77  ? 9.032   -19.349 24.655  1.00 36.28  ? 69  HIS H CA  1 
ATOM   12331 C C   . HIS H  1 77  ? 8.823   -17.948 24.165  1.00 39.47  ? 69  HIS H C   1 
ATOM   12332 O O   . HIS H  1 77  ? 7.727   -17.473 24.108  1.00 40.05  ? 69  HIS H O   1 
ATOM   12333 C CB  . HIS H  1 77  ? 7.929   -19.696 25.628  1.00 40.34  ? 69  HIS H CB  1 
ATOM   12334 C CG  . HIS H  1 77  ? 8.111   -20.994 26.329  1.00 48.58  ? 69  HIS H CG  1 
ATOM   12335 N ND1 . HIS H  1 77  ? 7.562   -22.160 25.874  1.00 48.88  ? 69  HIS H ND1 1 
ATOM   12336 C CD2 . HIS H  1 77  ? 8.742   -21.304 27.480  1.00 45.99  ? 69  HIS H CD2 1 
ATOM   12337 C CE1 . HIS H  1 77  ? 7.881   -23.142 26.691  1.00 49.26  ? 69  HIS H CE1 1 
ATOM   12338 N NE2 . HIS H  1 77  ? 8.598   -22.648 27.673  1.00 45.84  ? 69  HIS H NE2 1 
ATOM   12339 N N   . SER H  1 78  ? 9.902   -17.294 23.791  1.00 39.80  ? 70  SER H N   1 
ATOM   12340 C CA  . SER H  1 78  ? 9.892   -15.952 23.225  1.00 35.65  ? 70  SER H CA  1 
ATOM   12341 C C   . SER H  1 78  ? 10.890  -15.919 22.060  1.00 37.53  ? 70  SER H C   1 
ATOM   12342 O O   . SER H  1 78  ? 11.775  -16.771 22.001  1.00 35.43  ? 70  SER H O   1 
ATOM   12343 C CB  . SER H  1 78  ? 10.281  -14.960 24.315  1.00 31.12  ? 70  SER H CB  1 
ATOM   12344 O OG  . SER H  1 78  ? 11.274  -15.522 25.150  1.00 34.36  ? 70  SER H OG  1 
ATOM   12345 N N   . PRO H  1 79  ? 10.748  -14.948 21.129  1.00 36.35  ? 71  PRO H N   1 
ATOM   12346 C CA  . PRO H  1 79  ? 11.567  -14.853 19.909  1.00 30.59  ? 71  PRO H CA  1 
ATOM   12347 C C   . PRO H  1 79  ? 13.070  -14.900 20.148  1.00 35.27  ? 71  PRO H C   1 
ATOM   12348 O O   . PRO H  1 79  ? 13.568  -14.256 21.072  1.00 35.68  ? 71  PRO H O   1 
ATOM   12349 C CB  . PRO H  1 79  ? 11.196  -13.480 19.350  1.00 29.05  ? 71  PRO H CB  1 
ATOM   12350 C CG  . PRO H  1 79  ? 9.823   -13.266 19.802  1.00 34.17  ? 71  PRO H CG  1 
ATOM   12351 C CD  . PRO H  1 79  ? 9.736   -13.879 21.174  1.00 34.72  ? 71  PRO H CD  1 
ATOM   12352 N N   . ASP H  1 80  ? 13.778  -15.639 19.299  1.00 35.96  ? 72  ASP H N   1 
ATOM   12353 C CA  . ASP H  1 80  ? 15.216  -15.839 19.448  1.00 31.98  ? 72  ASP H CA  1 
ATOM   12354 C C   . ASP H  1 80  ? 15.999  -14.580 19.122  1.00 28.74  ? 72  ASP H C   1 
ATOM   12355 O O   . ASP H  1 80  ? 17.099  -14.379 19.635  1.00 29.72  ? 72  ASP H O   1 
ATOM   12356 C CB  . ASP H  1 80  ? 15.701  -16.970 18.527  1.00 40.98  ? 72  ASP H CB  1 
ATOM   12357 C CG  . ASP H  1 80  ? 14.934  -18.270 18.733  1.00 53.79  ? 72  ASP H CG  1 
ATOM   12358 O OD1 . ASP H  1 80  ? 14.652  -18.628 19.906  1.00 51.84  ? 72  ASP H OD1 1 
ATOM   12359 O OD2 . ASP H  1 80  ? 14.614  -18.930 17.717  1.00 49.80  ? 72  ASP H OD2 1 
ATOM   12360 N N   . GLN H  1 81  ? 15.445  -13.742 18.251  1.00 26.89  ? 73  GLN H N   1 
ATOM   12361 C CA  . GLN H  1 81  ? 16.159  -12.545 17.805  1.00 29.68  ? 73  GLN H CA  1 
ATOM   12362 C C   . GLN H  1 81  ? 15.237  -11.467 17.233  1.00 24.98  ? 73  GLN H C   1 
ATOM   12363 O O   . GLN H  1 81  ? 14.140  -11.760 16.764  1.00 28.07  ? 73  GLN H O   1 
ATOM   12364 C CB  . GLN H  1 81  ? 17.239  -12.920 16.790  1.00 25.59  ? 73  GLN H CB  1 
ATOM   12365 C CG  . GLN H  1 81  ? 16.757  -13.862 15.708  1.00 28.50  ? 73  GLN H CG  1 
ATOM   12366 C CD  . GLN H  1 81  ? 17.844  -14.213 14.702  1.00 42.73  ? 73  GLN H CD  1 
ATOM   12367 O OE1 . GLN H  1 81  ? 19.003  -13.800 14.838  1.00 35.08  ? 73  GLN H OE1 1 
ATOM   12368 N NE2 . GLN H  1 81  ? 17.469  -14.977 13.677  1.00 53.56  ? 73  GLN H NE2 1 
ATOM   12369 N N   . VAL H  1 82  ? 15.677  -10.214 17.294  1.00 22.56  ? 74  VAL H N   1 
ATOM   12370 C CA  . VAL H  1 82  ? 14.902  -9.103  16.740  1.00 22.08  ? 74  VAL H CA  1 
ATOM   12371 C C   . VAL H  1 82  ? 15.846  -8.090  16.100  1.00 20.33  ? 74  VAL H C   1 
ATOM   12372 O O   . VAL H  1 82  ? 17.044  -8.095  16.365  1.00 20.61  ? 74  VAL H O   1 
ATOM   12373 C CB  . VAL H  1 82  ? 14.049  -8.364  17.819  1.00 22.31  ? 74  VAL H CB  1 
ATOM   12374 C CG1 . VAL H  1 82  ? 13.057  -9.297  18.487  1.00 18.89  ? 74  VAL H CG1 1 
ATOM   12375 C CG2 . VAL H  1 82  ? 14.942  -7.718  18.860  1.00 19.54  ? 74  VAL H CG2 1 
ATOM   12376 N N   . SER H  1 83  ? 15.296  -7.230  15.251  1.00 19.94  ? 75  SER H N   1 
ATOM   12377 C CA  . SER H  1 83  ? 16.030  -6.088  14.714  1.00 20.36  ? 75  SER H CA  1 
ATOM   12378 C C   . SER H  1 83  ? 15.882  -4.851  15.607  1.00 22.60  ? 75  SER H C   1 
ATOM   12379 O O   . SER H  1 83  ? 14.784  -4.544  16.089  1.00 20.88  ? 75  SER H O   1 
ATOM   12380 C CB  . SER H  1 83  ? 15.532  -5.759  13.312  1.00 20.11  ? 75  SER H CB  1 
ATOM   12381 O OG  . SER H  1 83  ? 15.499  -6.926  12.517  1.00 26.49  ? 75  SER H OG  1 
ATOM   12382 N N   . VAL H  1 84  ? 16.991  -4.143  15.813  1.00 19.18  ? 76  VAL H N   1 
ATOM   12383 C CA  . VAL H  1 84  ? 17.029  -2.967  16.677  1.00 18.39  ? 76  VAL H CA  1 
ATOM   12384 C C   . VAL H  1 84  ? 17.773  -1.843  15.959  1.00 18.97  ? 76  VAL H C   1 
ATOM   12385 O O   . VAL H  1 84  ? 18.855  -2.078  15.430  1.00 18.68  ? 76  VAL H O   1 
ATOM   12386 C CB  . VAL H  1 84  ? 17.813  -3.284  17.964  1.00 16.28  ? 76  VAL H CB  1 
ATOM   12387 C CG1 . VAL H  1 84  ? 17.899  -2.075  18.857  1.00 14.26  ? 76  VAL H CG1 1 
ATOM   12388 C CG2 . VAL H  1 84  ? 17.212  -4.465  18.683  1.00 14.57  ? 76  VAL H CG2 1 
ATOM   12389 N N   . PRO H  1 85  ? 17.212  -0.614  15.951  1.00 21.74  ? 77  PRO H N   1 
ATOM   12390 C CA  . PRO H  1 85  ? 17.922  0.540   15.373  1.00 17.71  ? 77  PRO H CA  1 
ATOM   12391 C C   . PRO H  1 85  ? 19.252  0.753   16.088  1.00 17.76  ? 77  PRO H C   1 
ATOM   12392 O O   . PRO H  1 85  ? 19.305  0.637   17.313  1.00 21.15  ? 77  PRO H O   1 
ATOM   12393 C CB  . PRO H  1 85  ? 16.988  1.718   15.674  1.00 14.30  ? 77  PRO H CB  1 
ATOM   12394 C CG  . PRO H  1 85  ? 15.662  1.120   15.926  1.00 14.13  ? 77  PRO H CG  1 
ATOM   12395 C CD  . PRO H  1 85  ? 15.930  -0.216  16.558  1.00 18.57  ? 77  PRO H CD  1 
ATOM   12396 N N   . ILE H  1 86  ? 20.307  1.068   15.344  1.00 21.98  ? 78  ILE H N   1 
ATOM   12397 C CA  . ILE H  1 86  ? 21.662  1.085   15.909  1.00 18.84  ? 78  ILE H CA  1 
ATOM   12398 C C   . ILE H  1 86  ? 21.926  2.240   16.881  1.00 17.46  ? 78  ILE H C   1 
ATOM   12399 O O   . ILE H  1 86  ? 22.904  2.227   17.625  1.00 20.35  ? 78  ILE H O   1 
ATOM   12400 C CB  . ILE H  1 86  ? 22.763  0.997   14.805  1.00 17.28  ? 78  ILE H CB  1 
ATOM   12401 C CG1 . ILE H  1 86  ? 22.561  2.049   13.717  1.00 17.42  ? 78  ILE H CG1 1 
ATOM   12402 C CG2 . ILE H  1 86  ? 22.793  -0.395  14.183  1.00 13.98  ? 78  ILE H CG2 1 
ATOM   12403 C CD1 . ILE H  1 86  ? 23.764  2.162   12.760  1.00 15.12  ? 78  ILE H CD1 1 
ATOM   12404 N N   . SER H  1 87  ? 21.041  3.225   16.888  1.00 17.37  ? 79  SER H N   1 
ATOM   12405 C CA  . SER H  1 87  ? 21.127  4.317   17.845  1.00 16.41  ? 79  SER H CA  1 
ATOM   12406 C C   . SER H  1 87  ? 20.651  3.905   19.248  1.00 23.12  ? 79  SER H C   1 
ATOM   12407 O O   . SER H  1 87  ? 20.776  4.674   20.205  1.00 26.56  ? 79  SER H O   1 
ATOM   12408 C CB  . SER H  1 87  ? 20.300  5.491   17.341  1.00 21.78  ? 79  SER H CB  1 
ATOM   12409 O OG  . SER H  1 87  ? 18.989  5.060   17.013  1.00 25.62  ? 79  SER H OG  1 
ATOM   12410 N N   . SER H  1 88  ? 20.097  2.702   19.375  1.00 17.95  ? 80  SER H N   1 
ATOM   12411 C CA  . SER H  1 88  ? 19.772  2.165   20.689  1.00 19.08  ? 80  SER H CA  1 
ATOM   12412 C C   . SER H  1 88  ? 20.858  1.188   21.155  1.00 19.84  ? 80  SER H C   1 
ATOM   12413 O O   . SER H  1 88  ? 20.821  0.673   22.274  1.00 16.37  ? 80  SER H O   1 
ATOM   12414 C CB  . SER H  1 88  ? 18.402  1.477   20.680  1.00 23.34  ? 80  SER H CB  1 
ATOM   12415 O OG  . SER H  1 88  ? 17.378  2.356   20.254  1.00 23.25  ? 80  SER H OG  1 
ATOM   12416 N N   . LEU H  1 89  ? 21.831  0.937   20.289  1.00 19.41  ? 81  LEU H N   1 
ATOM   12417 C CA  . LEU H  1 89  ? 22.928  0.042   20.622  1.00 17.01  ? 81  LEU H CA  1 
ATOM   12418 C C   . LEU H  1 89  ? 24.274  0.739   20.581  1.00 18.75  ? 81  LEU H C   1 
ATOM   12419 O O   . LEU H  1 89  ? 24.457  1.731   19.877  1.00 18.41  ? 81  LEU H O   1 
ATOM   12420 C CB  . LEU H  1 89  ? 22.960  -1.117  19.640  1.00 20.60  ? 81  LEU H CB  1 
ATOM   12421 C CG  . LEU H  1 89  ? 21.824  -2.102  19.820  1.00 20.76  ? 81  LEU H CG  1 
ATOM   12422 C CD1 . LEU H  1 89  ? 22.014  -3.274  18.892  1.00 13.64  ? 81  LEU H CD1 1 
ATOM   12423 C CD2 . LEU H  1 89  ? 21.807  -2.537  21.274  1.00 20.94  ? 81  LEU H CD2 1 
ATOM   12424 N N   . TRP H  1 90  ? 25.219  0.216   21.350  1.00 22.00  ? 82  TRP H N   1 
ATOM   12425 C CA  . TRP H  1 90  ? 26.609  0.527   21.095  1.00 21.37  ? 82  TRP H CA  1 
ATOM   12426 C C   . TRP H  1 90  ? 27.015  -0.247  19.851  1.00 22.00  ? 82  TRP H C   1 
ATOM   12427 O O   . TRP H  1 90  ? 26.693  -1.433  19.717  1.00 19.65  ? 82  TRP H O   1 
ATOM   12428 C CB  . TRP H  1 90  ? 27.502  0.130   22.272  1.00 17.29  ? 82  TRP H CB  1 
ATOM   12429 C CG  . TRP H  1 90  ? 28.975  0.318   21.985  1.00 23.82  ? 82  TRP H CG  1 
ATOM   12430 C CD1 . TRP H  1 90  ? 29.710  1.462   22.159  1.00 24.91  ? 82  TRP H CD1 1 
ATOM   12431 C CD2 . TRP H  1 90  ? 29.883  -0.661  21.460  1.00 23.34  ? 82  TRP H CD2 1 
ATOM   12432 N NE1 . TRP H  1 90  ? 31.016  1.250   21.780  1.00 22.88  ? 82  TRP H NE1 1 
ATOM   12433 C CE2 . TRP H  1 90  ? 31.148  -0.046  21.356  1.00 20.98  ? 82  TRP H CE2 1 
ATOM   12434 C CE3 . TRP H  1 90  ? 29.751  -2.000  21.080  1.00 24.17  ? 82  TRP H CE3 1 
ATOM   12435 C CZ2 . TRP H  1 90  ? 32.268  -0.725  20.891  1.00 21.17  ? 82  TRP H CZ2 1 
ATOM   12436 C CZ3 . TRP H  1 90  ? 30.870  -2.670  20.616  1.00 22.94  ? 82  TRP H CZ3 1 
ATOM   12437 C CH2 . TRP H  1 90  ? 32.109  -2.031  20.525  1.00 19.76  ? 82  TRP H CH2 1 
ATOM   12438 N N   . VAL H  1 91  ? 27.688  0.436   18.931  1.00 21.30  ? 83  VAL H N   1 
ATOM   12439 C CA  . VAL H  1 91  ? 28.319  -0.214  17.792  1.00 18.47  ? 83  VAL H CA  1 
ATOM   12440 C C   . VAL H  1 91  ? 29.768  0.231   17.785  1.00 20.84  ? 83  VAL H C   1 
ATOM   12441 O O   . VAL H  1 91  ? 30.072  1.361   18.178  1.00 22.73  ? 83  VAL H O   1 
ATOM   12442 C CB  . VAL H  1 91  ? 27.649  0.135   16.443  1.00 17.89  ? 83  VAL H CB  1 
ATOM   12443 C CG1 . VAL H  1 91  ? 26.162  -0.186  16.471  1.00 15.50  ? 83  VAL H CG1 1 
ATOM   12444 C CG2 . VAL H  1 91  ? 27.878  1.590   16.077  1.00 20.67  ? 83  VAL H CG2 1 
ATOM   12445 N N   . PRO H  1 92  ? 30.681  -0.669  17.394  1.00 18.16  ? 84  PRO H N   1 
ATOM   12446 C CA  . PRO H  1 92  ? 32.102  -0.306  17.451  1.00 18.74  ? 84  PRO H CA  1 
ATOM   12447 C C   . PRO H  1 92  ? 32.477  0.824   16.483  1.00 17.31  ? 84  PRO H C   1 
ATOM   12448 O O   . PRO H  1 92  ? 31.913  0.903   15.399  1.00 17.44  ? 84  PRO H O   1 
ATOM   12449 C CB  . PRO H  1 92  ? 32.823  -1.621  17.118  1.00 21.32  ? 84  PRO H CB  1 
ATOM   12450 C CG  . PRO H  1 92  ? 31.757  -2.601  16.727  1.00 18.73  ? 84  PRO H CG  1 
ATOM   12451 C CD  . PRO H  1 92  ? 30.470  -2.119  17.258  1.00 16.76  ? 84  PRO H CD  1 
ATOM   12452 N N   . ASP H  1 93  ? 33.407  1.685   16.894  1.00 13.80  ? 85  ASP H N   1 
ATOM   12453 C CA  . ASP H  1 93  ? 33.771  2.884   16.140  1.00 16.11  ? 85  ASP H CA  1 
ATOM   12454 C C   . ASP H  1 93  ? 34.790  2.617   15.018  1.00 19.94  ? 85  ASP H C   1 
ATOM   12455 O O   . ASP H  1 93  ? 35.925  3.101   15.057  1.00 17.15  ? 85  ASP H O   1 
ATOM   12456 C CB  . ASP H  1 93  ? 34.291  3.968   17.098  1.00 15.16  ? 85  ASP H CB  1 
ATOM   12457 C CG  . ASP H  1 93  ? 35.576  3.561   17.824  1.00 21.23  ? 85  ASP H CG  1 
ATOM   12458 O OD1 . ASP H  1 93  ? 35.758  2.355   18.102  1.00 20.47  ? 85  ASP H OD1 1 
ATOM   12459 O OD2 . ASP H  1 93  ? 36.418  4.452   18.101  1.00 21.59  ? 85  ASP H OD2 1 
ATOM   12460 N N   . LEU H  1 94  ? 34.375  1.852   14.012  1.00 20.48  ? 86  LEU H N   1 
ATOM   12461 C CA  . LEU H  1 94  ? 35.305  1.372   12.993  1.00 20.44  ? 86  LEU H CA  1 
ATOM   12462 C C   . LEU H  1 94  ? 35.691  2.441   11.972  1.00 20.76  ? 86  LEU H C   1 
ATOM   12463 O O   . LEU H  1 94  ? 34.926  3.359   11.687  1.00 26.05  ? 86  LEU H O   1 
ATOM   12464 C CB  . LEU H  1 94  ? 34.735  0.147   12.288  1.00 21.42  ? 86  LEU H CB  1 
ATOM   12465 C CG  . LEU H  1 94  ? 34.490  -1.103  13.138  1.00 16.49  ? 86  LEU H CG  1 
ATOM   12466 C CD1 . LEU H  1 94  ? 33.954  -2.208  12.258  1.00 19.24  ? 86  LEU H CD1 1 
ATOM   12467 C CD2 . LEU H  1 94  ? 35.750  -1.559  13.845  1.00 17.15  ? 86  LEU H CD2 1 
ATOM   12468 N N   . ALA H  1 95  ? 36.900  2.331   11.442  1.00 24.06  ? 87  ALA H N   1 
ATOM   12469 C CA  . ALA H  1 95  ? 37.343  3.233   10.381  1.00 27.48  ? 87  ALA H CA  1 
ATOM   12470 C C   . ALA H  1 95  ? 38.312  2.547   9.428   1.00 24.27  ? 87  ALA H C   1 
ATOM   12471 O O   . ALA H  1 95  ? 38.968  1.576   9.775   1.00 28.91  ? 87  ALA H O   1 
ATOM   12472 C CB  . ALA H  1 95  ? 37.970  4.492   10.958  1.00 21.55  ? 87  ALA H CB  1 
ATOM   12473 N N   . ALA H  1 96  ? 38.382  3.058   8.213   1.00 31.48  ? 88  ALA H N   1 
ATOM   12474 C CA  . ALA H  1 96  ? 39.368  2.611   7.258   1.00 24.99  ? 88  ALA H CA  1 
ATOM   12475 C C   . ALA H  1 96  ? 40.380  3.732   7.145   1.00 26.65  ? 88  ALA H C   1 
ATOM   12476 O O   . ALA H  1 96  ? 40.017  4.878   6.853   1.00 22.93  ? 88  ALA H O   1 
ATOM   12477 C CB  . ALA H  1 96  ? 38.718  2.322   5.925   1.00 22.38  ? 88  ALA H CB  1 
ATOM   12478 N N   . TYR H  1 97  ? 41.643  3.394   7.403   1.00 30.61  ? 89  TYR H N   1 
ATOM   12479 C CA  . TYR H  1 97  ? 42.737  4.362   7.428   1.00 27.02  ? 89  TYR H CA  1 
ATOM   12480 C C   . TYR H  1 97  ? 43.025  4.915   6.035   1.00 28.66  ? 89  TYR H C   1 
ATOM   12481 O O   . TYR H  1 97  ? 43.337  6.106   5.864   1.00 25.53  ? 89  TYR H O   1 
ATOM   12482 C CB  . TYR H  1 97  ? 44.005  3.717   7.994   1.00 34.39  ? 89  TYR H CB  1 
ATOM   12483 C CG  . TYR H  1 97  ? 43.818  2.997   9.317   1.00 45.32  ? 89  TYR H CG  1 
ATOM   12484 C CD1 . TYR H  1 97  ? 44.155  3.600   10.523  1.00 40.82  ? 89  TYR H CD1 1 
ATOM   12485 C CD2 . TYR H  1 97  ? 43.318  1.703   9.356   1.00 45.10  ? 89  TYR H CD2 1 
ATOM   12486 C CE1 . TYR H  1 97  ? 43.984  2.931   11.727  1.00 42.03  ? 89  TYR H CE1 1 
ATOM   12487 C CE2 . TYR H  1 97  ? 43.142  1.032   10.551  1.00 45.33  ? 89  TYR H CE2 1 
ATOM   12488 C CZ  . TYR H  1 97  ? 43.473  1.643   11.736  1.00 47.66  ? 89  TYR H CZ  1 
ATOM   12489 O OH  . TYR H  1 97  ? 43.288  0.949   12.927  1.00 44.09  ? 89  TYR H OH  1 
ATOM   12490 N N   . ASN H  1 98  ? 42.921  4.048   5.034   1.00 26.19  ? 90  ASN H N   1 
ATOM   12491 C CA  . ASN H  1 98  ? 43.179  4.474   3.665   1.00 30.31  ? 90  ASN H CA  1 
ATOM   12492 C C   . ASN H  1 98  ? 41.910  4.885   2.925   1.00 33.52  ? 90  ASN H C   1 
ATOM   12493 O O   . ASN H  1 98  ? 41.930  5.089   1.711   1.00 37.11  ? 90  ASN H O   1 
ATOM   12494 C CB  . ASN H  1 98  ? 43.951  3.403   2.884   1.00 26.53  ? 90  ASN H CB  1 
ATOM   12495 C CG  . ASN H  1 98  ? 43.336  2.035   3.008   1.00 30.07  ? 90  ASN H CG  1 
ATOM   12496 O OD1 . ASN H  1 98  ? 42.714  1.704   4.023   1.00 39.54  ? 90  ASN H OD1 1 
ATOM   12497 N ND2 . ASN H  1 98  ? 43.498  1.227   1.978   1.00 26.18  ? 90  ASN H ND2 1 
ATOM   12498 N N   . ALA H  1 99  ? 40.807  5.014   3.652   1.00 26.14  ? 91  ALA H N   1 
ATOM   12499 C CA  . ALA H  1 99  ? 39.572  5.443   3.021   1.00 26.67  ? 91  ALA H CA  1 
ATOM   12500 C C   . ALA H  1 99  ? 39.673  6.904   2.604   1.00 25.11  ? 91  ALA H C   1 
ATOM   12501 O O   . ALA H  1 99  ? 40.102  7.743   3.385   1.00 28.43  ? 91  ALA H O   1 
ATOM   12502 C CB  . ALA H  1 99  ? 38.416  5.239   3.954   1.00 23.43  ? 91  ALA H CB  1 
ATOM   12503 N N   . ILE H  1 100 ? 39.275  7.219   1.377   1.00 23.40  ? 92  ILE H N   1 
ATOM   12504 C CA  . ILE H  1 100 ? 39.400  8.593   0.912   1.00 24.71  ? 92  ILE H CA  1 
ATOM   12505 C C   . ILE H  1 100 ? 38.067  9.279   0.627   1.00 27.39  ? 92  ILE H C   1 
ATOM   12506 O O   . ILE H  1 100 ? 38.019  10.316  -0.042  1.00 27.70  ? 92  ILE H O   1 
ATOM   12507 C CB  . ILE H  1 100 ? 40.324  8.683   -0.299  1.00 31.41  ? 92  ILE H CB  1 
ATOM   12508 C CG1 . ILE H  1 100 ? 39.866  7.696   -1.384  1.00 37.55  ? 92  ILE H CG1 1 
ATOM   12509 C CG2 . ILE H  1 100 ? 41.758  8.398   0.138   1.00 26.74  ? 92  ILE H CG2 1 
ATOM   12510 C CD1 . ILE H  1 100 ? 40.553  7.869   -2.743  1.00 31.49  ? 92  ILE H CD1 1 
ATOM   12511 N N   . SER H  1 101 ? 36.991  8.700   1.157   1.00 27.07  ? 93  SER H N   1 
ATOM   12512 C CA  . SER H  1 101 ? 35.658  9.292   1.093   1.00 20.17  ? 93  SER H CA  1 
ATOM   12513 C C   . SER H  1 101 ? 34.837  8.686   2.206   1.00 21.65  ? 93  SER H C   1 
ATOM   12514 O O   . SER H  1 101 ? 35.135  7.562   2.641   1.00 16.83  ? 93  SER H O   1 
ATOM   12515 C CB  . SER H  1 101 ? 34.990  8.966   -0.234  1.00 22.32  ? 93  SER H CB  1 
ATOM   12516 O OG  . SER H  1 101 ? 34.559  7.609   -0.261  1.00 20.69  ? 93  SER H OG  1 
ATOM   12517 N N   . LYS H  1 102 ? 33.802  9.416   2.645   1.00 25.57  ? 94  LYS H N   1 
ATOM   12518 C CA  . LYS H  1 102 ? 32.905  8.960   3.716   1.00 19.96  ? 94  LYS H CA  1 
ATOM   12519 C C   . LYS H  1 102 ? 32.354  7.603   3.335   1.00 19.61  ? 94  LYS H C   1 
ATOM   12520 O O   . LYS H  1 102 ? 32.171  7.321   2.163   1.00 21.73  ? 94  LYS H O   1 
ATOM   12521 C CB  . LYS H  1 102 ? 31.728  9.921   3.895   1.00 16.30  ? 94  LYS H CB  1 
ATOM   12522 C CG  . LYS H  1 102 ? 31.935  11.051  4.880   1.00 21.04  ? 94  LYS H CG  1 
ATOM   12523 C CD  . LYS H  1 102 ? 30.735  12.002  4.896   1.00 23.50  ? 94  LYS H CD  1 
ATOM   12524 C CE  . LYS H  1 102 ? 30.615  12.791  6.206   1.00 28.71  ? 94  LYS H CE  1 
ATOM   12525 N NZ  . LYS H  1 102 ? 29.826  12.088  7.282   1.00 32.04  ? 94  LYS H NZ  1 
ATOM   12526 N N   . PRO H  1 103 ? 32.102  6.741   4.315   1.00 21.12  ? 95  PRO H N   1 
ATOM   12527 C CA  . PRO H  1 103 ? 31.393  5.539   3.872   1.00 20.07  ? 95  PRO H CA  1 
ATOM   12528 C C   . PRO H  1 103 ? 29.928  5.878   3.550   1.00 25.78  ? 95  PRO H C   1 
ATOM   12529 O O   . PRO H  1 103 ? 29.281  6.587   4.319   1.00 31.69  ? 95  PRO H O   1 
ATOM   12530 C CB  . PRO H  1 103 ? 31.516  4.594   5.078   1.00 20.61  ? 95  PRO H CB  1 
ATOM   12531 C CG  . PRO H  1 103 ? 31.848  5.469   6.239   1.00 13.29  ? 95  PRO H CG  1 
ATOM   12532 C CD  . PRO H  1 103 ? 32.584  6.648   5.702   1.00 16.29  ? 95  PRO H CD  1 
ATOM   12533 N N   . GLU H  1 104 ? 29.437  5.413   2.406   1.00 25.12  ? 96  GLU H N   1 
ATOM   12534 C CA  . GLU H  1 104 ? 28.055  5.623   1.987   1.00 22.63  ? 96  GLU H CA  1 
ATOM   12535 C C   . GLU H  1 104 ? 27.302  4.337   2.339   1.00 23.39  ? 96  GLU H C   1 
ATOM   12536 O O   . GLU H  1 104 ? 27.524  3.305   1.718   1.00 25.16  ? 96  GLU H O   1 
ATOM   12537 C CB  . GLU H  1 104 ? 28.004  5.907   0.472   1.00 24.97  ? 96  GLU H CB  1 
ATOM   12538 C CG  . GLU H  1 104 ? 26.640  6.355   -0.114  1.00 32.66  ? 96  GLU H CG  1 
ATOM   12539 C CD  . GLU H  1 104 ? 26.661  6.564   -1.660  1.00 42.77  ? 96  GLU H CD  1 
ATOM   12540 O OE1 . GLU H  1 104 ? 27.637  6.142   -2.331  1.00 45.60  ? 96  GLU H OE1 1 
ATOM   12541 O OE2 . GLU H  1 104 ? 25.696  7.149   -2.211  1.00 35.29  ? 96  GLU H OE2 1 
ATOM   12542 N N   . VAL H  1 105 ? 26.447  4.383   3.361   1.00 24.04  ? 97  VAL H N   1 
ATOM   12543 C CA  . VAL H  1 105 ? 25.722  3.190   3.795   1.00 18.74  ? 97  VAL H CA  1 
ATOM   12544 C C   . VAL H  1 105 ? 24.459  3.037   2.974   1.00 22.50  ? 97  VAL H C   1 
ATOM   12545 O O   . VAL H  1 105 ? 23.591  3.909   2.986   1.00 27.09  ? 97  VAL H O   1 
ATOM   12546 C CB  . VAL H  1 105 ? 25.371  3.234   5.300   1.00 22.30  ? 97  VAL H CB  1 
ATOM   12547 C CG1 . VAL H  1 105 ? 24.364  2.141   5.658   1.00 21.20  ? 97  VAL H CG1 1 
ATOM   12548 C CG2 . VAL H  1 105 ? 26.619  3.091   6.141   1.00 18.85  ? 97  VAL H CG2 1 
ATOM   12549 N N   . LEU H  1 106 ? 24.364  1.922   2.258   1.00 25.43  ? 98  LEU H N   1 
ATOM   12550 C CA  . LEU H  1 106 ? 23.308  1.707   1.272   1.00 22.22  ? 98  LEU H CA  1 
ATOM   12551 C C   . LEU H  1 106 ? 22.044  1.077   1.887   1.00 28.56  ? 98  LEU H C   1 
ATOM   12552 O O   . LEU H  1 106 ? 20.942  1.231   1.360   1.00 32.46  ? 98  LEU H O   1 
ATOM   12553 C CB  . LEU H  1 106 ? 23.843  0.821   0.147   1.00 18.67  ? 98  LEU H CB  1 
ATOM   12554 C CG  . LEU H  1 106 ? 25.054  1.281   -0.674  1.00 17.42  ? 98  LEU H CG  1 
ATOM   12555 C CD1 . LEU H  1 106 ? 25.397  0.233   -1.688  1.00 20.13  ? 98  LEU H CD1 1 
ATOM   12556 C CD2 . LEU H  1 106 ? 24.807  2.592   -1.382  1.00 17.72  ? 98  LEU H CD2 1 
ATOM   12557 N N   . THR H  1 107 ? 22.215  0.386   3.010   1.00 20.72  ? 99  THR H N   1 
ATOM   12558 C CA  . THR H  1 107 ? 21.154  -0.390  3.625   1.00 22.87  ? 99  THR H CA  1 
ATOM   12559 C C   . THR H  1 107 ? 20.489  0.331   4.828   1.00 30.46  ? 99  THR H C   1 
ATOM   12560 O O   . THR H  1 107 ? 20.988  1.365   5.295   1.00 23.66  ? 99  THR H O   1 
ATOM   12561 C CB  . THR H  1 107 ? 21.708  -1.761  4.062   1.00 23.18  ? 99  THR H CB  1 
ATOM   12562 O OG1 . THR H  1 107 ? 23.031  -1.593  4.572   1.00 27.77  ? 99  THR H OG1 1 
ATOM   12563 C CG2 . THR H  1 107 ? 21.771  -2.690  2.892   1.00 26.18  ? 99  THR H CG2 1 
ATOM   12564 N N   . PRO H  1 108 ? 19.338  -0.198  5.308   1.00 26.80  ? 100 PRO H N   1 
ATOM   12565 C CA  . PRO H  1 108 ? 18.719  0.343   6.516   1.00 22.27  ? 100 PRO H CA  1 
ATOM   12566 C C   . PRO H  1 108 ? 19.644  0.145   7.684   1.00 20.87  ? 100 PRO H C   1 
ATOM   12567 O O   . PRO H  1 108 ? 20.219  -0.930  7.807   1.00 24.03  ? 100 PRO H O   1 
ATOM   12568 C CB  . PRO H  1 108 ? 17.488  -0.544  6.698   1.00 24.44  ? 100 PRO H CB  1 
ATOM   12569 C CG  . PRO H  1 108 ? 17.145  -0.976  5.340   1.00 29.61  ? 100 PRO H CG  1 
ATOM   12570 C CD  . PRO H  1 108 ? 18.456  -1.184  4.657   1.00 28.22  ? 100 PRO H CD  1 
ATOM   12571 N N   . GLN H  1 109 ? 19.784  1.160   8.526   1.00 19.11  ? 101 GLN H N   1 
ATOM   12572 C CA  . GLN H  1 109 ? 20.680  1.087   9.675   1.00 18.41  ? 101 GLN H CA  1 
ATOM   12573 C C   . GLN H  1 109 ? 20.099  0.278   10.871  1.00 21.41  ? 101 GLN H C   1 
ATOM   12574 O O   . GLN H  1 109 ? 19.734  0.841   11.912  1.00 16.12  ? 101 GLN H O   1 
ATOM   12575 C CB  . GLN H  1 109 ? 21.071  2.503   10.095  1.00 18.42  ? 101 GLN H CB  1 
ATOM   12576 C CG  . GLN H  1 109 ? 21.981  3.233   9.119   1.00 16.64  ? 101 GLN H CG  1 
ATOM   12577 C CD  . GLN H  1 109 ? 23.435  2.792   9.246   1.00 29.63  ? 101 GLN H CD  1 
ATOM   12578 O OE1 . GLN H  1 109 ? 23.729  1.601   9.411   1.00 29.71  ? 101 GLN H OE1 1 
ATOM   12579 N NE2 . GLN H  1 109 ? 24.353  3.753   9.189   1.00 30.26  ? 101 GLN H NE2 1 
ATOM   12580 N N   . LEU H  1 110 ? 20.033  -1.043  10.706  1.00 20.16  ? 102 LEU H N   1 
ATOM   12581 C CA  . LEU H  1 110 ? 19.463  -1.940  11.710  1.00 19.63  ? 102 LEU H CA  1 
ATOM   12582 C C   . LEU H  1 110 ? 20.426  -3.061  12.066  1.00 21.44  ? 102 LEU H C   1 
ATOM   12583 O O   . LEU H  1 110 ? 21.071  -3.631  11.193  1.00 26.87  ? 102 LEU H O   1 
ATOM   12584 C CB  . LEU H  1 110 ? 18.176  -2.579  11.188  1.00 15.32  ? 102 LEU H CB  1 
ATOM   12585 C CG  . LEU H  1 110 ? 17.018  -1.663  10.842  1.00 17.31  ? 102 LEU H CG  1 
ATOM   12586 C CD1 . LEU H  1 110 ? 15.764  -2.495  10.669  1.00 24.35  ? 102 LEU H CD1 1 
ATOM   12587 C CD2 . LEU H  1 110 ? 16.829  -0.670  11.958  1.00 24.97  ? 102 LEU H CD2 1 
ATOM   12588 N N   . ALA H  1 111 ? 20.501  -3.401  13.347  1.00 22.43  ? 103 ALA H N   1 
ATOM   12589 C CA  . ALA H  1 111 ? 21.304  -4.532  13.794  1.00 20.29  ? 103 ALA H CA  1 
ATOM   12590 C C   . ALA H  1 111 ? 20.367  -5.647  14.220  1.00 17.78  ? 103 ALA H C   1 
ATOM   12591 O O   . ALA H  1 111 ? 19.169  -5.440  14.321  1.00 18.38  ? 103 ALA H O   1 
ATOM   12592 C CB  . ALA H  1 111 ? 22.221  -4.121  14.963  1.00 14.62  ? 103 ALA H CB  1 
ATOM   12593 N N   . ARG H  1 112 ? 20.913  -6.830  14.459  1.00 19.69  ? 104 ARG H N   1 
ATOM   12594 C CA  . ARG H  1 112 ? 20.132  -7.917  15.016  1.00 20.29  ? 104 ARG H CA  1 
ATOM   12595 C C   . ARG H  1 112 ? 20.705  -8.206  16.379  1.00 19.31  ? 104 ARG H C   1 
ATOM   12596 O O   . ARG H  1 112 ? 21.889  -8.017  16.609  1.00 22.26  ? 104 ARG H O   1 
ATOM   12597 C CB  . ARG H  1 112 ? 20.202  -9.175  14.142  1.00 24.35  ? 104 ARG H CB  1 
ATOM   12598 C CG  . ARG H  1 112 ? 19.606  -9.010  12.757  1.00 25.74  ? 104 ARG H CG  1 
ATOM   12599 C CD  . ARG H  1 112 ? 18.072  -8.985  12.777  1.00 22.11  ? 104 ARG H CD  1 
ATOM   12600 N NE  . ARG H  1 112 ? 17.488  -10.275 13.143  1.00 25.13  ? 104 ARG H NE  1 
ATOM   12601 C CZ  . ARG H  1 112 ? 16.207  -10.591 12.959  1.00 27.39  ? 104 ARG H CZ  1 
ATOM   12602 N NH1 . ARG H  1 112 ? 15.381  -9.711  12.414  1.00 26.62  ? 104 ARG H NH1 1 
ATOM   12603 N NH2 . ARG H  1 112 ? 15.744  -11.783 13.317  1.00 27.78  ? 104 ARG H NH2 1 
ATOM   12604 N N   . VAL H  1 113 ? 19.856  -8.638  17.296  1.00 20.01  ? 105 VAL H N   1 
ATOM   12605 C CA  . VAL H  1 113 ? 20.303  -8.979  18.625  1.00 20.12  ? 105 VAL H CA  1 
ATOM   12606 C C   . VAL H  1 113 ? 19.698  -10.335 18.942  1.00 25.94  ? 105 VAL H C   1 
ATOM   12607 O O   . VAL H  1 113 ? 18.478  -10.501 18.927  1.00 27.12  ? 105 VAL H O   1 
ATOM   12608 C CB  . VAL H  1 113 ? 19.885  -7.910  19.651  1.00 18.12  ? 105 VAL H CB  1 
ATOM   12609 C CG1 . VAL H  1 113 ? 20.454  -8.221  20.999  1.00 16.51  ? 105 VAL H CG1 1 
ATOM   12610 C CG2 . VAL H  1 113 ? 20.353  -6.526  19.200  1.00 14.92  ? 105 VAL H CG2 1 
ATOM   12611 N N   . VAL H  1 114 ? 20.563  -11.316 19.168  1.00 27.09  ? 106 VAL H N   1 
ATOM   12612 C CA  . VAL H  1 114 ? 20.130  -12.679 19.440  1.00 28.40  ? 106 VAL H CA  1 
ATOM   12613 C C   . VAL H  1 114 ? 20.039  -12.801 20.949  1.00 25.00  ? 106 VAL H C   1 
ATOM   12614 O O   . VAL H  1 114 ? 20.696  -12.047 21.654  1.00 23.24  ? 106 VAL H O   1 
ATOM   12615 C CB  . VAL H  1 114 ? 21.145  -13.709 18.873  1.00 29.46  ? 106 VAL H CB  1 
ATOM   12616 C CG1 . VAL H  1 114 ? 20.584  -15.112 18.943  1.00 27.12  ? 106 VAL H CG1 1 
ATOM   12617 C CG2 . VAL H  1 114 ? 21.498  -13.367 17.433  1.00 27.21  ? 106 VAL H CG2 1 
ATOM   12618 N N   . SER H  1 115 ? 19.236  -13.735 21.452  1.00 25.47  ? 107 SER H N   1 
ATOM   12619 C CA  . SER H  1 115 ? 19.039  -13.845 22.890  1.00 23.02  ? 107 SER H CA  1 
ATOM   12620 C C   . SER H  1 115 ? 20.278  -14.351 23.638  1.00 28.41  ? 107 SER H C   1 
ATOM   12621 O O   . SER H  1 115 ? 20.309  -14.334 24.871  1.00 30.92  ? 107 SER H O   1 
ATOM   12622 C CB  . SER H  1 115 ? 17.804  -14.682 23.212  1.00 23.88  ? 107 SER H CB  1 
ATOM   12623 O OG  . SER H  1 115 ? 18.007  -16.047 22.939  1.00 30.45  ? 107 SER H OG  1 
ATOM   12624 N N   . ASP H  1 116 ? 21.285  -14.793 22.881  1.00 31.28  ? 108 ASP H N   1 
ATOM   12625 C CA  . ASP H  1 116 ? 22.625  -15.104 23.397  1.00 33.61  ? 108 ASP H CA  1 
ATOM   12626 C C   . ASP H  1 116 ? 23.198  -13.895 24.095  1.00 30.04  ? 108 ASP H C   1 
ATOM   12627 O O   . ASP H  1 116 ? 23.824  -14.008 25.144  1.00 36.96  ? 108 ASP H O   1 
ATOM   12628 C CB  . ASP H  1 116 ? 23.615  -15.390 22.253  1.00 31.56  ? 108 ASP H CB  1 
ATOM   12629 C CG  . ASP H  1 116 ? 23.126  -16.431 21.284  1.00 41.98  ? 108 ASP H CG  1 
ATOM   12630 O OD1 . ASP H  1 116 ? 21.937  -16.816 21.345  1.00 47.27  ? 108 ASP H OD1 1 
ATOM   12631 O OD2 . ASP H  1 116 ? 23.945  -16.860 20.438  1.00 62.69  ? 108 ASP H OD2 1 
ATOM   12632 N N   . GLY H  1 117 ? 23.010  -12.743 23.459  1.00 26.07  ? 109 GLY H N   1 
ATOM   12633 C CA  . GLY H  1 117 ? 23.679  -11.514 23.830  1.00 28.92  ? 109 GLY H CA  1 
ATOM   12634 C C   . GLY H  1 117 ? 24.515  -11.071 22.651  1.00 25.13  ? 109 GLY H C   1 
ATOM   12635 O O   . GLY H  1 117 ? 25.296  -10.123 22.727  1.00 26.28  ? 109 GLY H O   1 
ATOM   12636 N N   . GLU H  1 118 ? 24.337  -11.778 21.546  1.00 25.65  ? 110 GLU H N   1 
ATOM   12637 C CA  . GLU H  1 118 ? 25.149  -11.569 20.362  1.00 27.18  ? 110 GLU H CA  1 
ATOM   12638 C C   . GLU H  1 118 ? 24.535  -10.488 19.482  1.00 25.96  ? 110 GLU H C   1 
ATOM   12639 O O   . GLU H  1 118 ? 23.340  -10.522 19.175  1.00 21.54  ? 110 GLU H O   1 
ATOM   12640 C CB  . GLU H  1 118 ? 25.267  -12.883 19.592  1.00 28.67  ? 110 GLU H CB  1 
ATOM   12641 C CG  . GLU H  1 118 ? 26.296  -12.865 18.464  1.00 39.99  ? 110 GLU H CG  1 
ATOM   12642 C CD  . GLU H  1 118 ? 26.173  -14.067 17.510  1.00 49.94  ? 110 GLU H CD  1 
ATOM   12643 O OE1 . GLU H  1 118 ? 25.453  -15.040 17.851  1.00 53.09  ? 110 GLU H OE1 1 
ATOM   12644 O OE2 . GLU H  1 118 ? 26.796  -14.033 16.418  1.00 39.59  ? 110 GLU H OE2 1 
ATOM   12645 N N   . VAL H  1 119 ? 25.365  -9.534  19.075  1.00 25.22  ? 111 VAL H N   1 
ATOM   12646 C CA  . VAL H  1 119 ? 24.923  -8.420  18.238  1.00 23.53  ? 111 VAL H CA  1 
ATOM   12647 C C   . VAL H  1 119 ? 25.576  -8.497  16.854  1.00 23.95  ? 111 VAL H C   1 
ATOM   12648 O O   . VAL H  1 119 ? 26.790  -8.674  16.741  1.00 25.04  ? 111 VAL H O   1 
ATOM   12649 C CB  . VAL H  1 119 ? 25.288  -7.069  18.899  1.00 25.79  ? 111 VAL H CB  1 
ATOM   12650 C CG1 . VAL H  1 119 ? 24.573  -5.929  18.214  1.00 18.77  ? 111 VAL H CG1 1 
ATOM   12651 C CG2 . VAL H  1 119 ? 24.953  -7.101  20.388  1.00 21.95  ? 111 VAL H CG2 1 
ATOM   12652 N N   . LEU H  1 120 ? 24.778  -8.387  15.798  1.00 22.92  ? 112 LEU H N   1 
ATOM   12653 C CA  . LEU H  1 120 ? 25.319  -8.447  14.447  1.00 20.13  ? 112 LEU H CA  1 
ATOM   12654 C C   . LEU H  1 120 ? 24.877  -7.227  13.673  1.00 19.50  ? 112 LEU H C   1 
ATOM   12655 O O   . LEU H  1 120 ? 23.721  -6.838  13.743  1.00 23.31  ? 112 LEU H O   1 
ATOM   12656 C CB  . LEU H  1 120 ? 24.837  -9.685  13.694  1.00 22.65  ? 112 LEU H CB  1 
ATOM   12657 C CG  . LEU H  1 120 ? 24.424  -10.990 14.370  1.00 25.18  ? 112 LEU H CG  1 
ATOM   12658 C CD1 . LEU H  1 120 ? 24.285  -12.077 13.319  1.00 23.89  ? 112 LEU H CD1 1 
ATOM   12659 C CD2 . LEU H  1 120 ? 25.422  -11.422 15.391  1.00 35.76  ? 112 LEU H CD2 1 
ATOM   12660 N N   . TYR H  1 121 ? 25.791  -6.639  12.916  1.00 17.33  ? 113 TYR H N   1 
ATOM   12661 C CA  . TYR H  1 121 ? 25.478  -5.464  12.121  1.00 19.14  ? 113 TYR H CA  1 
ATOM   12662 C C   . TYR H  1 121 ? 26.249  -5.506  10.795  1.00 23.62  ? 113 TYR H C   1 
ATOM   12663 O O   . TYR H  1 121 ? 27.483  -5.478  10.780  1.00 23.77  ? 113 TYR H O   1 
ATOM   12664 C CB  . TYR H  1 121 ? 25.792  -4.198  12.926  1.00 16.57  ? 113 TYR H CB  1 
ATOM   12665 C CG  . TYR H  1 121 ? 25.720  -2.905  12.155  1.00 14.77  ? 113 TYR H CG  1 
ATOM   12666 C CD1 . TYR H  1 121 ? 24.577  -2.545  11.434  1.00 14.99  ? 113 TYR H CD1 1 
ATOM   12667 C CD2 . TYR H  1 121 ? 26.786  -2.031  12.167  1.00 11.39  ? 113 TYR H CD2 1 
ATOM   12668 C CE1 . TYR H  1 121 ? 24.525  -1.348  10.729  1.00 13.42  ? 113 TYR H CE1 1 
ATOM   12669 C CE2 . TYR H  1 121 ? 26.744  -0.852  11.470  1.00 13.25  ? 113 TYR H CE2 1 
ATOM   12670 C CZ  . TYR H  1 121 ? 25.620  -0.509  10.757  1.00 15.20  ? 113 TYR H CZ  1 
ATOM   12671 O OH  . TYR H  1 121 ? 25.622  0.695   10.087  1.00 17.01  ? 113 TYR H OH  1 
ATOM   12672 N N   . MET H  1 122 ? 25.512  -5.591  9.691   1.00 20.12  ? 114 MET H N   1 
ATOM   12673 C CA  . MET H  1 122 ? 26.115  -5.737  8.374   1.00 22.99  ? 114 MET H CA  1 
ATOM   12674 C C   . MET H  1 122 ? 25.547  -4.764  7.344   1.00 19.91  ? 114 MET H C   1 
ATOM   12675 O O   . MET H  1 122 ? 24.657  -5.100  6.567   1.00 22.83  ? 114 MET H O   1 
ATOM   12676 C CB  . MET H  1 122 ? 25.963  -7.170  7.858   1.00 27.49  ? 114 MET H CB  1 
ATOM   12677 C CG  . MET H  1 122 ? 26.741  -7.397  6.549   1.00 35.64  ? 114 MET H CG  1 
ATOM   12678 S SD  . MET H  1 122 ? 26.493  -9.008  5.766   1.00 54.13  ? 114 MET H SD  1 
ATOM   12679 C CE  . MET H  1 122 ? 24.940  -8.752  4.915   1.00 38.34  ? 114 MET H CE  1 
ATOM   12680 N N   . PRO H  1 123 ? 26.056  -3.541  7.338   1.00 14.97  ? 115 PRO H N   1 
ATOM   12681 C CA  . PRO H  1 123 ? 25.612  -2.619  6.300   1.00 17.82  ? 115 PRO H CA  1 
ATOM   12682 C C   . PRO H  1 123 ? 26.367  -2.877  4.998   1.00 26.48  ? 115 PRO H C   1 
ATOM   12683 O O   . PRO H  1 123 ? 27.480  -3.415  5.005   1.00 22.98  ? 115 PRO H O   1 
ATOM   12684 C CB  . PRO H  1 123 ? 26.021  -1.260  6.862   1.00 16.09  ? 115 PRO H CB  1 
ATOM   12685 C CG  . PRO H  1 123 ? 27.229  -1.558  7.654   1.00 17.78  ? 115 PRO H CG  1 
ATOM   12686 C CD  . PRO H  1 123 ? 26.974  -2.906  8.290   1.00 17.88  ? 115 PRO H CD  1 
ATOM   12687 N N   . SER H  1 124 ? 25.756  -2.496  3.884   1.00 25.68  ? 116 SER H N   1 
ATOM   12688 C CA  . SER H  1 124 ? 26.434  -2.520  2.601   1.00 23.02  ? 116 SER H CA  1 
ATOM   12689 C C   . SER H  1 124 ? 26.986  -1.130  2.389   1.00 22.44  ? 116 SER H C   1 
ATOM   12690 O O   . SER H  1 124 ? 26.250  -0.145  2.391   1.00 23.79  ? 116 SER H O   1 
ATOM   12691 C CB  . SER H  1 124 ? 25.466  -2.893  1.485   1.00 23.49  ? 116 SER H CB  1 
ATOM   12692 O OG  . SER H  1 124 ? 25.537  -1.979  0.409   1.00 28.53  ? 116 SER H OG  1 
ATOM   12693 N N   . ILE H  1 125 ? 28.294  -1.041  2.234   1.00 28.05  ? 117 ILE H N   1 
ATOM   12694 C CA  . ILE H  1 125 ? 28.924  0.257   2.111   1.00 25.95  ? 117 ILE H CA  1 
ATOM   12695 C C   . ILE H  1 125 ? 29.497  0.429   0.721   1.00 23.92  ? 117 ILE H C   1 
ATOM   12696 O O   . ILE H  1 125 ? 30.009  -0.508  0.133   1.00 23.32  ? 117 ILE H O   1 
ATOM   12697 C CB  . ILE H  1 125 ? 30.037  0.435   3.156   1.00 21.66  ? 117 ILE H CB  1 
ATOM   12698 C CG1 . ILE H  1 125 ? 29.458  0.293   4.572   1.00 20.72  ? 117 ILE H CG1 1 
ATOM   12699 C CG2 . ILE H  1 125 ? 30.737  1.777   2.964   1.00 19.42  ? 117 ILE H CG2 1 
ATOM   12700 C CD1 . ILE H  1 125 ? 30.493  0.378   5.685   1.00 15.46  ? 117 ILE H CD1 1 
ATOM   12701 N N   . ARG H  1 126 ? 29.367  1.631   0.190   1.00 24.37  ? 118 ARG H N   1 
ATOM   12702 C CA  . ARG H  1 126 ? 30.114  2.021   -0.973  1.00 23.62  ? 118 ARG H CA  1 
ATOM   12703 C C   . ARG H  1 126 ? 31.110  3.088   -0.549  1.00 29.68  ? 118 ARG H C   1 
ATOM   12704 O O   . ARG H  1 126 ? 30.729  4.145   -0.044  1.00 27.04  ? 118 ARG H O   1 
ATOM   12705 C CB  . ARG H  1 126 ? 29.198  2.558   -2.060  1.00 21.60  ? 118 ARG H CB  1 
ATOM   12706 C CG  . ARG H  1 126 ? 29.947  3.328   -3.101  1.00 22.69  ? 118 ARG H CG  1 
ATOM   12707 C CD  . ARG H  1 126 ? 29.249  3.264   -4.422  1.00 28.28  ? 118 ARG H CD  1 
ATOM   12708 N NE  . ARG H  1 126 ? 30.048  3.915   -5.451  1.00 33.15  ? 118 ARG H NE  1 
ATOM   12709 C CZ  . ARG H  1 126 ? 29.541  4.482   -6.536  1.00 32.04  ? 118 ARG H CZ  1 
ATOM   12710 N NH1 . ARG H  1 126 ? 28.230  4.478   -6.728  1.00 31.16  ? 118 ARG H NH1 1 
ATOM   12711 N NH2 . ARG H  1 126 ? 30.344  5.058   -7.423  1.00 33.19  ? 118 ARG H NH2 1 
ATOM   12712 N N   . GLN H  1 127 ? 32.389  2.814   -0.777  1.00 34.11  ? 119 GLN H N   1 
ATOM   12713 C CA  . GLN H  1 127 ? 33.448  3.722   -0.359  1.00 31.12  ? 119 GLN H CA  1 
ATOM   12714 C C   . GLN H  1 127 ? 34.670  3.683   -1.292  1.00 28.56  ? 119 GLN H C   1 
ATOM   12715 O O   . GLN H  1 127 ? 34.964  2.656   -1.897  1.00 29.31  ? 119 GLN H O   1 
ATOM   12716 C CB  . GLN H  1 127 ? 33.860  3.373   1.064   1.00 23.06  ? 119 GLN H CB  1 
ATOM   12717 C CG  . GLN H  1 127 ? 34.798  4.361   1.677   1.00 24.61  ? 119 GLN H CG  1 
ATOM   12718 C CD  . GLN H  1 127 ? 34.975  4.123   3.148   1.00 19.79  ? 119 GLN H CD  1 
ATOM   12719 O OE1 . GLN H  1 127 ? 34.775  3.015   3.643   1.00 15.56  ? 119 GLN H OE1 1 
ATOM   12720 N NE2 . GLN H  1 127 ? 35.335  5.168   3.860   1.00 18.66  ? 119 GLN H NE2 1 
ATOM   12721 N N   . ARG H  1 128 ? 35.377  4.805   -1.392  1.00 27.26  ? 120 ARG H N   1 
ATOM   12722 C CA  . ARG H  1 128 ? 36.599  4.888   -2.187  1.00 30.23  ? 120 ARG H CA  1 
ATOM   12723 C C   . ARG H  1 128 ? 37.852  4.771   -1.310  1.00 31.41  ? 120 ARG H C   1 
ATOM   12724 O O   . ARG H  1 128 ? 37.858  5.192   -0.150  1.00 31.09  ? 120 ARG H O   1 
ATOM   12725 C CB  . ARG H  1 128 ? 36.643  6.194   -2.991  1.00 28.34  ? 120 ARG H CB  1 
ATOM   12726 C CG  . ARG H  1 128 ? 35.326  6.573   -3.627  1.00 30.68  ? 120 ARG H CG  1 
ATOM   12727 C CD  . ARG H  1 128 ? 35.511  7.505   -4.798  1.00 39.69  ? 120 ARG H CD  1 
ATOM   12728 N NE  . ARG H  1 128 ? 36.486  8.568   -4.562  1.00 45.42  ? 120 ARG H NE  1 
ATOM   12729 C CZ  . ARG H  1 128 ? 37.537  8.805   -5.353  1.00 51.36  ? 120 ARG H CZ  1 
ATOM   12730 N NH1 . ARG H  1 128 ? 37.759  8.042   -6.421  1.00 41.42  ? 120 ARG H NH1 1 
ATOM   12731 N NH2 . ARG H  1 128 ? 38.369  9.805   -5.079  1.00 46.95  ? 120 ARG H NH2 1 
ATOM   12732 N N   . PHE H  1 129 ? 38.913  4.200   -1.870  1.00 28.87  ? 121 PHE H N   1 
ATOM   12733 C CA  . PHE H  1 129 ? 40.161  4.026   -1.138  1.00 29.93  ? 121 PHE H CA  1 
ATOM   12734 C C   . PHE H  1 129 ? 41.372  4.413   -1.964  1.00 33.17  ? 121 PHE H C   1 
ATOM   12735 O O   . PHE H  1 129 ? 41.288  4.564   -3.182  1.00 33.58  ? 121 PHE H O   1 
ATOM   12736 C CB  . PHE H  1 129 ? 40.334  2.578   -0.711  1.00 32.63  ? 121 PHE H CB  1 
ATOM   12737 C CG  . PHE H  1 129 ? 39.240  2.065   0.175   1.00 37.33  ? 121 PHE H CG  1 
ATOM   12738 C CD1 . PHE H  1 129 ? 38.050  1.597   -0.366  1.00 37.17  ? 121 PHE H CD1 1 
ATOM   12739 C CD2 . PHE H  1 129 ? 39.413  2.018   1.545   1.00 31.15  ? 121 PHE H CD2 1 
ATOM   12740 C CE1 . PHE H  1 129 ? 37.052  1.110   0.444   1.00 29.84  ? 121 PHE H CE1 1 
ATOM   12741 C CE2 . PHE H  1 129 ? 38.426  1.524   2.354   1.00 28.39  ? 121 PHE H CE2 1 
ATOM   12742 C CZ  . PHE H  1 129 ? 37.243  1.071   1.805   1.00 30.63  ? 121 PHE H CZ  1 
ATOM   12743 N N   . SER H  1 130 ? 42.500  4.562   -1.277  1.00 35.91  ? 122 SER H N   1 
ATOM   12744 C CA  . SER H  1 130 ? 43.795  4.752   -1.911  1.00 32.65  ? 122 SER H CA  1 
ATOM   12745 C C   . SER H  1 130 ? 44.644  3.526   -1.653  1.00 32.06  ? 122 SER H C   1 
ATOM   12746 O O   . SER H  1 130 ? 45.137  3.329   -0.545  1.00 33.27  ? 122 SER H O   1 
ATOM   12747 C CB  . SER H  1 130 ? 44.505  5.969   -1.327  1.00 30.67  ? 122 SER H CB  1 
ATOM   12748 O OG  . SER H  1 130 ? 45.884  5.950   -1.655  1.00 29.80  ? 122 SER H OG  1 
ATOM   12749 N N   . CYS H  1 131 ? 44.822  2.700   -2.672  1.00 34.07  ? 123 CYS H N   1 
ATOM   12750 C CA  . CYS H  1 131 ? 45.669  1.522   -2.529  1.00 40.67  ? 123 CYS H CA  1 
ATOM   12751 C C   . CYS H  1 131 ? 46.381  1.186   -3.839  1.00 36.82  ? 123 CYS H C   1 
ATOM   12752 O O   . CYS H  1 131 ? 46.358  1.976   -4.788  1.00 32.84  ? 123 CYS H O   1 
ATOM   12753 C CB  . CYS H  1 131 ? 44.839  0.338   -2.048  1.00 42.37  ? 123 CYS H CB  1 
ATOM   12754 S SG  . CYS H  1 131 ? 43.286  0.217   -2.946  1.00 54.62  ? 123 CYS H SG  1 
ATOM   12755 N N   . ASP H  1 132 ? 46.993  0.004   -3.885  1.00 40.40  ? 124 ASP H N   1 
ATOM   12756 C CA  . ASP H  1 132 ? 47.871  -0.389  -4.993  1.00 43.74  ? 124 ASP H CA  1 
ATOM   12757 C C   . ASP H  1 132 ? 47.172  -1.143  -6.117  1.00 42.64  ? 124 ASP H C   1 
ATOM   12758 O O   . ASP H  1 132 ? 46.994  -2.359  -6.034  1.00 46.24  ? 124 ASP H O   1 
ATOM   12759 C CB  . ASP H  1 132 ? 49.020  -1.253  -4.467  1.00 42.81  ? 124 ASP H CB  1 
ATOM   12760 C CG  . ASP H  1 132 ? 50.076  -1.526  -5.521  1.00 43.73  ? 124 ASP H CG  1 
ATOM   12761 O OD1 . ASP H  1 132 ? 50.219  -0.701  -6.458  1.00 38.54  ? 124 ASP H OD1 1 
ATOM   12762 O OD2 . ASP H  1 132 ? 50.767  -2.561  -5.394  1.00 40.84  ? 124 ASP H OD2 1 
ATOM   12763 N N   . VAL H  1 133 ? 46.803  -0.429  -7.176  1.00 39.57  ? 125 VAL H N   1 
ATOM   12764 C CA  . VAL H  1 133 ? 46.182  -1.073  -8.331  1.00 48.25  ? 125 VAL H CA  1 
ATOM   12765 C C   . VAL H  1 133 ? 47.103  -1.216  -9.540  1.00 52.69  ? 125 VAL H C   1 
ATOM   12766 O O   . VAL H  1 133 ? 46.632  -1.319  -10.669 1.00 52.99  ? 125 VAL H O   1 
ATOM   12767 C CB  . VAL H  1 133 ? 44.869  -0.380  -8.760  1.00 46.01  ? 125 VAL H CB  1 
ATOM   12768 C CG1 . VAL H  1 133 ? 43.749  -0.825  -7.853  1.00 53.37  ? 125 VAL H CG1 1 
ATOM   12769 C CG2 . VAL H  1 133 ? 45.011  1.133   -8.736  1.00 42.59  ? 125 VAL H CG2 1 
ATOM   12770 N N   . SER H  1 134 ? 48.411  -1.219  -9.307  1.00 50.05  ? 126 SER H N   1 
ATOM   12771 C CA  . SER H  1 134 ? 49.338  -1.556  -10.373 1.00 50.92  ? 126 SER H CA  1 
ATOM   12772 C C   . SER H  1 134 ? 49.293  -3.075  -10.538 1.00 51.03  ? 126 SER H C   1 
ATOM   12773 O O   . SER H  1 134 ? 49.445  -3.818  -9.563  1.00 52.46  ? 126 SER H O   1 
ATOM   12774 C CB  . SER H  1 134 ? 50.756  -1.070  -10.053 1.00 47.11  ? 126 SER H CB  1 
ATOM   12775 O OG  . SER H  1 134 ? 51.372  -1.883  -9.069  1.00 55.18  ? 126 SER H OG  1 
ATOM   12776 N N   . GLY H  1 135 ? 49.056  -3.530  -11.764 1.00 46.03  ? 127 GLY H N   1 
ATOM   12777 C CA  . GLY H  1 135 ? 48.933  -4.950  -12.033 1.00 47.39  ? 127 GLY H CA  1 
ATOM   12778 C C   . GLY H  1 135 ? 47.507  -5.314  -12.386 1.00 50.44  ? 127 GLY H C   1 
ATOM   12779 O O   . GLY H  1 135 ? 47.174  -6.484  -12.585 1.00 45.65  ? 127 GLY H O   1 
ATOM   12780 N N   . VAL H  1 136 ? 46.664  -4.291  -12.460 1.00 56.67  ? 128 VAL H N   1 
ATOM   12781 C CA  . VAL H  1 136 ? 45.244  -4.466  -12.744 1.00 52.39  ? 128 VAL H CA  1 
ATOM   12782 C C   . VAL H  1 136 ? 45.022  -5.211  -14.056 1.00 46.42  ? 128 VAL H C   1 
ATOM   12783 O O   . VAL H  1 136 ? 44.233  -6.154  -14.121 1.00 42.81  ? 128 VAL H O   1 
ATOM   12784 C CB  . VAL H  1 136 ? 44.503  -3.102  -12.769 1.00 47.90  ? 128 VAL H CB  1 
ATOM   12785 C CG1 . VAL H  1 136 ? 45.365  -2.027  -13.417 1.00 49.72  ? 128 VAL H CG1 1 
ATOM   12786 C CG2 . VAL H  1 136 ? 43.162  -3.226  -13.472 1.00 53.04  ? 128 VAL H CG2 1 
ATOM   12787 N N   . ASP H  1 137 ? 45.756  -4.800  -15.084 1.00 53.21  ? 129 ASP H N   1 
ATOM   12788 C CA  . ASP H  1 137 ? 45.571  -5.323  -16.433 1.00 52.39  ? 129 ASP H CA  1 
ATOM   12789 C C   . ASP H  1 137 ? 46.350  -6.604  -16.704 1.00 45.35  ? 129 ASP H C   1 
ATOM   12790 O O   . ASP H  1 137 ? 46.118  -7.259  -17.712 1.00 52.93  ? 129 ASP H O   1 
ATOM   12791 C CB  . ASP H  1 137 ? 45.922  -4.260  -17.473 1.00 43.43  ? 129 ASP H CB  1 
ATOM   12792 C CG  . ASP H  1 137 ? 45.230  -2.933  -17.202 1.00 53.44  ? 129 ASP H CG  1 
ATOM   12793 O OD1 . ASP H  1 137 ? 43.978  -2.879  -17.275 1.00 55.50  ? 129 ASP H OD1 1 
ATOM   12794 O OD2 . ASP H  1 137 ? 45.941  -1.945  -16.916 1.00 47.60  ? 129 ASP H OD2 1 
ATOM   12795 N N   . THR H  1 138 ? 47.276  -6.876  -15.784 1.00 46.47  ? 130 THR H N   1 
ATOM   12796 C CA  . THR H  1 138 ? 48.032  -8.115  -15.662 1.00 47.40  ? 130 THR H CA  1 
ATOM   12797 C C   . THR H  1 138 ? 47.189  -9.192  -14.987 1.00 46.50  ? 130 THR H C   1 
ATOM   12798 O O   . THR H  1 138 ? 46.133  -8.907  -14.422 1.00 49.55  ? 130 THR H O   1 
ATOM   12799 C CB  . THR H  1 138 ? 49.328  -7.909  -14.857 1.00 47.74  ? 130 THR H CB  1 
ATOM   12800 O OG1 . THR H  1 138 ? 49.034  -7.940  -13.455 1.00 56.75  ? 130 THR H OG1 1 
ATOM   12801 C CG2 . THR H  1 138 ? 49.966  -6.573  -15.207 1.00 23.21  ? 130 THR H CG2 1 
ATOM   12802 N N   . GLU H  1 139 ? 47.658  -10.431 -15.065 1.00 50.93  ? 131 GLU H N   1 
ATOM   12803 C CA  . GLU H  1 139 ? 46.867  -11.596 -14.675 1.00 54.93  ? 131 GLU H CA  1 
ATOM   12804 C C   . GLU H  1 139 ? 47.229  -12.050 -13.269 1.00 49.69  ? 131 GLU H C   1 
ATOM   12805 O O   . GLU H  1 139 ? 46.527  -12.857 -12.657 1.00 44.28  ? 131 GLU H O   1 
ATOM   12806 C CB  . GLU H  1 139 ? 47.043  -12.743 -15.672 1.00 57.18  ? 131 GLU H CB  1 
ATOM   12807 C CG  . GLU H  1 139 ? 45.752  -13.134 -16.380 1.00 66.77  ? 131 GLU H CG  1 
ATOM   12808 C CD  . GLU H  1 139 ? 45.834  -14.494 -17.062 1.00 75.85  ? 131 GLU H CD  1 
ATOM   12809 O OE1 . GLU H  1 139 ? 46.815  -14.740 -17.803 1.00 73.35  ? 131 GLU H OE1 1 
ATOM   12810 O OE2 . GLU H  1 139 ? 44.912  -15.318 -16.851 1.00 73.87  ? 131 GLU H OE2 1 
ATOM   12811 N N   . SER H  1 140 ? 48.347  -11.534 -12.771 1.00 51.00  ? 132 SER H N   1 
ATOM   12812 C CA  . SER H  1 140 ? 48.650  -11.627 -11.355 1.00 57.07  ? 132 SER H CA  1 
ATOM   12813 C C   . SER H  1 140 ? 47.580  -10.804 -10.635 1.00 58.59  ? 132 SER H C   1 
ATOM   12814 O O   . SER H  1 140 ? 47.202  -11.097 -9.498  1.00 49.19  ? 132 SER H O   1 
ATOM   12815 C CB  . SER H  1 140 ? 50.048  -11.071 -11.071 1.00 56.16  ? 132 SER H CB  1 
ATOM   12816 O OG  . SER H  1 140 ? 50.199  -9.753  -11.582 1.00 53.32  ? 132 SER H OG  1 
ATOM   12817 N N   . GLY H  1 141 ? 47.085  -9.782  -11.333 1.00 53.95  ? 133 GLY H N   1 
ATOM   12818 C CA  . GLY H  1 141 ? 46.032  -8.924  -10.832 1.00 50.31  ? 133 GLY H CA  1 
ATOM   12819 C C   . GLY H  1 141 ? 46.606  -7.765  -10.049 1.00 51.00  ? 133 GLY H C   1 
ATOM   12820 O O   . GLY H  1 141 ? 47.821  -7.577  -10.022 1.00 52.61  ? 133 GLY H O   1 
ATOM   12821 N N   . ALA H  1 142 ? 45.736  -6.972  -9.432  1.00 44.00  ? 134 ALA H N   1 
ATOM   12822 C CA  . ALA H  1 142 ? 46.201  -5.969  -8.489  1.00 47.38  ? 134 ALA H CA  1 
ATOM   12823 C C   . ALA H  1 142 ? 46.073  -6.577  -7.108  1.00 43.22  ? 134 ALA H C   1 
ATOM   12824 O O   . ALA H  1 142 ? 45.529  -7.671  -6.964  1.00 45.45  ? 134 ALA H O   1 
ATOM   12825 C CB  . ALA H  1 142 ? 45.387  -4.692  -8.602  1.00 44.42  ? 134 ALA H CB  1 
ATOM   12826 N N   . THR H  1 143 ? 46.601  -5.894  -6.099  1.00 43.33  ? 135 THR H N   1 
ATOM   12827 C CA  . THR H  1 143 ? 46.349  -6.288  -4.717  1.00 45.53  ? 135 THR H CA  1 
ATOM   12828 C C   . THR H  1 143 ? 46.258  -5.060  -3.814  1.00 46.98  ? 135 THR H C   1 
ATOM   12829 O O   . THR H  1 143 ? 47.259  -4.561  -3.301  1.00 48.47  ? 135 THR H O   1 
ATOM   12830 C CB  . THR H  1 143 ? 47.372  -7.319  -4.191  1.00 43.87  ? 135 THR H CB  1 
ATOM   12831 O OG1 . THR H  1 143 ? 47.339  -8.478  -5.028  1.00 42.85  ? 135 THR H OG1 1 
ATOM   12832 C CG2 . THR H  1 143 ? 47.026  -7.747  -2.769  1.00 50.05  ? 135 THR H CG2 1 
ATOM   12833 N N   . CYS H  1 144 ? 45.035  -4.569  -3.652  1.00 47.32  ? 136 CYS H N   1 
ATOM   12834 C CA  . CYS H  1 144 ? 44.769  -3.450  -2.772  1.00 45.78  ? 136 CYS H CA  1 
ATOM   12835 C C   . CYS H  1 144 ? 44.509  -3.929  -1.353  1.00 39.40  ? 136 CYS H C   1 
ATOM   12836 O O   . CYS H  1 144 ? 43.717  -4.845  -1.138  1.00 40.42  ? 136 CYS H O   1 
ATOM   12837 C CB  . CYS H  1 144 ? 43.561  -2.665  -3.257  1.00 41.59  ? 136 CYS H CB  1 
ATOM   12838 S SG  . CYS H  1 144 ? 42.723  -1.861  -1.875  1.00 55.69  ? 136 CYS H SG  1 
ATOM   12839 N N   . ARG H  1 145 ? 45.168  -3.297  -0.387  1.00 37.06  ? 137 ARG H N   1 
ATOM   12840 C CA  . ARG H  1 145 ? 44.981  -3.654  1.019   1.00 42.90  ? 137 ARG H CA  1 
ATOM   12841 C C   . ARG H  1 145 ? 44.164  -2.616  1.818   1.00 41.94  ? 137 ARG H C   1 
ATOM   12842 O O   . ARG H  1 145 ? 44.558  -1.456  1.953   1.00 33.20  ? 137 ARG H O   1 
ATOM   12843 C CB  . ARG H  1 145 ? 46.328  -3.976  1.686   1.00 42.70  ? 137 ARG H CB  1 
ATOM   12844 C CG  . ARG H  1 145 ? 46.833  -5.381  1.349   1.00 50.55  ? 137 ARG H CG  1 
ATOM   12845 C CD  . ARG H  1 145 ? 48.298  -5.598  1.702   1.00 52.15  ? 137 ARG H CD  1 
ATOM   12846 N NE  . ARG H  1 145 ? 48.963  -6.473  0.732   1.00 58.94  ? 137 ARG H NE  1 
ATOM   12847 C CZ  . ARG H  1 145 ? 49.286  -7.750  0.946   1.00 62.22  ? 137 ARG H CZ  1 
ATOM   12848 N NH1 . ARG H  1 145 ? 49.018  -8.330  2.109   1.00 65.10  ? 137 ARG H NH1 1 
ATOM   12849 N NH2 . ARG H  1 145 ? 49.889  -8.451  -0.007  1.00 54.14  ? 137 ARG H NH2 1 
ATOM   12850 N N   . ILE H  1 146 ? 43.015  -3.064  2.330   1.00 44.90  ? 138 ILE H N   1 
ATOM   12851 C CA  . ILE H  1 146 ? 42.096  -2.231  3.103   1.00 41.21  ? 138 ILE H CA  1 
ATOM   12852 C C   . ILE H  1 146 ? 42.323  -2.475  4.580   1.00 38.72  ? 138 ILE H C   1 
ATOM   12853 O O   . ILE H  1 146 ? 42.212  -3.608  5.041   1.00 40.34  ? 138 ILE H O   1 
ATOM   12854 C CB  . ILE H  1 146 ? 40.617  -2.605  2.828   1.00 44.64  ? 138 ILE H CB  1 
ATOM   12855 C CG1 . ILE H  1 146 ? 40.281  -2.556  1.325   1.00 36.04  ? 138 ILE H CG1 1 
ATOM   12856 C CG2 . ILE H  1 146 ? 39.690  -1.715  3.650   1.00 36.29  ? 138 ILE H CG2 1 
ATOM   12857 C CD1 . ILE H  1 146 ? 40.206  -1.172  0.739   1.00 25.28  ? 138 ILE H CD1 1 
ATOM   12858 N N   . LYS H  1 147 ? 42.628  -1.418  5.325   1.00 36.81  ? 139 LYS H N   1 
ATOM   12859 C CA  . LYS H  1 147 ? 42.856  -1.549  6.760   1.00 39.04  ? 139 LYS H CA  1 
ATOM   12860 C C   . LYS H  1 147 ? 41.695  -0.954  7.588   1.00 40.50  ? 139 LYS H C   1 
ATOM   12861 O O   . LYS H  1 147 ? 41.399  0.237   7.501   1.00 44.46  ? 139 LYS H O   1 
ATOM   12862 C CB  . LYS H  1 147 ? 44.188  -0.898  7.133   1.00 45.48  ? 139 LYS H CB  1 
ATOM   12863 C CG  . LYS H  1 147 ? 45.260  -0.990  6.035   1.00 54.23  ? 139 LYS H CG  1 
ATOM   12864 C CD  . LYS H  1 147 ? 46.611  -0.412  6.490   1.00 56.67  ? 139 LYS H CD  1 
ATOM   12865 C CE  . LYS H  1 147 ? 46.494  1.068   6.858   1.00 54.36  ? 139 LYS H CE  1 
ATOM   12866 N NZ  . LYS H  1 147 ? 47.710  1.607   7.528   1.00 52.69  ? 139 LYS H NZ  1 
ATOM   12867 N N   . ILE H  1 148 ? 41.043  -1.790  8.389   1.00 34.30  ? 140 ILE H N   1 
ATOM   12868 C CA  . ILE H  1 148 ? 39.893  -1.385  9.189   1.00 33.17  ? 140 ILE H CA  1 
ATOM   12869 C C   . ILE H  1 148 ? 40.084  -1.740  10.660  1.00 35.53  ? 140 ILE H C   1 
ATOM   12870 O O   . ILE H  1 148 ? 40.457  -2.868  10.964  1.00 37.92  ? 140 ILE H O   1 
ATOM   12871 C CB  . ILE H  1 148 ? 38.627  -2.126  8.722   1.00 34.27  ? 140 ILE H CB  1 
ATOM   12872 C CG1 . ILE H  1 148 ? 38.189  -1.621  7.352   1.00 30.03  ? 140 ILE H CG1 1 
ATOM   12873 C CG2 . ILE H  1 148 ? 37.492  -1.994  9.760   1.00 33.37  ? 140 ILE H CG2 1 
ATOM   12874 C CD1 . ILE H  1 148 ? 37.108  -2.470  6.736   1.00 28.41  ? 140 ILE H CD1 1 
ATOM   12875 N N   . GLY H  1 149 ? 39.807  -0.797  11.564  1.00 33.45  ? 141 GLY H N   1 
ATOM   12876 C CA  . GLY H  1 149 ? 39.811  -1.079  12.998  1.00 38.20  ? 141 GLY H CA  1 
ATOM   12877 C C   . GLY H  1 149 ? 39.127  -0.024  13.860  1.00 30.10  ? 141 GLY H C   1 
ATOM   12878 O O   . GLY H  1 149 ? 38.493  0.888   13.333  1.00 34.69  ? 141 GLY H O   1 
ATOM   12879 N N   . SER H  1 150 ? 39.252  -0.132  15.179  1.00 20.79  ? 142 SER H N   1 
ATOM   12880 C CA  . SER H  1 150 ? 38.750  0.924   16.056  1.00 22.45  ? 142 SER H CA  1 
ATOM   12881 C C   . SER H  1 150 ? 39.520  2.235   15.902  1.00 23.88  ? 142 SER H C   1 
ATOM   12882 O O   . SER H  1 150 ? 40.744  2.277   15.990  1.00 25.52  ? 142 SER H O   1 
ATOM   12883 C CB  . SER H  1 150 ? 38.778  0.497   17.528  1.00 28.43  ? 142 SER H CB  1 
ATOM   12884 O OG  . SER H  1 150 ? 38.307  1.542   18.380  1.00 24.62  ? 142 SER H OG  1 
ATOM   12885 N N   . TRP H  1 151 ? 38.789  3.316   15.695  1.00 23.04  ? 143 TRP H N   1 
ATOM   12886 C CA  . TRP H  1 151 ? 39.416  4.618   15.568  1.00 22.79  ? 143 TRP H CA  1 
ATOM   12887 C C   . TRP H  1 151 ? 39.885  5.176   16.920  1.00 23.20  ? 143 TRP H C   1 
ATOM   12888 O O   . TRP H  1 151 ? 40.978  5.721   17.010  1.00 23.57  ? 143 TRP H O   1 
ATOM   12889 C CB  . TRP H  1 151 ? 38.462  5.588   14.870  1.00 21.40  ? 143 TRP H CB  1 
ATOM   12890 C CG  . TRP H  1 151 ? 39.056  6.914   14.593  1.00 22.38  ? 143 TRP H CG  1 
ATOM   12891 C CD1 . TRP H  1 151 ? 38.645  8.126   15.077  1.00 19.39  ? 143 TRP H CD1 1 
ATOM   12892 C CD2 . TRP H  1 151 ? 40.189  7.173   13.771  1.00 23.23  ? 143 TRP H CD2 1 
ATOM   12893 N NE1 . TRP H  1 151 ? 39.454  9.126   14.593  1.00 17.97  ? 143 TRP H NE1 1 
ATOM   12894 C CE2 . TRP H  1 151 ? 40.413  8.565   13.793  1.00 21.83  ? 143 TRP H CE2 1 
ATOM   12895 C CE3 . TRP H  1 151 ? 41.040  6.364   13.019  1.00 22.72  ? 143 TRP H CE3 1 
ATOM   12896 C CZ2 . TRP H  1 151 ? 41.443  9.159   13.085  1.00 28.84  ? 143 TRP H CZ2 1 
ATOM   12897 C CZ3 . TRP H  1 151 ? 42.063  6.955   12.316  1.00 25.97  ? 143 TRP H CZ3 1 
ATOM   12898 C CH2 . TRP H  1 151 ? 42.259  8.337   12.350  1.00 27.71  ? 143 TRP H CH2 1 
ATOM   12899 N N   . THR H  1 152 ? 39.073  5.029   17.970  1.00 24.16  ? 144 THR H N   1 
ATOM   12900 C CA  . THR H  1 152 ? 39.418  5.619   19.271  1.00 20.99  ? 144 THR H CA  1 
ATOM   12901 C C   . THR H  1 152 ? 39.762  4.636   20.391  1.00 19.38  ? 144 THR H C   1 
ATOM   12902 O O   . THR H  1 152 ? 40.400  5.019   21.368  1.00 20.01  ? 144 THR H O   1 
ATOM   12903 C CB  . THR H  1 152 ? 38.328  6.604   19.779  1.00 20.93  ? 144 THR H CB  1 
ATOM   12904 O OG1 . THR H  1 152 ? 37.194  5.880   20.274  1.00 22.17  ? 144 THR H OG1 1 
ATOM   12905 C CG2 . THR H  1 152 ? 37.892  7.532   18.659  1.00 24.67  ? 144 THR H CG2 1 
ATOM   12906 N N   . HIS H  1 153 ? 39.355  3.379   20.260  1.00 21.21  ? 145 HIS H N   1 
ATOM   12907 C CA  . HIS H  1 153 ? 39.574  2.419   21.341  1.00 23.77  ? 145 HIS H CA  1 
ATOM   12908 C C   . HIS H  1 153 ? 40.769  1.498   21.101  1.00 26.37  ? 145 HIS H C   1 
ATOM   12909 O O   . HIS H  1 153 ? 40.709  0.613   20.254  1.00 28.97  ? 145 HIS H O   1 
ATOM   12910 C CB  . HIS H  1 153 ? 38.321  1.569   21.570  1.00 26.00  ? 145 HIS H CB  1 
ATOM   12911 C CG  . HIS H  1 153 ? 37.128  2.357   22.010  1.00 22.43  ? 145 HIS H CG  1 
ATOM   12912 N ND1 . HIS H  1 153 ? 36.308  3.021   21.126  1.00 20.08  ? 145 HIS H ND1 1 
ATOM   12913 C CD2 . HIS H  1 153 ? 36.616  2.585   23.241  1.00 25.33  ? 145 HIS H CD2 1 
ATOM   12914 C CE1 . HIS H  1 153 ? 35.342  3.626   21.791  1.00 22.49  ? 145 HIS H CE1 1 
ATOM   12915 N NE2 . HIS H  1 153 ? 35.506  3.378   23.078  1.00 25.37  ? 145 HIS H NE2 1 
ATOM   12916 N N   . HIS H  1 154 ? 41.787  1.654   21.952  1.00 27.64  ? 146 HIS H N   1 
ATOM   12917 C CA  . HIS H  1 154 ? 43.036  0.875   21.943  1.00 29.09  ? 146 HIS H CA  1 
ATOM   12918 C C   . HIS H  1 154 ? 42.902  -0.578  22.431  1.00 28.48  ? 146 HIS H C   1 
ATOM   12919 O O   . HIS H  1 154 ? 41.915  -0.942  23.070  1.00 31.04  ? 146 HIS H O   1 
ATOM   12920 C CB  . HIS H  1 154 ? 44.116  1.596   22.753  1.00 30.90  ? 146 HIS H CB  1 
ATOM   12921 C CG  . HIS H  1 154 ? 43.721  1.880   24.169  1.00 33.61  ? 146 HIS H CG  1 
ATOM   12922 N ND1 . HIS H  1 154 ? 43.598  0.890   25.120  1.00 32.30  ? 146 HIS H ND1 1 
ATOM   12923 C CD2 . HIS H  1 154 ? 43.422  3.042   24.796  1.00 36.46  ? 146 HIS H CD2 1 
ATOM   12924 C CE1 . HIS H  1 154 ? 43.240  1.430   26.271  1.00 40.57  ? 146 HIS H CE1 1 
ATOM   12925 N NE2 . HIS H  1 154 ? 43.126  2.735   26.102  1.00 37.71  ? 146 HIS H NE2 1 
ATOM   12926 N N   . SER H  1 155 ? 43.901  -1.400  22.102  1.00 28.66  ? 147 SER H N   1 
ATOM   12927 C CA  . SER H  1 155 ? 43.812  -2.862  22.212  1.00 31.73  ? 147 SER H CA  1 
ATOM   12928 C C   . SER H  1 155 ? 43.287  -3.418  23.538  1.00 28.52  ? 147 SER H C   1 
ATOM   12929 O O   . SER H  1 155 ? 42.748  -4.529  23.572  1.00 26.10  ? 147 SER H O   1 
ATOM   12930 C CB  . SER H  1 155 ? 45.157  -3.506  21.880  1.00 31.40  ? 147 SER H CB  1 
ATOM   12931 O OG  . SER H  1 155 ? 46.221  -2.763  22.454  1.00 38.28  ? 147 SER H OG  1 
ATOM   12932 N N   . ARG H  1 156 ? 43.448  -2.663  24.620  1.00 28.21  ? 148 ARG H N   1 
ATOM   12933 C CA  . ARG H  1 156 ? 42.907  -3.080  25.914  1.00 33.12  ? 148 ARG H CA  1 
ATOM   12934 C C   . ARG H  1 156 ? 41.385  -2.971  25.946  1.00 29.15  ? 148 ARG H C   1 
ATOM   12935 O O   . ARG H  1 156 ? 40.710  -3.758  26.598  1.00 30.50  ? 148 ARG H O   1 
ATOM   12936 C CB  . ARG H  1 156 ? 43.522  -2.259  27.049  1.00 40.95  ? 148 ARG H CB  1 
ATOM   12937 C CG  . ARG H  1 156 ? 45.039  -2.349  27.106  1.00 42.34  ? 148 ARG H CG  1 
ATOM   12938 C CD  . ARG H  1 156 ? 45.584  -2.019  28.482  1.00 47.45  ? 148 ARG H CD  1 
ATOM   12939 N NE  . ARG H  1 156 ? 46.901  -2.616  28.681  1.00 52.40  ? 148 ARG H NE  1 
ATOM   12940 C CZ  . ARG H  1 156 ? 47.103  -3.871  29.076  1.00 62.39  ? 148 ARG H CZ  1 
ATOM   12941 N NH1 . ARG H  1 156 ? 46.069  -4.670  29.324  1.00 67.91  ? 148 ARG H NH1 1 
ATOM   12942 N NH2 . ARG H  1 156 ? 48.340  -4.328  29.228  1.00 59.87  ? 148 ARG H NH2 1 
ATOM   12943 N N   . GLU H  1 157 ? 40.855  -1.993  25.222  1.00 28.13  ? 149 GLU H N   1 
ATOM   12944 C CA  . GLU H  1 157 ? 39.425  -1.741  25.169  1.00 25.22  ? 149 GLU H CA  1 
ATOM   12945 C C   . GLU H  1 157 ? 38.723  -2.588  24.099  1.00 30.36  ? 149 GLU H C   1 
ATOM   12946 O O   . GLU H  1 157 ? 37.718  -3.252  24.380  1.00 27.20  ? 149 GLU H O   1 
ATOM   12947 C CB  . GLU H  1 157 ? 39.182  -0.245  24.947  1.00 22.14  ? 149 GLU H CB  1 
ATOM   12948 C CG  . GLU H  1 157 ? 39.715  0.620   26.095  1.00 27.75  ? 149 GLU H CG  1 
ATOM   12949 C CD  . GLU H  1 157 ? 39.900  2.096   25.726  1.00 33.72  ? 149 GLU H CD  1 
ATOM   12950 O OE1 . GLU H  1 157 ? 40.406  2.388   24.619  1.00 27.20  ? 149 GLU H OE1 1 
ATOM   12951 O OE2 . GLU H  1 157 ? 39.547  2.970   26.553  1.00 32.18  ? 149 GLU H OE2 1 
ATOM   12952 N N   . ILE H  1 158 ? 39.260  -2.574  22.878  1.00 32.41  ? 150 ILE H N   1 
ATOM   12953 C CA  . ILE H  1 158 ? 38.650  -3.298  21.754  1.00 33.82  ? 150 ILE H CA  1 
ATOM   12954 C C   . ILE H  1 158 ? 39.633  -4.174  20.969  1.00 33.57  ? 150 ILE H C   1 
ATOM   12955 O O   . ILE H  1 158 ? 40.732  -3.741  20.611  1.00 26.25  ? 150 ILE H O   1 
ATOM   12956 C CB  . ILE H  1 158 ? 37.932  -2.340  20.756  1.00 30.49  ? 150 ILE H CB  1 
ATOM   12957 C CG1 . ILE H  1 158 ? 36.678  -1.740  21.388  1.00 31.67  ? 150 ILE H CG1 1 
ATOM   12958 C CG2 . ILE H  1 158 ? 37.526  -3.079  19.503  1.00 23.31  ? 150 ILE H CG2 1 
ATOM   12959 C CD1 . ILE H  1 158 ? 35.757  -1.087  20.385  1.00 25.43  ? 150 ILE H CD1 1 
ATOM   12960 N N   . SER H  1 159 ? 39.202  -5.402  20.688  1.00 37.46  ? 151 SER H N   1 
ATOM   12961 C CA  . SER H  1 159 ? 39.960  -6.358  19.891  1.00 34.35  ? 151 SER H CA  1 
ATOM   12962 C C   . SER H  1 159 ? 39.235  -6.711  18.570  1.00 37.91  ? 151 SER H C   1 
ATOM   12963 O O   . SER H  1 159 ? 38.041  -7.005  18.571  1.00 34.52  ? 151 SER H O   1 
ATOM   12964 C CB  . SER H  1 159 ? 40.203  -7.612  20.734  1.00 32.91  ? 151 SER H CB  1 
ATOM   12965 O OG  . SER H  1 159 ? 40.554  -8.717  19.929  1.00 52.14  ? 151 SER H OG  1 
ATOM   12966 N N   . VAL H  1 160 ? 39.953  -6.679  17.445  1.00 42.32  ? 152 VAL H N   1 
ATOM   12967 C CA  . VAL H  1 160 ? 39.351  -7.006  16.144  1.00 44.31  ? 152 VAL H CA  1 
ATOM   12968 C C   . VAL H  1 160 ? 39.854  -8.329  15.549  1.00 48.03  ? 152 VAL H C   1 
ATOM   12969 O O   . VAL H  1 160 ? 41.033  -8.487  15.236  1.00 52.14  ? 152 VAL H O   1 
ATOM   12970 C CB  . VAL H  1 160 ? 39.553  -5.880  15.103  1.00 41.23  ? 152 VAL H CB  1 
ATOM   12971 C CG1 . VAL H  1 160 ? 38.707  -4.662  15.433  1.00 40.24  ? 152 VAL H CG1 1 
ATOM   12972 C CG2 . VAL H  1 160 ? 40.975  -5.491  15.070  1.00 44.41  ? 152 VAL H CG2 1 
ATOM   12973 N N   . ASP H  1 161 ? 38.936  -9.279  15.398  1.00 52.38  ? 153 ASP H N   1 
ATOM   12974 C CA  . ASP H  1 161 ? 39.235  -10.589 14.829  1.00 50.17  ? 153 ASP H CA  1 
ATOM   12975 C C   . ASP H  1 161 ? 38.558  -10.745 13.465  1.00 47.01  ? 153 ASP H C   1 
ATOM   12976 O O   . ASP H  1 161 ? 37.519  -10.150 13.216  1.00 44.32  ? 153 ASP H O   1 
ATOM   12977 C CB  . ASP H  1 161 ? 38.762  -11.682 15.788  1.00 43.32  ? 153 ASP H CB  1 
ATOM   12978 C CG  . ASP H  1 161 ? 39.215  -11.430 17.220  1.00 55.39  ? 153 ASP H CG  1 
ATOM   12979 O OD1 . ASP H  1 161 ? 40.078  -10.545 17.413  1.00 49.55  ? 153 ASP H OD1 1 
ATOM   12980 O OD2 . ASP H  1 161 ? 38.716  -12.109 18.152  1.00 56.67  ? 153 ASP H OD2 1 
ATOM   12981 N N   . PRO H  1 162 ? 39.156  -11.529 12.563  1.00 52.30  ? 154 PRO H N   1 
ATOM   12982 C CA  . PRO H  1 162 ? 38.508  -11.703 11.263  1.00 52.09  ? 154 PRO H CA  1 
ATOM   12983 C C   . PRO H  1 162 ? 37.964  -13.115 11.074  1.00 54.78  ? 154 PRO H C   1 
ATOM   12984 O O   . PRO H  1 162 ? 38.116  -13.951 11.967  1.00 57.38  ? 154 PRO H O   1 
ATOM   12985 C CB  . PRO H  1 162 ? 39.647  -11.416 10.281  1.00 43.51  ? 154 PRO H CB  1 
ATOM   12986 C CG  . PRO H  1 162 ? 40.936  -11.675 11.089  1.00 53.00  ? 154 PRO H CG  1 
ATOM   12987 C CD  . PRO H  1 162 ? 40.551  -11.978 12.520  1.00 49.59  ? 154 PRO H CD  1 
ATOM   12988 N N   . THR H  1 163 ? 37.343  -13.363 9.922   1.00 56.80  ? 155 THR H N   1 
ATOM   12989 C CA  . THR H  1 163 ? 36.664  -14.631 9.640   1.00 58.57  ? 155 THR H CA  1 
ATOM   12990 C C   . THR H  1 163 ? 35.549  -14.880 10.650  1.00 60.85  ? 155 THR H C   1 
ATOM   12991 O O   . THR H  1 163 ? 34.743  -13.986 10.920  1.00 56.83  ? 155 THR H O   1 
ATOM   12992 C CB  . THR H  1 163 ? 37.647  -15.840 9.571   1.00 65.54  ? 155 THR H CB  1 
ATOM   12993 O OG1 . THR H  1 163 ? 37.964  -16.126 8.200   1.00 76.14  ? 155 THR H OG1 1 
ATOM   12994 C CG2 . THR H  1 163 ? 37.035  -17.085 10.208  1.00 66.63  ? 155 THR H CG2 1 
ATOM   12995 N N   . ASP H  1 168 ? 36.342  -18.147 -0.797  1.00 70.59  ? 160 ASP H N   1 
ATOM   12996 C CA  . ASP H  1 168 ? 34.897  -18.317 -0.890  1.00 72.70  ? 160 ASP H CA  1 
ATOM   12997 C C   . ASP H  1 168 ? 34.174  -16.983 -0.737  1.00 69.48  ? 160 ASP H C   1 
ATOM   12998 O O   . ASP H  1 168 ? 33.133  -16.901 -0.086  1.00 64.01  ? 160 ASP H O   1 
ATOM   12999 C CB  . ASP H  1 168 ? 34.405  -19.306 0.168   1.00 64.74  ? 160 ASP H CB  1 
ATOM   13000 C CG  . ASP H  1 168 ? 34.736  -18.862 1.580   1.00 66.56  ? 160 ASP H CG  1 
ATOM   13001 O OD1 . ASP H  1 168 ? 33.818  -18.836 2.427   1.00 67.22  ? 160 ASP H OD1 1 
ATOM   13002 O OD2 . ASP H  1 168 ? 35.913  -18.539 1.842   1.00 61.51  ? 160 ASP H OD2 1 
ATOM   13003 N N   . ASP H  1 169 ? 34.734  -15.939 -1.341  1.00 69.30  ? 161 ASP H N   1 
ATOM   13004 C CA  . ASP H  1 169 ? 34.144  -14.608 -1.273  1.00 75.65  ? 161 ASP H CA  1 
ATOM   13005 C C   . ASP H  1 169 ? 33.462  -14.239 -2.587  1.00 63.41  ? 161 ASP H C   1 
ATOM   13006 O O   . ASP H  1 169 ? 33.102  -13.083 -2.807  1.00 58.78  ? 161 ASP H O   1 
ATOM   13007 C CB  . ASP H  1 169 ? 35.210  -13.567 -0.924  1.00 73.99  ? 161 ASP H CB  1 
ATOM   13008 C CG  . ASP H  1 169 ? 34.619  -12.306 -0.325  1.00 55.16  ? 161 ASP H CG  1 
ATOM   13009 O OD1 . ASP H  1 169 ? 35.395  -11.392 0.024   1.00 44.00  ? 161 ASP H OD1 1 
ATOM   13010 O OD2 . ASP H  1 169 ? 33.378  -12.230 -0.202  1.00 58.21  ? 161 ASP H OD2 1 
ATOM   13011 N N   . SER H  1 170 ? 33.288  -15.230 -3.455  1.00 65.81  ? 162 SER H N   1 
ATOM   13012 C CA  . SER H  1 170 ? 32.650  -15.012 -4.748  1.00 69.70  ? 162 SER H CA  1 
ATOM   13013 C C   . SER H  1 170 ? 31.194  -15.467 -4.729  1.00 61.12  ? 162 SER H C   1 
ATOM   13014 O O   . SER H  1 170 ? 30.585  -15.674 -5.779  1.00 61.82  ? 162 SER H O   1 
ATOM   13015 C CB  . SER H  1 170 ? 33.415  -15.743 -5.853  1.00 64.02  ? 162 SER H CB  1 
ATOM   13016 O OG  . SER H  1 170 ? 33.674  -17.088 -5.491  1.00 60.37  ? 162 SER H OG  1 
ATOM   13017 N N   . GLU H  1 171 ? 30.674  -15.706 -3.526  1.00 30.00  ? 163 GLU H N   1 
ATOM   13018 C CA  . GLU H  1 171 ? 29.260  -16.030 -3.317  1.00 30.00  ? 163 GLU H CA  1 
ATOM   13019 C C   . GLU H  1 171 ? 28.298  -14.881 -3.641  1.00 30.00  ? 163 GLU H C   1 
ATOM   13020 O O   . GLU H  1 171 ? 27.249  -15.089 -4.251  1.00 30.00  ? 163 GLU H O   1 
ATOM   13021 C CB  . GLU H  1 171 ? 29.032  -16.509 -1.881  1.00 20.00  ? 163 GLU H CB  1 
ATOM   13022 C CG  . GLU H  1 171 ? 27.780  -17.352 -1.700  1.00 20.00  ? 163 GLU H CG  1 
ATOM   13023 C CD  . GLU H  1 171 ? 27.722  -18.024 -0.342  1.00 20.00  ? 163 GLU H CD  1 
ATOM   13024 O OE1 . GLU H  1 171 ? 26.607  -18.171 0.203   1.00 20.00  ? 163 GLU H OE1 1 
ATOM   13025 O OE2 . GLU H  1 171 ? 28.790  -18.405 0.181   1.00 20.00  ? 163 GLU H OE2 1 
ATOM   13026 N N   . TYR H  1 172 ? 28.670  -13.673 -3.226  1.00 47.62  ? 164 TYR H N   1 
ATOM   13027 C CA  . TYR H  1 172 ? 27.859  -12.471 -3.442  1.00 47.72  ? 164 TYR H CA  1 
ATOM   13028 C C   . TYR H  1 172 ? 28.420  -11.424 -4.419  1.00 42.61  ? 164 TYR H C   1 
ATOM   13029 O O   . TYR H  1 172 ? 27.793  -10.387 -4.634  1.00 44.60  ? 164 TYR H O   1 
ATOM   13030 C CB  . TYR H  1 172 ? 27.543  -11.803 -2.100  1.00 60.08  ? 164 TYR H CB  1 
ATOM   13031 C CG  . TYR H  1 172 ? 27.480  -12.765 -0.936  1.00 52.51  ? 164 TYR H CG  1 
ATOM   13032 C CD1 . TYR H  1 172 ? 28.540  -12.883 -0.048  1.00 51.65  ? 164 TYR H CD1 1 
ATOM   13033 C CD2 . TYR H  1 172 ? 26.359  -13.557 -0.725  1.00 49.16  ? 164 TYR H CD2 1 
ATOM   13034 C CE1 . TYR H  1 172 ? 28.487  -13.761 1.017   1.00 53.86  ? 164 TYR H CE1 1 
ATOM   13035 C CE2 . TYR H  1 172 ? 26.296  -14.439 0.337   1.00 57.95  ? 164 TYR H CE2 1 
ATOM   13036 C CZ  . TYR H  1 172 ? 27.362  -14.537 1.205   1.00 55.78  ? 164 TYR H CZ  1 
ATOM   13037 O OH  . TYR H  1 172 ? 27.304  -15.413 2.264   1.00 53.03  ? 164 TYR H OH  1 
ATOM   13038 N N   . PHE H  1 173 ? 29.586  -11.682 -5.004  1.00 49.37  ? 165 PHE H N   1 
ATOM   13039 C CA  . PHE H  1 173 ? 30.206  -10.716 -5.908  1.00 36.57  ? 165 PHE H CA  1 
ATOM   13040 C C   . PHE H  1 173 ? 29.381  -10.553 -7.179  1.00 34.92  ? 165 PHE H C   1 
ATOM   13041 O O   . PHE H  1 173 ? 28.849  -11.531 -7.704  1.00 41.68  ? 165 PHE H O   1 
ATOM   13042 C CB  . PHE H  1 173 ? 31.632  -11.146 -6.256  1.00 33.97  ? 165 PHE H CB  1 
ATOM   13043 C CG  . PHE H  1 173 ? 32.460  -10.054 -6.872  1.00 39.48  ? 165 PHE H CG  1 
ATOM   13044 C CD1 . PHE H  1 173 ? 32.799  -8.928  -6.141  1.00 37.04  ? 165 PHE H CD1 1 
ATOM   13045 C CD2 . PHE H  1 173 ? 32.900  -10.155 -8.181  1.00 33.63  ? 165 PHE H CD2 1 
ATOM   13046 C CE1 . PHE H  1 173 ? 33.562  -7.922  -6.704  1.00 34.32  ? 165 PHE H CE1 1 
ATOM   13047 C CE2 . PHE H  1 173 ? 33.662  -9.153  -8.751  1.00 38.00  ? 165 PHE H CE2 1 
ATOM   13048 C CZ  . PHE H  1 173 ? 33.994  -8.034  -8.011  1.00 36.29  ? 165 PHE H CZ  1 
ATOM   13049 N N   . SER H  1 174 ? 29.276  -9.325  -7.681  1.00 29.66  ? 166 SER H N   1 
ATOM   13050 C CA  . SER H  1 174 ? 28.541  -9.108  -8.920  1.00 29.07  ? 166 SER H CA  1 
ATOM   13051 C C   . SER H  1 174 ? 29.194  -9.794  -10.114 1.00 44.53  ? 166 SER H C   1 
ATOM   13052 O O   . SER H  1 174 ? 30.397  -9.653  -10.351 1.00 44.33  ? 166 SER H O   1 
ATOM   13053 C CB  . SER H  1 174 ? 28.426  -7.609  -9.205  1.00 27.48  ? 166 SER H CB  1 
ATOM   13054 O OG  . SER H  1 174 ? 27.477  -7.353  -10.227 1.00 33.64  ? 166 SER H OG  1 
ATOM   13055 N N   . GLN H  1 175 ? 28.391  -10.529 -10.873 1.00 51.12  ? 167 GLN H N   1 
ATOM   13056 C CA  . GLN H  1 175 ? 28.874  -11.169 -12.087 1.00 41.45  ? 167 GLN H CA  1 
ATOM   13057 C C   . GLN H  1 175 ? 28.882  -10.176 -13.246 1.00 38.85  ? 167 GLN H C   1 
ATOM   13058 O O   . GLN H  1 175 ? 29.257  -10.530 -14.362 1.00 33.35  ? 167 GLN H O   1 
ATOM   13059 C CB  . GLN H  1 175 ? 28.013  -12.388 -12.419 1.00 49.16  ? 167 GLN H CB  1 
ATOM   13060 C CG  . GLN H  1 175 ? 26.553  -12.058 -12.685 1.00 54.60  ? 167 GLN H CG  1 
ATOM   13061 C CD  . GLN H  1 175 ? 25.666  -13.292 -12.730 1.00 62.98  ? 167 GLN H CD  1 
ATOM   13062 O OE1 . GLN H  1 175 ? 26.042  -14.363 -12.248 1.00 70.12  ? 167 GLN H OE1 1 
ATOM   13063 N NE2 . GLN H  1 175 ? 24.479  -13.145 -13.310 1.00 64.97  ? 167 GLN H NE2 1 
ATOM   13064 N N   . TYR H  1 176 ? 28.477  -8.933  -12.967 1.00 39.72  ? 168 TYR H N   1 
ATOM   13065 C CA  . TYR H  1 176 ? 28.401  -7.878  -13.984 1.00 34.72  ? 168 TYR H CA  1 
ATOM   13066 C C   . TYR H  1 176 ? 29.459  -6.807  -13.775 1.00 30.84  ? 168 TYR H C   1 
ATOM   13067 O O   . TYR H  1 176 ? 29.486  -5.806  -14.488 1.00 29.95  ? 168 TYR H O   1 
ATOM   13068 C CB  . TYR H  1 176 ? 27.003  -7.246  -14.025 1.00 38.80  ? 168 TYR H CB  1 
ATOM   13069 C CG  . TYR H  1 176 ? 25.903  -8.258  -14.252 1.00 47.41  ? 168 TYR H CG  1 
ATOM   13070 C CD1 . TYR H  1 176 ? 25.729  -8.859  -15.500 1.00 46.43  ? 168 TYR H CD1 1 
ATOM   13071 C CD2 . TYR H  1 176 ? 25.053  -8.635  -13.219 1.00 46.92  ? 168 TYR H CD2 1 
ATOM   13072 C CE1 . TYR H  1 176 ? 24.735  -9.802  -15.713 1.00 47.60  ? 168 TYR H CE1 1 
ATOM   13073 C CE2 . TYR H  1 176 ? 24.051  -9.578  -13.423 1.00 54.19  ? 168 TYR H CE2 1 
ATOM   13074 C CZ  . TYR H  1 176 ? 23.899  -10.155 -14.673 1.00 53.41  ? 168 TYR H CZ  1 
ATOM   13075 O OH  . TYR H  1 176 ? 22.912  -11.088 -14.878 1.00 55.77  ? 168 TYR H OH  1 
ATOM   13076 N N   . SER H  1 177 ? 30.330  -7.023  -12.794 1.00 30.83  ? 169 SER H N   1 
ATOM   13077 C CA  . SER H  1 177 ? 31.468  -6.138  -12.572 1.00 35.20  ? 169 SER H CA  1 
ATOM   13078 C C   . SER H  1 177 ? 32.504  -6.353  -13.670 1.00 37.02  ? 169 SER H C   1 
ATOM   13079 O O   . SER H  1 177 ? 32.812  -7.495  -14.013 1.00 39.18  ? 169 SER H O   1 
ATOM   13080 C CB  . SER H  1 177 ? 32.103  -6.422  -11.205 1.00 38.93  ? 169 SER H CB  1 
ATOM   13081 O OG  . SER H  1 177 ? 33.293  -5.666  -11.000 1.00 33.80  ? 169 SER H OG  1 
ATOM   13082 N N   . ARG H  1 178 ? 33.058  -5.270  -14.211 1.00 36.12  ? 170 ARG H N   1 
ATOM   13083 C CA  . ARG H  1 178 ? 34.059  -5.401  -15.270 1.00 31.98  ? 170 ARG H CA  1 
ATOM   13084 C C   . ARG H  1 178 ? 35.413  -5.864  -14.707 1.00 36.82  ? 170 ARG H C   1 
ATOM   13085 O O   . ARG H  1 178 ? 36.431  -5.847  -15.406 1.00 52.26  ? 170 ARG H O   1 
ATOM   13086 C CB  . ARG H  1 178 ? 34.161  -4.119  -16.131 1.00 28.90  ? 170 ARG H CB  1 
ATOM   13087 C CG  . ARG H  1 178 ? 35.084  -3.016  -15.607 1.00 38.33  ? 170 ARG H CG  1 
ATOM   13088 C CD  . ARG H  1 178 ? 34.840  -1.650  -16.288 1.00 42.49  ? 170 ARG H CD  1 
ATOM   13089 N NE  . ARG H  1 178 ? 35.772  -0.604  -15.833 1.00 59.84  ? 170 ARG H NE  1 
ATOM   13090 C CZ  . ARG H  1 178 ? 35.600  0.157   -14.745 1.00 55.98  ? 170 ARG H CZ  1 
ATOM   13091 N NH1 . ARG H  1 178 ? 34.527  -0.005  -13.979 1.00 48.33  ? 170 ARG H NH1 1 
ATOM   13092 N NH2 . ARG H  1 178 ? 36.505  1.077   -14.408 1.00 45.67  ? 170 ARG H NH2 1 
ATOM   13093 N N   . PHE H  1 179 ? 35.409  -6.295  -13.447 1.00 31.36  ? 171 PHE H N   1 
ATOM   13094 C CA  . PHE H  1 179 ? 36.583  -6.882  -12.797 1.00 35.43  ? 171 PHE H CA  1 
ATOM   13095 C C   . PHE H  1 179 ? 36.203  -8.242  -12.224 1.00 34.66  ? 171 PHE H C   1 
ATOM   13096 O O   . PHE H  1 179 ? 35.061  -8.682  -12.352 1.00 37.60  ? 171 PHE H O   1 
ATOM   13097 C CB  . PHE H  1 179 ? 37.131  -5.970  -11.684 1.00 33.91  ? 171 PHE H CB  1 
ATOM   13098 C CG  . PHE H  1 179 ? 37.557  -4.620  -12.171 1.00 31.32  ? 171 PHE H CG  1 
ATOM   13099 C CD1 . PHE H  1 179 ? 36.630  -3.618  -12.375 1.00 30.73  ? 171 PHE H CD1 1 
ATOM   13100 C CD2 . PHE H  1 179 ? 38.881  -4.356  -12.448 1.00 37.00  ? 171 PHE H CD2 1 
ATOM   13101 C CE1 . PHE H  1 179 ? 37.018  -2.376  -12.841 1.00 33.73  ? 171 PHE H CE1 1 
ATOM   13102 C CE2 . PHE H  1 179 ? 39.271  -3.111  -12.921 1.00 36.54  ? 171 PHE H CE2 1 
ATOM   13103 C CZ  . PHE H  1 179 ? 38.336  -2.128  -13.126 1.00 30.16  ? 171 PHE H CZ  1 
ATOM   13104 N N   . GLU H  1 180 ? 37.159  -8.912  -11.597 1.00 33.42  ? 172 GLU H N   1 
ATOM   13105 C CA  . GLU H  1 180 ? 36.892  -10.216 -11.007 1.00 36.03  ? 172 GLU H CA  1 
ATOM   13106 C C   . GLU H  1 180 ? 37.851  -10.483 -9.867  1.00 36.50  ? 172 GLU H C   1 
ATOM   13107 O O   . GLU H  1 180 ? 38.955  -9.935  -9.820  1.00 38.60  ? 172 GLU H O   1 
ATOM   13108 C CB  . GLU H  1 180 ? 36.943  -11.344 -12.048 1.00 42.92  ? 172 GLU H CB  1 
ATOM   13109 C CG  . GLU H  1 180 ? 38.257  -11.486 -12.826 1.00 49.19  ? 172 GLU H CG  1 
ATOM   13110 C CD  . GLU H  1 180 ? 38.297  -12.758 -13.682 1.00 58.68  ? 172 GLU H CD  1 
ATOM   13111 O OE1 . GLU H  1 180 ? 38.128  -13.865 -13.120 1.00 60.30  ? 172 GLU H OE1 1 
ATOM   13112 O OE2 . GLU H  1 180 ? 38.493  -12.653 -14.915 1.00 54.19  ? 172 GLU H OE2 1 
ATOM   13113 N N   . ILE H  1 181 ? 37.417  -11.327 -8.945  1.00 35.05  ? 173 ILE H N   1 
ATOM   13114 C CA  . ILE H  1 181 ? 38.110  -11.473 -7.680  1.00 39.12  ? 173 ILE H CA  1 
ATOM   13115 C C   . ILE H  1 181 ? 38.837  -12.800 -7.607  1.00 42.11  ? 173 ILE H C   1 
ATOM   13116 O O   . ILE H  1 181 ? 38.228  -13.861 -7.739  1.00 39.91  ? 173 ILE H O   1 
ATOM   13117 C CB  . ILE H  1 181 ? 37.129  -11.353 -6.502  1.00 34.08  ? 173 ILE H CB  1 
ATOM   13118 C CG1 . ILE H  1 181 ? 36.638  -9.915  -6.376  1.00 36.06  ? 173 ILE H CG1 1 
ATOM   13119 C CG2 . ILE H  1 181 ? 37.777  -11.800 -5.210  1.00 40.66  ? 173 ILE H CG2 1 
ATOM   13120 C CD1 . ILE H  1 181 ? 35.891  -9.660  -5.086  1.00 43.77  ? 173 ILE H CD1 1 
ATOM   13121 N N   . LEU H  1 182 ? 40.160  -12.702 -7.718  1.00 40.60  ? 174 LEU H N   1 
ATOM   13122 C CA  . LEU H  1 182 ? 41.068  -13.846 -7.667  1.00 44.56  ? 174 LEU H CA  1 
ATOM   13123 C C   . LEU H  1 182 ? 41.148  -14.478 -6.289  1.00 48.63  ? 174 LEU H C   1 
ATOM   13124 O O   . LEU H  1 182 ? 41.172  -15.700 -6.141  1.00 48.33  ? 174 LEU H O   1 
ATOM   13125 C CB  . LEU H  1 182 ? 42.467  -13.437 -8.136  1.00 47.87  ? 174 LEU H CB  1 
ATOM   13126 C CG  . LEU H  1 182 ? 42.535  -12.599 -9.414  1.00 43.02  ? 174 LEU H CG  1 
ATOM   13127 C CD1 . LEU H  1 182 ? 43.974  -12.218 -9.730  1.00 44.39  ? 174 LEU H CD1 1 
ATOM   13128 C CD2 . LEU H  1 182 ? 41.905  -13.345 -10.580 1.00 43.31  ? 174 LEU H CD2 1 
ATOM   13129 N N   . ASP H  1 183 ? 41.198  -13.614 -5.283  1.00 47.73  ? 175 ASP H N   1 
ATOM   13130 C CA  . ASP H  1 183 ? 41.400  -14.028 -3.906  1.00 51.09  ? 175 ASP H CA  1 
ATOM   13131 C C   . ASP H  1 183 ? 40.987  -12.944 -2.921  1.00 50.02  ? 175 ASP H C   1 
ATOM   13132 O O   . ASP H  1 183 ? 40.845  -11.774 -3.277  1.00 54.44  ? 175 ASP H O   1 
ATOM   13133 C CB  . ASP H  1 183 ? 42.863  -14.415 -3.675  1.00 60.10  ? 175 ASP H CB  1 
ATOM   13134 C CG  . ASP H  1 183 ? 43.090  -15.048 -2.316  1.00 68.16  ? 175 ASP H CG  1 
ATOM   13135 O OD1 . ASP H  1 183 ? 42.094  -15.397 -1.648  1.00 63.92  ? 175 ASP H OD1 1 
ATOM   13136 O OD2 . ASP H  1 183 ? 44.264  -15.196 -1.916  1.00 78.05  ? 175 ASP H OD2 1 
ATOM   13137 N N   . VAL H  1 184 ? 40.804  -13.357 -1.675  1.00 53.04  ? 176 VAL H N   1 
ATOM   13138 C CA  . VAL H  1 184 ? 40.501  -12.457 -0.571  1.00 51.19  ? 176 VAL H CA  1 
ATOM   13139 C C   . VAL H  1 184 ? 40.981  -13.051 0.754   1.00 56.91  ? 176 VAL H C   1 
ATOM   13140 O O   . VAL H  1 184 ? 40.590  -14.166 1.136   1.00 46.23  ? 176 VAL H O   1 
ATOM   13141 C CB  . VAL H  1 184 ? 39.011  -12.119 -0.477  1.00 46.94  ? 176 VAL H CB  1 
ATOM   13142 C CG1 . VAL H  1 184 ? 38.734  -11.377 0.824   1.00 47.16  ? 176 VAL H CG1 1 
ATOM   13143 C CG2 . VAL H  1 184 ? 38.594  -11.282 -1.658  1.00 38.04  ? 176 VAL H CG2 1 
ATOM   13144 N N   . THR H  1 185 ? 41.843  -12.297 1.435   1.00 48.91  ? 177 THR H N   1 
ATOM   13145 C CA  . THR H  1 185 ? 42.408  -12.717 2.707   1.00 49.40  ? 177 THR H CA  1 
ATOM   13146 C C   . THR H  1 185 ? 42.175  -11.642 3.750   1.00 44.42  ? 177 THR H C   1 
ATOM   13147 O O   . THR H  1 185 ? 42.163  -10.454 3.431   1.00 45.43  ? 177 THR H O   1 
ATOM   13148 C CB  . THR H  1 185 ? 43.926  -12.992 2.598   1.00 59.96  ? 177 THR H CB  1 
ATOM   13149 O OG1 . THR H  1 185 ? 44.625  -11.772 2.317   1.00 59.93  ? 177 THR H OG1 1 
ATOM   13150 C CG2 . THR H  1 185 ? 44.204  -13.988 1.495   1.00 58.10  ? 177 THR H CG2 1 
ATOM   13151 N N   . GLN H  1 186 ? 41.982  -12.070 4.995   1.00 45.23  ? 178 GLN H N   1 
ATOM   13152 C CA  . GLN H  1 186 ? 41.765  -11.153 6.108   1.00 41.46  ? 178 GLN H CA  1 
ATOM   13153 C C   . GLN H  1 186 ? 42.667  -11.543 7.271   1.00 41.67  ? 178 GLN H C   1 
ATOM   13154 O O   . GLN H  1 186 ? 42.576  -12.658 7.794   1.00 39.02  ? 178 GLN H O   1 
ATOM   13155 C CB  . GLN H  1 186 ? 40.297  -11.172 6.542   1.00 48.05  ? 178 GLN H CB  1 
ATOM   13156 C CG  . GLN H  1 186 ? 39.347  -10.500 5.565   1.00 48.16  ? 178 GLN H CG  1 
ATOM   13157 C CD  . GLN H  1 186 ? 37.885  -10.796 5.854   1.00 48.75  ? 178 GLN H CD  1 
ATOM   13158 O OE1 . GLN H  1 186 ? 36.995  -10.308 5.152   1.00 43.26  ? 178 GLN H OE1 1 
ATOM   13159 N NE2 . GLN H  1 186 ? 37.629  -11.603 6.885   1.00 48.30  ? 178 GLN H NE2 1 
ATOM   13160 N N   . LYS H  1 187 ? 43.533  -10.616 7.669   1.00 42.28  ? 179 LYS H N   1 
ATOM   13161 C CA  . LYS H  1 187 ? 44.557  -10.892 8.672   1.00 46.85  ? 179 LYS H CA  1 
ATOM   13162 C C   . LYS H  1 187 ? 44.523  -9.877  9.822   1.00 49.65  ? 179 LYS H C   1 
ATOM   13163 O O   . LYS H  1 187 ? 44.360  -8.669  9.601   1.00 39.45  ? 179 LYS H O   1 
ATOM   13164 C CB  . LYS H  1 187 ? 45.950  -10.916 8.015   1.00 39.62  ? 179 LYS H CB  1 
ATOM   13165 C CG  . LYS H  1 187 ? 47.120  -11.111 8.982   1.00 48.72  ? 179 LYS H CG  1 
ATOM   13166 C CD  . LYS H  1 187 ? 47.461  -12.591 9.169   1.00 65.77  ? 179 LYS H CD  1 
ATOM   13167 C CE  . LYS H  1 187 ? 48.339  -12.848 10.398  1.00 58.54  ? 179 LYS H CE  1 
ATOM   13168 N NZ  . LYS H  1 187 ? 48.691  -14.296 10.546  1.00 43.76  ? 179 LYS H NZ  1 
ATOM   13169 N N   . LYS H  1 188 ? 44.674  -10.382 11.047  1.00 49.09  ? 180 LYS H N   1 
ATOM   13170 C CA  . LYS H  1 188 ? 44.808  -9.538  12.228  1.00 43.97  ? 180 LYS H CA  1 
ATOM   13171 C C   . LYS H  1 188 ? 46.156  -8.835  12.222  1.00 43.64  ? 180 LYS H C   1 
ATOM   13172 O O   . LYS H  1 188 ? 47.196  -9.454  11.995  1.00 49.42  ? 180 LYS H O   1 
ATOM   13173 C CB  . LYS H  1 188 ? 44.637  -10.362 13.511  1.00 47.56  ? 180 LYS H CB  1 
ATOM   13174 C CG  . LYS H  1 188 ? 44.682  -11.872 13.286  1.00 52.68  ? 180 LYS H CG  1 
ATOM   13175 C CD  . LYS H  1 188 ? 43.657  -12.591 14.156  1.00 63.91  ? 180 LYS H CD  1 
ATOM   13176 C CE  . LYS H  1 188 ? 43.306  -13.972 13.597  1.00 69.58  ? 180 LYS H CE  1 
ATOM   13177 N NZ  . LYS H  1 188 ? 42.031  -14.503 14.184  1.00 65.90  ? 180 LYS H NZ  1 
ATOM   13178 N N   . ASN H  1 189 ? 46.122  -7.534  12.468  1.00 45.38  ? 181 ASN H N   1 
ATOM   13179 C CA  . ASN H  1 189 ? 47.310  -6.695  12.471  1.00 47.49  ? 181 ASN H CA  1 
ATOM   13180 C C   . ASN H  1 189 ? 47.277  -5.879  13.754  1.00 47.30  ? 181 ASN H C   1 
ATOM   13181 O O   . ASN H  1 189 ? 46.238  -5.805  14.406  1.00 49.67  ? 181 ASN H O   1 
ATOM   13182 C CB  . ASN H  1 189 ? 47.281  -5.772  11.246  1.00 45.16  ? 181 ASN H CB  1 
ATOM   13183 C CG  . ASN H  1 189 ? 48.611  -5.083  10.982  1.00 53.76  ? 181 ASN H CG  1 
ATOM   13184 O OD1 . ASN H  1 189 ? 49.665  -5.522  11.451  1.00 55.41  ? 181 ASN H OD1 1 
ATOM   13185 N ND2 . ASN H  1 189 ? 48.566  -3.999  10.209  1.00 56.20  ? 181 ASN H ND2 1 
ATOM   13186 N N   . SER H  1 190 ? 48.403  -5.283  14.131  1.00 44.52  ? 182 SER H N   1 
ATOM   13187 C CA  . SER H  1 190 ? 48.428  -4.374  15.275  1.00 46.92  ? 182 SER H CA  1 
ATOM   13188 C C   . SER H  1 190 ? 49.308  -3.177  14.978  1.00 53.57  ? 182 SER H C   1 
ATOM   13189 O O   . SER H  1 190 ? 50.477  -3.328  14.626  1.00 59.54  ? 182 SER H O   1 
ATOM   13190 C CB  . SER H  1 190 ? 48.918  -5.075  16.540  1.00 46.10  ? 182 SER H CB  1 
ATOM   13191 O OG  . SER H  1 190 ? 47.971  -6.021  16.997  1.00 47.76  ? 182 SER H OG  1 
ATOM   13192 N N   . VAL H  1 191 ? 48.744  -1.984  15.122  1.00 49.55  ? 183 VAL H N   1 
ATOM   13193 C CA  . VAL H  1 191 ? 49.491  -0.769  14.845  1.00 51.01  ? 183 VAL H CA  1 
ATOM   13194 C C   . VAL H  1 191 ? 49.784  -0.003  16.129  1.00 52.70  ? 183 VAL H C   1 
ATOM   13195 O O   . VAL H  1 191 ? 49.057  -0.135  17.115  1.00 41.62  ? 183 VAL H O   1 
ATOM   13196 C CB  . VAL H  1 191 ? 48.714  0.164   13.914  1.00 52.09  ? 183 VAL H CB  1 
ATOM   13197 C CG1 . VAL H  1 191 ? 49.680  0.993   13.123  1.00 45.26  ? 183 VAL H CG1 1 
ATOM   13198 C CG2 . VAL H  1 191 ? 47.790  -0.630  12.996  1.00 44.64  ? 183 VAL H CG2 1 
ATOM   13199 N N   . THR H  1 192 ? 50.850  0.794   16.107  1.00 53.94  ? 184 THR H N   1 
ATOM   13200 C CA  . THR H  1 192 ? 51.155  1.709   17.204  1.00 55.16  ? 184 THR H CA  1 
ATOM   13201 C C   . THR H  1 192 ? 51.459  3.121   16.686  1.00 55.96  ? 184 THR H C   1 
ATOM   13202 O O   . THR H  1 192 ? 52.450  3.342   15.986  1.00 55.01  ? 184 THR H O   1 
ATOM   13203 C CB  . THR H  1 192 ? 52.314  1.194   18.084  1.00 55.15  ? 184 THR H CB  1 
ATOM   13204 O OG1 . THR H  1 192 ? 53.448  0.887   17.259  1.00 58.44  ? 184 THR H OG1 1 
ATOM   13205 C CG2 . THR H  1 192 ? 51.890  -0.055  18.851  1.00 37.31  ? 184 THR H CG2 1 
ATOM   13206 N N   . TYR H  1 193 ? 50.585  4.062   17.040  1.00 57.78  ? 185 TYR H N   1 
ATOM   13207 C CA  . TYR H  1 193 ? 50.696  5.461   16.634  1.00 61.90  ? 185 TYR H CA  1 
ATOM   13208 C C   . TYR H  1 193 ? 51.995  6.078   17.138  1.00 66.57  ? 185 TYR H C   1 
ATOM   13209 O O   . TYR H  1 193 ? 52.610  5.560   18.070  1.00 69.23  ? 185 TYR H O   1 
ATOM   13210 C CB  . TYR H  1 193 ? 49.479  6.252   17.144  1.00 62.30  ? 185 TYR H CB  1 
ATOM   13211 C CG  . TYR H  1 193 ? 49.787  7.393   18.104  1.00 71.52  ? 185 TYR H CG  1 
ATOM   13212 C CD1 . TYR H  1 193 ? 50.078  7.152   19.451  1.00 71.68  ? 185 TYR H CD1 1 
ATOM   13213 C CD2 . TYR H  1 193 ? 49.754  8.717   17.669  1.00 74.67  ? 185 TYR H CD2 1 
ATOM   13214 C CE1 . TYR H  1 193 ? 50.351  8.197   20.325  1.00 67.28  ? 185 TYR H CE1 1 
ATOM   13215 C CE2 . TYR H  1 193 ? 50.023  9.768   18.540  1.00 71.76  ? 185 TYR H CE2 1 
ATOM   13216 C CZ  . TYR H  1 193 ? 50.321  9.500   19.863  1.00 70.18  ? 185 TYR H CZ  1 
ATOM   13217 O OH  . TYR H  1 193 ? 50.586  10.542  20.719  1.00 60.98  ? 185 TYR H OH  1 
ATOM   13218 N N   . SER H  1 194 ? 52.409  7.183   16.521  1.00 68.64  ? 186 SER H N   1 
ATOM   13219 C CA  . SER H  1 194 ? 53.665  7.843   16.885  1.00 70.88  ? 186 SER H CA  1 
ATOM   13220 C C   . SER H  1 194 ? 53.413  9.255   17.418  1.00 66.67  ? 186 SER H C   1 
ATOM   13221 O O   . SER H  1 194 ? 53.174  9.446   18.615  1.00 64.59  ? 186 SER H O   1 
ATOM   13222 C CB  . SER H  1 194 ? 54.626  7.873   15.682  1.00 65.97  ? 186 SER H CB  1 
ATOM   13223 O OG  . SER H  1 194 ? 55.925  8.319   16.045  1.00 62.15  ? 186 SER H OG  1 
ATOM   13224 N N   . PRO H  1 197 ? 50.745  6.213   22.657  1.00 66.30  ? 189 PRO H N   1 
ATOM   13225 C CA  . PRO H  1 197 ? 51.562  5.227   23.378  1.00 67.09  ? 189 PRO H CA  1 
ATOM   13226 C C   . PRO H  1 197 ? 51.047  3.792   23.228  1.00 64.10  ? 189 PRO H C   1 
ATOM   13227 O O   . PRO H  1 197 ? 51.836  2.848   23.227  1.00 60.43  ? 189 PRO H O   1 
ATOM   13228 C CB  . PRO H  1 197 ? 51.455  5.681   24.842  1.00 58.94  ? 189 PRO H CB  1 
ATOM   13229 C CG  . PRO H  1 197 ? 50.195  6.474   24.909  1.00 61.45  ? 189 PRO H CG  1 
ATOM   13230 C CD  . PRO H  1 197 ? 50.055  7.141   23.572  1.00 66.33  ? 189 PRO H CD  1 
ATOM   13231 N N   . GLU H  1 198 ? 49.734  3.639   23.088  1.00 62.34  ? 190 GLU H N   1 
ATOM   13232 C CA  . GLU H  1 198 ? 49.100  2.322   23.066  1.00 50.10  ? 190 GLU H CA  1 
ATOM   13233 C C   . GLU H  1 198 ? 48.876  1.782   21.651  1.00 39.38  ? 190 GLU H C   1 
ATOM   13234 O O   . GLU H  1 198 ? 49.095  2.486   20.667  1.00 41.16  ? 190 GLU H O   1 
ATOM   13235 C CB  . GLU H  1 198 ? 47.768  2.405   23.800  1.00 50.63  ? 190 GLU H CB  1 
ATOM   13236 C CG  . GLU H  1 198 ? 46.941  3.619   23.383  1.00 58.04  ? 190 GLU H CG  1 
ATOM   13237 C CD  . GLU H  1 198 ? 47.056  4.777   24.359  1.00 64.07  ? 190 GLU H CD  1 
ATOM   13238 O OE1 . GLU H  1 198 ? 47.342  4.526   25.553  1.00 63.89  ? 190 GLU H OE1 1 
ATOM   13239 O OE2 . GLU H  1 198 ? 46.854  5.937   23.931  1.00 66.61  ? 190 GLU H OE2 1 
ATOM   13240 N N   . ALA H  1 199 ? 48.417  0.536   21.561  1.00 33.65  ? 191 ALA H N   1 
ATOM   13241 C CA  . ALA H  1 199 ? 48.233  -0.141  20.274  1.00 37.56  ? 191 ALA H CA  1 
ATOM   13242 C C   . ALA H  1 199 ? 46.771  -0.263  19.807  1.00 39.89  ? 191 ALA H C   1 
ATOM   13243 O O   . ALA H  1 199 ? 45.879  -0.601  20.593  1.00 37.95  ? 191 ALA H O   1 
ATOM   13244 C CB  . ALA H  1 199 ? 48.881  -1.526  20.312  1.00 36.09  ? 191 ALA H CB  1 
ATOM   13245 N N   . TYR H  1 200 ? 46.540  -0.013  18.519  1.00 35.59  ? 192 TYR H N   1 
ATOM   13246 C CA  . TYR H  1 200 ? 45.210  -0.156  17.930  1.00 33.18  ? 192 TYR H CA  1 
ATOM   13247 C C   . TYR H  1 200 ? 45.153  -1.359  16.997  1.00 36.43  ? 192 TYR H C   1 
ATOM   13248 O O   . TYR H  1 200 ? 45.803  -1.369  15.955  1.00 45.87  ? 192 TYR H O   1 
ATOM   13249 C CB  . TYR H  1 200 ? 44.803  1.118   17.173  1.00 32.06  ? 192 TYR H CB  1 
ATOM   13250 C CG  . TYR H  1 200 ? 44.833  2.373   18.021  1.00 32.97  ? 192 TYR H CG  1 
ATOM   13251 C CD1 . TYR H  1 200 ? 43.705  2.785   18.728  1.00 33.02  ? 192 TYR H CD1 1 
ATOM   13252 C CD2 . TYR H  1 200 ? 45.989  3.142   18.121  1.00 27.43  ? 192 TYR H CD2 1 
ATOM   13253 C CE1 . TYR H  1 200 ? 43.731  3.925   19.513  1.00 30.32  ? 192 TYR H CE1 1 
ATOM   13254 C CE2 . TYR H  1 200 ? 46.024  4.277   18.898  1.00 33.32  ? 192 TYR H CE2 1 
ATOM   13255 C CZ  . TYR H  1 200 ? 44.894  4.666   19.595  1.00 36.02  ? 192 TYR H CZ  1 
ATOM   13256 O OH  . TYR H  1 200 ? 44.926  5.798   20.377  1.00 47.34  ? 192 TYR H OH  1 
ATOM   13257 N N   . GLU H  1 201 ? 44.379  -2.373  17.370  1.00 34.25  ? 193 GLU H N   1 
ATOM   13258 C CA  . GLU H  1 201 ? 44.212  -3.544  16.518  1.00 35.71  ? 193 GLU H CA  1 
ATOM   13259 C C   . GLU H  1 201 ? 43.365  -3.214  15.297  1.00 39.96  ? 193 GLU H C   1 
ATOM   13260 O O   . GLU H  1 201 ? 42.494  -2.356  15.346  1.00 41.05  ? 193 GLU H O   1 
ATOM   13261 C CB  . GLU H  1 201 ? 43.572  -4.698  17.289  1.00 35.43  ? 193 GLU H CB  1 
ATOM   13262 C CG  . GLU H  1 201 ? 44.405  -5.241  18.437  1.00 38.50  ? 193 GLU H CG  1 
ATOM   13263 C CD  . GLU H  1 201 ? 43.946  -6.617  18.890  1.00 44.02  ? 193 GLU H CD  1 
ATOM   13264 O OE1 . GLU H  1 201 ? 44.536  -7.160  19.857  1.00 45.90  ? 193 GLU H OE1 1 
ATOM   13265 O OE2 . GLU H  1 201 ? 42.997  -7.157  18.274  1.00 39.58  ? 193 GLU H OE2 1 
ATOM   13266 N N   . ASP H  1 202 ? 43.619  -3.907  14.196  1.00 48.40  ? 194 ASP H N   1 
ATOM   13267 C CA  . ASP H  1 202 ? 42.854  -3.689  12.973  1.00 48.53  ? 194 ASP H CA  1 
ATOM   13268 C C   . ASP H  1 202 ? 42.849  -4.953  12.110  1.00 43.48  ? 194 ASP H C   1 
ATOM   13269 O O   . ASP H  1 202 ? 43.579  -5.901  12.388  1.00 48.16  ? 194 ASP H O   1 
ATOM   13270 C CB  . ASP H  1 202 ? 43.415  -2.505  12.199  1.00 46.90  ? 194 ASP H CB  1 
ATOM   13271 C CG  . ASP H  1 202 ? 44.569  -2.894  11.319  1.00 54.45  ? 194 ASP H CG  1 
ATOM   13272 O OD1 . ASP H  1 202 ? 44.310  -3.257  10.151  1.00 57.06  ? 194 ASP H OD1 1 
ATOM   13273 O OD2 . ASP H  1 202 ? 45.728  -2.843  11.792  1.00 57.15  ? 194 ASP H OD2 1 
ATOM   13274 N N   . VAL H  1 203 ? 42.016  -4.981  11.078  1.00 37.57  ? 195 VAL H N   1 
ATOM   13275 C CA  . VAL H  1 203 ? 42.000  -6.133  10.182  1.00 46.93  ? 195 VAL H CA  1 
ATOM   13276 C C   . VAL H  1 203 ? 42.404  -5.745  8.767   1.00 43.49  ? 195 VAL H C   1 
ATOM   13277 O O   . VAL H  1 203 ? 41.668  -5.038  8.082   1.00 37.91  ? 195 VAL H O   1 
ATOM   13278 C CB  . VAL H  1 203 ? 40.629  -6.833  10.144  1.00 44.33  ? 195 VAL H CB  1 
ATOM   13279 C CG1 . VAL H  1 203 ? 40.582  -7.834  8.995   1.00 39.40  ? 195 VAL H CG1 1 
ATOM   13280 C CG2 . VAL H  1 203 ? 40.341  -7.518  11.478  1.00 47.30  ? 195 VAL H CG2 1 
ATOM   13281 N N   . GLU H  1 204 ? 43.584  -6.196  8.342   1.00 46.00  ? 196 GLU H N   1 
ATOM   13282 C CA  . GLU H  1 204 ? 44.022  -5.988  6.964   1.00 46.52  ? 196 GLU H CA  1 
ATOM   13283 C C   . GLU H  1 204 ? 43.222  -6.919  6.070   1.00 38.93  ? 196 GLU H C   1 
ATOM   13284 O O   . GLU H  1 204 ? 43.208  -8.136  6.276   1.00 37.66  ? 196 GLU H O   1 
ATOM   13285 C CB  . GLU H  1 204 ? 45.526  -6.256  6.801   1.00 47.20  ? 196 GLU H CB  1 
ATOM   13286 C CG  . GLU H  1 204 ? 46.375  -5.032  6.418   1.00 54.31  ? 196 GLU H CG  1 
ATOM   13287 C CD  . GLU H  1 204 ? 46.761  -4.163  7.622   1.00 68.62  ? 196 GLU H CD  1 
ATOM   13288 O OE1 . GLU H  1 204 ? 46.131  -4.308  8.686   1.00 61.93  ? 196 GLU H OE1 1 
ATOM   13289 O OE2 . GLU H  1 204 ? 47.699  -3.338  7.515   1.00 73.76  ? 196 GLU H OE2 1 
ATOM   13290 N N   . VAL H  1 205 ? 42.525  -6.341  5.102   1.00 37.48  ? 197 VAL H N   1 
ATOM   13291 C CA  . VAL H  1 205 ? 41.834  -7.137  4.103   1.00 40.78  ? 197 VAL H CA  1 
ATOM   13292 C C   . VAL H  1 205 ? 42.561  -6.959  2.794   1.00 37.78  ? 197 VAL H C   1 
ATOM   13293 O O   . VAL H  1 205 ? 42.631  -5.850  2.266   1.00 35.86  ? 197 VAL H O   1 
ATOM   13294 C CB  . VAL H  1 205 ? 40.381  -6.697  3.910   1.00 41.45  ? 197 VAL H CB  1 
ATOM   13295 C CG1 . VAL H  1 205 ? 39.767  -7.426  2.705   1.00 36.09  ? 197 VAL H CG1 1 
ATOM   13296 C CG2 . VAL H  1 205 ? 39.573  -6.942  5.187   1.00 40.83  ? 197 VAL H CG2 1 
ATOM   13297 N N   . SER H  1 206 ? 43.118  -8.050  2.284   1.00 38.25  ? 198 SER H N   1 
ATOM   13298 C CA  . SER H  1 206 ? 43.828  -8.005  1.013   1.00 44.76  ? 198 SER H CA  1 
ATOM   13299 C C   . SER H  1 206 ? 42.922  -8.486  -0.112  1.00 38.87  ? 198 SER H C   1 
ATOM   13300 O O   . SER H  1 206 ? 42.554  -9.664  -0.173  1.00 37.35  ? 198 SER H O   1 
ATOM   13301 C CB  . SER H  1 206 ? 45.115  -8.831  1.084   1.00 49.47  ? 198 SER H CB  1 
ATOM   13302 O OG  . SER H  1 206 ? 45.957  -8.360  2.127   1.00 52.92  ? 198 SER H OG  1 
ATOM   13303 N N   . LEU H  1 207 ? 42.542  -7.554  -0.981  1.00 36.85  ? 199 LEU H N   1 
ATOM   13304 C CA  . LEU H  1 207 ? 41.678  -7.862  -2.115  1.00 40.84  ? 199 LEU H CA  1 
ATOM   13305 C C   . LEU H  1 207 ? 42.497  -7.908  -3.398  1.00 44.27  ? 199 LEU H C   1 
ATOM   13306 O O   . LEU H  1 207 ? 43.020  -6.883  -3.842  1.00 42.90  ? 199 LEU H O   1 
ATOM   13307 C CB  . LEU H  1 207 ? 40.547  -6.831  -2.253  1.00 36.51  ? 199 LEU H CB  1 
ATOM   13308 C CG  . LEU H  1 207 ? 39.675  -7.019  -3.508  1.00 37.48  ? 199 LEU H CG  1 
ATOM   13309 C CD1 . LEU H  1 207 ? 38.595  -8.071  -3.281  1.00 33.73  ? 199 LEU H CD1 1 
ATOM   13310 C CD2 . LEU H  1 207 ? 39.058  -5.714  -3.997  1.00 31.37  ? 199 LEU H CD2 1 
ATOM   13311 N N   . ASN H  1 208 ? 42.588  -9.102  -3.984  1.00 49.59  ? 200 ASN H N   1 
ATOM   13312 C CA  . ASN H  1 208 ? 43.389  -9.369  -5.184  1.00 40.47  ? 200 ASN H CA  1 
ATOM   13313 C C   . ASN H  1 208 ? 42.515  -9.582  -6.436  1.00 36.25  ? 200 ASN H C   1 
ATOM   13314 O O   . ASN H  1 208 ? 41.761  -10.558 -6.529  1.00 38.48  ? 200 ASN H O   1 
ATOM   13315 C CB  . ASN H  1 208 ? 44.320  -10.553 -4.889  1.00 45.69  ? 200 ASN H CB  1 
ATOM   13316 C CG  . ASN H  1 208 ? 44.858  -11.230 -6.138  1.00 50.50  ? 200 ASN H CG  1 
ATOM   13317 O OD1 . ASN H  1 208 ? 44.833  -12.462 -6.231  1.00 46.55  ? 200 ASN H OD1 1 
ATOM   13318 N ND2 . ASN H  1 208 ? 45.362  -10.440 -7.092  1.00 39.51  ? 200 ASN H ND2 1 
ATOM   13319 N N   . PHE H  1 209 ? 42.615  -8.652  -7.387  1.00 33.51  ? 201 PHE H N   1 
ATOM   13320 C CA  . PHE H  1 209 ? 41.651  -8.559  -8.495  1.00 42.73  ? 201 PHE H CA  1 
ATOM   13321 C C   . PHE H  1 209 ? 42.245  -8.061  -9.829  1.00 42.58  ? 201 PHE H C   1 
ATOM   13322 O O   . PHE H  1 209 ? 43.140  -7.208  -9.841  1.00 37.35  ? 201 PHE H O   1 
ATOM   13323 C CB  . PHE H  1 209 ? 40.490  -7.634  -8.095  1.00 34.06  ? 201 PHE H CB  1 
ATOM   13324 C CG  . PHE H  1 209 ? 40.869  -6.172  -8.029  1.00 31.93  ? 201 PHE H CG  1 
ATOM   13325 C CD1 . PHE H  1 209 ? 41.681  -5.693  -7.016  1.00 34.98  ? 201 PHE H CD1 1 
ATOM   13326 C CD2 . PHE H  1 209 ? 40.407  -5.278  -8.982  1.00 35.00  ? 201 PHE H CD2 1 
ATOM   13327 C CE1 . PHE H  1 209 ? 42.030  -4.363  -6.963  1.00 36.50  ? 201 PHE H CE1 1 
ATOM   13328 C CE2 . PHE H  1 209 ? 40.751  -3.941  -8.928  1.00 27.49  ? 201 PHE H CE2 1 
ATOM   13329 C CZ  . PHE H  1 209 ? 41.562  -3.488  -7.924  1.00 31.35  ? 201 PHE H CZ  1 
ATOM   13330 N N   . ARG H  1 210 ? 41.727  -8.573  -10.947 1.00 34.82  ? 202 ARG H N   1 
ATOM   13331 C CA  . ARG H  1 210 ? 42.176  -8.115  -12.264 1.00 45.99  ? 202 ARG H CA  1 
ATOM   13332 C C   . ARG H  1 210 ? 41.004  -7.734  -13.158 1.00 47.48  ? 202 ARG H C   1 
ATOM   13333 O O   . ARG H  1 210 ? 39.858  -8.054  -12.847 1.00 44.55  ? 202 ARG H O   1 
ATOM   13334 C CB  . ARG H  1 210 ? 43.028  -9.182  -12.963 1.00 49.54  ? 202 ARG H CB  1 
ATOM   13335 C CG  . ARG H  1 210 ? 42.330  -10.531 -13.093 1.00 54.39  ? 202 ARG H CG  1 
ATOM   13336 C CD  . ARG H  1 210 ? 43.002  -11.463 -14.109 1.00 52.93  ? 202 ARG H CD  1 
ATOM   13337 N NE  . ARG H  1 210 ? 42.252  -12.714 -14.230 1.00 56.21  ? 202 ARG H NE  1 
ATOM   13338 C CZ  . ARG H  1 210 ? 42.597  -13.859 -13.648 1.00 55.66  ? 202 ARG H CZ  1 
ATOM   13339 N NH1 . ARG H  1 210 ? 43.699  -13.930 -12.917 1.00 52.74  ? 202 ARG H NH1 1 
ATOM   13340 N NH2 . ARG H  1 210 ? 41.843  -14.938 -13.803 1.00 57.55  ? 202 ARG H NH2 1 
ATOM   13341 N N   . LYS H  1 211 ? 41.301  -7.068  -14.275 1.00 48.79  ? 203 LYS H N   1 
ATOM   13342 C CA  . LYS H  1 211 ? 40.268  -6.670  -15.231 1.00 47.82  ? 203 LYS H CA  1 
ATOM   13343 C C   . LYS H  1 211 ? 39.801  -7.862  -16.072 1.00 53.96  ? 203 LYS H C   1 
ATOM   13344 O O   . LYS H  1 211 ? 40.431  -8.920  -16.061 1.00 51.46  ? 203 LYS H O   1 
ATOM   13345 C CB  . LYS H  1 211 ? 40.763  -5.536  -16.137 1.00 42.87  ? 203 LYS H CB  1 
ATOM   13346 C CG  . LYS H  1 211 ? 39.629  -4.696  -16.697 1.00 43.48  ? 203 LYS H CG  1 
ATOM   13347 C CD  . LYS H  1 211 ? 40.015  -3.958  -17.952 1.00 52.69  ? 203 LYS H CD  1 
ATOM   13348 C CE  . LYS H  1 211 ? 38.773  -3.448  -18.674 1.00 52.52  ? 203 LYS H CE  1 
ATOM   13349 N NZ  . LYS H  1 211 ? 39.111  -2.636  -19.879 1.00 65.44  ? 203 LYS H NZ  1 
ATOM   13350 N N   . LYS H  1 212 ? 38.698  -7.690  -16.799 1.00 56.77  ? 204 LYS H N   1 
ATOM   13351 C CA  . LYS H  1 212 ? 38.149  -8.768  -17.624 1.00 57.64  ? 204 LYS H CA  1 
ATOM   13352 C C   . LYS H  1 212 ? 38.082  -8.452  -19.127 1.00 63.74  ? 204 LYS H C   1 
ATOM   13353 O O   . LYS H  1 212 ? 37.709  -7.350  -19.527 1.00 67.71  ? 204 LYS H O   1 
ATOM   13354 C CB  . LYS H  1 212 ? 36.770  -9.172  -17.104 1.00 55.72  ? 204 LYS H CB  1 
ATOM   13355 C CG  . LYS H  1 212 ? 36.808  -9.796  -15.715 1.00 50.87  ? 204 LYS H CG  1 
ATOM   13356 C CD  . LYS H  1 212 ? 35.942  -11.050 -15.653 1.00 49.72  ? 204 LYS H CD  1 
ATOM   13357 C CE  . LYS H  1 212 ? 34.720  -10.835 -14.798 1.00 38.21  ? 204 LYS H CE  1 
ATOM   13358 N NZ  . LYS H  1 212 ? 34.005  -9.606  -15.217 1.00 43.45  ? 204 LYS H NZ  1 
ATOM   13359 N N   . GLY H  1 213 ? 38.439  -9.432  -19.953 1.00 64.49  ? 205 GLY H N   1 
ATOM   13360 C CA  . GLY H  1 213 ? 38.432  -9.250  -21.393 1.00 64.65  ? 205 GLY H CA  1 
ATOM   13361 C C   . GLY H  1 213 ? 39.391  -10.192 -22.092 1.00 72.64  ? 205 GLY H C   1 
ATOM   13362 O O   . GLY H  1 213 ? 40.603  -9.972  -22.097 1.00 81.80  ? 205 GLY H O   1 
ATOM   13363 N N   . ASP I  1 1   ? 43.067  1.784   37.160  1.00 44.17  ? -7  ASP I N   1 
ATOM   13364 C CA  . ASP I  1 1   ? 44.272  2.007   36.369  1.00 54.19  ? -7  ASP I CA  1 
ATOM   13365 C C   . ASP I  1 1   ? 44.255  1.175   35.091  1.00 61.49  ? -7  ASP I C   1 
ATOM   13366 O O   . ASP I  1 1   ? 43.191  0.851   34.564  1.00 59.66  ? -7  ASP I O   1 
ATOM   13367 C CB  . ASP I  1 1   ? 45.520  1.682   37.191  1.00 55.32  ? -7  ASP I CB  1 
ATOM   13368 C CG  . ASP I  1 1   ? 45.284  0.570   38.195  1.00 64.29  ? -7  ASP I CG  1 
ATOM   13369 O OD1 . ASP I  1 1   ? 45.975  -0.467  38.108  1.00 72.51  ? -7  ASP I OD1 1 
ATOM   13370 O OD2 . ASP I  1 1   ? 44.408  0.734   39.070  1.00 60.76  ? -7  ASP I OD2 1 
ATOM   13371 N N   . TYR I  1 2   ? 45.427  0.768   34.632  1.00 63.36  ? -6  TYR I N   1 
ATOM   13372 C CA  . TYR I  1 2   ? 45.506  0.045   33.381  1.00 66.49  ? -6  TYR I CA  1 
ATOM   13373 C C   . TYR I  1 2   ? 44.654  -1.198  33.550  1.00 60.70  ? -6  TYR I C   1 
ATOM   13374 O O   . TYR I  1 2   ? 43.995  -1.648  32.613  1.00 62.03  ? -6  TYR I O   1 
ATOM   13375 C CB  . TYR I  1 2   ? 46.952  -0.339  33.068  1.00 74.69  ? -6  TYR I CB  1 
ATOM   13376 C CG  . TYR I  1 2   ? 47.888  0.843   32.950  1.00 84.44  ? -6  TYR I CG  1 
ATOM   13377 C CD1 . TYR I  1 2   ? 48.605  1.071   31.783  1.00 92.47  ? -6  TYR I CD1 1 
ATOM   13378 C CD2 . TYR I  1 2   ? 48.055  1.729   34.005  1.00 87.99  ? -6  TYR I CD2 1 
ATOM   13379 C CE1 . TYR I  1 2   ? 49.461  2.150   31.670  1.00 99.00  ? -6  TYR I CE1 1 
ATOM   13380 C CE2 . TYR I  1 2   ? 48.909  2.811   33.902  1.00 94.48  ? -6  TYR I CE2 1 
ATOM   13381 C CZ  . TYR I  1 2   ? 49.610  3.016   32.733  1.00 96.98  ? -6  TYR I CZ  1 
ATOM   13382 O OH  . TYR I  1 2   ? 50.461  4.092   32.625  1.00 84.59  ? -6  TYR I OH  1 
ATOM   13383 N N   . LYS I  1 3   ? 44.680  -1.755  34.754  1.00 56.11  ? -5  LYS I N   1 
ATOM   13384 C CA  . LYS I  1 3   ? 44.001  -3.022  35.022  1.00 61.39  ? -5  LYS I CA  1 
ATOM   13385 C C   . LYS I  1 3   ? 42.527  -2.840  35.367  1.00 62.52  ? -5  LYS I C   1 
ATOM   13386 O O   . LYS I  1 3   ? 41.860  -3.783  35.790  1.00 58.48  ? -5  LYS I O   1 
ATOM   13387 C CB  . LYS I  1 3   ? 44.703  -3.765  36.160  1.00 64.39  ? -5  LYS I CB  1 
ATOM   13388 C CG  . LYS I  1 3   ? 44.965  -5.240  35.891  1.00 66.33  ? -5  LYS I CG  1 
ATOM   13389 C CD  . LYS I  1 3   ? 46.034  -5.809  36.833  1.00 65.35  ? -5  LYS I CD  1 
ATOM   13390 C CE  . LYS I  1 3   ? 47.374  -5.082  36.701  1.00 52.40  ? -5  LYS I CE  1 
ATOM   13391 N NZ  . LYS I  1 3   ? 47.473  -3.858  37.552  1.00 52.54  ? -5  LYS I NZ  1 
ATOM   13392 N N   . ASP I  1 4   ? 42.027  -1.622  35.185  1.00 63.28  ? -4  ASP I N   1 
ATOM   13393 C CA  . ASP I  1 4   ? 40.642  -1.295  35.511  1.00 55.86  ? -4  ASP I CA  1 
ATOM   13394 C C   . ASP I  1 4   ? 39.886  -0.714  34.308  1.00 51.46  ? -4  ASP I C   1 
ATOM   13395 O O   . ASP I  1 4   ? 38.667  -0.549  34.361  1.00 47.45  ? -4  ASP I O   1 
ATOM   13396 C CB  . ASP I  1 4   ? 40.592  -0.327  36.697  1.00 45.55  ? -4  ASP I CB  1 
ATOM   13397 C CG  . ASP I  1 4   ? 40.786  -1.028  38.034  1.00 55.06  ? -4  ASP I CG  1 
ATOM   13398 O OD1 . ASP I  1 4   ? 40.119  -2.063  38.262  1.00 59.71  ? -4  ASP I OD1 1 
ATOM   13399 O OD2 . ASP I  1 4   ? 41.597  -0.542  38.859  1.00 54.38  ? -4  ASP I OD2 1 
ATOM   13400 N N   . ASP I  1 5   ? 40.617  -0.429  33.230  1.00 42.67  ? -3  ASP I N   1 
ATOM   13401 C CA  . ASP I  1 5   ? 40.051  0.132   32.004  1.00 40.29  ? -3  ASP I CA  1 
ATOM   13402 C C   . ASP I  1 5   ? 38.803  -0.602  31.480  1.00 43.04  ? -3  ASP I C   1 
ATOM   13403 O O   . ASP I  1 5   ? 37.935  0.017   30.859  1.00 41.87  ? -3  ASP I O   1 
ATOM   13404 C CB  . ASP I  1 5   ? 41.117  0.191   30.892  1.00 45.22  ? -3  ASP I CB  1 
ATOM   13405 C CG  . ASP I  1 5   ? 41.947  1.478   30.921  1.00 47.83  ? -3  ASP I CG  1 
ATOM   13406 O OD1 . ASP I  1 5   ? 42.245  1.995   32.020  1.00 43.83  ? -3  ASP I OD1 1 
ATOM   13407 O OD2 . ASP I  1 5   ? 42.307  1.974   29.828  1.00 58.22  ? -3  ASP I OD2 1 
ATOM   13408 N N   . ASP I  1 6   ? 38.706  -1.906  31.729  1.00 42.15  ? -2  ASP I N   1 
ATOM   13409 C CA  . ASP I  1 6   ? 37.595  -2.696  31.189  1.00 41.53  ? -2  ASP I CA  1 
ATOM   13410 C C   . ASP I  1 6   ? 36.446  -2.962  32.162  1.00 39.78  ? -2  ASP I C   1 
ATOM   13411 O O   . ASP I  1 6   ? 35.744  -3.974  32.055  1.00 41.37  ? -2  ASP I O   1 
ATOM   13412 C CB  . ASP I  1 6   ? 38.104  -4.011  30.595  1.00 42.08  ? -2  ASP I CB  1 
ATOM   13413 C CG  . ASP I  1 6   ? 38.930  -3.792  29.357  1.00 44.41  ? -2  ASP I CG  1 
ATOM   13414 O OD1 . ASP I  1 6   ? 38.967  -2.630  28.895  1.00 36.52  ? -2  ASP I OD1 1 
ATOM   13415 O OD2 . ASP I  1 6   ? 39.530  -4.767  28.848  1.00 46.00  ? -2  ASP I OD2 1 
ATOM   13416 N N   . ASP I  1 7   ? 36.253  -2.047  33.104  1.00 39.95  ? -1  ASP I N   1 
ATOM   13417 C CA  . ASP I  1 7   ? 35.144  -2.130  34.052  1.00 37.59  ? -1  ASP I CA  1 
ATOM   13418 C C   . ASP I  1 7   ? 33.995  -1.279  33.508  1.00 32.19  ? -1  ASP I C   1 
ATOM   13419 O O   . ASP I  1 7   ? 34.071  -0.049  33.511  1.00 29.75  ? -1  ASP I O   1 
ATOM   13420 C CB  . ASP I  1 7   ? 35.605  -1.628  35.426  1.00 36.05  ? -1  ASP I CB  1 
ATOM   13421 C CG  . ASP I  1 7   ? 34.582  -1.871  36.524  1.00 49.00  ? -1  ASP I CG  1 
ATOM   13422 O OD1 . ASP I  1 7   ? 33.415  -1.435  36.376  1.00 47.52  ? -1  ASP I OD1 1 
ATOM   13423 O OD2 . ASP I  1 7   ? 34.953  -2.495  37.547  1.00 56.55  ? -1  ASP I OD2 1 
ATOM   13424 N N   . LYS I  1 8   ? 32.939  -1.935  33.034  1.00 27.99  ? 0   LYS I N   1 
ATOM   13425 C CA  . LYS I  1 8   ? 31.883  -1.239  32.307  1.00 23.75  ? 0   LYS I CA  1 
ATOM   13426 C C   . LYS I  1 8   ? 31.129  -0.222  33.167  1.00 26.41  ? 0   LYS I C   1 
ATOM   13427 O O   . LYS I  1 8   ? 30.817  0.873   32.704  1.00 23.69  ? 0   LYS I O   1 
ATOM   13428 C CB  . LYS I  1 8   ? 30.913  -2.232  31.677  1.00 22.15  ? 0   LYS I CB  1 
ATOM   13429 C CG  . LYS I  1 8   ? 30.172  -1.662  30.500  1.00 21.55  ? 0   LYS I CG  1 
ATOM   13430 C CD  . LYS I  1 8   ? 29.110  -2.613  29.997  1.00 25.17  ? 0   LYS I CD  1 
ATOM   13431 C CE  . LYS I  1 8   ? 28.245  -1.945  28.939  1.00 23.21  ? 0   LYS I CE  1 
ATOM   13432 N NZ  . LYS I  1 8   ? 27.012  -2.742  28.690  1.00 43.27  ? 0   LYS I NZ  1 
ATOM   13433 N N   . LEU I  1 9   ? 30.848  -0.573  34.418  1.00 25.83  ? 1   LEU I N   1 
ATOM   13434 C CA  . LEU I  1 9   ? 30.243  0.384   35.347  1.00 27.69  ? 1   LEU I CA  1 
ATOM   13435 C C   . LEU I  1 9   ? 31.090  1.659   35.496  1.00 27.59  ? 1   LEU I C   1 
ATOM   13436 O O   . LEU I  1 9   ? 30.572  2.783   35.407  1.00 25.14  ? 1   LEU I O   1 
ATOM   13437 C CB  . LEU I  1 9   ? 30.026  -0.257  36.716  1.00 28.61  ? 1   LEU I CB  1 
ATOM   13438 C CG  . LEU I  1 9   ? 29.029  0.419   37.655  1.00 26.58  ? 1   LEU I CG  1 
ATOM   13439 C CD1 . LEU I  1 9   ? 27.617  0.289   37.093  1.00 25.11  ? 1   LEU I CD1 1 
ATOM   13440 C CD2 . LEU I  1 9   ? 29.129  -0.179  39.059  1.00 23.39  ? 1   LEU I CD2 1 
ATOM   13441 N N   . ASP I  1 10  ? 32.390  1.481   35.709  1.00 26.82  ? 2   ASP I N   1 
ATOM   13442 C CA  . ASP I  1 10  ? 33.307  2.611   35.878  1.00 27.05  ? 2   ASP I CA  1 
ATOM   13443 C C   . ASP I  1 10  ? 33.337  3.583   34.696  1.00 24.48  ? 2   ASP I C   1 
ATOM   13444 O O   . ASP I  1 10  ? 33.493  4.787   34.898  1.00 22.64  ? 2   ASP I O   1 
ATOM   13445 C CB  . ASP I  1 10  ? 34.737  2.134   36.161  1.00 35.25  ? 2   ASP I CB  1 
ATOM   13446 C CG  . ASP I  1 10  ? 34.905  1.537   37.550  1.00 37.70  ? 2   ASP I CG  1 
ATOM   13447 O OD1 . ASP I  1 10  ? 33.949  1.603   38.359  1.00 34.22  ? 2   ASP I OD1 1 
ATOM   13448 O OD2 . ASP I  1 10  ? 36.012  1.007   37.823  1.00 38.75  ? 2   ASP I OD2 1 
ATOM   13449 N N   . ARG I  1 11  ? 33.209  3.076   33.470  1.00 24.78  ? 3   ARG I N   1 
ATOM   13450 C CA  . ARG I  1 11  ? 33.215  3.964   32.302  1.00 20.70  ? 3   ARG I CA  1 
ATOM   13451 C C   . ARG I  1 11  ? 31.888  4.707   32.173  1.00 17.61  ? 3   ARG I C   1 
ATOM   13452 O O   . ARG I  1 11  ? 31.867  5.884   31.811  1.00 14.68  ? 3   ARG I O   1 
ATOM   13453 C CB  . ARG I  1 11  ? 33.525  3.207   31.014  1.00 20.83  ? 3   ARG I CB  1 
ATOM   13454 C CG  . ARG I  1 11  ? 34.698  2.267   31.109  1.00 20.66  ? 3   ARG I CG  1 
ATOM   13455 C CD  . ARG I  1 11  ? 34.810  1.427   29.861  1.00 23.71  ? 3   ARG I CD  1 
ATOM   13456 N NE  . ARG I  1 11  ? 35.208  2.246   28.727  1.00 23.47  ? 3   ARG I NE  1 
ATOM   13457 C CZ  . ARG I  1 11  ? 36.468  2.537   28.436  1.00 24.94  ? 3   ARG I CZ  1 
ATOM   13458 N NH1 . ARG I  1 11  ? 37.454  2.069   29.199  1.00 25.01  ? 3   ARG I NH1 1 
ATOM   13459 N NH2 . ARG I  1 11  ? 36.737  3.299   27.385  1.00 23.31  ? 3   ARG I NH2 1 
ATOM   13460 N N   . ALA I  1 12  ? 30.788  4.026   32.496  1.00 20.57  ? 4   ALA I N   1 
ATOM   13461 C CA  . ALA I  1 12  ? 29.478  4.673   32.515  1.00 15.42  ? 4   ALA I CA  1 
ATOM   13462 C C   . ALA I  1 12  ? 29.452  5.825   33.507  1.00 15.51  ? 4   ALA I C   1 
ATOM   13463 O O   . ALA I  1 12  ? 28.867  6.862   33.228  1.00 16.76  ? 4   ALA I O   1 
ATOM   13464 C CB  . ALA I  1 12  ? 28.397  3.690   32.829  1.00 12.71  ? 4   ALA I CB  1 
ATOM   13465 N N   . ASP I  1 13  ? 30.097  5.664   34.657  1.00 14.59  ? 5   ASP I N   1 
ATOM   13466 C CA  . ASP I  1 13  ? 30.046  6.719   35.666  1.00 14.40  ? 5   ASP I CA  1 
ATOM   13467 C C   . ASP I  1 13  ? 30.928  7.895   35.300  1.00 15.95  ? 5   ASP I C   1 
ATOM   13468 O O   . ASP I  1 13  ? 30.579  9.034   35.604  1.00 14.34  ? 5   ASP I O   1 
ATOM   13469 C CB  . ASP I  1 13  ? 30.430  6.215   37.063  1.00 15.92  ? 5   ASP I CB  1 
ATOM   13470 C CG  . ASP I  1 13  ? 29.543  5.099   37.546  1.00 16.42  ? 5   ASP I CG  1 
ATOM   13471 O OD1 . ASP I  1 13  ? 28.364  5.048   37.142  1.00 16.29  ? 5   ASP I OD1 1 
ATOM   13472 O OD2 . ASP I  1 13  ? 30.034  4.263   38.325  1.00 21.44  ? 5   ASP I OD2 1 
ATOM   13473 N N   . ILE I  1 14  ? 32.083  7.613   34.684  1.00 19.63  ? 6   ILE I N   1 
ATOM   13474 C CA  . ILE I  1 14  ? 32.980  8.659   34.171  1.00 13.55  ? 6   ILE I CA  1 
ATOM   13475 C C   . ILE I  1 14  ? 32.229  9.450   33.114  1.00 11.31  ? 6   ILE I C   1 
ATOM   13476 O O   . ILE I  1 14  ? 32.206  10.683  33.138  1.00 9.36   ? 6   ILE I O   1 
ATOM   13477 C CB  . ILE I  1 14  ? 34.288  8.065   33.578  1.00 16.02  ? 6   ILE I CB  1 
ATOM   13478 C CG1 . ILE I  1 14  ? 35.138  7.420   34.674  1.00 14.90  ? 6   ILE I CG1 1 
ATOM   13479 C CG2 . ILE I  1 14  ? 35.132  9.136   32.898  1.00 14.30  ? 6   ILE I CG2 1 
ATOM   13480 C CD1 . ILE I  1 14  ? 36.069  6.338   34.175  1.00 15.67  ? 6   ILE I CD1 1 
ATOM   13481 N N   . LEU I  1 15  ? 31.571  8.731   32.211  1.00 11.78  ? 7   LEU I N   1 
ATOM   13482 C CA  . LEU I  1 15  ? 30.788  9.377   31.154  1.00 13.14  ? 7   LEU I CA  1 
ATOM   13483 C C   . LEU I  1 15  ? 29.707  10.301  31.725  1.00 14.14  ? 7   LEU I C   1 
ATOM   13484 O O   . LEU I  1 15  ? 29.565  11.449  31.286  1.00 10.47  ? 7   LEU I O   1 
ATOM   13485 C CB  . LEU I  1 15  ? 30.172  8.334   30.231  1.00 12.88  ? 7   LEU I CB  1 
ATOM   13486 C CG  . LEU I  1 15  ? 29.727  8.903   28.892  1.00 20.39  ? 7   LEU I CG  1 
ATOM   13487 C CD1 . LEU I  1 15  ? 30.927  9.384   28.122  1.00 14.85  ? 7   LEU I CD1 1 
ATOM   13488 C CD2 . LEU I  1 15  ? 28.964  7.849   28.104  1.00 28.54  ? 7   LEU I CD2 1 
ATOM   13489 N N   . TYR I  1 16  ? 28.964  9.773   32.707  1.00 15.22  ? 8   TYR I N   1 
ATOM   13490 C CA  . TYR I  1 16  ? 27.994  10.509  33.520  1.00 10.74  ? 8   TYR I CA  1 
ATOM   13491 C C   . TYR I  1 16  ? 28.615  11.748  34.186  1.00 12.57  ? 8   TYR I C   1 
ATOM   13492 O O   . TYR I  1 16  ? 28.110  12.860  34.052  1.00 12.73  ? 8   TYR I O   1 
ATOM   13493 C CB  . TYR I  1 16  ? 27.414  9.562   34.573  1.00 14.83  ? 8   TYR I CB  1 
ATOM   13494 C CG  . TYR I  1 16  ? 26.577  10.226  35.643  1.00 17.56  ? 8   TYR I CG  1 
ATOM   13495 C CD1 . TYR I  1 16  ? 25.308  10.712  35.352  1.00 17.46  ? 8   TYR I CD1 1 
ATOM   13496 C CD2 . TYR I  1 16  ? 27.042  10.346  36.952  1.00 15.57  ? 8   TYR I CD2 1 
ATOM   13497 C CE1 . TYR I  1 16  ? 24.538  11.314  36.319  1.00 16.49  ? 8   TYR I CE1 1 
ATOM   13498 C CE2 . TYR I  1 16  ? 26.266  10.944  37.932  1.00 17.33  ? 8   TYR I CE2 1 
ATOM   13499 C CZ  . TYR I  1 16  ? 25.013  11.428  37.604  1.00 17.89  ? 8   TYR I CZ  1 
ATOM   13500 O OH  . TYR I  1 16  ? 24.219  12.041  38.550  1.00 20.86  ? 8   TYR I OH  1 
ATOM   13501 N N   . ASN I  1 17  ? 29.731  11.562  34.881  1.00 11.04  ? 9   ASN I N   1 
ATOM   13502 C CA  . ASN I  1 17  ? 30.440  12.690  35.465  1.00 10.95  ? 9   ASN I CA  1 
ATOM   13503 C C   . ASN I  1 17  ? 30.873  13.712  34.416  1.00 13.94  ? 9   ASN I C   1 
ATOM   13504 O O   . ASN I  1 17  ? 30.700  14.914  34.614  1.00 16.30  ? 9   ASN I O   1 
ATOM   13505 C CB  . ASN I  1 17  ? 31.635  12.223  36.308  1.00 11.09  ? 9   ASN I CB  1 
ATOM   13506 C CG  . ASN I  1 17  ? 31.246  11.198  37.351  1.00 11.80  ? 9   ASN I CG  1 
ATOM   13507 O OD1 . ASN I  1 17  ? 30.069  11.040  37.678  1.00 17.26  ? 9   ASN I OD1 1 
ATOM   13508 N ND2 . ASN I  1 17  ? 32.227  10.495  37.877  1.00 13.84  ? 9   ASN I ND2 1 
ATOM   13509 N N   . ILE I  1 18  ? 31.411  13.240  33.291  1.00 13.18  ? 10  ILE I N   1 
ATOM   13510 C CA  . ILE I  1 18  ? 31.793  14.148  32.215  1.00 13.04  ? 10  ILE I CA  1 
ATOM   13511 C C   . ILE I  1 18  ? 30.599  14.962  31.721  1.00 15.30  ? 10  ILE I C   1 
ATOM   13512 O O   . ILE I  1 18  ? 30.673  16.187  31.627  1.00 16.48  ? 10  ILE I O   1 
ATOM   13513 C CB  . ILE I  1 18  ? 32.501  13.418  31.055  1.00 14.50  ? 10  ILE I CB  1 
ATOM   13514 C CG1 . ILE I  1 18  ? 33.967  13.159  31.420  1.00 13.35  ? 10  ILE I CG1 1 
ATOM   13515 C CG2 . ILE I  1 18  ? 32.444  14.248  29.788  1.00 10.52  ? 10  ILE I CG2 1 
ATOM   13516 C CD1 . ILE I  1 18  ? 34.529  11.914  30.808  1.00 11.42  ? 10  ILE I CD1 1 
ATOM   13517 N N   . ARG I  1 19  ? 29.481  14.292  31.458  1.00 15.54  ? 11  ARG I N   1 
ATOM   13518 C CA  . ARG I  1 19  ? 28.290  14.980  30.945  1.00 15.11  ? 11  ARG I CA  1 
ATOM   13519 C C   . ARG I  1 19  ? 27.588  15.908  31.921  1.00 12.93  ? 11  ARG I C   1 
ATOM   13520 O O   . ARG I  1 19  ? 26.773  16.727  31.512  1.00 12.37  ? 11  ARG I O   1 
ATOM   13521 C CB  . ARG I  1 19  ? 27.280  13.980  30.402  1.00 15.75  ? 11  ARG I CB  1 
ATOM   13522 C CG  . ARG I  1 19  ? 27.704  13.355  29.110  1.00 16.46  ? 11  ARG I CG  1 
ATOM   13523 C CD  . ARG I  1 19  ? 26.795  12.223  28.761  1.00 17.47  ? 11  ARG I CD  1 
ATOM   13524 N NE  . ARG I  1 19  ? 26.981  11.872  27.366  1.00 25.55  ? 11  ARG I NE  1 
ATOM   13525 C CZ  . ARG I  1 19  ? 26.680  10.690  26.850  1.00 24.56  ? 11  ARG I CZ  1 
ATOM   13526 N NH1 . ARG I  1 19  ? 26.174  9.731   27.627  1.00 23.40  ? 11  ARG I NH1 1 
ATOM   13527 N NH2 . ARG I  1 19  ? 26.906  10.471  25.561  1.00 21.35  ? 11  ARG I NH2 1 
ATOM   13528 N N   . GLN I  1 20  ? 27.882  15.792  33.208  1.00 16.36  ? 12  GLN I N   1 
ATOM   13529 C CA  . GLN I  1 20  ? 27.273  16.711  34.161  1.00 13.59  ? 12  GLN I CA  1 
ATOM   13530 C C   . GLN I  1 20  ? 28.122  17.947  34.316  1.00 14.76  ? 12  GLN I C   1 
ATOM   13531 O O   . GLN I  1 20  ? 27.603  19.016  34.578  1.00 20.67  ? 12  GLN I O   1 
ATOM   13532 C CB  . GLN I  1 20  ? 27.062  16.048  35.513  1.00 14.52  ? 12  GLN I CB  1 
ATOM   13533 C CG  . GLN I  1 20  ? 26.044  14.932  35.490  1.00 14.61  ? 12  GLN I CG  1 
ATOM   13534 C CD  . GLN I  1 20  ? 25.128  15.002  36.677  1.00 26.44  ? 12  GLN I CD  1 
ATOM   13535 O OE1 . GLN I  1 20  ? 25.492  14.567  37.779  1.00 28.46  ? 12  GLN I OE1 1 
ATOM   13536 N NE2 . GLN I  1 20  ? 23.929  15.579  36.475  1.00 19.32  ? 12  GLN I NE2 1 
ATOM   13537 N N   . THR I  1 21  ? 29.431  17.801  34.142  1.00 16.90  ? 13  THR I N   1 
ATOM   13538 C CA  . THR I  1 21  ? 30.353  18.911  34.363  1.00 18.71  ? 13  THR I CA  1 
ATOM   13539 C C   . THR I  1 21  ? 30.559  19.714  33.083  1.00 14.44  ? 13  THR I C   1 
ATOM   13540 O O   . THR I  1 21  ? 30.808  20.913  33.115  1.00 16.65  ? 13  THR I O   1 
ATOM   13541 C CB  . THR I  1 21  ? 31.724  18.406  34.864  1.00 18.83  ? 13  THR I CB  1 
ATOM   13542 O OG1 . THR I  1 21  ? 31.537  17.559  35.997  1.00 22.73  ? 13  THR I OG1 1 
ATOM   13543 C CG2 . THR I  1 21  ? 32.599  19.557  35.280  1.00 22.45  ? 13  THR I CG2 1 
ATOM   13544 N N   . SER I  1 22  ? 30.442  19.037  31.953  1.00 14.64  ? 14  SER I N   1 
ATOM   13545 C CA  . SER I  1 22  ? 30.823  19.605  30.675  1.00 12.74  ? 14  SER I CA  1 
ATOM   13546 C C   . SER I  1 22  ? 29.883  20.695  30.186  1.00 13.72  ? 14  SER I C   1 
ATOM   13547 O O   . SER I  1 22  ? 28.685  20.490  30.105  1.00 14.18  ? 14  SER I O   1 
ATOM   13548 C CB  . SER I  1 22  ? 30.884  18.502  29.634  1.00 12.27  ? 14  SER I CB  1 
ATOM   13549 O OG  . SER I  1 22  ? 30.845  19.057  28.328  1.00 21.13  ? 14  SER I OG  1 
ATOM   13550 N N   . ARG I  1 23  ? 30.434  21.849  29.835  1.00 14.21  ? 15  ARG I N   1 
ATOM   13551 C CA  . ARG I  1 23  ? 29.643  22.878  29.172  1.00 16.51  ? 15  ARG I CA  1 
ATOM   13552 C C   . ARG I  1 23  ? 29.992  22.995  27.676  1.00 16.60  ? 15  ARG I C   1 
ATOM   13553 O O   . ARG I  1 23  ? 30.895  23.745  27.313  1.00 18.12  ? 15  ARG I O   1 
ATOM   13554 C CB  . ARG I  1 23  ? 29.864  24.230  29.834  1.00 14.19  ? 15  ARG I CB  1 
ATOM   13555 C CG  . ARG I  1 23  ? 29.593  24.258  31.294  1.00 18.16  ? 15  ARG I CG  1 
ATOM   13556 C CD  . ARG I  1 23  ? 29.398  25.691  31.730  1.00 24.26  ? 15  ARG I CD  1 
ATOM   13557 N NE  . ARG I  1 23  ? 29.684  25.875  33.147  1.00 25.19  ? 15  ARG I NE  1 
ATOM   13558 C CZ  . ARG I  1 23  ? 28.769  26.098  34.083  1.00 23.23  ? 15  ARG I CZ  1 
ATOM   13559 N NH1 . ARG I  1 23  ? 27.478  26.182  33.767  1.00 17.68  ? 15  ARG I NH1 1 
ATOM   13560 N NH2 . ARG I  1 23  ? 29.161  26.248  35.343  1.00 28.41  ? 15  ARG I NH2 1 
ATOM   13561 N N   . PRO I  1 24  ? 29.256  22.281  26.808  1.00 13.18  ? 16  PRO I N   1 
ATOM   13562 C CA  . PRO I  1 24  ? 29.556  22.209  25.379  1.00 14.39  ? 16  PRO I CA  1 
ATOM   13563 C C   . PRO I  1 24  ? 29.796  23.545  24.673  1.00 16.37  ? 16  PRO I C   1 
ATOM   13564 O O   . PRO I  1 24  ? 30.528  23.565  23.683  1.00 17.77  ? 16  PRO I O   1 
ATOM   13565 C CB  . PRO I  1 24  ? 28.316  21.518  24.818  1.00 13.35  ? 16  PRO I CB  1 
ATOM   13566 C CG  . PRO I  1 24  ? 27.937  20.600  25.885  1.00 13.30  ? 16  PRO I CG  1 
ATOM   13567 C CD  . PRO I  1 24  ? 28.124  21.402  27.149  1.00 15.18  ? 16  PRO I CD  1 
ATOM   13568 N N   . ASP I  1 25  ? 29.221  24.633  25.174  1.00 15.22  ? 17  ASP I N   1 
ATOM   13569 C CA  . ASP I  1 25  ? 29.268  25.906  24.462  1.00 13.40  ? 17  ASP I CA  1 
ATOM   13570 C C   . ASP I  1 25  ? 30.080  26.993  25.158  1.00 14.86  ? 17  ASP I C   1 
ATOM   13571 O O   . ASP I  1 25  ? 30.065  28.139  24.721  1.00 21.06  ? 17  ASP I O   1 
ATOM   13572 C CB  . ASP I  1 25  ? 27.848  26.435  24.205  1.00 14.19  ? 17  ASP I CB  1 
ATOM   13573 C CG  . ASP I  1 25  ? 26.963  25.432  23.453  1.00 20.11  ? 17  ASP I CG  1 
ATOM   13574 O OD1 . ASP I  1 25  ? 27.473  24.710  22.565  1.00 18.22  ? 17  ASP I OD1 1 
ATOM   13575 O OD2 . ASP I  1 25  ? 25.744  25.365  23.757  1.00 23.62  ? 17  ASP I OD2 1 
ATOM   13576 N N   . VAL I  1 26  ? 30.781  26.652  26.232  1.00 13.74  ? 18  VAL I N   1 
ATOM   13577 C CA  . VAL I  1 26  ? 31.555  27.649  26.975  1.00 17.15  ? 18  VAL I CA  1 
ATOM   13578 C C   . VAL I  1 26  ? 33.046  27.306  26.976  1.00 16.02  ? 18  VAL I C   1 
ATOM   13579 O O   . VAL I  1 26  ? 33.418  26.152  27.211  1.00 19.96  ? 18  VAL I O   1 
ATOM   13580 C CB  . VAL I  1 26  ? 31.015  27.813  28.426  1.00 16.47  ? 18  VAL I CB  1 
ATOM   13581 C CG1 . VAL I  1 26  ? 31.862  28.781  29.216  1.00 15.29  ? 18  VAL I CG1 1 
ATOM   13582 C CG2 . VAL I  1 26  ? 29.584  28.300  28.392  1.00 14.35  ? 18  VAL I CG2 1 
ATOM   13583 N N   . ILE I  1 27  ? 33.909  28.287  26.707  1.00 15.77  ? 19  ILE I N   1 
ATOM   13584 C CA  . ILE I  1 27  ? 35.342  27.979  26.651  1.00 18.25  ? 19  ILE I CA  1 
ATOM   13585 C C   . ILE I  1 27  ? 35.868  27.595  28.022  1.00 18.48  ? 19  ILE I C   1 
ATOM   13586 O O   . ILE I  1 27  ? 35.682  28.331  28.986  1.00 20.36  ? 19  ILE I O   1 
ATOM   13587 C CB  . ILE I  1 27  ? 36.208  29.118  26.049  1.00 20.22  ? 19  ILE I CB  1 
ATOM   13588 C CG1 . ILE I  1 27  ? 35.873  30.463  26.699  1.00 23.20  ? 19  ILE I CG1 1 
ATOM   13589 C CG2 . ILE I  1 27  ? 36.071  29.166  24.502  1.00 14.67  ? 19  ILE I CG2 1 
ATOM   13590 C CD1 . ILE I  1 27  ? 36.758  31.605  26.225  1.00 19.04  ? 19  ILE I CD1 1 
ATOM   13591 N N   . PRO I  1 28  ? 36.521  26.428  28.111  1.00 18.92  ? 20  PRO I N   1 
ATOM   13592 C CA  . PRO I  1 28  ? 37.095  25.950  29.373  1.00 18.42  ? 20  PRO I CA  1 
ATOM   13593 C C   . PRO I  1 28  ? 38.366  26.714  29.750  1.00 19.85  ? 20  PRO I C   1 
ATOM   13594 O O   . PRO I  1 28  ? 39.404  26.092  29.959  1.00 22.55  ? 20  PRO I O   1 
ATOM   13595 C CB  . PRO I  1 28  ? 37.427  24.483  29.072  1.00 19.10  ? 20  PRO I CB  1 
ATOM   13596 C CG  . PRO I  1 28  ? 37.700  24.459  27.609  1.00 18.39  ? 20  PRO I CG  1 
ATOM   13597 C CD  . PRO I  1 28  ? 36.860  25.551  26.975  1.00 17.01  ? 20  PRO I CD  1 
ATOM   13598 N N   . THR I  1 29  ? 38.290  28.042  29.808  1.00 19.05  ? 21  THR I N   1 
ATOM   13599 C CA  . THR I  1 29  ? 39.397  28.850  30.290  1.00 22.25  ? 21  THR I CA  1 
ATOM   13600 C C   . THR I  1 29  ? 39.559  28.605  31.787  1.00 28.87  ? 21  THR I C   1 
ATOM   13601 O O   . THR I  1 29  ? 38.583  28.472  32.515  1.00 24.95  ? 21  THR I O   1 
ATOM   13602 C CB  . THR I  1 29  ? 39.165  30.353  30.057  1.00 26.86  ? 21  THR I CB  1 
ATOM   13603 O OG1 . THR I  1 29  ? 37.927  30.748  30.668  1.00 27.35  ? 21  THR I OG1 1 
ATOM   13604 C CG2 . THR I  1 29  ? 39.117  30.669  28.575  1.00 24.91  ? 21  THR I CG2 1 
ATOM   13605 N N   . GLN I  1 30  ? 40.804  28.551  32.234  1.00 36.93  ? 22  GLN I N   1 
ATOM   13606 C CA  . GLN I  1 30  ? 41.113  28.191  33.598  1.00 38.57  ? 22  GLN I CA  1 
ATOM   13607 C C   . GLN I  1 30  ? 42.109  29.174  34.195  1.00 48.31  ? 22  GLN I C   1 
ATOM   13608 O O   . GLN I  1 30  ? 43.240  29.273  33.722  1.00 49.32  ? 22  GLN I O   1 
ATOM   13609 C CB  . GLN I  1 30  ? 41.668  26.769  33.652  1.00 39.45  ? 22  GLN I CB  1 
ATOM   13610 C CG  . GLN I  1 30  ? 41.777  26.216  35.066  1.00 63.00  ? 22  GLN I CG  1 
ATOM   13611 C CD  . GLN I  1 30  ? 41.724  24.697  35.112  1.00 67.09  ? 22  GLN I CD  1 
ATOM   13612 O OE1 . GLN I  1 30  ? 41.829  24.024  34.073  1.00 60.97  ? 22  GLN I OE1 1 
ATOM   13613 N NE2 . GLN I  1 30  ? 41.552  24.147  36.319  1.00 50.89  ? 22  GLN I NE2 1 
ATOM   13614 N N   . ARG I  1 31  ? 41.676  29.890  35.234  1.00 56.48  ? 23  ARG I N   1 
ATOM   13615 C CA  . ARG I  1 31  ? 42.501  30.896  35.913  1.00 67.26  ? 23  ARG I CA  1 
ATOM   13616 C C   . ARG I  1 31  ? 42.844  32.095  35.014  1.00 61.24  ? 23  ARG I C   1 
ATOM   13617 O O   . ARG I  1 31  ? 44.012  32.489  34.927  1.00 56.67  ? 23  ARG I O   1 
ATOM   13618 C CB  . ARG I  1 31  ? 43.791  30.269  36.475  1.00 68.21  ? 23  ARG I CB  1 
ATOM   13619 C CG  . ARG I  1 31  ? 43.643  29.519  37.793  1.00 63.96  ? 23  ARG I CG  1 
ATOM   13620 C CD  . ARG I  1 31  ? 44.126  30.381  38.958  1.00 79.54  ? 23  ARG I CD  1 
ATOM   13621 N NE  . ARG I  1 31  ? 44.661  29.597  40.073  1.00 90.23  ? 23  ARG I NE  1 
ATOM   13622 C CZ  . ARG I  1 31  ? 45.948  29.551  40.417  1.00 84.83  ? 23  ARG I CZ  1 
ATOM   13623 N NH1 . ARG I  1 31  ? 46.856  30.247  39.737  1.00 74.20  ? 23  ARG I NH1 1 
ATOM   13624 N NH2 . ARG I  1 31  ? 46.330  28.808  41.450  1.00 76.26  ? 23  ARG I NH2 1 
ATOM   13625 N N   . ASP I  1 32  ? 41.825  32.660  34.359  1.00 54.42  ? 24  ASP I N   1 
ATOM   13626 C CA  . ASP I  1 32  ? 41.974  33.823  33.461  1.00 51.18  ? 24  ASP I CA  1 
ATOM   13627 C C   . ASP I  1 32  ? 43.177  33.807  32.522  1.00 50.85  ? 24  ASP I C   1 
ATOM   13628 O O   . ASP I  1 32  ? 43.924  34.785  32.425  1.00 50.89  ? 24  ASP I O   1 
ATOM   13629 C CB  . ASP I  1 32  ? 41.947  35.134  34.239  1.00 54.42  ? 24  ASP I CB  1 
ATOM   13630 C CG  . ASP I  1 32  ? 40.574  35.460  34.758  1.00 55.87  ? 24  ASP I CG  1 
ATOM   13631 O OD1 . ASP I  1 32  ? 40.048  36.532  34.388  1.00 50.41  ? 24  ASP I OD1 1 
ATOM   13632 O OD2 . ASP I  1 32  ? 40.023  34.637  35.528  1.00 54.85  ? 24  ASP I OD2 1 
ATOM   13633 N N   . ARG I  1 33  ? 43.349  32.677  31.847  1.00 48.47  ? 25  ARG I N   1 
ATOM   13634 C CA  . ARG I  1 33  ? 44.350  32.511  30.817  1.00 32.80  ? 25  ARG I CA  1 
ATOM   13635 C C   . ARG I  1 33  ? 43.647  31.835  29.647  1.00 31.65  ? 25  ARG I C   1 
ATOM   13636 O O   . ARG I  1 33  ? 42.678  31.104  29.838  1.00 33.51  ? 25  ARG I O   1 
ATOM   13637 C CB  . ARG I  1 33  ? 45.495  31.642  31.332  1.00 42.71  ? 25  ARG I CB  1 
ATOM   13638 C CG  . ARG I  1 33  ? 46.183  32.178  32.581  1.00 49.76  ? 25  ARG I CG  1 
ATOM   13639 C CD  . ARG I  1 33  ? 47.344  31.279  32.996  1.00 63.24  ? 25  ARG I CD  1 
ATOM   13640 N NE  . ARG I  1 33  ? 47.836  31.586  34.340  1.00 80.16  ? 25  ARG I NE  1 
ATOM   13641 C CZ  . ARG I  1 33  ? 47.954  30.693  35.324  1.00 81.65  ? 25  ARG I CZ  1 
ATOM   13642 N NH1 . ARG I  1 33  ? 47.622  29.422  35.123  1.00 72.55  ? 25  ARG I NH1 1 
ATOM   13643 N NH2 . ARG I  1 33  ? 48.411  31.070  36.514  1.00 77.87  ? 25  ARG I NH2 1 
ATOM   13644 N N   . PRO I  1 34  ? 44.126  32.071  28.424  1.00 33.29  ? 26  PRO I N   1 
ATOM   13645 C CA  . PRO I  1 34  ? 43.393  31.511  27.290  1.00 27.92  ? 26  PRO I CA  1 
ATOM   13646 C C   . PRO I  1 34  ? 43.532  29.995  27.244  1.00 20.97  ? 26  PRO I C   1 
ATOM   13647 O O   . PRO I  1 34  ? 44.458  29.437  27.828  1.00 19.55  ? 26  PRO I O   1 
ATOM   13648 C CB  . PRO I  1 34  ? 44.087  32.157  26.081  1.00 30.88  ? 26  PRO I CB  1 
ATOM   13649 C CG  . PRO I  1 34  ? 44.888  33.329  26.665  1.00 25.51  ? 26  PRO I CG  1 
ATOM   13650 C CD  . PRO I  1 34  ? 45.311  32.829  27.989  1.00 26.92  ? 26  PRO I CD  1 
ATOM   13651 N N   . VAL I  1 35  ? 42.595  29.336  26.578  1.00 19.70  ? 27  VAL I N   1 
ATOM   13652 C CA  . VAL I  1 35  ? 42.663  27.898  26.423  1.00 17.22  ? 27  VAL I CA  1 
ATOM   13653 C C   . VAL I  1 35  ? 43.758  27.608  25.431  1.00 24.77  ? 27  VAL I C   1 
ATOM   13654 O O   . VAL I  1 35  ? 43.803  28.213  24.351  1.00 27.66  ? 27  VAL I O   1 
ATOM   13655 C CB  . VAL I  1 35  ? 41.375  27.334  25.838  1.00 16.68  ? 27  VAL I CB  1 
ATOM   13656 C CG1 . VAL I  1 35  ? 41.408  25.819  25.898  1.00 20.07  ? 27  VAL I CG1 1 
ATOM   13657 C CG2 . VAL I  1 35  ? 40.191  27.862  26.580  1.00 16.45  ? 27  VAL I CG2 1 
ATOM   13658 N N   . ALA I  1 36  ? 44.639  26.678  25.771  1.00 21.65  ? 28  ALA I N   1 
ATOM   13659 C CA  . ALA I  1 36  ? 45.750  26.382  24.881  1.00 20.53  ? 28  ALA I CA  1 
ATOM   13660 C C   . ALA I  1 36  ? 45.470  25.167  23.995  1.00 19.76  ? 28  ALA I C   1 
ATOM   13661 O O   . ALA I  1 36  ? 45.568  24.019  24.431  1.00 21.34  ? 28  ALA I O   1 
ATOM   13662 C CB  . ALA I  1 36  ? 47.030  26.205  25.671  1.00 19.92  ? 28  ALA I CB  1 
ATOM   13663 N N   . VAL I  1 37  ? 45.125  25.433  22.740  1.00 18.77  ? 29  VAL I N   1 
ATOM   13664 C CA  . VAL I  1 37  ? 44.808  24.370  21.799  1.00 21.76  ? 29  VAL I CA  1 
ATOM   13665 C C   . VAL I  1 37  ? 46.043  24.009  20.964  1.00 23.18  ? 29  VAL I C   1 
ATOM   13666 O O   . VAL I  1 37  ? 46.693  24.880  20.392  1.00 28.34  ? 29  VAL I O   1 
ATOM   13667 C CB  . VAL I  1 37  ? 43.610  24.772  20.871  1.00 19.99  ? 29  VAL I CB  1 
ATOM   13668 C CG1 . VAL I  1 37  ? 43.314  23.694  19.840  1.00 15.10  ? 29  VAL I CG1 1 
ATOM   13669 C CG2 . VAL I  1 37  ? 42.364  25.085  21.690  1.00 17.92  ? 29  VAL I CG2 1 
ATOM   13670 N N   . SER I  1 38  ? 46.360  22.721  20.912  1.00 18.97  ? 30  SER I N   1 
ATOM   13671 C CA  . SER I  1 38  ? 47.435  22.211  20.082  1.00 26.79  ? 30  SER I CA  1 
ATOM   13672 C C   . SER I  1 38  ? 46.887  21.567  18.810  1.00 32.92  ? 30  SER I C   1 
ATOM   13673 O O   . SER I  1 38  ? 45.974  20.743  18.875  1.00 31.32  ? 30  SER I O   1 
ATOM   13674 C CB  . SER I  1 38  ? 48.258  21.189  20.861  1.00 23.82  ? 30  SER I CB  1 
ATOM   13675 O OG  . SER I  1 38  ? 49.032  21.847  21.845  1.00 33.84  ? 30  SER I OG  1 
ATOM   13676 N N   . VAL I  1 39  ? 47.438  21.934  17.655  1.00 28.41  ? 31  VAL I N   1 
ATOM   13677 C CA  . VAL I  1 39  ? 46.986  21.337  16.409  1.00 27.78  ? 31  VAL I CA  1 
ATOM   13678 C C   . VAL I  1 39  ? 48.133  20.823  15.561  1.00 32.62  ? 31  VAL I C   1 
ATOM   13679 O O   . VAL I  1 39  ? 49.076  21.557  15.260  1.00 29.18  ? 31  VAL I O   1 
ATOM   13680 C CB  . VAL I  1 39  ? 46.228  22.335  15.540  1.00 34.04  ? 31  VAL I CB  1 
ATOM   13681 C CG1 . VAL I  1 39  ? 45.372  21.581  14.538  1.00 23.93  ? 31  VAL I CG1 1 
ATOM   13682 C CG2 . VAL I  1 39  ? 45.386  23.261  16.391  1.00 29.98  ? 31  VAL I CG2 1 
ATOM   13683 N N   . SER I  1 40  ? 48.032  19.566  15.153  1.00 30.75  ? 32  SER I N   1 
ATOM   13684 C CA  . SER I  1 40  ? 49.024  18.979  14.269  1.00 32.20  ? 32  SER I CA  1 
ATOM   13685 C C   . SER I  1 40  ? 48.369  18.226  13.104  1.00 35.52  ? 32  SER I C   1 
ATOM   13686 O O   . SER I  1 40  ? 47.756  17.169  13.293  1.00 30.21  ? 32  SER I O   1 
ATOM   13687 C CB  . SER I  1 40  ? 49.945  18.041  15.046  1.00 33.85  ? 32  SER I CB  1 
ATOM   13688 O OG  . SER I  1 40  ? 51.061  17.673  14.250  1.00 42.25  ? 32  SER I OG  1 
ATOM   13689 N N   . LEU I  1 41  ? 48.496  18.773  11.900  1.00 28.31  ? 33  LEU I N   1 
ATOM   13690 C CA  . LEU I  1 41  ? 48.015  18.076  10.718  1.00 29.98  ? 33  LEU I CA  1 
ATOM   13691 C C   . LEU I  1 41  ? 48.970  16.943  10.383  1.00 27.59  ? 33  LEU I C   1 
ATOM   13692 O O   . LEU I  1 41  ? 50.172  17.150  10.331  1.00 33.27  ? 33  LEU I O   1 
ATOM   13693 C CB  . LEU I  1 41  ? 47.926  19.028  9.534   1.00 25.45  ? 33  LEU I CB  1 
ATOM   13694 C CG  . LEU I  1 41  ? 47.092  20.286  9.732   1.00 27.60  ? 33  LEU I CG  1 
ATOM   13695 C CD1 . LEU I  1 41  ? 46.720  20.853  8.382   1.00 25.76  ? 33  LEU I CD1 1 
ATOM   13696 C CD2 . LEU I  1 41  ? 45.844  19.987  10.551  1.00 30.14  ? 33  LEU I CD2 1 
ATOM   13697 N N   . LYS I  1 42  ? 48.440  15.747  10.178  1.00 23.18  ? 34  LYS I N   1 
ATOM   13698 C CA  . LYS I  1 42  ? 49.262  14.632  9.753   1.00 22.39  ? 34  LYS I CA  1 
ATOM   13699 C C   . LYS I  1 42  ? 48.719  14.067  8.466   1.00 30.23  ? 34  LYS I C   1 
ATOM   13700 O O   . LYS I  1 42  ? 47.842  13.197  8.483   1.00 23.53  ? 34  LYS I O   1 
ATOM   13701 C CB  . LYS I  1 42  ? 49.392  13.560  10.831  1.00 26.47  ? 34  LYS I CB  1 
ATOM   13702 C CG  . LYS I  1 42  ? 50.297  14.013  11.987  1.00 41.89  ? 34  LYS I CG  1 
ATOM   13703 C CD  . LYS I  1 42  ? 50.961  12.847  12.726  1.00 44.39  ? 34  LYS I CD  1 
ATOM   13704 C CE  . LYS I  1 42  ? 51.793  13.342  13.909  1.00 39.61  ? 34  LYS I CE  1 
ATOM   13705 N NZ  . LYS I  1 42  ? 52.489  14.626  13.603  1.00 41.46  ? 34  LYS I NZ  1 
ATOM   13706 N N   . PHE I  1 43  ? 49.189  14.574  7.329   1.00 31.11  ? 35  PHE I N   1 
ATOM   13707 C CA  . PHE I  1 43  ? 48.547  14.299  6.037   1.00 21.40  ? 35  PHE I CA  1 
ATOM   13708 C C   . PHE I  1 43  ? 48.553  12.833  5.586   1.00 25.62  ? 35  PHE I C   1 
ATOM   13709 O O   . PHE I  1 43  ? 49.561  12.137  5.712   1.00 25.58  ? 35  PHE I O   1 
ATOM   13710 C CB  . PHE I  1 43  ? 49.163  15.177  4.944   1.00 21.14  ? 35  PHE I CB  1 
ATOM   13711 C CG  . PHE I  1 43  ? 49.190  16.640  5.285   1.00 25.21  ? 35  PHE I CG  1 
ATOM   13712 C CD1 . PHE I  1 43  ? 50.123  17.139  6.179   1.00 23.83  ? 35  PHE I CD1 1 
ATOM   13713 C CD2 . PHE I  1 43  ? 48.283  17.516  4.713   1.00 23.07  ? 35  PHE I CD2 1 
ATOM   13714 C CE1 . PHE I  1 43  ? 50.151  18.484  6.496   1.00 20.59  ? 35  PHE I CE1 1 
ATOM   13715 C CE2 . PHE I  1 43  ? 48.306  18.862  5.025   1.00 23.96  ? 35  PHE I CE2 1 
ATOM   13716 C CZ  . PHE I  1 43  ? 49.241  19.347  5.918   1.00 21.08  ? 35  PHE I CZ  1 
ATOM   13717 N N   . ILE I  1 44  ? 47.411  12.373  5.071   1.00 28.14  ? 36  ILE I N   1 
ATOM   13718 C CA  . ILE I  1 44  ? 47.282  11.014  4.536   1.00 30.11  ? 36  ILE I CA  1 
ATOM   13719 C C   . ILE I  1 44  ? 47.426  10.905  3.009   1.00 27.59  ? 36  ILE I C   1 
ATOM   13720 O O   . ILE I  1 44  ? 48.131  10.028  2.510   1.00 26.45  ? 36  ILE I O   1 
ATOM   13721 C CB  . ILE I  1 44  ? 45.944  10.373  4.954   1.00 24.06  ? 36  ILE I CB  1 
ATOM   13722 C CG1 . ILE I  1 44  ? 45.625  10.709  6.412   1.00 28.25  ? 36  ILE I CG1 1 
ATOM   13723 C CG2 . ILE I  1 44  ? 45.986  8.867   4.745   1.00 16.19  ? 36  ILE I CG2 1 
ATOM   13724 C CD1 . ILE I  1 44  ? 46.808  10.568  7.344   1.00 28.90  ? 36  ILE I CD1 1 
ATOM   13725 N N   . ASN I  1 45  ? 46.761  11.797  2.276   1.00 23.71  ? 37  ASN I N   1 
ATOM   13726 C CA  . ASN I  1 45  ? 46.854  11.834  0.820   1.00 26.65  ? 37  ASN I CA  1 
ATOM   13727 C C   . ASN I  1 45  ? 46.495  13.189  0.202   1.00 35.29  ? 37  ASN I C   1 
ATOM   13728 O O   . ASN I  1 45  ? 45.811  14.006  0.818   1.00 29.86  ? 37  ASN I O   1 
ATOM   13729 C CB  . ASN I  1 45  ? 45.988  10.734  0.202   1.00 28.41  ? 37  ASN I CB  1 
ATOM   13730 C CG  . ASN I  1 45  ? 46.685  10.013  -0.935  1.00 36.10  ? 37  ASN I CG  1 
ATOM   13731 O OD1 . ASN I  1 45  ? 46.254  10.084  -2.086  1.00 25.55  ? 37  ASN I OD1 1 
ATOM   13732 N ND2 . ASN I  1 45  ? 47.769  9.315   -0.618  1.00 33.74  ? 37  ASN I ND2 1 
ATOM   13733 N N   . ILE I  1 46  ? 46.953  13.402  -1.028  1.00 33.30  ? 38  ILE I N   1 
ATOM   13734 C CA  . ILE I  1 46  ? 46.508  14.495  -1.862  1.00 29.51  ? 38  ILE I CA  1 
ATOM   13735 C C   . ILE I  1 46  ? 45.780  13.875  -3.049  1.00 33.44  ? 38  ILE I C   1 
ATOM   13736 O O   . ILE I  1 46  ? 46.387  13.251  -3.920  1.00 39.39  ? 38  ILE I O   1 
ATOM   13737 C CB  . ILE I  1 46  ? 47.688  15.342  -2.368  1.00 24.48  ? 38  ILE I CB  1 
ATOM   13738 C CG1 . ILE I  1 46  ? 48.696  15.580  -1.242  1.00 24.55  ? 38  ILE I CG1 1 
ATOM   13739 C CG2 . ILE I  1 46  ? 47.191  16.664  -2.933  1.00 21.43  ? 38  ILE I CG2 1 
ATOM   13740 C CD1 . ILE I  1 46  ? 49.678  16.695  -1.527  1.00 23.54  ? 38  ILE I CD1 1 
ATOM   13741 N N   . LEU I  1 47  ? 44.449  14.031  -3.044  1.00 39.46  ? 39  LEU I N   1 
ATOM   13742 C CA  . LEU I  1 47  ? 43.537  13.603  -4.130  1.00 35.04  ? 39  LEU I CA  1 
ATOM   13743 C C   . LEU I  1 47  ? 43.534  14.293  -5.524  1.00 39.22  ? 39  LEU I C   1 
ATOM   13744 O O   . LEU I  1 47  ? 43.527  13.599  -6.540  1.00 44.17  ? 39  LEU I O   1 
ATOM   13745 C CB  . LEU I  1 47  ? 42.099  13.552  -3.599  1.00 31.81  ? 39  LEU I CB  1 
ATOM   13746 C CG  . LEU I  1 47  ? 41.739  12.347  -2.726  1.00 36.57  ? 39  LEU I CG  1 
ATOM   13747 C CD1 . LEU I  1 47  ? 41.177  11.217  -3.574  1.00 36.00  ? 39  LEU I CD1 1 
ATOM   13748 C CD2 . LEU I  1 47  ? 42.948  11.877  -1.932  1.00 42.82  ? 39  LEU I CD2 1 
ATOM   13749 N N   . GLU I  1 48  ? 43.546  15.629  -5.584  1.00 35.51  ? 40  GLU I N   1 
ATOM   13750 C CA  . GLU I  1 48  ? 43.631  16.314  -6.847  1.00 35.16  ? 40  GLU I CA  1 
ATOM   13751 C C   . GLU I  1 48  ? 44.526  17.507  -6.644  1.00 36.88  ? 40  GLU I C   1 
ATOM   13752 O O   . GLU I  1 48  ? 44.463  18.178  -5.614  1.00 43.81  ? 40  GLU I O   1 
ATOM   13753 C CB  . GLU I  1 48  ? 42.246  16.765  -7.311  1.00 32.54  ? 40  GLU I CB  1 
ATOM   13754 C CG  . GLU I  1 48  ? 41.489  15.719  -8.113  1.00 46.06  ? 40  GLU I CG  1 
ATOM   13755 C CD  . GLU I  1 48  ? 39.987  15.829  -7.944  1.00 68.49  ? 40  GLU I CD  1 
ATOM   13756 O OE1 . GLU I  1 48  ? 39.389  16.761  -8.523  1.00 78.08  ? 40  GLU I OE1 1 
ATOM   13757 O OE2 . GLU I  1 48  ? 39.403  14.985  -7.232  1.00 66.57  ? 40  GLU I OE2 1 
ATOM   13758 N N   . VAL I  1 49  ? 45.350  17.784  -7.637  1.00 33.72  ? 41  VAL I N   1 
ATOM   13759 C CA  . VAL I  1 49  ? 46.081  19.023  -7.653  1.00 26.51  ? 41  VAL I CA  1 
ATOM   13760 C C   . VAL I  1 49  ? 45.792  19.686  -8.981  1.00 28.43  ? 41  VAL I C   1 
ATOM   13761 O O   . VAL I  1 49  ? 45.601  19.014  -9.988  1.00 28.43  ? 41  VAL I O   1 
ATOM   13762 C CB  . VAL I  1 49  ? 47.565  18.746  -7.464  1.00 31.80  ? 41  VAL I CB  1 
ATOM   13763 C CG1 . VAL I  1 49  ? 48.407  19.519  -8.464  1.00 32.83  ? 41  VAL I CG1 1 
ATOM   13764 C CG2 . VAL I  1 49  ? 47.966  19.065  -6.043  1.00 29.87  ? 41  VAL I CG2 1 
ATOM   13765 N N   . ASN I  1 50  ? 45.713  21.003  -8.987  1.00 30.64  ? 42  ASN I N   1 
ATOM   13766 C CA  . ASN I  1 50  ? 45.420  21.697  -10.223 1.00 33.54  ? 42  ASN I CA  1 
ATOM   13767 C C   . ASN I  1 50  ? 46.218  22.982  -10.313 1.00 41.26  ? 42  ASN I C   1 
ATOM   13768 O O   . ASN I  1 50  ? 45.978  23.930  -9.554  1.00 35.57  ? 42  ASN I O   1 
ATOM   13769 C CB  . ASN I  1 50  ? 43.929  21.980  -10.342 1.00 37.44  ? 42  ASN I CB  1 
ATOM   13770 C CG  . ASN I  1 50  ? 43.513  22.288  -11.761 1.00 43.25  ? 42  ASN I CG  1 
ATOM   13771 O OD1 . ASN I  1 50  ? 43.830  23.355  -12.295 1.00 38.84  ? 42  ASN I OD1 1 
ATOM   13772 N ND2 . ASN I  1 50  ? 42.800  21.353  -12.385 1.00 39.31  ? 42  ASN I ND2 1 
ATOM   13773 N N   . GLU I  1 51  ? 47.167  22.989  -11.250 1.00 42.38  ? 43  GLU I N   1 
ATOM   13774 C CA  . GLU I  1 51  ? 48.171  24.041  -11.377 1.00 41.29  ? 43  GLU I CA  1 
ATOM   13775 C C   . GLU I  1 51  ? 47.555  25.319  -11.918 1.00 40.69  ? 43  GLU I C   1 
ATOM   13776 O O   . GLU I  1 51  ? 48.040  26.424  -11.649 1.00 38.03  ? 43  GLU I O   1 
ATOM   13777 C CB  . GLU I  1 51  ? 49.300  23.568  -12.303 1.00 43.23  ? 43  GLU I CB  1 
ATOM   13778 C CG  . GLU I  1 51  ? 50.508  24.492  -12.352 1.00 45.54  ? 43  GLU I CG  1 
ATOM   13779 C CD  . GLU I  1 51  ? 51.806  23.731  -12.489 1.00 49.21  ? 43  GLU I CD  1 
ATOM   13780 O OE1 . GLU I  1 51  ? 51.748  22.548  -12.889 1.00 47.50  ? 43  GLU I OE1 1 
ATOM   13781 O OE2 . GLU I  1 51  ? 52.878  24.309  -12.191 1.00 56.77  ? 43  GLU I OE2 1 
ATOM   13782 N N   . ILE I  1 52  ? 46.479  25.152  -12.680 1.00 40.67  ? 44  ILE I N   1 
ATOM   13783 C CA  . ILE I  1 52  ? 45.797  26.273  -13.304 1.00 40.64  ? 44  ILE I CA  1 
ATOM   13784 C C   . ILE I  1 52  ? 44.967  27.013  -12.263 1.00 41.48  ? 44  ILE I C   1 
ATOM   13785 O O   . ILE I  1 52  ? 45.206  28.187  -11.985 1.00 41.61  ? 44  ILE I O   1 
ATOM   13786 C CB  . ILE I  1 52  ? 44.858  25.797  -14.438 1.00 44.74  ? 44  ILE I CB  1 
ATOM   13787 C CG1 . ILE I  1 52  ? 45.499  24.666  -15.255 1.00 42.72  ? 44  ILE I CG1 1 
ATOM   13788 C CG2 . ILE I  1 52  ? 44.462  26.962  -15.320 1.00 43.93  ? 44  ILE I CG2 1 
ATOM   13789 C CD1 . ILE I  1 52  ? 46.344  25.129  -16.428 1.00 43.74  ? 44  ILE I CD1 1 
ATOM   13790 N N   . THR I  1 53  ? 43.995  26.312  -11.683 1.00 44.74  ? 45  THR I N   1 
ATOM   13791 C CA  . THR I  1 53  ? 43.053  26.915  -10.734 1.00 41.97  ? 45  THR I CA  1 
ATOM   13792 C C   . THR I  1 53  ? 43.674  27.267  -9.381  1.00 37.50  ? 45  THR I C   1 
ATOM   13793 O O   . THR I  1 53  ? 43.102  28.053  -8.628  1.00 42.45  ? 45  THR I O   1 
ATOM   13794 C CB  . THR I  1 53  ? 41.815  26.016  -10.491 1.00 41.59  ? 45  THR I CB  1 
ATOM   13795 O OG1 . THR I  1 53  ? 42.233  24.730  -10.012 1.00 43.12  ? 45  THR I OG1 1 
ATOM   13796 C CG2 . THR I  1 53  ? 41.010  25.843  -11.773 1.00 39.30  ? 45  THR I CG2 1 
ATOM   13797 N N   . ASN I  1 54  ? 44.840  26.692  -9.093  1.00 36.79  ? 46  ASN I N   1 
ATOM   13798 C CA  . ASN I  1 54  ? 45.545  26.910  -7.833  1.00 38.25  ? 46  ASN I CA  1 
ATOM   13799 C C   . ASN I  1 54  ? 44.765  26.359  -6.651  1.00 38.62  ? 46  ASN I C   1 
ATOM   13800 O O   . ASN I  1 54  ? 44.582  27.034  -5.638  1.00 37.38  ? 46  ASN I O   1 
ATOM   13801 C CB  . ASN I  1 54  ? 45.847  28.389  -7.610  1.00 39.31  ? 46  ASN I CB  1 
ATOM   13802 C CG  . ASN I  1 54  ? 47.317  28.705  -7.708  1.00 41.66  ? 46  ASN I CG  1 
ATOM   13803 O OD1 . ASN I  1 54  ? 48.159  27.807  -7.817  1.00 44.13  ? 46  ASN I OD1 1 
ATOM   13804 N ND2 . ASN I  1 54  ? 47.641  29.990  -7.655  1.00 37.37  ? 46  ASN I ND2 1 
ATOM   13805 N N   . GLU I  1 55  ? 44.304  25.126  -6.801  1.00 35.54  ? 47  GLU I N   1 
ATOM   13806 C CA  . GLU I  1 55  ? 43.510  24.469  -5.790  1.00 32.77  ? 47  GLU I CA  1 
ATOM   13807 C C   . GLU I  1 55  ? 44.018  23.061  -5.569  1.00 34.43  ? 47  GLU I C   1 
ATOM   13808 O O   . GLU I  1 55  ? 44.417  22.386  -6.509  1.00 36.30  ? 47  GLU I O   1 
ATOM   13809 C CB  . GLU I  1 55  ? 42.053  24.420  -6.231  1.00 36.50  ? 47  GLU I CB  1 
ATOM   13810 C CG  . GLU I  1 55  ? 41.435  25.782  -6.437  1.00 33.58  ? 47  GLU I CG  1 
ATOM   13811 C CD  . GLU I  1 55  ? 40.077  25.698  -7.079  1.00 42.12  ? 47  GLU I CD  1 
ATOM   13812 O OE1 . GLU I  1 55  ? 39.563  24.562  -7.223  1.00 43.01  ? 47  GLU I OE1 1 
ATOM   13813 O OE2 . GLU I  1 55  ? 39.528  26.768  -7.438  1.00 43.48  ? 47  GLU I OE2 1 
ATOM   13814 N N   . VAL I  1 56  ? 43.994  22.619  -4.319  1.00 32.91  ? 48  VAL I N   1 
ATOM   13815 C CA  . VAL I  1 56  ? 44.441  21.282  -3.981  1.00 29.87  ? 48  VAL I CA  1 
ATOM   13816 C C   . VAL I  1 56  ? 43.313  20.614  -3.195  1.00 32.92  ? 48  VAL I C   1 
ATOM   13817 O O   . VAL I  1 56  ? 42.395  21.292  -2.740  1.00 31.52  ? 48  VAL I O   1 
ATOM   13818 C CB  . VAL I  1 56  ? 45.754  21.343  -3.154  1.00 41.59  ? 48  VAL I CB  1 
ATOM   13819 C CG1 . VAL I  1 56  ? 45.484  21.893  -1.747  1.00 44.88  ? 48  VAL I CG1 1 
ATOM   13820 C CG2 . VAL I  1 56  ? 46.436  19.982  -3.079  1.00 34.66  ? 48  VAL I CG2 1 
ATOM   13821 N N   . ASP I  1 57  ? 43.386  19.295  -3.047  1.00 31.77  ? 49  ASP I N   1 
ATOM   13822 C CA  . ASP I  1 57  ? 42.372  18.508  -2.367  1.00 23.96  ? 49  ASP I CA  1 
ATOM   13823 C C   . ASP I  1 57  ? 43.066  17.492  -1.459  1.00 29.46  ? 49  ASP I C   1 
ATOM   13824 O O   . ASP I  1 57  ? 43.532  16.452  -1.921  1.00 36.36  ? 49  ASP I O   1 
ATOM   13825 C CB  . ASP I  1 57  ? 41.544  17.772  -3.414  1.00 33.84  ? 49  ASP I CB  1 
ATOM   13826 C CG  . ASP I  1 57  ? 40.085  17.642  -3.031  1.00 40.41  ? 49  ASP I CG  1 
ATOM   13827 O OD1 . ASP I  1 57  ? 39.328  18.621  -3.248  1.00 41.90  ? 49  ASP I OD1 1 
ATOM   13828 O OD2 . ASP I  1 57  ? 39.693  16.558  -2.534  1.00 37.45  ? 49  ASP I OD2 1 
ATOM   13829 N N   . VAL I  1 58  ? 43.122  17.782  -0.164  1.00 32.43  ? 50  VAL I N   1 
ATOM   13830 C CA  . VAL I  1 58  ? 43.937  17.004  0.771   1.00 23.20  ? 50  VAL I CA  1 
ATOM   13831 C C   . VAL I  1 58  ? 43.127  16.051  1.661   1.00 20.73  ? 50  VAL I C   1 
ATOM   13832 O O   . VAL I  1 58  ? 41.941  16.248  1.876   1.00 24.04  ? 50  VAL I O   1 
ATOM   13833 C CB  . VAL I  1 58  ? 44.725  17.954  1.670   1.00 20.44  ? 50  VAL I CB  1 
ATOM   13834 C CG1 . VAL I  1 58  ? 45.892  17.234  2.318   1.00 28.71  ? 50  VAL I CG1 1 
ATOM   13835 C CG2 . VAL I  1 58  ? 45.223  19.139  0.858   1.00 28.25  ? 50  VAL I CG2 1 
ATOM   13836 N N   . VAL I  1 59  ? 43.775  15.003  2.152   1.00 20.04  ? 51  VAL I N   1 
ATOM   13837 C CA  . VAL I  1 59  ? 43.236  14.185  3.226   1.00 22.60  ? 51  VAL I CA  1 
ATOM   13838 C C   . VAL I  1 59  ? 44.205  14.155  4.410   1.00 23.41  ? 51  VAL I C   1 
ATOM   13839 O O   . VAL I  1 59  ? 45.285  13.589  4.302   1.00 23.96  ? 51  VAL I O   1 
ATOM   13840 C CB  . VAL I  1 59  ? 42.982  12.752  2.764   1.00 23.55  ? 51  VAL I CB  1 
ATOM   13841 C CG1 . VAL I  1 59  ? 42.647  11.858  3.970   1.00 23.22  ? 51  VAL I CG1 1 
ATOM   13842 C CG2 . VAL I  1 59  ? 41.862  12.733  1.741   1.00 20.55  ? 51  VAL I CG2 1 
ATOM   13843 N N   . PHE I  1 60  ? 43.811  14.749  5.539   1.00 29.74  ? 52  PHE I N   1 
ATOM   13844 C CA  . PHE I  1 60  ? 44.706  14.910  6.705   1.00 27.71  ? 52  PHE I CA  1 
ATOM   13845 C C   . PHE I  1 60  ? 44.056  14.648  8.075   1.00 26.80  ? 52  PHE I C   1 
ATOM   13846 O O   . PHE I  1 60  ? 43.034  15.247  8.401   1.00 24.46  ? 52  PHE I O   1 
ATOM   13847 C CB  . PHE I  1 60  ? 45.308  16.319  6.710   1.00 24.89  ? 52  PHE I CB  1 
ATOM   13848 C CG  . PHE I  1 60  ? 44.280  17.429  6.829   1.00 23.10  ? 52  PHE I CG  1 
ATOM   13849 C CD1 . PHE I  1 60  ? 44.062  18.071  8.046   1.00 25.78  ? 52  PHE I CD1 1 
ATOM   13850 C CD2 . PHE I  1 60  ? 43.548  17.842  5.722   1.00 23.64  ? 52  PHE I CD2 1 
ATOM   13851 C CE1 . PHE I  1 60  ? 43.123  19.105  8.165   1.00 22.96  ? 52  PHE I CE1 1 
ATOM   13852 C CE2 . PHE I  1 60  ? 42.604  18.876  5.834   1.00 30.88  ? 52  PHE I CE2 1 
ATOM   13853 C CZ  . PHE I  1 60  ? 42.392  19.504  7.065   1.00 23.13  ? 52  PHE I CZ  1 
ATOM   13854 N N   . TRP I  1 61  ? 44.664  13.762  8.869   1.00 26.51  ? 53  TRP I N   1 
ATOM   13855 C CA  . TRP I  1 61  ? 44.290  13.578  10.274  1.00 25.53  ? 53  TRP I CA  1 
ATOM   13856 C C   . TRP I  1 61  ? 44.620  14.840  11.043  1.00 24.12  ? 53  TRP I C   1 
ATOM   13857 O O   . TRP I  1 61  ? 45.750  15.293  11.013  1.00 25.99  ? 53  TRP I O   1 
ATOM   13858 C CB  . TRP I  1 61  ? 45.043  12.398  10.897  1.00 23.56  ? 53  TRP I CB  1 
ATOM   13859 C CG  . TRP I  1 61  ? 44.658  11.057  10.312  1.00 30.65  ? 53  TRP I CG  1 
ATOM   13860 C CD1 . TRP I  1 61  ? 43.616  10.798  9.457   1.00 30.52  ? 53  TRP I CD1 1 
ATOM   13861 C CD2 . TRP I  1 61  ? 45.311  9.794   10.535  1.00 32.69  ? 53  TRP I CD2 1 
ATOM   13862 N NE1 . TRP I  1 61  ? 43.580  9.456   9.141   1.00 32.39  ? 53  TRP I NE1 1 
ATOM   13863 C CE2 . TRP I  1 61  ? 44.610  8.820   9.785   1.00 32.23  ? 53  TRP I CE2 1 
ATOM   13864 C CE3 . TRP I  1 61  ? 46.418  9.393   11.294  1.00 29.86  ? 53  TRP I CE3 1 
ATOM   13865 C CZ2 . TRP I  1 61  ? 44.983  7.476   9.773   1.00 30.71  ? 53  TRP I CZ2 1 
ATOM   13866 C CZ3 . TRP I  1 61  ? 46.779  8.052   11.282  1.00 31.19  ? 53  TRP I CZ3 1 
ATOM   13867 C CH2 . TRP I  1 61  ? 46.064  7.114   10.527  1.00 33.86  ? 53  TRP I CH2 1 
ATOM   13868 N N   . GLN I  1 62  ? 43.636  15.413  11.729  1.00 25.06  ? 54  GLN I N   1 
ATOM   13869 C CA  . GLN I  1 62  ? 43.863  16.641  12.490  1.00 24.49  ? 54  GLN I CA  1 
ATOM   13870 C C   . GLN I  1 62  ? 43.951  16.365  13.990  1.00 23.54  ? 54  GLN I C   1 
ATOM   13871 O O   . GLN I  1 62  ? 42.937  16.216  14.648  1.00 27.96  ? 54  GLN I O   1 
ATOM   13872 C CB  . GLN I  1 62  ? 42.757  17.655  12.183  1.00 23.68  ? 54  GLN I CB  1 
ATOM   13873 C CG  . GLN I  1 62  ? 42.769  18.926  13.023  1.00 26.26  ? 54  GLN I CG  1 
ATOM   13874 C CD  . GLN I  1 62  ? 41.627  19.876  12.655  1.00 30.26  ? 54  GLN I CD  1 
ATOM   13875 O OE1 . GLN I  1 62  ? 41.130  19.857  11.529  1.00 33.58  ? 54  GLN I OE1 1 
ATOM   13876 N NE2 . GLN I  1 62  ? 41.201  20.696  13.609  1.00 28.57  ? 54  GLN I NE2 1 
ATOM   13877 N N   . GLN I  1 63  ? 45.165  16.272  14.525  1.00 27.54  ? 55  GLN I N   1 
ATOM   13878 C CA  . GLN I  1 63  ? 45.345  16.038  15.953  1.00 23.74  ? 55  GLN I CA  1 
ATOM   13879 C C   . GLN I  1 63  ? 45.110  17.334  16.720  1.00 23.58  ? 55  GLN I C   1 
ATOM   13880 O O   . GLN I  1 63  ? 45.851  18.303  16.551  1.00 25.82  ? 55  GLN I O   1 
ATOM   13881 C CB  . GLN I  1 63  ? 46.745  15.509  16.261  1.00 33.68  ? 55  GLN I CB  1 
ATOM   13882 C CG  . GLN I  1 63  ? 47.152  14.224  15.529  1.00 38.29  ? 55  GLN I CG  1 
ATOM   13883 C CD  . GLN I  1 63  ? 48.267  13.463  16.256  1.00 43.98  ? 55  GLN I CD  1 
ATOM   13884 O OE1 . GLN I  1 63  ? 48.850  13.970  17.219  1.00 46.12  ? 55  GLN I OE1 1 
ATOM   13885 N NE2 . GLN I  1 63  ? 48.549  12.235  15.809  1.00 36.22  ? 55  GLN I NE2 1 
ATOM   13886 N N   . THR I  1 64  ? 44.067  17.352  17.548  1.00 22.35  ? 56  THR I N   1 
ATOM   13887 C CA  . THR I  1 64  ? 43.739  18.528  18.351  1.00 19.24  ? 56  THR I CA  1 
ATOM   13888 C C   . THR I  1 64  ? 43.768  18.169  19.820  1.00 17.94  ? 56  THR I C   1 
ATOM   13889 O O   . THR I  1 64  ? 43.159  17.187  20.235  1.00 16.63  ? 56  THR I O   1 
ATOM   13890 C CB  . THR I  1 64  ? 42.333  19.056  18.038  1.00 19.85  ? 56  THR I CB  1 
ATOM   13891 O OG1 . THR I  1 64  ? 42.035  18.845  16.652  1.00 29.52  ? 56  THR I OG1 1 
ATOM   13892 C CG2 . THR I  1 64  ? 42.231  20.540  18.368  1.00 13.69  ? 56  THR I CG2 1 
ATOM   13893 N N   . THR I  1 65  ? 44.483  18.947  20.618  1.00 17.16  ? 57  THR I N   1 
ATOM   13894 C CA  . THR I  1 65  ? 44.478  18.700  22.052  1.00 19.80  ? 57  THR I CA  1 
ATOM   13895 C C   . THR I  1 65  ? 44.317  19.983  22.838  1.00 17.41  ? 57  THR I C   1 
ATOM   13896 O O   . THR I  1 65  ? 44.732  21.052  22.404  1.00 15.31  ? 57  THR I O   1 
ATOM   13897 C CB  . THR I  1 65  ? 45.747  17.989  22.536  1.00 27.38  ? 57  THR I CB  1 
ATOM   13898 O OG1 . THR I  1 65  ? 46.866  18.882  22.427  1.00 33.87  ? 57  THR I OG1 1 
ATOM   13899 C CG2 . THR I  1 65  ? 46.007  16.721  21.726  1.00 23.29  ? 57  THR I CG2 1 
ATOM   13900 N N   . TRP I  1 66  ? 43.684  19.861  23.997  1.00 20.10  ? 58  TRP I N   1 
ATOM   13901 C CA  . TRP I  1 66  ? 43.568  20.964  24.941  1.00 19.43  ? 58  TRP I CA  1 
ATOM   13902 C C   . TRP I  1 66  ? 43.225  20.302  26.244  1.00 18.26  ? 58  TRP I C   1 
ATOM   13903 O O   . TRP I  1 66  ? 43.151  19.076  26.309  1.00 19.59  ? 58  TRP I O   1 
ATOM   13904 C CB  . TRP I  1 66  ? 42.495  21.973  24.504  1.00 21.42  ? 58  TRP I CB  1 
ATOM   13905 C CG  . TRP I  1 66  ? 41.116  21.389  24.376  1.00 20.68  ? 58  TRP I CG  1 
ATOM   13906 C CD1 . TRP I  1 66  ? 40.115  21.452  25.305  1.00 22.04  ? 58  TRP I CD1 1 
ATOM   13907 C CD2 . TRP I  1 66  ? 40.585  20.650  23.265  1.00 20.34  ? 58  TRP I CD2 1 
ATOM   13908 N NE1 . TRP I  1 66  ? 38.996  20.796  24.847  1.00 25.64  ? 58  TRP I NE1 1 
ATOM   13909 C CE2 . TRP I  1 66  ? 39.253  20.290  23.600  1.00 23.86  ? 58  TRP I CE2 1 
ATOM   13910 C CE3 . TRP I  1 66  ? 41.097  20.260  22.025  1.00 14.69  ? 58  TRP I CE3 1 
ATOM   13911 C CZ2 . TRP I  1 66  ? 38.427  19.557  22.734  1.00 18.06  ? 58  TRP I CZ2 1 
ATOM   13912 C CZ3 . TRP I  1 66  ? 40.278  19.531  21.167  1.00 18.98  ? 58  TRP I CZ3 1 
ATOM   13913 C CH2 . TRP I  1 66  ? 38.954  19.189  21.526  1.00 19.68  ? 58  TRP I CH2 1 
ATOM   13914 N N   . SER I  1 67  ? 43.020  21.079  27.293  1.00 24.76  ? 59  SER I N   1 
ATOM   13915 C CA  . SER I  1 67  ? 42.682  20.454  28.568  1.00 27.05  ? 59  SER I CA  1 
ATOM   13916 C C   . SER I  1 67  ? 41.546  21.187  29.275  1.00 26.78  ? 59  SER I C   1 
ATOM   13917 O O   . SER I  1 67  ? 41.433  22.418  29.172  1.00 28.07  ? 59  SER I O   1 
ATOM   13918 C CB  . SER I  1 67  ? 43.913  20.376  29.473  1.00 24.77  ? 59  SER I CB  1 
ATOM   13919 O OG  . SER I  1 67  ? 43.985  21.525  30.297  1.00 30.66  ? 59  SER I OG  1 
ATOM   13920 N N   . ASP I  1 68  ? 40.700  20.422  29.968  1.00 22.58  ? 60  ASP I N   1 
ATOM   13921 C CA  . ASP I  1 68  ? 39.634  20.981  30.808  1.00 27.08  ? 60  ASP I CA  1 
ATOM   13922 C C   . ASP I  1 68  ? 39.673  20.318  32.187  1.00 25.85  ? 60  ASP I C   1 
ATOM   13923 O O   . ASP I  1 68  ? 39.133  19.229  32.369  1.00 26.12  ? 60  ASP I O   1 
ATOM   13924 C CB  . ASP I  1 68  ? 38.264  20.775  30.162  1.00 24.60  ? 60  ASP I CB  1 
ATOM   13925 C CG  . ASP I  1 68  ? 37.126  21.400  30.972  1.00 29.94  ? 60  ASP I CG  1 
ATOM   13926 O OD1 . ASP I  1 68  ? 37.391  22.105  31.978  1.00 30.21  ? 60  ASP I OD1 1 
ATOM   13927 O OD2 . ASP I  1 68  ? 35.956  21.194  30.587  1.00 27.71  ? 60  ASP I OD2 1 
ATOM   13928 N N   . ARG I  1 69  ? 40.315  20.973  33.151  1.00 21.55  ? 61  ARG I N   1 
ATOM   13929 C CA  . ARG I  1 69  ? 40.642  20.306  34.402  1.00 23.29  ? 61  ARG I CA  1 
ATOM   13930 C C   . ARG I  1 69  ? 39.379  19.940  35.201  1.00 26.09  ? 61  ARG I C   1 
ATOM   13931 O O   . ARG I  1 69  ? 39.388  18.976  35.970  1.00 20.44  ? 61  ARG I O   1 
ATOM   13932 C CB  . ARG I  1 69  ? 41.659  21.122  35.223  1.00 24.01  ? 61  ARG I CB  1 
ATOM   13933 C CG  . ARG I  1 69  ? 43.118  20.578  35.195  1.00 36.20  ? 61  ARG I CG  1 
ATOM   13934 C CD  . ARG I  1 69  ? 44.171  21.666  35.532  1.00 43.74  ? 61  ARG I CD  1 
ATOM   13935 N NE  . ARG I  1 69  ? 45.416  21.118  36.086  1.00 63.86  ? 61  ARG I NE  1 
ATOM   13936 C CZ  . ARG I  1 69  ? 46.276  21.797  36.855  1.00 70.37  ? 61  ARG I CZ  1 
ATOM   13937 N NH1 . ARG I  1 69  ? 46.043  23.065  37.181  1.00 64.33  ? 61  ARG I NH1 1 
ATOM   13938 N NH2 . ARG I  1 69  ? 47.376  21.205  37.311  1.00 64.18  ? 61  ARG I NH2 1 
ATOM   13939 N N   . THR I  1 70  ? 38.290  20.684  34.982  1.00 25.01  ? 62  THR I N   1 
ATOM   13940 C CA  . THR I  1 70  ? 37.010  20.394  35.631  1.00 20.77  ? 62  THR I CA  1 
ATOM   13941 C C   . THR I  1 70  ? 36.521  18.982  35.266  1.00 24.81  ? 62  THR I C   1 
ATOM   13942 O O   . THR I  1 70  ? 35.778  18.346  36.036  1.00 24.49  ? 62  THR I O   1 
ATOM   13943 C CB  . THR I  1 70  ? 35.898  21.451  35.297  1.00 19.15  ? 62  THR I CB  1 
ATOM   13944 O OG1 . THR I  1 70  ? 35.362  21.211  33.994  1.00 23.66  ? 62  THR I OG1 1 
ATOM   13945 C CG2 . THR I  1 70  ? 36.416  22.886  35.367  1.00 10.15  ? 62  THR I CG2 1 
ATOM   13946 N N   . LEU I  1 71  ? 36.950  18.485  34.103  1.00 18.91  ? 63  LEU I N   1 
ATOM   13947 C CA  . LEU I  1 71  ? 36.585  17.133  33.677  1.00 19.03  ? 63  LEU I CA  1 
ATOM   13948 C C   . LEU I  1 71  ? 37.448  16.051  34.321  1.00 18.40  ? 63  LEU I C   1 
ATOM   13949 O O   . LEU I  1 71  ? 37.158  14.858  34.198  1.00 18.64  ? 63  LEU I O   1 
ATOM   13950 C CB  . LEU I  1 71  ? 36.652  16.991  32.158  1.00 20.74  ? 63  LEU I CB  1 
ATOM   13951 C CG  . LEU I  1 71  ? 35.715  17.852  31.319  1.00 21.76  ? 63  LEU I CG  1 
ATOM   13952 C CD1 . LEU I  1 71  ? 35.927  17.513  29.853  1.00 15.34  ? 63  LEU I CD1 1 
ATOM   13953 C CD2 . LEU I  1 71  ? 34.257  17.655  31.728  1.00 15.23  ? 63  LEU I CD2 1 
ATOM   13954 N N   . ALA I  1 72  ? 38.510  16.462  35.000  1.00 17.98  ? 64  ALA I N   1 
ATOM   13955 C CA  . ALA I  1 72  ? 39.408  15.496  35.616  1.00 17.29  ? 64  ALA I CA  1 
ATOM   13956 C C   . ALA I  1 72  ? 38.713  14.676  36.710  1.00 22.67  ? 64  ALA I C   1 
ATOM   13957 O O   . ALA I  1 72  ? 37.820  15.167  37.410  1.00 23.67  ? 64  ALA I O   1 
ATOM   13958 C CB  . ALA I  1 72  ? 40.633  16.191  36.163  1.00 11.26  ? 64  ALA I CB  1 
ATOM   13959 N N   . TRP I  1 73  ? 39.122  13.419  36.834  1.00 19.22  ? 65  TRP I N   1 
ATOM   13960 C CA  . TRP I  1 73  ? 38.690  12.562  37.929  1.00 19.26  ? 65  TRP I CA  1 
ATOM   13961 C C   . TRP I  1 73  ? 39.901  11.763  38.414  1.00 26.08  ? 65  TRP I C   1 
ATOM   13962 O O   . TRP I  1 73  ? 40.943  11.727  37.750  1.00 20.58  ? 65  TRP I O   1 
ATOM   13963 C CB  . TRP I  1 73  ? 37.567  11.614  37.497  1.00 16.99  ? 65  TRP I CB  1 
ATOM   13964 C CG  . TRP I  1 73  ? 38.014  10.461  36.604  1.00 19.90  ? 65  TRP I CG  1 
ATOM   13965 C CD1 . TRP I  1 73  ? 38.348  9.195   37.005  1.00 20.43  ? 65  TRP I CD1 1 
ATOM   13966 C CD2 . TRP I  1 73  ? 38.151  10.472  35.164  1.00 17.52  ? 65  TRP I CD2 1 
ATOM   13967 N NE1 . TRP I  1 73  ? 38.700  8.427   35.914  1.00 19.84  ? 65  TRP I NE1 1 
ATOM   13968 C CE2 . TRP I  1 73  ? 38.589  9.185   34.775  1.00 20.95  ? 65  TRP I CE2 1 
ATOM   13969 C CE3 . TRP I  1 73  ? 37.961  11.446  34.173  1.00 14.86  ? 65  TRP I CE3 1 
ATOM   13970 C CZ2 . TRP I  1 73  ? 38.839  8.848   33.428  1.00 22.36  ? 65  TRP I CZ2 1 
ATOM   13971 C CZ3 . TRP I  1 73  ? 38.218  11.108  32.837  1.00 15.55  ? 65  TRP I CZ3 1 
ATOM   13972 C CH2 . TRP I  1 73  ? 38.646  9.822   32.481  1.00 14.90  ? 65  TRP I CH2 1 
ATOM   13973 N N   . ASN I  1 74  ? 39.761  11.126  39.572  1.00 27.16  ? 66  ASN I N   1 
ATOM   13974 C CA  . ASN I  1 74  ? 40.846  10.358  40.153  1.00 28.72  ? 66  ASN I CA  1 
ATOM   13975 C C   . ASN I  1 74  ? 40.836  8.907   39.649  1.00 30.85  ? 66  ASN I C   1 
ATOM   13976 O O   . ASN I  1 74  ? 39.903  8.160   39.918  1.00 29.41  ? 66  ASN I O   1 
ATOM   13977 C CB  . ASN I  1 74  ? 40.762  10.446  41.677  1.00 31.98  ? 66  ASN I CB  1 
ATOM   13978 C CG  . ASN I  1 74  ? 42.012  9.968   42.365  1.00 39.89  ? 66  ASN I CG  1 
ATOM   13979 O OD1 . ASN I  1 74  ? 42.741  9.118   41.853  1.00 41.86  ? 66  ASN I OD1 1 
ATOM   13980 N ND2 . ASN I  1 74  ? 42.245  10.483  43.563  1.00 49.90  ? 66  ASN I ND2 1 
ATOM   13981 N N   . SER I  1 75  ? 41.884  8.514   38.924  1.00 30.19  ? 67  SER I N   1 
ATOM   13982 C CA  . SER I  1 75  ? 41.891  7.237   38.199  1.00 29.97  ? 67  SER I CA  1 
ATOM   13983 C C   . SER I  1 75  ? 42.578  6.052   38.892  1.00 35.27  ? 67  SER I C   1 
ATOM   13984 O O   . SER I  1 75  ? 42.910  5.069   38.230  1.00 36.15  ? 67  SER I O   1 
ATOM   13985 C CB  . SER I  1 75  ? 42.516  7.424   36.805  1.00 28.70  ? 67  SER I CB  1 
ATOM   13986 O OG  . SER I  1 75  ? 43.796  8.038   36.878  1.00 27.93  ? 67  SER I OG  1 
ATOM   13987 N N   . SER I  1 76  ? 42.786  6.132   40.203  1.00 34.86  ? 68  SER I N   1 
ATOM   13988 C CA  . SER I  1 76  ? 43.528  5.095   40.922  1.00 34.59  ? 68  SER I CA  1 
ATOM   13989 C C   . SER I  1 76  ? 42.982  3.683   40.753  1.00 38.82  ? 68  SER I C   1 
ATOM   13990 O O   . SER I  1 76  ? 43.754  2.730   40.631  1.00 39.07  ? 68  SER I O   1 
ATOM   13991 C CB  . SER I  1 76  ? 43.634  5.439   42.401  1.00 34.58  ? 68  SER I CB  1 
ATOM   13992 O OG  . SER I  1 76  ? 44.419  6.603   42.556  1.00 41.78  ? 68  SER I OG  1 
ATOM   13993 N N   . HIS I  1 77  ? 41.661  3.545   40.746  1.00 34.08  ? 69  HIS I N   1 
ATOM   13994 C CA  . HIS I  1 77  ? 41.054  2.241   40.491  1.00 38.04  ? 69  HIS I CA  1 
ATOM   13995 C C   . HIS I  1 77  ? 39.876  2.319   39.523  1.00 38.37  ? 69  HIS I C   1 
ATOM   13996 O O   . HIS I  1 77  ? 38.986  1.464   39.524  1.00 34.23  ? 69  HIS I O   1 
ATOM   13997 C CB  . HIS I  1 77  ? 40.668  1.560   41.796  1.00 41.13  ? 69  HIS I CB  1 
ATOM   13998 C CG  . HIS I  1 77  ? 41.840  1.236   42.667  1.00 50.93  ? 69  HIS I CG  1 
ATOM   13999 N ND1 . HIS I  1 77  ? 42.580  0.077   42.522  1.00 52.85  ? 69  HIS I ND1 1 
ATOM   14000 C CD2 . HIS I  1 77  ? 42.412  1.918   43.688  1.00 46.33  ? 69  HIS I CD2 1 
ATOM   14001 C CE1 . HIS I  1 77  ? 43.546  0.060   43.419  1.00 49.58  ? 69  HIS I CE1 1 
ATOM   14002 N NE2 . HIS I  1 77  ? 43.469  1.168   44.140  1.00 46.71  ? 69  HIS I NE2 1 
ATOM   14003 N N   . SER I  1 78  ? 39.905  3.361   38.694  1.00 39.93  ? 70  SER I N   1 
ATOM   14004 C CA  . SER I  1 78  ? 38.976  3.555   37.585  1.00 35.69  ? 70  SER I CA  1 
ATOM   14005 C C   . SER I  1 78  ? 39.795  3.775   36.289  1.00 32.34  ? 70  SER I C   1 
ATOM   14006 O O   . SER I  1 78  ? 40.986  4.051   36.362  1.00 30.05  ? 70  SER I O   1 
ATOM   14007 C CB  . SER I  1 78  ? 38.062  4.749   37.888  1.00 29.84  ? 70  SER I CB  1 
ATOM   14008 O OG  . SER I  1 78  ? 38.799  5.951   38.034  1.00 32.16  ? 70  SER I OG  1 
ATOM   14009 N N   . PRO I  1 79  ? 39.167  3.637   35.105  1.00 33.40  ? 71  PRO I N   1 
ATOM   14010 C CA  . PRO I  1 79  ? 39.863  3.771   33.816  1.00 26.71  ? 71  PRO I CA  1 
ATOM   14011 C C   . PRO I  1 79  ? 40.617  5.076   33.629  1.00 25.31  ? 71  PRO I C   1 
ATOM   14012 O O   . PRO I  1 79  ? 40.258  6.061   34.256  1.00 26.48  ? 71  PRO I O   1 
ATOM   14013 C CB  . PRO I  1 79  ? 38.721  3.692   32.812  1.00 30.18  ? 71  PRO I CB  1 
ATOM   14014 C CG  . PRO I  1 79  ? 37.744  2.798   33.468  1.00 30.08  ? 71  PRO I CG  1 
ATOM   14015 C CD  . PRO I  1 79  ? 37.784  3.166   34.918  1.00 27.95  ? 71  PRO I CD  1 
ATOM   14016 N N   . ASP I  1 80  ? 41.635  5.075   32.766  1.00 31.21  ? 72  ASP I N   1 
ATOM   14017 C CA  . ASP I  1 80  ? 42.511  6.238   32.565  1.00 27.40  ? 72  ASP I CA  1 
ATOM   14018 C C   . ASP I  1 80  ? 41.990  7.206   31.517  1.00 22.24  ? 72  ASP I C   1 
ATOM   14019 O O   . ASP I  1 80  ? 42.334  8.391   31.522  1.00 21.42  ? 72  ASP I O   1 
ATOM   14020 C CB  . ASP I  1 80  ? 43.908  5.782   32.153  1.00 31.81  ? 72  ASP I CB  1 
ATOM   14021 C CG  . ASP I  1 80  ? 44.586  4.968   33.221  1.00 49.16  ? 72  ASP I CG  1 
ATOM   14022 O OD1 . ASP I  1 80  ? 45.249  5.574   34.097  1.00 54.97  ? 72  ASP I OD1 1 
ATOM   14023 O OD2 . ASP I  1 80  ? 44.446  3.724   33.190  1.00 56.11  ? 72  ASP I OD2 1 
ATOM   14024 N N   . GLN I  1 81  ? 41.188  6.684   30.597  1.00 19.98  ? 73  GLN I N   1 
ATOM   14025 C CA  . GLN I  1 81  ? 40.529  7.508   29.603  1.00 19.53  ? 73  GLN I CA  1 
ATOM   14026 C C   . GLN I  1 81  ? 39.275  6.835   29.062  1.00 20.88  ? 73  GLN I C   1 
ATOM   14027 O O   . GLN I  1 81  ? 39.151  5.606   29.122  1.00 21.27  ? 73  GLN I O   1 
ATOM   14028 C CB  . GLN I  1 81  ? 41.498  7.832   28.471  1.00 26.69  ? 73  GLN I CB  1 
ATOM   14029 C CG  . GLN I  1 81  ? 42.551  6.760   28.229  1.00 31.45  ? 73  GLN I CG  1 
ATOM   14030 C CD  . GLN I  1 81  ? 43.712  7.268   27.394  1.00 38.20  ? 73  GLN I CD  1 
ATOM   14031 O OE1 . GLN I  1 81  ? 43.621  8.322   26.752  1.00 33.95  ? 73  GLN I OE1 1 
ATOM   14032 N NE2 . GLN I  1 81  ? 44.815  6.528   27.410  1.00 41.41  ? 73  GLN I NE2 1 
ATOM   14033 N N   . VAL I  1 82  ? 38.339  7.641   28.559  1.00 17.99  ? 74  VAL I N   1 
ATOM   14034 C CA  . VAL I  1 82  ? 37.150  7.116   27.883  1.00 18.10  ? 74  VAL I CA  1 
ATOM   14035 C C   . VAL I  1 82  ? 36.933  7.831   26.557  1.00 14.75  ? 74  VAL I C   1 
ATOM   14036 O O   . VAL I  1 82  ? 37.535  8.870   26.309  1.00 14.88  ? 74  VAL I O   1 
ATOM   14037 C CB  . VAL I  1 82  ? 35.842  7.205   28.757  1.00 18.53  ? 74  VAL I CB  1 
ATOM   14038 C CG1 . VAL I  1 82  ? 35.953  6.345   30.007  1.00 15.15  ? 74  VAL I CG1 1 
ATOM   14039 C CG2 . VAL I  1 82  ? 35.500  8.639   29.120  1.00 14.08  ? 74  VAL I CG2 1 
ATOM   14040 N N   . SER I  1 83  ? 36.082  7.262   25.704  1.00 19.68  ? 75  SER I N   1 
ATOM   14041 C CA  . SER I  1 83  ? 35.678  7.911   24.452  1.00 16.04  ? 75  SER I CA  1 
ATOM   14042 C C   . SER I  1 83  ? 34.347  8.602   24.684  1.00 17.92  ? 75  SER I C   1 
ATOM   14043 O O   . SER I  1 83  ? 33.458  8.061   25.358  1.00 14.80  ? 75  SER I O   1 
ATOM   14044 C CB  . SER I  1 83  ? 35.528  6.897   23.321  1.00 17.14  ? 75  SER I CB  1 
ATOM   14045 O OG  . SER I  1 83  ? 36.759  6.255   23.029  1.00 20.73  ? 75  SER I OG  1 
ATOM   14046 N N   . VAL I  1 84  ? 34.211  9.805   24.142  1.00 12.73  ? 76  VAL I N   1 
ATOM   14047 C CA  . VAL I  1 84  ? 33.032  10.608  24.399  1.00 13.85  ? 76  VAL I CA  1 
ATOM   14048 C C   . VAL I  1 84  ? 32.572  11.221  23.082  1.00 16.78  ? 76  VAL I C   1 
ATOM   14049 O O   . VAL I  1 84  ? 33.369  11.840  22.381  1.00 18.68  ? 76  VAL I O   1 
ATOM   14050 C CB  . VAL I  1 84  ? 33.359  11.722  25.427  1.00 13.75  ? 76  VAL I CB  1 
ATOM   14051 C CG1 . VAL I  1 84  ? 32.190  12.674  25.619  1.00 10.10  ? 76  VAL I CG1 1 
ATOM   14052 C CG2 . VAL I  1 84  ? 33.803  11.120  26.759  1.00 12.10  ? 76  VAL I CG2 1 
ATOM   14053 N N   . PRO I  1 85  ? 31.285  11.051  22.733  1.00 17.57  ? 77  PRO I N   1 
ATOM   14054 C CA  . PRO I  1 85  ? 30.781  11.688  21.510  1.00 16.99  ? 77  PRO I CA  1 
ATOM   14055 C C   . PRO I  1 85  ? 30.996  13.200  21.591  1.00 19.91  ? 77  PRO I C   1 
ATOM   14056 O O   . PRO I  1 85  ? 30.656  13.787  22.624  1.00 16.80  ? 77  PRO I O   1 
ATOM   14057 C CB  . PRO I  1 85  ? 29.281  11.373  21.541  1.00 11.33  ? 77  PRO I CB  1 
ATOM   14058 C CG  . PRO I  1 85  ? 29.139  10.205  22.459  1.00 10.97  ? 77  PRO I CG  1 
ATOM   14059 C CD  . PRO I  1 85  ? 30.219  10.363  23.483  1.00 14.80  ? 77  PRO I CD  1 
ATOM   14060 N N   . ILE I  1 86  ? 31.556  13.815  20.547  1.00 21.03  ? 78  ILE I N   1 
ATOM   14061 C CA  . ILE I  1 86  ? 31.928  15.233  20.629  1.00 20.05  ? 78  ILE I CA  1 
ATOM   14062 C C   . ILE I  1 86  ? 30.783  16.206  20.942  1.00 14.01  ? 78  ILE I C   1 
ATOM   14063 O O   . ILE I  1 86  ? 31.021  17.308  21.424  1.00 14.54  ? 78  ILE I O   1 
ATOM   14064 C CB  . ILE I  1 86  ? 32.693  15.726  19.372  1.00 17.90  ? 78  ILE I CB  1 
ATOM   14065 C CG1 . ILE I  1 86  ? 31.902  15.434  18.101  1.00 19.05  ? 78  ILE I CG1 1 
ATOM   14066 C CG2 . ILE I  1 86  ? 34.079  15.120  19.312  1.00 13.32  ? 78  ILE I CG2 1 
ATOM   14067 C CD1 . ILE I  1 86  ? 32.491  16.115  16.884  1.00 21.38  ? 78  ILE I CD1 1 
ATOM   14068 N N   . SER I  1 87  ? 29.547  15.812  20.670  1.00 13.48  ? 79  SER I N   1 
ATOM   14069 C CA  . SER I  1 87  ? 28.407  16.659  21.038  1.00 17.62  ? 79  SER I CA  1 
ATOM   14070 C C   . SER I  1 87  ? 28.228  16.821  22.578  1.00 16.17  ? 79  SER I C   1 
ATOM   14071 O O   . SER I  1 87  ? 27.492  17.690  23.035  1.00 17.64  ? 79  SER I O   1 
ATOM   14072 C CB  . SER I  1 87  ? 27.122  16.142  20.386  1.00 12.56  ? 79  SER I CB  1 
ATOM   14073 O OG  . SER I  1 87  ? 26.827  14.829  20.834  1.00 19.99  ? 79  SER I OG  1 
ATOM   14074 N N   . SER I  1 88  ? 28.916  15.993  23.360  1.00 12.84  ? 80  SER I N   1 
ATOM   14075 C CA  . SER I  1 88  ? 28.931  16.120  24.806  1.00 14.28  ? 80  SER I CA  1 
ATOM   14076 C C   . SER I  1 88  ? 30.023  17.052  25.363  1.00 17.07  ? 80  SER I C   1 
ATOM   14077 O O   . SER I  1 88  ? 30.041  17.323  26.564  1.00 15.22  ? 80  SER I O   1 
ATOM   14078 C CB  . SER I  1 88  ? 29.080  14.744  25.446  1.00 14.88  ? 80  SER I CB  1 
ATOM   14079 O OG  . SER I  1 88  ? 28.027  13.893  25.043  1.00 24.71  ? 80  SER I OG  1 
ATOM   14080 N N   . LEU I  1 89  ? 30.926  17.537  24.513  1.00 14.46  ? 81  LEU I N   1 
ATOM   14081 C CA  . LEU I  1 89  ? 32.053  18.344  24.989  1.00 13.12  ? 81  LEU I CA  1 
ATOM   14082 C C   . LEU I  1 89  ? 32.222  19.629  24.198  1.00 12.18  ? 81  LEU I C   1 
ATOM   14083 O O   . LEU I  1 89  ? 31.845  19.705  23.035  1.00 14.40  ? 81  LEU I O   1 
ATOM   14084 C CB  . LEU I  1 89  ? 33.360  17.571  24.854  1.00 14.88  ? 81  LEU I CB  1 
ATOM   14085 C CG  . LEU I  1 89  ? 33.541  16.156  25.366  1.00 13.10  ? 81  LEU I CG  1 
ATOM   14086 C CD1 . LEU I  1 89  ? 34.586  15.551  24.466  1.00 14.00  ? 81  LEU I CD1 1 
ATOM   14087 C CD2 . LEU I  1 89  ? 34.011  16.165  26.802  1.00 11.71  ? 81  LEU I CD2 1 
ATOM   14088 N N   . TRP I  1 90  ? 32.812  20.639  24.821  1.00 12.50  ? 82  TRP I N   1 
ATOM   14089 C CA  . TRP I  1 90  ? 33.247  21.791  24.065  1.00 14.04  ? 82  TRP I CA  1 
ATOM   14090 C C   . TRP I  1 90  ? 34.367  21.315  23.167  1.00 15.28  ? 82  TRP I C   1 
ATOM   14091 O O   . TRP I  1 90  ? 35.181  20.489  23.570  1.00 16.01  ? 82  TRP I O   1 
ATOM   14092 C CB  . TRP I  1 90  ? 33.756  22.893  24.977  1.00 11.80  ? 82  TRP I CB  1 
ATOM   14093 C CG  . TRP I  1 90  ? 34.308  24.094  24.229  1.00 15.50  ? 82  TRP I CG  1 
ATOM   14094 C CD1 . TRP I  1 90  ? 33.595  25.168  23.767  1.00 15.64  ? 82  TRP I CD1 1 
ATOM   14095 C CD2 . TRP I  1 90  ? 35.676  24.343  23.874  1.00 13.48  ? 82  TRP I CD2 1 
ATOM   14096 N NE1 . TRP I  1 90  ? 34.431  26.064  23.149  1.00 16.50  ? 82  TRP I NE1 1 
ATOM   14097 C CE2 . TRP I  1 90  ? 35.715  25.584  23.203  1.00 17.23  ? 82  TRP I CE2 1 
ATOM   14098 C CE3 . TRP I  1 90  ? 36.872  23.647  24.066  1.00 16.05  ? 82  TRP I CE3 1 
ATOM   14099 C CZ2 . TRP I  1 90  ? 36.905  26.140  22.724  1.00 12.52  ? 82  TRP I CZ2 1 
ATOM   14100 C CZ3 . TRP I  1 90  ? 38.051  24.201  23.586  1.00 12.29  ? 82  TRP I CZ3 1 
ATOM   14101 C CH2 . TRP I  1 90  ? 38.054  25.436  22.931  1.00 11.05  ? 82  TRP I CH2 1 
ATOM   14102 N N   . VAL I  1 91  ? 34.385  21.824  21.944  1.00 15.84  ? 83  VAL I N   1 
ATOM   14103 C CA  . VAL I  1 91  ? 35.418  21.509  20.962  1.00 15.62  ? 83  VAL I CA  1 
ATOM   14104 C C   . VAL I  1 91  ? 35.749  22.829  20.269  1.00 15.75  ? 83  VAL I C   1 
ATOM   14105 O O   . VAL I  1 91  ? 34.848  23.603  19.931  1.00 16.66  ? 83  VAL I O   1 
ATOM   14106 C CB  . VAL I  1 91  ? 34.912  20.454  19.948  1.00 15.46  ? 83  VAL I CB  1 
ATOM   14107 C CG1 . VAL I  1 91  ? 35.770  20.430  18.704  1.00 17.14  ? 83  VAL I CG1 1 
ATOM   14108 C CG2 . VAL I  1 91  ? 34.882  19.075  20.598  1.00 14.36  ? 83  VAL I CG2 1 
ATOM   14109 N N   . PRO I  1 92  ? 37.040  23.125  20.100  1.00 15.01  ? 84  PRO I N   1 
ATOM   14110 C CA  . PRO I  1 92  ? 37.400  24.465  19.614  1.00 17.49  ? 84  PRO I CA  1 
ATOM   14111 C C   . PRO I  1 92  ? 36.881  24.750  18.205  1.00 17.06  ? 84  PRO I C   1 
ATOM   14112 O O   . PRO I  1 92  ? 36.896  23.855  17.363  1.00 15.40  ? 84  PRO I O   1 
ATOM   14113 C CB  . PRO I  1 92  ? 38.935  24.470  19.667  1.00 13.57  ? 84  PRO I CB  1 
ATOM   14114 C CG  . PRO I  1 92  ? 39.334  23.052  19.811  1.00 16.64  ? 84  PRO I CG  1 
ATOM   14115 C CD  . PRO I  1 92  ? 38.216  22.337  20.494  1.00 16.59  ? 84  PRO I CD  1 
ATOM   14116 N N   . ASP I  1 93  ? 36.401  25.970  17.976  1.00 15.99  ? 85  ASP I N   1 
ATOM   14117 C CA  . ASP I  1 93  ? 35.810  26.343  16.690  1.00 19.64  ? 85  ASP I CA  1 
ATOM   14118 C C   . ASP I  1 93  ? 36.855  26.669  15.605  1.00 18.16  ? 85  ASP I C   1 
ATOM   14119 O O   . ASP I  1 93  ? 36.889  27.772  15.070  1.00 16.55  ? 85  ASP I O   1 
ATOM   14120 C CB  . ASP I  1 93  ? 34.788  27.485  16.861  1.00 18.33  ? 85  ASP I CB  1 
ATOM   14121 C CG  . ASP I  1 93  ? 35.423  28.801  17.302  1.00 22.18  ? 85  ASP I CG  1 
ATOM   14122 O OD1 . ASP I  1 93  ? 36.183  28.805  18.296  1.00 24.73  ? 85  ASP I OD1 1 
ATOM   14123 O OD2 . ASP I  1 93  ? 35.163  29.839  16.646  1.00 23.14  ? 85  ASP I OD2 1 
ATOM   14124 N N   . LEU I  1 94  ? 37.691  25.682  15.287  1.00 19.70  ? 86  LEU I N   1 
ATOM   14125 C CA  . LEU I  1 94  ? 38.775  25.835  14.321  1.00 19.76  ? 86  LEU I CA  1 
ATOM   14126 C C   . LEU I  1 94  ? 38.254  26.012  12.905  1.00 22.94  ? 86  LEU I C   1 
ATOM   14127 O O   . LEU I  1 94  ? 37.242  25.426  12.534  1.00 30.51  ? 86  LEU I O   1 
ATOM   14128 C CB  . LEU I  1 94  ? 39.704  24.622  14.369  1.00 17.93  ? 86  LEU I CB  1 
ATOM   14129 C CG  . LEU I  1 94  ? 40.431  24.379  15.698  1.00 24.78  ? 86  LEU I CG  1 
ATOM   14130 C CD1 . LEU I  1 94  ? 41.324  23.152  15.618  1.00 17.27  ? 86  LEU I CD1 1 
ATOM   14131 C CD2 . LEU I  1 94  ? 41.230  25.614  16.154  1.00 20.81  ? 86  LEU I CD2 1 
ATOM   14132 N N   . ALA I  1 95  ? 38.950  26.822  12.117  1.00 21.02  ? 87  ALA I N   1 
ATOM   14133 C CA  . ALA I  1 95  ? 38.610  27.021  10.710  1.00 21.94  ? 87  ALA I CA  1 
ATOM   14134 C C   . ALA I  1 95  ? 39.881  27.175  9.863   1.00 24.04  ? 87  ALA I C   1 
ATOM   14135 O O   . ALA I  1 95  ? 40.833  27.833  10.282  1.00 26.39  ? 87  ALA I O   1 
ATOM   14136 C CB  . ALA I  1 95  ? 37.719  28.248  10.560  1.00 17.08  ? 87  ALA I CB  1 
ATOM   14137 N N   . ALA I  1 96  ? 39.912  26.565  8.683   1.00 26.65  ? 88  ALA I N   1 
ATOM   14138 C CA  . ALA I  1 96  ? 41.022  26.793  7.748   1.00 25.47  ? 88  ALA I CA  1 
ATOM   14139 C C   . ALA I  1 96  ? 40.747  28.037  6.917   1.00 21.82  ? 88  ALA I C   1 
ATOM   14140 O O   . ALA I  1 96  ? 39.826  28.031  6.118   1.00 24.54  ? 88  ALA I O   1 
ATOM   14141 C CB  . ALA I  1 96  ? 41.192  25.608  6.850   1.00 24.64  ? 88  ALA I CB  1 
ATOM   14142 N N   . TYR I  1 97  ? 41.541  29.091  7.102   1.00 26.40  ? 89  TYR I N   1 
ATOM   14143 C CA  . TYR I  1 97  ? 41.303  30.403  6.464   1.00 27.70  ? 89  TYR I CA  1 
ATOM   14144 C C   . TYR I  1 97  ? 41.198  30.356  4.946   1.00 24.45  ? 89  TYR I C   1 
ATOM   14145 O O   . TYR I  1 97  ? 40.488  31.150  4.335   1.00 25.03  ? 89  TYR I O   1 
ATOM   14146 C CB  . TYR I  1 97  ? 42.402  31.403  6.843   1.00 28.15  ? 89  TYR I CB  1 
ATOM   14147 C CG  . TYR I  1 97  ? 42.373  31.840  8.287   1.00 29.05  ? 89  TYR I CG  1 
ATOM   14148 C CD1 . TYR I  1 97  ? 42.098  33.154  8.634   1.00 35.67  ? 89  TYR I CD1 1 
ATOM   14149 C CD2 . TYR I  1 97  ? 42.610  30.934  9.303   1.00 31.23  ? 89  TYR I CD2 1 
ATOM   14150 C CE1 . TYR I  1 97  ? 42.069  33.551  9.969   1.00 42.92  ? 89  TYR I CE1 1 
ATOM   14151 C CE2 . TYR I  1 97  ? 42.585  31.308  10.627  1.00 39.01  ? 89  TYR I CE2 1 
ATOM   14152 C CZ  . TYR I  1 97  ? 42.315  32.617  10.964  1.00 46.78  ? 89  TYR I CZ  1 
ATOM   14153 O OH  . TYR I  1 97  ? 42.289  32.970  12.304  1.00 46.17  ? 89  TYR I OH  1 
ATOM   14154 N N   . ASN I  1 98  ? 41.927  29.430  4.340   1.00 27.77  ? 90  ASN I N   1 
ATOM   14155 C CA  . ASN I  1 98  ? 41.955  29.304  2.891   1.00 31.45  ? 90  ASN I CA  1 
ATOM   14156 C C   . ASN I  1 98  ? 41.300  27.991  2.469   1.00 27.39  ? 90  ASN I C   1 
ATOM   14157 O O   . ASN I  1 98  ? 41.755  27.314  1.548   1.00 29.18  ? 90  ASN I O   1 
ATOM   14158 C CB  . ASN I  1 98  ? 43.398  29.399  2.375   1.00 25.07  ? 90  ASN I CB  1 
ATOM   14159 C CG  . ASN I  1 98  ? 44.302  28.342  2.988   1.00 27.87  ? 90  ASN I CG  1 
ATOM   14160 O OD1 . ASN I  1 98  ? 44.532  28.328  4.197   1.00 29.30  ? 90  ASN I OD1 1 
ATOM   14161 N ND2 . ASN I  1 98  ? 44.819  27.451  2.155   1.00 30.64  ? 90  ASN I ND2 1 
ATOM   14162 N N   . ALA I  1 99  ? 40.232  27.626  3.161   1.00 23.35  ? 91  ALA I N   1 
ATOM   14163 C CA  . ALA I  1 99  ? 39.467  26.462  2.765   1.00 21.66  ? 91  ALA I CA  1 
ATOM   14164 C C   . ALA I  1 99  ? 38.516  26.911  1.671   1.00 20.51  ? 91  ALA I C   1 
ATOM   14165 O O   . ALA I  1 99  ? 38.159  28.098  1.595   1.00 15.48  ? 91  ALA I O   1 
ATOM   14166 C CB  . ALA I  1 99  ? 38.705  25.910  3.935   1.00 22.17  ? 91  ALA I CB  1 
ATOM   14167 N N   . ILE I  1 100 ? 38.136  25.978  0.802   1.00 17.32  ? 92  ILE I N   1 
ATOM   14168 C CA  . ILE I  1 100 ? 37.157  26.284  -0.234  1.00 20.20  ? 92  ILE I CA  1 
ATOM   14169 C C   . ILE I  1 100 ? 36.057  25.224  -0.357  1.00 21.55  ? 92  ILE I C   1 
ATOM   14170 O O   . ILE I  1 100 ? 35.092  25.409  -1.094  1.00 20.59  ? 92  ILE I O   1 
ATOM   14171 C CB  . ILE I  1 100 ? 37.804  26.581  -1.602  1.00 23.85  ? 92  ILE I CB  1 
ATOM   14172 C CG1 . ILE I  1 100 ? 38.735  25.449  -2.028  1.00 25.65  ? 92  ILE I CG1 1 
ATOM   14173 C CG2 . ILE I  1 100 ? 38.549  27.919  -1.578  1.00 20.51  ? 92  ILE I CG2 1 
ATOM   14174 C CD1 . ILE I  1 100 ? 39.275  25.652  -3.420  1.00 26.54  ? 92  ILE I CD1 1 
ATOM   14175 N N   . SER I  1 101 ? 36.197  24.130  0.386   1.00 21.67  ? 93  SER I N   1 
ATOM   14176 C CA  . SER I  1 101 ? 35.101  23.188  0.567   1.00 20.91  ? 93  SER I CA  1 
ATOM   14177 C C   . SER I  1 101 ? 34.866  22.981  2.066   1.00 23.78  ? 93  SER I C   1 
ATOM   14178 O O   . SER I  1 101 ? 35.725  23.324  2.880   1.00 23.50  ? 93  SER I O   1 
ATOM   14179 C CB  . SER I  1 101 ? 35.410  21.862  -0.128  1.00 20.91  ? 93  SER I CB  1 
ATOM   14180 O OG  . SER I  1 101 ? 36.177  21.003  0.692   1.00 18.98  ? 93  SER I OG  1 
ATOM   14181 N N   . LYS I  1 102 ? 33.701  22.457  2.441   1.00 23.92  ? 94  LYS I N   1 
ATOM   14182 C CA  . LYS I  1 102 ? 33.442  22.145  3.846   1.00 20.93  ? 94  LYS I CA  1 
ATOM   14183 C C   . LYS I  1 102 ? 34.417  21.076  4.268   1.00 24.10  ? 94  LYS I C   1 
ATOM   14184 O O   . LYS I  1 102 ? 34.864  20.278  3.445   1.00 24.04  ? 94  LYS I O   1 
ATOM   14185 C CB  . LYS I  1 102 ? 32.026  21.604  4.063   1.00 19.87  ? 94  LYS I CB  1 
ATOM   14186 C CG  . LYS I  1 102 ? 30.912  22.580  3.710   1.00 27.04  ? 94  LYS I CG  1 
ATOM   14187 C CD  . LYS I  1 102 ? 29.577  22.222  4.383   1.00 33.57  ? 94  LYS I CD  1 
ATOM   14188 C CE  . LYS I  1 102 ? 29.065  20.855  3.961   1.00 39.65  ? 94  LYS I CE  1 
ATOM   14189 N NZ  . LYS I  1 102 ? 27.782  20.538  4.647   1.00 40.56  ? 94  LYS I NZ  1 
ATOM   14190 N N   . PRO I  1 103 ? 34.770  21.056  5.554   1.00 28.80  ? 95  PRO I N   1 
ATOM   14191 C CA  . PRO I  1 103 ? 35.513  19.871  5.991   1.00 24.29  ? 95  PRO I CA  1 
ATOM   14192 C C   . PRO I  1 103 ? 34.612  18.650  5.884   1.00 20.99  ? 95  PRO I C   1 
ATOM   14193 O O   . PRO I  1 103 ? 33.454  18.720  6.264   1.00 22.39  ? 95  PRO I O   1 
ATOM   14194 C CB  . PRO I  1 103 ? 35.862  20.179  7.453   1.00 14.75  ? 95  PRO I CB  1 
ATOM   14195 C CG  . PRO I  1 103 ? 35.044  21.368  7.824   1.00 18.53  ? 95  PRO I CG  1 
ATOM   14196 C CD  . PRO I  1 103 ? 34.713  22.111  6.581   1.00 21.64  ? 95  PRO I CD  1 
ATOM   14197 N N   . GLU I  1 104 ? 35.122  17.563  5.326   1.00 22.32  ? 96  GLU I N   1 
ATOM   14198 C CA  . GLU I  1 104 ? 34.348  16.336  5.236   1.00 21.09  ? 96  GLU I CA  1 
ATOM   14199 C C   . GLU I  1 104 ? 34.955  15.339  6.210   1.00 21.97  ? 96  GLU I C   1 
ATOM   14200 O O   . GLU I  1 104 ? 36.059  14.845  5.994   1.00 23.20  ? 96  GLU I O   1 
ATOM   14201 C CB  . GLU I  1 104 ? 34.381  15.793  3.805   1.00 24.08  ? 96  GLU I CB  1 
ATOM   14202 C CG  . GLU I  1 104 ? 33.334  14.734  3.479   1.00 27.87  ? 96  GLU I CG  1 
ATOM   14203 C CD  . GLU I  1 104 ? 33.431  14.228  2.028   1.00 53.26  ? 96  GLU I CD  1 
ATOM   14204 O OE1 . GLU I  1 104 ? 34.531  14.287  1.423   1.00 35.87  ? 96  GLU I OE1 1 
ATOM   14205 O OE2 . GLU I  1 104 ? 32.396  13.774  1.487   1.00 68.79  ? 96  GLU I OE2 1 
ATOM   14206 N N   . VAL I  1 105 ? 34.245  15.052  7.294   1.00 18.67  ? 97  VAL I N   1 
ATOM   14207 C CA  . VAL I  1 105 ? 34.794  14.179  8.317   1.00 17.27  ? 97  VAL I CA  1 
ATOM   14208 C C   . VAL I  1 105 ? 34.604  12.711  7.949   1.00 18.10  ? 97  VAL I C   1 
ATOM   14209 O O   . VAL I  1 105 ? 33.493  12.261  7.676   1.00 20.81  ? 97  VAL I O   1 
ATOM   14210 C CB  . VAL I  1 105 ? 34.222  14.513  9.729   1.00 14.36  ? 97  VAL I CB  1 
ATOM   14211 C CG1 . VAL I  1 105 ? 34.668  13.468  10.763  1.00 13.49  ? 97  VAL I CG1 1 
ATOM   14212 C CG2 . VAL I  1 105 ? 34.660  15.910  10.144  1.00 8.93   ? 97  VAL I CG2 1 
ATOM   14213 N N   . LEU I  1 106 ? 35.699  11.963  7.944   1.00 18.54  ? 98  LEU I N   1 
ATOM   14214 C CA  . LEU I  1 106 ? 35.647  10.566  7.533   1.00 19.89  ? 98  LEU I CA  1 
ATOM   14215 C C   . LEU I  1 106 ? 35.643  9.594   8.701   1.00 17.45  ? 98  LEU I C   1 
ATOM   14216 O O   . LEU I  1 106 ? 35.515  8.394   8.508   1.00 18.93  ? 98  LEU I O   1 
ATOM   14217 C CB  . LEU I  1 106 ? 36.839  10.244  6.634   1.00 23.37  ? 98  LEU I CB  1 
ATOM   14218 C CG  . LEU I  1 106 ? 37.053  11.181  5.452   1.00 20.85  ? 98  LEU I CG  1 
ATOM   14219 C CD1 . LEU I  1 106 ? 38.300  10.790  4.688   1.00 21.64  ? 98  LEU I CD1 1 
ATOM   14220 C CD2 . LEU I  1 106 ? 35.827  11.127  4.572   1.00 21.05  ? 98  LEU I CD2 1 
ATOM   14221 N N   . THR I  1 107 ? 35.795  10.103  9.915   1.00 20.66  ? 99  THR I N   1 
ATOM   14222 C CA  . THR I  1 107 ? 35.932  9.225   11.072  1.00 20.48  ? 99  THR I CA  1 
ATOM   14223 C C   . THR I  1 107 ? 34.770  9.397   12.031  1.00 17.57  ? 99  THR I C   1 
ATOM   14224 O O   . THR I  1 107 ? 34.054  10.397  11.933  1.00 14.06  ? 99  THR I O   1 
ATOM   14225 C CB  . THR I  1 107 ? 37.261  9.472   11.793  1.00 17.22  ? 99  THR I CB  1 
ATOM   14226 O OG1 . THR I  1 107 ? 37.678  10.830  11.581  1.00 19.07  ? 99  THR I OG1 1 
ATOM   14227 C CG2 . THR I  1 107 ? 38.298  8.540   11.227  1.00 23.51  ? 99  THR I CG2 1 
ATOM   14228 N N   . PRO I  1 108 ? 34.562  8.407   12.932  1.00 16.17  ? 100 PRO I N   1 
ATOM   14229 C CA  . PRO I  1 108 ? 33.559  8.544   13.994  1.00 14.96  ? 100 PRO I CA  1 
ATOM   14230 C C   . PRO I  1 108 ? 33.842  9.799   14.803  1.00 18.87  ? 100 PRO I C   1 
ATOM   14231 O O   . PRO I  1 108 ? 34.995  10.024  15.177  1.00 21.31  ? 100 PRO I O   1 
ATOM   14232 C CB  . PRO I  1 108 ? 33.793  7.306   14.860  1.00 13.02  ? 100 PRO I CB  1 
ATOM   14233 C CG  . PRO I  1 108 ? 34.334  6.301   13.934  1.00 19.49  ? 100 PRO I CG  1 
ATOM   14234 C CD  . PRO I  1 108 ? 35.169  7.063   12.929  1.00 17.81  ? 100 PRO I CD  1 
ATOM   14235 N N   . GLN I  1 109 ? 32.822  10.617  15.039  1.00 15.77  ? 101 GLN I N   1 
ATOM   14236 C CA  . GLN I  1 109 ? 32.990  11.810  15.854  1.00 17.81  ? 101 GLN I CA  1 
ATOM   14237 C C   . GLN I  1 109 ? 33.122  11.450  17.349  1.00 23.56  ? 101 GLN I C   1 
ATOM   14238 O O   . GLN I  1 109 ? 32.191  11.674  18.152  1.00 22.73  ? 101 GLN I O   1 
ATOM   14239 C CB  . GLN I  1 109 ? 31.816  12.767  15.631  1.00 20.24  ? 101 GLN I CB  1 
ATOM   14240 C CG  . GLN I  1 109 ? 31.557  13.142  14.177  1.00 21.55  ? 101 GLN I CG  1 
ATOM   14241 C CD  . GLN I  1 109 ? 32.407  14.312  13.699  1.00 24.50  ? 101 GLN I CD  1 
ATOM   14242 O OE1 . GLN I  1 109 ? 33.595  14.414  14.029  1.00 24.60  ? 101 GLN I OE1 1 
ATOM   14243 N NE2 . GLN I  1 109 ? 31.799  15.208  12.923  1.00 20.88  ? 101 GLN I NE2 1 
ATOM   14244 N N   . LEU I  1 110 ? 34.270  10.882  17.721  1.00 19.29  ? 102 LEU I N   1 
ATOM   14245 C CA  . LEU I  1 110 ? 34.539  10.559  19.128  1.00 21.49  ? 102 LEU I CA  1 
ATOM   14246 C C   . LEU I  1 110 ? 35.824  11.216  19.598  1.00 18.38  ? 102 LEU I C   1 
ATOM   14247 O O   . LEU I  1 110 ? 36.794  11.283  18.851  1.00 19.75  ? 102 LEU I O   1 
ATOM   14248 C CB  . LEU I  1 110 ? 34.631  9.048   19.344  1.00 17.64  ? 102 LEU I CB  1 
ATOM   14249 C CG  . LEU I  1 110 ? 33.356  8.264   19.073  1.00 16.13  ? 102 LEU I CG  1 
ATOM   14250 C CD1 . LEU I  1 110 ? 33.568  6.805   19.396  1.00 12.21  ? 102 LEU I CD1 1 
ATOM   14251 C CD2 . LEU I  1 110 ? 32.234  8.860   19.907  1.00 17.70  ? 102 LEU I CD2 1 
ATOM   14252 N N   . ALA I  1 111 ? 35.829  11.708  20.831  1.00 13.80  ? 103 ALA I N   1 
ATOM   14253 C CA  . ALA I  1 111 ? 37.054  12.240  21.415  1.00 16.25  ? 103 ALA I CA  1 
ATOM   14254 C C   . ALA I  1 111 ? 37.520  11.324  22.524  1.00 14.27  ? 103 ALA I C   1 
ATOM   14255 O O   . ALA I  1 111 ? 36.811  10.400  22.915  1.00 17.90  ? 103 ALA I O   1 
ATOM   14256 C CB  . ALA I  1 111 ? 36.841  13.653  21.949  1.00 15.66  ? 103 ALA I CB  1 
ATOM   14257 N N   . ARG I  1 112 ? 38.721  11.559  23.023  1.00 17.38  ? 104 ARG I N   1 
ATOM   14258 C CA  . ARG I  1 112 ? 39.148  10.863  24.228  1.00 17.71  ? 104 ARG I CA  1 
ATOM   14259 C C   . ARG I  1 112 ? 39.340  11.881  25.336  1.00 13.86  ? 104 ARG I C   1 
ATOM   14260 O O   . ARG I  1 112 ? 39.886  12.963  25.131  1.00 14.22  ? 104 ARG I O   1 
ATOM   14261 C CB  . ARG I  1 112 ? 40.423  10.047  23.997  1.00 17.36  ? 104 ARG I CB  1 
ATOM   14262 C CG  . ARG I  1 112 ? 40.274  8.931   22.976  1.00 15.57  ? 104 ARG I CG  1 
ATOM   14263 C CD  . ARG I  1 112 ? 39.647  7.664   23.538  1.00 14.00  ? 104 ARG I CD  1 
ATOM   14264 N NE  . ARG I  1 112 ? 40.518  6.987   24.495  1.00 16.86  ? 104 ARG I NE  1 
ATOM   14265 C CZ  . ARG I  1 112 ? 40.294  5.771   24.983  1.00 20.33  ? 104 ARG I CZ  1 
ATOM   14266 N NH1 . ARG I  1 112 ? 39.232  5.083   24.603  1.00 22.08  ? 104 ARG I NH1 1 
ATOM   14267 N NH2 . ARG I  1 112 ? 41.138  5.231   25.844  1.00 27.53  ? 104 ARG I NH2 1 
ATOM   14268 N N   . VAL I  1 113 ? 38.849  11.543  26.509  1.00 13.51  ? 105 VAL I N   1 
ATOM   14269 C CA  . VAL I  1 113 ? 39.131  12.351  27.680  1.00 17.53  ? 105 VAL I CA  1 
ATOM   14270 C C   . VAL I  1 113 ? 39.987  11.541  28.641  1.00 16.55  ? 105 VAL I C   1 
ATOM   14271 O O   . VAL I  1 113 ? 39.662  10.398  28.984  1.00 15.84  ? 105 VAL I O   1 
ATOM   14272 C CB  . VAL I  1 113 ? 37.846  12.806  28.374  1.00 17.49  ? 105 VAL I CB  1 
ATOM   14273 C CG1 . VAL I  1 113 ? 38.177  13.628  29.611  1.00 15.37  ? 105 VAL I CG1 1 
ATOM   14274 C CG2 . VAL I  1 113 ? 36.960  13.587  27.384  1.00 15.48  ? 105 VAL I CG2 1 
ATOM   14275 N N   . VAL I  1 114 ? 41.099  12.134  29.046  1.00 16.86  ? 106 VAL I N   1 
ATOM   14276 C CA  . VAL I  1 114 ? 42.015  11.495  29.976  1.00 19.95  ? 106 VAL I CA  1 
ATOM   14277 C C   . VAL I  1 114 ? 41.728  12.005  31.383  1.00 17.80  ? 106 VAL I C   1 
ATOM   14278 O O   . VAL I  1 114 ? 41.312  13.160  31.568  1.00 12.99  ? 106 VAL I O   1 
ATOM   14279 C CB  . VAL I  1 114 ? 43.474  11.806  29.590  1.00 22.54  ? 106 VAL I CB  1 
ATOM   14280 C CG1 . VAL I  1 114 ? 44.438  11.024  30.443  1.00 18.43  ? 106 VAL I CG1 1 
ATOM   14281 C CG2 . VAL I  1 114 ? 43.687  11.484  28.130  1.00 23.27  ? 106 VAL I CG2 1 
ATOM   14282 N N   . SER I  1 115 ? 41.954  11.125  32.356  1.00 18.98  ? 107 SER I N   1 
ATOM   14283 C CA  . SER I  1 115 ? 41.706  11.385  33.773  1.00 15.94  ? 107 SER I CA  1 
ATOM   14284 C C   . SER I  1 115 ? 42.299  12.676  34.323  1.00 16.05  ? 107 SER I C   1 
ATOM   14285 O O   . SER I  1 115 ? 41.781  13.221  35.296  1.00 20.58  ? 107 SER I O   1 
ATOM   14286 C CB  . SER I  1 115 ? 42.179  10.201  34.615  1.00 19.75  ? 107 SER I CB  1 
ATOM   14287 O OG  . SER I  1 115 ? 43.500  9.821   34.275  1.00 24.72  ? 107 SER I OG  1 
ATOM   14288 N N   . ASP I  1 116 ? 43.371  13.166  33.709  1.00 17.41  ? 108 ASP I N   1 
ATOM   14289 C CA  . ASP I  1 116 ? 43.960  14.446  34.103  1.00 16.99  ? 108 ASP I CA  1 
ATOM   14290 C C   . ASP I  1 116 ? 43.270  15.648  33.454  1.00 18.78  ? 108 ASP I C   1 
ATOM   14291 O O   . ASP I  1 116 ? 43.647  16.798  33.698  1.00 18.40  ? 108 ASP I O   1 
ATOM   14292 C CB  . ASP I  1 116 ? 45.454  14.474  33.797  1.00 16.41  ? 108 ASP I CB  1 
ATOM   14293 C CG  . ASP I  1 116 ? 45.751  14.414  32.307  1.00 27.99  ? 108 ASP I CG  1 
ATOM   14294 O OD1 . ASP I  1 116 ? 45.535  15.437  31.616  1.00 33.19  ? 108 ASP I OD1 1 
ATOM   14295 O OD2 . ASP I  1 116 ? 46.226  13.354  31.827  1.00 27.14  ? 108 ASP I OD2 1 
ATOM   14296 N N   . GLY I  1 117 ? 42.268  15.377  32.617  1.00 21.31  ? 109 GLY I N   1 
ATOM   14297 C CA  . GLY I  1 117 ? 41.448  16.425  32.031  1.00 20.84  ? 109 GLY I CA  1 
ATOM   14298 C C   . GLY I  1 117 ? 41.810  16.779  30.601  1.00 22.85  ? 109 GLY I C   1 
ATOM   14299 O O   . GLY I  1 117 ? 41.257  17.723  30.019  1.00 20.27  ? 109 GLY I O   1 
ATOM   14300 N N   . GLU I  1 118 ? 42.750  16.030  30.036  1.00 21.34  ? 110 GLU I N   1 
ATOM   14301 C CA  . GLU I  1 118 ? 43.195  16.283  28.684  1.00 20.65  ? 110 GLU I CA  1 
ATOM   14302 C C   . GLU I  1 118 ? 42.160  15.771  27.693  1.00 22.62  ? 110 GLU I C   1 
ATOM   14303 O O   . GLU I  1 118 ? 41.654  14.651  27.827  1.00 19.34  ? 110 GLU I O   1 
ATOM   14304 C CB  . GLU I  1 118 ? 44.536  15.606  28.428  1.00 25.76  ? 110 GLU I CB  1 
ATOM   14305 C CG  . GLU I  1 118 ? 45.535  16.517  27.728  1.00 34.58  ? 110 GLU I CG  1 
ATOM   14306 C CD  . GLU I  1 118 ? 46.182  15.878  26.517  1.00 34.55  ? 110 GLU I CD  1 
ATOM   14307 O OE1 . GLU I  1 118 ? 46.573  14.683  26.599  1.00 34.31  ? 110 GLU I OE1 1 
ATOM   14308 O OE2 . GLU I  1 118 ? 46.304  16.586  25.489  1.00 30.28  ? 110 GLU I OE2 1 
ATOM   14309 N N   . VAL I  1 119 ? 41.851  16.598  26.698  1.00 20.81  ? 111 VAL I N   1 
ATOM   14310 C CA  . VAL I  1 119 ? 40.932  16.216  25.634  1.00 20.64  ? 111 VAL I CA  1 
ATOM   14311 C C   . VAL I  1 119 ? 41.673  16.100  24.288  1.00 21.63  ? 111 VAL I C   1 
ATOM   14312 O O   . VAL I  1 119 ? 42.353  17.035  23.858  1.00 18.31  ? 111 VAL I O   1 
ATOM   14313 C CB  . VAL I  1 119 ? 39.762  17.221  25.520  1.00 18.86  ? 111 VAL I CB  1 
ATOM   14314 C CG1 . VAL I  1 119 ? 38.651  16.657  24.653  1.00 16.64  ? 111 VAL I CG1 1 
ATOM   14315 C CG2 . VAL I  1 119 ? 39.222  17.526  26.890  1.00 22.38  ? 111 VAL I CG2 1 
ATOM   14316 N N   . LEU I  1 120 ? 41.534  14.942  23.645  1.00 20.91  ? 112 LEU I N   1 
ATOM   14317 C CA  . LEU I  1 120 ? 42.144  14.677  22.351  1.00 20.72  ? 112 LEU I CA  1 
ATOM   14318 C C   . LEU I  1 120 ? 41.056  14.373  21.359  1.00 18.31  ? 112 LEU I C   1 
ATOM   14319 O O   . LEU I  1 120 ? 40.224  13.502  21.597  1.00 21.55  ? 112 LEU I O   1 
ATOM   14320 C CB  . LEU I  1 120 ? 43.047  13.453  22.423  1.00 21.80  ? 112 LEU I CB  1 
ATOM   14321 C CG  . LEU I  1 120 ? 43.744  13.251  23.761  1.00 28.20  ? 112 LEU I CG  1 
ATOM   14322 C CD1 . LEU I  1 120 ? 44.037  11.775  23.992  1.00 32.75  ? 112 LEU I CD1 1 
ATOM   14323 C CD2 . LEU I  1 120 ? 45.021  14.051  23.754  1.00 36.50  ? 112 LEU I CD2 1 
ATOM   14324 N N   . TYR I  1 121 ? 41.086  15.076  20.237  1.00 15.68  ? 113 TYR I N   1 
ATOM   14325 C CA  . TYR I  1 121 ? 40.153  14.858  19.149  1.00 13.72  ? 113 TYR I CA  1 
ATOM   14326 C C   . TYR I  1 121 ? 40.914  14.884  17.814  1.00 21.48  ? 113 TYR I C   1 
ATOM   14327 O O   . TYR I  1 121 ? 41.439  15.932  17.403  1.00 19.20  ? 113 TYR I O   1 
ATOM   14328 C CB  . TYR I  1 121 ? 39.076  15.946  19.182  1.00 13.24  ? 113 TYR I CB  1 
ATOM   14329 C CG  . TYR I  1 121 ? 38.097  15.835  18.059  1.00 10.67  ? 113 TYR I CG  1 
ATOM   14330 C CD1 . TYR I  1 121 ? 37.504  14.620  17.772  1.00 11.12  ? 113 TYR I CD1 1 
ATOM   14331 C CD2 . TYR I  1 121 ? 37.775  16.934  17.278  1.00 8.55   ? 113 TYR I CD2 1 
ATOM   14332 C CE1 . TYR I  1 121 ? 36.626  14.487  16.736  1.00 13.89  ? 113 TYR I CE1 1 
ATOM   14333 C CE2 . TYR I  1 121 ? 36.894  16.817  16.229  1.00 10.56  ? 113 TYR I CE2 1 
ATOM   14334 C CZ  . TYR I  1 121 ? 36.317  15.584  15.959  1.00 14.17  ? 113 TYR I CZ  1 
ATOM   14335 O OH  . TYR I  1 121 ? 35.419  15.423  14.922  1.00 13.54  ? 113 TYR I OH  1 
ATOM   14336 N N   . MET I  1 122 ? 40.993  13.733  17.147  1.00 20.87  ? 114 MET I N   1 
ATOM   14337 C CA  . MET I  1 122 ? 41.720  13.632  15.870  1.00 21.94  ? 114 MET I CA  1 
ATOM   14338 C C   . MET I  1 122 ? 40.851  13.061  14.744  1.00 20.56  ? 114 MET I C   1 
ATOM   14339 O O   . MET I  1 122 ? 40.874  11.851  14.460  1.00 17.85  ? 114 MET I O   1 
ATOM   14340 C CB  . MET I  1 122 ? 43.001  12.797  16.025  1.00 27.68  ? 114 MET I CB  1 
ATOM   14341 C CG  . MET I  1 122 ? 43.826  12.620  14.735  1.00 33.90  ? 114 MET I CG  1 
ATOM   14342 S SD  . MET I  1 122 ? 45.235  11.489  14.908  1.00 42.16  ? 114 MET I SD  1 
ATOM   14343 C CE  . MET I  1 122 ? 44.594  9.930   14.308  1.00 25.51  ? 114 MET I CE  1 
ATOM   14344 N N   . PRO I  1 123 ? 40.064  13.930  14.103  1.00 17.87  ? 115 PRO I N   1 
ATOM   14345 C CA  . PRO I  1 123 ? 39.287  13.494  12.940  1.00 19.55  ? 115 PRO I CA  1 
ATOM   14346 C C   . PRO I  1 123 ? 40.115  13.460  11.633  1.00 24.93  ? 115 PRO I C   1 
ATOM   14347 O O   . PRO I  1 123 ? 40.938  14.363  11.353  1.00 15.29  ? 115 PRO I O   1 
ATOM   14348 C CB  . PRO I  1 123 ? 38.194  14.558  12.846  1.00 15.97  ? 115 PRO I CB  1 
ATOM   14349 C CG  . PRO I  1 123 ? 38.840  15.800  13.392  1.00 12.06  ? 115 PRO I CG  1 
ATOM   14350 C CD  . PRO I  1 123 ? 39.777  15.325  14.481  1.00 14.14  ? 115 PRO I CD  1 
ATOM   14351 N N   . SER I  1 124 ? 39.899  12.408  10.843  1.00 22.78  ? 116 SER I N   1 
ATOM   14352 C CA  . SER I  1 124 ? 40.381  12.397  9.468   1.00 25.02  ? 116 SER I CA  1 
ATOM   14353 C C   . SER I  1 124 ? 39.500  13.318  8.626   1.00 21.66  ? 116 SER I C   1 
ATOM   14354 O O   . SER I  1 124 ? 38.275  13.314  8.757   1.00 22.39  ? 116 SER I O   1 
ATOM   14355 C CB  . SER I  1 124 ? 40.351  10.993  8.892   1.00 23.73  ? 116 SER I CB  1 
ATOM   14356 O OG  . SER I  1 124 ? 40.963  11.001  7.615   1.00 23.49  ? 116 SER I OG  1 
ATOM   14357 N N   . ILE I  1 125 ? 40.119  14.114  7.768   1.00 19.37  ? 117 ILE I N   1 
ATOM   14358 C CA  . ILE I  1 125 ? 39.379  15.126  7.025   1.00 19.08  ? 117 ILE I CA  1 
ATOM   14359 C C   . ILE I  1 125 ? 39.776  15.175  5.559   1.00 21.41  ? 117 ILE I C   1 
ATOM   14360 O O   . ILE I  1 125 ? 40.954  15.259  5.234   1.00 22.18  ? 117 ILE I O   1 
ATOM   14361 C CB  . ILE I  1 125 ? 39.577  16.531  7.637   1.00 21.70  ? 117 ILE I CB  1 
ATOM   14362 C CG1 . ILE I  1 125 ? 38.913  16.616  9.028   1.00 16.47  ? 117 ILE I CG1 1 
ATOM   14363 C CG2 . ILE I  1 125 ? 39.062  17.621  6.681   1.00 16.55  ? 117 ILE I CG2 1 
ATOM   14364 C CD1 . ILE I  1 125 ? 39.043  17.988  9.689   1.00 8.87   ? 117 ILE I CD1 1 
ATOM   14365 N N   . ARG I  1 126 ? 38.789  15.099  4.670   1.00 23.22  ? 118 ARG I N   1 
ATOM   14366 C CA  . ARG I  1 126 ? 39.015  15.438  3.273   1.00 19.39  ? 118 ARG I CA  1 
ATOM   14367 C C   . ARG I  1 126 ? 38.497  16.841  3.023   1.00 19.08  ? 118 ARG I C   1 
ATOM   14368 O O   . ARG I  1 126 ? 37.384  17.165  3.420   1.00 26.88  ? 118 ARG I O   1 
ATOM   14369 C CB  . ARG I  1 126 ? 38.319  14.461  2.341   1.00 23.01  ? 118 ARG I CB  1 
ATOM   14370 C CG  . ARG I  1 126 ? 38.422  14.899  0.897   1.00 27.45  ? 118 ARG I CG  1 
ATOM   14371 C CD  . ARG I  1 126 ? 38.051  13.815  -0.084  1.00 27.35  ? 118 ARG I CD  1 
ATOM   14372 N NE  . ARG I  1 126 ? 38.457  14.218  -1.427  1.00 40.12  ? 118 ARG I NE  1 
ATOM   14373 C CZ  . ARG I  1 126 ? 38.502  13.403  -2.476  1.00 39.60  ? 118 ARG I CZ  1 
ATOM   14374 N NH1 . ARG I  1 126 ? 38.170  12.123  -2.338  1.00 41.25  ? 118 ARG I NH1 1 
ATOM   14375 N NH2 . ARG I  1 126 ? 38.884  13.869  -3.661  1.00 41.67  ? 118 ARG I NH2 1 
ATOM   14376 N N   . GLN I  1 127 ? 39.304  17.681  2.386   1.00 18.93  ? 119 GLN I N   1 
ATOM   14377 C CA  . GLN I  1 127 ? 38.932  19.071  2.171   1.00 17.76  ? 119 GLN I CA  1 
ATOM   14378 C C   . GLN I  1 127 ? 39.779  19.716  1.073   1.00 22.65  ? 119 GLN I C   1 
ATOM   14379 O O   . GLN I  1 127 ? 40.912  19.302  0.825   1.00 18.53  ? 119 GLN I O   1 
ATOM   14380 C CB  . GLN I  1 127 ? 39.065  19.851  3.477   1.00 18.56  ? 119 GLN I CB  1 
ATOM   14381 C CG  . GLN I  1 127 ? 38.424  21.221  3.471   1.00 22.41  ? 119 GLN I CG  1 
ATOM   14382 C CD  . GLN I  1 127 ? 38.552  21.920  4.802   1.00 21.75  ? 119 GLN I CD  1 
ATOM   14383 O OE1 . GLN I  1 127 ? 38.153  23.072  4.952   1.00 18.78  ? 119 GLN I OE1 1 
ATOM   14384 N NE2 . GLN I  1 127 ? 39.114  21.222  5.782   1.00 24.90  ? 119 GLN I NE2 1 
ATOM   14385 N N   . ARG I  1 128 ? 39.206  20.735  0.437   1.00 21.35  ? 120 ARG I N   1 
ATOM   14386 C CA  . ARG I  1 128 ? 39.805  21.440  -0.683  1.00 23.99  ? 120 ARG I CA  1 
ATOM   14387 C C   . ARG I  1 128 ? 40.317  22.839  -0.285  1.00 24.49  ? 120 ARG I C   1 
ATOM   14388 O O   . ARG I  1 128 ? 39.649  23.560  0.461   1.00 27.58  ? 120 ARG I O   1 
ATOM   14389 C CB  . ARG I  1 128 ? 38.765  21.539  -1.809  1.00 30.89  ? 120 ARG I CB  1 
ATOM   14390 C CG  . ARG I  1 128 ? 39.308  22.038  -3.139  1.00 34.67  ? 120 ARG I CG  1 
ATOM   14391 C CD  . ARG I  1 128 ? 38.413  21.662  -4.312  1.00 39.70  ? 120 ARG I CD  1 
ATOM   14392 N NE  . ARG I  1 128 ? 39.034  22.089  -5.565  1.00 52.92  ? 120 ARG I NE  1 
ATOM   14393 C CZ  . ARG I  1 128 ? 39.927  21.372  -6.246  1.00 48.65  ? 120 ARG I CZ  1 
ATOM   14394 N NH1 . ARG I  1 128 ? 40.297  20.171  -5.812  1.00 41.12  ? 120 ARG I NH1 1 
ATOM   14395 N NH2 . ARG I  1 128 ? 40.450  21.854  -7.368  1.00 46.24  ? 120 ARG I NH2 1 
ATOM   14396 N N   . PHE I  1 129 ? 41.497  23.221  -0.780  1.00 26.32  ? 121 PHE I N   1 
ATOM   14397 C CA  . PHE I  1 129 ? 42.103  24.513  -0.426  1.00 26.55  ? 121 PHE I CA  1 
ATOM   14398 C C   . PHE I  1 129 ? 42.593  25.356  -1.596  1.00 33.25  ? 121 PHE I C   1 
ATOM   14399 O O   . PHE I  1 129 ? 42.913  24.850  -2.679  1.00 26.84  ? 121 PHE I O   1 
ATOM   14400 C CB  . PHE I  1 129 ? 43.304  24.331  0.498   1.00 25.03  ? 121 PHE I CB  1 
ATOM   14401 C CG  . PHE I  1 129 ? 43.006  23.574  1.733   1.00 24.32  ? 121 PHE I CG  1 
ATOM   14402 C CD1 . PHE I  1 129 ? 43.072  22.189  1.739   1.00 22.11  ? 121 PHE I CD1 1 
ATOM   14403 C CD2 . PHE I  1 129 ? 42.671  24.242  2.898   1.00 25.73  ? 121 PHE I CD2 1 
ATOM   14404 C CE1 . PHE I  1 129 ? 42.795  21.479  2.875   1.00 22.68  ? 121 PHE I CE1 1 
ATOM   14405 C CE2 . PHE I  1 129 ? 42.408  23.540  4.049   1.00 22.44  ? 121 PHE I CE2 1 
ATOM   14406 C CZ  . PHE I  1 129 ? 42.465  22.152  4.037   1.00 22.69  ? 121 PHE I CZ  1 
ATOM   14407 N N   . SER I  1 130 ? 42.680  26.654  -1.321  1.00 34.53  ? 122 SER I N   1 
ATOM   14408 C CA  . SER I  1 130 ? 43.287  27.629  -2.208  1.00 35.18  ? 122 SER I CA  1 
ATOM   14409 C C   . SER I  1 130 ? 44.701  27.958  -1.736  1.00 37.44  ? 122 SER I C   1 
ATOM   14410 O O   . SER I  1 130 ? 44.897  28.658  -0.742  1.00 38.39  ? 122 SER I O   1 
ATOM   14411 C CB  . SER I  1 130 ? 42.443  28.904  -2.246  1.00 29.50  ? 122 SER I CB  1 
ATOM   14412 O OG  . SER I  1 130 ? 43.263  30.059  -2.340  1.00 33.33  ? 122 SER I OG  1 
ATOM   14413 N N   . CYS I  1 131 ? 45.683  27.451  -2.467  1.00 39.72  ? 123 CYS I N   1 
ATOM   14414 C CA  . CYS I  1 131 ? 47.083  27.702  -2.170  1.00 45.72  ? 123 CYS I CA  1 
ATOM   14415 C C   . CYS I  1 131 ? 47.924  27.532  -3.440  1.00 47.53  ? 123 CYS I C   1 
ATOM   14416 O O   . CYS I  1 131 ? 47.453  26.958  -4.425  1.00 38.97  ? 123 CYS I O   1 
ATOM   14417 C CB  . CYS I  1 131 ? 47.552  26.733  -1.095  1.00 48.34  ? 123 CYS I CB  1 
ATOM   14418 S SG  . CYS I  1 131 ? 47.228  25.021  -1.546  1.00 58.09  ? 123 CYS I SG  1 
ATOM   14419 N N   . ASP I  1 132 ? 49.164  28.024  -3.403  1.00 55.34  ? 124 ASP I N   1 
ATOM   14420 C CA  . ASP I  1 132 ? 50.063  28.018  -4.568  1.00 48.62  ? 124 ASP I CA  1 
ATOM   14421 C C   . ASP I  1 132 ? 50.515  26.625  -5.016  1.00 43.58  ? 124 ASP I C   1 
ATOM   14422 O O   . ASP I  1 132 ? 51.252  25.936  -4.307  1.00 38.03  ? 124 ASP I O   1 
ATOM   14423 C CB  . ASP I  1 132 ? 51.292  28.881  -4.290  1.00 46.62  ? 124 ASP I CB  1 
ATOM   14424 C CG  . ASP I  1 132 ? 52.257  28.904  -5.454  1.00 50.24  ? 124 ASP I CG  1 
ATOM   14425 O OD1 . ASP I  1 132 ? 51.956  29.571  -6.474  1.00 45.71  ? 124 ASP I OD1 1 
ATOM   14426 O OD2 . ASP I  1 132 ? 53.319  28.252  -5.340  1.00 53.94  ? 124 ASP I OD2 1 
ATOM   14427 N N   . VAL I  1 133 ? 50.095  26.225  -6.211  1.00 37.71  ? 125 VAL I N   1 
ATOM   14428 C CA  . VAL I  1 133 ? 50.406  24.887  -6.690  1.00 42.37  ? 125 VAL I CA  1 
ATOM   14429 C C   . VAL I  1 133 ? 51.527  24.890  -7.738  1.00 48.41  ? 125 VAL I C   1 
ATOM   14430 O O   . VAL I  1 133 ? 52.056  23.836  -8.091  1.00 46.14  ? 125 VAL I O   1 
ATOM   14431 C CB  . VAL I  1 133 ? 49.154  24.200  -7.264  1.00 44.14  ? 125 VAL I CB  1 
ATOM   14432 C CG1 . VAL I  1 133 ? 49.324  22.692  -7.251  1.00 43.00  ? 125 VAL I CG1 1 
ATOM   14433 C CG2 . VAL I  1 133 ? 47.935  24.576  -6.455  1.00 40.49  ? 125 VAL I CG2 1 
ATOM   14434 N N   . SER I  1 134 ? 51.893  26.075  -8.221  1.00 43.99  ? 126 SER I N   1 
ATOM   14435 C CA  . SER I  1 134 ? 52.932  26.210  -9.237  1.00 43.16  ? 126 SER I CA  1 
ATOM   14436 C C   . SER I  1 134 ? 54.253  25.569  -8.817  1.00 46.02  ? 126 SER I C   1 
ATOM   14437 O O   . SER I  1 134 ? 54.816  25.898  -7.765  1.00 40.54  ? 126 SER I O   1 
ATOM   14438 C CB  . SER I  1 134 ? 53.169  27.683  -9.550  1.00 50.29  ? 126 SER I CB  1 
ATOM   14439 O OG  . SER I  1 134 ? 53.780  28.327  -8.447  1.00 50.54  ? 126 SER I OG  1 
ATOM   14440 N N   . GLY I  1 135 ? 54.741  24.651  -9.649  1.00 48.18  ? 127 GLY I N   1 
ATOM   14441 C CA  . GLY I  1 135 ? 56.009  23.990  -9.403  1.00 44.18  ? 127 GLY I CA  1 
ATOM   14442 C C   . GLY I  1 135 ? 55.858  22.539  -9.003  1.00 41.72  ? 127 GLY I C   1 
ATOM   14443 O O   . GLY I  1 135 ? 56.836  21.864  -8.705  1.00 41.81  ? 127 GLY I O   1 
ATOM   14444 N N   . VAL I  1 136 ? 54.623  22.060  -8.999  1.00 43.62  ? 128 VAL I N   1 
ATOM   14445 C CA  . VAL I  1 136 ? 54.320  20.698  -8.577  1.00 41.68  ? 128 VAL I CA  1 
ATOM   14446 C C   . VAL I  1 136 ? 55.132  19.664  -9.358  1.00 45.89  ? 128 VAL I C   1 
ATOM   14447 O O   . VAL I  1 136 ? 55.480  18.598  -8.833  1.00 43.57  ? 128 VAL I O   1 
ATOM   14448 C CB  . VAL I  1 136 ? 52.802  20.419  -8.712  1.00 40.28  ? 128 VAL I CB  1 
ATOM   14449 C CG1 . VAL I  1 136 ? 52.202  21.295  -9.797  1.00 42.69  ? 128 VAL I CG1 1 
ATOM   14450 C CG2 . VAL I  1 136 ? 52.524  18.943  -8.993  1.00 44.17  ? 128 VAL I CG2 1 
ATOM   14451 N N   . ASP I  1 137 ? 55.458  20.010  -10.603 1.00 47.29  ? 129 ASP I N   1 
ATOM   14452 C CA  . ASP I  1 137 ? 56.097  19.088  -11.544 1.00 49.90  ? 129 ASP I CA  1 
ATOM   14453 C C   . ASP I  1 137 ? 57.602  19.338  -11.725 1.00 54.80  ? 129 ASP I C   1 
ATOM   14454 O O   . ASP I  1 137 ? 58.308  18.502  -12.294 1.00 52.29  ? 129 ASP I O   1 
ATOM   14455 C CB  . ASP I  1 137 ? 55.368  19.151  -12.881 1.00 46.20  ? 129 ASP I CB  1 
ATOM   14456 C CG  . ASP I  1 137 ? 54.372  20.295  -12.932 1.00 51.07  ? 129 ASP I CG  1 
ATOM   14457 O OD1 . ASP I  1 137 ? 53.278  20.111  -13.511 1.00 52.54  ? 129 ASP I OD1 1 
ATOM   14458 O OD2 . ASP I  1 137 ? 54.683  21.376  -12.374 1.00 49.35  ? 129 ASP I OD2 1 
ATOM   14459 N N   . THR I  1 138 ? 58.079  20.488  -11.242 1.00 55.90  ? 130 THR I N   1 
ATOM   14460 C CA  . THR I  1 138 ? 59.515  20.733  -11.079 1.00 49.38  ? 130 THR I CA  1 
ATOM   14461 C C   . THR I  1 138 ? 60.053  19.890  -9.909  1.00 48.67  ? 130 THR I C   1 
ATOM   14462 O O   . THR I  1 138 ? 59.283  19.314  -9.145  1.00 50.86  ? 130 THR I O   1 
ATOM   14463 C CB  . THR I  1 138 ? 59.835  22.240  -10.851 1.00 47.06  ? 130 THR I CB  1 
ATOM   14464 O OG1 . THR I  1 138 ? 59.688  22.575  -9.464  1.00 41.10  ? 130 THR I OG1 1 
ATOM   14465 C CG2 . THR I  1 138 ? 58.932  23.134  -11.704 1.00 36.51  ? 130 THR I CG2 1 
ATOM   14466 N N   . GLU I  1 139 ? 61.372  19.802  -9.770  1.00 55.36  ? 131 GLU I N   1 
ATOM   14467 C CA  . GLU I  1 139 ? 61.949  18.943  -8.736  1.00 56.20  ? 131 GLU I CA  1 
ATOM   14468 C C   . GLU I  1 139 ? 61.964  19.628  -7.381  1.00 47.97  ? 131 GLU I C   1 
ATOM   14469 O O   . GLU I  1 139 ? 62.220  18.991  -6.357  1.00 42.70  ? 131 GLU I O   1 
ATOM   14470 C CB  . GLU I  1 139 ? 63.356  18.477  -9.125  1.00 58.63  ? 131 GLU I CB  1 
ATOM   14471 C CG  . GLU I  1 139 ? 63.369  17.419  -10.227 1.00 61.16  ? 131 GLU I CG  1 
ATOM   14472 C CD  . GLU I  1 139 ? 62.449  16.242  -9.920  1.00 64.68  ? 131 GLU I CD  1 
ATOM   14473 O OE1 . GLU I  1 139 ? 62.817  15.391  -9.077  1.00 63.56  ? 131 GLU I OE1 1 
ATOM   14474 O OE2 . GLU I  1 139 ? 61.352  16.175  -10.517 1.00 64.45  ? 131 GLU I OE2 1 
ATOM   14475 N N   . SER I  1 140 ? 61.684  20.928  -7.394  1.00 45.95  ? 132 SER I N   1 
ATOM   14476 C CA  . SER I  1 140 ? 61.583  21.723  -6.173  1.00 53.18  ? 132 SER I CA  1 
ATOM   14477 C C   . SER I  1 140 ? 60.170  21.676  -5.559  1.00 54.27  ? 132 SER I C   1 
ATOM   14478 O O   . SER I  1 140 ? 59.948  22.171  -4.449  1.00 53.51  ? 132 SER I O   1 
ATOM   14479 C CB  . SER I  1 140 ? 62.010  23.176  -6.441  1.00 55.08  ? 132 SER I CB  1 
ATOM   14480 O OG  . SER I  1 140 ? 61.331  23.731  -7.562  1.00 53.55  ? 132 SER I OG  1 
ATOM   14481 N N   . GLY I  1 141 ? 59.224  21.084  -6.290  1.00 49.08  ? 133 GLY I N   1 
ATOM   14482 C CA  . GLY I  1 141 ? 57.844  20.968  -5.843  1.00 41.30  ? 133 GLY I CA  1 
ATOM   14483 C C   . GLY I  1 141 ? 57.112  22.287  -5.631  1.00 45.28  ? 133 GLY I C   1 
ATOM   14484 O O   . GLY I  1 141 ? 57.702  23.367  -5.748  1.00 44.45  ? 133 GLY I O   1 
ATOM   14485 N N   . ALA I  1 142 ? 55.818  22.204  -5.324  1.00 41.49  ? 134 ALA I N   1 
ATOM   14486 C CA  . ALA I  1 142 ? 55.039  23.394  -4.985  1.00 40.05  ? 134 ALA I CA  1 
ATOM   14487 C C   . ALA I  1 142 ? 55.055  23.597  -3.481  1.00 38.28  ? 134 ALA I C   1 
ATOM   14488 O O   . ALA I  1 142 ? 55.382  22.671  -2.729  1.00 36.34  ? 134 ALA I O   1 
ATOM   14489 C CB  . ALA I  1 142 ? 53.616  23.265  -5.474  1.00 39.66  ? 134 ALA I CB  1 
ATOM   14490 N N   . THR I  1 143 ? 54.705  24.805  -3.044  1.00 35.90  ? 135 THR I N   1 
ATOM   14491 C CA  . THR I  1 143 ? 54.608  25.079  -1.615  1.00 35.01  ? 135 THR I CA  1 
ATOM   14492 C C   . THR I  1 143 ? 53.241  25.604  -1.198  1.00 34.89  ? 135 THR I C   1 
ATOM   14493 O O   . THR I  1 143 ? 52.888  26.765  -1.432  1.00 38.00  ? 135 THR I O   1 
ATOM   14494 C CB  . THR I  1 143 ? 55.727  26.001  -1.118  1.00 35.40  ? 135 THR I CB  1 
ATOM   14495 O OG1 . THR I  1 143 ? 56.963  25.276  -1.133  1.00 38.22  ? 135 THR I OG1 1 
ATOM   14496 C CG2 . THR I  1 143 ? 55.442  26.456  0.318   1.00 42.63  ? 135 THR I CG2 1 
ATOM   14497 N N   . CYS I  1 144 ? 52.485  24.720  -0.562  1.00 36.74  ? 136 CYS I N   1 
ATOM   14498 C CA  . CYS I  1 144 ? 51.112  24.990  -0.162  1.00 34.97  ? 136 CYS I CA  1 
ATOM   14499 C C   . CYS I  1 144 ? 51.049  25.429  1.299   1.00 35.76  ? 136 CYS I C   1 
ATOM   14500 O O   . CYS I  1 144 ? 51.421  24.665  2.190   1.00 32.43  ? 136 CYS I O   1 
ATOM   14501 C CB  . CYS I  1 144 ? 50.303  23.714  -0.342  1.00 29.16  ? 136 CYS I CB  1 
ATOM   14502 S SG  . CYS I  1 144 ? 48.568  23.877  0.047   1.00 67.12  ? 136 CYS I SG  1 
ATOM   14503 N N   . ARG I  1 145 ? 50.587  26.654  1.544   1.00 32.14  ? 137 ARG I N   1 
ATOM   14504 C CA  . ARG I  1 145 ? 50.435  27.147  2.915   1.00 34.35  ? 137 ARG I CA  1 
ATOM   14505 C C   . ARG I  1 145 ? 48.965  27.161  3.392   1.00 35.73  ? 137 ARG I C   1 
ATOM   14506 O O   . ARG I  1 145 ? 48.138  27.929  2.894   1.00 31.71  ? 137 ARG I O   1 
ATOM   14507 C CB  . ARG I  1 145 ? 51.071  28.538  3.081   1.00 39.29  ? 137 ARG I CB  1 
ATOM   14508 C CG  . ARG I  1 145 ? 52.543  28.628  2.666   1.00 46.62  ? 137 ARG I CG  1 
ATOM   14509 C CD  . ARG I  1 145 ? 53.214  29.893  3.212   1.00 49.72  ? 137 ARG I CD  1 
ATOM   14510 N NE  . ARG I  1 145 ? 52.457  31.113  2.921   1.00 64.86  ? 137 ARG I NE  1 
ATOM   14511 C CZ  . ARG I  1 145 ? 52.707  31.935  1.899   1.00 72.22  ? 137 ARG I CZ  1 
ATOM   14512 N NH1 . ARG I  1 145 ? 53.697  31.678  1.054   1.00 67.57  ? 137 ARG I NH1 1 
ATOM   14513 N NH2 . ARG I  1 145 ? 51.964  33.019  1.711   1.00 62.49  ? 137 ARG I NH2 1 
ATOM   14514 N N   . ILE I  1 146 ? 48.657  26.308  4.367   1.00 34.34  ? 138 ILE I N   1 
ATOM   14515 C CA  . ILE I  1 146 ? 47.315  26.221  4.940   1.00 31.28  ? 138 ILE I CA  1 
ATOM   14516 C C   . ILE I  1 146 ? 47.262  26.839  6.338   1.00 26.76  ? 138 ILE I C   1 
ATOM   14517 O O   . ILE I  1 146 ? 48.005  26.433  7.223   1.00 23.75  ? 138 ILE I O   1 
ATOM   14518 C CB  . ILE I  1 146 ? 46.847  24.762  5.001   1.00 29.29  ? 138 ILE I CB  1 
ATOM   14519 C CG1 . ILE I  1 146 ? 46.761  24.179  3.586   1.00 30.13  ? 138 ILE I CG1 1 
ATOM   14520 C CG2 . ILE I  1 146 ? 45.501  24.660  5.686   1.00 28.05  ? 138 ILE I CG2 1 
ATOM   14521 C CD1 . ILE I  1 146 ? 46.291  22.744  3.557   1.00 25.39  ? 138 ILE I CD1 1 
ATOM   14522 N N   . LYS I  1 147 ? 46.377  27.814  6.529   1.00 25.33  ? 139 LYS I N   1 
ATOM   14523 C CA  . LYS I  1 147 ? 46.347  28.605  7.762   1.00 32.18  ? 139 LYS I CA  1 
ATOM   14524 C C   . LYS I  1 147 ? 45.114  28.298  8.629   1.00 28.55  ? 139 LYS I C   1 
ATOM   14525 O O   . LYS I  1 147 ? 43.996  28.577  8.216   1.00 28.55  ? 139 LYS I O   1 
ATOM   14526 C CB  . LYS I  1 147 ? 46.388  30.094  7.403   1.00 33.62  ? 139 LYS I CB  1 
ATOM   14527 C CG  . LYS I  1 147 ? 47.192  30.963  8.361   1.00 38.51  ? 139 LYS I CG  1 
ATOM   14528 C CD  . LYS I  1 147 ? 47.571  32.315  7.732   1.00 52.58  ? 139 LYS I CD  1 
ATOM   14529 C CE  . LYS I  1 147 ? 48.380  33.194  8.696   1.00 55.58  ? 139 LYS I CE  1 
ATOM   14530 N NZ  . LYS I  1 147 ? 48.930  34.418  8.039   1.00 57.16  ? 139 LYS I NZ  1 
ATOM   14531 N N   . ILE I  1 148 ? 45.324  27.737  9.824   1.00 29.39  ? 140 ILE I N   1 
ATOM   14532 C CA  . ILE I  1 148 ? 44.229  27.296  10.710  1.00 28.77  ? 140 ILE I CA  1 
ATOM   14533 C C   . ILE I  1 148 ? 44.175  27.984  12.066  1.00 29.71  ? 140 ILE I C   1 
ATOM   14534 O O   . ILE I  1 148 ? 45.134  27.918  12.818  1.00 39.90  ? 140 ILE I O   1 
ATOM   14535 C CB  . ILE I  1 148 ? 44.371  25.821  11.080  1.00 24.12  ? 140 ILE I CB  1 
ATOM   14536 C CG1 . ILE I  1 148 ? 44.407  24.947  9.838   1.00 35.45  ? 140 ILE I CG1 1 
ATOM   14537 C CG2 . ILE I  1 148 ? 43.218  25.386  11.951  1.00 23.08  ? 140 ILE I CG2 1 
ATOM   14538 C CD1 . ILE I  1 148 ? 44.456  23.473  10.182  1.00 37.25  ? 140 ILE I CD1 1 
ATOM   14539 N N   . GLY I  1 149 ? 43.040  28.583  12.412  1.00 30.53  ? 141 GLY I N   1 
ATOM   14540 C CA  . GLY I  1 149 ? 42.858  29.130  13.747  1.00 31.28  ? 141 GLY I CA  1 
ATOM   14541 C C   . GLY I  1 149 ? 41.433  29.068  14.274  1.00 27.18  ? 141 GLY I C   1 
ATOM   14542 O O   . GLY I  1 149 ? 40.527  28.593  13.591  1.00 25.31  ? 141 GLY I O   1 
ATOM   14543 N N   . SER I  1 150 ? 41.235  29.542  15.503  1.00 26.80  ? 142 SER I N   1 
ATOM   14544 C CA  . SER I  1 150 ? 39.890  29.698  16.032  1.00 22.92  ? 142 SER I CA  1 
ATOM   14545 C C   . SER I  1 150 ? 39.151  30.667  15.143  1.00 20.95  ? 142 SER I C   1 
ATOM   14546 O O   . SER I  1 150 ? 39.720  31.647  14.684  1.00 29.45  ? 142 SER I O   1 
ATOM   14547 C CB  . SER I  1 150 ? 39.909  30.249  17.460  1.00 24.56  ? 142 SER I CB  1 
ATOM   14548 O OG  . SER I  1 150 ? 38.624  30.746  17.827  1.00 23.34  ? 142 SER I OG  1 
ATOM   14549 N N   . TRP I  1 151 ? 37.878  30.404  14.906  1.00 19.02  ? 143 TRP I N   1 
ATOM   14550 C CA  . TRP I  1 151 ? 37.121  31.249  14.010  1.00 19.58  ? 143 TRP I CA  1 
ATOM   14551 C C   . TRP I  1 151 ? 36.449  32.460  14.659  1.00 23.93  ? 143 TRP I C   1 
ATOM   14552 O O   . TRP I  1 151 ? 36.298  33.489  14.004  1.00 28.38  ? 143 TRP I O   1 
ATOM   14553 C CB  . TRP I  1 151 ? 36.118  30.418  13.221  1.00 19.12  ? 143 TRP I CB  1 
ATOM   14554 C CG  . TRP I  1 151 ? 35.241  31.229  12.342  1.00 21.75  ? 143 TRP I CG  1 
ATOM   14555 C CD1 . TRP I  1 151 ? 33.890  31.397  12.461  1.00 23.67  ? 143 TRP I CD1 1 
ATOM   14556 C CD2 . TRP I  1 151 ? 35.641  31.997  11.212  1.00 24.02  ? 143 TRP I CD2 1 
ATOM   14557 N NE1 . TRP I  1 151 ? 33.425  32.221  11.469  1.00 25.71  ? 143 TRP I NE1 1 
ATOM   14558 C CE2 . TRP I  1 151 ? 34.482  32.603  10.684  1.00 27.05  ? 143 TRP I CE2 1 
ATOM   14559 C CE3 . TRP I  1 151 ? 36.868  32.230  10.585  1.00 24.99  ? 143 TRP I CE3 1 
ATOM   14560 C CZ2 . TRP I  1 151 ? 34.512  33.424  9.564   1.00 27.19  ? 143 TRP I CZ2 1 
ATOM   14561 C CZ3 . TRP I  1 151 ? 36.896  33.051  9.466   1.00 29.46  ? 143 TRP I CZ3 1 
ATOM   14562 C CH2 . TRP I  1 151 ? 35.727  33.636  8.967   1.00 26.66  ? 143 TRP I CH2 1 
ATOM   14563 N N   . THR I  1 152 ? 36.039  32.352  15.923  1.00 22.38  ? 144 THR I N   1 
ATOM   14564 C CA  . THR I  1 152 ? 35.352  33.468  16.585  1.00 21.12  ? 144 THR I CA  1 
ATOM   14565 C C   . THR I  1 152 ? 36.045  33.967  17.848  1.00 22.63  ? 144 THR I C   1 
ATOM   14566 O O   . THR I  1 152 ? 35.773  35.076  18.304  1.00 21.97  ? 144 THR I O   1 
ATOM   14567 C CB  . THR I  1 152 ? 33.911  33.111  16.957  1.00 22.99  ? 144 THR I CB  1 
ATOM   14568 O OG1 . THR I  1 152 ? 33.911  32.006  17.879  1.00 21.21  ? 144 THR I OG1 1 
ATOM   14569 C CG2 . THR I  1 152 ? 33.110  32.754  15.709  1.00 23.29  ? 144 THR I CG2 1 
ATOM   14570 N N   . HIS I  1 153 ? 36.928  33.150  18.417  1.00 20.71  ? 145 HIS I N   1 
ATOM   14571 C CA  . HIS I  1 153 ? 37.617  33.522  19.653  1.00 25.21  ? 145 HIS I CA  1 
ATOM   14572 C C   . HIS I  1 153 ? 38.989  34.158  19.438  1.00 27.11  ? 145 HIS I C   1 
ATOM   14573 O O   . HIS I  1 153 ? 39.903  33.515  18.921  1.00 26.75  ? 145 HIS I O   1 
ATOM   14574 C CB  . HIS I  1 153 ? 37.772  32.305  20.565  1.00 23.05  ? 145 HIS I CB  1 
ATOM   14575 C CG  . HIS I  1 153 ? 36.471  31.706  20.985  1.00 22.43  ? 145 HIS I CG  1 
ATOM   14576 N ND1 . HIS I  1 153 ? 36.040  30.476  20.541  1.00 20.81  ? 145 HIS I ND1 1 
ATOM   14577 C CD2 . HIS I  1 153 ? 35.492  32.184  21.788  1.00 19.69  ? 145 HIS I CD2 1 
ATOM   14578 C CE1 . HIS I  1 153 ? 34.851  30.219  21.056  1.00 22.26  ? 145 HIS I CE1 1 
ATOM   14579 N NE2 . HIS I  1 153 ? 34.499  31.237  21.821  1.00 21.57  ? 145 HIS I NE2 1 
ATOM   14580 N N   . HIS I  1 154 ? 39.115  35.391  19.914  1.00 27.17  ? 146 HIS I N   1 
ATOM   14581 C CA  . HIS I  1 154 ? 40.348  36.153  19.839  1.00 30.01  ? 146 HIS I CA  1 
ATOM   14582 C C   . HIS I  1 154 ? 41.341  35.510  20.787  1.00 29.94  ? 146 HIS I C   1 
ATOM   14583 O O   . HIS I  1 154 ? 40.964  34.707  21.641  1.00 28.09  ? 146 HIS I O   1 
ATOM   14584 C CB  . HIS I  1 154 ? 40.106  37.611  20.231  1.00 33.05  ? 146 HIS I CB  1 
ATOM   14585 C CG  . HIS I  1 154 ? 39.367  37.774  21.522  1.00 40.67  ? 146 HIS I CG  1 
ATOM   14586 N ND1 . HIS I  1 154 ? 38.322  38.660  21.675  1.00 48.26  ? 146 HIS I ND1 1 
ATOM   14587 C CD2 . HIS I  1 154 ? 39.521  37.165  22.722  1.00 39.34  ? 146 HIS I CD2 1 
ATOM   14588 C CE1 . HIS I  1 154 ? 37.864  38.590  22.912  1.00 47.63  ? 146 HIS I CE1 1 
ATOM   14589 N NE2 . HIS I  1 154 ? 38.575  37.690  23.568  1.00 43.48  ? 146 HIS I NE2 1 
ATOM   14590 N N   . SER I  1 155 ? 42.613  35.846  20.626  1.00 32.62  ? 147 SER I N   1 
ATOM   14591 C CA  . SER I  1 155 ? 43.678  35.109  21.281  1.00 36.10  ? 147 SER I CA  1 
ATOM   14592 C C   . SER I  1 155 ? 43.518  35.122  22.795  1.00 31.08  ? 147 SER I C   1 
ATOM   14593 O O   . SER I  1 155 ? 43.779  34.112  23.449  1.00 30.88  ? 147 SER I O   1 
ATOM   14594 C CB  . SER I  1 155 ? 45.042  35.684  20.893  1.00 31.11  ? 147 SER I CB  1 
ATOM   14595 O OG  . SER I  1 155 ? 45.032  37.100  20.941  1.00 35.11  ? 147 SER I OG  1 
ATOM   14596 N N   . ARG I  1 156 ? 43.097  36.246  23.366  1.00 34.76  ? 148 ARG I N   1 
ATOM   14597 C CA  . ARG I  1 156 ? 42.949  36.286  24.820  1.00 34.01  ? 148 ARG I CA  1 
ATOM   14598 C C   . ARG I  1 156 ? 42.005  35.187  25.307  1.00 36.92  ? 148 ARG I C   1 
ATOM   14599 O O   . ARG I  1 156 ? 42.057  34.784  26.464  1.00 42.82  ? 148 ARG I O   1 
ATOM   14600 C CB  . ARG I  1 156 ? 42.429  37.663  25.236  1.00 37.25  ? 148 ARG I CB  1 
ATOM   14601 C CG  . ARG I  1 156 ? 42.481  38.651  24.076  1.00 44.96  ? 148 ARG I CG  1 
ATOM   14602 C CD  . ARG I  1 156 ? 42.199  40.081  24.481  1.00 59.52  ? 148 ARG I CD  1 
ATOM   14603 N NE  . ARG I  1 156 ? 40.787  40.318  24.769  1.00 71.78  ? 148 ARG I NE  1 
ATOM   14604 C CZ  . ARG I  1 156 ? 40.190  41.504  24.665  1.00 77.79  ? 148 ARG I CZ  1 
ATOM   14605 N NH1 . ARG I  1 156 ? 40.886  42.568  24.269  1.00 79.18  ? 148 ARG I NH1 1 
ATOM   14606 N NH2 . ARG I  1 156 ? 38.893  41.625  24.952  1.00 67.49  ? 148 ARG I NH2 1 
ATOM   14607 N N   . GLU I  1 157 ? 41.148  34.700  24.414  1.00 33.61  ? 149 GLU I N   1 
ATOM   14608 C CA  . GLU I  1 157 ? 40.228  33.614  24.735  1.00 24.23  ? 149 GLU I CA  1 
ATOM   14609 C C   . GLU I  1 157 ? 40.768  32.233  24.336  1.00 23.60  ? 149 GLU I C   1 
ATOM   14610 O O   . GLU I  1 157 ? 40.739  31.313  25.145  1.00 27.73  ? 149 GLU I O   1 
ATOM   14611 C CB  . GLU I  1 157 ? 38.853  33.890  24.125  1.00 25.78  ? 149 GLU I CB  1 
ATOM   14612 C CG  . GLU I  1 157 ? 38.277  35.238  24.562  1.00 29.98  ? 149 GLU I CG  1 
ATOM   14613 C CD  . GLU I  1 157 ? 37.021  35.626  23.803  1.00 30.78  ? 149 GLU I CD  1 
ATOM   14614 O OE1 . GLU I  1 157 ? 36.584  34.841  22.940  1.00 29.84  ? 149 GLU I OE1 1 
ATOM   14615 O OE2 . GLU I  1 157 ? 36.456  36.708  24.080  1.00 30.44  ? 149 GLU I OE2 1 
ATOM   14616 N N   . ILE I  1 158 ? 41.275  32.082  23.111  1.00 23.31  ? 150 ILE I N   1 
ATOM   14617 C CA  . ILE I  1 158 ? 41.934  30.836  22.699  1.00 19.78  ? 150 ILE I CA  1 
ATOM   14618 C C   . ILE I  1 158 ? 43.325  31.102  22.115  1.00 27.26  ? 150 ILE I C   1 
ATOM   14619 O O   . ILE I  1 158 ? 43.541  32.110  21.445  1.00 27.84  ? 150 ILE I O   1 
ATOM   14620 C CB  . ILE I  1 158 ? 41.089  30.062  21.659  1.00 24.10  ? 150 ILE I CB  1 
ATOM   14621 C CG1 . ILE I  1 158 ? 39.652  29.906  22.147  1.00 27.73  ? 150 ILE I CG1 1 
ATOM   14622 C CG2 . ILE I  1 158 ? 41.665  28.685  21.378  1.00 19.48  ? 150 ILE I CG2 1 
ATOM   14623 C CD1 . ILE I  1 158 ? 38.809  29.003  21.273  1.00 26.20  ? 150 ILE I CD1 1 
ATOM   14624 N N   . SER I  1 159 ? 44.275  30.209  22.376  1.00 28.26  ? 151 SER I N   1 
ATOM   14625 C CA  . SER I  1 159 ? 45.599  30.321  21.769  1.00 31.51  ? 151 SER I CA  1 
ATOM   14626 C C   . SER I  1 159 ? 45.953  29.025  21.042  1.00 34.89  ? 151 SER I C   1 
ATOM   14627 O O   . SER I  1 159 ? 45.573  27.938  21.484  1.00 28.63  ? 151 SER I O   1 
ATOM   14628 C CB  . SER I  1 159 ? 46.663  30.664  22.815  1.00 32.96  ? 151 SER I CB  1 
ATOM   14629 O OG  . SER I  1 159 ? 47.036  29.527  23.582  1.00 32.68  ? 151 SER I OG  1 
ATOM   14630 N N   . VAL I  1 160 ? 46.670  29.142  19.924  1.00 38.01  ? 152 VAL I N   1 
ATOM   14631 C CA  . VAL I  1 160 ? 46.992  27.971  19.106  1.00 39.90  ? 152 VAL I CA  1 
ATOM   14632 C C   . VAL I  1 160 ? 48.490  27.748  18.935  1.00 43.64  ? 152 VAL I C   1 
ATOM   14633 O O   . VAL I  1 160 ? 49.170  28.519  18.263  1.00 44.99  ? 152 VAL I O   1 
ATOM   14634 C CB  . VAL I  1 160 ? 46.360  28.045  17.714  1.00 41.23  ? 152 VAL I CB  1 
ATOM   14635 C CG1 . VAL I  1 160 ? 46.053  26.651  17.241  1.00 44.77  ? 152 VAL I CG1 1 
ATOM   14636 C CG2 . VAL I  1 160 ? 45.080  28.885  17.729  1.00 44.19  ? 152 VAL I CG2 1 
ATOM   14637 N N   . ASP I  1 161 ? 48.993  26.676  19.535  1.00 40.78  ? 153 ASP I N   1 
ATOM   14638 C CA  . ASP I  1 161 ? 50.425  26.439  19.594  1.00 48.73  ? 153 ASP I CA  1 
ATOM   14639 C C   . ASP I  1 161 ? 50.791  25.032  19.142  1.00 55.33  ? 153 ASP I C   1 
ATOM   14640 O O   . ASP I  1 161 ? 50.586  24.072  19.889  1.00 57.17  ? 153 ASP I O   1 
ATOM   14641 C CB  . ASP I  1 161 ? 50.925  26.657  21.021  1.00 59.31  ? 153 ASP I CB  1 
ATOM   14642 C CG  . ASP I  1 161 ? 50.349  27.915  21.656  1.00 61.16  ? 153 ASP I CG  1 
ATOM   14643 O OD1 . ASP I  1 161 ? 50.239  28.951  20.953  1.00 55.26  ? 153 ASP I OD1 1 
ATOM   14644 O OD2 . ASP I  1 161 ? 50.001  27.861  22.861  1.00 62.90  ? 153 ASP I OD2 1 
ATOM   14645 N N   . PRO I  1 162 ? 51.348  24.914  17.921  1.00 52.29  ? 154 PRO I N   1 
ATOM   14646 C CA  . PRO I  1 162 ? 51.832  23.675  17.301  1.00 47.21  ? 154 PRO I CA  1 
ATOM   14647 C C   . PRO I  1 162 ? 52.586  22.777  18.281  1.00 52.51  ? 154 PRO I C   1 
ATOM   14648 O O   . PRO I  1 162 ? 53.311  23.266  19.149  1.00 51.83  ? 154 PRO I O   1 
ATOM   14649 C CB  . PRO I  1 162 ? 52.788  24.186  16.228  1.00 50.27  ? 154 PRO I CB  1 
ATOM   14650 C CG  . PRO I  1 162 ? 52.225  25.490  15.831  1.00 47.60  ? 154 PRO I CG  1 
ATOM   14651 C CD  . PRO I  1 162 ? 51.601  26.086  17.065  1.00 46.08  ? 154 PRO I CD  1 
ATOM   14652 N N   . THR I  1 163 ? 52.411  21.469  18.133  1.00 59.12  ? 155 THR I N   1 
ATOM   14653 C CA  . THR I  1 163 ? 52.937  20.508  19.097  1.00 63.10  ? 155 THR I CA  1 
ATOM   14654 C C   . THR I  1 163 ? 54.464  20.416  19.060  1.00 67.45  ? 155 THR I C   1 
ATOM   14655 O O   . THR I  1 163 ? 55.146  20.772  20.026  1.00 68.45  ? 155 THR I O   1 
ATOM   14656 C CB  . THR I  1 163 ? 52.326  19.110  18.871  1.00 60.02  ? 155 THR I CB  1 
ATOM   14657 O OG1 . THR I  1 163 ? 52.972  18.468  17.764  1.00 57.81  ? 155 THR I OG1 1 
ATOM   14658 C CG2 . THR I  1 163 ? 50.826  19.228  18.590  1.00 48.25  ? 155 THR I CG2 1 
ATOM   14659 N N   . SER I  1 167 ? 56.794  17.893  14.772  1.00 47.82  ? 159 SER I N   1 
ATOM   14660 C CA  . SER I  1 167 ? 56.459  16.503  14.483  1.00 41.77  ? 159 SER I CA  1 
ATOM   14661 C C   . SER I  1 167 ? 56.602  16.187  12.998  1.00 43.16  ? 159 SER I C   1 
ATOM   14662 O O   . SER I  1 167 ? 56.789  17.083  12.169  1.00 43.04  ? 159 SER I O   1 
ATOM   14663 C CB  . SER I  1 167 ? 55.033  16.198  14.928  1.00 40.53  ? 159 SER I CB  1 
ATOM   14664 O OG  . SER I  1 167 ? 54.788  16.739  16.209  1.00 57.35  ? 159 SER I OG  1 
ATOM   14665 N N   . ASP I  1 168 ? 56.500  14.905  12.664  1.00 41.33  ? 160 ASP I N   1 
ATOM   14666 C CA  . ASP I  1 168 ? 56.607  14.465  11.275  1.00 40.96  ? 160 ASP I CA  1 
ATOM   14667 C C   . ASP I  1 168 ? 55.207  14.277  10.684  1.00 46.83  ? 160 ASP I C   1 
ATOM   14668 O O   . ASP I  1 168 ? 54.597  13.216  10.826  1.00 47.01  ? 160 ASP I O   1 
ATOM   14669 C CB  . ASP I  1 168 ? 57.418  13.165  11.187  1.00 37.13  ? 160 ASP I CB  1 
ATOM   14670 C CG  . ASP I  1 168 ? 57.805  12.809  9.763   1.00 38.83  ? 160 ASP I CG  1 
ATOM   14671 O OD1 . ASP I  1 168 ? 57.472  13.594  8.843   1.00 37.20  ? 160 ASP I OD1 1 
ATOM   14672 O OD2 . ASP I  1 168 ? 58.452  11.749  9.569   1.00 31.83  ? 160 ASP I OD2 1 
ATOM   14673 N N   . ASP I  1 169 ? 54.712  15.316  10.017  1.00 46.71  ? 161 ASP I N   1 
ATOM   14674 C CA  . ASP I  1 169 ? 53.351  15.351  9.486   1.00 35.98  ? 161 ASP I CA  1 
ATOM   14675 C C   . ASP I  1 169 ? 53.191  14.518  8.219   1.00 34.18  ? 161 ASP I C   1 
ATOM   14676 O O   . ASP I  1 169 ? 52.075  14.175  7.814   1.00 33.67  ? 161 ASP I O   1 
ATOM   14677 C CB  . ASP I  1 169 ? 52.985  16.798  9.214   1.00 31.00  ? 161 ASP I CB  1 
ATOM   14678 C CG  . ASP I  1 169 ? 53.543  17.723  10.270  1.00 44.49  ? 161 ASP I CG  1 
ATOM   14679 O OD1 . ASP I  1 169 ? 54.682  18.217  10.069  1.00 47.37  ? 161 ASP I OD1 1 
ATOM   14680 O OD2 . ASP I  1 169 ? 52.869  17.923  11.311  1.00 38.48  ? 161 ASP I OD2 1 
ATOM   14681 N N   . SER I  1 170 ? 54.324  14.177  7.618   1.00 36.25  ? 162 SER I N   1 
ATOM   14682 C CA  . SER I  1 170 ? 54.364  13.422  6.381   1.00 32.48  ? 162 SER I CA  1 
ATOM   14683 C C   . SER I  1 170 ? 54.574  11.944  6.661   1.00 32.37  ? 162 SER I C   1 
ATOM   14684 O O   . SER I  1 170 ? 54.761  11.156  5.741   1.00 37.08  ? 162 SER I O   1 
ATOM   14685 C CB  . SER I  1 170 ? 55.504  13.947  5.516   1.00 42.33  ? 162 SER I CB  1 
ATOM   14686 O OG  . SER I  1 170 ? 56.610  14.308  6.330   1.00 44.97  ? 162 SER I OG  1 
ATOM   14687 N N   . GLU I  1 171 ? 54.511  11.562  7.931   1.00 31.82  ? 163 GLU I N   1 
ATOM   14688 C CA  . GLU I  1 171 ? 54.910  10.211  8.329   1.00 36.03  ? 163 GLU I CA  1 
ATOM   14689 C C   . GLU I  1 171 ? 53.860  9.129   8.063   1.00 34.93  ? 163 GLU I C   1 
ATOM   14690 O O   . GLU I  1 171 ? 54.188  7.945   8.068   1.00 37.78  ? 163 GLU I O   1 
ATOM   14691 C CB  . GLU I  1 171 ? 55.419  10.179  9.794   1.00 33.55  ? 163 GLU I CB  1 
ATOM   14692 C CG  . GLU I  1 171 ? 54.496  9.522   10.824  1.00 38.55  ? 163 GLU I CG  1 
ATOM   14693 C CD  . GLU I  1 171 ? 54.700  10.052  12.261  1.00 46.61  ? 163 GLU I CD  1 
ATOM   14694 O OE1 . GLU I  1 171 ? 53.694  10.419  12.913  1.00 43.76  ? 163 GLU I OE1 1 
ATOM   14695 O OE2 . GLU I  1 171 ? 55.855  10.102  12.746  1.00 48.60  ? 163 GLU I OE2 1 
ATOM   14696 N N   . TYR I  1 172 ? 52.607  9.519   7.834   1.00 32.96  ? 164 TYR I N   1 
ATOM   14697 C CA  . TYR I  1 172 ? 51.560  8.531   7.566   1.00 26.20  ? 164 TYR I CA  1 
ATOM   14698 C C   . TYR I  1 172 ? 51.028  8.680   6.154   1.00 32.17  ? 164 TYR I C   1 
ATOM   14699 O O   . TYR I  1 172 ? 49.917  8.245   5.840   1.00 28.84  ? 164 TYR I O   1 
ATOM   14700 C CB  . TYR I  1 172 ? 50.413  8.665   8.557   1.00 32.29  ? 164 TYR I CB  1 
ATOM   14701 C CG  . TYR I  1 172 ? 50.802  8.362   9.975   1.00 35.27  ? 164 TYR I CG  1 
ATOM   14702 C CD1 . TYR I  1 172 ? 51.230  7.095   10.336  1.00 33.02  ? 164 TYR I CD1 1 
ATOM   14703 C CD2 . TYR I  1 172 ? 50.733  9.343   10.958  1.00 29.60  ? 164 TYR I CD2 1 
ATOM   14704 C CE1 . TYR I  1 172 ? 51.585  6.808   11.630  1.00 38.58  ? 164 TYR I CE1 1 
ATOM   14705 C CE2 . TYR I  1 172 ? 51.080  9.069   12.255  1.00 32.80  ? 164 TYR I CE2 1 
ATOM   14706 C CZ  . TYR I  1 172 ? 51.509  7.800   12.590  1.00 45.40  ? 164 TYR I CZ  1 
ATOM   14707 O OH  . TYR I  1 172 ? 51.862  7.518   13.888  1.00 55.19  ? 164 TYR I OH  1 
ATOM   14708 N N   . PHE I  1 173 ? 51.831  9.303   5.301   1.00 29.25  ? 165 PHE I N   1 
ATOM   14709 C CA  . PHE I  1 173 ? 51.421  9.571   3.944   1.00 25.94  ? 165 PHE I CA  1 
ATOM   14710 C C   . PHE I  1 173 ? 51.398  8.282   3.114   1.00 34.41  ? 165 PHE I C   1 
ATOM   14711 O O   . PHE I  1 173 ? 52.229  7.388   3.298   1.00 32.28  ? 165 PHE I O   1 
ATOM   14712 C CB  . PHE I  1 173 ? 52.336  10.612  3.334   1.00 28.19  ? 165 PHE I CB  1 
ATOM   14713 C CG  . PHE I  1 173 ? 51.740  11.331  2.170   1.00 29.82  ? 165 PHE I CG  1 
ATOM   14714 C CD1 . PHE I  1 173 ? 50.853  12.373  2.366   1.00 29.47  ? 165 PHE I CD1 1 
ATOM   14715 C CD2 . PHE I  1 173 ? 52.077  10.978  0.883   1.00 26.04  ? 165 PHE I CD2 1 
ATOM   14716 C CE1 . PHE I  1 173 ? 50.318  13.052  1.290   1.00 32.14  ? 165 PHE I CE1 1 
ATOM   14717 C CE2 . PHE I  1 173 ? 51.537  11.642  -0.194  1.00 29.94  ? 165 PHE I CE2 1 
ATOM   14718 C CZ  . PHE I  1 173 ? 50.660  12.680  0.006   1.00 32.24  ? 165 PHE I CZ  1 
ATOM   14719 N N   . SER I  1 174 ? 50.414  8.183   2.225   1.00 34.13  ? 166 SER I N   1 
ATOM   14720 C CA  . SER I  1 174 ? 50.206  6.988   1.428   1.00 28.72  ? 166 SER I CA  1 
ATOM   14721 C C   . SER I  1 174 ? 51.335  6.856   0.423   1.00 34.59  ? 166 SER I C   1 
ATOM   14722 O O   . SER I  1 174 ? 51.587  7.770   -0.371  1.00 37.90  ? 166 SER I O   1 
ATOM   14723 C CB  . SER I  1 174 ? 48.861  7.074   0.695   1.00 32.48  ? 166 SER I CB  1 
ATOM   14724 O OG  . SER I  1 174 ? 48.523  5.858   0.048   1.00 30.95  ? 166 SER I OG  1 
ATOM   14725 N N   . GLN I  1 175 ? 52.012  5.714   0.453   1.00 36.80  ? 167 GLN I N   1 
ATOM   14726 C CA  . GLN I  1 175 ? 53.047  5.424   -0.525  1.00 29.54  ? 167 GLN I CA  1 
ATOM   14727 C C   . GLN I  1 175 ? 52.430  5.335   -1.910  1.00 37.73  ? 167 GLN I C   1 
ATOM   14728 O O   . GLN I  1 175 ? 53.123  5.514   -2.917  1.00 44.10  ? 167 GLN I O   1 
ATOM   14729 C CB  . GLN I  1 175 ? 53.761  4.118   -0.183  1.00 29.95  ? 167 GLN I CB  1 
ATOM   14730 C CG  . GLN I  1 175 ? 53.037  2.882   -0.628  1.00 30.91  ? 167 GLN I CG  1 
ATOM   14731 C CD  . GLN I  1 175 ? 53.173  1.729   0.353   1.00 47.52  ? 167 GLN I CD  1 
ATOM   14732 O OE1 . GLN I  1 175 ? 52.889  1.873   1.548   1.00 45.61  ? 167 GLN I OE1 1 
ATOM   14733 N NE2 . GLN I  1 175 ? 53.607  0.575   -0.149  1.00 51.71  ? 167 GLN I NE2 1 
ATOM   14734 N N   . TYR I  1 176 ? 51.121  5.092   -1.961  1.00 33.82  ? 168 TYR I N   1 
ATOM   14735 C CA  . TYR I  1 176 ? 50.435  4.889   -3.230  1.00 36.83  ? 168 TYR I CA  1 
ATOM   14736 C C   . TYR I  1 176 ? 50.034  6.180   -3.931  1.00 33.96  ? 168 TYR I C   1 
ATOM   14737 O O   . TYR I  1 176 ? 49.674  6.168   -5.110  1.00 35.16  ? 168 TYR I O   1 
ATOM   14738 C CB  . TYR I  1 176 ? 49.238  3.976   -3.025  1.00 36.32  ? 168 TYR I CB  1 
ATOM   14739 C CG  . TYR I  1 176 ? 49.653  2.648   -2.458  1.00 34.41  ? 168 TYR I CG  1 
ATOM   14740 C CD1 . TYR I  1 176 ? 50.781  1.994   -2.929  1.00 36.23  ? 168 TYR I CD1 1 
ATOM   14741 C CD2 . TYR I  1 176 ? 48.934  2.056   -1.445  1.00 34.53  ? 168 TYR I CD2 1 
ATOM   14742 C CE1 . TYR I  1 176 ? 51.174  0.772   -2.407  1.00 35.05  ? 168 TYR I CE1 1 
ATOM   14743 C CE2 . TYR I  1 176 ? 49.319  0.838   -0.914  1.00 44.51  ? 168 TYR I CE2 1 
ATOM   14744 C CZ  . TYR I  1 176 ? 50.441  0.202   -1.396  1.00 38.31  ? 168 TYR I CZ  1 
ATOM   14745 O OH  . TYR I  1 176 ? 50.811  -1.011  -0.858  1.00 44.84  ? 168 TYR I OH  1 
ATOM   14746 N N   . SER I  1 177 ? 50.118  7.294   -3.215  1.00 26.76  ? 169 SER I N   1 
ATOM   14747 C CA  . SER I  1 177 ? 49.778  8.581   -3.804  1.00 31.89  ? 169 SER I CA  1 
ATOM   14748 C C   . SER I  1 177 ? 50.483  8.850   -5.134  1.00 34.86  ? 169 SER I C   1 
ATOM   14749 O O   . SER I  1 177 ? 51.591  8.383   -5.377  1.00 39.64  ? 169 SER I O   1 
ATOM   14750 C CB  . SER I  1 177 ? 50.073  9.724   -2.836  1.00 29.54  ? 169 SER I CB  1 
ATOM   14751 O OG  . SER I  1 177 ? 49.743  10.966  -3.441  1.00 28.33  ? 169 SER I OG  1 
ATOM   14752 N N   . ARG I  1 178 ? 49.814  9.620   -5.982  1.00 40.09  ? 170 ARG I N   1 
ATOM   14753 C CA  . ARG I  1 178 ? 50.360  10.114  -7.243  1.00 34.41  ? 170 ARG I CA  1 
ATOM   14754 C C   . ARG I  1 178 ? 51.326  11.248  -6.911  1.00 36.33  ? 170 ARG I C   1 
ATOM   14755 O O   . ARG I  1 178 ? 51.828  11.940  -7.795  1.00 43.94  ? 170 ARG I O   1 
ATOM   14756 C CB  . ARG I  1 178 ? 49.189  10.601  -8.116  1.00 37.83  ? 170 ARG I CB  1 
ATOM   14757 C CG  . ARG I  1 178 ? 49.481  11.231  -9.472  1.00 38.48  ? 170 ARG I CG  1 
ATOM   14758 C CD  . ARG I  1 178 ? 48.245  11.111  -10.387 1.00 45.61  ? 170 ARG I CD  1 
ATOM   14759 N NE  . ARG I  1 178 ? 47.784  12.368  -10.992 1.00 52.81  ? 170 ARG I NE  1 
ATOM   14760 C CZ  . ARG I  1 178 ? 46.837  13.161  -10.477 1.00 60.52  ? 170 ARG I CZ  1 
ATOM   14761 N NH1 . ARG I  1 178 ? 46.252  12.849  -9.321  1.00 56.70  ? 170 ARG I NH1 1 
ATOM   14762 N NH2 . ARG I  1 178 ? 46.476  14.276  -11.114 1.00 43.76  ? 170 ARG I NH2 1 
ATOM   14763 N N   . PHE I  1 179 ? 51.588  11.437  -5.621  1.00 35.08  ? 171 PHE I N   1 
ATOM   14764 C CA  . PHE I  1 179 ? 52.476  12.503  -5.163  1.00 35.60  ? 171 PHE I CA  1 
ATOM   14765 C C   . PHE I  1 179 ? 53.404  12.028  -4.043  1.00 35.90  ? 171 PHE I C   1 
ATOM   14766 O O   . PHE I  1 179 ? 53.338  10.875  -3.586  1.00 35.69  ? 171 PHE I O   1 
ATOM   14767 C CB  . PHE I  1 179 ? 51.674  13.718  -4.676  1.00 29.83  ? 171 PHE I CB  1 
ATOM   14768 C CG  . PHE I  1 179 ? 50.765  14.318  -5.715  1.00 33.19  ? 171 PHE I CG  1 
ATOM   14769 C CD1 . PHE I  1 179 ? 49.518  13.759  -5.981  1.00 32.22  ? 171 PHE I CD1 1 
ATOM   14770 C CD2 . PHE I  1 179 ? 51.141  15.461  -6.405  1.00 34.00  ? 171 PHE I CD2 1 
ATOM   14771 C CE1 . PHE I  1 179 ? 48.677  14.311  -6.934  1.00 32.41  ? 171 PHE I CE1 1 
ATOM   14772 C CE2 . PHE I  1 179 ? 50.299  16.023  -7.359  1.00 35.92  ? 171 PHE I CE2 1 
ATOM   14773 C CZ  . PHE I  1 179 ? 49.061  15.445  -7.620  1.00 31.34  ? 171 PHE I CZ  1 
ATOM   14774 N N   . GLU I  1 180 ? 54.275  12.931  -3.611  1.00 34.28  ? 172 GLU I N   1 
ATOM   14775 C CA  . GLU I  1 180 ? 55.158  12.677  -2.485  1.00 35.04  ? 172 GLU I CA  1 
ATOM   14776 C C   . GLU I  1 180 ? 55.491  13.997  -1.826  1.00 33.00  ? 172 GLU I C   1 
ATOM   14777 O O   . GLU I  1 180 ? 55.566  15.039  -2.484  1.00 34.95  ? 172 GLU I O   1 
ATOM   14778 C CB  . GLU I  1 180 ? 56.442  11.978  -2.935  1.00 50.44  ? 172 GLU I CB  1 
ATOM   14779 C CG  . GLU I  1 180 ? 56.540  10.502  -2.527  1.00 65.20  ? 172 GLU I CG  1 
ATOM   14780 C CD  . GLU I  1 180 ? 57.857  9.850   -2.961  1.00 75.28  ? 172 GLU I CD  1 
ATOM   14781 O OE1 . GLU I  1 180 ? 58.664  10.521  -3.653  1.00 66.21  ? 172 GLU I OE1 1 
ATOM   14782 O OE2 . GLU I  1 180 ? 58.079  8.665   -2.605  1.00 77.16  ? 172 GLU I OE2 1 
ATOM   14783 N N   . ILE I  1 181 ? 55.697  13.943  -0.520  1.00 31.38  ? 173 ILE I N   1 
ATOM   14784 C CA  . ILE I  1 181 ? 55.979  15.131  0.267   1.00 32.14  ? 173 ILE I CA  1 
ATOM   14785 C C   . ILE I  1 181 ? 57.486  15.304  0.457   1.00 35.71  ? 173 ILE I C   1 
ATOM   14786 O O   . ILE I  1 181 ? 58.184  14.390  0.910   1.00 35.43  ? 173 ILE I O   1 
ATOM   14787 C CB  . ILE I  1 181 ? 55.269  15.049  1.640   1.00 34.41  ? 173 ILE I CB  1 
ATOM   14788 C CG1 . ILE I  1 181 ? 53.758  15.216  1.463   1.00 30.69  ? 173 ILE I CG1 1 
ATOM   14789 C CG2 . ILE I  1 181 ? 55.819  16.091  2.600   1.00 39.38  ? 173 ILE I CG2 1 
ATOM   14790 C CD1 . ILE I  1 181 ? 52.977  15.046  2.735   1.00 36.86  ? 173 ILE I CD1 1 
ATOM   14791 N N   . LEU I  1 182 ? 58.000  16.425  -0.048  1.00 34.60  ? 174 LEU I N   1 
ATOM   14792 C CA  . LEU I  1 182 ? 59.391  16.832  0.151   1.00 36.07  ? 174 LEU I CA  1 
ATOM   14793 C C   . LEU I  1 182 ? 59.708  17.205  1.599   1.00 38.92  ? 174 LEU I C   1 
ATOM   14794 O O   . LEU I  1 182 ? 60.757  16.849  2.136   1.00 41.54  ? 174 LEU I O   1 
ATOM   14795 C CB  . LEU I  1 182 ? 59.744  17.997  -0.777  1.00 37.23  ? 174 LEU I CB  1 
ATOM   14796 C CG  . LEU I  1 182 ? 59.343  17.840  -2.245  1.00 37.42  ? 174 LEU I CG  1 
ATOM   14797 C CD1 . LEU I  1 182 ? 59.411  19.176  -2.968  1.00 43.26  ? 174 LEU I CD1 1 
ATOM   14798 C CD2 . LEU I  1 182 ? 60.222  16.808  -2.935  1.00 32.87  ? 174 LEU I CD2 1 
ATOM   14799 N N   . ASP I  1 183 ? 58.780  17.932  2.214   1.00 37.50  ? 175 ASP I N   1 
ATOM   14800 C CA  . ASP I  1 183 ? 58.918  18.419  3.584   1.00 39.03  ? 175 ASP I CA  1 
ATOM   14801 C C   . ASP I  1 183 ? 57.606  18.990  4.119   1.00 41.63  ? 175 ASP I C   1 
ATOM   14802 O O   . ASP I  1 183 ? 56.682  19.262  3.353   1.00 41.57  ? 175 ASP I O   1 
ATOM   14803 C CB  . ASP I  1 183 ? 60.023  19.474  3.668   1.00 39.04  ? 175 ASP I CB  1 
ATOM   14804 C CG  . ASP I  1 183 ? 60.659  19.543  5.042   1.00 47.70  ? 175 ASP I CG  1 
ATOM   14805 O OD1 . ASP I  1 183 ? 60.642  18.521  5.759   1.00 39.13  ? 175 ASP I OD1 1 
ATOM   14806 O OD2 . ASP I  1 183 ? 61.177  20.620  5.405   1.00 57.39  ? 175 ASP I OD2 1 
ATOM   14807 N N   . VAL I  1 184 ? 57.536  19.184  5.432   1.00 39.32  ? 176 VAL I N   1 
ATOM   14808 C CA  . VAL I  1 184 ? 56.422  19.905  6.044   1.00 35.83  ? 176 VAL I CA  1 
ATOM   14809 C C   . VAL I  1 184 ? 56.892  20.691  7.286   1.00 41.52  ? 176 VAL I C   1 
ATOM   14810 O O   . VAL I  1 184 ? 57.641  20.165  8.111   1.00 40.79  ? 176 VAL I O   1 
ATOM   14811 C CB  . VAL I  1 184 ? 55.292  18.944  6.480   1.00 40.77  ? 176 VAL I CB  1 
ATOM   14812 C CG1 . VAL I  1 184 ? 53.935  19.596  6.280   1.00 31.95  ? 176 VAL I CG1 1 
ATOM   14813 C CG2 . VAL I  1 184 ? 55.367  17.629  5.729   1.00 36.58  ? 176 VAL I CG2 1 
ATOM   14814 N N   . THR I  1 185 ? 56.447  21.942  7.417   1.00 35.22  ? 177 THR I N   1 
ATOM   14815 C CA  . THR I  1 185 ? 56.832  22.796  8.539   1.00 36.52  ? 177 THR I CA  1 
ATOM   14816 C C   . THR I  1 185 ? 55.593  23.418  9.182   1.00 40.91  ? 177 THR I C   1 
ATOM   14817 O O   . THR I  1 185 ? 54.612  23.680  8.488   1.00 41.86  ? 177 THR I O   1 
ATOM   14818 C CB  . THR I  1 185 ? 57.749  23.954  8.080   1.00 38.93  ? 177 THR I CB  1 
ATOM   14819 O OG1 . THR I  1 185 ? 56.948  25.056  7.634   1.00 43.82  ? 177 THR I OG1 1 
ATOM   14820 C CG2 . THR I  1 185 ? 58.668  23.514  6.949   1.00 41.16  ? 177 THR I CG2 1 
ATOM   14821 N N   . GLN I  1 186 ? 55.628  23.662  10.495  1.00 40.36  ? 178 GLN I N   1 
ATOM   14822 C CA  . GLN I  1 186 ? 54.495  24.316  11.176  1.00 35.75  ? 178 GLN I CA  1 
ATOM   14823 C C   . GLN I  1 186 ? 54.913  25.489  12.070  1.00 33.66  ? 178 GLN I C   1 
ATOM   14824 O O   . GLN I  1 186 ? 55.696  25.346  13.011  1.00 33.91  ? 178 GLN I O   1 
ATOM   14825 C CB  . GLN I  1 186 ? 53.636  23.308  11.950  1.00 35.85  ? 178 GLN I CB  1 
ATOM   14826 C CG  . GLN I  1 186 ? 52.926  22.301  11.052  1.00 38.69  ? 178 GLN I CG  1 
ATOM   14827 C CD  . GLN I  1 186 ? 52.076  21.294  11.817  1.00 41.94  ? 178 GLN I CD  1 
ATOM   14828 O OE1 . GLN I  1 186 ? 51.866  21.430  13.029  1.00 41.31  ? 178 GLN I OE1 1 
ATOM   14829 N NE2 . GLN I  1 186 ? 51.585  20.273  11.108  1.00 31.09  ? 178 GLN I NE2 1 
ATOM   14830 N N   . LYS I  1 187 ? 54.370  26.654  11.764  1.00 29.63  ? 179 LYS I N   1 
ATOM   14831 C CA  . LYS I  1 187 ? 54.787  27.879  12.411  1.00 32.94  ? 179 LYS I CA  1 
ATOM   14832 C C   . LYS I  1 187 ? 53.561  28.584  12.998  1.00 36.28  ? 179 LYS I C   1 
ATOM   14833 O O   . LYS I  1 187 ? 52.477  28.532  12.428  1.00 34.58  ? 179 LYS I O   1 
ATOM   14834 C CB  . LYS I  1 187 ? 55.546  28.745  11.393  1.00 32.96  ? 179 LYS I CB  1 
ATOM   14835 C CG  . LYS I  1 187 ? 55.339  30.248  11.476  1.00 41.04  ? 179 LYS I CG  1 
ATOM   14836 C CD  . LYS I  1 187 ? 56.111  30.939  10.359  1.00 48.45  ? 179 LYS I CD  1 
ATOM   14837 C CE  . LYS I  1 187 ? 55.879  32.448  10.322  1.00 55.14  ? 179 LYS I CE  1 
ATOM   14838 N NZ  . LYS I  1 187 ? 56.576  33.093  9.157   1.00 60.51  ? 179 LYS I NZ  1 
ATOM   14839 N N   . LYS I  1 188 ? 53.730  29.203  14.161  1.00 40.67  ? 180 LYS I N   1 
ATOM   14840 C CA  . LYS I  1 188 ? 52.659  29.965  14.792  1.00 39.35  ? 180 LYS I CA  1 
ATOM   14841 C C   . LYS I  1 188 ? 52.626  31.400  14.269  1.00 42.09  ? 180 LYS I C   1 
ATOM   14842 O O   . LYS I  1 188 ? 53.637  32.101  14.250  1.00 41.34  ? 180 LYS I O   1 
ATOM   14843 C CB  . LYS I  1 188 ? 52.819  29.948  16.317  1.00 43.57  ? 180 LYS I CB  1 
ATOM   14844 C CG  . LYS I  1 188 ? 51.996  30.992  17.068  1.00 51.53  ? 180 LYS I CG  1 
ATOM   14845 C CD  . LYS I  1 188 ? 52.147  30.825  18.582  1.00 51.71  ? 180 LYS I CD  1 
ATOM   14846 C CE  . LYS I  1 188 ? 51.448  31.951  19.332  1.00 56.65  ? 180 LYS I CE  1 
ATOM   14847 N NZ  . LYS I  1 188 ? 51.195  31.638  20.775  1.00 59.12  ? 180 LYS I NZ  1 
ATOM   14848 N N   . ASN I  1 189 ? 51.458  31.829  13.820  1.00 43.89  ? 181 ASN I N   1 
ATOM   14849 C CA  . ASN I  1 189 ? 51.273  33.214  13.431  1.00 42.69  ? 181 ASN I CA  1 
ATOM   14850 C C   . ASN I  1 189 ? 50.074  33.787  14.136  1.00 41.40  ? 181 ASN I C   1 
ATOM   14851 O O   . ASN I  1 189 ? 49.450  33.129  14.969  1.00 46.85  ? 181 ASN I O   1 
ATOM   14852 C CB  . ASN I  1 189 ? 51.093  33.351  11.918  1.00 49.94  ? 181 ASN I CB  1 
ATOM   14853 C CG  . ASN I  1 189 ? 52.394  33.631  11.207  1.00 56.94  ? 181 ASN I CG  1 
ATOM   14854 O OD1 . ASN I  1 189 ? 52.711  33.001  10.196  1.00 60.25  ? 181 ASN I OD1 1 
ATOM   14855 N ND2 . ASN I  1 189 ? 53.168  34.576  11.739  1.00 53.10  ? 181 ASN I ND2 1 
ATOM   14856 N N   . SER I  1 190 ? 49.758  35.026  13.806  1.00 39.01  ? 182 SER I N   1 
ATOM   14857 C CA  . SER I  1 190 ? 48.567  35.657  14.327  1.00 45.95  ? 182 SER I CA  1 
ATOM   14858 C C   . SER I  1 190 ? 47.989  36.434  13.165  1.00 49.94  ? 182 SER I C   1 
ATOM   14859 O O   . SER I  1 190 ? 48.443  36.272  12.035  1.00 57.77  ? 182 SER I O   1 
ATOM   14860 C CB  . SER I  1 190 ? 48.913  36.591  15.483  1.00 38.40  ? 182 SER I CB  1 
ATOM   14861 O OG  . SER I  1 190 ? 49.579  37.742  14.994  1.00 44.92  ? 182 SER I OG  1 
ATOM   14862 N N   . VAL I  1 191 ? 46.985  37.261  13.435  1.00 53.84  ? 183 VAL I N   1 
ATOM   14863 C CA  . VAL I  1 191 ? 46.435  38.166  12.430  1.00 51.36  ? 183 VAL I CA  1 
ATOM   14864 C C   . VAL I  1 191 ? 45.566  39.227  13.096  1.00 52.50  ? 183 VAL I C   1 
ATOM   14865 O O   . VAL I  1 191 ? 44.756  38.910  13.964  1.00 48.27  ? 183 VAL I O   1 
ATOM   14866 C CB  . VAL I  1 191 ? 45.621  37.416  11.348  1.00 46.64  ? 183 VAL I CB  1 
ATOM   14867 C CG1 . VAL I  1 191 ? 44.693  36.387  11.980  1.00 45.72  ? 183 VAL I CG1 1 
ATOM   14868 C CG2 . VAL I  1 191 ? 44.846  38.397  10.495  1.00 49.91  ? 183 VAL I CG2 1 
ATOM   14869 N N   . THR I  1 192 ? 45.762  40.486  12.706  1.00 56.77  ? 184 THR I N   1 
ATOM   14870 C CA  . THR I  1 192 ? 44.877  41.567  13.126  1.00 59.63  ? 184 THR I CA  1 
ATOM   14871 C C   . THR I  1 192 ? 44.043  42.023  11.931  1.00 64.29  ? 184 THR I C   1 
ATOM   14872 O O   . THR I  1 192 ? 44.561  42.144  10.818  1.00 56.41  ? 184 THR I O   1 
ATOM   14873 C CB  . THR I  1 192 ? 45.656  42.760  13.705  1.00 54.79  ? 184 THR I CB  1 
ATOM   14874 O OG1 . THR I  1 192 ? 46.744  42.279  14.500  1.00 59.23  ? 184 THR I OG1 1 
ATOM   14875 C CG2 . THR I  1 192 ? 44.749  43.616  14.575  1.00 58.21  ? 184 THR I CG2 1 
ATOM   14876 N N   . TYR I  1 193 ? 42.752  42.255  12.164  1.00 62.22  ? 185 TYR I N   1 
ATOM   14877 C CA  . TYR I  1 193 ? 41.833  42.666  11.107  1.00 62.94  ? 185 TYR I CA  1 
ATOM   14878 C C   . TYR I  1 193 ? 41.525  44.149  11.230  1.00 65.86  ? 185 TYR I C   1 
ATOM   14879 O O   . TYR I  1 193 ? 42.108  44.837  12.065  1.00 63.33  ? 185 TYR I O   1 
ATOM   14880 C CB  . TYR I  1 193 ? 40.539  41.845  11.156  1.00 64.91  ? 185 TYR I CB  1 
ATOM   14881 C CG  . TYR I  1 193 ? 39.702  42.054  12.409  1.00 75.69  ? 185 TYR I CG  1 
ATOM   14882 C CD1 . TYR I  1 193 ? 38.547  42.832  12.378  1.00 79.64  ? 185 TYR I CD1 1 
ATOM   14883 C CD2 . TYR I  1 193 ? 40.066  41.471  13.624  1.00 68.74  ? 185 TYR I CD2 1 
ATOM   14884 C CE1 . TYR I  1 193 ? 37.778  43.026  13.528  1.00 83.19  ? 185 TYR I CE1 1 
ATOM   14885 C CE2 . TYR I  1 193 ? 39.305  41.661  14.774  1.00 67.85  ? 185 TYR I CE2 1 
ATOM   14886 C CZ  . TYR I  1 193 ? 38.162  42.436  14.720  1.00 73.15  ? 185 TYR I CZ  1 
ATOM   14887 O OH  . TYR I  1 193 ? 37.406  42.621  15.856  1.00 67.58  ? 185 TYR I OH  1 
ATOM   14888 N N   . PRO I  1 197 ? 41.077  45.445  15.331  1.00 72.05  ? 189 PRO I N   1 
ATOM   14889 C CA  . PRO I  1 197 ? 40.937  45.799  16.749  1.00 72.47  ? 189 PRO I CA  1 
ATOM   14890 C C   . PRO I  1 197 ? 41.479  44.746  17.729  1.00 62.70  ? 189 PRO I C   1 
ATOM   14891 O O   . PRO I  1 197 ? 41.864  45.118  18.833  1.00 51.24  ? 189 PRO I O   1 
ATOM   14892 C CB  . PRO I  1 197 ? 39.429  45.962  16.901  1.00 65.68  ? 189 PRO I CB  1 
ATOM   14893 C CG  . PRO I  1 197 ? 39.017  46.537  15.572  1.00 65.10  ? 189 PRO I CG  1 
ATOM   14894 C CD  . PRO I  1 197 ? 39.917  45.899  14.539  1.00 66.67  ? 189 PRO I CD  1 
ATOM   14895 N N   . GLU I  1 198 ? 41.514  43.476  17.318  1.00 68.45  ? 190 GLU I N   1 
ATOM   14896 C CA  . GLU I  1 198 ? 42.003  42.367  18.151  1.00 57.34  ? 190 GLU I CA  1 
ATOM   14897 C C   . GLU I  1 198 ? 42.489  41.181  17.290  1.00 50.38  ? 190 GLU I C   1 
ATOM   14898 O O   . GLU I  1 198 ? 42.191  41.125  16.095  1.00 52.95  ? 190 GLU I O   1 
ATOM   14899 C CB  . GLU I  1 198 ? 40.930  41.935  19.160  1.00 58.28  ? 190 GLU I CB  1 
ATOM   14900 C CG  . GLU I  1 198 ? 39.483  42.173  18.707  1.00 60.72  ? 190 GLU I CG  1 
ATOM   14901 C CD  . GLU I  1 198 ? 38.476  42.101  19.855  1.00 59.89  ? 190 GLU I CD  1 
ATOM   14902 O OE1 . GLU I  1 198 ? 38.900  42.013  21.032  1.00 59.42  ? 190 GLU I OE1 1 
ATOM   14903 O OE2 . GLU I  1 198 ? 37.256  42.135  19.578  1.00 54.85  ? 190 GLU I OE2 1 
ATOM   14904 N N   . ALA I  1 199 ? 43.224  40.240  17.887  1.00 38.16  ? 191 ALA I N   1 
ATOM   14905 C CA  . ALA I  1 199 ? 44.015  39.274  17.104  1.00 39.34  ? 191 ALA I CA  1 
ATOM   14906 C C   . ALA I  1 199 ? 43.656  37.785  17.229  1.00 31.92  ? 191 ALA I C   1 
ATOM   14907 O O   . ALA I  1 199 ? 43.333  37.305  18.300  1.00 37.67  ? 191 ALA I O   1 
ATOM   14908 C CB  . ALA I  1 199 ? 45.513  39.476  17.371  1.00 36.61  ? 191 ALA I CB  1 
ATOM   14909 N N   . TYR I  1 200 ? 43.763  37.055  16.121  1.00 36.47  ? 192 TYR I N   1 
ATOM   14910 C CA  . TYR I  1 200 ? 43.413  35.636  16.074  1.00 33.98  ? 192 TYR I CA  1 
ATOM   14911 C C   . TYR I  1 200 ? 44.625  34.753  15.821  1.00 34.76  ? 192 TYR I C   1 
ATOM   14912 O O   . TYR I  1 200 ? 45.072  34.622  14.688  1.00 43.00  ? 192 TYR I O   1 
ATOM   14913 C CB  . TYR I  1 200 ? 42.369  35.369  14.979  1.00 32.07  ? 192 TYR I CB  1 
ATOM   14914 C CG  . TYR I  1 200 ? 41.097  36.140  15.180  1.00 30.77  ? 192 TYR I CG  1 
ATOM   14915 C CD1 . TYR I  1 200 ? 40.054  35.603  15.912  1.00 29.91  ? 192 TYR I CD1 1 
ATOM   14916 C CD2 . TYR I  1 200 ? 40.947  37.415  14.658  1.00 33.87  ? 192 TYR I CD2 1 
ATOM   14917 C CE1 . TYR I  1 200 ? 38.885  36.309  16.114  1.00 35.40  ? 192 TYR I CE1 1 
ATOM   14918 C CE2 . TYR I  1 200 ? 39.785  38.134  14.848  1.00 39.47  ? 192 TYR I CE2 1 
ATOM   14919 C CZ  . TYR I  1 200 ? 38.751  37.578  15.580  1.00 43.51  ? 192 TYR I CZ  1 
ATOM   14920 O OH  . TYR I  1 200 ? 37.583  38.286  15.789  1.00 40.60  ? 192 TYR I OH  1 
ATOM   14921 N N   . GLU I  1 201 ? 45.144  34.137  16.875  1.00 36.94  ? 193 GLU I N   1 
ATOM   14922 C CA  . GLU I  1 201 ? 46.222  33.163  16.746  1.00 36.97  ? 193 GLU I CA  1 
ATOM   14923 C C   . GLU I  1 201 ? 45.884  32.047  15.755  1.00 39.68  ? 193 GLU I C   1 
ATOM   14924 O O   . GLU I  1 201 ? 44.737  31.610  15.660  1.00 44.76  ? 193 GLU I O   1 
ATOM   14925 C CB  . GLU I  1 201 ? 46.562  32.565  18.116  1.00 32.44  ? 193 GLU I CB  1 
ATOM   14926 C CG  . GLU I  1 201 ? 47.040  33.605  19.120  1.00 34.50  ? 193 GLU I CG  1 
ATOM   14927 C CD  . GLU I  1 201 ? 48.066  33.063  20.107  1.00 45.57  ? 193 GLU I CD  1 
ATOM   14928 O OE1 . GLU I  1 201 ? 48.334  31.841  20.096  1.00 49.38  ? 193 GLU I OE1 1 
ATOM   14929 O OE2 . GLU I  1 201 ? 48.608  33.864  20.902  1.00 53.26  ? 193 GLU I OE2 1 
ATOM   14930 N N   . ASP I  1 202 ? 46.887  31.586  15.017  1.00 40.08  ? 194 ASP I N   1 
ATOM   14931 C CA  . ASP I  1 202 ? 46.687  30.484  14.086  1.00 35.00  ? 194 ASP I CA  1 
ATOM   14932 C C   . ASP I  1 202 ? 47.942  29.632  13.887  1.00 37.13  ? 194 ASP I C   1 
ATOM   14933 O O   . ASP I  1 202 ? 48.998  29.904  14.457  1.00 45.08  ? 194 ASP I O   1 
ATOM   14934 C CB  . ASP I  1 202 ? 46.196  31.010  12.740  1.00 35.86  ? 194 ASP I CB  1 
ATOM   14935 C CG  . ASP I  1 202 ? 47.317  31.588  11.896  1.00 42.76  ? 194 ASP I CG  1 
ATOM   14936 O OD1 . ASP I  1 202 ? 48.063  30.798  11.278  1.00 42.67  ? 194 ASP I OD1 1 
ATOM   14937 O OD2 . ASP I  1 202 ? 47.447  32.831  11.839  1.00 49.82  ? 194 ASP I OD2 1 
ATOM   14938 N N   . VAL I  1 203 ? 47.816  28.602  13.060  1.00 33.35  ? 195 VAL I N   1 
ATOM   14939 C CA  . VAL I  1 203 ? 48.934  27.733  12.722  1.00 38.39  ? 195 VAL I CA  1 
ATOM   14940 C C   . VAL I  1 203 ? 49.131  27.634  11.200  1.00 33.43  ? 195 VAL I C   1 
ATOM   14941 O O   . VAL I  1 203 ? 48.286  27.096  10.487  1.00 29.25  ? 195 VAL I O   1 
ATOM   14942 C CB  . VAL I  1 203 ? 48.740  26.333  13.336  1.00 34.54  ? 195 VAL I CB  1 
ATOM   14943 C CG1 . VAL I  1 203 ? 49.845  25.386  12.907  1.00 28.75  ? 195 VAL I CG1 1 
ATOM   14944 C CG2 . VAL I  1 203 ? 48.695  26.445  14.841  1.00 42.37  ? 195 VAL I CG2 1 
ATOM   14945 N N   . GLU I  1 204 ? 50.240  28.178  10.709  1.00 34.06  ? 196 GLU I N   1 
ATOM   14946 C CA  . GLU I  1 204 ? 50.581  28.063  9.298   1.00 30.93  ? 196 GLU I CA  1 
ATOM   14947 C C   . GLU I  1 204 ? 51.242  26.719  9.044   1.00 33.17  ? 196 GLU I C   1 
ATOM   14948 O O   . GLU I  1 204 ? 52.284  26.416  9.624   1.00 40.10  ? 196 GLU I O   1 
ATOM   14949 C CB  . GLU I  1 204 ? 51.532  29.178  8.869   1.00 28.16  ? 196 GLU I CB  1 
ATOM   14950 C CG  . GLU I  1 204 ? 50.874  30.503  8.578   1.00 38.56  ? 196 GLU I CG  1 
ATOM   14951 C CD  . GLU I  1 204 ? 51.617  31.288  7.508   1.00 55.11  ? 196 GLU I CD  1 
ATOM   14952 O OE1 . GLU I  1 204 ? 52.423  30.670  6.770   1.00 55.54  ? 196 GLU I OE1 1 
ATOM   14953 O OE2 . GLU I  1 204 ? 51.394  32.518  7.398   1.00 55.96  ? 196 GLU I OE2 1 
ATOM   14954 N N   . VAL I  1 205 ? 50.631  25.902  8.196   1.00 26.12  ? 197 VAL I N   1 
ATOM   14955 C CA  . VAL I  1 205 ? 51.275  24.677  7.758   1.00 29.53  ? 197 VAL I CA  1 
ATOM   14956 C C   . VAL I  1 205 ? 51.799  24.879  6.356   1.00 33.29  ? 197 VAL I C   1 
ATOM   14957 O O   . VAL I  1 205 ? 51.053  25.266  5.458   1.00 33.44  ? 197 VAL I O   1 
ATOM   14958 C CB  . VAL I  1 205 ? 50.326  23.476  7.744   1.00 31.43  ? 197 VAL I CB  1 
ATOM   14959 C CG1 . VAL I  1 205 ? 50.907  22.363  6.882   1.00 29.02  ? 197 VAL I CG1 1 
ATOM   14960 C CG2 . VAL I  1 205 ? 50.070  22.977  9.149   1.00 29.68  ? 197 VAL I CG2 1 
ATOM   14961 N N   . SER I  1 206 ? 53.089  24.627  6.173   1.00 40.25  ? 198 SER I N   1 
ATOM   14962 C CA  . SER I  1 206 ? 53.697  24.709  4.856   1.00 34.31  ? 198 SER I CA  1 
ATOM   14963 C C   . SER I  1 206 ? 54.072  23.317  4.358   1.00 35.50  ? 198 SER I C   1 
ATOM   14964 O O   . SER I  1 206 ? 54.813  22.580  5.012   1.00 30.94  ? 198 SER I O   1 
ATOM   14965 C CB  . SER I  1 206 ? 54.891  25.648  4.886   1.00 36.59  ? 198 SER I CB  1 
ATOM   14966 O OG  . SER I  1 206 ? 54.450  26.966  5.175   1.00 45.67  ? 198 SER I OG  1 
ATOM   14967 N N   . LEU I  1 207 ? 53.528  22.971  3.196   1.00 36.26  ? 199 LEU I N   1 
ATOM   14968 C CA  . LEU I  1 207 ? 53.625  21.630  2.646   1.00 33.50  ? 199 LEU I CA  1 
ATOM   14969 C C   . LEU I  1 207 ? 54.300  21.653  1.268   1.00 39.43  ? 199 LEU I C   1 
ATOM   14970 O O   . LEU I  1 207 ? 53.693  22.071  0.275   1.00 35.62  ? 199 LEU I O   1 
ATOM   14971 C CB  . LEU I  1 207 ? 52.223  21.034  2.551   1.00 32.61  ? 199 LEU I CB  1 
ATOM   14972 C CG  . LEU I  1 207 ? 52.034  19.629  1.988   1.00 35.45  ? 199 LEU I CG  1 
ATOM   14973 C CD1 . LEU I  1 207 ? 52.770  18.611  2.829   1.00 36.44  ? 199 LEU I CD1 1 
ATOM   14974 C CD2 . LEU I  1 207 ? 50.557  19.300  1.938   1.00 28.67  ? 199 LEU I CD2 1 
ATOM   14975 N N   . ASN I  1 208 ? 55.565  21.221  1.235   1.00 43.61  ? 200 ASN I N   1 
ATOM   14976 C CA  . ASN I  1 208 ? 56.365  21.104  0.008   1.00 41.54  ? 200 ASN I CA  1 
ATOM   14977 C C   . ASN I  1 208 ? 56.174  19.730  -0.650  1.00 41.02  ? 200 ASN I C   1 
ATOM   14978 O O   . ASN I  1 208 ? 56.645  18.706  -0.134  1.00 37.33  ? 200 ASN I O   1 
ATOM   14979 C CB  . ASN I  1 208 ? 57.857  21.311  0.326   1.00 44.21  ? 200 ASN I CB  1 
ATOM   14980 C CG  . ASN I  1 208 ? 58.533  22.319  -0.603  1.00 49.04  ? 200 ASN I CG  1 
ATOM   14981 O OD1 . ASN I  1 208 ? 58.674  22.083  -1.809  1.00 46.33  ? 200 ASN I OD1 1 
ATOM   14982 N ND2 . ASN I  1 208 ? 58.969  23.447  -0.035  1.00 42.54  ? 200 ASN I ND2 1 
ATOM   14983 N N   . PHE I  1 209 ? 55.485  19.696  -1.783  1.00 30.87  ? 201 PHE I N   1 
ATOM   14984 C CA  . PHE I  1 209 ? 55.189  18.417  -2.416  1.00 33.32  ? 201 PHE I CA  1 
ATOM   14985 C C   . PHE I  1 209 ? 55.424  18.494  -3.918  1.00 38.10  ? 201 PHE I C   1 
ATOM   14986 O O   . PHE I  1 209 ? 55.483  19.584  -4.490  1.00 36.29  ? 201 PHE I O   1 
ATOM   14987 C CB  . PHE I  1 209 ? 53.743  17.987  -2.119  1.00 32.21  ? 201 PHE I CB  1 
ATOM   14988 C CG  . PHE I  1 209 ? 52.695  18.818  -2.828  1.00 29.51  ? 201 PHE I CG  1 
ATOM   14989 C CD1 . PHE I  1 209 ? 52.513  20.159  -2.509  1.00 27.22  ? 201 PHE I CD1 1 
ATOM   14990 C CD2 . PHE I  1 209 ? 51.890  18.253  -3.807  1.00 24.02  ? 201 PHE I CD2 1 
ATOM   14991 C CE1 . PHE I  1 209 ? 51.564  20.925  -3.165  1.00 24.14  ? 201 PHE I CE1 1 
ATOM   14992 C CE2 . PHE I  1 209 ? 50.936  19.013  -4.459  1.00 24.61  ? 201 PHE I CE2 1 
ATOM   14993 C CZ  . PHE I  1 209 ? 50.774  20.353  -4.140  1.00 20.34  ? 201 PHE I CZ  1 
ATOM   14994 N N   . ARG I  1 210 ? 55.556  17.336  -4.556  1.00 36.52  ? 202 ARG I N   1 
ATOM   14995 C CA  . ARG I  1 210 ? 55.697  17.299  -6.004  1.00 37.12  ? 202 ARG I CA  1 
ATOM   14996 C C   . ARG I  1 210 ? 55.135  16.008  -6.604  1.00 37.08  ? 202 ARG I C   1 
ATOM   14997 O O   . ARG I  1 210 ? 54.913  15.023  -5.890  1.00 33.19  ? 202 ARG I O   1 
ATOM   14998 C CB  . ARG I  1 210 ? 57.163  17.478  -6.389  1.00 42.10  ? 202 ARG I CB  1 
ATOM   14999 C CG  . ARG I  1 210 ? 58.099  16.459  -5.759  1.00 42.84  ? 202 ARG I CG  1 
ATOM   15000 C CD  . ARG I  1 210 ? 58.999  15.835  -6.823  1.00 52.29  ? 202 ARG I CD  1 
ATOM   15001 N NE  . ARG I  1 210 ? 59.815  14.737  -6.305  1.00 50.41  ? 202 ARG I NE  1 
ATOM   15002 C CZ  . ARG I  1 210 ? 61.098  14.852  -5.982  1.00 46.07  ? 202 ARG I CZ  1 
ATOM   15003 N NH1 . ARG I  1 210 ? 61.715  16.025  -6.125  1.00 42.31  ? 202 ARG I NH1 1 
ATOM   15004 N NH2 . ARG I  1 210 ? 61.761  13.795  -5.516  1.00 35.69  ? 202 ARG I NH2 1 
ATOM   15005 N N   . LYS I  1 211 ? 54.897  16.020  -7.913  1.00 31.17  ? 203 LYS I N   1 
ATOM   15006 C CA  . LYS I  1 211 ? 54.458  14.815  -8.614  1.00 39.19  ? 203 LYS I CA  1 
ATOM   15007 C C   . LYS I  1 211 ? 55.526  13.712  -8.508  1.00 41.03  ? 203 LYS I C   1 
ATOM   15008 O O   . LYS I  1 211 ? 56.719  13.992  -8.585  1.00 41.79  ? 203 LYS I O   1 
ATOM   15009 C CB  . LYS I  1 211 ? 54.137  15.143  -10.081 1.00 39.06  ? 203 LYS I CB  1 
ATOM   15010 C CG  . LYS I  1 211 ? 53.264  14.114  -10.798 1.00 37.17  ? 203 LYS I CG  1 
ATOM   15011 C CD  . LYS I  1 211 ? 52.722  14.680  -12.104 1.00 40.70  ? 203 LYS I CD  1 
ATOM   15012 C CE  . LYS I  1 211 ? 52.408  13.569  -13.116 1.00 56.04  ? 203 LYS I CE  1 
ATOM   15013 N NZ  . LYS I  1 211 ? 52.621  13.990  -14.547 1.00 50.60  ? 203 LYS I NZ  1 
ATOM   15014 N N   . LYS I  1 212 ? 55.113  12.465  -8.303  1.00 42.05  ? 204 LYS I N   1 
ATOM   15015 C CA  . LYS I  1 212 ? 56.088  11.379  -8.197  1.00 40.14  ? 204 LYS I CA  1 
ATOM   15016 C C   . LYS I  1 212 ? 56.708  11.100  -9.562  1.00 43.33  ? 204 LYS I C   1 
ATOM   15017 O O   . LYS I  1 212 ? 56.275  11.663  -10.568 1.00 41.73  ? 204 LYS I O   1 
ATOM   15018 C CB  . LYS I  1 212 ? 55.458  10.105  -7.609  1.00 39.92  ? 204 LYS I CB  1 
ATOM   15019 C CG  . LYS I  1 212 ? 55.441  10.036  -6.077  1.00 41.15  ? 204 LYS I CG  1 
ATOM   15020 C CD  . LYS I  1 212 ? 54.683  8.809   -5.563  1.00 39.19  ? 204 LYS I CD  1 
ATOM   15021 C CE  . LYS I  1 212 ? 55.614  7.661   -5.201  1.00 43.41  ? 204 LYS I CE  1 
ATOM   15022 N NZ  . LYS I  1 212 ? 54.891  6.356   -5.086  1.00 41.90  ? 204 LYS I NZ  1 
ATOM   15023 N N   . GLY I  1 213 ? 57.727  10.242  -9.591  1.00 55.03  ? 205 GLY I N   1 
ATOM   15024 C CA  . GLY I  1 213 ? 58.381  9.858   -10.833 1.00 52.03  ? 205 GLY I CA  1 
ATOM   15025 C C   . GLY I  1 213 ? 59.068  11.010  -11.542 1.00 58.38  ? 205 GLY I C   1 
ATOM   15026 O O   . GLY I  1 213 ? 59.699  10.823  -12.586 1.00 64.82  ? 205 GLY I O   1 
ATOM   15027 N N   . ASP J  1 1   ? 34.620  43.953  31.186  1.00 50.25  ? -7  ASP J N   1 
ATOM   15028 C CA  . ASP J  1 1   ? 36.038  44.243  31.373  1.00 57.05  ? -7  ASP J CA  1 
ATOM   15029 C C   . ASP J  1 1   ? 36.919  43.368  30.473  1.00 57.27  ? -7  ASP J C   1 
ATOM   15030 O O   . ASP J  1 1   ? 36.435  42.466  29.792  1.00 54.46  ? -7  ASP J O   1 
ATOM   15031 C CB  . ASP J  1 1   ? 36.438  44.069  32.844  1.00 52.40  ? -7  ASP J CB  1 
ATOM   15032 C CG  . ASP J  1 1   ? 37.719  44.825  33.199  1.00 62.88  ? -7  ASP J CG  1 
ATOM   15033 O OD1 . ASP J  1 1   ? 37.800  46.041  32.901  1.00 59.85  ? -7  ASP J OD1 1 
ATOM   15034 O OD2 . ASP J  1 1   ? 38.651  44.200  33.759  1.00 59.23  ? -7  ASP J OD2 1 
ATOM   15035 N N   . TYR J  1 2   ? 38.216  43.651  30.479  1.00 56.26  ? -6  TYR J N   1 
ATOM   15036 C CA  . TYR J  1 2   ? 39.188  42.915  29.688  1.00 57.75  ? -6  TYR J CA  1 
ATOM   15037 C C   . TYR J  1 2   ? 39.825  41.822  30.531  1.00 59.06  ? -6  TYR J C   1 
ATOM   15038 O O   . TYR J  1 2   ? 40.010  40.695  30.066  1.00 57.29  ? -6  TYR J O   1 
ATOM   15039 C CB  . TYR J  1 2   ? 40.257  43.884  29.173  1.00 72.84  ? -6  TYR J CB  1 
ATOM   15040 C CG  . TYR J  1 2   ? 41.555  43.250  28.718  1.00 74.17  ? -6  TYR J CG  1 
ATOM   15041 C CD1 . TYR J  1 2   ? 42.778  43.666  29.242  1.00 69.89  ? -6  TYR J CD1 1 
ATOM   15042 C CD2 . TYR J  1 2   ? 41.560  42.243  27.758  1.00 79.73  ? -6  TYR J CD2 1 
ATOM   15043 C CE1 . TYR J  1 2   ? 43.971  43.090  28.819  1.00 81.11  ? -6  TYR J CE1 1 
ATOM   15044 C CE2 . TYR J  1 2   ? 42.744  41.661  27.333  1.00 79.01  ? -6  TYR J CE2 1 
ATOM   15045 C CZ  . TYR J  1 2   ? 43.944  42.086  27.860  1.00 85.03  ? -6  TYR J CZ  1 
ATOM   15046 O OH  . TYR J  1 2   ? 45.110  41.497  27.423  1.00 74.82  ? -6  TYR J OH  1 
ATOM   15047 N N   . LYS J  1 3   ? 40.152  42.156  31.777  1.00 59.18  ? -5  LYS J N   1 
ATOM   15048 C CA  . LYS J  1 3   ? 40.809  41.208  32.673  1.00 57.38  ? -5  LYS J CA  1 
ATOM   15049 C C   . LYS J  1 3   ? 39.851  40.105  33.112  1.00 51.93  ? -5  LYS J C   1 
ATOM   15050 O O   . LYS J  1 3   ? 40.250  39.177  33.811  1.00 54.29  ? -5  LYS J O   1 
ATOM   15051 C CB  . LYS J  1 3   ? 41.390  41.927  33.898  1.00 61.03  ? -5  LYS J CB  1 
ATOM   15052 C CG  . LYS J  1 3   ? 42.862  41.612  34.193  1.00 57.66  ? -5  LYS J CG  1 
ATOM   15053 C CD  . LYS J  1 3   ? 43.764  41.991  33.022  1.00 55.72  ? -5  LYS J CD  1 
ATOM   15054 C CE  . LYS J  1 3   ? 45.054  42.655  33.498  1.00 52.89  ? -5  LYS J CE  1 
ATOM   15055 N NZ  . LYS J  1 3   ? 45.834  41.817  34.453  1.00 35.41  ? -5  LYS J NZ  1 
ATOM   15056 N N   . ASP J  1 4   ? 38.591  40.209  32.689  1.00 56.49  ? -4  ASP J N   1 
ATOM   15057 C CA  . ASP J  1 4   ? 37.553  39.257  33.088  1.00 51.31  ? -4  ASP J CA  1 
ATOM   15058 C C   . ASP J  1 4   ? 36.970  38.439  31.933  1.00 43.04  ? -4  ASP J C   1 
ATOM   15059 O O   . ASP J  1 4   ? 36.065  37.644  32.149  1.00 41.35  ? -4  ASP J O   1 
ATOM   15060 C CB  . ASP J  1 4   ? 36.425  39.972  33.839  1.00 46.09  ? -4  ASP J CB  1 
ATOM   15061 C CG  . ASP J  1 4   ? 36.879  40.526  35.171  1.00 52.28  ? -4  ASP J CG  1 
ATOM   15062 O OD1 . ASP J  1 4   ? 37.316  39.725  36.025  1.00 56.91  ? -4  ASP J OD1 1 
ATOM   15063 O OD2 . ASP J  1 4   ? 36.800  41.756  35.365  1.00 52.97  ? -4  ASP J OD2 1 
ATOM   15064 N N   . ASP J  1 5   ? 37.492  38.634  30.723  1.00 43.28  ? -3  ASP J N   1 
ATOM   15065 C CA  . ASP J  1 5   ? 37.051  37.883  29.544  1.00 40.37  ? -3  ASP J CA  1 
ATOM   15066 C C   . ASP J  1 5   ? 37.108  36.371  29.772  1.00 38.42  ? -3  ASP J C   1 
ATOM   15067 O O   . ASP J  1 5   ? 36.276  35.626  29.249  1.00 34.94  ? -3  ASP J O   1 
ATOM   15068 C CB  . ASP J  1 5   ? 37.882  38.258  28.301  1.00 42.20  ? -3  ASP J CB  1 
ATOM   15069 C CG  . ASP J  1 5   ? 37.269  39.412  27.497  1.00 49.10  ? -3  ASP J CG  1 
ATOM   15070 O OD1 . ASP J  1 5   ? 36.240  39.971  27.934  1.00 37.61  ? -3  ASP J OD1 1 
ATOM   15071 O OD2 . ASP J  1 5   ? 37.825  39.769  26.430  1.00 51.51  ? -3  ASP J OD2 1 
ATOM   15072 N N   . ASP J  1 6   ? 38.075  35.920  30.564  1.00 35.12  ? -2  ASP J N   1 
ATOM   15073 C CA  . ASP J  1 6   ? 38.264  34.485  30.763  1.00 38.04  ? -2  ASP J CA  1 
ATOM   15074 C C   . ASP J  1 6   ? 37.676  33.884  32.051  1.00 37.06  ? -2  ASP J C   1 
ATOM   15075 O O   . ASP J  1 6   ? 38.022  32.761  32.419  1.00 35.40  ? -2  ASP J O   1 
ATOM   15076 C CB  . ASP J  1 6   ? 39.744  34.122  30.644  1.00 36.83  ? -2  ASP J CB  1 
ATOM   15077 C CG  . ASP J  1 6   ? 40.328  34.508  29.306  1.00 41.31  ? -2  ASP J CG  1 
ATOM   15078 O OD1 . ASP J  1 6   ? 39.553  34.906  28.412  1.00 36.15  ? -2  ASP J OD1 1 
ATOM   15079 O OD2 . ASP J  1 6   ? 41.564  34.403  29.144  1.00 50.28  ? -2  ASP J OD2 1 
ATOM   15080 N N   . ASP J  1 7   ? 36.794  34.604  32.737  1.00 33.20  ? -1  ASP J N   1 
ATOM   15081 C CA  . ASP J  1 7   ? 36.088  33.992  33.857  1.00 33.54  ? -1  ASP J CA  1 
ATOM   15082 C C   . ASP J  1 7   ? 35.067  33.013  33.295  1.00 30.84  ? -1  ASP J C   1 
ATOM   15083 O O   . ASP J  1 7   ? 34.086  33.424  32.673  1.00 30.98  ? -1  ASP J O   1 
ATOM   15084 C CB  . ASP J  1 7   ? 35.384  35.043  34.707  1.00 35.56  ? -1  ASP J CB  1 
ATOM   15085 C CG  . ASP J  1 7   ? 34.930  34.499  36.056  1.00 39.33  ? -1  ASP J CG  1 
ATOM   15086 O OD1 . ASP J  1 7   ? 34.801  33.257  36.219  1.00 35.84  ? -1  ASP J OD1 1 
ATOM   15087 O OD2 . ASP J  1 7   ? 34.707  35.330  36.963  1.00 47.67  ? -1  ASP J OD2 1 
ATOM   15088 N N   . LYS J  1 8   ? 35.288  31.720  33.509  1.00 24.87  ? 0   LYS J N   1 
ATOM   15089 C CA  . LYS J  1 8   ? 34.431  30.728  32.883  1.00 21.68  ? 0   LYS J CA  1 
ATOM   15090 C C   . LYS J  1 8   ? 32.975  30.837  33.320  1.00 27.34  ? 0   LYS J C   1 
ATOM   15091 O O   . LYS J  1 8   ? 32.064  30.775  32.487  1.00 25.13  ? 0   LYS J O   1 
ATOM   15092 C CB  . LYS J  1 8   ? 34.938  29.318  33.127  1.00 17.98  ? 0   LYS J CB  1 
ATOM   15093 C CG  . LYS J  1 8   ? 34.167  28.313  32.309  1.00 19.58  ? 0   LYS J CG  1 
ATOM   15094 C CD  . LYS J  1 8   ? 34.783  26.943  32.395  1.00 24.37  ? 0   LYS J CD  1 
ATOM   15095 C CE  . LYS J  1 8   ? 34.016  25.938  31.552  1.00 21.56  ? 0   LYS J CE  1 
ATOM   15096 N NZ  . LYS J  1 8   ? 34.491  24.562  31.860  1.00 30.77  ? 0   LYS J NZ  1 
ATOM   15097 N N   . LEU J  1 9   ? 32.766  31.010  34.624  1.00 26.05  ? 1   LEU J N   1 
ATOM   15098 C CA  . LEU J  1 9   ? 31.429  31.039  35.206  1.00 21.85  ? 1   LEU J CA  1 
ATOM   15099 C C   . LEU J  1 9   ? 30.622  32.216  34.670  1.00 22.80  ? 1   LEU J C   1 
ATOM   15100 O O   . LEU J  1 9   ? 29.467  32.064  34.273  1.00 19.40  ? 1   LEU J O   1 
ATOM   15101 C CB  . LEU J  1 9   ? 31.533  31.104  36.725  1.00 25.97  ? 1   LEU J CB  1 
ATOM   15102 C CG  . LEU J  1 9   ? 30.257  30.936  37.533  1.00 21.80  ? 1   LEU J CG  1 
ATOM   15103 C CD1 . LEU J  1 9   ? 29.570  29.648  37.131  1.00 22.25  ? 1   LEU J CD1 1 
ATOM   15104 C CD2 . LEU J  1 9   ? 30.595  30.944  39.001  1.00 15.69  ? 1   LEU J CD2 1 
ATOM   15105 N N   . ASP J  1 10  ? 31.251  33.385  34.646  1.00 25.26  ? 2   ASP J N   1 
ATOM   15106 C CA  . ASP J  1 10  ? 30.640  34.586  34.088  1.00 25.54  ? 2   ASP J CA  1 
ATOM   15107 C C   . ASP J  1 10  ? 30.200  34.370  32.640  1.00 22.29  ? 2   ASP J C   1 
ATOM   15108 O O   . ASP J  1 10  ? 29.195  34.914  32.189  1.00 21.42  ? 2   ASP J O   1 
ATOM   15109 C CB  . ASP J  1 10  ? 31.639  35.745  34.125  1.00 37.20  ? 2   ASP J CB  1 
ATOM   15110 C CG  . ASP J  1 10  ? 31.666  36.472  35.460  1.00 34.59  ? 2   ASP J CG  1 
ATOM   15111 O OD1 . ASP J  1 10  ? 30.646  36.461  36.171  1.00 35.08  ? 2   ASP J OD1 1 
ATOM   15112 O OD2 . ASP J  1 10  ? 32.713  37.079  35.782  1.00 40.74  ? 2   ASP J OD2 1 
ATOM   15113 N N   . ARG J  1 11  ? 30.981  33.594  31.903  1.00 27.60  ? 3   ARG J N   1 
ATOM   15114 C CA  . ARG J  1 11  ? 30.669  33.307  30.511  1.00 19.22  ? 3   ARG J CA  1 
ATOM   15115 C C   . ARG J  1 11  ? 29.442  32.421  30.433  1.00 19.04  ? 3   ARG J C   1 
ATOM   15116 O O   . ARG J  1 11  ? 28.463  32.745  29.769  1.00 17.86  ? 3   ARG J O   1 
ATOM   15117 C CB  . ARG J  1 11  ? 31.844  32.603  29.856  1.00 22.06  ? 3   ARG J CB  1 
ATOM   15118 C CG  . ARG J  1 11  ? 32.995  33.516  29.521  1.00 22.69  ? 3   ARG J CG  1 
ATOM   15119 C CD  . ARG J  1 11  ? 33.837  32.946  28.397  1.00 18.77  ? 3   ARG J CD  1 
ATOM   15120 N NE  . ARG J  1 11  ? 34.456  34.044  27.683  1.00 26.10  ? 3   ARG J NE  1 
ATOM   15121 C CZ  . ARG J  1 11  ? 34.374  34.231  26.373  1.00 27.02  ? 3   ARG J CZ  1 
ATOM   15122 N NH1 . ARG J  1 11  ? 33.724  33.370  25.614  1.00 27.58  ? 3   ARG J NH1 1 
ATOM   15123 N NH2 . ARG J  1 11  ? 34.953  35.280  25.821  1.00 32.59  ? 3   ARG J NH2 1 
ATOM   15124 N N   . ALA J  1 12  ? 29.505  31.303  31.144  1.00 20.89  ? 4   ALA J N   1 
ATOM   15125 C CA  . ALA J  1 12  ? 28.411  30.358  31.212  1.00 17.39  ? 4   ALA J CA  1 
ATOM   15126 C C   . ALA J  1 12  ? 27.114  31.041  31.668  1.00 22.23  ? 4   ALA J C   1 
ATOM   15127 O O   . ALA J  1 12  ? 26.019  30.702  31.201  1.00 21.43  ? 4   ALA J O   1 
ATOM   15128 C CB  . ALA J  1 12  ? 28.787  29.234  32.141  1.00 16.24  ? 4   ALA J CB  1 
ATOM   15129 N N   . ASP J  1 13  ? 27.253  32.015  32.567  1.00 19.31  ? 5   ASP J N   1 
ATOM   15130 C CA  . ASP J  1 13  ? 26.119  32.792  33.054  1.00 15.49  ? 5   ASP J CA  1 
ATOM   15131 C C   . ASP J  1 13  ? 25.577  33.766  32.023  1.00 17.56  ? 5   ASP J C   1 
ATOM   15132 O O   . ASP J  1 13  ? 24.361  33.905  31.888  1.00 18.43  ? 5   ASP J O   1 
ATOM   15133 C CB  . ASP J  1 13  ? 26.490  33.546  34.325  1.00 16.58  ? 5   ASP J CB  1 
ATOM   15134 C CG  . ASP J  1 13  ? 26.489  32.654  35.536  1.00 18.54  ? 5   ASP J CG  1 
ATOM   15135 O OD1 . ASP J  1 13  ? 25.725  31.670  35.539  1.00 14.59  ? 5   ASP J OD1 1 
ATOM   15136 O OD2 . ASP J  1 13  ? 27.253  32.928  36.483  1.00 25.99  ? 5   ASP J OD2 1 
ATOM   15137 N N   . ILE J  1 14  ? 26.469  34.462  31.322  1.00 18.09  ? 6   ILE J N   1 
ATOM   15138 C CA  . ILE J  1 14  ? 26.063  35.316  30.205  1.00 20.34  ? 6   ILE J CA  1 
ATOM   15139 C C   . ILE J  1 14  ? 25.267  34.498  29.168  1.00 15.30  ? 6   ILE J C   1 
ATOM   15140 O O   . ILE J  1 14  ? 24.234  34.940  28.659  1.00 11.68  ? 6   ILE J O   1 
ATOM   15141 C CB  . ILE J  1 14  ? 27.289  36.010  29.535  1.00 19.15  ? 6   ILE J CB  1 
ATOM   15142 C CG1 . ILE J  1 14  ? 27.796  37.166  30.396  1.00 14.93  ? 6   ILE J CG1 1 
ATOM   15143 C CG2 . ILE J  1 14  ? 26.921  36.547  28.163  1.00 15.78  ? 6   ILE J CG2 1 
ATOM   15144 C CD1 . ILE J  1 14  ? 29.263  37.461  30.225  1.00 18.27  ? 6   ILE J CD1 1 
ATOM   15145 N N   . LEU J  1 15  ? 25.743  33.293  28.889  1.00 11.13  ? 7   LEU J N   1 
ATOM   15146 C CA  . LEU J  1 15  ? 25.072  32.413  27.956  1.00 12.86  ? 7   LEU J CA  1 
ATOM   15147 C C   . LEU J  1 15  ? 23.654  32.082  28.416  1.00 17.35  ? 7   LEU J C   1 
ATOM   15148 O O   . LEU J  1 15  ? 22.689  32.194  27.634  1.00 13.38  ? 7   LEU J O   1 
ATOM   15149 C CB  . LEU J  1 15  ? 25.863  31.125  27.813  1.00 13.83  ? 7   LEU J CB  1 
ATOM   15150 C CG  . LEU J  1 15  ? 25.632  30.442  26.478  1.00 14.46  ? 7   LEU J CG  1 
ATOM   15151 C CD1 . LEU J  1 15  ? 26.129  31.347  25.382  1.00 13.50  ? 7   LEU J CD1 1 
ATOM   15152 C CD2 . LEU J  1 15  ? 26.367  29.122  26.465  1.00 19.10  ? 7   LEU J CD2 1 
ATOM   15153 N N   . TYR J  1 16  ? 23.542  31.651  29.679  1.00 16.98  ? 8   TYR J N   1 
ATOM   15154 C CA  . TYR J  1 16  ? 22.250  31.435  30.335  1.00 13.24  ? 8   TYR J CA  1 
ATOM   15155 C C   . TYR J  1 16  ? 21.334  32.651  30.226  1.00 11.45  ? 8   TYR J C   1 
ATOM   15156 O O   . TYR J  1 16  ? 20.178  32.513  29.837  1.00 10.96  ? 8   TYR J O   1 
ATOM   15157 C CB  . TYR J  1 16  ? 22.450  31.069  31.798  1.00 12.00  ? 8   TYR J CB  1 
ATOM   15158 C CG  . TYR J  1 16  ? 21.178  30.993  32.630  1.00 15.78  ? 8   TYR J CG  1 
ATOM   15159 C CD1 . TYR J  1 16  ? 20.262  29.968  32.439  1.00 17.33  ? 8   TYR J CD1 1 
ATOM   15160 C CD2 . TYR J  1 16  ? 20.919  31.918  33.643  1.00 12.80  ? 8   TYR J CD2 1 
ATOM   15161 C CE1 . TYR J  1 16  ? 19.120  29.874  33.212  1.00 17.81  ? 8   TYR J CE1 1 
ATOM   15162 C CE2 . TYR J  1 16  ? 19.783  31.829  34.418  1.00 15.10  ? 8   TYR J CE2 1 
ATOM   15163 C CZ  . TYR J  1 16  ? 18.881  30.805  34.204  1.00 19.62  ? 8   TYR J CZ  1 
ATOM   15164 O OH  . TYR J  1 16  ? 17.730  30.696  34.975  1.00 15.31  ? 8   TYR J OH  1 
ATOM   15165 N N   . ASN J  1 17  ? 21.842  33.834  30.561  1.00 8.64   ? 9   ASN J N   1 
ATOM   15166 C CA  . ASN J  1 17  ? 21.053  35.039  30.366  1.00 10.89  ? 9   ASN J CA  1 
ATOM   15167 C C   . ASN J  1 17  ? 20.559  35.149  28.927  1.00 13.46  ? 9   ASN J C   1 
ATOM   15168 O O   . ASN J  1 17  ? 19.359  35.233  28.694  1.00 13.39  ? 9   ASN J O   1 
ATOM   15169 C CB  . ASN J  1 17  ? 21.804  36.304  30.773  1.00 11.11  ? 9   ASN J CB  1 
ATOM   15170 C CG  . ASN J  1 17  ? 22.229  36.292  32.222  1.00 17.64  ? 9   ASN J CG  1 
ATOM   15171 O OD1 . ASN J  1 17  ? 21.758  35.478  33.018  1.00 17.09  ? 9   ASN J OD1 1 
ATOM   15172 N ND2 . ASN J  1 17  ? 23.128  37.202  32.576  1.00 25.18  ? 9   ASN J ND2 1 
ATOM   15173 N N   . ILE J  1 18  ? 21.488  35.105  27.973  1.00 14.87  ? 10  ILE J N   1 
ATOM   15174 C CA  . ILE J  1 18  ? 21.164  35.212  26.555  1.00 12.98  ? 10  ILE J CA  1 
ATOM   15175 C C   . ILE J  1 18  ? 20.129  34.163  26.135  1.00 15.22  ? 10  ILE J C   1 
ATOM   15176 O O   . ILE J  1 18  ? 19.158  34.484  25.458  1.00 13.97  ? 10  ILE J O   1 
ATOM   15177 C CB  . ILE J  1 18  ? 22.440  35.102  25.673  1.00 15.17  ? 10  ILE J CB  1 
ATOM   15178 C CG1 . ILE J  1 18  ? 23.356  36.312  25.895  1.00 17.94  ? 10  ILE J CG1 1 
ATOM   15179 C CG2 . ILE J  1 18  ? 22.089  34.942  24.183  1.00 11.16  ? 10  ILE J CG2 1 
ATOM   15180 C CD1 . ILE J  1 18  ? 24.710  36.213  25.182  1.00 13.25  ? 10  ILE J CD1 1 
ATOM   15181 N N   . ARG J  1 19  ? 20.313  32.913  26.548  1.00 13.95  ? 11  ARG J N   1 
ATOM   15182 C CA  . ARG J  1 19  ? 19.371  31.876  26.139  1.00 12.25  ? 11  ARG J CA  1 
ATOM   15183 C C   . ARG J  1 19  ? 17.992  32.051  26.774  1.00 12.73  ? 11  ARG J C   1 
ATOM   15184 O O   . ARG J  1 19  ? 16.968  31.669  26.209  1.00 13.59  ? 11  ARG J O   1 
ATOM   15185 C CB  . ARG J  1 19  ? 19.949  30.491  26.398  1.00 12.41  ? 11  ARG J CB  1 
ATOM   15186 C CG  . ARG J  1 19  ? 20.926  30.092  25.322  1.00 13.59  ? 11  ARG J CG  1 
ATOM   15187 C CD  . ARG J  1 19  ? 21.643  28.800  25.629  1.00 15.12  ? 11  ARG J CD  1 
ATOM   15188 N NE  . ARG J  1 19  ? 22.430  28.397  24.467  1.00 25.97  ? 11  ARG J NE  1 
ATOM   15189 C CZ  . ARG J  1 19  ? 23.342  27.433  24.465  1.00 18.12  ? 11  ARG J CZ  1 
ATOM   15190 N NH1 . ARG J  1 19  ? 23.603  26.758  25.576  1.00 11.34  ? 11  ARG J NH1 1 
ATOM   15191 N NH2 . ARG J  1 19  ? 23.985  27.154  23.339  1.00 13.63  ? 11  ARG J NH2 1 
ATOM   15192 N N   . GLN J  1 20  ? 17.962  32.665  27.944  1.00 16.02  ? 12  GLN J N   1 
ATOM   15193 C CA  . GLN J  1 20  ? 16.690  32.928  28.584  1.00 14.96  ? 12  GLN J CA  1 
ATOM   15194 C C   . GLN J  1 20  ? 15.932  34.027  27.853  1.00 14.53  ? 12  GLN J C   1 
ATOM   15195 O O   . GLN J  1 20  ? 14.799  33.824  27.450  1.00 13.77  ? 12  GLN J O   1 
ATOM   15196 C CB  . GLN J  1 20  ? 16.902  33.271  30.046  1.00 15.83  ? 12  GLN J CB  1 
ATOM   15197 C CG  . GLN J  1 20  ? 17.203  32.066  30.896  1.00 16.44  ? 12  GLN J CG  1 
ATOM   15198 C CD  . GLN J  1 20  ? 16.168  31.889  31.957  1.00 27.11  ? 12  GLN J CD  1 
ATOM   15199 O OE1 . GLN J  1 20  ? 16.109  32.677  32.909  1.00 28.30  ? 12  GLN J OE1 1 
ATOM   15200 N NE2 . GLN J  1 20  ? 15.313  30.870  31.796  1.00 24.31  ? 12  GLN J NE2 1 
ATOM   15201 N N   . THR J  1 21  ? 16.565  35.178  27.645  1.00 16.73  ? 13  THR J N   1 
ATOM   15202 C CA  . THR J  1 21  ? 15.868  36.297  27.010  1.00 17.18  ? 13  THR J CA  1 
ATOM   15203 C C   . THR J  1 21  ? 15.708  36.198  25.466  1.00 14.67  ? 13  THR J C   1 
ATOM   15204 O O   . THR J  1 21  ? 14.783  36.778  24.880  1.00 14.15  ? 13  THR J O   1 
ATOM   15205 C CB  . THR J  1 21  ? 16.412  37.692  27.486  1.00 16.89  ? 13  THR J CB  1 
ATOM   15206 O OG1 . THR J  1 21  ? 16.885  37.599  28.831  1.00 25.83  ? 13  THR J OG1 1 
ATOM   15207 C CG2 . THR J  1 21  ? 15.355  38.749  27.439  1.00 16.52  ? 13  THR J CG2 1 
ATOM   15208 N N   . SER J  1 22  ? 16.558  35.423  24.809  1.00 16.53  ? 14  SER J N   1 
ATOM   15209 C CA  . SER J  1 22  ? 16.562  35.416  23.342  1.00 12.73  ? 14  SER J CA  1 
ATOM   15210 C C   . SER J  1 22  ? 15.393  34.671  22.700  1.00 12.84  ? 14  SER J C   1 
ATOM   15211 O O   . SER J  1 22  ? 15.060  33.547  23.065  1.00 14.10  ? 14  SER J O   1 
ATOM   15212 C CB  . SER J  1 22  ? 17.900  34.899  22.820  1.00 10.79  ? 14  SER J CB  1 
ATOM   15213 O OG  . SER J  1 22  ? 17.766  34.199  21.600  1.00 19.71  ? 14  SER J OG  1 
ATOM   15214 N N   . ARG J  1 23  ? 14.774  35.319  21.730  1.00 12.64  ? 15  ARG J N   1 
ATOM   15215 C CA  . ARG J  1 23  ? 13.737  34.692  20.935  1.00 13.46  ? 15  ARG J CA  1 
ATOM   15216 C C   . ARG J  1 23  ? 14.208  34.487  19.496  1.00 14.71  ? 15  ARG J C   1 
ATOM   15217 O O   . ARG J  1 23  ? 14.029  35.370  18.657  1.00 12.81  ? 15  ARG J O   1 
ATOM   15218 C CB  . ARG J  1 23  ? 12.505  35.580  20.887  1.00 16.83  ? 15  ARG J CB  1 
ATOM   15219 C CG  . ARG J  1 23  ? 11.926  35.978  22.204  1.00 13.26  ? 15  ARG J CG  1 
ATOM   15220 C CD  . ARG J  1 23  ? 10.507  36.396  21.958  1.00 19.85  ? 15  ARG J CD  1 
ATOM   15221 N NE  . ARG J  1 23  ? 9.999   37.279  22.997  1.00 28.14  ? 15  ARG J NE  1 
ATOM   15222 C CZ  . ARG J  1 23  ? 9.176   36.899  23.967  1.00 21.29  ? 15  ARG J CZ  1 
ATOM   15223 N NH1 . ARG J  1 23  ? 8.755   35.638  24.039  1.00 13.50  ? 15  ARG J NH1 1 
ATOM   15224 N NH2 . ARG J  1 23  ? 8.778   37.793  24.861  1.00 23.12  ? 15  ARG J NH2 1 
ATOM   15225 N N   . PRO J  1 24  ? 14.776  33.307  19.203  1.00 15.79  ? 16  PRO J N   1 
ATOM   15226 C CA  . PRO J  1 24  ? 15.316  32.902  17.897  1.00 14.35  ? 16  PRO J CA  1 
ATOM   15227 C C   . PRO J  1 24  ? 14.430  33.181  16.672  1.00 15.19  ? 16  PRO J C   1 
ATOM   15228 O O   . PRO J  1 24  ? 14.973  33.332  15.590  1.00 25.69  ? 16  PRO J O   1 
ATOM   15229 C CB  . PRO J  1 24  ? 15.476  31.383  18.052  1.00 17.40  ? 16  PRO J CB  1 
ATOM   15230 C CG  . PRO J  1 24  ? 15.656  31.166  19.496  1.00 11.44  ? 16  PRO J CG  1 
ATOM   15231 C CD  . PRO J  1 24  ? 14.809  32.198  20.174  1.00 13.23  ? 16  PRO J CD  1 
ATOM   15232 N N   . ASP J  1 25  ? 13.113  33.247  16.820  1.00 16.96  ? 17  ASP J N   1 
ATOM   15233 C CA  . ASP J  1 25  ? 12.219  33.284  15.665  1.00 13.66  ? 17  ASP J CA  1 
ATOM   15234 C C   . ASP J  1 25  ? 11.387  34.569  15.513  1.00 15.55  ? 17  ASP J C   1 
ATOM   15235 O O   . ASP J  1 25  ? 10.469  34.639  14.684  1.00 16.45  ? 17  ASP J O   1 
ATOM   15236 C CB  . ASP J  1 25  ? 11.293  32.061  15.689  1.00 15.61  ? 17  ASP J CB  1 
ATOM   15237 C CG  . ASP J  1 25  ? 12.047  30.748  15.503  1.00 26.28  ? 17  ASP J CG  1 
ATOM   15238 O OD1 . ASP J  1 25  ? 13.065  30.733  14.760  1.00 33.21  ? 17  ASP J OD1 1 
ATOM   15239 O OD2 . ASP J  1 25  ? 11.618  29.728  16.097  1.00 19.75  ? 17  ASP J OD2 1 
ATOM   15240 N N   . VAL J  1 26  ? 11.712  35.582  16.302  1.00 14.36  ? 18  VAL J N   1 
ATOM   15241 C CA  . VAL J  1 26  ? 10.970  36.835  16.303  1.00 16.66  ? 18  VAL J CA  1 
ATOM   15242 C C   . VAL J  1 26  ? 11.925  37.997  16.022  1.00 17.96  ? 18  VAL J C   1 
ATOM   15243 O O   . VAL J  1 26  ? 13.009  38.045  16.605  1.00 17.83  ? 18  VAL J O   1 
ATOM   15244 C CB  . VAL J  1 26  ? 10.306  37.035  17.680  1.00 14.75  ? 18  VAL J CB  1 
ATOM   15245 C CG1 . VAL J  1 26  ? 9.426   38.277  17.699  1.00 15.25  ? 18  VAL J CG1 1 
ATOM   15246 C CG2 . VAL J  1 26  ? 9.506   35.809  18.034  1.00 13.56  ? 18  VAL J CG2 1 
ATOM   15247 N N   . ILE J  1 27  ? 11.548  38.932  15.144  1.00 22.48  ? 19  ILE J N   1 
ATOM   15248 C CA  . ILE J  1 27  ? 12.478  40.023  14.798  1.00 22.71  ? 19  ILE J CA  1 
ATOM   15249 C C   . ILE J  1 27  ? 12.667  40.990  15.951  1.00 18.72  ? 19  ILE J C   1 
ATOM   15250 O O   . ILE J  1 27  ? 11.705  41.418  16.568  1.00 19.79  ? 19  ILE J O   1 
ATOM   15251 C CB  . ILE J  1 27  ? 12.100  40.809  13.516  1.00 20.64  ? 19  ILE J CB  1 
ATOM   15252 C CG1 . ILE J  1 27  ? 10.791  41.556  13.700  1.00 19.91  ? 19  ILE J CG1 1 
ATOM   15253 C CG2 . ILE J  1 27  ? 12.038  39.890  12.310  1.00 19.74  ? 19  ILE J CG2 1 
ATOM   15254 C CD1 . ILE J  1 27  ? 10.397  42.306  12.492  1.00 21.39  ? 19  ILE J CD1 1 
ATOM   15255 N N   . PRO J  1 28  ? 13.925  41.315  16.255  1.00 14.99  ? 20  PRO J N   1 
ATOM   15256 C CA  . PRO J  1 28  ? 14.295  42.185  17.373  1.00 18.84  ? 20  PRO J CA  1 
ATOM   15257 C C   . PRO J  1 28  ? 14.064  43.660  17.091  1.00 28.81  ? 20  PRO J C   1 
ATOM   15258 O O   . PRO J  1 28  ? 15.035  44.419  17.114  1.00 34.88  ? 20  PRO J O   1 
ATOM   15259 C CB  . PRO J  1 28  ? 15.791  41.937  17.518  1.00 21.06  ? 20  PRO J CB  1 
ATOM   15260 C CG  . PRO J  1 28  ? 16.224  41.511  16.158  1.00 18.98  ? 20  PRO J CG  1 
ATOM   15261 C CD  . PRO J  1 28  ? 15.097  40.735  15.587  1.00 14.59  ? 20  PRO J CD  1 
ATOM   15262 N N   . THR J  1 29  ? 12.818  44.054  16.832  1.00 28.93  ? 21  THR J N   1 
ATOM   15263 C CA  . THR J  1 29  ? 12.493  45.455  16.601  1.00 30.16  ? 21  THR J CA  1 
ATOM   15264 C C   . THR J  1 29  ? 12.367  46.181  17.927  1.00 43.35  ? 21  THR J C   1 
ATOM   15265 O O   . THR J  1 29  ? 11.590  45.778  18.802  1.00 44.74  ? 21  THR J O   1 
ATOM   15266 C CB  . THR J  1 29  ? 11.166  45.628  15.852  1.00 34.68  ? 21  THR J CB  1 
ATOM   15267 O OG1 . THR J  1 29  ? 10.113  44.991  16.586  1.00 31.24  ? 21  THR J OG1 1 
ATOM   15268 C CG2 . THR J  1 29  ? 11.247  45.029  14.465  1.00 26.88  ? 21  THR J CG2 1 
ATOM   15269 N N   . GLN J  1 30  ? 13.103  47.285  18.057  1.00 47.03  ? 22  GLN J N   1 
ATOM   15270 C CA  . GLN J  1 30  ? 13.186  48.049  19.273  1.00 48.64  ? 22  GLN J CA  1 
ATOM   15271 C C   . GLN J  1 30  ? 12.661  49.414  19.052  1.00 57.45  ? 22  GLN J C   1 
ATOM   15272 O O   . GLN J  1 30  ? 13.083  50.045  18.172  1.00 55.64  ? 22  GLN J O   1 
ATOM   15273 C CB  . GLN J  1 30  ? 14.630  48.187  19.690  1.00 42.68  ? 22  GLN J CB  1 
ATOM   15274 C CG  . GLN J  1 30  ? 15.427  46.890  19.697  1.00 47.98  ? 22  GLN J CG  1 
ATOM   15275 C CD  . GLN J  1 30  ? 16.894  47.036  20.090  1.00 47.85  ? 22  GLN J CD  1 
ATOM   15276 O OE1 . GLN J  1 30  ? 17.605  46.079  20.176  1.00 32.55  ? 22  GLN J OE1 1 
ATOM   15277 N NE2 . GLN J  1 30  ? 17.318  48.232  20.357  1.00 57.10  ? 22  GLN J NE2 1 
ATOM   15278 N N   . ARG J  1 31  ? 11.709  49.847  19.873  1.00 64.25  ? 23  ARG J N   1 
ATOM   15279 C CA  . ARG J  1 31  ? 11.243  51.232  19.854  1.00 64.70  ? 23  ARG J CA  1 
ATOM   15280 C C   . ARG J  1 31  ? 10.391  51.604  18.639  1.00 60.86  ? 23  ARG J C   1 
ATOM   15281 O O   . ARG J  1 31  ? 10.202  52.785  18.350  1.00 51.23  ? 23  ARG J O   1 
ATOM   15282 C CB  . ARG J  1 31  ? 12.431  52.192  19.966  1.00 59.91  ? 23  ARG J CB  1 
ATOM   15283 C CG  . ARG J  1 31  ? 13.636  51.607  20.685  1.00 65.41  ? 23  ARG J CG  1 
ATOM   15284 C CD  . ARG J  1 31  ? 14.774  51.327  19.717  1.00 68.79  ? 23  ARG J CD  1 
ATOM   15285 N NE  . ARG J  1 31  ? 15.405  52.556  19.245  1.00 64.82  ? 23  ARG J NE  1 
ATOM   15286 C CZ  . ARG J  1 31  ? 16.504  52.592  18.498  1.00 64.46  ? 23  ARG J CZ  1 
ATOM   15287 N NH1 . ARG J  1 31  ? 17.100  51.464  18.136  1.00 62.71  ? 23  ARG J NH1 1 
ATOM   15288 N NH2 . ARG J  1 31  ? 17.009  53.757  18.114  1.00 65.47  ? 23  ARG J NH2 1 
ATOM   15289 N N   . ASP J  1 32  ? 9.876   50.604  17.931  1.00 61.68  ? 24  ASP J N   1 
ATOM   15290 C CA  . ASP J  1 32  ? 9.034   50.860  16.765  1.00 58.30  ? 24  ASP J CA  1 
ATOM   15291 C C   . ASP J  1 32  ? 9.838   51.228  15.514  1.00 52.04  ? 24  ASP J C   1 
ATOM   15292 O O   . ASP J  1 32  ? 9.268   51.624  14.498  1.00 53.74  ? 24  ASP J O   1 
ATOM   15293 C CB  . ASP J  1 32  ? 8.015   51.959  17.074  1.00 57.93  ? 24  ASP J CB  1 
ATOM   15294 C CG  . ASP J  1 32  ? 7.324   51.755  18.407  1.00 66.32  ? 24  ASP J CG  1 
ATOM   15295 O OD1 . ASP J  1 32  ? 7.320   50.610  18.907  1.00 68.46  ? 24  ASP J OD1 1 
ATOM   15296 O OD2 . ASP J  1 32  ? 6.786   52.739  18.956  1.00 68.23  ? 24  ASP J OD2 1 
ATOM   15297 N N   . ARG J  1 33  ? 11.159  51.092  15.592  1.00 50.42  ? 25  ARG J N   1 
ATOM   15298 C CA  . ARG J  1 33  ? 12.032  51.348  14.449  1.00 53.70  ? 25  ARG J CA  1 
ATOM   15299 C C   . ARG J  1 33  ? 12.562  50.010  13.955  1.00 46.04  ? 25  ARG J C   1 
ATOM   15300 O O   . ARG J  1 33  ? 13.050  49.205  14.749  1.00 43.17  ? 25  ARG J O   1 
ATOM   15301 C CB  . ARG J  1 33  ? 13.189  52.265  14.846  1.00 56.87  ? 25  ARG J CB  1 
ATOM   15302 C CG  . ARG J  1 33  ? 12.754  53.552  15.528  1.00 62.69  ? 25  ARG J CG  1 
ATOM   15303 C CD  . ARG J  1 33  ? 12.089  54.500  14.544  1.00 66.08  ? 25  ARG J CD  1 
ATOM   15304 N NE  . ARG J  1 33  ? 12.534  55.879  14.726  1.00 71.68  ? 25  ARG J NE  1 
ATOM   15305 C CZ  . ARG J  1 33  ? 13.807  56.260  14.713  1.00 71.68  ? 25  ARG J CZ  1 
ATOM   15306 N NH1 . ARG J  1 33  ? 14.768  55.366  14.526  1.00 63.83  ? 25  ARG J NH1 1 
ATOM   15307 N NH2 . ARG J  1 33  ? 14.121  57.537  14.887  1.00 69.16  ? 25  ARG J NH2 1 
ATOM   15308 N N   . PRO J  1 34  ? 12.448  49.754  12.655  1.00 37.18  ? 26  PRO J N   1 
ATOM   15309 C CA  . PRO J  1 34  ? 12.697  48.375  12.148  1.00 34.16  ? 26  PRO J CA  1 
ATOM   15310 C C   . PRO J  1 34  ? 14.146  47.868  12.340  1.00 28.89  ? 26  PRO J C   1 
ATOM   15311 O O   . PRO J  1 34  ? 14.969  48.698  12.726  1.00 32.18  ? 26  PRO J O   1 
ATOM   15312 C CB  . PRO J  1 34  ? 12.370  48.485  10.664  1.00 35.50  ? 26  PRO J CB  1 
ATOM   15313 C CG  . PRO J  1 34  ? 12.941  49.795  10.290  1.00 39.06  ? 26  PRO J CG  1 
ATOM   15314 C CD  . PRO J  1 34  ? 12.603  50.704  11.438  1.00 38.41  ? 26  PRO J CD  1 
ATOM   15315 N N   . VAL J  1 35  ? 14.473  46.582  12.116  1.00 22.60  ? 27  VAL J N   1 
ATOM   15316 C CA  . VAL J  1 35  ? 15.819  46.172  12.491  1.00 24.59  ? 27  VAL J CA  1 
ATOM   15317 C C   . VAL J  1 35  ? 16.860  46.620  11.467  1.00 27.41  ? 27  VAL J C   1 
ATOM   15318 O O   . VAL J  1 35  ? 16.824  46.208  10.302  1.00 23.64  ? 27  VAL J O   1 
ATOM   15319 C CB  . VAL J  1 35  ? 15.938  44.650  12.596  1.00 25.35  ? 27  VAL J CB  1 
ATOM   15320 C CG1 . VAL J  1 35  ? 17.190  44.286  13.355  1.00 20.08  ? 27  VAL J CG1 1 
ATOM   15321 C CG2 . VAL J  1 35  ? 14.712  44.061  13.266  1.00 27.26  ? 27  VAL J CG2 1 
ATOM   15322 N N   . ALA J  1 36  ? 17.797  47.445  11.916  1.00 25.33  ? 28  ALA J N   1 
ATOM   15323 C CA  . ALA J  1 36  ? 18.928  47.845  11.093  1.00 19.94  ? 28  ALA J CA  1 
ATOM   15324 C C   . ALA J  1 36  ? 19.996  46.759  10.996  1.00 19.06  ? 28  ALA J C   1 
ATOM   15325 O O   . ALA J  1 36  ? 20.907  46.712  11.820  1.00 22.58  ? 28  ALA J O   1 
ATOM   15326 C CB  . ALA J  1 36  ? 19.545  49.115  11.632  1.00 15.12  ? 28  ALA J CB  1 
ATOM   15327 N N   . VAL J  1 37  ? 19.898  45.908  9.978   1.00 21.17  ? 29  VAL J N   1 
ATOM   15328 C CA  . VAL J  1 37  ? 20.962  44.948  9.667   1.00 24.80  ? 29  VAL J CA  1 
ATOM   15329 C C   . VAL J  1 37  ? 22.006  45.586  8.752   1.00 28.37  ? 29  VAL J C   1 
ATOM   15330 O O   . VAL J  1 37  ? 21.655  46.195  7.735   1.00 31.97  ? 29  VAL J O   1 
ATOM   15331 C CB  . VAL J  1 37  ? 20.410  43.683  8.964   1.00 23.75  ? 29  VAL J CB  1 
ATOM   15332 C CG1 . VAL J  1 37  ? 21.542  42.807  8.480   1.00 23.26  ? 29  VAL J CG1 1 
ATOM   15333 C CG2 . VAL J  1 37  ? 19.498  42.903  9.894   1.00 27.47  ? 29  VAL J CG2 1 
ATOM   15334 N N   . SER J  1 38  ? 23.279  45.435  9.114   1.00 24.93  ? 30  SER J N   1 
ATOM   15335 C CA  . SER J  1 38  ? 24.396  45.964  8.330   1.00 29.39  ? 30  SER J CA  1 
ATOM   15336 C C   . SER J  1 38  ? 25.165  44.853  7.623   1.00 27.93  ? 30  SER J C   1 
ATOM   15337 O O   . SER J  1 38  ? 25.758  44.005  8.277   1.00 27.78  ? 30  SER J O   1 
ATOM   15338 C CB  . SER J  1 38  ? 25.366  46.725  9.238   1.00 27.94  ? 30  SER J CB  1 
ATOM   15339 O OG  . SER J  1 38  ? 24.678  47.618  10.105  1.00 36.26  ? 30  SER J OG  1 
ATOM   15340 N N   . VAL J  1 39  ? 25.172  44.857  6.292   1.00 34.03  ? 31  VAL J N   1 
ATOM   15341 C CA  . VAL J  1 39  ? 25.982  43.886  5.552   1.00 36.28  ? 31  VAL J CA  1 
ATOM   15342 C C   . VAL J  1 39  ? 27.175  44.504  4.839   1.00 40.61  ? 31  VAL J C   1 
ATOM   15343 O O   . VAL J  1 39  ? 27.197  45.702  4.557   1.00 45.83  ? 31  VAL J O   1 
ATOM   15344 C CB  . VAL J  1 39  ? 25.182  43.119  4.478   1.00 26.62  ? 31  VAL J CB  1 
ATOM   15345 C CG1 . VAL J  1 39  ? 25.241  41.633  4.745   1.00 25.78  ? 31  VAL J CG1 1 
ATOM   15346 C CG2 . VAL J  1 39  ? 23.768  43.599  4.418   1.00 32.75  ? 31  VAL J CG2 1 
ATOM   15347 N N   . SER J  1 40  ? 28.163  43.658  4.560   1.00 37.35  ? 32  SER J N   1 
ATOM   15348 C CA  . SER J  1 40  ? 29.225  43.952  3.613   1.00 34.81  ? 32  SER J CA  1 
ATOM   15349 C C   . SER J  1 40  ? 29.970  42.658  3.340   1.00 37.95  ? 32  SER J C   1 
ATOM   15350 O O   . SER J  1 40  ? 30.481  42.020  4.260   1.00 35.01  ? 32  SER J O   1 
ATOM   15351 C CB  . SER J  1 40  ? 30.184  45.007  4.151   1.00 38.03  ? 32  SER J CB  1 
ATOM   15352 O OG  . SER J  1 40  ? 30.927  44.498  5.238   1.00 43.43  ? 32  SER J OG  1 
ATOM   15353 N N   . LEU J  1 41  ? 30.019  42.259  2.075   1.00 39.23  ? 33  LEU J N   1 
ATOM   15354 C CA  . LEU J  1 41  ? 30.761  41.063  1.703   1.00 34.92  ? 33  LEU J CA  1 
ATOM   15355 C C   . LEU J  1 41  ? 32.249  41.380  1.597   1.00 33.96  ? 33  LEU J C   1 
ATOM   15356 O O   . LEU J  1 41  ? 32.629  42.430  1.101   1.00 36.99  ? 33  LEU J O   1 
ATOM   15357 C CB  . LEU J  1 41  ? 30.246  40.501  0.382   1.00 31.58  ? 33  LEU J CB  1 
ATOM   15358 C CG  . LEU J  1 41  ? 28.728  40.346  0.281   1.00 34.46  ? 33  LEU J CG  1 
ATOM   15359 C CD1 . LEU J  1 41  ? 28.355  39.613  -0.996  1.00 30.75  ? 33  LEU J CD1 1 
ATOM   15360 C CD2 . LEU J  1 41  ? 28.163  39.633  1.511   1.00 34.87  ? 33  LEU J CD2 1 
ATOM   15361 N N   . LYS J  1 42  ? 33.085  40.483  2.102   1.00 33.13  ? 34  LYS J N   1 
ATOM   15362 C CA  . LYS J  1 42  ? 34.514  40.598  1.909   1.00 28.92  ? 34  LYS J CA  1 
ATOM   15363 C C   . LYS J  1 42  ? 34.915  39.396  1.083   1.00 28.96  ? 34  LYS J C   1 
ATOM   15364 O O   . LYS J  1 42  ? 34.847  38.261  1.546   1.00 24.58  ? 34  LYS J O   1 
ATOM   15365 C CB  . LYS J  1 42  ? 35.273  40.607  3.237   1.00 31.10  ? 34  LYS J CB  1 
ATOM   15366 C CG  . LYS J  1 42  ? 34.792  41.640  4.252   1.00 45.21  ? 34  LYS J CG  1 
ATOM   15367 C CD  . LYS J  1 42  ? 34.834  43.078  3.727   1.00 46.75  ? 34  LYS J CD  1 
ATOM   15368 C CE  . LYS J  1 42  ? 34.452  44.071  4.837   1.00 41.38  ? 34  LYS J CE  1 
ATOM   15369 N NZ  . LYS J  1 42  ? 34.355  45.488  4.369   1.00 48.24  ? 34  LYS J NZ  1 
ATOM   15370 N N   . PHE J  1 43  ? 35.322  39.649  -0.155  1.00 31.52  ? 35  PHE J N   1 
ATOM   15371 C CA  . PHE J  1 43  ? 35.627  38.570  -1.072  1.00 26.53  ? 35  PHE J CA  1 
ATOM   15372 C C   . PHE J  1 43  ? 36.979  37.942  -0.768  1.00 27.52  ? 35  PHE J C   1 
ATOM   15373 O O   . PHE J  1 43  ? 37.940  38.635  -0.438  1.00 31.05  ? 35  PHE J O   1 
ATOM   15374 C CB  . PHE J  1 43  ? 35.512  39.049  -2.516  1.00 29.46  ? 35  PHE J CB  1 
ATOM   15375 C CG  . PHE J  1 43  ? 34.099  39.309  -2.942  1.00 24.75  ? 35  PHE J CG  1 
ATOM   15376 C CD1 . PHE J  1 43  ? 33.524  40.553  -2.758  1.00 25.26  ? 35  PHE J CD1 1 
ATOM   15377 C CD2 . PHE J  1 43  ? 33.334  38.297  -3.498  1.00 21.98  ? 35  PHE J CD2 1 
ATOM   15378 C CE1 . PHE J  1 43  ? 32.214  40.788  -3.136  1.00 28.26  ? 35  PHE J CE1 1 
ATOM   15379 C CE2 . PHE J  1 43  ? 32.029  38.527  -3.874  1.00 23.38  ? 35  PHE J CE2 1 
ATOM   15380 C CZ  . PHE J  1 43  ? 31.468  39.779  -3.694  1.00 22.73  ? 35  PHE J CZ  1 
ATOM   15381 N N   . ILE J  1 44  ? 37.016  36.617  -0.862  1.00 24.98  ? 36  ILE J N   1 
ATOM   15382 C CA  . ILE J  1 44  ? 38.145  35.818  -0.432  1.00 26.37  ? 36  ILE J CA  1 
ATOM   15383 C C   . ILE J  1 44  ? 38.641  35.014  -1.622  1.00 34.81  ? 36  ILE J C   1 
ATOM   15384 O O   . ILE J  1 44  ? 39.844  34.762  -1.755  1.00 40.24  ? 36  ILE J O   1 
ATOM   15385 C CB  . ILE J  1 44  ? 37.737  34.837  0.684   1.00 28.71  ? 36  ILE J CB  1 
ATOM   15386 C CG1 . ILE J  1 44  ? 37.197  35.594  1.905   1.00 28.83  ? 36  ILE J CG1 1 
ATOM   15387 C CG2 . ILE J  1 44  ? 38.908  33.949  1.079   1.00 27.02  ? 36  ILE J CG2 1 
ATOM   15388 C CD1 . ILE J  1 44  ? 38.274  36.151  2.819   1.00 33.39  ? 36  ILE J CD1 1 
ATOM   15389 N N   . ASN J  1 45  ? 37.719  34.616  -2.495  1.00 28.32  ? 37  ASN J N   1 
ATOM   15390 C CA  . ASN J  1 45  ? 38.113  33.862  -3.679  1.00 28.65  ? 37  ASN J CA  1 
ATOM   15391 C C   . ASN J  1 45  ? 37.117  33.834  -4.836  1.00 30.61  ? 37  ASN J C   1 
ATOM   15392 O O   . ASN J  1 45  ? 35.911  33.987  -4.646  1.00 24.18  ? 37  ASN J O   1 
ATOM   15393 C CB  . ASN J  1 45  ? 38.518  32.439  -3.302  1.00 26.28  ? 37  ASN J CB  1 
ATOM   15394 C CG  . ASN J  1 45  ? 39.800  32.019  -3.970  1.00 32.48  ? 37  ASN J CG  1 
ATOM   15395 O OD1 . ASN J  1 45  ? 40.078  32.423  -5.100  1.00 28.37  ? 37  ASN J OD1 1 
ATOM   15396 N ND2 . ASN J  1 45  ? 40.602  31.223  -3.271  1.00 33.84  ? 37  ASN J ND2 1 
ATOM   15397 N N   . ILE J  1 46  ? 37.648  33.653  -6.045  1.00 31.52  ? 38  ILE J N   1 
ATOM   15398 C CA  . ILE J  1 46  ? 36.827  33.384  -7.217  1.00 23.50  ? 38  ILE J CA  1 
ATOM   15399 C C   . ILE J  1 46  ? 37.374  32.126  -7.877  1.00 25.42  ? 38  ILE J C   1 
ATOM   15400 O O   . ILE J  1 46  ? 38.444  32.152  -8.476  1.00 35.00  ? 38  ILE J O   1 
ATOM   15401 C CB  . ILE J  1 46  ? 36.836  34.559  -8.193  1.00 23.67  ? 38  ILE J CB  1 
ATOM   15402 C CG1 . ILE J  1 46  ? 36.571  35.867  -7.446  1.00 24.27  ? 38  ILE J CG1 1 
ATOM   15403 C CG2 . ILE J  1 46  ? 35.803  34.341  -9.270  1.00 28.83  ? 38  ILE J CG2 1 
ATOM   15404 C CD1 . ILE J  1 46  ? 36.389  37.077  -8.318  1.00 20.92  ? 38  ILE J CD1 1 
ATOM   15405 N N   . LEU J  1 47  ? 36.644  31.023  -7.755  1.00 26.02  ? 39  LEU J N   1 
ATOM   15406 C CA  . LEU J  1 47  ? 37.175  29.696  -8.066  1.00 26.13  ? 39  LEU J CA  1 
ATOM   15407 C C   . LEU J  1 47  ? 36.807  29.209  -9.463  1.00 28.60  ? 39  LEU J C   1 
ATOM   15408 O O   . LEU J  1 47  ? 37.299  28.172  -9.922  1.00 27.91  ? 39  LEU J O   1 
ATOM   15409 C CB  . LEU J  1 47  ? 36.648  28.667  -7.056  1.00 28.60  ? 39  LEU J CB  1 
ATOM   15410 C CG  . LEU J  1 47  ? 36.622  29.007  -5.566  1.00 26.53  ? 39  LEU J CG  1 
ATOM   15411 C CD1 . LEU J  1 47  ? 35.740  28.011  -4.823  1.00 25.38  ? 39  LEU J CD1 1 
ATOM   15412 C CD2 . LEU J  1 47  ? 38.029  29.001  -5.003  1.00 27.01  ? 39  LEU J CD2 1 
ATOM   15413 N N   . GLU J  1 48  ? 35.837  29.878  -10.053 1.00 27.79  ? 40  GLU J N   1 
ATOM   15414 C CA  . GLU J  1 48  ? 35.400  29.521  -11.373 1.00 31.38  ? 40  GLU J CA  1 
ATOM   15415 C C   . GLU J  1 48  ? 34.786  30.739  -12.002 1.00 33.08  ? 40  GLU J C   1 
ATOM   15416 O O   . GLU J  1 48  ? 34.297  31.639  -11.320 1.00 32.36  ? 40  GLU J O   1 
ATOM   15417 C CB  . GLU J  1 48  ? 34.376  28.386  -11.311 1.00 32.82  ? 40  GLU J CB  1 
ATOM   15418 C CG  . GLU J  1 48  ? 34.693  27.213  -12.223 1.00 36.25  ? 40  GLU J CG  1 
ATOM   15419 C CD  . GLU J  1 48  ? 33.909  25.966  -11.863 1.00 54.81  ? 40  GLU J CD  1 
ATOM   15420 O OE1 . GLU J  1 48  ? 33.311  25.934  -10.767 1.00 57.50  ? 40  GLU J OE1 1 
ATOM   15421 O OE2 . GLU J  1 48  ? 33.890  25.019  -12.676 1.00 55.01  ? 40  GLU J OE2 1 
ATOM   15422 N N   . VAL J  1 49  ? 34.803  30.746  -13.319 1.00 31.61  ? 41  VAL J N   1 
ATOM   15423 C CA  . VAL J  1 49  ? 34.049  31.710  -14.084 1.00 34.91  ? 41  VAL J CA  1 
ATOM   15424 C C   . VAL J  1 49  ? 33.712  31.051  -15.413 1.00 38.75  ? 41  VAL J C   1 
ATOM   15425 O O   . VAL J  1 49  ? 34.548  30.377  -16.011 1.00 38.47  ? 41  VAL J O   1 
ATOM   15426 C CB  . VAL J  1 49  ? 34.848  33.021  -14.264 1.00 39.95  ? 41  VAL J CB  1 
ATOM   15427 C CG1 . VAL J  1 49  ? 34.166  33.946  -15.249 1.00 41.47  ? 41  VAL J CG1 1 
ATOM   15428 C CG2 . VAL J  1 49  ? 35.037  33.725  -12.916 1.00 33.11  ? 41  VAL J CG2 1 
ATOM   15429 N N   . ASN J  1 50  ? 32.467  31.194  -15.845 1.00 39.76  ? 42  ASN J N   1 
ATOM   15430 C CA  . ASN J  1 50  ? 32.047  30.629  -17.117 1.00 43.36  ? 42  ASN J CA  1 
ATOM   15431 C C   . ASN J  1 50  ? 31.484  31.712  -18.035 1.00 48.34  ? 42  ASN J C   1 
ATOM   15432 O O   . ASN J  1 50  ? 30.413  32.252  -17.773 1.00 46.67  ? 42  ASN J O   1 
ATOM   15433 C CB  . ASN J  1 50  ? 31.013  29.521  -16.902 1.00 43.38  ? 42  ASN J CB  1 
ATOM   15434 C CG  . ASN J  1 50  ? 31.069  28.459  -17.985 1.00 45.88  ? 42  ASN J CG  1 
ATOM   15435 O OD1 . ASN J  1 50  ? 31.684  28.665  -19.029 1.00 53.06  ? 42  ASN J OD1 1 
ATOM   15436 N ND2 . ASN J  1 50  ? 30.431  27.315  -17.740 1.00 43.97  ? 42  ASN J ND2 1 
ATOM   15437 N N   . GLU J  1 51  ? 32.220  32.036  -19.098 1.00 55.62  ? 43  GLU J N   1 
ATOM   15438 C CA  . GLU J  1 51  ? 31.763  33.005  -20.090 1.00 54.13  ? 43  GLU J CA  1 
ATOM   15439 C C   . GLU J  1 51  ? 30.650  32.370  -20.920 1.00 51.28  ? 43  GLU J C   1 
ATOM   15440 O O   . GLU J  1 51  ? 29.763  33.063  -21.427 1.00 46.42  ? 43  GLU J O   1 
ATOM   15441 C CB  . GLU J  1 51  ? 32.931  33.478  -20.970 1.00 66.42  ? 43  GLU J CB  1 
ATOM   15442 C CG  . GLU J  1 51  ? 32.652  34.743  -21.801 1.00 74.35  ? 43  GLU J CG  1 
ATOM   15443 C CD  . GLU J  1 51  ? 33.829  35.148  -22.692 1.00 78.15  ? 43  GLU J CD  1 
ATOM   15444 O OE1 . GLU J  1 51  ? 34.977  35.175  -22.190 1.00 72.53  ? 43  GLU J OE1 1 
ATOM   15445 O OE2 . GLU J  1 51  ? 33.601  35.432  -23.893 1.00 71.02  ? 43  GLU J OE2 1 
ATOM   15446 N N   . ILE J  1 52  ? 30.704  31.042  -21.026 1.00 47.15  ? 44  ILE J N   1 
ATOM   15447 C CA  . ILE J  1 52  ? 29.669  30.249  -21.686 1.00 48.07  ? 44  ILE J CA  1 
ATOM   15448 C C   . ILE J  1 52  ? 28.327  30.351  -20.950 1.00 50.40  ? 44  ILE J C   1 
ATOM   15449 O O   . ILE J  1 52  ? 27.372  30.942  -21.461 1.00 53.65  ? 44  ILE J O   1 
ATOM   15450 C CB  . ILE J  1 52  ? 30.089  28.750  -21.794 1.00 51.49  ? 44  ILE J CB  1 
ATOM   15451 C CG1 . ILE J  1 52  ? 31.299  28.572  -22.724 1.00 53.22  ? 44  ILE J CG1 1 
ATOM   15452 C CG2 . ILE J  1 52  ? 28.922  27.872  -22.245 1.00 55.46  ? 44  ILE J CG2 1 
ATOM   15453 C CD1 . ILE J  1 52  ? 31.065  28.994  -24.186 1.00 47.35  ? 44  ILE J CD1 1 
ATOM   15454 N N   . THR J  1 53  ? 28.261  29.788  -19.745 1.00 47.64  ? 45  THR J N   1 
ATOM   15455 C CA  . THR J  1 53  ? 26.990  29.665  -19.031 1.00 46.24  ? 45  THR J CA  1 
ATOM   15456 C C   . THR J  1 53  ? 26.613  30.879  -18.182 1.00 38.23  ? 45  THR J C   1 
ATOM   15457 O O   . THR J  1 53  ? 25.481  30.979  -17.736 1.00 35.17  ? 45  THR J O   1 
ATOM   15458 C CB  . THR J  1 53  ? 26.927  28.380  -18.162 1.00 46.74  ? 45  THR J CB  1 
ATOM   15459 O OG1 . THR J  1 53  ? 27.918  28.435  -17.126 1.00 49.56  ? 45  THR J OG1 1 
ATOM   15460 C CG2 . THR J  1 53  ? 27.150  27.142  -19.017 1.00 46.70  ? 45  THR J CG2 1 
ATOM   15461 N N   . ASN J  1 54  ? 27.551  31.803  -17.993 1.00 42.67  ? 46  ASN J N   1 
ATOM   15462 C CA  . ASN J  1 54  ? 27.354  32.967  -17.125 1.00 43.29  ? 46  ASN J CA  1 
ATOM   15463 C C   . ASN J  1 54  ? 27.195  32.555  -15.666 1.00 44.82  ? 46  ASN J C   1 
ATOM   15464 O O   . ASN J  1 54  ? 26.218  32.905  -14.993 1.00 39.64  ? 46  ASN J O   1 
ATOM   15465 C CB  . ASN J  1 54  ? 26.185  33.839  -17.592 1.00 42.63  ? 46  ASN J CB  1 
ATOM   15466 C CG  . ASN J  1 54  ? 26.613  34.918  -18.565 1.00 42.35  ? 46  ASN J CG  1 
ATOM   15467 O OD1 . ASN J  1 54  ? 27.686  35.512  -18.428 1.00 43.57  ? 46  ASN J OD1 1 
ATOM   15468 N ND2 . ASN J  1 54  ? 25.770  35.185  -19.551 1.00 40.31  ? 46  ASN J ND2 1 
ATOM   15469 N N   . GLU J  1 55  ? 28.177  31.800  -15.191 1.00 45.58  ? 47  GLU J N   1 
ATOM   15470 C CA  . GLU J  1 55  ? 28.157  31.267  -13.843 1.00 44.57  ? 47  GLU J CA  1 
ATOM   15471 C C   . GLU J  1 55  ? 29.467  31.569  -13.139 1.00 38.92  ? 47  GLU J C   1 
ATOM   15472 O O   . GLU J  1 55  ? 30.529  31.176  -13.610 1.00 42.15  ? 47  GLU J O   1 
ATOM   15473 C CB  . GLU J  1 55  ? 27.962  29.753  -13.877 1.00 42.20  ? 47  GLU J CB  1 
ATOM   15474 C CG  . GLU J  1 55  ? 26.591  29.288  -14.311 1.00 40.30  ? 47  GLU J CG  1 
ATOM   15475 C CD  . GLU J  1 55  ? 26.426  27.787  -14.139 1.00 52.06  ? 47  GLU J CD  1 
ATOM   15476 O OE1 . GLU J  1 55  ? 25.278  27.320  -14.007 1.00 49.48  ? 47  GLU J OE1 1 
ATOM   15477 O OE2 . GLU J  1 55  ? 27.451  27.070  -14.127 1.00 63.55  ? 47  GLU J OE2 1 
ATOM   15478 N N   . VAL J  1 56  ? 29.388  32.262  -12.011 1.00 32.29  ? 48  VAL J N   1 
ATOM   15479 C CA  . VAL J  1 56  ? 30.555  32.463  -11.165 1.00 29.59  ? 48  VAL J CA  1 
ATOM   15480 C C   . VAL J  1 56  ? 30.403  31.639  -9.871  1.00 30.53  ? 48  VAL J C   1 
ATOM   15481 O O   . VAL J  1 56  ? 29.301  31.483  -9.360  1.00 27.98  ? 48  VAL J O   1 
ATOM   15482 C CB  . VAL J  1 56  ? 30.761  33.957  -10.869 1.00 24.27  ? 48  VAL J CB  1 
ATOM   15483 C CG1 . VAL J  1 56  ? 29.554  34.517  -10.158 1.00 28.98  ? 48  VAL J CG1 1 
ATOM   15484 C CG2 . VAL J  1 56  ? 32.015  34.178  -10.057 1.00 23.74  ? 48  VAL J CG2 1 
ATOM   15485 N N   . ASP J  1 57  ? 31.502  31.071  -9.385  1.00 26.99  ? 49  ASP J N   1 
ATOM   15486 C CA  . ASP J  1 57  ? 31.508  30.307  -8.151  1.00 21.89  ? 49  ASP J CA  1 
ATOM   15487 C C   . ASP J  1 57  ? 32.449  31.051  -7.223  1.00 26.27  ? 49  ASP J C   1 
ATOM   15488 O O   . ASP J  1 57  ? 33.653  31.040  -7.441  1.00 28.64  ? 49  ASP J O   1 
ATOM   15489 C CB  . ASP J  1 57  ? 32.021  28.882  -8.397  1.00 27.74  ? 49  ASP J CB  1 
ATOM   15490 C CG  . ASP J  1 57  ? 31.765  27.937  -7.209  1.00 34.46  ? 49  ASP J CG  1 
ATOM   15491 O OD1 . ASP J  1 57  ? 30.656  27.968  -6.647  1.00 37.03  ? 49  ASP J OD1 1 
ATOM   15492 O OD2 . ASP J  1 57  ? 32.661  27.148  -6.836  1.00 33.45  ? 49  ASP J OD2 1 
ATOM   15493 N N   . VAL J  1 58  ? 31.908  31.718  -6.206  1.00 25.15  ? 50  VAL J N   1 
ATOM   15494 C CA  . VAL J  1 58  ? 32.731  32.543  -5.324  1.00 23.79  ? 50  VAL J CA  1 
ATOM   15495 C C   . VAL J  1 58  ? 32.734  32.129  -3.852  1.00 24.74  ? 50  VAL J C   1 
ATOM   15496 O O   . VAL J  1 58  ? 31.886  31.374  -3.401  1.00 24.61  ? 50  VAL J O   1 
ATOM   15497 C CB  . VAL J  1 58  ? 32.328  34.005  -5.395  1.00 22.86  ? 50  VAL J CB  1 
ATOM   15498 C CG1 . VAL J  1 58  ? 32.849  34.612  -6.661  1.00 29.52  ? 50  VAL J CG1 1 
ATOM   15499 C CG2 . VAL J  1 58  ? 30.835  34.121  -5.343  1.00 29.47  ? 50  VAL J CG2 1 
ATOM   15500 N N   . VAL J  1 59  ? 33.718  32.642  -3.123  1.00 24.16  ? 51  VAL J N   1 
ATOM   15501 C CA  . VAL J  1 59  ? 33.873  32.394  -1.704  1.00 21.89  ? 51  VAL J CA  1 
ATOM   15502 C C   . VAL J  1 59  ? 33.974  33.752  -1.041  1.00 24.16  ? 51  VAL J C   1 
ATOM   15503 O O   . VAL J  1 59  ? 34.822  34.561  -1.401  1.00 24.27  ? 51  VAL J O   1 
ATOM   15504 C CB  . VAL J  1 59  ? 35.154  31.590  -1.395  1.00 17.40  ? 51  VAL J CB  1 
ATOM   15505 C CG1 . VAL J  1 59  ? 35.493  31.684  0.088   1.00 19.39  ? 51  VAL J CG1 1 
ATOM   15506 C CG2 . VAL J  1 59  ? 35.004  30.143  -1.842  1.00 13.09  ? 51  VAL J CG2 1 
ATOM   15507 N N   . PHE J  1 60  ? 33.100  34.021  -0.082  1.00 25.23  ? 52  PHE J N   1 
ATOM   15508 C CA  . PHE J  1 60  ? 33.087  35.337  0.525   1.00 24.06  ? 52  PHE J CA  1 
ATOM   15509 C C   . PHE J  1 60  ? 32.693  35.285  1.984   1.00 23.42  ? 52  PHE J C   1 
ATOM   15510 O O   . PHE J  1 60  ? 32.029  34.353  2.417   1.00 22.76  ? 52  PHE J O   1 
ATOM   15511 C CB  . PHE J  1 60  ? 32.142  36.262  -0.242  1.00 25.69  ? 52  PHE J CB  1 
ATOM   15512 C CG  . PHE J  1 60  ? 30.724  35.778  -0.292  1.00 22.61  ? 52  PHE J CG  1 
ATOM   15513 C CD1 . PHE J  1 60  ? 29.803  36.181  0.666   1.00 28.91  ? 52  PHE J CD1 1 
ATOM   15514 C CD2 . PHE J  1 60  ? 30.301  34.938  -1.301  1.00 20.49  ? 52  PHE J CD2 1 
ATOM   15515 C CE1 . PHE J  1 60  ? 28.477  35.745  0.618   1.00 25.50  ? 52  PHE J CE1 1 
ATOM   15516 C CE2 . PHE J  1 60  ? 28.982  34.498  -1.353  1.00 27.37  ? 52  PHE J CE2 1 
ATOM   15517 C CZ  . PHE J  1 60  ? 28.069  34.901  -0.388  1.00 21.20  ? 52  PHE J CZ  1 
ATOM   15518 N N   . TRP J  1 61  ? 33.123  36.298  2.729   1.00 25.77  ? 53  TRP J N   1 
ATOM   15519 C CA  . TRP J  1 61  ? 32.740  36.483  4.117   1.00 22.60  ? 53  TRP J CA  1 
ATOM   15520 C C   . TRP J  1 61  ? 31.580  37.449  4.159   1.00 30.60  ? 53  TRP J C   1 
ATOM   15521 O O   . TRP J  1 61  ? 31.677  38.577  3.660   1.00 30.21  ? 53  TRP J O   1 
ATOM   15522 C CB  . TRP J  1 61  ? 33.905  37.037  4.938   1.00 23.03  ? 53  TRP J CB  1 
ATOM   15523 C CG  . TRP J  1 61  ? 34.959  36.027  5.159   1.00 24.81  ? 53  TRP J CG  1 
ATOM   15524 C CD1 . TRP J  1 61  ? 34.880  34.692  4.875   1.00 26.99  ? 53  TRP J CD1 1 
ATOM   15525 C CD2 . TRP J  1 61  ? 36.266  36.247  5.700   1.00 30.08  ? 53  TRP J CD2 1 
ATOM   15526 N NE1 . TRP J  1 61  ? 36.058  34.063  5.211   1.00 31.85  ? 53  TRP J NE1 1 
ATOM   15527 C CE2 . TRP J  1 61  ? 36.926  34.993  5.722   1.00 32.81  ? 53  TRP J CE2 1 
ATOM   15528 C CE3 . TRP J  1 61  ? 36.946  37.378  6.171   1.00 34.16  ? 53  TRP J CE3 1 
ATOM   15529 C CZ2 . TRP J  1 61  ? 38.232  34.839  6.198   1.00 31.59  ? 53  TRP J CZ2 1 
ATOM   15530 C CZ3 . TRP J  1 61  ? 38.242  37.222  6.644   1.00 38.84  ? 53  TRP J CZ3 1 
ATOM   15531 C CH2 . TRP J  1 61  ? 38.871  35.958  6.654   1.00 34.99  ? 53  TRP J CH2 1 
ATOM   15532 N N   . GLN J  1 62  ? 30.479  36.999  4.750   1.00 25.84  ? 54  GLN J N   1 
ATOM   15533 C CA  . GLN J  1 62  ? 29.282  37.817  4.856   1.00 27.70  ? 54  GLN J CA  1 
ATOM   15534 C C   . GLN J  1 62  ? 29.218  38.453  6.254   1.00 33.92  ? 54  GLN J C   1 
ATOM   15535 O O   . GLN J  1 62  ? 28.694  37.850  7.193   1.00 27.63  ? 54  GLN J O   1 
ATOM   15536 C CB  . GLN J  1 62  ? 28.052  36.947  4.586   1.00 26.77  ? 54  GLN J CB  1 
ATOM   15537 C CG  . GLN J  1 62  ? 26.726  37.669  4.508   1.00 25.01  ? 54  GLN J CG  1 
ATOM   15538 C CD  . GLN J  1 62  ? 25.566  36.702  4.344   1.00 29.63  ? 54  GLN J CD  1 
ATOM   15539 O OE1 . GLN J  1 62  ? 24.716  36.571  5.233   1.00 37.86  ? 54  GLN J OE1 1 
ATOM   15540 N NE2 . GLN J  1 62  ? 25.525  36.017  3.208   1.00 26.07  ? 54  GLN J NE2 1 
ATOM   15541 N N   . GLN J  1 63  ? 29.768  39.661  6.388   1.00 33.39  ? 55  GLN J N   1 
ATOM   15542 C CA  . GLN J  1 63  ? 29.726  40.372  7.655   1.00 24.75  ? 55  GLN J CA  1 
ATOM   15543 C C   . GLN J  1 63  ? 28.346  40.905  7.896   1.00 27.85  ? 55  GLN J C   1 
ATOM   15544 O O   . GLN J  1 63  ? 27.861  41.764  7.163   1.00 29.26  ? 55  GLN J O   1 
ATOM   15545 C CB  . GLN J  1 63  ? 30.710  41.526  7.687   1.00 34.04  ? 55  GLN J CB  1 
ATOM   15546 C CG  . GLN J  1 63  ? 32.144  41.078  7.539   1.00 49.87  ? 55  GLN J CG  1 
ATOM   15547 C CD  . GLN J  1 63  ? 33.139  42.187  7.797   1.00 58.00  ? 55  GLN J CD  1 
ATOM   15548 O OE1 . GLN J  1 63  ? 32.762  43.311  8.154   1.00 60.30  ? 55  GLN J OE1 1 
ATOM   15549 N NE2 . GLN J  1 63  ? 34.423  41.879  7.617   1.00 58.53  ? 55  GLN J NE2 1 
ATOM   15550 N N   . THR J  1 64  ? 27.724  40.388  8.947   1.00 23.58  ? 56  THR J N   1 
ATOM   15551 C CA  . THR J  1 64  ? 26.385  40.777  9.314   1.00 21.01  ? 56  THR J CA  1 
ATOM   15552 C C   . THR J  1 64  ? 26.405  41.223  10.768  1.00 22.48  ? 56  THR J C   1 
ATOM   15553 O O   . THR J  1 64  ? 26.965  40.534  11.629  1.00 20.35  ? 56  THR J O   1 
ATOM   15554 C CB  . THR J  1 64  ? 25.429  39.598  9.147   1.00 21.95  ? 56  THR J CB  1 
ATOM   15555 O OG1 . THR J  1 64  ? 25.973  38.676  8.194   1.00 29.00  ? 56  THR J OG1 1 
ATOM   15556 C CG2 . THR J  1 64  ? 24.062  40.074  8.671   1.00 20.35  ? 56  THR J CG2 1 
ATOM   15557 N N   . THR J  1 65  ? 25.820  42.390  11.034  1.00 19.37  ? 57  THR J N   1 
ATOM   15558 C CA  . THR J  1 65  ? 25.773  42.944  12.380  1.00 19.67  ? 57  THR J CA  1 
ATOM   15559 C C   . THR J  1 65  ? 24.430  43.615  12.596  1.00 22.60  ? 57  THR J C   1 
ATOM   15560 O O   . THR J  1 65  ? 23.825  44.111  11.647  1.00 23.23  ? 57  THR J O   1 
ATOM   15561 C CB  . THR J  1 65  ? 26.891  43.981  12.637  1.00 21.24  ? 57  THR J CB  1 
ATOM   15562 O OG1 . THR J  1 65  ? 26.691  45.130  11.801  1.00 26.78  ? 57  THR J OG1 1 
ATOM   15563 C CG2 . THR J  1 65  ? 28.254  43.390  12.360  1.00 19.60  ? 57  THR J CG2 1 
ATOM   15564 N N   . TRP J  1 66  ? 23.967  43.613  13.845  1.00 20.17  ? 58  TRP J N   1 
ATOM   15565 C CA  . TRP J  1 66  ? 22.683  44.211  14.209  1.00 22.97  ? 58  TRP J CA  1 
ATOM   15566 C C   . TRP J  1 66  ? 22.566  44.320  15.721  1.00 23.20  ? 58  TRP J C   1 
ATOM   15567 O O   . TRP J  1 66  ? 23.348  43.730  16.468  1.00 25.18  ? 58  TRP J O   1 
ATOM   15568 C CB  . TRP J  1 66  ? 21.507  43.396  13.661  1.00 21.47  ? 58  TRP J CB  1 
ATOM   15569 C CG  . TRP J  1 66  ? 21.431  41.991  14.209  1.00 23.74  ? 58  TRP J CG  1 
ATOM   15570 C CD1 . TRP J  1 66  ? 20.739  41.585  15.301  1.00 19.55  ? 58  TRP J CD1 1 
ATOM   15571 C CD2 . TRP J  1 66  ? 22.073  40.814  13.682  1.00 24.04  ? 58  TRP J CD2 1 
ATOM   15572 N NE1 . TRP J  1 66  ? 20.906  40.237  15.497  1.00 17.43  ? 58  TRP J NE1 1 
ATOM   15573 C CE2 . TRP J  1 66  ? 21.720  39.737  14.522  1.00 17.80  ? 58  TRP J CE2 1 
ATOM   15574 C CE3 . TRP J  1 66  ? 22.907  40.570  12.582  1.00 19.71  ? 58  TRP J CE3 1 
ATOM   15575 C CZ2 . TRP J  1 66  ? 22.168  38.436  14.305  1.00 17.19  ? 58  TRP J CZ2 1 
ATOM   15576 C CZ3 . TRP J  1 66  ? 23.358  39.277  12.366  1.00 18.89  ? 58  TRP J CZ3 1 
ATOM   15577 C CH2 . TRP J  1 66  ? 22.983  38.225  13.223  1.00 22.63  ? 58  TRP J CH2 1 
ATOM   15578 N N   . SER J  1 67  ? 21.585  45.077  16.176  1.00 23.55  ? 59  SER J N   1 
ATOM   15579 C CA  . SER J  1 67  ? 21.394  45.209  17.602  1.00 28.10  ? 59  SER J CA  1 
ATOM   15580 C C   . SER J  1 67  ? 20.116  44.578  18.133  1.00 29.07  ? 59  SER J C   1 
ATOM   15581 O O   . SER J  1 67  ? 19.044  44.695  17.527  1.00 25.78  ? 59  SER J O   1 
ATOM   15582 C CB  . SER J  1 67  ? 21.498  46.666  18.023  1.00 27.04  ? 59  SER J CB  1 
ATOM   15583 O OG  . SER J  1 67  ? 22.863  46.974  18.224  1.00 36.33  ? 59  SER J OG  1 
ATOM   15584 N N   . ASP J  1 68  ? 20.283  43.886  19.264  1.00 32.28  ? 60  ASP J N   1 
ATOM   15585 C CA  . ASP J  1 68  ? 19.205  43.392  20.125  1.00 32.41  ? 60  ASP J CA  1 
ATOM   15586 C C   . ASP J  1 68  ? 19.537  43.847  21.551  1.00 26.79  ? 60  ASP J C   1 
ATOM   15587 O O   . ASP J  1 68  ? 20.212  43.135  22.305  1.00 20.87  ? 60  ASP J O   1 
ATOM   15588 C CB  . ASP J  1 68  ? 19.132  41.860  20.075  1.00 30.62  ? 60  ASP J CB  1 
ATOM   15589 C CG  . ASP J  1 68  ? 17.841  41.307  20.674  1.00 31.50  ? 60  ASP J CG  1 
ATOM   15590 O OD1 . ASP J  1 68  ? 17.130  42.067  21.377  1.00 29.53  ? 60  ASP J OD1 1 
ATOM   15591 O OD2 . ASP J  1 68  ? 17.541  40.109  20.437  1.00 26.47  ? 60  ASP J OD2 1 
ATOM   15592 N N   . ARG J  1 69  ? 19.077  45.043  21.905  1.00 31.65  ? 61  ARG J N   1 
ATOM   15593 C CA  . ARG J  1 69  ? 19.430  45.651  23.184  1.00 27.91  ? 61  ARG J CA  1 
ATOM   15594 C C   . ARG J  1 69  ? 18.918  44.845  24.375  1.00 21.77  ? 61  ARG J C   1 
ATOM   15595 O O   . ARG J  1 69  ? 19.469  44.949  25.465  1.00 19.78  ? 61  ARG J O   1 
ATOM   15596 C CB  . ARG J  1 69  ? 18.948  47.108  23.268  1.00 30.18  ? 61  ARG J CB  1 
ATOM   15597 C CG  . ARG J  1 69  ? 19.898  48.162  22.671  1.00 37.84  ? 61  ARG J CG  1 
ATOM   15598 C CD  . ARG J  1 69  ? 19.094  49.328  22.056  1.00 44.13  ? 61  ARG J CD  1 
ATOM   15599 N NE  . ARG J  1 69  ? 19.672  50.654  22.290  1.00 50.85  ? 61  ARG J NE  1 
ATOM   15600 C CZ  . ARG J  1 69  ? 19.067  51.800  21.973  1.00 55.26  ? 61  ARG J CZ  1 
ATOM   15601 N NH1 . ARG J  1 69  ? 17.861  51.778  21.410  1.00 54.74  ? 61  ARG J NH1 1 
ATOM   15602 N NH2 . ARG J  1 69  ? 19.660  52.969  22.220  1.00 40.03  ? 61  ARG J NH2 1 
ATOM   15603 N N   . THR J  1 70  ? 17.891  44.024  24.176  1.00 18.45  ? 62  THR J N   1 
ATOM   15604 C CA  . THR J  1 70  ? 17.388  43.218  25.286  1.00 19.31  ? 62  THR J CA  1 
ATOM   15605 C C   . THR J  1 70  ? 18.365  42.112  25.698  1.00 18.95  ? 62  THR J C   1 
ATOM   15606 O O   . THR J  1 70  ? 18.173  41.459  26.720  1.00 24.37  ? 62  THR J O   1 
ATOM   15607 C CB  . THR J  1 70  ? 15.974  42.619  25.020  1.00 20.93  ? 62  THR J CB  1 
ATOM   15608 O OG1 . THR J  1 70  ? 16.066  41.521  24.103  1.00 26.09  ? 62  THR J OG1 1 
ATOM   15609 C CG2 . THR J  1 70  ? 15.011  43.681  24.477  1.00 12.30  ? 62  THR J CG2 1 
ATOM   15610 N N   . LEU J  1 71  ? 19.413  41.909  24.906  1.00 20.66  ? 63  LEU J N   1 
ATOM   15611 C CA  . LEU J  1 71  ? 20.450  40.926  25.220  1.00 18.92  ? 63  LEU J CA  1 
ATOM   15612 C C   . LEU J  1 71  ? 21.591  41.542  26.024  1.00 19.82  ? 63  LEU J C   1 
ATOM   15613 O O   . LEU J  1 71  ? 22.516  40.846  26.446  1.00 19.74  ? 63  LEU J O   1 
ATOM   15614 C CB  . LEU J  1 71  ? 21.021  40.333  23.939  1.00 17.56  ? 63  LEU J CB  1 
ATOM   15615 C CG  . LEU J  1 71  ? 20.056  39.553  23.049  1.00 22.90  ? 63  LEU J CG  1 
ATOM   15616 C CD1 . LEU J  1 71  ? 20.774  38.946  21.851  1.00 14.41  ? 63  LEU J CD1 1 
ATOM   15617 C CD2 . LEU J  1 71  ? 19.356  38.474  23.863  1.00 18.32  ? 63  LEU J CD2 1 
ATOM   15618 N N   . ALA J  1 72  ? 21.519  42.853  26.231  1.00 21.32  ? 64  ALA J N   1 
ATOM   15619 C CA  . ALA J  1 72  ? 22.618  43.597  26.838  1.00 22.70  ? 64  ALA J CA  1 
ATOM   15620 C C   . ALA J  1 72  ? 22.757  43.346  28.334  1.00 21.57  ? 64  ALA J C   1 
ATOM   15621 O O   . ALA J  1 72  ? 21.771  43.084  29.035  1.00 24.46  ? 64  ALA J O   1 
ATOM   15622 C CB  . ALA J  1 72  ? 22.472  45.102  26.557  1.00 19.90  ? 64  ALA J CB  1 
ATOM   15623 N N   . TRP J  1 73  ? 23.990  43.463  28.813  1.00 21.66  ? 65  TRP J N   1 
ATOM   15624 C CA  . TRP J  1 73  ? 24.304  43.287  30.222  1.00 22.64  ? 65  TRP J CA  1 
ATOM   15625 C C   . TRP J  1 73  ? 25.390  44.262  30.675  1.00 27.22  ? 65  TRP J C   1 
ATOM   15626 O O   . TRP J  1 73  ? 26.138  44.787  29.857  1.00 27.43  ? 65  TRP J O   1 
ATOM   15627 C CB  . TRP J  1 73  ? 24.714  41.827  30.508  1.00 24.44  ? 65  TRP J CB  1 
ATOM   15628 C CG  . TRP J  1 73  ? 26.102  41.401  30.059  1.00 22.02  ? 65  TRP J CG  1 
ATOM   15629 C CD1 . TRP J  1 73  ? 27.233  41.395  30.816  1.00 24.39  ? 65  TRP J CD1 1 
ATOM   15630 C CD2 . TRP J  1 73  ? 26.482  40.881  28.772  1.00 22.72  ? 65  TRP J CD2 1 
ATOM   15631 N NE1 . TRP J  1 73  ? 28.292  40.922  30.086  1.00 25.01  ? 65  TRP J NE1 1 
ATOM   15632 C CE2 . TRP J  1 73  ? 27.859  40.604  28.826  1.00 24.38  ? 65  TRP J CE2 1 
ATOM   15633 C CE3 . TRP J  1 73  ? 25.792  40.636  27.579  1.00 22.62  ? 65  TRP J CE3 1 
ATOM   15634 C CZ2 . TRP J  1 73  ? 28.565  40.093  27.733  1.00 25.83  ? 65  TRP J CZ2 1 
ATOM   15635 C CZ3 . TRP J  1 73  ? 26.489  40.128  26.500  1.00 21.28  ? 65  TRP J CZ3 1 
ATOM   15636 C CH2 . TRP J  1 73  ? 27.865  39.862  26.582  1.00 20.72  ? 65  TRP J CH2 1 
ATOM   15637 N N   . ASN J  1 74  ? 25.558  44.385  31.982  1.00 34.92  ? 66  ASN J N   1 
ATOM   15638 C CA  . ASN J  1 74  ? 26.674  45.096  32.565  1.00 30.63  ? 66  ASN J CA  1 
ATOM   15639 C C   . ASN J  1 74  ? 27.968  44.307  32.587  1.00 34.14  ? 66  ASN J C   1 
ATOM   15640 O O   . ASN J  1 74  ? 28.038  43.252  33.155  1.00 30.98  ? 66  ASN J O   1 
ATOM   15641 C CB  . ASN J  1 74  ? 26.308  45.528  33.966  1.00 35.40  ? 66  ASN J CB  1 
ATOM   15642 C CG  . ASN J  1 74  ? 27.273  46.527  34.532  1.00 46.55  ? 66  ASN J CG  1 
ATOM   15643 O OD1 . ASN J  1 74  ? 27.878  47.268  33.781  1.00 45.64  ? 66  ASN J OD1 1 
ATOM   15644 N ND2 . ASN J  1 74  ? 27.445  46.540  35.853  1.00 50.70  ? 66  ASN J ND2 1 
ATOM   15645 N N   . SER J  1 75  ? 29.005  44.878  31.992  1.00 36.27  ? 67  SER J N   1 
ATOM   15646 C CA  . SER J  1 75  ? 30.293  44.256  31.795  1.00 31.53  ? 67  SER J CA  1 
ATOM   15647 C C   . SER J  1 75  ? 31.358  44.931  32.592  1.00 38.47  ? 67  SER J C   1 
ATOM   15648 O O   . SER J  1 75  ? 32.491  44.904  32.262  1.00 39.59  ? 67  SER J O   1 
ATOM   15649 C CB  . SER J  1 75  ? 30.623  44.407  30.381  1.00 36.68  ? 67  SER J CB  1 
ATOM   15650 O OG  . SER J  1 75  ? 30.087  45.629  30.048  1.00 45.81  ? 67  SER J OG  1 
ATOM   15651 N N   . SER J  1 76  ? 30.969  45.583  33.660  1.00 49.58  ? 68  SER J N   1 
ATOM   15652 C CA  . SER J  1 76  ? 31.892  46.314  34.492  1.00 49.87  ? 68  SER J CA  1 
ATOM   15653 C C   . SER J  1 76  ? 32.866  45.348  35.022  1.00 51.45  ? 68  SER J C   1 
ATOM   15654 O O   . SER J  1 76  ? 34.016  45.657  35.210  1.00 53.02  ? 68  SER J O   1 
ATOM   15655 C CB  . SER J  1 76  ? 31.168  46.949  35.647  1.00 47.38  ? 68  SER J CB  1 
ATOM   15656 O OG  . SER J  1 76  ? 30.677  48.213  35.306  1.00 49.89  ? 68  SER J OG  1 
ATOM   15657 N N   . HIS J  1 77  ? 32.403  44.120  35.245  1.00 47.13  ? 69  HIS J N   1 
ATOM   15658 C CA  . HIS J  1 77  ? 33.260  43.061  35.773  1.00 43.84  ? 69  HIS J CA  1 
ATOM   15659 C C   . HIS J  1 77  ? 32.966  41.678  35.180  1.00 44.68  ? 69  HIS J C   1 
ATOM   15660 O O   . HIS J  1 77  ? 33.328  40.659  35.769  1.00 43.62  ? 69  HIS J O   1 
ATOM   15661 C CB  . HIS J  1 77  ? 33.157  43.006  37.300  1.00 53.74  ? 69  HIS J CB  1 
ATOM   15662 C CG  . HIS J  1 77  ? 33.266  44.344  37.962  1.00 61.90  ? 69  HIS J CG  1 
ATOM   15663 N ND1 . HIS J  1 77  ? 34.477  44.927  38.266  1.00 55.64  ? 69  HIS J ND1 1 
ATOM   15664 C CD2 . HIS J  1 77  ? 32.315  45.213  38.378  1.00 54.02  ? 69  HIS J CD2 1 
ATOM   15665 C CE1 . HIS J  1 77  ? 34.268  46.098  38.841  1.00 49.93  ? 69  HIS J CE1 1 
ATOM   15666 N NE2 . HIS J  1 77  ? 32.965  46.295  38.921  1.00 47.28  ? 69  HIS J NE2 1 
ATOM   15667 N N   . SER J  1 78  ? 32.318  41.644  34.019  1.00 41.85  ? 70  SER J N   1 
ATOM   15668 C CA  . SER J  1 78  ? 32.032  40.380  33.339  1.00 35.75  ? 70  SER J CA  1 
ATOM   15669 C C   . SER J  1 78  ? 32.511  40.512  31.892  1.00 34.81  ? 70  SER J C   1 
ATOM   15670 O O   . SER J  1 78  ? 32.615  41.629  31.384  1.00 37.32  ? 70  SER J O   1 
ATOM   15671 C CB  . SER J  1 78  ? 30.537  40.068  33.380  1.00 35.53  ? 70  SER J CB  1 
ATOM   15672 O OG  . SER J  1 78  ? 29.768  41.216  33.064  1.00 39.74  ? 70  SER J OG  1 
ATOM   15673 N N   . PRO J  1 79  ? 32.822  39.400  31.226  1.00 35.45  ? 71  PRO J N   1 
ATOM   15674 C CA  . PRO J  1 79  ? 33.481  39.508  29.912  1.00 27.19  ? 71  PRO J CA  1 
ATOM   15675 C C   . PRO J  1 79  ? 32.630  40.168  28.810  1.00 29.19  ? 71  PRO J C   1 
ATOM   15676 O O   . PRO J  1 79  ? 31.424  39.942  28.718  1.00 29.56  ? 71  PRO J O   1 
ATOM   15677 C CB  . PRO J  1 79  ? 33.765  38.048  29.549  1.00 28.61  ? 71  PRO J CB  1 
ATOM   15678 C CG  . PRO J  1 79  ? 33.884  37.355  30.863  1.00 28.53  ? 71  PRO J CG  1 
ATOM   15679 C CD  . PRO J  1 79  ? 32.907  38.037  31.779  1.00 32.71  ? 71  PRO J CD  1 
ATOM   15680 N N   . ASP J  1 80  ? 33.292  40.998  27.997  1.00 32.65  ? 72  ASP J N   1 
ATOM   15681 C CA  . ASP J  1 80  ? 32.670  42.012  27.165  1.00 30.78  ? 72  ASP J CA  1 
ATOM   15682 C C   . ASP J  1 80  ? 31.834  41.423  26.039  1.00 25.63  ? 72  ASP J C   1 
ATOM   15683 O O   . ASP J  1 80  ? 30.934  42.081  25.531  1.00 25.79  ? 72  ASP J O   1 
ATOM   15684 C CB  . ASP J  1 80  ? 33.721  42.972  26.620  1.00 33.52  ? 72  ASP J CB  1 
ATOM   15685 C CG  . ASP J  1 80  ? 33.624  44.340  27.251  1.00 51.32  ? 72  ASP J CG  1 
ATOM   15686 O OD1 . ASP J  1 80  ? 33.835  44.430  28.485  1.00 52.15  ? 72  ASP J OD1 1 
ATOM   15687 O OD2 . ASP J  1 80  ? 33.325  45.316  26.519  1.00 54.13  ? 72  ASP J OD2 1 
ATOM   15688 N N   . GLN J  1 81  ? 32.138  40.186  25.652  1.00 22.97  ? 73  GLN J N   1 
ATOM   15689 C CA  . GLN J  1 81  ? 31.375  39.482  24.628  1.00 20.76  ? 73  GLN J CA  1 
ATOM   15690 C C   . GLN J  1 81  ? 31.634  37.977  24.677  1.00 19.61  ? 73  GLN J C   1 
ATOM   15691 O O   . GLN J  1 81  ? 32.602  37.524  25.292  1.00 16.81  ? 73  GLN J O   1 
ATOM   15692 C CB  . GLN J  1 81  ? 31.681  40.043  23.234  1.00 25.62  ? 73  GLN J CB  1 
ATOM   15693 C CG  . GLN J  1 81  ? 33.075  40.607  23.093  1.00 26.80  ? 73  GLN J CG  1 
ATOM   15694 C CD  . GLN J  1 81  ? 33.617  40.490  21.692  1.00 34.04  ? 73  GLN J CD  1 
ATOM   15695 O OE1 . GLN J  1 81  ? 34.660  39.867  21.479  1.00 46.08  ? 73  GLN J OE1 1 
ATOM   15696 N NE2 . GLN J  1 81  ? 32.928  41.098  20.726  1.00 24.82  ? 73  GLN J NE2 1 
ATOM   15697 N N   . VAL J  1 82  ? 30.753  37.204  24.045  1.00 16.17  ? 74  VAL J N   1 
ATOM   15698 C CA  . VAL J  1 82  ? 30.878  35.750  24.040  1.00 18.97  ? 74  VAL J CA  1 
ATOM   15699 C C   . VAL J  1 82  ? 30.514  35.197  22.664  1.00 18.95  ? 74  VAL J C   1 
ATOM   15700 O O   . VAL J  1 82  ? 29.842  35.859  21.878  1.00 18.88  ? 74  VAL J O   1 
ATOM   15701 C CB  . VAL J  1 82  ? 29.933  35.081  25.083  1.00 15.61  ? 74  VAL J CB  1 
ATOM   15702 C CG1 . VAL J  1 82  ? 30.377  35.361  26.503  1.00 16.74  ? 74  VAL J CG1 1 
ATOM   15703 C CG2 . VAL J  1 82  ? 28.524  35.551  24.879  1.00 13.81  ? 74  VAL J CG2 1 
ATOM   15704 N N   . SER J  1 83  ? 30.950  33.978  22.376  1.00 16.47  ? 75  SER J N   1 
ATOM   15705 C CA  . SER J  1 83  ? 30.468  33.283  21.195  1.00 18.06  ? 75  SER J CA  1 
ATOM   15706 C C   . SER J  1 83  ? 29.176  32.572  21.557  1.00 14.82  ? 75  SER J C   1 
ATOM   15707 O O   . SER J  1 83  ? 29.079  31.972  22.621  1.00 15.64  ? 75  SER J O   1 
ATOM   15708 C CB  . SER J  1 83  ? 31.502  32.269  20.696  1.00 18.15  ? 75  SER J CB  1 
ATOM   15709 O OG  . SER J  1 83  ? 32.631  32.926  20.144  1.00 21.62  ? 75  SER J OG  1 
ATOM   15710 N N   . VAL J  1 84  ? 28.190  32.637  20.672  1.00 13.50  ? 76  VAL J N   1 
ATOM   15711 C CA  . VAL J  1 84  ? 26.908  31.975  20.890  1.00 14.19  ? 76  VAL J CA  1 
ATOM   15712 C C   . VAL J  1 84  ? 26.492  31.204  19.647  1.00 14.01  ? 76  VAL J C   1 
ATOM   15713 O O   . VAL J  1 84  ? 26.532  31.755  18.560  1.00 18.43  ? 76  VAL J O   1 
ATOM   15714 C CB  . VAL J  1 84  ? 25.798  32.999  21.192  1.00 14.80  ? 76  VAL J CB  1 
ATOM   15715 C CG1 . VAL J  1 84  ? 24.459  32.291  21.324  1.00 14.18  ? 76  VAL J CG1 1 
ATOM   15716 C CG2 . VAL J  1 84  ? 26.117  33.799  22.461  1.00 10.94  ? 76  VAL J CG2 1 
ATOM   15717 N N   . PRO J  1 85  ? 26.077  29.931  19.793  1.00 14.69  ? 77  PRO J N   1 
ATOM   15718 C CA  . PRO J  1 85  ? 25.609  29.197  18.610  1.00 12.45  ? 77  PRO J CA  1 
ATOM   15719 C C   . PRO J  1 85  ? 24.388  29.900  18.002  1.00 16.60  ? 77  PRO J C   1 
ATOM   15720 O O   . PRO J  1 85  ? 23.523  30.359  18.745  1.00 13.25  ? 77  PRO J O   1 
ATOM   15721 C CB  . PRO J  1 85  ? 25.192  27.844  19.180  1.00 7.73   ? 77  PRO J CB  1 
ATOM   15722 C CG  . PRO J  1 85  ? 25.846  27.758  20.485  1.00 11.95  ? 77  PRO J CG  1 
ATOM   15723 C CD  . PRO J  1 85  ? 25.928  29.136  21.019  1.00 11.31  ? 77  PRO J CD  1 
ATOM   15724 N N   . ILE J  1 86  ? 24.306  29.999  16.679  1.00 20.07  ? 78  ILE J N   1 
ATOM   15725 C CA  . ILE J  1 86  ? 23.189  30.736  16.078  1.00 18.50  ? 78  ILE J CA  1 
ATOM   15726 C C   . ILE J  1 86  ? 21.824  30.065  16.258  1.00 15.84  ? 78  ILE J C   1 
ATOM   15727 O O   . ILE J  1 86  ? 20.782  30.706  16.123  1.00 14.97  ? 78  ILE J O   1 
ATOM   15728 C CB  . ILE J  1 86  ? 23.435  31.038  14.619  1.00 14.92  ? 78  ILE J CB  1 
ATOM   15729 C CG1 . ILE J  1 86  ? 23.598  29.742  13.829  1.00 17.19  ? 78  ILE J CG1 1 
ATOM   15730 C CG2 . ILE J  1 86  ? 24.681  31.902  14.488  1.00 17.08  ? 78  ILE J CG2 1 
ATOM   15731 C CD1 . ILE J  1 86  ? 23.735  29.997  12.341  1.00 14.35  ? 78  ILE J CD1 1 
ATOM   15732 N N   . SER J  1 87  ? 21.830  28.783  16.588  1.00 12.54  ? 79  SER J N   1 
ATOM   15733 C CA  . SER J  1 87  ? 20.592  28.126  16.948  1.00 12.10  ? 79  SER J CA  1 
ATOM   15734 C C   . SER J  1 87  ? 19.883  28.846  18.110  1.00 12.03  ? 79  SER J C   1 
ATOM   15735 O O   . SER J  1 87  ? 18.663  28.839  18.170  1.00 14.49  ? 79  SER J O   1 
ATOM   15736 C CB  . SER J  1 87  ? 20.846  26.656  17.272  1.00 17.23  ? 79  SER J CB  1 
ATOM   15737 O OG  . SER J  1 87  ? 21.768  26.520  18.345  1.00 27.42  ? 79  SER J OG  1 
ATOM   15738 N N   . SER J  1 88  ? 20.649  29.483  19.002  1.00 12.34  ? 80  SER J N   1 
ATOM   15739 C CA  . SER J  1 88  ? 20.117  30.201  20.167  1.00 9.25   ? 80  SER J CA  1 
ATOM   15740 C C   . SER J  1 88  ? 19.697  31.652  19.887  1.00 13.28  ? 80  SER J C   1 
ATOM   15741 O O   . SER J  1 88  ? 19.052  32.291  20.721  1.00 11.61  ? 80  SER J O   1 
ATOM   15742 C CB  . SER J  1 88  ? 21.140  30.214  21.307  1.00 9.17   ? 80  SER J CB  1 
ATOM   15743 O OG  . SER J  1 88  ? 21.489  28.905  21.721  1.00 13.39  ? 80  SER J OG  1 
ATOM   15744 N N   . LEU J  1 89  ? 20.061  32.183  18.724  1.00 13.37  ? 81  LEU J N   1 
ATOM   15745 C CA  . LEU J  1 89  ? 19.797  33.590  18.442  1.00 11.64  ? 81  LEU J CA  1 
ATOM   15746 C C   . LEU J  1 89  ? 18.984  33.784  17.181  1.00 13.77  ? 81  LEU J C   1 
ATOM   15747 O O   . LEU J  1 89  ? 19.007  32.952  16.286  1.00 16.99  ? 81  LEU J O   1 
ATOM   15748 C CB  . LEU J  1 89  ? 21.102  34.349  18.290  1.00 10.72  ? 81  LEU J CB  1 
ATOM   15749 C CG  . LEU J  1 89  ? 21.948  34.531  19.533  1.00 9.75   ? 81  LEU J CG  1 
ATOM   15750 C CD1 . LEU J  1 89  ? 23.366  34.730  19.094  1.00 13.56  ? 81  LEU J CD1 1 
ATOM   15751 C CD2 . LEU J  1 89  ? 21.463  35.744  20.244  1.00 9.81   ? 81  LEU J CD2 1 
ATOM   15752 N N   . TRP J  1 90  ? 18.265  34.892  17.110  1.00 13.64  ? 82  TRP J N   1 
ATOM   15753 C CA  . TRP J  1 90  ? 17.680  35.294  15.852  1.00 15.50  ? 82  TRP J CA  1 
ATOM   15754 C C   . TRP J  1 90  ? 18.796  35.753  14.908  1.00 18.47  ? 82  TRP J C   1 
ATOM   15755 O O   . TRP J  1 90  ? 19.649  36.547  15.295  1.00 21.00  ? 82  TRP J O   1 
ATOM   15756 C CB  . TRP J  1 90  ? 16.662  36.420  16.059  1.00 15.16  ? 82  TRP J CB  1 
ATOM   15757 C CG  . TRP J  1 90  ? 16.058  36.920  14.766  1.00 18.34  ? 82  TRP J CG  1 
ATOM   15758 C CD1 . TRP J  1 90  ? 14.964  36.417  14.116  1.00 16.57  ? 82  TRP J CD1 1 
ATOM   15759 C CD2 . TRP J  1 90  ? 16.528  38.013  13.968  1.00 18.30  ? 82  TRP J CD2 1 
ATOM   15760 N NE1 . TRP J  1 90  ? 14.717  37.141  12.971  1.00 16.27  ? 82  TRP J NE1 1 
ATOM   15761 C CE2 . TRP J  1 90  ? 15.666  38.123  12.857  1.00 17.74  ? 82  TRP J CE2 1 
ATOM   15762 C CE3 . TRP J  1 90  ? 17.598  38.910  14.086  1.00 19.91  ? 82  TRP J CE3 1 
ATOM   15763 C CZ2 . TRP J  1 90  ? 15.846  39.086  11.868  1.00 20.15  ? 82  TRP J CZ2 1 
ATOM   15764 C CZ3 . TRP J  1 90  ? 17.771  39.873  13.106  1.00 18.58  ? 82  TRP J CZ3 1 
ATOM   15765 C CH2 . TRP J  1 90  ? 16.903  39.952  12.012  1.00 18.97  ? 82  TRP J CH2 1 
ATOM   15766 N N   . VAL J  1 91  ? 18.791  35.227  13.684  1.00 17.58  ? 83  VAL J N   1 
ATOM   15767 C CA  . VAL J  1 91  ? 19.621  35.723  12.597  1.00 18.36  ? 83  VAL J CA  1 
ATOM   15768 C C   . VAL J  1 91  ? 18.720  36.177  11.440  1.00 18.34  ? 83  VAL J C   1 
ATOM   15769 O O   . VAL J  1 91  ? 17.669  35.584  11.204  1.00 18.89  ? 83  VAL J O   1 
ATOM   15770 C CB  . VAL J  1 91  ? 20.579  34.637  12.097  1.00 18.95  ? 83  VAL J CB  1 
ATOM   15771 C CG1 . VAL J  1 91  ? 21.496  34.201  13.214  1.00 19.49  ? 83  VAL J CG1 1 
ATOM   15772 C CG2 . VAL J  1 91  ? 19.799  33.444  11.578  1.00 22.96  ? 83  VAL J CG2 1 
ATOM   15773 N N   . PRO J  1 92  ? 19.118  37.242  10.726  1.00 18.23  ? 84  PRO J N   1 
ATOM   15774 C CA  . PRO J  1 92  ? 18.356  37.723  9.562   1.00 17.31  ? 84  PRO J CA  1 
ATOM   15775 C C   . PRO J  1 92  ? 18.237  36.662  8.455   1.00 15.51  ? 84  PRO J C   1 
ATOM   15776 O O   . PRO J  1 92  ? 19.218  35.991  8.167   1.00 19.31  ? 84  PRO J O   1 
ATOM   15777 C CB  . PRO J  1 92  ? 19.195  38.908  9.061   1.00 20.20  ? 84  PRO J CB  1 
ATOM   15778 C CG  . PRO J  1 92  ? 19.993  39.342  10.247  1.00 20.41  ? 84  PRO J CG  1 
ATOM   15779 C CD  . PRO J  1 92  ? 20.290  38.089  11.012  1.00 17.60  ? 84  PRO J CD  1 
ATOM   15780 N N   . ASP J  1 93  ? 17.060  36.513  7.853   1.00 14.67  ? 85  ASP J N   1 
ATOM   15781 C CA  . ASP J  1 93  ? 16.861  35.537  6.782   1.00 16.62  ? 85  ASP J CA  1 
ATOM   15782 C C   . ASP J  1 93  ? 17.362  36.073  5.424   1.00 20.54  ? 85  ASP J C   1 
ATOM   15783 O O   . ASP J  1 93  ? 16.573  36.388  4.523   1.00 17.44  ? 85  ASP J O   1 
ATOM   15784 C CB  . ASP J  1 93  ? 15.387  35.103  6.697   1.00 13.41  ? 85  ASP J CB  1 
ATOM   15785 C CG  . ASP J  1 93  ? 14.433  36.276  6.511   1.00 18.29  ? 85  ASP J CG  1 
ATOM   15786 O OD1 . ASP J  1 93  ? 14.724  37.376  7.036   1.00 17.18  ? 85  ASP J OD1 1 
ATOM   15787 O OD2 . ASP J  1 93  ? 13.389  36.092  5.835   1.00 17.15  ? 85  ASP J OD2 1 
ATOM   15788 N N   . LEU J  1 94  ? 18.679  36.184  5.280   1.00 18.47  ? 86  LEU J N   1 
ATOM   15789 C CA  . LEU J  1 94  ? 19.217  36.811  4.086   1.00 20.67  ? 86  LEU J CA  1 
ATOM   15790 C C   . LEU J  1 94  ? 19.102  35.862  2.904   1.00 19.95  ? 86  LEU J C   1 
ATOM   15791 O O   . LEU J  1 94  ? 19.216  34.642  3.047   1.00 26.34  ? 86  LEU J O   1 
ATOM   15792 C CB  . LEU J  1 94  ? 20.657  37.283  4.304   1.00 17.85  ? 86  LEU J CB  1 
ATOM   15793 C CG  . LEU J  1 94  ? 20.787  38.412  5.329   1.00 16.50  ? 86  LEU J CG  1 
ATOM   15794 C CD1 . LEU J  1 94  ? 22.220  38.910  5.431   1.00 17.33  ? 86  LEU J CD1 1 
ATOM   15795 C CD2 . LEU J  1 94  ? 19.845  39.551  5.011   1.00 17.32  ? 86  LEU J CD2 1 
ATOM   15796 N N   . ALA J  1 95  ? 18.826  36.423  1.740   1.00 18.14  ? 87  ALA J N   1 
ATOM   15797 C CA  . ALA J  1 95  ? 18.800  35.626  0.525   1.00 25.68  ? 87  ALA J CA  1 
ATOM   15798 C C   . ALA J  1 95  ? 19.500  36.419  -0.558  1.00 24.50  ? 87  ALA J C   1 
ATOM   15799 O O   . ALA J  1 95  ? 19.466  37.660  -0.552  1.00 22.52  ? 87  ALA J O   1 
ATOM   15800 C CB  . ALA J  1 95  ? 17.351  35.292  0.113   1.00 19.23  ? 87  ALA J CB  1 
ATOM   15801 N N   . ALA J  1 96  ? 20.153  35.712  -1.474  1.00 26.78  ? 88  ALA J N   1 
ATOM   15802 C CA  . ALA J  1 96  ? 20.688  36.361  -2.671  1.00 27.24  ? 88  ALA J CA  1 
ATOM   15803 C C   . ALA J  1 96  ? 19.819  35.992  -3.850  1.00 26.71  ? 88  ALA J C   1 
ATOM   15804 O O   . ALA J  1 96  ? 19.674  34.815  -4.165  1.00 30.39  ? 88  ALA J O   1 
ATOM   15805 C CB  . ALA J  1 96  ? 22.111  35.957  -2.918  1.00 23.97  ? 88  ALA J CB  1 
ATOM   15806 N N   . TYR J  1 97  ? 19.246  37.006  -4.498  1.00 33.23  ? 89  TYR J N   1 
ATOM   15807 C CA  . TYR J  1 97  ? 18.268  36.814  -5.575  1.00 32.26  ? 89  TYR J CA  1 
ATOM   15808 C C   . TYR J  1 97  ? 18.814  36.054  -6.783  1.00 29.62  ? 89  TYR J C   1 
ATOM   15809 O O   . TYR J  1 97  ? 18.106  35.243  -7.386  1.00 30.91  ? 89  TYR J O   1 
ATOM   15810 C CB  . TYR J  1 97  ? 17.700  38.158  -6.027  1.00 30.65  ? 89  TYR J CB  1 
ATOM   15811 C CG  . TYR J  1 97  ? 17.110  38.979  -4.910  1.00 33.78  ? 89  TYR J CG  1 
ATOM   15812 C CD1 . TYR J  1 97  ? 15.740  39.058  -4.723  1.00 45.67  ? 89  TYR J CD1 1 
ATOM   15813 C CD2 . TYR J  1 97  ? 17.926  39.676  -4.036  1.00 40.21  ? 89  TYR J CD2 1 
ATOM   15814 C CE1 . TYR J  1 97  ? 15.201  39.818  -3.688  1.00 46.31  ? 89  TYR J CE1 1 
ATOM   15815 C CE2 . TYR J  1 97  ? 17.401  40.431  -3.000  1.00 41.93  ? 89  TYR J CE2 1 
ATOM   15816 C CZ  . TYR J  1 97  ? 16.045  40.501  -2.828  1.00 41.25  ? 89  TYR J CZ  1 
ATOM   15817 O OH  . TYR J  1 97  ? 15.544  41.261  -1.791  1.00 46.30  ? 89  TYR J OH  1 
ATOM   15818 N N   . ASN J  1 98  ? 20.069  36.318  -7.133  1.00 28.80  ? 90  ASN J N   1 
ATOM   15819 C CA  . ASN J  1 98  ? 20.673  35.693  -8.306  1.00 31.86  ? 90  ASN J CA  1 
ATOM   15820 C C   . ASN J  1 98  ? 21.516  34.455  -7.994  1.00 38.08  ? 90  ASN J C   1 
ATOM   15821 O O   . ASN J  1 98  ? 22.306  33.992  -8.843  1.00 30.62  ? 90  ASN J O   1 
ATOM   15822 C CB  . ASN J  1 98  ? 21.484  36.712  -9.103  1.00 27.59  ? 90  ASN J CB  1 
ATOM   15823 C CG  . ASN J  1 98  ? 22.441  37.503  -8.242  1.00 37.54  ? 90  ASN J CG  1 
ATOM   15824 O OD1 . ASN J  1 98  ? 22.119  37.872  -7.109  1.00 37.23  ? 90  ASN J OD1 1 
ATOM   15825 N ND2 . ASN J  1 98  ? 23.631  37.777  -8.779  1.00 38.36  ? 90  ASN J ND2 1 
ATOM   15826 N N   . ALA J  1 99  ? 21.340  33.916  -6.785  1.00 27.80  ? 91  ALA J N   1 
ATOM   15827 C CA  . ALA J  1 99  ? 22.046  32.700  -6.403  1.00 29.45  ? 91  ALA J CA  1 
ATOM   15828 C C   . ALA J  1 99  ? 21.475  31.531  -7.193  1.00 25.67  ? 91  ALA J C   1 
ATOM   15829 O O   . ALA J  1 99  ? 20.280  31.509  -7.476  1.00 24.61  ? 91  ALA J O   1 
ATOM   15830 C CB  . ALA J  1 99  ? 21.912  32.454  -4.913  1.00 29.14  ? 91  ALA J CB  1 
ATOM   15831 N N   . ILE J  1 100 ? 22.318  30.576  -7.576  1.00 21.75  ? 92  ILE J N   1 
ATOM   15832 C CA  . ILE J  1 100 ? 21.822  29.399  -8.285  1.00 19.61  ? 92  ILE J CA  1 
ATOM   15833 C C   . ILE J  1 100 ? 22.289  28.092  -7.665  1.00 21.13  ? 92  ILE J C   1 
ATOM   15834 O O   . ILE J  1 100 ? 21.989  27.020  -8.187  1.00 25.23  ? 92  ILE J O   1 
ATOM   15835 C CB  . ILE J  1 100 ? 22.160  29.401  -9.812  1.00 23.46  ? 92  ILE J CB  1 
ATOM   15836 C CG1 . ILE J  1 100 ? 23.669  29.284  -10.040 1.00 29.37  ? 92  ILE J CG1 1 
ATOM   15837 C CG2 . ILE J  1 100 ? 21.586  30.625  -10.508 1.00 21.81  ? 92  ILE J CG2 1 
ATOM   15838 C CD1 . ILE J  1 100 ? 24.063  29.267  -11.478 1.00 27.18  ? 92  ILE J CD1 1 
ATOM   15839 N N   . SER J  1 101 ? 23.030  28.177  -6.564  1.00 25.35  ? 93  SER J N   1 
ATOM   15840 C CA  . SER J  1 101 ? 23.284  27.004  -5.720  1.00 23.51  ? 93  SER J CA  1 
ATOM   15841 C C   . SER J  1 101 ? 22.909  27.332  -4.268  1.00 19.69  ? 93  SER J C   1 
ATOM   15842 O O   . SER J  1 101 ? 22.667  28.485  -3.938  1.00 19.64  ? 93  SER J O   1 
ATOM   15843 C CB  . SER J  1 101 ? 24.746  26.570  -5.813  1.00 21.36  ? 93  SER J CB  1 
ATOM   15844 O OG  . SER J  1 101 ? 25.600  27.488  -5.145  1.00 21.34  ? 93  SER J OG  1 
ATOM   15845 N N   . LYS J  1 102 ? 22.848  26.317  -3.414  1.00 20.97  ? 94  LYS J N   1 
ATOM   15846 C CA  . LYS J  1 102 ? 22.651  26.523  -1.977  1.00 24.67  ? 94  LYS J CA  1 
ATOM   15847 C C   . LYS J  1 102 ? 23.847  27.266  -1.370  1.00 25.79  ? 94  LYS J C   1 
ATOM   15848 O O   . LYS J  1 102 ? 24.971  27.120  -1.841  1.00 24.79  ? 94  LYS J O   1 
ATOM   15849 C CB  . LYS J  1 102 ? 22.500  25.167  -1.283  1.00 24.26  ? 94  LYS J CB  1 
ATOM   15850 C CG  . LYS J  1 102 ? 21.130  24.897  -0.708  1.00 29.00  ? 94  LYS J CG  1 
ATOM   15851 C CD  . LYS J  1 102 ? 20.903  23.405  -0.461  1.00 32.70  ? 94  LYS J CD  1 
ATOM   15852 C CE  . LYS J  1 102 ? 19.638  23.172  0.374   1.00 46.73  ? 94  LYS J CE  1 
ATOM   15853 N NZ  . LYS J  1 102 ? 19.055  21.797  0.209   1.00 47.21  ? 94  LYS J NZ  1 
ATOM   15854 N N   . PRO J  1 103 ? 23.621  28.071  -0.323  1.00 27.46  ? 95  PRO J N   1 
ATOM   15855 C CA  . PRO J  1 103 ? 24.838  28.593  0.314   1.00 22.04  ? 95  PRO J CA  1 
ATOM   15856 C C   . PRO J  1 103 ? 25.556  27.513  1.124   1.00 19.71  ? 95  PRO J C   1 
ATOM   15857 O O   . PRO J  1 103 ? 24.997  26.974  2.060   1.00 21.64  ? 95  PRO J O   1 
ATOM   15858 C CB  . PRO J  1 103 ? 24.328  29.724  1.220   1.00 17.61  ? 95  PRO J CB  1 
ATOM   15859 C CG  . PRO J  1 103 ? 22.849  29.573  1.280   1.00 17.30  ? 95  PRO J CG  1 
ATOM   15860 C CD  . PRO J  1 103 ? 22.402  28.788  0.087   1.00 21.12  ? 95  PRO J CD  1 
ATOM   15861 N N   . GLU J  1 104 ? 26.785  27.186  0.739   1.00 24.54  ? 96  GLU J N   1 
ATOM   15862 C CA  . GLU J  1 104 ? 27.592  26.210  1.466   1.00 24.24  ? 96  GLU J CA  1 
ATOM   15863 C C   . GLU J  1 104 ? 28.386  26.977  2.531   1.00 21.26  ? 96  GLU J C   1 
ATOM   15864 O O   . GLU J  1 104 ? 29.338  27.690  2.206   1.00 20.32  ? 96  GLU J O   1 
ATOM   15865 C CB  . GLU J  1 104 ? 28.523  25.463  0.484   1.00 29.22  ? 96  GLU J CB  1 
ATOM   15866 C CG  . GLU J  1 104 ? 29.293  24.241  1.043   1.00 29.75  ? 96  GLU J CG  1 
ATOM   15867 C CD  . GLU J  1 104 ? 30.405  23.722  0.080   1.00 49.65  ? 96  GLU J CD  1 
ATOM   15868 O OE1 . GLU J  1 104 ? 31.192  22.817  0.467   1.00 37.74  ? 96  GLU J OE1 1 
ATOM   15869 O OE2 . GLU J  1 104 ? 30.500  24.218  -1.071  1.00 51.70  ? 96  GLU J OE2 1 
ATOM   15870 N N   . VAL J  1 105 ? 27.972  26.869  3.795   1.00 20.28  ? 97  VAL J N   1 
ATOM   15871 C CA  . VAL J  1 105 ? 28.661  27.580  4.876   1.00 17.75  ? 97  VAL J CA  1 
ATOM   15872 C C   . VAL J  1 105 ? 29.922  26.805  5.257   1.00 17.73  ? 97  VAL J C   1 
ATOM   15873 O O   . VAL J  1 105 ? 29.863  25.609  5.543   1.00 15.74  ? 97  VAL J O   1 
ATOM   15874 C CB  . VAL J  1 105 ? 27.732  27.828  6.093   1.00 16.81  ? 97  VAL J CB  1 
ATOM   15875 C CG1 . VAL J  1 105 ? 28.513  28.326  7.297   1.00 15.75  ? 97  VAL J CG1 1 
ATOM   15876 C CG2 . VAL J  1 105 ? 26.654  28.820  5.733   1.00 12.35  ? 97  VAL J CG2 1 
ATOM   15877 N N   . LEU J  1 106 ? 31.064  27.486  5.226   1.00 18.25  ? 98  LEU J N   1 
ATOM   15878 C CA  . LEU J  1 106 ? 32.369  26.825  5.361   1.00 19.95  ? 98  LEU J CA  1 
ATOM   15879 C C   . LEU J  1 106 ? 32.908  26.903  6.792   1.00 24.74  ? 98  LEU J C   1 
ATOM   15880 O O   . LEU J  1 106 ? 33.819  26.146  7.155   1.00 21.75  ? 98  LEU J O   1 
ATOM   15881 C CB  . LEU J  1 106 ? 33.403  27.438  4.398   1.00 19.59  ? 98  LEU J CB  1 
ATOM   15882 C CG  . LEU J  1 106 ? 33.213  27.342  2.876   1.00 19.04  ? 98  LEU J CG  1 
ATOM   15883 C CD1 . LEU J  1 106 ? 34.185  28.234  2.142   1.00 14.93  ? 98  LEU J CD1 1 
ATOM   15884 C CD2 . LEU J  1 106 ? 33.394  25.923  2.409   1.00 22.32  ? 98  LEU J CD2 1 
ATOM   15885 N N   . THR J  1 107 ? 32.333  27.801  7.599   1.00 16.52  ? 99  THR J N   1 
ATOM   15886 C CA  . THR J  1 107 ? 32.868  28.116  8.919   1.00 17.66  ? 99  THR J CA  1 
ATOM   15887 C C   . THR J  1 107 ? 32.021  27.583  10.092  1.00 22.44  ? 99  THR J C   1 
ATOM   15888 O O   . THR J  1 107 ? 30.900  27.113  9.887   1.00 17.61  ? 99  THR J O   1 
ATOM   15889 C CB  . THR J  1 107 ? 33.076  29.633  9.062   1.00 20.06  ? 99  THR J CB  1 
ATOM   15890 O OG1 . THR J  1 107 ? 32.042  30.323  8.357   1.00 18.24  ? 99  THR J OG1 1 
ATOM   15891 C CG2 . THR J  1 107 ? 34.409  30.032  8.478   1.00 21.21  ? 99  THR J CG2 1 
ATOM   15892 N N   . PRO J  1 108 ? 32.580  27.609  11.323  1.00 21.37  ? 100 PRO J N   1 
ATOM   15893 C CA  . PRO J  1 108 ? 31.755  27.187  12.455  1.00 17.37  ? 100 PRO J CA  1 
ATOM   15894 C C   . PRO J  1 108 ? 30.648  28.169  12.693  1.00 18.29  ? 100 PRO J C   1 
ATOM   15895 O O   . PRO J  1 108 ? 30.796  29.372  12.518  1.00 21.84  ? 100 PRO J O   1 
ATOM   15896 C CB  . PRO J  1 108 ? 32.732  27.181  13.624  1.00 19.88  ? 100 PRO J CB  1 
ATOM   15897 C CG  . PRO J  1 108 ? 34.039  26.873  12.979  1.00 20.10  ? 100 PRO J CG  1 
ATOM   15898 C CD  . PRO J  1 108 ? 34.004  27.660  11.695  1.00 18.30  ? 100 PRO J CD  1 
ATOM   15899 N N   . GLN J  1 109 ? 29.529  27.615  13.112  1.00 21.74  ? 101 GLN J N   1 
ATOM   15900 C CA  . GLN J  1 109 ? 28.247  28.269  13.057  1.00 17.05  ? 101 GLN J CA  1 
ATOM   15901 C C   . GLN J  1 109 ? 27.986  29.062  14.346  1.00 17.72  ? 101 GLN J C   1 
ATOM   15902 O O   . GLN J  1 109 ? 26.987  28.848  15.038  1.00 15.05  ? 101 GLN J O   1 
ATOM   15903 C CB  . GLN J  1 109 ? 27.220  27.163  12.868  1.00 20.60  ? 101 GLN J CB  1 
ATOM   15904 C CG  . GLN J  1 109 ? 26.030  27.511  12.040  1.00 25.62  ? 101 GLN J CG  1 
ATOM   15905 C CD  . GLN J  1 109 ? 26.359  27.755  10.588  1.00 20.02  ? 101 GLN J CD  1 
ATOM   15906 O OE1 . GLN J  1 109 ? 26.739  28.862  10.203  1.00 19.66  ? 101 GLN J OE1 1 
ATOM   15907 N NE2 . GLN J  1 109 ? 26.174  26.732  9.763   1.00 19.97  ? 101 GLN J NE2 1 
ATOM   15908 N N   . LEU J  1 110 ? 28.899  29.977  14.668  1.00 19.78  ? 102 LEU J N   1 
ATOM   15909 C CA  . LEU J  1 110 ? 28.788  30.765  15.900  1.00 19.22  ? 102 LEU J CA  1 
ATOM   15910 C C   . LEU J  1 110 ? 28.711  32.254  15.596  1.00 18.00  ? 102 LEU J C   1 
ATOM   15911 O O   . LEU J  1 110 ? 29.310  32.727  14.628  1.00 22.50  ? 102 LEU J O   1 
ATOM   15912 C CB  . LEU J  1 110 ? 29.973  30.502  16.839  1.00 15.18  ? 102 LEU J CB  1 
ATOM   15913 C CG  . LEU J  1 110 ? 30.338  29.058  17.189  1.00 16.20  ? 102 LEU J CG  1 
ATOM   15914 C CD1 . LEU J  1 110 ? 31.246  29.021  18.399  1.00 19.73  ? 102 LEU J CD1 1 
ATOM   15915 C CD2 . LEU J  1 110 ? 29.103  28.216  17.449  1.00 18.18  ? 102 LEU J CD2 1 
ATOM   15916 N N   . ALA J  1 111 ? 27.979  32.987  16.427  1.00 12.37  ? 103 ALA J N   1 
ATOM   15917 C CA  . ALA J  1 111 ? 27.937  34.440  16.334  1.00 13.73  ? 103 ALA J CA  1 
ATOM   15918 C C   . ALA J  1 111 ? 28.678  35.014  17.527  1.00 15.19  ? 103 ALA J C   1 
ATOM   15919 O O   . ALA J  1 111 ? 29.015  34.285  18.449  1.00 16.75  ? 103 ALA J O   1 
ATOM   15920 C CB  . ALA J  1 111 ? 26.509  34.929  16.319  1.00 10.74  ? 103 ALA J CB  1 
ATOM   15921 N N   . ARG J  1 112 ? 28.974  36.306  17.503  1.00 16.35  ? 104 ARG J N   1 
ATOM   15922 C CA  . ARG J  1 112 ? 29.463  36.958  18.706  1.00 17.32  ? 104 ARG J CA  1 
ATOM   15923 C C   . ARG J  1 112 ? 28.362  37.863  19.187  1.00 18.03  ? 104 ARG J C   1 
ATOM   15924 O O   . ARG J  1 112 ? 27.678  38.500  18.382  1.00 19.71  ? 104 ARG J O   1 
ATOM   15925 C CB  . ARG J  1 112 ? 30.730  37.775  18.461  1.00 20.99  ? 104 ARG J CB  1 
ATOM   15926 C CG  . ARG J  1 112 ? 31.975  36.954  18.179  1.00 25.23  ? 104 ARG J CG  1 
ATOM   15927 C CD  . ARG J  1 112 ? 32.490  36.209  19.408  1.00 23.30  ? 104 ARG J CD  1 
ATOM   15928 N NE  . ARG J  1 112 ? 33.278  37.051  20.308  1.00 26.68  ? 104 ARG J NE  1 
ATOM   15929 C CZ  . ARG J  1 112 ? 34.146  36.571  21.196  1.00 25.43  ? 104 ARG J CZ  1 
ATOM   15930 N NH1 . ARG J  1 112 ? 34.335  35.264  21.281  1.00 24.65  ? 104 ARG J NH1 1 
ATOM   15931 N NH2 . ARG J  1 112 ? 34.830  37.382  21.994  1.00 26.96  ? 104 ARG J NH2 1 
ATOM   15932 N N   . VAL J  1 113 ? 28.174  37.892  20.501  1.00 18.39  ? 105 VAL J N   1 
ATOM   15933 C CA  . VAL J  1 113 ? 27.215  38.785  21.135  1.00 18.11  ? 105 VAL J CA  1 
ATOM   15934 C C   . VAL J  1 113 ? 27.984  39.719  22.045  1.00 18.19  ? 105 VAL J C   1 
ATOM   15935 O O   . VAL J  1 113 ? 28.745  39.270  22.904  1.00 18.78  ? 105 VAL J O   1 
ATOM   15936 C CB  . VAL J  1 113 ? 26.174  37.998  21.951  1.00 16.46  ? 105 VAL J CB  1 
ATOM   15937 C CG1 . VAL J  1 113 ? 25.391  38.926  22.861  1.00 14.29  ? 105 VAL J CG1 1 
ATOM   15938 C CG2 . VAL J  1 113 ? 25.246  37.248  21.016  1.00 12.40  ? 105 VAL J CG2 1 
ATOM   15939 N N   . VAL J  1 114 ? 27.802  41.018  21.846  1.00 19.74  ? 106 VAL J N   1 
ATOM   15940 C CA  . VAL J  1 114 ? 28.524  42.010  22.636  1.00 23.01  ? 106 VAL J CA  1 
ATOM   15941 C C   . VAL J  1 114 ? 27.681  42.548  23.802  1.00 21.15  ? 106 VAL J C   1 
ATOM   15942 O O   . VAL J  1 114 ? 26.451  42.572  23.729  1.00 19.95  ? 106 VAL J O   1 
ATOM   15943 C CB  . VAL J  1 114 ? 29.012  43.160  21.750  1.00 24.01  ? 106 VAL J CB  1 
ATOM   15944 C CG1 . VAL J  1 114 ? 30.261  43.779  22.336  1.00 21.97  ? 106 VAL J CG1 1 
ATOM   15945 C CG2 . VAL J  1 114 ? 29.307  42.645  20.353  1.00 25.81  ? 106 VAL J CG2 1 
ATOM   15946 N N   . SER J  1 115 ? 28.349  42.991  24.867  1.00 22.63  ? 107 SER J N   1 
ATOM   15947 C CA  . SER J  1 115 ? 27.673  43.374  26.115  1.00 27.08  ? 107 SER J CA  1 
ATOM   15948 C C   . SER J  1 115 ? 26.728  44.582  26.029  1.00 22.92  ? 107 SER J C   1 
ATOM   15949 O O   . SER J  1 115 ? 26.017  44.876  26.987  1.00 25.58  ? 107 SER J O   1 
ATOM   15950 C CB  . SER J  1 115 ? 28.681  43.573  27.253  1.00 26.71  ? 107 SER J CB  1 
ATOM   15951 O OG  . SER J  1 115 ? 29.247  44.870  27.224  1.00 31.52  ? 107 SER J OG  1 
ATOM   15952 N N   . ASP J  1 116 ? 26.714  45.258  24.885  1.00 18.83  ? 108 ASP J N   1 
ATOM   15953 C CA  . ASP J  1 116 ? 25.821  46.391  24.651  1.00 19.01  ? 108 ASP J CA  1 
ATOM   15954 C C   . ASP J  1 116 ? 24.620  45.991  23.796  1.00 24.35  ? 108 ASP J C   1 
ATOM   15955 O O   . ASP J  1 116 ? 23.773  46.828  23.467  1.00 22.19  ? 108 ASP J O   1 
ATOM   15956 C CB  . ASP J  1 116 ? 26.578  47.509  23.943  1.00 19.12  ? 108 ASP J CB  1 
ATOM   15957 C CG  . ASP J  1 116 ? 27.031  47.107  22.558  1.00 26.88  ? 108 ASP J CG  1 
ATOM   15958 O OD1 . ASP J  1 116 ? 26.323  47.435  21.583  1.00 41.77  ? 108 ASP J OD1 1 
ATOM   15959 O OD2 . ASP J  1 116 ? 28.079  46.438  22.438  1.00 26.92  ? 108 ASP J OD2 1 
ATOM   15960 N N   . GLY J  1 117 ? 24.568  44.716  23.410  1.00 25.58  ? 109 GLY J N   1 
ATOM   15961 C CA  . GLY J  1 117 ? 23.467  44.203  22.613  1.00 24.97  ? 109 GLY J CA  1 
ATOM   15962 C C   . GLY J  1 117 ? 23.781  43.985  21.140  1.00 28.16  ? 109 GLY J C   1 
ATOM   15963 O O   . GLY J  1 117 ? 22.936  43.500  20.377  1.00 26.73  ? 109 GLY J O   1 
ATOM   15964 N N   . GLU J  1 118 ? 24.987  44.347  20.719  1.00 28.17  ? 110 GLU J N   1 
ATOM   15965 C CA  . GLU J  1 118 ? 25.376  44.108  19.340  1.00 23.16  ? 110 GLU J CA  1 
ATOM   15966 C C   . GLU J  1 118 ? 25.650  42.632  19.089  1.00 19.53  ? 110 GLU J C   1 
ATOM   15967 O O   . GLU J  1 118 ? 26.324  41.974  19.883  1.00 17.63  ? 110 GLU J O   1 
ATOM   15968 C CB  . GLU J  1 118 ? 26.600  44.932  18.958  1.00 27.05  ? 110 GLU J CB  1 
ATOM   15969 C CG  . GLU J  1 118 ? 26.771  45.046  17.435  1.00 35.14  ? 110 GLU J CG  1 
ATOM   15970 C CD  . GLU J  1 118 ? 28.005  45.821  17.022  1.00 41.40  ? 110 GLU J CD  1 
ATOM   15971 O OE1 . GLU J  1 118 ? 28.770  46.251  17.920  1.00 43.91  ? 110 GLU J OE1 1 
ATOM   15972 O OE2 . GLU J  1 118 ? 28.203  45.998  15.797  1.00 40.33  ? 110 GLU J OE2 1 
ATOM   15973 N N   . VAL J  1 119 ? 25.115  42.122  17.982  1.00 15.98  ? 111 VAL J N   1 
ATOM   15974 C CA  . VAL J  1 119 ? 25.345  40.747  17.552  1.00 16.87  ? 111 VAL J CA  1 
ATOM   15975 C C   . VAL J  1 119 ? 26.125  40.736  16.221  1.00 21.92  ? 111 VAL J C   1 
ATOM   15976 O O   . VAL J  1 119 ? 25.778  41.470  15.290  1.00 20.98  ? 111 VAL J O   1 
ATOM   15977 C CB  . VAL J  1 119 ? 24.000  40.000  17.362  1.00 14.66  ? 111 VAL J CB  1 
ATOM   15978 C CG1 . VAL J  1 119 ? 24.237  38.524  17.099  1.00 15.37  ? 111 VAL J CG1 1 
ATOM   15979 C CG2 . VAL J  1 119 ? 23.137  40.160  18.576  1.00 15.73  ? 111 VAL J CG2 1 
ATOM   15980 N N   . LEU J  1 120 ? 27.164  39.908  16.126  1.00 18.45  ? 112 LEU J N   1 
ATOM   15981 C CA  . LEU J  1 120 ? 27.970  39.830  14.910  1.00 18.09  ? 112 LEU J CA  1 
ATOM   15982 C C   . LEU J  1 120 ? 27.984  38.409  14.380  1.00 22.11  ? 112 LEU J C   1 
ATOM   15983 O O   . LEU J  1 120 ? 28.395  37.490  15.087  1.00 26.42  ? 112 LEU J O   1 
ATOM   15984 C CB  . LEU J  1 120 ? 29.421  40.234  15.179  1.00 16.91  ? 112 LEU J CB  1 
ATOM   15985 C CG  . LEU J  1 120 ? 29.746  41.414  16.087  1.00 24.56  ? 112 LEU J CG  1 
ATOM   15986 C CD1 . LEU J  1 120 ? 30.923  41.056  16.991  1.00 23.27  ? 112 LEU J CD1 1 
ATOM   15987 C CD2 . LEU J  1 120 ? 30.079  42.635  15.262  1.00 23.67  ? 112 LEU J CD2 1 
ATOM   15988 N N   . TYR J  1 121 ? 27.564  38.224  13.134  1.00 15.43  ? 113 TYR J N   1 
ATOM   15989 C CA  . TYR J  1 121 ? 27.654  36.913  12.510  1.00 18.45  ? 113 TYR J CA  1 
ATOM   15990 C C   . TYR J  1 121 ? 28.401  37.012  11.152  1.00 21.44  ? 113 TYR J C   1 
ATOM   15991 O O   . TYR J  1 121 ? 27.952  37.703  10.228  1.00 20.02  ? 113 TYR J O   1 
ATOM   15992 C CB  . TYR J  1 121 ? 26.251  36.277  12.390  1.00 13.91  ? 113 TYR J CB  1 
ATOM   15993 C CG  . TYR J  1 121 ? 26.244  34.895  11.779  1.00 9.88   ? 113 TYR J CG  1 
ATOM   15994 C CD1 . TYR J  1 121 ? 27.055  33.895  12.287  1.00 9.94   ? 113 TYR J CD1 1 
ATOM   15995 C CD2 . TYR J  1 121 ? 25.419  34.590  10.700  1.00 10.56  ? 113 TYR J CD2 1 
ATOM   15996 C CE1 . TYR J  1 121 ? 27.069  32.626  11.727  1.00 14.97  ? 113 TYR J CE1 1 
ATOM   15997 C CE2 . TYR J  1 121 ? 25.415  33.316  10.130  1.00 9.88   ? 113 TYR J CE2 1 
ATOM   15998 C CZ  . TYR J  1 121 ? 26.249  32.340  10.648  1.00 15.34  ? 113 TYR J CZ  1 
ATOM   15999 O OH  . TYR J  1 121 ? 26.272  31.073  10.106  1.00 14.91  ? 113 TYR J OH  1 
ATOM   16000 N N   . MET J  1 122 ? 29.552  36.348  11.051  1.00 16.63  ? 114 MET J N   1 
ATOM   16001 C CA  . MET J  1 122 ? 30.352  36.414  9.832   1.00 18.77  ? 114 MET J CA  1 
ATOM   16002 C C   . MET J  1 122 ? 30.694  35.037  9.300   1.00 20.17  ? 114 MET J C   1 
ATOM   16003 O O   . MET J  1 122 ? 31.790  34.533  9.520   1.00 19.85  ? 114 MET J O   1 
ATOM   16004 C CB  . MET J  1 122 ? 31.645  37.213  10.033  1.00 22.07  ? 114 MET J CB  1 
ATOM   16005 C CG  . MET J  1 122 ? 32.236  37.722  8.692   1.00 36.53  ? 114 MET J CG  1 
ATOM   16006 S SD  . MET J  1 122 ? 33.881  38.496  8.737   1.00 42.87  ? 114 MET J SD  1 
ATOM   16007 C CE  . MET J  1 122 ? 34.934  37.049  8.904   1.00 24.98  ? 114 MET J CE  1 
ATOM   16008 N N   . PRO J  1 123 ? 29.749  34.413  8.598   1.00 17.31  ? 115 PRO J N   1 
ATOM   16009 C CA  . PRO J  1 123 ? 30.071  33.120  7.995   1.00 17.80  ? 115 PRO J CA  1 
ATOM   16010 C C   . PRO J  1 123 ? 30.852  33.266  6.682   1.00 20.76  ? 115 PRO J C   1 
ATOM   16011 O O   . PRO J  1 123 ? 30.723  34.267  5.953   1.00 18.93  ? 115 PRO J O   1 
ATOM   16012 C CB  . PRO J  1 123 ? 28.690  32.531  7.710   1.00 14.97  ? 115 PRO J CB  1 
ATOM   16013 C CG  . PRO J  1 123 ? 27.839  33.751  7.436   1.00 14.22  ? 115 PRO J CG  1 
ATOM   16014 C CD  . PRO J  1 123 ? 28.342  34.800  8.390   1.00 13.88  ? 115 PRO J CD  1 
ATOM   16015 N N   . SER J  1 124 ? 31.660  32.254  6.388   1.00 19.49  ? 116 SER J N   1 
ATOM   16016 C CA  . SER J  1 124 ? 32.294  32.127  5.081   1.00 23.27  ? 116 SER J CA  1 
ATOM   16017 C C   . SER J  1 124 ? 31.402  31.284  4.176   1.00 21.23  ? 116 SER J C   1 
ATOM   16018 O O   . SER J  1 124 ? 31.093  30.135  4.495   1.00 22.78  ? 116 SER J O   1 
ATOM   16019 C CB  . SER J  1 124 ? 33.671  31.480  5.203   1.00 18.98  ? 116 SER J CB  1 
ATOM   16020 O OG  . SER J  1 124 ? 34.360  31.565  3.970   1.00 22.77  ? 116 SER J OG  1 
ATOM   16021 N N   . ILE J  1 125 ? 30.983  31.854  3.054   1.00 17.09  ? 117 ILE J N   1 
ATOM   16022 C CA  . ILE J  1 125 ? 30.063  31.164  2.164   1.00 20.26  ? 117 ILE J CA  1 
ATOM   16023 C C   . ILE J  1 125 ? 30.664  30.863  0.797   1.00 24.36  ? 117 ILE J C   1 
ATOM   16024 O O   . ILE J  1 125 ? 31.344  31.698  0.201   1.00 22.55  ? 117 ILE J O   1 
ATOM   16025 C CB  . ILE J  1 125 ? 28.776  31.977  1.983   1.00 23.20  ? 117 ILE J CB  1 
ATOM   16026 C CG1 . ILE J  1 125 ? 28.040  32.070  3.325   1.00 19.01  ? 117 ILE J CG1 1 
ATOM   16027 C CG2 . ILE J  1 125 ? 27.903  31.385  0.862   1.00 18.20  ? 117 ILE J CG2 1 
ATOM   16028 C CD1 . ILE J  1 125 ? 26.808  32.919  3.285   1.00 20.10  ? 117 ILE J CD1 1 
ATOM   16029 N N   . ARG J  1 126 ? 30.427  29.650  0.315   1.00 26.75  ? 118 ARG J N   1 
ATOM   16030 C CA  . ARG J  1 126 ? 30.730  29.316  -1.061  1.00 21.19  ? 118 ARG J CA  1 
ATOM   16031 C C   . ARG J  1 126 ? 29.430  29.174  -1.845  1.00 25.36  ? 118 ARG J C   1 
ATOM   16032 O O   . ARG J  1 126 ? 28.649  28.246  -1.613  1.00 26.53  ? 118 ARG J O   1 
ATOM   16033 C CB  . ARG J  1 126 ? 31.533  28.031  -1.146  1.00 22.08  ? 118 ARG J CB  1 
ATOM   16034 C CG  . ARG J  1 126 ? 32.039  27.767  -2.546  1.00 23.91  ? 118 ARG J CG  1 
ATOM   16035 C CD  . ARG J  1 126 ? 32.263  26.301  -2.821  1.00 21.06  ? 118 ARG J CD  1 
ATOM   16036 N NE  . ARG J  1 126 ? 33.034  26.169  -4.049  1.00 34.98  ? 118 ARG J NE  1 
ATOM   16037 C CZ  . ARG J  1 126 ? 33.253  25.025  -4.684  1.00 39.50  ? 118 ARG J CZ  1 
ATOM   16038 N NH1 . ARG J  1 126 ? 32.749  23.886  -4.221  1.00 49.90  ? 118 ARG J NH1 1 
ATOM   16039 N NH2 . ARG J  1 126 ? 33.966  25.028  -5.792  1.00 29.47  ? 118 ARG J NH2 1 
ATOM   16040 N N   . GLN J  1 127 ? 29.201  30.098  -2.772  1.00 22.82  ? 119 GLN J N   1 
ATOM   16041 C CA  . GLN J  1 127 ? 27.968  30.110  -3.543  1.00 24.67  ? 119 GLN J CA  1 
ATOM   16042 C C   . GLN J  1 127 ? 28.189  30.348  -5.055  1.00 31.03  ? 119 GLN J C   1 
ATOM   16043 O O   . GLN J  1 127 ? 29.152  30.999  -5.475  1.00 21.10  ? 119 GLN J O   1 
ATOM   16044 C CB  . GLN J  1 127 ? 27.020  31.156  -2.962  1.00 20.80  ? 119 GLN J CB  1 
ATOM   16045 C CG  . GLN J  1 127 ? 25.594  30.981  -3.398  1.00 27.02  ? 119 GLN J CG  1 
ATOM   16046 C CD  . GLN J  1 127 ? 24.600  31.603  -2.434  1.00 25.27  ? 119 GLN J CD  1 
ATOM   16047 O OE1 . GLN J  1 127 ? 24.852  32.652  -1.842  1.00 24.57  ? 119 GLN J OE1 1 
ATOM   16048 N NE2 . GLN J  1 127 ? 23.460  30.952  -2.274  1.00 26.03  ? 119 GLN J NE2 1 
ATOM   16049 N N   . ARG J  1 128 ? 27.284  29.800  -5.863  1.00 32.23  ? 120 ARG J N   1 
ATOM   16050 C CA  . ARG J  1 128 ? 27.288  30.003  -7.306  1.00 23.75  ? 120 ARG J CA  1 
ATOM   16051 C C   . ARG J  1 128 ? 26.269  31.068  -7.690  1.00 27.32  ? 120 ARG J C   1 
ATOM   16052 O O   . ARG J  1 128 ? 25.126  31.044  -7.223  1.00 30.53  ? 120 ARG J O   1 
ATOM   16053 C CB  . ARG J  1 128 ? 26.971  28.696  -8.028  1.00 26.78  ? 120 ARG J CB  1 
ATOM   16054 C CG  . ARG J  1 128 ? 28.166  27.773  -8.204  1.00 29.88  ? 120 ARG J CG  1 
ATOM   16055 C CD  . ARG J  1 128 ? 27.732  26.322  -8.351  1.00 36.41  ? 120 ARG J CD  1 
ATOM   16056 N NE  . ARG J  1 128 ? 28.789  25.482  -8.917  1.00 44.87  ? 120 ARG J NE  1 
ATOM   16057 C CZ  . ARG J  1 128 ? 29.535  24.632  -8.216  1.00 49.57  ? 120 ARG J CZ  1 
ATOM   16058 N NH1 . ARG J  1 128 ? 29.342  24.501  -6.904  1.00 58.23  ? 120 ARG J NH1 1 
ATOM   16059 N NH2 . ARG J  1 128 ? 30.472  23.907  -8.827  1.00 31.86  ? 120 ARG J NH2 1 
ATOM   16060 N N   . PHE J  1 129 ? 26.692  32.006  -8.533  1.00 26.21  ? 121 PHE J N   1 
ATOM   16061 C CA  . PHE J  1 129 ? 25.830  33.092  -8.984  1.00 28.96  ? 121 PHE J CA  1 
ATOM   16062 C C   . PHE J  1 129 ? 25.759  33.165  -10.509 1.00 32.00  ? 121 PHE J C   1 
ATOM   16063 O O   . PHE J  1 129 ? 26.679  32.757  -11.214 1.00 33.28  ? 121 PHE J O   1 
ATOM   16064 C CB  . PHE J  1 129 ? 26.321  34.433  -8.445  1.00 26.60  ? 121 PHE J CB  1 
ATOM   16065 C CG  . PHE J  1 129 ? 26.353  34.513  -6.957  1.00 25.78  ? 121 PHE J CG  1 
ATOM   16066 C CD1 . PHE J  1 129 ? 27.448  34.058  -6.248  1.00 25.56  ? 121 PHE J CD1 1 
ATOM   16067 C CD2 . PHE J  1 129 ? 25.288  35.057  -6.260  1.00 31.89  ? 121 PHE J CD2 1 
ATOM   16068 C CE1 . PHE J  1 129 ? 27.475  34.135  -4.867  1.00 27.63  ? 121 PHE J CE1 1 
ATOM   16069 C CE2 . PHE J  1 129 ? 25.309  35.137  -4.879  1.00 25.58  ? 121 PHE J CE2 1 
ATOM   16070 C CZ  . PHE J  1 129 ? 26.403  34.681  -4.183  1.00 25.22  ? 121 PHE J CZ  1 
ATOM   16071 N N   . SER J  1 130 ? 24.657  33.697  -11.013 1.00 34.99  ? 122 SER J N   1 
ATOM   16072 C CA  . SER J  1 130 ? 24.535  33.947  -12.436 1.00 39.65  ? 122 SER J CA  1 
ATOM   16073 C C   . SER J  1 130 ? 24.587  35.451  -12.666 1.00 41.33  ? 122 SER J C   1 
ATOM   16074 O O   . SER J  1 130 ? 23.779  36.209  -12.108 1.00 38.65  ? 122 SER J O   1 
ATOM   16075 C CB  . SER J  1 130 ? 23.219  33.395  -12.968 1.00 37.19  ? 122 SER J CB  1 
ATOM   16076 O OG  . SER J  1 130 ? 22.223  34.405  -12.952 1.00 38.06  ? 122 SER J OG  1 
ATOM   16077 N N   . CYS J  1 131 ? 25.535  35.879  -13.491 1.00 37.18  ? 123 CYS J N   1 
ATOM   16078 C CA  . CYS J  1 131 ? 25.752  37.301  -13.705 1.00 46.70  ? 123 CYS J CA  1 
ATOM   16079 C C   . CYS J  1 131 ? 26.469  37.619  -15.024 1.00 52.03  ? 123 CYS J C   1 
ATOM   16080 O O   . CYS J  1 131 ? 26.718  36.729  -15.851 1.00 43.81  ? 123 CYS J O   1 
ATOM   16081 C CB  . CYS J  1 131 ? 26.525  37.895  -12.527 1.00 49.87  ? 123 CYS J CB  1 
ATOM   16082 S SG  . CYS J  1 131 ? 28.167  37.163  -12.268 1.00 69.39  ? 123 CYS J SG  1 
ATOM   16083 N N   . ASP J  1 132 ? 26.798  38.901  -15.192 1.00 51.97  ? 124 ASP J N   1 
ATOM   16084 C CA  . ASP J  1 132 ? 27.362  39.441  -16.430 1.00 56.25  ? 124 ASP J CA  1 
ATOM   16085 C C   . ASP J  1 132 ? 28.858  39.188  -16.507 1.00 54.65  ? 124 ASP J C   1 
ATOM   16086 O O   . ASP J  1 132 ? 29.661  40.036  -16.119 1.00 54.32  ? 124 ASP J O   1 
ATOM   16087 C CB  . ASP J  1 132 ? 27.110  40.946  -16.499 1.00 55.81  ? 124 ASP J CB  1 
ATOM   16088 C CG  . ASP J  1 132 ? 27.213  41.486  -17.901 1.00 55.48  ? 124 ASP J CG  1 
ATOM   16089 O OD1 . ASP J  1 132 ? 27.738  40.761  -18.781 1.00 51.11  ? 124 ASP J OD1 1 
ATOM   16090 O OD2 . ASP J  1 132 ? 26.761  42.634  -18.114 1.00 53.03  ? 124 ASP J OD2 1 
ATOM   16091 N N   . VAL J  1 133 ? 29.226  38.028  -17.028 1.00 47.36  ? 125 VAL J N   1 
ATOM   16092 C CA  . VAL J  1 133 ? 30.604  37.579  -16.952 1.00 52.32  ? 125 VAL J CA  1 
ATOM   16093 C C   . VAL J  1 133 ? 31.411  37.917  -18.217 1.00 54.42  ? 125 VAL J C   1 
ATOM   16094 O O   . VAL J  1 133 ? 32.641  38.015  -18.174 1.00 47.05  ? 125 VAL J O   1 
ATOM   16095 C CB  . VAL J  1 133 ? 30.655  36.076  -16.600 1.00 50.57  ? 125 VAL J CB  1 
ATOM   16096 C CG1 . VAL J  1 133 ? 31.482  35.299  -17.602 1.00 48.32  ? 125 VAL J CG1 1 
ATOM   16097 C CG2 . VAL J  1 133 ? 31.167  35.886  -15.168 1.00 45.45  ? 125 VAL J CG2 1 
ATOM   16098 N N   . SER J  1 134 ? 30.704  38.123  -19.325 1.00 59.94  ? 126 SER J N   1 
ATOM   16099 C CA  . SER J  1 134 ? 31.332  38.504  -20.585 1.00 63.23  ? 126 SER J CA  1 
ATOM   16100 C C   . SER J  1 134 ? 32.234  39.725  -20.380 1.00 64.39  ? 126 SER J C   1 
ATOM   16101 O O   . SER J  1 134 ? 31.859  40.682  -19.688 1.00 53.65  ? 126 SER J O   1 
ATOM   16102 C CB  . SER J  1 134 ? 30.273  38.774  -21.663 1.00 64.93  ? 126 SER J CB  1 
ATOM   16103 O OG  . SER J  1 134 ? 30.781  38.515  -22.965 1.00 65.62  ? 126 SER J OG  1 
ATOM   16104 N N   . GLY J  1 135 ? 33.434  39.659  -20.955 1.00 62.83  ? 127 GLY J N   1 
ATOM   16105 C CA  . GLY J  1 135 ? 34.427  40.707  -20.798 1.00 55.27  ? 127 GLY J CA  1 
ATOM   16106 C C   . GLY J  1 135 ? 35.375  40.478  -19.634 1.00 53.76  ? 127 GLY J C   1 
ATOM   16107 O O   . GLY J  1 135 ? 36.038  41.406  -19.172 1.00 51.22  ? 127 GLY J O   1 
ATOM   16108 N N   . VAL J  1 136 ? 35.446  39.240  -19.156 1.00 56.02  ? 128 VAL J N   1 
ATOM   16109 C CA  . VAL J  1 136 ? 36.315  38.909  -18.026 1.00 57.25  ? 128 VAL J CA  1 
ATOM   16110 C C   . VAL J  1 136 ? 37.788  38.914  -18.451 1.00 55.53  ? 128 VAL J C   1 
ATOM   16111 O O   . VAL J  1 136 ? 38.671  39.331  -17.689 1.00 49.58  ? 128 VAL J O   1 
ATOM   16112 C CB  . VAL J  1 136 ? 35.910  37.554  -17.360 1.00 50.64  ? 128 VAL J CB  1 
ATOM   16113 C CG1 . VAL J  1 136 ? 35.586  36.502  -18.414 1.00 46.88  ? 128 VAL J CG1 1 
ATOM   16114 C CG2 . VAL J  1 136 ? 36.987  37.057  -16.379 1.00 35.94  ? 128 VAL J CG2 1 
ATOM   16115 N N   . ASP J  1 137 ? 38.035  38.474  -19.683 1.00 54.31  ? 129 ASP J N   1 
ATOM   16116 C CA  . ASP J  1 137 ? 39.387  38.379  -20.228 1.00 53.65  ? 129 ASP J CA  1 
ATOM   16117 C C   . ASP J  1 137 ? 40.027  39.734  -20.538 1.00 49.63  ? 129 ASP J C   1 
ATOM   16118 O O   . ASP J  1 137 ? 41.250  39.853  -20.544 1.00 50.46  ? 129 ASP J O   1 
ATOM   16119 C CB  . ASP J  1 137 ? 39.383  37.526  -21.492 1.00 53.83  ? 129 ASP J CB  1 
ATOM   16120 C CG  . ASP J  1 137 ? 40.391  36.407  -21.436 1.00 57.15  ? 129 ASP J CG  1 
ATOM   16121 O OD1 . ASP J  1 137 ? 40.102  35.403  -20.752 1.00 61.25  ? 129 ASP J OD1 1 
ATOM   16122 O OD2 . ASP J  1 137 ? 41.461  36.526  -22.074 1.00 49.45  ? 129 ASP J OD2 1 
ATOM   16123 N N   . THR J  1 138 ? 39.131  40.711  -20.681 1.00 47.18  ? 130 THR J N   1 
ATOM   16124 C CA  . THR J  1 138 ? 39.396  42.122  -20.931 1.00 47.35  ? 130 THR J CA  1 
ATOM   16125 C C   . THR J  1 138 ? 39.872  42.897  -19.703 1.00 57.54  ? 130 THR J C   1 
ATOM   16126 O O   . THR J  1 138 ? 39.841  42.408  -18.574 1.00 60.25  ? 130 THR J O   1 
ATOM   16127 C CB  . THR J  1 138 ? 38.156  42.830  -21.513 1.00 49.27  ? 130 THR J CB  1 
ATOM   16128 O OG1 . THR J  1 138 ? 37.271  43.200  -20.448 1.00 55.30  ? 130 THR J OG1 1 
ATOM   16129 C CG2 . THR J  1 138 ? 37.424  41.912  -22.479 1.00 52.75  ? 130 THR J CG2 1 
ATOM   16130 N N   . GLU J  1 139 ? 40.327  44.115  -19.969 1.00 59.28  ? 131 GLU J N   1 
ATOM   16131 C CA  . GLU J  1 139 ? 41.159  44.927  -19.075 1.00 59.36  ? 131 GLU J CA  1 
ATOM   16132 C C   . GLU J  1 139 ? 40.336  45.773  -18.117 1.00 55.15  ? 131 GLU J C   1 
ATOM   16133 O O   . GLU J  1 139 ? 40.779  46.087  -17.002 1.00 42.68  ? 131 GLU J O   1 
ATOM   16134 C CB  . GLU J  1 139 ? 42.098  45.820  -19.892 1.00 54.08  ? 131 GLU J CB  1 
ATOM   16135 C CG  . GLU J  1 139 ? 43.424  45.169  -20.232 1.00 58.03  ? 131 GLU J CG  1 
ATOM   16136 C CD  . GLU J  1 139 ? 44.482  45.454  -19.188 1.00 58.15  ? 131 GLU J CD  1 
ATOM   16137 O OE1 . GLU J  1 139 ? 44.324  46.463  -18.470 1.00 56.55  ? 131 GLU J OE1 1 
ATOM   16138 O OE2 . GLU J  1 139 ? 45.466  44.681  -19.085 1.00 56.62  ? 131 GLU J OE2 1 
ATOM   16139 N N   . SER J  1 140 ? 39.150  46.163  -18.577 1.00 58.07  ? 132 SER J N   1 
ATOM   16140 C CA  . SER J  1 140 ? 38.161  46.806  -17.722 1.00 62.12  ? 132 SER J CA  1 
ATOM   16141 C C   . SER J  1 140 ? 37.472  45.712  -16.912 1.00 59.56  ? 132 SER J C   1 
ATOM   16142 O O   . SER J  1 140 ? 36.993  45.957  -15.807 1.00 57.67  ? 132 SER J O   1 
ATOM   16143 C CB  . SER J  1 140 ? 37.139  47.582  -18.557 1.00 61.96  ? 132 SER J CB  1 
ATOM   16144 O OG  . SER J  1 140 ? 36.418  46.722  -19.430 1.00 67.10  ? 132 SER J OG  1 
ATOM   16145 N N   . GLY J  1 141 ? 37.438  44.507  -17.484 1.00 60.31  ? 133 GLY J N   1 
ATOM   16146 C CA  . GLY J  1 141 ? 36.960  43.313  -16.810 1.00 51.66  ? 133 GLY J CA  1 
ATOM   16147 C C   . GLY J  1 141 ? 35.464  43.074  -16.905 1.00 52.83  ? 133 GLY J C   1 
ATOM   16148 O O   . GLY J  1 141 ? 34.738  43.821  -17.564 1.00 51.66  ? 133 GLY J O   1 
ATOM   16149 N N   . ALA J  1 142 ? 35.014  42.003  -16.254 1.00 55.32  ? 134 ALA J N   1 
ATOM   16150 C CA  . ALA J  1 142 ? 33.593  41.732  -16.072 1.00 50.67  ? 134 ALA J CA  1 
ATOM   16151 C C   . ALA J  1 142 ? 33.105  42.485  -14.835 1.00 47.99  ? 134 ALA J C   1 
ATOM   16152 O O   . ALA J  1 142 ? 33.889  42.752  -13.927 1.00 47.62  ? 134 ALA J O   1 
ATOM   16153 C CB  . ALA J  1 142 ? 33.360  40.236  -15.913 1.00 39.58  ? 134 ALA J CB  1 
ATOM   16154 N N   . THR J  1 143 ? 31.827  42.853  -14.804 1.00 44.96  ? 135 THR J N   1 
ATOM   16155 C CA  . THR J  1 143 ? 31.241  43.421  -13.589 1.00 51.49  ? 135 THR J CA  1 
ATOM   16156 C C   . THR J  1 143 ? 30.000  42.634  -13.140 1.00 49.52  ? 135 THR J C   1 
ATOM   16157 O O   . THR J  1 143 ? 28.888  42.849  -13.638 1.00 51.00  ? 135 THR J O   1 
ATOM   16158 C CB  . THR J  1 143 ? 30.930  44.941  -13.719 1.00 55.35  ? 135 THR J CB  1 
ATOM   16159 O OG1 . THR J  1 143 ? 32.155  45.679  -13.823 1.00 47.58  ? 135 THR J OG1 1 
ATOM   16160 C CG2 . THR J  1 143 ? 30.156  45.444  -12.491 1.00 55.71  ? 135 THR J CG2 1 
ATOM   16161 N N   . CYS J  1 144 ? 30.206  41.711  -12.202 1.00 48.43  ? 136 CYS J N   1 
ATOM   16162 C CA  . CYS J  1 144 ? 29.112  40.903  -11.672 1.00 49.57  ? 136 CYS J CA  1 
ATOM   16163 C C   . CYS J  1 144 ? 28.432  41.563  -10.475 1.00 40.93  ? 136 CYS J C   1 
ATOM   16164 O O   . CYS J  1 144 ? 29.094  42.034  -9.548  1.00 40.21  ? 136 CYS J O   1 
ATOM   16165 C CB  . CYS J  1 144 ? 29.593  39.501  -11.294 1.00 43.88  ? 136 CYS J CB  1 
ATOM   16166 S SG  . CYS J  1 144 ? 28.393  38.588  -10.268 1.00 66.96  ? 136 CYS J SG  1 
ATOM   16167 N N   . ARG J  1 145 ? 27.106  41.594  -10.500 1.00 38.05  ? 137 ARG J N   1 
ATOM   16168 C CA  . ARG J  1 145 ? 26.346  42.186  -9.399  1.00 49.73  ? 137 ARG J CA  1 
ATOM   16169 C C   . ARG J  1 145 ? 25.496  41.161  -8.619  1.00 37.04  ? 137 ARG J C   1 
ATOM   16170 O O   . ARG J  1 145 ? 24.645  40.474  -9.184  1.00 35.82  ? 137 ARG J O   1 
ATOM   16171 C CB  . ARG J  1 145 ? 25.501  43.367  -9.901  1.00 50.09  ? 137 ARG J CB  1 
ATOM   16172 C CG  . ARG J  1 145 ? 25.390  43.451  -11.418 1.00 55.05  ? 137 ARG J CG  1 
ATOM   16173 C CD  . ARG J  1 145 ? 24.878  44.817  -11.880 1.00 67.12  ? 137 ARG J CD  1 
ATOM   16174 N NE  . ARG J  1 145 ? 24.814  44.920  -13.342 1.00 75.48  ? 137 ARG J NE  1 
ATOM   16175 C CZ  . ARG J  1 145 ? 25.766  45.452  -14.105 1.00 67.72  ? 137 ARG J CZ  1 
ATOM   16176 N NH1 . ARG J  1 145 ? 26.870  45.938  -13.553 1.00 61.20  ? 137 ARG J NH1 1 
ATOM   16177 N NH2 . ARG J  1 145 ? 25.614  45.499  -15.423 1.00 66.38  ? 137 ARG J NH2 1 
ATOM   16178 N N   . ILE J  1 146 ? 25.754  41.054  -7.320  1.00 34.07  ? 138 ILE J N   1 
ATOM   16179 C CA  . ILE J  1 146 ? 25.004  40.146  -6.449  1.00 42.25  ? 138 ILE J CA  1 
ATOM   16180 C C   . ILE J  1 146 ? 24.034  40.918  -5.545  1.00 37.55  ? 138 ILE J C   1 
ATOM   16181 O O   . ILE J  1 146 ? 24.460  41.782  -4.774  1.00 32.20  ? 138 ILE J O   1 
ATOM   16182 C CB  . ILE J  1 146 ? 25.956  39.308  -5.556  1.00 37.08  ? 138 ILE J CB  1 
ATOM   16183 C CG1 . ILE J  1 146 ? 26.764  38.327  -6.402  1.00 31.98  ? 138 ILE J CG1 1 
ATOM   16184 C CG2 . ILE J  1 146 ? 25.180  38.541  -4.504  1.00 29.81  ? 138 ILE J CG2 1 
ATOM   16185 C CD1 . ILE J  1 146 ? 27.886  37.675  -5.641  1.00 28.69  ? 138 ILE J CD1 1 
ATOM   16186 N N   . LYS J  1 147 ? 22.740  40.613  -5.641  1.00 29.86  ? 139 LYS J N   1 
ATOM   16187 C CA  . LYS J  1 147 ? 21.749  41.255  -4.768  1.00 39.62  ? 139 LYS J CA  1 
ATOM   16188 C C   . LYS J  1 147 ? 21.473  40.470  -3.473  1.00 33.36  ? 139 LYS J C   1 
ATOM   16189 O O   . LYS J  1 147 ? 21.112  39.297  -3.501  1.00 30.48  ? 139 LYS J O   1 
ATOM   16190 C CB  . LYS J  1 147 ? 20.437  41.511  -5.514  1.00 44.97  ? 139 LYS J CB  1 
ATOM   16191 C CG  . LYS J  1 147 ? 20.521  42.535  -6.637  1.00 54.27  ? 139 LYS J CG  1 
ATOM   16192 C CD  . LYS J  1 147 ? 19.124  42.993  -7.028  1.00 62.13  ? 139 LYS J CD  1 
ATOM   16193 C CE  . LYS J  1 147 ? 19.162  44.099  -8.067  1.00 69.21  ? 139 LYS J CE  1 
ATOM   16194 N NZ  . LYS J  1 147 ? 17.792  44.589  -8.390  1.00 65.09  ? 139 LYS J NZ  1 
ATOM   16195 N N   . ILE J  1 148 ? 21.638  41.127  -2.335  1.00 38.09  ? 140 ILE J N   1 
ATOM   16196 C CA  . ILE J  1 148 ? 21.403  40.473  -1.051  1.00 36.33  ? 140 ILE J CA  1 
ATOM   16197 C C   . ILE J  1 148 ? 20.340  41.201  -0.243  1.00 35.56  ? 140 ILE J C   1 
ATOM   16198 O O   . ILE J  1 148 ? 20.534  42.355  0.116   1.00 38.48  ? 140 ILE J O   1 
ATOM   16199 C CB  . ILE J  1 148 ? 22.698  40.407  -0.215  1.00 32.41  ? 140 ILE J CB  1 
ATOM   16200 C CG1 . ILE J  1 148 ? 23.694  39.435  -0.850  1.00 40.44  ? 140 ILE J CG1 1 
ATOM   16201 C CG2 . ILE J  1 148 ? 22.410  39.965  1.199   1.00 24.85  ? 140 ILE J CG2 1 
ATOM   16202 C CD1 . ILE J  1 148 ? 24.871  39.105  0.053   1.00 39.08  ? 140 ILE J CD1 1 
ATOM   16203 N N   . GLY J  1 149 ? 19.230  40.529  0.059   1.00 36.17  ? 141 GLY J N   1 
ATOM   16204 C CA  . GLY J  1 149 ? 18.215  41.108  0.932   1.00 34.41  ? 141 GLY J CA  1 
ATOM   16205 C C   . GLY J  1 149 ? 17.502  40.142  1.867   1.00 27.37  ? 141 GLY J C   1 
ATOM   16206 O O   . GLY J  1 149 ? 17.816  38.947  1.907   1.00 21.45  ? 141 GLY J O   1 
ATOM   16207 N N   . SER J  1 150 ? 16.537  40.661  2.628   1.00 25.29  ? 142 SER J N   1 
ATOM   16208 C CA  . SER J  1 150 ? 15.683  39.799  3.442   1.00 20.77  ? 142 SER J CA  1 
ATOM   16209 C C   . SER J  1 150 ? 14.707  39.041  2.559   1.00 20.92  ? 142 SER J C   1 
ATOM   16210 O O   . SER J  1 150 ? 13.996  39.639  1.758   1.00 23.97  ? 142 SER J O   1 
ATOM   16211 C CB  . SER J  1 150 ? 14.896  40.602  4.490   1.00 26.15  ? 142 SER J CB  1 
ATOM   16212 O OG  . SER J  1 150 ? 14.185  39.743  5.388   1.00 23.34  ? 142 SER J OG  1 
ATOM   16213 N N   . TRP J  1 151 ? 14.649  37.727  2.732   1.00 18.96  ? 143 TRP J N   1 
ATOM   16214 C CA  . TRP J  1 151 ? 13.734  36.906  1.953   1.00 19.22  ? 143 TRP J CA  1 
ATOM   16215 C C   . TRP J  1 151 ? 12.230  37.046  2.258   1.00 21.40  ? 143 TRP J C   1 
ATOM   16216 O O   . TRP J  1 151 ? 11.415  36.812  1.374   1.00 23.31  ? 143 TRP J O   1 
ATOM   16217 C CB  . TRP J  1 151 ? 14.140  35.434  2.017   1.00 16.54  ? 143 TRP J CB  1 
ATOM   16218 C CG  . TRP J  1 151 ? 13.347  34.608  1.067   1.00 24.42  ? 143 TRP J CG  1 
ATOM   16219 C CD1 . TRP J  1 151 ? 12.538  33.555  1.368   1.00 23.29  ? 143 TRP J CD1 1 
ATOM   16220 C CD2 . TRP J  1 151 ? 13.270  34.782  -0.355  1.00 26.76  ? 143 TRP J CD2 1 
ATOM   16221 N NE1 . TRP J  1 151 ? 11.966  33.055  0.219   1.00 28.95  ? 143 TRP J NE1 1 
ATOM   16222 C CE2 . TRP J  1 151 ? 12.400  33.791  -0.851  1.00 25.71  ? 143 TRP J CE2 1 
ATOM   16223 C CE3 . TRP J  1 151 ? 13.854  35.678  -1.252  1.00 27.28  ? 143 TRP J CE3 1 
ATOM   16224 C CZ2 . TRP J  1 151 ? 12.097  33.672  -2.202  1.00 31.14  ? 143 TRP J CZ2 1 
ATOM   16225 C CZ3 . TRP J  1 151 ? 13.548  35.562  -2.599  1.00 35.13  ? 143 TRP J CZ3 1 
ATOM   16226 C CH2 . TRP J  1 151 ? 12.681  34.563  -3.062  1.00 32.10  ? 143 TRP J CH2 1 
ATOM   16227 N N   . THR J  1 152 ? 11.860  37.395  3.493   1.00 20.99  ? 144 THR J N   1 
ATOM   16228 C CA  . THR J  1 152 ? 10.446  37.389  3.890   1.00 19.91  ? 144 THR J CA  1 
ATOM   16229 C C   . THR J  1 152 ? 10.028  38.680  4.582   1.00 21.95  ? 144 THR J C   1 
ATOM   16230 O O   . THR J  1 152 ? 8.840   38.949  4.729   1.00 23.52  ? 144 THR J O   1 
ATOM   16231 C CB  . THR J  1 152 ? 10.074  36.195  4.836   1.00 19.35  ? 144 THR J CB  1 
ATOM   16232 O OG1 . THR J  1 152 ? 10.402  36.522  6.195   1.00 22.16  ? 144 THR J OG1 1 
ATOM   16233 C CG2 . THR J  1 152 ? 10.788  34.907  4.445   1.00 15.47  ? 144 THR J CG2 1 
ATOM   16234 N N   . HIS J  1 153 ? 10.999  39.480  5.010   1.00 22.16  ? 145 HIS J N   1 
ATOM   16235 C CA  . HIS J  1 153 ? 10.695  40.747  5.691   1.00 26.56  ? 145 HIS J CA  1 
ATOM   16236 C C   . HIS J  1 153 ? 10.865  42.006  4.815   1.00 28.86  ? 145 HIS J C   1 
ATOM   16237 O O   . HIS J  1 153 ? 11.848  42.128  4.089   1.00 33.05  ? 145 HIS J O   1 
ATOM   16238 C CB  . HIS J  1 153 ? 11.537  40.886  6.976   1.00 24.50  ? 145 HIS J CB  1 
ATOM   16239 C CG  . HIS J  1 153 ? 11.351  39.757  7.951   1.00 25.86  ? 145 HIS J CG  1 
ATOM   16240 N ND1 . HIS J  1 153 ? 12.164  38.642  7.965   1.00 21.67  ? 145 HIS J ND1 1 
ATOM   16241 C CD2 . HIS J  1 153 ? 10.438  39.565  8.935   1.00 23.22  ? 145 HIS J CD2 1 
ATOM   16242 C CE1 . HIS J  1 153 ? 11.760  37.814  8.912   1.00 18.64  ? 145 HIS J CE1 1 
ATOM   16243 N NE2 . HIS J  1 153 ? 10.716  38.352  9.517   1.00 18.45  ? 145 HIS J NE2 1 
ATOM   16244 N N   . HIS J  1 154 ? 9.899   42.928  4.893   1.00 33.50  ? 146 HIS J N   1 
ATOM   16245 C CA  . HIS J  1 154 ? 10.030  44.200  4.201   1.00 36.22  ? 146 HIS J CA  1 
ATOM   16246 C C   . HIS J  1 154 ? 10.672  45.250  5.084   1.00 36.63  ? 146 HIS J C   1 
ATOM   16247 O O   . HIS J  1 154 ? 11.001  44.976  6.255   1.00 33.33  ? 146 HIS J O   1 
ATOM   16248 C CB  . HIS J  1 154 ? 8.680   44.690  3.716   1.00 41.63  ? 146 HIS J CB  1 
ATOM   16249 C CG  . HIS J  1 154 ? 7.653   44.845  4.801   1.00 42.14  ? 146 HIS J CG  1 
ATOM   16250 N ND1 . HIS J  1 154 ? 6.811   43.824  5.185   1.00 41.54  ? 146 HIS J ND1 1 
ATOM   16251 C CD2 . HIS J  1 154 ? 7.301   45.918  5.547   1.00 41.41  ? 146 HIS J CD2 1 
ATOM   16252 C CE1 . HIS J  1 154 ? 5.998   44.254  6.137   1.00 41.59  ? 146 HIS J CE1 1 
ATOM   16253 N NE2 . HIS J  1 154 ? 6.269   45.523  6.369   1.00 42.11  ? 146 HIS J NE2 1 
ATOM   16254 N N   . SER J  1 155 ? 10.904  46.432  4.533   1.00 35.24  ? 147 SER J N   1 
ATOM   16255 C CA  . SER J  1 155 ? 11.682  47.428  5.217   1.00 34.48  ? 147 SER J CA  1 
ATOM   16256 C C   . SER J  1 155 ? 10.964  48.123  6.352   1.00 36.93  ? 147 SER J C   1 
ATOM   16257 O O   . SER J  1 155 ? 11.547  49.010  6.967   1.00 39.79  ? 147 SER J O   1 
ATOM   16258 C CB  . SER J  1 155 ? 12.138  48.481  4.217   1.00 41.17  ? 147 SER J CB  1 
ATOM   16259 O OG  . SER J  1 155 ? 10.975  49.216  3.809   1.00 33.43  ? 147 SER J OG  1 
ATOM   16260 N N   . ARG J  1 156 ? 9.699   47.776  6.591   1.00 37.50  ? 148 ARG J N   1 
ATOM   16261 C CA  . ARG J  1 156 ? 9.051   48.175  7.843   1.00 39.98  ? 148 ARG J CA  1 
ATOM   16262 C C   . ARG J  1 156 ? 9.524   47.239  8.957   1.00 30.16  ? 148 ARG J C   1 
ATOM   16263 O O   . ARG J  1 156 ? 9.666   47.642  10.111  1.00 32.11  ? 148 ARG J O   1 
ATOM   16264 C CB  . ARG J  1 156 ? 7.525   48.191  7.737   1.00 46.23  ? 148 ARG J CB  1 
ATOM   16265 C CG  . ARG J  1 156 ? 7.004   49.153  6.684   1.00 51.33  ? 148 ARG J CG  1 
ATOM   16266 C CD  . ARG J  1 156 ? 5.496   49.154  6.591   1.00 61.41  ? 148 ARG J CD  1 
ATOM   16267 N NE  . ARG J  1 156 ? 5.065   49.530  5.246   1.00 74.90  ? 148 ARG J NE  1 
ATOM   16268 C CZ  . ARG J  1 156 ? 4.174   48.854  4.522   1.00 76.38  ? 148 ARG J CZ  1 
ATOM   16269 N NH1 . ARG J  1 156 ? 3.593   47.765  5.019   1.00 67.31  ? 148 ARG J NH1 1 
ATOM   16270 N NH2 . ARG J  1 156 ? 3.858   49.271  3.298   1.00 63.95  ? 148 ARG J NH2 1 
ATOM   16271 N N   . GLU J  1 157 ? 9.802   45.995  8.577   1.00 25.00  ? 149 GLU J N   1 
ATOM   16272 C CA  . GLU J  1 157 ? 10.333  44.979  9.478   1.00 22.22  ? 149 GLU J CA  1 
ATOM   16273 C C   . GLU J  1 157 ? 11.871  44.914  9.508   1.00 26.22  ? 149 GLU J C   1 
ATOM   16274 O O   . GLU J  1 157 ? 12.479  45.036  10.578  1.00 22.02  ? 149 GLU J O   1 
ATOM   16275 C CB  . GLU J  1 157 ? 9.726   43.612  9.132   1.00 24.81  ? 149 GLU J CB  1 
ATOM   16276 C CG  . GLU J  1 157 ? 8.217   43.544  9.359   1.00 28.10  ? 149 GLU J CG  1 
ATOM   16277 C CD  . GLU J  1 157 ? 7.527   42.530  8.461   1.00 37.41  ? 149 GLU J CD  1 
ATOM   16278 O OE1 . GLU J  1 157 ? 8.187   42.061  7.502   1.00 36.34  ? 149 GLU J OE1 1 
ATOM   16279 O OE2 . GLU J  1 157 ? 6.334   42.202  8.713   1.00 31.15  ? 149 GLU J OE2 1 
ATOM   16280 N N   . ILE J  1 158 ? 12.501  44.726  8.345   1.00 26.04  ? 150 ILE J N   1 
ATOM   16281 C CA  . ILE J  1 158 ? 13.964  44.701  8.270   1.00 24.43  ? 150 ILE J CA  1 
ATOM   16282 C C   . ILE J  1 158 ? 14.528  45.672  7.235   1.00 30.65  ? 150 ILE J C   1 
ATOM   16283 O O   . ILE J  1 158 ? 14.093  45.708  6.084   1.00 29.70  ? 150 ILE J O   1 
ATOM   16284 C CB  . ILE J  1 158 ? 14.524  43.286  7.997   1.00 24.77  ? 150 ILE J CB  1 
ATOM   16285 C CG1 . ILE J  1 158 ? 14.203  42.354  9.155   1.00 23.51  ? 150 ILE J CG1 1 
ATOM   16286 C CG2 . ILE J  1 158 ? 16.037  43.321  7.821   1.00 26.39  ? 150 ILE J CG2 1 
ATOM   16287 C CD1 . ILE J  1 158 ? 14.915  41.033  9.064   1.00 22.79  ? 150 ILE J CD1 1 
ATOM   16288 N N   . SER J  1 159 ? 15.513  46.454  7.653   1.00 31.01  ? 151 SER J N   1 
ATOM   16289 C CA  . SER J  1 159 ? 16.143  47.401  6.759   1.00 33.50  ? 151 SER J CA  1 
ATOM   16290 C C   . SER J  1 159 ? 17.590  47.005  6.557   1.00 35.02  ? 151 SER J C   1 
ATOM   16291 O O   . SER J  1 159 ? 18.343  46.824  7.515   1.00 34.94  ? 151 SER J O   1 
ATOM   16292 C CB  . SER J  1 159 ? 16.040  48.823  7.310   1.00 37.78  ? 151 SER J CB  1 
ATOM   16293 O OG  . SER J  1 159 ? 16.891  49.004  8.426   1.00 40.81  ? 151 SER J OG  1 
ATOM   16294 N N   . VAL J  1 160 ? 18.003  46.918  5.296   1.00 41.52  ? 152 VAL J N   1 
ATOM   16295 C CA  . VAL J  1 160 ? 19.364  46.505  4.966   1.00 43.76  ? 152 VAL J CA  1 
ATOM   16296 C C   . VAL J  1 160 ? 20.248  47.690  4.582   1.00 43.52  ? 152 VAL J C   1 
ATOM   16297 O O   . VAL J  1 160 ? 19.886  48.502  3.730   1.00 47.67  ? 152 VAL J O   1 
ATOM   16298 C CB  . VAL J  1 160 ? 19.377  45.477  3.819   1.00 37.17  ? 152 VAL J CB  1 
ATOM   16299 C CG1 . VAL J  1 160 ? 20.664  44.665  3.850   1.00 39.04  ? 152 VAL J CG1 1 
ATOM   16300 C CG2 . VAL J  1 160 ? 18.162  44.566  3.909   1.00 41.25  ? 152 VAL J CG2 1 
ATOM   16301 N N   . ASP J  1 161 ? 21.408  47.777  5.225   1.00 44.00  ? 153 ASP J N   1 
ATOM   16302 C CA  . ASP J  1 161 ? 22.349  48.866  5.004   1.00 46.61  ? 153 ASP J CA  1 
ATOM   16303 C C   . ASP J  1 161 ? 23.753  48.329  4.741   1.00 49.86  ? 153 ASP J C   1 
ATOM   16304 O O   . ASP J  1 161 ? 24.129  47.265  5.231   1.00 45.91  ? 153 ASP J O   1 
ATOM   16305 C CB  . ASP J  1 161 ? 22.364  49.814  6.205   1.00 43.32  ? 153 ASP J CB  1 
ATOM   16306 C CG  . ASP J  1 161 ? 20.990  50.367  6.527   1.00 49.17  ? 153 ASP J CG  1 
ATOM   16307 O OD1 . ASP J  1 161 ? 20.316  50.866  5.602   1.00 45.57  ? 153 ASP J OD1 1 
ATOM   16308 O OD2 . ASP J  1 161 ? 20.584  50.303  7.707   1.00 52.19  ? 153 ASP J OD2 1 
ATOM   16309 N N   . PRO J  1 162 ? 24.514  49.080  3.955   1.00 55.51  ? 154 PRO J N   1 
ATOM   16310 C CA  . PRO J  1 162 ? 25.843  48.679  3.517   1.00 50.57  ? 154 PRO J CA  1 
ATOM   16311 C C   . PRO J  1 162 ? 26.853  49.556  4.205   1.00 54.06  ? 154 PRO J C   1 
ATOM   16312 O O   . PRO J  1 162 ? 26.827  50.784  4.127   1.00 56.48  ? 154 PRO J O   1 
ATOM   16313 C CB  . PRO J  1 162 ? 25.818  48.978  2.018   1.00 49.33  ? 154 PRO J CB  1 
ATOM   16314 C CG  . PRO J  1 162 ? 24.856  50.107  1.885   1.00 54.77  ? 154 PRO J CG  1 
ATOM   16315 C CD  . PRO J  1 162 ? 23.805  49.872  2.934   1.00 46.27  ? 154 PRO J CD  1 
ATOM   16316 N N   . THR J  1 163 ? 27.602  48.891  5.097   1.00 56.00  ? 155 THR J N   1 
ATOM   16317 C CA  . THR J  1 163 ? 28.585  49.504  6.017   1.00 57.29  ? 155 THR J CA  1 
ATOM   16318 C C   . THR J  1 163 ? 29.897  50.096  5.475   1.00 66.02  ? 155 THR J C   1 
ATOM   16319 O O   . THR J  1 163 ? 30.262  51.216  5.832   1.00 67.08  ? 155 THR J O   1 
ATOM   16320 C CB  . THR J  1 163 ? 28.944  48.529  7.159   1.00 56.06  ? 155 THR J CB  1 
ATOM   16321 O OG1 . THR J  1 163 ? 29.830  49.175  8.082   1.00 65.99  ? 155 THR J OG1 1 
ATOM   16322 C CG2 . THR J  1 163 ? 29.617  47.284  6.604   1.00 50.96  ? 155 THR J CG2 1 
ATOM   16323 N N   . THR J  1 164 ? 30.589  49.363  4.605   1.00 68.88  ? 156 THR J N   1 
ATOM   16324 C CA  . THR J  1 164 ? 31.683  49.939  3.843   1.00 79.12  ? 156 THR J CA  1 
ATOM   16325 C C   . THR J  1 164 ? 31.174  50.138  2.430   1.00 83.73  ? 156 THR J C   1 
ATOM   16326 O O   . THR J  1 164 ? 30.633  49.214  1.822   1.00 73.96  ? 156 THR J O   1 
ATOM   16327 C CB  . THR J  1 164 ? 32.911  49.013  3.820   1.00 78.68  ? 156 THR J CB  1 
ATOM   16328 O OG1 . THR J  1 164 ? 33.494  48.955  5.128   1.00 74.33  ? 156 THR J OG1 1 
ATOM   16329 C CG2 . THR J  1 164 ? 33.946  49.526  2.831   1.00 68.30  ? 156 THR J CG2 1 
ATOM   16330 N N   . GLU J  1 165 ? 31.334  51.346  1.908   1.00 87.55  ? 157 GLU J N   1 
ATOM   16331 C CA  . GLU J  1 165 ? 30.756  51.670  0.597   1.00 77.05  ? 157 GLU J CA  1 
ATOM   16332 C C   . GLU J  1 165 ? 31.716  51.397  -0.553  1.00 69.89  ? 157 GLU J C   1 
ATOM   16333 O O   . GLU J  1 165 ? 31.294  51.008  -1.645  1.00 58.07  ? 157 GLU J O   1 
ATOM   16334 C CB  . GLU J  1 165 ? 30.334  53.141  0.547   1.00 69.40  ? 157 GLU J CB  1 
ATOM   16335 C CG  . GLU J  1 165 ? 28.895  53.367  0.104   1.00 71.87  ? 157 GLU J CG  1 
ATOM   16336 C CD  . GLU J  1 165 ? 27.878  53.005  1.181   1.00 70.18  ? 157 GLU J CD  1 
ATOM   16337 O OE1 . GLU J  1 165 ? 28.262  52.897  2.369   1.00 66.83  ? 157 GLU J OE1 1 
ATOM   16338 O OE2 . GLU J  1 165 ? 26.690  52.828  0.832   1.00 63.10  ? 157 GLU J OE2 1 
ATOM   16339 N N   . ASN J  1 166 ? 33.005  51.611  -0.298  1.00 74.53  ? 158 ASN J N   1 
ATOM   16340 C CA  . ASN J  1 166 ? 34.032  51.457  -1.322  1.00 73.32  ? 158 ASN J CA  1 
ATOM   16341 C C   . ASN J  1 166 ? 35.313  50.784  -0.817  1.00 73.97  ? 158 ASN J C   1 
ATOM   16342 O O   . ASN J  1 166 ? 36.190  51.443  -0.249  1.00 73.38  ? 158 ASN J O   1 
ATOM   16343 C CB  . ASN J  1 166 ? 34.363  52.817  -1.944  1.00 70.20  ? 158 ASN J CB  1 
ATOM   16344 C CG  . ASN J  1 166 ? 34.649  52.722  -3.431  1.00 74.59  ? 158 ASN J CG  1 
ATOM   16345 O OD1 . ASN J  1 166 ? 35.773  52.426  -3.843  1.00 77.33  ? 158 ASN J OD1 1 
ATOM   16346 N ND2 . ASN J  1 166 ? 33.629  52.971  -4.247  1.00 68.99  ? 158 ASN J ND2 1 
ATOM   16347 N N   . SER J  1 167 ? 35.400  49.469  -1.020  1.00 75.66  ? 159 SER J N   1 
ATOM   16348 C CA  . SER J  1 167 ? 36.610  48.690  -0.747  1.00 72.83  ? 159 SER J CA  1 
ATOM   16349 C C   . SER J  1 167 ? 37.212  48.196  -2.064  1.00 79.83  ? 159 SER J C   1 
ATOM   16350 O O   . SER J  1 167 ? 36.608  48.361  -3.130  1.00 77.94  ? 159 SER J O   1 
ATOM   16351 C CB  . SER J  1 167 ? 36.298  47.481  0.148   1.00 66.68  ? 159 SER J CB  1 
ATOM   16352 O OG  . SER J  1 167 ? 36.615  47.729  1.506   1.00 70.87  ? 159 SER J OG  1 
ATOM   16353 N N   . ASP J  1 168 ? 38.411  47.616  -1.990  1.00 81.76  ? 160 ASP J N   1 
ATOM   16354 C CA  . ASP J  1 168 ? 38.930  46.775  -3.073  1.00 76.45  ? 160 ASP J CA  1 
ATOM   16355 C C   . ASP J  1 168 ? 39.199  45.368  -2.514  1.00 74.26  ? 160 ASP J C   1 
ATOM   16356 O O   . ASP J  1 168 ? 39.583  44.448  -3.244  1.00 69.36  ? 160 ASP J O   1 
ATOM   16357 C CB  . ASP J  1 168 ? 40.152  47.399  -3.790  1.00 76.64  ? 160 ASP J CB  1 
ATOM   16358 C CG  . ASP J  1 168 ? 41.290  47.774  -2.842  1.00 74.54  ? 160 ASP J CG  1 
ATOM   16359 O OD1 . ASP J  1 168 ? 41.087  47.781  -1.608  1.00 68.50  ? 160 ASP J OD1 1 
ATOM   16360 O OD2 . ASP J  1 168 ? 42.397  48.081  -3.344  1.00 78.97  ? 160 ASP J OD2 1 
ATOM   16361 N N   . ASP J  1 169 ? 39.004  45.196  -1.215  1.00 67.87  ? 161 ASP J N   1 
ATOM   16362 C CA  . ASP J  1 169 ? 39.047  43.865  -0.627  1.00 59.29  ? 161 ASP J CA  1 
ATOM   16363 C C   . ASP J  1 169 ? 40.400  43.221  -0.892  1.00 60.52  ? 161 ASP J C   1 
ATOM   16364 O O   . ASP J  1 169 ? 40.514  42.000  -0.996  1.00 53.65  ? 161 ASP J O   1 
ATOM   16365 C CB  . ASP J  1 169 ? 37.927  42.991  -1.193  1.00 58.42  ? 161 ASP J CB  1 
ATOM   16366 C CG  . ASP J  1 169 ? 36.588  43.262  -0.536  1.00 51.28  ? 161 ASP J CG  1 
ATOM   16367 O OD1 . ASP J  1 169 ? 36.563  43.960  0.499   1.00 57.86  ? 161 ASP J OD1 1 
ATOM   16368 O OD2 . ASP J  1 169 ? 35.561  42.776  -1.054  1.00 42.19  ? 161 ASP J OD2 1 
ATOM   16369 N N   . SER J  1 170 ? 41.423  44.059  -0.989  1.00 70.93  ? 162 SER J N   1 
ATOM   16370 C CA  . SER J  1 170 ? 42.810  43.603  -1.099  1.00 72.48  ? 162 SER J CA  1 
ATOM   16371 C C   . SER J  1 170 ? 43.300  42.980  0.210   1.00 65.90  ? 162 SER J C   1 
ATOM   16372 O O   . SER J  1 170 ? 44.266  42.208  0.231   1.00 56.51  ? 162 SER J O   1 
ATOM   16373 C CB  . SER J  1 170 ? 43.723  44.769  -1.507  1.00 68.51  ? 162 SER J CB  1 
ATOM   16374 O OG  . SER J  1 170 ? 43.652  45.832  -0.565  1.00 67.39  ? 162 SER J OG  1 
ATOM   16375 N N   . GLU J  1 171 ? 42.618  43.319  1.298   1.00 57.41  ? 163 GLU J N   1 
ATOM   16376 C CA  . GLU J  1 171 ? 42.934  42.764  2.600   1.00 63.75  ? 163 GLU J CA  1 
ATOM   16377 C C   . GLU J  1 171 ? 42.719  41.245  2.653   1.00 64.85  ? 163 GLU J C   1 
ATOM   16378 O O   . GLU J  1 171 ? 43.507  40.520  3.271   1.00 63.91  ? 163 GLU J O   1 
ATOM   16379 C CB  . GLU J  1 171 ? 42.091  43.460  3.672   1.00 63.86  ? 163 GLU J CB  1 
ATOM   16380 C CG  . GLU J  1 171 ? 42.898  44.277  4.675   1.00 67.95  ? 163 GLU J CG  1 
ATOM   16381 C CD  . GLU J  1 171 ? 43.560  43.416  5.741   1.00 71.74  ? 163 GLU J CD  1 
ATOM   16382 O OE1 . GLU J  1 171 ? 43.099  43.453  6.908   1.00 71.94  ? 163 GLU J OE1 1 
ATOM   16383 O OE2 . GLU J  1 171 ? 44.543  42.710  5.416   1.00 63.84  ? 163 GLU J OE2 1 
ATOM   16384 N N   . TYR J  1 172 ? 41.673  40.763  1.983   1.00 57.01  ? 164 TYR J N   1 
ATOM   16385 C CA  . TYR J  1 172 ? 41.195  39.403  2.217   1.00 43.79  ? 164 TYR J CA  1 
ATOM   16386 C C   . TYR J  1 172 ? 41.300  38.443  1.036   1.00 39.72  ? 164 TYR J C   1 
ATOM   16387 O O   . TYR J  1 172 ? 41.447  37.234  1.234   1.00 36.45  ? 164 TYR J O   1 
ATOM   16388 C CB  . TYR J  1 172 ? 39.758  39.451  2.734   1.00 49.37  ? 164 TYR J CB  1 
ATOM   16389 C CG  . TYR J  1 172 ? 39.594  40.366  3.926   1.00 56.59  ? 164 TYR J CG  1 
ATOM   16390 C CD1 . TYR J  1 172 ? 38.821  41.516  3.843   1.00 55.16  ? 164 TYR J CD1 1 
ATOM   16391 C CD2 . TYR J  1 172 ? 40.241  40.095  5.125   1.00 59.37  ? 164 TYR J CD2 1 
ATOM   16392 C CE1 . TYR J  1 172 ? 38.679  42.362  4.928   1.00 57.16  ? 164 TYR J CE1 1 
ATOM   16393 C CE2 . TYR J  1 172 ? 40.107  40.935  6.215   1.00 63.93  ? 164 TYR J CE2 1 
ATOM   16394 C CZ  . TYR J  1 172 ? 39.324  42.068  6.113   1.00 64.09  ? 164 TYR J CZ  1 
ATOM   16395 O OH  . TYR J  1 172 ? 39.190  42.906  7.201   1.00 62.97  ? 164 TYR J OH  1 
ATOM   16396 N N   . PHE J  1 173 ? 41.229  38.973  -0.182  1.00 36.10  ? 165 PHE J N   1 
ATOM   16397 C CA  . PHE J  1 173 ? 41.257  38.132  -1.381  1.00 35.44  ? 165 PHE J CA  1 
ATOM   16398 C C   . PHE J  1 173 ? 42.523  37.284  -1.524  1.00 37.55  ? 165 PHE J C   1 
ATOM   16399 O O   . PHE J  1 173 ? 43.641  37.748  -1.282  1.00 40.48  ? 165 PHE J O   1 
ATOM   16400 C CB  . PHE J  1 173 ? 41.032  38.963  -2.652  1.00 41.59  ? 165 PHE J CB  1 
ATOM   16401 C CG  . PHE J  1 173 ? 40.571  38.148  -3.836  1.00 41.08  ? 165 PHE J CG  1 
ATOM   16402 C CD1 . PHE J  1 173 ? 39.290  37.614  -3.867  1.00 31.75  ? 165 PHE J CD1 1 
ATOM   16403 C CD2 . PHE J  1 173 ? 41.419  37.905  -4.913  1.00 42.28  ? 165 PHE J CD2 1 
ATOM   16404 C CE1 . PHE J  1 173 ? 38.855  36.869  -4.958  1.00 40.44  ? 165 PHE J CE1 1 
ATOM   16405 C CE2 . PHE J  1 173 ? 40.990  37.148  -6.011  1.00 41.96  ? 165 PHE J CE2 1 
ATOM   16406 C CZ  . PHE J  1 173 ? 39.705  36.629  -6.033  1.00 34.86  ? 165 PHE J CZ  1 
ATOM   16407 N N   . SER J  1 174 ? 42.330  36.030  -1.915  1.00 37.85  ? 166 SER J N   1 
ATOM   16408 C CA  . SER J  1 174 ? 43.442  35.116  -2.113  1.00 35.81  ? 166 SER J CA  1 
ATOM   16409 C C   . SER J  1 174 ? 44.346  35.603  -3.228  1.00 39.84  ? 166 SER J C   1 
ATOM   16410 O O   . SER J  1 174 ? 43.886  35.902  -4.333  1.00 38.44  ? 166 SER J O   1 
ATOM   16411 C CB  . SER J  1 174 ? 42.933  33.721  -2.451  1.00 36.24  ? 166 SER J CB  1 
ATOM   16412 O OG  . SER J  1 174 ? 44.007  32.869  -2.794  1.00 38.22  ? 166 SER J OG  1 
ATOM   16413 N N   . GLN J  1 175 ? 45.636  35.682  -2.922  1.00 43.68  ? 167 GLN J N   1 
ATOM   16414 C CA  . GLN J  1 175 ? 46.640  36.045  -3.907  1.00 38.68  ? 167 GLN J CA  1 
ATOM   16415 C C   . GLN J  1 175 ? 46.801  34.904  -4.915  1.00 43.33  ? 167 GLN J C   1 
ATOM   16416 O O   . GLN J  1 175 ? 47.145  35.142  -6.078  1.00 40.19  ? 167 GLN J O   1 
ATOM   16417 C CB  . GLN J  1 175 ? 47.982  36.363  -3.225  1.00 30.48  ? 167 GLN J CB  1 
ATOM   16418 C CG  . GLN J  1 175 ? 48.772  35.126  -2.793  1.00 42.05  ? 167 GLN J CG  1 
ATOM   16419 C CD  . GLN J  1 175 ? 49.860  35.435  -1.781  1.00 49.40  ? 167 GLN J CD  1 
ATOM   16420 O OE1 . GLN J  1 175 ? 49.699  36.301  -0.923  1.00 48.47  ? 167 GLN J OE1 1 
ATOM   16421 N NE2 . GLN J  1 175 ? 50.973  34.716  -1.873  1.00 50.86  ? 167 GLN J NE2 1 
ATOM   16422 N N   . TYR J  1 176 ? 46.532  33.673  -4.471  1.00 40.74  ? 168 TYR J N   1 
ATOM   16423 C CA  . TYR J  1 176 ? 46.783  32.489  -5.292  1.00 36.37  ? 168 TYR J CA  1 
ATOM   16424 C C   . TYR J  1 176 ? 45.675  32.253  -6.310  1.00 38.86  ? 168 TYR J C   1 
ATOM   16425 O O   . TYR J  1 176 ? 45.782  31.381  -7.175  1.00 37.23  ? 168 TYR J O   1 
ATOM   16426 C CB  . TYR J  1 176 ? 46.962  31.246  -4.427  1.00 40.26  ? 168 TYR J CB  1 
ATOM   16427 C CG  . TYR J  1 176 ? 48.034  31.361  -3.368  1.00 51.54  ? 168 TYR J CG  1 
ATOM   16428 C CD1 . TYR J  1 176 ? 49.351  31.673  -3.706  1.00 50.39  ? 168 TYR J CD1 1 
ATOM   16429 C CD2 . TYR J  1 176 ? 47.735  31.133  -2.030  1.00 48.30  ? 168 TYR J CD2 1 
ATOM   16430 C CE1 . TYR J  1 176 ? 50.338  31.771  -2.731  1.00 48.14  ? 168 TYR J CE1 1 
ATOM   16431 C CE2 . TYR J  1 176 ? 48.708  31.218  -1.053  1.00 57.22  ? 168 TYR J CE2 1 
ATOM   16432 C CZ  . TYR J  1 176 ? 50.009  31.538  -1.405  1.00 61.84  ? 168 TYR J CZ  1 
ATOM   16433 O OH  . TYR J  1 176 ? 50.972  31.626  -0.418  1.00 62.22  ? 168 TYR J OH  1 
ATOM   16434 N N   . SER J  1 177 ? 44.614  33.043  -6.206  1.00 35.30  ? 169 SER J N   1 
ATOM   16435 C CA  . SER J  1 177 ? 43.496  32.979  -7.136  1.00 31.76  ? 169 SER J CA  1 
ATOM   16436 C C   . SER J  1 177 ? 43.945  33.214  -8.569  1.00 35.83  ? 169 SER J C   1 
ATOM   16437 O O   . SER J  1 177 ? 45.065  33.649  -8.820  1.00 32.36  ? 169 SER J O   1 
ATOM   16438 C CB  . SER J  1 177 ? 42.468  34.047  -6.759  1.00 36.88  ? 169 SER J CB  1 
ATOM   16439 O OG  . SER J  1 177 ? 41.532  34.270  -7.800  1.00 31.95  ? 169 SER J OG  1 
ATOM   16440 N N   . ARG J  1 178 ? 43.059  32.948  -9.516  1.00 38.30  ? 170 ARG J N   1 
ATOM   16441 C CA  . ARG J  1 178 ? 43.363  33.248  -10.904 1.00 32.14  ? 170 ARG J CA  1 
ATOM   16442 C C   . ARG J  1 178 ? 42.916  34.631  -11.327 1.00 35.60  ? 170 ARG J C   1 
ATOM   16443 O O   . ARG J  1 178 ? 43.247  35.090  -12.413 1.00 46.75  ? 170 ARG J O   1 
ATOM   16444 C CB  . ARG J  1 178 ? 42.741  32.218  -11.825 1.00 28.67  ? 170 ARG J CB  1 
ATOM   16445 C CG  . ARG J  1 178 ? 43.660  31.065  -12.101 1.00 39.02  ? 170 ARG J CG  1 
ATOM   16446 C CD  . ARG J  1 178 ? 43.555  30.694  -13.548 1.00 50.20  ? 170 ARG J CD  1 
ATOM   16447 N NE  . ARG J  1 178 ? 42.173  30.819  -13.983 1.00 53.39  ? 170 ARG J NE  1 
ATOM   16448 C CZ  . ARG J  1 178 ? 41.633  30.117  -14.974 1.00 61.63  ? 170 ARG J CZ  1 
ATOM   16449 N NH1 . ARG J  1 178 ? 42.363  29.230  -15.639 1.00 44.22  ? 170 ARG J NH1 1 
ATOM   16450 N NH2 . ARG J  1 178 ? 40.357  30.302  -15.294 1.00 72.22  ? 170 ARG J NH2 1 
ATOM   16451 N N   . PHE J  1 179 ? 42.170  35.302  -10.470 1.00 34.21  ? 171 PHE J N   1 
ATOM   16452 C CA  . PHE J  1 179 ? 41.549  36.556  -10.855 1.00 39.12  ? 171 PHE J CA  1 
ATOM   16453 C C   . PHE J  1 179 ? 42.019  37.693  -9.944  1.00 42.98  ? 171 PHE J C   1 
ATOM   16454 O O   . PHE J  1 179 ? 42.650  37.450  -8.907  1.00 44.96  ? 171 PHE J O   1 
ATOM   16455 C CB  . PHE J  1 179 ? 40.019  36.401  -10.840 1.00 31.11  ? 171 PHE J CB  1 
ATOM   16456 C CG  . PHE J  1 179 ? 39.525  35.218  -11.640 1.00 32.27  ? 171 PHE J CG  1 
ATOM   16457 C CD1 . PHE J  1 179 ? 39.413  33.967  -11.061 1.00 35.85  ? 171 PHE J CD1 1 
ATOM   16458 C CD2 . PHE J  1 179 ? 39.179  35.355  -12.972 1.00 37.95  ? 171 PHE J CD2 1 
ATOM   16459 C CE1 . PHE J  1 179 ? 38.968  32.876  -11.791 1.00 31.68  ? 171 PHE J CE1 1 
ATOM   16460 C CE2 . PHE J  1 179 ? 38.734  34.264  -13.705 1.00 38.22  ? 171 PHE J CE2 1 
ATOM   16461 C CZ  . PHE J  1 179 ? 38.632  33.023  -13.107 1.00 33.62  ? 171 PHE J CZ  1 
ATOM   16462 N N   . GLU J  1 180 ? 41.741  38.930  -10.344 1.00 36.46  ? 172 GLU J N   1 
ATOM   16463 C CA  . GLU J  1 180 ? 42.028  40.073  -9.493  1.00 40.51  ? 172 GLU J CA  1 
ATOM   16464 C C   . GLU J  1 180 ? 40.781  40.903  -9.402  1.00 41.20  ? 172 GLU J C   1 
ATOM   16465 O O   . GLU J  1 180 ? 40.064  41.058  -10.392 1.00 38.24  ? 172 GLU J O   1 
ATOM   16466 C CB  . GLU J  1 180 ? 43.136  40.957  -10.063 1.00 40.90  ? 172 GLU J CB  1 
ATOM   16467 C CG  . GLU J  1 180 ? 44.129  40.252  -10.950 1.00 48.47  ? 172 GLU J CG  1 
ATOM   16468 C CD  . GLU J  1 180 ? 45.161  41.188  -11.543 1.00 45.10  ? 172 GLU J CD  1 
ATOM   16469 O OE1 . GLU J  1 180 ? 44.935  41.683  -12.671 1.00 44.33  ? 172 GLU J OE1 1 
ATOM   16470 O OE2 . GLU J  1 180 ? 46.192  41.428  -10.878 1.00 40.69  ? 172 GLU J OE2 1 
ATOM   16471 N N   . ILE J  1 181 ? 40.528  41.441  -8.216  1.00 41.71  ? 173 ILE J N   1 
ATOM   16472 C CA  . ILE J  1 181 ? 39.459  42.405  -8.048  1.00 47.46  ? 173 ILE J CA  1 
ATOM   16473 C C   . ILE J  1 181 ? 40.020  43.780  -8.335  1.00 41.79  ? 173 ILE J C   1 
ATOM   16474 O O   . ILE J  1 181 ? 41.044  44.174  -7.778  1.00 36.71  ? 173 ILE J O   1 
ATOM   16475 C CB  . ILE J  1 181 ? 38.887  42.409  -6.615  1.00 50.22  ? 173 ILE J CB  1 
ATOM   16476 C CG1 . ILE J  1 181 ? 38.389  41.020  -6.231  1.00 44.88  ? 173 ILE J CG1 1 
ATOM   16477 C CG2 . ILE J  1 181 ? 37.771  43.449  -6.478  1.00 44.96  ? 173 ILE J CG2 1 
ATOM   16478 C CD1 . ILE J  1 181 ? 38.463  40.770  -4.752  1.00 49.94  ? 173 ILE J CD1 1 
ATOM   16479 N N   . LEU J  1 182 ? 39.335  44.504  -9.206  1.00 44.32  ? 174 LEU J N   1 
ATOM   16480 C CA  . LEU J  1 182 ? 39.671  45.888  -9.474  1.00 49.43  ? 174 LEU J CA  1 
ATOM   16481 C C   . LEU J  1 182 ? 38.974  46.777  -8.447  1.00 49.88  ? 174 LEU J C   1 
ATOM   16482 O O   . LEU J  1 182 ? 39.603  47.647  -7.846  1.00 52.72  ? 174 LEU J O   1 
ATOM   16483 C CB  . LEU J  1 182 ? 39.267  46.244  -10.903 1.00 43.97  ? 174 LEU J CB  1 
ATOM   16484 C CG  . LEU J  1 182 ? 39.684  45.089  -11.806 1.00 35.97  ? 174 LEU J CG  1 
ATOM   16485 C CD1 . LEU J  1 182 ? 39.173  45.263  -13.215 1.00 44.33  ? 174 LEU J CD1 1 
ATOM   16486 C CD2 . LEU J  1 182 ? 41.194  44.950  -11.781 1.00 35.85  ? 174 LEU J CD2 1 
ATOM   16487 N N   . ASP J  1 183 ? 37.685  46.528  -8.221  1.00 60.06  ? 175 ASP J N   1 
ATOM   16488 C CA  . ASP J  1 183 ? 36.900  47.347  -7.295  1.00 61.93  ? 175 ASP J CA  1 
ATOM   16489 C C   . ASP J  1 183 ? 35.570  46.706  -6.882  1.00 55.63  ? 175 ASP J C   1 
ATOM   16490 O O   . ASP J  1 183 ? 34.755  46.357  -7.739  1.00 53.49  ? 175 ASP J O   1 
ATOM   16491 C CB  . ASP J  1 183 ? 36.638  48.723  -7.917  1.00 59.65  ? 175 ASP J CB  1 
ATOM   16492 C CG  . ASP J  1 183 ? 35.861  49.644  -6.998  1.00 64.09  ? 175 ASP J CG  1 
ATOM   16493 O OD1 . ASP J  1 183 ? 34.664  49.881  -7.277  1.00 61.57  ? 175 ASP J OD1 1 
ATOM   16494 O OD2 . ASP J  1 183 ? 36.447  50.128  -6.001  1.00 62.10  ? 175 ASP J OD2 1 
ATOM   16495 N N   . VAL J  1 184 ? 35.359  46.561  -5.571  1.00 56.06  ? 176 VAL J N   1 
ATOM   16496 C CA  . VAL J  1 184 ? 34.057  46.156  -5.029  1.00 51.43  ? 176 VAL J CA  1 
ATOM   16497 C C   . VAL J  1 184 ? 33.257  47.348  -4.512  1.00 48.63  ? 176 VAL J C   1 
ATOM   16498 O O   . VAL J  1 184 ? 33.722  48.102  -3.660  1.00 55.99  ? 176 VAL J O   1 
ATOM   16499 C CB  . VAL J  1 184 ? 34.173  45.113  -3.892  1.00 50.59  ? 176 VAL J CB  1 
ATOM   16500 C CG1 . VAL J  1 184 ? 34.546  43.758  -4.444  1.00 50.37  ? 176 VAL J CG1 1 
ATOM   16501 C CG2 . VAL J  1 184 ? 35.172  45.551  -2.844  1.00 58.80  ? 176 VAL J CG2 1 
ATOM   16502 N N   . THR J  1 185 ? 32.051  47.516  -5.037  1.00 45.53  ? 177 THR J N   1 
ATOM   16503 C CA  . THR J  1 185 ? 31.177  48.601  -4.607  1.00 47.33  ? 177 THR J CA  1 
ATOM   16504 C C   . THR J  1 185 ? 29.809  48.064  -4.173  1.00 44.62  ? 177 THR J C   1 
ATOM   16505 O O   . THR J  1 185 ? 29.169  47.306  -4.899  1.00 44.39  ? 177 THR J O   1 
ATOM   16506 C CB  . THR J  1 185 ? 31.042  49.693  -5.703  1.00 45.84  ? 177 THR J CB  1 
ATOM   16507 O OG1 . THR J  1 185 ? 29.769  50.337  -5.598  1.00 48.27  ? 177 THR J OG1 1 
ATOM   16508 C CG2 . THR J  1 185 ? 31.173  49.088  -7.085  1.00 50.32  ? 177 THR J CG2 1 
ATOM   16509 N N   . GLN J  1 186 ? 29.383  48.440  -2.971  1.00 50.06  ? 178 GLN J N   1 
ATOM   16510 C CA  . GLN J  1 186 ? 28.100  47.997  -2.435  1.00 44.39  ? 178 GLN J CA  1 
ATOM   16511 C C   . GLN J  1 186 ? 27.231  49.192  -2.089  1.00 41.67  ? 178 GLN J C   1 
ATOM   16512 O O   . GLN J  1 186 ? 27.694  50.119  -1.428  1.00 49.92  ? 178 GLN J O   1 
ATOM   16513 C CB  . GLN J  1 186 ? 28.307  47.097  -1.215  1.00 44.40  ? 178 GLN J CB  1 
ATOM   16514 C CG  . GLN J  1 186 ? 29.589  47.386  -0.449  1.00 52.49  ? 178 GLN J CG  1 
ATOM   16515 C CD  . GLN J  1 186 ? 30.249  46.127  0.115   1.00 56.05  ? 178 GLN J CD  1 
ATOM   16516 O OE1 . GLN J  1 186 ? 29.701  45.026  0.015   1.00 44.70  ? 178 GLN J OE1 1 
ATOM   16517 N NE2 . GLN J  1 186 ? 31.437  46.290  0.710   1.00 55.58  ? 178 GLN J NE2 1 
ATOM   16518 N N   . LYS J  1 187 ? 25.980  49.171  -2.549  1.00 38.17  ? 179 LYS J N   1 
ATOM   16519 C CA  . LYS J  1 187 ? 25.040  50.273  -2.316  1.00 44.19  ? 179 LYS J CA  1 
ATOM   16520 C C   . LYS J  1 187 ? 23.646  49.765  -1.926  1.00 46.72  ? 179 LYS J C   1 
ATOM   16521 O O   . LYS J  1 187 ? 23.324  48.603  -2.160  1.00 46.61  ? 179 LYS J O   1 
ATOM   16522 C CB  . LYS J  1 187 ? 24.914  51.120  -3.579  1.00 40.93  ? 179 LYS J CB  1 
ATOM   16523 C CG  . LYS J  1 187 ? 24.234  50.369  -4.715  1.00 52.98  ? 179 LYS J CG  1 
ATOM   16524 C CD  . LYS J  1 187 ? 24.116  51.181  -5.998  1.00 55.15  ? 179 LYS J CD  1 
ATOM   16525 C CE  . LYS J  1 187 ? 23.814  50.263  -7.185  1.00 53.85  ? 179 LYS J CE  1 
ATOM   16526 N NZ  . LYS J  1 187 ? 23.445  51.014  -8.427  1.00 60.13  ? 179 LYS J NZ  1 
ATOM   16527 N N   . LYS J  1 188 ? 22.820  50.647  -1.355  1.00 49.95  ? 180 LYS J N   1 
ATOM   16528 C CA  . LYS J  1 188 ? 21.423  50.338  -1.007  1.00 39.86  ? 180 LYS J CA  1 
ATOM   16529 C C   . LYS J  1 188 ? 20.504  50.224  -2.229  1.00 45.40  ? 180 LYS J C   1 
ATOM   16530 O O   . LYS J  1 188 ? 20.858  50.661  -3.320  1.00 58.30  ? 180 LYS J O   1 
ATOM   16531 C CB  . LYS J  1 188 ? 20.869  51.413  -0.081  1.00 45.00  ? 180 LYS J CB  1 
ATOM   16532 C CG  . LYS J  1 188 ? 21.617  51.564  1.222   1.00 50.91  ? 180 LYS J CG  1 
ATOM   16533 C CD  . LYS J  1 188 ? 21.121  52.772  2.001   1.00 52.83  ? 180 LYS J CD  1 
ATOM   16534 C CE  . LYS J  1 188 ? 19.610  52.734  2.185   1.00 57.94  ? 180 LYS J CE  1 
ATOM   16535 N NZ  . LYS J  1 188 ? 19.133  53.828  3.083   1.00 69.18  ? 180 LYS J NZ  1 
ATOM   16536 N N   . ASN J  1 189 ? 19.313  49.661  -2.033  1.00 42.97  ? 181 ASN J N   1 
ATOM   16537 C CA  . ASN J  1 189 ? 18.388  49.392  -3.134  1.00 48.14  ? 181 ASN J CA  1 
ATOM   16538 C C   . ASN J  1 189 ? 17.010  48.915  -2.629  1.00 53.06  ? 181 ASN J C   1 
ATOM   16539 O O   . ASN J  1 189 ? 16.862  48.600  -1.448  1.00 54.26  ? 181 ASN J O   1 
ATOM   16540 C CB  . ASN J  1 189 ? 19.004  48.348  -4.078  1.00 46.92  ? 181 ASN J CB  1 
ATOM   16541 C CG  . ASN J  1 189 ? 18.198  48.153  -5.352  1.00 59.97  ? 181 ASN J CG  1 
ATOM   16542 O OD1 . ASN J  1 189 ? 17.649  49.110  -5.907  1.00 61.17  ? 181 ASN J OD1 1 
ATOM   16543 N ND2 . ASN J  1 189 ? 18.113  46.906  -5.817  1.00 56.80  ? 181 ASN J ND2 1 
ATOM   16544 N N   . SER J  1 190 ? 16.011  48.879  -3.518  1.00 53.75  ? 182 SER J N   1 
ATOM   16545 C CA  . SER J  1 190 ? 14.693  48.290  -3.238  1.00 46.01  ? 182 SER J CA  1 
ATOM   16546 C C   . SER J  1 190 ? 14.334  47.223  -4.283  1.00 48.59  ? 182 SER J C   1 
ATOM   16547 O O   . SER J  1 190 ? 13.195  46.748  -4.354  1.00 42.58  ? 182 SER J O   1 
ATOM   16548 C CB  . SER J  1 190 ? 13.600  49.365  -3.199  1.00 44.06  ? 182 SER J CB  1 
ATOM   16549 O OG  . SER J  1 190 ? 13.825  50.307  -2.161  1.00 46.73  ? 182 SER J OG  1 
ATOM   16550 N N   . GLU J  1 198 ? 4.739   47.006  -0.599  1.00 52.41  ? 190 GLU J N   1 
ATOM   16551 C CA  . GLU J  1 198 ? 5.655   46.179  0.142   1.00 53.04  ? 190 GLU J CA  1 
ATOM   16552 C C   . GLU J  1 198 ? 6.904   46.009  -0.674  1.00 43.58  ? 190 GLU J C   1 
ATOM   16553 O O   . GLU J  1 198 ? 6.912   45.342  -1.693  1.00 38.73  ? 190 GLU J O   1 
ATOM   16554 C CB  . GLU J  1 198 ? 5.017   44.817  0.439   1.00 57.95  ? 190 GLU J CB  1 
ATOM   16555 C CG  . GLU J  1 198 ? 4.558   44.659  1.871   1.00 58.33  ? 190 GLU J CG  1 
ATOM   16556 C CD  . GLU J  1 198 ? 5.017   43.341  2.509   1.00 58.26  ? 190 GLU J CD  1 
ATOM   16557 O OE1 . GLU J  1 198 ? 6.215   42.967  2.376   1.00 46.40  ? 190 GLU J OE1 1 
ATOM   16558 O OE2 . GLU J  1 198 ? 4.157   42.665  3.126   1.00 57.22  ? 190 GLU J OE2 1 
ATOM   16559 N N   . ALA J  1 199 ? 7.976   46.620  -0.253  1.00 37.98  ? 191 ALA J N   1 
ATOM   16560 C CA  . ALA J  1 199 ? 9.143   46.446  -1.055  1.00 48.46  ? 191 ALA J CA  1 
ATOM   16561 C C   . ALA J  1 199 ? 10.243  45.804  -0.186  1.00 43.74  ? 191 ALA J C   1 
ATOM   16562 O O   . ALA J  1 199 ? 9.977   45.591  0.966   1.00 43.47  ? 191 ALA J O   1 
ATOM   16563 C CB  . ALA J  1 199 ? 9.516   47.783  -1.564  1.00 47.95  ? 191 ALA J CB  1 
ATOM   16564 N N   . TYR J  1 200 ? 11.383  45.340  -0.721  1.00 46.64  ? 192 TYR J N   1 
ATOM   16565 C CA  . TYR J  1 200 ? 12.425  44.710  0.140   1.00 39.54  ? 192 TYR J CA  1 
ATOM   16566 C C   . TYR J  1 200 ? 13.803  45.385  0.025   1.00 46.34  ? 192 TYR J C   1 
ATOM   16567 O O   . TYR J  1 200 ? 14.446  45.352  -1.022  1.00 50.97  ? 192 TYR J O   1 
ATOM   16568 C CB  . TYR J  1 200 ? 12.555  43.189  -0.106  1.00 39.57  ? 192 TYR J CB  1 
ATOM   16569 C CG  . TYR J  1 200 ? 11.242  42.442  0.065   1.00 43.39  ? 192 TYR J CG  1 
ATOM   16570 C CD1 . TYR J  1 200 ? 10.375  42.283  -0.999  1.00 42.42  ? 192 TYR J CD1 1 
ATOM   16571 C CD2 . TYR J  1 200 ? 10.852  41.932  1.300   1.00 36.31  ? 192 TYR J CD2 1 
ATOM   16572 C CE1 . TYR J  1 200 ? 9.163   41.618  -0.850  1.00 46.35  ? 192 TYR J CE1 1 
ATOM   16573 C CE2 . TYR J  1 200 ? 9.643   41.267  1.455   1.00 35.78  ? 192 TYR J CE2 1 
ATOM   16574 C CZ  . TYR J  1 200 ? 8.799   41.115  0.369   1.00 42.74  ? 192 TYR J CZ  1 
ATOM   16575 O OH  . TYR J  1 200 ? 7.578   40.473  0.446   1.00 37.54  ? 192 TYR J OH  1 
ATOM   16576 N N   . GLU J  1 201 ? 14.225  46.043  1.097   1.00 47.20  ? 193 GLU J N   1 
ATOM   16577 C CA  . GLU J  1 201 ? 15.567  46.609  1.179   1.00 42.86  ? 193 GLU J CA  1 
ATOM   16578 C C   . GLU J  1 201 ? 16.622  45.531  0.966   1.00 44.77  ? 193 GLU J C   1 
ATOM   16579 O O   . GLU J  1 201 ? 16.406  44.347  1.253   1.00 47.06  ? 193 GLU J O   1 
ATOM   16580 C CB  . GLU J  1 201 ? 15.772  47.371  2.498   1.00 32.65  ? 193 GLU J CB  1 
ATOM   16581 C CG  . GLU J  1 201 ? 15.087  48.726  2.466   1.00 36.35  ? 193 GLU J CG  1 
ATOM   16582 C CD  . GLU J  1 201 ? 15.609  49.714  3.497   1.00 42.55  ? 193 GLU J CD  1 
ATOM   16583 O OE1 . GLU J  1 201 ? 16.731  49.509  4.017   1.00 39.77  ? 193 GLU J OE1 1 
ATOM   16584 O OE2 . GLU J  1 201 ? 14.892  50.708  3.780   1.00 43.82  ? 193 GLU J OE2 1 
ATOM   16585 N N   . ASP J  1 202 ? 17.754  45.953  0.423   1.00 50.56  ? 194 ASP J N   1 
ATOM   16586 C CA  . ASP J  1 202 ? 18.821  45.038  0.077   1.00 46.87  ? 194 ASP J CA  1 
ATOM   16587 C C   . ASP J  1 202 ? 20.090  45.819  -0.256  1.00 44.59  ? 194 ASP J C   1 
ATOM   16588 O O   . ASP J  1 202 ? 20.042  46.999  -0.606  1.00 44.14  ? 194 ASP J O   1 
ATOM   16589 C CB  . ASP J  1 202 ? 18.413  44.183  -1.122  1.00 45.10  ? 194 ASP J CB  1 
ATOM   16590 C CG  . ASP J  1 202 ? 18.325  44.988  -2.391  1.00 54.37  ? 194 ASP J CG  1 
ATOM   16591 O OD1 . ASP J  1 202 ? 18.836  44.530  -3.438  1.00 61.45  ? 194 ASP J OD1 1 
ATOM   16592 O OD2 . ASP J  1 202 ? 17.753  46.094  -2.335  1.00 56.61  ? 194 ASP J OD2 1 
ATOM   16593 N N   . VAL J  1 203 ? 21.225  45.147  -0.124  1.00 40.60  ? 195 VAL J N   1 
ATOM   16594 C CA  . VAL J  1 203 ? 22.503  45.709  -0.511  1.00 42.53  ? 195 VAL J CA  1 
ATOM   16595 C C   . VAL J  1 203 ? 22.975  45.093  -1.832  1.00 41.38  ? 195 VAL J C   1 
ATOM   16596 O O   . VAL J  1 203 ? 23.168  43.882  -1.941  1.00 36.33  ? 195 VAL J O   1 
ATOM   16597 C CB  . VAL J  1 203 ? 23.562  45.490  0.578   1.00 40.80  ? 195 VAL J CB  1 
ATOM   16598 C CG1 . VAL J  1 203 ? 24.924  45.941  0.084   1.00 38.16  ? 195 VAL J CG1 1 
ATOM   16599 C CG2 . VAL J  1 203 ? 23.170  46.237  1.848   1.00 43.09  ? 195 VAL J CG2 1 
ATOM   16600 N N   . GLU J  1 204 ? 23.141  45.938  -2.842  1.00 47.42  ? 196 GLU J N   1 
ATOM   16601 C CA  . GLU J  1 204 ? 23.673  45.486  -4.116  1.00 45.48  ? 196 GLU J CA  1 
ATOM   16602 C C   . GLU J  1 204 ? 25.188  45.542  -4.061  1.00 42.57  ? 196 GLU J C   1 
ATOM   16603 O O   . GLU J  1 204 ? 25.765  46.570  -3.712  1.00 43.15  ? 196 GLU J O   1 
ATOM   16604 C CB  . GLU J  1 204 ? 23.149  46.348  -5.262  1.00 43.42  ? 196 GLU J CB  1 
ATOM   16605 C CG  . GLU J  1 204 ? 23.242  45.667  -6.608  1.00 54.53  ? 196 GLU J CG  1 
ATOM   16606 C CD  . GLU J  1 204 ? 22.186  46.160  -7.573  1.00 67.99  ? 196 GLU J CD  1 
ATOM   16607 O OE1 . GLU J  1 204 ? 21.607  47.238  -7.300  1.00 64.41  ? 196 GLU J OE1 1 
ATOM   16608 O OE2 . GLU J  1 204 ? 21.935  45.469  -8.592  1.00 61.79  ? 196 GLU J OE2 1 
ATOM   16609 N N   . VAL J  1 205 ? 25.824  44.423  -4.377  1.00 38.15  ? 197 VAL J N   1 
ATOM   16610 C CA  . VAL J  1 205 ? 27.277  44.358  -4.429  1.00 45.29  ? 197 VAL J CA  1 
ATOM   16611 C C   . VAL J  1 205 ? 27.747  44.233  -5.877  1.00 46.39  ? 197 VAL J C   1 
ATOM   16612 O O   . VAL J  1 205 ? 27.301  43.345  -6.608  1.00 42.98  ? 197 VAL J O   1 
ATOM   16613 C CB  . VAL J  1 205 ? 27.812  43.168  -3.611  1.00 45.59  ? 197 VAL J CB  1 
ATOM   16614 C CG1 . VAL J  1 205 ? 29.307  42.961  -3.872  1.00 38.70  ? 197 VAL J CG1 1 
ATOM   16615 C CG2 . VAL J  1 205 ? 27.526  43.379  -2.135  1.00 35.30  ? 197 VAL J CG2 1 
ATOM   16616 N N   . SER J  1 206 ? 28.638  45.133  -6.289  1.00 53.22  ? 198 SER J N   1 
ATOM   16617 C CA  . SER J  1 206 ? 29.173  45.130  -7.651  1.00 43.79  ? 198 SER J CA  1 
ATOM   16618 C C   . SER J  1 206 ? 30.654  44.776  -7.651  1.00 42.24  ? 198 SER J C   1 
ATOM   16619 O O   . SER J  1 206 ? 31.470  45.514  -7.107  1.00 47.84  ? 198 SER J O   1 
ATOM   16620 C CB  . SER J  1 206 ? 28.943  46.487  -8.305  1.00 42.18  ? 198 SER J CB  1 
ATOM   16621 O OG  . SER J  1 206 ? 27.698  46.506  -8.978  1.00 50.40  ? 198 SER J OG  1 
ATOM   16622 N N   . LEU J  1 207 ? 30.993  43.643  -8.263  1.00 40.26  ? 199 LEU J N   1 
ATOM   16623 C CA  . LEU J  1 207 ? 32.348  43.091  -8.181  1.00 40.12  ? 199 LEU J CA  1 
ATOM   16624 C C   . LEU J  1 207 ? 33.093  43.078  -9.525  1.00 47.41  ? 199 LEU J C   1 
ATOM   16625 O O   . LEU J  1 207 ? 32.881  42.205  -10.375 1.00 41.66  ? 199 LEU J O   1 
ATOM   16626 C CB  . LEU J  1 207 ? 32.303  41.686  -7.568  1.00 37.18  ? 199 LEU J CB  1 
ATOM   16627 C CG  . LEU J  1 207 ? 33.542  40.789  -7.627  1.00 38.91  ? 199 LEU J CG  1 
ATOM   16628 C CD1 . LEU J  1 207 ? 34.778  41.455  -7.046  1.00 36.56  ? 199 LEU J CD1 1 
ATOM   16629 C CD2 . LEU J  1 207 ? 33.260  39.484  -6.911  1.00 31.27  ? 199 LEU J CD2 1 
ATOM   16630 N N   . ASN J  1 208 ? 33.977  44.056  -9.699  1.00 54.51  ? 200 ASN J N   1 
ATOM   16631 C CA  . ASN J  1 208 ? 34.770  44.188  -10.912 1.00 45.70  ? 200 ASN J CA  1 
ATOM   16632 C C   . ASN J  1 208 ? 36.040  43.352  -10.822 1.00 44.83  ? 200 ASN J C   1 
ATOM   16633 O O   . ASN J  1 208 ? 36.855  43.560  -9.923  1.00 47.27  ? 200 ASN J O   1 
ATOM   16634 C CB  . ASN J  1 208 ? 35.129  45.658  -11.142 1.00 54.59  ? 200 ASN J CB  1 
ATOM   16635 C CG  . ASN J  1 208 ? 35.059  46.060  -12.613 1.00 54.79  ? 200 ASN J CG  1 
ATOM   16636 O OD1 . ASN J  1 208 ? 35.389  45.271  -13.503 1.00 47.57  ? 200 ASN J OD1 1 
ATOM   16637 N ND2 . ASN J  1 208 ? 34.620  47.293  -12.870 1.00 45.91  ? 200 ASN J ND2 1 
ATOM   16638 N N   . PHE J  1 209 ? 36.203  42.421  -11.763 1.00 42.70  ? 201 PHE J N   1 
ATOM   16639 C CA  . PHE J  1 209 ? 37.315  41.470  -11.753 1.00 39.28  ? 201 PHE J CA  1 
ATOM   16640 C C   . PHE J  1 209 ? 37.754  41.109  -13.174 1.00 39.57  ? 201 PHE J C   1 
ATOM   16641 O O   . PHE J  1 209 ? 36.988  41.296  -14.118 1.00 40.74  ? 201 PHE J O   1 
ATOM   16642 C CB  . PHE J  1 209 ? 36.939  40.206  -10.947 1.00 36.28  ? 201 PHE J CB  1 
ATOM   16643 C CG  . PHE J  1 209 ? 35.858  39.346  -11.588 1.00 35.07  ? 201 PHE J CG  1 
ATOM   16644 C CD1 . PHE J  1 209 ? 34.570  39.836  -11.781 1.00 31.88  ? 201 PHE J CD1 1 
ATOM   16645 C CD2 . PHE J  1 209 ? 36.131  38.034  -11.968 1.00 29.92  ? 201 PHE J CD2 1 
ATOM   16646 C CE1 . PHE J  1 209 ? 33.589  39.052  -12.368 1.00 24.26  ? 201 PHE J CE1 1 
ATOM   16647 C CE2 . PHE J  1 209 ? 35.149  37.240  -12.547 1.00 23.24  ? 201 PHE J CE2 1 
ATOM   16648 C CZ  . PHE J  1 209 ? 33.879  37.751  -12.746 1.00 22.05  ? 201 PHE J CZ  1 
ATOM   16649 N N   . ARG J  1 210 ? 38.982  40.606  -13.318 1.00 39.82  ? 202 ARG J N   1 
ATOM   16650 C CA  . ARG J  1 210 ? 39.510  40.125  -14.612 1.00 47.50  ? 202 ARG J CA  1 
ATOM   16651 C C   . ARG J  1 210 ? 40.488  38.970  -14.387 1.00 41.29  ? 202 ARG J C   1 
ATOM   16652 O O   . ARG J  1 210 ? 41.047  38.843  -13.299 1.00 38.00  ? 202 ARG J O   1 
ATOM   16653 C CB  . ARG J  1 210 ? 40.233  41.248  -15.379 1.00 49.28  ? 202 ARG J CB  1 
ATOM   16654 C CG  . ARG J  1 210 ? 41.643  41.550  -14.853 1.00 47.66  ? 202 ARG J CG  1 
ATOM   16655 C CD  . ARG J  1 210 ? 42.341  42.702  -15.580 1.00 48.20  ? 202 ARG J CD  1 
ATOM   16656 N NE  . ARG J  1 210 ? 43.451  43.227  -14.778 1.00 49.10  ? 202 ARG J NE  1 
ATOM   16657 C CZ  . ARG J  1 210 ? 43.721  44.523  -14.616 1.00 43.10  ? 202 ARG J CZ  1 
ATOM   16658 N NH1 . ARG J  1 210 ? 42.968  45.443  -15.215 1.00 40.21  ? 202 ARG J NH1 1 
ATOM   16659 N NH2 . ARG J  1 210 ? 44.744  44.899  -13.853 1.00 29.39  ? 202 ARG J NH2 1 
ATOM   16660 N N   . LYS J  1 211 ? 40.708  38.135  -15.403 1.00 42.70  ? 203 LYS J N   1 
ATOM   16661 C CA  . LYS J  1 211 ? 41.724  37.086  -15.282 1.00 42.86  ? 203 LYS J CA  1 
ATOM   16662 C C   . LYS J  1 211 ? 43.094  37.745  -15.121 1.00 45.72  ? 203 LYS J C   1 
ATOM   16663 O O   . LYS J  1 211 ? 43.308  38.855  -15.602 1.00 46.18  ? 203 LYS J O   1 
ATOM   16664 C CB  . LYS J  1 211 ? 41.715  36.148  -16.491 1.00 39.96  ? 203 LYS J CB  1 
ATOM   16665 C CG  . LYS J  1 211 ? 42.669  34.966  -16.346 1.00 45.62  ? 203 LYS J CG  1 
ATOM   16666 C CD  . LYS J  1 211 ? 42.788  34.164  -17.630 1.00 51.81  ? 203 LYS J CD  1 
ATOM   16667 C CE  . LYS J  1 211 ? 43.879  33.113  -17.523 1.00 52.24  ? 203 LYS J CE  1 
ATOM   16668 N NZ  . LYS J  1 211 ? 44.167  32.495  -18.846 1.00 66.58  ? 203 LYS J NZ  1 
ATOM   16669 N N   . LYS J  1 212 ? 44.013  37.090  -14.422 1.00 48.24  ? 204 LYS J N   1 
ATOM   16670 C CA  . LYS J  1 212 ? 45.330  37.684  -14.212 1.00 49.54  ? 204 LYS J CA  1 
ATOM   16671 C C   . LYS J  1 212 ? 46.199  37.603  -15.458 1.00 53.87  ? 204 LYS J C   1 
ATOM   16672 O O   . LYS J  1 212 ? 46.084  36.664  -16.253 1.00 50.09  ? 204 LYS J O   1 
ATOM   16673 C CB  . LYS J  1 212 ? 46.052  37.042  -13.022 1.00 53.05  ? 204 LYS J CB  1 
ATOM   16674 C CG  . LYS J  1 212 ? 45.382  37.316  -11.688 1.00 45.12  ? 204 LYS J CG  1 
ATOM   16675 C CD  . LYS J  1 212 ? 46.338  37.225  -10.515 1.00 37.16  ? 204 LYS J CD  1 
ATOM   16676 C CE  . LYS J  1 212 ? 46.768  35.795  -10.271 1.00 46.07  ? 204 LYS J CE  1 
ATOM   16677 N NZ  . LYS J  1 212 ? 47.196  35.592  -8.857  1.00 48.37  ? 204 LYS J NZ  1 
ATOM   16678 N N   . GLY J  1 213 ? 47.058  38.607  -15.618 1.00 62.38  ? 205 GLY J N   1 
ATOM   16679 C CA  . GLY J  1 213 ? 48.050  38.632  -16.675 1.00 63.48  ? 205 GLY J CA  1 
ATOM   16680 C C   . GLY J  1 213 ? 49.449  38.764  -16.101 1.00 61.79  ? 205 GLY J C   1 
ATOM   16681 O O   . GLY J  1 213 ? 50.144  37.766  -15.895 1.00 70.06  ? 205 GLY J O   1 
HETATM 16682 C C01 . KK1 K  2 .   ? -6.426  -15.357 61.975  1.00 51.78  ? 301 KK1 A C01 1 
HETATM 16683 C C02 . KK1 K  2 .   ? -6.297  -13.812 61.934  1.00 58.49  ? 301 KK1 A C02 1 
HETATM 16684 C C03 . KK1 K  2 .   ? -6.899  -13.183 60.648  1.00 51.62  ? 301 KK1 A C03 1 
HETATM 16685 C C04 . KK1 K  2 .   ? -6.586  -11.655 60.499  1.00 44.53  ? 301 KK1 A C04 1 
HETATM 16686 C C05 . KK1 K  2 .   ? -6.108  -11.243 59.039  1.00 47.91  ? 301 KK1 A C05 1 
HETATM 16687 C C06 . KK1 K  2 .   ? -7.069  -11.747 57.881  1.00 49.08  ? 301 KK1 A C06 1 
HETATM 16688 C C07 . KK1 K  2 .   ? -6.463  -11.854 56.391  1.00 39.83  ? 301 KK1 A C07 1 
HETATM 16689 C C08 . KK1 K  2 .   ? -7.449  -11.331 55.221  1.00 31.27  ? 301 KK1 A C08 1 
HETATM 16690 N N09 . KK1 K  2 .   ? -6.987  -11.550 53.779  1.00 26.98  ? 301 KK1 A N09 1 
HETATM 16691 C C10 . KK1 K  2 .   ? -6.103  -10.666 53.043  1.00 26.30  ? 301 KK1 A C10 1 
HETATM 16692 C C11 . KK1 K  2 .   ? -6.517  -10.097 51.747  1.00 23.09  ? 301 KK1 A C11 1 
HETATM 16693 C C12 . KK1 K  2 .   ? -5.576  -9.242  51.055  1.00 17.86  ? 301 KK1 A C12 1 
HETATM 16694 N N13 . KK1 K  2 .   ? -4.360  -8.993  51.616  1.00 17.86  ? 301 KK1 A N13 1 
HETATM 16695 C C14 . KK1 K  2 .   ? -4.024  -9.555  52.820  1.00 21.33  ? 301 KK1 A C14 1 
HETATM 16696 N N15 . KK1 K  2 .   ? -2.736  -9.272  53.368  1.00 20.34  ? 301 KK1 A N15 1 
HETATM 16697 N N16 . KK1 K  2 .   ? -4.851  -10.387 53.575  1.00 28.16  ? 301 KK1 A N16 1 
HETATM 16698 C C17 . KK1 K  2 .   ? -5.817  -8.509  49.642  1.00 17.59  ? 301 KK1 A C17 1 
HETATM 16699 C C18 . KK1 K  2 .   ? -6.298  -9.185  48.494  1.00 16.60  ? 301 KK1 A C18 1 
HETATM 16700 C C19 . KK1 K  2 .   ? -6.491  -8.547  47.191  1.00 16.45  ? 301 KK1 A C19 1 
HETATM 16701 C C20 . KK1 K  2 .   ? -6.189  -7.181  47.002  1.00 14.77  ? 301 KK1 A C20 1 
HETATM 16702 O O21 . KK1 K  2 .   ? -6.374  -6.573  45.781  1.00 19.34  ? 301 KK1 A O21 1 
HETATM 16703 C C22 . KK1 K  2 .   ? -5.752  -5.257  45.579  1.00 16.81  ? 301 KK1 A C22 1 
HETATM 16704 C C23 . KK1 K  2 .   ? -5.689  -6.479  48.115  1.00 15.28  ? 301 KK1 A C23 1 
HETATM 16705 C C24 . KK1 K  2 .   ? -5.515  -7.142  49.378  1.00 17.35  ? 301 KK1 A C24 1 
HETATM 16706 C C1  . NAG L  3 .   ? 36.324  -5.346  42.892  1.00 48.69  ? 302 NAG A C1  1 
HETATM 16707 C C2  . NAG L  3 .   ? 36.804  -6.591  42.164  1.00 49.51  ? 302 NAG A C2  1 
HETATM 16708 C C3  . NAG L  3 .   ? 38.246  -6.866  42.568  1.00 56.20  ? 302 NAG A C3  1 
HETATM 16709 C C4  . NAG L  3 .   ? 39.080  -5.660  42.147  1.00 60.14  ? 302 NAG A C4  1 
HETATM 16710 C C5  . NAG L  3 .   ? 38.506  -4.407  42.810  1.00 57.59  ? 302 NAG A C5  1 
HETATM 16711 C C6  . NAG L  3 .   ? 39.287  -3.141  42.446  1.00 56.22  ? 302 NAG A C6  1 
HETATM 16712 C C7  . NAG L  3 .   ? 35.054  -8.086  41.468  1.00 55.52  ? 302 NAG A C7  1 
HETATM 16713 C C8  . NAG L  3 .   ? 34.093  -9.183  41.818  1.00 48.54  ? 302 NAG A C8  1 
HETATM 16714 N N2  . NAG L  3 .   ? 35.921  -7.713  42.409  1.00 55.39  ? 302 NAG A N2  1 
HETATM 16715 O O3  . NAG L  3 .   ? 38.720  -8.048  41.966  1.00 53.73  ? 302 NAG A O3  1 
HETATM 16716 O O4  . NAG L  3 .   ? 40.433  -5.826  42.512  1.00 68.89  ? 302 NAG A O4  1 
HETATM 16717 O O5  . NAG L  3 .   ? 37.135  -4.260  42.477  1.00 52.56  ? 302 NAG A O5  1 
HETATM 16718 O O6  . NAG L  3 .   ? 39.289  -2.937  41.053  1.00 48.78  ? 302 NAG A O6  1 
HETATM 16719 O O7  . NAG L  3 .   ? 35.019  -7.561  40.354  1.00 61.96  ? 302 NAG A O7  1 
HETATM 16720 P P   . PO4 M  4 .   ? 4.725   -6.005  41.171  1.00 17.19  ? 303 PO4 A P   1 
HETATM 16721 O O1  . PO4 M  4 .   ? 4.508   -5.264  39.892  1.00 14.87  ? 303 PO4 A O1  1 
HETATM 16722 O O2  . PO4 M  4 .   ? 3.762   -7.159  41.255  1.00 12.89  ? 303 PO4 A O2  1 
HETATM 16723 O O3  . PO4 M  4 .   ? 6.129   -6.557  41.272  1.00 14.41  ? 303 PO4 A O3  1 
HETATM 16724 O O4  . PO4 M  4 .   ? 4.521   -4.995  42.273  1.00 20.36  ? 303 PO4 A O4  1 
HETATM 16725 P P   . PO4 N  4 .   ? 23.852  9.857   50.565  1.00 21.27  ? 304 PO4 A P   1 
HETATM 16726 O O1  . PO4 N  4 .   ? 23.433  9.069   49.356  1.00 15.51  ? 304 PO4 A O1  1 
HETATM 16727 O O2  . PO4 N  4 .   ? 22.738  10.814  50.941  1.00 25.28  ? 304 PO4 A O2  1 
HETATM 16728 O O3  . PO4 N  4 .   ? 25.091  10.666  50.292  1.00 11.95  ? 304 PO4 A O3  1 
HETATM 16729 O O4  . PO4 N  4 .   ? 24.091  8.852   51.672  1.00 15.25  ? 304 PO4 A O4  1 
HETATM 16730 P P   . PO4 O  4 .   ? -10.082 5.470   79.886  1.00 70.89  ? 305 PO4 A P   1 
HETATM 16731 O O1  . PO4 O  4 .   ? -11.453 5.626   79.261  1.00 59.63  ? 305 PO4 A O1  1 
HETATM 16732 O O2  . PO4 O  4 .   ? -9.130  6.532   79.361  1.00 56.44  ? 305 PO4 A O2  1 
HETATM 16733 O O3  . PO4 O  4 .   ? -9.515  4.115   79.514  1.00 41.59  ? 305 PO4 A O3  1 
HETATM 16734 O O4  . PO4 O  4 .   ? -10.247 5.587   81.394  1.00 64.68  ? 305 PO4 A O4  1 
HETATM 16735 C C01 . KK1 P  2 .   ? -32.494 8.192   46.962  1.00 37.91  ? 301 KK1 B C01 1 
HETATM 16736 C C02 . KK1 P  2 .   ? -30.959 8.011   47.008  1.00 36.49  ? 301 KK1 B C02 1 
HETATM 16737 C C03 . KK1 P  2 .   ? -30.282 8.791   48.163  1.00 38.26  ? 301 KK1 B C03 1 
HETATM 16738 C C04 . KK1 P  2 .   ? -28.954 9.475   47.691  1.00 42.28  ? 301 KK1 B C04 1 
HETATM 16739 C C05 . KK1 P  2 .   ? -29.156 10.980  47.223  1.00 45.91  ? 301 KK1 B C05 1 
HETATM 16740 C C06 . KK1 P  2 .   ? -28.693 11.256  45.723  1.00 45.50  ? 301 KK1 B C06 1 
HETATM 16741 C C07 . KK1 P  2 .   ? -29.506 12.379  44.917  1.00 45.24  ? 301 KK1 B C07 1 
HETATM 16742 C C08 . KK1 P  2 .   ? -28.888 12.863  43.504  1.00 42.02  ? 301 KK1 B C08 1 
HETATM 16743 N N09 . KK1 P  2 .   ? -28.233 11.762  42.685  1.00 48.23  ? 301 KK1 B N09 1 
HETATM 16744 C C10 . KK1 P  2 .   ? -26.853 11.729  42.136  1.00 41.91  ? 301 KK1 B C10 1 
HETATM 16745 C C11 . KK1 P  2 .   ? -26.294 12.857  41.343  1.00 30.08  ? 301 KK1 B C11 1 
HETATM 16746 C C12 . KK1 P  2 .   ? -24.945 12.688  40.835  1.00 30.77  ? 301 KK1 B C12 1 
HETATM 16747 N N13 . KK1 P  2 .   ? -24.262 11.533  41.094  1.00 26.58  ? 301 KK1 B N13 1 
HETATM 16748 C C14 . KK1 P  2 .   ? -24.829 10.542  41.818  1.00 23.42  ? 301 KK1 B C14 1 
HETATM 16749 N N15 . KK1 P  2 .   ? -24.075 9.359   42.052  1.00 25.81  ? 301 KK1 B N15 1 
HETATM 16750 N N16 . KK1 P  2 .   ? -26.099 10.576  42.355  1.00 33.75  ? 301 KK1 B N16 1 
HETATM 16751 C C17 . KK1 P  2 .   ? -24.087 13.739  39.964  1.00 18.83  ? 301 KK1 B C17 1 
HETATM 16752 C C18 . KK1 P  2 .   ? -24.516 14.229  38.713  1.00 24.99  ? 301 KK1 B C18 1 
HETATM 16753 C C19 . KK1 P  2 .   ? -23.743 15.149  37.864  1.00 28.47  ? 301 KK1 B C19 1 
HETATM 16754 C C20 . KK1 P  2 .   ? -22.471 15.592  38.289  1.00 21.45  ? 301 KK1 B C20 1 
HETATM 16755 O O21 . KK1 P  2 .   ? -21.718 16.448  37.538  1.00 19.79  ? 301 KK1 B O21 1 
HETATM 16756 C C22 . KK1 P  2 .   ? -20.278 16.369  37.791  1.00 16.84  ? 301 KK1 B C22 1 
HETATM 16757 C C23 . KK1 P  2 .   ? -22.006 15.104  39.525  1.00 21.10  ? 301 KK1 B C23 1 
HETATM 16758 C C24 . KK1 P  2 .   ? -22.798 14.203  40.314  1.00 19.12  ? 301 KK1 B C24 1 
HETATM 16759 C C1  . NAG Q  3 .   ? -0.121  -18.276 24.344  1.00 66.90  ? 302 NAG B C1  1 
HETATM 16760 C C2  . NAG Q  3 .   ? -1.279  -19.022 23.665  1.00 66.01  ? 302 NAG B C2  1 
HETATM 16761 C C3  . NAG Q  3 .   ? -1.001  -20.485 23.319  1.00 69.34  ? 302 NAG B C3  1 
HETATM 16762 C C4  . NAG Q  3 .   ? 0.451   -20.724 22.943  1.00 69.13  ? 302 NAG B C4  1 
HETATM 16763 C C5  . NAG Q  3 .   ? 1.328   -20.115 24.028  1.00 65.88  ? 302 NAG B C5  1 
HETATM 16764 C C6  . NAG Q  3 .   ? 2.793   -20.510 23.891  1.00 59.78  ? 302 NAG B C6  1 
HETATM 16765 C C7  . NAG Q  3 .   ? -3.618  -18.574 24.084  1.00 73.65  ? 302 NAG B C7  1 
HETATM 16766 C C8  . NAG Q  3 .   ? -4.770  -18.682 25.045  1.00 60.45  ? 302 NAG B C8  1 
HETATM 16767 N N2  . NAG Q  3 .   ? -2.437  -18.978 24.538  1.00 66.84  ? 302 NAG B N2  1 
HETATM 16768 O O3  . NAG Q  3 .   ? -1.837  -20.896 22.259  1.00 68.21  ? 302 NAG B O3  1 
HETATM 16769 O O4  . NAG Q  3 .   ? 0.664   -22.112 22.844  1.00 76.27  ? 302 NAG B O4  1 
HETATM 16770 O O5  . NAG Q  3 .   ? 1.174   -18.714 23.968  1.00 65.91  ? 302 NAG B O5  1 
HETATM 16771 O O6  . NAG Q  3 .   ? 3.152   -20.480 22.529  1.00 74.05  ? 302 NAG B O6  1 
HETATM 16772 O O7  . NAG Q  3 .   ? -3.769  -18.133 22.941  1.00 73.83  ? 302 NAG B O7  1 
HETATM 16773 P P   . PO4 R  4 .   ? 4.280   -11.213 28.330  1.00 72.34  ? 303 PO4 B P   1 
HETATM 16774 O O1  . PO4 R  4 .   ? 5.389   -10.798 27.371  1.00 56.84  ? 303 PO4 B O1  1 
HETATM 16775 O O2  . PO4 R  4 .   ? 3.005   -10.490 27.947  1.00 48.30  ? 303 PO4 B O2  1 
HETATM 16776 O O3  . PO4 R  4 .   ? 4.003   -12.704 28.261  1.00 63.79  ? 303 PO4 B O3  1 
HETATM 16777 O O4  . PO4 R  4 .   ? 4.700   -10.880 29.747  1.00 37.34  ? 303 PO4 B O4  1 
HETATM 16778 C C01 . KK1 S  2 .   ? -17.973 37.403  57.493  1.00 18.73  ? 301 KK1 C C01 1 
HETATM 16779 C C02 . KK1 S  2 .   ? -18.119 37.766  55.980  1.00 16.94  ? 301 KK1 C C02 1 
HETATM 16780 C C03 . KK1 S  2 .   ? -17.753 39.260  55.630  1.00 24.34  ? 301 KK1 C C03 1 
HETATM 16781 C C04 . KK1 S  2 .   ? -18.322 39.687  54.203  1.00 44.66  ? 301 KK1 C C04 1 
HETATM 16782 C C05 . KK1 S  2 .   ? -17.986 41.168  53.694  1.00 40.58  ? 301 KK1 C C05 1 
HETATM 16783 C C06 . KK1 S  2 .   ? -17.982 41.332  52.081  1.00 51.04  ? 301 KK1 C C06 1 
HETATM 16784 C C07 . KK1 S  2 .   ? -16.812 42.274  51.427  1.00 48.35  ? 301 KK1 C C07 1 
HETATM 16785 C C08 . KK1 S  2 .   ? -16.432 42.098  49.840  1.00 40.29  ? 301 KK1 C C08 1 
HETATM 16786 N N09 . KK1 S  2 .   ? -14.908 42.117  49.484  1.00 34.57  ? 301 KK1 C N09 1 
HETATM 16787 C C10 . KK1 S  2 .   ? -14.326 41.319  48.391  1.00 28.72  ? 301 KK1 C C10 1 
HETATM 16788 C C11 . KK1 S  2 .   ? -12.876 41.343  48.076  1.00 20.49  ? 301 KK1 C C11 1 
HETATM 16789 C C12 . KK1 S  2 .   ? -12.413 40.504  46.974  1.00 22.72  ? 301 KK1 C C12 1 
HETATM 16790 N N13 . KK1 S  2 .   ? -13.311 39.742  46.283  1.00 22.32  ? 301 KK1 C N13 1 
HETATM 16791 C C14 . KK1 S  2 .   ? -14.631 39.761  46.630  1.00 26.45  ? 301 KK1 C C14 1 
HETATM 16792 N N15 . KK1 S  2 .   ? -15.557 38.949  45.899  1.00 29.52  ? 301 KK1 C N15 1 
HETATM 16793 N N16 . KK1 S  2 .   ? -15.180 40.520  47.664  1.00 36.15  ? 301 KK1 C N16 1 
HETATM 16794 C C17 . KK1 S  2 .   ? -10.876 40.371  46.437  1.00 20.93  ? 301 KK1 C C17 1 
HETATM 16795 C C18 . KK1 S  2 .   ? -10.253 41.406  45.688  1.00 24.09  ? 301 KK1 C C18 1 
HETATM 16796 C C19 . KK1 S  2 .   ? -8.896  41.357  45.142  1.00 21.65  ? 301 KK1 C C19 1 
HETATM 16797 C C20 . KK1 S  2 .   ? -8.095  40.215  45.325  1.00 14.17  ? 301 KK1 C C20 1 
HETATM 16798 O O21 . KK1 S  2 .   ? -6.820  40.175  44.818  1.00 18.44  ? 301 KK1 C O21 1 
HETATM 16799 C C22 . KK1 S  2 .   ? -6.121  38.876  44.791  1.00 19.15  ? 301 KK1 C C22 1 
HETATM 16800 C C23 . KK1 S  2 .   ? -8.667  39.156  46.051  1.00 16.14  ? 301 KK1 C C23 1 
HETATM 16801 C C24 . KK1 S  2 .   ? -10.024 39.242  46.580  1.00 20.21  ? 301 KK1 C C24 1 
HETATM 16802 C C1  . NAG T  3 .   ? -21.462 16.907  12.410  1.00 27.57  ? 302 NAG C C1  1 
HETATM 16803 C C2  . NAG T  3 .   ? -22.602 16.206  11.710  1.00 27.66  ? 302 NAG C C2  1 
HETATM 16804 C C3  . NAG T  3 .   ? -23.026 17.078  10.602  1.00 34.84  ? 302 NAG C C3  1 
HETATM 16805 C C4  . NAG T  3 .   ? -23.522 18.373  11.098  1.00 33.49  ? 302 NAG C C4  1 
HETATM 16806 C C5  . NAG T  3 .   ? -22.378 19.044  11.822  1.00 31.70  ? 302 NAG C C5  1 
HETATM 16807 C C6  . NAG T  3 .   ? -22.983 20.179  12.569  1.00 20.55  ? 302 NAG C C6  1 
HETATM 16808 C C7  . NAG T  3 .   ? -21.337 14.133  11.393  1.00 41.49  ? 302 NAG C C7  1 
HETATM 16809 C C8  . NAG T  3 .   ? -20.187 14.362  12.301  1.00 31.03  ? 302 NAG C C8  1 
HETATM 16810 N N2  . NAG T  3 .   ? -22.168 15.061  10.983  1.00 43.42  ? 302 NAG C N2  1 
HETATM 16811 O O3  . NAG T  3 .   ? -24.023 16.436  9.884   1.00 39.90  ? 302 NAG C O3  1 
HETATM 16812 O O4  . NAG T  3 .   ? -23.952 19.041  9.925   1.00 33.22  ? 302 NAG C O4  1 
HETATM 16813 O O5  . NAG T  3 .   ? -21.820 18.199  12.792  1.00 29.06  ? 302 NAG C O5  1 
HETATM 16814 O O6  . NAG T  3 .   ? -22.102 21.243  12.437  1.00 27.63  ? 302 NAG C O6  1 
HETATM 16815 O O7  . NAG T  3 .   ? -21.501 13.039  11.004  1.00 44.68  ? 302 NAG C O7  1 
HETATM 16816 P P   . PO4 U  4 .   ? -14.532 9.363   30.783  1.00 9.96   ? 303 PO4 C P   1 
HETATM 16817 O O1  . PO4 U  4 .   ? -14.442 8.281   29.737  1.00 5.90   ? 303 PO4 C O1  1 
HETATM 16818 O O2  . PO4 U  4 .   ? -15.949 9.854   30.943  1.00 8.35   ? 303 PO4 C O2  1 
HETATM 16819 O O3  . PO4 U  4 .   ? -13.690 10.548  30.443  1.00 7.48   ? 303 PO4 C O3  1 
HETATM 16820 O O4  . PO4 U  4 .   ? -14.054 8.790   32.090  1.00 12.48  ? 303 PO4 C O4  1 
HETATM 16821 P P   . PO4 V  4 .   ? -7.374  34.951  34.015  1.00 12.52  ? 304 PO4 C P   1 
HETATM 16822 O O1  . PO4 V  4 .   ? -8.210  34.846  32.763  1.00 7.70   ? 304 PO4 C O1  1 
HETATM 16823 O O2  . PO4 V  4 .   ? -5.902  34.884  33.732  1.00 14.27  ? 304 PO4 C O2  1 
HETATM 16824 O O3  . PO4 V  4 .   ? -7.714  33.792  34.915  1.00 15.00  ? 304 PO4 C O3  1 
HETATM 16825 O O4  . PO4 V  4 .   ? -7.649  36.274  34.694  1.00 13.58  ? 304 PO4 C O4  1 
HETATM 16826 P P   . PO4 W  4 .   ? -28.783 23.266  69.612  1.00 63.38  ? 305 PO4 C P   1 
HETATM 16827 O O1  . PO4 W  4 .   ? -29.866 23.587  68.605  1.00 47.31  ? 305 PO4 C O1  1 
HETATM 16828 O O2  . PO4 W  4 .   ? -27.478 23.919  69.197  1.00 51.68  ? 305 PO4 C O2  1 
HETATM 16829 O O3  . PO4 W  4 .   ? -28.593 21.765  69.670  1.00 52.34  ? 305 PO4 C O3  1 
HETATM 16830 O O4  . PO4 W  4 .   ? -29.203 23.779  70.976  1.00 66.56  ? 305 PO4 C O4  1 
HETATM 16831 C C01 . KK1 X  2 .   ? 6.393   34.846  70.383  1.00 30.57  ? 301 KK1 D C01 1 
HETATM 16832 C C02 . KK1 X  2 .   ? 7.321   35.256  69.214  1.00 30.41  ? 301 KK1 D C02 1 
HETATM 16833 C C03 . KK1 X  2 .   ? 8.577   36.042  69.693  1.00 35.00  ? 301 KK1 D C03 1 
HETATM 16834 C C04 . KK1 X  2 .   ? 9.784   35.896  68.693  1.00 37.03  ? 301 KK1 D C04 1 
HETATM 16835 C C05 . KK1 X  2 .   ? 10.546  37.260  68.382  1.00 39.00  ? 301 KK1 D C05 1 
HETATM 16836 C C06 . KK1 X  2 .   ? 10.852  37.482  66.838  1.00 46.90  ? 301 KK1 D C06 1 
HETATM 16837 C C07 . KK1 X  2 .   ? 12.354  37.883  66.484  1.00 47.72  ? 301 KK1 D C07 1 
HETATM 16838 C C08 . KK1 X  2 .   ? 12.742  38.238  64.954  1.00 43.95  ? 301 KK1 D C08 1 
HETATM 16839 N N09 . KK1 X  2 .   ? 13.958  37.475  64.328  1.00 54.28  ? 301 KK1 D N09 1 
HETATM 16840 C C10 . KK1 X  2 .   ? 13.961  37.029  62.933  1.00 39.34  ? 301 KK1 D C10 1 
HETATM 16841 C C11 . KK1 X  2 .   ? 14.991  36.109  62.394  1.00 40.91  ? 301 KK1 D C11 1 
HETATM 16842 C C12 . KK1 X  2 .   ? 14.879  35.739  60.988  1.00 35.34  ? 301 KK1 D C12 1 
HETATM 16843 N N13 . KK1 X  2 .   ? 13.835  36.234  60.254  1.00 33.16  ? 301 KK1 D N13 1 
HETATM 16844 C C14 . KK1 X  2 .   ? 12.921  37.076  60.828  1.00 30.87  ? 301 KK1 D C14 1 
HETATM 16845 N N15 . KK1 X  2 .   ? 11.837  37.587  60.040  1.00 28.97  ? 301 KK1 D N15 1 
HETATM 16846 N N16 . KK1 X  2 .   ? 12.943  37.487  62.136  1.00 37.49  ? 301 KK1 D N16 1 
HETATM 16847 C C17 . KK1 X  2 .   ? 15.886  34.723  60.155  1.00 31.59  ? 301 KK1 D C17 1 
HETATM 16848 C C18 . KK1 X  2 .   ? 17.278  34.929  60.020  1.00 39.33  ? 301 KK1 D C18 1 
HETATM 16849 C C19 . KK1 X  2 .   ? 18.200  34.066  59.277  1.00 34.70  ? 301 KK1 D C19 1 
HETATM 16850 C C20 . KK1 X  2 .   ? 17.705  32.923  58.615  1.00 31.00  ? 301 KK1 D C20 1 
HETATM 16851 O O21 . KK1 X  2 .   ? 18.526  32.075  57.901  1.00 28.00  ? 301 KK1 D O21 1 
HETATM 16852 C C22 . KK1 X  2 .   ? 17.843  31.067  57.093  1.00 23.34  ? 301 KK1 D C22 1 
HETATM 16853 C C23 . KK1 X  2 .   ? 16.324  32.686  58.714  1.00 30.04  ? 301 KK1 D C23 1 
HETATM 16854 C C24 . KK1 X  2 .   ? 15.466  33.562  59.458  1.00 31.22  ? 301 KK1 D C24 1 
HETATM 16855 C C1  . NAG Y  3 .   ? 1.186   51.577  23.968  1.00 63.55  ? 302 NAG D C1  1 
HETATM 16856 C C2  . NAG Y  3 .   ? 2.355   52.566  23.845  1.00 60.83  ? 302 NAG D C2  1 
HETATM 16857 C C3  . NAG Y  3 .   ? 1.893   53.842  23.133  1.00 67.77  ? 302 NAG D C3  1 
HETATM 16858 C C4  . NAG Y  3 .   ? 1.204   53.491  21.815  1.00 66.33  ? 302 NAG D C4  1 
HETATM 16859 C C5  . NAG Y  3 .   ? 0.119   52.457  22.105  1.00 75.40  ? 302 NAG D C5  1 
HETATM 16860 C C6  . NAG Y  3 .   ? -0.755  52.141  20.887  1.00 73.39  ? 302 NAG D C6  1 
HETATM 16861 C C7  . NAG Y  3 .   ? 4.050   52.171  25.550  1.00 64.25  ? 302 NAG D C7  1 
HETATM 16862 C C8  . NAG Y  3 .   ? 4.270   52.099  27.037  1.00 59.83  ? 302 NAG D C8  1 
HETATM 16863 N N2  . NAG Y  3 .   ? 2.976   52.851  25.130  1.00 55.20  ? 302 NAG D N2  1 
HETATM 16864 O O3  . NAG Y  3 .   ? 2.984   54.704  22.896  1.00 77.02  ? 302 NAG D O3  1 
HETATM 16865 O O4  . NAG Y  3 .   ? 0.641   54.630  21.205  1.00 65.15  ? 302 NAG D O4  1 
HETATM 16866 O O5  . NAG Y  3 .   ? 0.761   51.307  22.644  1.00 75.25  ? 302 NAG D O5  1 
HETATM 16867 O O6  . NAG Y  3 .   ? -1.964  51.523  21.289  1.00 65.94  ? 302 NAG D O6  1 
HETATM 16868 O O7  . NAG Y  3 .   ? 4.839   51.610  24.785  1.00 64.42  ? 302 NAG D O7  1 
HETATM 16869 P P   . PO4 Z  4 .   ? -14.400 30.041  75.253  1.00 69.76  ? 303 PO4 D P   1 
HETATM 16870 O O1  . PO4 Z  4 .   ? -13.861 29.188  74.130  1.00 77.22  ? 303 PO4 D O1  1 
HETATM 16871 O O2  . PO4 Z  4 .   ? -15.784 29.567  75.637  1.00 73.04  ? 303 PO4 D O2  1 
HETATM 16872 O O3  . PO4 Z  4 .   ? -14.499 31.479  74.779  1.00 56.98  ? 303 PO4 D O3  1 
HETATM 16873 O O4  . PO4 Z  4 .   ? -13.481 29.890  76.447  1.00 49.15  ? 303 PO4 D O4  1 
HETATM 16874 P P   . PO4 AA 4 .   ? -3.009  38.040  85.919  1.00 107.59 ? 304 PO4 D P   1 
HETATM 16875 O O1  . PO4 AA 4 .   ? -3.328  36.849  85.048  1.00 63.03  ? 304 PO4 D O1  1 
HETATM 16876 O O2  . PO4 AA 4 .   ? -3.747  39.252  85.404  1.00 77.54  ? 304 PO4 D O2  1 
HETATM 16877 O O3  . PO4 AA 4 .   ? -1.523  38.304  85.887  1.00 80.62  ? 304 PO4 D O3  1 
HETATM 16878 O O4  . PO4 AA 4 .   ? -3.439  37.755  87.339  1.00 76.26  ? 304 PO4 D O4  1 
HETATM 16879 C C01 . KK1 BA 2 .   ? 20.102  8.448   76.331  1.00 45.55  ? 301 KK1 E C01 1 
HETATM 16880 C C02 . KK1 BA 2 .   ? 20.511  7.973   74.906  1.00 69.04  ? 301 KK1 E C02 1 
HETATM 16881 C C03 . KK1 BA 2 .   ? 19.302  7.892   73.903  1.00 61.54  ? 301 KK1 E C03 1 
HETATM 16882 C C04 . KK1 BA 2 .   ? 19.632  7.077   72.590  1.00 52.37  ? 301 KK1 E C04 1 
HETATM 16883 C C05 . KK1 BA 2 .   ? 18.500  6.043   72.167  1.00 55.60  ? 301 KK1 E C05 1 
HETATM 16884 C C06 . KK1 BA 2 .   ? 18.367  5.815   70.600  1.00 53.22  ? 301 KK1 E C06 1 
HETATM 16885 C C07 . KK1 BA 2 .   ? 18.964  4.455   69.998  1.00 53.61  ? 301 KK1 E C07 1 
HETATM 16886 C C08 . KK1 BA 2 .   ? 18.605  4.147   68.469  1.00 35.38  ? 301 KK1 E C08 1 
HETATM 16887 N N09 . KK1 BA 2 .   ? 19.731  4.126   67.445  1.00 44.13  ? 301 KK1 E N09 1 
HETATM 16888 C C10 . KK1 BA 2 .   ? 19.667  4.805   66.119  1.00 47.46  ? 301 KK1 E C10 1 
HETATM 16889 C C11 . KK1 BA 2 .   ? 19.370  4.046   64.882  1.00 40.47  ? 301 KK1 E C11 1 
HETATM 16890 C C12 . KK1 BA 2 .   ? 19.322  4.772   63.621  1.00 32.36  ? 301 KK1 E C12 1 
HETATM 16891 N N13 . KK1 BA 2 .   ? 19.558  6.126   63.608  1.00 26.88  ? 301 KK1 E N13 1 
HETATM 16892 C C14 . KK1 BA 2 .   ? 19.835  6.775   64.798  1.00 28.88  ? 301 KK1 E C14 1 
HETATM 16893 N N15 . KK1 BA 2 .   ? 20.082  8.178   64.787  1.00 29.98  ? 301 KK1 E N15 1 
HETATM 16894 N N16 . KK1 BA 2 .   ? 19.897  6.174   66.052  1.00 42.14  ? 301 KK1 E N16 1 
HETATM 16895 C C17 . KK1 BA 2 .   ? 19.012  4.099   62.164  1.00 28.69  ? 301 KK1 E C17 1 
HETATM 16896 C C18 . KK1 BA 2 .   ? 19.791  3.028   61.640  1.00 29.86  ? 301 KK1 E C18 1 
HETATM 16897 C C19 . KK1 BA 2 .   ? 19.596  2.401   60.332  1.00 25.64  ? 301 KK1 E C19 1 
HETATM 16898 C C20 . KK1 BA 2 .   ? 18.570  2.859   59.477  1.00 25.24  ? 301 KK1 E C20 1 
HETATM 16899 O O21 . KK1 BA 2 .   ? 18.356  2.283   58.227  1.00 28.06  ? 301 KK1 E O21 1 
HETATM 16900 C C22 . KK1 BA 2 .   ? 17.324  2.907   57.405  1.00 23.49  ? 301 KK1 E C22 1 
HETATM 16901 C C23 . KK1 BA 2 .   ? 17.778  3.930   59.954  1.00 25.15  ? 301 KK1 E C23 1 
HETATM 16902 C C24 . KK1 BA 2 .   ? 17.999  4.519   61.255  1.00 27.16  ? 301 KK1 E C24 1 
HETATM 16903 C C1  . NAG CA 3 .   ? 36.870  37.417  42.001  1.00 55.63  ? 302 NAG E C1  1 
HETATM 16904 C C2  . NAG CA 3 .   ? 37.192  38.677  41.202  1.00 59.67  ? 302 NAG E C2  1 
HETATM 16905 C C3  . NAG CA 3 .   ? 38.688  38.736  40.931  1.00 64.70  ? 302 NAG E C3  1 
HETATM 16906 C C4  . NAG CA 3 .   ? 39.462  38.663  42.241  1.00 65.91  ? 302 NAG E C4  1 
HETATM 16907 C C5  . NAG CA 3 .   ? 38.977  37.530  43.154  1.00 61.49  ? 302 NAG E C5  1 
HETATM 16908 C C6  . NAG CA 3 .   ? 39.509  37.698  44.576  1.00 55.60  ? 302 NAG E C6  1 
HETATM 16909 C C7  . NAG CA 3 .   ? 35.771  39.820  39.598  1.00 66.79  ? 302 NAG E C7  1 
HETATM 16910 C C8  . NAG CA 3 .   ? 34.352  39.599  39.149  1.00 62.40  ? 302 NAG E C8  1 
HETATM 16911 N N2  . NAG CA 3 .   ? 36.452  38.730  39.954  1.00 65.28  ? 302 NAG E N2  1 
HETATM 16912 O O3  . NAG CA 3 .   ? 39.011  39.928  40.247  1.00 57.63  ? 302 NAG E O3  1 
HETATM 16913 O O4  . NAG CA 3 .   ? 40.819  38.464  41.919  1.00 66.57  ? 302 NAG E O4  1 
HETATM 16914 O O5  . NAG CA 3 .   ? 37.565  37.470  43.236  1.00 56.24  ? 302 NAG E O5  1 
HETATM 16915 O O6  . NAG CA 3 .   ? 40.919  37.658  44.594  1.00 57.45  ? 302 NAG E O6  1 
HETATM 16916 O O7  . NAG CA 3 .   ? 36.258  40.954  39.629  1.00 61.22  ? 302 NAG E O7  1 
HETATM 16917 P P   . PO4 DA 4 .   ? 16.310  35.280  46.275  1.00 14.66  ? 303 PO4 E P   1 
HETATM 16918 O O1  . PO4 DA 4 .   ? 16.383  36.512  45.400  1.00 12.54  ? 303 PO4 E O1  1 
HETATM 16919 O O2  . PO4 DA 4 .   ? 14.851  34.945  46.385  1.00 20.91  ? 303 PO4 E O2  1 
HETATM 16920 O O3  . PO4 DA 4 .   ? 17.049  34.118  45.693  1.00 8.96   ? 303 PO4 E O3  1 
HETATM 16921 O O4  . PO4 DA 4 .   ? 16.867  35.515  47.657  1.00 14.19  ? 303 PO4 E O4  1 
HETATM 16922 P P   . PO4 EA 4 .   ? -2.262  16.933  70.139  1.00 97.89  ? 304 PO4 E P   1 
HETATM 16923 O O1  . PO4 EA 4 .   ? -1.328  16.106  69.272  1.00 76.81  ? 304 PO4 E O1  1 
HETATM 16924 O O2  . PO4 EA 4 .   ? -3.446  17.414  69.324  1.00 79.51  ? 304 PO4 E O2  1 
HETATM 16925 O O3  . PO4 EA 4 .   ? -2.766  16.101  71.306  1.00 76.89  ? 304 PO4 E O3  1 
HETATM 16926 O O4  . PO4 EA 4 .   ? -1.519  18.144  70.670  1.00 72.91  ? 304 PO4 E O4  1 
HETATM 16927 P P   . PO4 FA 4 .   ? 21.530  33.842  72.546  1.00 103.48 ? 305 PO4 E P   1 
HETATM 16928 O O1  . PO4 FA 4 .   ? 22.229  33.656  71.221  1.00 87.09  ? 305 PO4 E O1  1 
HETATM 16929 O O2  . PO4 FA 4 .   ? 21.423  35.319  72.834  1.00 78.31  ? 305 PO4 E O2  1 
HETATM 16930 O O3  . PO4 FA 4 .   ? 20.187  33.135  72.460  1.00 81.97  ? 305 PO4 E O3  1 
HETATM 16931 O O4  . PO4 FA 4 .   ? 22.353  33.222  73.647  1.00 80.73  ? 305 PO4 E O4  1 
HETATM 16932 C C01 . KK1 GA 2 .   ? -1.038  14.108  -17.635 1.00 59.42  ? 301 KK1 F C01 1 
HETATM 16933 C C02 . KK1 GA 2 .   ? -0.244  13.957  -16.314 1.00 62.34  ? 301 KK1 F C02 1 
HETATM 16934 C C03 . KK1 GA 2 .   ? 0.658   12.681  -16.297 1.00 63.46  ? 301 KK1 F C03 1 
HETATM 16935 C C04 . KK1 GA 2 .   ? 1.035   12.210  -14.852 1.00 53.53  ? 301 KK1 F C04 1 
HETATM 16936 C C05 . KK1 GA 2 .   ? 0.894   10.649  -14.623 1.00 48.91  ? 301 KK1 F C05 1 
HETATM 16937 C C06 . KK1 GA 2 .   ? 0.597   10.274  -13.111 1.00 57.01  ? 301 KK1 F C06 1 
HETATM 16938 C C07 . KK1 GA 2 .   ? -0.435  9.089   -12.821 1.00 48.58  ? 301 KK1 F C07 1 
HETATM 16939 C C08 . KK1 GA 2 .   ? -0.252  8.328   -11.405 1.00 45.08  ? 301 KK1 F C08 1 
HETATM 16940 N N09 . KK1 GA 2 .   ? -1.272  8.658   -10.301 1.00 50.48  ? 301 KK1 F N09 1 
HETATM 16941 C C10 . KK1 GA 2 .   ? -0.904  9.290   -9.025  1.00 42.94  ? 301 KK1 F C10 1 
HETATM 16942 C C11 . KK1 GA 2 .   ? -0.731  8.484   -7.802  1.00 34.51  ? 301 KK1 F C11 1 
HETATM 16943 C C12 . KK1 GA 2 .   ? -0.363  9.178   -6.581  1.00 33.53  ? 301 KK1 F C12 1 
HETATM 16944 N N13 . KK1 GA 2 .   ? -0.185  10.537  -6.605  1.00 28.61  ? 301 KK1 F N13 1 
HETATM 16945 C C14 . KK1 GA 2 .   ? -0.365  11.227  -7.778  1.00 26.23  ? 301 KK1 F C14 1 
HETATM 16946 N N15 . KK1 GA 2 .   ? -0.184  12.634  -7.781  1.00 27.99  ? 301 KK1 F N15 1 
HETATM 16947 N N16 . KK1 GA 2 .   ? -0.716  10.665  -8.995  1.00 39.05  ? 301 KK1 F N16 1 
HETATM 16948 C C17 . KK1 GA 2 .   ? -0.127  8.455   -5.131  1.00 34.11  ? 301 KK1 F C17 1 
HETATM 16949 C C18 . KK1 GA 2 .   ? -1.017  7.476   -4.612  1.00 28.49  ? 301 KK1 F C18 1 
HETATM 16950 C C19 . KK1 GA 2 .   ? -0.848  6.814   -3.325  1.00 30.17  ? 301 KK1 F C19 1 
HETATM 16951 C C20 . KK1 GA 2 .   ? 0.237   7.140   -2.483  1.00 25.04  ? 301 KK1 F C20 1 
HETATM 16952 O O21 . KK1 GA 2 .   ? 0.400   6.526   -1.259  1.00 26.05  ? 301 KK1 F O21 1 
HETATM 16953 C C22 . KK1 GA 2 .   ? 1.663   6.774   -0.557  1.00 24.66  ? 301 KK1 F C22 1 
HETATM 16954 C C23 . KK1 GA 2 .   ? 1.132   8.117   -2.951  1.00 25.94  ? 301 KK1 F C23 1 
HETATM 16955 C C24 . KK1 GA 2 .   ? 0.946   8.740   -4.236  1.00 30.34  ? 301 KK1 F C24 1 
HETATM 16956 C C1  . NAG HA 3 .   ? -10.986 43.367  17.144  1.00 47.64  ? 302 NAG F C1  1 
HETATM 16957 C C2  . NAG HA 3 .   ? -12.502 43.424  17.188  1.00 55.53  ? 302 NAG F C2  1 
HETATM 16958 C C3  . NAG HA 3 .   ? -12.877 44.850  16.814  1.00 58.00  ? 302 NAG F C3  1 
HETATM 16959 C C4  . NAG HA 3 .   ? -12.254 45.797  17.845  1.00 63.59  ? 302 NAG F C4  1 
HETATM 16960 C C5  . NAG HA 3 .   ? -10.790 45.469  18.177  1.00 56.57  ? 302 NAG F C5  1 
HETATM 16961 C C6  . NAG HA 3 .   ? -10.353 46.157  19.468  1.00 56.27  ? 302 NAG F C6  1 
HETATM 16962 C C7  . NAG HA 3 .   ? -13.753 41.327  16.834  1.00 61.53  ? 302 NAG F C7  1 
HETATM 16963 C C8  . NAG HA 3 .   ? -13.554 40.962  18.283  1.00 62.87  ? 302 NAG F C8  1 
HETATM 16964 N N2  . NAG HA 3 .   ? -13.117 42.405  16.346  1.00 60.28  ? 302 NAG F N2  1 
HETATM 16965 O O3  . NAG HA 3 .   ? -14.282 44.994  16.796  1.00 63.01  ? 302 NAG F O3  1 
HETATM 16966 O O4  . NAG HA 3 .   ? -12.327 47.129  17.371  1.00 64.21  ? 302 NAG F O4  1 
HETATM 16967 O O5  . NAG HA 3 .   ? -10.540 44.075  18.279  1.00 50.81  ? 302 NAG F O5  1 
HETATM 16968 O O6  . NAG HA 3 .   ? -8.964  46.409  19.420  1.00 55.06  ? 302 NAG F O6  1 
HETATM 16969 O O7  . NAG HA 3 .   ? -14.487 40.624  16.140  1.00 59.34  ? 302 NAG F O7  1 
HETATM 16970 P P   . PO4 IA 4 .   ? 8.835   37.196  12.845  1.00 21.07  ? 303 PO4 F P   1 
HETATM 16971 O O1  . PO4 IA 4 .   ? 8.125   37.491  11.552  1.00 19.76  ? 303 PO4 F O1  1 
HETATM 16972 O O2  . PO4 IA 4 .   ? 10.274  36.865  12.556  1.00 20.18  ? 303 PO4 F O2  1 
HETATM 16973 O O3  . PO4 IA 4 .   ? 8.172   36.000  13.475  1.00 17.14  ? 303 PO4 F O3  1 
HETATM 16974 O O4  . PO4 IA 4 .   ? 8.771   38.403  13.759  1.00 17.74  ? 303 PO4 F O4  1 
HETATM 16975 P P   . PO4 JA 4 .   ? -3.031  39.619  19.707  1.00 71.91  ? 304 PO4 F P   1 
HETATM 16976 O O1  . PO4 JA 4 .   ? -2.789  38.330  18.956  1.00 45.71  ? 304 PO4 F O1  1 
HETATM 16977 O O2  . PO4 JA 4 .   ? -4.256  40.271  19.108  1.00 48.10  ? 304 PO4 F O2  1 
HETATM 16978 O O3  . PO4 JA 4 .   ? -1.809  40.514  19.544  1.00 46.96  ? 304 PO4 F O3  1 
HETATM 16979 O O4  . PO4 JA 4 .   ? -3.295  39.330  21.180  1.00 46.45  ? 304 PO4 F O4  1 
HETATM 16980 N N09 . KK1 KA 2 .   ? 22.067  -12.755 2.261   1.00 50.19  ? 301 KK1 G N09 1 
HETATM 16981 C C10 . KK1 KA 2 .   ? 21.278  -11.780 2.982   1.00 51.35  ? 301 KK1 G C10 1 
HETATM 16982 C C11 . KK1 KA 2 .   ? 21.729  -11.314 4.292   1.00 45.58  ? 301 KK1 G C11 1 
HETATM 16983 C C12 . KK1 KA 2 .   ? 20.936  -10.345 5.001   1.00 40.90  ? 301 KK1 G C12 1 
HETATM 16984 N N13 . KK1 KA 2 .   ? 19.773  -9.877  4.432   1.00 36.38  ? 301 KK1 G N13 1 
HETATM 16985 C C14 . KK1 KA 2 .   ? 19.396  -10.365 3.172   1.00 38.81  ? 301 KK1 G C14 1 
HETATM 16986 N N15 . KK1 KA 2 .   ? 18.192  -9.892  2.564   1.00 41.89  ? 301 KK1 G N15 1 
HETATM 16987 N N16 . KK1 KA 2 .   ? 20.110  -11.305 2.420   1.00 53.75  ? 301 KK1 G N16 1 
HETATM 16988 C C17 . KK1 KA 2 .   ? 21.373  -9.779  6.463   1.00 35.31  ? 301 KK1 G C17 1 
HETATM 16989 C C18 . KK1 KA 2 .   ? 21.829  -10.653 7.479   1.00 31.16  ? 301 KK1 G C18 1 
HETATM 16990 C C19 . KK1 KA 2 .   ? 22.240  -10.242 8.810   1.00 29.95  ? 301 KK1 G C19 1 
HETATM 16991 C C20 . KK1 KA 2 .   ? 22.204  -8.882  9.181   1.00 30.23  ? 301 KK1 G C20 1 
HETATM 16992 O O21 . KK1 KA 2 .   ? 22.601  -8.490  10.466  1.00 38.20  ? 301 KK1 G O21 1 
HETATM 16993 C C22 . KK1 KA 2 .   ? 22.362  -7.126  10.881  1.00 31.04  ? 301 KK1 G C22 1 
HETATM 16994 C C23 . KK1 KA 2 .   ? 21.756  -7.976  8.197   1.00 30.10  ? 301 KK1 G C23 1 
HETATM 16995 C C24 . KK1 KA 2 .   ? 21.356  -8.425  6.885   1.00 35.88  ? 301 KK1 G C24 1 
HETATM 16996 C C1  . NAG LA 3 .   ? -19.135 0.981   12.965  1.00 46.99  ? 302 NAG G C1  1 
HETATM 16997 C C2  . NAG LA 3 .   ? -19.567 -0.146  13.893  1.00 50.05  ? 302 NAG G C2  1 
HETATM 16998 C C3  . NAG LA 3 .   ? -21.088 -0.207  13.946  1.00 63.57  ? 302 NAG G C3  1 
HETATM 16999 C C4  . NAG LA 3 .   ? -21.648 1.166   14.336  1.00 63.58  ? 302 NAG G C4  1 
HETATM 17000 C C5  . NAG LA 3 .   ? -21.052 2.307   13.509  1.00 52.54  ? 302 NAG G C5  1 
HETATM 17001 C C6  . NAG LA 3 .   ? -21.418 3.646   14.145  1.00 47.15  ? 302 NAG G C6  1 
HETATM 17002 C C7  . NAG LA 3 .   ? -18.241 -2.174  14.248  1.00 53.96  ? 302 NAG G C7  1 
HETATM 17003 C C8  . NAG LA 3 .   ? -17.808 -1.605  15.568  1.00 47.62  ? 302 NAG G C8  1 
HETATM 17004 N N2  . NAG LA 3 .   ? -19.000 -1.411  13.458  1.00 57.86  ? 302 NAG G N2  1 
HETATM 17005 O O3  . NAG LA 3 .   ? -21.481 -1.196  14.878  1.00 61.32  ? 302 NAG G O3  1 
HETATM 17006 O O4  . NAG LA 3 .   ? -23.052 1.197   14.179  1.00 57.07  ? 302 NAG G O4  1 
HETATM 17007 O O5  . NAG LA 3 .   ? -19.642 2.217   13.433  1.00 45.62  ? 302 NAG G O5  1 
HETATM 17008 O O6  . NAG LA 3 .   ? -22.748 3.600   14.616  1.00 47.09  ? 302 NAG G O6  1 
HETATM 17009 O O7  . NAG LA 3 .   ? -17.893 -3.308  13.925  1.00 57.92  ? 302 NAG G O7  1 
HETATM 17010 P P   . PO4 MA 4 .   ? -3.665  14.282  6.808   1.00 17.48  ? 303 PO4 G P   1 
HETATM 17011 O O1  . PO4 MA 4 .   ? -4.135  13.282  5.780   1.00 16.29  ? 303 PO4 G O1  1 
HETATM 17012 O O2  . PO4 MA 4 .   ? -4.703  15.348  7.097   1.00 12.74  ? 303 PO4 G O2  1 
HETATM 17013 O O3  . PO4 MA 4 .   ? -2.401  14.968  6.344   1.00 19.35  ? 303 PO4 G O3  1 
HETATM 17014 O O4  . PO4 MA 4 .   ? -3.388  13.499  8.061   1.00 21.93  ? 303 PO4 G O4  1 
HETATM 17015 P P   . PO4 NA 4 .   ? -12.694 8.225   14.835  1.00 67.54  ? 304 PO4 G P   1 
HETATM 17016 O O1  . PO4 NA 4 .   ? -13.704 7.944   13.748  1.00 40.82  ? 304 PO4 G O1  1 
HETATM 17017 O O2  . PO4 NA 4 .   ? -11.682 9.227   14.325  1.00 37.31  ? 304 PO4 G O2  1 
HETATM 17018 O O3  . PO4 NA 4 .   ? -12.012 6.920   15.198  1.00 41.79  ? 304 PO4 G O3  1 
HETATM 17019 O O4  . PO4 NA 4 .   ? -13.374 8.813   16.060  1.00 51.58  ? 304 PO4 G O4  1 
HETATM 17020 N N09 . KK1 OA 2 .   ? 47.068  5.278   14.083  1.00 57.05  ? 301 KK1 H N09 1 
HETATM 17021 C C10 . KK1 OA 2 .   ? 45.742  5.305   14.659  1.00 53.67  ? 301 KK1 H C10 1 
HETATM 17022 C C11 . KK1 OA 2 .   ? 45.347  6.429   15.507  1.00 38.27  ? 301 KK1 H C11 1 
HETATM 17023 C C12 . KK1 OA 2 .   ? 44.025  6.446   16.075  1.00 34.75  ? 301 KK1 H C12 1 
HETATM 17024 N N13 . KK1 OA 2 .   ? 43.162  5.406   15.810  1.00 35.61  ? 301 KK1 H N13 1 
HETATM 17025 C C14 . KK1 OA 2 .   ? 43.603  4.357   14.989  1.00 34.01  ? 301 KK1 H C14 1 
HETATM 17026 N N15 . KK1 OA 2 .   ? 42.723  3.269   14.701  1.00 32.04  ? 301 KK1 H N15 1 
HETATM 17027 N N16 . KK1 OA 2 .   ? 44.869  4.267   14.399  1.00 50.34  ? 301 KK1 H N16 1 
HETATM 17028 C C17 . KK1 OA 2 .   ? 43.514  7.662   17.027  1.00 41.73  ? 301 KK1 H C17 1 
HETATM 17029 C C18 . KK1 OA 2 .   ? 44.280  8.094   18.137  1.00 39.70  ? 301 KK1 H C18 1 
HETATM 17030 C C19 . KK1 OA 2 .   ? 43.907  9.168   19.041  1.00 37.64  ? 301 KK1 H C19 1 
HETATM 17031 C C20 . KK1 OA 2 .   ? 42.699  9.873   18.853  1.00 38.67  ? 301 KK1 H C20 1 
HETATM 17032 O O21 . KK1 OA 2 .   ? 42.343  10.908  19.727  1.00 37.85  ? 301 KK1 H O21 1 
HETATM 17033 C C22 . KK1 OA 2 .   ? 41.113  10.791  20.478  1.00 30.61  ? 301 KK1 H C22 1 
HETATM 17034 C C23 . KK1 OA 2 .   ? 41.905  9.473   17.758  1.00 29.92  ? 301 KK1 H C23 1 
HETATM 17035 C C24 . KK1 OA 2 .   ? 42.312  8.401   16.882  1.00 31.86  ? 301 KK1 H C24 1 
HETATM 17036 C C1  . NAG PA 3 .   ? 13.772  -20.193 30.743  1.00 62.92  ? 302 NAG H C1  1 
HETATM 17037 C C2  . NAG PA 3 .   ? 14.449  -21.120 31.759  1.00 64.79  ? 302 NAG H C2  1 
HETATM 17038 C C3  . NAG PA 3 .   ? 13.747  -22.487 31.776  1.00 71.76  ? 302 NAG H C3  1 
HETATM 17039 C C4  . NAG PA 3 .   ? 12.225  -22.330 31.924  1.00 69.77  ? 302 NAG H C4  1 
HETATM 17040 C C5  . NAG PA 3 .   ? 11.695  -21.250 30.976  1.00 65.26  ? 302 NAG H C5  1 
HETATM 17041 C C6  . NAG PA 3 .   ? 10.190  -20.991 31.097  1.00 61.79  ? 302 NAG H C6  1 
HETATM 17042 C C7  . NAG PA 3 .   ? 16.760  -21.539 32.432  1.00 74.40  ? 302 NAG H C7  1 
HETATM 17043 C C8  . NAG PA 3 .   ? 17.483  -20.380 33.057  1.00 65.43  ? 302 NAG H C8  1 
HETATM 17044 N N2  . NAG PA 3 .   ? 15.869  -21.253 31.482  1.00 68.03  ? 302 NAG H N2  1 
HETATM 17045 O O3  . NAG PA 3 .   ? 14.276  -23.318 32.797  1.00 67.47  ? 302 NAG H O3  1 
HETATM 17046 O O4  . NAG PA 3 .   ? 11.585  -23.557 31.644  1.00 64.97  ? 302 NAG H O4  1 
HETATM 17047 O O5  . NAG PA 3 .   ? 12.428  -20.056 31.172  1.00 67.55  ? 302 NAG H O5  1 
HETATM 17048 O O6  . NAG PA 3 .   ? 9.778   -20.977 32.449  1.00 71.16  ? 302 NAG H O6  1 
HETATM 17049 O O7  . NAG PA 3 .   ? 16.992  -22.693 32.789  1.00 81.77  ? 302 NAG H O7  1 
HETATM 17050 P P   . PO4 QA 4 .   ? 11.596  -5.929  15.178  1.00 16.29  ? 303 PO4 H P   1 
HETATM 17051 O O1  . PO4 QA 4 .   ? 11.834  -4.980  14.022  1.00 17.14  ? 303 PO4 H O1  1 
HETATM 17052 O O2  . PO4 QA 4 .   ? 12.372  -7.207  15.062  1.00 23.58  ? 303 PO4 H O2  1 
HETATM 17053 O O3  . PO4 QA 4 .   ? 10.135  -6.295  15.193  1.00 20.63  ? 303 PO4 H O3  1 
HETATM 17054 O O4  . PO4 QA 4 .   ? 12.032  -5.283  16.462  1.00 19.14  ? 303 PO4 H O4  1 
HETATM 17055 P P   . PO4 RA 4 .   ? 33.632  4.512   26.154  1.00 16.13  ? 304 PO4 H P   1 
HETATM 17056 O O1  . PO4 RA 4 .   ? 33.084  4.300   24.773  1.00 28.40  ? 304 PO4 H O1  1 
HETATM 17057 O O2  . PO4 RA 4 .   ? 33.035  5.774   26.703  1.00 17.25  ? 304 PO4 H O2  1 
HETATM 17058 O O3  . PO4 RA 4 .   ? 35.120  4.724   26.104  1.00 20.05  ? 304 PO4 H O3  1 
HETATM 17059 O O4  . PO4 RA 4 .   ? 33.284  3.281   26.943  1.00 14.90  ? 304 PO4 H O4  1 
HETATM 17060 C C01 . KK1 SA 2 .   ? 49.101  36.835  4.844   1.00 62.58  ? 301 KK1 I C01 1 
HETATM 17061 C C02 . KK1 SA 2 .   ? 48.223  36.993  6.113   1.00 66.49  ? 301 KK1 I C02 1 
HETATM 17062 C C03 . KK1 SA 2 .   ? 46.924  36.112  6.082   1.00 63.88  ? 301 KK1 I C03 1 
HETATM 17063 C C04 . KK1 SA 2 .   ? 45.804  36.650  7.043   1.00 56.66  ? 301 KK1 I C04 1 
HETATM 17064 C C05 . KK1 SA 2 .   ? 44.319  36.262  6.632   1.00 54.19  ? 301 KK1 I C05 1 
HETATM 17065 C C06 . KK1 SA 2 .   ? 43.224  37.310  7.135   1.00 59.11  ? 301 KK1 I C06 1 
HETATM 17066 C C07 . KK1 SA 2 .   ? 42.372  36.946  8.458   1.00 49.81  ? 301 KK1 I C07 1 
HETATM 17067 C C08 . KK1 SA 2 .   ? 40.944  37.715  8.627   1.00 47.88  ? 301 KK1 I C08 1 
HETATM 17068 N N09 . KK1 SA 2 .   ? 40.469  38.030  10.058  1.00 44.85  ? 301 KK1 I N09 1 
HETATM 17069 C C10 . KK1 SA 2 .   ? 39.690  37.132  10.941  1.00 41.43  ? 301 KK1 I C10 1 
HETATM 17070 C C11 . KK1 SA 2 .   ? 38.302  37.475  11.335  1.00 42.59  ? 301 KK1 I C11 1 
HETATM 17071 C C12 . KK1 SA 2 .   ? 37.595  36.571  12.231  1.00 37.31  ? 301 KK1 I C12 1 
HETATM 17072 N N13 . KK1 SA 2 .   ? 38.225  35.433  12.683  1.00 34.94  ? 301 KK1 I N13 1 
HETATM 17073 C C14 . KK1 SA 2 .   ? 39.519  35.164  12.285  1.00 33.92  ? 301 KK1 I C14 1 
HETATM 17074 N N15 . KK1 SA 2 .   ? 40.150  33.980  12.765  1.00 30.64  ? 301 KK1 I N15 1 
HETATM 17075 N N16 . KK1 SA 2 .   ? 40.288  35.971  11.429  1.00 41.39  ? 301 KK1 I N16 1 
HETATM 17076 C C17 . KK1 SA 2 .   ? 36.066  36.768  12.745  1.00 32.56  ? 301 KK1 I C17 1 
HETATM 17077 C C18 . KK1 SA 2 .   ? 35.645  37.895  13.499  1.00 29.49  ? 301 KK1 I C18 1 
HETATM 17078 C C19 . KK1 SA 2 .   ? 34.290  38.093  13.998  1.00 30.71  ? 301 KK1 I C19 1 
HETATM 17079 C C20 . KK1 SA 2 .   ? 33.276  37.126  13.758  1.00 27.95  ? 301 KK1 I C20 1 
HETATM 17080 O O21 . KK1 SA 2 .   ? 31.973  37.316  14.229  1.00 28.69  ? 301 KK1 I O21 1 
HETATM 17081 C C22 . KK1 SA 2 .   ? 31.269  36.172  14.786  1.00 29.06  ? 301 KK1 I C22 1 
HETATM 17082 C C23 . KK1 SA 2 .   ? 33.654  35.986  13.020  1.00 30.41  ? 301 KK1 I C23 1 
HETATM 17083 C C24 . KK1 SA 2 .   ? 35.010  35.827  12.538  1.00 34.74  ? 301 KK1 I C24 1 
HETATM 17084 C C1  . NAG TA 3 .   ? 43.103  9.467   44.407  1.00 51.53  ? 302 NAG I C1  1 
HETATM 17085 C C2  . NAG TA 3 .   ? 43.590  10.184  45.648  1.00 48.25  ? 302 NAG I C2  1 
HETATM 17086 C C3  . NAG TA 3 .   ? 44.131  9.160   46.661  1.00 56.03  ? 302 NAG I C3  1 
HETATM 17087 C C4  . NAG TA 3 .   ? 42.953  8.322   47.010  1.00 61.00  ? 302 NAG I C4  1 
HETATM 17088 C C5  . NAG TA 3 .   ? 42.742  7.476   45.816  1.00 57.87  ? 302 NAG I C5  1 
HETATM 17089 C C6  . NAG TA 3 .   ? 41.738  6.405   46.098  1.00 60.42  ? 302 NAG I C6  1 
HETATM 17090 C C7  . NAG TA 3 .   ? 43.863  12.474  45.125  1.00 58.87  ? 302 NAG I C7  1 
HETATM 17091 C C8  . NAG TA 3 .   ? 44.653  13.685  45.405  1.00 38.22  ? 302 NAG I C8  1 
HETATM 17092 N N2  . NAG TA 3 .   ? 44.441  11.287  45.250  1.00 65.10  ? 302 NAG I N2  1 
HETATM 17093 O O3  . NAG TA 3 .   ? 44.509  9.629   47.953  1.00 55.25  ? 302 NAG I O3  1 
HETATM 17094 O O4  . NAG TA 3 .   ? 43.254  7.551   48.131  1.00 55.29  ? 302 NAG I O4  1 
HETATM 17095 O O5  . NAG TA 3 .   ? 42.259  8.421   44.860  1.00 62.09  ? 302 NAG I O5  1 
HETATM 17096 O O6  . NAG TA 3 .   ? 42.194  5.255   45.415  1.00 57.73  ? 302 NAG I O6  1 
HETATM 17097 O O7  . NAG TA 3 .   ? 42.717  12.598  44.813  1.00 61.80  ? 302 NAG I O7  1 
HETATM 17098 N N09 . KK1 UA 2 .   ? 10.355  40.152  -4.848  1.00 56.86  ? 301 KK1 J N09 1 
HETATM 17099 C C10 . KK1 UA 2 .   ? 10.673  39.632  -3.537  1.00 51.55  ? 301 KK1 J C10 1 
HETATM 17100 C C11 . KK1 UA 2 .   ? 9.763   38.683  -2.898  1.00 45.16  ? 301 KK1 J C11 1 
HETATM 17101 C C12 . KK1 UA 2 .   ? 10.089  38.172  -1.593  1.00 46.22  ? 301 KK1 J C12 1 
HETATM 17102 N N13 . KK1 UA 2 .   ? 11.249  38.586  -0.975  1.00 41.27  ? 301 KK1 J N13 1 
HETATM 17103 C C14 . KK1 UA 2 .   ? 12.079  39.498  -1.643  1.00 35.66  ? 301 KK1 J C14 1 
HETATM 17104 N N15 . KK1 UA 2 .   ? 13.286  39.940  -1.019  1.00 38.36  ? 301 KK1 J N15 1 
HETATM 17105 N N16 . KK1 UA 2 .   ? 11.833  40.041  -2.910  1.00 45.90  ? 301 KK1 J N16 1 
HETATM 17106 C C17 . KK1 UA 2 .   ? 9.126   37.114  -0.818  1.00 42.26  ? 301 KK1 J C17 1 
HETATM 17107 C C18 . KK1 UA 2 .   ? 7.735   37.345  -0.694  1.00 34.91  ? 301 KK1 J C18 1 
HETATM 17108 C C19 . KK1 UA 2 .   ? 6.799   36.461  -0.023  1.00 31.86  ? 301 KK1 J C19 1 
HETATM 17109 C C20 . KK1 UA 2 .   ? 7.248   35.263  0.572   1.00 35.54  ? 301 KK1 J C20 1 
HETATM 17110 O O21 . KK1 UA 2 .   ? 6.342   34.413  1.219   1.00 31.02  ? 301 KK1 J O21 1 
HETATM 17111 C C22 . KK1 UA 2 .   ? 6.732   33.045  1.472   1.00 22.02  ? 301 KK1 J C22 1 
HETATM 17112 C C23 . KK1 UA 2 .   ? 8.629   34.994  0.471   1.00 37.96  ? 301 KK1 J C23 1 
HETATM 17113 C C24 . KK1 UA 2 .   ? 9.527   35.899  -0.205  1.00 38.69  ? 301 KK1 J C24 1 
HETATM 17114 C C1  . NAG VA 3 .   ? 27.539  47.415  36.891  1.00 57.57  ? 302 NAG J C1  1 
HETATM 17115 C C2  . NAG VA 3 .   ? 26.500  48.532  37.063  1.00 57.16  ? 302 NAG J C2  1 
HETATM 17116 C C3  . NAG VA 3 .   ? 26.516  49.158  38.454  1.00 66.63  ? 302 NAG J C3  1 
HETATM 17117 C C4  . NAG VA 3 .   ? 27.956  49.437  38.848  1.00 67.06  ? 302 NAG J C4  1 
HETATM 17118 C C5  . NAG VA 3 .   ? 28.730  48.118  38.926  1.00 65.28  ? 302 NAG J C5  1 
HETATM 17119 C C6  . NAG VA 3 .   ? 28.864  47.688  40.393  1.00 62.12  ? 302 NAG J C6  1 
HETATM 17120 C C7  . NAG VA 3 .   ? 25.756  50.025  35.336  1.00 53.82  ? 302 NAG J C7  1 
HETATM 17121 C C8  . NAG VA 3 .   ? 26.153  50.884  34.166  1.00 45.31  ? 302 NAG J C8  1 
HETATM 17122 N N2  . NAG VA 3 .   ? 26.742  49.592  36.109  1.00 54.17  ? 302 NAG J N2  1 
HETATM 17123 O O3  . NAG VA 3 .   ? 25.903  48.317  39.411  1.00 70.49  ? 302 NAG J O3  1 
HETATM 17124 O O4  . NAG VA 3 .   ? 28.539  50.328  37.914  1.00 68.55  ? 302 NAG J O4  1 
HETATM 17125 O O5  . NAG VA 3 .   ? 28.122  47.081  38.154  1.00 62.24  ? 302 NAG J O5  1 
HETATM 17126 O O6  . NAG VA 3 .   ? 29.865  46.703  40.573  1.00 57.87  ? 302 NAG J O6  1 
HETATM 17127 O O7  . NAG VA 3 .   ? 24.579  49.739  35.564  1.00 48.29  ? 302 NAG J O7  1 
HETATM 17128 P P   . PO4 WA 4 .   ? 31.870  31.154  24.512  1.00 16.97  ? 303 PO4 J P   1 
HETATM 17129 O O1  . PO4 WA 4 .   ? 31.813  29.974  23.579  1.00 21.75  ? 303 PO4 J O1  1 
HETATM 17130 O O2  . PO4 WA 4 .   ? 30.496  31.631  24.878  1.00 15.28  ? 303 PO4 J O2  1 
HETATM 17131 O O3  . PO4 WA 4 .   ? 32.523  32.316  23.811  1.00 20.52  ? 303 PO4 J O3  1 
HETATM 17132 O O4  . PO4 WA 4 .   ? 32.662  30.726  25.728  1.00 17.13  ? 303 PO4 J O4  1 
HETATM 17133 O O   . HOH XA 5 .   ? 31.466  4.547   42.790  1.00 20.45  ? 401 HOH A O   1 
HETATM 17134 O O   . HOH XA 5 .   ? 16.708  -2.074  34.068  1.00 23.45  ? 402 HOH A O   1 
HETATM 17135 O O   . HOH XA 5 .   ? 3.173   0.385   57.314  1.00 18.91  ? 403 HOH A O   1 
HETATM 17136 O O   . HOH XA 5 .   ? 8.427   11.938  57.042  1.00 13.84  ? 404 HOH A O   1 
HETATM 17137 O O   . HOH XA 5 .   ? 31.400  1.317   41.758  1.00 29.10  ? 405 HOH A O   1 
HETATM 17138 O O   . HOH XA 5 .   ? 11.941  7.229   58.067  1.00 20.45  ? 406 HOH A O   1 
HETATM 17139 O O   . HOH XA 5 .   ? -8.837  7.685   77.066  1.00 32.78  ? 407 HOH A O   1 
HETATM 17140 O O   . HOH XA 5 .   ? 9.193   -0.160  38.316  1.00 6.35   ? 408 HOH A O   1 
HETATM 17141 O O   . HOH XA 5 .   ? 1.457   -3.048  88.197  1.00 29.78  ? 409 HOH A O   1 
HETATM 17142 O O   . HOH XA 5 .   ? 26.086  6.761   31.456  1.00 11.44  ? 410 HOH A O   1 
HETATM 17143 O O   . HOH XA 5 .   ? 23.866  11.630  41.751  1.00 14.12  ? 411 HOH A O   1 
HETATM 17144 O O   . HOH XA 5 .   ? 41.961  4.237   49.411  1.00 40.16  ? 412 HOH A O   1 
HETATM 17145 O O   . HOH XA 5 .   ? 3.183   10.307  57.335  1.00 15.35  ? 413 HOH A O   1 
HETATM 17146 O O   . HOH XA 5 .   ? 2.678   -1.096  59.550  1.00 25.85  ? 414 HOH A O   1 
HETATM 17147 O O   . HOH XA 5 .   ? 0.927   0.330   59.998  1.00 19.62  ? 415 HOH A O   1 
HETATM 17148 O O   . HOH XA 5 .   ? -1.820  -0.051  57.911  1.00 18.66  ? 416 HOH A O   1 
HETATM 17149 O O   . HOH XA 5 .   ? 11.777  8.963   42.100  1.00 22.24  ? 417 HOH A O   1 
HETATM 17150 O O   . HOH XA 5 .   ? 18.084  -8.359  59.069  1.00 20.72  ? 418 HOH A O   1 
HETATM 17151 O O   . HOH YA 5 .   ? -0.578  -11.293 24.836  1.00 24.45  ? 401 HOH B O   1 
HETATM 17152 O O   . HOH YA 5 .   ? -28.521 8.962   55.204  1.00 18.42  ? 402 HOH B O   1 
HETATM 17153 O O   . HOH YA 5 .   ? -9.046  6.810   37.112  1.00 16.18  ? 403 HOH B O   1 
HETATM 17154 O O   . HOH YA 5 .   ? -14.905 -10.016 72.835  1.00 34.59  ? 404 HOH B O   1 
HETATM 17155 O O   . HOH YA 5 .   ? -6.149  8.572   29.950  1.00 5.10   ? 405 HOH B O   1 
HETATM 17156 O O   . HOH YA 5 .   ? 7.580   -19.009 43.441  1.00 33.02  ? 406 HOH B O   1 
HETATM 17157 O O   . HOH YA 5 .   ? -19.916 -9.369  65.359  1.00 15.63  ? 407 HOH B O   1 
HETATM 17158 O O   . HOH YA 5 .   ? 0.449   4.264   48.427  1.00 12.63  ? 408 HOH B O   1 
HETATM 17159 O O   . HOH YA 5 .   ? -0.491  2.331   54.161  1.00 21.06  ? 409 HOH B O   1 
HETATM 17160 O O   . HOH YA 5 .   ? -19.382 11.007  49.584  1.00 15.70  ? 410 HOH B O   1 
HETATM 17161 O O   . HOH YA 5 .   ? -24.790 -11.034 46.792  1.00 20.23  ? 411 HOH B O   1 
HETATM 17162 O O   . HOH YA 5 .   ? -33.922 14.067  39.624  1.00 17.60  ? 412 HOH B O   1 
HETATM 17163 O O   . HOH YA 5 .   ? 3.372   -15.599 26.565  1.00 26.45  ? 413 HOH B O   1 
HETATM 17164 O O   . HOH YA 5 .   ? -24.774 10.035  27.529  1.00 41.06  ? 414 HOH B O   1 
HETATM 17165 O O   . HOH YA 5 .   ? -2.348  4.374   51.769  1.00 23.48  ? 415 HOH B O   1 
HETATM 17166 O O   . HOH YA 5 .   ? 6.716   0.551   34.313  1.00 22.18  ? 416 HOH B O   1 
HETATM 17167 O O   . HOH YA 5 .   ? -17.558 -6.983  37.367  1.00 17.21  ? 417 HOH B O   1 
HETATM 17168 O O   . HOH ZA 5 .   ? -8.754  26.629  37.448  1.00 9.31   ? 401 HOH C O   1 
HETATM 17169 O O   . HOH ZA 5 .   ? -14.913 26.151  43.069  1.00 17.34  ? 402 HOH C O   1 
HETATM 17170 O O   . HOH ZA 5 .   ? -13.785 24.336  45.784  1.00 22.63  ? 403 HOH C O   1 
HETATM 17171 O O   . HOH ZA 5 .   ? -3.586  26.108  53.401  1.00 20.07  ? 404 HOH C O   1 
HETATM 17172 O O   . HOH ZA 5 .   ? -12.053 14.289  46.555  1.00 6.90   ? 405 HOH C O   1 
HETATM 17173 O O   . HOH ZA 5 .   ? -14.645 21.073  57.703  1.00 29.03  ? 406 HOH C O   1 
HETATM 17174 O O   . HOH ZA 5 .   ? -15.274 0.468   23.091  1.00 24.12  ? 407 HOH C O   1 
HETATM 17175 O O   . HOH ZA 5 .   ? -11.131 22.973  47.586  1.00 21.13  ? 408 HOH C O   1 
HETATM 17176 O O   . HOH ZA 5 .   ? -10.439 13.028  42.611  1.00 7.19   ? 409 HOH C O   1 
HETATM 17177 O O   . HOH ZA 5 .   ? -28.685 16.809  39.810  1.00 22.44  ? 410 HOH C O   1 
HETATM 17178 O O   . HOH ZA 5 .   ? -21.296 30.395  30.739  1.00 9.96   ? 411 HOH C O   1 
HETATM 17179 O O   . HOH ZA 5 .   ? -18.710 24.415  64.362  1.00 26.68  ? 412 HOH C O   1 
HETATM 17180 O O   . HOH ZA 5 .   ? -4.177  28.401  31.041  1.00 5.38   ? 413 HOH C O   1 
HETATM 17181 O O   . HOH ZA 5 .   ? -15.313 28.834  50.467  1.00 13.74  ? 414 HOH C O   1 
HETATM 17182 O O   . HOH ZA 5 .   ? -17.496 26.770  48.845  1.00 18.76  ? 415 HOH C O   1 
HETATM 17183 O O   . HOH ZA 5 .   ? -36.143 18.962  56.039  1.00 17.73  ? 416 HOH C O   1 
HETATM 17184 O O   . HOH ZA 5 .   ? -10.496 26.683  27.118  1.00 17.85  ? 417 HOH C O   1 
HETATM 17185 O O   . HOH ZA 5 .   ? -11.134 24.907  30.124  1.00 11.17  ? 418 HOH C O   1 
HETATM 17186 O O   . HOH ZA 5 .   ? -4.788  13.214  26.545  1.00 19.34  ? 419 HOH C O   1 
HETATM 17187 O O   . HOH ZA 5 .   ? -5.760  20.801  29.512  1.00 25.42  ? 420 HOH C O   1 
HETATM 17188 O O   . HOH ZA 5 .   ? -6.534  27.390  22.239  1.00 38.49  ? 421 HOH C O   1 
HETATM 17189 O O   . HOH ZA 5 .   ? -4.548  26.599  22.888  1.00 26.71  ? 422 HOH C O   1 
HETATM 17190 O O   . HOH ZA 5 .   ? -35.461 31.197  53.704  1.00 28.77  ? 423 HOH C O   1 
HETATM 17191 O O   . HOH ZA 5 .   ? -2.334  19.254  26.675  1.00 16.24  ? 424 HOH C O   1 
HETATM 17192 O O   . HOH ZA 5 .   ? -15.565 14.167  17.619  1.00 16.52  ? 425 HOH C O   1 
HETATM 17193 O O   . HOH ZA 5 .   ? -14.532 11.438  18.860  1.00 25.37  ? 426 HOH C O   1 
HETATM 17194 O O   . HOH AB 5 .   ? -9.395  26.815  49.687  1.00 18.58  ? 401 HOH D O   1 
HETATM 17195 O O   . HOH AB 5 .   ? 0.486   34.745  57.942  1.00 19.67  ? 402 HOH D O   1 
HETATM 17196 O O   . HOH AB 5 .   ? 4.465   33.214  53.014  1.00 13.26  ? 403 HOH D O   1 
HETATM 17197 O O   . HOH AB 5 .   ? 5.218   31.395  44.207  1.00 8.19   ? 404 HOH D O   1 
HETATM 17198 O O   . HOH AB 5 .   ? -14.545 50.653  58.315  1.00 21.24  ? 405 HOH D O   1 
HETATM 17199 O O   . HOH AB 5 .   ? -16.511 44.862  65.562  1.00 20.54  ? 406 HOH D O   1 
HETATM 17200 O O   . HOH AB 5 .   ? -6.224  26.507  62.767  1.00 34.16  ? 407 HOH D O   1 
HETATM 17201 O O   . HOH AB 5 .   ? 7.824   32.586  45.610  1.00 12.27  ? 408 HOH D O   1 
HETATM 17202 O O   . HOH AB 5 .   ? -7.052  27.346  48.802  1.00 9.11   ? 409 HOH D O   1 
HETATM 17203 O O   . HOH AB 5 .   ? 3.412   49.977  29.273  1.00 29.70  ? 410 HOH D O   1 
HETATM 17204 O O   . HOH AB 5 .   ? -2.430  47.003  23.495  1.00 36.38  ? 411 HOH D O   1 
HETATM 17205 O O   . HOH AB 5 .   ? 9.429   40.266  68.592  1.00 41.33  ? 412 HOH D O   1 
HETATM 17206 O O   . HOH AB 5 .   ? -12.496 36.476  23.280  1.00 23.67  ? 413 HOH D O   1 
HETATM 17207 O O   . HOH AB 5 .   ? -16.889 46.420  63.906  1.00 22.19  ? 414 HOH D O   1 
HETATM 17208 O O   . HOH AB 5 .   ? 13.098  42.641  55.772  1.00 24.03  ? 415 HOH D O   1 
HETATM 17209 O O   . HOH AB 5 .   ? -20.979 39.786  59.057  1.00 18.80  ? 416 HOH D O   1 
HETATM 17210 O O   . HOH AB 5 .   ? -12.140 27.942  76.820  1.00 30.08  ? 417 HOH D O   1 
HETATM 17211 O O   . HOH AB 5 .   ? -14.770 30.850  71.946  1.00 34.69  ? 418 HOH D O   1 
HETATM 17212 O O   . HOH AB 5 .   ? 13.328  35.687  31.932  1.00 21.27  ? 419 HOH D O   1 
HETATM 17213 O O   . HOH AB 5 .   ? -11.553 29.857  78.148  1.00 25.24  ? 420 HOH D O   1 
HETATM 17214 O O   . HOH AB 5 .   ? -10.427 36.432  21.843  1.00 26.08  ? 421 HOH D O   1 
HETATM 17215 O O   . HOH AB 5 .   ? -4.191  42.290  86.888  1.00 25.19  ? 422 HOH D O   1 
HETATM 17216 O O   . HOH BB 5 .   ? 10.513  10.222  66.345  1.00 22.80  ? 401 HOH E O   1 
HETATM 17217 O O   . HOH BB 5 .   ? 26.284  36.567  39.955  1.00 18.13  ? 402 HOH E O   1 
HETATM 17218 O O   . HOH BB 5 .   ? 17.181  16.032  50.894  1.00 12.63  ? 403 HOH E O   1 
HETATM 17219 O O   . HOH BB 5 .   ? 26.473  27.077  36.635  1.00 10.50  ? 404 HOH E O   1 
HETATM 17220 O O   . HOH BB 5 .   ? 28.021  18.441  39.172  1.00 23.14  ? 405 HOH E O   1 
HETATM 17221 O O   . HOH BB 5 .   ? -3.673  23.804  68.868  1.00 28.81  ? 406 HOH E O   1 
HETATM 17222 O O   . HOH BB 5 .   ? 14.832  13.613  51.052  1.00 7.58   ? 407 HOH E O   1 
HETATM 17223 O O   . HOH BB 5 .   ? 2.292   19.883  66.556  1.00 28.93  ? 408 HOH E O   1 
HETATM 17224 O O   . HOH BB 5 .   ? 12.638  18.002  64.768  1.00 20.79  ? 409 HOH E O   1 
HETATM 17225 O O   . HOH BB 5 .   ? 4.722   28.955  55.639  1.00 20.70  ? 410 HOH E O   1 
HETATM 17226 O O   . HOH BB 5 .   ? 5.862   25.836  55.373  1.00 13.81  ? 411 HOH E O   1 
HETATM 17227 O O   . HOH BB 5 .   ? 6.760   37.810  73.473  1.00 32.41  ? 412 HOH E O   1 
HETATM 17228 O O   . HOH BB 5 .   ? 28.684  35.272  40.625  1.00 22.11  ? 413 HOH E O   1 
HETATM 17229 O O   . HOH BB 5 .   ? 15.708  18.877  50.493  1.00 17.77  ? 414 HOH E O   1 
HETATM 17230 O O   . HOH BB 5 .   ? 11.790  14.852  64.295  1.00 14.37  ? 415 HOH E O   1 
HETATM 17231 O O   . HOH BB 5 .   ? 14.021  24.755  40.216  1.00 20.15  ? 416 HOH E O   1 
HETATM 17232 O O   . HOH BB 5 .   ? 33.561  17.461  54.951  1.00 27.94  ? 417 HOH E O   1 
HETATM 17233 O O   . HOH BB 5 .   ? 6.998   30.863  64.661  1.00 20.32  ? 418 HOH E O   1 
HETATM 17234 O O   . HOH CB 5 .   ? 1.377   28.033  27.194  1.00 20.56  ? 401 HOH F O   1 
HETATM 17235 O O   . HOH CB 5 .   ? 16.853  37.291  -10.954 1.00 35.20  ? 402 HOH F O   1 
HETATM 17236 O O   . HOH CB 5 .   ? 12.140  29.637  1.722   1.00 20.11  ? 403 HOH F O   1 
HETATM 17237 O O   . HOH CB 5 .   ? -5.153  23.163  18.427  1.00 18.98  ? 404 HOH F O   1 
HETATM 17238 O O   . HOH CB 5 .   ? 8.952   31.419  1.733   1.00 18.46  ? 405 HOH F O   1 
HETATM 17239 O O   . HOH CB 5 .   ? -5.660  32.599  16.986  1.00 16.45  ? 406 HOH F O   1 
HETATM 17240 O O   . HOH CB 5 .   ? -0.167  25.856  6.794   1.00 16.69  ? 407 HOH F O   1 
HETATM 17241 O O   . HOH CB 5 .   ? 8.996   19.694  -6.799  1.00 27.34  ? 408 HOH F O   1 
HETATM 17242 O O   . HOH CB 5 .   ? 8.197   21.571  -5.694  1.00 34.76  ? 409 HOH F O   1 
HETATM 17243 O O   . HOH DB 5 .   ? -15.022 19.696  13.046  1.00 13.60  ? 401 HOH G O   1 
HETATM 17244 O O   . HOH DB 5 .   ? 17.172  9.738   -21.317 1.00 32.24  ? 402 HOH G O   1 
HETATM 17245 O O   . HOH DB 5 .   ? -6.744  10.737  25.444  1.00 13.57  ? 403 HOH G O   1 
HETATM 17246 O O   . HOH DB 5 .   ? -6.593  4.354   14.337  1.00 15.87  ? 404 HOH G O   1 
HETATM 17247 O O   . HOH DB 5 .   ? 5.695   -16.556 0.998   1.00 41.93  ? 405 HOH G O   1 
HETATM 17248 O O   . HOH DB 5 .   ? 26.473  7.173   -22.473 1.00 17.07  ? 406 HOH G O   1 
HETATM 17249 O O   . HOH DB 5 .   ? 12.042  13.954  0.221   1.00 25.76  ? 407 HOH G O   1 
HETATM 17250 O O   . HOH DB 5 .   ? 19.460  -7.874  -31.257 1.00 37.01  ? 408 HOH G O   1 
HETATM 17251 O O   . HOH DB 5 .   ? 24.465  6.032   -23.142 1.00 22.60  ? 409 HOH G O   1 
HETATM 17252 O O   . HOH EB 5 .   ? 17.133  -8.048  26.442  1.00 14.94  ? 401 HOH H O   1 
HETATM 17253 O O   . HOH EB 5 .   ? 11.152  -12.413 26.632  1.00 13.02  ? 402 HOH H O   1 
HETATM 17254 O O   . HOH EB 5 .   ? 17.284  2.123   32.436  1.00 23.79  ? 403 HOH H O   1 
HETATM 17255 O O   . HOH EB 5 .   ? 20.533  4.039   5.544   1.00 21.60  ? 404 HOH H O   1 
HETATM 17256 O O   . HOH EB 5 .   ? 8.891   -1.603  22.688  1.00 17.19  ? 405 HOH H O   1 
HETATM 17257 O O   . HOH EB 5 .   ? 24.610  -9.496  -4.800  1.00 27.89  ? 406 HOH H O   1 
HETATM 17258 O O   . HOH EB 5 .   ? 25.516  5.303   27.012  1.00 14.99  ? 407 HOH H O   1 
HETATM 17259 O O   . HOH EB 5 .   ? 18.422  2.234   3.323   1.00 30.76  ? 408 HOH H O   1 
HETATM 17260 O O   . HOH EB 5 .   ? 8.557   -1.581  33.745  1.00 15.04  ? 409 HOH H O   1 
HETATM 17261 O O   . HOH EB 5 .   ? 38.625  11.884  -6.090  1.00 30.52  ? 410 HOH H O   1 
HETATM 17262 O O   . HOH EB 5 .   ? 0.781   -10.768 21.097  1.00 32.62  ? 411 HOH H O   1 
HETATM 17263 O O   . HOH EB 5 .   ? 19.736  3.994   13.530  1.00 17.54  ? 412 HOH H O   1 
HETATM 17264 O O   . HOH EB 5 .   ? 47.087  2.886   1.283   1.00 21.38  ? 413 HOH H O   1 
HETATM 17265 O O   . HOH EB 5 .   ? 48.000  1.340   3.999   1.00 38.39  ? 414 HOH H O   1 
HETATM 17266 O O   . HOH FB 5 .   ? 35.962  7.527   39.034  1.00 23.17  ? 401 HOH I O   1 
HETATM 17267 O O   . HOH FB 5 .   ? 34.530  15.684  36.674  1.00 21.86  ? 402 HOH I O   1 
HETATM 17268 O O   . HOH FB 5 .   ? 31.387  23.278  21.114  1.00 17.58  ? 403 HOH I O   1 
HETATM 17269 O O   . HOH FB 5 .   ? 38.409  24.195  7.857   1.00 16.49  ? 404 HOH I O   1 
HETATM 17270 O O   . HOH FB 5 .   ? 44.626  24.254  27.302  1.00 22.50  ? 405 HOH I O   1 
HETATM 17271 O O   . HOH FB 5 .   ? 34.709  13.682  35.554  1.00 20.74  ? 406 HOH I O   1 
HETATM 17272 O O   . HOH FB 5 .   ? 44.356  10.058  38.851  1.00 25.95  ? 407 HOH I O   1 
HETATM 17273 O O   . HOH FB 5 .   ? 25.781  9.520   30.443  1.00 20.36  ? 408 HOH I O   1 
HETATM 17274 O O   . HOH FB 5 .   ? 33.432  25.720  19.747  1.00 22.73  ? 409 HOH I O   1 
HETATM 17275 O O   . HOH FB 5 .   ? 28.503  21.537  36.303  1.00 31.64  ? 410 HOH I O   1 
HETATM 17276 O O   . HOH FB 5 .   ? 28.888  24.066  36.704  1.00 37.06  ? 411 HOH I O   1 
HETATM 17277 O O   . HOH GB 5 .   ? 28.228  37.682  34.475  1.00 24.33  ? 401 HOH J O   1 
HETATM 17278 O O   . HOH GB 5 .   ? 42.620  34.206  1.333   1.00 26.02  ? 402 HOH J O   1 
HETATM 17279 O O   . HOH GB 5 .   ? 37.010  27.454  -17.683 1.00 11.23  ? 403 HOH J O   1 
HETATM 17280 O O   . HOH GB 5 .   ? 22.402  38.843  28.413  1.00 15.63  ? 404 HOH J O   1 
HETATM 17281 O O   . HOH GB 5 .   ? 24.353  38.160  29.902  1.00 20.49  ? 405 HOH J O   1 
HETATM 17282 O O   . HOH GB 5 .   ? 27.215  40.313  34.319  1.00 24.35  ? 406 HOH J O   1 
HETATM 17283 O O   . HOH GB 5 .   ? 45.789  37.852  0.329   1.00 25.92  ? 407 HOH J O   1 
HETATM 17284 O O   . HOH GB 5 .   ? 29.864  24.839  9.446   1.00 16.26  ? 408 HOH J O   1 
HETATM 17285 O O   . HOH GB 5 .   ? 17.100  31.436  37.936  1.00 15.79  ? 409 HOH J O   1 
HETATM 17286 O O   . HOH GB 5 .   ? 21.259  32.527  -0.906  1.00 23.00  ? 410 HOH J O   1 
HETATM 17287 O O   . HOH GB 5 .   ? 28.293  24.566  7.867   1.00 19.50  ? 411 HOH J O   1 
HETATM 17288 O O   . HOH GB 5 .   ? 34.383  27.453  -19.011 1.00 21.72  ? 412 HOH J O   1 
HETATM 17289 O O   . HOH GB 5 .   ? 14.533  37.683  30.363  1.00 16.30  ? 413 HOH J O   1 
HETATM 17290 O O   . HOH GB 5 .   ? 30.201  31.162  10.881  1.00 19.69  ? 414 HOH J O   1 
HETATM 17291 O O   . HOH GB 5 .   ? 25.133  28.133  30.300  1.00 14.92  ? 415 HOH J O   1 
HETATM 17292 O O   . HOH GB 5 .   ? 22.966  27.808  28.635  1.00 14.42  ? 416 HOH J O   1 
HETATM 17293 O O   . HOH GB 5 .   ? 25.112  46.924  13.720  1.00 23.98  ? 417 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   ASP 1   -7  -7  ASP ASP A . n 
A 1 2   TYR 2   -6  -6  TYR TYR A . n 
A 1 3   LYS 3   -5  -5  LYS LYS A . n 
A 1 4   ASP 4   -4  -4  ASP ASP A . n 
A 1 5   ASP 5   -3  -3  ASP ASP A . n 
A 1 6   ASP 6   -2  -2  ASP ASP A . n 
A 1 7   ASP 7   -1  -1  ASP ASP A . n 
A 1 8   LYS 8   0   0   LYS LYS A . n 
A 1 9   LEU 9   1   1   LEU LEU A . n 
A 1 10  ASP 10  2   2   ASP ASP A . n 
A 1 11  ARG 11  3   3   ARG ARG A . n 
A 1 12  ALA 12  4   4   ALA ALA A . n 
A 1 13  ASP 13  5   5   ASP ASP A . n 
A 1 14  ILE 14  6   6   ILE ILE A . n 
A 1 15  LEU 15  7   7   LEU LEU A . n 
A 1 16  TYR 16  8   8   TYR TYR A . n 
A 1 17  ASN 17  9   9   ASN ASN A . n 
A 1 18  ILE 18  10  10  ILE ILE A . n 
A 1 19  ARG 19  11  11  ARG ARG A . n 
A 1 20  GLN 20  12  12  GLN GLN A . n 
A 1 21  THR 21  13  13  THR THR A . n 
A 1 22  SER 22  14  14  SER SER A . n 
A 1 23  ARG 23  15  15  ARG ARG A . n 
A 1 24  PRO 24  16  16  PRO PRO A . n 
A 1 25  ASP 25  17  17  ASP ASP A . n 
A 1 26  VAL 26  18  18  VAL VAL A . n 
A 1 27  ILE 27  19  19  ILE ILE A . n 
A 1 28  PRO 28  20  20  PRO PRO A . n 
A 1 29  THR 29  21  21  THR THR A . n 
A 1 30  GLN 30  22  22  GLN GLN A . n 
A 1 31  ARG 31  23  23  ARG ARG A . n 
A 1 32  ASP 32  24  24  ASP ASP A . n 
A 1 33  ARG 33  25  25  ARG ARG A . n 
A 1 34  PRO 34  26  26  PRO PRO A . n 
A 1 35  VAL 35  27  27  VAL VAL A . n 
A 1 36  ALA 36  28  28  ALA ALA A . n 
A 1 37  VAL 37  29  29  VAL VAL A . n 
A 1 38  SER 38  30  30  SER SER A . n 
A 1 39  VAL 39  31  31  VAL VAL A . n 
A 1 40  SER 40  32  32  SER SER A . n 
A 1 41  LEU 41  33  33  LEU LEU A . n 
A 1 42  LYS 42  34  34  LYS LYS A . n 
A 1 43  PHE 43  35  35  PHE PHE A . n 
A 1 44  ILE 44  36  36  ILE ILE A . n 
A 1 45  ASN 45  37  37  ASN ASN A . n 
A 1 46  ILE 46  38  38  ILE ILE A . n 
A 1 47  LEU 47  39  39  LEU LEU A . n 
A 1 48  GLU 48  40  40  GLU GLU A . n 
A 1 49  VAL 49  41  41  VAL VAL A . n 
A 1 50  ASN 50  42  42  ASN ASN A . n 
A 1 51  GLU 51  43  43  GLU GLU A . n 
A 1 52  ILE 52  44  44  ILE ILE A . n 
A 1 53  THR 53  45  45  THR THR A . n 
A 1 54  ASN 54  46  46  ASN ASN A . n 
A 1 55  GLU 55  47  47  GLU GLU A . n 
A 1 56  VAL 56  48  48  VAL VAL A . n 
A 1 57  ASP 57  49  49  ASP ASP A . n 
A 1 58  VAL 58  50  50  VAL VAL A . n 
A 1 59  VAL 59  51  51  VAL VAL A . n 
A 1 60  PHE 60  52  52  PHE PHE A . n 
A 1 61  TRP 61  53  53  TRP TRP A . n 
A 1 62  GLN 62  54  54  GLN GLN A . n 
A 1 63  GLN 63  55  55  GLN GLN A . n 
A 1 64  THR 64  56  56  THR THR A . n 
A 1 65  THR 65  57  57  THR THR A . n 
A 1 66  TRP 66  58  58  TRP TRP A . n 
A 1 67  SER 67  59  59  SER SER A . n 
A 1 68  ASP 68  60  60  ASP ASP A . n 
A 1 69  ARG 69  61  61  ARG ARG A . n 
A 1 70  THR 70  62  62  THR THR A . n 
A 1 71  LEU 71  63  63  LEU LEU A . n 
A 1 72  ALA 72  64  64  ALA ALA A . n 
A 1 73  TRP 73  65  65  TRP TRP A . n 
A 1 74  ASN 74  66  66  ASN ASN A . n 
A 1 75  SER 75  67  67  SER SER A . n 
A 1 76  SER 76  68  68  SER SER A . n 
A 1 77  HIS 77  69  69  HIS HIS A . n 
A 1 78  SER 78  70  70  SER SER A . n 
A 1 79  PRO 79  71  71  PRO PRO A . n 
A 1 80  ASP 80  72  72  ASP ASP A . n 
A 1 81  GLN 81  73  73  GLN GLN A . n 
A 1 82  VAL 82  74  74  VAL VAL A . n 
A 1 83  SER 83  75  75  SER SER A . n 
A 1 84  VAL 84  76  76  VAL VAL A . n 
A 1 85  PRO 85  77  77  PRO PRO A . n 
A 1 86  ILE 86  78  78  ILE ILE A . n 
A 1 87  SER 87  79  79  SER SER A . n 
A 1 88  SER 88  80  80  SER SER A . n 
A 1 89  LEU 89  81  81  LEU LEU A . n 
A 1 90  TRP 90  82  82  TRP TRP A . n 
A 1 91  VAL 91  83  83  VAL VAL A . n 
A 1 92  PRO 92  84  84  PRO PRO A . n 
A 1 93  ASP 93  85  85  ASP ASP A . n 
A 1 94  LEU 94  86  86  LEU LEU A . n 
A 1 95  ALA 95  87  87  ALA ALA A . n 
A 1 96  ALA 96  88  88  ALA ALA A . n 
A 1 97  TYR 97  89  89  TYR TYR A . n 
A 1 98  ASN 98  90  90  ASN ASN A . n 
A 1 99  ALA 99  91  91  ALA ALA A . n 
A 1 100 ILE 100 92  92  ILE ILE A . n 
A 1 101 SER 101 93  93  SER SER A . n 
A 1 102 LYS 102 94  94  LYS LYS A . n 
A 1 103 PRO 103 95  95  PRO PRO A . n 
A 1 104 GLU 104 96  96  GLU GLU A . n 
A 1 105 VAL 105 97  97  VAL VAL A . n 
A 1 106 LEU 106 98  98  LEU LEU A . n 
A 1 107 THR 107 99  99  THR THR A . n 
A 1 108 PRO 108 100 100 PRO PRO A . n 
A 1 109 GLN 109 101 101 GLN GLN A . n 
A 1 110 LEU 110 102 102 LEU LEU A . n 
A 1 111 ALA 111 103 103 ALA ALA A . n 
A 1 112 ARG 112 104 104 ARG ARG A . n 
A 1 113 VAL 113 105 105 VAL VAL A . n 
A 1 114 VAL 114 106 106 VAL VAL A . n 
A 1 115 SER 115 107 107 SER SER A . n 
A 1 116 ASP 116 108 108 ASP ASP A . n 
A 1 117 GLY 117 109 109 GLY GLY A . n 
A 1 118 GLU 118 110 110 GLU GLU A . n 
A 1 119 VAL 119 111 111 VAL VAL A . n 
A 1 120 LEU 120 112 112 LEU LEU A . n 
A 1 121 TYR 121 113 113 TYR TYR A . n 
A 1 122 MET 122 114 114 MET MET A . n 
A 1 123 PRO 123 115 115 PRO PRO A . n 
A 1 124 SER 124 116 116 SER SER A . n 
A 1 125 ILE 125 117 117 ILE ILE A . n 
A 1 126 ARG 126 118 118 ARG ARG A . n 
A 1 127 GLN 127 119 119 GLN GLN A . n 
A 1 128 ARG 128 120 120 ARG ARG A . n 
A 1 129 PHE 129 121 121 PHE PHE A . n 
A 1 130 SER 130 122 122 SER SER A . n 
A 1 131 CYS 131 123 123 CYS CYS A . n 
A 1 132 ASP 132 124 124 ASP ASP A . n 
A 1 133 VAL 133 125 125 VAL VAL A . n 
A 1 134 SER 134 126 126 SER SER A . n 
A 1 135 GLY 135 127 127 GLY GLY A . n 
A 1 136 VAL 136 128 128 VAL VAL A . n 
A 1 137 ASP 137 129 129 ASP ASP A . n 
A 1 138 THR 138 130 130 THR THR A . n 
A 1 139 GLU 139 131 131 GLU GLU A . n 
A 1 140 SER 140 132 132 SER SER A . n 
A 1 141 GLY 141 133 133 GLY GLY A . n 
A 1 142 ALA 142 134 134 ALA ALA A . n 
A 1 143 THR 143 135 135 THR THR A . n 
A 1 144 CYS 144 136 136 CYS CYS A . n 
A 1 145 ARG 145 137 137 ARG ARG A . n 
A 1 146 ILE 146 138 138 ILE ILE A . n 
A 1 147 LYS 147 139 139 LYS LYS A . n 
A 1 148 ILE 148 140 140 ILE ILE A . n 
A 1 149 GLY 149 141 141 GLY GLY A . n 
A 1 150 SER 150 142 142 SER SER A . n 
A 1 151 TRP 151 143 143 TRP TRP A . n 
A 1 152 THR 152 144 144 THR THR A . n 
A 1 153 HIS 153 145 145 HIS HIS A . n 
A 1 154 HIS 154 146 146 HIS HIS A . n 
A 1 155 SER 155 147 147 SER SER A . n 
A 1 156 ARG 156 148 148 ARG ARG A . n 
A 1 157 GLU 157 149 149 GLU GLU A . n 
A 1 158 ILE 158 150 150 ILE ILE A . n 
A 1 159 SER 159 151 151 SER SER A . n 
A 1 160 VAL 160 152 152 VAL VAL A . n 
A 1 161 ASP 161 153 153 ASP ASP A . n 
A 1 162 PRO 162 154 154 PRO PRO A . n 
A 1 163 THR 163 155 155 THR THR A . n 
A 1 164 THR 164 156 156 THR THR A . n 
A 1 165 GLU 165 157 157 GLU GLU A . n 
A 1 166 ASN 166 158 158 ASN ASN A . n 
A 1 167 SER 167 159 159 SER SER A . n 
A 1 168 ASP 168 160 160 ASP ASP A . n 
A 1 169 ASP 169 161 161 ASP ASP A . n 
A 1 170 SER 170 162 162 SER SER A . n 
A 1 171 GLU 171 163 163 GLU GLU A . n 
A 1 172 TYR 172 164 164 TYR TYR A . n 
A 1 173 PHE 173 165 165 PHE PHE A . n 
A 1 174 SER 174 166 166 SER SER A . n 
A 1 175 GLN 175 167 167 GLN GLN A . n 
A 1 176 TYR 176 168 168 TYR TYR A . n 
A 1 177 SER 177 169 169 SER SER A . n 
A 1 178 ARG 178 170 170 ARG ARG A . n 
A 1 179 PHE 179 171 171 PHE PHE A . n 
A 1 180 GLU 180 172 172 GLU GLU A . n 
A 1 181 ILE 181 173 173 ILE ILE A . n 
A 1 182 LEU 182 174 174 LEU LEU A . n 
A 1 183 ASP 183 175 175 ASP ASP A . n 
A 1 184 VAL 184 176 176 VAL VAL A . n 
A 1 185 THR 185 177 177 THR THR A . n 
A 1 186 GLN 186 178 178 GLN GLN A . n 
A 1 187 LYS 187 179 179 LYS LYS A . n 
A 1 188 LYS 188 180 180 LYS LYS A . n 
A 1 189 ASN 189 181 181 ASN ASN A . n 
A 1 190 SER 190 182 182 SER SER A . n 
A 1 191 VAL 191 183 183 VAL VAL A . n 
A 1 192 THR 192 184 ?   ?   ?   A . n 
A 1 193 TYR 193 185 ?   ?   ?   A . n 
A 1 194 SER 194 186 ?   ?   ?   A . n 
A 1 195 CYS 195 187 ?   ?   ?   A . n 
A 1 196 CYS 196 188 ?   ?   ?   A . n 
A 1 197 PRO 197 189 ?   ?   ?   A . n 
A 1 198 GLU 198 190 190 GLU GLU A . n 
A 1 199 ALA 199 191 191 ALA ALA A . n 
A 1 200 TYR 200 192 192 TYR TYR A . n 
A 1 201 GLU 201 193 193 GLU GLU A . n 
A 1 202 ASP 202 194 194 ASP ASP A . n 
A 1 203 VAL 203 195 195 VAL VAL A . n 
A 1 204 GLU 204 196 196 GLU GLU A . n 
A 1 205 VAL 205 197 197 VAL VAL A . n 
A 1 206 SER 206 198 198 SER SER A . n 
A 1 207 LEU 207 199 199 LEU LEU A . n 
A 1 208 ASN 208 200 200 ASN ASN A . n 
A 1 209 PHE 209 201 201 PHE PHE A . n 
A 1 210 ARG 210 202 202 ARG ARG A . n 
A 1 211 LYS 211 203 203 LYS LYS A . n 
A 1 212 LYS 212 204 204 LYS LYS A . n 
A 1 213 GLY 213 205 205 GLY GLY A . n 
A 1 214 ARG 214 206 ?   ?   ?   A . n 
A 1 215 SER 215 207 ?   ?   ?   A . n 
A 1 216 GLU 216 208 ?   ?   ?   A . n 
A 1 217 ILE 217 209 ?   ?   ?   A . n 
B 1 1   ASP 1   -7  ?   ?   ?   B . n 
B 1 2   TYR 2   -6  ?   ?   ?   B . n 
B 1 3   LYS 3   -5  -5  LYS LYS B . n 
B 1 4   ASP 4   -4  -4  ASP ASP B . n 
B 1 5   ASP 5   -3  -3  ASP ASP B . n 
B 1 6   ASP 6   -2  -2  ASP ASP B . n 
B 1 7   ASP 7   -1  -1  ASP ASP B . n 
B 1 8   LYS 8   0   0   LYS LYS B . n 
B 1 9   LEU 9   1   1   LEU LEU B . n 
B 1 10  ASP 10  2   2   ASP ASP B . n 
B 1 11  ARG 11  3   3   ARG ARG B . n 
B 1 12  ALA 12  4   4   ALA ALA B . n 
B 1 13  ASP 13  5   5   ASP ASP B . n 
B 1 14  ILE 14  6   6   ILE ILE B . n 
B 1 15  LEU 15  7   7   LEU LEU B . n 
B 1 16  TYR 16  8   8   TYR TYR B . n 
B 1 17  ASN 17  9   9   ASN ASN B . n 
B 1 18  ILE 18  10  10  ILE ILE B . n 
B 1 19  ARG 19  11  11  ARG ARG B . n 
B 1 20  GLN 20  12  12  GLN GLN B . n 
B 1 21  THR 21  13  13  THR THR B . n 
B 1 22  SER 22  14  14  SER SER B . n 
B 1 23  ARG 23  15  15  ARG ARG B . n 
B 1 24  PRO 24  16  16  PRO PRO B . n 
B 1 25  ASP 25  17  17  ASP ASP B . n 
B 1 26  VAL 26  18  18  VAL VAL B . n 
B 1 27  ILE 27  19  19  ILE ILE B . n 
B 1 28  PRO 28  20  20  PRO PRO B . n 
B 1 29  THR 29  21  21  THR THR B . n 
B 1 30  GLN 30  22  22  GLN GLN B . n 
B 1 31  ARG 31  23  23  ARG ARG B . n 
B 1 32  ASP 32  24  24  ASP ASP B . n 
B 1 33  ARG 33  25  25  ARG ARG B . n 
B 1 34  PRO 34  26  26  PRO PRO B . n 
B 1 35  VAL 35  27  27  VAL VAL B . n 
B 1 36  ALA 36  28  28  ALA ALA B . n 
B 1 37  VAL 37  29  29  VAL VAL B . n 
B 1 38  SER 38  30  30  SER SER B . n 
B 1 39  VAL 39  31  31  VAL VAL B . n 
B 1 40  SER 40  32  32  SER SER B . n 
B 1 41  LEU 41  33  33  LEU LEU B . n 
B 1 42  LYS 42  34  34  LYS LYS B . n 
B 1 43  PHE 43  35  35  PHE PHE B . n 
B 1 44  ILE 44  36  36  ILE ILE B . n 
B 1 45  ASN 45  37  37  ASN ASN B . n 
B 1 46  ILE 46  38  38  ILE ILE B . n 
B 1 47  LEU 47  39  39  LEU LEU B . n 
B 1 48  GLU 48  40  40  GLU GLU B . n 
B 1 49  VAL 49  41  41  VAL VAL B . n 
B 1 50  ASN 50  42  42  ASN ASN B . n 
B 1 51  GLU 51  43  43  GLU GLU B . n 
B 1 52  ILE 52  44  44  ILE ILE B . n 
B 1 53  THR 53  45  45  THR THR B . n 
B 1 54  ASN 54  46  46  ASN ASN B . n 
B 1 55  GLU 55  47  47  GLU GLU B . n 
B 1 56  VAL 56  48  48  VAL VAL B . n 
B 1 57  ASP 57  49  49  ASP ASP B . n 
B 1 58  VAL 58  50  50  VAL VAL B . n 
B 1 59  VAL 59  51  51  VAL VAL B . n 
B 1 60  PHE 60  52  52  PHE PHE B . n 
B 1 61  TRP 61  53  53  TRP TRP B . n 
B 1 62  GLN 62  54  54  GLN GLN B . n 
B 1 63  GLN 63  55  55  GLN GLN B . n 
B 1 64  THR 64  56  56  THR THR B . n 
B 1 65  THR 65  57  57  THR THR B . n 
B 1 66  TRP 66  58  58  TRP TRP B . n 
B 1 67  SER 67  59  59  SER SER B . n 
B 1 68  ASP 68  60  60  ASP ASP B . n 
B 1 69  ARG 69  61  61  ARG ARG B . n 
B 1 70  THR 70  62  62  THR THR B . n 
B 1 71  LEU 71  63  63  LEU LEU B . n 
B 1 72  ALA 72  64  64  ALA ALA B . n 
B 1 73  TRP 73  65  65  TRP TRP B . n 
B 1 74  ASN 74  66  66  ASN ASN B . n 
B 1 75  SER 75  67  67  SER SER B . n 
B 1 76  SER 76  68  68  SER SER B . n 
B 1 77  HIS 77  69  69  HIS HIS B . n 
B 1 78  SER 78  70  70  SER SER B . n 
B 1 79  PRO 79  71  71  PRO PRO B . n 
B 1 80  ASP 80  72  72  ASP ASP B . n 
B 1 81  GLN 81  73  73  GLN GLN B . n 
B 1 82  VAL 82  74  74  VAL VAL B . n 
B 1 83  SER 83  75  75  SER SER B . n 
B 1 84  VAL 84  76  76  VAL VAL B . n 
B 1 85  PRO 85  77  77  PRO PRO B . n 
B 1 86  ILE 86  78  78  ILE ILE B . n 
B 1 87  SER 87  79  79  SER SER B . n 
B 1 88  SER 88  80  80  SER SER B . n 
B 1 89  LEU 89  81  81  LEU LEU B . n 
B 1 90  TRP 90  82  82  TRP TRP B . n 
B 1 91  VAL 91  83  83  VAL VAL B . n 
B 1 92  PRO 92  84  84  PRO PRO B . n 
B 1 93  ASP 93  85  85  ASP ASP B . n 
B 1 94  LEU 94  86  86  LEU LEU B . n 
B 1 95  ALA 95  87  87  ALA ALA B . n 
B 1 96  ALA 96  88  88  ALA ALA B . n 
B 1 97  TYR 97  89  89  TYR TYR B . n 
B 1 98  ASN 98  90  90  ASN ASN B . n 
B 1 99  ALA 99  91  91  ALA ALA B . n 
B 1 100 ILE 100 92  92  ILE ILE B . n 
B 1 101 SER 101 93  93  SER SER B . n 
B 1 102 LYS 102 94  94  LYS LYS B . n 
B 1 103 PRO 103 95  95  PRO PRO B . n 
B 1 104 GLU 104 96  96  GLU GLU B . n 
B 1 105 VAL 105 97  97  VAL VAL B . n 
B 1 106 LEU 106 98  98  LEU LEU B . n 
B 1 107 THR 107 99  99  THR THR B . n 
B 1 108 PRO 108 100 100 PRO PRO B . n 
B 1 109 GLN 109 101 101 GLN GLN B . n 
B 1 110 LEU 110 102 102 LEU LEU B . n 
B 1 111 ALA 111 103 103 ALA ALA B . n 
B 1 112 ARG 112 104 104 ARG ARG B . n 
B 1 113 VAL 113 105 105 VAL VAL B . n 
B 1 114 VAL 114 106 106 VAL VAL B . n 
B 1 115 SER 115 107 107 SER SER B . n 
B 1 116 ASP 116 108 108 ASP ASP B . n 
B 1 117 GLY 117 109 109 GLY GLY B . n 
B 1 118 GLU 118 110 110 GLU GLU B . n 
B 1 119 VAL 119 111 111 VAL VAL B . n 
B 1 120 LEU 120 112 112 LEU LEU B . n 
B 1 121 TYR 121 113 113 TYR TYR B . n 
B 1 122 MET 122 114 114 MET MET B . n 
B 1 123 PRO 123 115 115 PRO PRO B . n 
B 1 124 SER 124 116 116 SER SER B . n 
B 1 125 ILE 125 117 117 ILE ILE B . n 
B 1 126 ARG 126 118 118 ARG ARG B . n 
B 1 127 GLN 127 119 119 GLN GLN B . n 
B 1 128 ARG 128 120 120 ARG ARG B . n 
B 1 129 PHE 129 121 121 PHE PHE B . n 
B 1 130 SER 130 122 122 SER SER B . n 
B 1 131 CYS 131 123 123 CYS CYS B . n 
B 1 132 ASP 132 124 124 ASP ASP B . n 
B 1 133 VAL 133 125 125 VAL VAL B . n 
B 1 134 SER 134 126 126 SER SER B . n 
B 1 135 GLY 135 127 127 GLY GLY B . n 
B 1 136 VAL 136 128 128 VAL VAL B . n 
B 1 137 ASP 137 129 129 ASP ASP B . n 
B 1 138 THR 138 130 130 THR THR B . n 
B 1 139 GLU 139 131 131 GLU GLU B . n 
B 1 140 SER 140 132 132 SER SER B . n 
B 1 141 GLY 141 133 133 GLY GLY B . n 
B 1 142 ALA 142 134 134 ALA ALA B . n 
B 1 143 THR 143 135 135 THR THR B . n 
B 1 144 CYS 144 136 136 CYS CYS B . n 
B 1 145 ARG 145 137 137 ARG ARG B . n 
B 1 146 ILE 146 138 138 ILE ILE B . n 
B 1 147 LYS 147 139 139 LYS LYS B . n 
B 1 148 ILE 148 140 140 ILE ILE B . n 
B 1 149 GLY 149 141 141 GLY GLY B . n 
B 1 150 SER 150 142 142 SER SER B . n 
B 1 151 TRP 151 143 143 TRP TRP B . n 
B 1 152 THR 152 144 144 THR THR B . n 
B 1 153 HIS 153 145 145 HIS HIS B . n 
B 1 154 HIS 154 146 146 HIS HIS B . n 
B 1 155 SER 155 147 147 SER SER B . n 
B 1 156 ARG 156 148 148 ARG ARG B . n 
B 1 157 GLU 157 149 149 GLU GLU B . n 
B 1 158 ILE 158 150 150 ILE ILE B . n 
B 1 159 SER 159 151 151 SER SER B . n 
B 1 160 VAL 160 152 152 VAL VAL B . n 
B 1 161 ASP 161 153 153 ASP ASP B . n 
B 1 162 PRO 162 154 154 PRO PRO B . n 
B 1 163 THR 163 155 155 THR THR B . n 
B 1 164 THR 164 156 156 THR THR B . n 
B 1 165 GLU 165 157 157 GLU GLU B . n 
B 1 166 ASN 166 158 158 ASN ASN B . n 
B 1 167 SER 167 159 159 SER SER B . n 
B 1 168 ASP 168 160 160 ASP ASP B . n 
B 1 169 ASP 169 161 161 ASP ASP B . n 
B 1 170 SER 170 162 162 SER SER B . n 
B 1 171 GLU 171 163 163 GLU GLU B . n 
B 1 172 TYR 172 164 164 TYR TYR B . n 
B 1 173 PHE 173 165 165 PHE PHE B . n 
B 1 174 SER 174 166 166 SER SER B . n 
B 1 175 GLN 175 167 167 GLN GLN B . n 
B 1 176 TYR 176 168 168 TYR TYR B . n 
B 1 177 SER 177 169 169 SER SER B . n 
B 1 178 ARG 178 170 170 ARG ARG B . n 
B 1 179 PHE 179 171 171 PHE PHE B . n 
B 1 180 GLU 180 172 172 GLU GLU B . n 
B 1 181 ILE 181 173 173 ILE ILE B . n 
B 1 182 LEU 182 174 174 LEU LEU B . n 
B 1 183 ASP 183 175 175 ASP ASP B . n 
B 1 184 VAL 184 176 176 VAL VAL B . n 
B 1 185 THR 185 177 177 THR THR B . n 
B 1 186 GLN 186 178 178 GLN GLN B . n 
B 1 187 LYS 187 179 179 LYS LYS B . n 
B 1 188 LYS 188 180 180 LYS LYS B . n 
B 1 189 ASN 189 181 181 ASN ASN B . n 
B 1 190 SER 190 182 182 SER SER B . n 
B 1 191 VAL 191 183 183 VAL VAL B . n 
B 1 192 THR 192 184 184 THR THR B . n 
B 1 193 TYR 193 185 ?   ?   ?   B . n 
B 1 194 SER 194 186 ?   ?   ?   B . n 
B 1 195 CYS 195 187 ?   ?   ?   B . n 
B 1 196 CYS 196 188 ?   ?   ?   B . n 
B 1 197 PRO 197 189 189 PRO PRO B . n 
B 1 198 GLU 198 190 190 GLU GLU B . n 
B 1 199 ALA 199 191 191 ALA ALA B . n 
B 1 200 TYR 200 192 192 TYR TYR B . n 
B 1 201 GLU 201 193 193 GLU GLU B . n 
B 1 202 ASP 202 194 194 ASP ASP B . n 
B 1 203 VAL 203 195 195 VAL VAL B . n 
B 1 204 GLU 204 196 196 GLU GLU B . n 
B 1 205 VAL 205 197 197 VAL VAL B . n 
B 1 206 SER 206 198 198 SER SER B . n 
B 1 207 LEU 207 199 199 LEU LEU B . n 
B 1 208 ASN 208 200 200 ASN ASN B . n 
B 1 209 PHE 209 201 201 PHE PHE B . n 
B 1 210 ARG 210 202 202 ARG ARG B . n 
B 1 211 LYS 211 203 203 LYS LYS B . n 
B 1 212 LYS 212 204 204 LYS LYS B . n 
B 1 213 GLY 213 205 205 GLY GLY B . n 
B 1 214 ARG 214 206 ?   ?   ?   B . n 
B 1 215 SER 215 207 ?   ?   ?   B . n 
B 1 216 GLU 216 208 ?   ?   ?   B . n 
B 1 217 ILE 217 209 ?   ?   ?   B . n 
C 1 1   ASP 1   -7  -7  ASP ASP C . n 
C 1 2   TYR 2   -6  -6  TYR TYR C . n 
C 1 3   LYS 3   -5  -5  LYS LYS C . n 
C 1 4   ASP 4   -4  -4  ASP ASP C . n 
C 1 5   ASP 5   -3  -3  ASP ASP C . n 
C 1 6   ASP 6   -2  -2  ASP ASP C . n 
C 1 7   ASP 7   -1  -1  ASP ASP C . n 
C 1 8   LYS 8   0   0   LYS LYS C . n 
C 1 9   LEU 9   1   1   LEU LEU C . n 
C 1 10  ASP 10  2   2   ASP ASP C . n 
C 1 11  ARG 11  3   3   ARG ARG C . n 
C 1 12  ALA 12  4   4   ALA ALA C . n 
C 1 13  ASP 13  5   5   ASP ASP C . n 
C 1 14  ILE 14  6   6   ILE ILE C . n 
C 1 15  LEU 15  7   7   LEU LEU C . n 
C 1 16  TYR 16  8   8   TYR TYR C . n 
C 1 17  ASN 17  9   9   ASN ASN C . n 
C 1 18  ILE 18  10  10  ILE ILE C . n 
C 1 19  ARG 19  11  11  ARG ARG C . n 
C 1 20  GLN 20  12  12  GLN GLN C . n 
C 1 21  THR 21  13  13  THR THR C . n 
C 1 22  SER 22  14  14  SER SER C . n 
C 1 23  ARG 23  15  15  ARG ARG C . n 
C 1 24  PRO 24  16  16  PRO PRO C . n 
C 1 25  ASP 25  17  17  ASP ASP C . n 
C 1 26  VAL 26  18  18  VAL VAL C . n 
C 1 27  ILE 27  19  19  ILE ILE C . n 
C 1 28  PRO 28  20  20  PRO PRO C . n 
C 1 29  THR 29  21  21  THR THR C . n 
C 1 30  GLN 30  22  22  GLN GLN C . n 
C 1 31  ARG 31  23  23  ARG ARG C . n 
C 1 32  ASP 32  24  24  ASP ASP C . n 
C 1 33  ARG 33  25  25  ARG ARG C . n 
C 1 34  PRO 34  26  26  PRO PRO C . n 
C 1 35  VAL 35  27  27  VAL VAL C . n 
C 1 36  ALA 36  28  28  ALA ALA C . n 
C 1 37  VAL 37  29  29  VAL VAL C . n 
C 1 38  SER 38  30  30  SER SER C . n 
C 1 39  VAL 39  31  31  VAL VAL C . n 
C 1 40  SER 40  32  32  SER SER C . n 
C 1 41  LEU 41  33  33  LEU LEU C . n 
C 1 42  LYS 42  34  34  LYS LYS C . n 
C 1 43  PHE 43  35  35  PHE PHE C . n 
C 1 44  ILE 44  36  36  ILE ILE C . n 
C 1 45  ASN 45  37  37  ASN ASN C . n 
C 1 46  ILE 46  38  38  ILE ILE C . n 
C 1 47  LEU 47  39  39  LEU LEU C . n 
C 1 48  GLU 48  40  40  GLU GLU C . n 
C 1 49  VAL 49  41  41  VAL VAL C . n 
C 1 50  ASN 50  42  42  ASN ASN C . n 
C 1 51  GLU 51  43  43  GLU GLU C . n 
C 1 52  ILE 52  44  44  ILE ILE C . n 
C 1 53  THR 53  45  45  THR THR C . n 
C 1 54  ASN 54  46  46  ASN ASN C . n 
C 1 55  GLU 55  47  47  GLU GLU C . n 
C 1 56  VAL 56  48  48  VAL VAL C . n 
C 1 57  ASP 57  49  49  ASP ASP C . n 
C 1 58  VAL 58  50  50  VAL VAL C . n 
C 1 59  VAL 59  51  51  VAL VAL C . n 
C 1 60  PHE 60  52  52  PHE PHE C . n 
C 1 61  TRP 61  53  53  TRP TRP C . n 
C 1 62  GLN 62  54  54  GLN GLN C . n 
C 1 63  GLN 63  55  55  GLN GLN C . n 
C 1 64  THR 64  56  56  THR THR C . n 
C 1 65  THR 65  57  57  THR THR C . n 
C 1 66  TRP 66  58  58  TRP TRP C . n 
C 1 67  SER 67  59  59  SER SER C . n 
C 1 68  ASP 68  60  60  ASP ASP C . n 
C 1 69  ARG 69  61  61  ARG ARG C . n 
C 1 70  THR 70  62  62  THR THR C . n 
C 1 71  LEU 71  63  63  LEU LEU C . n 
C 1 72  ALA 72  64  64  ALA ALA C . n 
C 1 73  TRP 73  65  65  TRP TRP C . n 
C 1 74  ASN 74  66  66  ASN ASN C . n 
C 1 75  SER 75  67  67  SER SER C . n 
C 1 76  SER 76  68  68  SER SER C . n 
C 1 77  HIS 77  69  69  HIS HIS C . n 
C 1 78  SER 78  70  70  SER SER C . n 
C 1 79  PRO 79  71  71  PRO PRO C . n 
C 1 80  ASP 80  72  72  ASP ASP C . n 
C 1 81  GLN 81  73  73  GLN GLN C . n 
C 1 82  VAL 82  74  74  VAL VAL C . n 
C 1 83  SER 83  75  75  SER SER C . n 
C 1 84  VAL 84  76  76  VAL VAL C . n 
C 1 85  PRO 85  77  77  PRO PRO C . n 
C 1 86  ILE 86  78  78  ILE ILE C . n 
C 1 87  SER 87  79  79  SER SER C . n 
C 1 88  SER 88  80  80  SER SER C . n 
C 1 89  LEU 89  81  81  LEU LEU C . n 
C 1 90  TRP 90  82  82  TRP TRP C . n 
C 1 91  VAL 91  83  83  VAL VAL C . n 
C 1 92  PRO 92  84  84  PRO PRO C . n 
C 1 93  ASP 93  85  85  ASP ASP C . n 
C 1 94  LEU 94  86  86  LEU LEU C . n 
C 1 95  ALA 95  87  87  ALA ALA C . n 
C 1 96  ALA 96  88  88  ALA ALA C . n 
C 1 97  TYR 97  89  89  TYR TYR C . n 
C 1 98  ASN 98  90  90  ASN ASN C . n 
C 1 99  ALA 99  91  91  ALA ALA C . n 
C 1 100 ILE 100 92  92  ILE ILE C . n 
C 1 101 SER 101 93  93  SER SER C . n 
C 1 102 LYS 102 94  94  LYS LYS C . n 
C 1 103 PRO 103 95  95  PRO PRO C . n 
C 1 104 GLU 104 96  96  GLU GLU C . n 
C 1 105 VAL 105 97  97  VAL VAL C . n 
C 1 106 LEU 106 98  98  LEU LEU C . n 
C 1 107 THR 107 99  99  THR THR C . n 
C 1 108 PRO 108 100 100 PRO PRO C . n 
C 1 109 GLN 109 101 101 GLN GLN C . n 
C 1 110 LEU 110 102 102 LEU LEU C . n 
C 1 111 ALA 111 103 103 ALA ALA C . n 
C 1 112 ARG 112 104 104 ARG ARG C . n 
C 1 113 VAL 113 105 105 VAL VAL C . n 
C 1 114 VAL 114 106 106 VAL VAL C . n 
C 1 115 SER 115 107 107 SER SER C . n 
C 1 116 ASP 116 108 108 ASP ASP C . n 
C 1 117 GLY 117 109 109 GLY GLY C . n 
C 1 118 GLU 118 110 110 GLU GLU C . n 
C 1 119 VAL 119 111 111 VAL VAL C . n 
C 1 120 LEU 120 112 112 LEU LEU C . n 
C 1 121 TYR 121 113 113 TYR TYR C . n 
C 1 122 MET 122 114 114 MET MET C . n 
C 1 123 PRO 123 115 115 PRO PRO C . n 
C 1 124 SER 124 116 116 SER SER C . n 
C 1 125 ILE 125 117 117 ILE ILE C . n 
C 1 126 ARG 126 118 118 ARG ARG C . n 
C 1 127 GLN 127 119 119 GLN GLN C . n 
C 1 128 ARG 128 120 120 ARG ARG C . n 
C 1 129 PHE 129 121 121 PHE PHE C . n 
C 1 130 SER 130 122 122 SER SER C . n 
C 1 131 CYS 131 123 123 CYS CYS C . n 
C 1 132 ASP 132 124 124 ASP ASP C . n 
C 1 133 VAL 133 125 125 VAL VAL C . n 
C 1 134 SER 134 126 126 SER SER C . n 
C 1 135 GLY 135 127 127 GLY GLY C . n 
C 1 136 VAL 136 128 128 VAL VAL C . n 
C 1 137 ASP 137 129 129 ASP ASP C . n 
C 1 138 THR 138 130 130 THR THR C . n 
C 1 139 GLU 139 131 131 GLU GLU C . n 
C 1 140 SER 140 132 132 SER SER C . n 
C 1 141 GLY 141 133 133 GLY GLY C . n 
C 1 142 ALA 142 134 134 ALA ALA C . n 
C 1 143 THR 143 135 135 THR THR C . n 
C 1 144 CYS 144 136 136 CYS CYS C . n 
C 1 145 ARG 145 137 137 ARG ARG C . n 
C 1 146 ILE 146 138 138 ILE ILE C . n 
C 1 147 LYS 147 139 139 LYS LYS C . n 
C 1 148 ILE 148 140 140 ILE ILE C . n 
C 1 149 GLY 149 141 141 GLY GLY C . n 
C 1 150 SER 150 142 142 SER SER C . n 
C 1 151 TRP 151 143 143 TRP TRP C . n 
C 1 152 THR 152 144 144 THR THR C . n 
C 1 153 HIS 153 145 145 HIS HIS C . n 
C 1 154 HIS 154 146 146 HIS HIS C . n 
C 1 155 SER 155 147 147 SER SER C . n 
C 1 156 ARG 156 148 148 ARG ARG C . n 
C 1 157 GLU 157 149 149 GLU GLU C . n 
C 1 158 ILE 158 150 150 ILE ILE C . n 
C 1 159 SER 159 151 151 SER SER C . n 
C 1 160 VAL 160 152 152 VAL VAL C . n 
C 1 161 ASP 161 153 153 ASP ASP C . n 
C 1 162 PRO 162 154 154 PRO PRO C . n 
C 1 163 THR 163 155 155 THR THR C . n 
C 1 164 THR 164 156 156 THR THR C . n 
C 1 165 GLU 165 157 157 GLU GLU C . n 
C 1 166 ASN 166 158 158 ASN ASN C . n 
C 1 167 SER 167 159 159 SER SER C . n 
C 1 168 ASP 168 160 160 ASP ASP C . n 
C 1 169 ASP 169 161 161 ASP ASP C . n 
C 1 170 SER 170 162 162 SER SER C . n 
C 1 171 GLU 171 163 163 GLU GLU C . n 
C 1 172 TYR 172 164 164 TYR TYR C . n 
C 1 173 PHE 173 165 165 PHE PHE C . n 
C 1 174 SER 174 166 166 SER SER C . n 
C 1 175 GLN 175 167 167 GLN GLN C . n 
C 1 176 TYR 176 168 168 TYR TYR C . n 
C 1 177 SER 177 169 169 SER SER C . n 
C 1 178 ARG 178 170 170 ARG ARG C . n 
C 1 179 PHE 179 171 171 PHE PHE C . n 
C 1 180 GLU 180 172 172 GLU GLU C . n 
C 1 181 ILE 181 173 173 ILE ILE C . n 
C 1 182 LEU 182 174 174 LEU LEU C . n 
C 1 183 ASP 183 175 175 ASP ASP C . n 
C 1 184 VAL 184 176 176 VAL VAL C . n 
C 1 185 THR 185 177 177 THR THR C . n 
C 1 186 GLN 186 178 178 GLN GLN C . n 
C 1 187 LYS 187 179 179 LYS LYS C . n 
C 1 188 LYS 188 180 180 LYS LYS C . n 
C 1 189 ASN 189 181 181 ASN ASN C . n 
C 1 190 SER 190 182 182 SER SER C . n 
C 1 191 VAL 191 183 183 VAL VAL C . n 
C 1 192 THR 192 184 184 THR THR C . n 
C 1 193 TYR 193 185 ?   ?   ?   C . n 
C 1 194 SER 194 186 ?   ?   ?   C . n 
C 1 195 CYS 195 187 ?   ?   ?   C . n 
C 1 196 CYS 196 188 ?   ?   ?   C . n 
C 1 197 PRO 197 189 189 PRO PRO C . n 
C 1 198 GLU 198 190 190 GLU GLU C . n 
C 1 199 ALA 199 191 191 ALA ALA C . n 
C 1 200 TYR 200 192 192 TYR TYR C . n 
C 1 201 GLU 201 193 193 GLU GLU C . n 
C 1 202 ASP 202 194 194 ASP ASP C . n 
C 1 203 VAL 203 195 195 VAL VAL C . n 
C 1 204 GLU 204 196 196 GLU GLU C . n 
C 1 205 VAL 205 197 197 VAL VAL C . n 
C 1 206 SER 206 198 198 SER SER C . n 
C 1 207 LEU 207 199 199 LEU LEU C . n 
C 1 208 ASN 208 200 200 ASN ASN C . n 
C 1 209 PHE 209 201 201 PHE PHE C . n 
C 1 210 ARG 210 202 202 ARG ARG C . n 
C 1 211 LYS 211 203 203 LYS LYS C . n 
C 1 212 LYS 212 204 204 LYS LYS C . n 
C 1 213 GLY 213 205 205 GLY GLY C . n 
C 1 214 ARG 214 206 ?   ?   ?   C . n 
C 1 215 SER 215 207 ?   ?   ?   C . n 
C 1 216 GLU 216 208 ?   ?   ?   C . n 
C 1 217 ILE 217 209 ?   ?   ?   C . n 
D 1 1   ASP 1   -7  -7  ASP ASP D . n 
D 1 2   TYR 2   -6  -6  TYR TYR D . n 
D 1 3   LYS 3   -5  -5  LYS LYS D . n 
D 1 4   ASP 4   -4  -4  ASP ASP D . n 
D 1 5   ASP 5   -3  -3  ASP ASP D . n 
D 1 6   ASP 6   -2  -2  ASP ASP D . n 
D 1 7   ASP 7   -1  -1  ASP ASP D . n 
D 1 8   LYS 8   0   0   LYS LYS D . n 
D 1 9   LEU 9   1   1   LEU LEU D . n 
D 1 10  ASP 10  2   2   ASP ASP D . n 
D 1 11  ARG 11  3   3   ARG ARG D . n 
D 1 12  ALA 12  4   4   ALA ALA D . n 
D 1 13  ASP 13  5   5   ASP ASP D . n 
D 1 14  ILE 14  6   6   ILE ILE D . n 
D 1 15  LEU 15  7   7   LEU LEU D . n 
D 1 16  TYR 16  8   8   TYR TYR D . n 
D 1 17  ASN 17  9   9   ASN ASN D . n 
D 1 18  ILE 18  10  10  ILE ILE D . n 
D 1 19  ARG 19  11  11  ARG ARG D . n 
D 1 20  GLN 20  12  12  GLN GLN D . n 
D 1 21  THR 21  13  13  THR THR D . n 
D 1 22  SER 22  14  14  SER SER D . n 
D 1 23  ARG 23  15  15  ARG ARG D . n 
D 1 24  PRO 24  16  16  PRO PRO D . n 
D 1 25  ASP 25  17  17  ASP ASP D . n 
D 1 26  VAL 26  18  18  VAL VAL D . n 
D 1 27  ILE 27  19  19  ILE ILE D . n 
D 1 28  PRO 28  20  20  PRO PRO D . n 
D 1 29  THR 29  21  21  THR THR D . n 
D 1 30  GLN 30  22  22  GLN GLN D . n 
D 1 31  ARG 31  23  23  ARG ARG D . n 
D 1 32  ASP 32  24  24  ASP ASP D . n 
D 1 33  ARG 33  25  25  ARG ARG D . n 
D 1 34  PRO 34  26  26  PRO PRO D . n 
D 1 35  VAL 35  27  27  VAL VAL D . n 
D 1 36  ALA 36  28  28  ALA ALA D . n 
D 1 37  VAL 37  29  29  VAL VAL D . n 
D 1 38  SER 38  30  30  SER SER D . n 
D 1 39  VAL 39  31  31  VAL VAL D . n 
D 1 40  SER 40  32  32  SER SER D . n 
D 1 41  LEU 41  33  33  LEU LEU D . n 
D 1 42  LYS 42  34  34  LYS LYS D . n 
D 1 43  PHE 43  35  35  PHE PHE D . n 
D 1 44  ILE 44  36  36  ILE ILE D . n 
D 1 45  ASN 45  37  37  ASN ASN D . n 
D 1 46  ILE 46  38  38  ILE ILE D . n 
D 1 47  LEU 47  39  39  LEU LEU D . n 
D 1 48  GLU 48  40  40  GLU GLU D . n 
D 1 49  VAL 49  41  41  VAL VAL D . n 
D 1 50  ASN 50  42  42  ASN ASN D . n 
D 1 51  GLU 51  43  43  GLU GLU D . n 
D 1 52  ILE 52  44  44  ILE ILE D . n 
D 1 53  THR 53  45  45  THR THR D . n 
D 1 54  ASN 54  46  46  ASN ASN D . n 
D 1 55  GLU 55  47  47  GLU GLU D . n 
D 1 56  VAL 56  48  48  VAL VAL D . n 
D 1 57  ASP 57  49  49  ASP ASP D . n 
D 1 58  VAL 58  50  50  VAL VAL D . n 
D 1 59  VAL 59  51  51  VAL VAL D . n 
D 1 60  PHE 60  52  52  PHE PHE D . n 
D 1 61  TRP 61  53  53  TRP TRP D . n 
D 1 62  GLN 62  54  54  GLN GLN D . n 
D 1 63  GLN 63  55  55  GLN GLN D . n 
D 1 64  THR 64  56  56  THR THR D . n 
D 1 65  THR 65  57  57  THR THR D . n 
D 1 66  TRP 66  58  58  TRP TRP D . n 
D 1 67  SER 67  59  59  SER SER D . n 
D 1 68  ASP 68  60  60  ASP ASP D . n 
D 1 69  ARG 69  61  61  ARG ARG D . n 
D 1 70  THR 70  62  62  THR THR D . n 
D 1 71  LEU 71  63  63  LEU LEU D . n 
D 1 72  ALA 72  64  64  ALA ALA D . n 
D 1 73  TRP 73  65  65  TRP TRP D . n 
D 1 74  ASN 74  66  66  ASN ASN D . n 
D 1 75  SER 75  67  67  SER SER D . n 
D 1 76  SER 76  68  68  SER SER D . n 
D 1 77  HIS 77  69  69  HIS HIS D . n 
D 1 78  SER 78  70  70  SER SER D . n 
D 1 79  PRO 79  71  71  PRO PRO D . n 
D 1 80  ASP 80  72  72  ASP ASP D . n 
D 1 81  GLN 81  73  73  GLN GLN D . n 
D 1 82  VAL 82  74  74  VAL VAL D . n 
D 1 83  SER 83  75  75  SER SER D . n 
D 1 84  VAL 84  76  76  VAL VAL D . n 
D 1 85  PRO 85  77  77  PRO PRO D . n 
D 1 86  ILE 86  78  78  ILE ILE D . n 
D 1 87  SER 87  79  79  SER SER D . n 
D 1 88  SER 88  80  80  SER SER D . n 
D 1 89  LEU 89  81  81  LEU LEU D . n 
D 1 90  TRP 90  82  82  TRP TRP D . n 
D 1 91  VAL 91  83  83  VAL VAL D . n 
D 1 92  PRO 92  84  84  PRO PRO D . n 
D 1 93  ASP 93  85  85  ASP ASP D . n 
D 1 94  LEU 94  86  86  LEU LEU D . n 
D 1 95  ALA 95  87  87  ALA ALA D . n 
D 1 96  ALA 96  88  88  ALA ALA D . n 
D 1 97  TYR 97  89  89  TYR TYR D . n 
D 1 98  ASN 98  90  90  ASN ASN D . n 
D 1 99  ALA 99  91  91  ALA ALA D . n 
D 1 100 ILE 100 92  92  ILE ILE D . n 
D 1 101 SER 101 93  93  SER SER D . n 
D 1 102 LYS 102 94  94  LYS LYS D . n 
D 1 103 PRO 103 95  95  PRO PRO D . n 
D 1 104 GLU 104 96  96  GLU GLU D . n 
D 1 105 VAL 105 97  97  VAL VAL D . n 
D 1 106 LEU 106 98  98  LEU LEU D . n 
D 1 107 THR 107 99  99  THR THR D . n 
D 1 108 PRO 108 100 100 PRO PRO D . n 
D 1 109 GLN 109 101 101 GLN GLN D . n 
D 1 110 LEU 110 102 102 LEU LEU D . n 
D 1 111 ALA 111 103 103 ALA ALA D . n 
D 1 112 ARG 112 104 104 ARG ARG D . n 
D 1 113 VAL 113 105 105 VAL VAL D . n 
D 1 114 VAL 114 106 106 VAL VAL D . n 
D 1 115 SER 115 107 107 SER SER D . n 
D 1 116 ASP 116 108 108 ASP ASP D . n 
D 1 117 GLY 117 109 109 GLY GLY D . n 
D 1 118 GLU 118 110 110 GLU GLU D . n 
D 1 119 VAL 119 111 111 VAL VAL D . n 
D 1 120 LEU 120 112 112 LEU LEU D . n 
D 1 121 TYR 121 113 113 TYR TYR D . n 
D 1 122 MET 122 114 114 MET MET D . n 
D 1 123 PRO 123 115 115 PRO PRO D . n 
D 1 124 SER 124 116 116 SER SER D . n 
D 1 125 ILE 125 117 117 ILE ILE D . n 
D 1 126 ARG 126 118 118 ARG ARG D . n 
D 1 127 GLN 127 119 119 GLN GLN D . n 
D 1 128 ARG 128 120 120 ARG ARG D . n 
D 1 129 PHE 129 121 121 PHE PHE D . n 
D 1 130 SER 130 122 122 SER SER D . n 
D 1 131 CYS 131 123 123 CYS CYS D . n 
D 1 132 ASP 132 124 124 ASP ASP D . n 
D 1 133 VAL 133 125 125 VAL VAL D . n 
D 1 134 SER 134 126 126 SER SER D . n 
D 1 135 GLY 135 127 127 GLY GLY D . n 
D 1 136 VAL 136 128 128 VAL VAL D . n 
D 1 137 ASP 137 129 129 ASP ASP D . n 
D 1 138 THR 138 130 130 THR THR D . n 
D 1 139 GLU 139 131 131 GLU GLU D . n 
D 1 140 SER 140 132 132 SER SER D . n 
D 1 141 GLY 141 133 133 GLY GLY D . n 
D 1 142 ALA 142 134 134 ALA ALA D . n 
D 1 143 THR 143 135 135 THR THR D . n 
D 1 144 CYS 144 136 136 CYS CYS D . n 
D 1 145 ARG 145 137 137 ARG ARG D . n 
D 1 146 ILE 146 138 138 ILE ILE D . n 
D 1 147 LYS 147 139 139 LYS LYS D . n 
D 1 148 ILE 148 140 140 ILE ILE D . n 
D 1 149 GLY 149 141 141 GLY GLY D . n 
D 1 150 SER 150 142 142 SER SER D . n 
D 1 151 TRP 151 143 143 TRP TRP D . n 
D 1 152 THR 152 144 144 THR THR D . n 
D 1 153 HIS 153 145 145 HIS HIS D . n 
D 1 154 HIS 154 146 146 HIS HIS D . n 
D 1 155 SER 155 147 147 SER SER D . n 
D 1 156 ARG 156 148 148 ARG ARG D . n 
D 1 157 GLU 157 149 149 GLU GLU D . n 
D 1 158 ILE 158 150 150 ILE ILE D . n 
D 1 159 SER 159 151 151 SER SER D . n 
D 1 160 VAL 160 152 152 VAL VAL D . n 
D 1 161 ASP 161 153 153 ASP ASP D . n 
D 1 162 PRO 162 154 154 PRO PRO D . n 
D 1 163 THR 163 155 155 THR THR D . n 
D 1 164 THR 164 156 156 THR THR D . n 
D 1 165 GLU 165 157 157 GLU GLU D . n 
D 1 166 ASN 166 158 158 ASN ASN D . n 
D 1 167 SER 167 159 159 SER SER D . n 
D 1 168 ASP 168 160 160 ASP ASP D . n 
D 1 169 ASP 169 161 161 ASP ASP D . n 
D 1 170 SER 170 162 162 SER SER D . n 
D 1 171 GLU 171 163 163 GLU GLU D . n 
D 1 172 TYR 172 164 164 TYR TYR D . n 
D 1 173 PHE 173 165 165 PHE PHE D . n 
D 1 174 SER 174 166 166 SER SER D . n 
D 1 175 GLN 175 167 167 GLN GLN D . n 
D 1 176 TYR 176 168 168 TYR TYR D . n 
D 1 177 SER 177 169 169 SER SER D . n 
D 1 178 ARG 178 170 170 ARG ARG D . n 
D 1 179 PHE 179 171 171 PHE PHE D . n 
D 1 180 GLU 180 172 172 GLU GLU D . n 
D 1 181 ILE 181 173 173 ILE ILE D . n 
D 1 182 LEU 182 174 174 LEU LEU D . n 
D 1 183 ASP 183 175 175 ASP ASP D . n 
D 1 184 VAL 184 176 176 VAL VAL D . n 
D 1 185 THR 185 177 177 THR THR D . n 
D 1 186 GLN 186 178 178 GLN GLN D . n 
D 1 187 LYS 187 179 179 LYS LYS D . n 
D 1 188 LYS 188 180 180 LYS LYS D . n 
D 1 189 ASN 189 181 181 ASN ASN D . n 
D 1 190 SER 190 182 182 SER SER D . n 
D 1 191 VAL 191 183 183 VAL VAL D . n 
D 1 192 THR 192 184 184 THR THR D . n 
D 1 193 TYR 193 185 185 TYR TYR D . n 
D 1 194 SER 194 186 186 SER SER D . n 
D 1 195 CYS 195 187 187 CYS CYS D . n 
D 1 196 CYS 196 188 188 CYS CYS D . n 
D 1 197 PRO 197 189 189 PRO PRO D . n 
D 1 198 GLU 198 190 190 GLU GLU D . n 
D 1 199 ALA 199 191 191 ALA ALA D . n 
D 1 200 TYR 200 192 192 TYR TYR D . n 
D 1 201 GLU 201 193 193 GLU GLU D . n 
D 1 202 ASP 202 194 194 ASP ASP D . n 
D 1 203 VAL 203 195 195 VAL VAL D . n 
D 1 204 GLU 204 196 196 GLU GLU D . n 
D 1 205 VAL 205 197 197 VAL VAL D . n 
D 1 206 SER 206 198 198 SER SER D . n 
D 1 207 LEU 207 199 199 LEU LEU D . n 
D 1 208 ASN 208 200 200 ASN ASN D . n 
D 1 209 PHE 209 201 201 PHE PHE D . n 
D 1 210 ARG 210 202 202 ARG ARG D . n 
D 1 211 LYS 211 203 203 LYS LYS D . n 
D 1 212 LYS 212 204 204 LYS LYS D . n 
D 1 213 GLY 213 205 205 GLY GLY D . n 
D 1 214 ARG 214 206 ?   ?   ?   D . n 
D 1 215 SER 215 207 ?   ?   ?   D . n 
D 1 216 GLU 216 208 ?   ?   ?   D . n 
D 1 217 ILE 217 209 ?   ?   ?   D . n 
E 1 1   ASP 1   -7  -7  ASP ASP E . n 
E 1 2   TYR 2   -6  -6  TYR TYR E . n 
E 1 3   LYS 3   -5  -5  LYS LYS E . n 
E 1 4   ASP 4   -4  -4  ASP ASP E . n 
E 1 5   ASP 5   -3  -3  ASP ASP E . n 
E 1 6   ASP 6   -2  -2  ASP ASP E . n 
E 1 7   ASP 7   -1  -1  ASP ASP E . n 
E 1 8   LYS 8   0   0   LYS LYS E . n 
E 1 9   LEU 9   1   1   LEU LEU E . n 
E 1 10  ASP 10  2   2   ASP ASP E . n 
E 1 11  ARG 11  3   3   ARG ARG E . n 
E 1 12  ALA 12  4   4   ALA ALA E . n 
E 1 13  ASP 13  5   5   ASP ASP E . n 
E 1 14  ILE 14  6   6   ILE ILE E . n 
E 1 15  LEU 15  7   7   LEU LEU E . n 
E 1 16  TYR 16  8   8   TYR TYR E . n 
E 1 17  ASN 17  9   9   ASN ASN E . n 
E 1 18  ILE 18  10  10  ILE ILE E . n 
E 1 19  ARG 19  11  11  ARG ARG E . n 
E 1 20  GLN 20  12  12  GLN GLN E . n 
E 1 21  THR 21  13  13  THR THR E . n 
E 1 22  SER 22  14  14  SER SER E . n 
E 1 23  ARG 23  15  15  ARG ARG E . n 
E 1 24  PRO 24  16  16  PRO PRO E . n 
E 1 25  ASP 25  17  17  ASP ASP E . n 
E 1 26  VAL 26  18  18  VAL VAL E . n 
E 1 27  ILE 27  19  19  ILE ILE E . n 
E 1 28  PRO 28  20  20  PRO PRO E . n 
E 1 29  THR 29  21  21  THR THR E . n 
E 1 30  GLN 30  22  22  GLN GLN E . n 
E 1 31  ARG 31  23  23  ARG ARG E . n 
E 1 32  ASP 32  24  24  ASP ASP E . n 
E 1 33  ARG 33  25  25  ARG ARG E . n 
E 1 34  PRO 34  26  26  PRO PRO E . n 
E 1 35  VAL 35  27  27  VAL VAL E . n 
E 1 36  ALA 36  28  28  ALA ALA E . n 
E 1 37  VAL 37  29  29  VAL VAL E . n 
E 1 38  SER 38  30  30  SER SER E . n 
E 1 39  VAL 39  31  31  VAL VAL E . n 
E 1 40  SER 40  32  32  SER SER E . n 
E 1 41  LEU 41  33  33  LEU LEU E . n 
E 1 42  LYS 42  34  34  LYS LYS E . n 
E 1 43  PHE 43  35  35  PHE PHE E . n 
E 1 44  ILE 44  36  36  ILE ILE E . n 
E 1 45  ASN 45  37  37  ASN ASN E . n 
E 1 46  ILE 46  38  38  ILE ILE E . n 
E 1 47  LEU 47  39  39  LEU LEU E . n 
E 1 48  GLU 48  40  40  GLU GLU E . n 
E 1 49  VAL 49  41  41  VAL VAL E . n 
E 1 50  ASN 50  42  42  ASN ASN E . n 
E 1 51  GLU 51  43  43  GLU GLU E . n 
E 1 52  ILE 52  44  44  ILE ILE E . n 
E 1 53  THR 53  45  45  THR THR E . n 
E 1 54  ASN 54  46  46  ASN ASN E . n 
E 1 55  GLU 55  47  47  GLU GLU E . n 
E 1 56  VAL 56  48  48  VAL VAL E . n 
E 1 57  ASP 57  49  49  ASP ASP E . n 
E 1 58  VAL 58  50  50  VAL VAL E . n 
E 1 59  VAL 59  51  51  VAL VAL E . n 
E 1 60  PHE 60  52  52  PHE PHE E . n 
E 1 61  TRP 61  53  53  TRP TRP E . n 
E 1 62  GLN 62  54  54  GLN GLN E . n 
E 1 63  GLN 63  55  55  GLN GLN E . n 
E 1 64  THR 64  56  56  THR THR E . n 
E 1 65  THR 65  57  57  THR THR E . n 
E 1 66  TRP 66  58  58  TRP TRP E . n 
E 1 67  SER 67  59  59  SER SER E . n 
E 1 68  ASP 68  60  60  ASP ASP E . n 
E 1 69  ARG 69  61  61  ARG ARG E . n 
E 1 70  THR 70  62  62  THR THR E . n 
E 1 71  LEU 71  63  63  LEU LEU E . n 
E 1 72  ALA 72  64  64  ALA ALA E . n 
E 1 73  TRP 73  65  65  TRP TRP E . n 
E 1 74  ASN 74  66  66  ASN ASN E . n 
E 1 75  SER 75  67  67  SER SER E . n 
E 1 76  SER 76  68  68  SER SER E . n 
E 1 77  HIS 77  69  69  HIS HIS E . n 
E 1 78  SER 78  70  70  SER SER E . n 
E 1 79  PRO 79  71  71  PRO PRO E . n 
E 1 80  ASP 80  72  72  ASP ASP E . n 
E 1 81  GLN 81  73  73  GLN GLN E . n 
E 1 82  VAL 82  74  74  VAL VAL E . n 
E 1 83  SER 83  75  75  SER SER E . n 
E 1 84  VAL 84  76  76  VAL VAL E . n 
E 1 85  PRO 85  77  77  PRO PRO E . n 
E 1 86  ILE 86  78  78  ILE ILE E . n 
E 1 87  SER 87  79  79  SER SER E . n 
E 1 88  SER 88  80  80  SER SER E . n 
E 1 89  LEU 89  81  81  LEU LEU E . n 
E 1 90  TRP 90  82  82  TRP TRP E . n 
E 1 91  VAL 91  83  83  VAL VAL E . n 
E 1 92  PRO 92  84  84  PRO PRO E . n 
E 1 93  ASP 93  85  85  ASP ASP E . n 
E 1 94  LEU 94  86  86  LEU LEU E . n 
E 1 95  ALA 95  87  87  ALA ALA E . n 
E 1 96  ALA 96  88  88  ALA ALA E . n 
E 1 97  TYR 97  89  89  TYR TYR E . n 
E 1 98  ASN 98  90  90  ASN ASN E . n 
E 1 99  ALA 99  91  91  ALA ALA E . n 
E 1 100 ILE 100 92  92  ILE ILE E . n 
E 1 101 SER 101 93  93  SER SER E . n 
E 1 102 LYS 102 94  94  LYS LYS E . n 
E 1 103 PRO 103 95  95  PRO PRO E . n 
E 1 104 GLU 104 96  96  GLU GLU E . n 
E 1 105 VAL 105 97  97  VAL VAL E . n 
E 1 106 LEU 106 98  98  LEU LEU E . n 
E 1 107 THR 107 99  99  THR THR E . n 
E 1 108 PRO 108 100 100 PRO PRO E . n 
E 1 109 GLN 109 101 101 GLN GLN E . n 
E 1 110 LEU 110 102 102 LEU LEU E . n 
E 1 111 ALA 111 103 103 ALA ALA E . n 
E 1 112 ARG 112 104 104 ARG ARG E . n 
E 1 113 VAL 113 105 105 VAL VAL E . n 
E 1 114 VAL 114 106 106 VAL VAL E . n 
E 1 115 SER 115 107 107 SER SER E . n 
E 1 116 ASP 116 108 108 ASP ASP E . n 
E 1 117 GLY 117 109 109 GLY GLY E . n 
E 1 118 GLU 118 110 110 GLU GLU E . n 
E 1 119 VAL 119 111 111 VAL VAL E . n 
E 1 120 LEU 120 112 112 LEU LEU E . n 
E 1 121 TYR 121 113 113 TYR TYR E . n 
E 1 122 MET 122 114 114 MET MET E . n 
E 1 123 PRO 123 115 115 PRO PRO E . n 
E 1 124 SER 124 116 116 SER SER E . n 
E 1 125 ILE 125 117 117 ILE ILE E . n 
E 1 126 ARG 126 118 118 ARG ARG E . n 
E 1 127 GLN 127 119 119 GLN GLN E . n 
E 1 128 ARG 128 120 120 ARG ARG E . n 
E 1 129 PHE 129 121 121 PHE PHE E . n 
E 1 130 SER 130 122 122 SER SER E . n 
E 1 131 CYS 131 123 123 CYS CYS E . n 
E 1 132 ASP 132 124 124 ASP ASP E . n 
E 1 133 VAL 133 125 125 VAL VAL E . n 
E 1 134 SER 134 126 126 SER SER E . n 
E 1 135 GLY 135 127 127 GLY GLY E . n 
E 1 136 VAL 136 128 128 VAL VAL E . n 
E 1 137 ASP 137 129 129 ASP ASP E . n 
E 1 138 THR 138 130 130 THR THR E . n 
E 1 139 GLU 139 131 131 GLU GLU E . n 
E 1 140 SER 140 132 132 SER SER E . n 
E 1 141 GLY 141 133 133 GLY GLY E . n 
E 1 142 ALA 142 134 134 ALA ALA E . n 
E 1 143 THR 143 135 135 THR THR E . n 
E 1 144 CYS 144 136 136 CYS CYS E . n 
E 1 145 ARG 145 137 137 ARG ARG E . n 
E 1 146 ILE 146 138 138 ILE ILE E . n 
E 1 147 LYS 147 139 139 LYS LYS E . n 
E 1 148 ILE 148 140 140 ILE ILE E . n 
E 1 149 GLY 149 141 141 GLY GLY E . n 
E 1 150 SER 150 142 142 SER SER E . n 
E 1 151 TRP 151 143 143 TRP TRP E . n 
E 1 152 THR 152 144 144 THR THR E . n 
E 1 153 HIS 153 145 145 HIS HIS E . n 
E 1 154 HIS 154 146 146 HIS HIS E . n 
E 1 155 SER 155 147 147 SER SER E . n 
E 1 156 ARG 156 148 148 ARG ARG E . n 
E 1 157 GLU 157 149 149 GLU GLU E . n 
E 1 158 ILE 158 150 150 ILE ILE E . n 
E 1 159 SER 159 151 151 SER SER E . n 
E 1 160 VAL 160 152 152 VAL VAL E . n 
E 1 161 ASP 161 153 153 ASP ASP E . n 
E 1 162 PRO 162 154 154 PRO PRO E . n 
E 1 163 THR 163 155 155 THR THR E . n 
E 1 164 THR 164 156 ?   ?   ?   E . n 
E 1 165 GLU 165 157 ?   ?   ?   E . n 
E 1 166 ASN 166 158 ?   ?   ?   E . n 
E 1 167 SER 167 159 159 SER SER E . n 
E 1 168 ASP 168 160 160 ASP ASP E . n 
E 1 169 ASP 169 161 161 ASP ASP E . n 
E 1 170 SER 170 162 162 SER SER E . n 
E 1 171 GLU 171 163 163 GLU GLU E . n 
E 1 172 TYR 172 164 164 TYR TYR E . n 
E 1 173 PHE 173 165 165 PHE PHE E . n 
E 1 174 SER 174 166 166 SER SER E . n 
E 1 175 GLN 175 167 167 GLN GLN E . n 
E 1 176 TYR 176 168 168 TYR TYR E . n 
E 1 177 SER 177 169 169 SER SER E . n 
E 1 178 ARG 178 170 170 ARG ARG E . n 
E 1 179 PHE 179 171 171 PHE PHE E . n 
E 1 180 GLU 180 172 172 GLU GLU E . n 
E 1 181 ILE 181 173 173 ILE ILE E . n 
E 1 182 LEU 182 174 174 LEU LEU E . n 
E 1 183 ASP 183 175 175 ASP ASP E . n 
E 1 184 VAL 184 176 176 VAL VAL E . n 
E 1 185 THR 185 177 177 THR THR E . n 
E 1 186 GLN 186 178 178 GLN GLN E . n 
E 1 187 LYS 187 179 179 LYS LYS E . n 
E 1 188 LYS 188 180 180 LYS LYS E . n 
E 1 189 ASN 189 181 181 ASN ASN E . n 
E 1 190 SER 190 182 182 SER SER E . n 
E 1 191 VAL 191 183 183 VAL VAL E . n 
E 1 192 THR 192 184 184 THR THR E . n 
E 1 193 TYR 193 185 ?   ?   ?   E . n 
E 1 194 SER 194 186 ?   ?   ?   E . n 
E 1 195 CYS 195 187 ?   ?   ?   E . n 
E 1 196 CYS 196 188 ?   ?   ?   E . n 
E 1 197 PRO 197 189 ?   ?   ?   E . n 
E 1 198 GLU 198 190 190 GLU GLU E . n 
E 1 199 ALA 199 191 191 ALA ALA E . n 
E 1 200 TYR 200 192 192 TYR TYR E . n 
E 1 201 GLU 201 193 193 GLU GLU E . n 
E 1 202 ASP 202 194 194 ASP ASP E . n 
E 1 203 VAL 203 195 195 VAL VAL E . n 
E 1 204 GLU 204 196 196 GLU GLU E . n 
E 1 205 VAL 205 197 197 VAL VAL E . n 
E 1 206 SER 206 198 198 SER SER E . n 
E 1 207 LEU 207 199 199 LEU LEU E . n 
E 1 208 ASN 208 200 200 ASN ASN E . n 
E 1 209 PHE 209 201 201 PHE PHE E . n 
E 1 210 ARG 210 202 202 ARG ARG E . n 
E 1 211 LYS 211 203 203 LYS LYS E . n 
E 1 212 LYS 212 204 204 LYS LYS E . n 
E 1 213 GLY 213 205 205 GLY GLY E . n 
E 1 214 ARG 214 206 ?   ?   ?   E . n 
E 1 215 SER 215 207 ?   ?   ?   E . n 
E 1 216 GLU 216 208 ?   ?   ?   E . n 
E 1 217 ILE 217 209 ?   ?   ?   E . n 
F 1 1   ASP 1   -7  -7  ASP ASP F . n 
F 1 2   TYR 2   -6  -6  TYR TYR F . n 
F 1 3   LYS 3   -5  -5  LYS LYS F . n 
F 1 4   ASP 4   -4  -4  ASP ASP F . n 
F 1 5   ASP 5   -3  -3  ASP ASP F . n 
F 1 6   ASP 6   -2  -2  ASP ASP F . n 
F 1 7   ASP 7   -1  -1  ASP ASP F . n 
F 1 8   LYS 8   0   0   LYS LYS F . n 
F 1 9   LEU 9   1   1   LEU LEU F . n 
F 1 10  ASP 10  2   2   ASP ASP F . n 
F 1 11  ARG 11  3   3   ARG ARG F . n 
F 1 12  ALA 12  4   4   ALA ALA F . n 
F 1 13  ASP 13  5   5   ASP ASP F . n 
F 1 14  ILE 14  6   6   ILE ILE F . n 
F 1 15  LEU 15  7   7   LEU LEU F . n 
F 1 16  TYR 16  8   8   TYR TYR F . n 
F 1 17  ASN 17  9   9   ASN ASN F . n 
F 1 18  ILE 18  10  10  ILE ILE F . n 
F 1 19  ARG 19  11  11  ARG ARG F . n 
F 1 20  GLN 20  12  12  GLN GLN F . n 
F 1 21  THR 21  13  13  THR THR F . n 
F 1 22  SER 22  14  14  SER SER F . n 
F 1 23  ARG 23  15  15  ARG ARG F . n 
F 1 24  PRO 24  16  16  PRO PRO F . n 
F 1 25  ASP 25  17  17  ASP ASP F . n 
F 1 26  VAL 26  18  18  VAL VAL F . n 
F 1 27  ILE 27  19  19  ILE ILE F . n 
F 1 28  PRO 28  20  20  PRO PRO F . n 
F 1 29  THR 29  21  21  THR THR F . n 
F 1 30  GLN 30  22  22  GLN GLN F . n 
F 1 31  ARG 31  23  23  ARG ARG F . n 
F 1 32  ASP 32  24  24  ASP ASP F . n 
F 1 33  ARG 33  25  25  ARG ARG F . n 
F 1 34  PRO 34  26  26  PRO PRO F . n 
F 1 35  VAL 35  27  27  VAL VAL F . n 
F 1 36  ALA 36  28  28  ALA ALA F . n 
F 1 37  VAL 37  29  29  VAL VAL F . n 
F 1 38  SER 38  30  30  SER SER F . n 
F 1 39  VAL 39  31  31  VAL VAL F . n 
F 1 40  SER 40  32  32  SER SER F . n 
F 1 41  LEU 41  33  33  LEU LEU F . n 
F 1 42  LYS 42  34  34  LYS LYS F . n 
F 1 43  PHE 43  35  35  PHE PHE F . n 
F 1 44  ILE 44  36  36  ILE ILE F . n 
F 1 45  ASN 45  37  37  ASN ASN F . n 
F 1 46  ILE 46  38  38  ILE ILE F . n 
F 1 47  LEU 47  39  39  LEU LEU F . n 
F 1 48  GLU 48  40  40  GLU GLU F . n 
F 1 49  VAL 49  41  41  VAL VAL F . n 
F 1 50  ASN 50  42  42  ASN ASN F . n 
F 1 51  GLU 51  43  43  GLU GLU F . n 
F 1 52  ILE 52  44  44  ILE ILE F . n 
F 1 53  THR 53  45  45  THR THR F . n 
F 1 54  ASN 54  46  46  ASN ASN F . n 
F 1 55  GLU 55  47  47  GLU GLU F . n 
F 1 56  VAL 56  48  48  VAL VAL F . n 
F 1 57  ASP 57  49  49  ASP ASP F . n 
F 1 58  VAL 58  50  50  VAL VAL F . n 
F 1 59  VAL 59  51  51  VAL VAL F . n 
F 1 60  PHE 60  52  52  PHE PHE F . n 
F 1 61  TRP 61  53  53  TRP TRP F . n 
F 1 62  GLN 62  54  54  GLN GLN F . n 
F 1 63  GLN 63  55  55  GLN GLN F . n 
F 1 64  THR 64  56  56  THR THR F . n 
F 1 65  THR 65  57  57  THR THR F . n 
F 1 66  TRP 66  58  58  TRP TRP F . n 
F 1 67  SER 67  59  59  SER SER F . n 
F 1 68  ASP 68  60  60  ASP ASP F . n 
F 1 69  ARG 69  61  61  ARG ARG F . n 
F 1 70  THR 70  62  62  THR THR F . n 
F 1 71  LEU 71  63  63  LEU LEU F . n 
F 1 72  ALA 72  64  64  ALA ALA F . n 
F 1 73  TRP 73  65  65  TRP TRP F . n 
F 1 74  ASN 74  66  66  ASN ASN F . n 
F 1 75  SER 75  67  67  SER SER F . n 
F 1 76  SER 76  68  68  SER SER F . n 
F 1 77  HIS 77  69  69  HIS HIS F . n 
F 1 78  SER 78  70  70  SER SER F . n 
F 1 79  PRO 79  71  71  PRO PRO F . n 
F 1 80  ASP 80  72  72  ASP ASP F . n 
F 1 81  GLN 81  73  73  GLN GLN F . n 
F 1 82  VAL 82  74  74  VAL VAL F . n 
F 1 83  SER 83  75  75  SER SER F . n 
F 1 84  VAL 84  76  76  VAL VAL F . n 
F 1 85  PRO 85  77  77  PRO PRO F . n 
F 1 86  ILE 86  78  78  ILE ILE F . n 
F 1 87  SER 87  79  79  SER SER F . n 
F 1 88  SER 88  80  80  SER SER F . n 
F 1 89  LEU 89  81  81  LEU LEU F . n 
F 1 90  TRP 90  82  82  TRP TRP F . n 
F 1 91  VAL 91  83  83  VAL VAL F . n 
F 1 92  PRO 92  84  84  PRO PRO F . n 
F 1 93  ASP 93  85  85  ASP ASP F . n 
F 1 94  LEU 94  86  86  LEU LEU F . n 
F 1 95  ALA 95  87  87  ALA ALA F . n 
F 1 96  ALA 96  88  88  ALA ALA F . n 
F 1 97  TYR 97  89  89  TYR TYR F . n 
F 1 98  ASN 98  90  90  ASN ASN F . n 
F 1 99  ALA 99  91  91  ALA ALA F . n 
F 1 100 ILE 100 92  92  ILE ILE F . n 
F 1 101 SER 101 93  93  SER SER F . n 
F 1 102 LYS 102 94  94  LYS LYS F . n 
F 1 103 PRO 103 95  95  PRO PRO F . n 
F 1 104 GLU 104 96  96  GLU GLU F . n 
F 1 105 VAL 105 97  97  VAL VAL F . n 
F 1 106 LEU 106 98  98  LEU LEU F . n 
F 1 107 THR 107 99  99  THR THR F . n 
F 1 108 PRO 108 100 100 PRO PRO F . n 
F 1 109 GLN 109 101 101 GLN GLN F . n 
F 1 110 LEU 110 102 102 LEU LEU F . n 
F 1 111 ALA 111 103 103 ALA ALA F . n 
F 1 112 ARG 112 104 104 ARG ARG F . n 
F 1 113 VAL 113 105 105 VAL VAL F . n 
F 1 114 VAL 114 106 106 VAL VAL F . n 
F 1 115 SER 115 107 107 SER SER F . n 
F 1 116 ASP 116 108 108 ASP ASP F . n 
F 1 117 GLY 117 109 109 GLY GLY F . n 
F 1 118 GLU 118 110 110 GLU GLU F . n 
F 1 119 VAL 119 111 111 VAL VAL F . n 
F 1 120 LEU 120 112 112 LEU LEU F . n 
F 1 121 TYR 121 113 113 TYR TYR F . n 
F 1 122 MET 122 114 114 MET MET F . n 
F 1 123 PRO 123 115 115 PRO PRO F . n 
F 1 124 SER 124 116 116 SER SER F . n 
F 1 125 ILE 125 117 117 ILE ILE F . n 
F 1 126 ARG 126 118 118 ARG ARG F . n 
F 1 127 GLN 127 119 119 GLN GLN F . n 
F 1 128 ARG 128 120 120 ARG ARG F . n 
F 1 129 PHE 129 121 121 PHE PHE F . n 
F 1 130 SER 130 122 122 SER SER F . n 
F 1 131 CYS 131 123 123 CYS CYS F . n 
F 1 132 ASP 132 124 124 ASP ASP F . n 
F 1 133 VAL 133 125 125 VAL VAL F . n 
F 1 134 SER 134 126 126 SER SER F . n 
F 1 135 GLY 135 127 127 GLY GLY F . n 
F 1 136 VAL 136 128 128 VAL VAL F . n 
F 1 137 ASP 137 129 129 ASP ASP F . n 
F 1 138 THR 138 130 130 THR THR F . n 
F 1 139 GLU 139 131 131 GLU GLU F . n 
F 1 140 SER 140 132 132 SER SER F . n 
F 1 141 GLY 141 133 133 GLY GLY F . n 
F 1 142 ALA 142 134 134 ALA ALA F . n 
F 1 143 THR 143 135 135 THR THR F . n 
F 1 144 CYS 144 136 136 CYS CYS F . n 
F 1 145 ARG 145 137 137 ARG ARG F . n 
F 1 146 ILE 146 138 138 ILE ILE F . n 
F 1 147 LYS 147 139 139 LYS LYS F . n 
F 1 148 ILE 148 140 140 ILE ILE F . n 
F 1 149 GLY 149 141 141 GLY GLY F . n 
F 1 150 SER 150 142 142 SER SER F . n 
F 1 151 TRP 151 143 143 TRP TRP F . n 
F 1 152 THR 152 144 144 THR THR F . n 
F 1 153 HIS 153 145 145 HIS HIS F . n 
F 1 154 HIS 154 146 146 HIS HIS F . n 
F 1 155 SER 155 147 147 SER SER F . n 
F 1 156 ARG 156 148 148 ARG ARG F . n 
F 1 157 GLU 157 149 149 GLU GLU F . n 
F 1 158 ILE 158 150 150 ILE ILE F . n 
F 1 159 SER 159 151 151 SER SER F . n 
F 1 160 VAL 160 152 152 VAL VAL F . n 
F 1 161 ASP 161 153 153 ASP ASP F . n 
F 1 162 PRO 162 154 154 PRO PRO F . n 
F 1 163 THR 163 155 155 THR THR F . n 
F 1 164 THR 164 156 ?   ?   ?   F . n 
F 1 165 GLU 165 157 157 GLU GLU F . n 
F 1 166 ASN 166 158 158 ASN ASN F . n 
F 1 167 SER 167 159 159 SER SER F . n 
F 1 168 ASP 168 160 160 ASP ASP F . n 
F 1 169 ASP 169 161 161 ASP ASP F . n 
F 1 170 SER 170 162 162 SER SER F . n 
F 1 171 GLU 171 163 163 GLU GLU F . n 
F 1 172 TYR 172 164 164 TYR TYR F . n 
F 1 173 PHE 173 165 165 PHE PHE F . n 
F 1 174 SER 174 166 166 SER SER F . n 
F 1 175 GLN 175 167 167 GLN GLN F . n 
F 1 176 TYR 176 168 168 TYR TYR F . n 
F 1 177 SER 177 169 169 SER SER F . n 
F 1 178 ARG 178 170 170 ARG ARG F . n 
F 1 179 PHE 179 171 171 PHE PHE F . n 
F 1 180 GLU 180 172 172 GLU GLU F . n 
F 1 181 ILE 181 173 173 ILE ILE F . n 
F 1 182 LEU 182 174 174 LEU LEU F . n 
F 1 183 ASP 183 175 175 ASP ASP F . n 
F 1 184 VAL 184 176 176 VAL VAL F . n 
F 1 185 THR 185 177 177 THR THR F . n 
F 1 186 GLN 186 178 178 GLN GLN F . n 
F 1 187 LYS 187 179 179 LYS LYS F . n 
F 1 188 LYS 188 180 180 LYS LYS F . n 
F 1 189 ASN 189 181 181 ASN ASN F . n 
F 1 190 SER 190 182 182 SER SER F . n 
F 1 191 VAL 191 183 183 VAL VAL F . n 
F 1 192 THR 192 184 184 THR THR F . n 
F 1 193 TYR 193 185 ?   ?   ?   F . n 
F 1 194 SER 194 186 ?   ?   ?   F . n 
F 1 195 CYS 195 187 ?   ?   ?   F . n 
F 1 196 CYS 196 188 188 CYS CYS F . n 
F 1 197 PRO 197 189 189 PRO PRO F . n 
F 1 198 GLU 198 190 190 GLU GLU F . n 
F 1 199 ALA 199 191 191 ALA ALA F . n 
F 1 200 TYR 200 192 192 TYR TYR F . n 
F 1 201 GLU 201 193 193 GLU GLU F . n 
F 1 202 ASP 202 194 194 ASP ASP F . n 
F 1 203 VAL 203 195 195 VAL VAL F . n 
F 1 204 GLU 204 196 196 GLU GLU F . n 
F 1 205 VAL 205 197 197 VAL VAL F . n 
F 1 206 SER 206 198 198 SER SER F . n 
F 1 207 LEU 207 199 199 LEU LEU F . n 
F 1 208 ASN 208 200 200 ASN ASN F . n 
F 1 209 PHE 209 201 201 PHE PHE F . n 
F 1 210 ARG 210 202 202 ARG ARG F . n 
F 1 211 LYS 211 203 203 LYS LYS F . n 
F 1 212 LYS 212 204 204 LYS LYS F . n 
F 1 213 GLY 213 205 205 GLY GLY F . n 
F 1 214 ARG 214 206 ?   ?   ?   F . n 
F 1 215 SER 215 207 ?   ?   ?   F . n 
F 1 216 GLU 216 208 ?   ?   ?   F . n 
F 1 217 ILE 217 209 ?   ?   ?   F . n 
G 1 1   ASP 1   -7  -7  ASP ASP G . n 
G 1 2   TYR 2   -6  -6  TYR TYR G . n 
G 1 3   LYS 3   -5  -5  LYS LYS G . n 
G 1 4   ASP 4   -4  -4  ASP ASP G . n 
G 1 5   ASP 5   -3  -3  ASP ASP G . n 
G 1 6   ASP 6   -2  -2  ASP ASP G . n 
G 1 7   ASP 7   -1  -1  ASP ASP G . n 
G 1 8   LYS 8   0   0   LYS LYS G . n 
G 1 9   LEU 9   1   1   LEU LEU G . n 
G 1 10  ASP 10  2   2   ASP ASP G . n 
G 1 11  ARG 11  3   3   ARG ARG G . n 
G 1 12  ALA 12  4   4   ALA ALA G . n 
G 1 13  ASP 13  5   5   ASP ASP G . n 
G 1 14  ILE 14  6   6   ILE ILE G . n 
G 1 15  LEU 15  7   7   LEU LEU G . n 
G 1 16  TYR 16  8   8   TYR TYR G . n 
G 1 17  ASN 17  9   9   ASN ASN G . n 
G 1 18  ILE 18  10  10  ILE ILE G . n 
G 1 19  ARG 19  11  11  ARG ARG G . n 
G 1 20  GLN 20  12  12  GLN GLN G . n 
G 1 21  THR 21  13  13  THR THR G . n 
G 1 22  SER 22  14  14  SER SER G . n 
G 1 23  ARG 23  15  15  ARG ARG G . n 
G 1 24  PRO 24  16  16  PRO PRO G . n 
G 1 25  ASP 25  17  17  ASP ASP G . n 
G 1 26  VAL 26  18  18  VAL VAL G . n 
G 1 27  ILE 27  19  19  ILE ILE G . n 
G 1 28  PRO 28  20  20  PRO PRO G . n 
G 1 29  THR 29  21  21  THR THR G . n 
G 1 30  GLN 30  22  22  GLN GLN G . n 
G 1 31  ARG 31  23  23  ARG ARG G . n 
G 1 32  ASP 32  24  24  ASP ASP G . n 
G 1 33  ARG 33  25  25  ARG ARG G . n 
G 1 34  PRO 34  26  26  PRO PRO G . n 
G 1 35  VAL 35  27  27  VAL VAL G . n 
G 1 36  ALA 36  28  28  ALA ALA G . n 
G 1 37  VAL 37  29  29  VAL VAL G . n 
G 1 38  SER 38  30  30  SER SER G . n 
G 1 39  VAL 39  31  31  VAL VAL G . n 
G 1 40  SER 40  32  32  SER SER G . n 
G 1 41  LEU 41  33  33  LEU LEU G . n 
G 1 42  LYS 42  34  34  LYS LYS G . n 
G 1 43  PHE 43  35  35  PHE PHE G . n 
G 1 44  ILE 44  36  36  ILE ILE G . n 
G 1 45  ASN 45  37  37  ASN ASN G . n 
G 1 46  ILE 46  38  38  ILE ILE G . n 
G 1 47  LEU 47  39  39  LEU LEU G . n 
G 1 48  GLU 48  40  40  GLU GLU G . n 
G 1 49  VAL 49  41  41  VAL VAL G . n 
G 1 50  ASN 50  42  42  ASN ASN G . n 
G 1 51  GLU 51  43  43  GLU GLU G . n 
G 1 52  ILE 52  44  44  ILE ILE G . n 
G 1 53  THR 53  45  45  THR THR G . n 
G 1 54  ASN 54  46  46  ASN ASN G . n 
G 1 55  GLU 55  47  47  GLU GLU G . n 
G 1 56  VAL 56  48  48  VAL VAL G . n 
G 1 57  ASP 57  49  49  ASP ASP G . n 
G 1 58  VAL 58  50  50  VAL VAL G . n 
G 1 59  VAL 59  51  51  VAL VAL G . n 
G 1 60  PHE 60  52  52  PHE PHE G . n 
G 1 61  TRP 61  53  53  TRP TRP G . n 
G 1 62  GLN 62  54  54  GLN GLN G . n 
G 1 63  GLN 63  55  55  GLN GLN G . n 
G 1 64  THR 64  56  56  THR THR G . n 
G 1 65  THR 65  57  57  THR THR G . n 
G 1 66  TRP 66  58  58  TRP TRP G . n 
G 1 67  SER 67  59  59  SER SER G . n 
G 1 68  ASP 68  60  60  ASP ASP G . n 
G 1 69  ARG 69  61  61  ARG ARG G . n 
G 1 70  THR 70  62  62  THR THR G . n 
G 1 71  LEU 71  63  63  LEU LEU G . n 
G 1 72  ALA 72  64  64  ALA ALA G . n 
G 1 73  TRP 73  65  65  TRP TRP G . n 
G 1 74  ASN 74  66  66  ASN ASN G . n 
G 1 75  SER 75  67  67  SER SER G . n 
G 1 76  SER 76  68  68  SER SER G . n 
G 1 77  HIS 77  69  69  HIS HIS G . n 
G 1 78  SER 78  70  70  SER SER G . n 
G 1 79  PRO 79  71  71  PRO PRO G . n 
G 1 80  ASP 80  72  72  ASP ASP G . n 
G 1 81  GLN 81  73  73  GLN GLN G . n 
G 1 82  VAL 82  74  74  VAL VAL G . n 
G 1 83  SER 83  75  75  SER SER G . n 
G 1 84  VAL 84  76  76  VAL VAL G . n 
G 1 85  PRO 85  77  77  PRO PRO G . n 
G 1 86  ILE 86  78  78  ILE ILE G . n 
G 1 87  SER 87  79  79  SER SER G . n 
G 1 88  SER 88  80  80  SER SER G . n 
G 1 89  LEU 89  81  81  LEU LEU G . n 
G 1 90  TRP 90  82  82  TRP TRP G . n 
G 1 91  VAL 91  83  83  VAL VAL G . n 
G 1 92  PRO 92  84  84  PRO PRO G . n 
G 1 93  ASP 93  85  85  ASP ASP G . n 
G 1 94  LEU 94  86  86  LEU LEU G . n 
G 1 95  ALA 95  87  87  ALA ALA G . n 
G 1 96  ALA 96  88  88  ALA ALA G . n 
G 1 97  TYR 97  89  89  TYR TYR G . n 
G 1 98  ASN 98  90  90  ASN ASN G . n 
G 1 99  ALA 99  91  91  ALA ALA G . n 
G 1 100 ILE 100 92  92  ILE ILE G . n 
G 1 101 SER 101 93  93  SER SER G . n 
G 1 102 LYS 102 94  94  LYS LYS G . n 
G 1 103 PRO 103 95  95  PRO PRO G . n 
G 1 104 GLU 104 96  96  GLU GLU G . n 
G 1 105 VAL 105 97  97  VAL VAL G . n 
G 1 106 LEU 106 98  98  LEU LEU G . n 
G 1 107 THR 107 99  99  THR THR G . n 
G 1 108 PRO 108 100 100 PRO PRO G . n 
G 1 109 GLN 109 101 101 GLN GLN G . n 
G 1 110 LEU 110 102 102 LEU LEU G . n 
G 1 111 ALA 111 103 103 ALA ALA G . n 
G 1 112 ARG 112 104 104 ARG ARG G . n 
G 1 113 VAL 113 105 105 VAL VAL G . n 
G 1 114 VAL 114 106 106 VAL VAL G . n 
G 1 115 SER 115 107 107 SER SER G . n 
G 1 116 ASP 116 108 108 ASP ASP G . n 
G 1 117 GLY 117 109 109 GLY GLY G . n 
G 1 118 GLU 118 110 110 GLU GLU G . n 
G 1 119 VAL 119 111 111 VAL VAL G . n 
G 1 120 LEU 120 112 112 LEU LEU G . n 
G 1 121 TYR 121 113 113 TYR TYR G . n 
G 1 122 MET 122 114 114 MET MET G . n 
G 1 123 PRO 123 115 115 PRO PRO G . n 
G 1 124 SER 124 116 116 SER SER G . n 
G 1 125 ILE 125 117 117 ILE ILE G . n 
G 1 126 ARG 126 118 118 ARG ARG G . n 
G 1 127 GLN 127 119 119 GLN GLN G . n 
G 1 128 ARG 128 120 120 ARG ARG G . n 
G 1 129 PHE 129 121 121 PHE PHE G . n 
G 1 130 SER 130 122 122 SER SER G . n 
G 1 131 CYS 131 123 123 CYS CYS G . n 
G 1 132 ASP 132 124 124 ASP ASP G . n 
G 1 133 VAL 133 125 125 VAL VAL G . n 
G 1 134 SER 134 126 126 SER SER G . n 
G 1 135 GLY 135 127 127 GLY GLY G . n 
G 1 136 VAL 136 128 128 VAL VAL G . n 
G 1 137 ASP 137 129 129 ASP ASP G . n 
G 1 138 THR 138 130 130 THR THR G . n 
G 1 139 GLU 139 131 131 GLU GLU G . n 
G 1 140 SER 140 132 132 SER SER G . n 
G 1 141 GLY 141 133 133 GLY GLY G . n 
G 1 142 ALA 142 134 134 ALA ALA G . n 
G 1 143 THR 143 135 135 THR THR G . n 
G 1 144 CYS 144 136 136 CYS CYS G . n 
G 1 145 ARG 145 137 137 ARG ARG G . n 
G 1 146 ILE 146 138 138 ILE ILE G . n 
G 1 147 LYS 147 139 139 LYS LYS G . n 
G 1 148 ILE 148 140 140 ILE ILE G . n 
G 1 149 GLY 149 141 141 GLY GLY G . n 
G 1 150 SER 150 142 142 SER SER G . n 
G 1 151 TRP 151 143 143 TRP TRP G . n 
G 1 152 THR 152 144 144 THR THR G . n 
G 1 153 HIS 153 145 145 HIS HIS G . n 
G 1 154 HIS 154 146 146 HIS HIS G . n 
G 1 155 SER 155 147 147 SER SER G . n 
G 1 156 ARG 156 148 148 ARG ARG G . n 
G 1 157 GLU 157 149 149 GLU GLU G . n 
G 1 158 ILE 158 150 150 ILE ILE G . n 
G 1 159 SER 159 151 151 SER SER G . n 
G 1 160 VAL 160 152 152 VAL VAL G . n 
G 1 161 ASP 161 153 153 ASP ASP G . n 
G 1 162 PRO 162 154 154 PRO PRO G . n 
G 1 163 THR 163 155 155 THR THR G . n 
G 1 164 THR 164 156 156 THR THR G . n 
G 1 165 GLU 165 157 157 GLU GLU G . n 
G 1 166 ASN 166 158 158 ASN ASN G . n 
G 1 167 SER 167 159 159 SER SER G . n 
G 1 168 ASP 168 160 ?   ?   ?   G . n 
G 1 169 ASP 169 161 ?   ?   ?   G . n 
G 1 170 SER 170 162 162 SER SER G . n 
G 1 171 GLU 171 163 163 GLU GLU G . n 
G 1 172 TYR 172 164 164 TYR TYR G . n 
G 1 173 PHE 173 165 165 PHE PHE G . n 
G 1 174 SER 174 166 166 SER SER G . n 
G 1 175 GLN 175 167 167 GLN GLN G . n 
G 1 176 TYR 176 168 168 TYR TYR G . n 
G 1 177 SER 177 169 169 SER SER G . n 
G 1 178 ARG 178 170 170 ARG ARG G . n 
G 1 179 PHE 179 171 171 PHE PHE G . n 
G 1 180 GLU 180 172 172 GLU GLU G . n 
G 1 181 ILE 181 173 173 ILE ILE G . n 
G 1 182 LEU 182 174 174 LEU LEU G . n 
G 1 183 ASP 183 175 175 ASP ASP G . n 
G 1 184 VAL 184 176 176 VAL VAL G . n 
G 1 185 THR 185 177 177 THR THR G . n 
G 1 186 GLN 186 178 178 GLN GLN G . n 
G 1 187 LYS 187 179 179 LYS LYS G . n 
G 1 188 LYS 188 180 180 LYS LYS G . n 
G 1 189 ASN 189 181 181 ASN ASN G . n 
G 1 190 SER 190 182 182 SER SER G . n 
G 1 191 VAL 191 183 183 VAL VAL G . n 
G 1 192 THR 192 184 184 THR THR G . n 
G 1 193 TYR 193 185 185 TYR TYR G . n 
G 1 194 SER 194 186 ?   ?   ?   G . n 
G 1 195 CYS 195 187 ?   ?   ?   G . n 
G 1 196 CYS 196 188 ?   ?   ?   G . n 
G 1 197 PRO 197 189 189 PRO PRO G . n 
G 1 198 GLU 198 190 190 GLU GLU G . n 
G 1 199 ALA 199 191 191 ALA ALA G . n 
G 1 200 TYR 200 192 192 TYR TYR G . n 
G 1 201 GLU 201 193 193 GLU GLU G . n 
G 1 202 ASP 202 194 194 ASP ASP G . n 
G 1 203 VAL 203 195 195 VAL VAL G . n 
G 1 204 GLU 204 196 196 GLU GLU G . n 
G 1 205 VAL 205 197 197 VAL VAL G . n 
G 1 206 SER 206 198 198 SER SER G . n 
G 1 207 LEU 207 199 199 LEU LEU G . n 
G 1 208 ASN 208 200 200 ASN ASN G . n 
G 1 209 PHE 209 201 201 PHE PHE G . n 
G 1 210 ARG 210 202 202 ARG ARG G . n 
G 1 211 LYS 211 203 203 LYS LYS G . n 
G 1 212 LYS 212 204 204 LYS LYS G . n 
G 1 213 GLY 213 205 205 GLY GLY G . n 
G 1 214 ARG 214 206 ?   ?   ?   G . n 
G 1 215 SER 215 207 ?   ?   ?   G . n 
G 1 216 GLU 216 208 ?   ?   ?   G . n 
G 1 217 ILE 217 209 ?   ?   ?   G . n 
H 1 1   ASP 1   -7  -7  ASP ASP H . n 
H 1 2   TYR 2   -6  -6  TYR TYR H . n 
H 1 3   LYS 3   -5  -5  LYS LYS H . n 
H 1 4   ASP 4   -4  -4  ASP ASP H . n 
H 1 5   ASP 5   -3  -3  ASP ASP H . n 
H 1 6   ASP 6   -2  -2  ASP ASP H . n 
H 1 7   ASP 7   -1  -1  ASP ASP H . n 
H 1 8   LYS 8   0   0   LYS LYS H . n 
H 1 9   LEU 9   1   1   LEU LEU H . n 
H 1 10  ASP 10  2   2   ASP ASP H . n 
H 1 11  ARG 11  3   3   ARG ARG H . n 
H 1 12  ALA 12  4   4   ALA ALA H . n 
H 1 13  ASP 13  5   5   ASP ASP H . n 
H 1 14  ILE 14  6   6   ILE ILE H . n 
H 1 15  LEU 15  7   7   LEU LEU H . n 
H 1 16  TYR 16  8   8   TYR TYR H . n 
H 1 17  ASN 17  9   9   ASN ASN H . n 
H 1 18  ILE 18  10  10  ILE ILE H . n 
H 1 19  ARG 19  11  11  ARG ARG H . n 
H 1 20  GLN 20  12  12  GLN GLN H . n 
H 1 21  THR 21  13  13  THR THR H . n 
H 1 22  SER 22  14  14  SER SER H . n 
H 1 23  ARG 23  15  15  ARG ARG H . n 
H 1 24  PRO 24  16  16  PRO PRO H . n 
H 1 25  ASP 25  17  17  ASP ASP H . n 
H 1 26  VAL 26  18  18  VAL VAL H . n 
H 1 27  ILE 27  19  19  ILE ILE H . n 
H 1 28  PRO 28  20  20  PRO PRO H . n 
H 1 29  THR 29  21  21  THR THR H . n 
H 1 30  GLN 30  22  22  GLN GLN H . n 
H 1 31  ARG 31  23  23  ARG ARG H . n 
H 1 32  ASP 32  24  24  ASP ASP H . n 
H 1 33  ARG 33  25  25  ARG ARG H . n 
H 1 34  PRO 34  26  26  PRO PRO H . n 
H 1 35  VAL 35  27  27  VAL VAL H . n 
H 1 36  ALA 36  28  28  ALA ALA H . n 
H 1 37  VAL 37  29  29  VAL VAL H . n 
H 1 38  SER 38  30  30  SER SER H . n 
H 1 39  VAL 39  31  31  VAL VAL H . n 
H 1 40  SER 40  32  32  SER SER H . n 
H 1 41  LEU 41  33  33  LEU LEU H . n 
H 1 42  LYS 42  34  34  LYS LYS H . n 
H 1 43  PHE 43  35  35  PHE PHE H . n 
H 1 44  ILE 44  36  36  ILE ILE H . n 
H 1 45  ASN 45  37  37  ASN ASN H . n 
H 1 46  ILE 46  38  38  ILE ILE H . n 
H 1 47  LEU 47  39  39  LEU LEU H . n 
H 1 48  GLU 48  40  40  GLU GLU H . n 
H 1 49  VAL 49  41  41  VAL VAL H . n 
H 1 50  ASN 50  42  42  ASN ASN H . n 
H 1 51  GLU 51  43  43  GLU GLU H . n 
H 1 52  ILE 52  44  44  ILE ILE H . n 
H 1 53  THR 53  45  45  THR THR H . n 
H 1 54  ASN 54  46  46  ASN ASN H . n 
H 1 55  GLU 55  47  47  GLU GLU H . n 
H 1 56  VAL 56  48  48  VAL VAL H . n 
H 1 57  ASP 57  49  49  ASP ASP H . n 
H 1 58  VAL 58  50  50  VAL VAL H . n 
H 1 59  VAL 59  51  51  VAL VAL H . n 
H 1 60  PHE 60  52  52  PHE PHE H . n 
H 1 61  TRP 61  53  53  TRP TRP H . n 
H 1 62  GLN 62  54  54  GLN GLN H . n 
H 1 63  GLN 63  55  55  GLN GLN H . n 
H 1 64  THR 64  56  56  THR THR H . n 
H 1 65  THR 65  57  57  THR THR H . n 
H 1 66  TRP 66  58  58  TRP TRP H . n 
H 1 67  SER 67  59  59  SER SER H . n 
H 1 68  ASP 68  60  60  ASP ASP H . n 
H 1 69  ARG 69  61  61  ARG ARG H . n 
H 1 70  THR 70  62  62  THR THR H . n 
H 1 71  LEU 71  63  63  LEU LEU H . n 
H 1 72  ALA 72  64  64  ALA ALA H . n 
H 1 73  TRP 73  65  65  TRP TRP H . n 
H 1 74  ASN 74  66  66  ASN ASN H . n 
H 1 75  SER 75  67  67  SER SER H . n 
H 1 76  SER 76  68  68  SER SER H . n 
H 1 77  HIS 77  69  69  HIS HIS H . n 
H 1 78  SER 78  70  70  SER SER H . n 
H 1 79  PRO 79  71  71  PRO PRO H . n 
H 1 80  ASP 80  72  72  ASP ASP H . n 
H 1 81  GLN 81  73  73  GLN GLN H . n 
H 1 82  VAL 82  74  74  VAL VAL H . n 
H 1 83  SER 83  75  75  SER SER H . n 
H 1 84  VAL 84  76  76  VAL VAL H . n 
H 1 85  PRO 85  77  77  PRO PRO H . n 
H 1 86  ILE 86  78  78  ILE ILE H . n 
H 1 87  SER 87  79  79  SER SER H . n 
H 1 88  SER 88  80  80  SER SER H . n 
H 1 89  LEU 89  81  81  LEU LEU H . n 
H 1 90  TRP 90  82  82  TRP TRP H . n 
H 1 91  VAL 91  83  83  VAL VAL H . n 
H 1 92  PRO 92  84  84  PRO PRO H . n 
H 1 93  ASP 93  85  85  ASP ASP H . n 
H 1 94  LEU 94  86  86  LEU LEU H . n 
H 1 95  ALA 95  87  87  ALA ALA H . n 
H 1 96  ALA 96  88  88  ALA ALA H . n 
H 1 97  TYR 97  89  89  TYR TYR H . n 
H 1 98  ASN 98  90  90  ASN ASN H . n 
H 1 99  ALA 99  91  91  ALA ALA H . n 
H 1 100 ILE 100 92  92  ILE ILE H . n 
H 1 101 SER 101 93  93  SER SER H . n 
H 1 102 LYS 102 94  94  LYS LYS H . n 
H 1 103 PRO 103 95  95  PRO PRO H . n 
H 1 104 GLU 104 96  96  GLU GLU H . n 
H 1 105 VAL 105 97  97  VAL VAL H . n 
H 1 106 LEU 106 98  98  LEU LEU H . n 
H 1 107 THR 107 99  99  THR THR H . n 
H 1 108 PRO 108 100 100 PRO PRO H . n 
H 1 109 GLN 109 101 101 GLN GLN H . n 
H 1 110 LEU 110 102 102 LEU LEU H . n 
H 1 111 ALA 111 103 103 ALA ALA H . n 
H 1 112 ARG 112 104 104 ARG ARG H . n 
H 1 113 VAL 113 105 105 VAL VAL H . n 
H 1 114 VAL 114 106 106 VAL VAL H . n 
H 1 115 SER 115 107 107 SER SER H . n 
H 1 116 ASP 116 108 108 ASP ASP H . n 
H 1 117 GLY 117 109 109 GLY GLY H . n 
H 1 118 GLU 118 110 110 GLU GLU H . n 
H 1 119 VAL 119 111 111 VAL VAL H . n 
H 1 120 LEU 120 112 112 LEU LEU H . n 
H 1 121 TYR 121 113 113 TYR TYR H . n 
H 1 122 MET 122 114 114 MET MET H . n 
H 1 123 PRO 123 115 115 PRO PRO H . n 
H 1 124 SER 124 116 116 SER SER H . n 
H 1 125 ILE 125 117 117 ILE ILE H . n 
H 1 126 ARG 126 118 118 ARG ARG H . n 
H 1 127 GLN 127 119 119 GLN GLN H . n 
H 1 128 ARG 128 120 120 ARG ARG H . n 
H 1 129 PHE 129 121 121 PHE PHE H . n 
H 1 130 SER 130 122 122 SER SER H . n 
H 1 131 CYS 131 123 123 CYS CYS H . n 
H 1 132 ASP 132 124 124 ASP ASP H . n 
H 1 133 VAL 133 125 125 VAL VAL H . n 
H 1 134 SER 134 126 126 SER SER H . n 
H 1 135 GLY 135 127 127 GLY GLY H . n 
H 1 136 VAL 136 128 128 VAL VAL H . n 
H 1 137 ASP 137 129 129 ASP ASP H . n 
H 1 138 THR 138 130 130 THR THR H . n 
H 1 139 GLU 139 131 131 GLU GLU H . n 
H 1 140 SER 140 132 132 SER SER H . n 
H 1 141 GLY 141 133 133 GLY GLY H . n 
H 1 142 ALA 142 134 134 ALA ALA H . n 
H 1 143 THR 143 135 135 THR THR H . n 
H 1 144 CYS 144 136 136 CYS CYS H . n 
H 1 145 ARG 145 137 137 ARG ARG H . n 
H 1 146 ILE 146 138 138 ILE ILE H . n 
H 1 147 LYS 147 139 139 LYS LYS H . n 
H 1 148 ILE 148 140 140 ILE ILE H . n 
H 1 149 GLY 149 141 141 GLY GLY H . n 
H 1 150 SER 150 142 142 SER SER H . n 
H 1 151 TRP 151 143 143 TRP TRP H . n 
H 1 152 THR 152 144 144 THR THR H . n 
H 1 153 HIS 153 145 145 HIS HIS H . n 
H 1 154 HIS 154 146 146 HIS HIS H . n 
H 1 155 SER 155 147 147 SER SER H . n 
H 1 156 ARG 156 148 148 ARG ARG H . n 
H 1 157 GLU 157 149 149 GLU GLU H . n 
H 1 158 ILE 158 150 150 ILE ILE H . n 
H 1 159 SER 159 151 151 SER SER H . n 
H 1 160 VAL 160 152 152 VAL VAL H . n 
H 1 161 ASP 161 153 153 ASP ASP H . n 
H 1 162 PRO 162 154 154 PRO PRO H . n 
H 1 163 THR 163 155 155 THR THR H . n 
H 1 164 THR 164 156 ?   ?   ?   H . n 
H 1 165 GLU 165 157 ?   ?   ?   H . n 
H 1 166 ASN 166 158 ?   ?   ?   H . n 
H 1 167 SER 167 159 ?   ?   ?   H . n 
H 1 168 ASP 168 160 160 ASP ASP H . n 
H 1 169 ASP 169 161 161 ASP ASP H . n 
H 1 170 SER 170 162 162 SER SER H . n 
H 1 171 GLU 171 163 163 GLU GLU H . n 
H 1 172 TYR 172 164 164 TYR TYR H . n 
H 1 173 PHE 173 165 165 PHE PHE H . n 
H 1 174 SER 174 166 166 SER SER H . n 
H 1 175 GLN 175 167 167 GLN GLN H . n 
H 1 176 TYR 176 168 168 TYR TYR H . n 
H 1 177 SER 177 169 169 SER SER H . n 
H 1 178 ARG 178 170 170 ARG ARG H . n 
H 1 179 PHE 179 171 171 PHE PHE H . n 
H 1 180 GLU 180 172 172 GLU GLU H . n 
H 1 181 ILE 181 173 173 ILE ILE H . n 
H 1 182 LEU 182 174 174 LEU LEU H . n 
H 1 183 ASP 183 175 175 ASP ASP H . n 
H 1 184 VAL 184 176 176 VAL VAL H . n 
H 1 185 THR 185 177 177 THR THR H . n 
H 1 186 GLN 186 178 178 GLN GLN H . n 
H 1 187 LYS 187 179 179 LYS LYS H . n 
H 1 188 LYS 188 180 180 LYS LYS H . n 
H 1 189 ASN 189 181 181 ASN ASN H . n 
H 1 190 SER 190 182 182 SER SER H . n 
H 1 191 VAL 191 183 183 VAL VAL H . n 
H 1 192 THR 192 184 184 THR THR H . n 
H 1 193 TYR 193 185 185 TYR TYR H . n 
H 1 194 SER 194 186 186 SER SER H . n 
H 1 195 CYS 195 187 ?   ?   ?   H . n 
H 1 196 CYS 196 188 ?   ?   ?   H . n 
H 1 197 PRO 197 189 189 PRO PRO H . n 
H 1 198 GLU 198 190 190 GLU GLU H . n 
H 1 199 ALA 199 191 191 ALA ALA H . n 
H 1 200 TYR 200 192 192 TYR TYR H . n 
H 1 201 GLU 201 193 193 GLU GLU H . n 
H 1 202 ASP 202 194 194 ASP ASP H . n 
H 1 203 VAL 203 195 195 VAL VAL H . n 
H 1 204 GLU 204 196 196 GLU GLU H . n 
H 1 205 VAL 205 197 197 VAL VAL H . n 
H 1 206 SER 206 198 198 SER SER H . n 
H 1 207 LEU 207 199 199 LEU LEU H . n 
H 1 208 ASN 208 200 200 ASN ASN H . n 
H 1 209 PHE 209 201 201 PHE PHE H . n 
H 1 210 ARG 210 202 202 ARG ARG H . n 
H 1 211 LYS 211 203 203 LYS LYS H . n 
H 1 212 LYS 212 204 204 LYS LYS H . n 
H 1 213 GLY 213 205 205 GLY GLY H . n 
H 1 214 ARG 214 206 ?   ?   ?   H . n 
H 1 215 SER 215 207 ?   ?   ?   H . n 
H 1 216 GLU 216 208 ?   ?   ?   H . n 
H 1 217 ILE 217 209 ?   ?   ?   H . n 
I 1 1   ASP 1   -7  -7  ASP ASP I . n 
I 1 2   TYR 2   -6  -6  TYR TYR I . n 
I 1 3   LYS 3   -5  -5  LYS LYS I . n 
I 1 4   ASP 4   -4  -4  ASP ASP I . n 
I 1 5   ASP 5   -3  -3  ASP ASP I . n 
I 1 6   ASP 6   -2  -2  ASP ASP I . n 
I 1 7   ASP 7   -1  -1  ASP ASP I . n 
I 1 8   LYS 8   0   0   LYS LYS I . n 
I 1 9   LEU 9   1   1   LEU LEU I . n 
I 1 10  ASP 10  2   2   ASP ASP I . n 
I 1 11  ARG 11  3   3   ARG ARG I . n 
I 1 12  ALA 12  4   4   ALA ALA I . n 
I 1 13  ASP 13  5   5   ASP ASP I . n 
I 1 14  ILE 14  6   6   ILE ILE I . n 
I 1 15  LEU 15  7   7   LEU LEU I . n 
I 1 16  TYR 16  8   8   TYR TYR I . n 
I 1 17  ASN 17  9   9   ASN ASN I . n 
I 1 18  ILE 18  10  10  ILE ILE I . n 
I 1 19  ARG 19  11  11  ARG ARG I . n 
I 1 20  GLN 20  12  12  GLN GLN I . n 
I 1 21  THR 21  13  13  THR THR I . n 
I 1 22  SER 22  14  14  SER SER I . n 
I 1 23  ARG 23  15  15  ARG ARG I . n 
I 1 24  PRO 24  16  16  PRO PRO I . n 
I 1 25  ASP 25  17  17  ASP ASP I . n 
I 1 26  VAL 26  18  18  VAL VAL I . n 
I 1 27  ILE 27  19  19  ILE ILE I . n 
I 1 28  PRO 28  20  20  PRO PRO I . n 
I 1 29  THR 29  21  21  THR THR I . n 
I 1 30  GLN 30  22  22  GLN GLN I . n 
I 1 31  ARG 31  23  23  ARG ARG I . n 
I 1 32  ASP 32  24  24  ASP ASP I . n 
I 1 33  ARG 33  25  25  ARG ARG I . n 
I 1 34  PRO 34  26  26  PRO PRO I . n 
I 1 35  VAL 35  27  27  VAL VAL I . n 
I 1 36  ALA 36  28  28  ALA ALA I . n 
I 1 37  VAL 37  29  29  VAL VAL I . n 
I 1 38  SER 38  30  30  SER SER I . n 
I 1 39  VAL 39  31  31  VAL VAL I . n 
I 1 40  SER 40  32  32  SER SER I . n 
I 1 41  LEU 41  33  33  LEU LEU I . n 
I 1 42  LYS 42  34  34  LYS LYS I . n 
I 1 43  PHE 43  35  35  PHE PHE I . n 
I 1 44  ILE 44  36  36  ILE ILE I . n 
I 1 45  ASN 45  37  37  ASN ASN I . n 
I 1 46  ILE 46  38  38  ILE ILE I . n 
I 1 47  LEU 47  39  39  LEU LEU I . n 
I 1 48  GLU 48  40  40  GLU GLU I . n 
I 1 49  VAL 49  41  41  VAL VAL I . n 
I 1 50  ASN 50  42  42  ASN ASN I . n 
I 1 51  GLU 51  43  43  GLU GLU I . n 
I 1 52  ILE 52  44  44  ILE ILE I . n 
I 1 53  THR 53  45  45  THR THR I . n 
I 1 54  ASN 54  46  46  ASN ASN I . n 
I 1 55  GLU 55  47  47  GLU GLU I . n 
I 1 56  VAL 56  48  48  VAL VAL I . n 
I 1 57  ASP 57  49  49  ASP ASP I . n 
I 1 58  VAL 58  50  50  VAL VAL I . n 
I 1 59  VAL 59  51  51  VAL VAL I . n 
I 1 60  PHE 60  52  52  PHE PHE I . n 
I 1 61  TRP 61  53  53  TRP TRP I . n 
I 1 62  GLN 62  54  54  GLN GLN I . n 
I 1 63  GLN 63  55  55  GLN GLN I . n 
I 1 64  THR 64  56  56  THR THR I . n 
I 1 65  THR 65  57  57  THR THR I . n 
I 1 66  TRP 66  58  58  TRP TRP I . n 
I 1 67  SER 67  59  59  SER SER I . n 
I 1 68  ASP 68  60  60  ASP ASP I . n 
I 1 69  ARG 69  61  61  ARG ARG I . n 
I 1 70  THR 70  62  62  THR THR I . n 
I 1 71  LEU 71  63  63  LEU LEU I . n 
I 1 72  ALA 72  64  64  ALA ALA I . n 
I 1 73  TRP 73  65  65  TRP TRP I . n 
I 1 74  ASN 74  66  66  ASN ASN I . n 
I 1 75  SER 75  67  67  SER SER I . n 
I 1 76  SER 76  68  68  SER SER I . n 
I 1 77  HIS 77  69  69  HIS HIS I . n 
I 1 78  SER 78  70  70  SER SER I . n 
I 1 79  PRO 79  71  71  PRO PRO I . n 
I 1 80  ASP 80  72  72  ASP ASP I . n 
I 1 81  GLN 81  73  73  GLN GLN I . n 
I 1 82  VAL 82  74  74  VAL VAL I . n 
I 1 83  SER 83  75  75  SER SER I . n 
I 1 84  VAL 84  76  76  VAL VAL I . n 
I 1 85  PRO 85  77  77  PRO PRO I . n 
I 1 86  ILE 86  78  78  ILE ILE I . n 
I 1 87  SER 87  79  79  SER SER I . n 
I 1 88  SER 88  80  80  SER SER I . n 
I 1 89  LEU 89  81  81  LEU LEU I . n 
I 1 90  TRP 90  82  82  TRP TRP I . n 
I 1 91  VAL 91  83  83  VAL VAL I . n 
I 1 92  PRO 92  84  84  PRO PRO I . n 
I 1 93  ASP 93  85  85  ASP ASP I . n 
I 1 94  LEU 94  86  86  LEU LEU I . n 
I 1 95  ALA 95  87  87  ALA ALA I . n 
I 1 96  ALA 96  88  88  ALA ALA I . n 
I 1 97  TYR 97  89  89  TYR TYR I . n 
I 1 98  ASN 98  90  90  ASN ASN I . n 
I 1 99  ALA 99  91  91  ALA ALA I . n 
I 1 100 ILE 100 92  92  ILE ILE I . n 
I 1 101 SER 101 93  93  SER SER I . n 
I 1 102 LYS 102 94  94  LYS LYS I . n 
I 1 103 PRO 103 95  95  PRO PRO I . n 
I 1 104 GLU 104 96  96  GLU GLU I . n 
I 1 105 VAL 105 97  97  VAL VAL I . n 
I 1 106 LEU 106 98  98  LEU LEU I . n 
I 1 107 THR 107 99  99  THR THR I . n 
I 1 108 PRO 108 100 100 PRO PRO I . n 
I 1 109 GLN 109 101 101 GLN GLN I . n 
I 1 110 LEU 110 102 102 LEU LEU I . n 
I 1 111 ALA 111 103 103 ALA ALA I . n 
I 1 112 ARG 112 104 104 ARG ARG I . n 
I 1 113 VAL 113 105 105 VAL VAL I . n 
I 1 114 VAL 114 106 106 VAL VAL I . n 
I 1 115 SER 115 107 107 SER SER I . n 
I 1 116 ASP 116 108 108 ASP ASP I . n 
I 1 117 GLY 117 109 109 GLY GLY I . n 
I 1 118 GLU 118 110 110 GLU GLU I . n 
I 1 119 VAL 119 111 111 VAL VAL I . n 
I 1 120 LEU 120 112 112 LEU LEU I . n 
I 1 121 TYR 121 113 113 TYR TYR I . n 
I 1 122 MET 122 114 114 MET MET I . n 
I 1 123 PRO 123 115 115 PRO PRO I . n 
I 1 124 SER 124 116 116 SER SER I . n 
I 1 125 ILE 125 117 117 ILE ILE I . n 
I 1 126 ARG 126 118 118 ARG ARG I . n 
I 1 127 GLN 127 119 119 GLN GLN I . n 
I 1 128 ARG 128 120 120 ARG ARG I . n 
I 1 129 PHE 129 121 121 PHE PHE I . n 
I 1 130 SER 130 122 122 SER SER I . n 
I 1 131 CYS 131 123 123 CYS CYS I . n 
I 1 132 ASP 132 124 124 ASP ASP I . n 
I 1 133 VAL 133 125 125 VAL VAL I . n 
I 1 134 SER 134 126 126 SER SER I . n 
I 1 135 GLY 135 127 127 GLY GLY I . n 
I 1 136 VAL 136 128 128 VAL VAL I . n 
I 1 137 ASP 137 129 129 ASP ASP I . n 
I 1 138 THR 138 130 130 THR THR I . n 
I 1 139 GLU 139 131 131 GLU GLU I . n 
I 1 140 SER 140 132 132 SER SER I . n 
I 1 141 GLY 141 133 133 GLY GLY I . n 
I 1 142 ALA 142 134 134 ALA ALA I . n 
I 1 143 THR 143 135 135 THR THR I . n 
I 1 144 CYS 144 136 136 CYS CYS I . n 
I 1 145 ARG 145 137 137 ARG ARG I . n 
I 1 146 ILE 146 138 138 ILE ILE I . n 
I 1 147 LYS 147 139 139 LYS LYS I . n 
I 1 148 ILE 148 140 140 ILE ILE I . n 
I 1 149 GLY 149 141 141 GLY GLY I . n 
I 1 150 SER 150 142 142 SER SER I . n 
I 1 151 TRP 151 143 143 TRP TRP I . n 
I 1 152 THR 152 144 144 THR THR I . n 
I 1 153 HIS 153 145 145 HIS HIS I . n 
I 1 154 HIS 154 146 146 HIS HIS I . n 
I 1 155 SER 155 147 147 SER SER I . n 
I 1 156 ARG 156 148 148 ARG ARG I . n 
I 1 157 GLU 157 149 149 GLU GLU I . n 
I 1 158 ILE 158 150 150 ILE ILE I . n 
I 1 159 SER 159 151 151 SER SER I . n 
I 1 160 VAL 160 152 152 VAL VAL I . n 
I 1 161 ASP 161 153 153 ASP ASP I . n 
I 1 162 PRO 162 154 154 PRO PRO I . n 
I 1 163 THR 163 155 155 THR THR I . n 
I 1 164 THR 164 156 ?   ?   ?   I . n 
I 1 165 GLU 165 157 ?   ?   ?   I . n 
I 1 166 ASN 166 158 ?   ?   ?   I . n 
I 1 167 SER 167 159 159 SER SER I . n 
I 1 168 ASP 168 160 160 ASP ASP I . n 
I 1 169 ASP 169 161 161 ASP ASP I . n 
I 1 170 SER 170 162 162 SER SER I . n 
I 1 171 GLU 171 163 163 GLU GLU I . n 
I 1 172 TYR 172 164 164 TYR TYR I . n 
I 1 173 PHE 173 165 165 PHE PHE I . n 
I 1 174 SER 174 166 166 SER SER I . n 
I 1 175 GLN 175 167 167 GLN GLN I . n 
I 1 176 TYR 176 168 168 TYR TYR I . n 
I 1 177 SER 177 169 169 SER SER I . n 
I 1 178 ARG 178 170 170 ARG ARG I . n 
I 1 179 PHE 179 171 171 PHE PHE I . n 
I 1 180 GLU 180 172 172 GLU GLU I . n 
I 1 181 ILE 181 173 173 ILE ILE I . n 
I 1 182 LEU 182 174 174 LEU LEU I . n 
I 1 183 ASP 183 175 175 ASP ASP I . n 
I 1 184 VAL 184 176 176 VAL VAL I . n 
I 1 185 THR 185 177 177 THR THR I . n 
I 1 186 GLN 186 178 178 GLN GLN I . n 
I 1 187 LYS 187 179 179 LYS LYS I . n 
I 1 188 LYS 188 180 180 LYS LYS I . n 
I 1 189 ASN 189 181 181 ASN ASN I . n 
I 1 190 SER 190 182 182 SER SER I . n 
I 1 191 VAL 191 183 183 VAL VAL I . n 
I 1 192 THR 192 184 184 THR THR I . n 
I 1 193 TYR 193 185 185 TYR TYR I . n 
I 1 194 SER 194 186 ?   ?   ?   I . n 
I 1 195 CYS 195 187 ?   ?   ?   I . n 
I 1 196 CYS 196 188 ?   ?   ?   I . n 
I 1 197 PRO 197 189 189 PRO PRO I . n 
I 1 198 GLU 198 190 190 GLU GLU I . n 
I 1 199 ALA 199 191 191 ALA ALA I . n 
I 1 200 TYR 200 192 192 TYR TYR I . n 
I 1 201 GLU 201 193 193 GLU GLU I . n 
I 1 202 ASP 202 194 194 ASP ASP I . n 
I 1 203 VAL 203 195 195 VAL VAL I . n 
I 1 204 GLU 204 196 196 GLU GLU I . n 
I 1 205 VAL 205 197 197 VAL VAL I . n 
I 1 206 SER 206 198 198 SER SER I . n 
I 1 207 LEU 207 199 199 LEU LEU I . n 
I 1 208 ASN 208 200 200 ASN ASN I . n 
I 1 209 PHE 209 201 201 PHE PHE I . n 
I 1 210 ARG 210 202 202 ARG ARG I . n 
I 1 211 LYS 211 203 203 LYS LYS I . n 
I 1 212 LYS 212 204 204 LYS LYS I . n 
I 1 213 GLY 213 205 205 GLY GLY I . n 
I 1 214 ARG 214 206 ?   ?   ?   I . n 
I 1 215 SER 215 207 ?   ?   ?   I . n 
I 1 216 GLU 216 208 ?   ?   ?   I . n 
I 1 217 ILE 217 209 ?   ?   ?   I . n 
J 1 1   ASP 1   -7  -7  ASP ASP J . n 
J 1 2   TYR 2   -6  -6  TYR TYR J . n 
J 1 3   LYS 3   -5  -5  LYS LYS J . n 
J 1 4   ASP 4   -4  -4  ASP ASP J . n 
J 1 5   ASP 5   -3  -3  ASP ASP J . n 
J 1 6   ASP 6   -2  -2  ASP ASP J . n 
J 1 7   ASP 7   -1  -1  ASP ASP J . n 
J 1 8   LYS 8   0   0   LYS LYS J . n 
J 1 9   LEU 9   1   1   LEU LEU J . n 
J 1 10  ASP 10  2   2   ASP ASP J . n 
J 1 11  ARG 11  3   3   ARG ARG J . n 
J 1 12  ALA 12  4   4   ALA ALA J . n 
J 1 13  ASP 13  5   5   ASP ASP J . n 
J 1 14  ILE 14  6   6   ILE ILE J . n 
J 1 15  LEU 15  7   7   LEU LEU J . n 
J 1 16  TYR 16  8   8   TYR TYR J . n 
J 1 17  ASN 17  9   9   ASN ASN J . n 
J 1 18  ILE 18  10  10  ILE ILE J . n 
J 1 19  ARG 19  11  11  ARG ARG J . n 
J 1 20  GLN 20  12  12  GLN GLN J . n 
J 1 21  THR 21  13  13  THR THR J . n 
J 1 22  SER 22  14  14  SER SER J . n 
J 1 23  ARG 23  15  15  ARG ARG J . n 
J 1 24  PRO 24  16  16  PRO PRO J . n 
J 1 25  ASP 25  17  17  ASP ASP J . n 
J 1 26  VAL 26  18  18  VAL VAL J . n 
J 1 27  ILE 27  19  19  ILE ILE J . n 
J 1 28  PRO 28  20  20  PRO PRO J . n 
J 1 29  THR 29  21  21  THR THR J . n 
J 1 30  GLN 30  22  22  GLN GLN J . n 
J 1 31  ARG 31  23  23  ARG ARG J . n 
J 1 32  ASP 32  24  24  ASP ASP J . n 
J 1 33  ARG 33  25  25  ARG ARG J . n 
J 1 34  PRO 34  26  26  PRO PRO J . n 
J 1 35  VAL 35  27  27  VAL VAL J . n 
J 1 36  ALA 36  28  28  ALA ALA J . n 
J 1 37  VAL 37  29  29  VAL VAL J . n 
J 1 38  SER 38  30  30  SER SER J . n 
J 1 39  VAL 39  31  31  VAL VAL J . n 
J 1 40  SER 40  32  32  SER SER J . n 
J 1 41  LEU 41  33  33  LEU LEU J . n 
J 1 42  LYS 42  34  34  LYS LYS J . n 
J 1 43  PHE 43  35  35  PHE PHE J . n 
J 1 44  ILE 44  36  36  ILE ILE J . n 
J 1 45  ASN 45  37  37  ASN ASN J . n 
J 1 46  ILE 46  38  38  ILE ILE J . n 
J 1 47  LEU 47  39  39  LEU LEU J . n 
J 1 48  GLU 48  40  40  GLU GLU J . n 
J 1 49  VAL 49  41  41  VAL VAL J . n 
J 1 50  ASN 50  42  42  ASN ASN J . n 
J 1 51  GLU 51  43  43  GLU GLU J . n 
J 1 52  ILE 52  44  44  ILE ILE J . n 
J 1 53  THR 53  45  45  THR THR J . n 
J 1 54  ASN 54  46  46  ASN ASN J . n 
J 1 55  GLU 55  47  47  GLU GLU J . n 
J 1 56  VAL 56  48  48  VAL VAL J . n 
J 1 57  ASP 57  49  49  ASP ASP J . n 
J 1 58  VAL 58  50  50  VAL VAL J . n 
J 1 59  VAL 59  51  51  VAL VAL J . n 
J 1 60  PHE 60  52  52  PHE PHE J . n 
J 1 61  TRP 61  53  53  TRP TRP J . n 
J 1 62  GLN 62  54  54  GLN GLN J . n 
J 1 63  GLN 63  55  55  GLN GLN J . n 
J 1 64  THR 64  56  56  THR THR J . n 
J 1 65  THR 65  57  57  THR THR J . n 
J 1 66  TRP 66  58  58  TRP TRP J . n 
J 1 67  SER 67  59  59  SER SER J . n 
J 1 68  ASP 68  60  60  ASP ASP J . n 
J 1 69  ARG 69  61  61  ARG ARG J . n 
J 1 70  THR 70  62  62  THR THR J . n 
J 1 71  LEU 71  63  63  LEU LEU J . n 
J 1 72  ALA 72  64  64  ALA ALA J . n 
J 1 73  TRP 73  65  65  TRP TRP J . n 
J 1 74  ASN 74  66  66  ASN ASN J . n 
J 1 75  SER 75  67  67  SER SER J . n 
J 1 76  SER 76  68  68  SER SER J . n 
J 1 77  HIS 77  69  69  HIS HIS J . n 
J 1 78  SER 78  70  70  SER SER J . n 
J 1 79  PRO 79  71  71  PRO PRO J . n 
J 1 80  ASP 80  72  72  ASP ASP J . n 
J 1 81  GLN 81  73  73  GLN GLN J . n 
J 1 82  VAL 82  74  74  VAL VAL J . n 
J 1 83  SER 83  75  75  SER SER J . n 
J 1 84  VAL 84  76  76  VAL VAL J . n 
J 1 85  PRO 85  77  77  PRO PRO J . n 
J 1 86  ILE 86  78  78  ILE ILE J . n 
J 1 87  SER 87  79  79  SER SER J . n 
J 1 88  SER 88  80  80  SER SER J . n 
J 1 89  LEU 89  81  81  LEU LEU J . n 
J 1 90  TRP 90  82  82  TRP TRP J . n 
J 1 91  VAL 91  83  83  VAL VAL J . n 
J 1 92  PRO 92  84  84  PRO PRO J . n 
J 1 93  ASP 93  85  85  ASP ASP J . n 
J 1 94  LEU 94  86  86  LEU LEU J . n 
J 1 95  ALA 95  87  87  ALA ALA J . n 
J 1 96  ALA 96  88  88  ALA ALA J . n 
J 1 97  TYR 97  89  89  TYR TYR J . n 
J 1 98  ASN 98  90  90  ASN ASN J . n 
J 1 99  ALA 99  91  91  ALA ALA J . n 
J 1 100 ILE 100 92  92  ILE ILE J . n 
J 1 101 SER 101 93  93  SER SER J . n 
J 1 102 LYS 102 94  94  LYS LYS J . n 
J 1 103 PRO 103 95  95  PRO PRO J . n 
J 1 104 GLU 104 96  96  GLU GLU J . n 
J 1 105 VAL 105 97  97  VAL VAL J . n 
J 1 106 LEU 106 98  98  LEU LEU J . n 
J 1 107 THR 107 99  99  THR THR J . n 
J 1 108 PRO 108 100 100 PRO PRO J . n 
J 1 109 GLN 109 101 101 GLN GLN J . n 
J 1 110 LEU 110 102 102 LEU LEU J . n 
J 1 111 ALA 111 103 103 ALA ALA J . n 
J 1 112 ARG 112 104 104 ARG ARG J . n 
J 1 113 VAL 113 105 105 VAL VAL J . n 
J 1 114 VAL 114 106 106 VAL VAL J . n 
J 1 115 SER 115 107 107 SER SER J . n 
J 1 116 ASP 116 108 108 ASP ASP J . n 
J 1 117 GLY 117 109 109 GLY GLY J . n 
J 1 118 GLU 118 110 110 GLU GLU J . n 
J 1 119 VAL 119 111 111 VAL VAL J . n 
J 1 120 LEU 120 112 112 LEU LEU J . n 
J 1 121 TYR 121 113 113 TYR TYR J . n 
J 1 122 MET 122 114 114 MET MET J . n 
J 1 123 PRO 123 115 115 PRO PRO J . n 
J 1 124 SER 124 116 116 SER SER J . n 
J 1 125 ILE 125 117 117 ILE ILE J . n 
J 1 126 ARG 126 118 118 ARG ARG J . n 
J 1 127 GLN 127 119 119 GLN GLN J . n 
J 1 128 ARG 128 120 120 ARG ARG J . n 
J 1 129 PHE 129 121 121 PHE PHE J . n 
J 1 130 SER 130 122 122 SER SER J . n 
J 1 131 CYS 131 123 123 CYS CYS J . n 
J 1 132 ASP 132 124 124 ASP ASP J . n 
J 1 133 VAL 133 125 125 VAL VAL J . n 
J 1 134 SER 134 126 126 SER SER J . n 
J 1 135 GLY 135 127 127 GLY GLY J . n 
J 1 136 VAL 136 128 128 VAL VAL J . n 
J 1 137 ASP 137 129 129 ASP ASP J . n 
J 1 138 THR 138 130 130 THR THR J . n 
J 1 139 GLU 139 131 131 GLU GLU J . n 
J 1 140 SER 140 132 132 SER SER J . n 
J 1 141 GLY 141 133 133 GLY GLY J . n 
J 1 142 ALA 142 134 134 ALA ALA J . n 
J 1 143 THR 143 135 135 THR THR J . n 
J 1 144 CYS 144 136 136 CYS CYS J . n 
J 1 145 ARG 145 137 137 ARG ARG J . n 
J 1 146 ILE 146 138 138 ILE ILE J . n 
J 1 147 LYS 147 139 139 LYS LYS J . n 
J 1 148 ILE 148 140 140 ILE ILE J . n 
J 1 149 GLY 149 141 141 GLY GLY J . n 
J 1 150 SER 150 142 142 SER SER J . n 
J 1 151 TRP 151 143 143 TRP TRP J . n 
J 1 152 THR 152 144 144 THR THR J . n 
J 1 153 HIS 153 145 145 HIS HIS J . n 
J 1 154 HIS 154 146 146 HIS HIS J . n 
J 1 155 SER 155 147 147 SER SER J . n 
J 1 156 ARG 156 148 148 ARG ARG J . n 
J 1 157 GLU 157 149 149 GLU GLU J . n 
J 1 158 ILE 158 150 150 ILE ILE J . n 
J 1 159 SER 159 151 151 SER SER J . n 
J 1 160 VAL 160 152 152 VAL VAL J . n 
J 1 161 ASP 161 153 153 ASP ASP J . n 
J 1 162 PRO 162 154 154 PRO PRO J . n 
J 1 163 THR 163 155 155 THR THR J . n 
J 1 164 THR 164 156 156 THR THR J . n 
J 1 165 GLU 165 157 157 GLU GLU J . n 
J 1 166 ASN 166 158 158 ASN ASN J . n 
J 1 167 SER 167 159 159 SER SER J . n 
J 1 168 ASP 168 160 160 ASP ASP J . n 
J 1 169 ASP 169 161 161 ASP ASP J . n 
J 1 170 SER 170 162 162 SER SER J . n 
J 1 171 GLU 171 163 163 GLU GLU J . n 
J 1 172 TYR 172 164 164 TYR TYR J . n 
J 1 173 PHE 173 165 165 PHE PHE J . n 
J 1 174 SER 174 166 166 SER SER J . n 
J 1 175 GLN 175 167 167 GLN GLN J . n 
J 1 176 TYR 176 168 168 TYR TYR J . n 
J 1 177 SER 177 169 169 SER SER J . n 
J 1 178 ARG 178 170 170 ARG ARG J . n 
J 1 179 PHE 179 171 171 PHE PHE J . n 
J 1 180 GLU 180 172 172 GLU GLU J . n 
J 1 181 ILE 181 173 173 ILE ILE J . n 
J 1 182 LEU 182 174 174 LEU LEU J . n 
J 1 183 ASP 183 175 175 ASP ASP J . n 
J 1 184 VAL 184 176 176 VAL VAL J . n 
J 1 185 THR 185 177 177 THR THR J . n 
J 1 186 GLN 186 178 178 GLN GLN J . n 
J 1 187 LYS 187 179 179 LYS LYS J . n 
J 1 188 LYS 188 180 180 LYS LYS J . n 
J 1 189 ASN 189 181 181 ASN ASN J . n 
J 1 190 SER 190 182 182 SER SER J . n 
J 1 191 VAL 191 183 ?   ?   ?   J . n 
J 1 192 THR 192 184 ?   ?   ?   J . n 
J 1 193 TYR 193 185 ?   ?   ?   J . n 
J 1 194 SER 194 186 ?   ?   ?   J . n 
J 1 195 CYS 195 187 ?   ?   ?   J . n 
J 1 196 CYS 196 188 ?   ?   ?   J . n 
J 1 197 PRO 197 189 ?   ?   ?   J . n 
J 1 198 GLU 198 190 190 GLU GLU J . n 
J 1 199 ALA 199 191 191 ALA ALA J . n 
J 1 200 TYR 200 192 192 TYR TYR J . n 
J 1 201 GLU 201 193 193 GLU GLU J . n 
J 1 202 ASP 202 194 194 ASP ASP J . n 
J 1 203 VAL 203 195 195 VAL VAL J . n 
J 1 204 GLU 204 196 196 GLU GLU J . n 
J 1 205 VAL 205 197 197 VAL VAL J . n 
J 1 206 SER 206 198 198 SER SER J . n 
J 1 207 LEU 207 199 199 LEU LEU J . n 
J 1 208 ASN 208 200 200 ASN ASN J . n 
J 1 209 PHE 209 201 201 PHE PHE J . n 
J 1 210 ARG 210 202 202 ARG ARG J . n 
J 1 211 LYS 211 203 203 LYS LYS J . n 
J 1 212 LYS 212 204 204 LYS LYS J . n 
J 1 213 GLY 213 205 205 GLY GLY J . n 
J 1 214 ARG 214 206 ?   ?   ?   J . n 
J 1 215 SER 215 207 ?   ?   ?   J . n 
J 1 216 GLU 216 208 ?   ?   ?   J . n 
J 1 217 ILE 217 209 ?   ?   ?   J . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
K  2 KK1 1  301 1   KK1 KK1 A . 
L  3 NAG 1  302 1   NAG NAG A . 
M  4 PO4 1  303 1   PO4 PO4 A . 
N  4 PO4 1  304 2   PO4 PO4 A . 
O  4 PO4 1  305 16  PO4 PO4 A . 
P  2 KK1 1  301 5   KK1 KK1 B . 
Q  3 NAG 1  302 10  NAG NAG B . 
R  4 PO4 1  303 17  PO4 PO4 B . 
S  2 KK1 1  301 3   KK1 KK1 C . 
T  3 NAG 1  302 302 NAG NAG C . 
U  4 PO4 1  303 3   PO4 PO4 C . 
V  4 PO4 1  304 4   PO4 PO4 C . 
W  4 PO4 1  305 11  PO4 PO4 C . 
X  2 KK1 1  301 6   KK1 KK1 D . 
Y  3 NAG 1  302 302 NAG NAG D . 
Z  4 PO4 1  303 15  PO4 PO4 D . 
AA 4 PO4 1  304 25  PO4 PO4 D . 
BA 2 KK1 1  301 4   KK1 KK1 E . 
CA 3 NAG 1  302 4   NAG NAG E . 
DA 4 PO4 1  303 5   PO4 PO4 E . 
EA 4 PO4 1  304 24  PO4 PO4 E . 
FA 4 PO4 1  305 26  PO4 PO4 E . 
GA 2 KK1 1  301 2   KK1 KK1 F . 
HA 3 NAG 1  302 5   NAG NAG F . 
IA 4 PO4 1  303 6   PO4 PO4 F . 
JA 4 PO4 1  304 23  PO4 PO4 F . 
KA 2 KK1 1  301 301 KK1 KK1 G . 
LA 3 NAG 1  302 6   NAG NAG G . 
MA 4 PO4 1  303 7   PO4 PO4 G . 
NA 4 PO4 1  304 14  PO4 PO4 G . 
OA 2 KK1 1  301 301 KK1 KK1 H . 
PA 3 NAG 1  302 302 NAG NAG H . 
QA 4 PO4 1  303 8   PO4 PO4 H . 
RA 4 PO4 1  304 9   PO4 PO4 H . 
SA 2 KK1 1  301 9   KK1 KK1 I . 
TA 3 NAG 1  302 8   NAG NAG I . 
UA 2 KK1 1  301 301 KK1 KK1 J . 
VA 3 NAG 1  302 9   NAG NAG J . 
WA 4 PO4 1  303 10  PO4 PO4 J . 
XA 5 HOH 1  401 1   HOH HOH A . 
XA 5 HOH 2  402 2   HOH HOH A . 
XA 5 HOH 3  403 4   HOH HOH A . 
XA 5 HOH 4  404 33  HOH HOH A . 
XA 5 HOH 5  405 37  HOH HOH A . 
XA 5 HOH 6  406 38  HOH HOH A . 
XA 5 HOH 7  407 55  HOH HOH A . 
XA 5 HOH 8  408 63  HOH HOH A . 
XA 5 HOH 9  409 68  HOH HOH A . 
XA 5 HOH 10 410 80  HOH HOH A . 
XA 5 HOH 11 411 85  HOH HOH A . 
XA 5 HOH 12 412 90  HOH HOH A . 
XA 5 HOH 13 413 105 HOH HOH A . 
XA 5 HOH 14 414 145 HOH HOH A . 
XA 5 HOH 15 415 146 HOH HOH A . 
XA 5 HOH 16 416 147 HOH HOH A . 
XA 5 HOH 17 417 153 HOH HOH A . 
XA 5 HOH 18 418 156 HOH HOH A . 
YA 5 HOH 1  401 7   HOH HOH B . 
YA 5 HOH 2  402 8   HOH HOH B . 
YA 5 HOH 3  403 29  HOH HOH B . 
YA 5 HOH 4  404 35  HOH HOH B . 
YA 5 HOH 5  405 40  HOH HOH B . 
YA 5 HOH 6  406 47  HOH HOH B . 
YA 5 HOH 7  407 52  HOH HOH B . 
YA 5 HOH 8  408 56  HOH HOH B . 
YA 5 HOH 9  409 57  HOH HOH B . 
YA 5 HOH 10 410 69  HOH HOH B . 
YA 5 HOH 11 411 70  HOH HOH B . 
YA 5 HOH 12 412 71  HOH HOH B . 
YA 5 HOH 13 413 97  HOH HOH B . 
YA 5 HOH 14 414 111 HOH HOH B . 
YA 5 HOH 15 415 116 HOH HOH B . 
YA 5 HOH 16 416 129 HOH HOH B . 
YA 5 HOH 17 417 130 HOH HOH B . 
ZA 5 HOH 1  401 9   HOH HOH C . 
ZA 5 HOH 2  402 10  HOH HOH C . 
ZA 5 HOH 3  403 11  HOH HOH C . 
ZA 5 HOH 4  404 13  HOH HOH C . 
ZA 5 HOH 5  405 14  HOH HOH C . 
ZA 5 HOH 6  406 31  HOH HOH C . 
ZA 5 HOH 7  407 51  HOH HOH C . 
ZA 5 HOH 8  408 58  HOH HOH C . 
ZA 5 HOH 9  409 59  HOH HOH C . 
ZA 5 HOH 10 410 72  HOH HOH C . 
ZA 5 HOH 11 411 73  HOH HOH C . 
ZA 5 HOH 12 412 74  HOH HOH C . 
ZA 5 HOH 13 413 84  HOH HOH C . 
ZA 5 HOH 14 414 92  HOH HOH C . 
ZA 5 HOH 15 415 93  HOH HOH C . 
ZA 5 HOH 16 416 94  HOH HOH C . 
ZA 5 HOH 17 417 98  HOH HOH C . 
ZA 5 HOH 18 418 99  HOH HOH C . 
ZA 5 HOH 19 419 108 HOH HOH C . 
ZA 5 HOH 20 420 110 HOH HOH C . 
ZA 5 HOH 21 421 119 HOH HOH C . 
ZA 5 HOH 22 422 120 HOH HOH C . 
ZA 5 HOH 23 423 131 HOH HOH C . 
ZA 5 HOH 24 424 154 HOH HOH C . 
ZA 5 HOH 25 425 159 HOH HOH C . 
ZA 5 HOH 26 426 160 HOH HOH C . 
AB 5 HOH 1  401 12  HOH HOH D . 
AB 5 HOH 2  402 15  HOH HOH D . 
AB 5 HOH 3  403 41  HOH HOH D . 
AB 5 HOH 4  404 46  HOH HOH D . 
AB 5 HOH 5  405 49  HOH HOH D . 
AB 5 HOH 6  406 50  HOH HOH D . 
AB 5 HOH 7  407 64  HOH HOH D . 
AB 5 HOH 8  408 66  HOH HOH D . 
AB 5 HOH 9  409 86  HOH HOH D . 
AB 5 HOH 10 410 88  HOH HOH D . 
AB 5 HOH 11 411 89  HOH HOH D . 
AB 5 HOH 12 412 95  HOH HOH D . 
AB 5 HOH 13 413 100 HOH HOH D . 
AB 5 HOH 14 414 107 HOH HOH D . 
AB 5 HOH 15 415 112 HOH HOH D . 
AB 5 HOH 16 416 114 HOH HOH D . 
AB 5 HOH 17 417 117 HOH HOH D . 
AB 5 HOH 18 418 118 HOH HOH D . 
AB 5 HOH 19 419 122 HOH HOH D . 
AB 5 HOH 20 420 150 HOH HOH D . 
AB 5 HOH 21 421 161 HOH HOH D . 
AB 5 HOH 22 422 163 HOH HOH D . 
BB 5 HOH 1  401 3   HOH HOH E . 
BB 5 HOH 2  402 42  HOH HOH E . 
BB 5 HOH 3  403 43  HOH HOH E . 
BB 5 HOH 4  404 61  HOH HOH E . 
BB 5 HOH 5  405 62  HOH HOH E . 
BB 5 HOH 6  406 65  HOH HOH E . 
BB 5 HOH 7  407 67  HOH HOH E . 
BB 5 HOH 8  408 75  HOH HOH E . 
BB 5 HOH 9  409 76  HOH HOH E . 
BB 5 HOH 10 410 77  HOH HOH E . 
BB 5 HOH 11 411 78  HOH HOH E . 
BB 5 HOH 12 412 96  HOH HOH E . 
BB 5 HOH 13 413 106 HOH HOH E . 
BB 5 HOH 14 414 126 HOH HOH E . 
BB 5 HOH 15 415 127 HOH HOH E . 
BB 5 HOH 16 416 134 HOH HOH E . 
BB 5 HOH 17 417 135 HOH HOH E . 
BB 5 HOH 18 418 136 HOH HOH E . 
CB 5 HOH 1  401 16  HOH HOH F . 
CB 5 HOH 2  402 17  HOH HOH F . 
CB 5 HOH 3  403 18  HOH HOH F . 
CB 5 HOH 4  404 34  HOH HOH F . 
CB 5 HOH 5  405 124 HOH HOH F . 
CB 5 HOH 6  406 137 HOH HOH F . 
CB 5 HOH 7  407 138 HOH HOH F . 
CB 5 HOH 8  408 157 HOH HOH F . 
CB 5 HOH 9  409 158 HOH HOH F . 
DB 5 HOH 1  401 32  HOH HOH G . 
DB 5 HOH 2  402 53  HOH HOH G . 
DB 5 HOH 3  403 54  HOH HOH G . 
DB 5 HOH 4  404 79  HOH HOH G . 
DB 5 HOH 5  405 113 HOH HOH G . 
DB 5 HOH 6  406 139 HOH HOH G . 
DB 5 HOH 7  407 140 HOH HOH G . 
DB 5 HOH 8  408 141 HOH HOH G . 
DB 5 HOH 9  409 155 HOH HOH G . 
EB 5 HOH 1  401 5   HOH HOH H . 
EB 5 HOH 2  402 6   HOH HOH H . 
EB 5 HOH 3  403 19  HOH HOH H . 
EB 5 HOH 4  404 30  HOH HOH H . 
EB 5 HOH 5  405 39  HOH HOH H . 
EB 5 HOH 6  406 87  HOH HOH H . 
EB 5 HOH 7  407 101 HOH HOH H . 
EB 5 HOH 8  408 104 HOH HOH H . 
EB 5 HOH 9  409 109 HOH HOH H . 
EB 5 HOH 10 410 115 HOH HOH H . 
EB 5 HOH 11 411 123 HOH HOH H . 
EB 5 HOH 12 412 142 HOH HOH H . 
EB 5 HOH 13 413 143 HOH HOH H . 
EB 5 HOH 14 414 151 HOH HOH H . 
FB 5 HOH 1  401 20  HOH HOH I . 
FB 5 HOH 2  402 21  HOH HOH I . 
FB 5 HOH 3  403 22  HOH HOH I . 
FB 5 HOH 4  404 23  HOH HOH I . 
FB 5 HOH 5  405 36  HOH HOH I . 
FB 5 HOH 6  406 81  HOH HOH I . 
FB 5 HOH 7  407 91  HOH HOH I . 
FB 5 HOH 8  408 102 HOH HOH I . 
FB 5 HOH 9  409 125 HOH HOH I . 
FB 5 HOH 10 410 148 HOH HOH I . 
FB 5 HOH 11 411 149 HOH HOH I . 
GB 5 HOH 1  401 24  HOH HOH J . 
GB 5 HOH 2  402 25  HOH HOH J . 
GB 5 HOH 3  403 26  HOH HOH J . 
GB 5 HOH 4  404 27  HOH HOH J . 
GB 5 HOH 5  405 28  HOH HOH J . 
GB 5 HOH 6  406 44  HOH HOH J . 
GB 5 HOH 7  407 45  HOH HOH J . 
GB 5 HOH 8  408 48  HOH HOH J . 
GB 5 HOH 9  409 60  HOH HOH J . 
GB 5 HOH 10 410 82  HOH HOH J . 
GB 5 HOH 11 411 83  HOH HOH J . 
GB 5 HOH 12 412 103 HOH HOH J . 
GB 5 HOH 13 413 121 HOH HOH J . 
GB 5 HOH 14 414 128 HOH HOH J . 
GB 5 HOH 15 415 132 HOH HOH J . 
GB 5 HOH 16 416 133 HOH HOH J . 
GB 5 HOH 17 417 144 HOH HOH J . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  J ASN 74 J ASN 66 ? ASN 'GLYCOSYLATION SITE' 
2  B ASN 74 B ASN 66 ? ASN 'GLYCOSYLATION SITE' 
3  A ASN 74 A ASN 66 ? ASN 'GLYCOSYLATION SITE' 
4  E ASN 74 E ASN 66 ? ASN 'GLYCOSYLATION SITE' 
5  F ASN 74 F ASN 66 ? ASN 'GLYCOSYLATION SITE' 
6  G ASN 74 G ASN 66 ? ASN 'GLYCOSYLATION SITE' 
7  I ASN 74 I ASN 66 ? ASN 'GLYCOSYLATION SITE' 
8  C ASN 74 C ASN 66 ? ASN 'GLYCOSYLATION SITE' 
9  D ASN 74 D ASN 66 ? ASN 'GLYCOSYLATION SITE' 
10 H ASN 74 H ASN 66 ? ASN 'GLYCOSYLATION SITE' 
# 
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 pentameric 5 
2 author_and_software_defined_assembly PISA pentameric 5 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,XA,YA,ZA,AB,BB  
2 1 F,G,H,I,J,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,CB,DB,EB,FB,GB 
# 
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)' 18960 ? 
1 MORE         -115  ? 
1 'SSA (A^2)'  42970 ? 
2 'ABSA (A^2)' 18600 ? 
2 MORE         -103  ? 
2 'SSA (A^2)'  43440 ? 
# 
_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_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 2014-07-16 
2 'Structure model' 1 1 2014-07-30 
3 'Structure model' 1 2 2014-08-13 
4 'Structure model' 1 3 2018-01-24 
# 
_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         ? 
# 
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' 'Database references' 
2 3 'Structure model' 'Database references' 
3 4 'Structure model' 'Structure summary'   
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    4 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            audit_author 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    4 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_audit_author.name' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .                           ? 1 
PHASER   phasing           .                           ? 2 
PHENIX   refinement        '(phenix.refine: 1.8_1069)' ? 3 
HKL-2000 'data reduction'  .                           ? 4 
HKL-2000 'data scaling'    .                           ? 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 HIS A 69 ? ? -141.16 21.56 
2 1 HIS D 69 ? ? -160.43 30.21 
3 1 HIS H 69 ? ? -145.17 28.74 
4 1 HIS J 69 ? ? -143.08 20.35 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 N 1 G KK1 301 ? C01 ? KA KK1 1 C01 
2  1 N 1 G KK1 301 ? C02 ? KA KK1 1 C02 
3  1 N 1 G KK1 301 ? C03 ? KA KK1 1 C03 
4  1 N 1 G KK1 301 ? C04 ? KA KK1 1 C04 
5  1 N 1 G KK1 301 ? C05 ? KA KK1 1 C05 
6  1 N 1 G KK1 301 ? C06 ? KA KK1 1 C06 
7  1 N 1 G KK1 301 ? C07 ? KA KK1 1 C07 
8  1 N 1 G KK1 301 ? C08 ? KA KK1 1 C08 
9  1 N 1 H KK1 301 ? C01 ? OA KK1 1 C01 
10 1 N 1 H KK1 301 ? C02 ? OA KK1 1 C02 
11 1 N 1 H KK1 301 ? C03 ? OA KK1 1 C03 
12 1 N 1 H KK1 301 ? C04 ? OA KK1 1 C04 
13 1 N 1 H KK1 301 ? C05 ? OA KK1 1 C05 
14 1 N 1 H KK1 301 ? C06 ? OA KK1 1 C06 
15 1 N 1 H KK1 301 ? C07 ? OA KK1 1 C07 
16 1 N 1 H KK1 301 ? C08 ? OA KK1 1 C08 
17 1 N 1 J KK1 301 ? C01 ? UA KK1 1 C01 
18 1 N 1 J KK1 301 ? C02 ? UA KK1 1 C02 
19 1 N 1 J KK1 301 ? C03 ? UA KK1 1 C03 
20 1 N 1 J KK1 301 ? C04 ? UA KK1 1 C04 
21 1 N 1 J KK1 301 ? C05 ? UA KK1 1 C05 
22 1 N 1 J KK1 301 ? C06 ? UA KK1 1 C06 
23 1 N 1 J KK1 301 ? C07 ? UA KK1 1 C07 
24 1 N 1 J KK1 301 ? C08 ? UA KK1 1 C08 
# 
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 THR 184 ? A THR 192 
2  1 Y 1 A TYR 185 ? A TYR 193 
3  1 Y 1 A SER 186 ? A SER 194 
4  1 Y 1 A CYS 187 ? A CYS 195 
5  1 Y 1 A CYS 188 ? A CYS 196 
6  1 Y 1 A PRO 189 ? A PRO 197 
7  1 Y 1 A ARG 206 ? A ARG 214 
8  1 Y 1 A SER 207 ? A SER 215 
9  1 Y 1 A GLU 208 ? A GLU 216 
10 1 Y 1 A ILE 209 ? A ILE 217 
11 1 Y 1 B ASP -7  ? B ASP 1   
12 1 Y 1 B TYR -6  ? B TYR 2   
13 1 Y 1 B TYR 185 ? B TYR 193 
14 1 Y 1 B SER 186 ? B SER 194 
15 1 Y 1 B CYS 187 ? B CYS 195 
16 1 Y 1 B CYS 188 ? B CYS 196 
17 1 Y 1 B ARG 206 ? B ARG 214 
18 1 Y 1 B SER 207 ? B SER 215 
19 1 Y 1 B GLU 208 ? B GLU 216 
20 1 Y 1 B ILE 209 ? B ILE 217 
21 1 Y 1 C TYR 185 ? C TYR 193 
22 1 Y 1 C SER 186 ? C SER 194 
23 1 Y 1 C CYS 187 ? C CYS 195 
24 1 Y 1 C CYS 188 ? C CYS 196 
25 1 Y 1 C ARG 206 ? C ARG 214 
26 1 Y 1 C SER 207 ? C SER 215 
27 1 Y 1 C GLU 208 ? C GLU 216 
28 1 Y 1 C ILE 209 ? C ILE 217 
29 1 Y 1 D ARG 206 ? D ARG 214 
30 1 Y 1 D SER 207 ? D SER 215 
31 1 Y 1 D GLU 208 ? D GLU 216 
32 1 Y 1 D ILE 209 ? D ILE 217 
33 1 Y 1 E THR 156 ? E THR 164 
34 1 Y 1 E GLU 157 ? E GLU 165 
35 1 Y 1 E ASN 158 ? E ASN 166 
36 1 Y 1 E TYR 185 ? E TYR 193 
37 1 Y 1 E SER 186 ? E SER 194 
38 1 Y 1 E CYS 187 ? E CYS 195 
39 1 Y 1 E CYS 188 ? E CYS 196 
40 1 Y 1 E PRO 189 ? E PRO 197 
41 1 Y 1 E ARG 206 ? E ARG 214 
42 1 Y 1 E SER 207 ? E SER 215 
43 1 Y 1 E GLU 208 ? E GLU 216 
44 1 Y 1 E ILE 209 ? E ILE 217 
45 1 Y 1 F THR 156 ? F THR 164 
46 1 Y 1 F TYR 185 ? F TYR 193 
47 1 Y 1 F SER 186 ? F SER 194 
48 1 Y 1 F CYS 187 ? F CYS 195 
49 1 Y 1 F ARG 206 ? F ARG 214 
50 1 Y 1 F SER 207 ? F SER 215 
51 1 Y 1 F GLU 208 ? F GLU 216 
52 1 Y 1 F ILE 209 ? F ILE 217 
53 1 Y 1 G ASP 160 ? G ASP 168 
54 1 Y 1 G ASP 161 ? G ASP 169 
55 1 Y 1 G SER 186 ? G SER 194 
56 1 Y 1 G CYS 187 ? G CYS 195 
57 1 Y 1 G CYS 188 ? G CYS 196 
58 1 Y 1 G ARG 206 ? G ARG 214 
59 1 Y 1 G SER 207 ? G SER 215 
60 1 Y 1 G GLU 208 ? G GLU 216 
61 1 Y 1 G ILE 209 ? G ILE 217 
62 1 Y 1 H THR 156 ? H THR 164 
63 1 Y 1 H GLU 157 ? H GLU 165 
64 1 Y 1 H ASN 158 ? H ASN 166 
65 1 Y 1 H SER 159 ? H SER 167 
66 1 Y 1 H CYS 187 ? H CYS 195 
67 1 Y 1 H CYS 188 ? H CYS 196 
68 1 Y 1 H ARG 206 ? H ARG 214 
69 1 Y 1 H SER 207 ? H SER 215 
70 1 Y 1 H GLU 208 ? H GLU 216 
71 1 Y 1 H ILE 209 ? H ILE 217 
72 1 Y 1 I THR 156 ? I THR 164 
73 1 Y 1 I GLU 157 ? I GLU 165 
74 1 Y 1 I ASN 158 ? I ASN 166 
75 1 Y 1 I SER 186 ? I SER 194 
76 1 Y 1 I CYS 187 ? I CYS 195 
77 1 Y 1 I CYS 188 ? I CYS 196 
78 1 Y 1 I ARG 206 ? I ARG 214 
79 1 Y 1 I SER 207 ? I SER 215 
80 1 Y 1 I GLU 208 ? I GLU 216 
81 1 Y 1 I ILE 209 ? I ILE 217 
82 1 Y 1 J VAL 183 ? J VAL 191 
83 1 Y 1 J THR 184 ? J THR 192 
84 1 Y 1 J TYR 185 ? J TYR 193 
85 1 Y 1 J SER 186 ? J SER 194 
86 1 Y 1 J CYS 187 ? J CYS 195 
87 1 Y 1 J CYS 188 ? J CYS 196 
88 1 Y 1 J PRO 189 ? J PRO 197 
89 1 Y 1 J ARG 206 ? J ARG 214 
90 1 Y 1 J SER 207 ? J SER 215 
91 1 Y 1 J GLU 208 ? J GLU 216 
92 1 Y 1 J ILE 209 ? J ILE 217 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '6-(4-methoxyphenyl)-N~4~-octylpyrimidine-2,4-diamine' KK1 
3 N-ACETYL-D-GLUCOSAMINE                                 NAG 
4 'PHOSPHATE ION'                                        PO4 
5 water                                                  HOH 
# 
