data_3SH1
# 
_entry.id   3SH1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3SH1         
RCSB  RCSB066191   
WWPDB D_1000066191 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 2BYR . unspecified 
PDB 3SIO . unspecified 
PDB 3T4M . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3SH1 
_pdbx_database_status.recvd_initial_deposition_date   2011-06-15 
_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.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Nemecz, A.'   1 
'Taylor, P.W.' 2 
# 
_citation.id                        primary 
_citation.title                     
;Creating an alpha-7 nicotinic acetylcholine recognition domain from the  
acetylcholine binding protein: crystallographic and ligand selectivity analyses
;
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_volume            286 
_citation.page_first                42555 
_citation.page_last                 42565 
_citation.year                      2011 
_citation.journal_id_ASTM           JBCHA3 
_citation.country                   US 
_citation.journal_id_ISSN           0021-9258 
_citation.journal_id_CSD            0071 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   22009746 
_citation.pdbx_database_id_DOI      10.1074/jbc.M111.286583 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Nemecz, A.' 1 
primary 'Taylor, P.' 2 
# 
_cell.entry_id           3SH1 
_cell.length_a           85.793 
_cell.length_b           140.183 
_cell.length_c           136.806 
_cell.angle_alpha        90.00 
_cell.angle_beta         105.20 
_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                         3SH1 
_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 'Soluble acetylcholine receptor' 26323.051 10 ? ? 'unp entry 18-236' ? 
2 non-polymer syn 'MAGNESIUM ION'                  24.305    5  ? ? ?                  ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE           221.208   19 ? ? ?                  ? 
4 non-polymer syn METHYLLYCACONITINE               682.800   10 ? ? ?                  ? 
5 non-polymer syn '(4R)-2-METHYLPENTANE-2,4-DIOL'  118.174   5  ? ? ?                  ? 
6 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'  118.174   7  ? ? ?                  ? 
7 non-polymer syn 'ACETATE ION'                    59.044    1  ? ? ?                  ? 
8 non-polymer man BETA-D-MANNOSE                   180.156   2  ? ? ?                  ? 
9 water       nat water                            18.015    71 ? ? ?                  ? 
# 
_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       
;DYKDDDDKLHSQANLMRLKSDLFNRSPMYPGPTKDDPLTVYLSFSLLDIVKADSSTNEVDLVYWEQQSWKLNSLMWDPNE
YGNITDFRTSAADIWTPDITAYSSTRPVQVLSPQNALVNSSGHVQYLPAQRLSFMCDPTGVDSEEGATCAVKFGSWSYGG
WEIDLKTDTDQVDLSSYYASSKYEILSATQTRSERFYECCKEPYPDVNLVVKFRERRAGNGFFRNLFDSR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;DYKDDDDKLHSQANLMRLKSDLFNRSPMYPGPTKDDPLTVYLSFSLLDIVKADSSTNEVDLVYWEQQSWKLNSLMWDPNE
YGNITDFRTSAADIWTPDITAYSSTRPVQVLSPQNALVNSSGHVQYLPAQRLSFMCDPTGVDSEEGATCAVKFGSWSYGG
WEIDLKTDTDQVDLSSYYASSKYEILSATQTRSERFYECCKEPYPDVNLVVKFRERRAGNGFFRNLFDSR
;
_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  HIS n 
1 11  SER n 
1 12  GLN n 
1 13  ALA n 
1 14  ASN n 
1 15  LEU n 
1 16  MET n 
1 17  ARG n 
1 18  LEU n 
1 19  LYS n 
1 20  SER n 
1 21  ASP n 
1 22  LEU n 
1 23  PHE n 
1 24  ASN n 
1 25  ARG n 
1 26  SER n 
1 27  PRO n 
1 28  MET n 
1 29  TYR n 
1 30  PRO n 
1 31  GLY n 
1 32  PRO n 
1 33  THR n 
1 34  LYS n 
1 35  ASP n 
1 36  ASP n 
1 37  PRO n 
1 38  LEU n 
1 39  THR n 
1 40  VAL n 
1 41  TYR n 
1 42  LEU n 
1 43  SER n 
1 44  PHE n 
1 45  SER n 
1 46  LEU n 
1 47  LEU n 
1 48  ASP n 
1 49  ILE n 
1 50  VAL n 
1 51  LYS n 
1 52  ALA n 
1 53  ASP n 
1 54  SER n 
1 55  SER n 
1 56  THR n 
1 57  ASN n 
1 58  GLU n 
1 59  VAL n 
1 60  ASP n 
1 61  LEU n 
1 62  VAL n 
1 63  TYR n 
1 64  TRP n 
1 65  GLU n 
1 66  GLN n 
1 67  GLN n 
1 68  SER n 
1 69  TRP n 
1 70  LYS n 
1 71  LEU n 
1 72  ASN n 
1 73  SER n 
1 74  LEU n 
1 75  MET n 
1 76  TRP n 
1 77  ASP n 
1 78  PRO n 
1 79  ASN n 
1 80  GLU n 
1 81  TYR n 
1 82  GLY n 
1 83  ASN n 
1 84  ILE n 
1 85  THR n 
1 86  ASP n 
1 87  PHE n 
1 88  ARG n 
1 89  THR n 
1 90  SER n 
1 91  ALA n 
1 92  ALA n 
1 93  ASP n 
1 94  ILE n 
1 95  TRP n 
1 96  THR n 
1 97  PRO n 
1 98  ASP n 
1 99  ILE n 
1 100 THR n 
1 101 ALA n 
1 102 TYR n 
1 103 SER n 
1 104 SER n 
1 105 THR n 
1 106 ARG n 
1 107 PRO n 
1 108 VAL n 
1 109 GLN n 
1 110 VAL n 
1 111 LEU n 
1 112 SER n 
1 113 PRO n 
1 114 GLN n 
1 115 ASN n 
1 116 ALA n 
1 117 LEU n 
1 118 VAL n 
1 119 ASN n 
1 120 SER n 
1 121 SER n 
1 122 GLY n 
1 123 HIS n 
1 124 VAL n 
1 125 GLN n 
1 126 TYR n 
1 127 LEU n 
1 128 PRO n 
1 129 ALA n 
1 130 GLN n 
1 131 ARG n 
1 132 LEU n 
1 133 SER n 
1 134 PHE n 
1 135 MET n 
1 136 CYS n 
1 137 ASP n 
1 138 PRO n 
1 139 THR n 
1 140 GLY n 
1 141 VAL n 
1 142 ASP n 
1 143 SER n 
1 144 GLU n 
1 145 GLU n 
1 146 GLY n 
1 147 ALA n 
1 148 THR n 
1 149 CYS n 
1 150 ALA n 
1 151 VAL n 
1 152 LYS n 
1 153 PHE n 
1 154 GLY n 
1 155 SER n 
1 156 TRP n 
1 157 SER n 
1 158 TYR n 
1 159 GLY n 
1 160 GLY n 
1 161 TRP n 
1 162 GLU n 
1 163 ILE n 
1 164 ASP n 
1 165 LEU n 
1 166 LYS n 
1 167 THR n 
1 168 ASP n 
1 169 THR n 
1 170 ASP n 
1 171 GLN n 
1 172 VAL n 
1 173 ASP n 
1 174 LEU n 
1 175 SER n 
1 176 SER n 
1 177 TYR n 
1 178 TYR n 
1 179 ALA n 
1 180 SER n 
1 181 SER n 
1 182 LYS n 
1 183 TYR n 
1 184 GLU n 
1 185 ILE n 
1 186 LEU n 
1 187 SER n 
1 188 ALA n 
1 189 THR n 
1 190 GLN n 
1 191 THR n 
1 192 ARG n 
1 193 SER n 
1 194 GLU n 
1 195 ARG n 
1 196 PHE n 
1 197 TYR n 
1 198 GLU n 
1 199 CYS n 
1 200 CYS n 
1 201 LYS n 
1 202 GLU n 
1 203 PRO n 
1 204 TYR n 
1 205 PRO n 
1 206 ASP n 
1 207 VAL n 
1 208 ASN n 
1 209 LEU n 
1 210 VAL n 
1 211 VAL n 
1 212 LYS n 
1 213 PHE n 
1 214 ARG n 
1 215 GLU n 
1 216 ARG n 
1 217 ARG n 
1 218 ALA n 
1 219 GLY n 
1 220 ASN n 
1 221 GLY n 
1 222 PHE n 
1 223 PHE n 
1 224 ARG n 
1 225 ASN n 
1 226 LEU n 
1 227 PHE n 
1 228 ASP n 
1 229 SER n 
1 230 ARG 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               'California sea hare' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'LOC100533247 soluble acetylcholine receptor' 
_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      'Aplysia californica' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     6500 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      '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          Plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       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                    Q8WSF8_APLCA 
_struct_ref.pdbx_db_accession          Q8WSF8 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;HSQANLMRLKSDLFNRSPMYPGPTKDDPLTVTLGFTLQDIVKADSSTNEVDLVYYEQQRWKLNSLMWDPNEYGNITDFRT
SAADIWTPDITAYSSTRPVQVLSPQIAVVTHDGSVMFIPAQRLSFMCDPTGVDSEEGATCAVKFGSWVYSGFEIDLKTDT
DQVDLSSYYASSKYEILSATQTRQVQHYSCCPEPYIDVNLVVKFRERRAGNGFFRNLFD
;
_struct_ref.pdbx_align_begin           18 
_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 3SH1 A 10 ? 228 ? Q8WSF8 18 ? 236 ? 1 219 
2  1 3SH1 B 10 ? 228 ? Q8WSF8 18 ? 236 ? 1 219 
3  1 3SH1 C 10 ? 228 ? Q8WSF8 18 ? 236 ? 1 219 
4  1 3SH1 D 10 ? 228 ? Q8WSF8 18 ? 236 ? 1 219 
5  1 3SH1 E 10 ? 228 ? Q8WSF8 18 ? 236 ? 1 219 
6  1 3SH1 F 10 ? 228 ? Q8WSF8 18 ? 236 ? 1 219 
7  1 3SH1 G 10 ? 228 ? Q8WSF8 18 ? 236 ? 1 219 
8  1 3SH1 H 10 ? 228 ? Q8WSF8 18 ? 236 ? 1 219 
9  1 3SH1 I 10 ? 228 ? Q8WSF8 18 ? 236 ? 1 219 
10 1 3SH1 J 10 ? 228 ? Q8WSF8 18 ? 236 ? 1 219 
# 
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  3SH1 ASP A 1   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -8  1   
1  3SH1 TYR A 2   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -7  2   
1  3SH1 LYS A 3   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -6  3   
1  3SH1 ASP A 4   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -5  4   
1  3SH1 ASP A 5   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -4  5   
1  3SH1 ASP A 6   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -3  6   
1  3SH1 ASP A 7   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -2  7   
1  3SH1 LYS A 8   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -1  8   
1  3SH1 LEU A 9   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      0   9   
1  3SH1 TYR A 41  ? UNP Q8WSF8 THR 49  'ENGINEERED MUTATION' 32  10  
1  3SH1 SER A 43  ? UNP Q8WSF8 GLY 51  'ENGINEERED MUTATION' 34  11  
1  3SH1 SER A 45  ? UNP Q8WSF8 THR 53  'ENGINEERED MUTATION' 36  12  
1  3SH1 LEU A 47  ? UNP Q8WSF8 GLN 55  'ENGINEERED MUTATION' 38  13  
1  3SH1 TRP A 64  ? UNP Q8WSF8 TYR 72  'ENGINEERED MUTATION' 55  14  
1  3SH1 SER A 68  ? UNP Q8WSF8 ARG 76  'ENGINEERED MUTATION' 59  15  
1  3SH1 ASN A 115 ? UNP Q8WSF8 ILE 123 'ENGINEERED MUTATION' 106 16  
1  3SH1 LEU A 117 ? UNP Q8WSF8 VAL 125 'ENGINEERED MUTATION' 108 17  
1  3SH1 ASN A 119 ? UNP Q8WSF8 THR 127 'ENGINEERED MUTATION' 110 18  
1  3SH1 SER A 120 ? UNP Q8WSF8 HIS 128 'ENGINEERED MUTATION' 111 19  
1  3SH1 SER A 121 ? UNP Q8WSF8 ASP 129 'ENGINEERED MUTATION' 112 20  
1  3SH1 HIS A 123 ? UNP Q8WSF8 SER 131 'ENGINEERED MUTATION' 114 21  
1  3SH1 GLN A 125 ? UNP Q8WSF8 MET 133 'ENGINEERED MUTATION' 116 22  
1  3SH1 TYR A 126 ? UNP Q8WSF8 PHE 134 'ENGINEERED MUTATION' 117 23  
1  3SH1 LEU A 127 ? UNP Q8WSF8 ILE 135 'ENGINEERED MUTATION' 118 24  
1  3SH1 SER A 157 ? UNP Q8WSF8 VAL 165 'ENGINEERED MUTATION' 148 25  
1  3SH1 GLY A 159 ? UNP Q8WSF8 SER 167 'ENGINEERED MUTATION' 150 26  
1  3SH1 TRP A 161 ? UNP Q8WSF8 PHE 169 'ENGINEERED MUTATION' 152 27  
1  3SH1 SER A 193 ? UNP Q8WSF8 GLN 201 'ENGINEERED MUTATION' 184 28  
1  3SH1 GLU A 194 ? UNP Q8WSF8 VAL 202 'ENGINEERED MUTATION' 185 29  
1  3SH1 ARG A 195 ? UNP Q8WSF8 GLN 203 'ENGINEERED MUTATION' 186 30  
1  3SH1 PHE A 196 ? UNP Q8WSF8 HIS 204 'ENGINEERED MUTATION' 187 31  
1  3SH1 GLU A 198 ? UNP Q8WSF8 SER 206 'ENGINEERED MUTATION' 189 32  
1  3SH1 LYS A 201 ? UNP Q8WSF8 PRO 209 'ENGINEERED MUTATION' 192 33  
1  3SH1 PRO A 205 ? UNP Q8WSF8 ILE 213 'ENGINEERED MUTATION' 196 34  
1  3SH1 SER A 229 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      220 35  
1  3SH1 ARG A 230 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      221 36  
2  3SH1 ASP B 1   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -8  37  
2  3SH1 TYR B 2   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -7  38  
2  3SH1 LYS B 3   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -6  39  
2  3SH1 ASP B 4   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -5  40  
2  3SH1 ASP B 5   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -4  41  
2  3SH1 ASP B 6   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -3  42  
2  3SH1 ASP B 7   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -2  43  
2  3SH1 LYS B 8   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -1  44  
2  3SH1 LEU B 9   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      0   45  
2  3SH1 TYR B 41  ? UNP Q8WSF8 THR 49  'ENGINEERED MUTATION' 32  46  
2  3SH1 SER B 43  ? UNP Q8WSF8 GLY 51  'ENGINEERED MUTATION' 34  47  
2  3SH1 SER B 45  ? UNP Q8WSF8 THR 53  'ENGINEERED MUTATION' 36  48  
2  3SH1 LEU B 47  ? UNP Q8WSF8 GLN 55  'ENGINEERED MUTATION' 38  49  
2  3SH1 TRP B 64  ? UNP Q8WSF8 TYR 72  'ENGINEERED MUTATION' 55  50  
2  3SH1 SER B 68  ? UNP Q8WSF8 ARG 76  'ENGINEERED MUTATION' 59  51  
2  3SH1 ASN B 115 ? UNP Q8WSF8 ILE 123 'ENGINEERED MUTATION' 106 52  
2  3SH1 LEU B 117 ? UNP Q8WSF8 VAL 125 'ENGINEERED MUTATION' 108 53  
2  3SH1 ASN B 119 ? UNP Q8WSF8 THR 127 'ENGINEERED MUTATION' 110 54  
2  3SH1 SER B 120 ? UNP Q8WSF8 HIS 128 'ENGINEERED MUTATION' 111 55  
2  3SH1 SER B 121 ? UNP Q8WSF8 ASP 129 'ENGINEERED MUTATION' 112 56  
2  3SH1 HIS B 123 ? UNP Q8WSF8 SER 131 'ENGINEERED MUTATION' 114 57  
2  3SH1 GLN B 125 ? UNP Q8WSF8 MET 133 'ENGINEERED MUTATION' 116 58  
2  3SH1 TYR B 126 ? UNP Q8WSF8 PHE 134 'ENGINEERED MUTATION' 117 59  
2  3SH1 LEU B 127 ? UNP Q8WSF8 ILE 135 'ENGINEERED MUTATION' 118 60  
2  3SH1 SER B 157 ? UNP Q8WSF8 VAL 165 'ENGINEERED MUTATION' 148 61  
2  3SH1 GLY B 159 ? UNP Q8WSF8 SER 167 'ENGINEERED MUTATION' 150 62  
2  3SH1 TRP B 161 ? UNP Q8WSF8 PHE 169 'ENGINEERED MUTATION' 152 63  
2  3SH1 SER B 193 ? UNP Q8WSF8 GLN 201 'ENGINEERED MUTATION' 184 64  
2  3SH1 GLU B 194 ? UNP Q8WSF8 VAL 202 'ENGINEERED MUTATION' 185 65  
2  3SH1 ARG B 195 ? UNP Q8WSF8 GLN 203 'ENGINEERED MUTATION' 186 66  
2  3SH1 PHE B 196 ? UNP Q8WSF8 HIS 204 'ENGINEERED MUTATION' 187 67  
2  3SH1 GLU B 198 ? UNP Q8WSF8 SER 206 'ENGINEERED MUTATION' 189 68  
2  3SH1 LYS B 201 ? UNP Q8WSF8 PRO 209 'ENGINEERED MUTATION' 192 69  
2  3SH1 PRO B 205 ? UNP Q8WSF8 ILE 213 'ENGINEERED MUTATION' 196 70  
2  3SH1 SER B 229 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      220 71  
2  3SH1 ARG B 230 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      221 72  
3  3SH1 ASP C 1   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -8  73  
3  3SH1 TYR C 2   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -7  74  
3  3SH1 LYS C 3   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -6  75  
3  3SH1 ASP C 4   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -5  76  
3  3SH1 ASP C 5   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -4  77  
3  3SH1 ASP C 6   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -3  78  
3  3SH1 ASP C 7   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -2  79  
3  3SH1 LYS C 8   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -1  80  
3  3SH1 LEU C 9   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      0   81  
3  3SH1 TYR C 41  ? UNP Q8WSF8 THR 49  'ENGINEERED MUTATION' 32  82  
3  3SH1 SER C 43  ? UNP Q8WSF8 GLY 51  'ENGINEERED MUTATION' 34  83  
3  3SH1 SER C 45  ? UNP Q8WSF8 THR 53  'ENGINEERED MUTATION' 36  84  
3  3SH1 LEU C 47  ? UNP Q8WSF8 GLN 55  'ENGINEERED MUTATION' 38  85  
3  3SH1 TRP C 64  ? UNP Q8WSF8 TYR 72  'ENGINEERED MUTATION' 55  86  
3  3SH1 SER C 68  ? UNP Q8WSF8 ARG 76  'ENGINEERED MUTATION' 59  87  
3  3SH1 ASN C 115 ? UNP Q8WSF8 ILE 123 'ENGINEERED MUTATION' 106 88  
3  3SH1 LEU C 117 ? UNP Q8WSF8 VAL 125 'ENGINEERED MUTATION' 108 89  
3  3SH1 ASN C 119 ? UNP Q8WSF8 THR 127 'ENGINEERED MUTATION' 110 90  
3  3SH1 SER C 120 ? UNP Q8WSF8 HIS 128 'ENGINEERED MUTATION' 111 91  
3  3SH1 SER C 121 ? UNP Q8WSF8 ASP 129 'ENGINEERED MUTATION' 112 92  
3  3SH1 HIS C 123 ? UNP Q8WSF8 SER 131 'ENGINEERED MUTATION' 114 93  
3  3SH1 GLN C 125 ? UNP Q8WSF8 MET 133 'ENGINEERED MUTATION' 116 94  
3  3SH1 TYR C 126 ? UNP Q8WSF8 PHE 134 'ENGINEERED MUTATION' 117 95  
3  3SH1 LEU C 127 ? UNP Q8WSF8 ILE 135 'ENGINEERED MUTATION' 118 96  
3  3SH1 SER C 157 ? UNP Q8WSF8 VAL 165 'ENGINEERED MUTATION' 148 97  
3  3SH1 GLY C 159 ? UNP Q8WSF8 SER 167 'ENGINEERED MUTATION' 150 98  
3  3SH1 TRP C 161 ? UNP Q8WSF8 PHE 169 'ENGINEERED MUTATION' 152 99  
3  3SH1 SER C 193 ? UNP Q8WSF8 GLN 201 'ENGINEERED MUTATION' 184 100 
3  3SH1 GLU C 194 ? UNP Q8WSF8 VAL 202 'ENGINEERED MUTATION' 185 101 
3  3SH1 ARG C 195 ? UNP Q8WSF8 GLN 203 'ENGINEERED MUTATION' 186 102 
3  3SH1 PHE C 196 ? UNP Q8WSF8 HIS 204 'ENGINEERED MUTATION' 187 103 
3  3SH1 GLU C 198 ? UNP Q8WSF8 SER 206 'ENGINEERED MUTATION' 189 104 
3  3SH1 LYS C 201 ? UNP Q8WSF8 PRO 209 'ENGINEERED MUTATION' 192 105 
3  3SH1 PRO C 205 ? UNP Q8WSF8 ILE 213 'ENGINEERED MUTATION' 196 106 
3  3SH1 SER C 229 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      220 107 
3  3SH1 ARG C 230 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      221 108 
4  3SH1 ASP D 1   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -8  109 
4  3SH1 TYR D 2   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -7  110 
4  3SH1 LYS D 3   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -6  111 
4  3SH1 ASP D 4   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -5  112 
4  3SH1 ASP D 5   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -4  113 
4  3SH1 ASP D 6   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -3  114 
4  3SH1 ASP D 7   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -2  115 
4  3SH1 LYS D 8   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -1  116 
4  3SH1 LEU D 9   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      0   117 
4  3SH1 TYR D 41  ? UNP Q8WSF8 THR 49  'ENGINEERED MUTATION' 32  118 
4  3SH1 SER D 43  ? UNP Q8WSF8 GLY 51  'ENGINEERED MUTATION' 34  119 
4  3SH1 SER D 45  ? UNP Q8WSF8 THR 53  'ENGINEERED MUTATION' 36  120 
4  3SH1 LEU D 47  ? UNP Q8WSF8 GLN 55  'ENGINEERED MUTATION' 38  121 
4  3SH1 TRP D 64  ? UNP Q8WSF8 TYR 72  'ENGINEERED MUTATION' 55  122 
4  3SH1 SER D 68  ? UNP Q8WSF8 ARG 76  'ENGINEERED MUTATION' 59  123 
4  3SH1 ASN D 115 ? UNP Q8WSF8 ILE 123 'ENGINEERED MUTATION' 106 124 
4  3SH1 LEU D 117 ? UNP Q8WSF8 VAL 125 'ENGINEERED MUTATION' 108 125 
4  3SH1 ASN D 119 ? UNP Q8WSF8 THR 127 'ENGINEERED MUTATION' 110 126 
4  3SH1 SER D 120 ? UNP Q8WSF8 HIS 128 'ENGINEERED MUTATION' 111 127 
4  3SH1 SER D 121 ? UNP Q8WSF8 ASP 129 'ENGINEERED MUTATION' 112 128 
4  3SH1 HIS D 123 ? UNP Q8WSF8 SER 131 'ENGINEERED MUTATION' 114 129 
4  3SH1 GLN D 125 ? UNP Q8WSF8 MET 133 'ENGINEERED MUTATION' 116 130 
4  3SH1 TYR D 126 ? UNP Q8WSF8 PHE 134 'ENGINEERED MUTATION' 117 131 
4  3SH1 LEU D 127 ? UNP Q8WSF8 ILE 135 'ENGINEERED MUTATION' 118 132 
4  3SH1 SER D 157 ? UNP Q8WSF8 VAL 165 'ENGINEERED MUTATION' 148 133 
4  3SH1 GLY D 159 ? UNP Q8WSF8 SER 167 'ENGINEERED MUTATION' 150 134 
4  3SH1 TRP D 161 ? UNP Q8WSF8 PHE 169 'ENGINEERED MUTATION' 152 135 
4  3SH1 SER D 193 ? UNP Q8WSF8 GLN 201 'ENGINEERED MUTATION' 184 136 
4  3SH1 GLU D 194 ? UNP Q8WSF8 VAL 202 'ENGINEERED MUTATION' 185 137 
4  3SH1 ARG D 195 ? UNP Q8WSF8 GLN 203 'ENGINEERED MUTATION' 186 138 
4  3SH1 PHE D 196 ? UNP Q8WSF8 HIS 204 'ENGINEERED MUTATION' 187 139 
4  3SH1 GLU D 198 ? UNP Q8WSF8 SER 206 'ENGINEERED MUTATION' 189 140 
4  3SH1 LYS D 201 ? UNP Q8WSF8 PRO 209 'ENGINEERED MUTATION' 192 141 
4  3SH1 PRO D 205 ? UNP Q8WSF8 ILE 213 'ENGINEERED MUTATION' 196 142 
4  3SH1 SER D 229 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      220 143 
4  3SH1 ARG D 230 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      221 144 
5  3SH1 ASP E 1   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -8  145 
5  3SH1 TYR E 2   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -7  146 
5  3SH1 LYS E 3   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -6  147 
5  3SH1 ASP E 4   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -5  148 
5  3SH1 ASP E 5   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -4  149 
5  3SH1 ASP E 6   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -3  150 
5  3SH1 ASP E 7   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -2  151 
5  3SH1 LYS E 8   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -1  152 
5  3SH1 LEU E 9   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      0   153 
5  3SH1 TYR E 41  ? UNP Q8WSF8 THR 49  'ENGINEERED MUTATION' 32  154 
5  3SH1 SER E 43  ? UNP Q8WSF8 GLY 51  'ENGINEERED MUTATION' 34  155 
5  3SH1 SER E 45  ? UNP Q8WSF8 THR 53  'ENGINEERED MUTATION' 36  156 
5  3SH1 LEU E 47  ? UNP Q8WSF8 GLN 55  'ENGINEERED MUTATION' 38  157 
5  3SH1 TRP E 64  ? UNP Q8WSF8 TYR 72  'ENGINEERED MUTATION' 55  158 
5  3SH1 SER E 68  ? UNP Q8WSF8 ARG 76  'ENGINEERED MUTATION' 59  159 
5  3SH1 ASN E 115 ? UNP Q8WSF8 ILE 123 'ENGINEERED MUTATION' 106 160 
5  3SH1 LEU E 117 ? UNP Q8WSF8 VAL 125 'ENGINEERED MUTATION' 108 161 
5  3SH1 ASN E 119 ? UNP Q8WSF8 THR 127 'ENGINEERED MUTATION' 110 162 
5  3SH1 SER E 120 ? UNP Q8WSF8 HIS 128 'ENGINEERED MUTATION' 111 163 
5  3SH1 SER E 121 ? UNP Q8WSF8 ASP 129 'ENGINEERED MUTATION' 112 164 
5  3SH1 HIS E 123 ? UNP Q8WSF8 SER 131 'ENGINEERED MUTATION' 114 165 
5  3SH1 GLN E 125 ? UNP Q8WSF8 MET 133 'ENGINEERED MUTATION' 116 166 
5  3SH1 TYR E 126 ? UNP Q8WSF8 PHE 134 'ENGINEERED MUTATION' 117 167 
5  3SH1 LEU E 127 ? UNP Q8WSF8 ILE 135 'ENGINEERED MUTATION' 118 168 
5  3SH1 SER E 157 ? UNP Q8WSF8 VAL 165 'ENGINEERED MUTATION' 148 169 
5  3SH1 GLY E 159 ? UNP Q8WSF8 SER 167 'ENGINEERED MUTATION' 150 170 
5  3SH1 TRP E 161 ? UNP Q8WSF8 PHE 169 'ENGINEERED MUTATION' 152 171 
5  3SH1 SER E 193 ? UNP Q8WSF8 GLN 201 'ENGINEERED MUTATION' 184 172 
5  3SH1 GLU E 194 ? UNP Q8WSF8 VAL 202 'ENGINEERED MUTATION' 185 173 
5  3SH1 ARG E 195 ? UNP Q8WSF8 GLN 203 'ENGINEERED MUTATION' 186 174 
5  3SH1 PHE E 196 ? UNP Q8WSF8 HIS 204 'ENGINEERED MUTATION' 187 175 
5  3SH1 GLU E 198 ? UNP Q8WSF8 SER 206 'ENGINEERED MUTATION' 189 176 
5  3SH1 LYS E 201 ? UNP Q8WSF8 PRO 209 'ENGINEERED MUTATION' 192 177 
5  3SH1 PRO E 205 ? UNP Q8WSF8 ILE 213 'ENGINEERED MUTATION' 196 178 
5  3SH1 SER E 229 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      220 179 
5  3SH1 ARG E 230 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      221 180 
6  3SH1 ASP F 1   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -8  181 
6  3SH1 TYR F 2   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -7  182 
6  3SH1 LYS F 3   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -6  183 
6  3SH1 ASP F 4   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -5  184 
6  3SH1 ASP F 5   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -4  185 
6  3SH1 ASP F 6   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -3  186 
6  3SH1 ASP F 7   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -2  187 
6  3SH1 LYS F 8   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -1  188 
6  3SH1 LEU F 9   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      0   189 
6  3SH1 TYR F 41  ? UNP Q8WSF8 THR 49  'ENGINEERED MUTATION' 32  190 
6  3SH1 SER F 43  ? UNP Q8WSF8 GLY 51  'ENGINEERED MUTATION' 34  191 
6  3SH1 SER F 45  ? UNP Q8WSF8 THR 53  'ENGINEERED MUTATION' 36  192 
6  3SH1 LEU F 47  ? UNP Q8WSF8 GLN 55  'ENGINEERED MUTATION' 38  193 
6  3SH1 TRP F 64  ? UNP Q8WSF8 TYR 72  'ENGINEERED MUTATION' 55  194 
6  3SH1 SER F 68  ? UNP Q8WSF8 ARG 76  'ENGINEERED MUTATION' 59  195 
6  3SH1 ASN F 115 ? UNP Q8WSF8 ILE 123 'ENGINEERED MUTATION' 106 196 
6  3SH1 LEU F 117 ? UNP Q8WSF8 VAL 125 'ENGINEERED MUTATION' 108 197 
6  3SH1 ASN F 119 ? UNP Q8WSF8 THR 127 'ENGINEERED MUTATION' 110 198 
6  3SH1 SER F 120 ? UNP Q8WSF8 HIS 128 'ENGINEERED MUTATION' 111 199 
6  3SH1 SER F 121 ? UNP Q8WSF8 ASP 129 'ENGINEERED MUTATION' 112 200 
6  3SH1 HIS F 123 ? UNP Q8WSF8 SER 131 'ENGINEERED MUTATION' 114 201 
6  3SH1 GLN F 125 ? UNP Q8WSF8 MET 133 'ENGINEERED MUTATION' 116 202 
6  3SH1 TYR F 126 ? UNP Q8WSF8 PHE 134 'ENGINEERED MUTATION' 117 203 
6  3SH1 LEU F 127 ? UNP Q8WSF8 ILE 135 'ENGINEERED MUTATION' 118 204 
6  3SH1 SER F 157 ? UNP Q8WSF8 VAL 165 'ENGINEERED MUTATION' 148 205 
6  3SH1 GLY F 159 ? UNP Q8WSF8 SER 167 'ENGINEERED MUTATION' 150 206 
6  3SH1 TRP F 161 ? UNP Q8WSF8 PHE 169 'ENGINEERED MUTATION' 152 207 
6  3SH1 SER F 193 ? UNP Q8WSF8 GLN 201 'ENGINEERED MUTATION' 184 208 
6  3SH1 GLU F 194 ? UNP Q8WSF8 VAL 202 'ENGINEERED MUTATION' 185 209 
6  3SH1 ARG F 195 ? UNP Q8WSF8 GLN 203 'ENGINEERED MUTATION' 186 210 
6  3SH1 PHE F 196 ? UNP Q8WSF8 HIS 204 'ENGINEERED MUTATION' 187 211 
6  3SH1 GLU F 198 ? UNP Q8WSF8 SER 206 'ENGINEERED MUTATION' 189 212 
6  3SH1 LYS F 201 ? UNP Q8WSF8 PRO 209 'ENGINEERED MUTATION' 192 213 
6  3SH1 PRO F 205 ? UNP Q8WSF8 ILE 213 'ENGINEERED MUTATION' 196 214 
6  3SH1 SER F 229 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      220 215 
6  3SH1 ARG F 230 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      221 216 
7  3SH1 ASP G 1   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -8  217 
7  3SH1 TYR G 2   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -7  218 
7  3SH1 LYS G 3   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -6  219 
7  3SH1 ASP G 4   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -5  220 
7  3SH1 ASP G 5   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -4  221 
7  3SH1 ASP G 6   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -3  222 
7  3SH1 ASP G 7   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -2  223 
7  3SH1 LYS G 8   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -1  224 
7  3SH1 LEU G 9   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      0   225 
7  3SH1 TYR G 41  ? UNP Q8WSF8 THR 49  'ENGINEERED MUTATION' 32  226 
7  3SH1 SER G 43  ? UNP Q8WSF8 GLY 51  'ENGINEERED MUTATION' 34  227 
7  3SH1 SER G 45  ? UNP Q8WSF8 THR 53  'ENGINEERED MUTATION' 36  228 
7  3SH1 LEU G 47  ? UNP Q8WSF8 GLN 55  'ENGINEERED MUTATION' 38  229 
7  3SH1 TRP G 64  ? UNP Q8WSF8 TYR 72  'ENGINEERED MUTATION' 55  230 
7  3SH1 SER G 68  ? UNP Q8WSF8 ARG 76  'ENGINEERED MUTATION' 59  231 
7  3SH1 ASN G 115 ? UNP Q8WSF8 ILE 123 'ENGINEERED MUTATION' 106 232 
7  3SH1 LEU G 117 ? UNP Q8WSF8 VAL 125 'ENGINEERED MUTATION' 108 233 
7  3SH1 ASN G 119 ? UNP Q8WSF8 THR 127 'ENGINEERED MUTATION' 110 234 
7  3SH1 SER G 120 ? UNP Q8WSF8 HIS 128 'ENGINEERED MUTATION' 111 235 
7  3SH1 SER G 121 ? UNP Q8WSF8 ASP 129 'ENGINEERED MUTATION' 112 236 
7  3SH1 HIS G 123 ? UNP Q8WSF8 SER 131 'ENGINEERED MUTATION' 114 237 
7  3SH1 GLN G 125 ? UNP Q8WSF8 MET 133 'ENGINEERED MUTATION' 116 238 
7  3SH1 TYR G 126 ? UNP Q8WSF8 PHE 134 'ENGINEERED MUTATION' 117 239 
7  3SH1 LEU G 127 ? UNP Q8WSF8 ILE 135 'ENGINEERED MUTATION' 118 240 
7  3SH1 SER G 157 ? UNP Q8WSF8 VAL 165 'ENGINEERED MUTATION' 148 241 
7  3SH1 GLY G 159 ? UNP Q8WSF8 SER 167 'ENGINEERED MUTATION' 150 242 
7  3SH1 TRP G 161 ? UNP Q8WSF8 PHE 169 'ENGINEERED MUTATION' 152 243 
7  3SH1 SER G 193 ? UNP Q8WSF8 GLN 201 'ENGINEERED MUTATION' 184 244 
7  3SH1 GLU G 194 ? UNP Q8WSF8 VAL 202 'ENGINEERED MUTATION' 185 245 
7  3SH1 ARG G 195 ? UNP Q8WSF8 GLN 203 'ENGINEERED MUTATION' 186 246 
7  3SH1 PHE G 196 ? UNP Q8WSF8 HIS 204 'ENGINEERED MUTATION' 187 247 
7  3SH1 GLU G 198 ? UNP Q8WSF8 SER 206 'ENGINEERED MUTATION' 189 248 
7  3SH1 LYS G 201 ? UNP Q8WSF8 PRO 209 'ENGINEERED MUTATION' 192 249 
7  3SH1 PRO G 205 ? UNP Q8WSF8 ILE 213 'ENGINEERED MUTATION' 196 250 
7  3SH1 SER G 229 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      220 251 
7  3SH1 ARG G 230 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      221 252 
8  3SH1 ASP H 1   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -8  253 
8  3SH1 TYR H 2   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -7  254 
8  3SH1 LYS H 3   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -6  255 
8  3SH1 ASP H 4   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -5  256 
8  3SH1 ASP H 5   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -4  257 
8  3SH1 ASP H 6   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -3  258 
8  3SH1 ASP H 7   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -2  259 
8  3SH1 LYS H 8   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -1  260 
8  3SH1 LEU H 9   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      0   261 
8  3SH1 TYR H 41  ? UNP Q8WSF8 THR 49  'ENGINEERED MUTATION' 32  262 
8  3SH1 SER H 43  ? UNP Q8WSF8 GLY 51  'ENGINEERED MUTATION' 34  263 
8  3SH1 SER H 45  ? UNP Q8WSF8 THR 53  'ENGINEERED MUTATION' 36  264 
8  3SH1 LEU H 47  ? UNP Q8WSF8 GLN 55  'ENGINEERED MUTATION' 38  265 
8  3SH1 TRP H 64  ? UNP Q8WSF8 TYR 72  'ENGINEERED MUTATION' 55  266 
8  3SH1 SER H 68  ? UNP Q8WSF8 ARG 76  'ENGINEERED MUTATION' 59  267 
8  3SH1 ASN H 115 ? UNP Q8WSF8 ILE 123 'ENGINEERED MUTATION' 106 268 
8  3SH1 LEU H 117 ? UNP Q8WSF8 VAL 125 'ENGINEERED MUTATION' 108 269 
8  3SH1 ASN H 119 ? UNP Q8WSF8 THR 127 'ENGINEERED MUTATION' 110 270 
8  3SH1 SER H 120 ? UNP Q8WSF8 HIS 128 'ENGINEERED MUTATION' 111 271 
8  3SH1 SER H 121 ? UNP Q8WSF8 ASP 129 'ENGINEERED MUTATION' 112 272 
8  3SH1 HIS H 123 ? UNP Q8WSF8 SER 131 'ENGINEERED MUTATION' 114 273 
8  3SH1 GLN H 125 ? UNP Q8WSF8 MET 133 'ENGINEERED MUTATION' 116 274 
8  3SH1 TYR H 126 ? UNP Q8WSF8 PHE 134 'ENGINEERED MUTATION' 117 275 
8  3SH1 LEU H 127 ? UNP Q8WSF8 ILE 135 'ENGINEERED MUTATION' 118 276 
8  3SH1 SER H 157 ? UNP Q8WSF8 VAL 165 'ENGINEERED MUTATION' 148 277 
8  3SH1 GLY H 159 ? UNP Q8WSF8 SER 167 'ENGINEERED MUTATION' 150 278 
8  3SH1 TRP H 161 ? UNP Q8WSF8 PHE 169 'ENGINEERED MUTATION' 152 279 
8  3SH1 SER H 193 ? UNP Q8WSF8 GLN 201 'ENGINEERED MUTATION' 184 280 
8  3SH1 GLU H 194 ? UNP Q8WSF8 VAL 202 'ENGINEERED MUTATION' 185 281 
8  3SH1 ARG H 195 ? UNP Q8WSF8 GLN 203 'ENGINEERED MUTATION' 186 282 
8  3SH1 PHE H 196 ? UNP Q8WSF8 HIS 204 'ENGINEERED MUTATION' 187 283 
8  3SH1 GLU H 198 ? UNP Q8WSF8 SER 206 'ENGINEERED MUTATION' 189 284 
8  3SH1 LYS H 201 ? UNP Q8WSF8 PRO 209 'ENGINEERED MUTATION' 192 285 
8  3SH1 PRO H 205 ? UNP Q8WSF8 ILE 213 'ENGINEERED MUTATION' 196 286 
8  3SH1 SER H 229 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      220 287 
8  3SH1 ARG H 230 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      221 288 
9  3SH1 ASP I 1   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -8  289 
9  3SH1 TYR I 2   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -7  290 
9  3SH1 LYS I 3   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -6  291 
9  3SH1 ASP I 4   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -5  292 
9  3SH1 ASP I 5   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -4  293 
9  3SH1 ASP I 6   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -3  294 
9  3SH1 ASP I 7   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -2  295 
9  3SH1 LYS I 8   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -1  296 
9  3SH1 LEU I 9   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      0   297 
9  3SH1 TYR I 41  ? UNP Q8WSF8 THR 49  'ENGINEERED MUTATION' 32  298 
9  3SH1 SER I 43  ? UNP Q8WSF8 GLY 51  'ENGINEERED MUTATION' 34  299 
9  3SH1 SER I 45  ? UNP Q8WSF8 THR 53  'ENGINEERED MUTATION' 36  300 
9  3SH1 LEU I 47  ? UNP Q8WSF8 GLN 55  'ENGINEERED MUTATION' 38  301 
9  3SH1 TRP I 64  ? UNP Q8WSF8 TYR 72  'ENGINEERED MUTATION' 55  302 
9  3SH1 SER I 68  ? UNP Q8WSF8 ARG 76  'ENGINEERED MUTATION' 59  303 
9  3SH1 ASN I 115 ? UNP Q8WSF8 ILE 123 'ENGINEERED MUTATION' 106 304 
9  3SH1 LEU I 117 ? UNP Q8WSF8 VAL 125 'ENGINEERED MUTATION' 108 305 
9  3SH1 ASN I 119 ? UNP Q8WSF8 THR 127 'ENGINEERED MUTATION' 110 306 
9  3SH1 SER I 120 ? UNP Q8WSF8 HIS 128 'ENGINEERED MUTATION' 111 307 
9  3SH1 SER I 121 ? UNP Q8WSF8 ASP 129 'ENGINEERED MUTATION' 112 308 
9  3SH1 HIS I 123 ? UNP Q8WSF8 SER 131 'ENGINEERED MUTATION' 114 309 
9  3SH1 GLN I 125 ? UNP Q8WSF8 MET 133 'ENGINEERED MUTATION' 116 310 
9  3SH1 TYR I 126 ? UNP Q8WSF8 PHE 134 'ENGINEERED MUTATION' 117 311 
9  3SH1 LEU I 127 ? UNP Q8WSF8 ILE 135 'ENGINEERED MUTATION' 118 312 
9  3SH1 SER I 157 ? UNP Q8WSF8 VAL 165 'ENGINEERED MUTATION' 148 313 
9  3SH1 GLY I 159 ? UNP Q8WSF8 SER 167 'ENGINEERED MUTATION' 150 314 
9  3SH1 TRP I 161 ? UNP Q8WSF8 PHE 169 'ENGINEERED MUTATION' 152 315 
9  3SH1 SER I 193 ? UNP Q8WSF8 GLN 201 'ENGINEERED MUTATION' 184 316 
9  3SH1 GLU I 194 ? UNP Q8WSF8 VAL 202 'ENGINEERED MUTATION' 185 317 
9  3SH1 ARG I 195 ? UNP Q8WSF8 GLN 203 'ENGINEERED MUTATION' 186 318 
9  3SH1 PHE I 196 ? UNP Q8WSF8 HIS 204 'ENGINEERED MUTATION' 187 319 
9  3SH1 GLU I 198 ? UNP Q8WSF8 SER 206 'ENGINEERED MUTATION' 189 320 
9  3SH1 LYS I 201 ? UNP Q8WSF8 PRO 209 'ENGINEERED MUTATION' 192 321 
9  3SH1 PRO I 205 ? UNP Q8WSF8 ILE 213 'ENGINEERED MUTATION' 196 322 
9  3SH1 SER I 229 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      220 323 
9  3SH1 ARG I 230 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      221 324 
10 3SH1 ASP J 1   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -8  325 
10 3SH1 TYR J 2   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -7  326 
10 3SH1 LYS J 3   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -6  327 
10 3SH1 ASP J 4   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -5  328 
10 3SH1 ASP J 5   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -4  329 
10 3SH1 ASP J 6   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -3  330 
10 3SH1 ASP J 7   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -2  331 
10 3SH1 LYS J 8   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      -1  332 
10 3SH1 LEU J 9   ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      0   333 
10 3SH1 TYR J 41  ? UNP Q8WSF8 THR 49  'ENGINEERED MUTATION' 32  334 
10 3SH1 SER J 43  ? UNP Q8WSF8 GLY 51  'ENGINEERED MUTATION' 34  335 
10 3SH1 SER J 45  ? UNP Q8WSF8 THR 53  'ENGINEERED MUTATION' 36  336 
10 3SH1 LEU J 47  ? UNP Q8WSF8 GLN 55  'ENGINEERED MUTATION' 38  337 
10 3SH1 TRP J 64  ? UNP Q8WSF8 TYR 72  'ENGINEERED MUTATION' 55  338 
10 3SH1 SER J 68  ? UNP Q8WSF8 ARG 76  'ENGINEERED MUTATION' 59  339 
10 3SH1 ASN J 115 ? UNP Q8WSF8 ILE 123 'ENGINEERED MUTATION' 106 340 
10 3SH1 LEU J 117 ? UNP Q8WSF8 VAL 125 'ENGINEERED MUTATION' 108 341 
10 3SH1 ASN J 119 ? UNP Q8WSF8 THR 127 'ENGINEERED MUTATION' 110 342 
10 3SH1 SER J 120 ? UNP Q8WSF8 HIS 128 'ENGINEERED MUTATION' 111 343 
10 3SH1 SER J 121 ? UNP Q8WSF8 ASP 129 'ENGINEERED MUTATION' 112 344 
10 3SH1 HIS J 123 ? UNP Q8WSF8 SER 131 'ENGINEERED MUTATION' 114 345 
10 3SH1 GLN J 125 ? UNP Q8WSF8 MET 133 'ENGINEERED MUTATION' 116 346 
10 3SH1 TYR J 126 ? UNP Q8WSF8 PHE 134 'ENGINEERED MUTATION' 117 347 
10 3SH1 LEU J 127 ? UNP Q8WSF8 ILE 135 'ENGINEERED MUTATION' 118 348 
10 3SH1 SER J 157 ? UNP Q8WSF8 VAL 165 'ENGINEERED MUTATION' 148 349 
10 3SH1 GLY J 159 ? UNP Q8WSF8 SER 167 'ENGINEERED MUTATION' 150 350 
10 3SH1 TRP J 161 ? UNP Q8WSF8 PHE 169 'ENGINEERED MUTATION' 152 351 
10 3SH1 SER J 193 ? UNP Q8WSF8 GLN 201 'ENGINEERED MUTATION' 184 352 
10 3SH1 GLU J 194 ? UNP Q8WSF8 VAL 202 'ENGINEERED MUTATION' 185 353 
10 3SH1 ARG J 195 ? UNP Q8WSF8 GLN 203 'ENGINEERED MUTATION' 186 354 
10 3SH1 PHE J 196 ? UNP Q8WSF8 HIS 204 'ENGINEERED MUTATION' 187 355 
10 3SH1 GLU J 198 ? UNP Q8WSF8 SER 206 'ENGINEERED MUTATION' 189 356 
10 3SH1 LYS J 201 ? UNP Q8WSF8 PRO 209 'ENGINEERED MUTATION' 192 357 
10 3SH1 PRO J 205 ? UNP Q8WSF8 ILE 213 'ENGINEERED MUTATION' 196 358 
10 3SH1 SER J 229 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      220 359 
10 3SH1 ARG J 230 ? UNP Q8WSF8 ?   ?   'EXPRESSION TAG'      221 360 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACT non-polymer         . 'ACETATE ION'                   ? 'C2 H3 O2 -1'    59.044  
ALA 'L-peptide linking' y ALANINE                         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                 ? 'C4 H7 N O4'     133.103 
BMA D-saccharide        . BETA-D-MANNOSE                  ? 'C6 H12 O6'      180.156 
CYS 'L-peptide linking' y CYSTEINE                        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                 ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                      ? 'C5 H11 N O2 S'  149.211 
MG  non-polymer         . 'MAGNESIUM ION'                 ? 'Mg 2'           24.305  
MLK non-polymer         . METHYLLYCACONITINE              ? 'C37 H50 N2 O10' 682.800 
MPD non-polymer         . '(4S)-2-METHYL-2,4-PENTANEDIOL' ? 'C6 H14 O2'      118.174 
MRD non-polymer         . '(4R)-2-METHYLPENTANE-2,4-DIOL' ? 'C6 H14 O2'      118.174 
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 
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          3SH1 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.02 
_exptl_crystal.density_percent_sol   59.22 
_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              6.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
'30%MPD, 0.1M Na Cacodylate, 0.2M Magnesium Acetate, pH 6.5, 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   2011-02-03 
_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                    'Double crystal, 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   1.000 
_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             ? 
_diffrn_source.pdbx_wavelength_list        1.000 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     3SH1 
_reflns.observed_criterion_sigma_I   -3 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             50.00 
_reflns.d_resolution_high            2.90 
_reflns.number_obs                   85106 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         73.4 
_reflns.pdbx_Rmerge_I_obs            0.138 
_reflns.pdbx_Rsym_value              0.138 
_reflns.pdbx_netI_over_sigmaI        13.909 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              7.5 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.90 
_reflns_shell.d_res_low              2.95 
_reflns_shell.percent_possible_all   95.7 
_reflns_shell.Rmerge_I_obs           0.952 
_reflns_shell.pdbx_Rsym_value        0.000 
_reflns_shell.meanI_over_sigI_obs    1.50 
_reflns_shell.pdbx_redundancy        6.6 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 3SH1 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     64746 
_refine.ls_number_reflns_all                     64773 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.19 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             48.054 
_refine.ls_d_res_high                            2.900 
_refine.ls_percent_reflns_obs                    93.51 
_refine.ls_R_factor_obs                          0.2140 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2130 
_refine.ls_R_factor_R_free                       0.2580 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 2.35 
_refine.ls_number_reflns_R_free                  1521 
_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]                            32.5208 
_refine.aniso_B[2][2]                            -11.0835 
_refine.aniso_B[3][3]                            -21.4373 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -10.4671 
_refine.aniso_B[2][3]                            -0.0000 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.303 
_refine.solvent_model_param_bsol                 44.137 
_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                      'Modified via pymol PDB entry 2BYR' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             Isotropic 
_refine.pdbx_stereochemistry_target_values       MLHL 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.38 
_refine.pdbx_overall_phase_error                 28.89 
_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.pdbx_overall_ESU_R                       ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        17224 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         883 
_refine_hist.number_atoms_solvent             71 
_refine_hist.number_atoms_total               18178 
_refine_hist.d_res_high                       2.900 
_refine_hist.d_res_low                        48.054 
# 
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           0.013  ? ? 18884 'X-RAY DIFFRACTION' ? 
f_angle_d          1.442  ? ? 25916 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 20.148 ? ? 7207  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.092  ? ? 2889  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.007  ? ? 3250  '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' . 2.9000 2.9936  4800 0.3273 78.00 0.3861 . . 118 . . . . 
'X-RAY DIFFRACTION' . 2.9936 3.1006  5120 0.2795 84.00 0.3113 . . 106 . . . . 
'X-RAY DIFFRACTION' . 3.1006 3.2247  5443 0.2496 89.00 0.3349 . . 127 . . . . 
'X-RAY DIFFRACTION' . 3.2247 3.3714  5656 0.2360 92.00 0.3088 . . 143 . . . . 
'X-RAY DIFFRACTION' . 3.3714 3.5491  5813 0.2126 95.00 0.2876 . . 145 . . . . 
'X-RAY DIFFRACTION' . 3.5491 3.7714  5915 0.2027 97.00 0.2518 . . 148 . . . . 
'X-RAY DIFFRACTION' . 3.7714 4.0625  5981 0.1959 97.00 0.2671 . . 140 . . . . 
'X-RAY DIFFRACTION' . 4.0625 4.4710  6062 0.1736 99.00 0.2190 . . 146 . . . . 
'X-RAY DIFFRACTION' . 4.4710 5.1173  6112 0.1657 99.00 0.1932 . . 149 . . . . 
'X-RAY DIFFRACTION' . 5.1173 6.4448  6102 0.2170 99.00 0.2485 . . 148 . . . . 
'X-RAY DIFFRACTION' . 6.4448 48.0609 6221 0.2357 99.00 0.2653 . . 151 . . . . 
# 
_struct.entry_id                  3SH1 
_struct.title                     'Ac-AChBP ligand binding domain mutated to human alpha-7 nAChR' 
_struct.pdbx_descriptor           'Soluble acetylcholine receptor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3SH1 
_struct_keywords.pdbx_keywords   RECEPTOR 
_struct_keywords.text            
'Human nicotinic acetylcholine receptor binding protein, Methyllycaconitine Binding, Glycosylation, RECEPTOR' 
# 
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 3 ? 
N  N N 4 ? 
O  N N 5 ? 
P  N N 6 ? 
Q  N N 6 ? 
R  N N 2 ? 
S  N N 3 ? 
T  N N 3 ? 
U  N N 4 ? 
V  N N 5 ? 
W  N N 2 ? 
X  N N 3 ? 
Y  N N 4 ? 
Z  N N 6 ? 
AA N N 5 ? 
BA N N 3 ? 
CA N N 3 ? 
DA N N 4 ? 
EA N N 2 ? 
FA N N 3 ? 
GA N N 3 ? 
HA N N 5 ? 
IA N N 3 ? 
JA N N 4 ? 
KA N N 5 ? 
LA N N 3 ? 
MA N N 4 ? 
NA N N 7 ? 
OA N N 3 ? 
PA N N 3 ? 
QA N N 4 ? 
RA N N 6 ? 
SA N N 6 ? 
TA N N 3 ? 
UA N N 3 ? 
VA N N 8 ? 
WA N N 4 ? 
XA N N 2 ? 
YA N N 3 ? 
ZA N N 3 ? 
AB N N 4 ? 
BB N N 6 ? 
CB N N 6 ? 
DB N N 3 ? 
EB N N 3 ? 
FB N N 8 ? 
GB N N 4 ? 
HB N N 9 ? 
IB N N 9 ? 
JB N N 9 ? 
KB N N 9 ? 
LB N N 9 ? 
MB N N 9 ? 
NB N N 9 ? 
OB N N 9 ? 
PB N N 9 ? 
QB N N 9 ? 
# 
_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 4  ? ASN A 24 ? ASP A -5 ASN A 15 1 ? 21 
HELX_P HELX_P2  2  ASN A 72 ? MET A 75 ? ASN A 63 MET A 66 5 ? 4  
HELX_P HELX_P3  3  ASP A 77 ? GLY A 82 ? ASP A 68 GLY A 73 5 ? 6  
HELX_P HELX_P4  4  ALA A 92 ? ILE A 94 ? ALA A 83 ILE A 85 5 ? 3  
HELX_P HELX_P5  5  ASP B 4  ? ASN B 24 ? ASP B -5 ASN B 15 1 ? 21 
HELX_P HELX_P6  6  ASN B 72 ? MET B 75 ? ASN B 63 MET B 66 5 ? 4  
HELX_P HELX_P7  7  ASP B 77 ? TYR B 81 ? ASP B 68 TYR B 72 5 ? 5  
HELX_P HELX_P8  8  ALA B 92 ? ILE B 94 ? ALA B 83 ILE B 85 5 ? 3  
HELX_P HELX_P9  9  ASP C 4  ? ASN C 24 ? ASP C -5 ASN C 15 1 ? 21 
HELX_P HELX_P10 10 ASN C 72 ? MET C 75 ? ASN C 63 MET C 66 5 ? 4  
HELX_P HELX_P11 11 ASP C 77 ? GLY C 82 ? ASP C 68 GLY C 73 5 ? 6  
HELX_P HELX_P12 12 ASP D 5  ? ASN D 24 ? ASP D -4 ASN D 15 1 ? 20 
HELX_P HELX_P13 13 ASN D 72 ? MET D 75 ? ASN D 63 MET D 66 5 ? 4  
HELX_P HELX_P14 14 ASP E 4  ? ASN E 24 ? ASP E -5 ASN E 15 1 ? 21 
HELX_P HELX_P15 15 ASP F 4  ? ASN F 24 ? ASP F -5 ASN F 15 1 ? 21 
HELX_P HELX_P16 16 ASP F 77 ? GLY F 82 ? ASP F 68 GLY F 73 5 ? 6  
HELX_P HELX_P17 17 ALA F 92 ? ILE F 94 ? ALA F 83 ILE F 85 5 ? 3  
HELX_P HELX_P18 18 ASP G 4  ? ASN G 24 ? ASP G -5 ASN G 15 1 ? 21 
HELX_P HELX_P19 19 ALA G 92 ? ILE G 94 ? ALA G 83 ILE G 85 5 ? 3  
HELX_P HELX_P20 20 ASP H 5  ? PHE H 23 ? ASP H -4 PHE H 14 1 ? 19 
HELX_P HELX_P21 21 ASN H 72 ? MET H 75 ? ASN H 63 MET H 66 5 ? 4  
HELX_P HELX_P22 22 ASP H 77 ? GLY H 82 ? ASP H 68 GLY H 73 5 ? 6  
HELX_P HELX_P23 23 ALA H 92 ? ILE H 94 ? ALA H 83 ILE H 85 5 ? 3  
HELX_P HELX_P24 24 ASP I 5  ? ASN I 24 ? ASP I -4 ASN I 15 1 ? 20 
HELX_P HELX_P25 25 ASP I 77 ? GLY I 82 ? ASP I 68 GLY I 73 5 ? 6  
HELX_P HELX_P26 26 ALA I 92 ? ILE I 94 ? ALA I 83 ILE I 85 5 ? 3  
HELX_P HELX_P27 27 ASP J 4  ? PHE J 23 ? ASP J -5 PHE J 14 1 ? 20 
# 
_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 136 SG  ? ? ? 1_555 A  CYS 149 SG ? ? A CYS 127 A CYS 140 1_555 ? ? ? ? ? ? ? 1.751 ? 
disulf2  disulf ? ? A  CYS 199 SG  ? ? ? 1_555 A  CYS 200 SG ? ? A CYS 190 A CYS 191 1_555 ? ? ? ? ? ? ? 2.619 ? 
disulf3  disulf ? ? B  CYS 136 SG  ? ? ? 1_555 B  CYS 149 SG ? ? B CYS 127 B CYS 140 1_555 ? ? ? ? ? ? ? 2.016 ? 
disulf4  disulf ? ? B  CYS 199 SG  ? ? ? 1_555 B  CYS 200 SG ? ? B CYS 190 B CYS 191 1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf5  disulf ? ? C  CYS 136 SG  ? ? ? 1_555 C  CYS 149 SG ? ? C CYS 127 C CYS 140 1_555 ? ? ? ? ? ? ? 1.751 ? 
disulf6  disulf ? ? C  CYS 199 SG  ? ? ? 1_555 C  CYS 200 SG ? ? C CYS 190 C CYS 191 1_555 ? ? ? ? ? ? ? 2.386 ? 
disulf7  disulf ? ? D  CYS 136 SG  ? ? ? 1_555 D  CYS 149 SG ? ? D CYS 127 D CYS 140 1_555 ? ? ? ? ? ? ? 2.017 ? 
disulf8  disulf ? ? D  CYS 199 SG  ? ? ? 1_555 D  CYS 200 SG ? ? D CYS 190 D CYS 191 1_555 ? ? ? ? ? ? ? 2.082 ? 
disulf9  disulf ? ? E  CYS 136 SG  ? ? ? 1_555 E  CYS 149 SG ? ? E CYS 127 E CYS 140 1_555 ? ? ? ? ? ? ? 1.650 ? 
disulf10 disulf ? ? E  CYS 199 SG  ? ? ? 1_555 E  CYS 200 SG ? ? E CYS 190 E CYS 191 1_555 ? ? ? ? ? ? ? 2.290 ? 
disulf11 disulf ? ? F  CYS 136 SG  ? ? ? 1_555 F  CYS 149 SG ? ? F CYS 127 F CYS 140 1_555 ? ? ? ? ? ? ? 2.017 ? 
disulf12 disulf ? ? F  CYS 199 SG  ? ? ? 1_555 F  CYS 200 SG ? ? F CYS 190 F CYS 191 1_555 ? ? ? ? ? ? ? 2.339 ? 
disulf13 disulf ? ? G  CYS 136 SG  ? ? ? 1_555 G  CYS 149 SG ? ? G CYS 127 G CYS 140 1_555 ? ? ? ? ? ? ? 2.023 ? 
disulf14 disulf ? ? G  CYS 199 SG  ? ? ? 1_555 G  CYS 200 SG ? ? G CYS 190 G CYS 191 1_555 ? ? ? ? ? ? ? 2.281 ? 
disulf15 disulf ? ? H  CYS 136 SG  ? ? ? 1_555 H  CYS 149 SG ? ? H CYS 127 H CYS 140 1_555 ? ? ? ? ? ? ? 2.001 ? 
disulf16 disulf ? ? H  CYS 199 SG  ? ? ? 1_555 H  CYS 200 SG ? ? H CYS 190 H CYS 191 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf17 disulf ? ? I  CYS 136 SG  ? ? ? 1_555 I  CYS 149 SG ? ? I CYS 127 I CYS 140 1_555 ? ? ? ? ? ? ? 2.023 ? 
disulf18 disulf ? ? I  CYS 199 SG  ? ? ? 1_555 I  CYS 200 SG ? ? I CYS 190 I CYS 191 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf19 disulf ? ? J  CYS 136 SG  ? ? ? 1_555 J  CYS 149 SG ? ? J CYS 127 J CYS 140 1_555 ? ? ? ? ? ? ? 2.010 ? 
disulf20 disulf ? ? J  CYS 199 SG  ? ? ? 1_555 J  CYS 200 SG ? ? J CYS 190 J CYS 191 1_555 ? ? ? ? ? ? ? 2.057 ? 
covale1  covale ? ? A  ASN 119 ND2 ? ? ? 1_555 L  NAG .   C1 ? ? A ASN 110 A NAG 250 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale2  covale ? ? B  ASN 119 ND2 ? ? ? 1_555 S  NAG .   C1 ? ? B ASN 110 B NAG 250 1_555 ? ? ? ? ? ? ? 1.497 ? 
covale3  covale ? ? C  ASN 119 ND2 ? ? ? 1_555 X  NAG .   C1 ? ? C ASN 110 C NAG 250 1_555 ? ? ? ? ? ? ? 1.726 ? 
covale4  covale ? ? D  ASN 119 ND2 ? ? ? 1_555 BA NAG .   C1 ? ? D ASN 110 D NAG 250 1_555 ? ? ? ? ? ? ? 1.483 ? 
covale5  covale ? ? E  ASN 119 ND2 ? ? ? 1_555 FA NAG .   C1 ? ? E ASN 110 E NAG 250 1_555 ? ? ? ? ? ? ? 1.625 ? 
covale6  covale ? ? F  ASN 119 ND2 ? ? ? 1_555 LA NAG .   C1 ? ? F ASN 110 F NAG 250 1_555 ? ? ? ? ? ? ? 1.494 ? 
covale7  covale ? ? G  ASN 119 ND2 ? ? ? 1_555 OA NAG .   C1 ? ? G ASN 110 G NAG 250 1_555 ? ? ? ? ? ? ? 1.458 ? 
covale8  covale ? ? H  ASN 119 ND2 ? ? ? 1_555 TA NAG .   C1 ? ? H ASN 110 H NAG 250 1_555 ? ? ? ? ? ? ? 1.588 ? 
covale9  covale ? ? I  ASN 119 ND2 ? ? ? 1_555 YA NAG .   C1 ? ? I ASN 110 I NAG 250 1_555 ? ? ? ? ? ? ? 1.444 ? 
covale10 covale ? ? J  ASN 119 ND2 ? ? ? 1_555 DB NAG .   C1 ? ? J ASN 110 J NAG 250 1_555 ? ? ? ? ? ? ? 1.818 ? 
covale11 covale ? ? B  ASN 83  ND2 A ? ? 1_555 T  NAG .   C1 A ? B ASN 74  B NAG 275 1_555 ? ? ? ? ? ? ? 1.524 ? 
covale12 covale ? ? B  ASN 83  ND2 B ? ? 1_555 T  NAG .   C1 B ? B ASN 74  B NAG 275 1_555 ? ? ? ? ? ? ? 1.377 ? 
covale13 covale ? ? E  ASN 83  ND2 A ? ? 1_555 IA NAG .   C1 A ? E ASN 74  E NAG 275 1_555 ? ? ? ? ? ? ? 1.531 ? 
covale14 covale ? ? E  ASN 83  ND2 B ? ? 1_555 IA NAG .   C1 B ? E ASN 74  E NAG 275 1_555 ? ? ? ? ? ? ? 1.473 ? 
covale15 covale ? ? I  ASN 83  ND2 A ? ? 1_555 ZA NAG .   C1 A ? I ASN 74  I NAG 275 1_555 ? ? ? ? ? ? ? 1.506 ? 
covale16 covale ? ? I  ASN 83  ND2 B ? ? 1_555 ZA NAG .   C1 B ? I ASN 74  I NAG 275 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale17 covale ? ? L  NAG .   O4  ? ? ? 1_555 M  NAG .   C1 ? ? A NAG 250 A NAG 251 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale18 covale ? ? BA NAG .   O4  ? ? ? 1_555 CA NAG .   C1 ? ? D NAG 250 D NAG 251 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale19 covale ? ? FA NAG .   O4  ? ? ? 1_555 GA NAG .   C1 ? ? E NAG 250 E NAG 251 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale20 covale ? ? OA NAG .   O4  ? ? ? 1_555 PA NAG .   C1 ? ? G NAG 250 G NAG 251 1_555 ? ? ? ? ? ? ? 1.439 ? 
covale21 covale ? ? TA NAG .   O4  ? ? ? 1_555 UA NAG .   C1 ? ? H NAG 250 H NAG 251 1_555 ? ? ? ? ? ? ? 1.347 ? 
covale22 covale ? ? UA NAG .   O4  ? ? ? 1_555 VA BMA .   C1 ? ? H NAG 251 H BMA 252 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale23 covale ? ? DB NAG .   O4  ? ? ? 1_555 EB NAG .   C1 ? ? J NAG 250 J NAG 251 1_555 ? ? ? ? ? ? ? 1.390 ? 
covale24 covale ? ? EB NAG .   O4  ? ? ? 1_555 FB BMA .   C1 ? ? J NAG 251 J BMA 252 1_555 ? ? ? ? ? ? ? 1.453 ? 
metalc1  metalc ? ? G  ASP 6   OD2 ? ? ? 1_555 K  MG  .   MG ? ? G ASP -3  A MG  222 1_555 ? ? ? ? ? ? ? 2.041 ? 
metalc2  metalc ? ? I  ASP 6   OD2 ? ? ? 1_555 XA MG  .   MG ? ? I ASP -3  I MG  222 1_555 ? ? ? ? ? ? ? 2.073 ? 
metalc3  metalc ? ? J  ASP 6   OD2 ? ? ? 1_555 W  MG  .   MG ? ? J ASP -3  C MG  222 1_555 ? ? ? ? ? ? ? 2.093 ? 
metalc4  metalc ? ? D  ASP 6   OD1 ? ? ? 1_555 XA MG  .   MG ? ? D ASP -3  I MG  222 1_555 ? ? ? ? ? ? ? 2.101 ? 
metalc5  metalc ? ? A  ASP 6   OD2 ? ? ? 1_555 K  MG  .   MG ? ? A ASP -3  A MG  222 1_555 ? ? ? ? ? ? ? 2.129 ? 
metalc6  metalc ? ? G  ASP 6   OD1 ? ? ? 1_555 K  MG  .   MG ? ? G ASP -3  A MG  222 1_555 ? ? ? ? ? ? ? 2.233 ? 
metalc7  metalc ? ? F  ASP 6   OD2 ? ? ? 1_555 R  MG  .   MG ? ? F ASP -3  B MG  222 1_555 ? ? ? ? ? ? ? 2.237 ? 
metalc8  metalc ? ? B  ASP 6   OD1 ? ? ? 1_555 R  MG  .   MG ? ? B ASP -3  B MG  222 1_555 ? ? ? ? ? ? ? 2.256 ? 
metalc9  metalc ? ? B  ASP 6   OD2 ? ? ? 1_555 R  MG  .   MG ? ? B ASP -3  B MG  222 1_555 ? ? ? ? ? ? ? 2.256 ? 
metalc10 metalc ? ? H  ASP 6   OD2 ? ? ? 1_555 EA MG  .   MG ? ? H ASP -3  E MG  222 1_555 ? ? ? ? ? ? ? 2.294 ? 
metalc11 metalc ? ? C  ASP 6   OD2 ? ? ? 1_555 W  MG  .   MG ? ? C ASP -3  C MG  222 1_555 ? ? ? ? ? ? ? 2.297 ? 
metalc12 metalc ? ? C  ASP 6   OD1 ? ? ? 1_555 W  MG  .   MG ? ? C ASP -3  C MG  222 1_555 ? ? ? ? ? ? ? 2.312 ? 
metalc13 metalc ? ? E  ASP 6   OD1 ? ? ? 1_555 EA MG  .   MG ? ? E ASP -3  E MG  222 1_555 ? ? ? ? ? ? ? 2.372 ? 
metalc14 metalc ? ? A  ASP 6   OD1 ? ? ? 1_555 K  MG  .   MG ? ? A ASP -3  A MG  222 1_555 ? ? ? ? ? ? ? 2.404 ? 
metalc15 metalc ? ? F  ASP 6   OD1 ? ? ? 1_555 R  MG  .   MG ? ? F ASP -3  B MG  222 1_555 ? ? ? ? ? ? ? 2.450 ? 
metalc16 metalc ? ? I  ASP 6   OD1 ? ? ? 1_555 XA MG  .   MG ? ? I ASP -3  I MG  222 1_555 ? ? ? ? ? ? ? 2.509 ? 
metalc17 metalc ? ? E  ASP 6   OD2 ? ? ? 1_555 EA MG  .   MG ? ? E ASP -3  E MG  222 1_555 ? ? ? ? ? ? ? 2.531 ? 
metalc18 metalc ? ? J  ASP 6   OD1 ? ? ? 1_555 W  MG  .   MG ? ? J ASP -3  C MG  222 1_555 ? ? ? ? ? ? ? 2.599 ? 
metalc19 metalc ? ? D  ASP 6   OD2 ? ? ? 1_555 XA MG  .   MG ? ? D ASP -3  I MG  222 1_555 ? ? ? ? ? ? ? 2.681 ? 
metalc20 metalc ? ? H  ASP 6   OD1 ? ? ? 1_555 EA MG  .   MG ? ? H ASP -3  E MG  222 1_555 ? ? ? ? ? ? ? 2.846 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
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  ? 4 ? 
J  ? 6 ? 
K  ? 6 ? 
L  ? 4 ? 
M  ? 6 ? 
N  ? 6 ? 
O  ? 4 ? 
P  ? 6 ? 
Q  ? 6 ? 
R  ? 4 ? 
S  ? 6 ? 
T  ? 6 ? 
U  ? 4 ? 
V  ? 6 ? 
W  ? 6 ? 
X  ? 4 ? 
Y  ? 6 ? 
Z  ? 6 ? 
AA ? 4 ? 
AB ? 6 ? 
AC ? 6 ? 
AD ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A  1 2 ? anti-parallel 
A  2 3 ? anti-parallel 
A  3 4 ? anti-parallel 
A  4 5 ? anti-parallel 
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 
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 
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 
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 
# 
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 ASP A 86  ? SER A 90  ? ASP A 77  SER A 81  
A  2 ASN A 115 ? ASN A 119 ? ASN A 106 ASN A 110 
A  3 HIS A 123 ? TYR A 126 ? HIS A 114 TYR A 117 
A  4 GLU A 58  ? LYS A 70  ? GLU A 49  LYS A 61  
A  5 ALA A 129 ? MET A 135 ? ALA A 120 MET A 126 
A  6 GLN A 109 ? VAL A 110 ? GLN A 100 VAL A 101 
B  1 ASP A 86  ? SER A 90  ? ASP A 77  SER A 81  
B  2 ASN A 115 ? ASN A 119 ? ASN A 106 ASN A 110 
B  3 HIS A 123 ? TYR A 126 ? HIS A 114 TYR A 117 
B  4 GLU A 58  ? LYS A 70  ? GLU A 49  LYS A 61  
B  5 LEU A 38  ? ASP A 53  ? LEU A 29  ASP A 44  
B  6 ILE A 163 ? THR A 167 ? ILE A 154 THR A 158 
C  1 ILE A 99  ? ALA A 101 ? ILE A 90  ALA A 92  
C  2 ALA A 147 ? SER A 155 ? ALA A 138 SER A 146 
C  3 TYR A 204 ? GLU A 215 ? TYR A 195 GLU A 206 
C  4 TYR A 183 ? ARG A 195 ? TYR A 174 ARG A 186 
D  1 ASP B 86  ? SER B 90  ? ASP B 77  SER B 81  
D  2 ASN B 115 ? ASN B 119 ? ASN B 106 ASN B 110 
D  3 HIS B 123 ? TYR B 126 ? HIS B 114 TYR B 117 
D  4 GLU B 58  ? LYS B 70  ? GLU B 49  LYS B 61  
D  5 ALA B 129 ? MET B 135 ? ALA B 120 MET B 126 
D  6 GLN B 109 ? VAL B 110 ? GLN B 100 VAL B 101 
E  1 ASP B 86  ? SER B 90  ? ASP B 77  SER B 81  
E  2 ASN B 115 ? ASN B 119 ? ASN B 106 ASN B 110 
E  3 HIS B 123 ? TYR B 126 ? HIS B 114 TYR B 117 
E  4 GLU B 58  ? LYS B 70  ? GLU B 49  LYS B 61  
E  5 LEU B 38  ? ASP B 53  ? LEU B 29  ASP B 44  
E  6 ILE B 163 ? THR B 167 ? ILE B 154 THR B 158 
F  1 ILE B 99  ? ALA B 101 ? ILE B 90  ALA B 92  
F  2 ALA B 147 ? SER B 155 ? ALA B 138 SER B 146 
F  3 TYR B 204 ? GLU B 215 ? TYR B 195 GLU B 206 
F  4 TYR B 183 ? ARG B 195 ? TYR B 174 ARG B 186 
G  1 ASP C 86  ? SER C 90  ? ASP C 77  SER C 81  
G  2 ASN C 115 ? ASN C 119 ? ASN C 106 ASN C 110 
G  3 HIS C 123 ? TYR C 126 ? HIS C 114 TYR C 117 
G  4 GLU C 58  ? LYS C 70  ? GLU C 49  LYS C 61  
G  5 ALA C 129 ? MET C 135 ? ALA C 120 MET C 126 
G  6 GLN C 109 ? VAL C 110 ? GLN C 100 VAL C 101 
H  1 ASP C 86  ? SER C 90  ? ASP C 77  SER C 81  
H  2 ASN C 115 ? ASN C 119 ? ASN C 106 ASN C 110 
H  3 HIS C 123 ? TYR C 126 ? HIS C 114 TYR C 117 
H  4 GLU C 58  ? LYS C 70  ? GLU C 49  LYS C 61  
H  5 LEU C 38  ? ASP C 53  ? LEU C 29  ASP C 44  
H  6 ILE C 163 ? THR C 167 ? ILE C 154 THR C 158 
I  1 ILE C 99  ? ALA C 101 ? ILE C 90  ALA C 92  
I  2 ALA C 147 ? SER C 155 ? ALA C 138 SER C 146 
I  3 TYR C 204 ? GLU C 215 ? TYR C 195 GLU C 206 
I  4 TYR C 183 ? ARG C 195 ? TYR C 174 ARG C 186 
J  1 ASP D 86  ? SER D 90  ? ASP D 77  SER D 81  
J  2 ASN D 115 ? ASN D 119 ? ASN D 106 ASN D 110 
J  3 HIS D 123 ? TYR D 126 ? HIS D 114 TYR D 117 
J  4 GLU D 58  ? LYS D 70  ? GLU D 49  LYS D 61  
J  5 ALA D 129 ? MET D 135 ? ALA D 120 MET D 126 
J  6 GLN D 109 ? VAL D 110 ? GLN D 100 VAL D 101 
K  1 ASP D 86  ? SER D 90  ? ASP D 77  SER D 81  
K  2 ASN D 115 ? ASN D 119 ? ASN D 106 ASN D 110 
K  3 HIS D 123 ? TYR D 126 ? HIS D 114 TYR D 117 
K  4 GLU D 58  ? LYS D 70  ? GLU D 49  LYS D 61  
K  5 LEU D 38  ? ASP D 53  ? LEU D 29  ASP D 44  
K  6 ILE D 163 ? LYS D 166 ? ILE D 154 LYS D 157 
L  1 ILE D 99  ? ALA D 101 ? ILE D 90  ALA D 92  
L  2 ALA D 147 ? SER D 155 ? ALA D 138 SER D 146 
L  3 CYS D 200 ? GLU D 215 ? CYS D 191 GLU D 206 
L  4 TYR D 183 ? TYR D 197 ? TYR D 174 TYR D 188 
M  1 ASP E 86  ? SER E 90  ? ASP E 77  SER E 81  
M  2 ASN E 115 ? ASN E 119 ? ASN E 106 ASN E 110 
M  3 SER E 121 ? TYR E 126 ? SER E 112 TYR E 117 
M  4 GLU E 58  ? MET E 75  ? GLU E 49  MET E 66  
M  5 ALA E 129 ? MET E 135 ? ALA E 120 MET E 126 
M  6 GLN E 109 ? VAL E 110 ? GLN E 100 VAL E 101 
N  1 ASP E 86  ? SER E 90  ? ASP E 77  SER E 81  
N  2 ASN E 115 ? ASN E 119 ? ASN E 106 ASN E 110 
N  3 SER E 121 ? TYR E 126 ? SER E 112 TYR E 117 
N  4 GLU E 58  ? MET E 75  ? GLU E 49  MET E 66  
N  5 LEU E 38  ? ASP E 53  ? LEU E 29  ASP E 44  
N  6 ILE E 163 ? THR E 167 ? ILE E 154 THR E 158 
O  1 ILE E 99  ? ALA E 101 ? ILE E 90  ALA E 92  
O  2 ALA E 147 ? SER E 155 ? ALA E 138 SER E 146 
O  3 TYR E 204 ? GLU E 215 ? TYR E 195 GLU E 206 
O  4 TYR E 183 ? ARG E 195 ? TYR E 174 ARG E 186 
P  1 ASP F 86  ? SER F 90  ? ASP F 77  SER F 81  
P  2 ASN F 115 ? ASN F 119 ? ASN F 106 ASN F 110 
P  3 HIS F 123 ? TYR F 126 ? HIS F 114 TYR F 117 
P  4 GLU F 58  ? LYS F 70  ? GLU F 49  LYS F 61  
P  5 ALA F 129 ? MET F 135 ? ALA F 120 MET F 126 
P  6 GLN F 109 ? VAL F 110 ? GLN F 100 VAL F 101 
Q  1 ASP F 86  ? SER F 90  ? ASP F 77  SER F 81  
Q  2 ASN F 115 ? ASN F 119 ? ASN F 106 ASN F 110 
Q  3 HIS F 123 ? TYR F 126 ? HIS F 114 TYR F 117 
Q  4 GLU F 58  ? LYS F 70  ? GLU F 49  LYS F 61  
Q  5 LEU F 38  ? ASP F 53  ? LEU F 29  ASP F 44  
Q  6 ILE F 163 ? THR F 167 ? ILE F 154 THR F 158 
R  1 ILE F 99  ? ALA F 101 ? ILE F 90  ALA F 92  
R  2 ALA F 147 ? SER F 155 ? ALA F 138 SER F 146 
R  3 PRO F 203 ? GLU F 215 ? PRO F 194 GLU F 206 
R  4 TYR F 183 ? PHE F 196 ? TYR F 174 PHE F 187 
S  1 ASP G 86  ? SER G 90  ? ASP G 77  SER G 81  
S  2 ASN G 115 ? ASN G 119 ? ASN G 106 ASN G 110 
S  3 SER G 121 ? TYR G 126 ? SER G 112 TYR G 117 
S  4 GLU G 58  ? MET G 75  ? GLU G 49  MET G 66  
S  5 ALA G 129 ? MET G 135 ? ALA G 120 MET G 126 
S  6 GLN G 109 ? VAL G 110 ? GLN G 100 VAL G 101 
T  1 ASP G 86  ? SER G 90  ? ASP G 77  SER G 81  
T  2 ASN G 115 ? ASN G 119 ? ASN G 106 ASN G 110 
T  3 SER G 121 ? TYR G 126 ? SER G 112 TYR G 117 
T  4 GLU G 58  ? MET G 75  ? GLU G 49  MET G 66  
T  5 LEU G 38  ? ASP G 53  ? LEU G 29  ASP G 44  
T  6 ILE G 163 ? THR G 167 ? ILE G 154 THR G 158 
U  1 ILE G 99  ? ALA G 101 ? ILE G 90  ALA G 92  
U  2 ALA G 147 ? SER G 155 ? ALA G 138 SER G 146 
U  3 TYR G 204 ? GLU G 215 ? TYR G 195 GLU G 206 
U  4 TYR G 183 ? ARG G 195 ? TYR G 174 ARG G 186 
V  1 ASP H 86  ? SER H 90  ? ASP H 77  SER H 81  
V  2 ASN H 115 ? ASN H 119 ? ASN H 106 ASN H 110 
V  3 HIS H 123 ? TYR H 126 ? HIS H 114 TYR H 117 
V  4 GLU H 58  ? LYS H 70  ? GLU H 49  LYS H 61  
V  5 ALA H 129 ? MET H 135 ? ALA H 120 MET H 126 
V  6 SER H 104 ? VAL H 110 ? SER H 95  VAL H 101 
W  1 ASP H 86  ? SER H 90  ? ASP H 77  SER H 81  
W  2 ASN H 115 ? ASN H 119 ? ASN H 106 ASN H 110 
W  3 HIS H 123 ? TYR H 126 ? HIS H 114 TYR H 117 
W  4 GLU H 58  ? LYS H 70  ? GLU H 49  LYS H 61  
W  5 LEU H 38  ? ASP H 53  ? LEU H 29  ASP H 44  
W  6 ILE H 163 ? THR H 167 ? ILE H 154 THR H 158 
X  1 ILE H 99  ? ALA H 101 ? ILE H 90  ALA H 92  
X  2 ALA H 147 ? SER H 155 ? ALA H 138 SER H 146 
X  3 CYS H 200 ? GLU H 215 ? CYS H 191 GLU H 206 
X  4 TYR H 183 ? TYR H 197 ? TYR H 174 TYR H 188 
Y  1 ASP I 86  ? SER I 90  ? ASP I 77  SER I 81  
Y  2 ASN I 115 ? ASN I 119 ? ASN I 106 ASN I 110 
Y  3 SER I 121 ? TYR I 126 ? SER I 112 TYR I 117 
Y  4 GLU I 58  ? MET I 75  ? GLU I 49  MET I 66  
Y  5 ALA I 129 ? MET I 135 ? ALA I 120 MET I 126 
Y  6 GLN I 109 ? VAL I 110 ? GLN I 100 VAL I 101 
Z  1 ASP I 86  ? SER I 90  ? ASP I 77  SER I 81  
Z  2 ASN I 115 ? ASN I 119 ? ASN I 106 ASN I 110 
Z  3 SER I 121 ? TYR I 126 ? SER I 112 TYR I 117 
Z  4 GLU I 58  ? MET I 75  ? GLU I 49  MET I 66  
Z  5 LEU I 38  ? ASP I 53  ? LEU I 29  ASP I 44  
Z  6 ILE I 163 ? LYS I 166 ? ILE I 154 LYS I 157 
AA 1 ILE I 99  ? ALA I 101 ? ILE I 90  ALA I 92  
AA 2 ALA I 147 ? SER I 155 ? ALA I 138 SER I 146 
AA 3 TYR I 204 ? GLU I 215 ? TYR I 195 GLU I 206 
AA 4 TYR I 183 ? ARG I 195 ? TYR I 174 ARG I 186 
AB 1 ASP J 86  ? SER J 90  ? ASP J 77  SER J 81  
AB 2 ASN J 115 ? ASN J 119 ? ASN J 106 ASN J 110 
AB 3 HIS J 123 ? TYR J 126 ? HIS J 114 TYR J 117 
AB 4 GLU J 58  ? LYS J 70  ? GLU J 49  LYS J 61  
AB 5 ALA J 129 ? MET J 135 ? ALA J 120 MET J 126 
AB 6 GLN J 109 ? VAL J 110 ? GLN J 100 VAL J 101 
AC 1 ASP J 86  ? SER J 90  ? ASP J 77  SER J 81  
AC 2 ASN J 115 ? ASN J 119 ? ASN J 106 ASN J 110 
AC 3 HIS J 123 ? TYR J 126 ? HIS J 114 TYR J 117 
AC 4 GLU J 58  ? LYS J 70  ? GLU J 49  LYS J 61  
AC 5 LEU J 38  ? ASP J 53  ? LEU J 29  ASP J 44  
AC 6 ILE J 163 ? THR J 167 ? ILE J 154 THR J 158 
AD 1 ILE J 99  ? ALA J 101 ? ILE J 90  ALA J 92  
AD 2 ALA J 147 ? SER J 155 ? ALA J 138 SER J 146 
AD 3 ASP J 206 ? GLU J 215 ? ASP J 197 GLU J 206 
AD 4 TYR J 183 ? SER J 193 ? TYR J 174 SER J 184 
# 
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 THR A 89  ? N THR A 80  O ALA A 116 ? O ALA A 107 
A  2 3 N LEU A 117 ? N LEU A 108 O GLN A 125 ? O GLN A 116 
A  3 4 O VAL A 124 ? O VAL A 115 N TRP A 69  ? N TRP A 60  
A  4 5 N LEU A 61  ? N LEU A 52  O LEU A 132 ? O LEU A 123 
A  5 6 O ARG A 131 ? O ARG A 122 N GLN A 109 ? N GLN A 100 
B  1 2 N THR A 89  ? N THR A 80  O ALA A 116 ? O ALA A 107 
B  2 3 N LEU A 117 ? N LEU A 108 O GLN A 125 ? O GLN A 116 
B  3 4 O VAL A 124 ? O VAL A 115 N TRP A 69  ? N TRP A 60  
B  4 5 O GLN A 66  ? O GLN A 57  N SER A 43  ? N SER A 34  
B  5 6 N LEU A 38  ? N LEU A 29  O ASP A 164 ? O ASP A 155 
C  1 2 N THR A 100 ? N THR A 91  O GLY A 154 ? O GLY A 145 
C  2 3 N CYS A 149 ? N CYS A 140 O VAL A 211 ? O VAL A 202 
C  3 4 O ARG A 214 ? O ARG A 205 N GLU A 184 ? N GLU A 175 
D  1 2 N THR B 89  ? N THR B 80  O ALA B 116 ? O ALA B 107 
D  2 3 N LEU B 117 ? N LEU B 108 O GLN B 125 ? O GLN B 116 
D  3 4 O VAL B 124 ? O VAL B 115 N TRP B 69  ? N TRP B 60  
D  4 5 N LEU B 61  ? N LEU B 52  O LEU B 132 ? O LEU B 123 
D  5 6 O ARG B 131 ? O ARG B 122 N GLN B 109 ? N GLN B 100 
E  1 2 N THR B 89  ? N THR B 80  O ALA B 116 ? O ALA B 107 
E  2 3 N LEU B 117 ? N LEU B 108 O GLN B 125 ? O GLN B 116 
E  3 4 O VAL B 124 ? O VAL B 115 N TRP B 69  ? N TRP B 60  
E  4 5 O GLN B 66  ? O GLN B 57  N SER B 43  ? N SER B 34  
E  5 6 N VAL B 40  ? N VAL B 31  O ASP B 164 ? O ASP B 155 
F  1 2 N THR B 100 ? N THR B 91  O GLY B 154 ? O GLY B 145 
F  2 3 N ALA B 147 ? N ALA B 138 O PHE B 213 ? O PHE B 204 
F  3 4 O ASN B 208 ? O ASN B 199 N THR B 191 ? N THR B 182 
G  1 2 N THR C 89  ? N THR C 80  O ALA C 116 ? O ALA C 107 
G  2 3 N LEU C 117 ? N LEU C 108 O GLN C 125 ? O GLN C 116 
G  3 4 O VAL C 124 ? O VAL C 115 N TRP C 69  ? N TRP C 60  
G  4 5 N TYR C 63  ? N TYR C 54  O GLN C 130 ? O GLN C 121 
G  5 6 O ARG C 131 ? O ARG C 122 N GLN C 109 ? N GLN C 100 
H  1 2 N THR C 89  ? N THR C 80  O ALA C 116 ? O ALA C 107 
H  2 3 N LEU C 117 ? N LEU C 108 O GLN C 125 ? O GLN C 116 
H  3 4 O VAL C 124 ? O VAL C 115 N TRP C 69  ? N TRP C 60  
H  4 5 O ASP C 60  ? O ASP C 51  N LYS C 51  ? N LYS C 42  
H  5 6 N LEU C 42  ? N LEU C 33  O LYS C 166 ? O LYS C 157 
I  1 2 N THR C 100 ? N THR C 91  O GLY C 154 ? O GLY C 145 
I  2 3 N CYS C 149 ? N CYS C 140 O VAL C 211 ? O VAL C 202 
I  3 4 O ARG C 214 ? O ARG C 205 N GLU C 184 ? N GLU C 175 
J  1 2 N THR D 89  ? N THR D 80  O ALA D 116 ? O ALA D 107 
J  2 3 N LEU D 117 ? N LEU D 108 O GLN D 125 ? O GLN D 116 
J  3 4 O TYR D 126 ? O TYR D 117 N GLN D 67  ? N GLN D 58  
J  4 5 N TYR D 63  ? N TYR D 54  O GLN D 130 ? O GLN D 121 
J  5 6 O ARG D 131 ? O ARG D 122 N GLN D 109 ? N GLN D 100 
K  1 2 N THR D 89  ? N THR D 80  O ALA D 116 ? O ALA D 107 
K  2 3 N LEU D 117 ? N LEU D 108 O GLN D 125 ? O GLN D 116 
K  3 4 O TYR D 126 ? O TYR D 117 N GLN D 67  ? N GLN D 58  
K  4 5 O SER D 68  ? O SER D 59  N TYR D 41  ? N TYR D 32  
K  5 6 N VAL D 40  ? N VAL D 31  O ASP D 164 ? O ASP D 155 
L  1 2 N THR D 100 ? N THR D 91  O GLY D 154 ? O GLY D 145 
L  2 3 N VAL D 151 ? N VAL D 142 O LEU D 209 ? O LEU D 200 
L  3 4 O ASN D 208 ? O ASN D 199 N THR D 191 ? N THR D 182 
M  1 2 N PHE E 87  ? N PHE E 78  O VAL E 118 ? O VAL E 109 
M  2 3 N ASN E 119 ? N ASN E 110 O GLY E 122 ? O GLY E 113 
M  3 4 O TYR E 126 ? O TYR E 117 N GLN E 67  ? N GLN E 58  
M  4 5 N LEU E 61  ? N LEU E 52  O LEU E 132 ? O LEU E 123 
M  5 6 O ARG E 131 ? O ARG E 122 N GLN E 109 ? N GLN E 100 
N  1 2 N PHE E 87  ? N PHE E 78  O VAL E 118 ? O VAL E 109 
N  2 3 N ASN E 119 ? N ASN E 110 O GLY E 122 ? O GLY E 113 
N  3 4 O TYR E 126 ? O TYR E 117 N GLN E 67  ? N GLN E 58  
N  4 5 O GLU E 58  ? O GLU E 49  N ASP E 53  ? N ASP E 44  
N  5 6 N LEU E 38  ? N LEU E 29  O ASP E 164 ? O ASP E 155 
O  1 2 N THR E 100 ? N THR E 91  O GLY E 154 ? O GLY E 145 
O  2 3 N ALA E 147 ? N ALA E 138 O PHE E 213 ? O PHE E 204 
O  3 4 O LYS E 212 ? O LYS E 203 N LEU E 186 ? N LEU E 177 
P  1 2 N PHE F 87  ? N PHE F 78  O VAL F 118 ? O VAL F 109 
P  2 3 N LEU F 117 ? N LEU F 108 O GLN F 125 ? O GLN F 116 
P  3 4 O VAL F 124 ? O VAL F 115 N TRP F 69  ? N TRP F 60  
P  4 5 N TYR F 63  ? N TYR F 54  O GLN F 130 ? O GLN F 121 
P  5 6 O ARG F 131 ? O ARG F 122 N GLN F 109 ? N GLN F 100 
Q  1 2 N PHE F 87  ? N PHE F 78  O VAL F 118 ? O VAL F 109 
Q  2 3 N LEU F 117 ? N LEU F 108 O GLN F 125 ? O GLN F 116 
Q  3 4 O VAL F 124 ? O VAL F 115 N TRP F 69  ? N TRP F 60  
Q  4 5 O VAL F 62  ? O VAL F 53  N ASP F 48  ? N ASP F 39  
Q  5 6 N LEU F 38  ? N LEU F 29  O ASP F 164 ? O ASP F 155 
R  1 2 N THR F 100 ? N THR F 91  O GLY F 154 ? O GLY F 145 
R  2 3 N CYS F 149 ? N CYS F 140 O VAL F 211 ? O VAL F 202 
R  3 4 O TYR F 204 ? O TYR F 195 N ARG F 195 ? N ARG F 186 
S  1 2 N THR G 89  ? N THR G 80  O ALA G 116 ? O ALA G 107 
S  2 3 N LEU G 117 ? N LEU G 108 O GLN G 125 ? O GLN G 116 
S  3 4 O VAL G 124 ? O VAL G 115 N TRP G 69  ? N TRP G 60  
S  4 5 N TYR G 63  ? N TYR G 54  O GLN G 130 ? O GLN G 121 
S  5 6 O ARG G 131 ? O ARG G 122 N GLN G 109 ? N GLN G 100 
T  1 2 N THR G 89  ? N THR G 80  O ALA G 116 ? O ALA G 107 
T  2 3 N LEU G 117 ? N LEU G 108 O GLN G 125 ? O GLN G 116 
T  3 4 O VAL G 124 ? O VAL G 115 N TRP G 69  ? N TRP G 60  
T  4 5 O VAL G 62  ? O VAL G 53  N ASP G 48  ? N ASP G 39  
T  5 6 N LEU G 38  ? N LEU G 29  O ASP G 164 ? O ASP G 155 
U  1 2 N THR G 100 ? N THR G 91  O GLY G 154 ? O GLY G 145 
U  2 3 N ALA G 147 ? N ALA G 138 O PHE G 213 ? O PHE G 204 
U  3 4 O ASN G 208 ? O ASN G 199 N THR G 191 ? N THR G 182 
V  1 2 N PHE H 87  ? N PHE H 78  O VAL H 118 ? O VAL H 109 
V  2 3 N LEU H 117 ? N LEU H 108 O GLN H 125 ? O GLN H 116 
V  3 4 O VAL H 124 ? O VAL H 115 N TRP H 69  ? N TRP H 60  
V  4 5 N LEU H 61  ? N LEU H 52  O LEU H 132 ? O LEU H 123 
V  5 6 O SER H 133 ? O SER H 124 N THR H 105 ? N THR H 96  
W  1 2 N PHE H 87  ? N PHE H 78  O VAL H 118 ? O VAL H 109 
W  2 3 N LEU H 117 ? N LEU H 108 O GLN H 125 ? O GLN H 116 
W  3 4 O VAL H 124 ? O VAL H 115 N TRP H 69  ? N TRP H 60  
W  4 5 O GLN H 66  ? O GLN H 57  N SER H 43  ? N SER H 34  
W  5 6 N LEU H 38  ? N LEU H 29  O ASP H 164 ? O ASP H 155 
X  1 2 N THR H 100 ? N THR H 91  O GLY H 154 ? O GLY H 145 
X  2 3 N VAL H 151 ? N VAL H 142 O LEU H 209 ? O LEU H 200 
X  3 4 O ASN H 208 ? O ASN H 199 N THR H 191 ? N THR H 182 
Y  1 2 N PHE I 87  ? N PHE I 78  O VAL I 118 ? O VAL I 109 
Y  2 3 N ASN I 119 ? N ASN I 110 O GLY I 122 ? O GLY I 113 
Y  3 4 O VAL I 124 ? O VAL I 115 N TRP I 69  ? N TRP I 60  
Y  4 5 N LEU I 61  ? N LEU I 52  O LEU I 132 ? O LEU I 123 
Y  5 6 O ARG I 131 ? O ARG I 122 N GLN I 109 ? N GLN I 100 
Z  1 2 N PHE I 87  ? N PHE I 78  O VAL I 118 ? O VAL I 109 
Z  2 3 N ASN I 119 ? N ASN I 110 O GLY I 122 ? O GLY I 113 
Z  3 4 O VAL I 124 ? O VAL I 115 N TRP I 69  ? N TRP I 60  
Z  4 5 O SER I 68  ? O SER I 59  N TYR I 41  ? N TYR I 32  
Z  5 6 N LEU I 38  ? N LEU I 29  O ASP I 164 ? O ASP I 155 
AA 1 2 N THR I 100 ? N THR I 91  O GLY I 154 ? O GLY I 145 
AA 2 3 N VAL I 151 ? N VAL I 142 O LEU I 209 ? O LEU I 200 
AA 3 4 O ASN I 208 ? O ASN I 199 N THR I 191 ? N THR I 182 
AB 1 2 N THR J 89  ? N THR J 80  O ALA J 116 ? O ALA J 107 
AB 2 3 N LEU J 117 ? N LEU J 108 O GLN J 125 ? O GLN J 116 
AB 3 4 O VAL J 124 ? O VAL J 115 N TRP J 69  ? N TRP J 60  
AB 4 5 N LEU J 61  ? N LEU J 52  O LEU J 132 ? O LEU J 123 
AB 5 6 O ARG J 131 ? O ARG J 122 N GLN J 109 ? N GLN J 100 
AC 1 2 N THR J 89  ? N THR J 80  O ALA J 116 ? O ALA J 107 
AC 2 3 N LEU J 117 ? N LEU J 108 O GLN J 125 ? O GLN J 116 
AC 3 4 O VAL J 124 ? O VAL J 115 N TRP J 69  ? N TRP J 60  
AC 4 5 O ASP J 60  ? O ASP J 51  N LYS J 51  ? N LYS J 42  
AC 5 6 N LEU J 38  ? N LEU J 29  O ASP J 164 ? O ASP J 155 
AD 1 2 N THR J 100 ? N THR J 91  O GLY J 154 ? O GLY J 145 
AD 2 3 N ALA J 147 ? N ALA J 138 O PHE J 213 ? O PHE J 204 
AD 3 4 O ASN J 208 ? O ASN J 199 N THR J 191 ? N THR J 182 
# 
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 ? ? ? ? 4  'BINDING SITE FOR RESIDUE MG A 222'  
AC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG A 250' 
AC3 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG A 251' 
AC4 Software ? ? ? ? 14 'BINDING SITE FOR RESIDUE MLK A 301' 
AC5 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE MRD A 305' 
AC6 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE MPD A 223' 
AC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE MPD A 306' 
AC8 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE MG B 222'  
AC9 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG B 250' 
BC1 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG B 275' 
BC2 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE MLK B 301' 
BC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE MRD B 305' 
BC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE MG C 222'  
BC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG C 250' 
BC6 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE MLK C 301' 
BC7 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MPD C 306' 
BC8 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE MRD D 305' 
BC9 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG D 250' 
CC1 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG D 251' 
CC2 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE MLK D 301' 
CC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE MG E 222'  
CC4 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG E 250' 
CC5 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG E 251' 
CC6 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE MRD E 305' 
CC7 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG E 275' 
CC8 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE MLK E 301' 
CC9 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE MRD F 305' 
DC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG F 250' 
DC2 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE MLK F 301' 
DC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG G 250' 
DC4 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG G 251' 
DC5 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE MLK G 301' 
DC6 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE MPD G 305' 
DC7 Software ? ? ? ? 3  'BINDING SITE FOR RESIDUE MPD G 222' 
DC8 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG H 250' 
DC9 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG H 251' 
EC1 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE BMA H 252' 
EC2 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE MLK H 301' 
EC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE MG I 222'  
EC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG I 250' 
EC5 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG I 275' 
EC6 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE MLK I 301' 
EC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE MPD J 305' 
EC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE MPD I 305' 
EC9 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE NAG J 250' 
FC1 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG J 251' 
FC2 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE BMA J 252' 
FC3 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE MLK J 301' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 4  ASP A  6   ? ASP A -3  . ? 1_555 ? 
2   AC1 4  HIS A  10  ? HIS A 1   . ? 1_555 ? 
3   AC1 4  ASP G  6   ? ASP G -3  . ? 1_555 ? 
4   AC1 4  HIS G  10  ? HIS G 1   . ? 1_555 ? 
5   AC2 4  ASN A  119 ? ASN A 110 . ? 1_555 ? 
6   AC2 4  SER A  121 ? SER A 112 . ? 1_555 ? 
7   AC2 4  GLN A  125 ? GLN A 116 . ? 1_555 ? 
8   AC2 4  NAG M  .   ? NAG A 251 . ? 1_555 ? 
9   AC3 1  NAG L  .   ? NAG A 250 . ? 1_555 ? 
10  AC4 14 TYR A  102 ? TYR A 93  . ? 1_555 ? 
11  AC4 14 SER A  103 ? SER A 94  . ? 1_555 ? 
12  AC4 14 LYS A  152 ? LYS A 143 . ? 1_555 ? 
13  AC4 14 SER A  155 ? SER A 146 . ? 1_555 ? 
14  AC4 14 TRP A  156 ? TRP A 147 . ? 1_555 ? 
15  AC4 14 TYR A  158 ? TYR A 149 . ? 1_555 ? 
16  AC4 14 ARG A  195 ? ARG A 186 . ? 1_555 ? 
17  AC4 14 TYR A  204 ? TYR A 195 . ? 1_555 ? 
18  AC4 14 ASP A  206 ? ASP A 197 . ? 1_555 ? 
19  AC4 14 LEU E  47  ? LEU E 38  . ? 1_555 ? 
20  AC4 14 TRP E  64  ? TRP E 55  . ? 1_555 ? 
21  AC4 14 GLN E  125 ? GLN E 116 . ? 1_555 ? 
22  AC4 14 LEU E  127 ? LEU E 118 . ? 1_555 ? 
23  AC4 14 SER E  176 ? SER E 167 . ? 1_555 ? 
24  AC5 3  TRP A  95  ? TRP A 86  . ? 1_555 ? 
25  AC5 3  TYR A  158 ? TYR A 149 . ? 1_555 ? 
26  AC5 3  LYS E  19  ? LYS E 10  . ? 1_555 ? 
27  AC6 6  THR A  89  ? THR A 80  . ? 1_555 ? 
28  AC6 6  SER A  90  ? SER A 81  . ? 1_555 ? 
29  AC6 6  ASN A  115 ? ASN A 106 . ? 1_555 ? 
30  AC6 6  TRP B  95  ? TRP B 86  . ? 1_555 ? 
31  AC6 6  THR B  96  ? THR B 87  . ? 1_555 ? 
32  AC6 6  TYR B  158 ? TYR B 149 . ? 1_555 ? 
33  AC7 4  ALA A  91  ? ALA A 82  . ? 1_555 ? 
34  AC7 4  ALA A  92  ? ALA A 83  . ? 1_555 ? 
35  AC7 4  ILE A  94  ? ILE A 85  . ? 1_555 ? 
36  AC7 4  THR A  96  ? THR A 87  . ? 1_555 ? 
37  AC8 4  ASP B  6   ? ASP B -3  . ? 1_555 ? 
38  AC8 4  HIS B  10  ? HIS B 1   . ? 1_555 ? 
39  AC8 4  ASP F  6   ? ASP F -3  . ? 1_555 ? 
40  AC8 4  HIS F  10  ? HIS F 1   . ? 1_555 ? 
41  AC9 4  ASN B  119 ? ASN B 110 . ? 1_555 ? 
42  AC9 4  SER B  120 ? SER B 111 . ? 1_555 ? 
43  AC9 4  SER B  121 ? SER B 112 . ? 1_555 ? 
44  AC9 4  HIS B  123 ? HIS B 114 . ? 1_555 ? 
45  BC1 2  ASN B  83  ? ASN B 74  . ? 1_555 ? 
46  BC1 2  LYS C  34  ? LYS C 25  . ? 1_555 ? 
47  BC2 12 TRP A  64  ? TRP A 55  . ? 1_555 ? 
48  BC2 12 LEU A  127 ? LEU A 118 . ? 1_555 ? 
49  BC2 12 SER A  176 ? SER A 167 . ? 1_555 ? 
50  BC2 12 TYR B  102 ? TYR B 93  . ? 1_555 ? 
51  BC2 12 LYS B  152 ? LYS B 143 . ? 1_555 ? 
52  BC2 12 SER B  155 ? SER B 146 . ? 1_555 ? 
53  BC2 12 TRP B  156 ? TRP B 147 . ? 1_555 ? 
54  BC2 12 TYR B  158 ? TYR B 149 . ? 1_555 ? 
55  BC2 12 ARG B  195 ? ARG B 186 . ? 1_555 ? 
56  BC2 12 TYR B  197 ? TYR B 188 . ? 1_555 ? 
57  BC2 12 TYR B  204 ? TYR B 195 . ? 1_555 ? 
58  BC2 12 ASP B  206 ? ASP B 197 . ? 1_555 ? 
59  BC3 5  THR B  89  ? THR B 80  . ? 1_555 ? 
60  BC3 5  SER B  90  ? SER B 81  . ? 1_555 ? 
61  BC3 5  ASN B  115 ? ASN B 106 . ? 1_555 ? 
62  BC3 5  TRP C  95  ? TRP C 86  . ? 1_555 ? 
63  BC3 5  TYR C  158 ? TYR C 149 . ? 1_555 ? 
64  BC4 4  ASP C  6   ? ASP C -3  . ? 1_555 ? 
65  BC4 4  HIS C  10  ? HIS C 1   . ? 1_555 ? 
66  BC4 4  ASP J  6   ? ASP J -3  . ? 1_555 ? 
67  BC4 4  HIS J  10  ? HIS J 1   . ? 1_555 ? 
68  BC5 4  THR C  85  ? THR C 76  . ? 1_555 ? 
69  BC5 4  ASN C  119 ? ASN C 110 . ? 1_555 ? 
70  BC5 4  SER C  121 ? SER C 112 . ? 1_555 ? 
71  BC5 4  HIS C  123 ? HIS C 114 . ? 1_555 ? 
72  BC6 13 TRP B  64  ? TRP B 55  . ? 1_555 ? 
73  BC6 13 GLN B  125 ? GLN B 116 . ? 1_555 ? 
74  BC6 13 LEU B  127 ? LEU B 118 . ? 1_555 ? 
75  BC6 13 SER B  176 ? SER B 167 . ? 1_555 ? 
76  BC6 13 TYR C  102 ? TYR C 93  . ? 1_555 ? 
77  BC6 13 LYS C  152 ? LYS C 143 . ? 1_555 ? 
78  BC6 13 TRP C  156 ? TRP C 147 . ? 1_555 ? 
79  BC6 13 TYR C  158 ? TYR C 149 . ? 1_555 ? 
80  BC6 13 ARG C  195 ? ARG C 186 . ? 1_555 ? 
81  BC6 13 TYR C  197 ? TYR C 188 . ? 1_555 ? 
82  BC6 13 TYR C  204 ? TYR C 195 . ? 1_555 ? 
83  BC6 13 ASP C  206 ? ASP C 197 . ? 1_555 ? 
84  BC6 13 HOH JB .   ? HOH C 333 . ? 1_555 ? 
85  BC7 7  ASP C  21  ? ASP C 12  . ? 1_555 ? 
86  BC7 7  LEU C  22  ? LEU C 13  . ? 1_555 ? 
87  BC7 7  ARG C  25  ? ARG C 16  . ? 1_555 ? 
88  BC7 7  SER C  73  ? SER C 64  . ? 1_555 ? 
89  BC7 7  MET C  75  ? MET C 66  . ? 1_555 ? 
90  BC7 7  TRP C  76  ? TRP C 67  . ? 1_555 ? 
91  BC7 7  TYR C  81  ? TYR C 72  . ? 1_555 ? 
92  BC8 3  ASN C  115 ? ASN C 106 . ? 1_555 ? 
93  BC8 3  TRP D  95  ? TRP D 86  . ? 1_555 ? 
94  BC8 3  TYR D  158 ? TYR D 149 . ? 1_555 ? 
95  BC9 6  THR D  85  ? THR D 76  . ? 1_555 ? 
96  BC9 6  ASN D  119 ? ASN D 110 . ? 1_555 ? 
97  BC9 6  SER D  120 ? SER D 111 . ? 1_555 ? 
98  BC9 6  SER D  121 ? SER D 112 . ? 1_555 ? 
99  BC9 6  HIS D  123 ? HIS D 114 . ? 1_555 ? 
100 BC9 6  NAG CA .   ? NAG D 251 . ? 1_555 ? 
101 CC1 1  NAG BA .   ? NAG D 250 . ? 1_555 ? 
102 CC2 11 TRP C  64  ? TRP C 55  . ? 1_555 ? 
103 CC2 11 GLN C  125 ? GLN C 116 . ? 1_555 ? 
104 CC2 11 LEU C  127 ? LEU C 118 . ? 1_555 ? 
105 CC2 11 SER C  176 ? SER C 167 . ? 1_555 ? 
106 CC2 11 TYR D  102 ? TYR D 93  . ? 1_555 ? 
107 CC2 11 LYS D  152 ? LYS D 143 . ? 1_555 ? 
108 CC2 11 TRP D  156 ? TRP D 147 . ? 1_555 ? 
109 CC2 11 TYR D  158 ? TYR D 149 . ? 1_555 ? 
110 CC2 11 TYR D  197 ? TYR D 188 . ? 1_555 ? 
111 CC2 11 TYR D  204 ? TYR D 195 . ? 1_555 ? 
112 CC2 11 ASP D  206 ? ASP D 197 . ? 1_555 ? 
113 CC3 4  ASP E  6   ? ASP E -3  . ? 1_555 ? 
114 CC3 4  HIS E  10  ? HIS E 1   . ? 1_555 ? 
115 CC3 4  ASP H  6   ? ASP H -3  . ? 1_555 ? 
116 CC3 4  HIS H  10  ? HIS H 1   . ? 1_555 ? 
117 CC4 5  THR E  85  ? THR E 76  . ? 1_555 ? 
118 CC4 5  ASN E  119 ? ASN E 110 . ? 1_555 ? 
119 CC4 5  SER E  121 ? SER E 112 . ? 1_555 ? 
120 CC4 5  HIS E  123 ? HIS E 114 . ? 1_555 ? 
121 CC4 5  NAG GA .   ? NAG E 251 . ? 1_555 ? 
122 CC5 2  NAG FA .   ? NAG E 250 . ? 1_555 ? 
123 CC5 2  HOH LB .   ? HOH E 327 . ? 1_555 ? 
124 CC6 2  TRP E  95  ? TRP E 86  . ? 1_555 ? 
125 CC6 2  TYR E  158 ? TYR E 149 . ? 1_555 ? 
126 CC7 2  ASN E  83  ? ASN E 74  . ? 1_555 ? 
127 CC7 2  THR E  85  ? THR E 76  . ? 1_555 ? 
128 CC8 13 TRP D  64  ? TRP D 55  . ? 1_555 ? 
129 CC8 13 LEU D  127 ? LEU D 118 . ? 1_555 ? 
130 CC8 13 SER D  176 ? SER D 167 . ? 1_555 ? 
131 CC8 13 TYR E  102 ? TYR E 93  . ? 1_555 ? 
132 CC8 13 LYS E  152 ? LYS E 143 . ? 1_555 ? 
133 CC8 13 SER E  155 ? SER E 146 . ? 1_555 ? 
134 CC8 13 TRP E  156 ? TRP E 147 . ? 1_555 ? 
135 CC8 13 SER E  157 ? SER E 148 . ? 1_555 ? 
136 CC8 13 TYR E  158 ? TYR E 149 . ? 1_555 ? 
137 CC8 13 ARG E  195 ? ARG E 186 . ? 1_555 ? 
138 CC8 13 TYR E  197 ? TYR E 188 . ? 1_555 ? 
139 CC8 13 TYR E  204 ? TYR E 195 . ? 1_555 ? 
140 CC8 13 ASP E  206 ? ASP E 197 . ? 1_555 ? 
141 CC9 3  TRP F  95  ? TRP F 86  . ? 1_555 ? 
142 CC9 3  TYR F  158 ? TYR F 149 . ? 1_555 ? 
143 CC9 3  SER J  90  ? SER J 81  . ? 1_555 ? 
144 DC1 4  ASN F  119 ? ASN F 110 . ? 1_555 ? 
145 DC1 4  SER F  120 ? SER F 111 . ? 1_555 ? 
146 DC1 4  SER F  121 ? SER F 112 . ? 1_555 ? 
147 DC1 4  HIS F  123 ? HIS F 114 . ? 1_555 ? 
148 DC2 12 TYR F  102 ? TYR F 93  . ? 1_555 ? 
149 DC2 12 LYS F  152 ? LYS F 143 . ? 1_555 ? 
150 DC2 12 TRP F  156 ? TRP F 147 . ? 1_555 ? 
151 DC2 12 TYR F  158 ? TYR F 149 . ? 1_555 ? 
152 DC2 12 ARG F  195 ? ARG F 186 . ? 1_555 ? 
153 DC2 12 TYR F  197 ? TYR F 188 . ? 1_555 ? 
154 DC2 12 TYR F  204 ? TYR F 195 . ? 1_555 ? 
155 DC2 12 ASP F  206 ? ASP F 197 . ? 1_555 ? 
156 DC2 12 TRP J  64  ? TRP J 55  . ? 1_555 ? 
157 DC2 12 GLN J  125 ? GLN J 116 . ? 1_555 ? 
158 DC2 12 LEU J  127 ? LEU J 118 . ? 1_555 ? 
159 DC2 12 SER J  176 ? SER J 167 . ? 1_555 ? 
160 DC3 4  THR G  85  ? THR G 76  . ? 1_555 ? 
161 DC3 4  ASN G  119 ? ASN G 110 . ? 1_555 ? 
162 DC3 4  HIS G  123 ? HIS G 114 . ? 1_555 ? 
163 DC3 4  NAG PA .   ? NAG G 251 . ? 1_555 ? 
164 DC4 2  HIS G  123 ? HIS G 114 . ? 1_555 ? 
165 DC4 2  NAG OA .   ? NAG G 250 . ? 1_555 ? 
166 DC5 12 TRP F  64  ? TRP F 55  . ? 1_555 ? 
167 DC5 12 GLN F  125 ? GLN F 116 . ? 1_555 ? 
168 DC5 12 LEU F  127 ? LEU F 118 . ? 1_555 ? 
169 DC5 12 SER F  176 ? SER F 167 . ? 1_555 ? 
170 DC5 12 TYR G  102 ? TYR G 93  . ? 1_555 ? 
171 DC5 12 LYS G  152 ? LYS G 143 . ? 1_555 ? 
172 DC5 12 SER G  155 ? SER G 146 . ? 1_555 ? 
173 DC5 12 TRP G  156 ? TRP G 147 . ? 1_555 ? 
174 DC5 12 TYR G  158 ? TYR G 149 . ? 1_555 ? 
175 DC5 12 ARG G  195 ? ARG G 186 . ? 1_555 ? 
176 DC5 12 TYR G  204 ? TYR G 195 . ? 1_555 ? 
177 DC5 12 ASP G  206 ? ASP G 197 . ? 1_555 ? 
178 DC6 3  ASN F  115 ? ASN F 106 . ? 1_555 ? 
179 DC6 3  TRP G  95  ? TRP G 86  . ? 1_555 ? 
180 DC6 3  TYR G  158 ? TYR G 149 . ? 1_555 ? 
181 DC7 3  ASN G  115 ? ASN G 106 . ? 1_555 ? 
182 DC7 3  TRP H  95  ? TRP H 86  . ? 1_555 ? 
183 DC7 3  TYR H  158 ? TYR H 149 . ? 1_555 ? 
184 DC8 4  ASN H  119 ? ASN H 110 . ? 1_555 ? 
185 DC8 4  SER H  121 ? SER H 112 . ? 1_555 ? 
186 DC8 4  HIS H  123 ? HIS H 114 . ? 1_555 ? 
187 DC8 4  NAG UA .   ? NAG H 251 . ? 1_555 ? 
188 DC9 2  NAG TA .   ? NAG H 250 . ? 1_555 ? 
189 DC9 2  BMA VA .   ? BMA H 252 . ? 1_555 ? 
190 EC1 2  NAG UA .   ? NAG H 251 . ? 1_555 ? 
191 EC1 2  HOH OB .   ? HOH H 338 . ? 1_555 ? 
192 EC2 12 TRP G  64  ? TRP G 55  . ? 1_555 ? 
193 EC2 12 GLN G  125 ? GLN G 116 . ? 1_555 ? 
194 EC2 12 LEU G  127 ? LEU G 118 . ? 1_555 ? 
195 EC2 12 SER G  176 ? SER G 167 . ? 1_555 ? 
196 EC2 12 TYR H  102 ? TYR H 93  . ? 1_555 ? 
197 EC2 12 LYS H  152 ? LYS H 143 . ? 1_555 ? 
198 EC2 12 SER H  155 ? SER H 146 . ? 1_555 ? 
199 EC2 12 TRP H  156 ? TRP H 147 . ? 1_555 ? 
200 EC2 12 TYR H  158 ? TYR H 149 . ? 1_555 ? 
201 EC2 12 ARG H  195 ? ARG H 186 . ? 1_555 ? 
202 EC2 12 TYR H  204 ? TYR H 195 . ? 1_555 ? 
203 EC2 12 ASP H  206 ? ASP H 197 . ? 1_555 ? 
204 EC3 4  ASP D  6   ? ASP D -3  . ? 1_555 ? 
205 EC3 4  HIS D  10  ? HIS D 1   . ? 1_555 ? 
206 EC3 4  ASP I  6   ? ASP I -3  . ? 1_555 ? 
207 EC3 4  HIS I  10  ? HIS I 1   . ? 1_555 ? 
208 EC4 4  ASN I  119 ? ASN I 110 . ? 1_555 ? 
209 EC4 4  SER I  121 ? SER I 112 . ? 1_555 ? 
210 EC4 4  HIS I  123 ? HIS I 114 . ? 1_555 ? 
211 EC4 4  HOH PB .   ? HOH I 335 . ? 1_555 ? 
212 EC5 1  ASN I  83  ? ASN I 74  . ? 1_555 ? 
213 EC6 13 TRP H  64  ? TRP H 55  . ? 1_555 ? 
214 EC6 13 GLN H  125 ? GLN H 116 . ? 1_555 ? 
215 EC6 13 LEU H  127 ? LEU H 118 . ? 1_555 ? 
216 EC6 13 SER H  176 ? SER H 167 . ? 1_555 ? 
217 EC6 13 TYR I  102 ? TYR I 93  . ? 1_555 ? 
218 EC6 13 SER I  103 ? SER I 94  . ? 1_555 ? 
219 EC6 13 LYS I  152 ? LYS I 143 . ? 1_555 ? 
220 EC6 13 SER I  155 ? SER I 146 . ? 1_555 ? 
221 EC6 13 TRP I  156 ? TRP I 147 . ? 1_555 ? 
222 EC6 13 TYR I  158 ? TYR I 149 . ? 1_555 ? 
223 EC6 13 TYR I  197 ? TYR I 188 . ? 1_555 ? 
224 EC6 13 CYS I  199 ? CYS I 190 . ? 1_555 ? 
225 EC6 13 TYR I  204 ? TYR I 195 . ? 1_555 ? 
226 EC7 4  ARG I  88  ? ARG I 79  . ? 1_555 ? 
227 EC7 4  PRO J  30  ? PRO J 21  . ? 1_555 ? 
228 EC7 4  TRP J  95  ? TRP J 86  . ? 1_555 ? 
229 EC7 4  TYR J  158 ? TYR J 149 . ? 1_555 ? 
230 EC8 5  LYS H  19  ? LYS H 10  . ? 1_555 ? 
231 EC8 5  SER H  90  ? SER H 81  . ? 1_555 ? 
232 EC8 5  ASN H  115 ? ASN H 106 . ? 1_555 ? 
233 EC8 5  TRP I  95  ? TRP I 86  . ? 1_555 ? 
234 EC8 5  TYR I  158 ? TYR I 149 . ? 1_555 ? 
235 EC9 6  THR J  85  ? THR J 76  . ? 1_555 ? 
236 EC9 6  ASN J  119 ? ASN J 110 . ? 1_555 ? 
237 EC9 6  SER J  120 ? SER J 111 . ? 1_555 ? 
238 EC9 6  SER J  121 ? SER J 112 . ? 1_555 ? 
239 EC9 6  HIS J  123 ? HIS J 114 . ? 1_555 ? 
240 EC9 6  NAG EB .   ? NAG J 251 . ? 1_555 ? 
241 FC1 2  NAG DB .   ? NAG J 250 . ? 1_555 ? 
242 FC1 2  BMA FB .   ? BMA J 252 . ? 1_555 ? 
243 FC2 1  NAG EB .   ? NAG J 251 . ? 1_555 ? 
244 FC3 11 TRP I  64  ? TRP I 55  . ? 1_555 ? 
245 FC3 11 SER I  176 ? SER I 167 . ? 1_555 ? 
246 FC3 11 TYR J  102 ? TYR J 93  . ? 1_555 ? 
247 FC3 11 LYS J  152 ? LYS J 143 . ? 1_555 ? 
248 FC3 11 SER J  155 ? SER J 146 . ? 1_555 ? 
249 FC3 11 TRP J  156 ? TRP J 147 . ? 1_555 ? 
250 FC3 11 TYR J  158 ? TYR J 149 . ? 1_555 ? 
251 FC3 11 ARG J  195 ? ARG J 186 . ? 1_555 ? 
252 FC3 11 TYR J  197 ? TYR J 188 . ? 1_555 ? 
253 FC3 11 TYR J  204 ? TYR J 195 . ? 1_555 ? 
254 FC3 11 ASP J  206 ? ASP J 197 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3SH1 
_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                    3SH1 
_atom_sites.fract_transf_matrix[1][1]   0.011656 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003167 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007134 
_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]   0.007575 
_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  
MG 
N  
O  
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 4   ? 25.758  -9.905  67.772 1.00 87.83  ? -5  ASP A N   1 
ATOM   2     C  CA  . ASP A  1 4   ? 25.892  -10.626 66.518 1.00 94.01  ? -5  ASP A CA  1 
ATOM   3     C  C   . ASP A  1 4   ? 24.636  -10.542 65.641 1.00 94.62  ? -5  ASP A C   1 
ATOM   4     O  O   . ASP A  1 4   ? 24.720  -10.761 64.431 1.00 96.30  ? -5  ASP A O   1 
ATOM   5     C  CB  . ASP A  1 4   ? 26.275  -12.091 66.760 1.00 100.75 ? -5  ASP A CB  1 
ATOM   6     C  CG  . ASP A  1 4   ? 27.357  -12.582 65.801 1.00 100.63 ? -5  ASP A CG  1 
ATOM   7     O  OD1 . ASP A  1 4   ? 28.446  -11.973 65.765 1.00 103.30 ? -5  ASP A OD1 1 
ATOM   8     O  OD2 . ASP A  1 4   ? 27.122  -13.571 65.074 1.00 96.81  ? -5  ASP A OD2 1 
ATOM   9     N  N   . ASP A  1 5   ? 23.480  -10.231 66.229 1.00 91.26  ? -4  ASP A N   1 
ATOM   10    C  CA  . ASP A  1 5   ? 22.255  -10.073 65.436 1.00 87.31  ? -4  ASP A CA  1 
ATOM   11    C  C   . ASP A  1 5   ? 22.440  -9.053  64.321 1.00 82.82  ? -4  ASP A C   1 
ATOM   12    O  O   . ASP A  1 5   ? 22.213  -9.340  63.144 1.00 80.44  ? -4  ASP A O   1 
ATOM   13    C  CB  . ASP A  1 5   ? 21.087  -9.663  66.321 1.00 90.77  ? -4  ASP A CB  1 
ATOM   14    C  CG  . ASP A  1 5   ? 20.642  -10.779 67.232 1.00 100.14 ? -4  ASP A CG  1 
ATOM   15    O  OD1 . ASP A  1 5   ? 21.334  -11.822 67.274 1.00 91.23  ? -4  ASP A OD1 1 
ATOM   16    O  OD2 . ASP A  1 5   ? 19.604  -10.611 67.906 1.00 103.37 ? -4  ASP A OD2 1 
ATOM   17    N  N   . ASP A  1 6   ? 22.870  -7.861  64.703 1.00 81.13  ? -3  ASP A N   1 
ATOM   18    C  CA  . ASP A  1 6   ? 23.125  -6.803  63.743 1.00 81.49  ? -3  ASP A CA  1 
ATOM   19    C  C   . ASP A  1 6   ? 24.035  -7.311  62.626 1.00 79.41  ? -3  ASP A C   1 
ATOM   20    O  O   . ASP A  1 6   ? 23.761  -7.102  61.447 1.00 71.80  ? -3  ASP A O   1 
ATOM   21    C  CB  . ASP A  1 6   ? 23.747  -5.598  64.454 1.00 76.55  ? -3  ASP A CB  1 
ATOM   22    C  CG  . ASP A  1 6   ? 23.817  -4.370  63.573 1.00 81.24  ? -3  ASP A CG  1 
ATOM   23    O  OD1 . ASP A  1 6   ? 22.743  -3.835  63.197 1.00 73.70  ? -3  ASP A OD1 1 
ATOM   24    O  OD2 . ASP A  1 6   ? 24.953  -3.932  63.267 1.00 80.70  ? -3  ASP A OD2 1 
ATOM   25    N  N   . ASP A  1 7   ? 25.116  -7.979  63.001 1.00 79.79  ? -2  ASP A N   1 
ATOM   26    C  CA  . ASP A  1 7   ? 26.024  -8.538  62.019 1.00 77.80  ? -2  ASP A CA  1 
ATOM   27    C  C   . ASP A  1 7   ? 25.264  -9.455  61.083 1.00 76.35  ? -2  ASP A C   1 
ATOM   28    O  O   . ASP A  1 7   ? 25.580  -9.532  59.900 1.00 77.15  ? -2  ASP A O   1 
ATOM   29    C  CB  . ASP A  1 7   ? 27.165  -9.290  62.699 1.00 84.27  ? -2  ASP A CB  1 
ATOM   30    C  CG  . ASP A  1 7   ? 28.251  -8.359  63.217 1.00 102.60 ? -2  ASP A CG  1 
ATOM   31    O  OD1 . ASP A  1 7   ? 29.283  -8.877  63.705 1.00 108.57 ? -2  ASP A OD1 1 
ATOM   32    O  OD2 . ASP A  1 7   ? 28.079  -7.116  63.128 1.00 95.32  ? -2  ASP A OD2 1 
ATOM   33    N  N   . LYS A  1 8   ? 24.255  -10.147 61.604 1.00 73.51  ? -1  LYS A N   1 
ATOM   34    C  CA  . LYS A  1 8   ? 23.434  -11.025 60.769 1.00 72.86  ? -1  LYS A CA  1 
ATOM   35    C  C   . LYS A  1 8   ? 22.514  -10.234 59.823 1.00 74.27  ? -1  LYS A C   1 
ATOM   36    O  O   . LYS A  1 8   ? 22.332  -10.584 58.647 1.00 66.29  ? -1  LYS A O   1 
ATOM   37    C  CB  . LYS A  1 8   ? 22.639  -12.008 61.636 1.00 65.27  ? -1  LYS A CB  1 
ATOM   38    C  CG  . LYS A  1 8   ? 23.309  -13.369 61.740 1.00 75.29  ? -1  LYS A CG  1 
ATOM   39    C  CD  . LYS A  1 8   ? 23.092  -14.033 63.093 1.00 84.95  ? -1  LYS A CD  1 
ATOM   40    C  CE  . LYS A  1 8   ? 21.744  -14.719 63.196 1.00 85.27  ? -1  LYS A CE  1 
ATOM   41    N  NZ  . LYS A  1 8   ? 21.650  -15.496 64.461 1.00 77.62  ? -1  LYS A NZ  1 
ATOM   42    N  N   . LEU A  1 9   ? 21.946  -9.158  60.348 1.00 73.89  ? 0   LEU A N   1 
ATOM   43    C  CA  . LEU A  1 9   ? 21.091  -8.279  59.572 1.00 69.08  ? 0   LEU A CA  1 
ATOM   44    C  C   . LEU A  1 9   ? 21.870  -7.550  58.466 1.00 69.70  ? 0   LEU A C   1 
ATOM   45    O  O   . LEU A  1 9   ? 21.351  -7.344  57.372 1.00 69.41  ? 0   LEU A O   1 
ATOM   46    C  CB  . LEU A  1 9   ? 20.443  -7.268  60.507 1.00 69.01  ? 0   LEU A CB  1 
ATOM   47    C  CG  . LEU A  1 9   ? 19.254  -6.535  59.919 1.00 72.40  ? 0   LEU A CG  1 
ATOM   48    C  CD1 . LEU A  1 9   ? 17.993  -7.351  60.142 1.00 63.55  ? 0   LEU A CD1 1 
ATOM   49    C  CD2 . LEU A  1 9   ? 19.148  -5.148  60.540 1.00 72.25  ? 0   LEU A CD2 1 
ATOM   50    N  N   . HIS A  1 10  ? 23.108  -7.159  58.758 1.00 69.31  ? 1   HIS A N   1 
ATOM   51    C  CA  . HIS A  1 10  ? 23.978  -6.523  57.777 1.00 57.65  ? 1   HIS A CA  1 
ATOM   52    C  C   . HIS A  1 10  ? 24.479  -7.490  56.733 1.00 65.85  ? 1   HIS A C   1 
ATOM   53    O  O   . HIS A  1 10  ? 24.849  -7.077  55.643 1.00 66.50  ? 1   HIS A O   1 
ATOM   54    C  CB  . HIS A  1 10  ? 25.202  -5.923  58.446 1.00 64.16  ? 1   HIS A CB  1 
ATOM   55    C  CG  . HIS A  1 10  ? 24.944  -4.616  59.105 1.00 76.89  ? 1   HIS A CG  1 
ATOM   56    N  ND1 . HIS A  1 10  ? 25.249  -3.409  58.508 1.00 76.70  ? 1   HIS A ND1 1 
ATOM   57    C  CD2 . HIS A  1 10  ? 24.407  -4.312  60.309 1.00 73.72  ? 1   HIS A CD2 1 
ATOM   58    C  CE1 . HIS A  1 10  ? 24.910  -2.424  59.318 1.00 80.25  ? 1   HIS A CE1 1 
ATOM   59    N  NE2 . HIS A  1 10  ? 24.401  -2.949  60.421 1.00 65.56  ? 1   HIS A NE2 1 
ATOM   60    N  N   . SER A  1 11  ? 24.545  -8.772  57.069 1.00 67.46  ? 2   SER A N   1 
ATOM   61    C  CA  . SER A  1 11  ? 25.023  -9.748  56.106 1.00 58.42  ? 2   SER A CA  1 
ATOM   62    C  C   . SER A  1 11  ? 23.945  -9.933  55.056 1.00 61.27  ? 2   SER A C   1 
ATOM   63    O  O   . SER A  1 11  ? 24.236  -9.984  53.871 1.00 64.08  ? 2   SER A O   1 
ATOM   64    C  CB  . SER A  1 11  ? 25.359  -11.071 56.785 1.00 66.42  ? 2   SER A CB  1 
ATOM   65    O  OG  . SER A  1 11  ? 24.196  -11.671 57.323 1.00 73.02  ? 2   SER A OG  1 
ATOM   66    N  N   . GLN A  1 12  ? 22.695  -10.010 55.502 1.00 65.52  ? 3   GLN A N   1 
ATOM   67    C  CA  . GLN A  1 12  ? 21.554  -10.156 54.606 1.00 61.31  ? 3   GLN A CA  1 
ATOM   68    C  C   . GLN A  1 12  ? 21.293  -8.910  53.775 1.00 65.24  ? 3   GLN A C   1 
ATOM   69    O  O   . GLN A  1 12  ? 20.862  -8.995  52.625 1.00 68.98  ? 3   GLN A O   1 
ATOM   70    C  CB  . GLN A  1 12  ? 20.290  -10.445 55.394 1.00 63.56  ? 3   GLN A CB  1 
ATOM   71    C  CG  . GLN A  1 12  ? 20.264  -11.739 56.132 1.00 68.63  ? 3   GLN A CG  1 
ATOM   72    C  CD  . GLN A  1 12  ? 19.028  -11.821 56.991 1.00 79.69  ? 3   GLN A CD  1 
ATOM   73    O  OE1 . GLN A  1 12  ? 18.056  -11.103 56.748 1.00 71.76  ? 3   GLN A OE1 1 
ATOM   74    N  NE2 . GLN A  1 12  ? 19.056  -12.679 58.012 1.00 80.36  ? 3   GLN A NE2 1 
ATOM   75    N  N   . ALA A  1 13  ? 21.502  -7.744  54.370 1.00 63.78  ? 4   ALA A N   1 
ATOM   76    C  CA  . ALA A  1 13  ? 21.337  -6.505  53.631 1.00 62.02  ? 4   ALA A CA  1 
ATOM   77    C  C   . ALA A  1 13  ? 22.382  -6.442  52.526 1.00 59.89  ? 4   ALA A C   1 
ATOM   78    O  O   . ALA A  1 13  ? 22.077  -6.097  51.396 1.00 62.73  ? 4   ALA A O   1 
ATOM   79    C  CB  . ALA A  1 13  ? 21.453  -5.328  54.554 1.00 55.05  ? 4   ALA A CB  1 
ATOM   80    N  N   . ASN A  1 14  ? 23.614  -6.796  52.862 1.00 58.03  ? 5   ASN A N   1 
ATOM   81    C  CA  . ASN A  1 14  ? 24.691  -6.872  51.887 1.00 60.44  ? 5   ASN A CA  1 
ATOM   82    C  C   . ASN A  1 14  ? 24.407  -7.796  50.727 1.00 62.32  ? 5   ASN A C   1 
ATOM   83    O  O   . ASN A  1 14  ? 24.647  -7.442  49.576 1.00 66.42  ? 5   ASN A O   1 
ATOM   84    C  CB  . ASN A  1 14  ? 25.975  -7.339  52.553 1.00 64.36  ? 5   ASN A CB  1 
ATOM   85    C  CG  . ASN A  1 14  ? 26.712  -6.219  53.228 1.00 66.11  ? 5   ASN A CG  1 
ATOM   86    O  OD1 . ASN A  1 14  ? 26.657  -5.070  52.776 1.00 68.40  ? 5   ASN A OD1 1 
ATOM   87    N  ND2 . ASN A  1 14  ? 27.418  -6.539  54.314 1.00 61.54  ? 5   ASN A ND2 1 
ATOM   88    N  N   . LEU A  1 15  ? 23.927  -8.996  51.028 1.00 62.44  ? 6   LEU A N   1 
ATOM   89    C  CA  . LEU A  1 15  ? 23.622  -9.968  49.976 1.00 66.39  ? 6   LEU A CA  1 
ATOM   90    C  C   . LEU A  1 15  ? 22.519  -9.486  49.031 1.00 60.74  ? 6   LEU A C   1 
ATOM   91    O  O   . LEU A  1 15  ? 22.677  -9.557  47.821 1.00 60.94  ? 6   LEU A O   1 
ATOM   92    C  CB  . LEU A  1 15  ? 23.261  -11.333 50.569 1.00 58.35  ? 6   LEU A CB  1 
ATOM   93    C  CG  . LEU A  1 15  ? 22.879  -12.403 49.554 1.00 61.52  ? 6   LEU A CG  1 
ATOM   94    C  CD1 . LEU A  1 15  ? 24.014  -12.588 48.564 1.00 59.42  ? 6   LEU A CD1 1 
ATOM   95    C  CD2 . LEU A  1 15  ? 22.515  -13.709 50.263 1.00 52.75  ? 6   LEU A CD2 1 
ATOM   96    N  N   . MET A  1 16  ? 21.409  -9.003  49.584 1.00 58.67  ? 7   MET A N   1 
ATOM   97    C  CA  . MET A  1 16  ? 20.334  -8.467  48.763 1.00 63.62  ? 7   MET A CA  1 
ATOM   98    C  C   . MET A  1 16  ? 20.865  -7.350  47.852 1.00 62.23  ? 7   MET A C   1 
ATOM   99    O  O   . MET A  1 16  ? 20.503  -7.273  46.682 1.00 58.57  ? 7   MET A O   1 
ATOM   100   C  CB  . MET A  1 16  ? 19.185  -7.938  49.628 1.00 64.89  ? 7   MET A CB  1 
ATOM   101   C  CG  . MET A  1 16  ? 18.285  -8.980  50.292 1.00 67.08  ? 7   MET A CG  1 
ATOM   102   S  SD  . MET A  1 16  ? 17.164  -8.170  51.487 1.00 106.30 ? 7   MET A SD  1 
ATOM   103   C  CE  . MET A  1 16  ? 16.473  -9.541  52.413 1.00 81.15  ? 7   MET A CE  1 
ATOM   104   N  N   . ARG A  1 17  ? 21.727  -6.492  48.397 1.00 62.73  ? 8   ARG A N   1 
ATOM   105   C  CA  . ARG A  1 17  ? 22.302  -5.385  47.639 1.00 60.75  ? 8   ARG A CA  1 
ATOM   106   C  C   . ARG A  1 17  ? 23.235  -5.855  46.518 1.00 64.07  ? 8   ARG A C   1 
ATOM   107   O  O   . ARG A  1 17  ? 23.177  -5.333  45.407 1.00 64.64  ? 8   ARG A O   1 
ATOM   108   C  CB  . ARG A  1 17  ? 23.015  -4.393  48.562 1.00 61.06  ? 8   ARG A CB  1 
ATOM   109   C  CG  . ARG A  1 17  ? 23.696  -3.221  47.833 1.00 59.70  ? 8   ARG A CG  1 
ATOM   110   C  CD  . ARG A  1 17  ? 24.199  -2.146  48.802 1.00 63.52  ? 8   ARG A CD  1 
ATOM   111   N  NE  . ARG A  1 17  ? 25.083  -2.692  49.831 1.00 63.02  ? 8   ARG A NE  1 
ATOM   112   C  CZ  . ARG A  1 17  ? 26.407  -2.750  49.725 1.00 68.42  ? 8   ARG A CZ  1 
ATOM   113   N  NH1 . ARG A  1 17  ? 27.011  -2.277  48.639 1.00 62.61  ? 8   ARG A NH1 1 
ATOM   114   N  NH2 . ARG A  1 17  ? 27.130  -3.279  50.708 1.00 58.05  ? 8   ARG A NH2 1 
ATOM   115   N  N   . LEU A  1 18  ? 24.085  -6.840  46.798 1.00 62.68  ? 9   LEU A N   1 
ATOM   116   C  CA  . LEU A  1 18  ? 24.933  -7.432  45.757 1.00 61.88  ? 9   LEU A CA  1 
ATOM   117   C  C   . LEU A  1 18  ? 24.105  -8.055  44.636 1.00 66.37  ? 9   LEU A C   1 
ATOM   118   O  O   . LEU A  1 18  ? 24.399  -7.898  43.448 1.00 66.67  ? 9   LEU A O   1 
ATOM   119   C  CB  . LEU A  1 18  ? 25.834  -8.509  46.339 1.00 61.70  ? 9   LEU A CB  1 
ATOM   120   C  CG  . LEU A  1 18  ? 26.589  -9.267  45.253 1.00 57.70  ? 9   LEU A CG  1 
ATOM   121   C  CD1 . LEU A  1 18  ? 27.436  -8.311  44.435 1.00 52.84  ? 9   LEU A CD1 1 
ATOM   122   C  CD2 . LEU A  1 18  ? 27.443  -10.367 45.860 1.00 56.86  ? 9   LEU A CD2 1 
ATOM   123   N  N   . LYS A  1 19  ? 23.069  -8.781  45.030 1.00 65.10  ? 10  LYS A N   1 
ATOM   124   C  CA  . LYS A  1 19  ? 22.152  -9.371  44.076 1.00 66.26  ? 10  LYS A CA  1 
ATOM   125   C  C   . LYS A  1 19  ? 21.446  -8.318  43.213 1.00 67.81  ? 10  LYS A C   1 
ATOM   126   O  O   . LYS A  1 19  ? 21.379  -8.455  41.997 1.00 70.92  ? 10  LYS A O   1 
ATOM   127   C  CB  . LYS A  1 19  ? 21.146  -10.267 44.796 1.00 65.18  ? 10  LYS A CB  1 
ATOM   128   C  CG  . LYS A  1 19  ? 21.661  -11.676 45.056 1.00 60.65  ? 10  LYS A CG  1 
ATOM   129   C  CD  . LYS A  1 19  ? 20.526  -12.583 45.435 1.00 54.51  ? 10  LYS A CD  1 
ATOM   130   C  CE  . LYS A  1 19  ? 20.951  -14.009 45.414 1.00 62.58  ? 10  LYS A CE  1 
ATOM   131   N  NZ  . LYS A  1 19  ? 19.778  -14.877 45.671 1.00 76.09  ? 10  LYS A NZ  1 
ATOM   132   N  N   . SER A  1 20  ? 20.926  -7.275  43.848 1.00 67.72  ? 11  SER A N   1 
ATOM   133   C  CA  . SER A  1 20  ? 20.273  -6.167  43.149 1.00 73.35  ? 11  SER A CA  1 
ATOM   134   C  C   . SER A  1 20  ? 21.181  -5.476  42.111 1.00 74.59  ? 11  SER A C   1 
ATOM   135   O  O   . SER A  1 20  ? 20.737  -5.136  41.024 1.00 78.73  ? 11  SER A O   1 
ATOM   136   C  CB  . SER A  1 20  ? 19.753  -5.165  44.183 1.00 74.46  ? 11  SER A CB  1 
ATOM   137   O  OG  . SER A  1 20  ? 19.247  -3.991  43.586 1.00 79.39  ? 11  SER A OG  1 
ATOM   138   N  N   . ASP A  1 21  ? 22.461  -5.344  42.443 1.00 74.55  ? 12  ASP A N   1 
ATOM   139   C  CA  . ASP A  1 21  ? 23.439  -4.759  41.530 1.00 78.32  ? 12  ASP A CA  1 
ATOM   140   C  C   . ASP A  1 21  ? 23.629  -5.564  40.240 1.00 78.41  ? 12  ASP A C   1 
ATOM   141   O  O   . ASP A  1 21  ? 23.738  -4.987  39.159 1.00 89.96  ? 12  ASP A O   1 
ATOM   142   C  CB  . ASP A  1 21  ? 24.786  -4.578  42.235 1.00 82.00  ? 12  ASP A CB  1 
ATOM   143   C  CG  . ASP A  1 21  ? 24.885  -3.258  42.974 1.00 82.89  ? 12  ASP A CG  1 
ATOM   144   O  OD1 . ASP A  1 21  ? 23.902  -2.874  43.641 1.00 63.24  ? 12  ASP A OD1 1 
ATOM   145   O  OD2 . ASP A  1 21  ? 25.946  -2.605  42.887 1.00 95.77  ? 12  ASP A OD2 1 
ATOM   146   N  N   . LEU A  1 22  ? 23.668  -6.891  40.350 1.00 77.81  ? 13  LEU A N   1 
ATOM   147   C  CA  . LEU A  1 22  ? 23.848  -7.741  39.173 1.00 77.40  ? 13  LEU A CA  1 
ATOM   148   C  C   . LEU A  1 22  ? 22.594  -7.944  38.285 1.00 80.05  ? 13  LEU A C   1 
ATOM   149   O  O   . LEU A  1 22  ? 22.672  -7.764  37.077 1.00 84.70  ? 13  LEU A O   1 
ATOM   150   C  CB  . LEU A  1 22  ? 24.485  -9.079  39.588 1.00 76.72  ? 13  LEU A CB  1 
ATOM   151   C  CG  . LEU A  1 22  ? 25.609  -8.960  40.630 1.00 71.53  ? 13  LEU A CG  1 
ATOM   152   C  CD1 . LEU A  1 22  ? 26.265  -10.283 40.893 1.00 65.00  ? 13  LEU A CD1 1 
ATOM   153   C  CD2 . LEU A  1 22  ? 26.660  -7.970  40.213 1.00 76.41  ? 13  LEU A CD2 1 
ATOM   154   N  N   . PHE A  1 23  ? 21.448  -8.285  38.888 1.00 79.97  ? 14  PHE A N   1 
ATOM   155   C  CA  . PHE A  1 23  ? 20.255  -8.711  38.127 1.00 83.53  ? 14  PHE A CA  1 
ATOM   156   C  C   . PHE A  1 23  ? 19.229  -7.612  37.864 1.00 83.18  ? 14  PHE A C   1 
ATOM   157   O  O   . PHE A  1 23  ? 18.197  -7.869  37.252 1.00 80.10  ? 14  PHE A O   1 
ATOM   158   C  CB  . PHE A  1 23  ? 19.517  -9.850  38.867 1.00 88.45  ? 14  PHE A CB  1 
ATOM   159   C  CG  . PHE A  1 23  ? 20.414  -10.976 39.335 1.00 84.69  ? 14  PHE A CG  1 
ATOM   160   C  CD1 . PHE A  1 23  ? 21.610  -11.261 38.682 1.00 78.77  ? 14  PHE A CD1 1 
ATOM   161   C  CD2 . PHE A  1 23  ? 20.044  -11.761 40.418 1.00 79.34  ? 14  PHE A CD2 1 
ATOM   162   C  CE1 . PHE A  1 23  ? 22.417  -12.287 39.110 1.00 69.91  ? 14  PHE A CE1 1 
ATOM   163   C  CE2 . PHE A  1 23  ? 20.850  -12.794 40.845 1.00 76.00  ? 14  PHE A CE2 1 
ATOM   164   C  CZ  . PHE A  1 23  ? 22.039  -13.055 40.184 1.00 70.77  ? 14  PHE A CZ  1 
ATOM   165   N  N   . ASN A  1 24  ? 19.498  -6.423  38.400 1.00 88.16  ? 15  ASN A N   1 
ATOM   166   C  CA  . ASN A  1 24  ? 18.602  -5.248  38.380 1.00 93.43  ? 15  ASN A CA  1 
ATOM   167   C  C   . ASN A  1 24  ? 19.278  -3.930  37.963 1.00 97.34  ? 15  ASN A C   1 
ATOM   168   O  O   . ASN A  1 24  ? 18.736  -3.141  37.187 1.00 98.53  ? 15  ASN A O   1 
ATOM   169   C  CB  . ASN A  1 24  ? 17.977  -4.974  39.754 1.00 93.88  ? 15  ASN A CB  1 
ATOM   170   C  CG  . ASN A  1 24  ? 17.160  -6.148  40.286 1.00 92.83  ? 15  ASN A CG  1 
ATOM   171   O  OD1 . ASN A  1 24  ? 17.225  -7.265  39.768 1.00 98.51  ? 15  ASN A OD1 1 
ATOM   172   N  ND2 . ASN A  1 24  ? 16.395  -5.894  41.341 1.00 85.25  ? 15  ASN A ND2 1 
ATOM   173   N  N   . ARG A  1 25  ? 20.432  -3.674  38.564 1.00 96.80  ? 16  ARG A N   1 
ATOM   174   C  CA  . ARG A  1 25  ? 21.315  -2.612  38.126 1.00 97.92  ? 16  ARG A CA  1 
ATOM   175   C  C   . ARG A  1 25  ? 21.634  -2.858  36.654 1.00 107.24 ? 16  ARG A C   1 
ATOM   176   O  O   . ARG A  1 25  ? 21.374  -1.981  35.833 1.00 114.35 ? 16  ARG A O   1 
ATOM   177   C  CB  . ARG A  1 25  ? 22.607  -2.648  38.967 1.00 97.47  ? 16  ARG A CB  1 
ATOM   178   C  CG  . ARG A  1 25  ? 23.758  -1.813  38.429 0.00 97.92  ? 16  ARG A CG  1 
ATOM   179   C  CD  . ARG A  1 25  ? 24.964  -1.872  39.368 0.00 95.56  ? 16  ARG A CD  1 
ATOM   180   N  NE  . ARG A  1 25  ? 26.026  -0.941  38.990 0.00 96.46  ? 16  ARG A NE  1 
ATOM   181   C  CZ  . ARG A  1 25  ? 26.922  -1.174  38.036 0.00 95.94  ? 16  ARG A CZ  1 
ATOM   182   N  NH1 . ARG A  1 25  ? 26.883  -2.308  37.350 0.00 101.80 ? 16  ARG A NH1 1 
ATOM   183   N  NH2 . ARG A  1 25  ? 27.854  -0.271  37.762 0.00 90.26  ? 16  ARG A NH2 1 
ATOM   184   N  N   . SER A  1 26  ? 22.229  -4.005  36.316 1.00 99.89  ? 17  SER A N   1 
ATOM   185   C  CA  . SER A  1 26  ? 22.568  -4.280  34.921 1.00 114.34 ? 17  SER A CA  1 
ATOM   186   C  C   . SER A  1 26  ? 21.772  -5.438  34.349 1.00 113.87 ? 17  SER A C   1 
ATOM   187   O  O   . SER A  1 26  ? 21.463  -6.402  35.034 1.00 108.95 ? 17  SER A O   1 
ATOM   188   C  CB  . SER A  1 26  ? 24.074  -4.535  34.740 1.00 106.41 ? 17  SER A CB  1 
ATOM   189   O  OG  . SER A  1 26  ? 24.818  -3.405  35.141 1.00 99.62  ? 17  SER A OG  1 
ATOM   190   N  N   . PRO A  1 27  ? 21.430  -5.328  33.061 1.00 117.44 ? 18  PRO A N   1 
ATOM   191   C  CA  . PRO A  1 27  ? 20.568  -6.235  32.291 1.00 112.52 ? 18  PRO A CA  1 
ATOM   192   C  C   . PRO A  1 27  ? 21.250  -7.554  31.953 1.00 107.73 ? 18  PRO A C   1 
ATOM   193   O  O   . PRO A  1 27  ? 22.447  -7.511  31.685 1.00 107.57 ? 18  PRO A O   1 
ATOM   194   C  CB  . PRO A  1 27  ? 20.271  -5.448  31.001 1.00 105.05 ? 18  PRO A CB  1 
ATOM   195   C  CG  . PRO A  1 27  ? 21.421  -4.478  30.911 1.00 116.12 ? 18  PRO A CG  1 
ATOM   196   C  CD  . PRO A  1 27  ? 21.860  -4.165  32.279 1.00 117.64 ? 18  PRO A CD  1 
ATOM   197   N  N   . MET A  1 28  ? 20.487  -8.650  31.837 1.00 109.07 ? 19  MET A N   1 
ATOM   198   C  CA  . MET A  1 28  ? 21.041  -10.011 31.720 1.00 101.32 ? 19  MET A CA  1 
ATOM   199   C  C   . MET A  1 28  ? 21.915  -10.204 30.472 1.00 94.48  ? 19  MET A C   1 
ATOM   200   O  O   . MET A  1 28  ? 21.568  -9.740  29.381 1.00 88.32  ? 19  MET A O   1 
ATOM   201   C  CB  . MET A  1 28  ? 19.909  -11.057 31.752 1.00 88.03  ? 19  MET A CB  1 
ATOM   202   C  CG  . MET A  1 28  ? 20.339  -12.514 31.929 1.00 83.01  ? 19  MET A CG  1 
ATOM   203   S  SD  . MET A  1 28  ? 19.004  -13.687 32.364 1.00 94.93  ? 19  MET A SD  1 
ATOM   204   C  CE  . MET A  1 28  ? 18.398  -13.008 33.928 1.00 76.47  ? 19  MET A CE  1 
ATOM   205   N  N   . TYR A  1 29  ? 23.028  -10.913 30.654 1.00 82.52  ? 20  TYR A N   1 
ATOM   206   C  CA  . TYR A  1 29  ? 24.009  -11.225 29.609 1.00 74.48  ? 20  TYR A CA  1 
ATOM   207   C  C   . TYR A  1 29  ? 23.336  -11.877 28.377 1.00 76.86  ? 20  TYR A C   1 
ATOM   208   O  O   . TYR A  1 29  ? 22.649  -12.907 28.486 1.00 77.71  ? 20  TYR A O   1 
ATOM   209   C  CB  . TYR A  1 29  ? 25.078  -12.120 30.259 1.00 64.21  ? 20  TYR A CB  1 
ATOM   210   C  CG  . TYR A  1 29  ? 26.149  -12.729 29.389 1.00 62.45  ? 20  TYR A CG  1 
ATOM   211   C  CD1 . TYR A  1 29  ? 27.280  -12.011 29.020 1.00 64.46  ? 20  TYR A CD1 1 
ATOM   212   C  CD2 . TYR A  1 29  ? 26.059  -14.051 28.992 1.00 64.35  ? 20  TYR A CD2 1 
ATOM   213   C  CE1 . TYR A  1 29  ? 28.273  -12.593 28.234 1.00 69.57  ? 20  TYR A CE1 1 
ATOM   214   C  CE2 . TYR A  1 29  ? 27.034  -14.640 28.210 1.00 66.95  ? 20  TYR A CE2 1 
ATOM   215   C  CZ  . TYR A  1 29  ? 28.139  -13.918 27.832 1.00 71.82  ? 20  TYR A CZ  1 
ATOM   216   O  OH  . TYR A  1 29  ? 29.094  -14.546 27.055 1.00 65.68  ? 20  TYR A OH  1 
ATOM   217   N  N   . PRO A  1 30  ? 23.526  -11.261 27.197 1.00 69.98  ? 21  PRO A N   1 
ATOM   218   C  CA  . PRO A  1 30  ? 22.904  -11.604 25.912 1.00 70.89  ? 21  PRO A CA  1 
ATOM   219   C  C   . PRO A  1 30  ? 23.371  -12.942 25.402 1.00 70.12  ? 21  PRO A C   1 
ATOM   220   O  O   . PRO A  1 30  ? 22.817  -13.438 24.419 1.00 70.22  ? 21  PRO A O   1 
ATOM   221   C  CB  . PRO A  1 30  ? 23.378  -10.492 24.980 1.00 69.08  ? 21  PRO A CB  1 
ATOM   222   C  CG  . PRO A  1 30  ? 24.662  -10.044 25.567 1.00 71.59  ? 21  PRO A CG  1 
ATOM   223   C  CD  . PRO A  1 30  ? 24.483  -10.152 27.053 1.00 75.12  ? 21  PRO A CD  1 
ATOM   224   N  N   . GLY A  1 31  ? 24.427  -13.462 26.023 1.00 62.51  ? 22  GLY A N   1 
ATOM   225   C  CA  . GLY A  1 31  ? 25.043  -14.709 25.627 1.00 65.66  ? 22  GLY A CA  1 
ATOM   226   C  C   . GLY A  1 31  ? 26.361  -14.427 24.945 1.00 69.42  ? 22  GLY A C   1 
ATOM   227   O  O   . GLY A  1 31  ? 26.689  -13.270 24.684 1.00 68.19  ? 22  GLY A O   1 
ATOM   228   N  N   . PRO A  1 32  ? 27.140  -15.483 24.674 1.00 71.85  ? 23  PRO A N   1 
ATOM   229   C  CA  . PRO A  1 32  ? 28.425  -15.335 23.981 1.00 70.68  ? 23  PRO A CA  1 
ATOM   230   C  C   . PRO A  1 32  ? 28.272  -15.032 22.490 1.00 66.85  ? 23  PRO A C   1 
ATOM   231   O  O   . PRO A  1 32  ? 27.226  -15.299 21.894 1.00 67.62  ? 23  PRO A O   1 
ATOM   232   C  CB  . PRO A  1 32  ? 29.101  -16.693 24.199 1.00 68.31  ? 23  PRO A CB  1 
ATOM   233   C  CG  . PRO A  1 32  ? 27.986  -17.637 24.412 1.00 68.31  ? 23  PRO A CG  1 
ATOM   234   C  CD  . PRO A  1 32  ? 26.904  -16.868 25.112 1.00 67.39  ? 23  PRO A CD  1 
ATOM   235   N  N   . THR A  1 33  ? 29.322  -14.459 21.912 1.00 68.23  ? 24  THR A N   1 
ATOM   236   C  CA  . THR A  1 33  ? 29.362  -14.123 20.496 1.00 77.60  ? 24  THR A CA  1 
ATOM   237   C  C   . THR A  1 33  ? 30.774  -14.358 19.976 1.00 80.60  ? 24  THR A C   1 
ATOM   238   O  O   . THR A  1 33  ? 31.629  -14.851 20.716 1.00 81.21  ? 24  THR A O   1 
ATOM   239   C  CB  . THR A  1 33  ? 28.963  -12.663 20.255 1.00 73.71  ? 24  THR A CB  1 
ATOM   240   O  OG1 . THR A  1 33  ? 29.817  -11.805 21.013 1.00 68.36  ? 24  THR A OG1 1 
ATOM   241   C  CG2 . THR A  1 33  ? 27.542  -12.435 20.696 1.00 74.95  ? 24  THR A CG2 1 
ATOM   242   N  N   . LYS A  1 34  ? 31.020  -14.012 18.713 1.00 72.18  ? 25  LYS A N   1 
ATOM   243   C  CA  . LYS A  1 34  ? 32.347  -14.189 18.126 1.00 73.09  ? 25  LYS A CA  1 
ATOM   244   C  C   . LYS A  1 34  ? 33.385  -13.339 18.857 1.00 81.35  ? 25  LYS A C   1 
ATOM   245   O  O   . LYS A  1 34  ? 34.509  -13.790 19.100 1.00 75.39  ? 25  LYS A O   1 
ATOM   246   C  CB  . LYS A  1 34  ? 32.338  -13.830 16.634 1.00 86.68  ? 25  LYS A CB  1 
ATOM   247   C  CG  . LYS A  1 34  ? 31.421  -14.683 15.756 1.00 83.55  ? 25  LYS A CG  1 
ATOM   248   C  CD  . LYS A  1 34  ? 31.376  -14.124 14.342 0.00 93.78  ? 25  LYS A CD  1 
ATOM   249   C  CE  . LYS A  1 34  ? 30.371  -14.863 13.474 0.00 96.18  ? 25  LYS A CE  1 
ATOM   250   N  NZ  . LYS A  1 34  ? 30.446  -14.421 12.052 0.00 99.42  ? 25  LYS A NZ  1 
ATOM   251   N  N   . ASP A  1 35  ? 32.991  -12.114 19.213 1.00 83.19  ? 26  ASP A N   1 
ATOM   252   C  CA  . ASP A  1 35  ? 33.903  -11.126 19.791 1.00 78.94  ? 26  ASP A CA  1 
ATOM   253   C  C   . ASP A  1 35  ? 33.973  -11.227 21.296 1.00 80.56  ? 26  ASP A C   1 
ATOM   254   O  O   . ASP A  1 35  ? 34.737  -10.502 21.930 1.00 86.68  ? 26  ASP A O   1 
ATOM   255   C  CB  . ASP A  1 35  ? 33.468  -9.697  19.446 1.00 79.40  ? 26  ASP A CB  1 
ATOM   256   C  CG  . ASP A  1 35  ? 32.860  -9.584  18.067 1.00 90.91  ? 26  ASP A CG  1 
ATOM   257   O  OD1 . ASP A  1 35  ? 33.624  -9.465  17.081 1.00 96.99  ? 26  ASP A OD1 1 
ATOM   258   O  OD2 . ASP A  1 35  ? 31.612  -9.602  17.974 1.00 88.00  ? 26  ASP A OD2 1 
ATOM   259   N  N   . ASP A  1 36  ? 33.127  -12.075 21.870 1.00 81.30  ? 27  ASP A N   1 
ATOM   260   C  CA  . ASP A  1 36  ? 33.080  -12.243 23.317 1.00 81.99  ? 27  ASP A CA  1 
ATOM   261   C  C   . ASP A  1 36  ? 32.879  -13.718 23.628 1.00 74.39  ? 27  ASP A C   1 
ATOM   262   O  O   . ASP A  1 36  ? 31.905  -14.090 24.268 1.00 73.84  ? 27  ASP A O   1 
ATOM   263   C  CB  . ASP A  1 36  ? 31.914  -11.409 23.859 1.00 78.72  ? 27  ASP A CB  1 
ATOM   264   C  CG  . ASP A  1 36  ? 31.943  -11.249 25.354 1.00 83.17  ? 27  ASP A CG  1 
ATOM   265   O  OD1 . ASP A  1 36  ? 30.861  -10.982 25.930 1.00 77.74  ? 27  ASP A OD1 1 
ATOM   266   O  OD2 . ASP A  1 36  ? 33.038  -11.382 25.946 1.00 88.34  ? 27  ASP A OD2 1 
ATOM   267   N  N   . PRO A  1 37  ? 33.819  -14.568 23.205 1.00 74.92  ? 28  PRO A N   1 
ATOM   268   C  CA  . PRO A  1 37  ? 33.506  -15.991 23.304 1.00 70.59  ? 28  PRO A CA  1 
ATOM   269   C  C   . PRO A  1 37  ? 33.565  -16.473 24.746 1.00 70.46  ? 28  PRO A C   1 
ATOM   270   O  O   . PRO A  1 37  ? 34.124  -15.794 25.613 1.00 63.12  ? 28  PRO A O   1 
ATOM   271   C  CB  . PRO A  1 37  ? 34.598  -16.645 22.463 1.00 66.90  ? 28  PRO A CB  1 
ATOM   272   C  CG  . PRO A  1 37  ? 35.754  -15.737 22.602 1.00 73.61  ? 28  PRO A CG  1 
ATOM   273   C  CD  . PRO A  1 37  ? 35.193  -14.340 22.729 1.00 79.87  ? 28  PRO A CD  1 
ATOM   274   N  N   . LEU A  1 38  ? 32.975  -17.642 24.980 1.00 69.80  ? 29  LEU A N   1 
ATOM   275   C  CA  . LEU A  1 38  ? 32.876  -18.240 26.307 1.00 68.31  ? 29  LEU A CA  1 
ATOM   276   C  C   . LEU A  1 38  ? 33.391  -19.691 26.355 1.00 67.27  ? 29  LEU A C   1 
ATOM   277   O  O   . LEU A  1 38  ? 33.145  -20.491 25.449 1.00 63.87  ? 29  LEU A O   1 
ATOM   278   C  CB  . LEU A  1 38  ? 31.420  -18.195 26.766 1.00 64.35  ? 29  LEU A CB  1 
ATOM   279   C  CG  . LEU A  1 38  ? 31.119  -18.704 28.165 1.00 59.68  ? 29  LEU A CG  1 
ATOM   280   C  CD1 . LEU A  1 38  ? 31.916  -17.902 29.182 1.00 56.70  ? 29  LEU A CD1 1 
ATOM   281   C  CD2 . LEU A  1 38  ? 29.628  -18.627 28.428 1.00 60.58  ? 29  LEU A CD2 1 
ATOM   282   N  N   . THR A  1 39  ? 34.108  -20.022 27.422 1.00 64.14  ? 30  THR A N   1 
ATOM   283   C  CA  . THR A  1 39  ? 34.533  -21.396 27.658 1.00 66.11  ? 30  THR A CA  1 
ATOM   284   C  C   . THR A  1 39  ? 33.695  -22.018 28.771 1.00 60.13  ? 30  THR A C   1 
ATOM   285   O  O   . THR A  1 39  ? 33.550  -21.451 29.839 1.00 60.46  ? 30  THR A O   1 
ATOM   286   C  CB  . THR A  1 39  ? 36.020  -21.451 28.032 1.00 67.76  ? 30  THR A CB  1 
ATOM   287   O  OG1 . THR A  1 39  ? 36.767  -20.675 27.090 1.00 70.16  ? 30  THR A OG1 1 
ATOM   288   C  CG2 . THR A  1 39  ? 36.534  -22.880 28.028 1.00 65.19  ? 30  THR A CG2 1 
ATOM   289   N  N   . VAL A  1 40  ? 33.133  -23.185 28.506 1.00 62.74  ? 31  VAL A N   1 
ATOM   290   C  CA  . VAL A  1 40  ? 32.324  -23.887 29.490 1.00 61.26  ? 31  VAL A CA  1 
ATOM   291   C  C   . VAL A  1 40  ? 32.944  -25.239 29.795 1.00 64.29  ? 31  VAL A C   1 
ATOM   292   O  O   . VAL A  1 40  ? 33.113  -26.052 28.892 1.00 71.88  ? 31  VAL A O   1 
ATOM   293   C  CB  . VAL A  1 40  ? 30.910  -24.119 28.948 1.00 61.67  ? 31  VAL A CB  1 
ATOM   294   C  CG1 . VAL A  1 40  ? 30.067  -24.894 29.941 1.00 56.78  ? 31  VAL A CG1 1 
ATOM   295   C  CG2 . VAL A  1 40  ? 30.265  -22.797 28.595 1.00 64.78  ? 31  VAL A CG2 1 
ATOM   296   N  N   . TYR A  1 41  ? 33.277  -25.487 31.061 1.00 65.76  ? 32  TYR A N   1 
ATOM   297   C  CA  . TYR A  1 41  ? 33.825  -26.786 31.464 1.00 67.85  ? 32  TYR A CA  1 
ATOM   298   C  C   . TYR A  1 41  ? 32.740  -27.796 31.844 1.00 66.52  ? 32  TYR A C   1 
ATOM   299   O  O   . TYR A  1 41  ? 31.825  -27.482 32.607 1.00 63.91  ? 32  TYR A O   1 
ATOM   300   C  CB  . TYR A  1 41  ? 34.824  -26.636 32.609 1.00 61.87  ? 32  TYR A CB  1 
ATOM   301   C  CG  . TYR A  1 41  ? 36.124  -25.974 32.215 1.00 70.95  ? 32  TYR A CG  1 
ATOM   302   C  CD1 . TYR A  1 41  ? 37.121  -26.688 31.552 1.00 76.78  ? 32  TYR A CD1 1 
ATOM   303   C  CD2 . TYR A  1 41  ? 36.368  -24.632 32.522 1.00 71.51  ? 32  TYR A CD2 1 
ATOM   304   C  CE1 . TYR A  1 41  ? 38.325  -26.077 31.197 1.00 82.54  ? 32  TYR A CE1 1 
ATOM   305   C  CE2 . TYR A  1 41  ? 37.563  -24.013 32.178 1.00 67.75  ? 32  TYR A CE2 1 
ATOM   306   C  CZ  . TYR A  1 41  ? 38.541  -24.737 31.515 1.00 78.17  ? 32  TYR A CZ  1 
ATOM   307   O  OH  . TYR A  1 41  ? 39.731  -24.123 31.172 1.00 80.54  ? 32  TYR A OH  1 
ATOM   308   N  N   . LEU A  1 42  ? 32.865  -29.008 31.301 1.00 67.46  ? 33  LEU A N   1 
ATOM   309   C  CA  . LEU A  1 42  ? 31.939  -30.104 31.571 1.00 62.67  ? 33  LEU A CA  1 
ATOM   310   C  C   . LEU A  1 42  ? 32.632  -31.262 32.231 1.00 62.99  ? 33  LEU A C   1 
ATOM   311   O  O   . LEU A  1 42  ? 33.696  -31.685 31.807 1.00 72.10  ? 33  LEU A O   1 
ATOM   312   C  CB  . LEU A  1 42  ? 31.323  -30.629 30.281 1.00 62.31  ? 33  LEU A CB  1 
ATOM   313   C  CG  . LEU A  1 42  ? 30.230  -29.803 29.624 1.00 65.98  ? 33  LEU A CG  1 
ATOM   314   C  CD1 . LEU A  1 42  ? 29.444  -30.711 28.720 1.00 63.16  ? 33  LEU A CD1 1 
ATOM   315   C  CD2 . LEU A  1 42  ? 29.326  -29.209 30.682 1.00 70.89  ? 33  LEU A CD2 1 
ATOM   316   N  N   . SER A  1 43  ? 32.011  -31.782 33.271 1.00 65.23  ? 34  SER A N   1 
ATOM   317   C  CA  . SER A  1 43  ? 32.462  -33.009 33.887 1.00 63.30  ? 34  SER A CA  1 
ATOM   318   C  C   . SER A  1 43  ? 31.235  -33.790 34.304 1.00 65.89  ? 34  SER A C   1 
ATOM   319   O  O   . SER A  1 43  ? 30.298  -33.226 34.865 1.00 65.81  ? 34  SER A O   1 
ATOM   320   C  CB  . SER A  1 43  ? 33.323  -32.718 35.104 1.00 66.31  ? 34  SER A CB  1 
ATOM   321   O  OG  . SER A  1 43  ? 33.789  -33.930 35.671 1.00 78.90  ? 34  SER A OG  1 
ATOM   322   N  N   . PHE A  1 44  ? 31.253  -35.091 34.048 1.00 64.58  ? 35  PHE A N   1 
ATOM   323   C  CA  . PHE A  1 44  ? 30.147  -35.958 34.423 1.00 66.38  ? 35  PHE A CA  1 
ATOM   324   C  C   . PHE A  1 44  ? 30.446  -36.826 35.647 1.00 64.80  ? 35  PHE A C   1 
ATOM   325   O  O   . PHE A  1 44  ? 31.589  -37.178 35.932 1.00 64.48  ? 35  PHE A O   1 
ATOM   326   C  CB  . PHE A  1 44  ? 29.729  -36.840 33.251 1.00 58.13  ? 35  PHE A CB  1 
ATOM   327   C  CG  . PHE A  1 44  ? 29.274  -36.068 32.064 1.00 69.32  ? 35  PHE A CG  1 
ATOM   328   C  CD1 . PHE A  1 44  ? 27.933  -35.756 31.899 1.00 66.49  ? 35  PHE A CD1 1 
ATOM   329   C  CD2 . PHE A  1 44  ? 30.188  -35.627 31.115 1.00 69.45  ? 35  PHE A CD2 1 
ATOM   330   C  CE1 . PHE A  1 44  ? 27.508  -35.024 30.801 1.00 64.64  ? 35  PHE A CE1 1 
ATOM   331   C  CE2 . PHE A  1 44  ? 29.770  -34.895 30.011 1.00 62.30  ? 35  PHE A CE2 1 
ATOM   332   C  CZ  . PHE A  1 44  ? 28.431  -34.591 29.855 1.00 60.60  ? 35  PHE A CZ  1 
ATOM   333   N  N   . SER A  1 45  ? 29.391  -37.111 36.391 1.00 62.20  ? 36  SER A N   1 
ATOM   334   C  CA  . SER A  1 45  ? 29.419  -38.100 37.439 1.00 56.76  ? 36  SER A CA  1 
ATOM   335   C  C   . SER A  1 45  ? 28.251  -39.067 37.196 1.00 57.56  ? 36  SER A C   1 
ATOM   336   O  O   . SER A  1 45  ? 27.093  -38.664 37.109 1.00 55.60  ? 36  SER A O   1 
ATOM   337   C  CB  . SER A  1 45  ? 29.308  -37.409 38.795 1.00 53.40  ? 36  SER A CB  1 
ATOM   338   O  OG  . SER A  1 45  ? 29.696  -38.275 39.829 1.00 54.68  ? 36  SER A OG  1 
ATOM   339   N  N   . LEU A  1 46  ? 28.568  -40.345 37.050 1.00 59.12  ? 37  LEU A N   1 
ATOM   340   C  CA  . LEU A  1 46  ? 27.564  -41.369 36.811 1.00 54.84  ? 37  LEU A CA  1 
ATOM   341   C  C   . LEU A  1 46  ? 26.953  -41.987 38.048 1.00 62.64  ? 37  LEU A C   1 
ATOM   342   O  O   . LEU A  1 46  ? 27.656  -42.566 38.880 1.00 63.84  ? 37  LEU A O   1 
ATOM   343   C  CB  . LEU A  1 46  ? 28.194  -42.530 36.078 1.00 56.43  ? 37  LEU A CB  1 
ATOM   344   C  CG  . LEU A  1 46  ? 27.941  -42.478 34.591 1.00 66.82  ? 37  LEU A CG  1 
ATOM   345   C  CD1 . LEU A  1 46  ? 28.660  -43.624 33.891 1.00 72.10  ? 37  LEU A CD1 1 
ATOM   346   C  CD2 . LEU A  1 46  ? 26.440  -42.569 34.414 1.00 73.63  ? 37  LEU A CD2 1 
ATOM   347   N  N   . LEU A  1 47  ? 25.637  -41.881 38.157 1.00 61.48  ? 38  LEU A N   1 
ATOM   348   C  CA  . LEU A  1 47  ? 24.917  -42.375 39.332 1.00 56.63  ? 38  LEU A CA  1 
ATOM   349   C  C   . LEU A  1 47  ? 24.322  -43.768 39.205 1.00 60.43  ? 38  LEU A C   1 
ATOM   350   O  O   . LEU A  1 47  ? 24.613  -44.646 40.017 1.00 59.20  ? 38  LEU A O   1 
ATOM   351   C  CB  . LEU A  1 47  ? 23.863  -41.359 39.755 1.00 52.26  ? 38  LEU A CB  1 
ATOM   352   C  CG  . LEU A  1 47  ? 24.335  -40.421 40.863 1.00 55.98  ? 38  LEU A CG  1 
ATOM   353   C  CD1 . LEU A  1 47  ? 25.711  -39.852 40.576 1.00 56.93  ? 38  LEU A CD1 1 
ATOM   354   C  CD2 . LEU A  1 47  ? 23.321  -39.332 41.055 1.00 58.24  ? 38  LEU A CD2 1 
ATOM   355   N  N   . ASP A  1 48  ? 23.435  -43.949 38.231 1.00 54.15  ? 39  ASP A N   1 
ATOM   356   C  CA  . ASP A  1 48  ? 22.838  -45.251 37.996 1.00 49.69  ? 39  ASP A CA  1 
ATOM   357   C  C   . ASP A  1 48  ? 22.555  -45.515 36.518 1.00 53.43  ? 39  ASP A C   1 
ATOM   358   O  O   . ASP A  1 48  ? 22.212  -44.607 35.760 1.00 57.55  ? 39  ASP A O   1 
ATOM   359   C  CB  . ASP A  1 48  ? 21.533  -45.346 38.778 1.00 49.94  ? 39  ASP A CB  1 
ATOM   360   C  CG  . ASP A  1 48  ? 21.118  -46.769 39.037 1.00 57.47  ? 39  ASP A CG  1 
ATOM   361   O  OD1 . ASP A  1 48  ? 21.756  -47.682 38.478 1.00 54.28  ? 39  ASP A OD1 1 
ATOM   362   O  OD2 . ASP A  1 48  ? 20.156  -46.982 39.800 1.00 60.51  ? 39  ASP A OD2 1 
ATOM   363   N  N   . ILE A  1 49  ? 22.672  -46.766 36.098 1.00 47.95  ? 40  ILE A N   1 
ATOM   364   C  CA  . ILE A  1 49  ? 22.020  -47.128 34.860 1.00 52.27  ? 40  ILE A CA  1 
ATOM   365   C  C   . ILE A  1 49  ? 20.752  -47.847 35.274 1.00 52.19  ? 40  ILE A C   1 
ATOM   366   O  O   . ILE A  1 49  ? 20.782  -49.000 35.658 1.00 59.70  ? 40  ILE A O   1 
ATOM   367   C  CB  . ILE A  1 49  ? 22.900  -48.055 34.002 1.00 54.96  ? 40  ILE A CB  1 
ATOM   368   C  CG1 . ILE A  1 49  ? 24.156  -47.307 33.550 1.00 53.23  ? 40  ILE A CG1 1 
ATOM   369   C  CG2 . ILE A  1 49  ? 22.115  -48.585 32.811 1.00 52.92  ? 40  ILE A CG2 1 
ATOM   370   C  CD1 . ILE A  1 49  ? 24.914  -47.973 32.437 1.00 54.60  ? 40  ILE A CD1 1 
ATOM   371   N  N   . VAL A  1 50  ? 19.616  -47.188 35.133 1.00 53.03  ? 41  VAL A N   1 
ATOM   372   C  CA  . VAL A  1 50  ? 18.400  -47.742 35.690 1.00 53.74  ? 41  VAL A CA  1 
ATOM   373   C  C   . VAL A  1 50  ? 17.826  -48.862 34.844 1.00 55.13  ? 41  VAL A C   1 
ATOM   374   O  O   . VAL A  1 50  ? 17.355  -49.863 35.377 1.00 54.83  ? 41  VAL A O   1 
ATOM   375   C  CB  . VAL A  1 50  ? 17.334  -46.675 35.872 1.00 53.66  ? 41  VAL A CB  1 
ATOM   376   C  CG1 . VAL A  1 50  ? 16.085  -47.295 36.487 1.00 52.97  ? 41  VAL A CG1 1 
ATOM   377   C  CG2 . VAL A  1 50  ? 17.878  -45.546 36.720 1.00 52.32  ? 41  VAL A CG2 1 
ATOM   378   N  N   . LYS A  1 51  ? 17.850  -48.671 33.527 1.00 61.17  ? 42  LYS A N   1 
ATOM   379   C  CA  . LYS A  1 51  ? 17.217  -49.589 32.583 1.00 60.63  ? 42  LYS A CA  1 
ATOM   380   C  C   . LYS A  1 51  ? 17.976  -49.591 31.260 1.00 66.07  ? 42  LYS A C   1 
ATOM   381   O  O   . LYS A  1 51  ? 18.427  -48.539 30.794 1.00 65.72  ? 42  LYS A O   1 
ATOM   382   C  CB  . LYS A  1 51  ? 15.771  -49.144 32.342 1.00 52.13  ? 42  LYS A CB  1 
ATOM   383   C  CG  . LYS A  1 51  ? 14.980  -50.000 31.407 1.00 59.23  ? 42  LYS A CG  1 
ATOM   384   C  CD  . LYS A  1 51  ? 13.897  -49.174 30.731 1.00 70.98  ? 42  LYS A CD  1 
ATOM   385   C  CE  . LYS A  1 51  ? 12.793  -48.799 31.698 1.00 67.89  ? 42  LYS A CE  1 
ATOM   386   N  NZ  . LYS A  1 51  ? 12.107  -50.015 32.212 1.00 73.94  ? 42  LYS A NZ  1 
ATOM   387   N  N   . ALA A  1 52  ? 18.101  -50.766 30.643 1.00 67.59  ? 43  ALA A N   1 
ATOM   388   C  CA  . ALA A  1 52  ? 18.558  -50.852 29.257 1.00 61.80  ? 43  ALA A CA  1 
ATOM   389   C  C   . ALA A  1 52  ? 17.496  -51.610 28.490 1.00 61.50  ? 43  ALA A C   1 
ATOM   390   O  O   . ALA A  1 52  ? 17.283  -52.791 28.723 1.00 76.75  ? 43  ALA A O   1 
ATOM   391   C  CB  . ALA A  1 52  ? 19.903  -51.563 29.166 1.00 56.26  ? 43  ALA A CB  1 
ATOM   392   N  N   . ASP A  1 53  ? 16.822  -50.939 27.570 1.00 62.86  ? 44  ASP A N   1 
ATOM   393   C  CA  . ASP A  1 53  ? 15.737  -51.571 26.825 1.00 66.13  ? 44  ASP A CA  1 
ATOM   394   C  C   . ASP A  1 53  ? 16.207  -52.126 25.464 1.00 66.33  ? 44  ASP A C   1 
ATOM   395   O  O   . ASP A  1 53  ? 16.596  -51.374 24.565 1.00 61.34  ? 44  ASP A O   1 
ATOM   396   C  CB  . ASP A  1 53  ? 14.555  -50.604 26.676 1.00 70.36  ? 44  ASP A CB  1 
ATOM   397   C  CG  . ASP A  1 53  ? 13.299  -51.287 26.167 1.00 71.48  ? 44  ASP A CG  1 
ATOM   398   O  OD1 . ASP A  1 53  ? 13.403  -52.039 25.179 1.00 72.50  ? 44  ASP A OD1 1 
ATOM   399   O  OD2 . ASP A  1 53  ? 12.211  -51.078 26.749 1.00 69.05  ? 44  ASP A OD2 1 
ATOM   400   N  N   . SER A  1 54  ? 16.162  -53.454 25.345 1.00 69.85  ? 45  SER A N   1 
ATOM   401   C  CA  . SER A  1 54  ? 16.617  -54.183 24.161 1.00 65.88  ? 45  SER A CA  1 
ATOM   402   C  C   . SER A  1 54  ? 15.622  -54.046 23.013 1.00 63.69  ? 45  SER A C   1 
ATOM   403   O  O   . SER A  1 54  ? 16.007  -54.011 21.841 1.00 62.17  ? 45  SER A O   1 
ATOM   404   C  CB  . SER A  1 54  ? 16.806  -55.666 24.498 1.00 68.32  ? 45  SER A CB  1 
ATOM   405   O  OG  . SER A  1 54  ? 16.949  -55.865 25.899 1.00 82.07  ? 45  SER A OG  1 
ATOM   406   N  N   . SER A  1 55  ? 14.342  -53.958 23.360 1.00 64.01  ? 46  SER A N   1 
ATOM   407   C  CA  . SER A  1 55  ? 13.285  -53.817 22.363 1.00 64.17  ? 46  SER A CA  1 
ATOM   408   C  C   . SER A  1 55  ? 13.232  -52.451 21.642 1.00 64.88  ? 46  SER A C   1 
ATOM   409   O  O   . SER A  1 55  ? 12.959  -52.410 20.443 1.00 57.07  ? 46  SER A O   1 
ATOM   410   C  CB  . SER A  1 55  ? 11.921  -54.177 22.963 1.00 64.01  ? 46  SER A CB  1 
ATOM   411   O  OG  . SER A  1 55  ? 11.472  -53.186 23.857 1.00 72.45  ? 46  SER A OG  1 
ATOM   412   N  N   . THR A  1 56  ? 13.437  -51.343 22.366 1.00 66.60  ? 47  THR A N   1 
ATOM   413   C  CA  . THR A  1 56  ? 13.547  -50.011 21.732 1.00 64.77  ? 47  THR A CA  1 
ATOM   414   C  C   . THR A  1 56  ? 14.976  -49.470 21.503 1.00 60.78  ? 47  THR A C   1 
ATOM   415   O  O   . THR A  1 56  ? 15.148  -48.404 20.922 1.00 53.80  ? 47  THR A O   1 
ATOM   416   C  CB  . THR A  1 56  ? 12.714  -48.941 22.475 1.00 58.67  ? 47  THR A CB  1 
ATOM   417   O  OG1 . THR A  1 56  ? 13.148  -48.868 23.837 1.00 69.33  ? 47  THR A OG1 1 
ATOM   418   C  CG2 . THR A  1 56  ? 11.236  -49.278 22.449 1.00 47.00  ? 47  THR A CG2 1 
ATOM   419   N  N   . ASN A  1 57  ? 15.991  -50.202 21.948 1.00 63.54  ? 48  ASN A N   1 
ATOM   420   C  CA  . ASN A  1 57  ? 17.377  -49.713 21.913 1.00 66.92  ? 48  ASN A CA  1 
ATOM   421   C  C   . ASN A  1 57  ? 17.600  -48.392 22.648 1.00 74.89  ? 48  ASN A C   1 
ATOM   422   O  O   . ASN A  1 57  ? 18.343  -47.520 22.186 1.00 72.94  ? 48  ASN A O   1 
ATOM   423   C  CB  . ASN A  1 57  ? 17.894  -49.606 20.482 1.00 67.58  ? 48  ASN A CB  1 
ATOM   424   C  CG  . ASN A  1 57  ? 18.549  -50.888 20.010 1.00 73.77  ? 48  ASN A CG  1 
ATOM   425   O  OD1 . ASN A  1 57  ? 18.425  -51.935 20.649 1.00 69.25  ? 48  ASN A OD1 1 
ATOM   426   N  ND2 . ASN A  1 57  ? 19.249  -50.814 18.888 1.00 70.60  ? 48  ASN A ND2 1 
ATOM   427   N  N   . GLU A  1 58  ? 16.962  -48.262 23.809 1.00 73.41  ? 49  GLU A N   1 
ATOM   428   C  CA  . GLU A  1 58  ? 17.022  -47.042 24.596 1.00 66.18  ? 49  GLU A CA  1 
ATOM   429   C  C   . GLU A  1 58  ? 17.707  -47.341 25.918 1.00 62.18  ? 49  GLU A C   1 
ATOM   430   O  O   . GLU A  1 58  ? 17.416  -48.342 26.546 1.00 65.33  ? 49  GLU A O   1 
ATOM   431   C  CB  . GLU A  1 58  ? 15.604  -46.545 24.885 1.00 64.09  ? 49  GLU A CB  1 
ATOM   432   C  CG  . GLU A  1 58  ? 14.894  -45.827 23.757 1.00 58.19  ? 49  GLU A CG  1 
ATOM   433   C  CD  . GLU A  1 58  ? 13.486  -45.395 24.150 1.00 62.69  ? 49  GLU A CD  1 
ATOM   434   O  OE1 . GLU A  1 58  ? 12.708  -46.225 24.673 1.00 58.04  ? 49  GLU A OE1 1 
ATOM   435   O  OE2 . GLU A  1 58  ? 13.159  -44.211 23.951 1.00 64.17  ? 49  GLU A OE2 1 
ATOM   436   N  N   . VAL A  1 59  ? 18.594  -46.470 26.371 1.00 63.96  ? 50  VAL A N   1 
ATOM   437   C  CA  . VAL A  1 59  ? 19.101  -46.628 27.737 1.00 71.43  ? 50  VAL A CA  1 
ATOM   438   C  C   . VAL A  1 59  ? 18.794  -45.431 28.661 1.00 62.98  ? 50  VAL A C   1 
ATOM   439   O  O   . VAL A  1 59  ? 18.881  -44.274 28.252 1.00 59.31  ? 50  VAL A O   1 
ATOM   440   C  CB  . VAL A  1 59  ? 20.595  -47.013 27.750 1.00 63.86  ? 50  VAL A CB  1 
ATOM   441   C  CG1 . VAL A  1 59  ? 21.198  -46.750 29.090 1.00 58.18  ? 50  VAL A CG1 1 
ATOM   442   C  CG2 . VAL A  1 59  ? 20.742  -48.472 27.397 1.00 71.56  ? 50  VAL A CG2 1 
ATOM   443   N  N   . ASP A  1 60  ? 18.399  -45.736 29.894 1.00 56.34  ? 51  ASP A N   1 
ATOM   444   C  CA  . ASP A  1 60  ? 18.091  -44.723 30.899 1.00 56.77  ? 51  ASP A CA  1 
ATOM   445   C  C   . ASP A  1 60  ? 19.246  -44.560 31.878 1.00 56.44  ? 51  ASP A C   1 
ATOM   446   O  O   . ASP A  1 60  ? 19.698  -45.523 32.480 1.00 51.62  ? 51  ASP A O   1 
ATOM   447   C  CB  . ASP A  1 60  ? 16.829  -45.095 31.670 1.00 54.20  ? 51  ASP A CB  1 
ATOM   448   C  CG  . ASP A  1 60  ? 15.599  -45.148 30.788 1.00 67.28  ? 51  ASP A CG  1 
ATOM   449   O  OD1 . ASP A  1 60  ? 15.724  -45.081 29.539 1.00 66.31  ? 51  ASP A OD1 1 
ATOM   450   O  OD2 . ASP A  1 60  ? 14.495  -45.285 31.353 1.00 70.57  ? 51  ASP A OD2 1 
ATOM   451   N  N   . LEU A  1 61  ? 19.708  -43.324 32.033 1.00 52.66  ? 52  LEU A N   1 
ATOM   452   C  CA  . LEU A  1 61  ? 20.842  -43.004 32.886 1.00 51.76  ? 52  LEU A CA  1 
ATOM   453   C  C   . LEU A  1 61  ? 20.431  -41.997 33.930 1.00 55.24  ? 52  LEU A C   1 
ATOM   454   O  O   . LEU A  1 61  ? 19.654  -41.079 33.641 1.00 52.25  ? 52  LEU A O   1 
ATOM   455   C  CB  . LEU A  1 61  ? 21.924  -42.336 32.063 1.00 54.24  ? 52  LEU A CB  1 
ATOM   456   C  CG  . LEU A  1 61  ? 23.364  -42.553 32.478 1.00 60.81  ? 52  LEU A CG  1 
ATOM   457   C  CD1 . LEU A  1 61  ? 23.799  -43.852 31.827 1.00 67.52  ? 52  LEU A CD1 1 
ATOM   458   C  CD2 . LEU A  1 61  ? 24.228  -41.388 31.999 1.00 54.01  ? 52  LEU A CD2 1 
ATOM   459   N  N   . VAL A  1 62  ? 20.954  -42.157 35.142 1.00 51.02  ? 53  VAL A N   1 
ATOM   460   C  CA  . VAL A  1 62  ? 20.938  -41.065 36.113 1.00 47.74  ? 53  VAL A CA  1 
ATOM   461   C  C   . VAL A  1 62  ? 22.368  -40.586 36.362 1.00 48.16  ? 53  VAL A C   1 
ATOM   462   O  O   . VAL A  1 62  ? 23.261  -41.369 36.659 1.00 49.13  ? 53  VAL A O   1 
ATOM   463   C  CB  . VAL A  1 62  ? 20.255  -41.427 37.441 1.00 43.34  ? 53  VAL A CB  1 
ATOM   464   C  CG1 . VAL A  1 62  ? 20.025  -40.182 38.220 1.00 45.96  ? 53  VAL A CG1 1 
ATOM   465   C  CG2 . VAL A  1 62  ? 18.925  -42.113 37.208 1.00 40.55  ? 53  VAL A CG2 1 
ATOM   466   N  N   . TYR A  1 63  ? 22.589  -39.291 36.221 1.00 48.58  ? 54  TYR A N   1 
ATOM   467   C  CA  . TYR A  1 63  ? 23.939  -38.760 36.332 1.00 53.06  ? 54  TYR A CA  1 
ATOM   468   C  C   . TYR A  1 63  ? 23.916  -37.302 36.782 1.00 49.24  ? 54  TYR A C   1 
ATOM   469   O  O   . TYR A  1 63  ? 22.875  -36.655 36.751 1.00 48.11  ? 54  TYR A O   1 
ATOM   470   C  CB  . TYR A  1 63  ? 24.658  -38.894 34.986 1.00 55.90  ? 54  TYR A CB  1 
ATOM   471   C  CG  . TYR A  1 63  ? 24.011  -38.066 33.897 1.00 56.67  ? 54  TYR A CG  1 
ATOM   472   C  CD1 . TYR A  1 63  ? 24.417  -36.757 33.659 1.00 55.33  ? 54  TYR A CD1 1 
ATOM   473   C  CD2 . TYR A  1 63  ? 22.972  -38.580 33.135 1.00 56.47  ? 54  TYR A CD2 1 
ATOM   474   C  CE1 . TYR A  1 63  ? 23.820  -35.999 32.701 1.00 55.56  ? 54  TYR A CE1 1 
ATOM   475   C  CE2 . TYR A  1 63  ? 22.365  -37.820 32.167 1.00 55.75  ? 54  TYR A CE2 1 
ATOM   476   C  CZ  . TYR A  1 63  ? 22.795  -36.533 31.954 1.00 57.97  ? 54  TYR A CZ  1 
ATOM   477   O  OH  . TYR A  1 63  ? 22.197  -35.779 30.982 1.00 62.99  ? 54  TYR A OH  1 
ATOM   478   N  N   . TRP A  1 64  ? 25.062  -36.801 37.223 1.00 53.25  ? 55  TRP A N   1 
ATOM   479   C  CA  . TRP A  1 64  ? 25.217  -35.379 37.518 1.00 58.77  ? 55  TRP A CA  1 
ATOM   480   C  C   . TRP A  1 64  ? 26.088  -34.749 36.461 1.00 56.24  ? 55  TRP A C   1 
ATOM   481   O  O   . TRP A  1 64  ? 27.159  -35.254 36.147 1.00 53.81  ? 55  TRP A O   1 
ATOM   482   C  CB  . TRP A  1 64  ? 25.932  -35.158 38.845 1.00 64.93  ? 55  TRP A CB  1 
ATOM   483   C  CG  . TRP A  1 64  ? 25.239  -35.661 40.057 1.00 69.32  ? 55  TRP A CG  1 
ATOM   484   C  CD1 . TRP A  1 64  ? 23.888  -35.746 40.275 1.00 70.58  ? 55  TRP A CD1 1 
ATOM   485   C  CD2 . TRP A  1 64  ? 25.868  -36.146 41.236 1.00 65.98  ? 55  TRP A CD2 1 
ATOM   486   N  NE1 . TRP A  1 64  ? 23.646  -36.257 41.531 1.00 67.37  ? 55  TRP A NE1 1 
ATOM   487   C  CE2 . TRP A  1 64  ? 24.849  -36.509 42.141 1.00 67.89  ? 55  TRP A CE2 1 
ATOM   488   C  CE3 . TRP A  1 64  ? 27.200  -36.305 41.621 1.00 72.94  ? 55  TRP A CE3 1 
ATOM   489   C  CZ2 . TRP A  1 64  ? 25.118  -37.024 43.396 1.00 73.23  ? 55  TRP A CZ2 1 
ATOM   490   C  CZ3 . TRP A  1 64  ? 27.466  -36.821 42.864 1.00 81.38  ? 55  TRP A CZ3 1 
ATOM   491   C  CH2 . TRP A  1 64  ? 26.431  -37.177 43.739 1.00 80.82  ? 55  TRP A CH2 1 
ATOM   492   N  N   . GLU A  1 65  ? 25.654  -33.617 35.940 1.00 54.99  ? 56  GLU A N   1 
ATOM   493   C  CA  . GLU A  1 65  ? 26.439  -32.945 34.939 1.00 55.74  ? 56  GLU A CA  1 
ATOM   494   C  C   . GLU A  1 65  ? 26.976  -31.641 35.477 1.00 56.01  ? 56  GLU A C   1 
ATOM   495   O  O   . GLU A  1 65  ? 26.211  -30.711 35.689 1.00 56.66  ? 56  GLU A O   1 
ATOM   496   C  CB  . GLU A  1 65  ? 25.578  -32.675 33.720 1.00 60.53  ? 56  GLU A CB  1 
ATOM   497   C  CG  . GLU A  1 65  ? 26.248  -31.830 32.677 1.00 63.42  ? 56  GLU A CG  1 
ATOM   498   C  CD  . GLU A  1 65  ? 25.438  -31.771 31.420 1.00 64.12  ? 56  GLU A CD  1 
ATOM   499   O  OE1 . GLU A  1 65  ? 24.424  -32.501 31.331 1.00 64.50  ? 56  GLU A OE1 1 
ATOM   500   O  OE2 . GLU A  1 65  ? 25.814  -30.997 30.522 1.00 67.25  ? 56  GLU A OE2 1 
ATOM   501   N  N   . GLN A  1 66  ? 28.289  -31.574 35.688 1.00 57.36  ? 57  GLN A N   1 
ATOM   502   C  CA  . GLN A  1 66  ? 28.926  -30.324 36.067 1.00 60.66  ? 57  GLN A CA  1 
ATOM   503   C  C   . GLN A  1 66  ? 29.191  -29.412 34.854 1.00 64.37  ? 57  GLN A C   1 
ATOM   504   O  O   . GLN A  1 66  ? 29.892  -29.784 33.907 1.00 60.19  ? 57  GLN A O   1 
ATOM   505   C  CB  . GLN A  1 66  ? 30.212  -30.579 36.850 1.00 63.66  ? 57  GLN A CB  1 
ATOM   506   C  CG  . GLN A  1 66  ? 30.666  -29.352 37.654 1.00 69.42  ? 57  GLN A CG  1 
ATOM   507   C  CD  . GLN A  1 66  ? 31.948  -29.568 38.469 1.00 77.15  ? 57  GLN A CD  1 
ATOM   508   O  OE1 . GLN A  1 66  ? 32.425  -30.695 38.649 1.00 89.51  ? 57  GLN A OE1 1 
ATOM   509   N  NE2 . GLN A  1 66  ? 32.509  -28.473 38.962 1.00 69.03  ? 57  GLN A NE2 1 
ATOM   510   N  N   . GLN A  1 67  ? 28.606  -28.218 34.895 1.00 60.21  ? 58  GLN A N   1 
ATOM   511   C  CA  . GLN A  1 67  ? 28.850  -27.179 33.909 1.00 53.99  ? 58  GLN A CA  1 
ATOM   512   C  C   . GLN A  1 67  ? 29.449  -26.008 34.665 1.00 57.67  ? 58  GLN A C   1 
ATOM   513   O  O   . GLN A  1 67  ? 28.928  -25.629 35.707 1.00 57.82  ? 58  GLN A O   1 
ATOM   514   C  CB  . GLN A  1 67  ? 27.533  -26.731 33.291 1.00 49.42  ? 58  GLN A CB  1 
ATOM   515   C  CG  . GLN A  1 67  ? 26.578  -27.857 32.984 1.00 57.31  ? 58  GLN A CG  1 
ATOM   516   C  CD  . GLN A  1 67  ? 25.399  -27.411 32.129 1.00 67.48  ? 58  GLN A CD  1 
ATOM   517   O  OE1 . GLN A  1 67  ? 25.178  -26.213 31.925 1.00 69.43  ? 58  GLN A OE1 1 
ATOM   518   N  NE2 . GLN A  1 67  ? 24.636  -28.379 31.617 1.00 61.39  ? 58  GLN A NE2 1 
ATOM   519   N  N   . SER A  1 68  ? 30.551  -25.444 34.186 1.00 57.17  ? 59  SER A N   1 
ATOM   520   C  CA  . SER A  1 68  ? 31.058  -24.208 34.800 1.00 64.81  ? 59  SER A CA  1 
ATOM   521   C  C   . SER A  1 68  ? 31.676  -23.217 33.800 1.00 62.57  ? 59  SER A C   1 
ATOM   522   O  O   . SER A  1 68  ? 32.205  -23.615 32.763 1.00 62.38  ? 59  SER A O   1 
ATOM   523   C  CB  . SER A  1 68  ? 31.982  -24.484 36.008 1.00 62.46  ? 59  SER A CB  1 
ATOM   524   O  OG  . SER A  1 68  ? 32.827  -25.593 35.797 1.00 62.82  ? 59  SER A OG  1 
ATOM   525   N  N   . TRP A  1 69  ? 31.565  -21.926 34.099 1.00 56.55  ? 60  TRP A N   1 
ATOM   526   C  CA  . TRP A  1 69  ? 32.010  -20.892 33.165 1.00 62.04  ? 60  TRP A CA  1 
ATOM   527   C  C   . TRP A  1 69  ? 32.285  -19.568 33.855 1.00 60.04  ? 60  TRP A C   1 
ATOM   528   O  O   . TRP A  1 69  ? 31.851  -19.366 34.981 1.00 62.85  ? 60  TRP A O   1 
ATOM   529   C  CB  . TRP A  1 69  ? 30.969  -20.690 32.075 1.00 60.46  ? 60  TRP A CB  1 
ATOM   530   C  CG  . TRP A  1 69  ? 29.659  -20.203 32.592 1.00 59.42  ? 60  TRP A CG  1 
ATOM   531   C  CD1 . TRP A  1 69  ? 29.249  -18.911 32.683 1.00 54.62  ? 60  TRP A CD1 1 
ATOM   532   C  CD2 . TRP A  1 69  ? 28.576  -21.007 33.085 1.00 58.40  ? 60  TRP A CD2 1 
ATOM   533   N  NE1 . TRP A  1 69  ? 27.980  -18.856 33.200 1.00 57.39  ? 60  TRP A NE1 1 
ATOM   534   C  CE2 . TRP A  1 69  ? 27.545  -20.129 33.454 1.00 52.21  ? 60  TRP A CE2 1 
ATOM   535   C  CE3 . TRP A  1 69  ? 28.383  -22.384 33.248 1.00 56.79  ? 60  TRP A CE3 1 
ATOM   536   C  CZ2 . TRP A  1 69  ? 26.335  -20.578 33.969 1.00 54.52  ? 60  TRP A CZ2 1 
ATOM   537   C  CZ3 . TRP A  1 69  ? 27.184  -22.828 33.767 1.00 53.38  ? 60  TRP A CZ3 1 
ATOM   538   C  CH2 . TRP A  1 69  ? 26.174  -21.929 34.115 1.00 53.42  ? 60  TRP A CH2 1 
ATOM   539   N  N   . LYS A  1 70  ? 33.007  -18.670 33.187 1.00 64.39  ? 61  LYS A N   1 
ATOM   540   C  CA  . LYS A  1 70  ? 33.283  -17.342 33.758 1.00 70.96  ? 61  LYS A CA  1 
ATOM   541   C  C   . LYS A  1 70  ? 32.570  -16.223 32.986 1.00 69.14  ? 61  LYS A C   1 
ATOM   542   O  O   . LYS A  1 70  ? 32.536  -16.221 31.752 1.00 73.84  ? 61  LYS A O   1 
ATOM   543   C  CB  . LYS A  1 70  ? 34.797  -17.072 33.829 1.00 69.89  ? 61  LYS A CB  1 
ATOM   544   C  CG  . LYS A  1 70  ? 35.199  -15.810 34.580 1.00 77.57  ? 61  LYS A CG  1 
ATOM   545   C  CD  . LYS A  1 70  ? 36.518  -15.254 34.056 1.00 90.57  ? 61  LYS A CD  1 
ATOM   546   C  CE  . LYS A  1 70  ? 36.865  -13.911 34.684 1.00 94.81  ? 61  LYS A CE  1 
ATOM   547   N  NZ  . LYS A  1 70  ? 37.480  -14.054 36.032 1.00 78.64  ? 61  LYS A NZ  1 
ATOM   548   N  N   . LEU A  1 71  ? 31.983  -15.286 33.720 1.00 61.80  ? 62  LEU A N   1 
ATOM   549   C  CA  . LEU A  1 71  ? 31.370  -14.113 33.115 1.00 65.82  ? 62  LEU A CA  1 
ATOM   550   C  C   . LEU A  1 71  ? 31.899  -12.880 33.816 1.00 68.60  ? 62  LEU A C   1 
ATOM   551   O  O   . LEU A  1 71  ? 31.884  -12.807 35.036 1.00 68.62  ? 62  LEU A O   1 
ATOM   552   C  CB  . LEU A  1 71  ? 29.845  -14.150 33.239 1.00 65.56  ? 62  LEU A CB  1 
ATOM   553   C  CG  . LEU A  1 71  ? 29.038  -15.027 32.286 1.00 65.32  ? 62  LEU A CG  1 
ATOM   554   C  CD1 . LEU A  1 71  ? 27.556  -14.718 32.429 1.00 60.19  ? 62  LEU A CD1 1 
ATOM   555   C  CD2 . LEU A  1 71  ? 29.502  -14.819 30.855 1.00 65.44  ? 62  LEU A CD2 1 
ATOM   556   N  N   . ASN A  1 72  ? 32.371  -11.907 33.051 1.00 74.07  ? 63  ASN A N   1 
ATOM   557   C  CA  . ASN A  1 72  ? 32.882  -10.691 33.655 1.00 69.24  ? 63  ASN A CA  1 
ATOM   558   C  C   . ASN A  1 72  ? 31.756  -9.873  34.268 1.00 59.99  ? 63  ASN A C   1 
ATOM   559   O  O   . ASN A  1 72  ? 31.989  -9.101  35.187 1.00 61.77  ? 63  ASN A O   1 
ATOM   560   C  CB  . ASN A  1 72  ? 33.686  -9.865  32.639 1.00 78.08  ? 63  ASN A CB  1 
ATOM   561   C  CG  . ASN A  1 72  ? 34.977  -10.559 32.203 1.00 82.02  ? 63  ASN A CG  1 
ATOM   562   O  OD1 . ASN A  1 72  ? 35.546  -11.367 32.939 1.00 84.39  ? 63  ASN A OD1 1 
ATOM   563   N  ND2 . ASN A  1 72  ? 35.439  -10.245 31.000 1.00 78.89  ? 63  ASN A ND2 1 
ATOM   564   N  N   . SER A  1 73  ? 30.535  -10.046 33.768 1.00 61.73  ? 64  SER A N   1 
ATOM   565   C  CA  . SER A  1 73  ? 29.418  -9.237  34.259 1.00 62.95  ? 64  SER A CA  1 
ATOM   566   C  C   . SER A  1 73  ? 28.974  -9.701  35.634 1.00 64.90  ? 64  SER A C   1 
ATOM   567   O  O   . SER A  1 73  ? 28.190  -9.029  36.303 1.00 64.73  ? 64  SER A O   1 
ATOM   568   C  CB  . SER A  1 73  ? 28.239  -9.194  33.273 1.00 54.79  ? 64  SER A CB  1 
ATOM   569   O  OG  . SER A  1 73  ? 27.740  -10.482 32.967 1.00 64.93  ? 64  SER A OG  1 
ATOM   570   N  N   . LEU A  1 74  ? 29.486  -10.860 36.037 1.00 62.31  ? 65  LEU A N   1 
ATOM   571   C  CA  . LEU A  1 74  ? 29.238  -11.440 37.361 1.00 65.80  ? 65  LEU A CA  1 
ATOM   572   C  C   . LEU A  1 74  ? 30.302  -11.161 38.436 1.00 65.77  ? 65  LEU A C   1 
ATOM   573   O  O   . LEU A  1 74  ? 30.249  -11.759 39.508 1.00 64.20  ? 65  LEU A O   1 
ATOM   574   C  CB  . LEU A  1 74  ? 29.031  -12.949 37.253 1.00 64.04  ? 65  LEU A CB  1 
ATOM   575   C  CG  . LEU A  1 74  ? 27.713  -13.440 36.678 1.00 54.62  ? 65  LEU A CG  1 
ATOM   576   C  CD1 . LEU A  1 74  ? 27.731  -14.948 36.697 1.00 52.58  ? 65  LEU A CD1 1 
ATOM   577   C  CD2 . LEU A  1 74  ? 26.553  -12.900 37.475 1.00 45.42  ? 65  LEU A CD2 1 
ATOM   578   N  N   . MET A  1 75  ? 31.303  -10.335 38.129 1.00 68.03  ? 66  MET A N   1 
ATOM   579   C  CA  . MET A  1 75  ? 32.377  -10.039 39.083 1.00 65.88  ? 66  MET A CA  1 
ATOM   580   C  C   . MET A  1 75  ? 31.995  -9.014  40.147 1.00 64.37  ? 66  MET A C   1 
ATOM   581   O  O   . MET A  1 75  ? 31.123  -8.182  39.925 1.00 67.34  ? 66  MET A O   1 
ATOM   582   C  CB  . MET A  1 75  ? 33.629  -9.573  38.356 1.00 61.24  ? 66  MET A CB  1 
ATOM   583   C  CG  . MET A  1 75  ? 34.309  -10.668 37.586 1.00 68.33  ? 66  MET A CG  1 
ATOM   584   S  SD  . MET A  1 75  ? 35.792  -10.079 36.763 1.00 84.29  ? 66  MET A SD  1 
ATOM   585   C  CE  . MET A  1 75  ? 37.042  -10.924 37.739 1.00 72.11  ? 66  MET A CE  1 
ATOM   586   N  N   . TRP A  1 76  ? 32.627  -9.114  41.314 1.00 57.25  ? 67  TRP A N   1 
ATOM   587   C  CA  . TRP A  1 76  ? 32.517  -8.092  42.351 1.00 63.11  ? 67  TRP A CA  1 
ATOM   588   C  C   . TRP A  1 76  ? 33.708  -8.142  43.331 1.00 72.79  ? 67  TRP A C   1 
ATOM   589   O  O   . TRP A  1 76  ? 34.401  -9.153  43.446 1.00 68.49  ? 67  TRP A O   1 
ATOM   590   C  CB  . TRP A  1 76  ? 31.172  -8.186  43.098 1.00 67.25  ? 67  TRP A CB  1 
ATOM   591   C  CG  . TRP A  1 76  ? 31.078  -9.330  44.082 1.00 64.74  ? 67  TRP A CG  1 
ATOM   592   C  CD1 . TRP A  1 76  ? 31.459  -9.314  45.387 1.00 63.14  ? 67  TRP A CD1 1 
ATOM   593   C  CD2 . TRP A  1 76  ? 30.574  -10.654 43.827 1.00 66.21  ? 67  TRP A CD2 1 
ATOM   594   N  NE1 . TRP A  1 76  ? 31.225  -10.533 45.964 1.00 64.80  ? 67  TRP A NE1 1 
ATOM   595   C  CE2 . TRP A  1 76  ? 30.685  -11.374 45.032 1.00 64.51  ? 67  TRP A CE2 1 
ATOM   596   C  CE3 . TRP A  1 76  ? 30.045  -11.296 42.699 1.00 61.83  ? 67  TRP A CE3 1 
ATOM   597   C  CZ2 . TRP A  1 76  ? 30.281  -12.714 45.141 1.00 64.83  ? 67  TRP A CZ2 1 
ATOM   598   C  CZ3 . TRP A  1 76  ? 29.646  -12.625 42.813 1.00 61.54  ? 67  TRP A CZ3 1 
ATOM   599   C  CH2 . TRP A  1 76  ? 29.767  -13.318 44.025 1.00 61.02  ? 67  TRP A CH2 1 
ATOM   600   N  N   . ASP A  1 77  ? 33.935  -7.031  44.027 1.00 77.36  ? 68  ASP A N   1 
ATOM   601   C  CA  . ASP A  1 77  ? 34.981  -6.924  45.032 1.00 69.17  ? 68  ASP A CA  1 
ATOM   602   C  C   . ASP A  1 77  ? 34.324  -7.071  46.400 1.00 74.84  ? 68  ASP A C   1 
ATOM   603   O  O   . ASP A  1 77  ? 33.581  -6.189  46.845 1.00 72.56  ? 68  ASP A O   1 
ATOM   604   C  CB  . ASP A  1 77  ? 35.721  -5.583  44.885 1.00 67.36  ? 68  ASP A CB  1 
ATOM   605   C  CG  . ASP A  1 77  ? 36.497  -5.180  46.135 1.00 84.47  ? 68  ASP A CG  1 
ATOM   606   O  OD1 . ASP A  1 77  ? 37.077  -6.056  46.821 1.00 82.11  ? 68  ASP A OD1 1 
ATOM   607   O  OD2 . ASP A  1 77  ? 36.530  -3.963  46.426 1.00 89.70  ? 68  ASP A OD2 1 
ATOM   608   N  N   . PRO A  1 78  ? 34.601  -8.200  47.066 1.00 74.79  ? 69  PRO A N   1 
ATOM   609   C  CA  . PRO A  1 78  ? 34.033  -8.605  48.354 1.00 75.80  ? 69  PRO A CA  1 
ATOM   610   C  C   . PRO A  1 78  ? 34.047  -7.493  49.405 1.00 79.38  ? 69  PRO A C   1 
ATOM   611   O  O   . PRO A  1 78  ? 33.140  -7.447  50.235 1.00 77.90  ? 69  PRO A O   1 
ATOM   612   C  CB  . PRO A  1 78  ? 34.972  -9.724  48.800 1.00 74.78  ? 69  PRO A CB  1 
ATOM   613   C  CG  . PRO A  1 78  ? 35.518  -10.301 47.535 1.00 67.65  ? 69  PRO A CG  1 
ATOM   614   C  CD  . PRO A  1 78  ? 35.422  -9.263  46.460 1.00 71.85  ? 69  PRO A CD  1 
ATOM   615   N  N   . ASN A  1 79  ? 35.049  -6.616  49.379 1.00 86.02  ? 70  ASN A N   1 
ATOM   616   C  CA  . ASN A  1 79  ? 35.138  -5.544  50.377 1.00 88.29  ? 70  ASN A CA  1 
ATOM   617   C  C   . ASN A  1 79  ? 33.968  -4.578  50.310 1.00 83.62  ? 70  ASN A C   1 
ATOM   618   O  O   . ASN A  1 79  ? 33.520  -4.084  51.347 1.00 79.28  ? 70  ASN A O   1 
ATOM   619   C  CB  . ASN A  1 79  ? 36.458  -4.772  50.268 1.00 84.90  ? 70  ASN A CB  1 
ATOM   620   C  CG  . ASN A  1 79  ? 37.666  -5.656  50.480 1.00 93.03  ? 70  ASN A CG  1 
ATOM   621   O  OD1 . ASN A  1 79  ? 37.812  -6.296  51.526 1.00 89.12  ? 70  ASN A OD1 1 
ATOM   622   N  ND2 . ASN A  1 79  ? 38.530  -5.722  49.470 1.00 94.99  ? 70  ASN A ND2 1 
ATOM   623   N  N   . GLU A  1 80  ? 33.478  -4.314  49.103 1.00 78.47  ? 71  GLU A N   1 
ATOM   624   C  CA  . GLU A  1 80  ? 32.390  -3.363  48.909 1.00 78.50  ? 71  GLU A CA  1 
ATOM   625   C  C   . GLU A  1 80  ? 31.065  -3.932  49.404 1.00 76.90  ? 71  GLU A C   1 
ATOM   626   O  O   . GLU A  1 80  ? 30.045  -3.243  49.405 1.00 70.95  ? 71  GLU A O   1 
ATOM   627   C  CB  . GLU A  1 80  ? 32.277  -2.973  47.435 1.00 72.61  ? 71  GLU A CB  1 
ATOM   628   C  CG  . GLU A  1 80  ? 31.167  -1.978  47.140 0.00 80.04  ? 71  GLU A CG  1 
ATOM   629   C  CD  . GLU A  1 80  ? 31.295  -1.353  45.765 0.00 86.49  ? 71  GLU A CD  1 
ATOM   630   O  OE1 . GLU A  1 80  ? 32.303  -1.623  45.079 0.00 89.08  ? 71  GLU A OE1 1 
ATOM   631   O  OE2 . GLU A  1 80  ? 30.388  -0.591  45.370 0.00 88.08  ? 71  GLU A OE2 1 
ATOM   632   N  N   . TYR A  1 81  ? 31.087  -5.193  49.823 1.00 78.10  ? 72  TYR A N   1 
ATOM   633   C  CA  . TYR A  1 81  ? 29.875  -6.002  49.879 1.00 72.57  ? 72  TYR A CA  1 
ATOM   634   C  C   . TYR A  1 81  ? 29.895  -6.947  51.075 1.00 73.44  ? 72  TYR A C   1 
ATOM   635   O  O   . TYR A  1 81  ? 29.164  -7.937  51.109 1.00 71.07  ? 72  TYR A O   1 
ATOM   636   C  CB  . TYR A  1 81  ? 29.703  -6.798  48.583 1.00 66.35  ? 72  TYR A CB  1 
ATOM   637   C  CG  . TYR A  1 81  ? 29.023  -6.024  47.476 1.00 66.66  ? 72  TYR A CG  1 
ATOM   638   C  CD1 . TYR A  1 81  ? 27.691  -5.648  47.583 1.00 63.22  ? 72  TYR A CD1 1 
ATOM   639   C  CD2 . TYR A  1 81  ? 29.713  -5.670  46.325 1.00 65.33  ? 72  TYR A CD2 1 
ATOM   640   C  CE1 . TYR A  1 81  ? 27.065  -4.941  46.574 1.00 62.56  ? 72  TYR A CE1 1 
ATOM   641   C  CE2 . TYR A  1 81  ? 29.095  -4.963  45.311 1.00 65.70  ? 72  TYR A CE2 1 
ATOM   642   C  CZ  . TYR A  1 81  ? 27.771  -4.602  45.441 1.00 70.22  ? 72  TYR A CZ  1 
ATOM   643   O  OH  . TYR A  1 81  ? 27.152  -3.898  44.434 1.00 65.07  ? 72  TYR A OH  1 
ATOM   644   N  N   . GLY A  1 82  ? 30.735  -6.634  52.056 1.00 75.90  ? 73  GLY A N   1 
ATOM   645   C  CA  . GLY A  1 82  ? 30.723  -7.340  53.324 1.00 68.98  ? 73  GLY A CA  1 
ATOM   646   C  C   . GLY A  1 82  ? 31.546  -8.612  53.286 1.00 70.60  ? 73  GLY A C   1 
ATOM   647   O  O   . GLY A  1 82  ? 31.289  -9.552  54.037 1.00 64.23  ? 73  GLY A O   1 
ATOM   648   N  N   . ASN A  1 83  ? 32.541  -8.640  52.405 1.00 80.27  ? 74  ASN A N   1 
ATOM   649   C  CA  . ASN A  1 83  ? 33.400  -9.808  52.257 1.00 83.53  ? 74  ASN A CA  1 
ATOM   650   C  C   . ASN A  1 83  ? 32.609  -11.065 51.912 1.00 76.94  ? 74  ASN A C   1 
ATOM   651   O  O   . ASN A  1 83  ? 32.958  -12.166 52.337 1.00 77.61  ? 74  ASN A O   1 
ATOM   652   C  CB  . ASN A  1 83  ? 34.219  -10.036 53.529 1.00 88.10  ? 74  ASN A CB  1 
ATOM   653   C  CG  . ASN A  1 83  ? 35.372  -9.060  53.663 1.00 95.35  ? 74  ASN A CG  1 
ATOM   654   O  OD1 . ASN A  1 83  ? 35.963  -8.640  52.668 1.00 96.78  ? 74  ASN A OD1 1 
ATOM   655   N  ND2 . ASN A  1 83  ? 35.698  -8.695  54.897 1.00 90.39  ? 74  ASN A ND2 1 
ATOM   656   N  N   . ILE A  1 84  ? 31.542  -10.893 51.138 1.00 74.68  ? 75  ILE A N   1 
ATOM   657   C  CA  . ILE A  1 84  ? 30.834  -12.018 50.557 1.00 75.46  ? 75  ILE A CA  1 
ATOM   658   C  C   . ILE A  1 84  ? 31.663  -12.443 49.355 1.00 70.82  ? 75  ILE A C   1 
ATOM   659   O  O   . ILE A  1 84  ? 31.852  -11.670 48.418 1.00 66.71  ? 75  ILE A O   1 
ATOM   660   C  CB  . ILE A  1 84  ? 29.433  -11.591 50.062 1.00 69.30  ? 75  ILE A CB  1 
ATOM   661   C  CG1 . ILE A  1 84  ? 28.527  -11.234 51.239 1.00 55.05  ? 75  ILE A CG1 1 
ATOM   662   C  CG2 . ILE A  1 84  ? 28.805  -12.677 49.199 1.00 61.96  ? 75  ILE A CG2 1 
ATOM   663   C  CD1 . ILE A  1 84  ? 27.149  -10.837 50.826 1.00 57.40  ? 75  ILE A CD1 1 
ATOM   664   N  N   . THR A  1 85  ? 32.212  -13.654 49.417 1.00 73.55  ? 76  THR A N   1 
ATOM   665   C  CA  . THR A  1 85  ? 32.971  -14.193 48.298 1.00 70.04  ? 76  THR A CA  1 
ATOM   666   C  C   . THR A  1 85  ? 32.179  -15.090 47.350 1.00 67.02  ? 76  THR A C   1 
ATOM   667   O  O   . THR A  1 85  ? 32.655  -15.384 46.268 1.00 71.67  ? 76  THR A O   1 
ATOM   668   C  CB  . THR A  1 85  ? 34.205  -14.973 48.804 1.00 77.82  ? 76  THR A CB  1 
ATOM   669   O  OG1 . THR A  1 85  ? 33.817  -15.822 49.891 1.00 73.49  ? 76  THR A OG1 1 
ATOM   670   C  CG2 . THR A  1 85  ? 35.276  -14.015 49.300 1.00 78.34  ? 76  THR A CG2 1 
ATOM   671   N  N   . ASP A  1 86  ? 30.988  -15.531 47.747 1.00 64.83  ? 77  ASP A N   1 
ATOM   672   C  CA  . ASP A  1 86  ? 30.117  -16.281 46.841 1.00 58.36  ? 77  ASP A CA  1 
ATOM   673   C  C   . ASP A  1 86  ? 28.673  -16.333 47.298 1.00 57.12  ? 77  ASP A C   1 
ATOM   674   O  O   . ASP A  1 86  ? 28.389  -16.076 48.464 1.00 56.76  ? 77  ASP A O   1 
ATOM   675   C  CB  . ASP A  1 86  ? 30.649  -17.679 46.574 1.00 59.28  ? 77  ASP A CB  1 
ATOM   676   C  CG  . ASP A  1 86  ? 30.759  -18.507 47.814 1.00 62.29  ? 77  ASP A CG  1 
ATOM   677   O  OD1 . ASP A  1 86  ? 29.795  -18.564 48.614 1.00 55.88  ? 77  ASP A OD1 1 
ATOM   678   O  OD2 . ASP A  1 86  ? 31.827  -19.123 47.967 1.00 75.52  ? 77  ASP A OD2 1 
ATOM   679   N  N   . PHE A  1 87  ? 27.767  -16.677 46.386 1.00 51.97  ? 78  PHE A N   1 
ATOM   680   C  CA  . PHE A  1 87  ? 26.368  -16.897 46.758 1.00 55.98  ? 78  PHE A CA  1 
ATOM   681   C  C   . PHE A  1 87  ? 25.646  -17.983 45.937 1.00 58.35  ? 78  PHE A C   1 
ATOM   682   O  O   . PHE A  1 87  ? 26.115  -18.405 44.883 1.00 58.55  ? 78  PHE A O   1 
ATOM   683   C  CB  . PHE A  1 87  ? 25.587  -15.579 46.740 1.00 52.83  ? 78  PHE A CB  1 
ATOM   684   C  CG  . PHE A  1 87  ? 25.383  -15.018 45.376 1.00 57.94  ? 78  PHE A CG  1 
ATOM   685   C  CD1 . PHE A  1 87  ? 24.176  -15.185 44.724 1.00 60.63  ? 78  PHE A CD1 1 
ATOM   686   C  CD2 . PHE A  1 87  ? 26.399  -14.328 44.732 1.00 63.25  ? 78  PHE A CD2 1 
ATOM   687   C  CE1 . PHE A  1 87  ? 23.978  -14.674 43.455 1.00 60.73  ? 78  PHE A CE1 1 
ATOM   688   C  CE2 . PHE A  1 87  ? 26.207  -13.816 43.455 1.00 62.01  ? 78  PHE A CE2 1 
ATOM   689   C  CZ  . PHE A  1 87  ? 24.997  -13.991 42.820 1.00 58.02  ? 78  PHE A CZ  1 
ATOM   690   N  N   . ARG A  1 88  ? 24.518  -18.456 46.456 1.00 62.99  ? 79  ARG A N   1 
ATOM   691   C  CA  . ARG A  1 88  ? 23.651  -19.375 45.721 1.00 59.17  ? 79  ARG A CA  1 
ATOM   692   C  C   . ARG A  1 88  ? 22.539  -18.588 45.058 1.00 60.58  ? 79  ARG A C   1 
ATOM   693   O  O   . ARG A  1 88  ? 22.068  -17.581 45.602 1.00 62.19  ? 79  ARG A O   1 
ATOM   694   C  CB  . ARG A  1 88  ? 23.032  -20.418 46.646 1.00 58.63  ? 79  ARG A CB  1 
ATOM   695   C  CG  . ARG A  1 88  ? 23.945  -21.558 46.986 1.00 61.00  ? 79  ARG A CG  1 
ATOM   696   C  CD  . ARG A  1 88  ? 24.988  -21.147 47.997 1.00 69.55  ? 79  ARG A CD  1 
ATOM   697   N  NE  . ARG A  1 88  ? 25.932  -22.236 48.245 1.00 78.63  ? 79  ARG A NE  1 
ATOM   698   C  CZ  . ARG A  1 88  ? 26.928  -22.182 49.123 1.00 72.87  ? 79  ARG A CZ  1 
ATOM   699   N  NH1 . ARG A  1 88  ? 27.738  -23.226 49.276 1.00 58.91  ? 79  ARG A NH1 1 
ATOM   700   N  NH2 . ARG A  1 88  ? 27.109  -21.082 49.842 1.00 75.36  ? 79  ARG A NH2 1 
ATOM   701   N  N   . THR A  1 89  ? 22.129  -19.022 43.874 1.00 56.79  ? 80  THR A N   1 
ATOM   702   C  CA  . THR A  1 89  ? 21.008  -18.374 43.203 1.00 60.63  ? 80  THR A CA  1 
ATOM   703   C  C   . THR A  1 89  ? 20.234  -19.341 42.342 1.00 53.28  ? 80  THR A C   1 
ATOM   704   O  O   . THR A  1 89  ? 20.776  -20.320 41.854 1.00 48.82  ? 80  THR A O   1 
ATOM   705   C  CB  . THR A  1 89  ? 21.451  -17.174 42.327 1.00 63.90  ? 80  THR A CB  1 
ATOM   706   O  OG1 . THR A  1 89  ? 20.319  -16.335 42.058 1.00 70.00  ? 80  THR A OG1 1 
ATOM   707   C  CG2 . THR A  1 89  ? 22.062  -17.645 41.002 1.00 56.15  ? 80  THR A CG2 1 
ATOM   708   N  N   . SER A  1 90  ? 18.955  -19.044 42.171 1.00 57.17  ? 81  SER A N   1 
ATOM   709   C  CA  . SER A  1 90  ? 18.106  -19.735 41.216 1.00 63.77  ? 81  SER A CA  1 
ATOM   710   C  C   . SER A  1 90  ? 18.764  -19.715 39.839 1.00 62.74  ? 81  SER A C   1 
ATOM   711   O  O   . SER A  1 90  ? 19.211  -18.661 39.391 1.00 64.26  ? 81  SER A O   1 
ATOM   712   C  CB  . SER A  1 90  ? 16.768  -19.004 41.143 1.00 64.27  ? 81  SER A CB  1 
ATOM   713   O  OG  . SER A  1 90  ? 15.874  -19.649 40.265 1.00 69.05  ? 81  SER A OG  1 
ATOM   714   N  N   . ALA A  1 91  ? 18.837  -20.868 39.170 1.00 58.12  ? 82  ALA A N   1 
ATOM   715   C  CA  . ALA A  1 91  ? 19.410  -20.926 37.824 1.00 56.27  ? 82  ALA A CA  1 
ATOM   716   C  C   . ALA A  1 91  ? 18.612  -20.075 36.815 1.00 65.82  ? 82  ALA A C   1 
ATOM   717   O  O   . ALA A  1 91  ? 19.147  -19.649 35.788 1.00 68.86  ? 82  ALA A O   1 
ATOM   718   C  CB  . ALA A  1 91  ? 19.526  -22.355 37.355 1.00 49.09  ? 82  ALA A CB  1 
ATOM   719   N  N   . ALA A  1 92  ? 17.338  -19.825 37.117 1.00 64.11  ? 83  ALA A N   1 
ATOM   720   C  CA  . ALA A  1 92  ? 16.474  -18.982 36.287 1.00 66.56  ? 83  ALA A CA  1 
ATOM   721   C  C   . ALA A  1 92  ? 16.978  -17.543 36.197 1.00 68.63  ? 83  ALA A C   1 
ATOM   722   O  O   . ALA A  1 92  ? 16.712  -16.835 35.223 1.00 72.10  ? 83  ALA A O   1 
ATOM   723   C  CB  . ALA A  1 92  ? 15.062  -18.991 36.841 1.00 59.92  ? 83  ALA A CB  1 
ATOM   724   N  N   . ASP A  1 93  ? 17.700  -17.120 37.225 1.00 63.94  ? 84  ASP A N   1 
ATOM   725   C  CA  . ASP A  1 93  ? 18.113  -15.733 37.376 1.00 67.58  ? 84  ASP A CA  1 
ATOM   726   C  C   . ASP A  1 93  ? 19.334  -15.392 36.540 1.00 66.09  ? 84  ASP A C   1 
ATOM   727   O  O   . ASP A  1 93  ? 19.614  -14.217 36.302 1.00 73.49  ? 84  ASP A O   1 
ATOM   728   C  CB  . ASP A  1 93  ? 18.422  -15.414 38.850 1.00 73.65  ? 84  ASP A CB  1 
ATOM   729   C  CG  . ASP A  1 93  ? 17.168  -15.300 39.716 1.00 78.25  ? 84  ASP A CG  1 
ATOM   730   O  OD1 . ASP A  1 93  ? 16.039  -15.287 39.159 1.00 73.89  ? 84  ASP A OD1 1 
ATOM   731   O  OD2 . ASP A  1 93  ? 17.326  -15.207 40.959 1.00 82.94  ? 84  ASP A OD2 1 
ATOM   732   N  N   . ILE A  1 94  ? 20.075  -16.412 36.119 1.00 63.57  ? 85  ILE A N   1 
ATOM   733   C  CA  . ILE A  1 94  ? 21.310  -16.201 35.367 1.00 61.24  ? 85  ILE A CA  1 
ATOM   734   C  C   . ILE A  1 94  ? 21.248  -16.864 33.994 1.00 64.45  ? 85  ILE A C   1 
ATOM   735   O  O   . ILE A  1 94  ? 20.515  -17.839 33.794 1.00 67.93  ? 85  ILE A O   1 
ATOM   736   C  CB  . ILE A  1 94  ? 22.557  -16.740 36.125 1.00 61.18  ? 85  ILE A CB  1 
ATOM   737   C  CG1 . ILE A  1 94  ? 22.370  -18.225 36.487 1.00 59.72  ? 85  ILE A CG1 1 
ATOM   738   C  CG2 . ILE A  1 94  ? 22.879  -15.879 37.352 1.00 48.44  ? 85  ILE A CG2 1 
ATOM   739   C  CD1 . ILE A  1 94  ? 23.672  -19.004 36.681 1.00 49.11  ? 85  ILE A CD1 1 
ATOM   740   N  N   . TRP A  1 95  ? 22.009  -16.327 33.044 1.00 60.65  ? 86  TRP A N   1 
ATOM   741   C  CA  . TRP A  1 95  ? 22.136  -16.948 31.732 1.00 59.40  ? 86  TRP A CA  1 
ATOM   742   C  C   . TRP A  1 95  ? 22.789  -18.302 31.908 1.00 60.71  ? 86  TRP A C   1 
ATOM   743   O  O   . TRP A  1 95  ? 23.799  -18.413 32.590 1.00 65.97  ? 86  TRP A O   1 
ATOM   744   C  CB  . TRP A  1 95  ? 23.023  -16.105 30.823 1.00 60.26  ? 86  TRP A CB  1 
ATOM   745   C  CG  . TRP A  1 95  ? 23.290  -16.742 29.496 1.00 58.28  ? 86  TRP A CG  1 
ATOM   746   C  CD1 . TRP A  1 95  ? 22.592  -16.548 28.347 1.00 57.17  ? 86  TRP A CD1 1 
ATOM   747   C  CD2 . TRP A  1 95  ? 24.330  -17.678 29.182 1.00 53.68  ? 86  TRP A CD2 1 
ATOM   748   N  NE1 . TRP A  1 95  ? 23.132  -17.300 27.333 1.00 62.69  ? 86  TRP A NE1 1 
ATOM   749   C  CE2 . TRP A  1 95  ? 24.198  -18.005 27.822 1.00 57.71  ? 86  TRP A CE2 1 
ATOM   750   C  CE3 . TRP A  1 95  ? 25.359  -18.266 29.917 1.00 54.19  ? 86  TRP A CE3 1 
ATOM   751   C  CZ2 . TRP A  1 95  ? 25.058  -18.890 27.180 1.00 58.80  ? 86  TRP A CZ2 1 
ATOM   752   C  CZ3 . TRP A  1 95  ? 26.213  -19.147 29.279 1.00 54.49  ? 86  TRP A CZ3 1 
ATOM   753   C  CH2 . TRP A  1 95  ? 26.059  -19.447 27.921 1.00 55.14  ? 86  TRP A CH2 1 
ATOM   754   N  N   . THR A  1 96  ? 22.226  -19.338 31.309 1.00 55.43  ? 87  THR A N   1 
ATOM   755   C  CA  . THR A  1 96  ? 22.840  -20.644 31.419 1.00 55.98  ? 87  THR A CA  1 
ATOM   756   C  C   . THR A  1 96  ? 23.115  -21.125 30.023 1.00 58.31  ? 87  THR A C   1 
ATOM   757   O  O   . THR A  1 96  ? 22.341  -20.829 29.113 1.00 64.48  ? 87  THR A O   1 
ATOM   758   C  CB  . THR A  1 96  ? 21.941  -21.651 32.173 1.00 62.32  ? 87  THR A CB  1 
ATOM   759   O  OG1 . THR A  1 96  ? 20.618  -21.642 31.618 1.00 61.88  ? 87  THR A OG1 1 
ATOM   760   C  CG2 . THR A  1 96  ? 21.873  -21.290 33.657 1.00 55.39  ? 87  THR A CG2 1 
ATOM   761   N  N   . PRO A  1 97  ? 24.227  -21.854 29.838 1.00 59.23  ? 88  PRO A N   1 
ATOM   762   C  CA  . PRO A  1 97  ? 24.620  -22.347 28.513 1.00 57.03  ? 88  PRO A CA  1 
ATOM   763   C  C   . PRO A  1 97  ? 23.646  -23.407 28.037 1.00 55.35  ? 88  PRO A C   1 
ATOM   764   O  O   . PRO A  1 97  ? 23.144  -24.127 28.883 1.00 61.39  ? 88  PRO A O   1 
ATOM   765   C  CB  . PRO A  1 97  ? 25.998  -22.966 28.772 1.00 55.70  ? 88  PRO A CB  1 
ATOM   766   C  CG  . PRO A  1 97  ? 26.011  -23.292 30.216 1.00 50.10  ? 88  PRO A CG  1 
ATOM   767   C  CD  . PRO A  1 97  ? 25.211  -22.214 30.872 1.00 54.26  ? 88  PRO A CD  1 
ATOM   768   N  N   . ASP A  1 98  ? 23.405  -23.545 26.736 1.00 56.70  ? 89  ASP A N   1 
ATOM   769   C  CA  . ASP A  1 98  ? 22.426  -24.534 26.328 1.00 55.02  ? 89  ASP A CA  1 
ATOM   770   C  C   . ASP A  1 98  ? 23.157  -25.792 25.874 1.00 57.36  ? 89  ASP A C   1 
ATOM   771   O  O   . ASP A  1 98  ? 23.544  -25.934 24.736 1.00 64.50  ? 89  ASP A O   1 
ATOM   772   C  CB  . ASP A  1 98  ? 21.598  -23.960 25.166 1.00 56.02  ? 89  ASP A CB  1 
ATOM   773   C  CG  . ASP A  1 98  ? 22.444  -23.662 23.898 1.00 61.69  ? 89  ASP A CG  1 
ATOM   774   O  OD1 . ASP A  1 98  ? 23.655  -23.373 24.009 1.00 53.04  ? 89  ASP A OD1 1 
ATOM   775   O  OD2 . ASP A  1 98  ? 21.886  -23.720 22.777 1.00 60.55  ? 89  ASP A OD2 1 
ATOM   776   N  N   . ILE A  1 99  ? 23.169  -26.781 26.744 1.00 58.17  ? 90  ILE A N   1 
ATOM   777   C  CA  . ILE A  1 99  ? 23.961  -27.979 26.548 1.00 58.35  ? 90  ILE A CA  1 
ATOM   778   C  C   . ILE A  1 99  ? 22.910  -29.058 26.523 1.00 61.15  ? 90  ILE A C   1 
ATOM   779   O  O   . ILE A  1 99  ? 21.989  -29.029 27.338 1.00 62.37  ? 90  ILE A O   1 
ATOM   780   C  CB  . ILE A  1 99  ? 24.956  -28.213 27.723 1.00 61.39  ? 90  ILE A CB  1 
ATOM   781   C  CG1 . ILE A  1 99  ? 26.002  -27.095 27.787 1.00 60.89  ? 90  ILE A CG1 1 
ATOM   782   C  CG2 . ILE A  1 99  ? 25.651  -29.560 27.621 1.00 53.72  ? 90  ILE A CG2 1 
ATOM   783   C  CD1 . ILE A  1 99  ? 26.981  -27.089 26.653 1.00 58.59  ? 90  ILE A CD1 1 
ATOM   784   N  N   . THR A  1 100 ? 23.018  -29.974 25.565 1.00 61.08  ? 91  THR A N   1 
ATOM   785   C  CA  . THR A  1 100 ? 21.998  -30.985 25.346 1.00 57.99  ? 91  THR A CA  1 
ATOM   786   C  C   . THR A  1 100 ? 22.663  -32.306 25.061 1.00 58.42  ? 91  THR A C   1 
ATOM   787   O  O   . THR A  1 100 ? 23.764  -32.357 24.518 1.00 59.63  ? 91  THR A O   1 
ATOM   788   C  CB  . THR A  1 100 ? 21.137  -30.680 24.106 1.00 56.39  ? 91  THR A CB  1 
ATOM   789   O  OG1 . THR A  1 100 ? 20.811  -29.295 24.064 1.00 64.30  ? 91  THR A OG1 1 
ATOM   790   C  CG2 . THR A  1 100 ? 19.857  -31.488 24.135 1.00 62.01  ? 91  THR A CG2 1 
ATOM   791   N  N   . ALA A  1 101 ? 21.980  -33.376 25.429 1.00 53.01  ? 92  ALA A N   1 
ATOM   792   C  CA  . ALA A  1 101 ? 22.308  -34.680 24.914 1.00 59.25  ? 92  ALA A CA  1 
ATOM   793   C  C   . ALA A  1 101 ? 21.751  -34.741 23.472 1.00 64.13  ? 92  ALA A C   1 
ATOM   794   O  O   . ALA A  1 101 ? 20.558  -34.488 23.246 1.00 61.50  ? 92  ALA A O   1 
ATOM   795   C  CB  . ALA A  1 101 ? 21.701  -35.756 25.814 1.00 52.77  ? 92  ALA A CB  1 
ATOM   796   N  N   . TYR A  1 102 ? 22.616  -35.073 22.520 1.00 61.97  ? 93  TYR A N   1 
ATOM   797   C  CA  . TYR A  1 102 ? 22.260  -35.024 21.107 1.00 63.22  ? 93  TYR A CA  1 
ATOM   798   C  C   . TYR A  1 102 ? 21.369  -36.200 20.724 1.00 66.13  ? 93  TYR A C   1 
ATOM   799   O  O   . TYR A  1 102 ? 20.556  -36.102 19.804 1.00 60.49  ? 93  TYR A O   1 
ATOM   800   C  CB  . TYR A  1 102 ? 23.518  -35.016 20.237 1.00 67.61  ? 93  TYR A CB  1 
ATOM   801   C  CG  . TYR A  1 102 ? 24.280  -33.711 20.269 1.00 60.58  ? 93  TYR A CG  1 
ATOM   802   C  CD1 . TYR A  1 102 ? 23.621  -32.504 20.462 1.00 65.22  ? 93  TYR A CD1 1 
ATOM   803   C  CD2 . TYR A  1 102 ? 25.658  -33.685 20.105 1.00 64.31  ? 93  TYR A CD2 1 
ATOM   804   C  CE1 . TYR A  1 102 ? 24.313  -31.309 20.491 1.00 69.25  ? 93  TYR A CE1 1 
ATOM   805   C  CE2 . TYR A  1 102 ? 26.359  -32.494 20.133 1.00 61.86  ? 93  TYR A CE2 1 
ATOM   806   C  CZ  . TYR A  1 102 ? 25.682  -31.310 20.326 1.00 65.47  ? 93  TYR A CZ  1 
ATOM   807   O  OH  . TYR A  1 102 ? 26.376  -30.122 20.355 1.00 59.30  ? 93  TYR A OH  1 
ATOM   808   N  N   . SER A  1 103 ? 21.527  -37.312 21.434 1.00 57.65  ? 94  SER A N   1 
ATOM   809   C  CA  . SER A  1 103 ? 20.907  -38.570 21.037 1.00 57.50  ? 94  SER A CA  1 
ATOM   810   C  C   . SER A  1 103 ? 19.960  -39.080 22.117 1.00 57.19  ? 94  SER A C   1 
ATOM   811   O  O   . SER A  1 103 ? 19.566  -40.246 22.110 1.00 53.63  ? 94  SER A O   1 
ATOM   812   C  CB  . SER A  1 103 ? 21.975  -39.622 20.735 1.00 64.04  ? 94  SER A CB  1 
ATOM   813   O  OG  . SER A  1 103 ? 22.756  -39.900 21.884 1.00 64.36  ? 94  SER A OG  1 
ATOM   814   N  N   . SER A  1 104 ? 19.598  -38.200 23.044 1.00 55.45  ? 95  SER A N   1 
ATOM   815   C  CA  . SER A  1 104 ? 18.413  -38.399 23.869 1.00 59.84  ? 95  SER A CA  1 
ATOM   816   C  C   . SER A  1 104 ? 17.208  -38.786 23.019 1.00 59.01  ? 95  SER A C   1 
ATOM   817   O  O   . SER A  1 104 ? 17.086  -38.362 21.870 1.00 59.25  ? 95  SER A O   1 
ATOM   818   C  CB  . SER A  1 104 ? 18.104  -37.137 24.676 1.00 54.85  ? 95  SER A CB  1 
ATOM   819   O  OG  . SER A  1 104 ? 17.298  -36.241 23.931 1.00 58.15  ? 95  SER A OG  1 
ATOM   820   N  N   . THR A  1 105 ? 16.320  -39.593 23.591 1.00 54.77  ? 96  THR A N   1 
ATOM   821   C  CA  . THR A  1 105 ? 15.101  -39.998 22.903 1.00 56.67  ? 96  THR A CA  1 
ATOM   822   C  C   . THR A  1 105 ? 13.861  -39.599 23.697 1.00 55.45  ? 96  THR A C   1 
ATOM   823   O  O   . THR A  1 105 ? 12.734  -39.848 23.271 1.00 54.03  ? 96  THR A O   1 
ATOM   824   C  CB  . THR A  1 105 ? 15.071  -41.518 22.655 1.00 60.20  ? 96  THR A CB  1 
ATOM   825   O  OG1 . THR A  1 105 ? 14.702  -42.195 23.863 1.00 56.01  ? 96  THR A OG1 1 
ATOM   826   C  CG2 . THR A  1 105 ? 16.436  -42.009 22.200 1.00 55.93  ? 96  THR A CG2 1 
ATOM   827   N  N   A ARG A  1 106 ? 14.079  -38.977 24.852 0.50 54.64  ? 97  ARG A N   1 
ATOM   828   N  N   B ARG A  1 106 ? 14.078  -38.981 24.852 0.50 55.03  ? 97  ARG A N   1 
ATOM   829   C  CA  A ARG A  1 106 ? 12.989  -38.395 25.638 0.50 51.75  ? 97  ARG A CA  1 
ATOM   830   C  CA  B ARG A  1 106 ? 12.984  -38.381 25.609 0.50 51.75  ? 97  ARG A CA  1 
ATOM   831   C  C   A ARG A  1 106 ? 13.432  -37.037 26.141 0.50 51.66  ? 97  ARG A C   1 
ATOM   832   C  C   B ARG A  1 106 ? 13.436  -37.057 26.184 0.50 51.52  ? 97  ARG A C   1 
ATOM   833   O  O   A ARG A  1 106 ? 14.610  -36.698 26.060 0.50 55.57  ? 97  ARG A O   1 
ATOM   834   O  O   B ARG A  1 106 ? 14.627  -36.760 26.193 0.50 55.61  ? 97  ARG A O   1 
ATOM   835   C  CB  A ARG A  1 106 ? 12.613  -39.283 26.827 0.50 50.23  ? 97  ARG A CB  1 
ATOM   836   C  CB  B ARG A  1 106 ? 12.489  -39.319 26.710 0.50 50.32  ? 97  ARG A CB  1 
ATOM   837   C  CG  A ARG A  1 106 ? 11.938  -40.613 26.477 0.50 52.97  ? 97  ARG A CG  1 
ATOM   838   C  CG  B ARG A  1 106 ? 11.534  -40.398 26.203 0.50 53.46  ? 97  ARG A CG  1 
ATOM   839   C  CD  A ARG A  1 106 ? 10.489  -40.446 26.019 0.50 52.12  ? 97  ARG A CD  1 
ATOM   840   C  CD  B ARG A  1 106 ? 10.978  -41.245 27.330 0.50 51.87  ? 97  ARG A CD  1 
ATOM   841   N  NE  A ARG A  1 106 ? 9.797   -41.731 25.952 0.50 53.24  ? 97  ARG A NE  1 
ATOM   842   N  NE  B ARG A  1 106 ? 11.819  -42.394 27.654 0.50 54.68  ? 97  ARG A NE  1 
ATOM   843   C  CZ  A ARG A  1 106 ? 8.526   -41.882 25.588 0.50 52.00  ? 97  ARG A CZ  1 
ATOM   844   C  CZ  B ARG A  1 106 ? 11.542  -43.641 27.295 0.50 52.86  ? 97  ARG A CZ  1 
ATOM   845   N  NH1 A ARG A  1 106 ? 7.811   -40.815 25.257 0.50 45.20  ? 97  ARG A NH1 1 
ATOM   846   N  NH1 B ARG A  1 106 ? 10.449  -43.895 26.592 0.50 53.07  ? 97  ARG A NH1 1 
ATOM   847   N  NH2 A ARG A  1 106 ? 7.970   -43.095 25.557 0.50 42.12  ? 97  ARG A NH2 1 
ATOM   848   N  NH2 B ARG A  1 106 ? 12.352  -44.631 27.641 0.50 52.99  ? 97  ARG A NH2 1 
ATOM   849   N  N   . PRO A  1 107 ? 12.488  -36.231 26.629 1.00 50.79  ? 98  PRO A N   1 
ATOM   850   C  CA  . PRO A  1 107 ? 12.887  -34.970 27.273 1.00 49.35  ? 98  PRO A CA  1 
ATOM   851   C  C   . PRO A  1 107 ? 13.676  -35.222 28.592 1.00 49.85  ? 98  PRO A C   1 
ATOM   852   O  O   . PRO A  1 107 ? 13.236  -36.016 29.427 1.00 51.37  ? 98  PRO A O   1 
ATOM   853   C  CB  . PRO A  1 107 ? 11.545  -34.291 27.560 1.00 45.73  ? 98  PRO A CB  1 
ATOM   854   C  CG  . PRO A  1 107 ? 10.526  -35.033 26.762 1.00 41.85  ? 98  PRO A CG  1 
ATOM   855   C  CD  . PRO A  1 107 ? 11.033  -36.411 26.567 1.00 45.48  ? 98  PRO A CD  1 
ATOM   856   N  N   . VAL A  1 108 ? 14.817  -34.566 28.776 1.00 48.22  ? 99  VAL A N   1 
ATOM   857   C  CA  . VAL A  1 108 ? 15.643  -34.795 29.965 1.00 49.31  ? 99  VAL A CA  1 
ATOM   858   C  C   . VAL A  1 108 ? 14.888  -34.493 31.252 1.00 49.76  ? 99  VAL A C   1 
ATOM   859   O  O   . VAL A  1 108 ? 14.275  -33.450 31.384 1.00 39.39  ? 99  VAL A O   1 
ATOM   860   C  CB  . VAL A  1 108 ? 16.932  -33.938 29.966 1.00 52.01  ? 99  VAL A CB  1 
ATOM   861   C  CG1 . VAL A  1 108 ? 17.743  -34.186 31.228 1.00 54.70  ? 99  VAL A CG1 1 
ATOM   862   C  CG2 . VAL A  1 108 ? 17.770  -34.237 28.752 1.00 62.02  ? 99  VAL A CG2 1 
ATOM   863   N  N   . GLN A  1 109 ? 14.942  -35.406 32.213 1.00 52.96  ? 100 GLN A N   1 
ATOM   864   C  CA  . GLN A  1 109 ? 14.299  -35.148 33.495 1.00 51.57  ? 100 GLN A CA  1 
ATOM   865   C  C   . GLN A  1 109 ? 15.253  -34.644 34.597 1.00 53.14  ? 100 GLN A C   1 
ATOM   866   O  O   . GLN A  1 109 ? 16.310  -35.224 34.840 1.00 54.08  ? 100 GLN A O   1 
ATOM   867   C  CB  . GLN A  1 109 ? 13.503  -36.356 33.944 1.00 47.16  ? 100 GLN A CB  1 
ATOM   868   C  CG  . GLN A  1 109 ? 12.197  -36.472 33.239 1.00 47.71  ? 100 GLN A CG  1 
ATOM   869   C  CD  . GLN A  1 109 ? 11.545  -37.792 33.515 1.00 56.34  ? 100 GLN A CD  1 
ATOM   870   O  OE1 . GLN A  1 109 ? 12.181  -38.839 33.433 1.00 48.76  ? 100 GLN A OE1 1 
ATOM   871   N  NE2 . GLN A  1 109 ? 10.274  -37.754 33.872 1.00 55.91  ? 100 GLN A NE2 1 
ATOM   872   N  N   . VAL A  1 110 ? 14.862  -33.548 35.243 1.00 44.58  ? 101 VAL A N   1 
ATOM   873   C  CA  . VAL A  1 110 ? 15.688  -32.915 36.247 1.00 50.84  ? 101 VAL A CA  1 
ATOM   874   C  C   . VAL A  1 110 ? 15.332  -33.391 37.670 1.00 54.29  ? 101 VAL A C   1 
ATOM   875   O  O   . VAL A  1 110 ? 14.187  -33.263 38.110 1.00 56.32  ? 101 VAL A O   1 
ATOM   876   C  CB  . VAL A  1 110 ? 15.640  -31.384 36.105 1.00 55.11  ? 101 VAL A CB  1 
ATOM   877   C  CG1 . VAL A  1 110 ? 16.442  -30.721 37.215 1.00 52.14  ? 101 VAL A CG1 1 
ATOM   878   C  CG2 . VAL A  1 110 ? 16.179  -30.969 34.724 1.00 45.81  ? 101 VAL A CG2 1 
ATOM   879   N  N   . LEU A  1 111 ? 16.310  -34.004 38.343 1.00 50.37  ? 102 LEU A N   1 
ATOM   880   C  CA  . LEU A  1 111 ? 16.099  -34.607 39.660 1.00 48.98  ? 102 LEU A CA  1 
ATOM   881   C  C   . LEU A  1 111 ? 16.423  -33.724 40.872 1.00 47.60  ? 102 LEU A C   1 
ATOM   882   O  O   . LEU A  1 111 ? 16.006  -34.026 41.981 1.00 52.85  ? 102 LEU A O   1 
ATOM   883   C  CB  . LEU A  1 111 ? 16.879  -35.924 39.754 1.00 42.77  ? 102 LEU A CB  1 
ATOM   884   C  CG  . LEU A  1 111 ? 16.660  -36.864 38.564 1.00 51.47  ? 102 LEU A CG  1 
ATOM   885   C  CD1 . LEU A  1 111 ? 17.560  -38.072 38.647 1.00 46.39  ? 102 LEU A CD1 1 
ATOM   886   C  CD2 . LEU A  1 111 ? 15.207  -37.272 38.460 1.00 46.14  ? 102 LEU A CD2 1 
ATOM   887   N  N   . SER A  1 112 ? 17.087  -32.601 40.629 1.00 47.45  ? 103 SER A N   1 
ATOM   888   C  CA  . SER A  1 112 ? 17.641  -31.751 41.672 1.00 49.21  ? 103 SER A CA  1 
ATOM   889   C  C   . SER A  1 112 ? 17.109  -30.332 41.535 1.00 49.20  ? 103 SER A C   1 
ATOM   890   O  O   . SER A  1 112 ? 16.650  -29.954 40.469 1.00 45.19  ? 103 SER A O   1 
ATOM   891   C  CB  . SER A  1 112 ? 19.163  -31.721 41.544 1.00 52.78  ? 103 SER A CB  1 
ATOM   892   O  OG  . SER A  1 112 ? 19.580  -30.943 40.430 1.00 49.93  ? 103 SER A OG  1 
ATOM   893   N  N   . PRO A  1 113 ? 17.159  -29.535 42.620 1.00 49.74  ? 104 PRO A N   1 
ATOM   894   C  CA  . PRO A  1 113 ? 16.777  -28.129 42.506 1.00 47.19  ? 104 PRO A CA  1 
ATOM   895   C  C   . PRO A  1 113 ? 17.706  -27.427 41.534 1.00 57.92  ? 104 PRO A C   1 
ATOM   896   O  O   . PRO A  1 113 ? 18.885  -27.793 41.429 1.00 57.04  ? 104 PRO A O   1 
ATOM   897   C  CB  . PRO A  1 113 ? 16.979  -27.607 43.916 1.00 41.44  ? 104 PRO A CB  1 
ATOM   898   C  CG  . PRO A  1 113 ? 16.742  -28.756 44.751 1.00 43.78  ? 104 PRO A CG  1 
ATOM   899   C  CD  . PRO A  1 113 ? 17.398  -29.892 44.019 1.00 50.97  ? 104 PRO A CD  1 
ATOM   900   N  N   . GLN A  1 114 ? 17.187  -26.450 40.795 1.00 60.42  ? 105 GLN A N   1 
ATOM   901   C  CA  . GLN A  1 114 ? 18.025  -25.858 39.788 1.00 52.29  ? 105 GLN A CA  1 
ATOM   902   C  C   . GLN A  1 114 ? 18.490  -24.558 40.373 1.00 56.37  ? 105 GLN A C   1 
ATOM   903   O  O   . GLN A  1 114 ? 17.795  -23.537 40.343 1.00 59.02  ? 105 GLN A O   1 
ATOM   904   C  CB  . GLN A  1 114 ? 17.216  -25.677 38.521 1.00 39.62  ? 105 GLN A CB  1 
ATOM   905   C  CG  . GLN A  1 114 ? 16.733  -27.013 38.000 1.00 48.77  ? 105 GLN A CG  1 
ATOM   906   C  CD  . GLN A  1 114 ? 16.010  -26.920 36.667 1.00 64.40  ? 105 GLN A CD  1 
ATOM   907   O  OE1 . GLN A  1 114 ? 14.820  -26.614 36.625 1.00 68.54  ? 105 GLN A OE1 1 
ATOM   908   N  NE2 . GLN A  1 114 ? 16.725  -27.194 35.568 1.00 50.13  ? 105 GLN A NE2 1 
ATOM   909   N  N   . ASN A  1 115 ? 19.745  -24.603 40.801 1.00 54.76  ? 106 ASN A N   1 
ATOM   910   C  CA  . ASN A  1 115 ? 20.339  -23.584 41.633 1.00 53.51  ? 106 ASN A CA  1 
ATOM   911   C  C   . ASN A  1 115 ? 21.793  -23.561 41.255 1.00 53.66  ? 106 ASN A C   1 
ATOM   912   O  O   . ASN A  1 115 ? 22.367  -24.599 40.949 1.00 57.46  ? 106 ASN A O   1 
ATOM   913   C  CB  . ASN A  1 115 ? 20.175  -23.936 43.112 1.00 51.79  ? 106 ASN A CB  1 
ATOM   914   C  CG  . ASN A  1 115 ? 18.793  -23.574 43.662 1.00 61.30  ? 106 ASN A CG  1 
ATOM   915   O  OD1 . ASN A  1 115 ? 18.188  -22.570 43.269 1.00 56.43  ? 106 ASN A OD1 1 
ATOM   916   N  ND2 . ASN A  1 115 ? 18.292  -24.395 44.583 1.00 60.06  ? 106 ASN A ND2 1 
ATOM   917   N  N   . ALA A  1 116 ? 22.385  -22.376 41.248 1.00 58.21  ? 107 ALA A N   1 
ATOM   918   C  CA  . ALA A  1 116 ? 23.775  -22.235 40.853 1.00 57.54  ? 107 ALA A CA  1 
ATOM   919   C  C   . ALA A  1 116 ? 24.620  -21.561 41.938 1.00 57.63  ? 107 ALA A C   1 
ATOM   920   O  O   . ALA A  1 116 ? 24.114  -20.819 42.781 1.00 58.49  ? 107 ALA A O   1 
ATOM   921   C  CB  . ALA A  1 116 ? 23.884  -21.485 39.519 1.00 53.03  ? 107 ALA A CB  1 
ATOM   922   N  N   . LEU A  1 117 ? 25.911  -21.861 41.915 1.00 59.25  ? 108 LEU A N   1 
ATOM   923   C  CA  . LEU A  1 117 ? 26.881  -21.209 42.770 1.00 62.43  ? 108 LEU A CA  1 
ATOM   924   C  C   . LEU A  1 117 ? 27.670  -20.165 41.980 1.00 66.93  ? 108 LEU A C   1 
ATOM   925   O  O   . LEU A  1 117 ? 28.278  -20.465 40.945 1.00 62.87  ? 108 LEU A O   1 
ATOM   926   C  CB  . LEU A  1 117 ? 27.846  -22.239 43.344 1.00 68.61  ? 108 LEU A CB  1 
ATOM   927   C  CG  . LEU A  1 117 ? 28.943  -21.609 44.194 1.00 67.17  ? 108 LEU A CG  1 
ATOM   928   C  CD1 . LEU A  1 117 ? 28.315  -20.987 45.425 1.00 64.28  ? 108 LEU A CD1 1 
ATOM   929   C  CD2 . LEU A  1 117 ? 29.977  -22.652 44.554 1.00 63.79  ? 108 LEU A CD2 1 
ATOM   930   N  N   . VAL A  1 118 ? 27.657  -18.931 42.467 1.00 64.17  ? 109 VAL A N   1 
ATOM   931   C  CA  . VAL A  1 118 ? 28.375  -17.858 41.800 1.00 62.77  ? 109 VAL A CA  1 
ATOM   932   C  C   . VAL A  1 118 ? 29.408  -17.331 42.771 1.00 60.61  ? 109 VAL A C   1 
ATOM   933   O  O   . VAL A  1 118 ? 29.144  -17.269 43.966 1.00 61.60  ? 109 VAL A O   1 
ATOM   934   C  CB  . VAL A  1 118 ? 27.428  -16.691 41.423 1.00 57.52  ? 109 VAL A CB  1 
ATOM   935   C  CG1 . VAL A  1 118 ? 28.132  -15.704 40.506 1.00 51.79  ? 109 VAL A CG1 1 
ATOM   936   C  CG2 . VAL A  1 118 ? 26.163  -17.210 40.776 1.00 56.97  ? 109 VAL A CG2 1 
ATOM   937   N  N   . ASN A  1 119 ? 30.579  -16.947 42.287 1.00 58.99  ? 110 ASN A N   1 
ATOM   938   C  CA  . ASN A  1 119 ? 31.435  -16.206 43.180 1.00 64.54  ? 110 ASN A CA  1 
ATOM   939   C  C   . ASN A  1 119 ? 32.164  -14.982 42.619 1.00 65.56  ? 110 ASN A C   1 
ATOM   940   O  O   . ASN A  1 119 ? 32.132  -14.719 41.419 1.00 66.91  ? 110 ASN A O   1 
ATOM   941   C  CB  . ASN A  1 119 ? 32.531  -17.158 43.887 1.00 68.52  ? 110 ASN A CB  1 
ATOM   942   C  CG  . ASN A  1 119 ? 33.466  -17.724 42.893 1.00 70.65  ? 110 ASN A CG  1 
ATOM   943   O  OD1 . ASN A  1 119 ? 33.569  -17.252 41.760 1.00 70.55  ? 110 ASN A OD1 1 
ATOM   944   N  ND2 . ASN A  1 119 ? 34.195  -18.735 43.318 1.00 87.24  ? 110 ASN A ND2 1 
ATOM   945   N  N   . SER A  1 120 ? 32.860  -14.279 43.510 1.00 64.93  ? 111 SER A N   1 
ATOM   946   C  CA  . SER A  1 120 ? 33.367  -12.934 43.245 1.00 65.16  ? 111 SER A CA  1 
ATOM   947   C  C   . SER A  1 120 ? 34.242  -12.809 41.989 1.00 68.05  ? 111 SER A C   1 
ATOM   948   O  O   . SER A  1 120 ? 34.282  -11.746 41.372 1.00 69.11  ? 111 SER A O   1 
ATOM   949   C  CB  . SER A  1 120 ? 34.052  -12.334 44.495 1.00 65.61  ? 111 SER A CB  1 
ATOM   950   O  OG  . SER A  1 120 ? 35.151  -13.104 44.960 1.00 70.32  ? 111 SER A OG  1 
ATOM   951   N  N   . SER A  1 121 ? 34.921  -13.889 41.604 1.00 67.10  ? 112 SER A N   1 
ATOM   952   C  CA  . SER A  1 121 ? 35.748  -13.884 40.396 1.00 67.32  ? 112 SER A CA  1 
ATOM   953   C  C   . SER A  1 121 ? 34.874  -13.973 39.140 1.00 74.15  ? 112 SER A C   1 
ATOM   954   O  O   . SER A  1 121 ? 35.329  -13.715 38.019 1.00 72.80  ? 112 SER A O   1 
ATOM   955   C  CB  . SER A  1 121 ? 36.775  -15.018 40.435 1.00 67.54  ? 112 SER A CB  1 
ATOM   956   O  OG  . SER A  1 121 ? 36.151  -16.266 40.678 1.00 75.56  ? 112 SER A OG  1 
ATOM   957   N  N   . GLY A  1 122 ? 33.609  -14.328 39.344 1.00 69.65  ? 113 GLY A N   1 
ATOM   958   C  CA  . GLY A  1 122 ? 32.646  -14.368 38.267 1.00 64.22  ? 113 GLY A CA  1 
ATOM   959   C  C   . GLY A  1 122 ? 32.382  -15.761 37.739 1.00 68.41  ? 113 GLY A C   1 
ATOM   960   O  O   . GLY A  1 122 ? 31.635  -15.900 36.766 1.00 63.72  ? 113 GLY A O   1 
ATOM   961   N  N   . HIS A  1 123 ? 32.975  -16.782 38.371 1.00 67.16  ? 114 HIS A N   1 
ATOM   962   C  CA  . HIS A  1 123 ? 32.775  -18.173 37.952 1.00 64.32  ? 114 HIS A CA  1 
ATOM   963   C  C   . HIS A  1 123 ? 31.427  -18.700 38.401 1.00 62.30  ? 114 HIS A C   1 
ATOM   964   O  O   . HIS A  1 123 ? 31.024  -18.503 39.537 1.00 67.20  ? 114 HIS A O   1 
ATOM   965   C  CB  . HIS A  1 123 ? 33.842  -19.105 38.515 1.00 70.10  ? 114 HIS A CB  1 
ATOM   966   C  CG  . HIS A  1 123 ? 35.222  -18.844 38.000 1.00 83.27  ? 114 HIS A CG  1 
ATOM   967   N  ND1 . HIS A  1 123 ? 36.149  -18.112 38.709 1.00 89.27  ? 114 HIS A ND1 1 
ATOM   968   C  CD2 . HIS A  1 123 ? 35.842  -19.239 36.862 1.00 83.85  ? 114 HIS A CD2 1 
ATOM   969   C  CE1 . HIS A  1 123 ? 37.281  -18.058 38.026 1.00 92.29  ? 114 HIS A CE1 1 
ATOM   970   N  NE2 . HIS A  1 123 ? 37.120  -18.732 36.902 1.00 88.06  ? 114 HIS A NE2 1 
ATOM   971   N  N   . VAL A  1 124 ? 30.735  -19.384 37.502 1.00 65.65  ? 115 VAL A N   1 
ATOM   972   C  CA  . VAL A  1 124 ? 29.480  -20.040 37.839 1.00 64.45  ? 115 VAL A CA  1 
ATOM   973   C  C   . VAL A  1 124 ? 29.655  -21.558 37.846 1.00 60.33  ? 115 VAL A C   1 
ATOM   974   O  O   . VAL A  1 124 ? 30.415  -22.113 37.058 1.00 61.17  ? 115 VAL A O   1 
ATOM   975   C  CB  . VAL A  1 124 ? 28.365  -19.628 36.867 1.00 55.22  ? 115 VAL A CB  1 
ATOM   976   C  CG1 . VAL A  1 124 ? 27.059  -20.276 37.245 1.00 55.95  ? 115 VAL A CG1 1 
ATOM   977   C  CG2 . VAL A  1 124 ? 28.216  -18.142 36.894 1.00 52.53  ? 115 VAL A CG2 1 
ATOM   978   N  N   . GLN A  1 125 ? 28.959  -22.220 38.756 1.00 59.49  ? 116 GLN A N   1 
ATOM   979   C  CA  . GLN A  1 125 ? 29.027  -23.665 38.887 1.00 60.30  ? 116 GLN A CA  1 
ATOM   980   C  C   . GLN A  1 125 ? 27.597  -24.155 38.946 1.00 55.89  ? 116 GLN A C   1 
ATOM   981   O  O   . GLN A  1 125 ? 26.847  -23.764 39.822 1.00 55.82  ? 116 GLN A O   1 
ATOM   982   C  CB  . GLN A  1 125 ? 29.727  -24.017 40.193 1.00 66.65  ? 116 GLN A CB  1 
ATOM   983   C  CG  . GLN A  1 125 ? 30.834  -25.054 40.109 1.00 76.11  ? 116 GLN A CG  1 
ATOM   984   C  CD  . GLN A  1 125 ? 31.693  -25.064 41.378 1.00 89.58  ? 116 GLN A CD  1 
ATOM   985   O  OE1 . GLN A  1 125 ? 32.107  -24.007 41.875 1.00 94.14  ? 116 GLN A OE1 1 
ATOM   986   N  NE2 . GLN A  1 125 ? 31.947  -26.255 41.916 1.00 76.84  ? 116 GLN A NE2 1 
ATOM   987   N  N   . TYR A  1 126 ? 27.198  -24.996 38.013 1.00 53.84  ? 117 TYR A N   1 
ATOM   988   C  CA  . TYR A  1 126 ? 25.840  -25.503 38.043 1.00 53.17  ? 117 TYR A CA  1 
ATOM   989   C  C   . TYR A  1 126 ? 25.891  -27.015 37.869 1.00 54.37  ? 117 TYR A C   1 
ATOM   990   O  O   . TYR A  1 126 ? 26.361  -27.511 36.853 1.00 55.88  ? 117 TYR A O   1 
ATOM   991   C  CB  . TYR A  1 126 ? 25.041  -24.805 36.943 1.00 53.16  ? 117 TYR A CB  1 
ATOM   992   C  CG  . TYR A  1 126 ? 23.637  -25.293 36.682 1.00 57.75  ? 117 TYR A CG  1 
ATOM   993   C  CD1 . TYR A  1 126 ? 22.689  -25.338 37.695 1.00 57.03  ? 117 TYR A CD1 1 
ATOM   994   C  CD2 . TYR A  1 126 ? 23.241  -25.655 35.395 1.00 54.13  ? 117 TYR A CD2 1 
ATOM   995   C  CE1 . TYR A  1 126 ? 21.386  -25.763 37.445 1.00 53.40  ? 117 TYR A CE1 1 
ATOM   996   C  CE2 . TYR A  1 126 ? 21.951  -26.076 35.134 1.00 56.66  ? 117 TYR A CE2 1 
ATOM   997   C  CZ  . TYR A  1 126 ? 21.023  -26.127 36.166 1.00 62.09  ? 117 TYR A CZ  1 
ATOM   998   O  OH  . TYR A  1 126 ? 19.734  -26.557 35.908 1.00 59.15  ? 117 TYR A OH  1 
ATOM   999   N  N   . LEU A  1 127 ? 25.339  -27.729 38.869 1.00 60.56  ? 118 LEU A N   1 
ATOM   1000  C  CA  A LEU A  1 127 ? 25.303  -29.200 38.718 0.50 59.30  ? 118 LEU A CA  1 
ATOM   1001  C  CA  B LEU A  1 127 ? 25.325  -29.180 38.721 0.50 59.30  ? 118 LEU A CA  1 
ATOM   1002  C  C   . LEU A  1 127 ? 23.900  -29.522 38.924 1.00 57.65  ? 118 LEU A C   1 
ATOM   1003  O  O   . LEU A  1 127 ? 23.257  -29.179 39.933 1.00 64.29  ? 118 LEU A O   1 
ATOM   1004  C  CB  A LEU A  1 127 ? 26.025  -29.969 39.752 0.50 62.33  ? 118 LEU A CB  1 
ATOM   1005  C  CB  B LEU A  1 127 ? 26.187  -29.944 39.704 0.50 62.33  ? 118 LEU A CB  1 
ATOM   1006  C  CG  A LEU A  1 127 ? 27.468  -29.673 39.835 0.50 63.18  ? 118 LEU A CG  1 
ATOM   1007  C  CG  B LEU A  1 127 ? 26.284  -31.449 39.355 0.50 64.77  ? 118 LEU A CG  1 
ATOM   1008  C  CD1 A LEU A  1 127 ? 27.574  -28.272 40.331 0.50 58.19  ? 118 LEU A CD1 1 
ATOM   1009  C  CD1 B LEU A  1 127 ? 27.561  -31.906 39.969 0.50 65.93  ? 118 LEU A CD1 1 
ATOM   1010  C  CD2 A LEU A  1 127 ? 27.991  -30.646 40.819 0.50 64.96  ? 118 LEU A CD2 1 
ATOM   1011  C  CD2 B LEU A  1 127 ? 25.113  -32.132 39.946 0.50 67.46  ? 118 LEU A CD2 1 
ATOM   1012  N  N   . PRO A  1 128 ? 23.308  -30.140 37.884 1.00 51.76  ? 119 PRO A N   1 
ATOM   1013  C  CA  . PRO A  1 128 ? 21.973  -30.668 38.169 1.00 55.41  ? 119 PRO A CA  1 
ATOM   1014  C  C   . PRO A  1 128 ? 21.878  -32.177 37.981 1.00 56.02  ? 119 PRO A C   1 
ATOM   1015  O  O   . PRO A  1 128 ? 22.277  -32.693 36.937 1.00 57.72  ? 119 PRO A O   1 
ATOM   1016  C  CB  . PRO A  1 128 ? 21.102  -29.963 37.129 1.00 60.28  ? 119 PRO A CB  1 
ATOM   1017  C  CG  . PRO A  1 128 ? 22.015  -29.770 35.968 1.00 53.07  ? 119 PRO A CG  1 
ATOM   1018  C  CD  . PRO A  1 128 ? 23.391  -29.541 36.539 1.00 48.42  ? 119 PRO A CD  1 
ATOM   1019  N  N   . ALA A  1 129 ? 21.236  -32.897 38.890 1.00 48.85  ? 120 ALA A N   1 
ATOM   1020  C  CA  . ALA A  1 129 ? 21.060  -34.328 38.655 1.00 57.22  ? 120 ALA A CA  1 
ATOM   1021  C  C   . ALA A  1 129 ? 19.949  -34.498 37.570 1.00 56.15  ? 120 ALA A C   1 
ATOM   1022  O  O   . ALA A  1 129 ? 18.921  -33.823 37.626 1.00 53.12  ? 120 ALA A O   1 
ATOM   1023  C  CB  . ALA A  1 129 ? 20.675  -35.037 39.935 1.00 52.41  ? 120 ALA A CB  1 
ATOM   1024  N  N   . GLN A  1 130 ? 20.167  -35.394 36.603 1.00 51.59  ? 121 GLN A N   1 
ATOM   1025  C  CA  . GLN A  1 130 ? 19.271  -35.709 35.510 1.00 55.89  ? 121 GLN A CA  1 
ATOM   1026  C  C   . GLN A  1 130 ? 19.076  -37.199 35.307 1.00 52.30  ? 121 GLN A C   1 
ATOM   1027  O  O   . GLN A  1 130 ? 19.961  -37.999 35.617 1.00 48.83  ? 121 GLN A O   1 
ATOM   1028  C  CB  . GLN A  1 130 ? 19.778  -35.058 34.226 1.00 59.62  ? 121 GLN A CB  1 
ATOM   1029  C  CG  . GLN A  1 130 ? 19.830  -33.549 34.316 1.00 62.03  ? 121 GLN A CG  1 
ATOM   1030  C  CD  . GLN A  1 130 ? 20.694  -32.941 33.244 1.00 71.88  ? 121 GLN A CD  1 
ATOM   1031  O  OE1 . GLN A  1 130 ? 21.453  -33.636 32.575 1.00 70.40  ? 121 GLN A OE1 1 
ATOM   1032  N  NE2 . GLN A  1 130 ? 20.583  -31.633 33.070 1.00 82.48  ? 121 GLN A NE2 1 
ATOM   1033  N  N   . ARG A  1 131 ? 17.885  -37.548 34.826 1.00 48.62  ? 122 ARG A N   1 
ATOM   1034  C  CA  . ARG A  1 131 ? 17.649  -38.834 34.187 1.00 50.69  ? 122 ARG A CA  1 
ATOM   1035  C  C   . ARG A  1 131 ? 17.477  -38.614 32.682 1.00 54.33  ? 122 ARG A C   1 
ATOM   1036  O  O   . ARG A  1 131 ? 16.479  -38.031 32.225 1.00 55.85  ? 122 ARG A O   1 
ATOM   1037  C  CB  . ARG A  1 131 ? 16.409  -39.522 34.742 1.00 39.14  ? 122 ARG A CB  1 
ATOM   1038  C  CG  . ARG A  1 131 ? 16.339  -40.968 34.356 1.00 40.69  ? 122 ARG A CG  1 
ATOM   1039  C  CD  . ARG A  1 131 ? 14.999  -41.558 34.728 1.00 49.02  ? 122 ARG A CD  1 
ATOM   1040  N  NE  . ARG A  1 131 ? 14.770  -42.881 34.142 1.00 53.59  ? 122 ARG A NE  1 
ATOM   1041  C  CZ  . ARG A  1 131 ? 14.166  -43.883 34.772 1.00 55.34  ? 122 ARG A CZ  1 
ATOM   1042  N  NH1 . ARG A  1 131 ? 13.751  -43.720 36.017 1.00 57.36  ? 122 ARG A NH1 1 
ATOM   1043  N  NH2 . ARG A  1 131 ? 13.983  -45.054 34.169 1.00 50.45  ? 122 ARG A NH2 1 
ATOM   1044  N  N   . LEU A  1 132 ? 18.455  -39.091 31.918 1.00 53.02  ? 123 LEU A N   1 
ATOM   1045  C  CA  . LEU A  1 132 ? 18.422  -39.036 30.458 1.00 51.67  ? 123 LEU A CA  1 
ATOM   1046  C  C   . LEU A  1 132 ? 18.144  -40.416 29.867 1.00 49.87  ? 123 LEU A C   1 
ATOM   1047  O  O   . LEU A  1 132 ? 18.774  -41.389 30.246 1.00 53.55  ? 123 LEU A O   1 
ATOM   1048  C  CB  . LEU A  1 132 ? 19.780  -38.555 29.966 1.00 50.68  ? 123 LEU A CB  1 
ATOM   1049  C  CG  . LEU A  1 132 ? 20.067  -38.492 28.477 1.00 54.08  ? 123 LEU A CG  1 
ATOM   1050  C  CD1 . LEU A  1 132 ? 19.314  -37.325 27.875 1.00 57.77  ? 123 LEU A CD1 1 
ATOM   1051  C  CD2 . LEU A  1 132 ? 21.564  -38.348 28.245 1.00 54.64  ? 123 LEU A CD2 1 
ATOM   1052  N  N   . SER A  1 133 ? 17.198  -40.531 28.950 1.00 50.06  ? 124 SER A N   1 
ATOM   1053  C  CA  . SER A  1 133 ? 17.161  -41.765 28.168 1.00 55.66  ? 124 SER A CA  1 
ATOM   1054  C  C   . SER A  1 133 ? 17.564  -41.481 26.732 1.00 54.23  ? 124 SER A C   1 
ATOM   1055  O  O   . SER A  1 133 ? 17.134  -40.503 26.132 1.00 49.89  ? 124 SER A O   1 
ATOM   1056  C  CB  . SER A  1 133 ? 15.860  -42.579 28.334 1.00 54.44  ? 124 SER A CB  1 
ATOM   1057  O  OG  . SER A  1 133 ? 14.771  -42.091 27.592 1.00 53.33  ? 124 SER A OG  1 
ATOM   1058  N  N   . PHE A  1 134 ? 18.452  -42.316 26.211 1.00 63.77  ? 125 PHE A N   1 
ATOM   1059  C  CA  . PHE A  1 134 ? 19.094  -42.009 24.941 1.00 69.52  ? 125 PHE A CA  1 
ATOM   1060  C  C   . PHE A  1 134 ? 19.322  -43.239 24.034 1.00 68.45  ? 125 PHE A C   1 
ATOM   1061  O  O   . PHE A  1 134 ? 19.033  -44.379 24.445 1.00 67.16  ? 125 PHE A O   1 
ATOM   1062  C  CB  . PHE A  1 134 ? 20.405  -41.263 25.223 1.00 64.24  ? 125 PHE A CB  1 
ATOM   1063  C  CG  . PHE A  1 134 ? 21.441  -42.098 25.890 1.00 66.05  ? 125 PHE A CG  1 
ATOM   1064  C  CD1 . PHE A  1 134 ? 22.444  -42.692 25.144 1.00 70.74  ? 125 PHE A CD1 1 
ATOM   1065  C  CD2 . PHE A  1 134 ? 21.406  -42.310 27.257 1.00 69.16  ? 125 PHE A CD2 1 
ATOM   1066  C  CE1 . PHE A  1 134 ? 23.408  -43.481 25.744 1.00 67.40  ? 125 PHE A CE1 1 
ATOM   1067  C  CE2 . PHE A  1 134 ? 22.370  -43.101 27.876 1.00 70.78  ? 125 PHE A CE2 1 
ATOM   1068  C  CZ  . PHE A  1 134 ? 23.374  -43.684 27.111 1.00 73.20  ? 125 PHE A CZ  1 
ATOM   1069  N  N   . MET A  1 135 ? 19.867  -43.018 22.829 1.00 64.90  ? 126 MET A N   1 
ATOM   1070  C  CA  . MET A  1 135 ? 19.982  -44.104 21.850 1.00 61.74  ? 126 MET A CA  1 
ATOM   1071  C  C   . MET A  1 135 ? 21.172  -44.997 22.165 1.00 62.95  ? 126 MET A C   1 
ATOM   1072  O  O   . MET A  1 135 ? 22.323  -44.565 22.074 1.00 62.46  ? 126 MET A O   1 
ATOM   1073  C  CB  . MET A  1 135 ? 20.193  -43.531 20.455 1.00 49.77  ? 126 MET A CB  1 
ATOM   1074  C  CG  . MET A  1 135 ? 18.999  -42.846 19.863 1.00 50.68  ? 126 MET A CG  1 
ATOM   1075  S  SD  . MET A  1 135 ? 19.540  -41.663 18.624 1.00 58.53  ? 126 MET A SD  1 
ATOM   1076  C  CE  . MET A  1 135 ? 18.158  -40.540 18.647 1.00 51.46  ? 126 MET A CE  1 
ATOM   1077  N  N   . CYS A  1 136 ? 20.892  -46.259 22.468 1.00 54.38  ? 127 CYS A N   1 
ATOM   1078  C  CA  . CYS A  1 136 ? 21.944  -47.209 22.763 1.00 61.05  ? 127 CYS A CA  1 
ATOM   1079  C  C   . CYS A  1 136 ? 21.560  -48.641 22.420 1.00 72.15  ? 127 CYS A C   1 
ATOM   1080  O  O   . CYS A  1 136 ? 20.405  -49.038 22.577 1.00 72.77  ? 127 CYS A O   1 
ATOM   1081  C  CB  . CYS A  1 136 ? 22.336  -47.112 24.233 1.00 73.88  ? 127 CYS A CB  1 
ATOM   1082  S  SG  . CYS A  1 136 ? 23.104  -48.582 24.915 1.00 70.72  ? 127 CYS A SG  1 
ATOM   1083  N  N   . ASP A  1 137 ? 22.542  -49.417 21.967 1.00 78.75  ? 128 ASP A N   1 
ATOM   1084  C  CA  . ASP A  1 137 ? 22.358  -50.849 21.767 1.00 71.02  ? 128 ASP A CA  1 
ATOM   1085  C  C   . ASP A  1 137 ? 22.920  -51.668 22.930 1.00 76.48  ? 128 ASP A C   1 
ATOM   1086  O  O   . ASP A  1 137 ? 24.140  -51.798 23.084 1.00 74.84  ? 128 ASP A O   1 
ATOM   1087  C  CB  . ASP A  1 137 ? 23.020  -51.290 20.478 1.00 75.54  ? 128 ASP A CB  1 
ATOM   1088  C  CG  . ASP A  1 137 ? 22.551  -52.655 20.036 1.00 79.96  ? 128 ASP A CG  1 
ATOM   1089  O  OD1 . ASP A  1 137 ? 21.456  -53.069 20.470 1.00 78.26  ? 128 ASP A OD1 1 
ATOM   1090  O  OD2 . ASP A  1 137 ? 23.265  -53.313 19.253 1.00 84.51  ? 128 ASP A OD2 1 
ATOM   1091  N  N   . PRO A  1 138 ? 22.019  -52.252 23.730 1.00 71.83  ? 129 PRO A N   1 
ATOM   1092  C  CA  . PRO A  1 138 ? 22.317  -52.996 24.950 1.00 63.62  ? 129 PRO A CA  1 
ATOM   1093  C  C   . PRO A  1 138 ? 23.120  -54.274 24.692 1.00 80.69  ? 129 PRO A C   1 
ATOM   1094  O  O   . PRO A  1 138 ? 23.768  -54.766 25.619 1.00 79.61  ? 129 PRO A O   1 
ATOM   1095  C  CB  . PRO A  1 138 ? 20.926  -53.384 25.468 1.00 65.06  ? 129 PRO A CB  1 
ATOM   1096  C  CG  . PRO A  1 138 ? 19.957  -52.588 24.718 1.00 63.92  ? 129 PRO A CG  1 
ATOM   1097  C  CD  . PRO A  1 138 ? 20.583  -52.267 23.416 1.00 74.84  ? 129 PRO A CD  1 
ATOM   1098  N  N   . THR A  1 139 ? 23.072  -54.812 23.472 1.00 79.35  ? 130 THR A N   1 
ATOM   1099  C  CA  . THR A  1 139 ? 23.612  -56.154 23.222 1.00 84.50  ? 130 THR A CA  1 
ATOM   1100  C  C   . THR A  1 139 ? 25.074  -56.322 23.647 1.00 83.58  ? 130 THR A C   1 
ATOM   1101  O  O   . THR A  1 139 ? 25.950  -55.541 23.260 1.00 75.27  ? 130 THR A O   1 
ATOM   1102  C  CB  . THR A  1 139 ? 23.424  -56.611 21.755 1.00 80.27  ? 130 THR A CB  1 
ATOM   1103  O  OG1 . THR A  1 139 ? 24.244  -55.816 20.894 1.00 81.74  ? 130 THR A OG1 1 
ATOM   1104  C  CG2 . THR A  1 139 ? 21.963  -56.496 21.340 1.00 75.29  ? 130 THR A CG2 1 
ATOM   1105  N  N   . GLY A  1 140 ? 25.320  -57.381 24.417 1.00 81.11  ? 131 GLY A N   1 
ATOM   1106  C  CA  . GLY A  1 140 ? 26.605  -57.610 25.049 1.00 76.88  ? 131 GLY A CA  1 
ATOM   1107  C  C   . GLY A  1 140 ? 26.520  -57.389 26.545 1.00 78.00  ? 131 GLY A C   1 
ATOM   1108  O  O   . GLY A  1 140 ? 27.420  -57.754 27.293 1.00 82.20  ? 131 GLY A O   1 
ATOM   1109  N  N   . VAL A  1 141 ? 25.417  -56.799 26.985 1.00 78.32  ? 132 VAL A N   1 
ATOM   1110  C  CA  . VAL A  1 141 ? 25.246  -56.449 28.384 1.00 76.32  ? 132 VAL A CA  1 
ATOM   1111  C  C   . VAL A  1 141 ? 25.086  -57.693 29.266 1.00 76.53  ? 132 VAL A C   1 
ATOM   1112  O  O   . VAL A  1 141 ? 25.318  -57.641 30.477 1.00 73.15  ? 132 VAL A O   1 
ATOM   1113  C  CB  . VAL A  1 141 ? 24.074  -55.449 28.571 1.00 69.70  ? 132 VAL A CB  1 
ATOM   1114  C  CG1 . VAL A  1 141 ? 22.741  -56.069 28.175 1.00 63.62  ? 132 VAL A CG1 1 
ATOM   1115  C  CG2 . VAL A  1 141 ? 24.034  -54.945 29.992 1.00 71.22  ? 132 VAL A CG2 1 
ATOM   1116  N  N   . ASP A  1 142 ? 24.690  -58.803 28.641 1.00 78.68  ? 133 ASP A N   1 
ATOM   1117  C  CA  . ASP A  1 142 ? 24.581  -60.121 29.295 1.00 85.17  ? 133 ASP A CA  1 
ATOM   1118  C  C   . ASP A  1 142 ? 25.831  -60.999 29.110 1.00 83.61  ? 133 ASP A C   1 
ATOM   1119  O  O   . ASP A  1 142 ? 25.843  -62.174 29.478 1.00 78.02  ? 133 ASP A O   1 
ATOM   1120  C  CB  . ASP A  1 142 ? 23.333  -60.873 28.817 1.00 80.23  ? 133 ASP A CB  1 
ATOM   1121  C  CG  . ASP A  1 142 ? 23.318  -61.090 27.312 1.00 81.82  ? 133 ASP A CG  1 
ATOM   1122  O  OD1 . ASP A  1 142 ? 23.978  -60.321 26.578 1.00 77.39  ? 133 ASP A OD1 1 
ATOM   1123  O  OD2 . ASP A  1 142 ? 22.635  -62.033 26.862 1.00 84.41  ? 133 ASP A OD2 1 
ATOM   1124  N  N   . SER A  1 143 ? 26.856  -60.429 28.485 1.00 86.79  ? 134 SER A N   1 
ATOM   1125  C  CA  . SER A  1 143 ? 28.115  -61.117 28.256 1.00 80.86  ? 134 SER A CA  1 
ATOM   1126  C  C   . SER A  1 143 ? 29.111  -60.714 29.312 1.00 83.20  ? 134 SER A C   1 
ATOM   1127  O  O   . SER A  1 143 ? 28.805  -59.943 30.214 1.00 82.22  ? 134 SER A O   1 
ATOM   1128  C  CB  . SER A  1 143 ? 28.704  -60.712 26.907 1.00 81.60  ? 134 SER A CB  1 
ATOM   1129  O  OG  . SER A  1 143 ? 29.739  -59.755 27.088 1.00 77.74  ? 134 SER A OG  1 
ATOM   1130  N  N   . GLU A  1 144 ? 30.321  -61.230 29.167 1.00 87.17  ? 135 GLU A N   1 
ATOM   1131  C  CA  . GLU A  1 144 ? 31.445  -60.817 29.984 1.00 89.53  ? 135 GLU A CA  1 
ATOM   1132  C  C   . GLU A  1 144 ? 31.917  -59.460 29.480 1.00 88.25  ? 135 GLU A C   1 
ATOM   1133  O  O   . GLU A  1 144 ? 31.963  -58.498 30.238 1.00 93.77  ? 135 GLU A O   1 
ATOM   1134  C  CB  . GLU A  1 144 ? 32.574  -61.854 29.971 1.00 94.77  ? 135 GLU A CB  1 
ATOM   1135  C  CG  . GLU A  1 144 ? 33.457  -61.831 31.220 1.00 88.61  ? 135 GLU A CG  1 
ATOM   1136  C  CD  . GLU A  1 144 ? 32.780  -62.442 32.446 1.00 96.62  ? 135 GLU A CD  1 
ATOM   1137  O  OE1 . GLU A  1 144 ? 31.556  -62.255 32.631 1.00 93.74  ? 135 GLU A OE1 1 
ATOM   1138  O  OE2 . GLU A  1 144 ? 33.478  -63.121 33.229 1.00 98.93  ? 135 GLU A OE2 1 
ATOM   1139  N  N   . GLU A  1 145 ? 32.325  -59.404 28.216 1.00 82.68  ? 136 GLU A N   1 
ATOM   1140  C  CA  . GLU A  1 145 ? 32.805  -58.163 27.613 1.00 85.40  ? 136 GLU A CA  1 
ATOM   1141  C  C   . GLU A  1 145 ? 31.865  -56.981 27.870 1.00 86.62  ? 136 GLU A C   1 
ATOM   1142  O  O   . GLU A  1 145 ? 32.325  -55.874 28.133 1.00 87.92  ? 136 GLU A O   1 
ATOM   1143  C  CB  . GLU A  1 145 ? 33.044  -58.334 26.103 1.00 86.45  ? 136 GLU A CB  1 
ATOM   1144  C  CG  . GLU A  1 145 ? 34.176  -59.295 25.726 1.00 90.83  ? 136 GLU A CG  1 
ATOM   1145  C  CD  . GLU A  1 145 ? 33.839  -60.763 25.999 1.00 95.34  ? 136 GLU A CD  1 
ATOM   1146  O  OE1 . GLU A  1 145 ? 32.673  -61.063 26.339 1.00 90.90  ? 136 GLU A OE1 1 
ATOM   1147  O  OE2 . GLU A  1 145 ? 34.743  -61.619 25.875 1.00 86.45  ? 136 GLU A OE2 1 
ATOM   1148  N  N   . GLY A  1 146 ? 30.556  -57.204 27.792 1.00 84.57  ? 137 GLY A N   1 
ATOM   1149  C  CA  . GLY A  1 146 ? 29.600  -56.134 28.037 1.00 76.67  ? 137 GLY A CA  1 
ATOM   1150  C  C   . GLY A  1 146 ? 29.254  -55.249 26.843 1.00 79.82  ? 137 GLY A C   1 
ATOM   1151  O  O   . GLY A  1 146 ? 29.986  -55.183 25.851 1.00 75.83  ? 137 GLY A O   1 
ATOM   1152  N  N   . ALA A  1 147 ? 28.114  -54.572 26.942 1.00 80.08  ? 138 ALA A N   1 
ATOM   1153  C  CA  . ALA A  1 147 ? 27.676  -53.616 25.923 1.00 79.98  ? 138 ALA A CA  1 
ATOM   1154  C  C   . ALA A  1 147 ? 28.453  -52.298 25.975 1.00 77.29  ? 138 ALA A C   1 
ATOM   1155  O  O   . ALA A  1 147 ? 29.086  -51.977 26.985 1.00 74.29  ? 138 ALA A O   1 
ATOM   1156  C  CB  . ALA A  1 147 ? 26.183  -53.354 26.042 1.00 73.51  ? 138 ALA A CB  1 
ATOM   1157  N  N   . THR A  1 148 ? 28.419  -51.549 24.875 1.00 70.92  ? 139 THR A N   1 
ATOM   1158  C  CA  . THR A  1 148 ? 28.999  -50.209 24.849 1.00 73.43  ? 139 THR A CA  1 
ATOM   1159  C  C   . THR A  1 148 ? 28.055  -49.197 24.220 1.00 63.82  ? 139 THR A C   1 
ATOM   1160  O  O   . THR A  1 148 ? 27.439  -49.469 23.195 1.00 71.67  ? 139 THR A O   1 
ATOM   1161  C  CB  . THR A  1 148 ? 30.338  -50.161 24.097 1.00 75.36  ? 139 THR A CB  1 
ATOM   1162  O  OG1 . THR A  1 148 ? 31.245  -51.106 24.677 1.00 89.01  ? 139 THR A OG1 1 
ATOM   1163  C  CG2 . THR A  1 148 ? 30.943  -48.768 24.188 1.00 65.33  ? 139 THR A CG2 1 
ATOM   1164  N  N   . CYS A  1 149 ? 27.942  -48.033 24.847 1.00 70.52  ? 140 CYS A N   1 
ATOM   1165  C  CA  . CYS A  1 149 ? 27.142  -46.927 24.326 1.00 69.42  ? 140 CYS A CA  1 
ATOM   1166  C  C   . CYS A  1 149 ? 27.852  -45.590 24.444 1.00 68.46  ? 140 CYS A C   1 
ATOM   1167  O  O   . CYS A  1 149 ? 28.768  -45.429 25.259 1.00 66.90  ? 140 CYS A O   1 
ATOM   1168  C  CB  . CYS A  1 149 ? 25.806  -46.835 25.046 1.00 69.98  ? 140 CYS A CB  1 
ATOM   1169  S  SG  . CYS A  1 149 ? 24.831  -48.300 24.860 1.00 80.57  ? 140 CYS A SG  1 
ATOM   1170  N  N   . ALA A  1 150 ? 27.423  -44.634 23.630 1.00 59.58  ? 141 ALA A N   1 
ATOM   1171  C  CA  . ALA A  1 150 ? 27.924  -43.274 23.726 1.00 61.10  ? 141 ALA A CA  1 
ATOM   1172  C  C   . ALA A  1 150 ? 26.862  -42.227 23.405 1.00 61.74  ? 141 ALA A C   1 
ATOM   1173  O  O   . ALA A  1 150 ? 25.899  -42.488 22.678 1.00 62.91  ? 141 ALA A O   1 
ATOM   1174  C  CB  . ALA A  1 150 ? 29.142  -43.089 22.858 1.00 59.50  ? 141 ALA A CB  1 
ATOM   1175  N  N   . VAL A  1 151 ? 27.052  -41.048 23.983 1.00 59.93  ? 142 VAL A N   1 
ATOM   1176  C  CA  . VAL A  1 151 ? 26.181  -39.898 23.791 1.00 57.30  ? 142 VAL A CA  1 
ATOM   1177  C  C   . VAL A  1 151 ? 27.077  -38.690 23.641 1.00 61.98  ? 142 VAL A C   1 
ATOM   1178  O  O   . VAL A  1 151 ? 28.048  -38.555 24.380 1.00 65.14  ? 142 VAL A O   1 
ATOM   1179  C  CB  . VAL A  1 151 ? 25.333  -39.597 25.042 1.00 68.86  ? 142 VAL A CB  1 
ATOM   1180  C  CG1 . VAL A  1 151 ? 24.097  -38.811 24.662 1.00 64.44  ? 142 VAL A CG1 1 
ATOM   1181  C  CG2 . VAL A  1 151 ? 24.967  -40.862 25.793 1.00 64.64  ? 142 VAL A CG2 1 
ATOM   1182  N  N   . LYS A  1 152 ? 26.754  -37.799 22.711 1.00 66.79  ? 143 LYS A N   1 
ATOM   1183  C  CA  . LYS A  1 152 ? 27.494  -36.546 22.594 1.00 67.76  ? 143 LYS A CA  1 
ATOM   1184  C  C   . LYS A  1 152 ? 26.744  -35.409 23.299 1.00 62.92  ? 143 LYS A C   1 
ATOM   1185  O  O   . LYS A  1 152 ? 25.516  -35.338 23.246 1.00 63.29  ? 143 LYS A O   1 
ATOM   1186  C  CB  . LYS A  1 152 ? 27.777  -36.217 21.125 1.00 69.61  ? 143 LYS A CB  1 
ATOM   1187  C  CG  . LYS A  1 152 ? 28.978  -36.958 20.552 1.00 75.03  ? 143 LYS A CG  1 
ATOM   1188  C  CD  . LYS A  1 152 ? 28.860  -37.122 19.043 1.00 82.19  ? 143 LYS A CD  1 
ATOM   1189  C  CE  . LYS A  1 152 ? 29.984  -37.975 18.467 1.00 84.55  ? 143 LYS A CE  1 
ATOM   1190  N  NZ  . LYS A  1 152 ? 31.314  -37.338 18.664 1.00 84.40  ? 143 LYS A NZ  1 
ATOM   1191  N  N   . PHE A  1 153 ? 27.485  -34.550 23.993 1.00 56.06  ? 144 PHE A N   1 
ATOM   1192  C  CA  . PHE A  1 153 ? 26.916  -33.357 24.609 1.00 56.88  ? 144 PHE A CA  1 
ATOM   1193  C  C   . PHE A  1 153 ? 27.651  -32.146 24.076 1.00 60.86  ? 144 PHE A C   1 
ATOM   1194  O  O   . PHE A  1 153 ? 28.871  -32.158 23.995 1.00 68.24  ? 144 PHE A O   1 
ATOM   1195  C  CB  . PHE A  1 153 ? 27.097  -33.377 26.125 1.00 58.63  ? 144 PHE A CB  1 
ATOM   1196  C  CG  . PHE A  1 153 ? 26.289  -34.427 26.837 1.00 57.13  ? 144 PHE A CG  1 
ATOM   1197  C  CD1 . PHE A  1 153 ? 25.099  -34.095 27.455 1.00 56.43  ? 144 PHE A CD1 1 
ATOM   1198  C  CD2 . PHE A  1 153 ? 26.740  -35.727 26.923 1.00 55.04  ? 144 PHE A CD2 1 
ATOM   1199  C  CE1 . PHE A  1 153 ? 24.368  -35.039 28.122 1.00 55.33  ? 144 PHE A CE1 1 
ATOM   1200  C  CE2 . PHE A  1 153 ? 26.009  -36.674 27.588 1.00 59.30  ? 144 PHE A CE2 1 
ATOM   1201  C  CZ  . PHE A  1 153 ? 24.820  -36.330 28.188 1.00 55.96  ? 144 PHE A CZ  1 
ATOM   1202  N  N   . GLY A  1 154 ? 26.924  -31.097 23.718 1.00 56.84  ? 145 GLY A N   1 
ATOM   1203  C  CA  . GLY A  1 154 ? 27.559  -29.853 23.333 1.00 56.35  ? 145 GLY A CA  1 
ATOM   1204  C  C   . GLY A  1 154 ? 26.487  -28.797 23.266 1.00 59.04  ? 145 GLY A C   1 
ATOM   1205  O  O   . GLY A  1 154 ? 25.357  -29.047 23.688 1.00 59.07  ? 145 GLY A O   1 
ATOM   1206  N  N   . SER A  1 155 ? 26.815  -27.625 22.733 1.00 55.29  ? 146 SER A N   1 
ATOM   1207  C  CA  . SER A  1 155 ? 25.782  -26.622 22.525 1.00 58.27  ? 146 SER A CA  1 
ATOM   1208  C  C   . SER A  1 155 ? 24.907  -26.976 21.338 1.00 59.72  ? 146 SER A C   1 
ATOM   1209  O  O   . SER A  1 155 ? 25.373  -27.575 20.378 1.00 65.40  ? 146 SER A O   1 
ATOM   1210  C  CB  . SER A  1 155 ? 26.366  -25.234 22.327 1.00 58.06  ? 146 SER A CB  1 
ATOM   1211  O  OG  . SER A  1 155 ? 25.300  -24.306 22.261 1.00 58.16  ? 146 SER A OG  1 
ATOM   1212  N  N   . TRP A  1 156 ? 23.618  -26.680 21.439 1.00 60.04  ? 147 TRP A N   1 
ATOM   1213  C  CA  . TRP A  1 156 ? 22.720  -26.826 20.301 1.00 67.49  ? 147 TRP A CA  1 
ATOM   1214  C  C   . TRP A  1 156 ? 22.820  -25.719 19.242 1.00 66.15  ? 147 TRP A C   1 
ATOM   1215  O  O   . TRP A  1 156 ? 22.992  -26.002 18.066 1.00 70.93  ? 147 TRP A O   1 
ATOM   1216  C  CB  . TRP A  1 156 ? 21.282  -26.939 20.802 1.00 60.55  ? 147 TRP A CB  1 
ATOM   1217  C  CG  . TRP A  1 156 ? 20.298  -27.459 19.809 1.00 60.78  ? 147 TRP A CG  1 
ATOM   1218  C  CD1 . TRP A  1 156 ? 19.249  -26.782 19.267 1.00 61.46  ? 147 TRP A CD1 1 
ATOM   1219  C  CD2 . TRP A  1 156 ? 20.259  -28.770 19.250 1.00 60.94  ? 147 TRP A CD2 1 
ATOM   1220  N  NE1 . TRP A  1 156 ? 18.557  -27.588 18.410 1.00 55.22  ? 147 TRP A NE1 1 
ATOM   1221  C  CE2 . TRP A  1 156 ? 19.156  -28.817 18.384 1.00 58.19  ? 147 TRP A CE2 1 
ATOM   1222  C  CE3 . TRP A  1 156 ? 21.048  -29.911 19.400 1.00 59.93  ? 147 TRP A CE3 1 
ATOM   1223  C  CZ2 . TRP A  1 156 ? 18.822  -29.961 17.678 1.00 57.79  ? 147 TRP A CZ2 1 
ATOM   1224  C  CZ3 . TRP A  1 156 ? 20.715  -31.039 18.695 1.00 56.05  ? 147 TRP A CZ3 1 
ATOM   1225  C  CH2 . TRP A  1 156 ? 19.615  -31.060 17.846 1.00 58.80  ? 147 TRP A CH2 1 
ATOM   1226  N  N   . SER A  1 157 ? 22.660  -24.474 19.659 1.00 62.45  ? 148 SER A N   1 
ATOM   1227  C  CA  . SER A  1 157 ? 22.698  -23.344 18.727 1.00 65.49  ? 148 SER A CA  1 
ATOM   1228  C  C   . SER A  1 157 ? 23.984  -22.529 18.635 1.00 62.75  ? 148 SER A C   1 
ATOM   1229  O  O   . SER A  1 157 ? 24.049  -21.587 17.865 1.00 63.53  ? 148 SER A O   1 
ATOM   1230  C  CB  . SER A  1 157 ? 21.468  -22.420 18.874 1.00 69.09  ? 148 SER A CB  1 
ATOM   1231  O  OG  . SER A  1 157 ? 21.039  -22.270 20.214 1.00 76.78  ? 148 SER A OG  1 
ATOM   1232  N  N   . TYR A  1 158 ? 25.000  -22.852 19.429 1.00 68.84  ? 149 TYR A N   1 
ATOM   1233  C  CA  . TYR A  1 158 ? 26.241  -22.077 19.413 1.00 62.90  ? 149 TYR A CA  1 
ATOM   1234  C  C   . TYR A  1 158 ? 27.361  -22.912 18.822 1.00 70.80  ? 149 TYR A C   1 
ATOM   1235  O  O   . TYR A  1 158 ? 27.347  -24.144 18.897 1.00 76.53  ? 149 TYR A O   1 
ATOM   1236  C  CB  . TYR A  1 158 ? 26.649  -21.618 20.812 1.00 56.24  ? 149 TYR A CB  1 
ATOM   1237  C  CG  . TYR A  1 158 ? 25.834  -20.491 21.406 1.00 64.09  ? 149 TYR A CG  1 
ATOM   1238  C  CD1 . TYR A  1 158 ? 26.163  -19.161 21.155 1.00 68.91  ? 149 TYR A CD1 1 
ATOM   1239  C  CD2 . TYR A  1 158 ? 24.754  -20.749 22.247 1.00 61.41  ? 149 TYR A CD2 1 
ATOM   1240  C  CE1 . TYR A  1 158 ? 25.426  -18.109 21.710 1.00 66.61  ? 149 TYR A CE1 1 
ATOM   1241  C  CE2 . TYR A  1 158 ? 24.011  -19.713 22.807 1.00 66.63  ? 149 TYR A CE2 1 
ATOM   1242  C  CZ  . TYR A  1 158 ? 24.352  -18.388 22.537 1.00 71.14  ? 149 TYR A CZ  1 
ATOM   1243  O  OH  . TYR A  1 158 ? 23.624  -17.345 23.088 1.00 64.13  ? 149 TYR A OH  1 
ATOM   1244  N  N   . GLY A  1 159 ? 28.328  -22.243 18.218 1.00 64.38  ? 150 GLY A N   1 
ATOM   1245  C  CA  . GLY A  1 159 ? 29.459  -22.942 17.650 1.00 69.76  ? 150 GLY A CA  1 
ATOM   1246  C  C   . GLY A  1 159 ? 30.676  -22.777 18.523 1.00 67.55  ? 150 GLY A C   1 
ATOM   1247  O  O   . GLY A  1 159 ? 30.617  -22.079 19.529 1.00 68.71  ? 150 GLY A O   1 
ATOM   1248  N  N   . GLY A  1 160 ? 31.777  -23.411 18.129 1.00 72.30  ? 151 GLY A N   1 
ATOM   1249  C  CA  . GLY A  1 160 ? 33.034  -23.335 18.856 1.00 73.80  ? 151 GLY A CA  1 
ATOM   1250  C  C   . GLY A  1 160 ? 33.657  -21.954 18.987 1.00 70.61  ? 151 GLY A C   1 
ATOM   1251  O  O   . GLY A  1 160 ? 34.456  -21.725 19.900 1.00 65.12  ? 151 GLY A O   1 
ATOM   1252  N  N   . TRP A  1 161 ? 33.302  -21.046 18.077 1.00 70.80  ? 152 TRP A N   1 
ATOM   1253  C  CA  . TRP A  1 161 ? 33.775  -19.659 18.112 1.00 72.93  ? 152 TRP A CA  1 
ATOM   1254  C  C   . TRP A  1 161 ? 33.004  -18.793 19.109 1.00 71.70  ? 152 TRP A C   1 
ATOM   1255  O  O   . TRP A  1 161 ? 33.456  -17.718 19.489 1.00 75.38  ? 152 TRP A O   1 
ATOM   1256  C  CB  . TRP A  1 161 ? 33.686  -19.015 16.725 1.00 82.38  ? 152 TRP A CB  1 
ATOM   1257  C  CG  . TRP A  1 161 ? 34.761  -19.428 15.763 1.00 89.83  ? 152 TRP A CG  1 
ATOM   1258  C  CD1 . TRP A  1 161 ? 35.989  -19.946 16.069 1.00 92.46  ? 152 TRP A CD1 1 
ATOM   1259  C  CD2 . TRP A  1 161 ? 34.700  -19.361 14.334 1.00 86.20  ? 152 TRP A CD2 1 
ATOM   1260  N  NE1 . TRP A  1 161 ? 36.694  -20.202 14.918 1.00 98.45  ? 152 TRP A NE1 1 
ATOM   1261  C  CE2 . TRP A  1 161 ? 35.923  -19.855 13.837 1.00 88.61  ? 152 TRP A CE2 1 
ATOM   1262  C  CE3 . TRP A  1 161 ? 33.726  -18.935 13.425 1.00 88.93  ? 152 TRP A CE3 1 
ATOM   1263  C  CZ2 . TRP A  1 161 ? 36.200  -19.941 12.477 1.00 89.85  ? 152 TRP A CZ2 1 
ATOM   1264  C  CZ3 . TRP A  1 161 ? 34.002  -19.019 12.071 1.00 100.26 ? 152 TRP A CZ3 1 
ATOM   1265  C  CH2 . TRP A  1 161 ? 35.230  -19.518 11.611 1.00 98.03  ? 152 TRP A CH2 1 
ATOM   1266  N  N   . GLU A  1 162 ? 31.827  -19.255 19.509 1.00 74.64  ? 153 GLU A N   1 
ATOM   1267  C  CA  . GLU A  1 162 ? 31.036  -18.588 20.541 1.00 72.13  ? 153 GLU A CA  1 
ATOM   1268  C  C   . GLU A  1 162 ? 31.019  -19.258 21.911 1.00 67.63  ? 153 GLU A C   1 
ATOM   1269  O  O   . GLU A  1 162 ? 31.135  -18.595 22.936 1.00 64.18  ? 153 GLU A O   1 
ATOM   1270  C  CB  . GLU A  1 162 ? 29.557  -18.541 20.169 1.00 71.54  ? 153 GLU A CB  1 
ATOM   1271  C  CG  . GLU A  1 162 ? 29.217  -17.622 19.010 1.00 72.70  ? 153 GLU A CG  1 
ATOM   1272  C  CD  . GLU A  1 162 ? 29.393  -18.279 17.654 1.00 77.11  ? 153 GLU A CD  1 
ATOM   1273  O  OE1 . GLU A  1 162 ? 29.073  -19.480 17.511 1.00 70.00  ? 153 GLU A OE1 1 
ATOM   1274  O  OE2 . GLU A  1 162 ? 29.848  -17.580 16.724 1.00 85.60  ? 153 GLU A OE2 1 
ATOM   1275  N  N   . ILE A  1 163 ? 30.814  -20.573 21.908 1.00 65.77  ? 154 ILE A N   1 
ATOM   1276  C  CA  . ILE A  1 163 ? 30.976  -21.426 23.087 1.00 69.56  ? 154 ILE A CA  1 
ATOM   1277  C  C   . ILE A  1 163 ? 32.012  -22.545 22.889 1.00 69.46  ? 154 ILE A C   1 
ATOM   1278  O  O   . ILE A  1 163 ? 31.829  -23.433 22.056 1.00 62.16  ? 154 ILE A O   1 
ATOM   1279  C  CB  . ILE A  1 163 ? 29.629  -22.075 23.508 1.00 69.27  ? 154 ILE A CB  1 
ATOM   1280  C  CG1 . ILE A  1 163 ? 28.671  -21.027 24.082 1.00 64.48  ? 154 ILE A CG1 1 
ATOM   1281  C  CG2 . ILE A  1 163 ? 29.860  -23.178 24.526 1.00 70.71  ? 154 ILE A CG2 1 
ATOM   1282  C  CD1 . ILE A  1 163 ? 27.328  -21.585 24.498 1.00 61.06  ? 154 ILE A CD1 1 
ATOM   1283  N  N   . ASP A  1 164 ? 33.088  -22.508 23.673 1.00 70.72  ? 155 ASP A N   1 
ATOM   1284  C  CA  . ASP A  1 164 ? 34.089  -23.568 23.633 1.00 70.24  ? 155 ASP A CA  1 
ATOM   1285  C  C   . ASP A  1 164 ? 33.885  -24.594 24.749 1.00 69.54  ? 155 ASP A C   1 
ATOM   1286  O  O   . ASP A  1 164 ? 33.724  -24.237 25.907 1.00 66.50  ? 155 ASP A O   1 
ATOM   1287  C  CB  . ASP A  1 164 ? 35.501  -22.988 23.711 1.00 68.46  ? 155 ASP A CB  1 
ATOM   1288  C  CG  . ASP A  1 164 ? 36.571  -24.035 23.451 1.00 78.68  ? 155 ASP A CG  1 
ATOM   1289  O  OD1 . ASP A  1 164 ? 36.273  -25.047 22.766 1.00 67.58  ? 155 ASP A OD1 1 
ATOM   1290  O  OD2 . ASP A  1 164 ? 37.711  -23.839 23.934 1.00 78.59  ? 155 ASP A OD2 1 
ATOM   1291  N  N   . LEU A  1 165 ? 33.897  -25.873 24.390 1.00 71.68  ? 156 LEU A N   1 
ATOM   1292  C  CA  . LEU A  1 165 ? 33.744  -26.950 25.359 1.00 68.13  ? 156 LEU A CA  1 
ATOM   1293  C  C   . LEU A  1 165 ? 35.086  -27.468 25.824 1.00 73.39  ? 156 LEU A C   1 
ATOM   1294  O  O   . LEU A  1 165 ? 36.031  -27.567 25.043 1.00 81.17  ? 156 LEU A O   1 
ATOM   1295  C  CB  . LEU A  1 165 ? 32.958  -28.107 24.763 1.00 60.26  ? 156 LEU A CB  1 
ATOM   1296  C  CG  . LEU A  1 165 ? 31.471  -27.995 25.025 1.00 57.18  ? 156 LEU A CG  1 
ATOM   1297  C  CD1 . LEU A  1 165 ? 30.821  -29.312 24.757 1.00 55.32  ? 156 LEU A CD1 1 
ATOM   1298  C  CD2 . LEU A  1 165 ? 31.267  -27.596 26.459 1.00 61.19  ? 156 LEU A CD2 1 
ATOM   1299  N  N   . LYS A  1 166 ? 35.171  -27.803 27.101 1.00 66.14  ? 157 LYS A N   1 
ATOM   1300  C  CA  . LYS A  1 166 ? 36.389  -28.374 27.638 1.00 76.16  ? 157 LYS A CA  1 
ATOM   1301  C  C   . LYS A  1 166 ? 36.075  -29.296 28.792 1.00 79.77  ? 157 LYS A C   1 
ATOM   1302  O  O   . LYS A  1 166 ? 35.036  -29.178 29.438 1.00 75.08  ? 157 LYS A O   1 
ATOM   1303  C  CB  . LYS A  1 166 ? 37.387  -27.288 28.063 1.00 75.41  ? 157 LYS A CB  1 
ATOM   1304  C  CG  . LYS A  1 166 ? 38.302  -26.826 26.925 1.00 80.70  ? 157 LYS A CG  1 
ATOM   1305  C  CD  . LYS A  1 166 ? 39.164  -25.628 27.320 1.00 85.46  ? 157 LYS A CD  1 
ATOM   1306  C  CE  . LYS A  1 166 ? 39.815  -24.981 26.089 1.00 89.58  ? 157 LYS A CE  1 
ATOM   1307  N  NZ  . LYS A  1 166 ? 39.783  -23.483 26.156 1.00 73.79  ? 157 LYS A NZ  1 
ATOM   1308  N  N   . THR A  1 167 ? 36.976  -30.238 29.023 1.00 86.85  ? 158 THR A N   1 
ATOM   1309  C  CA  . THR A  1 167 ? 36.857  -31.141 30.149 1.00 83.25  ? 158 THR A CA  1 
ATOM   1310  C  C   . THR A  1 167 ? 38.052  -31.005 31.091 1.00 81.07  ? 158 THR A C   1 
ATOM   1311  O  O   . THR A  1 167 ? 39.171  -30.682 30.685 1.00 79.10  ? 158 THR A O   1 
ATOM   1312  C  CB  . THR A  1 167 ? 36.681  -32.613 29.698 1.00 88.35  ? 158 THR A CB  1 
ATOM   1313  O  OG1 . THR A  1 167 ? 37.570  -32.899 28.613 1.00 94.47  ? 158 THR A OG1 1 
ATOM   1314  C  CG2 . THR A  1 167 ? 35.249  -32.877 29.249 1.00 74.14  ? 158 THR A CG2 1 
ATOM   1315  N  N   . ASP A  1 168 ? 37.779  -31.233 32.364 1.00 85.71  ? 159 ASP A N   1 
ATOM   1316  C  CA  . ASP A  1 168 ? 38.789  -31.190 33.395 1.00 86.61  ? 159 ASP A CA  1 
ATOM   1317  C  C   . ASP A  1 168 ? 39.700  -32.389 33.223 1.00 91.36  ? 159 ASP A C   1 
ATOM   1318  O  O   . ASP A  1 168 ? 40.921  -32.252 33.155 1.00 90.22  ? 159 ASP A O   1 
ATOM   1319  C  CB  . ASP A  1 168 ? 38.088  -31.252 34.743 1.00 93.13  ? 159 ASP A CB  1 
ATOM   1320  C  CG  . ASP A  1 168 ? 37.003  -30.188 34.883 1.00 98.68  ? 159 ASP A CG  1 
ATOM   1321  O  OD1 . ASP A  1 168 ? 37.199  -29.072 34.350 1.00 99.08  ? 159 ASP A OD1 1 
ATOM   1322  O  OD2 . ASP A  1 168 ? 35.955  -30.454 35.516 1.00 93.70  ? 159 ASP A OD2 1 
ATOM   1323  N  N   . THR A  1 169 ? 39.078  -33.563 33.145 1.00 91.13  ? 160 THR A N   1 
ATOM   1324  C  CA  . THR A  1 169 ? 39.757  -34.829 32.910 1.00 84.60  ? 160 THR A CA  1 
ATOM   1325  C  C   . THR A  1 169 ? 38.975  -35.614 31.861 1.00 78.32  ? 160 THR A C   1 
ATOM   1326  O  O   . THR A  1 169 ? 37.837  -35.266 31.548 1.00 79.85  ? 160 THR A O   1 
ATOM   1327  C  CB  . THR A  1 169 ? 39.806  -35.660 34.199 1.00 83.67  ? 160 THR A CB  1 
ATOM   1328  O  OG1 . THR A  1 169 ? 40.276  -36.982 33.907 1.00 80.13  ? 160 THR A OG1 1 
ATOM   1329  C  CG2 . THR A  1 169 ? 38.416  -35.756 34.811 1.00 79.92  ? 160 THR A CG2 1 
ATOM   1330  N  N   . ASP A  1 170 ? 39.591  -36.665 31.322 1.00 79.76  ? 161 ASP A N   1 
ATOM   1331  C  CA  . ASP A  1 170 ? 38.918  -37.628 30.430 1.00 84.37  ? 161 ASP A CA  1 
ATOM   1332  C  C   . ASP A  1 170 ? 38.221  -38.760 31.204 1.00 83.94  ? 161 ASP A C   1 
ATOM   1333  O  O   . ASP A  1 170 ? 37.689  -39.711 30.608 1.00 69.52  ? 161 ASP A O   1 
ATOM   1334  C  CB  . ASP A  1 170 ? 39.901  -38.227 29.415 1.00 80.00  ? 161 ASP A CB  1 
ATOM   1335  C  CG  . ASP A  1 170 ? 40.182  -37.296 28.240 1.00 89.62  ? 161 ASP A CG  1 
ATOM   1336  O  OD1 . ASP A  1 170 ? 40.186  -36.054 28.425 1.00 84.07  ? 161 ASP A OD1 1 
ATOM   1337  O  OD2 . ASP A  1 170 ? 40.399  -37.821 27.124 1.00 91.96  ? 161 ASP A OD2 1 
ATOM   1338  N  N   . GLN A  1 171 ? 38.273  -38.656 32.535 1.00 87.17  ? 162 GLN A N   1 
ATOM   1339  C  CA  . GLN A  1 171 ? 37.754  -39.673 33.447 1.00 79.87  ? 162 GLN A CA  1 
ATOM   1340  C  C   . GLN A  1 171 ? 36.416  -39.309 34.085 1.00 75.35  ? 162 GLN A C   1 
ATOM   1341  O  O   . GLN A  1 171 ? 36.343  -38.421 34.946 1.00 79.39  ? 162 GLN A O   1 
ATOM   1342  C  CB  . GLN A  1 171 ? 38.780  -39.936 34.552 1.00 87.06  ? 162 GLN A CB  1 
ATOM   1343  C  CG  . GLN A  1 171 ? 39.903  -40.859 34.129 1.00 91.99  ? 162 GLN A CG  1 
ATOM   1344  C  CD  . GLN A  1 171 ? 39.388  -42.229 33.736 1.00 101.93 ? 162 GLN A CD  1 
ATOM   1345  O  OE1 . GLN A  1 171 ? 38.189  -42.504 33.822 1.00 103.07 ? 162 GLN A OE1 1 
ATOM   1346  N  NE2 . GLN A  1 171 ? 40.291  -43.099 33.302 1.00 103.65 ? 162 GLN A NE2 1 
ATOM   1347  N  N   . VAL A  1 172 ? 35.367  -40.019 33.673 1.00 69.57  ? 163 VAL A N   1 
ATOM   1348  C  CA  . VAL A  1 172 ? 34.044  -39.851 34.258 1.00 67.33  ? 163 VAL A CA  1 
ATOM   1349  C  C   . VAL A  1 172 ? 34.118  -40.313 35.690 1.00 68.43  ? 163 VAL A C   1 
ATOM   1350  O  O   . VAL A  1 172 ? 34.764  -41.325 35.977 1.00 66.78  ? 163 VAL A O   1 
ATOM   1351  C  CB  . VAL A  1 172 ? 32.999  -40.696 33.532 1.00 60.42  ? 163 VAL A CB  1 
ATOM   1352  C  CG1 . VAL A  1 172 ? 31.671  -40.665 34.272 1.00 55.11  ? 163 VAL A CG1 1 
ATOM   1353  C  CG2 . VAL A  1 172 ? 32.847  -40.207 32.122 1.00 60.57  ? 163 VAL A CG2 1 
ATOM   1354  N  N   . ASP A  1 173 ? 33.447  -39.589 36.582 1.00 58.62  ? 164 ASP A N   1 
ATOM   1355  C  CA  . ASP A  1 173 ? 33.496  -39.913 37.997 1.00 56.78  ? 164 ASP A CA  1 
ATOM   1356  C  C   . ASP A  1 173 ? 32.477  -40.994 38.381 1.00 65.60  ? 164 ASP A C   1 
ATOM   1357  O  O   . ASP A  1 173 ? 31.267  -40.816 38.253 1.00 62.67  ? 164 ASP A O   1 
ATOM   1358  C  CB  . ASP A  1 173 ? 33.241  -38.649 38.811 1.00 55.58  ? 164 ASP A CB  1 
ATOM   1359  C  CG  . ASP A  1 173 ? 33.397  -38.866 40.288 1.00 60.78  ? 164 ASP A CG  1 
ATOM   1360  O  OD1 . ASP A  1 173 ? 33.736  -39.988 40.713 1.00 65.97  ? 164 ASP A OD1 1 
ATOM   1361  O  OD2 . ASP A  1 173 ? 33.195  -37.901 41.032 1.00 61.62  ? 164 ASP A OD2 1 
ATOM   1362  N  N   . LEU A  1 174 ? 33.007  -42.134 38.823 1.00 68.30  ? 165 LEU A N   1 
ATOM   1363  C  CA  . LEU A  1 174 ? 32.206  -43.259 39.294 1.00 62.16  ? 165 LEU A CA  1 
ATOM   1364  C  C   . LEU A  1 174 ? 32.083  -43.381 40.814 1.00 57.24  ? 165 LEU A C   1 
ATOM   1365  O  O   . LEU A  1 174 ? 31.486  -44.332 41.326 1.00 52.02  ? 165 LEU A O   1 
ATOM   1366  C  CB  . LEU A  1 174 ? 32.709  -44.550 38.664 1.00 55.40  ? 165 LEU A CB  1 
ATOM   1367  C  CG  . LEU A  1 174 ? 32.867  -44.379 37.161 1.00 57.19  ? 165 LEU A CG  1 
ATOM   1368  C  CD1 . LEU A  1 174 ? 33.396  -45.637 36.566 1.00 64.53  ? 165 LEU A CD1 1 
ATOM   1369  C  CD2 . LEU A  1 174 ? 31.543  -44.033 36.545 1.00 62.65  ? 165 LEU A CD2 1 
ATOM   1370  N  N   . SER A  1 175 ? 32.676  -42.446 41.542 1.00 55.16  ? 166 SER A N   1 
ATOM   1371  C  CA  . SER A  1 175 ? 32.748  -42.603 42.993 1.00 57.30  ? 166 SER A CA  1 
ATOM   1372  C  C   . SER A  1 175 ? 31.380  -42.611 43.669 1.00 56.64  ? 166 SER A C   1 
ATOM   1373  O  O   . SER A  1 175 ? 31.235  -43.137 44.757 1.00 58.06  ? 166 SER A O   1 
ATOM   1374  C  CB  . SER A  1 175 ? 33.646  -41.546 43.619 1.00 53.82  ? 166 SER A CB  1 
ATOM   1375  O  OG  . SER A  1 175 ? 33.097  -40.257 43.458 1.00 63.03  ? 166 SER A OG  1 
ATOM   1376  N  N   . SER A  1 176 ? 30.391  -41.999 43.031 1.00 65.87  ? 167 SER A N   1 
ATOM   1377  C  CA  . SER A  1 176 ? 29.017  -41.977 43.530 1.00 56.82  ? 167 SER A CA  1 
ATOM   1378  C  C   . SER A  1 176 ? 28.099  -43.041 42.924 1.00 59.76  ? 167 SER A C   1 
ATOM   1379  O  O   . SER A  1 176 ? 26.885  -42.999 43.123 1.00 59.66  ? 167 SER A O   1 
ATOM   1380  C  CB  . SER A  1 176 ? 28.412  -40.587 43.377 1.00 65.67  ? 167 SER A CB  1 
ATOM   1381  O  OG  . SER A  1 176 ? 29.114  -39.657 44.180 1.00 68.00  ? 167 SER A OG  1 
ATOM   1382  N  N   . TYR A  1 177 ? 28.663  -43.941 42.124 1.00 57.04  ? 168 TYR A N   1 
ATOM   1383  C  CA  . TYR A  1 177 ? 27.845  -44.902 41.384 1.00 57.14  ? 168 TYR A CA  1 
ATOM   1384  C  C   . TYR A  1 177 ? 27.220  -45.985 42.259 1.00 56.25  ? 168 TYR A C   1 
ATOM   1385  O  O   . TYR A  1 177 ? 27.904  -46.637 43.040 1.00 61.39  ? 168 TYR A O   1 
ATOM   1386  C  CB  . TYR A  1 177 ? 28.623  -45.534 40.227 1.00 51.73  ? 168 TYR A CB  1 
ATOM   1387  C  CG  . TYR A  1 177 ? 27.736  -46.366 39.352 1.00 49.65  ? 168 TYR A CG  1 
ATOM   1388  C  CD1 . TYR A  1 177 ? 27.083  -45.801 38.260 1.00 48.99  ? 168 TYR A CD1 1 
ATOM   1389  C  CD2 . TYR A  1 177 ? 27.515  -47.707 39.632 1.00 47.94  ? 168 TYR A CD2 1 
ATOM   1390  C  CE1 . TYR A  1 177 ? 26.243  -46.557 37.449 1.00 49.40  ? 168 TYR A CE1 1 
ATOM   1391  C  CE2 . TYR A  1 177 ? 26.671  -48.471 38.833 1.00 59.80  ? 168 TYR A CE2 1 
ATOM   1392  C  CZ  . TYR A  1 177 ? 26.040  -47.887 37.735 1.00 56.09  ? 168 TYR A CZ  1 
ATOM   1393  O  OH  . TYR A  1 177 ? 25.210  -48.635 36.938 1.00 47.14  ? 168 TYR A OH  1 
ATOM   1394  N  N   . TYR A  1 178 ? 25.915  -46.171 42.111 1.00 53.55  ? 169 TYR A N   1 
ATOM   1395  C  CA  . TYR A  1 178 ? 25.141  -47.039 42.989 1.00 54.75  ? 169 TYR A CA  1 
ATOM   1396  C  C   . TYR A  1 178 ? 25.663  -48.463 42.952 1.00 61.90  ? 169 TYR A C   1 
ATOM   1397  O  O   . TYR A  1 178 ? 25.721  -49.081 41.888 1.00 64.93  ? 169 TYR A O   1 
ATOM   1398  C  CB  . TYR A  1 178 ? 23.672  -46.979 42.560 1.00 57.87  ? 169 TYR A CB  1 
ATOM   1399  C  CG  . TYR A  1 178 ? 22.706  -47.889 43.283 1.00 62.45  ? 169 TYR A CG  1 
ATOM   1400  C  CD1 . TYR A  1 178 ? 22.717  -48.002 44.667 1.00 59.18  ? 169 TYR A CD1 1 
ATOM   1401  C  CD2 . TYR A  1 178 ? 21.739  -48.603 42.572 1.00 61.13  ? 169 TYR A CD2 1 
ATOM   1402  C  CE1 . TYR A  1 178 ? 21.809  -48.828 45.322 1.00 61.50  ? 169 TYR A CE1 1 
ATOM   1403  C  CE2 . TYR A  1 178 ? 20.829  -49.429 43.218 1.00 58.28  ? 169 TYR A CE2 1 
ATOM   1404  C  CZ  . TYR A  1 178 ? 20.870  -49.533 44.596 1.00 61.03  ? 169 TYR A CZ  1 
ATOM   1405  O  OH  . TYR A  1 178 ? 19.984  -50.343 45.266 1.00 65.39  ? 169 TYR A OH  1 
ATOM   1406  N  N   . ALA A  1 179 ? 25.999  -48.989 44.130 1.00 67.05  ? 170 ALA A N   1 
ATOM   1407  C  CA  . ALA A  1 179 ? 26.643  -50.297 44.250 1.00 65.81  ? 170 ALA A CA  1 
ATOM   1408  C  C   . ALA A  1 179 ? 25.709  -51.456 43.864 1.00 66.61  ? 170 ALA A C   1 
ATOM   1409  O  O   . ALA A  1 179 ? 26.116  -52.412 43.207 1.00 68.03  ? 170 ALA A O   1 
ATOM   1410  C  CB  . ALA A  1 179 ? 27.183  -50.488 45.661 1.00 53.05  ? 170 ALA A CB  1 
ATOM   1411  N  N   . SER A  1 180 ? 24.451  -51.346 44.263 1.00 63.25  ? 171 SER A N   1 
ATOM   1412  C  CA  . SER A  1 180 ? 23.468  -52.399 44.057 1.00 66.66  ? 171 SER A CA  1 
ATOM   1413  C  C   . SER A  1 180 ? 22.706  -52.286 42.732 1.00 67.21  ? 171 SER A C   1 
ATOM   1414  O  O   . SER A  1 180 ? 21.704  -52.968 42.536 1.00 67.18  ? 171 SER A O   1 
ATOM   1415  C  CB  . SER A  1 180 ? 22.529  -52.535 45.253 1.00 69.12  ? 171 SER A CB  1 
ATOM   1416  O  OG  . SER A  1 180 ? 23.251  -52.930 46.407 1.00 62.40  ? 171 SER A OG  1 
ATOM   1417  N  N   . SER A  1 181 ? 23.147  -51.374 41.867 1.00 59.66  ? 172 SER A N   1 
ATOM   1418  C  CA  . SER A  1 181 ? 22.545  -51.183 40.547 1.00 64.93  ? 172 SER A CA  1 
ATOM   1419  C  C   . SER A  1 181 ? 22.495  -52.466 39.748 1.00 62.64  ? 172 SER A C   1 
ATOM   1420  O  O   . SER A  1 181 ? 23.350  -53.318 39.891 1.00 62.53  ? 172 SER A O   1 
ATOM   1421  C  CB  . SER A  1 181 ? 23.339  -50.156 39.734 1.00 65.98  ? 172 SER A CB  1 
ATOM   1422  O  OG  . SER A  1 181 ? 22.887  -50.062 38.380 1.00 51.16  ? 172 SER A OG  1 
ATOM   1423  N  N   . LYS A  1 182 ? 21.472  -52.594 38.913 1.00 59.89  ? 173 LYS A N   1 
ATOM   1424  C  CA  . LYS A  1 182 ? 21.321  -53.748 38.048 1.00 61.04  ? 173 LYS A CA  1 
ATOM   1425  C  C   . LYS A  1 182 ? 22.498  -53.941 37.099 1.00 61.79  ? 173 LYS A C   1 
ATOM   1426  O  O   . LYS A  1 182 ? 22.712  -55.042 36.585 1.00 67.49  ? 173 LYS A O   1 
ATOM   1427  C  CB  . LYS A  1 182 ? 20.036  -53.612 37.241 1.00 63.74  ? 173 LYS A CB  1 
ATOM   1428  C  CG  . LYS A  1 182 ? 18.856  -54.174 37.945 1.00 63.84  ? 173 LYS A CG  1 
ATOM   1429  C  CD  . LYS A  1 182 ? 19.169  -55.591 38.350 1.00 63.48  ? 173 LYS A CD  1 
ATOM   1430  C  CE  . LYS A  1 182 ? 18.148  -56.513 37.776 1.00 57.69  ? 173 LYS A CE  1 
ATOM   1431  N  NZ  . LYS A  1 182 ? 16.875  -55.777 37.788 1.00 71.09  ? 173 LYS A NZ  1 
ATOM   1432  N  N   . TYR A  1 183 ? 23.254  -52.874 36.865 1.00 59.79  ? 174 TYR A N   1 
ATOM   1433  C  CA  . TYR A  1 183 ? 24.335  -52.906 35.886 1.00 64.75  ? 174 TYR A CA  1 
ATOM   1434  C  C   . TYR A  1 183 ? 25.650  -52.422 36.492 1.00 63.27  ? 174 TYR A C   1 
ATOM   1435  O  O   . TYR A  1 183 ? 25.666  -51.544 37.342 1.00 57.03  ? 174 TYR A O   1 
ATOM   1436  C  CB  . TYR A  1 183 ? 23.971  -52.078 34.634 1.00 59.59  ? 174 TYR A CB  1 
ATOM   1437  C  CG  . TYR A  1 183 ? 22.708  -52.534 33.938 1.00 59.88  ? 174 TYR A CG  1 
ATOM   1438  C  CD1 . TYR A  1 183 ? 22.738  -53.563 33.006 1.00 62.98  ? 174 TYR A CD1 1 
ATOM   1439  C  CD2 . TYR A  1 183 ? 21.487  -51.940 34.215 1.00 53.99  ? 174 TYR A CD2 1 
ATOM   1440  C  CE1 . TYR A  1 183 ? 21.582  -53.991 32.372 1.00 62.07  ? 174 TYR A CE1 1 
ATOM   1441  C  CE2 . TYR A  1 183 ? 20.326  -52.363 33.591 1.00 59.65  ? 174 TYR A CE2 1 
ATOM   1442  C  CZ  . TYR A  1 183 ? 20.376  -53.388 32.664 1.00 64.41  ? 174 TYR A CZ  1 
ATOM   1443  O  OH  . TYR A  1 183 ? 19.221  -53.813 32.029 1.00 50.53  ? 174 TYR A OH  1 
ATOM   1444  N  N   . GLU A  1 184 ? 26.745  -53.007 36.027 1.00 67.98  ? 175 GLU A N   1 
ATOM   1445  C  CA  . GLU A  1 184 ? 28.090  -52.707 36.494 1.00 67.73  ? 175 GLU A CA  1 
ATOM   1446  C  C   . GLU A  1 184 ? 28.748  -51.791 35.476 1.00 68.18  ? 175 GLU A C   1 
ATOM   1447  O  O   . GLU A  1 184 ? 28.558  -51.980 34.281 1.00 74.74  ? 175 GLU A O   1 
ATOM   1448  C  CB  . GLU A  1 184 ? 28.874  -54.009 36.496 1.00 79.57  ? 175 GLU A CB  1 
ATOM   1449  C  CG  . GLU A  1 184 ? 29.645  -54.376 37.741 1.00 74.18  ? 175 GLU A CG  1 
ATOM   1450  C  CD  . GLU A  1 184 ? 30.335  -55.718 37.552 1.00 86.62  ? 175 GLU A CD  1 
ATOM   1451  O  OE1 . GLU A  1 184 ? 29.630  -56.742 37.374 1.00 82.85  ? 175 GLU A OE1 1 
ATOM   1452  O  OE2 . GLU A  1 184 ? 31.583  -55.745 37.545 1.00 92.67  ? 175 GLU A OE2 1 
ATOM   1453  N  N   . ILE A  1 185 ? 29.532  -50.818 35.927 1.00 64.77  ? 176 ILE A N   1 
ATOM   1454  C  CA  . ILE A  1 185 ? 30.259  -49.947 35.008 1.00 66.74  ? 176 ILE A CA  1 
ATOM   1455  C  C   . ILE A  1 185 ? 31.701  -50.439 34.843 1.00 71.09  ? 176 ILE A C   1 
ATOM   1456  O  O   . ILE A  1 185 ? 32.500  -50.346 35.779 1.00 69.69  ? 176 ILE A O   1 
ATOM   1457  C  CB  . ILE A  1 185 ? 30.276  -48.490 35.537 1.00 61.02  ? 176 ILE A CB  1 
ATOM   1458  C  CG1 . ILE A  1 185 ? 28.854  -47.930 35.647 1.00 53.55  ? 176 ILE A CG1 1 
ATOM   1459  C  CG2 . ILE A  1 185 ? 31.190  -47.597 34.701 1.00 66.83  ? 176 ILE A CG2 1 
ATOM   1460  C  CD1 . ILE A  1 185 ? 28.015  -48.158 34.445 1.00 59.48  ? 176 ILE A CD1 1 
ATOM   1461  N  N   . LEU A  1 186 ? 32.037  -50.951 33.661 1.00 70.80  ? 177 LEU A N   1 
ATOM   1462  C  CA  . LEU A  1 186 ? 33.399  -51.411 33.375 1.00 71.17  ? 177 LEU A CA  1 
ATOM   1463  C  C   . LEU A  1 186 ? 34.359  -50.246 33.082 1.00 79.56  ? 177 LEU A C   1 
ATOM   1464  O  O   . LEU A  1 186 ? 35.461  -50.175 33.636 1.00 76.18  ? 177 LEU A O   1 
ATOM   1465  C  CB  . LEU A  1 186 ? 33.390  -52.415 32.221 1.00 81.65  ? 177 LEU A CB  1 
ATOM   1466  C  CG  . LEU A  1 186 ? 32.447  -53.613 32.396 1.00 80.30  ? 177 LEU A CG  1 
ATOM   1467  C  CD1 . LEU A  1 186 ? 32.272  -54.390 31.103 1.00 63.74  ? 177 LEU A CD1 1 
ATOM   1468  C  CD2 . LEU A  1 186 ? 32.938  -54.515 33.513 1.00 73.41  ? 177 LEU A CD2 1 
ATOM   1469  N  N   . SER A  1 187 ? 33.933  -49.330 32.216 1.00 81.09  ? 178 SER A N   1 
ATOM   1470  C  CA  . SER A  1 187 ? 34.631  -48.052 32.052 1.00 80.46  ? 178 SER A CA  1 
ATOM   1471  C  C   . SER A  1 187 ? 33.693  -46.941 31.578 1.00 72.87  ? 178 SER A C   1 
ATOM   1472  O  O   . SER A  1 187 ? 32.674  -47.199 30.937 1.00 72.95  ? 178 SER A O   1 
ATOM   1473  C  CB  . SER A  1 187 ? 35.820  -48.187 31.096 1.00 84.46  ? 178 SER A CB  1 
ATOM   1474  O  OG  . SER A  1 187 ? 35.396  -48.544 29.791 1.00 87.22  ? 178 SER A OG  1 
ATOM   1475  N  N   . ALA A  1 188 ? 34.034  -45.708 31.927 1.00 69.90  ? 179 ALA A N   1 
ATOM   1476  C  CA  . ALA A  1 188 ? 33.333  -44.538 31.427 1.00 64.44  ? 179 ALA A CA  1 
ATOM   1477  C  C   . ALA A  1 188 ? 34.354  -43.459 31.087 1.00 65.34  ? 179 ALA A C   1 
ATOM   1478  O  O   . ALA A  1 188 ? 35.153  -43.064 31.926 1.00 63.39  ? 179 ALA A O   1 
ATOM   1479  C  CB  . ALA A  1 188 ? 32.340  -44.039 32.460 1.00 63.20  ? 179 ALA A CB  1 
ATOM   1480  N  N   . THR A  1 189 ? 34.346  -42.981 29.854 1.00 66.21  ? 180 THR A N   1 
ATOM   1481  C  CA  . THR A  1 189 ? 35.296  -41.938 29.492 1.00 73.98  ? 180 THR A CA  1 
ATOM   1482  C  C   . THR A  1 189 ? 34.566  -40.661 29.046 1.00 75.08  ? 180 THR A C   1 
ATOM   1483  O  O   . THR A  1 189 ? 33.447  -40.736 28.531 1.00 72.49  ? 180 THR A O   1 
ATOM   1484  C  CB  . THR A  1 189 ? 36.307  -42.434 28.414 1.00 70.86  ? 180 THR A CB  1 
ATOM   1485  O  OG1 . THR A  1 189 ? 35.612  -42.783 27.216 1.00 74.98  ? 180 THR A OG1 1 
ATOM   1486  C  CG2 . THR A  1 189 ? 37.057  -43.657 28.899 1.00 67.20  ? 180 THR A CG2 1 
ATOM   1487  N  N   . GLN A  1 190 ? 35.171  -39.493 29.275 1.00 71.72  ? 181 GLN A N   1 
ATOM   1488  C  CA  . GLN A  1 190 ? 34.629  -38.259 28.707 1.00 63.81  ? 181 GLN A CA  1 
ATOM   1489  C  C   . GLN A  1 190 ? 35.664  -37.492 27.879 1.00 66.44  ? 181 GLN A C   1 
ATOM   1490  O  O   . GLN A  1 190 ? 36.616  -36.928 28.408 1.00 69.90  ? 181 GLN A O   1 
ATOM   1491  C  CB  . GLN A  1 190 ? 34.007  -37.382 29.787 1.00 58.21  ? 181 GLN A CB  1 
ATOM   1492  C  CG  . GLN A  1 190 ? 34.963  -36.852 30.812 1.00 66.29  ? 181 GLN A CG  1 
ATOM   1493  C  CD  . GLN A  1 190 ? 34.233  -36.262 32.001 1.00 72.11  ? 181 GLN A CD  1 
ATOM   1494  O  OE1 . GLN A  1 190 ? 33.051  -36.538 32.203 1.00 64.97  ? 181 GLN A OE1 1 
ATOM   1495  N  NE2 . GLN A  1 190 ? 34.929  -35.445 32.793 1.00 63.57  ? 181 GLN A NE2 1 
ATOM   1496  N  N   . THR A  1 191 ? 35.420  -37.438 26.571 1.00 70.18  ? 182 THR A N   1 
ATOM   1497  C  CA  . THR A  1 191 ? 36.407  -37.000 25.587 1.00 73.35  ? 182 THR A CA  1 
ATOM   1498  C  C   . THR A  1 191 ? 35.908  -35.855 24.723 1.00 63.55  ? 182 THR A C   1 
ATOM   1499  O  O   . THR A  1 191 ? 34.830  -35.937 24.152 1.00 68.67  ? 182 THR A O   1 
ATOM   1500  C  CB  . THR A  1 191 ? 36.740  -38.145 24.620 1.00 72.28  ? 182 THR A CB  1 
ATOM   1501  O  OG1 . THR A  1 191 ? 37.050  -39.337 25.363 1.00 71.57  ? 182 THR A OG1 1 
ATOM   1502  C  CG2 . THR A  1 191 ? 37.909  -37.747 23.722 1.00 62.88  ? 182 THR A CG2 1 
ATOM   1503  N  N   . ARG A  1 192 ? 36.705  -34.800 24.603 1.00 63.90  ? 183 ARG A N   1 
ATOM   1504  C  CA  . ARG A  1 192 ? 36.358  -33.679 23.729 1.00 64.99  ? 183 ARG A CA  1 
ATOM   1505  C  C   . ARG A  1 192 ? 36.772  -33.923 22.275 1.00 72.18  ? 183 ARG A C   1 
ATOM   1506  O  O   . ARG A  1 192 ? 37.823  -34.498 22.000 1.00 73.38  ? 183 ARG A O   1 
ATOM   1507  C  CB  . ARG A  1 192 ? 37.014  -32.393 24.225 1.00 62.01  ? 183 ARG A CB  1 
ATOM   1508  C  CG  . ARG A  1 192 ? 36.589  -31.183 23.451 1.00 68.90  ? 183 ARG A CG  1 
ATOM   1509  C  CD  . ARG A  1 192 ? 37.469  -29.974 23.705 1.00 66.91  ? 183 ARG A CD  1 
ATOM   1510  N  NE  . ARG A  1 192 ? 37.139  -28.915 22.751 1.00 76.76  ? 183 ARG A NE  1 
ATOM   1511  C  CZ  . ARG A  1 192 ? 38.028  -28.226 22.043 1.00 78.95  ? 183 ARG A CZ  1 
ATOM   1512  N  NH1 . ARG A  1 192 ? 39.325  -28.465 22.179 1.00 80.42  ? 183 ARG A NH1 1 
ATOM   1513  N  NH2 . ARG A  1 192 ? 37.617  -27.288 21.201 1.00 78.11  ? 183 ARG A NH2 1 
ATOM   1514  N  N   . SER A  1 193 ? 35.945  -33.478 21.341 1.00 77.69  ? 184 SER A N   1 
ATOM   1515  C  CA  . SER A  1 193 ? 36.293  -33.558 19.925 1.00 84.03  ? 184 SER A CA  1 
ATOM   1516  C  C   . SER A  1 193 ? 35.716  -32.356 19.172 1.00 79.80  ? 184 SER A C   1 
ATOM   1517  O  O   . SER A  1 193 ? 34.691  -31.815 19.576 1.00 78.31  ? 184 SER A O   1 
ATOM   1518  C  CB  . SER A  1 193 ? 35.794  -34.879 19.321 1.00 84.07  ? 184 SER A CB  1 
ATOM   1519  O  OG  . SER A  1 193 ? 34.388  -35.001 19.430 1.00 87.94  ? 184 SER A OG  1 
ATOM   1520  N  N   . GLU A  1 194 ? 36.380  -31.934 18.096 1.00 82.78  ? 185 GLU A N   1 
ATOM   1521  C  CA  . GLU A  1 194 ? 35.894  -30.816 17.281 1.00 79.51  ? 185 GLU A CA  1 
ATOM   1522  C  C   . GLU A  1 194 ? 35.406  -31.295 15.927 1.00 81.40  ? 185 GLU A C   1 
ATOM   1523  O  O   . GLU A  1 194 ? 36.130  -31.966 15.203 1.00 72.55  ? 185 GLU A O   1 
ATOM   1524  C  CB  . GLU A  1 194 ? 36.976  -29.760 17.060 1.00 72.69  ? 185 GLU A CB  1 
ATOM   1525  C  CG  . GLU A  1 194 ? 37.585  -29.214 18.309 1.00 78.71  ? 185 GLU A CG  1 
ATOM   1526  C  CD  . GLU A  1 194 ? 38.498  -28.043 18.031 1.00 90.96  ? 185 GLU A CD  1 
ATOM   1527  O  OE1 . GLU A  1 194 ? 39.702  -28.143 18.353 1.00 98.42  ? 185 GLU A OE1 1 
ATOM   1528  O  OE2 . GLU A  1 194 ? 38.010  -27.021 17.496 1.00 92.21  ? 185 GLU A OE2 1 
ATOM   1529  N  N   . ARG A  1 195 ? 34.172  -30.929 15.602 1.00 86.97  ? 186 ARG A N   1 
ATOM   1530  C  CA  . ARG A  1 195 ? 33.571  -31.243 14.315 1.00 85.09  ? 186 ARG A CA  1 
ATOM   1531  C  C   . ARG A  1 195 ? 33.825  -30.067 13.382 1.00 86.56  ? 186 ARG A C   1 
ATOM   1532  O  O   . ARG A  1 195 ? 33.587  -28.918 13.733 1.00 86.29  ? 186 ARG A O   1 
ATOM   1533  C  CB  . ARG A  1 195 ? 32.065  -31.482 14.465 1.00 80.48  ? 186 ARG A CB  1 
ATOM   1534  C  CG  . ARG A  1 195 ? 31.500  -32.471 13.478 1.00 76.52  ? 186 ARG A CG  1 
ATOM   1535  C  CD  . ARG A  1 195 ? 32.217  -33.800 13.602 1.00 97.75  ? 186 ARG A CD  1 
ATOM   1536  N  NE  . ARG A  1 195 ? 31.896  -34.503 14.840 1.00 111.12 ? 186 ARG A NE  1 
ATOM   1537  C  CZ  . ARG A  1 195 ? 32.685  -35.410 15.405 1.00 109.34 ? 186 ARG A CZ  1 
ATOM   1538  N  NH1 . ARG A  1 195 ? 33.850  -35.715 14.850 1.00 102.40 ? 186 ARG A NH1 1 
ATOM   1539  N  NH2 . ARG A  1 195 ? 32.316  -36.006 16.530 1.00 100.31 ? 186 ARG A NH2 1 
ATOM   1540  N  N   . PHE A  1 196 ? 34.305  -30.359 12.186 1.00 93.30  ? 187 PHE A N   1 
ATOM   1541  C  CA  . PHE A  1 196 ? 34.675  -29.324 11.246 1.00 88.58  ? 187 PHE A CA  1 
ATOM   1542  C  C   . PHE A  1 196 ? 33.950  -29.589 9.967  1.00 95.00  ? 187 PHE A C   1 
ATOM   1543  O  O   . PHE A  1 196 ? 33.420  -30.680 9.773  1.00 97.06  ? 187 PHE A O   1 
ATOM   1544  C  CB  . PHE A  1 196 ? 36.162  -29.403 10.964 1.00 89.77  ? 187 PHE A CB  1 
ATOM   1545  C  CG  . PHE A  1 196 ? 36.960  -28.399 11.701 1.00 84.94  ? 187 PHE A CG  1 
ATOM   1546  C  CD1 . PHE A  1 196 ? 37.900  -28.795 12.636 1.00 83.44  ? 187 PHE A CD1 1 
ATOM   1547  C  CD2 . PHE A  1 196 ? 36.758  -27.052 11.472 1.00 79.77  ? 187 PHE A CD2 1 
ATOM   1548  C  CE1 . PHE A  1 196 ? 38.642  -27.857 13.321 1.00 88.33  ? 187 PHE A CE1 1 
ATOM   1549  C  CE2 . PHE A  1 196 ? 37.491  -26.112 12.147 1.00 87.19  ? 187 PHE A CE2 1 
ATOM   1550  C  CZ  . PHE A  1 196 ? 38.435  -26.511 13.077 1.00 91.86  ? 187 PHE A CZ  1 
ATOM   1551  N  N   . TYR A  1 197 ? 33.916  -28.594 9.090  1.00 104.24 ? 188 TYR A N   1 
ATOM   1552  C  CA  . TYR A  1 197 ? 33.441  -28.837 7.731  1.00 120.62 ? 188 TYR A CA  1 
ATOM   1553  C  C   . TYR A  1 197 ? 34.340  -28.229 6.650  1.00 113.94 ? 188 TYR A C   1 
ATOM   1554  O  O   . TYR A  1 197 ? 34.995  -27.196 6.852  1.00 102.22 ? 188 TYR A O   1 
ATOM   1555  C  CB  . TYR A  1 197 ? 31.985  -28.385 7.550  1.00 121.93 ? 188 TYR A CB  1 
ATOM   1556  C  CG  . TYR A  1 197 ? 31.015  -29.065 8.489  1.00 111.15 ? 188 TYR A CG  1 
ATOM   1557  C  CD1 . TYR A  1 197 ? 30.136  -28.315 9.253  1.00 108.74 ? 188 TYR A CD1 1 
ATOM   1558  C  CD2 . TYR A  1 197 ? 30.970  -30.452 8.600  1.00 106.99 ? 188 TYR A CD2 1 
ATOM   1559  C  CE1 . TYR A  1 197 ? 29.244  -28.915 10.113 1.00 116.22 ? 188 TYR A CE1 1 
ATOM   1560  C  CE2 . TYR A  1 197 ? 30.081  -31.070 9.461  1.00 114.10 ? 188 TYR A CE2 1 
ATOM   1561  C  CZ  . TYR A  1 197 ? 29.216  -30.291 10.217 1.00 124.88 ? 188 TYR A CZ  1 
ATOM   1562  O  OH  . TYR A  1 197 ? 28.319  -30.877 11.086 1.00 121.29 ? 188 TYR A OH  1 
ATOM   1563  N  N   . GLU A  1 198 ? 34.374  -28.905 5.504  1.00 115.84 ? 189 GLU A N   1 
ATOM   1564  C  CA  . GLU A  1 198 ? 34.931  -28.313 4.295  1.00 120.14 ? 189 GLU A CA  1 
ATOM   1565  C  C   . GLU A  1 198 ? 34.060  -27.104 3.989  1.00 115.87 ? 189 GLU A C   1 
ATOM   1566  O  O   . GLU A  1 198 ? 34.545  -25.987 3.806  1.00 104.07 ? 189 GLU A O   1 
ATOM   1567  C  CB  . GLU A  1 198 ? 34.869  -29.304 3.147  1.00 115.12 ? 189 GLU A CB  1 
ATOM   1568  C  CG  . GLU A  1 198 ? 35.611  -28.877 1.876  1.00 113.73 ? 189 GLU A CG  1 
ATOM   1569  C  CD  . GLU A  1 198 ? 35.946  -30.045 0.958  1.00 120.76 ? 189 GLU A CD  1 
ATOM   1570  O  OE1 . GLU A  1 198 ? 35.802  -31.213 1.376  1.00 119.74 ? 189 GLU A OE1 1 
ATOM   1571  O  OE2 . GLU A  1 198 ? 36.362  -29.787 -0.190 1.00 124.60 ? 189 GLU A OE2 1 
ATOM   1572  N  N   . CYS A  1 199 ? 32.752  -27.339 4.009  1.00 112.15 ? 190 CYS A N   1 
ATOM   1573  C  CA  . CYS A  1 199 ? 31.758  -26.342 3.627  1.00 108.94 ? 190 CYS A CA  1 
ATOM   1574  C  C   . CYS A  1 199 ? 31.758  -25.002 4.357  1.00 106.05 ? 190 CYS A C   1 
ATOM   1575  O  O   . CYS A  1 199 ? 31.980  -23.960 3.744  1.00 99.89  ? 190 CYS A O   1 
ATOM   1576  C  CB  . CYS A  1 199 ? 30.347  -26.915 3.787  1.00 105.32 ? 190 CYS A CB  1 
ATOM   1577  S  SG  . CYS A  1 199 ? 29.596  -26.821 5.429  1.00 96.72  ? 190 CYS A SG  1 
ATOM   1578  N  N   . CYS A  1 200 ? 31.525  -25.054 5.665  1.00 110.33 ? 191 CYS A N   1 
ATOM   1579  C  CA  . CYS A  1 200 ? 31.444  -23.878 6.520  1.00 109.46 ? 191 CYS A CA  1 
ATOM   1580  C  C   . CYS A  1 200 ? 32.489  -23.933 7.650  1.00 93.39  ? 191 CYS A C   1 
ATOM   1581  O  O   . CYS A  1 200 ? 32.590  -24.921 8.364  1.00 89.46  ? 191 CYS A O   1 
ATOM   1582  C  CB  . CYS A  1 200 ? 30.012  -23.772 7.044  1.00 112.56 ? 191 CYS A CB  1 
ATOM   1583  S  SG  . CYS A  1 200 ? 28.792  -24.359 5.815  1.00 107.82 ? 191 CYS A SG  1 
ATOM   1584  N  N   . LYS A  1 201 ? 33.203  -22.829 7.838  1.00 86.47  ? 192 LYS A N   1 
ATOM   1585  C  CA  . LYS A  1 201 ? 34.541  -22.789 8.448  1.00 93.86  ? 192 LYS A CA  1 
ATOM   1586  C  C   . LYS A  1 201 ? 34.667  -22.811 9.987  1.00 97.45  ? 192 LYS A C   1 
ATOM   1587  O  O   . LYS A  1 201 ? 35.783  -22.806 10.514 1.00 93.52  ? 192 LYS A O   1 
ATOM   1588  C  CB  . LYS A  1 201 ? 35.213  -21.503 7.950  1.00 99.87  ? 192 LYS A CB  1 
ATOM   1589  C  CG  . LYS A  1 201 ? 34.171  -20.402 7.682  1.00 101.57 ? 192 LYS A CG  1 
ATOM   1590  C  CD  . LYS A  1 201 ? 34.774  -19.017 7.535  0.00 102.71 ? 192 LYS A CD  1 
ATOM   1591  C  CE  . LYS A  1 201 ? 34.924  -18.353 8.888  0.00 101.75 ? 192 LYS A CE  1 
ATOM   1592  N  NZ  . LYS A  1 201 ? 35.839  -17.185 8.857  0.00 103.13 ? 192 LYS A NZ  1 
ATOM   1593  N  N   . GLU A  1 202 ? 33.549  -22.828 10.707 1.00 100.46 ? 193 GLU A N   1 
ATOM   1594  C  CA  . GLU A  1 202 ? 33.584  -22.737 12.175 1.00 91.41  ? 193 GLU A CA  1 
ATOM   1595  C  C   . GLU A  1 202 ? 33.551  -24.084 12.932 1.00 83.62  ? 193 GLU A C   1 
ATOM   1596  O  O   . GLU A  1 202 ? 32.620  -24.869 12.773 1.00 76.65  ? 193 GLU A O   1 
ATOM   1597  C  CB  . GLU A  1 202 ? 32.434  -21.851 12.654 1.00 85.46  ? 193 GLU A CB  1 
ATOM   1598  C  CG  . GLU A  1 202 ? 32.348  -21.709 14.172 1.00 83.91  ? 193 GLU A CG  1 
ATOM   1599  C  CD  . GLU A  1 202 ? 31.118  -20.932 14.600 1.00 81.19  ? 193 GLU A CD  1 
ATOM   1600  O  OE1 . GLU A  1 202 ? 30.174  -20.845 13.791 1.00 86.83  ? 193 GLU A OE1 1 
ATOM   1601  O  OE2 . GLU A  1 202 ? 31.089  -20.407 15.729 1.00 70.58  ? 193 GLU A OE2 1 
ATOM   1602  N  N   . PRO A  1 203 ? 34.551  -24.337 13.793 1.00 80.75  ? 194 PRO A N   1 
ATOM   1603  C  CA  . PRO A  1 203 ? 34.606  -25.640 14.488 1.00 86.53  ? 194 PRO A CA  1 
ATOM   1604  C  C   . PRO A  1 203 ? 33.394  -25.880 15.392 1.00 78.06  ? 194 PRO A C   1 
ATOM   1605  O  O   . PRO A  1 203 ? 32.895  -24.921 15.960 1.00 78.10  ? 194 PRO A O   1 
ATOM   1606  C  CB  . PRO A  1 203 ? 35.858  -25.517 15.364 1.00 79.02  ? 194 PRO A CB  1 
ATOM   1607  C  CG  . PRO A  1 203 ? 36.003  -24.037 15.600 1.00 79.94  ? 194 PRO A CG  1 
ATOM   1608  C  CD  . PRO A  1 203 ? 35.539  -23.379 14.320 1.00 76.44  ? 194 PRO A CD  1 
ATOM   1609  N  N   . TYR A  1 204 ? 32.922  -27.107 15.568 1.00 71.32  ? 195 TYR A N   1 
ATOM   1610  C  CA  . TYR A  1 204 ? 31.923  -27.238 16.608 1.00 73.01  ? 195 TYR A CA  1 
ATOM   1611  C  C   . TYR A  1 204 ? 32.348  -28.253 17.646 1.00 73.09  ? 195 TYR A C   1 
ATOM   1612  O  O   . TYR A  1 204 ? 32.734  -29.376 17.316 1.00 60.59  ? 195 TYR A O   1 
ATOM   1613  C  CB  . TYR A  1 204 ? 30.592  -27.665 15.986 1.00 74.80  ? 195 TYR A CB  1 
ATOM   1614  C  CG  . TYR A  1 204 ? 29.993  -26.607 15.088 1.00 81.62  ? 195 TYR A CG  1 
ATOM   1615  C  CD1 . TYR A  1 204 ? 29.315  -25.526 15.622 1.00 74.73  ? 195 TYR A CD1 1 
ATOM   1616  C  CD2 . TYR A  1 204 ? 30.117  -26.684 13.707 1.00 89.45  ? 195 TYR A CD2 1 
ATOM   1617  C  CE1 . TYR A  1 204 ? 28.777  -24.554 14.815 1.00 82.69  ? 195 TYR A CE1 1 
ATOM   1618  C  CE2 . TYR A  1 204 ? 29.579  -25.709 12.884 1.00 82.79  ? 195 TYR A CE2 1 
ATOM   1619  C  CZ  . TYR A  1 204 ? 28.908  -24.646 13.444 1.00 84.51  ? 195 TYR A CZ  1 
ATOM   1620  O  OH  . TYR A  1 204 ? 28.366  -23.668 12.638 1.00 79.56  ? 195 TYR A OH  1 
ATOM   1621  N  N   . PRO A  1 205 ? 32.222  -27.870 18.927 1.00 66.92  ? 196 PRO A N   1 
ATOM   1622  C  CA  . PRO A  1 205 ? 32.687  -28.911 19.829 1.00 67.19  ? 196 PRO A CA  1 
ATOM   1623  C  C   . PRO A  1 205 ? 31.577  -29.804 20.360 1.00 73.03  ? 196 PRO A C   1 
ATOM   1624  O  O   . PRO A  1 205 ? 30.388  -29.502 20.226 1.00 68.40  ? 196 PRO A O   1 
ATOM   1625  C  CB  . PRO A  1 205 ? 33.343  -28.112 20.959 1.00 63.69  ? 196 PRO A CB  1 
ATOM   1626  C  CG  . PRO A  1 205 ? 33.581  -26.738 20.369 1.00 66.29  ? 196 PRO A CG  1 
ATOM   1627  C  CD  . PRO A  1 205 ? 32.399  -26.531 19.500 1.00 62.08  ? 196 PRO A CD  1 
ATOM   1628  N  N   . ASP A  1 206 ? 32.005  -30.863 21.038 1.00 67.35  ? 197 ASP A N   1 
ATOM   1629  C  CA  . ASP A  1 206 ? 31.136  -31.748 21.771 1.00 60.55  ? 197 ASP A CA  1 
ATOM   1630  C  C   . ASP A  1 206 ? 32.007  -32.529 22.744 1.00 68.05  ? 197 ASP A C   1 
ATOM   1631  O  O   . ASP A  1 206 ? 33.227  -32.580 22.585 1.00 67.91  ? 197 ASP A O   1 
ATOM   1632  C  CB  . ASP A  1 206 ? 30.328  -32.661 20.842 1.00 68.36  ? 197 ASP A CB  1 
ATOM   1633  C  CG  . ASP A  1 206 ? 31.180  -33.708 20.149 1.00 78.99  ? 197 ASP A CG  1 
ATOM   1634  O  OD1 . ASP A  1 206 ? 31.612  -34.672 20.822 1.00 78.67  ? 197 ASP A OD1 1 
ATOM   1635  O  OD2 . ASP A  1 206 ? 31.387  -33.583 18.920 1.00 87.24  ? 197 ASP A OD2 1 
ATOM   1636  N  N   . VAL A  1 207 ? 31.375  -33.111 23.756 1.00 61.62  ? 198 VAL A N   1 
ATOM   1637  C  CA  . VAL A  1 207 ? 32.036  -34.012 24.671 1.00 54.97  ? 198 VAL A CA  1 
ATOM   1638  C  C   . VAL A  1 207 ? 31.337  -35.338 24.520 1.00 60.68  ? 198 VAL A C   1 
ATOM   1639  O  O   . VAL A  1 207 ? 30.115  -35.398 24.533 1.00 59.86  ? 198 VAL A O   1 
ATOM   1640  C  CB  . VAL A  1 207 ? 31.928  -33.519 26.118 1.00 58.47  ? 198 VAL A CB  1 
ATOM   1641  C  CG1 . VAL A  1 207 ? 32.111  -34.663 27.092 1.00 54.10  ? 198 VAL A CG1 1 
ATOM   1642  C  CG2 . VAL A  1 207 ? 32.945  -32.415 26.380 1.00 60.75  ? 198 VAL A CG2 1 
ATOM   1643  N  N   . ASN A  1 208 ? 32.118  -36.397 24.345 1.00 67.15  ? 199 ASN A N   1 
ATOM   1644  C  CA  . ASN A  1 208 ? 31.572  -37.714 24.068 1.00 67.90  ? 199 ASN A CA  1 
ATOM   1645  C  C   . ASN A  1 208 ? 31.665  -38.565 25.312 1.00 62.28  ? 199 ASN A C   1 
ATOM   1646  O  O   . ASN A  1 208 ? 32.754  -38.918 25.749 1.00 69.88  ? 199 ASN A O   1 
ATOM   1647  C  CB  . ASN A  1 208 ? 32.317  -38.379 22.888 1.00 73.93  ? 199 ASN A CB  1 
ATOM   1648  C  CG  . ASN A  1 208 ? 31.486  -39.474 22.175 1.00 70.78  ? 199 ASN A CG  1 
ATOM   1649  O  OD1 . ASN A  1 208 ? 30.482  -39.968 22.691 1.00 68.15  ? 199 ASN A OD1 1 
ATOM   1650  N  ND2 . ASN A  1 208 ? 31.930  -39.857 20.984 1.00 81.80  ? 199 ASN A ND2 1 
ATOM   1651  N  N   . LEU A  1 209 ? 30.512  -38.892 25.879 1.00 62.24  ? 200 LEU A N   1 
ATOM   1652  C  CA  . LEU A  1 209 ? 30.458  -39.799 27.012 1.00 70.59  ? 200 LEU A CA  1 
ATOM   1653  C  C   . LEU A  1 209 ? 30.309  -41.220 26.468 1.00 69.67  ? 200 LEU A C   1 
ATOM   1654  O  O   . LEU A  1 209 ? 29.312  -41.555 25.831 1.00 64.81  ? 200 LEU A O   1 
ATOM   1655  C  CB  . LEU A  1 209 ? 29.277  -39.441 27.926 1.00 68.05  ? 200 LEU A CB  1 
ATOM   1656  C  CG  . LEU A  1 209 ? 29.068  -40.244 29.209 1.00 62.31  ? 200 LEU A CG  1 
ATOM   1657  C  CD1 . LEU A  1 209 ? 30.209  -39.994 30.131 1.00 66.77  ? 200 LEU A CD1 1 
ATOM   1658  C  CD2 . LEU A  1 209 ? 27.782  -39.856 29.885 1.00 58.52  ? 200 LEU A CD2 1 
ATOM   1659  N  N   . VAL A  1 210 ? 31.320  -42.046 26.703 1.00 71.52  ? 201 VAL A N   1 
ATOM   1660  C  CA  . VAL A  1 210 ? 31.301  -43.431 26.245 1.00 72.85  ? 201 VAL A CA  1 
ATOM   1661  C  C   . VAL A  1 210 ? 31.267  -44.342 27.465 1.00 72.18  ? 201 VAL A C   1 
ATOM   1662  O  O   . VAL A  1 210 ? 32.084  -44.189 28.380 1.00 65.06  ? 201 VAL A O   1 
ATOM   1663  C  CB  . VAL A  1 210 ? 32.542  -43.768 25.400 1.00 65.09  ? 201 VAL A CB  1 
ATOM   1664  C  CG1 . VAL A  1 210 ? 32.310  -45.058 24.623 1.00 53.93  ? 201 VAL A CG1 1 
ATOM   1665  C  CG2 . VAL A  1 210 ? 32.884  -42.609 24.483 1.00 56.10  ? 201 VAL A CG2 1 
ATOM   1666  N  N   . VAL A  1 211 ? 30.325  -45.285 27.479 1.00 68.69  ? 202 VAL A N   1 
ATOM   1667  C  CA  . VAL A  1 211 ? 30.117  -46.127 28.653 1.00 70.93  ? 202 VAL A CA  1 
ATOM   1668  C  C   . VAL A  1 211 ? 30.108  -47.608 28.330 1.00 68.43  ? 202 VAL A C   1 
ATOM   1669  O  O   . VAL A  1 211 ? 29.291  -48.072 27.553 1.00 65.54  ? 202 VAL A O   1 
ATOM   1670  C  CB  . VAL A  1 211 ? 28.789  -45.796 29.348 1.00 70.15  ? 202 VAL A CB  1 
ATOM   1671  C  CG1 . VAL A  1 211 ? 28.568  -46.712 30.548 1.00 63.57  ? 202 VAL A CG1 1 
ATOM   1672  C  CG2 . VAL A  1 211 ? 28.763  -44.341 29.754 1.00 64.20  ? 202 VAL A CG2 1 
ATOM   1673  N  N   . LYS A  1 212 ? 31.023  -48.344 28.946 1.00 70.96  ? 203 LYS A N   1 
ATOM   1674  C  CA  . LYS A  1 212 ? 31.042  -49.798 28.845 1.00 79.73  ? 203 LYS A CA  1 
ATOM   1675  C  C   . LYS A  1 212 ? 30.460  -50.433 30.111 1.00 74.07  ? 203 LYS A C   1 
ATOM   1676  O  O   . LYS A  1 212 ? 30.958  -50.207 31.213 1.00 73.07  ? 203 LYS A O   1 
ATOM   1677  C  CB  . LYS A  1 212 ? 32.468  -50.296 28.590 1.00 87.07  ? 203 LYS A CB  1 
ATOM   1678  C  CG  . LYS A  1 212 ? 32.782  -50.544 27.115 1.00 86.07  ? 203 LYS A CG  1 
ATOM   1679  C  CD  . LYS A  1 212 ? 34.284  -50.593 26.854 1.00 90.47  ? 203 LYS A CD  1 
ATOM   1680  C  CE  . LYS A  1 212 ? 34.907  -49.214 27.021 1.00 88.65  ? 203 LYS A CE  1 
ATOM   1681  N  NZ  . LYS A  1 212 ? 36.365  -49.213 26.713 1.00 95.32  ? 203 LYS A NZ  1 
ATOM   1682  N  N   . PHE A  1 213 ? 29.400  -51.221 29.946 1.00 69.50  ? 204 PHE A N   1 
ATOM   1683  C  CA  . PHE A  1 213 ? 28.644  -51.722 31.087 1.00 69.33  ? 204 PHE A CA  1 
ATOM   1684  C  C   . PHE A  1 213 ? 28.074  -53.112 30.852 1.00 71.48  ? 204 PHE A C   1 
ATOM   1685  O  O   . PHE A  1 213 ? 27.787  -53.487 29.715 1.00 73.76  ? 204 PHE A O   1 
ATOM   1686  C  CB  . PHE A  1 213 ? 27.519  -50.737 31.452 1.00 74.74  ? 204 PHE A CB  1 
ATOM   1687  C  CG  . PHE A  1 213 ? 26.434  -50.612 30.407 1.00 61.86  ? 204 PHE A CG  1 
ATOM   1688  C  CD1 . PHE A  1 213 ? 25.177  -51.152 30.628 1.00 58.44  ? 204 PHE A CD1 1 
ATOM   1689  C  CD2 . PHE A  1 213 ? 26.666  -49.943 29.218 1.00 66.67  ? 204 PHE A CD2 1 
ATOM   1690  C  CE1 . PHE A  1 213 ? 24.176  -51.031 29.680 1.00 60.98  ? 204 PHE A CE1 1 
ATOM   1691  C  CE2 . PHE A  1 213 ? 25.666  -49.826 28.254 1.00 60.67  ? 204 PHE A CE2 1 
ATOM   1692  C  CZ  . PHE A  1 213 ? 24.424  -50.367 28.485 1.00 54.98  ? 204 PHE A CZ  1 
ATOM   1693  N  N   . ARG A  1 214 ? 27.910  -53.875 31.929 1.00 71.23  ? 205 ARG A N   1 
ATOM   1694  C  CA  . ARG A  1 214 ? 27.339  -55.215 31.831 1.00 76.72  ? 205 ARG A CA  1 
ATOM   1695  C  C   . ARG A  1 214 ? 26.367  -55.474 32.975 1.00 74.59  ? 205 ARG A C   1 
ATOM   1696  O  O   . ARG A  1 214 ? 26.392  -54.766 33.978 1.00 64.92  ? 205 ARG A O   1 
ATOM   1697  C  CB  . ARG A  1 214 ? 28.448  -56.274 31.819 1.00 76.30  ? 205 ARG A CB  1 
ATOM   1698  C  CG  . ARG A  1 214 ? 29.323  -56.279 33.058 1.00 77.54  ? 205 ARG A CG  1 
ATOM   1699  C  CD  . ARG A  1 214 ? 30.443  -57.310 32.938 1.00 83.60  ? 205 ARG A CD  1 
ATOM   1700  N  NE  . ARG A  1 214 ? 30.995  -57.680 34.242 1.00 86.14  ? 205 ARG A NE  1 
ATOM   1701  C  CZ  . ARG A  1 214 ? 32.253  -58.051 34.452 1.00 80.23  ? 205 ARG A CZ  1 
ATOM   1702  N  NH1 . ARG A  1 214 ? 33.117  -58.103 33.447 1.00 79.47  ? 205 ARG A NH1 1 
ATOM   1703  N  NH2 . ARG A  1 214 ? 32.650  -58.365 35.675 1.00 74.80  ? 205 ARG A NH2 1 
ATOM   1704  N  N   . GLU A  1 215 ? 25.499  -56.473 32.813 1.00 73.29  ? 206 GLU A N   1 
ATOM   1705  C  CA  . GLU A  1 215 ? 24.656  -56.921 33.916 1.00 68.44  ? 206 GLU A CA  1 
ATOM   1706  C  C   . GLU A  1 215 ? 25.572  -57.453 35.009 1.00 79.11  ? 206 GLU A C   1 
ATOM   1707  O  O   . GLU A  1 215 ? 26.599  -58.077 34.723 1.00 81.98  ? 206 GLU A O   1 
ATOM   1708  C  CB  . GLU A  1 215 ? 23.696  -58.024 33.481 1.00 63.24  ? 206 GLU A CB  1 
ATOM   1709  C  CG  . GLU A  1 215 ? 22.852  -57.701 32.266 1.00 72.88  ? 206 GLU A CG  1 
ATOM   1710  C  CD  . GLU A  1 215 ? 21.896  -58.828 31.908 1.00 84.61  ? 206 GLU A CD  1 
ATOM   1711  O  OE1 . GLU A  1 215 ? 22.365  -59.964 31.685 1.00 85.87  ? 206 GLU A OE1 1 
ATOM   1712  O  OE2 . GLU A  1 215 ? 20.672  -58.584 31.856 1.00 86.71  ? 206 GLU A OE2 1 
ATOM   1713  N  N   . ARG A  1 216 ? 25.218  -57.192 36.264 1.00 80.66  ? 207 ARG A N   1 
ATOM   1714  C  CA  . ARG A  1 216 ? 26.021  -57.663 37.381 1.00 76.21  ? 207 ARG A CA  1 
ATOM   1715  C  C   . ARG A  1 216 ? 25.807  -59.145 37.561 1.00 84.60  ? 207 ARG A C   1 
ATOM   1716  O  O   . ARG A  1 216 ? 24.805  -59.688 37.100 1.00 93.27  ? 207 ARG A O   1 
ATOM   1717  C  CB  . ARG A  1 216 ? 25.664  -56.909 38.650 1.00 70.26  ? 207 ARG A CB  1 
ATOM   1718  C  CG  . ARG A  1 216 ? 26.453  -55.623 38.775 1.00 87.17  ? 207 ARG A CG  1 
ATOM   1719  C  CD  . ARG A  1 216 ? 25.955  -54.711 39.897 1.00 88.42  ? 207 ARG A CD  1 
ATOM   1720  N  NE  . ARG A  1 216 ? 26.685  -54.876 41.149 1.00 92.19  ? 207 ARG A NE  1 
ATOM   1721  C  CZ  . ARG A  1 216 ? 26.113  -55.200 42.298 1.00 100.07 ? 207 ARG A CZ  1 
ATOM   1722  N  NH1 . ARG A  1 216 ? 26.848  -55.324 43.393 1.00 101.61 ? 207 ARG A NH1 1 
ATOM   1723  N  NH2 . ARG A  1 216 ? 24.803  -55.390 42.351 1.00 86.90  ? 207 ARG A NH2 1 
ATOM   1724  N  N   . ARG A  1 217 ? 26.746  -59.812 38.218 1.00 89.29  ? 208 ARG A N   1 
ATOM   1725  C  CA  . ARG A  1 217 ? 26.577  -61.236 38.490 1.00 101.08 ? 208 ARG A CA  1 
ATOM   1726  C  C   . ARG A  1 217 ? 26.655  -61.529 39.992 1.00 94.70  ? 208 ARG A C   1 
ATOM   1727  O  O   . ARG A  1 217 ? 25.715  -61.239 40.738 1.00 83.68  ? 208 ARG A O   1 
ATOM   1728  C  CB  . ARG A  1 217 ? 27.606  -62.063 37.712 1.00 96.22  ? 208 ARG A CB  1 
ATOM   1729  C  CG  . ARG A  1 217 ? 27.680  -61.737 36.232 0.00 94.01  ? 208 ARG A CG  1 
ATOM   1730  C  CD  . ARG A  1 217 ? 29.002  -62.209 35.653 0.00 95.64  ? 208 ARG A CD  1 
ATOM   1731  N  NE  . ARG A  1 217 ? 30.124  -61.773 36.480 0.00 95.46  ? 208 ARG A NE  1 
ATOM   1732  C  CZ  . ARG A  1 217 ? 31.326  -62.341 36.472 0.00 96.18  ? 208 ARG A CZ  1 
ATOM   1733  N  NH1 . ARG A  1 217 ? 31.571  -63.376 35.680 0.00 97.52  ? 208 ARG A NH1 1 
ATOM   1734  N  NH2 . ARG A  1 217 ? 32.285  -61.879 37.261 0.00 96.22  ? 208 ARG A NH2 1 
ATOM   1735  N  N   . LYS B  1 3   ? -21.022 -5.927  65.245 1.00 100.81 ? -6  LYS B N   1 
ATOM   1736  C  CA  . LYS B  1 3   ? -21.566 -7.147  65.819 1.00 106.51 ? -6  LYS B CA  1 
ATOM   1737  C  C   . LYS B  1 3   ? -20.441 -8.157  66.047 1.00 108.42 ? -6  LYS B C   1 
ATOM   1738  O  O   . LYS B  1 3   ? -19.309 -7.782  66.355 1.00 95.39  ? -6  LYS B O   1 
ATOM   1739  C  CB  . LYS B  1 3   ? -22.645 -7.722  64.890 1.00 106.76 ? -6  LYS B CB  1 
ATOM   1740  C  CG  . LYS B  1 3   ? -23.402 -8.937  65.435 1.00 117.48 ? -6  LYS B CG  1 
ATOM   1741  C  CD  . LYS B  1 3   ? -23.873 -8.705  66.862 1.00 122.76 ? -6  LYS B CD  1 
ATOM   1742  C  CE  . LYS B  1 3   ? -24.489 -9.959  67.469 1.00 117.91 ? -6  LYS B CE  1 
ATOM   1743  N  NZ  . LYS B  1 3   ? -24.951 -9.694  68.864 1.00 122.82 ? -6  LYS B NZ  1 
ATOM   1744  N  N   . ASP B  1 4   ? -20.774 -9.438  65.910 1.00 118.10 ? -5  ASP B N   1 
ATOM   1745  C  CA  . ASP B  1 4   ? -19.794 -10.514 65.838 1.00 114.91 ? -5  ASP B CA  1 
ATOM   1746  C  C   . ASP B  1 4   ? -19.235 -10.525 64.407 1.00 98.68  ? -5  ASP B C   1 
ATOM   1747  O  O   . ASP B  1 4   ? -18.318 -11.279 64.075 1.00 91.11  ? -5  ASP B O   1 
ATOM   1748  C  CB  . ASP B  1 4   ? -20.454 -11.851 66.207 1.00 114.30 ? -5  ASP B CB  1 
ATOM   1749  C  CG  . ASP B  1 4   ? -19.467 -12.860 66.778 1.00 117.06 ? -5  ASP B CG  1 
ATOM   1750  O  OD1 . ASP B  1 4   ? -19.155 -12.789 67.989 1.00 113.71 ? -5  ASP B OD1 1 
ATOM   1751  O  OD2 . ASP B  1 4   ? -19.015 -13.736 66.013 1.00 116.10 ? -5  ASP B OD2 1 
ATOM   1752  N  N   . ASP B  1 5   ? -19.819 -9.681  63.563 1.00 93.17  ? -4  ASP B N   1 
ATOM   1753  C  CA  . ASP B  1 5   ? -19.289 -9.426  62.231 1.00 95.70  ? -4  ASP B CA  1 
ATOM   1754  C  C   . ASP B  1 5   ? -18.032 -8.554  62.259 1.00 93.24  ? -4  ASP B C   1 
ATOM   1755  O  O   . ASP B  1 5   ? -17.038 -8.878  61.618 1.00 92.74  ? -4  ASP B O   1 
ATOM   1756  C  CB  . ASP B  1 5   ? -20.350 -8.771  61.346 1.00 96.57  ? -4  ASP B CB  1 
ATOM   1757  C  CG  . ASP B  1 5   ? -21.494 -9.702  61.029 1.00 96.06  ? -4  ASP B CG  1 
ATOM   1758  O  OD1 . ASP B  1 5   ? -21.259 -10.925 60.924 1.00 95.54  ? -4  ASP B OD1 1 
ATOM   1759  O  OD2 . ASP B  1 5   ? -22.630 -9.211  60.886 1.00 95.33  ? -4  ASP B OD2 1 
ATOM   1760  N  N   . ASP B  1 6   ? -18.077 -7.444  62.991 1.00 95.16  ? -3  ASP B N   1 
ATOM   1761  C  CA  . ASP B  1 6   ? -16.929 -6.541  63.086 1.00 88.44  ? -3  ASP B CA  1 
ATOM   1762  C  C   . ASP B  1 6   ? -15.645 -7.300  63.449 1.00 87.40  ? -3  ASP B C   1 
ATOM   1763  O  O   . ASP B  1 6   ? -14.570 -7.026  62.904 1.00 81.20  ? -3  ASP B O   1 
ATOM   1764  C  CB  . ASP B  1 6   ? -17.195 -5.440  64.115 1.00 85.91  ? -3  ASP B CB  1 
ATOM   1765  C  CG  . ASP B  1 6   ? -16.321 -4.222  63.899 1.00 84.19  ? -3  ASP B CG  1 
ATOM   1766  O  OD1 . ASP B  1 6   ? -15.327 -4.336  63.160 1.00 81.84  ? -3  ASP B OD1 1 
ATOM   1767  O  OD2 . ASP B  1 6   ? -16.612 -3.145  64.460 1.00 84.62  ? -3  ASP B OD2 1 
ATOM   1768  N  N   . ASP B  1 7   ? -15.775 -8.252  64.371 1.00 88.38  ? -2  ASP B N   1 
ATOM   1769  C  CA  . ASP B  1 7   ? -14.669 -9.105  64.792 1.00 81.07  ? -2  ASP B CA  1 
ATOM   1770  C  C   . ASP B  1 7   ? -14.044 -9.858  63.617 1.00 77.07  ? -2  ASP B C   1 
ATOM   1771  O  O   . ASP B  1 7   ? -12.831 -10.047 63.563 1.00 70.33  ? -2  ASP B O   1 
ATOM   1772  C  CB  . ASP B  1 7   ? -15.159 -10.100 65.850 1.00 91.02  ? -2  ASP B CB  1 
ATOM   1773  C  CG  . ASP B  1 7   ? -14.711 -9.733  67.266 1.00 92.07  ? -2  ASP B CG  1 
ATOM   1774  O  OD1 . ASP B  1 7   ? -14.337 -8.557  67.500 1.00 74.43  ? -2  ASP B OD1 1 
ATOM   1775  O  OD2 . ASP B  1 7   ? -14.740 -10.634 68.144 1.00 84.18  ? -2  ASP B OD2 1 
ATOM   1776  N  N   . LYS B  1 8   ? -14.882 -10.284 62.678 1.00 81.42  ? -1  LYS B N   1 
ATOM   1777  C  CA  . LYS B  1 8   ? -14.423 -10.992 61.481 1.00 77.64  ? -1  LYS B CA  1 
ATOM   1778  C  C   . LYS B  1 8   ? -13.769 -10.076 60.435 1.00 81.14  ? -1  LYS B C   1 
ATOM   1779  O  O   . LYS B  1 8   ? -12.859 -10.500 59.727 1.00 80.80  ? -1  LYS B O   1 
ATOM   1780  C  CB  . LYS B  1 8   ? -15.586 -11.747 60.831 1.00 77.22  ? -1  LYS B CB  1 
ATOM   1781  C  CG  . LYS B  1 8   ? -16.243 -12.778 61.726 1.00 85.34  ? -1  LYS B CG  1 
ATOM   1782  C  CD  . LYS B  1 8   ? -17.502 -13.343 61.083 1.00 87.67  ? -1  LYS B CD  1 
ATOM   1783  C  CE  . LYS B  1 8   ? -18.045 -14.506 61.903 1.00 83.70  ? -1  LYS B CE  1 
ATOM   1784  N  NZ  . LYS B  1 8   ? -19.510 -14.697 61.705 1.00 80.99  ? -1  LYS B NZ  1 
ATOM   1785  N  N   . LEU B  1 9   ? -14.241 -8.833  60.329 1.00 79.61  ? 0   LEU B N   1 
ATOM   1786  C  CA  . LEU B  1 9   ? -13.704 -7.887  59.353 1.00 71.40  ? 0   LEU B CA  1 
ATOM   1787  C  C   . LEU B  1 9   ? -12.301 -7.446  59.723 1.00 69.04  ? 0   LEU B C   1 
ATOM   1788  O  O   . LEU B  1 9   ? -11.427 -7.375  58.859 1.00 65.92  ? 0   LEU B O   1 
ATOM   1789  C  CB  . LEU B  1 9   ? -14.608 -6.665  59.214 1.00 79.10  ? 0   LEU B CB  1 
ATOM   1790  C  CG  . LEU B  1 9   ? -15.850 -6.828  58.340 1.00 87.24  ? 0   LEU B CG  1 
ATOM   1791  C  CD1 . LEU B  1 9   ? -16.623 -8.082  58.736 1.00 91.34  ? 0   LEU B CD1 1 
ATOM   1792  C  CD2 . LEU B  1 9   ? -16.739 -5.595  58.412 1.00 73.16  ? 0   LEU B CD2 1 
ATOM   1793  N  N   . HIS B  1 10  ? -12.098 -7.134  61.003 1.00 65.77  ? 1   HIS B N   1 
ATOM   1794  C  CA  . HIS B  1 10  ? -10.772 -6.800  61.516 1.00 66.40  ? 1   HIS B CA  1 
ATOM   1795  C  C   . HIS B  1 10  ? -9.890  -8.007  61.370 1.00 68.22  ? 1   HIS B C   1 
ATOM   1796  O  O   . HIS B  1 10  ? -8.688  -7.893  61.148 1.00 70.56  ? 1   HIS B O   1 
ATOM   1797  C  CB  . HIS B  1 10  ? -10.827 -6.447  62.997 1.00 68.85  ? 1   HIS B CB  1 
ATOM   1798  C  CG  . HIS B  1 10  ? -11.421 -5.101  63.280 1.00 70.29  ? 1   HIS B CG  1 
ATOM   1799  N  ND1 . HIS B  1 10  ? -10.649 -4.007  63.591 1.00 73.23  ? 1   HIS B ND1 1 
ATOM   1800  C  CD2 . HIS B  1 10  ? -12.702 -4.687  63.308 1.00 70.40  ? 1   HIS B CD2 1 
ATOM   1801  C  CE1 . HIS B  1 10  ? -11.440 -2.963  63.804 1.00 69.40  ? 1   HIS B CE1 1 
ATOM   1802  N  NE2 . HIS B  1 10  ? -12.689 -3.351  63.627 1.00 63.25  ? 1   HIS B NE2 1 
ATOM   1803  N  N   . SER B  1 11  ? -10.511 -9.168  61.532 1.00 70.89  ? 2   SER B N   1 
ATOM   1804  C  CA  . SER B  1 11  ? -9.831  -10.444 61.459 1.00 66.68  ? 2   SER B CA  1 
ATOM   1805  C  C   . SER B  1 11  ? -9.135  -10.571 60.107 1.00 68.29  ? 2   SER B C   1 
ATOM   1806  O  O   . SER B  1 11  ? -7.929  -10.827 60.040 1.00 69.18  ? 2   SER B O   1 
ATOM   1807  C  CB  . SER B  1 11  ? -10.848 -11.568 61.673 1.00 67.09  ? 2   SER B CB  1 
ATOM   1808  O  OG  . SER B  1 11  ? -10.223 -12.835 61.737 1.00 75.90  ? 2   SER B OG  1 
ATOM   1809  N  N   . GLN B  1 12  ? -9.904  -10.370 59.036 1.00 65.18  ? 3   GLN B N   1 
ATOM   1810  C  CA  . GLN B  1 12  ? -9.391  -10.443 57.673 1.00 65.57  ? 3   GLN B CA  1 
ATOM   1811  C  C   . GLN B  1 12  ? -8.384  -9.327  57.425 1.00 68.10  ? 3   GLN B C   1 
ATOM   1812  O  O   . GLN B  1 12  ? -7.259  -9.571  56.996 1.00 70.75  ? 3   GLN B O   1 
ATOM   1813  C  CB  . GLN B  1 12  ? -10.536 -10.334 56.656 1.00 70.19  ? 3   GLN B CB  1 
ATOM   1814  C  CG  . GLN B  1 12  ? -11.587 -11.428 56.730 1.00 66.87  ? 3   GLN B CG  1 
ATOM   1815  C  CD  . GLN B  1 12  ? -12.826 -11.090 55.923 1.00 72.52  ? 3   GLN B CD  1 
ATOM   1816  O  OE1 . GLN B  1 12  ? -12.739 -10.471 54.868 1.00 67.40  ? 3   GLN B OE1 1 
ATOM   1817  N  NE2 . GLN B  1 12  ? -13.989 -11.487 56.422 1.00 76.34  ? 3   GLN B NE2 1 
ATOM   1818  N  N   . ALA B  1 13  ? -8.796  -8.099  57.705 1.00 63.33  ? 4   ALA B N   1 
ATOM   1819  C  CA  . ALA B  1 13  ? -7.953  -6.940  57.469 1.00 65.26  ? 4   ALA B CA  1 
ATOM   1820  C  C   . ALA B  1 13  ? -6.586  -7.001  58.174 1.00 62.28  ? 4   ALA B C   1 
ATOM   1821  O  O   . ALA B  1 13  ? -5.568  -6.590  57.620 1.00 66.57  ? 4   ALA B O   1 
ATOM   1822  C  CB  . ALA B  1 13  ? -8.701  -5.690  57.855 1.00 52.27  ? 4   ALA B CB  1 
ATOM   1823  N  N   . ASN B  1 14  ? -6.559  -7.509  59.395 1.00 58.65  ? 5   ASN B N   1 
ATOM   1824  C  CA  . ASN B  1 14  ? -5.301  -7.629  60.127 1.00 64.64  ? 5   ASN B CA  1 
ATOM   1825  C  C   . ASN B  1 14  ? -4.353  -8.636  59.500 1.00 63.33  ? 5   ASN B C   1 
ATOM   1826  O  O   . ASN B  1 14  ? -3.133  -8.514  59.619 1.00 64.16  ? 5   ASN B O   1 
ATOM   1827  C  CB  . ASN B  1 14  ? -5.563  -8.022  61.581 1.00 66.64  ? 5   ASN B CB  1 
ATOM   1828  C  CG  . ASN B  1 14  ? -6.148  -6.891  62.386 1.00 62.95  ? 5   ASN B CG  1 
ATOM   1829  O  OD1 . ASN B  1 14  ? -5.873  -5.722  62.121 1.00 65.25  ? 5   ASN B OD1 1 
ATOM   1830  N  ND2 . ASN B  1 14  ? -6.958  -7.229  63.373 1.00 61.90  ? 5   ASN B ND2 1 
ATOM   1831  N  N   . LEU B  1 15  ? -4.933  -9.643  58.857 1.00 59.83  ? 6   LEU B N   1 
ATOM   1832  C  CA  . LEU B  1 15  ? -4.174  -10.701 58.213 1.00 57.83  ? 6   LEU B CA  1 
ATOM   1833  C  C   . LEU B  1 15  ? -3.608  -10.224 56.874 1.00 60.02  ? 6   LEU B C   1 
ATOM   1834  O  O   . LEU B  1 15  ? -2.441  -10.452 56.544 1.00 55.31  ? 6   LEU B O   1 
ATOM   1835  C  CB  . LEU B  1 15  ? -5.069  -11.924 58.022 1.00 54.70  ? 6   LEU B CB  1 
ATOM   1836  C  CG  . LEU B  1 15  ? -4.353  -13.162 57.495 1.00 53.30  ? 6   LEU B CG  1 
ATOM   1837  C  CD1 . LEU B  1 15  ? -3.200  -13.496 58.404 1.00 52.47  ? 6   LEU B CD1 1 
ATOM   1838  C  CD2 . LEU B  1 15  ? -5.304  -14.319 57.371 1.00 46.31  ? 6   LEU B CD2 1 
ATOM   1839  N  N   . MET B  1 16  ? -4.458  -9.560  56.100 1.00 66.29  ? 7   MET B N   1 
ATOM   1840  C  CA  . MET B  1 16  ? -4.038  -8.973  54.841 1.00 65.93  ? 7   MET B CA  1 
ATOM   1841  C  C   . MET B  1 16  ? -2.929  -7.996  55.145 1.00 60.13  ? 7   MET B C   1 
ATOM   1842  O  O   . MET B  1 16  ? -1.907  -7.959  54.460 1.00 64.51  ? 7   MET B O   1 
ATOM   1843  C  CB  . MET B  1 16  ? -5.211  -8.276  54.164 1.00 62.72  ? 7   MET B CB  1 
ATOM   1844  C  CG  . MET B  1 16  ? -6.127  -9.234  53.436 1.00 68.14  ? 7   MET B CG  1 
ATOM   1845  S  SD  . MET B  1 16  ? -7.597  -8.420  52.800 1.00 101.04 ? 7   MET B SD  1 
ATOM   1846  C  CE  . MET B  1 16  ? -8.409  -9.756  51.919 1.00 90.72  ? 7   MET B CE  1 
ATOM   1847  N  N   . ARG B  1 17  ? -3.135  -7.228  56.204 1.00 56.79  ? 8   ARG B N   1 
ATOM   1848  C  CA  . ARG B  1 17  ? -2.144  -6.282  56.663 1.00 61.50  ? 8   ARG B CA  1 
ATOM   1849  C  C   . ARG B  1 17  ? -0.851  -7.006  57.045 1.00 64.55  ? 8   ARG B C   1 
ATOM   1850  O  O   . ARG B  1 17  ? 0.230   -6.631  56.594 1.00 69.11  ? 8   ARG B O   1 
ATOM   1851  C  CB  . ARG B  1 17  ? -2.705  -5.452  57.828 1.00 64.96  ? 8   ARG B CB  1 
ATOM   1852  C  CG  . ARG B  1 17  ? -1.857  -4.234  58.226 1.00 64.86  ? 8   ARG B CG  1 
ATOM   1853  C  CD  . ARG B  1 17  ? -2.666  -3.214  59.024 1.00 57.16  ? 8   ARG B CD  1 
ATOM   1854  N  NE  . ARG B  1 17  ? -3.268  -3.783  60.225 1.00 62.55  ? 8   ARG B NE  1 
ATOM   1855  C  CZ  . ARG B  1 17  ? -2.649  -3.879  61.400 1.00 67.88  ? 8   ARG B CZ  1 
ATOM   1856  N  NH1 . ARG B  1 17  ? -1.402  -3.445  61.534 1.00 65.53  ? 8   ARG B NH1 1 
ATOM   1857  N  NH2 . ARG B  1 17  ? -3.271  -4.418  62.440 1.00 62.25  ? 8   ARG B NH2 1 
ATOM   1858  N  N   . LEU B  1 18  ? -0.959  -8.055  57.854 1.00 61.80  ? 9   LEU B N   1 
ATOM   1859  C  CA  . LEU B  1 18  ? 0.225   -8.772  58.324 1.00 61.75  ? 9   LEU B CA  1 
ATOM   1860  C  C   . LEU B  1 18  ? 1.000   -9.417  57.174 1.00 60.91  ? 9   LEU B C   1 
ATOM   1861  O  O   . LEU B  1 18  ? 2.233   -9.443  57.173 1.00 61.07  ? 9   LEU B O   1 
ATOM   1862  C  CB  . LEU B  1 18  ? -0.161  -9.813  59.380 1.00 60.05  ? 9   LEU B CB  1 
ATOM   1863  C  CG  . LEU B  1 18  ? 0.871   -10.887 59.750 1.00 59.01  ? 9   LEU B CG  1 
ATOM   1864  C  CD1 . LEU B  1 18  ? 2.183   -10.285 60.169 1.00 57.64  ? 9   LEU B CD1 1 
ATOM   1865  C  CD2 . LEU B  1 18  ? 0.349   -11.809 60.832 1.00 65.20  ? 9   LEU B CD2 1 
ATOM   1866  N  N   . LYS B  1 19  ? 0.276   -9.922  56.185 1.00 54.85  ? 10  LYS B N   1 
ATOM   1867  C  CA  . LYS B  1 19  ? 0.913   -10.593 55.072 1.00 56.95  ? 10  LYS B CA  1 
ATOM   1868  C  C   . LYS B  1 19  ? 1.643   -9.599  54.206 1.00 63.33  ? 10  LYS B C   1 
ATOM   1869  O  O   . LYS B  1 19  ? 2.680   -9.912  53.632 1.00 64.36  ? 10  LYS B O   1 
ATOM   1870  C  CB  . LYS B  1 19  ? -0.123  -11.352 54.265 1.00 59.23  ? 10  LYS B CB  1 
ATOM   1871  C  CG  . LYS B  1 19  ? -0.809  -12.434 55.061 1.00 58.55  ? 10  LYS B CG  1 
ATOM   1872  C  CD  . LYS B  1 19  ? -0.610  -13.787 54.441 1.00 58.28  ? 10  LYS B CD  1 
ATOM   1873  C  CE  . LYS B  1 19  ? -1.850  -14.215 53.677 1.00 58.82  ? 10  LYS B CE  1 
ATOM   1874  N  NZ  . LYS B  1 19  ? -1.728  -15.621 53.224 1.00 64.12  ? 10  LYS B NZ  1 
ATOM   1875  N  N   . SER B  1 20  ? 1.099   -8.388  54.130 1.00 70.60  ? 11  SER B N   1 
ATOM   1876  C  CA  . SER B  1 20  ? 1.717   -7.302  53.371 1.00 76.92  ? 11  SER B CA  1 
ATOM   1877  C  C   . SER B  1 20  ? 3.006   -6.782  54.011 1.00 74.48  ? 11  SER B C   1 
ATOM   1878  O  O   . SER B  1 20  ? 3.973   -6.501  53.316 1.00 85.93  ? 11  SER B O   1 
ATOM   1879  C  CB  . SER B  1 20  ? 0.742   -6.144  53.201 1.00 69.97  ? 11  SER B CB  1 
ATOM   1880  O  OG  . SER B  1 20  ? 0.602   -5.451  54.428 1.00 72.22  ? 11  SER B OG  1 
ATOM   1881  N  N   . ASP B  1 21  ? 3.030   -6.645  55.328 1.00 64.27  ? 12  ASP B N   1 
ATOM   1882  C  CA  . ASP B  1 21  ? 4.228   -6.123  55.972 1.00 77.02  ? 12  ASP B CA  1 
ATOM   1883  C  C   . ASP B  1 21  ? 5.408   -7.046  55.787 1.00 80.83  ? 12  ASP B C   1 
ATOM   1884  O  O   . ASP B  1 21  ? 6.538   -6.595  55.591 1.00 90.53  ? 12  ASP B O   1 
ATOM   1885  C  CB  . ASP B  1 21  ? 3.989   -5.853  57.452 1.00 73.99  ? 12  ASP B CB  1 
ATOM   1886  C  CG  . ASP B  1 21  ? 2.939   -4.804  57.664 1.00 81.40  ? 12  ASP B CG  1 
ATOM   1887  O  OD1 . ASP B  1 21  ? 2.543   -4.187  56.654 1.00 88.88  ? 12  ASP B OD1 1 
ATOM   1888  O  OD2 . ASP B  1 21  ? 2.505   -4.598  58.815 1.00 76.06  ? 12  ASP B OD2 1 
ATOM   1889  N  N   . LEU B  1 22  ? 5.147   -8.345  55.868 1.00 80.70  ? 13  LEU B N   1 
ATOM   1890  C  CA  . LEU B  1 22  ? 6.198   -9.324  55.665 1.00 73.86  ? 13  LEU B CA  1 
ATOM   1891  C  C   . LEU B  1 22  ? 6.631   -9.408  54.197 1.00 83.62  ? 13  LEU B C   1 
ATOM   1892  O  O   . LEU B  1 22  ? 7.804   -9.191  53.879 1.00 90.25  ? 13  LEU B O   1 
ATOM   1893  C  CB  . LEU B  1 22  ? 5.734   -10.684 56.187 1.00 67.81  ? 13  LEU B CB  1 
ATOM   1894  C  CG  . LEU B  1 22  ? 5.260   -10.696 57.652 1.00 66.52  ? 13  LEU B CG  1 
ATOM   1895  C  CD1 . LEU B  1 22  ? 4.769   -12.073 58.076 1.00 59.82  ? 13  LEU B CD1 1 
ATOM   1896  C  CD2 . LEU B  1 22  ? 6.345   -10.226 58.602 1.00 54.23  ? 13  LEU B CD2 1 
ATOM   1897  N  N   . PHE B  1 23  ? 5.674   -9.680  53.307 1.00 86.12  ? 14  PHE B N   1 
ATOM   1898  C  CA  . PHE B  1 23  ? 5.977   -9.963  51.895 1.00 88.71  ? 14  PHE B CA  1 
ATOM   1899  C  C   . PHE B  1 23  ? 6.184   -8.771  50.953 1.00 92.56  ? 14  PHE B C   1 
ATOM   1900  O  O   . PHE B  1 23  ? 7.096   -8.789  50.128 1.00 102.08 ? 14  PHE B O   1 
ATOM   1901  C  CB  . PHE B  1 23  ? 4.953   -10.951 51.314 1.00 80.19  ? 14  PHE B CB  1 
ATOM   1902  C  CG  . PHE B  1 23  ? 4.819   -12.220 52.118 1.00 68.19  ? 14  PHE B CG  1 
ATOM   1903  C  CD1 . PHE B  1 23  ? 5.917   -12.777 52.738 1.00 62.18  ? 14  PHE B CD1 1 
ATOM   1904  C  CD2 . PHE B  1 23  ? 3.591   -12.832 52.274 1.00 64.07  ? 14  PHE B CD2 1 
ATOM   1905  C  CE1 . PHE B  1 23  ? 5.792   -13.920 53.476 1.00 64.19  ? 14  PHE B CE1 1 
ATOM   1906  C  CE2 . PHE B  1 23  ? 3.463   -13.976 53.021 1.00 60.49  ? 14  PHE B CE2 1 
ATOM   1907  C  CZ  . PHE B  1 23  ? 4.559   -14.523 53.619 1.00 57.37  ? 14  PHE B CZ  1 
ATOM   1908  N  N   . ASN B  1 24  ? 5.318   -7.764  51.047 1.00 97.36  ? 15  ASN B N   1 
ATOM   1909  C  CA  . ASN B  1 24  ? 5.431   -6.552  50.210 1.00 103.00 ? 15  ASN B CA  1 
ATOM   1910  C  C   . ASN B  1 24  ? 6.406   -5.446  50.679 1.00 105.96 ? 15  ASN B C   1 
ATOM   1911  O  O   . ASN B  1 24  ? 7.124   -4.862  49.865 1.00 110.95 ? 15  ASN B O   1 
ATOM   1912  C  CB  . ASN B  1 24  ? 4.047   -5.972  49.878 1.00 94.34  ? 15  ASN B CB  1 
ATOM   1913  C  CG  . ASN B  1 24  ? 3.175   -6.952  49.105 1.00 97.80  ? 15  ASN B CG  1 
ATOM   1914  O  OD1 . ASN B  1 24  ? 3.643   -7.999  48.655 1.00 99.26  ? 15  ASN B OD1 1 
ATOM   1915  N  ND2 . ASN B  1 24  ? 1.902   -6.614  48.948 1.00 94.49  ? 15  ASN B ND2 1 
ATOM   1916  N  N   . ARG B  1 25  ? 6.425   -5.153  51.977 1.00 98.25  ? 16  ARG B N   1 
ATOM   1917  C  CA  . ARG B  1 25  ? 7.287   -4.091  52.489 1.00 100.03 ? 16  ARG B CA  1 
ATOM   1918  C  C   . ARG B  1 25  ? 8.673   -4.606  52.871 1.00 104.51 ? 16  ARG B C   1 
ATOM   1919  O  O   . ARG B  1 25  ? 9.528   -3.845  53.324 1.00 107.17 ? 16  ARG B O   1 
ATOM   1920  C  CB  . ARG B  1 25  ? 6.648   -3.365  53.677 1.00 102.47 ? 16  ARG B CB  1 
ATOM   1921  C  CG  . ARG B  1 25  ? 7.518   -2.220  54.214 1.00 112.36 ? 16  ARG B CG  1 
ATOM   1922  C  CD  . ARG B  1 25  ? 7.054   -1.671  55.565 1.00 103.73 ? 16  ARG B CD  1 
ATOM   1923  N  NE  . ARG B  1 25  ? 6.883   -2.716  56.571 1.00 99.80  ? 16  ARG B NE  1 
ATOM   1924  C  CZ  . ARG B  1 25  ? 7.834   -3.112  57.415 1.00 105.53 ? 16  ARG B CZ  1 
ATOM   1925  N  NH1 . ARG B  1 25  ? 9.037   -2.546  57.384 1.00 103.56 ? 16  ARG B NH1 1 
ATOM   1926  N  NH2 . ARG B  1 25  ? 7.583   -4.075  58.293 1.00 101.82 ? 16  ARG B NH2 1 
ATOM   1927  N  N   . SER B  1 26  ? 8.900   -5.899  52.695 1.00 102.14 ? 17  SER B N   1 
ATOM   1928  C  CA  . SER B  1 26  ? 10.239  -6.439  52.885 1.00 108.94 ? 17  SER B CA  1 
ATOM   1929  C  C   . SER B  1 26  ? 10.547  -7.411  51.749 1.00 109.79 ? 17  SER B C   1 
ATOM   1930  O  O   . SER B  1 26  ? 9.657   -8.128  51.286 1.00 104.71 ? 17  SER B O   1 
ATOM   1931  C  CB  . SER B  1 26  ? 10.384  -7.112  54.264 1.00 106.22 ? 17  SER B CB  1 
ATOM   1932  O  OG  . SER B  1 26  ? 10.402  -6.161  55.328 1.00 90.50  ? 17  SER B OG  1 
ATOM   1933  N  N   . PRO B  1 27  ? 11.808  -7.422  51.280 1.00 112.56 ? 18  PRO B N   1 
ATOM   1934  C  CA  . PRO B  1 27  ? 12.223  -8.334  50.209 1.00 104.90 ? 18  PRO B CA  1 
ATOM   1935  C  C   . PRO B  1 27  ? 12.177  -9.757  50.718 1.00 101.46 ? 18  PRO B C   1 
ATOM   1936  O  O   . PRO B  1 27  ? 12.159  -9.950  51.935 1.00 100.76 ? 18  PRO B O   1 
ATOM   1937  C  CB  . PRO B  1 27  ? 13.681  -7.937  49.951 1.00 95.74  ? 18  PRO B CB  1 
ATOM   1938  C  CG  . PRO B  1 27  ? 13.822  -6.568  50.520 1.00 102.62 ? 18  PRO B CG  1 
ATOM   1939  C  CD  . PRO B  1 27  ? 12.908  -6.545  51.708 1.00 108.17 ? 18  PRO B CD  1 
ATOM   1940  N  N   . MET B  1 28  ? 12.154  -10.735 49.818 1.00 96.53  ? 19  MET B N   1 
ATOM   1941  C  CA  . MET B  1 28  ? 12.239  -12.122 50.247 1.00 96.05  ? 19  MET B CA  1 
ATOM   1942  C  C   . MET B  1 28  ? 13.643  -12.420 50.798 1.00 92.65  ? 19  MET B C   1 
ATOM   1943  O  O   . MET B  1 28  ? 14.654  -11.891 50.314 1.00 80.54  ? 19  MET B O   1 
ATOM   1944  C  CB  . MET B  1 28  ? 11.860  -13.099 49.124 1.00 91.10  ? 19  MET B CB  1 
ATOM   1945  C  CG  . MET B  1 28  ? 11.780  -14.565 49.590 1.00 87.94  ? 19  MET B CG  1 
ATOM   1946  S  SD  . MET B  1 28  ? 11.381  -15.766 48.289 1.00 98.94  ? 19  MET B SD  1 
ATOM   1947  C  CE  . MET B  1 28  ? 9.674   -15.335 47.880 1.00 66.90  ? 19  MET B CE  1 
ATOM   1948  N  N   . TYR B  1 29  ? 13.677  -13.252 51.835 1.00 89.99  ? 20  TYR B N   1 
ATOM   1949  C  CA  . TYR B  1 29  ? 14.907  -13.694 52.474 1.00 80.93  ? 20  TYR B CA  1 
ATOM   1950  C  C   . TYR B  1 29  ? 15.814  -14.253 51.378 1.00 76.07  ? 20  TYR B C   1 
ATOM   1951  O  O   . TYR B  1 29  ? 15.378  -15.064 50.563 1.00 80.00  ? 20  TYR B O   1 
ATOM   1952  C  CB  . TYR B  1 29  ? 14.534  -14.737 53.548 1.00 79.81  ? 20  TYR B CB  1 
ATOM   1953  C  CG  . TYR B  1 29  ? 15.654  -15.511 54.224 1.00 73.11  ? 20  TYR B CG  1 
ATOM   1954  C  CD1 . TYR B  1 29  ? 16.462  -14.920 55.186 1.00 72.05  ? 20  TYR B CD1 1 
ATOM   1955  C  CD2 . TYR B  1 29  ? 15.859  -16.856 53.939 1.00 69.08  ? 20  TYR B CD2 1 
ATOM   1956  C  CE1 . TYR B  1 29  ? 17.467  -15.643 55.811 1.00 68.66  ? 20  TYR B CE1 1 
ATOM   1957  C  CE2 . TYR B  1 29  ? 16.853  -17.582 54.563 1.00 63.17  ? 20  TYR B CE2 1 
ATOM   1958  C  CZ  . TYR B  1 29  ? 17.651  -16.976 55.492 1.00 65.29  ? 20  TYR B CZ  1 
ATOM   1959  O  OH  . TYR B  1 29  ? 18.638  -17.714 56.107 1.00 73.98  ? 20  TYR B OH  1 
ATOM   1960  N  N   . PRO B  1 30  ? 17.060  -13.768 51.319 1.00 62.47  ? 21  PRO B N   1 
ATOM   1961  C  CA  . PRO B  1 30  ? 18.109  -14.124 50.363 1.00 61.51  ? 21  PRO B CA  1 
ATOM   1962  C  C   . PRO B  1 30  ? 18.606  -15.547 50.535 1.00 65.84  ? 21  PRO B C   1 
ATOM   1963  O  O   . PRO B  1 30  ? 19.302  -16.067 49.655 1.00 70.43  ? 21  PRO B O   1 
ATOM   1964  C  CB  . PRO B  1 30  ? 19.235  -13.165 50.720 1.00 60.69  ? 21  PRO B CB  1 
ATOM   1965  C  CG  . PRO B  1 30  ? 19.026  -12.870 52.118 1.00 60.38  ? 21  PRO B CG  1 
ATOM   1966  C  CD  . PRO B  1 30  ? 17.546  -12.791 52.298 1.00 69.51  ? 21  PRO B CD  1 
ATOM   1967  N  N   . GLY B  1 31  ? 18.283  -16.149 51.673 1.00 60.29  ? 22  GLY B N   1 
ATOM   1968  C  CA  . GLY B  1 31  ? 18.809  -17.450 52.025 1.00 62.90  ? 22  GLY B CA  1 
ATOM   1969  C  C   . GLY B  1 31  ? 19.871  -17.378 53.108 1.00 61.28  ? 22  GLY B C   1 
ATOM   1970  O  O   . GLY B  1 31  ? 20.370  -16.309 53.428 1.00 64.01  ? 22  GLY B O   1 
ATOM   1971  N  N   . PRO B  1 32  ? 20.223  -18.529 53.689 1.00 63.40  ? 23  PRO B N   1 
ATOM   1972  C  CA  . PRO B  1 32  ? 21.306  -18.597 54.673 1.00 60.09  ? 23  PRO B CA  1 
ATOM   1973  C  C   . PRO B  1 32  ? 22.666  -18.220 54.098 1.00 58.68  ? 23  PRO B C   1 
ATOM   1974  O  O   . PRO B  1 32  ? 22.939  -18.463 52.934 1.00 66.32  ? 23  PRO B O   1 
ATOM   1975  C  CB  . PRO B  1 32  ? 21.311  -20.077 55.073 1.00 59.70  ? 23  PRO B CB  1 
ATOM   1976  C  CG  . PRO B  1 32  ? 20.614  -20.784 53.960 1.00 58.10  ? 23  PRO B CG  1 
ATOM   1977  C  CD  . PRO B  1 32  ? 19.576  -19.838 53.495 1.00 61.31  ? 23  PRO B CD  1 
ATOM   1978  N  N   . THR B  1 33  ? 23.516  -17.628 54.920 1.00 65.45  ? 24  THR B N   1 
ATOM   1979  C  CA  . THR B  1 33  ? 24.910  -17.413 54.553 1.00 68.68  ? 24  THR B CA  1 
ATOM   1980  C  C   . THR B  1 33  ? 25.805  -17.861 55.710 1.00 70.99  ? 24  THR B C   1 
ATOM   1981  O  O   . THR B  1 33  ? 25.318  -18.141 56.814 1.00 62.74  ? 24  THR B O   1 
ATOM   1982  C  CB  . THR B  1 33  ? 25.203  -15.940 54.176 1.00 70.66  ? 24  THR B CB  1 
ATOM   1983  O  OG1 . THR B  1 33  ? 25.007  -15.092 55.313 1.00 70.79  ? 24  THR B OG1 1 
ATOM   1984  C  CG2 . THR B  1 33  ? 24.289  -15.487 53.059 1.00 61.84  ? 24  THR B CG2 1 
ATOM   1985  N  N   . LYS B  1 34  ? 27.105  -17.964 55.443 1.00 73.83  ? 25  LYS B N   1 
ATOM   1986  C  CA  . LYS B  1 34  ? 28.071  -18.354 56.465 1.00 74.95  ? 25  LYS B CA  1 
ATOM   1987  C  C   . LYS B  1 34  ? 27.970  -17.434 57.690 1.00 72.98  ? 25  LYS B C   1 
ATOM   1988  O  O   . LYS B  1 34  ? 28.205  -17.875 58.819 1.00 64.82  ? 25  LYS B O   1 
ATOM   1989  C  CB  . LYS B  1 34  ? 29.494  -18.373 55.886 1.00 73.14  ? 25  LYS B CB  1 
ATOM   1990  C  CG  . LYS B  1 34  ? 29.895  -17.066 55.209 1.00 83.84  ? 25  LYS B CG  1 
ATOM   1991  C  CD  . LYS B  1 34  ? 31.273  -17.135 54.546 1.00 86.90  ? 25  LYS B CD  1 
ATOM   1992  C  CE  . LYS B  1 34  ? 31.629  -15.778 53.918 1.00 94.50  ? 25  LYS B CE  1 
ATOM   1993  N  NZ  . LYS B  1 34  ? 33.005  -15.711 53.345 1.00 83.62  ? 25  LYS B NZ  1 
ATOM   1994  N  N   . ASP B  1 35  ? 27.604  -16.170 57.457 1.00 65.17  ? 26  ASP B N   1 
ATOM   1995  C  CA  . ASP B  1 35  ? 27.378  -15.210 58.534 1.00 62.19  ? 26  ASP B CA  1 
ATOM   1996  C  C   . ASP B  1 35  ? 25.925  -15.216 59.011 1.00 66.41  ? 26  ASP B C   1 
ATOM   1997  O  O   . ASP B  1 35  ? 25.584  -14.571 60.002 1.00 64.65  ? 26  ASP B O   1 
ATOM   1998  C  CB  . ASP B  1 35  ? 27.750  -13.781 58.107 1.00 75.74  ? 26  ASP B CB  1 
ATOM   1999  C  CG  . ASP B  1 35  ? 29.188  -13.653 57.598 1.00 87.47  ? 26  ASP B CG  1 
ATOM   2000  O  OD1 . ASP B  1 35  ? 30.084  -14.387 58.069 1.00 82.54  ? 26  ASP B OD1 1 
ATOM   2001  O  OD2 . ASP B  1 35  ? 29.421  -12.794 56.719 1.00 86.14  ? 26  ASP B OD2 1 
ATOM   2002  N  N   . ASP B  1 36  ? 25.060  -15.919 58.296 1.00 67.91  ? 27  ASP B N   1 
ATOM   2003  C  CA  . ASP B  1 36  ? 23.663  -16.038 58.705 1.00 68.23  ? 27  ASP B CA  1 
ATOM   2004  C  C   . ASP B  1 36  ? 23.155  -17.462 58.414 1.00 67.90  ? 27  ASP B C   1 
ATOM   2005  O  O   . ASP B  1 36  ? 22.395  -17.684 57.471 1.00 65.50  ? 27  ASP B O   1 
ATOM   2006  C  CB  . ASP B  1 36  ? 22.822  -14.966 57.996 1.00 66.23  ? 27  ASP B CB  1 
ATOM   2007  C  CG  . ASP B  1 36  ? 21.371  -14.953 58.446 1.00 70.41  ? 27  ASP B CG  1 
ATOM   2008  O  OD1 . ASP B  1 36  ? 21.112  -15.091 59.665 1.00 74.50  ? 27  ASP B OD1 1 
ATOM   2009  O  OD2 . ASP B  1 36  ? 20.489  -14.808 57.569 1.00 72.36  ? 27  ASP B OD2 1 
ATOM   2010  N  N   . PRO B  1 37  ? 23.601  -18.440 59.213 1.00 67.94  ? 28  PRO B N   1 
ATOM   2011  C  CA  . PRO B  1 37  ? 23.247  -19.839 59.002 1.00 62.35  ? 28  PRO B CA  1 
ATOM   2012  C  C   . PRO B  1 37  ? 21.863  -20.134 59.550 1.00 64.28  ? 28  PRO B C   1 
ATOM   2013  O  O   . PRO B  1 37  ? 21.385  -19.451 60.457 1.00 56.03  ? 28  PRO B O   1 
ATOM   2014  C  CB  . PRO B  1 37  ? 24.313  -20.583 59.797 1.00 60.29  ? 28  PRO B CB  1 
ATOM   2015  C  CG  . PRO B  1 37  ? 24.726  -19.616 60.871 1.00 59.02  ? 28  PRO B CG  1 
ATOM   2016  C  CD  . PRO B  1 37  ? 24.143  -18.247 60.562 1.00 64.53  ? 28  PRO B CD  1 
ATOM   2017  N  N   . LEU B  1 38  ? 21.235  -21.158 58.993 1.00 64.17  ? 29  LEU B N   1 
ATOM   2018  C  CA  . LEU B  1 38  ? 19.877  -21.520 59.344 1.00 61.30  ? 29  LEU B CA  1 
ATOM   2019  C  C   . LEU B  1 38  ? 19.810  -23.007 59.630 1.00 64.00  ? 29  LEU B C   1 
ATOM   2020  O  O   . LEU B  1 38  ? 20.459  -23.822 58.968 1.00 62.03  ? 29  LEU B O   1 
ATOM   2021  C  CB  . LEU B  1 38  ? 18.943  -21.185 58.184 1.00 65.66  ? 29  LEU B CB  1 
ATOM   2022  C  CG  . LEU B  1 38  ? 17.469  -21.576 58.302 1.00 64.39  ? 29  LEU B CG  1 
ATOM   2023  C  CD1 . LEU B  1 38  ? 16.711  -20.622 59.218 1.00 60.74  ? 29  LEU B CD1 1 
ATOM   2024  C  CD2 . LEU B  1 38  ? 16.830  -21.618 56.926 1.00 61.62  ? 29  LEU B CD2 1 
ATOM   2025  N  N   . THR B  1 39  ? 19.017  -23.364 60.624 1.00 63.95  ? 30  THR B N   1 
ATOM   2026  C  CA  . THR B  1 39  ? 18.860  -24.758 60.983 1.00 57.49  ? 30  THR B CA  1 
ATOM   2027  C  C   . THR B  1 39  ? 17.569  -25.312 60.391 1.00 54.93  ? 30  THR B C   1 
ATOM   2028  O  O   . THR B  1 39  ? 16.499  -24.731 60.523 1.00 60.48  ? 30  THR B O   1 
ATOM   2029  C  CB  . THR B  1 39  ? 18.917  -24.926 62.516 1.00 60.13  ? 30  THR B CB  1 
ATOM   2030  O  OG1 . THR B  1 39  ? 20.286  -24.885 62.931 1.00 61.65  ? 30  THR B OG1 1 
ATOM   2031  C  CG2 . THR B  1 39  ? 18.308  -26.236 62.947 1.00 61.10  ? 30  THR B CG2 1 
ATOM   2032  N  N   . VAL B  1 40  ? 17.670  -26.433 59.708 1.00 53.07  ? 31  VAL B N   1 
ATOM   2033  C  CA  . VAL B  1 40  ? 16.476  -27.042 59.162 1.00 59.67  ? 31  VAL B CA  1 
ATOM   2034  C  C   . VAL B  1 40  ? 16.223  -28.377 59.841 1.00 56.82  ? 31  VAL B C   1 
ATOM   2035  O  O   . VAL B  1 40  ? 17.129  -29.196 59.971 1.00 54.40  ? 31  VAL B O   1 
ATOM   2036  C  CB  . VAL B  1 40  ? 16.574  -27.225 57.625 1.00 53.37  ? 31  VAL B CB  1 
ATOM   2037  C  CG1 . VAL B  1 40  ? 15.246  -27.678 57.049 1.00 45.94  ? 31  VAL B CG1 1 
ATOM   2038  C  CG2 . VAL B  1 40  ? 16.995  -25.936 56.985 1.00 55.53  ? 31  VAL B CG2 1 
ATOM   2039  N  N   . TYR B  1 41  ? 14.991  -28.586 60.287 1.00 54.30  ? 32  TYR B N   1 
ATOM   2040  C  CA  . TYR B  1 41  ? 14.619  -29.880 60.818 1.00 57.74  ? 32  TYR B CA  1 
ATOM   2041  C  C   . TYR B  1 41  ? 13.862  -30.697 59.785 1.00 57.16  ? 32  TYR B C   1 
ATOM   2042  O  O   . TYR B  1 41  ? 12.860  -30.253 59.240 1.00 57.85  ? 32  TYR B O   1 
ATOM   2043  C  CB  . TYR B  1 41  ? 13.785  -29.741 62.088 1.00 65.30  ? 32  TYR B CB  1 
ATOM   2044  C  CG  . TYR B  1 41  ? 14.515  -29.135 63.271 1.00 70.20  ? 32  TYR B CG  1 
ATOM   2045  C  CD1 . TYR B  1 41  ? 15.132  -29.944 64.231 1.00 65.24  ? 32  TYR B CD1 1 
ATOM   2046  C  CD2 . TYR B  1 41  ? 14.564  -27.745 63.442 1.00 71.86  ? 32  TYR B CD2 1 
ATOM   2047  C  CE1 . TYR B  1 41  ? 15.786  -29.386 65.328 1.00 71.45  ? 32  TYR B CE1 1 
ATOM   2048  C  CE2 . TYR B  1 41  ? 15.214  -27.172 64.525 1.00 75.02  ? 32  TYR B CE2 1 
ATOM   2049  C  CZ  . TYR B  1 41  ? 15.823  -27.996 65.467 1.00 87.01  ? 32  TYR B CZ  1 
ATOM   2050  O  OH  . TYR B  1 41  ? 16.469  -27.417 66.537 1.00 74.55  ? 32  TYR B OH  1 
ATOM   2051  N  N   . LEU B  1 42  ? 14.350  -31.906 59.541 1.00 57.90  ? 33  LEU B N   1 
ATOM   2052  C  CA  . LEU B  1 42  ? 13.743  -32.816 58.595 1.00 54.07  ? 33  LEU B CA  1 
ATOM   2053  C  C   . LEU B  1 42  ? 13.242  -34.057 59.309 1.00 58.30  ? 33  LEU B C   1 
ATOM   2054  O  O   . LEU B  1 42  ? 14.015  -34.751 59.955 1.00 66.26  ? 33  LEU B O   1 
ATOM   2055  C  CB  . LEU B  1 42  ? 14.789  -33.232 57.575 1.00 54.10  ? 33  LEU B CB  1 
ATOM   2056  C  CG  . LEU B  1 42  ? 14.285  -33.405 56.151 1.00 58.18  ? 33  LEU B CG  1 
ATOM   2057  C  CD1 . LEU B  1 42  ? 13.977  -32.040 55.548 1.00 63.92  ? 33  LEU B CD1 1 
ATOM   2058  C  CD2 . LEU B  1 42  ? 15.311  -34.150 55.322 1.00 55.12  ? 33  LEU B CD2 1 
ATOM   2059  N  N   . SER B  1 43  ? 11.950  -34.339 59.193 1.00 58.55  ? 34  SER B N   1 
ATOM   2060  C  CA  . SER B  1 43  ? 11.369  -35.553 59.770 1.00 60.63  ? 34  SER B CA  1 
ATOM   2061  C  C   . SER B  1 43  ? 10.439  -36.289 58.771 1.00 59.99  ? 34  SER B C   1 
ATOM   2062  O  O   . SER B  1 43  ? 9.724   -35.656 57.999 1.00 58.32  ? 34  SER B O   1 
ATOM   2063  C  CB  . SER B  1 43  ? 10.618  -35.209 61.051 1.00 56.39  ? 34  SER B CB  1 
ATOM   2064  O  OG  . SER B  1 43  ? 10.204  -36.380 61.725 1.00 66.73  ? 34  SER B OG  1 
ATOM   2065  N  N   . PHE B  1 44  ? 10.427  -37.622 58.805 1.00 56.68  ? 35  PHE B N   1 
ATOM   2066  C  CA  . PHE B  1 44  ? 9.631   -38.405 57.852 1.00 55.55  ? 35  PHE B CA  1 
ATOM   2067  C  C   . PHE B  1 44  ? 8.481   -39.179 58.474 1.00 53.45  ? 35  PHE B C   1 
ATOM   2068  O  O   . PHE B  1 44  ? 8.468   -39.471 59.655 1.00 58.11  ? 35  PHE B O   1 
ATOM   2069  C  CB  . PHE B  1 44  ? 10.518  -39.374 57.089 1.00 50.50  ? 35  PHE B CB  1 
ATOM   2070  C  CG  . PHE B  1 44  ? 11.573  -38.698 56.286 1.00 53.15  ? 35  PHE B CG  1 
ATOM   2071  C  CD1 . PHE B  1 44  ? 11.297  -38.225 55.023 1.00 48.62  ? 35  PHE B CD1 1 
ATOM   2072  C  CD2 . PHE B  1 44  ? 12.837  -38.513 56.797 1.00 50.72  ? 35  PHE B CD2 1 
ATOM   2073  C  CE1 . PHE B  1 44  ? 12.265  -37.595 54.281 1.00 47.13  ? 35  PHE B CE1 1 
ATOM   2074  C  CE2 . PHE B  1 44  ? 13.807  -37.882 56.043 1.00 51.49  ? 35  PHE B CE2 1 
ATOM   2075  C  CZ  . PHE B  1 44  ? 13.512  -37.424 54.785 1.00 42.97  ? 35  PHE B CZ  1 
ATOM   2076  N  N   . SER B  1 45  ? 7.478   -39.454 57.667 1.00 53.11  ? 36  SER B N   1 
ATOM   2077  C  CA  . SER B  1 45  ? 6.368   -40.279 58.081 1.00 55.54  ? 36  SER B CA  1 
ATOM   2078  C  C   . SER B  1 45  ? 6.011   -41.155 56.870 1.00 55.17  ? 36  SER B C   1 
ATOM   2079  O  O   . SER B  1 45  ? 5.779   -40.637 55.784 1.00 53.66  ? 36  SER B O   1 
ATOM   2080  C  CB  . SER B  1 45  ? 5.217   -39.366 58.501 1.00 53.82  ? 36  SER B CB  1 
ATOM   2081  O  OG  . SER B  1 45  ? 4.108   -40.091 58.980 1.00 66.58  ? 36  SER B OG  1 
ATOM   2082  N  N   . LEU B  1 46  ? 6.014   -42.467 56.990 1.00 55.24  ? 37  LEU B N   1 
ATOM   2083  C  CA  . LEU B  1 46  ? 5.763   -43.267 55.811 1.00 55.35  ? 37  LEU B CA  1 
ATOM   2084  C  C   . LEU B  1 46  ? 4.350   -43.735 55.670 1.00 59.77  ? 37  LEU B C   1 
ATOM   2085  O  O   . LEU B  1 46  ? 3.791   -44.286 56.587 1.00 56.01  ? 37  LEU B O   1 
ATOM   2086  C  CB  . LEU B  1 46  ? 6.636   -44.490 55.795 1.00 54.71  ? 37  LEU B CB  1 
ATOM   2087  C  CG  . LEU B  1 46  ? 8.121   -44.360 56.044 1.00 65.73  ? 37  LEU B CG  1 
ATOM   2088  C  CD1 . LEU B  1 46  ? 8.807   -45.458 55.330 1.00 54.94  ? 37  LEU B CD1 1 
ATOM   2089  C  CD2 . LEU B  1 46  ? 8.603   -43.053 55.580 1.00 71.21  ? 37  LEU B CD2 1 
ATOM   2090  N  N   . LEU B  1 47  ? 3.783   -43.495 54.496 1.00 54.31  ? 38  LEU B N   1 
ATOM   2091  C  CA  . LEU B  1 47  ? 2.437   -43.894 54.157 1.00 57.20  ? 38  LEU B CA  1 
ATOM   2092  C  C   . LEU B  1 47  ? 2.338   -45.151 53.346 1.00 57.43  ? 38  LEU B C   1 
ATOM   2093  O  O   . LEU B  1 47  ? 1.471   -45.948 53.559 1.00 56.19  ? 38  LEU B O   1 
ATOM   2094  C  CB  . LEU B  1 47  ? 1.761   -42.799 53.378 1.00 51.88  ? 38  LEU B CB  1 
ATOM   2095  C  CG  . LEU B  1 47  ? 1.136   -41.750 54.242 1.00 57.75  ? 38  LEU B CG  1 
ATOM   2096  C  CD1 . LEU B  1 47  ? 2.226   -41.091 54.915 1.00 57.04  ? 38  LEU B CD1 1 
ATOM   2097  C  CD2 . LEU B  1 47  ? 0.472   -40.824 53.357 1.00 68.76  ? 38  LEU B CD2 1 
ATOM   2098  N  N   . ASP B  1 48  ? 3.205   -45.331 52.385 1.00 48.53  ? 39  ASP B N   1 
ATOM   2099  C  CA  . ASP B  1 48  ? 3.124   -46.548 51.602 1.00 50.23  ? 39  ASP B CA  1 
ATOM   2100  C  C   . ASP B  1 48  ? 4.422   -46.912 50.867 1.00 55.05  ? 39  ASP B C   1 
ATOM   2101  O  O   . ASP B  1 48  ? 5.096   -46.036 50.326 1.00 52.89  ? 39  ASP B O   1 
ATOM   2102  C  CB  . ASP B  1 48  ? 1.974   -46.394 50.599 1.00 46.56  ? 39  ASP B CB  1 
ATOM   2103  C  CG  . ASP B  1 48  ? 1.404   -47.716 50.153 1.00 56.18  ? 39  ASP B CG  1 
ATOM   2104  O  OD1 . ASP B  1 48  ? 1.617   -48.700 50.887 1.00 56.06  ? 39  ASP B OD1 1 
ATOM   2105  O  OD2 . ASP B  1 48  ? 0.747   -47.777 49.081 1.00 50.97  ? 39  ASP B OD2 1 
ATOM   2106  N  N   . ILE B  1 49  ? 4.733   -48.200 50.745 1.00 50.80  ? 40  ILE B N   1 
ATOM   2107  C  CA  . ILE B  1 49  ? 5.668   -48.582 49.696 1.00 53.43  ? 40  ILE B CA  1 
ATOM   2108  C  C   . ILE B  1 49  ? 4.850   -49.165 48.534 1.00 52.77  ? 40  ILE B C   1 
ATOM   2109  O  O   . ILE B  1 49  ? 4.345   -50.283 48.609 1.00 57.73  ? 40  ILE B O   1 
ATOM   2110  C  CB  . ILE B  1 49  ? 6.711   -49.593 50.176 1.00 47.47  ? 40  ILE B CB  1 
ATOM   2111  C  CG1 . ILE B  1 49  ? 7.549   -49.004 51.296 1.00 47.58  ? 40  ILE B CG1 1 
ATOM   2112  C  CG2 . ILE B  1 49  ? 7.627   -49.996 49.030 1.00 42.77  ? 40  ILE B CG2 1 
ATOM   2113  C  CD1 . ILE B  1 49  ? 8.724   -49.890 51.693 1.00 45.19  ? 40  ILE B CD1 1 
ATOM   2114  N  N   . VAL B  1 50  ? 4.735   -48.406 47.452 1.00 46.90  ? 41  VAL B N   1 
ATOM   2115  C  CA  . VAL B  1 50  ? 3.852   -48.808 46.367 1.00 55.98  ? 41  VAL B CA  1 
ATOM   2116  C  C   . VAL B  1 50  ? 4.389   -49.948 45.511 1.00 58.97  ? 41  VAL B C   1 
ATOM   2117  O  O   . VAL B  1 50  ? 3.705   -50.950 45.297 1.00 63.33  ? 41  VAL B O   1 
ATOM   2118  C  CB  . VAL B  1 50  ? 3.499   -47.646 45.450 1.00 50.68  ? 41  VAL B CB  1 
ATOM   2119  C  CG1 . VAL B  1 50  ? 2.406   -48.088 44.507 1.00 55.62  ? 41  VAL B CG1 1 
ATOM   2120  C  CG2 . VAL B  1 50  ? 3.047   -46.465 46.269 1.00 52.19  ? 41  VAL B CG2 1 
ATOM   2121  N  N   . LYS B  1 51  ? 5.608   -49.807 45.014 1.00 50.07  ? 42  LYS B N   1 
ATOM   2122  C  CA  . LYS B  1 51  ? 6.169   -50.907 44.262 1.00 57.53  ? 42  LYS B CA  1 
ATOM   2123  C  C   . LYS B  1 51  ? 7.650   -51.061 44.449 1.00 56.58  ? 42  LYS B C   1 
ATOM   2124  O  O   . LYS B  1 51  ? 8.376   -50.088 44.676 1.00 49.43  ? 42  LYS B O   1 
ATOM   2125  C  CB  . LYS B  1 51  ? 5.768   -50.894 42.761 1.00 61.96  ? 42  LYS B CB  1 
ATOM   2126  C  CG  . LYS B  1 51  ? 6.478   -49.926 41.782 1.00 59.15  ? 42  LYS B CG  1 
ATOM   2127  C  CD  . LYS B  1 51  ? 6.079   -50.299 40.328 1.00 63.66  ? 42  LYS B CD  1 
ATOM   2128  C  CE  . LYS B  1 51  ? 6.182   -49.150 39.320 1.00 69.96  ? 42  LYS B CE  1 
ATOM   2129  N  NZ  . LYS B  1 51  ? 7.579   -48.733 38.967 1.00 75.00  ? 42  LYS B NZ  1 
ATOM   2130  N  N   . ALA B  1 52  ? 8.072   -52.320 44.396 1.00 57.52  ? 43  ALA B N   1 
ATOM   2131  C  CA  . ALA B  1 52  ? 9.478   -52.656 44.311 1.00 59.27  ? 43  ALA B CA  1 
ATOM   2132  C  C   . ALA B  1 52  ? 9.638   -53.238 42.930 1.00 59.37  ? 43  ALA B C   1 
ATOM   2133  O  O   . ALA B  1 52  ? 8.898   -54.136 42.552 1.00 65.09  ? 43  ALA B O   1 
ATOM   2134  C  CB  . ALA B  1 52  ? 9.876   -53.673 45.385 1.00 54.81  ? 43  ALA B CB  1 
ATOM   2135  N  N   . ASP B  1 53  ? 10.574  -52.699 42.162 1.00 63.16  ? 44  ASP B N   1 
ATOM   2136  C  CA  . ASP B  1 53  ? 10.793  -53.155 40.805 1.00 65.70  ? 44  ASP B CA  1 
ATOM   2137  C  C   . ASP B  1 53  ? 12.166  -53.789 40.725 1.00 66.77  ? 44  ASP B C   1 
ATOM   2138  O  O   . ASP B  1 53  ? 13.183  -53.094 40.782 1.00 65.41  ? 44  ASP B O   1 
ATOM   2139  C  CB  . ASP B  1 53  ? 10.693  -51.977 39.849 1.00 64.44  ? 44  ASP B CB  1 
ATOM   2140  C  CG  . ASP B  1 53  ? 10.609  -52.398 38.415 1.00 65.80  ? 44  ASP B CG  1 
ATOM   2141  O  OD1 . ASP B  1 53  ? 9.493   -52.345 37.868 1.00 74.71  ? 44  ASP B OD1 1 
ATOM   2142  O  OD2 . ASP B  1 53  ? 11.655  -52.752 37.833 1.00 65.87  ? 44  ASP B OD2 1 
ATOM   2143  N  N   . SER B  1 54  ? 12.176  -55.112 40.571 1.00 69.06  ? 45  SER B N   1 
ATOM   2144  C  CA  . SER B  1 54  ? 13.393  -55.903 40.653 1.00 64.67  ? 45  SER B CA  1 
ATOM   2145  C  C   . SER B  1 54  ? 14.087  -55.934 39.301 1.00 63.53  ? 45  SER B C   1 
ATOM   2146  O  O   . SER B  1 54  ? 15.230  -56.364 39.210 1.00 59.63  ? 45  SER B O   1 
ATOM   2147  C  CB  . SER B  1 54  ? 13.083  -57.316 41.168 1.00 64.52  ? 45  SER B CB  1 
ATOM   2148  O  OG  . SER B  1 54  ? 11.805  -57.764 40.741 1.00 61.61  ? 45  SER B OG  1 
ATOM   2149  N  N   . SER B  1 55  ? 13.388  -55.452 38.268 1.00 60.41  ? 46  SER B N   1 
ATOM   2150  C  CA  . SER B  1 55  ? 13.937  -55.337 36.915 1.00 54.40  ? 46  SER B CA  1 
ATOM   2151  C  C   . SER B  1 55  ? 14.849  -54.129 36.716 1.00 64.54  ? 46  SER B C   1 
ATOM   2152  O  O   . SER B  1 55  ? 15.849  -54.228 36.000 1.00 60.31  ? 46  SER B O   1 
ATOM   2153  C  CB  . SER B  1 55  ? 12.792  -55.272 35.908 1.00 52.39  ? 46  SER B CB  1 
ATOM   2154  O  OG  . SER B  1 55  ? 11.678  -54.597 36.476 1.00 69.62  ? 46  SER B OG  1 
ATOM   2155  N  N   . THR B  1 56  ? 14.426  -52.971 37.244 1.00 64.88  ? 47  THR B N   1 
ATOM   2156  C  CA  . THR B  1 56  ? 15.258  -51.753 37.347 1.00 60.47  ? 47  THR B CA  1 
ATOM   2157  C  C   . THR B  1 56  ? 16.007  -51.463 38.683 1.00 60.69  ? 47  THR B C   1 
ATOM   2158  O  O   . THR B  1 56  ? 16.832  -50.547 38.745 1.00 60.40  ? 47  THR B O   1 
ATOM   2159  C  CB  . THR B  1 56  ? 14.436  -50.497 37.017 1.00 61.84  ? 47  THR B CB  1 
ATOM   2160  O  OG1 . THR B  1 56  ? 13.386  -50.345 37.975 1.00 68.71  ? 47  THR B OG1 1 
ATOM   2161  C  CG2 . THR B  1 56  ? 13.819  -50.581 35.624 1.00 59.02  ? 47  THR B CG2 1 
ATOM   2162  N  N   . ASN B  1 57  ? 15.718  -52.217 39.743 1.00 63.38  ? 48  ASN B N   1 
ATOM   2163  C  CA  . ASN B  1 57  ? 16.133  -51.817 41.087 1.00 57.84  ? 48  ASN B CA  1 
ATOM   2164  C  C   . ASN B  1 57  ? 15.721  -50.378 41.478 1.00 59.89  ? 48  ASN B C   1 
ATOM   2165  O  O   . ASN B  1 57  ? 16.583  -49.531 41.717 1.00 53.58  ? 48  ASN B O   1 
ATOM   2166  C  CB  . ASN B  1 57  ? 17.622  -52.045 41.332 1.00 60.18  ? 48  ASN B CB  1 
ATOM   2167  C  CG  . ASN B  1 57  ? 17.991  -53.517 41.443 1.00 61.92  ? 48  ASN B CG  1 
ATOM   2168  O  OD1 . ASN B  1 57  ? 17.133  -54.387 41.544 1.00 67.30  ? 48  ASN B OD1 1 
ATOM   2169  N  ND2 . ASN B  1 57  ? 19.286  -53.794 41.433 1.00 61.49  ? 48  ASN B ND2 1 
ATOM   2170  N  N   . GLU B  1 58  ? 14.418  -50.084 41.434 1.00 56.64  ? 49  GLU B N   1 
ATOM   2171  C  CA  . GLU B  1 58  ? 13.877  -48.863 42.029 1.00 53.48  ? 49  GLU B CA  1 
ATOM   2172  C  C   . GLU B  1 58  ? 12.648  -49.181 42.863 1.00 54.83  ? 49  GLU B C   1 
ATOM   2173  O  O   . GLU B  1 58  ? 11.825  -49.997 42.463 1.00 57.79  ? 49  GLU B O   1 
ATOM   2174  C  CB  . GLU B  1 58  ? 13.445  -47.852 40.966 1.00 53.78  ? 49  GLU B CB  1 
ATOM   2175  C  CG  . GLU B  1 58  ? 14.369  -47.677 39.781 1.00 57.07  ? 49  GLU B CG  1 
ATOM   2176  C  CD  . GLU B  1 58  ? 13.698  -46.908 38.644 1.00 63.17  ? 49  GLU B CD  1 
ATOM   2177  O  OE1 . GLU B  1 58  ? 12.646  -47.367 38.143 1.00 61.00  ? 49  GLU B OE1 1 
ATOM   2178  O  OE2 . GLU B  1 58  ? 14.211  -45.834 38.264 1.00 61.22  ? 49  GLU B OE2 1 
ATOM   2179  N  N   . VAL B  1 59  ? 12.509  -48.500 43.999 1.00 48.39  ? 50  VAL B N   1 
ATOM   2180  C  CA  . VAL B  1 59  ? 11.308  -48.604 44.836 1.00 48.08  ? 50  VAL B CA  1 
ATOM   2181  C  C   . VAL B  1 59  ? 10.514  -47.275 44.839 1.00 45.24  ? 50  VAL B C   1 
ATOM   2182  O  O   . VAL B  1 59  ? 11.085  -46.190 44.773 1.00 44.52  ? 50  VAL B O   1 
ATOM   2183  C  CB  . VAL B  1 59  ? 11.668  -49.068 46.287 1.00 52.78  ? 50  VAL B CB  1 
ATOM   2184  C  CG1 . VAL B  1 59  ? 10.496  -48.939 47.216 1.00 47.89  ? 50  VAL B CG1 1 
ATOM   2185  C  CG2 . VAL B  1 59  ? 12.149  -50.502 46.277 1.00 58.47  ? 50  VAL B CG2 1 
ATOM   2186  N  N   . ASP B  1 60  ? 9.192   -47.367 44.892 1.00 44.64  ? 51  ASP B N   1 
ATOM   2187  C  CA  . ASP B  1 60  ? 8.357   -46.173 44.907 1.00 49.25  ? 51  ASP B CA  1 
ATOM   2188  C  C   . ASP B  1 60  ? 7.730   -46.010 46.261 1.00 47.70  ? 51  ASP B C   1 
ATOM   2189  O  O   . ASP B  1 60  ? 7.033   -46.903 46.736 1.00 49.06  ? 51  ASP B O   1 
ATOM   2190  C  CB  . ASP B  1 60  ? 7.241   -46.247 43.862 1.00 53.30  ? 51  ASP B CB  1 
ATOM   2191  C  CG  . ASP B  1 60  ? 7.768   -46.228 42.453 1.00 55.11  ? 51  ASP B CG  1 
ATOM   2192  O  OD1 . ASP B  1 60  ? 9.000   -46.078 42.276 1.00 53.22  ? 51  ASP B OD1 1 
ATOM   2193  O  OD2 . ASP B  1 60  ? 6.943   -46.363 41.526 1.00 64.71  ? 51  ASP B OD2 1 
ATOM   2194  N  N   . LEU B  1 61  ? 7.949   -44.849 46.861 1.00 43.56  ? 52  LEU B N   1 
ATOM   2195  C  CA  . LEU B  1 61  ? 7.554   -44.617 48.235 1.00 45.43  ? 52  LEU B CA  1 
ATOM   2196  C  C   . LEU B  1 61  ? 6.670   -43.388 48.314 1.00 45.54  ? 52  LEU B C   1 
ATOM   2197  O  O   . LEU B  1 61  ? 6.946   -42.398 47.661 1.00 49.07  ? 52  LEU B O   1 
ATOM   2198  C  CB  . LEU B  1 61  ? 8.819   -44.432 49.071 1.00 48.82  ? 52  LEU B CB  1 
ATOM   2199  C  CG  . LEU B  1 61  ? 8.712   -43.997 50.530 1.00 56.96  ? 52  LEU B CG  1 
ATOM   2200  C  CD1 . LEU B  1 61  ? 8.277   -45.167 51.396 1.00 58.90  ? 52  LEU B CD1 1 
ATOM   2201  C  CD2 . LEU B  1 61  ? 10.041  -43.415 51.014 1.00 51.10  ? 52  LEU B CD2 1 
ATOM   2202  N  N   . VAL B  1 62  ? 5.594   -43.463 49.089 1.00 47.25  ? 53  VAL B N   1 
ATOM   2203  C  CA  . VAL B  1 62  ? 4.783   -42.289 49.437 1.00 47.76  ? 53  VAL B CA  1 
ATOM   2204  C  C   . VAL B  1 62  ? 4.982   -41.896 50.902 1.00 45.74  ? 53  VAL B C   1 
ATOM   2205  O  O   . VAL B  1 62  ? 4.735   -42.693 51.790 1.00 51.57  ? 53  VAL B O   1 
ATOM   2206  C  CB  . VAL B  1 62  ? 3.298   -42.590 49.272 1.00 48.42  ? 53  VAL B CB  1 
ATOM   2207  C  CG1 . VAL B  1 62  ? 2.449   -41.428 49.783 1.00 41.89  ? 53  VAL B CG1 1 
ATOM   2208  C  CG2 . VAL B  1 62  ? 3.002   -42.926 47.840 1.00 44.28  ? 53  VAL B CG2 1 
ATOM   2209  N  N   . TYR B  1 63  ? 5.403   -40.668 51.168 1.00 45.39  ? 54  TYR B N   1 
ATOM   2210  C  CA  . TYR B  1 63  ? 5.720   -40.276 52.534 1.00 49.57  ? 54  TYR B CA  1 
ATOM   2211  C  C   . TYR B  1 63  ? 5.464   -38.816 52.778 1.00 45.88  ? 54  TYR B C   1 
ATOM   2212  O  O   . TYR B  1 63  ? 5.333   -38.046 51.853 1.00 50.93  ? 54  TYR B O   1 
ATOM   2213  C  CB  . TYR B  1 63  ? 7.186   -40.560 52.828 1.00 48.79  ? 54  TYR B CB  1 
ATOM   2214  C  CG  . TYR B  1 63  ? 8.082   -39.815 51.910 1.00 46.48  ? 54  TYR B CG  1 
ATOM   2215  C  CD1 . TYR B  1 63  ? 8.732   -38.669 52.327 1.00 50.75  ? 54  TYR B CD1 1 
ATOM   2216  C  CD2 . TYR B  1 63  ? 8.249   -40.230 50.605 1.00 47.50  ? 54  TYR B CD2 1 
ATOM   2217  C  CE1 . TYR B  1 63  ? 9.551   -37.961 51.468 1.00 50.42  ? 54  TYR B CE1 1 
ATOM   2218  C  CE2 . TYR B  1 63  ? 9.054   -39.538 49.736 1.00 51.79  ? 54  TYR B CE2 1 
ATOM   2219  C  CZ  . TYR B  1 63  ? 9.708   -38.403 50.172 1.00 55.96  ? 54  TYR B CZ  1 
ATOM   2220  O  OH  . TYR B  1 63  ? 10.515  -37.718 49.295 1.00 56.37  ? 54  TYR B OH  1 
ATOM   2221  N  N   . TRP B  1 64  ? 5.387   -38.431 54.040 1.00 51.37  ? 55  TRP B N   1 
ATOM   2222  C  CA  . TRP B  1 64  ? 5.365   -37.022 54.378 1.00 50.35  ? 55  TRP B CA  1 
ATOM   2223  C  C   . TRP B  1 64  ? 6.746   -36.644 54.814 1.00 50.69  ? 55  TRP B C   1 
ATOM   2224  O  O   . TRP B  1 64  ? 7.417   -37.386 55.513 1.00 48.48  ? 55  TRP B O   1 
ATOM   2225  C  CB  . TRP B  1 64  ? 4.386   -36.731 55.492 1.00 55.05  ? 55  TRP B CB  1 
ATOM   2226  C  CG  . TRP B  1 64  ? 3.006   -37.131 55.153 1.00 64.48  ? 55  TRP B CG  1 
ATOM   2227  C  CD1 . TRP B  1 64  ? 2.457   -37.230 53.904 1.00 59.94  ? 55  TRP B CD1 1 
ATOM   2228  C  CD2 . TRP B  1 64  ? 1.985   -37.523 56.075 1.00 66.56  ? 55  TRP B CD2 1 
ATOM   2229  N  NE1 . TRP B  1 64  ? 1.147   -37.648 53.997 1.00 66.56  ? 55  TRP B NE1 1 
ATOM   2230  C  CE2 . TRP B  1 64  ? 0.836   -37.832 55.321 1.00 68.77  ? 55  TRP B CE2 1 
ATOM   2231  C  CE3 . TRP B  1 64  ? 1.928   -37.634 57.465 1.00 64.78  ? 55  TRP B CE3 1 
ATOM   2232  C  CZ2 . TRP B  1 64  ? -0.351  -38.245 55.917 1.00 67.01  ? 55  TRP B CZ2 1 
ATOM   2233  C  CZ3 . TRP B  1 64  ? 0.748   -38.043 58.047 1.00 68.73  ? 55  TRP B CZ3 1 
ATOM   2234  C  CH2 . TRP B  1 64  ? -0.372  -38.342 57.278 1.00 66.27  ? 55  TRP B CH2 1 
ATOM   2235  N  N   . GLU B  1 65  ? 7.178   -35.491 54.336 1.00 54.58  ? 56  GLU B N   1 
ATOM   2236  C  CA  . GLU B  1 65  ? 8.448   -34.927 54.692 1.00 48.69  ? 56  GLU B CA  1 
ATOM   2237  C  C   . GLU B  1 65  ? 8.115   -33.662 55.434 1.00 54.87  ? 56  GLU B C   1 
ATOM   2238  O  O   . GLU B  1 65  ? 7.581   -32.727 54.844 1.00 60.93  ? 56  GLU B O   1 
ATOM   2239  C  CB  . GLU B  1 65  ? 9.217   -34.601 53.428 1.00 48.28  ? 56  GLU B CB  1 
ATOM   2240  C  CG  . GLU B  1 65  ? 10.541  -33.952 53.667 1.00 57.22  ? 56  GLU B CG  1 
ATOM   2241  C  CD  . GLU B  1 65  ? 11.348  -33.855 52.396 1.00 62.36  ? 56  GLU B CD  1 
ATOM   2242  O  OE1 . GLU B  1 65  ? 11.044  -34.597 51.436 1.00 59.37  ? 56  GLU B OE1 1 
ATOM   2243  O  OE2 . GLU B  1 65  ? 12.288  -33.033 52.359 1.00 70.34  ? 56  GLU B OE2 1 
ATOM   2244  N  N   . GLN B  1 66  ? 8.392   -33.635 56.733 1.00 54.87  ? 57  GLN B N   1 
ATOM   2245  C  CA  . GLN B  1 66  ? 8.170   -32.432 57.510 1.00 55.43  ? 57  GLN B CA  1 
ATOM   2246  C  C   . GLN B  1 66  ? 9.427   -31.598 57.625 1.00 56.94  ? 57  GLN B C   1 
ATOM   2247  O  O   . GLN B  1 66  ? 10.448  -32.056 58.145 1.00 58.18  ? 57  GLN B O   1 
ATOM   2248  C  CB  . GLN B  1 66  ? 7.647   -32.731 58.907 1.00 62.54  ? 57  GLN B CB  1 
ATOM   2249  C  CG  . GLN B  1 66  ? 7.507   -31.450 59.711 1.00 70.11  ? 57  GLN B CG  1 
ATOM   2250  C  CD  . GLN B  1 66  ? 7.215   -31.678 61.164 1.00 74.86  ? 57  GLN B CD  1 
ATOM   2251  O  OE1 . GLN B  1 66  ? 6.771   -32.750 61.564 1.00 88.56  ? 57  GLN B OE1 1 
ATOM   2252  N  NE2 . GLN B  1 66  ? 7.465   -30.665 61.972 1.00 77.68  ? 57  GLN B NE2 1 
ATOM   2253  N  N   . GLN B  1 67  ? 9.322   -30.362 57.143 1.00 56.04  ? 58  GLN B N   1 
ATOM   2254  C  CA  . GLN B  1 67  ? 10.389  -29.377 57.206 1.00 53.71  ? 58  GLN B CA  1 
ATOM   2255  C  C   . GLN B  1 67  ? 10.001  -28.278 58.186 1.00 51.79  ? 58  GLN B C   1 
ATOM   2256  O  O   . GLN B  1 67  ? 8.864   -27.818 58.172 1.00 53.25  ? 58  GLN B O   1 
ATOM   2257  C  CB  . GLN B  1 67  ? 10.622  -28.813 55.811 1.00 55.02  ? 58  GLN B CB  1 
ATOM   2258  C  CG  . GLN B  1 67  ? 10.768  -29.906 54.778 1.00 57.68  ? 58  GLN B CG  1 
ATOM   2259  C  CD  . GLN B  1 67  ? 11.354  -29.395 53.499 1.00 64.00  ? 58  GLN B CD  1 
ATOM   2260  O  OE1 . GLN B  1 67  ? 11.752  -28.236 53.418 1.00 63.93  ? 58  GLN B OE1 1 
ATOM   2261  N  NE2 . GLN B  1 67  ? 11.413  -30.250 52.481 1.00 61.89  ? 58  GLN B NE2 1 
ATOM   2262  N  N   . SER B  1 68  ? 10.934  -27.900 59.061 1.00 58.95  ? 59  SER B N   1 
ATOM   2263  C  CA  . SER B  1 68  ? 10.734  -26.818 60.036 1.00 59.69  ? 59  SER B CA  1 
ATOM   2264  C  C   . SER B  1 68  ? 11.978  -25.950 60.072 1.00 59.76  ? 59  SER B C   1 
ATOM   2265  O  O   . SER B  1 68  ? 13.105  -26.448 60.023 1.00 61.72  ? 59  SER B O   1 
ATOM   2266  C  CB  . SER B  1 68  ? 10.465  -27.361 61.452 1.00 56.78  ? 59  SER B CB  1 
ATOM   2267  O  OG  . SER B  1 68  ? 9.259   -28.104 61.521 1.00 64.27  ? 59  SER B OG  1 
ATOM   2268  N  N   . TRP B  1 69  ? 11.773  -24.647 60.145 1.00 56.07  ? 60  TRP B N   1 
ATOM   2269  C  CA  . TRP B  1 69  ? 12.879  -23.716 60.308 1.00 58.97  ? 60  TRP B CA  1 
ATOM   2270  C  C   . TRP B  1 69  ? 12.346  -22.407 60.921 1.00 62.53  ? 60  TRP B C   1 
ATOM   2271  O  O   . TRP B  1 69  ? 11.133  -22.190 60.984 1.00 61.67  ? 60  TRP B O   1 
ATOM   2272  C  CB  . TRP B  1 69  ? 13.648  -23.509 58.984 1.00 57.47  ? 60  TRP B CB  1 
ATOM   2273  C  CG  . TRP B  1 69  ? 12.861  -22.803 57.912 1.00 56.21  ? 60  TRP B CG  1 
ATOM   2274  C  CD1 . TRP B  1 69  ? 12.783  -21.453 57.699 1.00 55.78  ? 60  TRP B CD1 1 
ATOM   2275  C  CD2 . TRP B  1 69  ? 12.034  -23.413 56.918 1.00 55.00  ? 60  TRP B CD2 1 
ATOM   2276  N  NE1 . TRP B  1 69  ? 11.955  -21.188 56.635 1.00 55.26  ? 60  TRP B NE1 1 
ATOM   2277  C  CE2 . TRP B  1 69  ? 11.483  -22.374 56.135 1.00 56.02  ? 60  TRP B CE2 1 
ATOM   2278  C  CE3 . TRP B  1 69  ? 11.702  -24.740 56.611 1.00 56.82  ? 60  TRP B CE3 1 
ATOM   2279  C  CZ2 . TRP B  1 69  ? 10.619  -22.621 55.065 1.00 56.74  ? 60  TRP B CZ2 1 
ATOM   2280  C  CZ3 . TRP B  1 69  ? 10.848  -24.987 55.548 1.00 52.03  ? 60  TRP B CZ3 1 
ATOM   2281  C  CH2 . TRP B  1 69  ? 10.316  -23.931 54.787 1.00 55.69  ? 60  TRP B CH2 1 
ATOM   2282  N  N   . LYS B  1 70  ? 13.238  -21.564 61.425 1.00 61.32  ? 61  LYS B N   1 
ATOM   2283  C  CA  . LYS B  1 70  ? 12.816  -20.325 62.056 1.00 56.31  ? 61  LYS B CA  1 
ATOM   2284  C  C   . LYS B  1 70  ? 13.550  -19.174 61.394 1.00 60.37  ? 61  LYS B C   1 
ATOM   2285  O  O   . LYS B  1 70  ? 14.771  -19.193 61.295 1.00 66.25  ? 61  LYS B O   1 
ATOM   2286  C  CB  . LYS B  1 70  ? 13.106  -20.390 63.557 1.00 62.20  ? 61  LYS B CB  1 
ATOM   2287  C  CG  . LYS B  1 70  ? 12.911  -19.103 64.340 1.00 70.82  ? 61  LYS B CG  1 
ATOM   2288  C  CD  . LYS B  1 70  ? 14.226  -18.352 64.525 1.00 72.05  ? 61  LYS B CD  1 
ATOM   2289  C  CE  . LYS B  1 70  ? 14.022  -17.091 65.364 1.00 81.97  ? 61  LYS B CE  1 
ATOM   2290  N  NZ  . LYS B  1 70  ? 13.617  -17.405 66.772 1.00 87.72  ? 61  LYS B NZ  1 
ATOM   2291  N  N   . LEU B  1 71  ? 12.812  -18.185 60.903 1.00 63.03  ? 62  LEU B N   1 
ATOM   2292  C  CA  . LEU B  1 71  ? 13.445  -17.016 60.288 1.00 64.54  ? 62  LEU B CA  1 
ATOM   2293  C  C   . LEU B  1 71  ? 13.162  -15.772 61.124 1.00 70.77  ? 62  LEU B C   1 
ATOM   2294  O  O   . LEU B  1 71  ? 12.023  -15.543 61.532 1.00 70.68  ? 62  LEU B O   1 
ATOM   2295  C  CB  . LEU B  1 71  ? 12.994  -16.817 58.829 1.00 53.97  ? 62  LEU B CB  1 
ATOM   2296  C  CG  . LEU B  1 71  ? 13.657  -17.675 57.738 1.00 53.71  ? 62  LEU B CG  1 
ATOM   2297  C  CD1 . LEU B  1 71  ? 13.132  -17.272 56.386 1.00 62.88  ? 62  LEU B CD1 1 
ATOM   2298  C  CD2 . LEU B  1 71  ? 15.166  -17.564 57.734 1.00 53.44  ? 62  LEU B CD2 1 
ATOM   2299  N  N   . ASN B  1 72  ? 14.198  -14.980 61.396 1.00 72.24  ? 63  ASN B N   1 
ATOM   2300  C  CA  . ASN B  1 72  ? 14.007  -13.759 62.158 1.00 60.63  ? 63  ASN B CA  1 
ATOM   2301  C  C   . ASN B  1 72  ? 13.079  -12.821 61.418 1.00 58.06  ? 63  ASN B C   1 
ATOM   2302  O  O   . ASN B  1 72  ? 12.208  -12.218 62.022 1.00 59.84  ? 63  ASN B O   1 
ATOM   2303  C  CB  . ASN B  1 72  ? 15.345  -13.103 62.504 1.00 71.83  ? 63  ASN B CB  1 
ATOM   2304  C  CG  . ASN B  1 72  ? 16.000  -13.734 63.739 1.00 78.60  ? 63  ASN B CG  1 
ATOM   2305  O  OD1 . ASN B  1 72  ? 15.304  -14.238 64.624 1.00 76.35  ? 63  ASN B OD1 1 
ATOM   2306  N  ND2 . ASN B  1 72  ? 17.333  -13.714 63.797 1.00 70.37  ? 63  ASN B ND2 1 
ATOM   2307  N  N   . SER B  1 73  ? 13.213  -12.762 60.096 1.00 61.70  ? 64  SER B N   1 
ATOM   2308  C  CA  . SER B  1 73  ? 12.399  -11.858 59.275 1.00 62.00  ? 64  SER B CA  1 
ATOM   2309  C  C   . SER B  1 73  ? 10.910  -12.221 59.152 1.00 60.69  ? 64  SER B C   1 
ATOM   2310  O  O   . SER B  1 73  ? 10.139  -11.454 58.581 1.00 57.20  ? 64  SER B O   1 
ATOM   2311  C  CB  . SER B  1 73  ? 13.007  -11.706 57.883 1.00 58.63  ? 64  SER B CB  1 
ATOM   2312  O  OG  . SER B  1 73  ? 13.181  -12.971 57.277 1.00 62.52  ? 64  SER B OG  1 
ATOM   2313  N  N   . LEU B  1 74  ? 10.517  -13.390 59.655 1.00 60.69  ? 65  LEU B N   1 
ATOM   2314  C  CA  . LEU B  1 74  ? 9.099   -13.780 59.744 1.00 60.83  ? 65  LEU B CA  1 
ATOM   2315  C  C   . LEU B  1 74  ? 8.432   -13.540 61.109 1.00 61.28  ? 65  LEU B C   1 
ATOM   2316  O  O   . LEU B  1 74  ? 7.279   -13.929 61.323 1.00 61.03  ? 65  LEU B O   1 
ATOM   2317  C  CB  . LEU B  1 74  ? 8.912   -15.239 59.343 1.00 60.89  ? 65  LEU B CB  1 
ATOM   2318  C  CG  . LEU B  1 74  ? 9.355   -15.574 57.934 1.00 54.98  ? 65  LEU B CG  1 
ATOM   2319  C  CD1 . LEU B  1 74  ? 9.161   -17.041 57.716 1.00 50.37  ? 65  LEU B CD1 1 
ATOM   2320  C  CD2 . LEU B  1 74  ? 8.554   -14.754 56.939 1.00 59.19  ? 65  LEU B CD2 1 
ATOM   2321  N  N   . MET B  1 75  ? 9.169   -12.946 62.039 1.00 61.52  ? 66  MET B N   1 
ATOM   2322  C  CA  . MET B  1 75  ? 8.634   -12.656 63.362 1.00 59.69  ? 66  MET B CA  1 
ATOM   2323  C  C   . MET B  1 75  ? 7.673   -11.470 63.394 1.00 65.76  ? 66  MET B C   1 
ATOM   2324  O  O   . MET B  1 75  ? 7.780   -10.535 62.593 1.00 53.25  ? 66  MET B O   1 
ATOM   2325  C  CB  . MET B  1 75  ? 9.769   -12.382 64.335 1.00 58.65  ? 66  MET B CB  1 
ATOM   2326  C  CG  . MET B  1 75  ? 10.732  -13.526 64.486 1.00 69.80  ? 66  MET B CG  1 
ATOM   2327  S  SD  . MET B  1 75  ? 11.931  -13.149 65.752 1.00 80.02  ? 66  MET B SD  1 
ATOM   2328  C  CE  . MET B  1 75  ? 10.818  -12.782 67.111 1.00 65.28  ? 66  MET B CE  1 
ATOM   2329  N  N   . TRP B  1 76  ? 6.733   -11.516 64.335 1.00 66.63  ? 67  TRP B N   1 
ATOM   2330  C  CA  . TRP B  1 76  ? 5.897   -10.360 64.623 1.00 64.04  ? 67  TRP B CA  1 
ATOM   2331  C  C   . TRP B  1 76  ? 5.295   -10.367 66.032 1.00 69.03  ? 67  TRP B C   1 
ATOM   2332  O  O   . TRP B  1 76  ? 5.314   -11.375 66.745 1.00 62.39  ? 67  TRP B O   1 
ATOM   2333  C  CB  . TRP B  1 76  ? 4.825   -10.167 63.554 1.00 56.66  ? 67  TRP B CB  1 
ATOM   2334  C  CG  . TRP B  1 76  ? 3.672   -11.094 63.674 1.00 64.43  ? 67  TRP B CG  1 
ATOM   2335  C  CD1 . TRP B  1 76  ? 2.505   -10.857 64.324 1.00 64.59  ? 67  TRP B CD1 1 
ATOM   2336  C  CD2 . TRP B  1 76  ? 3.558   -12.411 63.110 1.00 71.35  ? 67  TRP B CD2 1 
ATOM   2337  N  NE1 . TRP B  1 76  ? 1.668   -11.938 64.211 1.00 64.50  ? 67  TRP B NE1 1 
ATOM   2338  C  CE2 . TRP B  1 76  ? 2.290   -12.908 63.469 1.00 66.55  ? 67  TRP B CE2 1 
ATOM   2339  C  CE3 . TRP B  1 76  ? 4.402   -13.216 62.333 1.00 63.89  ? 67  TRP B CE3 1 
ATOM   2340  C  CZ2 . TRP B  1 76  ? 1.847   -14.166 63.082 1.00 58.60  ? 67  TRP B CZ2 1 
ATOM   2341  C  CZ3 . TRP B  1 76  ? 3.961   -14.458 61.957 1.00 60.03  ? 67  TRP B CZ3 1 
ATOM   2342  C  CH2 . TRP B  1 76  ? 2.696   -14.924 62.330 1.00 58.53  ? 67  TRP B CH2 1 
ATOM   2343  N  N   . ASP B  1 77  ? 4.806   -9.201  66.438 1.00 74.89  ? 68  ASP B N   1 
ATOM   2344  C  CA  . ASP B  1 77  ? 4.100   -9.063  67.696 1.00 68.43  ? 68  ASP B CA  1 
ATOM   2345  C  C   . ASP B  1 77  ? 2.615   -9.208  67.448 1.00 68.42  ? 68  ASP B C   1 
ATOM   2346  O  O   . ASP B  1 77  ? 2.004   -8.354  66.802 1.00 63.65  ? 68  ASP B O   1 
ATOM   2347  C  CB  . ASP B  1 77  ? 4.378   -7.699  68.305 1.00 77.18  ? 68  ASP B CB  1 
ATOM   2348  C  CG  . ASP B  1 77  ? 3.697   -7.509  69.645 1.00 85.46  ? 68  ASP B CG  1 
ATOM   2349  O  OD1 . ASP B  1 77  ? 3.247   -8.517  70.246 1.00 77.76  ? 68  ASP B OD1 1 
ATOM   2350  O  OD2 . ASP B  1 77  ? 3.626   -6.343  70.097 1.00 89.90  ? 68  ASP B OD2 1 
ATOM   2351  N  N   . PRO B  1 78  ? 2.038   -10.307 67.946 1.00 64.65  ? 69  PRO B N   1 
ATOM   2352  C  CA  . PRO B  1 78  ? 0.608   -10.607 67.868 1.00 69.57  ? 69  PRO B CA  1 
ATOM   2353  C  C   . PRO B  1 78  ? -0.273  -9.466  68.373 1.00 75.99  ? 69  PRO B C   1 
ATOM   2354  O  O   . PRO B  1 78  ? -1.270  -9.188  67.710 1.00 72.07  ? 69  PRO B O   1 
ATOM   2355  C  CB  . PRO B  1 78  ? 0.469   -11.840 68.754 1.00 68.09  ? 69  PRO B CB  1 
ATOM   2356  C  CG  . PRO B  1 78  ? 1.776   -12.529 68.608 1.00 64.48  ? 69  PRO B CG  1 
ATOM   2357  C  CD  . PRO B  1 78  ? 2.806   -11.437 68.491 1.00 61.29  ? 69  PRO B CD  1 
ATOM   2358  N  N   . ASN B  1 79  ? 0.084   -8.821  69.490 1.00 78.73  ? 70  ASN B N   1 
ATOM   2359  C  CA  . ASN B  1 79  ? -0.684  -7.682  70.013 1.00 75.56  ? 70  ASN B CA  1 
ATOM   2360  C  C   . ASN B  1 79  ? -0.924  -6.632  68.935 1.00 77.52  ? 70  ASN B C   1 
ATOM   2361  O  O   . ASN B  1 79  ? -1.967  -5.977  68.896 1.00 72.38  ? 70  ASN B O   1 
ATOM   2362  C  CB  . ASN B  1 79  ? 0.047   -7.012  71.176 1.00 74.14  ? 70  ASN B CB  1 
ATOM   2363  C  CG  . ASN B  1 79  ? 0.293   -7.950  72.337 1.00 86.22  ? 70  ASN B CG  1 
ATOM   2364  O  OD1 . ASN B  1 79  ? -0.530  -8.811  72.638 1.00 89.02  ? 70  ASN B OD1 1 
ATOM   2365  N  ND2 . ASN B  1 79  ? 1.433   -7.783  73.003 1.00 82.76  ? 70  ASN B ND2 1 
ATOM   2366  N  N   . GLU B  1 80  ? 0.066   -6.481  68.064 1.00 75.28  ? 71  GLU B N   1 
ATOM   2367  C  CA  . GLU B  1 80  ? 0.054   -5.461  67.031 1.00 68.68  ? 71  GLU B CA  1 
ATOM   2368  C  C   . GLU B  1 80  ? -0.798  -5.821  65.789 1.00 75.99  ? 71  GLU B C   1 
ATOM   2369  O  O   . GLU B  1 80  ? -1.251  -4.923  65.072 1.00 70.82  ? 71  GLU B O   1 
ATOM   2370  C  CB  . GLU B  1 80  ? 1.496   -5.131  66.646 1.00 72.10  ? 71  GLU B CB  1 
ATOM   2371  C  CG  . GLU B  1 80  ? 1.692   -3.790  65.965 1.00 88.28  ? 71  GLU B CG  1 
ATOM   2372  C  CD  . GLU B  1 80  ? 3.140   -3.575  65.532 1.00 101.15 ? 71  GLU B CD  1 
ATOM   2373  O  OE1 . GLU B  1 80  ? 4.045   -4.136  66.199 1.00 93.85  ? 71  GLU B OE1 1 
ATOM   2374  O  OE2 . GLU B  1 80  ? 3.372   -2.858  64.526 1.00 89.67  ? 71  GLU B OE2 1 
ATOM   2375  N  N   . TYR B  1 81  ? -0.959  -7.109  65.469 1.00 80.48  ? 72  TYR B N   1 
ATOM   2376  C  CA  . TYR B  1 81  ? -2.024  -7.488  64.540 1.00 71.37  ? 72  TYR B CA  1 
ATOM   2377  C  C   . TYR B  1 81  ? -3.029  -8.401  65.215 1.00 69.06  ? 72  TYR B C   1 
ATOM   2378  O  O   . TYR B  1 81  ? -2.772  -9.590  65.307 1.00 82.44  ? 72  TYR B O   1 
ATOM   2379  C  CB  . TYR B  1 81  ? -1.422  -8.287  63.378 1.00 68.12  ? 72  TYR B CB  1 
ATOM   2380  C  CG  . TYR B  1 81  ? -0.211  -7.660  62.716 1.00 62.13  ? 72  TYR B CG  1 
ATOM   2381  C  CD1 . TYR B  1 81  ? -0.329  -7.006  61.499 1.00 61.61  ? 72  TYR B CD1 1 
ATOM   2382  C  CD2 . TYR B  1 81  ? 1.047   -7.734  63.300 1.00 62.59  ? 72  TYR B CD2 1 
ATOM   2383  C  CE1 . TYR B  1 81  ? 0.763   -6.427  60.893 1.00 66.76  ? 72  TYR B CE1 1 
ATOM   2384  C  CE2 . TYR B  1 81  ? 2.148   -7.155  62.704 1.00 65.04  ? 72  TYR B CE2 1 
ATOM   2385  C  CZ  . TYR B  1 81  ? 1.998   -6.502  61.499 1.00 68.29  ? 72  TYR B CZ  1 
ATOM   2386  O  OH  . TYR B  1 81  ? 3.086   -5.926  60.889 1.00 65.74  ? 72  TYR B OH  1 
ATOM   2387  N  N   . GLY B  1 82  ? -4.196  -7.907  65.619 1.00 69.14  ? 73  GLY B N   1 
ATOM   2388  C  CA  . GLY B  1 82  ? -5.335  -8.775  65.899 1.00 72.01  ? 73  GLY B CA  1 
ATOM   2389  C  C   . GLY B  1 82  ? -5.101  -9.934  66.857 1.00 75.81  ? 73  GLY B C   1 
ATOM   2390  O  O   . GLY B  1 82  ? -5.968  -10.807 66.952 1.00 76.68  ? 73  GLY B O   1 
ATOM   2391  N  N   . ASN B  1 83  ? -3.984  -9.960  67.572 1.00 72.24  ? 74  ASN B N   1 
ATOM   2392  C  CA  A ASN B  1 83  ? -3.511  -11.140 68.288 0.70 77.95  ? 74  ASN B CA  1 
ATOM   2393  C  CA  B ASN B  1 83  ? -3.578  -11.165 68.331 0.30 78.09  ? 74  ASN B CA  1 
ATOM   2394  C  C   . ASN B  1 83  ? -3.573  -12.423 67.456 1.00 76.52  ? 74  ASN B C   1 
ATOM   2395  O  O   . ASN B  1 83  ? -4.071  -13.461 67.876 1.00 78.86  ? 74  ASN B O   1 
ATOM   2396  C  CB  A ASN B  1 83  ? -4.198  -11.295 69.644 0.70 84.53  ? 74  ASN B CB  1 
ATOM   2397  C  CB  B ASN B  1 83  ? -4.349  -11.376 69.648 0.30 84.55  ? 74  ASN B CB  1 
ATOM   2398  C  CG  A ASN B  1 83  ? -3.415  -10.612 70.750 0.70 87.62  ? 74  ASN B CG  1 
ATOM   2399  C  CG  B ASN B  1 83  ? -3.748  -12.514 70.501 0.30 88.34  ? 74  ASN B CG  1 
ATOM   2400  O  OD1 A ASN B  1 83  ? -2.496  -11.185 71.311 0.70 88.41  ? 74  ASN B OD1 1 
ATOM   2401  O  OD1 B ASN B  1 83  ? -2.638  -12.988 70.270 0.30 87.32  ? 74  ASN B OD1 1 
ATOM   2402  N  ND2 A ASN B  1 83  ? -3.744  -9.372  71.029 0.70 90.81  ? 74  ASN B ND2 1 
ATOM   2403  N  ND2 B ASN B  1 83  ? -4.534  -12.968 71.508 0.30 94.37  ? 74  ASN B ND2 1 
ATOM   2404  N  N   . ILE B  1 84  ? -3.061  -12.302 66.227 1.00 78.01  ? 75  ILE B N   1 
ATOM   2405  C  CA  . ILE B  1 84  ? -2.973  -13.402 65.273 1.00 68.06  ? 75  ILE B CA  1 
ATOM   2406  C  C   . ILE B  1 84  ? -1.636  -14.034 65.530 1.00 68.78  ? 75  ILE B C   1 
ATOM   2407  O  O   . ILE B  1 84  ? -0.616  -13.377 65.383 1.00 71.35  ? 75  ILE B O   1 
ATOM   2408  C  CB  . ILE B  1 84  ? -2.903  -12.861 63.814 1.00 65.69  ? 75  ILE B CB  1 
ATOM   2409  C  CG1 . ILE B  1 84  ? -4.262  -12.391 63.297 1.00 64.64  ? 75  ILE B CG1 1 
ATOM   2410  C  CG2 . ILE B  1 84  ? -2.352  -13.914 62.877 1.00 67.14  ? 75  ILE B CG2 1 
ATOM   2411  C  CD1 . ILE B  1 84  ? -4.272  -12.137 61.798 1.00 64.05  ? 75  ILE B CD1 1 
ATOM   2412  N  N   . THR B  1 85  ? -1.637  -15.273 66.002 1.00 67.75  ? 76  THR B N   1 
ATOM   2413  C  CA  . THR B  1 85  ? -0.374  -15.927 66.276 1.00 66.94  ? 76  THR B CA  1 
ATOM   2414  C  C   . THR B  1 85  ? 0.201   -16.784 65.159 1.00 65.99  ? 76  THR B C   1 
ATOM   2415  O  O   . THR B  1 85  ? 1.369   -17.162 65.215 1.00 67.28  ? 76  THR B O   1 
ATOM   2416  C  CB  . THR B  1 85  ? -0.495  -16.765 67.528 1.00 70.11  ? 76  THR B CB  1 
ATOM   2417  O  OG1 . THR B  1 85  ? -1.831  -17.283 67.604 1.00 63.00  ? 76  THR B OG1 1 
ATOM   2418  C  CG2 . THR B  1 85  ? -0.204  -15.901 68.751 1.00 69.51  ? 76  THR B CG2 1 
ATOM   2419  N  N   . ASP B  1 86  ? -0.612  -17.112 64.162 1.00 61.03  ? 77  ASP B N   1 
ATOM   2420  C  CA  . ASP B  1 86  ? -0.120  -17.872 63.015 1.00 56.29  ? 77  ASP B CA  1 
ATOM   2421  C  C   . ASP B  1 86  ? -1.045  -17.751 61.820 1.00 51.84  ? 77  ASP B C   1 
ATOM   2422  O  O   . ASP B  1 86  ? -2.191  -17.351 61.979 1.00 54.43  ? 77  ASP B O   1 
ATOM   2423  C  CB  . ASP B  1 86  ? 0.169   -19.337 63.374 1.00 65.14  ? 77  ASP B CB  1 
ATOM   2424  C  CG  . ASP B  1 86  ? -1.070  -20.112 63.759 1.00 67.21  ? 77  ASP B CG  1 
ATOM   2425  O  OD1 . ASP B  1 86  ? -2.154  -19.859 63.199 1.00 60.23  ? 77  ASP B OD1 1 
ATOM   2426  O  OD2 . ASP B  1 86  ? -0.946  -20.995 64.624 1.00 66.46  ? 77  ASP B OD2 1 
ATOM   2427  N  N   . PHE B  1 87  ? -0.544  -18.084 60.632 1.00 48.97  ? 78  PHE B N   1 
ATOM   2428  C  CA  . PHE B  1 87  ? -1.355  -18.056 59.412 1.00 54.77  ? 78  PHE B CA  1 
ATOM   2429  C  C   . PHE B  1 87  ? -0.819  -19.045 58.370 1.00 52.71  ? 78  PHE B C   1 
ATOM   2430  O  O   . PHE B  1 87  ? 0.351   -19.420 58.419 1.00 51.86  ? 78  PHE B O   1 
ATOM   2431  C  CB  . PHE B  1 87  ? -1.382  -16.637 58.841 1.00 51.97  ? 78  PHE B CB  1 
ATOM   2432  C  CG  . PHE B  1 87  ? -0.050  -16.171 58.325 1.00 56.33  ? 78  PHE B CG  1 
ATOM   2433  C  CD1 . PHE B  1 87  ? 0.817   -15.465 59.144 1.00 49.26  ? 78  PHE B CD1 1 
ATOM   2434  C  CD2 . PHE B  1 87  ? 0.342   -16.455 57.018 1.00 55.33  ? 78  PHE B CD2 1 
ATOM   2435  C  CE1 . PHE B  1 87  ? 2.044   -15.049 58.674 1.00 52.90  ? 78  PHE B CE1 1 
ATOM   2436  C  CE2 . PHE B  1 87  ? 1.573   -16.042 56.539 1.00 53.76  ? 78  PHE B CE2 1 
ATOM   2437  C  CZ  . PHE B  1 87  ? 2.423   -15.337 57.363 1.00 56.71  ? 78  PHE B CZ  1 
ATOM   2438  N  N   . ARG B  1 88  ? -1.667  -19.480 57.439 1.00 51.53  ? 79  ARG B N   1 
ATOM   2439  C  CA  . ARG B  1 88  ? -1.203  -20.384 56.372 1.00 56.51  ? 79  ARG B CA  1 
ATOM   2440  C  C   . ARG B  1 88  ? -0.906  -19.569 55.120 1.00 56.74  ? 79  ARG B C   1 
ATOM   2441  O  O   . ARG B  1 88  ? -1.636  -18.630 54.803 1.00 63.00  ? 79  ARG B O   1 
ATOM   2442  C  CB  . ARG B  1 88  ? -2.213  -21.506 56.024 1.00 53.20  ? 79  ARG B CB  1 
ATOM   2443  C  CG  . ARG B  1 88  ? -3.197  -21.957 57.108 1.00 51.03  ? 79  ARG B CG  1 
ATOM   2444  C  CD  . ARG B  1 88  ? -2.509  -22.643 58.253 1.00 56.09  ? 79  ARG B CD  1 
ATOM   2445  N  NE  . ARG B  1 88  ? -3.424  -23.434 59.078 1.00 66.15  ? 79  ARG B NE  1 
ATOM   2446  C  CZ  . ARG B  1 88  ? -3.993  -23.021 60.211 1.00 66.14  ? 79  ARG B CZ  1 
ATOM   2447  N  NH1 . ARG B  1 88  ? -4.801  -23.834 60.882 1.00 63.98  ? 79  ARG B NH1 1 
ATOM   2448  N  NH2 . ARG B  1 88  ? -3.759  -21.800 60.677 1.00 69.84  ? 79  ARG B NH2 1 
ATOM   2449  N  N   . THR B  1 89  ? 0.167   -19.917 54.415 1.00 53.88  ? 80  THR B N   1 
ATOM   2450  C  CA  . THR B  1 89  ? 0.494   -19.241 53.163 1.00 54.27  ? 80  THR B CA  1 
ATOM   2451  C  C   . THR B  1 89  ? 0.941   -20.220 52.084 1.00 58.85  ? 80  THR B C   1 
ATOM   2452  O  O   . THR B  1 89  ? 1.264   -21.372 52.369 1.00 61.14  ? 80  THR B O   1 
ATOM   2453  C  CB  . THR B  1 89  ? 1.576   -18.152 53.353 1.00 59.19  ? 80  THR B CB  1 
ATOM   2454  O  OG1 . THR B  1 89  ? 1.460   -17.166 52.312 1.00 64.47  ? 80  THR B OG1 1 
ATOM   2455  C  CG2 . THR B  1 89  ? 2.977   -18.751 53.346 1.00 49.45  ? 80  THR B CG2 1 
ATOM   2456  N  N   . SER B  1 90  ? 0.951   -19.768 50.838 1.00 59.27  ? 81  SER B N   1 
ATOM   2457  C  CA  . SER B  1 90  ? 1.402   -20.618 49.748 1.00 58.01  ? 81  SER B CA  1 
ATOM   2458  C  C   . SER B  1 90  ? 2.903   -20.847 49.890 1.00 58.48  ? 81  SER B C   1 
ATOM   2459  O  O   . SER B  1 90  ? 3.636   -19.926 50.237 1.00 57.81  ? 81  SER B O   1 
ATOM   2460  C  CB  . SER B  1 90  ? 1.083   -19.963 48.410 1.00 57.65  ? 81  SER B CB  1 
ATOM   2461  O  OG  . SER B  1 90  ? 1.907   -20.497 47.391 1.00 62.25  ? 81  SER B OG  1 
ATOM   2462  N  N   . ALA B  1 91  ? 3.378   -22.062 49.638 1.00 52.23  ? 82  ALA B N   1 
ATOM   2463  C  CA  . ALA B  1 91  ? 4.806   -22.302 49.803 1.00 53.29  ? 82  ALA B CA  1 
ATOM   2464  C  C   . ALA B  1 91  ? 5.641   -21.392 48.902 1.00 54.50  ? 82  ALA B C   1 
ATOM   2465  O  O   . ALA B  1 91  ? 6.796   -21.102 49.205 1.00 54.37  ? 82  ALA B O   1 
ATOM   2466  C  CB  . ALA B  1 91  ? 5.153   -23.765 49.585 1.00 45.52  ? 82  ALA B CB  1 
ATOM   2467  N  N   . ALA B  1 92  ? 5.048   -20.930 47.806 1.00 52.44  ? 83  ALA B N   1 
ATOM   2468  C  CA  . ALA B  1 92  ? 5.740   -20.029 46.886 1.00 56.62  ? 83  ALA B CA  1 
ATOM   2469  C  C   . ALA B  1 92  ? 5.938   -18.597 47.423 1.00 62.28  ? 83  ALA B C   1 
ATOM   2470  O  O   . ALA B  1 92  ? 6.836   -17.882 46.967 1.00 61.44  ? 83  ALA B O   1 
ATOM   2471  C  CB  . ALA B  1 92  ? 5.038   -19.999 45.564 1.00 56.37  ? 83  ALA B CB  1 
ATOM   2472  N  N   . ASP B  1 93  ? 5.111   -18.185 48.385 1.00 58.40  ? 84  ASP B N   1 
ATOM   2473  C  CA  . ASP B  1 93  ? 5.253   -16.860 48.998 1.00 58.72  ? 84  ASP B CA  1 
ATOM   2474  C  C   . ASP B  1 93  ? 6.469   -16.730 49.904 1.00 57.87  ? 84  ASP B C   1 
ATOM   2475  O  O   . ASP B  1 93  ? 6.912   -15.618 50.149 1.00 63.78  ? 84  ASP B O   1 
ATOM   2476  C  CB  . ASP B  1 93  ? 4.004   -16.444 49.793 1.00 59.44  ? 84  ASP B CB  1 
ATOM   2477  C  CG  . ASP B  1 93  ? 2.798   -16.191 48.913 1.00 66.13  ? 84  ASP B CG  1 
ATOM   2478  O  OD1 . ASP B  1 93  ? 2.969   -16.051 47.684 1.00 67.29  ? 84  ASP B OD1 1 
ATOM   2479  O  OD2 . ASP B  1 93  ? 1.672   -16.126 49.458 1.00 68.59  ? 84  ASP B OD2 1 
ATOM   2480  N  N   . ILE B  1 94  ? 6.989   -17.843 50.424 1.00 55.07  ? 85  ILE B N   1 
ATOM   2481  C  CA  . ILE B  1 94  ? 8.169   -17.792 51.299 1.00 59.48  ? 85  ILE B CA  1 
ATOM   2482  C  C   . ILE B  1 94  ? 9.367   -18.505 50.699 1.00 54.79  ? 85  ILE B C   1 
ATOM   2483  O  O   . ILE B  1 94  ? 9.272   -19.155 49.665 1.00 56.54  ? 85  ILE B O   1 
ATOM   2484  C  CB  . ILE B  1 94  ? 7.930   -18.486 52.663 1.00 55.54  ? 85  ILE B CB  1 
ATOM   2485  C  CG1 . ILE B  1 94  ? 7.452   -19.922 52.431 1.00 56.02  ? 85  ILE B CG1 1 
ATOM   2486  C  CG2 . ILE B  1 94  ? 6.987   -17.668 53.561 1.00 51.79  ? 85  ILE B CG2 1 
ATOM   2487  C  CD1 . ILE B  1 94  ? 7.246   -20.711 53.685 1.00 55.70  ? 85  ILE B CD1 1 
ATOM   2488  N  N   . TRP B  1 95  ? 10.487  -18.424 51.393 1.00 48.88  ? 86  TRP B N   1 
ATOM   2489  C  CA  . TRP B  1 95  ? 11.693  -19.085 50.963 1.00 45.61  ? 86  TRP B CA  1 
ATOM   2490  C  C   . TRP B  1 95  ? 11.574  -20.508 51.449 1.00 52.42  ? 86  TRP B C   1 
ATOM   2491  O  O   . TRP B  1 95  ? 11.029  -20.741 52.523 1.00 58.54  ? 86  TRP B O   1 
ATOM   2492  C  CB  . TRP B  1 95  ? 12.892  -18.400 51.599 1.00 51.84  ? 86  TRP B CB  1 
ATOM   2493  C  CG  . TRP B  1 95  ? 14.164  -19.128 51.428 1.00 53.03  ? 86  TRP B CG  1 
ATOM   2494  C  CD1 . TRP B  1 95  ? 15.094  -18.911 50.469 1.00 57.15  ? 86  TRP B CD1 1 
ATOM   2495  C  CD2 . TRP B  1 95  ? 14.667  -20.198 52.241 1.00 57.47  ? 86  TRP B CD2 1 
ATOM   2496  N  NE1 . TRP B  1 95  ? 16.150  -19.773 50.622 1.00 63.20  ? 86  TRP B NE1 1 
ATOM   2497  C  CE2 . TRP B  1 95  ? 15.912  -20.579 51.704 1.00 58.34  ? 86  TRP B CE2 1 
ATOM   2498  C  CE3 . TRP B  1 95  ? 14.185  -20.874 53.374 1.00 55.40  ? 86  TRP B CE3 1 
ATOM   2499  C  CZ2 . TRP B  1 95  ? 16.686  -21.603 52.250 1.00 55.01  ? 86  TRP B CZ2 1 
ATOM   2500  C  CZ3 . TRP B  1 95  ? 14.959  -21.900 53.919 1.00 55.99  ? 86  TRP B CZ3 1 
ATOM   2501  C  CH2 . TRP B  1 95  ? 16.196  -22.246 53.359 1.00 55.56  ? 86  TRP B CH2 1 
ATOM   2502  N  N   . THR B  1 96  ? 12.032  -21.469 50.656 1.00 51.49  ? 87  THR B N   1 
ATOM   2503  C  CA  . THR B  1 96  ? 12.065  -22.857 51.100 1.00 45.10  ? 87  THR B CA  1 
ATOM   2504  C  C   . THR B  1 96  ? 13.462  -23.430 50.902 1.00 48.02  ? 87  THR B C   1 
ATOM   2505  O  O   . THR B  1 96  ? 14.155  -23.086 49.937 1.00 50.86  ? 87  THR B O   1 
ATOM   2506  C  CB  . THR B  1 96  ? 11.000  -23.749 50.402 1.00 50.31  ? 87  THR B CB  1 
ATOM   2507  O  OG1 . THR B  1 96  ? 11.016  -23.520 48.986 1.00 54.51  ? 87  THR B OG1 1 
ATOM   2508  C  CG2 . THR B  1 96  ? 9.608   -23.468 50.950 1.00 44.04  ? 87  THR B CG2 1 
ATOM   2509  N  N   . PRO B  1 97  ? 13.887  -24.297 51.832 1.00 50.07  ? 88  PRO B N   1 
ATOM   2510  C  CA  . PRO B  1 97  ? 15.188  -24.950 51.714 1.00 45.78  ? 88  PRO B CA  1 
ATOM   2511  C  C   . PRO B  1 97  ? 15.141  -25.924 50.562 1.00 49.40  ? 88  PRO B C   1 
ATOM   2512  O  O   . PRO B  1 97  ? 14.109  -26.563 50.316 1.00 44.86  ? 88  PRO B O   1 
ATOM   2513  C  CB  . PRO B  1 97  ? 15.315  -25.712 53.039 1.00 48.11  ? 88  PRO B CB  1 
ATOM   2514  C  CG  . PRO B  1 97  ? 13.926  -25.933 53.490 1.00 45.21  ? 88  PRO B CG  1 
ATOM   2515  C  CD  . PRO B  1 97  ? 13.167  -24.721 53.046 1.00 49.36  ? 88  PRO B CD  1 
ATOM   2516  N  N   . ASP B  1 98  ? 16.252  -26.105 49.875 1.00 46.35  ? 89  ASP B N   1 
ATOM   2517  C  CA  . ASP B  1 98  ? 16.142  -27.004 48.780 1.00 47.25  ? 89  ASP B CA  1 
ATOM   2518  C  C   . ASP B  1 98  ? 16.681  -28.329 49.263 1.00 53.82  ? 89  ASP B C   1 
ATOM   2519  O  O   . ASP B  1 98  ? 17.869  -28.608 49.184 1.00 60.49  ? 89  ASP B O   1 
ATOM   2520  C  CB  . ASP B  1 98  ? 17.015  -26.475 47.647 1.00 56.09  ? 89  ASP B CB  1 
ATOM   2521  C  CG  . ASP B  1 98  ? 18.462  -26.269 48.069 1.00 56.99  ? 89  ASP B CG  1 
ATOM   2522  O  OD1 . ASP B  1 98  ? 18.698  -26.024 49.274 1.00 53.96  ? 89  ASP B OD1 1 
ATOM   2523  O  OD2 . ASP B  1 98  ? 19.362  -26.360 47.198 1.00 58.32  ? 89  ASP B OD2 1 
ATOM   2524  N  N   . ILE B  1 99  ? 15.760  -29.221 49.581 1.00 49.31  ? 90  ILE B N   1 
ATOM   2525  C  CA  . ILE B  1 99  ? 16.132  -30.473 50.193 1.00 50.40  ? 90  ILE B CA  1 
ATOM   2526  C  C   . ILE B  1 99  ? 15.735  -31.446 49.131 1.00 49.01  ? 90  ILE B C   1 
ATOM   2527  O  O   . ILE B  1 99  ? 14.700  -31.273 48.506 1.00 48.69  ? 90  ILE B O   1 
ATOM   2528  C  CB  . ILE B  1 99  ? 15.352  -30.761 51.498 1.00 49.56  ? 90  ILE B CB  1 
ATOM   2529  C  CG1 . ILE B  1 99  ? 15.543  -29.637 52.517 1.00 60.04  ? 90  ILE B CG1 1 
ATOM   2530  C  CG2 . ILE B  1 99  ? 15.828  -32.039 52.123 1.00 49.06  ? 90  ILE B CG2 1 
ATOM   2531  C  CD1 . ILE B  1 99  ? 16.972  -29.454 52.989 1.00 56.73  ? 90  ILE B CD1 1 
ATOM   2532  N  N   . THR B  1 100 ? 16.566  -32.451 48.904 1.00 43.36  ? 91  THR B N   1 
ATOM   2533  C  CA  . THR B  1 100 ? 16.335  -33.382 47.825 1.00 45.24  ? 91  THR B CA  1 
ATOM   2534  C  C   . THR B  1 100 ? 16.717  -34.760 48.242 1.00 43.95  ? 91  THR B C   1 
ATOM   2535  O  O   . THR B  1 100 ? 17.650  -34.941 49.000 1.00 47.55  ? 91  THR B O   1 
ATOM   2536  C  CB  . THR B  1 100 ? 17.242  -33.098 46.627 1.00 44.64  ? 91  THR B CB  1 
ATOM   2537  O  OG1 . THR B  1 100 ? 17.083  -31.754 46.213 1.00 56.61  ? 91  THR B OG1 1 
ATOM   2538  C  CG2 . THR B  1 100 ? 16.869  -33.988 45.474 1.00 52.67  ? 91  THR B CG2 1 
ATOM   2539  N  N   . ALA B  1 101 ? 16.007  -35.734 47.699 1.00 48.32  ? 92  ALA B N   1 
ATOM   2540  C  CA  . ALA B  1 101 ? 16.474  -37.104 47.676 1.00 48.03  ? 92  ALA B CA  1 
ATOM   2541  C  C   . ALA B  1 101 ? 17.670  -37.180 46.721 1.00 50.92  ? 92  ALA B C   1 
ATOM   2542  O  O   . ALA B  1 101 ? 17.578  -36.755 45.567 1.00 54.88  ? 92  ALA B O   1 
ATOM   2543  C  CB  . ALA B  1 101 ? 15.359  -38.003 47.207 1.00 45.15  ? 92  ALA B CB  1 
ATOM   2544  N  N   . TYR B  1 102 ? 18.797  -37.689 47.211 1.00 47.40  ? 93  TYR B N   1 
ATOM   2545  C  CA  . TYR B  1 102 ? 20.038  -37.718 46.442 1.00 47.75  ? 93  TYR B CA  1 
ATOM   2546  C  C   . TYR B  1 102 ? 20.079  -38.869 45.454 1.00 43.66  ? 93  TYR B C   1 
ATOM   2547  O  O   . TYR B  1 102 ? 20.798  -38.830 44.462 1.00 56.29  ? 93  TYR B O   1 
ATOM   2548  C  CB  . TYR B  1 102 ? 21.241  -37.814 47.384 1.00 56.66  ? 93  TYR B CB  1 
ATOM   2549  C  CG  . TYR B  1 102 ? 21.535  -36.551 48.162 1.00 58.34  ? 93  TYR B CG  1 
ATOM   2550  C  CD1 . TYR B  1 102 ? 20.990  -35.339 47.776 1.00 52.58  ? 93  TYR B CD1 1 
ATOM   2551  C  CD2 . TYR B  1 102 ? 22.361  -36.573 49.271 1.00 54.61  ? 93  TYR B CD2 1 
ATOM   2552  C  CE1 . TYR B  1 102 ? 21.251  -34.199 48.465 1.00 53.22  ? 93  TYR B CE1 1 
ATOM   2553  C  CE2 . TYR B  1 102 ? 22.623  -35.431 49.968 1.00 51.66  ? 93  TYR B CE2 1 
ATOM   2554  C  CZ  . TYR B  1 102 ? 22.064  -34.247 49.560 1.00 53.82  ? 93  TYR B CZ  1 
ATOM   2555  O  OH  . TYR B  1 102 ? 22.310  -33.084 50.238 1.00 49.32  ? 93  TYR B OH  1 
ATOM   2556  N  N   . SER B  1 103 ? 19.370  -39.928 45.798 1.00 44.87  ? 94  SER B N   1 
ATOM   2557  C  CA  . SER B  1 103 ? 19.218  -41.125 44.981 1.00 46.51  ? 94  SER B CA  1 
ATOM   2558  C  C   . SER B  1 103 ? 17.938  -41.226 44.155 1.00 51.59  ? 94  SER B C   1 
ATOM   2559  O  O   . SER B  1 103 ? 17.632  -42.304 43.668 1.00 56.37  ? 94  SER B O   1 
ATOM   2560  C  CB  . SER B  1 103 ? 19.444  -42.392 45.794 1.00 44.57  ? 94  SER B CB  1 
ATOM   2561  O  OG  . SER B  1 103 ? 18.627  -42.387 46.938 1.00 58.64  ? 94  SER B OG  1 
ATOM   2562  N  N   . SER B  1 104 ? 17.118  -40.181 44.107 1.00 51.75  ? 95  SER B N   1 
ATOM   2563  C  CA  . SER B  1 104 ? 15.906  -40.239 43.284 1.00 47.68  ? 95  SER B CA  1 
ATOM   2564  C  C   . SER B  1 104 ? 16.240  -40.573 41.826 1.00 50.56  ? 95  SER B C   1 
ATOM   2565  O  O   . SER B  1 104 ? 17.225  -40.078 41.287 1.00 51.27  ? 95  SER B O   1 
ATOM   2566  C  CB  . SER B  1 104 ? 15.129  -38.932 43.355 1.00 49.77  ? 95  SER B CB  1 
ATOM   2567  O  OG  . SER B  1 104 ? 15.808  -37.895 42.671 1.00 57.72  ? 95  SER B OG  1 
ATOM   2568  N  N   . THR B  1 105 ? 15.467  -41.492 41.239 1.00 56.93  ? 96  THR B N   1 
ATOM   2569  C  CA  . THR B  1 105 ? 15.530  -41.849 39.811 1.00 50.42  ? 96  THR B CA  1 
ATOM   2570  C  C   . THR B  1 105 ? 14.473  -41.217 38.890 1.00 46.04  ? 96  THR B C   1 
ATOM   2571  O  O   . THR B  1 105 ? 14.471  -41.470 37.702 1.00 46.10  ? 96  THR B O   1 
ATOM   2572  C  CB  . THR B  1 105 ? 15.426  -43.365 39.626 1.00 49.42  ? 96  THR B CB  1 
ATOM   2573  O  OG1 . THR B  1 105 ? 14.189  -43.815 40.186 1.00 52.49  ? 96  THR B OG1 1 
ATOM   2574  C  CG2 . THR B  1 105 ? 16.581  -44.068 40.303 1.00 47.56  ? 96  THR B CG2 1 
ATOM   2575  N  N   . ARG B  1 106 ? 13.542  -40.459 39.450 1.00 54.53  ? 97  ARG B N   1 
ATOM   2576  C  CA  . ARG B  1 106 ? 12.517  -39.741 38.682 1.00 49.84  ? 97  ARG B CA  1 
ATOM   2577  C  C   . ARG B  1 106 ? 12.213  -38.437 39.412 1.00 51.26  ? 97  ARG B C   1 
ATOM   2578  O  O   . ARG B  1 106 ? 12.478  -38.318 40.611 1.00 56.51  ? 97  ARG B O   1 
ATOM   2579  C  CB  . ARG B  1 106 ? 11.236  -40.572 38.523 1.00 49.66  ? 97  ARG B CB  1 
ATOM   2580  C  CG  . ARG B  1 106 ? 11.393  -41.884 37.746 1.00 50.59  ? 97  ARG B CG  1 
ATOM   2581  C  CD  . ARG B  1 106 ? 10.055  -42.608 37.573 1.00 60.25  ? 97  ARG B CD  1 
ATOM   2582  N  NE  . ARG B  1 106 ? 10.206  -44.069 37.528 1.00 70.61  ? 97  ARG B NE  1 
ATOM   2583  C  CZ  . ARG B  1 106 ? 9.281   -44.934 37.959 1.00 79.23  ? 97  ARG B CZ  1 
ATOM   2584  N  NH1 . ARG B  1 106 ? 8.134   -44.490 38.471 1.00 74.80  ? 97  ARG B NH1 1 
ATOM   2585  N  NH2 . ARG B  1 106 ? 9.498   -46.244 37.891 1.00 77.44  ? 97  ARG B NH2 1 
ATOM   2586  N  N   . PRO B  1 107 ? 11.678  -37.438 38.706 1.00 54.01  ? 98  PRO B N   1 
ATOM   2587  C  CA  . PRO B  1 107 ? 11.345  -36.223 39.462 1.00 48.67  ? 98  PRO B CA  1 
ATOM   2588  C  C   . PRO B  1 107 ? 10.264  -36.548 40.479 1.00 47.59  ? 98  PRO B C   1 
ATOM   2589  O  O   . PRO B  1 107 ? 9.399   -37.383 40.197 1.00 48.94  ? 98  PRO B O   1 
ATOM   2590  C  CB  . PRO B  1 107 ? 10.803  -35.265 38.392 1.00 45.02  ? 98  PRO B CB  1 
ATOM   2591  C  CG  . PRO B  1 107 ? 11.187  -35.867 37.074 1.00 53.07  ? 98  PRO B CG  1 
ATOM   2592  C  CD  . PRO B  1 107 ? 11.293  -37.348 37.290 1.00 53.49  ? 98  PRO B CD  1 
ATOM   2593  N  N   . VAL B  1 108 ? 10.317  -35.920 41.648 1.00 51.13  ? 99  VAL B N   1 
ATOM   2594  C  CA  . VAL B  1 108 ? 9.378   -36.249 42.719 1.00 54.36  ? 99  VAL B CA  1 
ATOM   2595  C  C   . VAL B  1 108 ? 7.996   -35.742 42.363 1.00 56.11  ? 99  VAL B C   1 
ATOM   2596  O  O   . VAL B  1 108 ? 7.862   -34.748 41.650 1.00 54.83  ? 99  VAL B O   1 
ATOM   2597  C  CB  . VAL B  1 108 ? 9.806   -35.667 44.081 1.00 51.74  ? 99  VAL B CB  1 
ATOM   2598  C  CG1 . VAL B  1 108 ? 8.727   -35.893 45.118 1.00 55.53  ? 99  VAL B CG1 1 
ATOM   2599  C  CG2 . VAL B  1 108 ? 11.103  -36.288 44.530 1.00 53.77  ? 99  VAL B CG2 1 
ATOM   2600  N  N   . GLN B  1 109 ? 6.972   -36.438 42.838 1.00 47.98  ? 100 GLN B N   1 
ATOM   2601  C  CA  . GLN B  1 109 ? 5.617   -36.019 42.570 1.00 48.88  ? 100 GLN B CA  1 
ATOM   2602  C  C   . GLN B  1 109 ? 4.946   -35.617 43.851 1.00 49.36  ? 100 GLN B C   1 
ATOM   2603  O  O   . GLN B  1 109 ? 4.897   -36.385 44.795 1.00 56.53  ? 100 GLN B O   1 
ATOM   2604  C  CB  . GLN B  1 109 ? 4.818   -37.130 41.916 1.00 49.11  ? 100 GLN B CB  1 
ATOM   2605  C  CG  . GLN B  1 109 ? 5.565   -37.860 40.830 1.00 58.09  ? 100 GLN B CG  1 
ATOM   2606  C  CD  . GLN B  1 109 ? 4.634   -38.610 39.912 1.00 49.82  ? 100 GLN B CD  1 
ATOM   2607  O  OE1 . GLN B  1 109 ? 4.187   -39.714 40.226 1.00 54.75  ? 100 GLN B OE1 1 
ATOM   2608  N  NE2 . GLN B  1 109 ? 4.317   -38.006 38.779 1.00 43.17  ? 100 GLN B NE2 1 
ATOM   2609  N  N   . VAL B  1 110 ? 4.412   -34.408 43.865 1.00 47.45  ? 101 VAL B N   1 
ATOM   2610  C  CA  . VAL B  1 110 ? 3.745   -33.870 45.024 1.00 50.33  ? 101 VAL B CA  1 
ATOM   2611  C  C   . VAL B  1 110 ? 2.277   -34.270 45.047 1.00 47.30  ? 101 VAL B C   1 
ATOM   2612  O  O   . VAL B  1 110 ? 1.567   -34.100 44.074 1.00 46.97  ? 101 VAL B O   1 
ATOM   2613  C  CB  . VAL B  1 110 ? 3.879   -32.372 45.020 1.00 53.99  ? 101 VAL B CB  1 
ATOM   2614  C  CG1 . VAL B  1 110 ? 5.362   -32.012 45.078 1.00 54.51  ? 101 VAL B CG1 1 
ATOM   2615  C  CG2 . VAL B  1 110 ? 3.246   -31.821 43.748 1.00 65.67  ? 101 VAL B CG2 1 
ATOM   2616  N  N   . LEU B  1 111 ? 1.860   -34.850 46.166 1.00 48.78  ? 102 LEU B N   1 
ATOM   2617  C  CA  . LEU B  1 111 ? 0.504   -35.339 46.376 1.00 44.50  ? 102 LEU B CA  1 
ATOM   2618  C  C   . LEU B  1 111 ? -0.380  -34.373 47.157 1.00 43.33  ? 102 LEU B C   1 
ATOM   2619  O  O   . LEU B  1 111 ? -1.561  -34.632 47.387 1.00 49.41  ? 102 LEU B O   1 
ATOM   2620  C  CB  . LEU B  1 111 ? 0.573   -36.703 47.069 1.00 46.49  ? 102 LEU B CB  1 
ATOM   2621  C  CG  . LEU B  1 111 ? 1.564   -37.612 46.339 1.00 46.20  ? 102 LEU B CG  1 
ATOM   2622  C  CD1 . LEU B  1 111 ? 1.727   -38.935 47.013 1.00 46.92  ? 102 LEU B CD1 1 
ATOM   2623  C  CD2 . LEU B  1 111 ? 1.083   -37.812 44.935 1.00 45.59  ? 102 LEU B CD2 1 
ATOM   2624  N  N   . SER B  1 112 ? 0.199   -33.255 47.565 1.00 44.30  ? 103 SER B N   1 
ATOM   2625  C  CA  . SER B  1 112 ? -0.491  -32.336 48.463 1.00 44.71  ? 103 SER B CA  1 
ATOM   2626  C  C   . SER B  1 112 ? -0.378  -30.898 47.997 1.00 44.85  ? 103 SER B C   1 
ATOM   2627  O  O   . SER B  1 112 ? 0.513   -30.570 47.209 1.00 43.34  ? 103 SER B O   1 
ATOM   2628  C  CB  . SER B  1 112 ? 0.063   -32.464 49.895 1.00 49.38  ? 103 SER B CB  1 
ATOM   2629  O  OG  . SER B  1 112 ? 1.347   -31.867 50.054 1.00 48.31  ? 103 SER B OG  1 
ATOM   2630  N  N   . PRO B  1 113 ? -1.291  -30.039 48.473 1.00 42.95  ? 104 PRO B N   1 
ATOM   2631  C  CA  . PRO B  1 113 ? -1.186  -28.602 48.242 1.00 39.26  ? 104 PRO B CA  1 
ATOM   2632  C  C   . PRO B  1 113 ? 0.138   -28.105 48.759 1.00 47.24  ? 104 PRO B C   1 
ATOM   2633  O  O   . PRO B  1 113 ? 0.643   -28.675 49.733 1.00 50.14  ? 104 PRO B O   1 
ATOM   2634  C  CB  . PRO B  1 113 ? -2.326  -28.048 49.080 1.00 39.64  ? 104 PRO B CB  1 
ATOM   2635  C  CG  . PRO B  1 113 ? -3.353  -29.114 49.012 1.00 40.00  ? 104 PRO B CG  1 
ATOM   2636  C  CD  . PRO B  1 113 ? -2.582  -30.394 49.082 1.00 45.90  ? 104 PRO B CD  1 
ATOM   2637  N  N   . GLN B  1 114 ? 0.722   -27.086 48.135 1.00 49.85  ? 105 GLN B N   1 
ATOM   2638  C  CA  . GLN B  1 114 ? 1.932   -26.562 48.740 1.00 54.11  ? 105 GLN B CA  1 
ATOM   2639  C  C   . GLN B  1 114 ? 1.649   -25.271 49.489 1.00 49.54  ? 105 GLN B C   1 
ATOM   2640  O  O   . GLN B  1 114 ? 1.616   -24.172 48.938 1.00 48.22  ? 105 GLN B O   1 
ATOM   2641  C  CB  . GLN B  1 114 ? 3.017   -26.385 47.690 1.00 52.04  ? 105 GLN B CB  1 
ATOM   2642  C  CG  . GLN B  1 114 ? 3.776   -27.677 47.424 1.00 59.51  ? 105 GLN B CG  1 
ATOM   2643  C  CD  . GLN B  1 114 ? 4.226   -27.793 45.988 1.00 63.56  ? 105 GLN B CD  1 
ATOM   2644  O  OE1 . GLN B  1 114 ? 3.626   -27.200 45.095 1.00 63.03  ? 105 GLN B OE1 1 
ATOM   2645  N  NE2 . GLN B  1 114 ? 5.292   -28.549 45.757 1.00 64.37  ? 105 GLN B NE2 1 
ATOM   2646  N  N   . ASN B  1 115 ? 1.609   -25.434 50.801 1.00 52.12  ? 106 ASN B N   1 
ATOM   2647  C  CA  . ASN B  1 115 ? 1.176   -24.404 51.717 1.00 55.57  ? 106 ASN B CA  1 
ATOM   2648  C  C   . ASN B  1 115 ? 2.008   -24.620 52.948 1.00 55.13  ? 106 ASN B C   1 
ATOM   2649  O  O   . ASN B  1 115 ? 2.335   -25.754 53.290 1.00 54.33  ? 106 ASN B O   1 
ATOM   2650  C  CB  . ASN B  1 115 ? -0.308  -24.562 52.070 1.00 54.31  ? 106 ASN B CB  1 
ATOM   2651  C  CG  . ASN B  1 115 ? -1.239  -24.193 50.918 1.00 57.69  ? 106 ASN B CG  1 
ATOM   2652  O  OD1 . ASN B  1 115 ? -0.937  -23.314 50.107 1.00 59.33  ? 106 ASN B OD1 1 
ATOM   2653  N  ND2 . ASN B  1 115 ? -2.381  -24.868 50.847 1.00 59.76  ? 106 ASN B ND2 1 
ATOM   2654  N  N   . ALA B  1 116 ? 2.363   -23.533 53.613 1.00 53.99  ? 107 ALA B N   1 
ATOM   2655  C  CA  . ALA B  1 116 ? 3.153   -23.619 54.822 1.00 52.80  ? 107 ALA B CA  1 
ATOM   2656  C  C   . ALA B  1 116 ? 2.384   -22.965 55.955 1.00 53.13  ? 107 ALA B C   1 
ATOM   2657  O  O   . ALA B  1 116 ? 1.434   -22.220 55.720 1.00 50.20  ? 107 ALA B O   1 
ATOM   2658  C  CB  . ALA B  1 116 ? 4.502   -22.947 54.619 1.00 52.93  ? 107 ALA B CB  1 
ATOM   2659  N  N   . LEU B  1 117 ? 2.770   -23.280 57.186 1.00 54.35  ? 108 LEU B N   1 
ATOM   2660  C  CA  . LEU B  1 117 ? 2.269   -22.555 58.340 1.00 55.58  ? 108 LEU B CA  1 
ATOM   2661  C  C   . LEU B  1 117 ? 3.407   -21.728 58.931 1.00 59.14  ? 108 LEU B C   1 
ATOM   2662  O  O   . LEU B  1 117 ? 4.530   -22.205 59.073 1.00 56.87  ? 108 LEU B O   1 
ATOM   2663  C  CB  . LEU B  1 117 ? 1.644   -23.490 59.379 1.00 54.40  ? 108 LEU B CB  1 
ATOM   2664  C  CG  . LEU B  1 117 ? 0.951   -22.757 60.539 1.00 66.84  ? 108 LEU B CG  1 
ATOM   2665  C  CD1 . LEU B  1 117 ? -0.280  -23.512 60.998 1.00 70.56  ? 108 LEU B CD1 1 
ATOM   2666  C  CD2 . LEU B  1 117 ? 1.908   -22.491 61.714 1.00 62.43  ? 108 LEU B CD2 1 
ATOM   2667  N  N   . VAL B  1 118 ? 3.110   -20.469 59.237 1.00 57.60  ? 109 VAL B N   1 
ATOM   2668  C  CA  . VAL B  1 118 ? 4.100   -19.549 59.774 1.00 57.70  ? 109 VAL B CA  1 
ATOM   2669  C  C   . VAL B  1 118 ? 3.515   -19.023 61.067 1.00 58.11  ? 109 VAL B C   1 
ATOM   2670  O  O   . VAL B  1 118 ? 2.320   -18.726 61.111 1.00 60.89  ? 109 VAL B O   1 
ATOM   2671  C  CB  . VAL B  1 118 ? 4.362   -18.356 58.790 1.00 47.77  ? 109 VAL B CB  1 
ATOM   2672  C  CG1 . VAL B  1 118 ? 5.469   -17.466 59.285 1.00 54.38  ? 109 VAL B CG1 1 
ATOM   2673  C  CG2 . VAL B  1 118 ? 4.732   -18.865 57.431 1.00 48.57  ? 109 VAL B CG2 1 
ATOM   2674  N  N   . ASN B  1 119 ? 4.333   -18.892 62.111 1.00 57.28  ? 110 ASN B N   1 
ATOM   2675  C  CA  . ASN B  1 119 ? 3.849   -18.270 63.346 1.00 66.45  ? 110 ASN B CA  1 
ATOM   2676  C  C   . ASN B  1 119 ? 4.714   -17.160 63.918 1.00 62.78  ? 110 ASN B C   1 
ATOM   2677  O  O   . ASN B  1 119 ? 5.828   -16.925 63.458 1.00 61.87  ? 110 ASN B O   1 
ATOM   2678  C  CB  . ASN B  1 119 ? 3.431   -19.288 64.408 1.00 68.00  ? 110 ASN B CB  1 
ATOM   2679  C  CG  . ASN B  1 119 ? 4.603   -19.984 65.080 1.00 67.43  ? 110 ASN B CG  1 
ATOM   2680  O  OD1 . ASN B  1 119 ? 5.741   -19.533 65.055 1.00 64.82  ? 110 ASN B OD1 1 
ATOM   2681  N  ND2 . ASN B  1 119 ? 4.295   -21.107 65.711 1.00 78.50  ? 110 ASN B ND2 1 
ATOM   2682  N  N   . SER B  1 120 ? 4.157   -16.454 64.892 1.00 60.65  ? 111 SER B N   1 
ATOM   2683  C  CA  . SER B  1 120 ? 4.668   -15.148 65.267 1.00 67.59  ? 111 SER B CA  1 
ATOM   2684  C  C   . SER B  1 120 ? 6.147   -15.113 65.673 1.00 68.33  ? 111 SER B C   1 
ATOM   2685  O  O   . SER B  1 120 ? 6.781   -14.063 65.565 1.00 72.63  ? 111 SER B O   1 
ATOM   2686  C  CB  . SER B  1 120 ? 3.755   -14.459 66.297 1.00 65.99  ? 111 SER B CB  1 
ATOM   2687  O  OG  . SER B  1 120 ? 3.616   -15.217 67.487 1.00 75.48  ? 111 SER B OG  1 
ATOM   2688  N  N   . SER B  1 121 ? 6.712   -16.237 66.107 1.00 57.83  ? 112 SER B N   1 
ATOM   2689  C  CA  . SER B  1 121 ? 8.133   -16.246 66.476 1.00 61.90  ? 112 SER B CA  1 
ATOM   2690  C  C   . SER B  1 121 ? 9.058   -16.615 65.311 1.00 64.57  ? 112 SER B C   1 
ATOM   2691  O  O   . SER B  1 121 ? 10.275  -16.750 65.468 1.00 61.71  ? 112 SER B O   1 
ATOM   2692  C  CB  . SER B  1 121 ? 8.375   -17.146 67.677 1.00 64.88  ? 112 SER B CB  1 
ATOM   2693  O  OG  . SER B  1 121 ? 7.578   -18.312 67.587 1.00 79.05  ? 112 SER B OG  1 
ATOM   2694  N  N   . GLY B  1 122 ? 8.455   -16.786 64.141 1.00 67.02  ? 113 GLY B N   1 
ATOM   2695  C  CA  . GLY B  1 122 ? 9.198   -16.958 62.908 1.00 63.28  ? 113 GLY B CA  1 
ATOM   2696  C  C   . GLY B  1 122 ? 9.474   -18.398 62.541 1.00 64.94  ? 113 GLY B C   1 
ATOM   2697  O  O   . GLY B  1 122 ? 10.329  -18.655 61.695 1.00 57.01  ? 113 GLY B O   1 
ATOM   2698  N  N   . HIS B  1 123 ? 8.766   -19.326 63.187 1.00 64.80  ? 114 HIS B N   1 
ATOM   2699  C  CA  . HIS B  1 123 ? 8.824   -20.744 62.827 1.00 61.38  ? 114 HIS B CA  1 
ATOM   2700  C  C   . HIS B  1 123 ? 7.906   -21.091 61.647 1.00 60.35  ? 114 HIS B C   1 
ATOM   2701  O  O   . HIS B  1 123 ? 6.744   -20.670 61.572 1.00 56.91  ? 114 HIS B O   1 
ATOM   2702  C  CB  . HIS B  1 123 ? 8.489   -21.636 64.026 1.00 69.84  ? 114 HIS B CB  1 
ATOM   2703  C  CG  . HIS B  1 123 ? 9.524   -21.604 65.104 1.00 77.97  ? 114 HIS B CG  1 
ATOM   2704  N  ND1 . HIS B  1 123 ? 9.453   -20.739 66.175 1.00 78.58  ? 114 HIS B ND1 1 
ATOM   2705  C  CD2 . HIS B  1 123 ? 10.665  -22.315 65.264 1.00 73.03  ? 114 HIS B CD2 1 
ATOM   2706  C  CE1 . HIS B  1 123 ? 10.507  -20.922 66.953 1.00 73.37  ? 114 HIS B CE1 1 
ATOM   2707  N  NE2 . HIS B  1 123 ? 11.258  -21.870 66.421 1.00 72.36  ? 114 HIS B NE2 1 
ATOM   2708  N  N   . VAL B  1 124 ? 8.455   -21.867 60.726 1.00 57.43  ? 115 VAL B N   1 
ATOM   2709  C  CA  . VAL B  1 124 ? 7.729   -22.305 59.556 1.00 50.66  ? 115 VAL B CA  1 
ATOM   2710  C  C   . VAL B  1 124 ? 7.682   -23.816 59.552 1.00 52.50  ? 115 VAL B C   1 
ATOM   2711  O  O   . VAL B  1 124 ? 8.674   -24.493 59.837 1.00 51.73  ? 115 VAL B O   1 
ATOM   2712  C  CB  . VAL B  1 124 ? 8.407   -21.829 58.274 1.00 50.77  ? 115 VAL B CB  1 
ATOM   2713  C  CG1 . VAL B  1 124 ? 7.698   -22.393 57.048 1.00 52.59  ? 115 VAL B CG1 1 
ATOM   2714  C  CG2 . VAL B  1 124 ? 8.428   -20.329 58.238 1.00 49.65  ? 115 VAL B CG2 1 
ATOM   2715  N  N   . GLN B  1 125 ? 6.506   -24.333 59.231 1.00 59.85  ? 116 GLN B N   1 
ATOM   2716  C  CA  . GLN B  1 125 ? 6.298   -25.759 59.140 1.00 60.09  ? 116 GLN B CA  1 
ATOM   2717  C  C   . GLN B  1 125 ? 5.725   -26.151 57.775 1.00 48.26  ? 116 GLN B C   1 
ATOM   2718  O  O   . GLN B  1 125 ? 4.600   -25.828 57.447 1.00 52.20  ? 116 GLN B O   1 
ATOM   2719  C  CB  . GLN B  1 125 ? 5.375   -26.189 60.267 1.00 58.35  ? 116 GLN B CB  1 
ATOM   2720  C  CG  . GLN B  1 125 ? 5.316   -27.676 60.458 1.00 78.09  ? 116 GLN B CG  1 
ATOM   2721  C  CD  . GLN B  1 125 ? 4.767   -28.046 61.814 1.00 90.34  ? 116 GLN B CD  1 
ATOM   2722  O  OE1 . GLN B  1 125 ? 4.913   -27.290 62.777 1.00 87.28  ? 116 GLN B OE1 1 
ATOM   2723  N  NE2 . GLN B  1 125 ? 4.126   -29.210 61.900 1.00 95.66  ? 116 GLN B NE2 1 
ATOM   2724  N  N   . TYR B  1 126 ? 6.504   -26.878 56.996 1.00 44.20  ? 117 TYR B N   1 
ATOM   2725  C  CA  . TYR B  1 126 ? 6.101   -27.250 55.653 1.00 49.96  ? 117 TYR B CA  1 
ATOM   2726  C  C   . TYR B  1 126 ? 6.057   -28.785 55.496 1.00 52.09  ? 117 TYR B C   1 
ATOM   2727  O  O   . TYR B  1 126 ? 7.086   -29.447 55.601 1.00 50.00  ? 117 TYR B O   1 
ATOM   2728  C  CB  . TYR B  1 126 ? 7.061   -26.581 54.651 1.00 48.40  ? 117 TYR B CB  1 
ATOM   2729  C  CG  . TYR B  1 126 ? 6.820   -26.904 53.200 1.00 45.12  ? 117 TYR B CG  1 
ATOM   2730  C  CD1 . TYR B  1 126 ? 5.559   -26.765 52.634 1.00 51.83  ? 117 TYR B CD1 1 
ATOM   2731  C  CD2 . TYR B  1 126 ? 7.858   -27.347 52.386 1.00 52.80  ? 117 TYR B CD2 1 
ATOM   2732  C  CE1 . TYR B  1 126 ? 5.332   -27.077 51.292 1.00 53.28  ? 117 TYR B CE1 1 
ATOM   2733  C  CE2 . TYR B  1 126 ? 7.644   -27.663 51.045 1.00 52.85  ? 117 TYR B CE2 1 
ATOM   2734  C  CZ  . TYR B  1 126 ? 6.378   -27.522 50.505 1.00 52.86  ? 117 TYR B CZ  1 
ATOM   2735  O  OH  . TYR B  1 126 ? 6.148   -27.829 49.179 1.00 51.39  ? 117 TYR B OH  1 
ATOM   2736  N  N   . LEU B  1 127 ? 4.870   -29.346 55.243 1.00 53.18  ? 118 LEU B N   1 
ATOM   2737  C  CA  . LEU B  1 127 ? 4.710   -30.805 55.122 1.00 54.74  ? 118 LEU B CA  1 
ATOM   2738  C  C   . LEU B  1 127 ? 4.126   -31.295 53.794 1.00 49.65  ? 118 LEU B C   1 
ATOM   2739  O  O   . LEU B  1 127 ? 2.949   -31.662 53.745 1.00 47.07  ? 118 LEU B O   1 
ATOM   2740  C  CB  . LEU B  1 127 ? 3.802   -31.349 56.231 1.00 58.04  ? 118 LEU B CB  1 
ATOM   2741  C  CG  . LEU B  1 127 ? 4.095   -31.089 57.705 1.00 77.03  ? 118 LEU B CG  1 
ATOM   2742  C  CD1 . LEU B  1 127 ? 3.872   -29.620 58.090 1.00 77.88  ? 118 LEU B CD1 1 
ATOM   2743  C  CD2 . LEU B  1 127 ? 3.202   -31.985 58.523 1.00 79.45  ? 118 LEU B CD2 1 
ATOM   2744  N  N   . PRO B  1 128 ? 4.940   -31.315 52.724 1.00 47.97  ? 119 PRO B N   1 
ATOM   2745  C  CA  . PRO B  1 128 ? 4.565   -31.902 51.427 1.00 48.48  ? 119 PRO B CA  1 
ATOM   2746  C  C   . PRO B  1 128 ? 4.439   -33.423 51.452 1.00 52.78  ? 119 PRO B C   1 
ATOM   2747  O  O   . PRO B  1 128 ? 5.357   -34.101 51.912 1.00 52.39  ? 119 PRO B O   1 
ATOM   2748  C  CB  . PRO B  1 128 ? 5.735   -31.530 50.528 1.00 41.60  ? 119 PRO B CB  1 
ATOM   2749  C  CG  . PRO B  1 128 ? 6.870   -31.315 51.453 1.00 50.51  ? 119 PRO B CG  1 
ATOM   2750  C  CD  . PRO B  1 128 ? 6.309   -30.782 52.714 1.00 45.38  ? 119 PRO B CD  1 
ATOM   2751  N  N   . ALA B  1 129 ? 3.343   -33.954 50.917 1.00 52.43  ? 120 ALA B N   1 
ATOM   2752  C  CA  . ALA B  1 129 ? 3.200   -35.394 50.737 1.00 47.04  ? 120 ALA B CA  1 
ATOM   2753  C  C   . ALA B  1 129 ? 3.803   -35.697 49.378 1.00 50.18  ? 120 ALA B C   1 
ATOM   2754  O  O   . ALA B  1 129 ? 3.548   -34.981 48.421 1.00 55.10  ? 120 ALA B O   1 
ATOM   2755  C  CB  . ALA B  1 129 ? 1.751   -35.785 50.777 1.00 40.85  ? 120 ALA B CB  1 
ATOM   2756  N  N   . GLN B  1 130 ? 4.639   -36.721 49.284 1.00 49.53  ? 121 GLN B N   1 
ATOM   2757  C  CA  . GLN B  1 130 ? 5.372   -36.951 48.043 1.00 51.07  ? 121 GLN B CA  1 
ATOM   2758  C  C   . GLN B  1 130 ? 5.376   -38.408 47.610 1.00 48.92  ? 121 GLN B C   1 
ATOM   2759  O  O   . GLN B  1 130 ? 5.321   -39.312 48.437 1.00 48.92  ? 121 GLN B O   1 
ATOM   2760  C  CB  . GLN B  1 130 ? 6.826   -36.471 48.177 1.00 53.30  ? 121 GLN B CB  1 
ATOM   2761  C  CG  . GLN B  1 130 ? 6.986   -35.056 48.721 1.00 56.99  ? 121 GLN B CG  1 
ATOM   2762  C  CD  . GLN B  1 130 ? 8.379   -34.512 48.491 1.00 57.58  ? 121 GLN B CD  1 
ATOM   2763  O  OE1 . GLN B  1 130 ? 9.371   -35.129 48.879 1.00 58.81  ? 121 GLN B OE1 1 
ATOM   2764  N  NE2 . GLN B  1 130 ? 8.463   -33.360 47.834 1.00 54.55  ? 121 GLN B NE2 1 
ATOM   2765  N  N   . ARG B  1 131 ? 5.445   -38.632 46.301 1.00 51.78  ? 122 ARG B N   1 
ATOM   2766  C  CA  . ARG B  1 131 ? 5.812   -39.947 45.797 1.00 49.00  ? 122 ARG B CA  1 
ATOM   2767  C  C   . ARG B  1 131 ? 7.192   -39.890 45.158 1.00 47.93  ? 122 ARG B C   1 
ATOM   2768  O  O   . ARG B  1 131 ? 7.423   -39.116 44.229 1.00 55.84  ? 122 ARG B O   1 
ATOM   2769  C  CB  . ARG B  1 131 ? 4.778   -40.479 44.815 1.00 44.38  ? 122 ARG B CB  1 
ATOM   2770  C  CG  . ARG B  1 131 ? 5.071   -41.894 44.348 1.00 41.12  ? 122 ARG B CG  1 
ATOM   2771  C  CD  . ARG B  1 131 ? 4.167   -42.237 43.220 1.00 46.01  ? 122 ARG B CD  1 
ATOM   2772  N  NE  . ARG B  1 131 ? 4.512   -43.484 42.565 1.00 55.12  ? 122 ARG B NE  1 
ATOM   2773  C  CZ  . ARG B  1 131 ? 3.705   -44.537 42.540 1.00 58.18  ? 122 ARG B CZ  1 
ATOM   2774  N  NH1 . ARG B  1 131 ? 2.520   -44.468 43.140 1.00 54.01  ? 122 ARG B NH1 1 
ATOM   2775  N  NH2 . ARG B  1 131 ? 4.076   -45.653 41.922 1.00 57.83  ? 122 ARG B NH2 1 
ATOM   2776  N  N   . LEU B  1 132 ? 8.103   -40.713 45.663 1.00 41.22  ? 123 LEU B N   1 
ATOM   2777  C  CA  . LEU B  1 132 ? 9.489   -40.707 45.222 1.00 46.44  ? 123 LEU B CA  1 
ATOM   2778  C  C   . LEU B  1 132 ? 9.940   -42.094 44.759 1.00 46.27  ? 123 LEU B C   1 
ATOM   2779  O  O   . LEU B  1 132 ? 9.584   -43.101 45.362 1.00 53.77  ? 123 LEU B O   1 
ATOM   2780  C  CB  . LEU B  1 132 ? 10.389  -40.209 46.360 1.00 48.37  ? 123 LEU B CB  1 
ATOM   2781  C  CG  . LEU B  1 132 ? 11.885  -40.499 46.267 1.00 45.28  ? 123 LEU B CG  1 
ATOM   2782  C  CD1 . LEU B  1 132 ? 12.590  -39.396 45.544 1.00 48.51  ? 123 LEU B CD1 1 
ATOM   2783  C  CD2 . LEU B  1 132 ? 12.464  -40.644 47.633 1.00 49.20  ? 123 LEU B CD2 1 
ATOM   2784  N  N   . SER B  1 133 ? 10.708  -42.140 43.676 1.00 43.47  ? 124 SER B N   1 
ATOM   2785  C  CA  . SER B  1 133 ? 11.359  -43.370 43.231 1.00 45.76  ? 124 SER B CA  1 
ATOM   2786  C  C   . SER B  1 133 ? 12.841  -43.224 43.484 1.00 48.20  ? 124 SER B C   1 
ATOM   2787  O  O   . SER B  1 133 ? 13.439  -42.248 43.068 1.00 56.03  ? 124 SER B O   1 
ATOM   2788  C  CB  . SER B  1 133 ? 11.122  -43.612 41.741 1.00 48.50  ? 124 SER B CB  1 
ATOM   2789  O  OG  . SER B  1 133 ? 9.749   -43.833 41.490 1.00 52.06  ? 124 SER B OG  1 
ATOM   2790  N  N   . PHE B  1 134 ? 13.449  -44.173 44.177 1.00 47.63  ? 125 PHE B N   1 
ATOM   2791  C  CA  . PHE B  1 134 ? 14.856  -44.032 44.504 1.00 48.61  ? 125 PHE B CA  1 
ATOM   2792  C  C   . PHE B  1 134 ? 15.535  -45.352 44.278 1.00 51.74  ? 125 PHE B C   1 
ATOM   2793  O  O   . PHE B  1 134 ? 14.855  -46.377 44.185 1.00 54.17  ? 125 PHE B O   1 
ATOM   2794  C  CB  . PHE B  1 134 ? 15.026  -43.571 45.954 1.00 51.96  ? 125 PHE B CB  1 
ATOM   2795  C  CG  . PHE B  1 134 ? 14.318  -44.442 46.959 1.00 52.07  ? 125 PHE B CG  1 
ATOM   2796  C  CD1 . PHE B  1 134 ? 15.025  -45.357 47.727 1.00 55.18  ? 125 PHE B CD1 1 
ATOM   2797  C  CD2 . PHE B  1 134 ? 12.945  -44.339 47.140 1.00 49.42  ? 125 PHE B CD2 1 
ATOM   2798  C  CE1 . PHE B  1 134 ? 14.369  -46.158 48.643 1.00 52.97  ? 125 PHE B CE1 1 
ATOM   2799  C  CE2 . PHE B  1 134 ? 12.282  -45.132 48.060 1.00 51.05  ? 125 PHE B CE2 1 
ATOM   2800  C  CZ  . PHE B  1 134 ? 12.990  -46.042 48.807 1.00 51.06  ? 125 PHE B CZ  1 
ATOM   2801  N  N   . MET B  1 135 ? 16.866  -45.345 44.224 1.00 52.55  ? 126 MET B N   1 
ATOM   2802  C  CA  . MET B  1 135 ? 17.582  -46.546 43.831 1.00 56.28  ? 126 MET B CA  1 
ATOM   2803  C  C   . MET B  1 135 ? 17.558  -47.531 44.969 1.00 48.28  ? 126 MET B C   1 
ATOM   2804  O  O   . MET B  1 135 ? 18.113  -47.273 46.006 1.00 56.11  ? 126 MET B O   1 
ATOM   2805  C  CB  . MET B  1 135 ? 19.030  -46.190 43.541 1.00 48.17  ? 126 MET B CB  1 
ATOM   2806  C  CG  . MET B  1 135 ? 19.168  -45.113 42.529 1.00 50.67  ? 126 MET B CG  1 
ATOM   2807  S  SD  . MET B  1 135 ? 20.807  -44.432 42.514 1.00 59.45  ? 126 MET B SD  1 
ATOM   2808  C  CE  . MET B  1 135 ? 20.558  -43.094 41.346 1.00 51.34  ? 126 MET B CE  1 
ATOM   2809  N  N   . CYS B  1 136 ? 16.948  -48.683 44.762 1.00 55.98  ? 127 CYS B N   1 
ATOM   2810  C  CA  . CYS B  1 136 ? 16.895  -49.695 45.801 1.00 59.53  ? 127 CYS B CA  1 
ATOM   2811  C  C   . CYS B  1 136 ? 16.920  -51.083 45.178 1.00 61.70  ? 127 CYS B C   1 
ATOM   2812  O  O   . CYS B  1 136 ? 16.249  -51.320 44.181 1.00 65.59  ? 127 CYS B O   1 
ATOM   2813  C  CB  . CYS B  1 136 ? 15.648  -49.482 46.659 1.00 56.26  ? 127 CYS B CB  1 
ATOM   2814  S  SG  . CYS B  1 136 ? 15.010  -50.939 47.481 1.00 65.61  ? 127 CYS B SG  1 
ATOM   2815  N  N   . ASP B  1 137 ? 17.696  -51.992 45.758 1.00 63.31  ? 128 ASP B N   1 
ATOM   2816  C  CA  . ASP B  1 137 ? 17.669  -53.395 45.352 1.00 62.96  ? 128 ASP B CA  1 
ATOM   2817  C  C   . ASP B  1 137 ? 16.714  -54.191 46.269 1.00 59.01  ? 128 ASP B C   1 
ATOM   2818  O  O   . ASP B  1 137 ? 16.992  -54.390 47.439 1.00 68.37  ? 128 ASP B O   1 
ATOM   2819  C  CB  . ASP B  1 137 ? 19.090  -53.972 45.367 1.00 67.08  ? 128 ASP B CB  1 
ATOM   2820  C  CG  . ASP B  1 137 ? 19.125  -55.453 45.028 1.00 72.31  ? 128 ASP B CG  1 
ATOM   2821  O  OD1 . ASP B  1 137 ? 18.040  -56.013 44.806 1.00 69.06  ? 128 ASP B OD1 1 
ATOM   2822  O  OD2 . ASP B  1 137 ? 20.219  -56.064 45.001 1.00 69.12  ? 128 ASP B OD2 1 
ATOM   2823  N  N   . PRO B  1 138 ? 15.563  -54.607 45.738 1.00 58.45  ? 129 PRO B N   1 
ATOM   2824  C  CA  . PRO B  1 138 ? 14.478  -55.344 46.401 1.00 62.54  ? 129 PRO B CA  1 
ATOM   2825  C  C   . PRO B  1 138 ? 14.853  -56.774 46.843 1.00 65.58  ? 129 PRO B C   1 
ATOM   2826  O  O   . PRO B  1 138 ? 14.038  -57.435 47.492 1.00 63.20  ? 129 PRO B O   1 
ATOM   2827  C  CB  . PRO B  1 138 ? 13.308  -55.275 45.408 1.00 60.26  ? 129 PRO B CB  1 
ATOM   2828  C  CG  . PRO B  1 138 ? 13.916  -54.961 44.115 1.00 62.36  ? 129 PRO B CG  1 
ATOM   2829  C  CD  . PRO B  1 138 ? 15.222  -54.258 44.349 1.00 61.74  ? 129 PRO B CD  1 
ATOM   2830  N  N   . THR B  1 139 ? 16.022  -57.264 46.425 1.00 63.53  ? 130 THR B N   1 
ATOM   2831  C  CA  . THR B  1 139 ? 16.416  -58.644 46.688 1.00 63.23  ? 130 THR B CA  1 
ATOM   2832  C  C   . THR B  1 139 ? 16.174  -58.937 48.144 1.00 66.49  ? 130 THR B C   1 
ATOM   2833  O  O   . THR B  1 139 ? 16.524  -58.138 49.010 1.00 64.30  ? 130 THR B O   1 
ATOM   2834  C  CB  . THR B  1 139 ? 17.927  -58.877 46.482 1.00 59.46  ? 130 THR B CB  1 
ATOM   2835  O  OG1 . THR B  1 139 ? 18.260  -58.800 45.098 1.00 65.12  ? 130 THR B OG1 1 
ATOM   2836  C  CG2 . THR B  1 139 ? 18.315  -60.253 46.968 1.00 59.71  ? 130 THR B CG2 1 
ATOM   2837  N  N   . GLY B  1 140 ? 15.547  -60.079 48.402 1.00 66.23  ? 131 GLY B N   1 
ATOM   2838  C  CA  . GLY B  1 140 ? 15.273  -60.515 49.754 1.00 68.45  ? 131 GLY B CA  1 
ATOM   2839  C  C   . GLY B  1 140 ? 13.956  -60.015 50.310 1.00 72.22  ? 131 GLY B C   1 
ATOM   2840  O  O   . GLY B  1 140 ? 13.658  -60.226 51.484 1.00 69.08  ? 131 GLY B O   1 
ATOM   2841  N  N   . VAL B  1 141 ? 13.160  -59.355 49.477 1.00 76.49  ? 132 VAL B N   1 
ATOM   2842  C  CA  . VAL B  1 141 ? 11.911  -58.771 49.953 1.00 77.34  ? 132 VAL B CA  1 
ATOM   2843  C  C   . VAL B  1 141 ? 10.813  -59.836 50.024 1.00 75.20  ? 132 VAL B C   1 
ATOM   2844  O  O   . VAL B  1 141 ? 9.792   -59.647 50.689 1.00 70.66  ? 132 VAL B O   1 
ATOM   2845  C  CB  . VAL B  1 141 ? 11.468  -57.594 49.066 1.00 72.74  ? 132 VAL B CB  1 
ATOM   2846  C  CG1 . VAL B  1 141 ? 10.880  -58.117 47.750 1.00 70.40  ? 132 VAL B CG1 1 
ATOM   2847  C  CG2 . VAL B  1 141 ? 10.477  -56.709 49.811 1.00 60.52  ? 132 VAL B CG2 1 
ATOM   2848  N  N   . ASP B  1 142 ? 11.051  -60.955 49.340 1.00 79.28  ? 133 ASP B N   1 
ATOM   2849  C  CA  . ASP B  1 142 ? 10.180  -62.134 49.391 1.00 81.24  ? 133 ASP B CA  1 
ATOM   2850  C  C   . ASP B  1 142 ? 10.594  -63.130 50.491 1.00 83.04  ? 133 ASP B C   1 
ATOM   2851  O  O   . ASP B  1 142 ? 10.007  -64.198 50.608 1.00 84.99  ? 133 ASP B O   1 
ATOM   2852  C  CB  . ASP B  1 142 ? 10.111  -62.831 48.024 1.00 79.38  ? 133 ASP B CB  1 
ATOM   2853  C  CG  . ASP B  1 142 ? 11.489  -63.128 47.430 1.00 85.12  ? 133 ASP B CG  1 
ATOM   2854  O  OD1 . ASP B  1 142 ? 12.437  -62.333 47.622 1.00 79.37  ? 133 ASP B OD1 1 
ATOM   2855  O  OD2 . ASP B  1 142 ? 11.613  -64.165 46.746 1.00 84.41  ? 133 ASP B OD2 1 
ATOM   2856  N  N   . SER B  1 143 ? 11.607  -62.771 51.281 1.00 82.50  ? 134 SER B N   1 
ATOM   2857  C  CA  . SER B  1 143 ? 12.071  -63.580 52.406 1.00 77.13  ? 134 SER B CA  1 
ATOM   2858  C  C   . SER B  1 143 ? 11.596  -63.022 53.753 1.00 83.57  ? 134 SER B C   1 
ATOM   2859  O  O   . SER B  1 143 ? 10.817  -62.079 53.785 1.00 86.72  ? 134 SER B O   1 
ATOM   2860  C  CB  . SER B  1 143 ? 13.596  -63.714 52.378 1.00 81.41  ? 134 SER B CB  1 
ATOM   2861  O  OG  . SER B  1 143 ? 14.242  -62.721 53.153 1.00 73.49  ? 134 SER B OG  1 
ATOM   2862  N  N   . GLU B  1 144 ? 12.046  -63.627 54.854 1.00 88.85  ? 135 GLU B N   1 
ATOM   2863  C  CA  A GLU B  1 144 ? 11.654  -63.179 56.194 0.60 91.52  ? 135 GLU B CA  1 
ATOM   2864  C  CA  B GLU B  1 144 ? 11.680  -63.199 56.207 0.40 91.50  ? 135 GLU B CA  1 
ATOM   2865  C  C   . GLU B  1 144 ? 12.440  -61.966 56.700 1.00 88.08  ? 135 GLU B C   1 
ATOM   2866  O  O   . GLU B  1 144 ? 11.874  -61.105 57.376 1.00 85.22  ? 135 GLU B O   1 
ATOM   2867  C  CB  A GLU B  1 144 ? 11.716  -64.328 57.207 0.60 93.77  ? 135 GLU B CB  1 
ATOM   2868  C  CB  B GLU B  1 144 ? 11.894  -64.342 57.197 0.40 93.67  ? 135 GLU B CB  1 
ATOM   2869  C  CG  A GLU B  1 144 ? 10.573  -65.325 57.061 0.60 95.55  ? 135 GLU B CG  1 
ATOM   2870  C  CG  B GLU B  1 144 ? 11.779  -63.934 58.652 0.40 94.08  ? 135 GLU B CG  1 
ATOM   2871  C  CD  A GLU B  1 144 ? 9.208   -64.649 57.035 0.60 96.55  ? 135 GLU B CD  1 
ATOM   2872  C  CD  B GLU B  1 144 ? 12.115  -65.070 59.582 0.40 96.93  ? 135 GLU B CD  1 
ATOM   2873  O  OE1 A GLU B  1 144 ? 8.946   -63.808 57.919 0.60 103.08 ? 135 GLU B OE1 1 
ATOM   2874  O  OE1 B GLU B  1 144 ? 12.036  -64.885 60.816 0.40 99.46  ? 135 GLU B OE1 1 
ATOM   2875  O  OE2 A GLU B  1 144 ? 8.398   -64.948 56.130 0.60 88.50  ? 135 GLU B OE2 1 
ATOM   2876  O  OE2 B GLU B  1 144 ? 12.461  -66.151 59.067 0.40 94.61  ? 135 GLU B OE2 1 
ATOM   2877  N  N   . GLU B  1 145 ? 13.732  -61.900 56.385 1.00 86.72  ? 136 GLU B N   1 
ATOM   2878  C  CA  . GLU B  1 145 ? 14.558  -60.750 56.759 1.00 85.36  ? 136 GLU B CA  1 
ATOM   2879  C  C   . GLU B  1 145 ? 14.177  -59.528 55.943 1.00 80.58  ? 136 GLU B C   1 
ATOM   2880  O  O   . GLU B  1 145 ? 14.516  -58.401 56.295 1.00 79.51  ? 136 GLU B O   1 
ATOM   2881  C  CB  . GLU B  1 145 ? 16.050  -61.042 56.574 1.00 83.45  ? 136 GLU B CB  1 
ATOM   2882  C  CG  . GLU B  1 145 ? 16.365  -62.037 55.479 1.00 93.67  ? 136 GLU B CG  1 
ATOM   2883  C  CD  . GLU B  1 145 ? 15.933  -63.454 55.840 1.00 102.61 ? 136 GLU B CD  1 
ATOM   2884  O  OE1 . GLU B  1 145 ? 16.227  -63.904 56.972 1.00 89.12  ? 136 GLU B OE1 1 
ATOM   2885  O  OE2 . GLU B  1 145 ? 15.287  -64.114 54.993 1.00 108.54 ? 136 GLU B OE2 1 
ATOM   2886  N  N   . GLY B  1 146 ? 13.461  -59.760 54.853 1.00 79.98  ? 137 GLY B N   1 
ATOM   2887  C  CA  . GLY B  1 146 ? 13.090  -58.695 53.950 1.00 69.73  ? 137 GLY B CA  1 
ATOM   2888  C  C   . GLY B  1 146 ? 14.313  -58.082 53.300 1.00 69.61  ? 137 GLY B C   1 
ATOM   2889  O  O   . GLY B  1 146 ? 15.422  -58.618 53.370 1.00 72.76  ? 137 GLY B O   1 
ATOM   2890  N  N   . ALA B  1 147 ? 14.109  -56.937 52.667 1.00 67.14  ? 138 ALA B N   1 
ATOM   2891  C  CA  . ALA B  1 147 ? 15.187  -56.254 51.986 1.00 62.57  ? 138 ALA B CA  1 
ATOM   2892  C  C   . ALA B  1 147 ? 15.351  -54.909 52.658 1.00 56.94  ? 138 ALA B C   1 
ATOM   2893  O  O   . ALA B  1 147 ? 14.442  -54.432 53.340 1.00 60.21  ? 138 ALA B O   1 
ATOM   2894  C  CB  . ALA B  1 147 ? 14.862  -56.098 50.523 1.00 58.64  ? 138 ALA B CB  1 
ATOM   2895  N  N   . THR B  1 148 ? 16.523  -54.313 52.501 1.00 55.20  ? 139 THR B N   1 
ATOM   2896  C  CA  . THR B  1 148 ? 16.790  -53.040 53.144 1.00 59.85  ? 139 THR B CA  1 
ATOM   2897  C  C   . THR B  1 148 ? 17.333  -52.033 52.144 1.00 60.85  ? 139 THR B C   1 
ATOM   2898  O  O   . THR B  1 148 ? 18.251  -52.346 51.385 1.00 57.71  ? 139 THR B O   1 
ATOM   2899  C  CB  . THR B  1 148 ? 17.783  -53.197 54.310 1.00 63.69  ? 139 THR B CB  1 
ATOM   2900  O  OG1 . THR B  1 148 ? 17.299  -54.189 55.228 1.00 72.44  ? 139 THR B OG1 1 
ATOM   2901  C  CG2 . THR B  1 148 ? 17.971  -51.875 55.041 1.00 52.58  ? 139 THR B CG2 1 
ATOM   2902  N  N   . CYS B  1 149 ? 16.749  -50.832 52.150 1.00 56.36  ? 140 CYS B N   1 
ATOM   2903  C  CA  . CYS B  1 149 ? 17.226  -49.716 51.335 1.00 58.62  ? 140 CYS B CA  1 
ATOM   2904  C  C   . CYS B  1 149 ? 17.496  -48.436 52.120 1.00 55.14  ? 140 CYS B C   1 
ATOM   2905  O  O   . CYS B  1 149 ? 17.000  -48.242 53.225 1.00 57.35  ? 140 CYS B O   1 
ATOM   2906  C  CB  . CYS B  1 149 ? 16.241  -49.432 50.211 1.00 59.06  ? 140 CYS B CB  1 
ATOM   2907  S  SG  . CYS B  1 149 ? 16.428  -50.624 48.879 1.00 73.27  ? 140 CYS B SG  1 
ATOM   2908  N  N   . ALA B  1 150 ? 18.296  -47.551 51.551 1.00 54.28  ? 141 ALA B N   1 
ATOM   2909  C  CA  . ALA B  1 150 ? 18.462  -46.241 52.167 1.00 51.26  ? 141 ALA B CA  1 
ATOM   2910  C  C   . ALA B  1 150 ? 18.480  -45.114 51.134 1.00 49.18  ? 141 ALA B C   1 
ATOM   2911  O  O   . ALA B  1 150 ? 18.948  -45.286 50.008 1.00 58.07  ? 141 ALA B O   1 
ATOM   2912  C  CB  . ALA B  1 150 ? 19.709  -46.201 53.047 1.00 49.31  ? 141 ALA B CB  1 
ATOM   2913  N  N   . VAL B  1 151 ? 17.933  -43.971 51.524 1.00 47.77  ? 142 VAL B N   1 
ATOM   2914  C  CA  . VAL B  1 151 ? 18.019  -42.757 50.731 1.00 47.62  ? 142 VAL B CA  1 
ATOM   2915  C  C   . VAL B  1 151 ? 18.384  -41.545 51.592 1.00 45.88  ? 142 VAL B C   1 
ATOM   2916  O  O   . VAL B  1 151 ? 17.686  -41.219 52.549 1.00 47.85  ? 142 VAL B O   1 
ATOM   2917  C  CB  . VAL B  1 151 ? 16.702  -42.515 49.908 1.00 53.23  ? 142 VAL B CB  1 
ATOM   2918  C  CG1 . VAL B  1 151 ? 15.459  -42.726 50.765 1.00 52.26  ? 142 VAL B CG1 1 
ATOM   2919  C  CG2 . VAL B  1 151 ? 16.707  -41.140 49.216 1.00 44.92  ? 142 VAL B CG2 1 
ATOM   2920  N  N   . LYS B  1 152 ? 19.490  -40.894 51.244 1.00 44.14  ? 143 LYS B N   1 
ATOM   2921  C  CA  . LYS B  1 152 ? 19.917  -39.655 51.901 1.00 45.80  ? 143 LYS B CA  1 
ATOM   2922  C  C   . LYS B  1 152 ? 19.206  -38.402 51.399 1.00 53.21  ? 143 LYS B C   1 
ATOM   2923  O  O   . LYS B  1 152 ? 19.119  -38.162 50.195 1.00 52.34  ? 143 LYS B O   1 
ATOM   2924  C  CB  . LYS B  1 152 ? 21.416  -39.454 51.717 1.00 48.48  ? 143 LYS B CB  1 
ATOM   2925  C  CG  . LYS B  1 152 ? 22.229  -40.508 52.393 1.00 59.64  ? 143 LYS B CG  1 
ATOM   2926  C  CD  . LYS B  1 152 ? 23.652  -40.508 51.928 1.00 70.75  ? 143 LYS B CD  1 
ATOM   2927  C  CE  . LYS B  1 152 ? 24.343  -41.727 52.488 1.00 78.02  ? 143 LYS B CE  1 
ATOM   2928  N  NZ  . LYS B  1 152 ? 24.163  -41.763 53.981 1.00 85.14  ? 143 LYS B NZ  1 
ATOM   2929  N  N   . PHE B  1 153 ? 18.711  -37.594 52.330 1.00 49.37  ? 144 PHE B N   1 
ATOM   2930  C  CA  . PHE B  1 153 ? 18.125  -36.300 51.996 1.00 49.92  ? 144 PHE B CA  1 
ATOM   2931  C  C   . PHE B  1 153 ? 19.018  -35.183 52.478 1.00 49.43  ? 144 PHE B C   1 
ATOM   2932  O  O   . PHE B  1 153 ? 19.596  -35.286 53.548 1.00 49.92  ? 144 PHE B O   1 
ATOM   2933  C  CB  . PHE B  1 153 ? 16.763  -36.127 52.670 1.00 49.86  ? 144 PHE B CB  1 
ATOM   2934  C  CG  . PHE B  1 153 ? 15.664  -36.962 52.070 1.00 50.33  ? 144 PHE B CG  1 
ATOM   2935  C  CD1 . PHE B  1 153 ? 14.829  -36.433 51.087 1.00 48.20  ? 144 PHE B CD1 1 
ATOM   2936  C  CD2 . PHE B  1 153 ? 15.447  -38.262 52.504 1.00 44.05  ? 144 PHE B CD2 1 
ATOM   2937  C  CE1 . PHE B  1 153 ? 13.816  -37.184 50.543 1.00 45.10  ? 144 PHE B CE1 1 
ATOM   2938  C  CE2 . PHE B  1 153 ? 14.433  -39.011 51.960 1.00 48.27  ? 144 PHE B CE2 1 
ATOM   2939  C  CZ  . PHE B  1 153 ? 13.614  -38.467 50.975 1.00 47.02  ? 144 PHE B CZ  1 
ATOM   2940  N  N   . GLY B  1 154 ? 19.102  -34.104 51.703 1.00 50.55  ? 145 GLY B N   1 
ATOM   2941  C  CA  . GLY B  1 154 ? 19.747  -32.882 52.157 1.00 49.73  ? 145 GLY B CA  1 
ATOM   2942  C  C   . GLY B  1 154 ? 19.691  -31.697 51.209 1.00 46.49  ? 145 GLY B C   1 
ATOM   2943  O  O   . GLY B  1 154 ? 19.123  -31.771 50.140 1.00 47.43  ? 145 GLY B O   1 
ATOM   2944  N  N   . SER B  1 155 ? 20.283  -30.586 51.615 1.00 41.97  ? 146 SER B N   1 
ATOM   2945  C  CA  . SER B  1 155 ? 20.397  -29.459 50.732 1.00 40.01  ? 146 SER B CA  1 
ATOM   2946  C  C   . SER B  1 155 ? 21.274  -29.863 49.594 1.00 48.42  ? 146 SER B C   1 
ATOM   2947  O  O   . SER B  1 155 ? 22.302  -30.498 49.793 1.00 41.66  ? 146 SER B O   1 
ATOM   2948  C  CB  . SER B  1 155 ? 21.022  -28.262 51.427 1.00 51.30  ? 146 SER B CB  1 
ATOM   2949  O  OG  . SER B  1 155 ? 21.088  -27.156 50.544 1.00 51.97  ? 146 SER B OG  1 
ATOM   2950  N  N   . TRP B  1 156 ? 20.845  -29.493 48.389 1.00 60.55  ? 147 TRP B N   1 
ATOM   2951  C  CA  . TRP B  1 156 ? 21.613  -29.751 47.189 1.00 57.20  ? 147 TRP B CA  1 
ATOM   2952  C  C   . TRP B  1 156 ? 22.757  -28.761 47.070 1.00 57.85  ? 147 TRP B C   1 
ATOM   2953  O  O   . TRP B  1 156 ? 23.901  -29.133 46.802 1.00 55.93  ? 147 TRP B O   1 
ATOM   2954  C  CB  . TRP B  1 156 ? 20.714  -29.653 45.959 1.00 55.30  ? 147 TRP B CB  1 
ATOM   2955  C  CG  . TRP B  1 156 ? 21.434  -30.069 44.716 1.00 61.58  ? 147 TRP B CG  1 
ATOM   2956  C  CD1 . TRP B  1 156 ? 21.809  -29.278 43.673 1.00 55.44  ? 147 TRP B CD1 1 
ATOM   2957  C  CD2 . TRP B  1 156 ? 21.912  -31.382 44.416 1.00 60.48  ? 147 TRP B CD2 1 
ATOM   2958  N  NE1 . TRP B  1 156 ? 22.477  -30.021 42.736 1.00 56.32  ? 147 TRP B NE1 1 
ATOM   2959  C  CE2 . TRP B  1 156 ? 22.557  -31.317 43.172 1.00 60.51  ? 147 TRP B CE2 1 
ATOM   2960  C  CE3 . TRP B  1 156 ? 21.863  -32.603 45.084 1.00 58.60  ? 147 TRP B CE3 1 
ATOM   2961  C  CZ2 . TRP B  1 156 ? 23.143  -32.429 42.583 1.00 63.20  ? 147 TRP B CZ2 1 
ATOM   2962  C  CZ3 . TRP B  1 156 ? 22.437  -33.704 44.493 1.00 62.23  ? 147 TRP B CZ3 1 
ATOM   2963  C  CH2 . TRP B  1 156 ? 23.067  -33.612 43.259 1.00 65.59  ? 147 TRP B CH2 1 
ATOM   2964  N  N   . SER B  1 157 ? 22.412  -27.491 47.254 1.00 57.92  ? 148 SER B N   1 
ATOM   2965  C  CA  . SER B  1 157 ? 23.339  -26.382 47.033 1.00 59.16  ? 148 SER B CA  1 
ATOM   2966  C  C   . SER B  1 157 ? 24.056  -25.740 48.234 1.00 60.90  ? 148 SER B C   1 
ATOM   2967  O  O   . SER B  1 157 ? 24.901  -24.882 48.022 1.00 64.89  ? 148 SER B O   1 
ATOM   2968  C  CB  . SER B  1 157 ? 22.627  -25.301 46.216 1.00 67.34  ? 148 SER B CB  1 
ATOM   2969  O  OG  . SER B  1 157 ? 21.929  -25.875 45.110 1.00 64.84  ? 148 SER B OG  1 
ATOM   2970  N  N   . TYR B  1 158 ? 23.750  -26.155 49.469 1.00 61.13  ? 149 TYR B N   1 
ATOM   2971  C  CA  . TYR B  1 158 ? 24.318  -25.522 50.677 1.00 55.57  ? 149 TYR B CA  1 
ATOM   2972  C  C   . TYR B  1 158 ? 25.039  -26.512 51.587 1.00 64.64  ? 149 TYR B C   1 
ATOM   2973  O  O   . TYR B  1 158 ? 24.596  -27.646 51.777 1.00 59.10  ? 149 TYR B O   1 
ATOM   2974  C  CB  . TYR B  1 158 ? 23.247  -24.815 51.526 1.00 53.74  ? 149 TYR B CB  1 
ATOM   2975  C  CG  . TYR B  1 158 ? 22.611  -23.579 50.925 1.00 59.05  ? 149 TYR B CG  1 
ATOM   2976  C  CD1 . TYR B  1 158 ? 23.137  -22.315 51.156 1.00 60.97  ? 149 TYR B CD1 1 
ATOM   2977  C  CD2 . TYR B  1 158 ? 21.459  -23.677 50.146 1.00 63.52  ? 149 TYR B CD2 1 
ATOM   2978  C  CE1 . TYR B  1 158 ? 22.542  -21.177 50.609 1.00 70.09  ? 149 TYR B CE1 1 
ATOM   2979  C  CE2 . TYR B  1 158 ? 20.856  -22.555 49.591 1.00 64.92  ? 149 TYR B CE2 1 
ATOM   2980  C  CZ  . TYR B  1 158 ? 21.395  -21.304 49.824 1.00 72.32  ? 149 TYR B CZ  1 
ATOM   2981  O  OH  . TYR B  1 158 ? 20.777  -20.196 49.271 1.00 61.85  ? 149 TYR B OH  1 
ATOM   2982  N  N   . GLY B  1 159 ? 26.139  -26.050 52.172 1.00 62.53  ? 150 GLY B N   1 
ATOM   2983  C  CA  . GLY B  1 159 ? 26.904  -26.830 53.119 1.00 55.11  ? 150 GLY B CA  1 
ATOM   2984  C  C   . GLY B  1 159 ? 26.526  -26.604 54.573 1.00 61.22  ? 150 GLY B C   1 
ATOM   2985  O  O   . GLY B  1 159 ? 25.628  -25.834 54.897 1.00 57.70  ? 150 GLY B O   1 
ATOM   2986  N  N   . GLY B  1 160 ? 27.253  -27.275 55.457 1.00 64.20  ? 151 GLY B N   1 
ATOM   2987  C  CA  . GLY B  1 160 ? 26.886  -27.361 56.854 1.00 55.61  ? 151 GLY B CA  1 
ATOM   2988  C  C   . GLY B  1 160 ? 27.027  -26.075 57.621 1.00 57.07  ? 151 GLY B C   1 
ATOM   2989  O  O   . GLY B  1 160 ? 26.401  -25.922 58.664 1.00 59.66  ? 151 GLY B O   1 
ATOM   2990  N  N   . TRP B  1 161 ? 27.848  -25.157 57.123 1.00 56.26  ? 152 TRP B N   1 
ATOM   2991  C  CA  . TRP B  1 161 ? 28.007  -23.855 57.777 1.00 67.14  ? 152 TRP B CA  1 
ATOM   2992  C  C   . TRP B  1 161 ? 26.889  -22.852 57.443 1.00 70.80  ? 152 TRP B C   1 
ATOM   2993  O  O   . TRP B  1 161 ? 26.661  -21.886 58.191 1.00 62.64  ? 152 TRP B O   1 
ATOM   2994  C  CB  . TRP B  1 161 ? 29.367  -23.253 57.429 1.00 70.11  ? 152 TRP B CB  1 
ATOM   2995  C  CG  . TRP B  1 161 ? 30.515  -23.987 58.039 1.00 78.35  ? 152 TRP B CG  1 
ATOM   2996  C  CD1 . TRP B  1 161 ? 30.497  -24.755 59.177 1.00 73.59  ? 152 TRP B CD1 1 
ATOM   2997  C  CD2 . TRP B  1 161 ? 31.861  -24.026 57.549 1.00 86.36  ? 152 TRP B CD2 1 
ATOM   2998  N  NE1 . TRP B  1 161 ? 31.752  -25.265 59.421 1.00 72.48  ? 152 TRP B NE1 1 
ATOM   2999  C  CE2 . TRP B  1 161 ? 32.606  -24.834 58.436 1.00 82.19  ? 152 TRP B CE2 1 
ATOM   3000  C  CE3 . TRP B  1 161 ? 32.512  -23.453 56.444 1.00 77.36  ? 152 TRP B CE3 1 
ATOM   3001  C  CZ2 . TRP B  1 161 ? 33.964  -25.085 58.251 1.00 82.03  ? 152 TRP B CZ2 1 
ATOM   3002  C  CZ3 . TRP B  1 161 ? 33.860  -23.703 56.264 1.00 76.78  ? 152 TRP B CZ3 1 
ATOM   3003  C  CH2 . TRP B  1 161 ? 34.572  -24.513 57.162 1.00 87.39  ? 152 TRP B CH2 1 
ATOM   3004  N  N   . GLU B  1 162 ? 26.206  -23.094 56.319 1.00 65.66  ? 153 GLU B N   1 
ATOM   3005  C  CA  . GLU B  1 162 ? 25.053  -22.303 55.894 1.00 60.20  ? 153 GLU B CA  1 
ATOM   3006  C  C   . GLU B  1 162 ? 23.707  -22.912 56.292 1.00 56.79  ? 153 GLU B C   1 
ATOM   3007  O  O   . GLU B  1 162 ? 22.900  -22.281 56.969 1.00 59.33  ? 153 GLU B O   1 
ATOM   3008  C  CB  . GLU B  1 162 ? 25.068  -22.105 54.384 1.00 60.49  ? 153 GLU B CB  1 
ATOM   3009  C  CG  . GLU B  1 162 ? 26.263  -21.313 53.859 1.00 71.00  ? 153 GLU B CG  1 
ATOM   3010  C  CD  . GLU B  1 162 ? 27.441  -22.187 53.443 1.00 69.88  ? 153 GLU B CD  1 
ATOM   3011  O  OE1 . GLU B  1 162 ? 27.265  -23.088 52.606 1.00 67.75  ? 153 GLU B OE1 1 
ATOM   3012  O  OE2 . GLU B  1 162 ? 28.559  -21.965 53.944 1.00 73.19  ? 153 GLU B OE2 1 
ATOM   3013  N  N   . ILE B  1 163 ? 23.454  -24.136 55.856 1.00 49.40  ? 154 ILE B N   1 
ATOM   3014  C  CA  . ILE B  1 163 ? 22.267  -24.864 56.302 1.00 60.42  ? 154 ILE B CA  1 
ATOM   3015  C  C   . ILE B  1 163 ? 22.620  -26.038 57.219 1.00 60.63  ? 154 ILE B C   1 
ATOM   3016  O  O   . ILE B  1 163 ? 23.376  -26.944 56.850 1.00 50.91  ? 154 ILE B O   1 
ATOM   3017  C  CB  . ILE B  1 163 ? 21.414  -25.405 55.122 1.00 62.90  ? 154 ILE B CB  1 
ATOM   3018  C  CG1 . ILE B  1 163 ? 20.719  -24.270 54.374 1.00 55.69  ? 154 ILE B CG1 1 
ATOM   3019  C  CG2 . ILE B  1 163 ? 20.378  -26.391 55.635 1.00 57.27  ? 154 ILE B CG2 1 
ATOM   3020  C  CD1 . ILE B  1 163 ? 19.889  -24.726 53.225 1.00 49.92  ? 154 ILE B CD1 1 
ATOM   3021  N  N   . ASP B  1 164 ? 22.049  -26.028 58.412 1.00 55.50  ? 155 ASP B N   1 
ATOM   3022  C  CA  . ASP B  1 164 ? 22.339  -27.070 59.369 1.00 57.18  ? 155 ASP B CA  1 
ATOM   3023  C  C   . ASP B  1 164 ? 21.164  -28.032 59.469 1.00 58.38  ? 155 ASP B C   1 
ATOM   3024  O  O   . ASP B  1 164 ? 20.081  -27.650 59.901 1.00 62.03  ? 155 ASP B O   1 
ATOM   3025  C  CB  . ASP B  1 164 ? 22.648  -26.448 60.729 1.00 65.65  ? 155 ASP B CB  1 
ATOM   3026  C  CG  . ASP B  1 164 ? 23.137  -27.463 61.742 1.00 67.44  ? 155 ASP B CG  1 
ATOM   3027  O  OD1 . ASP B  1 164 ? 23.902  -28.398 61.366 1.00 58.11  ? 155 ASP B OD1 1 
ATOM   3028  O  OD2 . ASP B  1 164 ? 22.732  -27.308 62.915 1.00 61.31  ? 155 ASP B OD2 1 
ATOM   3029  N  N   . LEU B  1 165 ? 21.383  -29.279 59.062 1.00 55.89  ? 156 LEU B N   1 
ATOM   3030  C  CA  . LEU B  1 165 ? 20.332  -30.282 59.105 1.00 52.61  ? 156 LEU B CA  1 
ATOM   3031  C  C   . LEU B  1 165 ? 20.291  -30.958 60.451 1.00 59.10  ? 156 LEU B C   1 
ATOM   3032  O  O   . LEU B  1 165 ? 21.311  -31.385 60.972 1.00 67.46  ? 156 LEU B O   1 
ATOM   3033  C  CB  . LEU B  1 165 ? 20.552  -31.347 58.045 1.00 53.70  ? 156 LEU B CB  1 
ATOM   3034  C  CG  . LEU B  1 165 ? 19.810  -31.244 56.716 1.00 53.45  ? 156 LEU B CG  1 
ATOM   3035  C  CD1 . LEU B  1 165 ? 20.167  -32.463 55.904 1.00 52.21  ? 156 LEU B CD1 1 
ATOM   3036  C  CD2 . LEU B  1 165 ? 18.300  -31.130 56.896 1.00 53.61  ? 156 LEU B CD2 1 
ATOM   3037  N  N   . LYS B  1 166 ? 19.103  -31.047 61.020 1.00 62.83  ? 157 LYS B N   1 
ATOM   3038  C  CA  . LYS B  1 166 ? 18.914  -31.764 62.265 1.00 59.96  ? 157 LYS B CA  1 
ATOM   3039  C  C   . LYS B  1 166 ? 17.687  -32.614 62.077 1.00 63.87  ? 157 LYS B C   1 
ATOM   3040  O  O   . LYS B  1 166 ? 16.961  -32.455 61.102 1.00 67.67  ? 157 LYS B O   1 
ATOM   3041  C  CB  . LYS B  1 166 ? 18.758  -30.803 63.439 1.00 60.99  ? 157 LYS B CB  1 
ATOM   3042  C  CG  . LYS B  1 166 ? 20.076  -30.144 63.816 1.00 68.22  ? 157 LYS B CG  1 
ATOM   3043  C  CD  . LYS B  1 166 ? 20.091  -29.542 65.220 1.00 66.57  ? 157 LYS B CD  1 
ATOM   3044  C  CE  . LYS B  1 166 ? 21.524  -29.128 65.576 1.00 78.38  ? 157 LYS B CE  1 
ATOM   3045  N  NZ  . LYS B  1 166 ? 21.675  -28.453 66.892 1.00 65.84  ? 157 LYS B NZ  1 
ATOM   3046  N  N   . THR B  1 167 ? 17.463  -33.550 62.977 1.00 68.18  ? 158 THR B N   1 
ATOM   3047  C  CA  . THR B  1 167 ? 16.339  -34.445 62.795 1.00 73.47  ? 158 THR B CA  1 
ATOM   3048  C  C   . THR B  1 167 ? 15.576  -34.580 64.100 1.00 78.04  ? 158 THR B C   1 
ATOM   3049  O  O   . THR B  1 167 ? 16.153  -34.474 65.193 1.00 77.98  ? 158 THR B O   1 
ATOM   3050  C  CB  . THR B  1 167 ? 16.791  -35.810 62.251 1.00 65.28  ? 158 THR B CB  1 
ATOM   3051  O  OG1 . THR B  1 167 ? 15.652  -36.525 61.774 1.00 68.57  ? 158 THR B OG1 1 
ATOM   3052  C  CG2 . THR B  1 167 ? 17.507  -36.607 63.325 1.00 67.32  ? 158 THR B CG2 1 
ATOM   3053  N  N   . ASP B  1 168 ? 14.273  -34.796 63.981 1.00 76.07  ? 159 ASP B N   1 
ATOM   3054  C  CA  A ASP B  1 168 ? 13.382  -34.869 65.138 0.50 83.91  ? 159 ASP B CA  1 
ATOM   3055  C  CA  B ASP B  1 168 ? 13.408  -34.832 65.156 0.50 83.92  ? 159 ASP B CA  1 
ATOM   3056  C  C   . ASP B  1 168 ? 13.703  -36.022 66.099 1.00 91.92  ? 159 ASP B C   1 
ATOM   3057  O  O   . ASP B  1 168 ? 13.937  -35.822 67.299 1.00 84.06  ? 159 ASP B O   1 
ATOM   3058  C  CB  A ASP B  1 168 ? 11.938  -34.998 64.654 0.50 82.09  ? 159 ASP B CB  1 
ATOM   3059  C  CB  B ASP B  1 168 ? 11.929  -34.787 64.737 0.50 82.22  ? 159 ASP B CB  1 
ATOM   3060  C  CG  A ASP B  1 168 ? 10.976  -35.314 65.774 0.50 81.50  ? 159 ASP B CG  1 
ATOM   3061  C  CG  B ASP B  1 168 ? 11.534  -33.461 64.065 0.50 78.50  ? 159 ASP B CG  1 
ATOM   3062  O  OD1 A ASP B  1 168 ? 9.942   -35.963 65.509 0.50 74.01  ? 159 ASP B OD1 1 
ATOM   3063  O  OD1 B ASP B  1 168 ? 12.282  -32.462 64.156 0.50 71.87  ? 159 ASP B OD1 1 
ATOM   3064  O  OD2 A ASP B  1 168 ? 11.257  -34.907 66.920 0.50 82.16  ? 159 ASP B OD2 1 
ATOM   3065  O  OD2 B ASP B  1 168 ? 10.453  -33.417 63.446 0.50 78.90  ? 159 ASP B OD2 1 
ATOM   3066  N  N   . THR B  1 169 ? 13.708  -37.235 65.547 1.00 83.10  ? 160 THR B N   1 
ATOM   3067  C  CA  . THR B  1 169 ? 13.843  -38.495 66.274 1.00 73.02  ? 160 THR B CA  1 
ATOM   3068  C  C   . THR B  1 169 ? 14.798  -39.341 65.478 1.00 75.74  ? 160 THR B C   1 
ATOM   3069  O  O   . THR B  1 169 ? 15.213  -38.927 64.413 1.00 83.40  ? 160 THR B O   1 
ATOM   3070  C  CB  . THR B  1 169 ? 12.517  -39.228 66.282 1.00 75.54  ? 160 THR B CB  1 
ATOM   3071  O  OG1 . THR B  1 169 ? 11.491  -38.309 66.658 1.00 85.18  ? 160 THR B OG1 1 
ATOM   3072  C  CG2 . THR B  1 169 ? 12.542  -40.377 67.255 1.00 77.18  ? 160 THR B CG2 1 
ATOM   3073  N  N   . ASP B  1 170 ? 15.232  -40.483 65.986 1.00 75.64  ? 161 ASP B N   1 
ATOM   3074  C  CA  . ASP B  1 170 ? 15.836  -41.429 65.047 1.00 81.30  ? 161 ASP B CA  1 
ATOM   3075  C  C   . ASP B  1 170 ? 14.780  -42.411 64.573 1.00 72.40  ? 161 ASP B C   1 
ATOM   3076  O  O   . ASP B  1 170 ? 15.059  -43.311 63.791 1.00 67.00  ? 161 ASP B O   1 
ATOM   3077  C  CB  . ASP B  1 170 ? 17.078  -42.141 65.602 1.00 87.28  ? 161 ASP B CB  1 
ATOM   3078  C  CG  . ASP B  1 170 ? 16.783  -42.969 66.834 1.00 95.91  ? 161 ASP B CG  1 
ATOM   3079  O  OD1 . ASP B  1 170 ? 16.113  -44.024 66.689 1.00 82.95  ? 161 ASP B OD1 1 
ATOM   3080  O  OD2 . ASP B  1 170 ? 17.247  -42.565 67.938 1.00 97.42  ? 161 ASP B OD2 1 
ATOM   3081  N  N   . GLN B  1 171 ? 13.558  -42.216 65.046 1.00 72.07  ? 162 GLN B N   1 
ATOM   3082  C  CA  . GLN B  1 171 ? 12.467  -43.099 64.672 1.00 72.82  ? 162 GLN B CA  1 
ATOM   3083  C  C   . GLN B  1 171 ? 11.500  -42.425 63.720 1.00 73.73  ? 162 GLN B C   1 
ATOM   3084  O  O   . GLN B  1 171 ? 10.881  -41.403 64.044 1.00 71.81  ? 162 GLN B O   1 
ATOM   3085  C  CB  . GLN B  1 171 ? 11.728  -43.618 65.901 1.00 82.05  ? 162 GLN B CB  1 
ATOM   3086  C  CG  . GLN B  1 171 ? 12.626  -44.365 66.876 1.00 86.47  ? 162 GLN B CG  1 
ATOM   3087  C  CD  . GLN B  1 171 ? 13.338  -45.543 66.228 1.00 90.56  ? 162 GLN B CD  1 
ATOM   3088  O  OE1 . GLN B  1 171 ? 12.825  -46.166 65.291 1.00 86.59  ? 162 GLN B OE1 1 
ATOM   3089  N  NE2 . GLN B  1 171 ? 14.528  -45.858 66.730 1.00 95.88  ? 162 GLN B NE2 1 
ATOM   3090  N  N   . VAL B  1 172 ? 11.402  -43.021 62.536 1.00 64.36  ? 163 VAL B N   1 
ATOM   3091  C  CA  . VAL B  1 172 ? 10.543  -42.570 61.471 1.00 49.08  ? 163 VAL B CA  1 
ATOM   3092  C  C   . VAL B  1 172 ? 9.128   -42.959 61.849 1.00 53.49  ? 163 VAL B C   1 
ATOM   3093  O  O   . VAL B  1 172 ? 8.898   -44.084 62.267 1.00 54.91  ? 163 VAL B O   1 
ATOM   3094  C  CB  . VAL B  1 172 ? 10.956  -43.289 60.209 1.00 48.81  ? 163 VAL B CB  1 
ATOM   3095  C  CG1 . VAL B  1 172 ? 9.928   -43.105 59.113 1.00 56.78  ? 163 VAL B CG1 1 
ATOM   3096  C  CG2 . VAL B  1 172 ? 12.330  -42.818 59.790 1.00 45.97  ? 163 VAL B CG2 1 
ATOM   3097  N  N   . ASP B  1 173 ? 8.174   -42.045 61.709 1.00 49.03  ? 164 ASP B N   1 
ATOM   3098  C  CA  . ASP B  1 173 ? 6.838   -42.291 62.215 1.00 44.96  ? 164 ASP B CA  1 
ATOM   3099  C  C   . ASP B  1 173 ? 6.117   -43.277 61.303 1.00 52.18  ? 164 ASP B C   1 
ATOM   3100  O  O   . ASP B  1 173 ? 5.923   -43.025 60.117 1.00 55.36  ? 164 ASP B O   1 
ATOM   3101  C  CB  . ASP B  1 173 ? 6.102   -40.954 62.265 1.00 46.07  ? 164 ASP B CB  1 
ATOM   3102  C  CG  . ASP B  1 173 ? 4.629   -41.099 62.542 1.00 55.70  ? 164 ASP B CG  1 
ATOM   3103  O  OD1 . ASP B  1 173 ? 4.223   -42.142 63.107 1.00 56.01  ? 164 ASP B OD1 1 
ATOM   3104  O  OD2 . ASP B  1 173 ? 3.880   -40.156 62.195 1.00 54.61  ? 164 ASP B OD2 1 
ATOM   3105  N  N   . LEU B  1 174 ? 5.749   -44.427 61.855 1.00 48.90  ? 165 LEU B N   1 
ATOM   3106  C  CA  . LEU B  1 174 ? 4.976   -45.421 61.112 1.00 48.30  ? 165 LEU B CA  1 
ATOM   3107  C  C   . LEU B  1 174 ? 3.475   -45.414 61.432 1.00 54.54  ? 165 LEU B C   1 
ATOM   3108  O  O   . LEU B  1 174 ? 2.730   -46.251 60.913 1.00 51.75  ? 165 LEU B O   1 
ATOM   3109  C  CB  . LEU B  1 174 ? 5.576   -46.820 61.257 1.00 47.41  ? 165 LEU B CB  1 
ATOM   3110  C  CG  . LEU B  1 174 ? 7.070   -46.982 60.942 1.00 49.04  ? 165 LEU B CG  1 
ATOM   3111  C  CD1 . LEU B  1 174 ? 7.579   -48.313 61.467 1.00 43.44  ? 165 LEU B CD1 1 
ATOM   3112  C  CD2 . LEU B  1 174 ? 7.376   -46.851 59.474 1.00 42.30  ? 165 LEU B CD2 1 
ATOM   3113  N  N   . SER B  1 175 ? 3.037   -44.504 62.302 1.00 47.95  ? 166 SER B N   1 
ATOM   3114  C  CA  . SER B  1 175 ? 1.658   -44.535 62.783 1.00 44.67  ? 166 SER B CA  1 
ATOM   3115  C  C   . SER B  1 175 ? 0.596   -44.374 61.694 1.00 53.96  ? 166 SER B C   1 
ATOM   3116  O  O   . SER B  1 175 ? -0.529  -44.824 61.867 1.00 55.93  ? 166 SER B O   1 
ATOM   3117  C  CB  . SER B  1 175 ? 1.438   -43.516 63.890 1.00 40.64  ? 166 SER B CB  1 
ATOM   3118  O  OG  . SER B  1 175 ? 1.472   -42.196 63.410 1.00 45.93  ? 166 SER B OG  1 
ATOM   3119  N  N   . SER B  1 176 ? 0.950   -43.690 60.604 1.00 58.74  ? 167 SER B N   1 
ATOM   3120  C  CA  . SER B  1 176 ? 0.060   -43.475 59.449 1.00 61.27  ? 167 SER B CA  1 
ATOM   3121  C  C   . SER B  1 176 ? 0.258   -44.436 58.261 1.00 60.80  ? 167 SER B C   1 
ATOM   3122  O  O   . SER B  1 176 ? -0.403  -44.309 57.230 1.00 66.33  ? 167 SER B O   1 
ATOM   3123  C  CB  . SER B  1 176 ? 0.157   -42.030 58.970 1.00 55.77  ? 167 SER B CB  1 
ATOM   3124  O  OG  . SER B  1 176 ? -0.334  -41.149 59.962 1.00 65.27  ? 167 SER B OG  1 
ATOM   3125  N  N   . TYR B  1 177 ? 1.184   -45.378 58.398 1.00 60.05  ? 168 TYR B N   1 
ATOM   3126  C  CA  . TYR B  1 177 ? 1.494   -46.294 57.315 1.00 55.99  ? 168 TYR B CA  1 
ATOM   3127  C  C   . TYR B  1 177 ? 0.293   -47.155 56.982 1.00 58.44  ? 168 TYR B C   1 
ATOM   3128  O  O   . TYR B  1 177 ? -0.522  -47.478 57.839 1.00 58.95  ? 168 TYR B O   1 
ATOM   3129  C  CB  . TYR B  1 177 ? 2.704   -47.164 57.644 1.00 48.93  ? 168 TYR B CB  1 
ATOM   3130  C  CG  . TYR B  1 177 ? 3.161   -48.014 56.486 1.00 50.77  ? 168 TYR B CG  1 
ATOM   3131  C  CD1 . TYR B  1 177 ? 4.145   -47.568 55.625 1.00 54.22  ? 168 TYR B CD1 1 
ATOM   3132  C  CD2 . TYR B  1 177 ? 2.601   -49.260 56.251 1.00 51.10  ? 168 TYR B CD2 1 
ATOM   3133  C  CE1 . TYR B  1 177 ? 4.563   -48.333 54.568 1.00 52.89  ? 168 TYR B CE1 1 
ATOM   3134  C  CE2 . TYR B  1 177 ? 3.010   -50.039 55.202 1.00 53.04  ? 168 TYR B CE2 1 
ATOM   3135  C  CZ  . TYR B  1 177 ? 3.995   -49.573 54.357 1.00 55.48  ? 168 TYR B CZ  1 
ATOM   3136  O  OH  . TYR B  1 177 ? 4.420   -50.338 53.290 1.00 53.37  ? 168 TYR B OH  1 
ATOM   3137  N  N   . TYR B  1 178 ? 0.194   -47.525 55.717 1.00 56.46  ? 169 TYR B N   1 
ATOM   3138  C  CA  . TYR B  1 178 ? -0.988  -48.186 55.206 1.00 57.22  ? 169 TYR B CA  1 
ATOM   3139  C  C   . TYR B  1 178 ? -0.965  -49.665 55.538 1.00 59.05  ? 169 TYR B C   1 
ATOM   3140  O  O   . TYR B  1 178 ? -0.028  -50.383 55.179 1.00 57.05  ? 169 TYR B O   1 
ATOM   3141  C  CB  . TYR B  1 178 ? -1.090  -47.955 53.697 1.00 60.70  ? 169 TYR B CB  1 
ATOM   3142  C  CG  . TYR B  1 178 ? -2.223  -48.676 53.032 1.00 54.88  ? 169 TYR B CG  1 
ATOM   3143  C  CD1 . TYR B  1 178 ? -3.534  -48.485 53.447 1.00 52.32  ? 169 TYR B CD1 1 
ATOM   3144  C  CD2 . TYR B  1 178 ? -1.983  -49.532 51.972 1.00 56.99  ? 169 TYR B CD2 1 
ATOM   3145  C  CE1 . TYR B  1 178 ? -4.574  -49.140 52.834 1.00 53.23  ? 169 TYR B CE1 1 
ATOM   3146  C  CE2 . TYR B  1 178 ? -3.012  -50.190 51.349 1.00 58.81  ? 169 TYR B CE2 1 
ATOM   3147  C  CZ  . TYR B  1 178 ? -4.302  -49.990 51.786 1.00 57.92  ? 169 TYR B CZ  1 
ATOM   3148  O  OH  . TYR B  1 178 ? -5.316  -50.657 51.164 1.00 59.97  ? 169 TYR B OH  1 
ATOM   3149  N  N   . ALA B  1 179 ? -2.012  -50.098 56.237 1.00 63.35  ? 170 ALA B N   1 
ATOM   3150  C  CA  . ALA B  1 179 ? -2.132  -51.462 56.758 1.00 58.00  ? 170 ALA B CA  1 
ATOM   3151  C  C   . ALA B  1 179 ? -2.152  -52.537 55.680 1.00 65.13  ? 170 ALA B C   1 
ATOM   3152  O  O   . ALA B  1 179 ? -1.655  -53.635 55.899 1.00 56.71  ? 170 ALA B O   1 
ATOM   3153  C  CB  . ALA B  1 179 ? -3.378  -51.577 57.611 1.00 36.82  ? 170 ALA B CB  1 
ATOM   3154  N  N   . SER B  1 180 ? -2.767  -52.213 54.541 1.00 59.57  ? 171 SER B N   1 
ATOM   3155  C  CA  . SER B  1 180 ? -2.990  -53.148 53.427 1.00 59.47  ? 171 SER B CA  1 
ATOM   3156  C  C   . SER B  1 180 ? -1.949  -53.120 52.305 1.00 59.11  ? 171 SER B C   1 
ATOM   3157  O  O   . SER B  1 180 ? -2.166  -53.678 51.232 1.00 61.02  ? 171 SER B O   1 
ATOM   3158  C  CB  . SER B  1 180 ? -4.412  -53.035 52.880 1.00 65.93  ? 171 SER B CB  1 
ATOM   3159  O  OG  . SER B  1 180 ? -5.352  -53.235 53.923 1.00 67.74  ? 171 SER B OG  1 
ATOM   3160  N  N   . SER B  1 181 ? -0.873  -52.381 52.523 1.00 59.39  ? 172 SER B N   1 
ATOM   3161  C  CA  . SER B  1 181 ? 0.210   -52.296 51.558 1.00 59.20  ? 172 SER B CA  1 
ATOM   3162  C  C   . SER B  1 181 ? 0.772   -53.668 51.197 1.00 57.44  ? 172 SER B C   1 
ATOM   3163  O  O   . SER B  1 181 ? 0.824   -54.566 52.030 1.00 58.06  ? 172 SER B O   1 
ATOM   3164  C  CB  . SER B  1 181 ? 1.318   -51.411 52.124 1.00 57.76  ? 172 SER B CB  1 
ATOM   3165  O  OG  . SER B  1 181 ? 2.533   -51.607 51.433 1.00 59.50  ? 172 SER B OG  1 
ATOM   3166  N  N   . LYS B  1 182 ? 1.198   -53.817 49.946 1.00 56.60  ? 173 LYS B N   1 
ATOM   3167  C  CA  . LYS B  1 182 ? 1.834   -55.050 49.491 1.00 63.92  ? 173 LYS B CA  1 
ATOM   3168  C  C   . LYS B  1 182 ? 3.082   -55.311 50.311 1.00 58.75  ? 173 LYS B C   1 
ATOM   3169  O  O   . LYS B  1 182 ? 3.649   -56.394 50.260 1.00 61.36  ? 173 LYS B O   1 
ATOM   3170  C  CB  . LYS B  1 182 ? 2.235   -54.951 48.015 1.00 55.77  ? 173 LYS B CB  1 
ATOM   3171  C  CG  . LYS B  1 182 ? 1.077   -54.765 47.053 1.00 63.63  ? 173 LYS B CG  1 
ATOM   3172  C  CD  . LYS B  1 182 ? 0.416   -56.086 46.719 1.00 62.09  ? 173 LYS B CD  1 
ATOM   3173  C  CE  . LYS B  1 182 ? 1.444   -57.068 46.205 1.00 63.51  ? 173 LYS B CE  1 
ATOM   3174  N  NZ  . LYS B  1 182 ? 0.798   -58.244 45.597 1.00 65.13  ? 173 LYS B NZ  1 
ATOM   3175  N  N   . TYR B  1 183 ? 3.523   -54.304 51.050 1.00 53.18  ? 174 TYR B N   1 
ATOM   3176  C  CA  . TYR B  1 183 ? 4.721   -54.456 51.854 1.00 60.48  ? 174 TYR B CA  1 
ATOM   3177  C  C   . TYR B  1 183 ? 4.531   -54.041 53.306 1.00 62.13  ? 174 TYR B C   1 
ATOM   3178  O  O   . TYR B  1 183 ? 3.885   -53.043 53.598 1.00 61.86  ? 174 TYR B O   1 
ATOM   3179  C  CB  . TYR B  1 183 ? 5.880   -53.685 51.238 1.00 58.50  ? 174 TYR B CB  1 
ATOM   3180  C  CG  . TYR B  1 183 ? 6.168   -54.118 49.844 1.00 53.12  ? 174 TYR B CG  1 
ATOM   3181  C  CD1 . TYR B  1 183 ? 6.916   -55.250 49.594 1.00 59.20  ? 174 TYR B CD1 1 
ATOM   3182  C  CD2 . TYR B  1 183 ? 5.672   -53.409 48.774 1.00 54.88  ? 174 TYR B CD2 1 
ATOM   3183  C  CE1 . TYR B  1 183 ? 7.174   -55.652 48.306 1.00 59.36  ? 174 TYR B CE1 1 
ATOM   3184  C  CE2 . TYR B  1 183 ? 5.923   -53.802 47.493 1.00 57.41  ? 174 TYR B CE2 1 
ATOM   3185  C  CZ  . TYR B  1 183 ? 6.673   -54.919 47.263 1.00 52.90  ? 174 TYR B CZ  1 
ATOM   3186  O  OH  . TYR B  1 183 ? 6.923   -55.300 45.976 1.00 61.58  ? 174 TYR B OH  1 
ATOM   3187  N  N   . GLU B  1 184 ? 5.100   -54.828 54.208 1.00 61.98  ? 175 GLU B N   1 
ATOM   3188  C  CA  . GLU B  1 184 ? 5.140   -54.461 55.608 1.00 66.40  ? 175 GLU B CA  1 
ATOM   3189  C  C   . GLU B  1 184 ? 6.529   -53.930 55.953 1.00 65.31  ? 175 GLU B C   1 
ATOM   3190  O  O   . GLU B  1 184 ? 7.523   -54.284 55.312 1.00 57.63  ? 175 GLU B O   1 
ATOM   3191  C  CB  . GLU B  1 184 ? 4.678   -55.599 56.534 1.00 65.97  ? 175 GLU B CB  1 
ATOM   3192  C  CG  . GLU B  1 184 ? 5.199   -56.998 56.216 1.00 73.56  ? 175 GLU B CG  1 
ATOM   3193  C  CD  . GLU B  1 184 ? 4.758   -58.045 57.253 1.00 80.39  ? 175 GLU B CD  1 
ATOM   3194  O  OE1 . GLU B  1 184 ? 4.177   -57.660 58.295 1.00 76.60  ? 175 GLU B OE1 1 
ATOM   3195  O  OE2 . GLU B  1 184 ? 4.994   -59.255 57.026 1.00 75.22  ? 175 GLU B OE2 1 
ATOM   3196  N  N   . ILE B  1 185 ? 6.556   -52.997 56.899 1.00 65.50  ? 176 ILE B N   1 
ATOM   3197  C  CA  . ILE B  1 185 ? 7.782   -52.347 57.340 1.00 63.96  ? 176 ILE B CA  1 
ATOM   3198  C  C   . ILE B  1 185 ? 8.322   -52.991 58.630 1.00 64.56  ? 176 ILE B C   1 
ATOM   3199  O  O   . ILE B  1 185 ? 7.659   -52.993 59.675 1.00 60.11  ? 176 ILE B O   1 
ATOM   3200  C  CB  . ILE B  1 185 ? 7.546   -50.843 57.574 1.00 55.40  ? 176 ILE B CB  1 
ATOM   3201  C  CG1 . ILE B  1 185 ? 6.729   -50.256 56.439 1.00 51.59  ? 176 ILE B CG1 1 
ATOM   3202  C  CG2 . ILE B  1 185 ? 8.859   -50.104 57.659 1.00 55.20  ? 176 ILE B CG2 1 
ATOM   3203  C  CD1 . ILE B  1 185 ? 7.592   -49.766 55.310 1.00 57.04  ? 176 ILE B CD1 1 
ATOM   3204  N  N   . LEU B  1 186 ? 9.518   -53.559 58.533 1.00 60.57  ? 177 LEU B N   1 
ATOM   3205  C  CA  . LEU B  1 186 ? 10.177  -54.160 59.674 1.00 56.68  ? 177 LEU B CA  1 
ATOM   3206  C  C   . LEU B  1 186 ? 10.804  -53.084 60.553 1.00 62.26  ? 177 LEU B C   1 
ATOM   3207  O  O   . LEU B  1 186 ? 10.642  -53.087 61.775 1.00 65.71  ? 177 LEU B O   1 
ATOM   3208  C  CB  . LEU B  1 186 ? 11.217  -55.174 59.195 1.00 59.51  ? 177 LEU B CB  1 
ATOM   3209  C  CG  . LEU B  1 186 ? 10.609  -56.219 58.246 1.00 64.09  ? 177 LEU B CG  1 
ATOM   3210  C  CD1 . LEU B  1 186 ? 11.657  -57.148 57.632 1.00 64.44  ? 177 LEU B CD1 1 
ATOM   3211  C  CD2 . LEU B  1 186 ? 9.478   -57.006 58.917 1.00 50.81  ? 177 LEU B CD2 1 
ATOM   3212  N  N   . SER B  1 187 ? 11.526  -52.165 59.927 1.00 62.23  ? 178 SER B N   1 
ATOM   3213  C  CA  . SER B  1 187 ? 12.043  -51.003 60.633 1.00 64.70  ? 178 SER B CA  1 
ATOM   3214  C  C   . SER B  1 187 ? 12.229  -49.816 59.691 1.00 62.47  ? 178 SER B C   1 
ATOM   3215  O  O   . SER B  1 187 ? 12.511  -49.980 58.509 1.00 57.56  ? 178 SER B O   1 
ATOM   3216  C  CB  . SER B  1 187 ? 13.347  -51.332 61.389 1.00 58.44  ? 178 SER B CB  1 
ATOM   3217  O  OG  . SER B  1 187 ? 14.377  -51.789 60.527 1.00 61.08  ? 178 SER B OG  1 
ATOM   3218  N  N   . ALA B  1 188 ? 12.041  -48.617 60.221 1.00 64.67  ? 179 ALA B N   1 
ATOM   3219  C  CA  . ALA B  1 188 ? 12.365  -47.404 59.493 1.00 58.88  ? 179 ALA B CA  1 
ATOM   3220  C  C   . ALA B  1 188 ? 13.026  -46.418 60.456 1.00 59.79  ? 179 ALA B C   1 
ATOM   3221  O  O   . ALA B  1 188 ? 12.455  -46.058 61.486 1.00 60.79  ? 179 ALA B O   1 
ATOM   3222  C  CB  . ALA B  1 188 ? 11.111  -46.816 58.901 1.00 56.46  ? 179 ALA B CB  1 
ATOM   3223  N  N   . THR B  1 189 ? 14.230  -45.982 60.125 1.00 53.03  ? 180 THR B N   1 
ATOM   3224  C  CA  . THR B  1 189 ? 14.915  -45.028 60.974 1.00 53.48  ? 180 THR B CA  1 
ATOM   3225  C  C   . THR B  1 189 ? 15.439  -43.838 60.165 1.00 56.74  ? 180 THR B C   1 
ATOM   3226  O  O   . THR B  1 189 ? 15.730  -43.970 58.976 1.00 56.37  ? 180 THR B O   1 
ATOM   3227  C  CB  . THR B  1 189 ? 16.021  -45.717 61.810 1.00 53.73  ? 180 THR B CB  1 
ATOM   3228  O  OG1 . THR B  1 189 ? 17.006  -46.305 60.956 1.00 53.56  ? 180 THR B OG1 1 
ATOM   3229  C  CG2 . THR B  1 189 ? 15.413  -46.809 62.652 1.00 60.18  ? 180 THR B CG2 1 
ATOM   3230  N  N   . GLN B  1 190 ? 15.525  -42.674 60.804 1.00 55.85  ? 181 GLN B N   1 
ATOM   3231  C  CA  . GLN B  1 190 ? 16.051  -41.480 60.155 1.00 51.86  ? 181 GLN B CA  1 
ATOM   3232  C  C   . GLN B  1 190 ? 17.200  -40.919 60.968 1.00 51.11  ? 181 GLN B C   1 
ATOM   3233  O  O   . GLN B  1 190 ? 17.014  -40.444 62.075 1.00 57.01  ? 181 GLN B O   1 
ATOM   3234  C  CB  . GLN B  1 190 ? 14.953  -40.432 59.962 1.00 48.88  ? 181 GLN B CB  1 
ATOM   3235  C  CG  . GLN B  1 190 ? 14.417  -39.849 61.239 1.00 53.10  ? 181 GLN B CG  1 
ATOM   3236  C  CD  . GLN B  1 190 ? 13.054  -39.238 61.079 1.00 55.27  ? 181 GLN B CD  1 
ATOM   3237  O  OE1 . GLN B  1 190 ? 12.340  -39.556 60.155 1.00 66.19  ? 181 GLN B OE1 1 
ATOM   3238  N  NE2 . GLN B  1 190 ? 12.683  -38.359 61.986 1.00 65.88  ? 181 GLN B NE2 1 
ATOM   3239  N  N   . THR B  1 191 ? 18.392  -40.960 60.393 1.00 53.30  ? 182 THR B N   1 
ATOM   3240  C  CA  . THR B  1 191 ? 19.619  -40.623 61.101 1.00 56.89  ? 182 THR B CA  1 
ATOM   3241  C  C   . THR B  1 191 ? 20.344  -39.416 60.491 1.00 55.93  ? 182 THR B C   1 
ATOM   3242  O  O   . THR B  1 191 ? 20.545  -39.349 59.286 1.00 52.84  ? 182 THR B O   1 
ATOM   3243  C  CB  . THR B  1 191 ? 20.570  -41.823 61.084 1.00 55.01  ? 182 THR B CB  1 
ATOM   3244  O  OG1 . THR B  1 191 ? 19.829  -43.016 61.371 1.00 56.01  ? 182 THR B OG1 1 
ATOM   3245  C  CG2 . THR B  1 191 ? 21.655  -41.636 62.106 1.00 57.73  ? 182 THR B CG2 1 
ATOM   3246  N  N   . ARG B  1 192 ? 20.739  -38.460 61.321 1.00 53.82  ? 183 ARG B N   1 
ATOM   3247  C  CA  . ARG B  1 192 ? 21.535  -37.351 60.831 1.00 48.00  ? 183 ARG B CA  1 
ATOM   3248  C  C   . ARG B  1 192 ? 22.972  -37.810 60.664 1.00 50.67  ? 183 ARG B C   1 
ATOM   3249  O  O   . ARG B  1 192 ? 23.426  -38.681 61.385 1.00 59.46  ? 183 ARG B O   1 
ATOM   3250  C  CB  . ARG B  1 192 ? 21.453  -36.193 61.802 1.00 53.27  ? 183 ARG B CB  1 
ATOM   3251  C  CG  . ARG B  1 192 ? 22.149  -34.939 61.340 1.00 53.66  ? 183 ARG B CG  1 
ATOM   3252  C  CD  . ARG B  1 192 ? 22.584  -34.129 62.556 1.00 62.86  ? 183 ARG B CD  1 
ATOM   3253  N  NE  . ARG B  1 192 ? 23.130  -32.838 62.170 1.00 62.20  ? 183 ARG B NE  1 
ATOM   3254  C  CZ  . ARG B  1 192 ? 24.419  -32.598 61.971 1.00 58.66  ? 183 ARG B CZ  1 
ATOM   3255  N  NH1 . ARG B  1 192 ? 25.303  -33.563 62.127 1.00 56.00  ? 183 ARG B NH1 1 
ATOM   3256  N  NH2 . ARG B  1 192 ? 24.825  -31.387 61.610 1.00 57.60  ? 183 ARG B NH2 1 
ATOM   3257  N  N   . SER B  1 193 ? 23.683  -37.258 59.695 1.00 47.93  ? 184 SER B N   1 
ATOM   3258  C  CA  . SER B  1 193 ? 25.056  -37.663 59.450 1.00 51.56  ? 184 SER B CA  1 
ATOM   3259  C  C   . SER B  1 193 ? 25.789  -36.542 58.800 1.00 58.89  ? 184 SER B C   1 
ATOM   3260  O  O   . SER B  1 193 ? 25.168  -35.654 58.232 1.00 59.72  ? 184 SER B O   1 
ATOM   3261  C  CB  . SER B  1 193 ? 25.094  -38.831 58.502 1.00 61.52  ? 184 SER B CB  1 
ATOM   3262  O  OG  . SER B  1 193 ? 23.971  -39.646 58.729 1.00 72.32  ? 184 SER B OG  1 
ATOM   3263  N  N   . GLU B  1 194 ? 27.111  -36.576 58.881 1.00 57.56  ? 185 GLU B N   1 
ATOM   3264  C  CA  . GLU B  1 194 ? 27.907  -35.589 58.178 1.00 65.83  ? 185 GLU B CA  1 
ATOM   3265  C  C   . GLU B  1 194 ? 29.176  -36.130 57.558 1.00 65.62  ? 185 GLU B C   1 
ATOM   3266  O  O   . GLU B  1 194 ? 29.797  -37.034 58.091 1.00 72.11  ? 185 GLU B O   1 
ATOM   3267  C  CB  . GLU B  1 194 ? 28.205  -34.369 59.044 1.00 66.65  ? 185 GLU B CB  1 
ATOM   3268  C  CG  . GLU B  1 194 ? 28.392  -34.590 60.505 1.00 63.61  ? 185 GLU B CG  1 
ATOM   3269  C  CD  . GLU B  1 194 ? 28.442  -33.267 61.242 1.00 84.91  ? 185 GLU B CD  1 
ATOM   3270  O  OE1 . GLU B  1 194 ? 29.452  -33.042 61.943 1.00 90.21  ? 185 GLU B OE1 1 
ATOM   3271  O  OE2 . GLU B  1 194 ? 27.481  -32.456 61.113 1.00 79.07  ? 185 GLU B OE2 1 
ATOM   3272  N  N   . ARG B  1 195 ? 29.563  -35.538 56.434 1.00 67.43  ? 186 ARG B N   1 
ATOM   3273  C  CA  . ARG B  1 195 ? 30.663  -36.035 55.616 1.00 78.63  ? 186 ARG B CA  1 
ATOM   3274  C  C   . ARG B  1 195 ? 31.729  -34.965 55.534 1.00 75.70  ? 186 ARG B C   1 
ATOM   3275  O  O   . ARG B  1 195 ? 31.478  -33.800 55.823 1.00 71.26  ? 186 ARG B O   1 
ATOM   3276  C  CB  . ARG B  1 195 ? 30.183  -36.348 54.182 1.00 80.11  ? 186 ARG B CB  1 
ATOM   3277  C  CG  . ARG B  1 195 ? 29.935  -37.812 53.850 1.00 71.62  ? 186 ARG B CG  1 
ATOM   3278  C  CD  . ARG B  1 195 ? 28.503  -38.203 54.133 1.00 75.53  ? 186 ARG B CD  1 
ATOM   3279  N  NE  . ARG B  1 195 ? 28.344  -39.646 54.024 1.00 86.65  ? 186 ARG B NE  1 
ATOM   3280  C  CZ  . ARG B  1 195 ? 27.335  -40.334 54.557 1.00 87.89  ? 186 ARG B CZ  1 
ATOM   3281  N  NH1 . ARG B  1 195 ? 26.390  -39.698 55.247 1.00 77.56  ? 186 ARG B NH1 1 
ATOM   3282  N  NH2 . ARG B  1 195 ? 27.275  -41.663 54.408 1.00 80.66  ? 186 ARG B NH2 1 
ATOM   3283  N  N   . PHE B  1 196 ? 32.928  -35.365 55.147 1.00 77.98  ? 187 PHE B N   1 
ATOM   3284  C  CA  . PHE B  1 196 ? 33.924  -34.385 54.782 1.00 80.42  ? 187 PHE B CA  1 
ATOM   3285  C  C   . PHE B  1 196 ? 34.537  -34.691 53.413 1.00 92.12  ? 187 PHE B C   1 
ATOM   3286  O  O   . PHE B  1 196 ? 34.578  -35.847 52.986 1.00 92.06  ? 187 PHE B O   1 
ATOM   3287  C  CB  . PHE B  1 196 ? 34.943  -34.263 55.899 1.00 78.73  ? 187 PHE B CB  1 
ATOM   3288  C  CG  . PHE B  1 196 ? 34.366  -33.678 57.155 1.00 77.02  ? 187 PHE B CG  1 
ATOM   3289  C  CD1 . PHE B  1 196 ? 34.429  -32.313 57.390 1.00 77.72  ? 187 PHE B CD1 1 
ATOM   3290  C  CD2 . PHE B  1 196 ? 33.724  -34.479 58.080 1.00 68.53  ? 187 PHE B CD2 1 
ATOM   3291  C  CE1 . PHE B  1 196 ? 33.889  -31.766 58.538 1.00 75.87  ? 187 PHE B CE1 1 
ATOM   3292  C  CE2 . PHE B  1 196 ? 33.180  -33.932 59.227 1.00 70.07  ? 187 PHE B CE2 1 
ATOM   3293  C  CZ  . PHE B  1 196 ? 33.266  -32.578 59.457 1.00 68.86  ? 187 PHE B CZ  1 
ATOM   3294  N  N   . TYR B  1 197 ? 34.947  -33.642 52.702 1.00 101.44 ? 188 TYR B N   1 
ATOM   3295  C  CA  . TYR B  1 197 ? 35.498  -33.786 51.349 1.00 113.40 ? 188 TYR B CA  1 
ATOM   3296  C  C   . TYR B  1 197 ? 36.957  -33.348 51.272 1.00 121.40 ? 188 TYR B C   1 
ATOM   3297  O  O   . TYR B  1 197 ? 37.372  -32.409 51.961 1.00 116.93 ? 188 TYR B O   1 
ATOM   3298  C  CB  . TYR B  1 197 ? 34.690  -32.986 50.310 1.00 111.98 ? 188 TYR B CB  1 
ATOM   3299  C  CG  . TYR B  1 197 ? 33.288  -33.493 50.071 1.00 107.53 ? 188 TYR B CG  1 
ATOM   3300  C  CD1 . TYR B  1 197 ? 33.057  -34.676 49.375 1.00 104.37 ? 188 TYR B CD1 1 
ATOM   3301  C  CD2 . TYR B  1 197 ? 32.190  -32.781 50.536 1.00 102.19 ? 188 TYR B CD2 1 
ATOM   3302  C  CE1 . TYR B  1 197 ? 31.767  -35.141 49.159 1.00 99.58  ? 188 TYR B CE1 1 
ATOM   3303  C  CE2 . TYR B  1 197 ? 30.900  -33.237 50.328 1.00 99.08  ? 188 TYR B CE2 1 
ATOM   3304  C  CZ  . TYR B  1 197 ? 30.693  -34.414 49.638 1.00 96.49  ? 188 TYR B CZ  1 
ATOM   3305  O  OH  . TYR B  1 197 ? 29.403  -34.851 49.443 1.00 84.21  ? 188 TYR B OH  1 
ATOM   3306  N  N   . GLU B  1 198 ? 37.718  -34.011 50.401 1.00 127.02 ? 189 GLU B N   1 
ATOM   3307  C  CA  . GLU B  1 198 ? 39.118  -33.669 50.199 1.00 123.23 ? 189 GLU B CA  1 
ATOM   3308  C  C   . GLU B  1 198 ? 39.162  -32.171 50.040 1.00 111.83 ? 189 GLU B C   1 
ATOM   3309  O  O   . GLU B  1 198 ? 40.032  -31.496 50.581 1.00 107.62 ? 189 GLU B O   1 
ATOM   3310  C  CB  . GLU B  1 198 ? 39.660  -34.327 48.934 1.00 116.59 ? 189 GLU B CB  1 
ATOM   3311  C  CG  . GLU B  1 198 ? 40.527  -35.538 49.172 1.00 122.32 ? 189 GLU B CG  1 
ATOM   3312  C  CD  . GLU B  1 198 ? 41.033  -36.121 47.879 1.00 131.84 ? 189 GLU B CD  1 
ATOM   3313  O  OE1 . GLU B  1 198 ? 40.194  -36.466 47.021 1.00 127.55 ? 189 GLU B OE1 1 
ATOM   3314  O  OE2 . GLU B  1 198 ? 42.266  -36.215 47.711 1.00 126.00 ? 189 GLU B OE2 1 
ATOM   3315  N  N   . CYS B  1 199 ? 38.180  -31.654 49.317 1.00 112.82 ? 190 CYS B N   1 
ATOM   3316  C  CA  . CYS B  1 199 ? 38.092  -30.226 49.091 1.00 116.11 ? 190 CYS B CA  1 
ATOM   3317  C  C   . CYS B  1 199 ? 38.125  -29.382 50.377 1.00 108.89 ? 190 CYS B C   1 
ATOM   3318  O  O   . CYS B  1 199 ? 38.975  -28.504 50.506 1.00 108.82 ? 190 CYS B O   1 
ATOM   3319  C  CB  . CYS B  1 199 ? 36.860  -29.887 48.244 1.00 111.19 ? 190 CYS B CB  1 
ATOM   3320  S  SG  . CYS B  1 199 ? 35.359  -29.502 49.174 1.00 132.07 ? 190 CYS B SG  1 
ATOM   3321  N  N   . CYS B  1 200 ? 37.238  -29.650 51.336 1.00 107.49 ? 191 CYS B N   1 
ATOM   3322  C  CA  . CYS B  1 200 ? 36.932  -28.619 52.338 1.00 115.02 ? 191 CYS B CA  1 
ATOM   3323  C  C   . CYS B  1 200 ? 36.749  -29.029 53.802 1.00 105.91 ? 191 CYS B C   1 
ATOM   3324  O  O   . CYS B  1 200 ? 36.439  -30.174 54.121 1.00 100.39 ? 191 CYS B O   1 
ATOM   3325  C  CB  . CYS B  1 200 ? 35.681  -27.837 51.921 1.00 111.84 ? 191 CYS B CB  1 
ATOM   3326  S  SG  . CYS B  1 200 ? 35.377  -27.714 50.149 1.00 134.80 ? 191 CYS B SG  1 
ATOM   3327  N  N   . LYS B  1 201 ? 36.907  -28.033 54.670 1.00 97.83  ? 192 LYS B N   1 
ATOM   3328  C  CA  . LYS B  1 201 ? 36.684  -28.160 56.102 1.00 91.10  ? 192 LYS B CA  1 
ATOM   3329  C  C   . LYS B  1 201 ? 35.195  -28.110 56.440 1.00 85.65  ? 192 LYS B C   1 
ATOM   3330  O  O   . LYS B  1 201 ? 34.763  -28.692 57.424 1.00 82.38  ? 192 LYS B O   1 
ATOM   3331  C  CB  . LYS B  1 201 ? 37.408  -27.025 56.819 0.00 97.67  ? 192 LYS B CB  1 
ATOM   3332  C  CG  . LYS B  1 201 ? 38.579  -26.488 56.021 0.00 103.82 ? 192 LYS B CG  1 
ATOM   3333  C  CD  . LYS B  1 201 ? 38.709  -24.984 56.145 0.00 107.80 ? 192 LYS B CD  1 
ATOM   3334  C  CE  . LYS B  1 201 ? 39.554  -24.437 55.010 0.00 112.13 ? 192 LYS B CE  1 
ATOM   3335  N  NZ  . LYS B  1 201 ? 38.908  -24.691 53.692 0.00 111.62 ? 192 LYS B NZ  1 
ATOM   3336  N  N   . GLU B  1 202 ? 34.409  -27.415 55.626 1.00 82.33  ? 193 GLU B N   1 
ATOM   3337  C  CA  . GLU B  1 202 ? 32.969  -27.341 55.855 1.00 75.97  ? 193 GLU B CA  1 
ATOM   3338  C  C   . GLU B  1 202 ? 32.291  -28.700 55.721 1.00 82.47  ? 193 GLU B C   1 
ATOM   3339  O  O   . GLU B  1 202 ? 32.355  -29.326 54.654 1.00 83.78  ? 193 GLU B O   1 
ATOM   3340  C  CB  . GLU B  1 202 ? 32.320  -26.369 54.877 1.00 88.83  ? 193 GLU B CB  1 
ATOM   3341  C  CG  . GLU B  1 202 ? 30.815  -26.243 55.034 1.00 77.46  ? 193 GLU B CG  1 
ATOM   3342  C  CD  . GLU B  1 202 ? 30.214  -25.183 54.132 1.00 78.58  ? 193 GLU B CD  1 
ATOM   3343  O  OE1 . GLU B  1 202 ? 29.137  -24.664 54.490 1.00 78.01  ? 193 GLU B OE1 1 
ATOM   3344  O  OE2 . GLU B  1 202 ? 30.803  -24.869 53.072 1.00 77.64  ? 193 GLU B OE2 1 
ATOM   3345  N  N   . PRO B  1 203 ? 31.609  -29.143 56.795 1.00 73.75  ? 194 PRO B N   1 
ATOM   3346  C  CA  . PRO B  1 203 ? 30.906  -30.430 56.868 1.00 71.18  ? 194 PRO B CA  1 
ATOM   3347  C  C   . PRO B  1 203 ? 29.638  -30.455 56.011 1.00 69.72  ? 194 PRO B C   1 
ATOM   3348  O  O   . PRO B  1 203 ? 29.016  -29.423 55.802 1.00 70.41  ? 194 PRO B O   1 
ATOM   3349  C  CB  . PRO B  1 203 ? 30.516  -30.509 58.341 1.00 67.08  ? 194 PRO B CB  1 
ATOM   3350  C  CG  . PRO B  1 203 ? 30.308  -29.110 58.724 1.00 60.61  ? 194 PRO B CG  1 
ATOM   3351  C  CD  . PRO B  1 203 ? 31.369  -28.331 57.998 1.00 67.16  ? 194 PRO B CD  1 
ATOM   3352  N  N   . TYR B  1 204 ? 29.267  -31.612 55.486 1.00 65.35  ? 195 TYR B N   1 
ATOM   3353  C  CA  . TYR B  1 204 ? 27.999  -31.706 54.783 1.00 68.10  ? 195 TYR B CA  1 
ATOM   3354  C  C   . TYR B  1 204 ? 27.058  -32.686 55.472 1.00 65.34  ? 195 TYR B C   1 
ATOM   3355  O  O   . TYR B  1 204 ? 27.308  -33.892 55.503 1.00 64.36  ? 195 TYR B O   1 
ATOM   3356  C  CB  . TYR B  1 204 ? 28.214  -32.026 53.291 1.00 71.36  ? 195 TYR B CB  1 
ATOM   3357  C  CG  . TYR B  1 204 ? 28.973  -30.941 52.540 1.00 74.49  ? 195 TYR B CG  1 
ATOM   3358  C  CD1 . TYR B  1 204 ? 28.301  -29.962 51.825 1.00 77.84  ? 195 TYR B CD1 1 
ATOM   3359  C  CD2 . TYR B  1 204 ? 30.359  -30.885 52.566 1.00 78.87  ? 195 TYR B CD2 1 
ATOM   3360  C  CE1 . TYR B  1 204 ? 28.991  -28.962 51.148 1.00 74.16  ? 195 TYR B CE1 1 
ATOM   3361  C  CE2 . TYR B  1 204 ? 31.054  -29.891 51.895 1.00 85.44  ? 195 TYR B CE2 1 
ATOM   3362  C  CZ  . TYR B  1 204 ? 30.368  -28.934 51.184 1.00 81.77  ? 195 TYR B CZ  1 
ATOM   3363  O  OH  . TYR B  1 204 ? 31.069  -27.955 50.511 1.00 89.84  ? 195 TYR B OH  1 
ATOM   3364  N  N   . PRO B  1 205 ? 26.004  -32.158 56.095 1.00 59.26  ? 196 PRO B N   1 
ATOM   3365  C  CA  . PRO B  1 205 ? 24.927  -32.974 56.653 1.00 58.75  ? 196 PRO B CA  1 
ATOM   3366  C  C   . PRO B  1 205 ? 23.940  -33.501 55.623 1.00 61.46  ? 196 PRO B C   1 
ATOM   3367  O  O   . PRO B  1 205 ? 23.601  -32.794 54.665 1.00 60.89  ? 196 PRO B O   1 
ATOM   3368  C  CB  . PRO B  1 205 ? 24.231  -32.026 57.627 1.00 54.34  ? 196 PRO B CB  1 
ATOM   3369  C  CG  . PRO B  1 205 ? 24.505  -30.694 57.121 1.00 54.31  ? 196 PRO B CG  1 
ATOM   3370  C  CD  . PRO B  1 205 ? 25.813  -30.730 56.379 1.00 59.01  ? 196 PRO B CD  1 
ATOM   3371  N  N   . ASP B  1 206 ? 23.502  -34.737 55.843 1.00 52.81  ? 197 ASP B N   1 
ATOM   3372  C  CA  . ASP B  1 206 ? 22.321  -35.314 55.228 1.00 50.14  ? 197 ASP B CA  1 
ATOM   3373  C  C   . ASP B  1 206 ? 21.546  -36.094 56.290 1.00 50.48  ? 197 ASP B C   1 
ATOM   3374  O  O   . ASP B  1 206 ? 22.062  -36.339 57.361 1.00 51.76  ? 197 ASP B O   1 
ATOM   3375  C  CB  . ASP B  1 206 ? 22.713  -36.252 54.110 1.00 53.35  ? 197 ASP B CB  1 
ATOM   3376  C  CG  . ASP B  1 206 ? 23.702  -37.292 54.547 1.00 69.16  ? 197 ASP B CG  1 
ATOM   3377  O  OD1 . ASP B  1 206 ? 23.277  -38.282 55.207 1.00 70.18  ? 197 ASP B OD1 1 
ATOM   3378  O  OD2 . ASP B  1 206 ? 24.901  -37.118 54.207 1.00 69.16  ? 197 ASP B OD2 1 
ATOM   3379  N  N   . VAL B  1 207 ? 20.300  -36.455 56.016 1.00 51.23  ? 198 VAL B N   1 
ATOM   3380  C  CA  . VAL B  1 207 ? 19.559  -37.342 56.906 1.00 49.40  ? 198 VAL B CA  1 
ATOM   3381  C  C   . VAL B  1 207 ? 19.379  -38.656 56.159 1.00 51.09  ? 198 VAL B C   1 
ATOM   3382  O  O   . VAL B  1 207 ? 18.904  -38.666 55.038 1.00 54.36  ? 198 VAL B O   1 
ATOM   3383  C  CB  . VAL B  1 207 ? 18.194  -36.746 57.340 1.00 44.50  ? 198 VAL B CB  1 
ATOM   3384  C  CG1 . VAL B  1 207 ? 17.321  -37.792 57.996 1.00 50.74  ? 198 VAL B CG1 1 
ATOM   3385  C  CG2 . VAL B  1 207 ? 18.409  -35.609 58.292 1.00 51.30  ? 198 VAL B CG2 1 
ATOM   3386  N  N   . ASN B  1 208 ? 19.788  -39.756 56.766 1.00 46.79  ? 199 ASN B N   1 
ATOM   3387  C  CA  . ASN B  1 208 ? 19.731  -41.045 56.121 1.00 49.75  ? 199 ASN B CA  1 
ATOM   3388  C  C   . ASN B  1 208 ? 18.460  -41.778 56.533 1.00 51.19  ? 199 ASN B C   1 
ATOM   3389  O  O   . ASN B  1 208 ? 18.297  -42.142 57.687 1.00 52.81  ? 199 ASN B O   1 
ATOM   3390  C  CB  . ASN B  1 208 ? 20.984  -41.848 56.491 1.00 55.15  ? 199 ASN B CB  1 
ATOM   3391  C  CG  . ASN B  1 208 ? 21.138  -43.128 55.678 1.00 63.88  ? 199 ASN B CG  1 
ATOM   3392  O  OD1 . ASN B  1 208 ? 20.536  -43.294 54.610 1.00 51.82  ? 199 ASN B OD1 1 
ATOM   3393  N  ND2 . ASN B  1 208 ? 21.965  -44.042 56.184 1.00 59.81  ? 199 ASN B ND2 1 
ATOM   3394  N  N   . LEU B  1 209 ? 17.559  -41.986 55.579 1.00 49.32  ? 200 LEU B N   1 
ATOM   3395  C  CA  . LEU B  1 209 ? 16.344  -42.755 55.806 1.00 48.48  ? 200 LEU B CA  1 
ATOM   3396  C  C   . LEU B  1 209 ? 16.602  -44.200 55.383 1.00 53.39  ? 200 LEU B C   1 
ATOM   3397  O  O   . LEU B  1 209 ? 16.937  -44.477 54.238 1.00 51.84  ? 200 LEU B O   1 
ATOM   3398  C  CB  . LEU B  1 209 ? 15.190  -42.150 55.014 1.00 47.04  ? 200 LEU B CB  1 
ATOM   3399  C  CG  . LEU B  1 209 ? 13.861  -42.896 55.005 1.00 55.08  ? 200 LEU B CG  1 
ATOM   3400  C  CD1 . LEU B  1 209 ? 13.345  -43.022 56.406 1.00 53.00  ? 200 LEU B CD1 1 
ATOM   3401  C  CD2 . LEU B  1 209 ? 12.856  -42.169 54.137 1.00 47.05  ? 200 LEU B CD2 1 
ATOM   3402  N  N   . VAL B  1 210 ? 16.485  -45.124 56.325 1.00 53.88  ? 201 VAL B N   1 
ATOM   3403  C  CA  . VAL B  1 210 ? 16.794  -46.520 56.055 1.00 53.16  ? 201 VAL B CA  1 
ATOM   3404  C  C   . VAL B  1 210 ? 15.539  -47.326 56.311 1.00 54.96  ? 201 VAL B C   1 
ATOM   3405  O  O   . VAL B  1 210 ? 14.994  -47.332 57.431 1.00 51.05  ? 201 VAL B O   1 
ATOM   3406  C  CB  . VAL B  1 210 ? 17.938  -47.046 56.964 1.00 52.93  ? 201 VAL B CB  1 
ATOM   3407  C  CG1 . VAL B  1 210 ? 18.115  -48.542 56.795 1.00 43.38  ? 201 VAL B CG1 1 
ATOM   3408  C  CG2 . VAL B  1 210 ? 19.241  -46.310 56.684 1.00 49.26  ? 201 VAL B CG2 1 
ATOM   3409  N  N   . VAL B  1 211 ? 15.066  -47.997 55.268 1.00 51.42  ? 202 VAL B N   1 
ATOM   3410  C  CA  . VAL B  1 211 ? 13.839  -48.770 55.391 1.00 49.53  ? 202 VAL B CA  1 
ATOM   3411  C  C   . VAL B  1 211 ? 14.034  -50.255 55.169 1.00 51.15  ? 202 VAL B C   1 
ATOM   3412  O  O   . VAL B  1 211 ? 14.658  -50.686 54.211 1.00 55.46  ? 202 VAL B O   1 
ATOM   3413  C  CB  . VAL B  1 211 ? 12.732  -48.240 54.485 1.00 50.80  ? 202 VAL B CB  1 
ATOM   3414  C  CG1 . VAL B  1 211 ? 11.422  -48.894 54.852 1.00 50.82  ? 202 VAL B CG1 1 
ATOM   3415  C  CG2 . VAL B  1 211 ? 12.623  -46.729 54.633 1.00 49.43  ? 202 VAL B CG2 1 
ATOM   3416  N  N   . LYS B  1 212 ? 13.503  -51.033 56.099 1.00 63.73  ? 203 LYS B N   1 
ATOM   3417  C  CA  . LYS B  1 212 ? 13.552  -52.479 56.030 1.00 63.12  ? 203 LYS B CA  1 
ATOM   3418  C  C   . LYS B  1 212 ? 12.106  -52.922 55.872 1.00 62.81  ? 203 LYS B C   1 
ATOM   3419  O  O   . LYS B  1 212 ? 11.236  -52.531 56.655 1.00 64.25  ? 203 LYS B O   1 
ATOM   3420  C  CB  . LYS B  1 212 ? 14.173  -53.039 57.310 1.00 69.58  ? 203 LYS B CB  1 
ATOM   3421  C  CG  . LYS B  1 212 ? 14.679  -54.480 57.222 1.00 76.65  ? 203 LYS B CG  1 
ATOM   3422  C  CD  . LYS B  1 212 ? 15.961  -54.630 58.059 1.00 85.51  ? 203 LYS B CD  1 
ATOM   3423  C  CE  . LYS B  1 212 ? 16.369  -56.080 58.267 1.00 88.76  ? 203 LYS B CE  1 
ATOM   3424  N  NZ  . LYS B  1 212 ? 15.559  -56.726 59.333 1.00 86.90  ? 203 LYS B NZ  1 
ATOM   3425  N  N   . PHE B  1 213 ? 11.844  -53.699 54.829 1.00 63.49  ? 204 PHE B N   1 
ATOM   3426  C  CA  . PHE B  1 213 ? 10.481  -54.080 54.482 1.00 63.56  ? 204 PHE B CA  1 
ATOM   3427  C  C   . PHE B  1 213 ? 10.509  -55.441 53.825 1.00 59.58  ? 204 PHE B C   1 
ATOM   3428  O  O   . PHE B  1 213 ? 11.563  -55.893 53.384 1.00 58.49  ? 204 PHE B O   1 
ATOM   3429  C  CB  . PHE B  1 213 ? 9.842   -53.042 53.542 1.00 64.32  ? 204 PHE B CB  1 
ATOM   3430  C  CG  . PHE B  1 213 ? 10.571  -52.864 52.222 1.00 62.29  ? 204 PHE B CG  1 
ATOM   3431  C  CD1 . PHE B  1 213 ? 10.013  -53.328 51.035 1.00 51.46  ? 204 PHE B CD1 1 
ATOM   3432  C  CD2 . PHE B  1 213 ? 11.811  -52.232 52.175 1.00 58.45  ? 204 PHE B CD2 1 
ATOM   3433  C  CE1 . PHE B  1 213 ? 10.684  -53.169 49.844 1.00 54.44  ? 204 PHE B CE1 1 
ATOM   3434  C  CE2 . PHE B  1 213 ? 12.484  -52.070 50.987 1.00 53.16  ? 204 PHE B CE2 1 
ATOM   3435  C  CZ  . PHE B  1 213 ? 11.922  -52.540 49.819 1.00 55.31  ? 204 PHE B CZ  1 
ATOM   3436  N  N   . ARG B  1 214 ? 9.355   -56.094 53.775 1.00 60.00  ? 205 ARG B N   1 
ATOM   3437  C  CA  . ARG B  1 214 ? 9.221   -57.365 53.076 1.00 63.99  ? 205 ARG B CA  1 
ATOM   3438  C  C   . ARG B  1 214 ? 7.786   -57.504 52.620 1.00 64.33  ? 205 ARG B C   1 
ATOM   3439  O  O   . ARG B  1 214 ? 6.887   -56.864 53.163 1.00 61.65  ? 205 ARG B O   1 
ATOM   3440  C  CB  . ARG B  1 214 ? 9.569   -58.538 53.991 1.00 70.08  ? 205 ARG B CB  1 
ATOM   3441  C  CG  . ARG B  1 214 ? 8.650   -58.641 55.184 1.00 67.65  ? 205 ARG B CG  1 
ATOM   3442  C  CD  . ARG B  1 214 ? 8.497   -60.063 55.663 1.00 73.38  ? 205 ARG B CD  1 
ATOM   3443  N  NE  . ARG B  1 214 ? 7.506   -60.128 56.730 1.00 78.19  ? 205 ARG B NE  1 
ATOM   3444  C  CZ  . ARG B  1 214 ? 7.798   -60.328 58.009 1.00 72.72  ? 205 ARG B CZ  1 
ATOM   3445  N  NH1 . ARG B  1 214 ? 9.055   -60.509 58.379 1.00 66.50  ? 205 ARG B NH1 1 
ATOM   3446  N  NH2 . ARG B  1 214 ? 6.830   -60.361 58.912 1.00 69.50  ? 205 ARG B NH2 1 
ATOM   3447  N  N   . GLU B  1 215 ? 7.559   -58.349 51.629 1.00 67.03  ? 206 GLU B N   1 
ATOM   3448  C  CA  . GLU B  1 215 ? 6.203   -58.523 51.161 1.00 68.96  ? 206 GLU B CA  1 
ATOM   3449  C  C   . GLU B  1 215 ? 5.348   -58.935 52.338 1.00 65.56  ? 206 GLU B C   1 
ATOM   3450  O  O   . GLU B  1 215 ? 5.643   -59.901 53.036 1.00 64.91  ? 206 GLU B O   1 
ATOM   3451  C  CB  . GLU B  1 215 ? 6.124   -59.576 50.059 1.00 66.94  ? 206 GLU B CB  1 
ATOM   3452  C  CG  . GLU B  1 215 ? 6.941   -59.238 48.836 1.00 72.91  ? 206 GLU B CG  1 
ATOM   3453  C  CD  . GLU B  1 215 ? 6.999   -60.388 47.867 1.00 80.91  ? 206 GLU B CD  1 
ATOM   3454  O  OE1 . GLU B  1 215 ? 7.314   -61.513 48.323 1.00 76.29  ? 206 GLU B OE1 1 
ATOM   3455  O  OE2 . GLU B  1 215 ? 6.716   -60.166 46.664 1.00 73.85  ? 206 GLU B OE2 1 
ATOM   3456  N  N   . ARG B  1 216 ? 4.281   -58.189 52.555 1.00 62.53  ? 207 ARG B N   1 
ATOM   3457  C  CA  . ARG B  1 216 ? 3.312   -58.577 53.544 1.00 71.10  ? 207 ARG B CA  1 
ATOM   3458  C  C   . ARG B  1 216 ? 2.704   -59.865 53.040 1.00 78.02  ? 207 ARG B C   1 
ATOM   3459  O  O   . ARG B  1 216 ? 2.743   -60.132 51.837 1.00 80.89  ? 207 ARG B O   1 
ATOM   3460  C  CB  . ARG B  1 216 ? 2.234   -57.512 53.657 1.00 71.92  ? 207 ARG B CB  1 
ATOM   3461  C  CG  . ARG B  1 216 ? 1.160   -57.820 54.660 1.00 74.45  ? 207 ARG B CG  1 
ATOM   3462  C  CD  . ARG B  1 216 ? 0.072   -56.783 54.567 1.00 77.63  ? 207 ARG B CD  1 
ATOM   3463  N  NE  . ARG B  1 216 ? 0.609   -55.443 54.789 1.00 79.84  ? 207 ARG B NE  1 
ATOM   3464  C  CZ  . ARG B  1 216 ? 0.946   -54.964 55.986 1.00 85.89  ? 207 ARG B CZ  1 
ATOM   3465  N  NH1 . ARG B  1 216 ? 0.806   -55.730 57.074 1.00 89.47  ? 207 ARG B NH1 1 
ATOM   3466  N  NH2 . ARG B  1 216 ? 1.425   -53.723 56.099 1.00 72.03  ? 207 ARG B NH2 1 
ATOM   3467  N  N   . ARG B  1 217 ? 2.177   -60.677 53.954 1.00 81.68  ? 208 ARG B N   1 
ATOM   3468  C  CA  . ARG B  1 217 ? 1.321   -61.801 53.569 1.00 93.79  ? 208 ARG B CA  1 
ATOM   3469  C  C   . ARG B  1 217 ? 0.611   -62.434 54.764 1.00 98.63  ? 208 ARG B C   1 
ATOM   3470  O  O   . ARG B  1 217 ? -0.319  -63.226 54.593 1.00 103.18 ? 208 ARG B O   1 
ATOM   3471  C  CB  . ARG B  1 217 ? 2.088   -62.858 52.757 1.00 90.83  ? 208 ARG B CB  1 
ATOM   3472  C  CG  . ARG B  1 217 ? 1.201   -63.636 51.774 1.00 82.15  ? 208 ARG B CG  1 
ATOM   3473  C  CD  . ARG B  1 217 ? 1.994   -64.117 50.570 0.00 89.33  ? 208 ARG B CD  1 
ATOM   3474  N  NE  . ARG B  1 217 ? 2.070   -63.108 49.516 0.00 89.81  ? 208 ARG B NE  1 
ATOM   3475  C  CZ  . ARG B  1 217 ? 2.917   -63.158 48.493 0.00 89.84  ? 208 ARG B CZ  1 
ATOM   3476  N  NH1 . ARG B  1 217 ? 3.774   -64.165 48.388 0.00 90.49  ? 208 ARG B NH1 1 
ATOM   3477  N  NH2 . ARG B  1 217 ? 2.915   -62.199 47.577 0.00 87.89  ? 208 ARG B NH2 1 
ATOM   3478  N  N   . LYS C  1 3   ? -31.816 -1.265  21.590 1.00 90.58  ? -6  LYS C N   1 
ATOM   3479  C  CA  . LYS C  1 3   ? -33.184 -1.750  21.691 1.00 91.90  ? -6  LYS C CA  1 
ATOM   3480  C  C   . LYS C  1 3   ? -33.243 -3.062  22.480 1.00 93.17  ? -6  LYS C C   1 
ATOM   3481  O  O   . LYS C  1 3   ? -33.227 -3.061  23.707 1.00 84.84  ? -6  LYS C O   1 
ATOM   3482  C  CB  . LYS C  1 3   ? -33.775 -1.931  20.290 1.00 94.99  ? -6  LYS C CB  1 
ATOM   3483  C  CG  . LYS C  1 3   ? -32.908 -2.746  19.335 1.00 87.30  ? -6  LYS C CG  1 
ATOM   3484  C  CD  . LYS C  1 3   ? -33.723 -3.256  18.160 1.00 91.29  ? -6  LYS C CD  1 
ATOM   3485  C  CE  . LYS C  1 3   ? -32.992 -4.349  17.416 1.00 89.34  ? -6  LYS C CE  1 
ATOM   3486  N  NZ  . LYS C  1 3   ? -33.049 -5.623  18.176 1.00 95.06  ? -6  LYS C NZ  1 
ATOM   3487  N  N   . ASP C  1 4   ? -33.336 -4.170  21.750 1.00 105.30 ? -5  ASP C N   1 
ATOM   3488  C  CA  . ASP C  1 4   ? -33.170 -5.514  22.282 1.00 96.47  ? -5  ASP C CA  1 
ATOM   3489  C  C   . ASP C  1 4   ? -31.692 -5.674  22.633 1.00 91.82  ? -5  ASP C C   1 
ATOM   3490  O  O   . ASP C  1 4   ? -31.342 -6.303  23.624 1.00 93.75  ? -5  ASP C O   1 
ATOM   3491  C  CB  . ASP C  1 4   ? -33.565 -6.523  21.195 1.00 102.06 ? -5  ASP C CB  1 
ATOM   3492  C  CG  . ASP C  1 4   ? -33.971 -7.877  21.751 1.00 117.77 ? -5  ASP C CG  1 
ATOM   3493  O  OD1 . ASP C  1 4   ? -33.679 -8.159  22.938 1.00 114.68 ? -5  ASP C OD1 1 
ATOM   3494  O  OD2 . ASP C  1 4   ? -34.581 -8.662  20.987 1.00 110.19 ? -5  ASP C OD2 1 
ATOM   3495  N  N   . ASP C  1 5   ? -30.836 -5.080  21.802 1.00 94.13  ? -4  ASP C N   1 
ATOM   3496  C  CA  A ASP C  1 5   ? -29.391 -5.166  21.953 0.35 96.93  ? -4  ASP C CA  1 
ATOM   3497  C  CA  B ASP C  1 5   ? -29.383 -5.169  21.972 0.65 96.94  ? -4  ASP C CA  1 
ATOM   3498  C  C   . ASP C  1 5   ? -28.888 -4.199  23.025 1.00 93.76  ? -4  ASP C C   1 
ATOM   3499  O  O   . ASP C  1 5   ? -27.773 -4.321  23.519 1.00 89.88  ? -4  ASP C O   1 
ATOM   3500  C  CB  A ASP C  1 5   ? -28.710 -4.860  20.614 0.35 103.12 ? -4  ASP C CB  1 
ATOM   3501  C  CB  B ASP C  1 5   ? -28.646 -4.910  20.648 0.65 103.25 ? -4  ASP C CB  1 
ATOM   3502  C  CG  A ASP C  1 5   ? -29.290 -5.668  19.455 0.35 97.52  ? -4  ASP C CG  1 
ATOM   3503  C  CG  B ASP C  1 5   ? -27.115 -4.876  20.807 0.65 105.56 ? -4  ASP C CG  1 
ATOM   3504  O  OD1 A ASP C  1 5   ? -29.500 -6.889  19.612 0.35 94.47  ? -4  ASP C OD1 1 
ATOM   3505  O  OD1 B ASP C  1 5   ? -26.592 -5.355  21.838 0.65 96.16  ? -4  ASP C OD1 1 
ATOM   3506  O  OD2 A ASP C  1 5   ? -29.532 -5.077  18.381 0.35 91.53  ? -4  ASP C OD2 1 
ATOM   3507  O  OD2 B ASP C  1 5   ? -26.429 -4.382  19.885 0.65 101.47 ? -4  ASP C OD2 1 
ATOM   3508  N  N   . ASP C  1 6   ? -29.707 -3.224  23.373 1.00 92.81  ? -3  ASP C N   1 
ATOM   3509  C  CA  . ASP C  1 6   ? -29.307 -2.342  24.447 1.00 89.81  ? -3  ASP C CA  1 
ATOM   3510  C  C   . ASP C  1 6   ? -29.258 -3.162  25.734 1.00 88.37  ? -3  ASP C C   1 
ATOM   3511  O  O   . ASP C  1 6   ? -28.265 -3.122  26.455 1.00 89.37  ? -3  ASP C O   1 
ATOM   3512  C  CB  . ASP C  1 6   ? -30.263 -1.162  24.581 1.00 93.76  ? -3  ASP C CB  1 
ATOM   3513  C  CG  . ASP C  1 6   ? -29.778 -0.129  25.583 1.00 92.86  ? -3  ASP C CG  1 
ATOM   3514  O  OD1 . ASP C  1 6   ? -28.640 0.373   25.439 1.00 85.60  ? -3  ASP C OD1 1 
ATOM   3515  O  OD2 . ASP C  1 6   ? -30.536 0.175   26.529 1.00 94.92  ? -3  ASP C OD2 1 
ATOM   3516  N  N   . ASP C  1 7   ? -30.323 -3.919  26.003 1.00 89.56  ? -2  ASP C N   1 
ATOM   3517  C  CA  . ASP C  1 7   ? -30.392 -4.783  27.184 1.00 92.28  ? -2  ASP C CA  1 
ATOM   3518  C  C   . ASP C  1 7   ? -29.189 -5.699  27.244 1.00 91.36  ? -2  ASP C C   1 
ATOM   3519  O  O   . ASP C  1 7   ? -28.650 -5.968  28.317 1.00 87.82  ? -2  ASP C O   1 
ATOM   3520  C  CB  . ASP C  1 7   ? -31.658 -5.636  27.163 1.00 89.41  ? -2  ASP C CB  1 
ATOM   3521  C  CG  . ASP C  1 7   ? -32.918 -4.809  27.245 1.00 103.92 ? -2  ASP C CG  1 
ATOM   3522  O  OD1 . ASP C  1 7   ? -32.818 -3.563  27.218 1.00 104.54 ? -2  ASP C OD1 1 
ATOM   3523  O  OD2 . ASP C  1 7   ? -34.012 -5.407  27.325 1.00 107.56 ? -2  ASP C OD2 1 
ATOM   3524  N  N   . LYS C  1 8   ? -28.785 -6.184  26.076 1.00 91.86  ? -1  LYS C N   1 
ATOM   3525  C  CA  . LYS C  1 8   ? -27.605 -7.028  25.939 1.00 91.56  ? -1  LYS C CA  1 
ATOM   3526  C  C   . LYS C  1 8   ? -26.357 -6.349  26.528 1.00 84.46  ? -1  LYS C C   1 
ATOM   3527  O  O   . LYS C  1 8   ? -25.629 -6.954  27.311 1.00 82.46  ? -1  LYS C O   1 
ATOM   3528  C  CB  . LYS C  1 8   ? -27.382 -7.379  24.460 1.00 94.37  ? -1  LYS C CB  1 
ATOM   3529  C  CG  . LYS C  1 8   ? -27.348 -8.869  24.129 1.00 90.52  ? -1  LYS C CG  1 
ATOM   3530  C  CD  . LYS C  1 8   ? -28.707 -9.414  23.714 1.00 92.47  ? -1  LYS C CD  1 
ATOM   3531  C  CE  . LYS C  1 8   ? -28.560 -10.811 23.112 1.00 96.14  ? -1  LYS C CE  1 
ATOM   3532  N  NZ  . LYS C  1 8   ? -29.851 -11.543 23.024 1.00 95.71  ? -1  LYS C NZ  1 
ATOM   3533  N  N   . LEU C  1 9   ? -26.134 -5.110  26.142 1.00 79.37  ? 0   LEU C N   1 
ATOM   3534  C  CA  . LEU C  1 9   ? -24.982 -4.397  26.613 1.00 77.87  ? 0   LEU C CA  1 
ATOM   3535  C  C   . LEU C  1 9   ? -24.993 -4.148  28.083 1.00 81.98  ? 0   LEU C C   1 
ATOM   3536  O  O   . LEU C  1 9   ? -24.030 -4.380  28.766 1.00 77.44  ? 0   LEU C O   1 
ATOM   3537  C  CB  . LEU C  1 9   ? -24.911 -3.068  25.907 1.00 80.48  ? 0   LEU C CB  1 
ATOM   3538  C  CG  . LEU C  1 9   ? -24.253 -3.122  24.545 1.00 85.33  ? 0   LEU C CG  1 
ATOM   3539  C  CD1 . LEU C  1 9   ? -24.371 -1.807  23.898 1.00 87.76  ? 0   LEU C CD1 1 
ATOM   3540  C  CD2 . LEU C  1 9   ? -22.831 -3.417  24.746 1.00 78.29  ? 0   LEU C CD2 1 
ATOM   3541  N  N   . HIS C  1 10  ? -26.113 -3.693  28.579 1.00 81.23  ? 1   HIS C N   1 
ATOM   3542  C  CA  . HIS C  1 10  ? -26.241 -3.427  29.992 1.00 72.40  ? 1   HIS C CA  1 
ATOM   3543  C  C   . HIS C  1 10  ? -25.958 -4.724  30.729 1.00 80.31  ? 1   HIS C C   1 
ATOM   3544  O  O   . HIS C  1 10  ? -25.330 -4.717  31.790 1.00 82.25  ? 1   HIS C O   1 
ATOM   3545  C  CB  . HIS C  1 10  ? -27.621 -2.856  30.318 1.00 75.42  ? 1   HIS C CB  1 
ATOM   3546  C  CG  . HIS C  1 10  ? -27.859 -1.499  29.729 1.00 85.21  ? 1   HIS C CG  1 
ATOM   3547  N  ND1 . HIS C  1 10  ? -27.394 -0.340  30.314 1.00 79.61  ? 1   HIS C ND1 1 
ATOM   3548  C  CD2 . HIS C  1 10  ? -28.495 -1.118  28.594 1.00 91.13  ? 1   HIS C CD2 1 
ATOM   3549  C  CE1 . HIS C  1 10  ? -27.740 0.696   29.567 1.00 87.55  ? 1   HIS C CE1 1 
ATOM   3550  N  NE2 . HIS C  1 10  ? -28.408 0.250   28.521 1.00 81.71  ? 1   HIS C NE2 1 
ATOM   3551  N  N   . SER C  1 11  ? -26.388 -5.844  30.146 1.00 81.51  ? 2   SER C N   1 
ATOM   3552  C  CA  . SER C  1 11  ? -26.110 -7.165  30.709 1.00 74.93  ? 2   SER C CA  1 
ATOM   3553  C  C   . SER C  1 11  ? -24.617 -7.408  30.857 1.00 76.96  ? 2   SER C C   1 
ATOM   3554  O  O   . SER C  1 11  ? -24.133 -7.743  31.940 1.00 71.52  ? 2   SER C O   1 
ATOM   3555  C  CB  . SER C  1 11  ? -26.699 -8.260  29.827 1.00 78.44  ? 2   SER C CB  1 
ATOM   3556  O  OG  . SER C  1 11  ? -28.106 -8.155  29.756 1.00 91.01  ? 2   SER C OG  1 
ATOM   3557  N  N   . GLN C  1 12  ? -23.894 -7.251  29.752 1.00 74.64  ? 3   GLN C N   1 
ATOM   3558  C  CA  . GLN C  1 12  ? -22.451 -7.456  29.743 1.00 73.48  ? 3   GLN C CA  1 
ATOM   3559  C  C   . GLN C  1 12  ? -21.741 -6.494  30.685 1.00 74.66  ? 3   GLN C C   1 
ATOM   3560  O  O   . GLN C  1 12  ? -20.965 -6.922  31.533 1.00 75.11  ? 3   GLN C O   1 
ATOM   3561  C  CB  . GLN C  1 12  ? -21.896 -7.324  28.325 1.00 78.28  ? 3   GLN C CB  1 
ATOM   3562  C  CG  . GLN C  1 12  ? -22.597 -8.226  27.316 1.00 83.72  ? 3   GLN C CG  1 
ATOM   3563  C  CD  . GLN C  1 12  ? -21.917 -8.251  25.959 1.00 83.58  ? 3   GLN C CD  1 
ATOM   3564  O  OE1 . GLN C  1 12  ? -21.303 -7.268  25.533 1.00 81.23  ? 3   GLN C OE1 1 
ATOM   3565  N  NE2 . GLN C  1 12  ? -22.018 -9.383  25.275 1.00 77.05  ? 3   GLN C NE2 1 
ATOM   3566  N  N   . ALA C  1 13  ? -22.019 -5.198  30.532 1.00 80.61  ? 4   ALA C N   1 
ATOM   3567  C  CA  . ALA C  1 13  ? -21.438 -4.150  31.382 1.00 77.28  ? 4   ALA C CA  1 
ATOM   3568  C  C   . ALA C  1 13  ? -21.673 -4.383  32.872 1.00 69.09  ? 4   ALA C C   1 
ATOM   3569  O  O   . ALA C  1 13  ? -20.753 -4.270  33.683 1.00 69.97  ? 4   ALA C O   1 
ATOM   3570  C  CB  . ALA C  1 13  ? -21.977 -2.792  30.977 1.00 66.68  ? 4   ALA C CB  1 
ATOM   3571  N  N   . ASN C  1 14  ? -22.911 -4.699  33.226 1.00 66.13  ? 5   ASN C N   1 
ATOM   3572  C  CA  . ASN C  1 14  ? -23.263 -4.987  34.608 1.00 68.29  ? 5   ASN C CA  1 
ATOM   3573  C  C   . ASN C  1 14  ? -22.383 -6.043  35.274 1.00 65.42  ? 5   ASN C C   1 
ATOM   3574  O  O   . ASN C  1 14  ? -21.909 -5.852  36.381 1.00 71.12  ? 5   ASN C O   1 
ATOM   3575  C  CB  . ASN C  1 14  ? -24.712 -5.445  34.672 1.00 71.58  ? 5   ASN C CB  1 
ATOM   3576  C  CG  . ASN C  1 14  ? -25.672 -4.304  34.708 1.00 67.38  ? 5   ASN C CG  1 
ATOM   3577  O  OD1 . ASN C  1 14  ? -25.337 -3.223  35.186 1.00 69.66  ? 5   ASN C OD1 1 
ATOM   3578  N  ND2 . ASN C  1 14  ? -26.885 -4.534  34.226 1.00 66.79  ? 5   ASN C ND2 1 
ATOM   3579  N  N   . LEU C  1 15  ? -22.188 -7.165  34.596 1.00 69.24  ? 6   LEU C N   1 
ATOM   3580  C  CA  . LEU C  1 15  ? -21.421 -8.280  35.130 1.00 66.09  ? 6   LEU C CA  1 
ATOM   3581  C  C   . LEU C  1 15  ? -19.923 -8.006  35.152 1.00 69.60  ? 6   LEU C C   1 
ATOM   3582  O  O   . LEU C  1 15  ? -19.210 -8.516  36.012 1.00 70.33  ? 6   LEU C O   1 
ATOM   3583  C  CB  . LEU C  1 15  ? -21.691 -9.530  34.306 1.00 68.25  ? 6   LEU C CB  1 
ATOM   3584  C  CG  . LEU C  1 15  ? -20.899 -10.775 34.674 1.00 53.98  ? 6   LEU C CG  1 
ATOM   3585  C  CD1 . LEU C  1 15  ? -21.378 -11.314 35.990 1.00 48.04  ? 6   LEU C CD1 1 
ATOM   3586  C  CD2 . LEU C  1 15  ? -21.113 -11.786 33.579 1.00 61.95  ? 6   LEU C CD2 1 
ATOM   3587  N  N   . MET C  1 16  ? -19.437 -7.222  34.194 1.00 68.78  ? 7   MET C N   1 
ATOM   3588  C  CA  . MET C  1 16  ? -18.037 -6.818  34.203 1.00 68.82  ? 7   MET C CA  1 
ATOM   3589  C  C   . MET C  1 16  ? -17.820 -5.882  35.395 1.00 65.86  ? 7   MET C C   1 
ATOM   3590  O  O   . MET C  1 16  ? -16.767 -5.885  36.035 1.00 62.51  ? 7   MET C O   1 
ATOM   3591  C  CB  . MET C  1 16  ? -17.655 -6.146  32.883 1.00 65.06  ? 7   MET C CB  1 
ATOM   3592  C  CG  . MET C  1 16  ? -17.309 -7.092  31.723 1.00 66.23  ? 7   MET C CG  1 
ATOM   3593  S  SD  . MET C  1 16  ? -17.259 -6.170  30.153 1.00 101.60 ? 7   MET C SD  1 
ATOM   3594  C  CE  . MET C  1 16  ? -16.805 -7.419  28.953 1.00 97.71  ? 7   MET C CE  1 
ATOM   3595  N  N   . ARG C  1 17  ? -18.842 -5.095  35.700 1.00 66.09  ? 8   ARG C N   1 
ATOM   3596  C  CA  . ARG C  1 17  ? -18.779 -4.178  36.829 1.00 70.79  ? 8   ARG C CA  1 
ATOM   3597  C  C   . ARG C  1 17  ? -18.843 -4.924  38.159 1.00 66.18  ? 8   ARG C C   1 
ATOM   3598  O  O   . ARG C  1 17  ? -18.135 -4.586  39.096 1.00 66.55  ? 8   ARG C O   1 
ATOM   3599  C  CB  . ARG C  1 17  ? -19.895 -3.128  36.736 1.00 71.71  ? 8   ARG C CB  1 
ATOM   3600  C  CG  . ARG C  1 17  ? -19.860 -2.088  37.851 1.00 71.28  ? 8   ARG C CG  1 
ATOM   3601  C  CD  . ARG C  1 17  ? -20.799 -0.930  37.570 1.00 71.42  ? 8   ARG C CD  1 
ATOM   3602  N  NE  . ARG C  1 17  ? -22.158 -1.374  37.276 1.00 77.57  ? 8   ARG C NE  1 
ATOM   3603  C  CZ  . ARG C  1 17  ? -23.149 -1.406  38.165 1.00 77.82  ? 8   ARG C CZ  1 
ATOM   3604  N  NH1 . ARG C  1 17  ? -22.943 -1.018  39.422 1.00 57.84  ? 8   ARG C NH1 1 
ATOM   3605  N  NH2 . ARG C  1 17  ? -24.354 -1.826  37.790 1.00 72.94  ? 8   ARG C NH2 1 
ATOM   3606  N  N   . LEU C  1 18  ? -19.695 -5.940  38.238 1.00 68.18  ? 9   LEU C N   1 
ATOM   3607  C  CA  . LEU C  1 18  ? -19.803 -6.753  39.445 1.00 68.88  ? 9   LEU C CA  1 
ATOM   3608  C  C   . LEU C  1 18  ? -18.483 -7.447  39.745 1.00 69.44  ? 9   LEU C C   1 
ATOM   3609  O  O   . LEU C  1 18  ? -18.010 -7.429  40.870 1.00 65.43  ? 9   LEU C O   1 
ATOM   3610  C  CB  . LEU C  1 18  ? -20.909 -7.804  39.303 1.00 68.46  ? 9   LEU C CB  1 
ATOM   3611  C  CG  . LEU C  1 18  ? -21.104 -8.744  40.505 1.00 67.03  ? 9   LEU C CG  1 
ATOM   3612  C  CD1 . LEU C  1 18  ? -21.422 -7.970  41.783 1.00 51.56  ? 9   LEU C CD1 1 
ATOM   3613  C  CD2 . LEU C  1 18  ? -22.183 -9.780  40.211 1.00 61.73  ? 9   LEU C CD2 1 
ATOM   3614  N  N   . LYS C  1 19  ? -17.895 -8.067  38.730 1.00 69.14  ? 10  LYS C N   1 
ATOM   3615  C  CA  . LYS C  1 19  ? -16.657 -8.806  38.917 1.00 68.96  ? 10  LYS C CA  1 
ATOM   3616  C  C   . LYS C  1 19  ? -15.524 -7.858  39.245 1.00 71.04  ? 10  LYS C C   1 
ATOM   3617  O  O   . LYS C  1 19  ? -14.586 -8.219  39.938 1.00 75.88  ? 10  LYS C O   1 
ATOM   3618  C  CB  . LYS C  1 19  ? -16.337 -9.673  37.691 1.00 62.45  ? 10  LYS C CB  1 
ATOM   3619  C  CG  . LYS C  1 19  ? -17.162 -10.960 37.644 1.00 58.25  ? 10  LYS C CG  1 
ATOM   3620  C  CD  . LYS C  1 19  ? -17.118 -11.619 36.286 1.00 59.96  ? 10  LYS C CD  1 
ATOM   3621  C  CE  . LYS C  1 19  ? -16.245 -12.864 36.296 1.00 70.51  ? 10  LYS C CE  1 
ATOM   3622  N  NZ  . LYS C  1 19  ? -15.944 -13.336 34.911 1.00 72.60  ? 10  LYS C NZ  1 
ATOM   3623  N  N   . SER C  1 20  ? -15.622 -6.631  38.757 1.00 73.42  ? 11  SER C N   1 
ATOM   3624  C  CA  . SER C  1 20  ? -14.611 -5.636  39.069 1.00 76.16  ? 11  SER C CA  1 
ATOM   3625  C  C   . SER C  1 20  ? -14.661 -5.203  40.536 1.00 74.35  ? 11  SER C C   1 
ATOM   3626  O  O   . SER C  1 20  ? -13.626 -5.034  41.153 1.00 79.48  ? 11  SER C O   1 
ATOM   3627  C  CB  . SER C  1 20  ? -14.721 -4.430  38.134 1.00 76.17  ? 11  SER C CB  1 
ATOM   3628  O  OG  . SER C  1 20  ? -13.621 -3.556  38.318 1.00 80.62  ? 11  SER C OG  1 
ATOM   3629  N  N   . ASP C  1 21  ? -15.858 -5.039  41.092 1.00 69.95  ? 12  ASP C N   1 
ATOM   3630  C  CA  . ASP C  1 21  ? -16.009 -4.647  42.496 1.00 78.44  ? 12  ASP C CA  1 
ATOM   3631  C  C   . ASP C  1 21  ? -15.518 -5.715  43.475 1.00 85.06  ? 12  ASP C C   1 
ATOM   3632  O  O   . ASP C  1 21  ? -14.950 -5.399  44.518 1.00 92.72  ? 12  ASP C O   1 
ATOM   3633  C  CB  . ASP C  1 21  ? -17.469 -4.320  42.821 1.00 78.19  ? 12  ASP C CB  1 
ATOM   3634  C  CG  . ASP C  1 21  ? -17.919 -2.998  42.234 1.00 76.95  ? 12  ASP C CG  1 
ATOM   3635  O  OD1 . ASP C  1 21  ? -17.506 -2.670  41.116 1.00 69.13  ? 12  ASP C OD1 1 
ATOM   3636  O  OD2 . ASP C  1 21  ? -18.684 -2.272  42.893 1.00 101.59 ? 12  ASP C OD2 1 
ATOM   3637  N  N   . LEU C  1 22  ? -15.759 -6.977  43.141 1.00 80.77  ? 13  LEU C N   1 
ATOM   3638  C  CA  . LEU C  1 22  ? -15.389 -8.097  43.994 1.00 73.79  ? 13  LEU C CA  1 
ATOM   3639  C  C   . LEU C  1 22  ? -13.897 -8.448  43.908 1.00 82.12  ? 13  LEU C C   1 
ATOM   3640  O  O   . LEU C  1 22  ? -13.268 -8.736  44.923 1.00 91.43  ? 13  LEU C O   1 
ATOM   3641  C  CB  . LEU C  1 22  ? -16.242 -9.314  43.636 1.00 72.77  ? 13  LEU C CB  1 
ATOM   3642  C  CG  . LEU C  1 22  ? -17.750 -9.166  43.823 1.00 64.59  ? 13  LEU C CG  1 
ATOM   3643  C  CD1 . LEU C  1 22  ? -18.481 -10.356 43.252 1.00 60.26  ? 13  LEU C CD1 1 
ATOM   3644  C  CD2 . LEU C  1 22  ? -18.086 -8.999  45.271 1.00 66.42  ? 13  LEU C CD2 1 
ATOM   3645  N  N   . PHE C  1 23  ? -13.347 -8.411  42.694 1.00 79.90  ? 14  PHE C N   1 
ATOM   3646  C  CA  . PHE C  1 23  ? -12.007 -8.940  42.381 1.00 84.03  ? 14  PHE C CA  1 
ATOM   3647  C  C   . PHE C  1 23  ? -10.840 -8.008  42.084 1.00 87.06  ? 14  PHE C C   1 
ATOM   3648  O  O   . PHE C  1 23  ? -9.722  -8.244  42.517 1.00 83.32  ? 14  PHE C O   1 
ATOM   3649  C  CB  . PHE C  1 23  ? -12.030 -9.799  41.110 1.00 84.25  ? 14  PHE C CB  1 
ATOM   3650  C  CG  . PHE C  1 23  ? -12.917 -11.005 41.205 1.00 76.33  ? 14  PHE C CG  1 
ATOM   3651  C  CD1 . PHE C  1 23  ? -13.356 -11.465 42.429 1.00 78.71  ? 14  PHE C CD1 1 
ATOM   3652  C  CD2 . PHE C  1 23  ? -13.310 -11.677 40.072 1.00 72.89  ? 14  PHE C CD2 1 
ATOM   3653  C  CE1 . PHE C  1 23  ? -14.170 -12.566 42.517 1.00 68.40  ? 14  PHE C CE1 1 
ATOM   3654  C  CE2 . PHE C  1 23  ? -14.125 -12.775 40.162 1.00 75.00  ? 14  PHE C CE2 1 
ATOM   3655  C  CZ  . PHE C  1 23  ? -14.555 -13.216 41.390 1.00 64.05  ? 14  PHE C CZ  1 
ATOM   3656  N  N   . ASN C  1 24  ? -11.092 -7.009  41.249 1.00 93.11  ? 15  ASN C N   1 
ATOM   3657  C  CA  . ASN C  1 24  ? -10.124 -5.951  40.974 1.00 97.62  ? 15  ASN C CA  1 
ATOM   3658  C  C   . ASN C  1 24  ? -10.189 -4.794  41.995 1.00 98.49  ? 15  ASN C C   1 
ATOM   3659  O  O   . ASN C  1 24  ? -9.168  -4.176  42.303 1.00 88.41  ? 15  ASN C O   1 
ATOM   3660  C  CB  . ASN C  1 24  ? -10.290 -5.438  39.529 1.00 93.60  ? 15  ASN C CB  1 
ATOM   3661  C  CG  . ASN C  1 24  ? -10.399 -6.577  38.501 1.00 100.46 ? 15  ASN C CG  1 
ATOM   3662  O  OD1 . ASN C  1 24  ? -9.741  -7.615  38.621 1.00 99.40  ? 15  ASN C OD1 1 
ATOM   3663  N  ND2 . ASN C  1 24  ? -11.241 -6.381  37.491 1.00 99.09  ? 15  ASN C ND2 1 
ATOM   3664  N  N   . ARG C  1 25  ? -11.390 -4.496  42.500 1.00 99.10  ? 16  ARG C N   1 
ATOM   3665  C  CA  . ARG C  1 25  ? -11.561 -3.495  43.563 1.00 96.83  ? 16  ARG C CA  1 
ATOM   3666  C  C   . ARG C  1 25  ? -11.254 -4.019  44.971 1.00 103.64 ? 16  ARG C C   1 
ATOM   3667  O  O   . ARG C  1 25  ? -10.743 -3.281  45.817 1.00 104.24 ? 16  ARG C O   1 
ATOM   3668  C  CB  . ARG C  1 25  ? -12.969 -2.876  43.563 1.00 97.00  ? 16  ARG C CB  1 
ATOM   3669  C  CG  . ARG C  1 25  ? -13.391 -2.370  44.962 1.00 108.03 ? 16  ARG C CG  1 
ATOM   3670  C  CD  . ARG C  1 25  ? -14.522 -1.330  44.961 1.00 105.81 ? 16  ARG C CD  1 
ATOM   3671  N  NE  . ARG C  1 25  ? -15.864 -1.906  45.070 1.00 111.98 ? 16  ARG C NE  1 
ATOM   3672  C  CZ  . ARG C  1 25  ? -16.581 -1.959  46.195 1.00 112.00 ? 16  ARG C CZ  1 
ATOM   3673  N  NH1 . ARG C  1 25  ? -16.094 -1.463  47.333 1.00 95.13  ? 16  ARG C NH1 1 
ATOM   3674  N  NH2 . ARG C  1 25  ? -17.795 -2.506  46.180 1.00 106.68 ? 16  ARG C NH2 1 
ATOM   3675  N  N   . SER C  1 26  ? -11.568 -5.284  45.228 1.00 98.49  ? 17  SER C N   1 
ATOM   3676  C  CA  . SER C  1 26  ? -11.294 -5.850  46.543 1.00 110.92 ? 17  SER C CA  1 
ATOM   3677  C  C   . SER C  1 26  ? -10.244 -6.956  46.418 1.00 111.33 ? 17  SER C C   1 
ATOM   3678  O  O   . SER C  1 26  ? -10.171 -7.632  45.393 1.00 105.32 ? 17  SER C O   1 
ATOM   3679  C  CB  . SER C  1 26  ? -12.577 -6.386  47.198 1.00 107.24 ? 17  SER C CB  1 
ATOM   3680  O  OG  . SER C  1 26  ? -13.389 -5.342  47.712 1.00 94.34  ? 17  SER C OG  1 
ATOM   3681  N  N   . PRO C  1 27  ? -9.413  -7.122  47.462 1.00 111.79 ? 18  PRO C N   1 
ATOM   3682  C  CA  . PRO C  1 27  ? -8.306  -8.091  47.511 1.00 108.41 ? 18  PRO C CA  1 
ATOM   3683  C  C   . PRO C  1 27  ? -8.832  -9.506  47.679 1.00 105.33 ? 18  PRO C C   1 
ATOM   3684  O  O   . PRO C  1 27  ? -9.787  -9.681  48.437 1.00 104.80 ? 18  PRO C O   1 
ATOM   3685  C  CB  . PRO C  1 27  ? -7.567  -7.691  48.782 1.00 102.94 ? 18  PRO C CB  1 
ATOM   3686  C  CG  . PRO C  1 27  ? -8.655  -7.162  49.668 1.00 105.96 ? 18  PRO C CG  1 
ATOM   3687  C  CD  . PRO C  1 27  ? -9.608  -6.442  48.755 1.00 101.65 ? 18  PRO C CD  1 
ATOM   3688  N  N   . MET C  1 28  ? -8.225  -10.494 47.022 1.00 105.88 ? 19  MET C N   1 
ATOM   3689  C  CA  . MET C  1 28  ? -8.699  -11.864 47.193 1.00 100.29 ? 19  MET C CA  1 
ATOM   3690  C  C   . MET C  1 28  ? -8.683  -12.179 48.683 1.00 102.24 ? 19  MET C C   1 
ATOM   3691  O  O   . MET C  1 28  ? -7.777  -11.764 49.420 1.00 98.25  ? 19  MET C O   1 
ATOM   3692  C  CB  . MET C  1 28  ? -7.874  -12.897 46.404 1.00 96.22  ? 19  MET C CB  1 
ATOM   3693  C  CG  . MET C  1 28  ? -8.491  -14.318 46.425 1.00 86.06  ? 19  MET C CG  1 
ATOM   3694  S  SD  . MET C  1 28  ? -7.485  -15.674 45.732 1.00 98.92  ? 19  MET C SD  1 
ATOM   3695  C  CE  . MET C  1 28  ? -7.216  -15.119 44.034 1.00 73.59  ? 19  MET C CE  1 
ATOM   3696  N  N   . TYR C  1 29  ? -9.713  -12.898 49.109 1.00 94.71  ? 20  TYR C N   1 
ATOM   3697  C  CA  . TYR C  1 29  ? -9.910  -13.293 50.496 1.00 84.55  ? 20  TYR C CA  1 
ATOM   3698  C  C   . TYR C  1 29  ? -8.680  -14.059 51.036 1.00 78.28  ? 20  TYR C C   1 
ATOM   3699  O  O   . TYR C  1 29  ? -8.142  -14.939 50.355 1.00 84.78  ? 20  TYR C O   1 
ATOM   3700  C  CB  . TYR C  1 29  ? -11.223 -14.092 50.534 1.00 80.53  ? 20  TYR C CB  1 
ATOM   3701  C  CG  . TYR C  1 29  ? -11.549 -14.905 51.758 1.00 72.70  ? 20  TYR C CG  1 
ATOM   3702  C  CD1 . TYR C  1 29  ? -11.254 -16.259 51.800 1.00 72.97  ? 20  TYR C CD1 1 
ATOM   3703  C  CD2 . TYR C  1 29  ? -12.213 -14.343 52.836 1.00 66.88  ? 20  TYR C CD2 1 
ATOM   3704  C  CE1 . TYR C  1 29  ? -11.568 -17.027 52.894 1.00 70.48  ? 20  TYR C CE1 1 
ATOM   3705  C  CE2 . TYR C  1 29  ? -12.534 -15.102 53.941 1.00 70.22  ? 20  TYR C CE2 1 
ATOM   3706  C  CZ  . TYR C  1 29  ? -12.206 -16.454 53.961 1.00 75.79  ? 20  TYR C CZ  1 
ATOM   3707  O  OH  . TYR C  1 29  ? -12.508 -17.256 55.045 1.00 76.97  ? 20  TYR C OH  1 
ATOM   3708  N  N   . PRO C  1 30  ? -8.210  -13.686 52.241 1.00 67.96  ? 21  PRO C N   1 
ATOM   3709  C  CA  . PRO C  1 30  ? -6.975  -14.147 52.896 1.00 65.51  ? 21  PRO C CA  1 
ATOM   3710  C  C   . PRO C  1 30  ? -7.020  -15.602 53.358 1.00 67.22  ? 21  PRO C C   1 
ATOM   3711  O  O   . PRO C  1 30  ? -5.978  -16.174 53.699 1.00 64.57  ? 21  PRO C O   1 
ATOM   3712  C  CB  . PRO C  1 30  ? -6.844  -13.209 54.095 1.00 63.11  ? 21  PRO C CB  1 
ATOM   3713  C  CG  . PRO C  1 30  ? -8.249  -12.884 54.448 1.00 66.04  ? 21  PRO C CG  1 
ATOM   3714  C  CD  . PRO C  1 30  ? -9.018  -12.848 53.144 1.00 75.75  ? 21  PRO C CD  1 
ATOM   3715  N  N   . GLY C  1 31  ? -8.220  -16.175 53.406 1.00 63.65  ? 22  GLY C N   1 
ATOM   3716  C  CA  . GLY C  1 31  ? -8.406  -17.521 53.912 1.00 65.23  ? 22  GLY C CA  1 
ATOM   3717  C  C   . GLY C  1 31  ? -9.095  -17.503 55.254 1.00 64.85  ? 22  GLY C C   1 
ATOM   3718  O  O   . GLY C  1 31  ? -9.087  -16.483 55.937 1.00 69.62  ? 22  GLY C O   1 
ATOM   3719  N  N   . PRO C  1 32  ? -9.704  -18.631 55.645 1.00 64.93  ? 23  PRO C N   1 
ATOM   3720  C  CA  . PRO C  1 32  ? -10.407 -18.646 56.921 1.00 57.07  ? 23  PRO C CA  1 
ATOM   3721  C  C   . PRO C  1 32  ? -9.398  -18.533 58.030 1.00 60.57  ? 23  PRO C C   1 
ATOM   3722  O  O   . PRO C  1 32  ? -8.205  -18.761 57.824 1.00 58.10  ? 23  PRO C O   1 
ATOM   3723  C  CB  . PRO C  1 32  ? -11.028 -20.034 56.948 1.00 57.89  ? 23  PRO C CB  1 
ATOM   3724  C  CG  . PRO C  1 32  ? -10.058 -20.861 56.223 1.00 59.75  ? 23  PRO C CG  1 
ATOM   3725  C  CD  . PRO C  1 32  ? -9.592  -19.983 55.080 1.00 67.42  ? 23  PRO C CD  1 
ATOM   3726  N  N   . THR C  1 33  ? -9.893  -18.168 59.204 1.00 67.90  ? 24  THR C N   1 
ATOM   3727  C  CA  . THR C  1 33  ? -9.080  -18.029 60.398 1.00 63.33  ? 24  THR C CA  1 
ATOM   3728  C  C   . THR C  1 33  ? -9.876  -18.580 61.560 1.00 62.33  ? 24  THR C C   1 
ATOM   3729  O  O   . THR C  1 33  ? -11.058 -18.865 61.416 1.00 61.28  ? 24  THR C O   1 
ATOM   3730  C  CB  . THR C  1 33  ? -8.713  -16.560 60.649 1.00 67.20  ? 24  THR C CB  1 
ATOM   3731  O  OG1 . THR C  1 33  ? -9.882  -15.740 60.526 1.00 67.81  ? 24  THR C OG1 1 
ATOM   3732  C  CG2 . THR C  1 33  ? -7.693  -16.101 59.627 1.00 63.36  ? 24  THR C CG2 1 
ATOM   3733  N  N   . LYS C  1 34  ? -9.220  -18.767 62.699 1.00 72.83  ? 25  LYS C N   1 
ATOM   3734  C  CA  . LYS C  1 34  ? -9.904  -19.165 63.926 1.00 71.64  ? 25  LYS C CA  1 
ATOM   3735  C  C   . LYS C  1 34  ? -10.957 -18.113 64.298 1.00 67.42  ? 25  LYS C C   1 
ATOM   3736  O  O   . LYS C  1 34  ? -12.004 -18.441 64.853 1.00 66.74  ? 25  LYS C O   1 
ATOM   3737  C  CB  . LYS C  1 34  ? -8.892  -19.351 65.060 1.00 71.34  ? 25  LYS C CB  1 
ATOM   3738  C  CG  . LYS C  1 34  ? -8.457  -18.044 65.689 1.00 80.10  ? 25  LYS C CG  1 
ATOM   3739  C  CD  . LYS C  1 34  ? -7.064  -18.096 66.296 1.00 83.17  ? 25  LYS C CD  1 
ATOM   3740  C  CE  . LYS C  1 34  ? -6.697  -16.718 66.844 1.00 82.11  ? 25  LYS C CE  1 
ATOM   3741  N  NZ  . LYS C  1 34  ? -5.322  -16.652 67.411 1.00 87.66  ? 25  LYS C NZ  1 
ATOM   3742  N  N   . ASP C  1 35  ? -10.682 -16.853 63.964 1.00 65.57  ? 26  ASP C N   1 
ATOM   3743  C  CA  . ASP C  1 35  ? -11.634 -15.758 64.191 1.00 72.35  ? 26  ASP C CA  1 
ATOM   3744  C  C   . ASP C  1 35  ? -12.642 -15.555 63.052 1.00 69.14  ? 26  ASP C C   1 
ATOM   3745  O  O   . ASP C  1 35  ? -13.610 -14.813 63.197 1.00 67.67  ? 26  ASP C O   1 
ATOM   3746  C  CB  . ASP C  1 35  ? -10.897 -14.438 64.444 1.00 71.28  ? 26  ASP C CB  1 
ATOM   3747  C  CG  . ASP C  1 35  ? -10.284 -14.364 65.825 1.00 78.66  ? 26  ASP C CG  1 
ATOM   3748  O  OD1 . ASP C  1 35  ? -9.049  -14.547 65.941 1.00 83.47  ? 26  ASP C OD1 1 
ATOM   3749  O  OD2 . ASP C  1 35  ? -11.040 -14.118 66.792 1.00 77.79  ? 26  ASP C OD2 1 
ATOM   3750  N  N   . ASP C  1 36  ? -12.393 -16.186 61.912 1.00 65.25  ? 27  ASP C N   1 
ATOM   3751  C  CA  . ASP C  1 36  ? -13.300 -16.102 60.778 1.00 65.43  ? 27  ASP C CA  1 
ATOM   3752  C  C   . ASP C  1 36  ? -13.328 -17.470 60.129 1.00 67.61  ? 27  ASP C C   1 
ATOM   3753  O  O   . ASP C  1 36  ? -12.759 -17.645 59.054 1.00 65.00  ? 27  ASP C O   1 
ATOM   3754  C  CB  . ASP C  1 36  ? -12.789 -15.047 59.785 1.00 70.67  ? 27  ASP C CB  1 
ATOM   3755  C  CG  . ASP C  1 36  ? -13.731 -14.822 58.608 1.00 74.10  ? 27  ASP C CG  1 
ATOM   3756  O  OD1 . ASP C  1 36  ? -14.918 -15.200 58.710 1.00 75.78  ? 27  ASP C OD1 1 
ATOM   3757  O  OD2 . ASP C  1 36  ? -13.279 -14.257 57.586 1.00 68.05  ? 27  ASP C OD2 1 
ATOM   3758  N  N   . PRO C  1 37  ? -13.974 -18.457 60.786 1.00 69.82  ? 28  PRO C N   1 
ATOM   3759  C  CA  . PRO C  1 37  ? -13.876 -19.832 60.300 1.00 59.32  ? 28  PRO C CA  1 
ATOM   3760  C  C   . PRO C  1 37  ? -14.865 -20.037 59.182 1.00 61.59  ? 28  PRO C C   1 
ATOM   3761  O  O   . PRO C  1 37  ? -15.674 -19.161 58.913 1.00 63.43  ? 28  PRO C O   1 
ATOM   3762  C  CB  . PRO C  1 37  ? -14.313 -20.665 61.513 1.00 60.36  ? 28  PRO C CB  1 
ATOM   3763  C  CG  . PRO C  1 37  ? -14.552 -19.698 62.630 1.00 67.10  ? 28  PRO C CG  1 
ATOM   3764  C  CD  . PRO C  1 37  ? -14.835 -18.383 61.972 1.00 67.64  ? 28  PRO C CD  1 
ATOM   3765  N  N   . LEU C  1 38  ? -14.840 -21.211 58.575 1.00 63.76  ? 29  LEU C N   1 
ATOM   3766  C  CA  . LEU C  1 38  ? -15.604 -21.441 57.365 1.00 55.16  ? 29  LEU C CA  1 
ATOM   3767  C  C   . LEU C  1 38  ? -16.014 -22.895 57.298 1.00 61.05  ? 29  LEU C C   1 
ATOM   3768  O  O   . LEU C  1 38  ? -15.270 -23.772 57.731 1.00 59.16  ? 29  LEU C O   1 
ATOM   3769  C  CB  . LEU C  1 38  ? -14.732 -21.119 56.168 1.00 54.21  ? 29  LEU C CB  1 
ATOM   3770  C  CG  . LEU C  1 38  ? -15.349 -21.481 54.839 1.00 59.43  ? 29  LEU C CG  1 
ATOM   3771  C  CD1 . LEU C  1 38  ? -16.357 -20.407 54.507 1.00 67.17  ? 29  LEU C CD1 1 
ATOM   3772  C  CD2 . LEU C  1 38  ? -14.276 -21.582 53.777 1.00 58.15  ? 29  LEU C CD2 1 
ATOM   3773  N  N   . THR C  1 39  ? -17.198 -23.158 56.757 1.00 63.20  ? 30  THR C N   1 
ATOM   3774  C  CA  . THR C  1 39  ? -17.607 -24.539 56.523 1.00 62.29  ? 30  THR C CA  1 
ATOM   3775  C  C   . THR C  1 39  ? -17.680 -24.869 55.028 1.00 61.29  ? 30  THR C C   1 
ATOM   3776  O  O   . THR C  1 39  ? -18.349 -24.190 54.261 1.00 60.15  ? 30  THR C O   1 
ATOM   3777  C  CB  . THR C  1 39  ? -18.954 -24.879 57.200 1.00 60.76  ? 30  THR C CB  1 
ATOM   3778  O  OG1 . THR C  1 39  ? -18.914 -24.486 58.575 1.00 55.44  ? 30  THR C OG1 1 
ATOM   3779  C  CG2 . THR C  1 39  ? -19.233 -26.375 57.114 1.00 56.96  ? 30  THR C CG2 1 
ATOM   3780  N  N   . VAL C  1 40  ? -16.967 -25.920 54.638 1.00 59.94  ? 31  VAL C N   1 
ATOM   3781  C  CA  . VAL C  1 40  ? -17.019 -26.455 53.293 1.00 56.99  ? 31  VAL C CA  1 
ATOM   3782  C  C   . VAL C  1 40  ? -17.826 -27.734 53.330 1.00 57.78  ? 31  VAL C C   1 
ATOM   3783  O  O   . VAL C  1 40  ? -17.588 -28.590 54.173 1.00 55.04  ? 31  VAL C O   1 
ATOM   3784  C  CB  . VAL C  1 40  ? -15.607 -26.807 52.794 1.00 58.56  ? 31  VAL C CB  1 
ATOM   3785  C  CG1 . VAL C  1 40  ? -15.634 -27.270 51.324 1.00 50.83  ? 31  VAL C CG1 1 
ATOM   3786  C  CG2 . VAL C  1 40  ? -14.674 -25.625 52.990 1.00 59.97  ? 31  VAL C CG2 1 
ATOM   3787  N  N   . TYR C  1 41  ? -18.776 -27.864 52.411 1.00 58.97  ? 32  TYR C N   1 
ATOM   3788  C  CA  . TYR C  1 41  ? -19.515 -29.110 52.238 1.00 60.80  ? 32  TYR C CA  1 
ATOM   3789  C  C   . TYR C  1 41  ? -18.938 -29.943 51.111 1.00 60.45  ? 32  TYR C C   1 
ATOM   3790  O  O   . TYR C  1 41  ? -18.710 -29.423 50.019 1.00 62.10  ? 32  TYR C O   1 
ATOM   3791  C  CB  . TYR C  1 41  ? -20.978 -28.812 51.943 1.00 60.64  ? 32  TYR C CB  1 
ATOM   3792  C  CG  . TYR C  1 41  ? -21.670 -28.209 53.123 1.00 69.35  ? 32  TYR C CG  1 
ATOM   3793  C  CD1 . TYR C  1 41  ? -22.426 -28.997 53.985 1.00 66.16  ? 32  TYR C CD1 1 
ATOM   3794  C  CD2 . TYR C  1 41  ? -21.537 -26.855 53.404 1.00 67.60  ? 32  TYR C CD2 1 
ATOM   3795  C  CE1 . TYR C  1 41  ? -23.050 -28.447 55.068 1.00 65.90  ? 32  TYR C CE1 1 
ATOM   3796  C  CE2 . TYR C  1 41  ? -22.155 -26.292 54.491 1.00 63.90  ? 32  TYR C CE2 1 
ATOM   3797  C  CZ  . TYR C  1 41  ? -22.912 -27.090 55.316 1.00 74.70  ? 32  TYR C CZ  1 
ATOM   3798  O  OH  . TYR C  1 41  ? -23.534 -26.528 56.403 1.00 86.44  ? 32  TYR C OH  1 
ATOM   3799  N  N   . LEU C  1 42  ? -18.706 -31.227 51.377 1.00 52.51  ? 33  LEU C N   1 
ATOM   3800  C  CA  . LEU C  1 42  ? -18.306 -32.161 50.328 1.00 55.30  ? 33  LEU C CA  1 
ATOM   3801  C  C   . LEU C  1 42  ? -19.403 -33.152 49.972 1.00 58.46  ? 33  LEU C C   1 
ATOM   3802  O  O   . LEU C  1 42  ? -20.165 -33.600 50.818 1.00 65.59  ? 33  LEU C O   1 
ATOM   3803  C  CB  . LEU C  1 42  ? -17.053 -32.928 50.712 1.00 55.48  ? 33  LEU C CB  1 
ATOM   3804  C  CG  . LEU C  1 42  ? -15.786 -32.107 50.864 1.00 65.03  ? 33  LEU C CG  1 
ATOM   3805  C  CD1 . LEU C  1 42  ? -14.634 -32.984 50.446 1.00 68.28  ? 33  LEU C CD1 1 
ATOM   3806  C  CD2 . LEU C  1 42  ? -15.835 -30.842 50.024 1.00 62.20  ? 33  LEU C CD2 1 
ATOM   3807  N  N   . SER C  1 43  ? -19.474 -33.487 48.696 1.00 62.06  ? 34  SER C N   1 
ATOM   3808  C  CA  . SER C  1 43  ? -20.482 -34.398 48.195 1.00 63.18  ? 34  SER C CA  1 
ATOM   3809  C  C   . SER C  1 43  ? -19.801 -35.188 47.078 1.00 60.85  ? 34  SER C C   1 
ATOM   3810  O  O   . SER C  1 43  ? -19.066 -34.611 46.284 1.00 54.83  ? 34  SER C O   1 
ATOM   3811  C  CB  . SER C  1 43  ? -21.664 -33.575 47.665 1.00 62.42  ? 34  SER C CB  1 
ATOM   3812  O  OG  . SER C  1 43  ? -22.844 -34.348 47.561 1.00 78.24  ? 34  SER C OG  1 
ATOM   3813  N  N   . PHE C  1 44  ? -20.023 -36.498 47.004 1.00 61.63  ? 35  PHE C N   1 
ATOM   3814  C  CA  . PHE C  1 44  ? -19.376 -37.290 45.947 1.00 56.35  ? 35  PHE C CA  1 
ATOM   3815  C  C   . PHE C  1 44  ? -20.371 -37.952 45.013 1.00 60.78  ? 35  PHE C C   1 
ATOM   3816  O  O   . PHE C  1 44  ? -21.413 -38.442 45.444 1.00 68.26  ? 35  PHE C O   1 
ATOM   3817  C  CB  . PHE C  1 44  ? -18.408 -38.327 46.515 1.00 48.77  ? 35  PHE C CB  1 
ATOM   3818  C  CG  . PHE C  1 44  ? -17.193 -37.729 47.143 1.00 53.48  ? 35  PHE C CG  1 
ATOM   3819  C  CD1 . PHE C  1 44  ? -16.041 -37.546 46.406 1.00 51.25  ? 35  PHE C CD1 1 
ATOM   3820  C  CD2 . PHE C  1 44  ? -17.208 -37.331 48.469 1.00 49.98  ? 35  PHE C CD2 1 
ATOM   3821  C  CE1 . PHE C  1 44  ? -14.920 -36.990 46.984 1.00 53.14  ? 35  PHE C CE1 1 
ATOM   3822  C  CE2 . PHE C  1 44  ? -16.091 -36.770 49.052 1.00 46.91  ? 35  PHE C CE2 1 
ATOM   3823  C  CZ  . PHE C  1 44  ? -14.945 -36.601 48.315 1.00 51.70  ? 35  PHE C CZ  1 
ATOM   3824  N  N   . SER C  1 45  ? -20.049 -37.926 43.726 1.00 57.53  ? 36  SER C N   1 
ATOM   3825  C  CA  . SER C  1 45  ? -20.825 -38.604 42.711 1.00 50.62  ? 36  SER C CA  1 
ATOM   3826  C  C   . SER C  1 45  ? -19.830 -39.493 41.993 1.00 51.03  ? 36  SER C C   1 
ATOM   3827  O  O   . SER C  1 45  ? -18.913 -39.017 41.345 1.00 52.13  ? 36  SER C O   1 
ATOM   3828  C  CB  . SER C  1 45  ? -21.426 -37.574 41.766 1.00 52.63  ? 36  SER C CB  1 
ATOM   3829  O  OG  . SER C  1 45  ? -22.667 -37.998 41.262 1.00 66.01  ? 36  SER C OG  1 
ATOM   3830  N  N   . LEU C  1 46  ? -20.010 -40.797 42.134 1.00 56.21  ? 37  LEU C N   1 
ATOM   3831  C  CA  . LEU C  1 46  ? -19.072 -41.785 41.618 1.00 51.97  ? 37  LEU C CA  1 
ATOM   3832  C  C   . LEU C  1 46  ? -19.390 -42.209 40.170 1.00 58.43  ? 37  LEU C C   1 
ATOM   3833  O  O   . LEU C  1 46  ? -20.549 -42.426 39.795 1.00 54.65  ? 37  LEU C O   1 
ATOM   3834  C  CB  . LEU C  1 46  ? -19.095 -42.998 42.524 1.00 57.87  ? 37  LEU C CB  1 
ATOM   3835  C  CG  . LEU C  1 46  ? -17.761 -43.697 42.703 1.00 68.28  ? 37  LEU C CG  1 
ATOM   3836  C  CD1 . LEU C  1 46  ? -16.794 -42.712 43.335 1.00 68.14  ? 37  LEU C CD1 1 
ATOM   3837  C  CD2 . LEU C  1 46  ? -17.941 -44.950 43.561 1.00 62.21  ? 37  LEU C CD2 1 
ATOM   3838  N  N   . LEU C  1 47  ? -18.338 -42.342 39.372 1.00 55.31  ? 38  LEU C N   1 
ATOM   3839  C  CA  . LEU C  1 47  ? -18.450 -42.409 37.921 1.00 54.02  ? 38  LEU C CA  1 
ATOM   3840  C  C   . LEU C  1 47  ? -17.926 -43.718 37.331 1.00 58.02  ? 38  LEU C C   1 
ATOM   3841  O  O   . LEU C  1 47  ? -18.641 -44.433 36.610 1.00 62.04  ? 38  LEU C O   1 
ATOM   3842  C  CB  . LEU C  1 47  ? -17.738 -41.214 37.284 1.00 51.40  ? 38  LEU C CB  1 
ATOM   3843  C  CG  . LEU C  1 47  ? -18.646 -40.241 36.529 1.00 59.82  ? 38  LEU C CG  1 
ATOM   3844  C  CD1 . LEU C  1 47  ? -19.761 -39.736 37.422 1.00 58.80  ? 38  LEU C CD1 1 
ATOM   3845  C  CD2 . LEU C  1 47  ? -17.838 -39.084 35.987 1.00 63.24  ? 38  LEU C CD2 1 
ATOM   3846  N  N   . ASP C  1 48  ? -16.641 -43.966 37.540 1.00 49.22  ? 39  ASP C N   1 
ATOM   3847  C  CA  . ASP C  1 48  ? -16.041 -45.202 37.092 1.00 52.71  ? 39  ASP C CA  1 
ATOM   3848  C  C   . ASP C  1 48  ? -14.964 -45.648 38.051 1.00 51.42  ? 39  ASP C C   1 
ATOM   3849  O  O   . ASP C  1 48  ? -14.105 -44.852 38.409 1.00 52.58  ? 39  ASP C O   1 
ATOM   3850  C  CB  . ASP C  1 48  ? -15.397 -44.980 35.721 1.00 54.60  ? 39  ASP C CB  1 
ATOM   3851  C  CG  . ASP C  1 48  ? -15.359 -46.232 34.890 1.00 61.91  ? 39  ASP C CG  1 
ATOM   3852  O  OD1 . ASP C  1 48  ? -15.719 -47.295 35.427 1.00 60.02  ? 39  ASP C OD1 1 
ATOM   3853  O  OD2 . ASP C  1 48  ? -14.972 -46.162 33.705 1.00 64.55  ? 39  ASP C OD2 1 
ATOM   3854  N  N   . ILE C  1 49  ? -14.947 -46.926 38.408 1.00 50.51  ? 40  ILE C N   1 
ATOM   3855  C  CA  . ILE C  1 49  ? -13.710 -47.497 38.911 1.00 47.74  ? 40  ILE C CA  1 
ATOM   3856  C  C   . ILE C  1 49  ? -13.044 -48.062 37.657 1.00 54.85  ? 40  ILE C C   1 
ATOM   3857  O  O   . ILE C  1 49  ? -13.513 -49.029 37.051 1.00 57.80  ? 40  ILE C O   1 
ATOM   3858  C  CB  . ILE C  1 49  ? -13.959 -48.597 39.951 1.00 46.23  ? 40  ILE C CB  1 
ATOM   3859  C  CG1 . ILE C  1 49  ? -14.841 -48.059 41.072 1.00 48.36  ? 40  ILE C CG1 1 
ATOM   3860  C  CG2 . ILE C  1 49  ? -12.652 -49.098 40.522 1.00 45.09  ? 40  ILE C CG2 1 
ATOM   3861  C  CD1 . ILE C  1 49  ? -14.873 -48.927 42.299 1.00 43.43  ? 40  ILE C CD1 1 
ATOM   3862  N  N   . VAL C  1 50  ? -11.965 -47.411 37.248 1.00 53.29  ? 41  VAL C N   1 
ATOM   3863  C  CA  . VAL C  1 50  ? -11.309 -47.722 35.990 1.00 52.75  ? 41  VAL C CA  1 
ATOM   3864  C  C   . VAL C  1 50  ? -10.392 -48.935 36.058 1.00 56.54  ? 41  VAL C C   1 
ATOM   3865  O  O   . VAL C  1 50  ? -10.410 -49.794 35.175 1.00 59.43  ? 41  VAL C O   1 
ATOM   3866  C  CB  . VAL C  1 50  ? -10.526 -46.518 35.479 1.00 50.81  ? 41  VAL C CB  1 
ATOM   3867  C  CG1 . VAL C  1 50  ? -9.881  -46.848 34.150 1.00 49.78  ? 41  VAL C CG1 1 
ATOM   3868  C  CG2 . VAL C  1 50  ? -11.445 -45.306 35.377 1.00 47.51  ? 41  VAL C CG2 1 
ATOM   3869  N  N   . LYS C  1 51  ? -9.574  -48.987 37.099 1.00 55.29  ? 42  LYS C N   1 
ATOM   3870  C  CA  . LYS C  1 51  ? -8.576  -50.032 37.223 1.00 52.96  ? 42  LYS C CA  1 
ATOM   3871  C  C   . LYS C  1 51  ? -8.324  -50.395 38.677 1.00 53.77  ? 42  LYS C C   1 
ATOM   3872  O  O   . LYS C  1 51  ? -8.197  -49.515 39.522 1.00 55.55  ? 42  LYS C O   1 
ATOM   3873  C  CB  . LYS C  1 51  ? -7.273  -49.542 36.590 1.00 52.02  ? 42  LYS C CB  1 
ATOM   3874  C  CG  . LYS C  1 51  ? -6.107  -50.441 36.847 1.00 57.10  ? 42  LYS C CG  1 
ATOM   3875  C  CD  . LYS C  1 51  ? -5.053  -50.283 35.788 1.00 59.44  ? 42  LYS C CD  1 
ATOM   3876  C  CE  . LYS C  1 51  ? -4.037  -49.229 36.159 1.00 61.31  ? 42  LYS C CE  1 
ATOM   3877  N  NZ  . LYS C  1 51  ? -3.022  -49.108 35.074 1.00 79.75  ? 42  LYS C NZ  1 
ATOM   3878  N  N   . ALA C  1 52  ? -8.191  -51.687 38.968 1.00 64.83  ? 43  ALA C N   1 
ATOM   3879  C  CA  . ALA C  1 52  ? -7.790  -52.130 40.313 1.00 60.58  ? 43  ALA C CA  1 
ATOM   3880  C  C   . ALA C  1 52  ? -6.469  -52.883 40.196 1.00 62.80  ? 43  ALA C C   1 
ATOM   3881  O  O   . ALA C  1 52  ? -6.384  -53.876 39.461 1.00 68.31  ? 43  ALA C O   1 
ATOM   3882  C  CB  . ALA C  1 52  ? -8.858  -53.001 40.932 1.00 47.77  ? 43  ALA C CB  1 
ATOM   3883  N  N   . ASP C  1 53  ? -5.430  -52.400 40.875 1.00 55.58  ? 44  ASP C N   1 
ATOM   3884  C  CA  . ASP C  1 53  ? -4.099  -52.969 40.678 1.00 58.23  ? 44  ASP C CA  1 
ATOM   3885  C  C   . ASP C  1 53  ? -3.688  -53.803 41.882 1.00 64.33  ? 44  ASP C C   1 
ATOM   3886  O  O   . ASP C  1 53  ? -3.365  -53.265 42.938 1.00 61.91  ? 44  ASP C O   1 
ATOM   3887  C  CB  . ASP C  1 53  ? -3.070  -51.865 40.410 1.00 56.87  ? 44  ASP C CB  1 
ATOM   3888  C  CG  . ASP C  1 53  ? -1.862  -52.359 39.617 1.00 58.29  ? 44  ASP C CG  1 
ATOM   3889  O  OD1 . ASP C  1 53  ? -1.492  -53.537 39.769 1.00 57.87  ? 44  ASP C OD1 1 
ATOM   3890  O  OD2 . ASP C  1 53  ? -1.277  -51.571 38.838 1.00 58.03  ? 44  ASP C OD2 1 
ATOM   3891  N  N   . SER C  1 54  ? -3.668  -55.121 41.695 1.00 61.72  ? 45  SER C N   1 
ATOM   3892  C  CA  . SER C  1 54  ? -3.407  -56.052 42.782 1.00 57.86  ? 45  SER C CA  1 
ATOM   3893  C  C   . SER C  1 54  ? -1.921  -56.332 42.962 1.00 60.05  ? 45  SER C C   1 
ATOM   3894  O  O   . SER C  1 54  ? -1.528  -56.961 43.934 1.00 64.45  ? 45  SER C O   1 
ATOM   3895  C  CB  . SER C  1 54  ? -4.195  -57.352 42.591 1.00 58.75  ? 45  SER C CB  1 
ATOM   3896  O  OG  . SER C  1 54  ? -4.093  -57.835 41.259 1.00 73.22  ? 45  SER C OG  1 
ATOM   3897  N  N   . SER C  1 55  ? -1.100  -55.876 42.023 1.00 60.17  ? 46  SER C N   1 
ATOM   3898  C  CA  . SER C  1 55  ? 0.351   -55.916 42.193 1.00 62.88  ? 46  SER C CA  1 
ATOM   3899  C  C   . SER C  1 55  ? 0.889   -54.789 43.073 1.00 64.61  ? 46  SER C C   1 
ATOM   3900  O  O   . SER C  1 55  ? 1.776   -54.995 43.899 1.00 69.31  ? 46  SER C O   1 
ATOM   3901  C  CB  . SER C  1 55  ? 1.049   -55.882 40.841 1.00 62.31  ? 46  SER C CB  1 
ATOM   3902  O  OG  . SER C  1 55  ? 0.519   -54.852 40.033 1.00 57.59  ? 46  SER C OG  1 
ATOM   3903  N  N   . THR C  1 56  ? 0.415   -53.576 42.824 1.00 63.56  ? 47  THR C N   1 
ATOM   3904  C  CA  . THR C  1 56  ? 0.784   -52.422 43.638 1.00 64.20  ? 47  THR C CA  1 
ATOM   3905  C  C   . THR C  1 56  ? -0.247  -51.997 44.698 1.00 58.64  ? 47  THR C C   1 
ATOM   3906  O  O   . THR C  1 56  ? -0.029  -51.033 45.418 1.00 62.21  ? 47  THR C O   1 
ATOM   3907  C  CB  . THR C  1 56  ? 1.172   -51.232 42.734 1.00 67.05  ? 47  THR C CB  1 
ATOM   3908  O  OG1 . THR C  1 56  ? 0.072   -50.917 41.874 1.00 66.55  ? 47  THR C OG1 1 
ATOM   3909  C  CG2 . THR C  1 56  ? 2.391   -51.587 41.868 1.00 60.63  ? 47  THR C CG2 1 
ATOM   3910  N  N   . ASN C  1 57  ? -1.378  -52.689 44.766 1.00 58.07  ? 48  ASN C N   1 
ATOM   3911  C  CA  . ASN C  1 57  ? -2.496  -52.276 45.628 1.00 55.55  ? 48  ASN C CA  1 
ATOM   3912  C  C   . ASN C  1 57  ? -2.879  -50.801 45.524 1.00 56.52  ? 48  ASN C C   1 
ATOM   3913  O  O   . ASN C  1 57  ? -3.037  -50.135 46.540 1.00 55.23  ? 48  ASN C O   1 
ATOM   3914  C  CB  . ASN C  1 57  ? -2.241  -52.597 47.102 1.00 57.80  ? 48  ASN C CB  1 
ATOM   3915  C  CG  . ASN C  1 57  ? -2.470  -54.064 47.453 1.00 62.38  ? 48  ASN C CG  1 
ATOM   3916  O  OD1 . ASN C  1 57  ? -3.047  -54.833 46.678 1.00 63.13  ? 48  ASN C OD1 1 
ATOM   3917  N  ND2 . ASN C  1 57  ? -2.019  -54.452 48.645 1.00 54.93  ? 48  ASN C ND2 1 
ATOM   3918  N  N   . GLU C  1 58  ? -3.017  -50.295 44.300 1.00 61.93  ? 49  GLU C N   1 
ATOM   3919  C  CA  . GLU C  1 58  ? -3.566  -48.959 44.054 1.00 58.44  ? 49  GLU C CA  1 
ATOM   3920  C  C   . GLU C  1 58  ? -4.819  -49.139 43.212 1.00 55.30  ? 49  GLU C C   1 
ATOM   3921  O  O   . GLU C  1 58  ? -4.860  -50.034 42.384 1.00 56.63  ? 49  GLU C O   1 
ATOM   3922  C  CB  . GLU C  1 58  ? -2.592  -48.081 43.257 1.00 60.95  ? 49  GLU C CB  1 
ATOM   3923  C  CG  . GLU C  1 58  ? -1.099  -48.326 43.464 1.00 61.20  ? 49  GLU C CG  1 
ATOM   3924  C  CD  . GLU C  1 58  ? -0.246  -47.388 42.608 1.00 61.41  ? 49  GLU C CD  1 
ATOM   3925  O  OE1 . GLU C  1 58  ? 0.361   -47.842 41.608 1.00 58.50  ? 49  GLU C OE1 1 
ATOM   3926  O  OE2 . GLU C  1 58  ? -0.186  -46.185 42.936 1.00 56.44  ? 49  GLU C OE2 1 
ATOM   3927  N  N   . VAL C  1 59  ? -5.829  -48.293 43.410 1.00 54.82  ? 50  VAL C N   1 
ATOM   3928  C  CA  . VAL C  1 59  ? -7.011  -48.284 42.540 1.00 53.49  ? 50  VAL C CA  1 
ATOM   3929  C  C   . VAL C  1 59  ? -7.167  -46.939 41.825 1.00 53.35  ? 50  VAL C C   1 
ATOM   3930  O  O   . VAL C  1 59  ? -6.781  -45.909 42.351 1.00 50.97  ? 50  VAL C O   1 
ATOM   3931  C  CB  . VAL C  1 59  ? -8.304  -48.631 43.316 1.00 53.13  ? 50  VAL C CB  1 
ATOM   3932  C  CG1 . VAL C  1 59  ? -9.537  -48.255 42.517 1.00 45.57  ? 50  VAL C CG1 1 
ATOM   3933  C  CG2 . VAL C  1 59  ? -8.333  -50.109 43.648 1.00 59.86  ? 50  VAL C CG2 1 
ATOM   3934  N  N   . ASP C  1 60  ? -7.715  -46.962 40.612 1.00 57.51  ? 51  ASP C N   1 
ATOM   3935  C  CA  . ASP C  1 60  ? -7.971  -45.740 39.836 1.00 56.62  ? 51  ASP C CA  1 
ATOM   3936  C  C   . ASP C  1 60  ? -9.464  -45.435 39.749 1.00 53.25  ? 51  ASP C C   1 
ATOM   3937  O  O   . ASP C  1 60  ? -10.259 -46.263 39.324 1.00 54.77  ? 51  ASP C O   1 
ATOM   3938  C  CB  . ASP C  1 60  ? -7.338  -45.823 38.443 1.00 52.46  ? 51  ASP C CB  1 
ATOM   3939  C  CG  . ASP C  1 60  ? -5.816  -45.880 38.501 1.00 60.82  ? 51  ASP C CG  1 
ATOM   3940  O  OD1 . ASP C  1 60  ? -5.267  -46.099 39.611 1.00 50.19  ? 51  ASP C OD1 1 
ATOM   3941  O  OD2 . ASP C  1 60  ? -5.168  -45.718 37.437 1.00 62.62  ? 51  ASP C OD2 1 
ATOM   3942  N  N   . LEU C  1 61  ? -9.837  -44.258 40.192 1.00 52.14  ? 52  LEU C N   1 
ATOM   3943  C  CA  . LEU C  1 61  ? -11.219 -43.885 40.312 1.00 52.93  ? 52  LEU C CA  1 
ATOM   3944  C  C   . LEU C  1 61  ? -11.540 -42.600 39.608 1.00 52.92  ? 52  LEU C C   1 
ATOM   3945  O  O   . LEU C  1 61  ? -10.746 -41.711 39.585 1.00 51.99  ? 52  LEU C O   1 
ATOM   3946  C  CB  . LEU C  1 61  ? -11.481 -43.653 41.774 1.00 52.76  ? 52  LEU C CB  1 
ATOM   3947  C  CG  . LEU C  1 61  ? -12.790 -43.180 42.361 1.00 64.77  ? 52  LEU C CG  1 
ATOM   3948  C  CD1 . LEU C  1 61  ? -13.779 -44.218 42.059 1.00 60.51  ? 52  LEU C CD1 1 
ATOM   3949  C  CD2 . LEU C  1 61  ? -12.725 -43.002 43.804 1.00 54.16  ? 52  LEU C CD2 1 
ATOM   3950  N  N   . VAL C  1 62  ? -12.725 -42.504 39.044 1.00 50.87  ? 53  VAL C N   1 
ATOM   3951  C  CA  . VAL C  1 62  ? -13.177 -41.264 38.429 1.00 52.74  ? 53  VAL C CA  1 
ATOM   3952  C  C   . VAL C  1 62  ? -14.427 -40.795 39.149 1.00 50.42  ? 53  VAL C C   1 
ATOM   3953  O  O   . VAL C  1 62  ? -15.356 -41.567 39.331 1.00 56.03  ? 53  VAL C O   1 
ATOM   3954  C  CB  . VAL C  1 62  ? -13.479 -41.427 36.910 1.00 48.28  ? 53  VAL C CB  1 
ATOM   3955  C  CG1 . VAL C  1 62  ? -14.183 -40.216 36.400 1.00 44.72  ? 53  VAL C CG1 1 
ATOM   3956  C  CG2 . VAL C  1 62  ? -12.202 -41.672 36.122 1.00 44.43  ? 53  VAL C CG2 1 
ATOM   3957  N  N   . TYR C  1 63  ? -14.443 -39.542 39.588 1.00 47.35  ? 54  TYR C N   1 
ATOM   3958  C  CA  . TYR C  1 63  ? -15.639 -39.008 40.224 1.00 52.57  ? 54  TYR C CA  1 
ATOM   3959  C  C   . TYR C  1 63  ? -15.776 -37.512 40.043 1.00 53.31  ? 54  TYR C C   1 
ATOM   3960  O  O   . TYR C  1 63  ? -14.846 -36.833 39.607 1.00 51.73  ? 54  TYR C O   1 
ATOM   3961  C  CB  . TYR C  1 63  ? -15.573 -39.281 41.732 1.00 58.87  ? 54  TYR C CB  1 
ATOM   3962  C  CG  . TYR C  1 63  ? -14.289 -38.768 42.346 1.00 51.05  ? 54  TYR C CG  1 
ATOM   3963  C  CD1 . TYR C  1 63  ? -14.252 -37.578 43.045 1.00 46.88  ? 54  TYR C CD1 1 
ATOM   3964  C  CD2 . TYR C  1 63  ? -13.110 -39.467 42.182 1.00 52.81  ? 54  TYR C CD2 1 
ATOM   3965  C  CE1 . TYR C  1 63  ? -13.079 -37.117 43.569 1.00 53.00  ? 54  TYR C CE1 1 
ATOM   3966  C  CE2 . TYR C  1 63  ? -11.942 -39.019 42.690 1.00 51.94  ? 54  TYR C CE2 1 
ATOM   3967  C  CZ  . TYR C  1 63  ? -11.921 -37.850 43.385 1.00 55.69  ? 54  TYR C CZ  1 
ATOM   3968  O  OH  . TYR C  1 63  ? -10.716 -37.424 43.898 1.00 60.16  ? 54  TYR C OH  1 
ATOM   3969  N  N   . TRP C  1 64  ? -16.920 -37.007 40.493 1.00 51.30  ? 55  TRP C N   1 
ATOM   3970  C  CA  . TRP C  1 64  ? -17.158 -35.586 40.606 1.00 55.61  ? 55  TRP C CA  1 
ATOM   3971  C  C   . TRP C  1 64  ? -17.164 -35.345 42.097 1.00 54.59  ? 55  TRP C C   1 
ATOM   3972  O  O   . TRP C  1 64  ? -17.677 -36.160 42.856 1.00 52.13  ? 55  TRP C O   1 
ATOM   3973  C  CB  . TRP C  1 64  ? -18.508 -35.172 40.002 1.00 57.65  ? 55  TRP C CB  1 
ATOM   3974  C  CG  . TRP C  1 64  ? -18.666 -35.475 38.527 1.00 65.44  ? 55  TRP C CG  1 
ATOM   3975  C  CD1 . TRP C  1 64  ? -17.682 -35.511 37.569 1.00 62.42  ? 55  TRP C CD1 1 
ATOM   3976  C  CD2 . TRP C  1 64  ? -19.885 -35.795 37.856 1.00 66.17  ? 55  TRP C CD2 1 
ATOM   3977  N  NE1 . TRP C  1 64  ? -18.222 -35.830 36.350 1.00 62.96  ? 55  TRP C NE1 1 
ATOM   3978  C  CE2 . TRP C  1 64  ? -19.570 -36.015 36.500 1.00 66.81  ? 55  TRP C CE2 1 
ATOM   3979  C  CE3 . TRP C  1 64  ? -21.211 -35.919 38.271 1.00 66.42  ? 55  TRP C CE3 1 
ATOM   3980  C  CZ2 . TRP C  1 64  ? -20.535 -36.360 35.565 1.00 72.08  ? 55  TRP C CZ2 1 
ATOM   3981  C  CZ3 . TRP C  1 64  ? -22.163 -36.255 37.339 1.00 70.62  ? 55  TRP C CZ3 1 
ATOM   3982  C  CH2 . TRP C  1 64  ? -21.823 -36.473 36.003 1.00 72.43  ? 55  TRP C CH2 1 
ATOM   3983  N  N   . GLU C  1 65  ? -16.565 -34.235 42.506 1.00 52.55  ? 56  GLU C N   1 
ATOM   3984  C  CA  . GLU C  1 65  ? -16.495 -33.847 43.893 1.00 48.40  ? 56  GLU C CA  1 
ATOM   3985  C  C   . GLU C  1 65  ? -17.116 -32.479 43.949 1.00 53.32  ? 56  GLU C C   1 
ATOM   3986  O  O   . GLU C  1 65  ? -16.596 -31.542 43.371 1.00 55.84  ? 56  GLU C O   1 
ATOM   3987  C  CB  . GLU C  1 65  ? -15.034 -33.801 44.321 1.00 54.02  ? 56  GLU C CB  1 
ATOM   3988  C  CG  . GLU C  1 65  ? -14.745 -33.109 45.625 1.00 54.32  ? 56  GLU C CG  1 
ATOM   3989  C  CD  . GLU C  1 65  ? -13.303 -33.306 46.050 1.00 59.56  ? 56  GLU C CD  1 
ATOM   3990  O  OE1 . GLU C  1 65  ? -12.556 -33.986 45.315 1.00 53.35  ? 56  GLU C OE1 1 
ATOM   3991  O  OE2 . GLU C  1 65  ? -12.911 -32.796 47.120 1.00 63.48  ? 56  GLU C OE2 1 
ATOM   3992  N  N   . GLN C  1 66  ? -18.250 -32.369 44.622 1.00 56.40  ? 57  GLN C N   1 
ATOM   3993  C  CA  . GLN C  1 66  ? -18.932 -31.094 44.765 1.00 55.41  ? 57  GLN C CA  1 
ATOM   3994  C  C   . GLN C  1 66  ? -18.420 -30.407 46.023 1.00 54.00  ? 57  GLN C C   1 
ATOM   3995  O  O   . GLN C  1 66  ? -18.386 -30.999 47.098 1.00 56.50  ? 57  GLN C O   1 
ATOM   3996  C  CB  . GLN C  1 66  ? -20.443 -31.311 44.839 1.00 55.88  ? 57  GLN C CB  1 
ATOM   3997  C  CG  . GLN C  1 66  ? -21.274 -30.066 44.614 1.00 62.24  ? 57  GLN C CG  1 
ATOM   3998  C  CD  . GLN C  1 66  ? -22.574 -30.104 45.389 1.00 74.05  ? 57  GLN C CD  1 
ATOM   3999  O  OE1 . GLN C  1 66  ? -22.565 -30.280 46.613 1.00 84.38  ? 57  GLN C OE1 1 
ATOM   4000  N  NE2 . GLN C  1 66  ? -23.700 -29.947 44.691 1.00 57.08  ? 57  GLN C NE2 1 
ATOM   4001  N  N   . GLN C  1 67  ? -17.992 -29.161 45.879 1.00 56.34  ? 58  GLN C N   1 
ATOM   4002  C  CA  . GLN C  1 67  ? -17.495 -28.389 47.006 1.00 50.95  ? 58  GLN C CA  1 
ATOM   4003  C  C   . GLN C  1 67  ? -18.286 -27.115 47.113 1.00 52.43  ? 58  GLN C C   1 
ATOM   4004  O  O   . GLN C  1 67  ? -18.509 -26.447 46.126 1.00 58.58  ? 58  GLN C O   1 
ATOM   4005  C  CB  . GLN C  1 67  ? -16.029 -28.040 46.804 1.00 47.60  ? 58  GLN C CB  1 
ATOM   4006  C  CG  . GLN C  1 67  ? -15.141 -29.243 46.689 1.00 57.90  ? 58  GLN C CG  1 
ATOM   4007  C  CD  . GLN C  1 67  ? -13.687 -28.884 46.808 1.00 66.72  ? 58  GLN C CD  1 
ATOM   4008  O  OE1 . GLN C  1 67  ? -13.334 -27.706 46.818 1.00 72.30  ? 58  GLN C OE1 1 
ATOM   4009  N  NE2 . GLN C  1 67  ? -12.829 -29.891 46.909 1.00 64.77  ? 58  GLN C NE2 1 
ATOM   4010  N  N   . SER C  1 68  ? -18.733 -26.765 48.301 1.00 54.60  ? 59  SER C N   1 
ATOM   4011  C  CA  . SER C  1 68  ? -19.343 -25.457 48.456 1.00 54.62  ? 59  SER C CA  1 
ATOM   4012  C  C   . SER C  1 68  ? -19.025 -24.813 49.794 1.00 54.06  ? 59  SER C C   1 
ATOM   4013  O  O   . SER C  1 68  ? -18.845 -25.469 50.813 1.00 56.58  ? 59  SER C O   1 
ATOM   4014  C  CB  . SER C  1 68  ? -20.854 -25.497 48.195 1.00 53.40  ? 59  SER C CB  1 
ATOM   4015  O  OG  . SER C  1 68  ? -21.469 -26.566 48.886 1.00 61.37  ? 59  SER C OG  1 
ATOM   4016  N  N   . TRP C  1 69  ? -18.937 -23.501 49.768 1.00 53.20  ? 60  TRP C N   1 
ATOM   4017  C  CA  . TRP C  1 69  ? -18.764 -22.755 50.972 1.00 52.98  ? 60  TRP C CA  1 
ATOM   4018  C  C   . TRP C  1 69  ? -19.448 -21.441 50.765 1.00 56.44  ? 60  TRP C C   1 
ATOM   4019  O  O   . TRP C  1 69  ? -20.023 -21.207 49.709 1.00 55.22  ? 60  TRP C O   1 
ATOM   4020  C  CB  . TRP C  1 69  ? -17.287 -22.571 51.277 1.00 55.21  ? 60  TRP C CB  1 
ATOM   4021  C  CG  . TRP C  1 69  ? -16.512 -21.959 50.205 1.00 48.15  ? 60  TRP C CG  1 
ATOM   4022  C  CD1 . TRP C  1 69  ? -16.117 -20.669 50.128 1.00 52.38  ? 60  TRP C CD1 1 
ATOM   4023  C  CD2 . TRP C  1 69  ? -15.996 -22.611 49.047 1.00 51.97  ? 60  TRP C CD2 1 
ATOM   4024  N  NE1 . TRP C  1 69  ? -15.389 -20.463 48.989 1.00 54.57  ? 60  TRP C NE1 1 
ATOM   4025  C  CE2 . TRP C  1 69  ? -15.302 -21.642 48.305 1.00 48.79  ? 60  TRP C CE2 1 
ATOM   4026  C  CE3 . TRP C  1 69  ? -16.067 -23.915 48.558 1.00 56.02  ? 60  TRP C CE3 1 
ATOM   4027  C  CZ2 . TRP C  1 69  ? -14.675 -21.938 47.103 1.00 48.31  ? 60  TRP C CZ2 1 
ATOM   4028  C  CZ3 . TRP C  1 69  ? -15.448 -24.204 47.361 1.00 53.43  ? 60  TRP C CZ3 1 
ATOM   4029  C  CH2 . TRP C  1 69  ? -14.763 -23.219 46.645 1.00 49.16  ? 60  TRP C CH2 1 
ATOM   4030  N  N   . LYS C  1 70  ? -19.416 -20.593 51.781 1.00 61.75  ? 61  LYS C N   1 
ATOM   4031  C  CA  . LYS C  1 70  ? -20.007 -19.274 51.654 1.00 66.42  ? 61  LYS C CA  1 
ATOM   4032  C  C   . LYS C  1 70  ? -19.037 -18.231 52.174 1.00 64.23  ? 61  LYS C C   1 
ATOM   4033  O  O   . LYS C  1 70  ? -18.378 -18.433 53.195 1.00 68.69  ? 61  LYS C O   1 
ATOM   4034  C  CB  . LYS C  1 70  ? -21.334 -19.221 52.407 1.00 68.82  ? 61  LYS C CB  1 
ATOM   4035  C  CG  . LYS C  1 70  ? -22.074 -17.900 52.338 1.00 71.23  ? 61  LYS C CG  1 
ATOM   4036  C  CD  . LYS C  1 70  ? -23.456 -18.049 52.978 1.00 84.19  ? 61  LYS C CD  1 
ATOM   4037  C  CE  . LYS C  1 70  ? -24.215 -16.733 53.046 1.00 86.66  ? 61  LYS C CE  1 
ATOM   4038  N  NZ  . LYS C  1 70  ? -25.698 -16.932 52.973 1.00 77.46  ? 61  LYS C NZ  1 
ATOM   4039  N  N   . LEU C  1 71  ? -18.925 -17.127 51.455 1.00 58.88  ? 62  LEU C N   1 
ATOM   4040  C  CA  . LEU C  1 71  ? -18.119 -16.013 51.924 1.00 61.25  ? 62  LEU C CA  1 
ATOM   4041  C  C   . LEU C  1 71  ? -18.982 -14.763 51.936 1.00 67.43  ? 62  LEU C C   1 
ATOM   4042  O  O   . LEU C  1 71  ? -19.668 -14.465 50.954 1.00 71.19  ? 62  LEU C O   1 
ATOM   4043  C  CB  . LEU C  1 71  ? -16.904 -15.797 51.021 1.00 65.85  ? 62  LEU C CB  1 
ATOM   4044  C  CG  . LEU C  1 71  ? -15.923 -16.946 50.804 1.00 64.68  ? 62  LEU C CG  1 
ATOM   4045  C  CD1 . LEU C  1 71  ? -14.714 -16.461 50.016 1.00 61.15  ? 62  LEU C CD1 1 
ATOM   4046  C  CD2 . LEU C  1 71  ? -15.495 -17.560 52.124 1.00 56.60  ? 62  LEU C CD2 1 
ATOM   4047  N  N   . ASN C  1 72  ? -18.963 -14.034 53.045 1.00 66.81  ? 63  ASN C N   1 
ATOM   4048  C  CA  . ASN C  1 72  ? -19.678 -12.766 53.092 1.00 70.87  ? 63  ASN C CA  1 
ATOM   4049  C  C   . ASN C  1 72  ? -19.112 -11.822 52.032 1.00 66.49  ? 63  ASN C C   1 
ATOM   4050  O  O   . ASN C  1 72  ? -19.857 -11.081 51.387 1.00 70.12  ? 63  ASN C O   1 
ATOM   4051  C  CB  . ASN C  1 72  ? -19.616 -12.153 54.496 1.00 68.18  ? 63  ASN C CB  1 
ATOM   4052  C  CG  . ASN C  1 72  ? -20.343 -12.997 55.521 1.00 80.09  ? 63  ASN C CG  1 
ATOM   4053  O  OD1 . ASN C  1 72  ? -21.470 -13.443 55.283 1.00 80.12  ? 63  ASN C OD1 1 
ATOM   4054  N  ND2 . ASN C  1 72  ? -19.693 -13.253 56.653 1.00 77.46  ? 63  ASN C ND2 1 
ATOM   4055  N  N   . SER C  1 73  ? -17.795 -11.883 51.833 1.00 65.91  ? 64  SER C N   1 
ATOM   4056  C  CA  . SER C  1 73  ? -17.114 -10.983 50.902 1.00 59.59  ? 64  SER C CA  1 
ATOM   4057  C  C   . SER C  1 73  ? -17.537 -11.157 49.465 1.00 65.74  ? 64  SER C C   1 
ATOM   4058  O  O   . SER C  1 73  ? -17.242 -10.300 48.640 1.00 76.67  ? 64  SER C O   1 
ATOM   4059  C  CB  . SER C  1 73  ? -15.585 -11.069 51.015 1.00 57.20  ? 64  SER C CB  1 
ATOM   4060  O  OG  . SER C  1 73  ? -15.128 -12.385 51.229 1.00 60.83  ? 64  SER C OG  1 
ATOM   4061  N  N   . LEU C  1 74  ? -18.224 -12.262 49.179 1.00 69.33  ? 65  LEU C N   1 
ATOM   4062  C  CA  . LEU C  1 74  ? -18.755 -12.576 47.850 1.00 61.54  ? 65  LEU C CA  1 
ATOM   4063  C  C   . LEU C  1 74  ? -20.227 -12.209 47.601 1.00 63.31  ? 65  LEU C C   1 
ATOM   4064  O  O   . LEU C  1 74  ? -20.758 -12.501 46.537 1.00 69.27  ? 65  LEU C O   1 
ATOM   4065  C  CB  . LEU C  1 74  ? -18.574 -14.060 47.576 1.00 62.01  ? 65  LEU C CB  1 
ATOM   4066  C  CG  . LEU C  1 74  ? -17.145 -14.529 47.338 1.00 63.22  ? 65  LEU C CG  1 
ATOM   4067  C  CD1 . LEU C  1 74  ? -17.152 -15.888 46.700 1.00 57.18  ? 65  LEU C CD1 1 
ATOM   4068  C  CD2 . LEU C  1 74  ? -16.440 -13.545 46.441 1.00 60.80  ? 65  LEU C CD2 1 
ATOM   4069  N  N   . MET C  1 75  ? -20.894 -11.602 48.578 1.00 69.01  ? 66  MET C N   1 
ATOM   4070  C  CA  . MET C  1 75  ? -22.279 -11.154 48.403 1.00 67.17  ? 66  MET C CA  1 
ATOM   4071  C  C   . MET C  1 75  ? -22.421 -9.870  47.591 1.00 73.77  ? 66  MET C C   1 
ATOM   4072  O  O   . MET C  1 75  ? -21.481 -9.071  47.457 1.00 73.22  ? 66  MET C O   1 
ATOM   4073  C  CB  . MET C  1 75  ? -22.959 -10.935 49.744 1.00 63.81  ? 66  MET C CB  1 
ATOM   4074  C  CG  . MET C  1 75  ? -22.743 -12.052 50.724 1.00 69.79  ? 66  MET C CG  1 
ATOM   4075  S  SD  . MET C  1 75  ? -23.580 -11.744 52.282 1.00 84.77  ? 66  MET C SD  1 
ATOM   4076  C  CE  . MET C  1 75  ? -25.309 -12.006 51.816 1.00 70.02  ? 66  MET C CE  1 
ATOM   4077  N  N   . TRP C  1 76  ? -23.610 -9.694  47.029 1.00 67.59  ? 67  TRP C N   1 
ATOM   4078  C  CA  . TRP C  1 76  ? -24.001 -8.425  46.453 1.00 69.46  ? 67  TRP C CA  1 
ATOM   4079  C  C   . TRP C  1 76  ? -25.519 -8.338  46.382 1.00 76.38  ? 67  TRP C C   1 
ATOM   4080  O  O   . TRP C  1 76  ? -26.218 -9.348  46.491 1.00 74.03  ? 67  TRP C O   1 
ATOM   4081  C  CB  . TRP C  1 76  ? -23.405 -8.261  45.069 1.00 70.84  ? 67  TRP C CB  1 
ATOM   4082  C  CG  . TRP C  1 76  ? -24.030 -9.153  44.046 1.00 68.10  ? 67  TRP C CG  1 
ATOM   4083  C  CD1 . TRP C  1 76  ? -25.111 -8.873  43.273 1.00 66.57  ? 67  TRP C CD1 1 
ATOM   4084  C  CD2 . TRP C  1 76  ? -23.610 -10.475 43.689 1.00 70.59  ? 67  TRP C CD2 1 
ATOM   4085  N  NE1 . TRP C  1 76  ? -25.390 -9.933  42.448 1.00 70.85  ? 67  TRP C NE1 1 
ATOM   4086  C  CE2 . TRP C  1 76  ? -24.482 -10.928 42.683 1.00 63.56  ? 67  TRP C CE2 1 
ATOM   4087  C  CE3 . TRP C  1 76  ? -22.578 -11.315 44.119 1.00 68.44  ? 67  TRP C CE3 1 
ATOM   4088  C  CZ2 . TRP C  1 76  ? -24.355 -12.177 42.101 1.00 62.24  ? 67  TRP C CZ2 1 
ATOM   4089  C  CZ3 . TRP C  1 76  ? -22.458 -12.552 43.543 1.00 62.40  ? 67  TRP C CZ3 1 
ATOM   4090  C  CH2 . TRP C  1 76  ? -23.340 -12.973 42.543 1.00 65.86  ? 67  TRP C CH2 1 
ATOM   4091  N  N   . ASP C  1 77  ? -26.020 -7.119  46.212 1.00 78.30  ? 68  ASP C N   1 
ATOM   4092  C  CA  . ASP C  1 77  ? -27.440 -6.885  46.020 1.00 78.06  ? 68  ASP C CA  1 
ATOM   4093  C  C   . ASP C  1 77  ? -27.695 -6.946  44.518 1.00 74.53  ? 68  ASP C C   1 
ATOM   4094  O  O   . ASP C  1 77  ? -27.173 -6.129  43.765 1.00 78.55  ? 68  ASP C O   1 
ATOM   4095  C  CB  . ASP C  1 77  ? -27.811 -5.511  46.588 1.00 86.90  ? 68  ASP C CB  1 
ATOM   4096  C  CG  . ASP C  1 77  ? -29.302 -5.348  46.835 1.00 92.67  ? 68  ASP C CG  1 
ATOM   4097  O  OD1 . ASP C  1 77  ? -30.106 -5.938  46.078 1.00 87.97  ? 68  ASP C OD1 1 
ATOM   4098  O  OD2 . ASP C  1 77  ? -29.664 -4.613  47.785 1.00 92.12  ? 68  ASP C OD2 1 
ATOM   4099  N  N   . PRO C  1 78  ? -28.462 -7.944  44.070 1.00 70.84  ? 69  PRO C N   1 
ATOM   4100  C  CA  . PRO C  1 78  ? -28.776 -8.052  42.649 1.00 69.50  ? 69  PRO C CA  1 
ATOM   4101  C  C   . PRO C  1 78  ? -29.422 -6.787  42.080 1.00 79.19  ? 69  PRO C C   1 
ATOM   4102  O  O   . PRO C  1 78  ? -29.341 -6.598  40.874 1.00 75.64  ? 69  PRO C O   1 
ATOM   4103  C  CB  . PRO C  1 78  ? -29.759 -9.220  42.608 1.00 72.56  ? 69  PRO C CB  1 
ATOM   4104  C  CG  . PRO C  1 78  ? -29.354 -10.079 43.726 1.00 71.46  ? 69  PRO C CG  1 
ATOM   4105  C  CD  . PRO C  1 78  ? -28.885 -9.142  44.812 1.00 77.39  ? 69  PRO C CD  1 
ATOM   4106  N  N   . ASN C  1 79  ? -30.036 -5.941  42.910 1.00 84.07  ? 70  ASN C N   1 
ATOM   4107  C  CA  . ASN C  1 79  ? -30.657 -4.702  42.414 1.00 82.91  ? 70  ASN C CA  1 
ATOM   4108  C  C   . ASN C  1 79  ? -29.650 -3.703  41.854 1.00 75.94  ? 70  ASN C C   1 
ATOM   4109  O  O   . ASN C  1 79  ? -29.894 -3.046  40.844 1.00 72.31  ? 70  ASN C O   1 
ATOM   4110  C  CB  . ASN C  1 79  ? -31.491 -4.022  43.501 1.00 84.66  ? 70  ASN C CB  1 
ATOM   4111  C  CG  . ASN C  1 79  ? -32.707 -4.832  43.897 1.00 93.54  ? 70  ASN C CG  1 
ATOM   4112  O  OD1 . ASN C  1 79  ? -33.331 -4.580  44.933 1.00 95.45  ? 70  ASN C OD1 1 
ATOM   4113  N  ND2 . ASN C  1 79  ? -33.052 -5.820  43.071 1.00 81.52  ? 70  ASN C ND2 1 
ATOM   4114  N  N   . GLU C  1 80  ? -28.507 -3.596  42.523 1.00 75.93  ? 71  GLU C N   1 
ATOM   4115  C  CA  . GLU C  1 80  ? -27.496 -2.610  42.162 1.00 77.47  ? 71  GLU C CA  1 
ATOM   4116  C  C   . GLU C  1 80  ? -26.772 -3.006  40.880 1.00 71.92  ? 71  GLU C C   1 
ATOM   4117  O  O   . GLU C  1 80  ? -25.875 -2.300  40.419 1.00 68.52  ? 71  GLU C O   1 
ATOM   4118  C  CB  . GLU C  1 80  ? -26.490 -2.432  43.300 1.00 82.70  ? 71  GLU C CB  1 
ATOM   4119  C  CG  . GLU C  1 80  ? -27.126 -2.246  44.668 1.00 86.21  ? 71  GLU C CG  1 
ATOM   4120  C  CD  . GLU C  1 80  ? -26.106 -1.942  45.747 1.00 93.79  ? 71  GLU C CD  1 
ATOM   4121  O  OE1 . GLU C  1 80  ? -26.510 -1.764  46.916 1.00 94.18  ? 71  GLU C OE1 1 
ATOM   4122  O  OE2 . GLU C  1 80  ? -24.900 -1.882  45.428 1.00 88.04  ? 71  GLU C OE2 1 
ATOM   4123  N  N   . TYR C  1 81  ? -27.167 -4.139  40.308 1.00 76.40  ? 72  TYR C N   1 
ATOM   4124  C  CA  . TYR C  1 81  ? -26.284 -4.903  39.434 1.00 73.35  ? 72  TYR C CA  1 
ATOM   4125  C  C   . TYR C  1 81  ? -27.071 -5.619  38.341 1.00 72.94  ? 72  TYR C C   1 
ATOM   4126  O  O   . TYR C  1 81  ? -26.612 -6.617  37.786 1.00 74.07  ? 72  TYR C O   1 
ATOM   4127  C  CB  . TYR C  1 81  ? -25.471 -5.914  40.245 1.00 65.72  ? 72  TYR C CB  1 
ATOM   4128  C  CG  . TYR C  1 81  ? -24.202 -5.344  40.838 1.00 67.69  ? 72  TYR C CG  1 
ATOM   4129  C  CD1 . TYR C  1 81  ? -23.155 -4.936  40.023 1.00 61.97  ? 72  TYR C CD1 1 
ATOM   4130  C  CD2 . TYR C  1 81  ? -24.051 -5.215  42.212 1.00 71.56  ? 72  TYR C CD2 1 
ATOM   4131  C  CE1 . TYR C  1 81  ? -21.994 -4.415  40.560 1.00 72.78  ? 72  TYR C CE1 1 
ATOM   4132  C  CE2 . TYR C  1 81  ? -22.893 -4.695  42.758 1.00 71.41  ? 72  TYR C CE2 1 
ATOM   4133  C  CZ  . TYR C  1 81  ? -21.868 -4.296  41.927 1.00 72.98  ? 72  TYR C CZ  1 
ATOM   4134  O  OH  . TYR C  1 81  ? -20.713 -3.778  42.466 1.00 62.08  ? 72  TYR C OH  1 
ATOM   4135  N  N   . GLY C  1 82  ? -28.257 -5.103  38.037 1.00 73.56  ? 73  GLY C N   1 
ATOM   4136  C  CA  . GLY C  1 82  ? -29.031 -5.585  36.909 1.00 62.62  ? 73  GLY C CA  1 
ATOM   4137  C  C   . GLY C  1 82  ? -29.822 -6.836  37.241 1.00 65.19  ? 73  GLY C C   1 
ATOM   4138  O  O   . GLY C  1 82  ? -30.244 -7.570  36.348 1.00 57.35  ? 73  GLY C O   1 
ATOM   4139  N  N   . ASN C  1 83  ? -30.022 -7.077  38.532 1.00 72.53  ? 74  ASN C N   1 
ATOM   4140  C  CA  . ASN C  1 83  ? -30.565 -8.345  38.999 1.00 75.01  ? 74  ASN C CA  1 
ATOM   4141  C  C   . ASN C  1 83  ? -29.779 -9.566  38.509 1.00 73.80  ? 74  ASN C C   1 
ATOM   4142  O  O   . ASN C  1 83  ? -30.379 -10.586 38.191 1.00 79.78  ? 74  ASN C O   1 
ATOM   4143  C  CB  . ASN C  1 83  ? -32.049 -8.490  38.653 1.00 84.25  ? 74  ASN C CB  1 
ATOM   4144  C  CG  . ASN C  1 83  ? -32.911 -7.427  39.315 1.00 91.60  ? 74  ASN C CG  1 
ATOM   4145  O  OD1 . ASN C  1 83  ? -33.308 -7.576  40.474 1.00 83.76  ? 74  ASN C OD1 1 
ATOM   4146  N  ND2 . ASN C  1 83  ? -33.206 -6.340  38.560 1.00 90.03  ? 74  ASN C ND2 1 
ATOM   4147  N  N   . ILE C  1 84  ? -28.451 -9.473  38.442 1.00 65.77  ? 75  ILE C N   1 
ATOM   4148  C  CA  . ILE C  1 84  ? -27.654 -10.685 38.309 1.00 67.13  ? 75  ILE C CA  1 
ATOM   4149  C  C   . ILE C  1 84  ? -27.715 -11.414 39.654 1.00 74.20  ? 75  ILE C C   1 
ATOM   4150  O  O   . ILE C  1 84  ? -27.352 -10.845 40.687 1.00 65.72  ? 75  ILE C O   1 
ATOM   4151  C  CB  . ILE C  1 84  ? -26.172 -10.374 37.976 1.00 65.41  ? 75  ILE C CB  1 
ATOM   4152  C  CG1 . ILE C  1 84  ? -26.027 -9.785  36.575 1.00 56.45  ? 75  ILE C CG1 1 
ATOM   4153  C  CG2 . ILE C  1 84  ? -25.310 -11.629 38.091 1.00 68.57  ? 75  ILE C CG2 1 
ATOM   4154  C  CD1 . ILE C  1 84  ? -24.584 -9.568  36.144 1.00 61.22  ? 75  ILE C CD1 1 
ATOM   4155  N  N   . THR C  1 85  ? -28.202 -12.655 39.659 1.00 73.87  ? 76  THR C N   1 
ATOM   4156  C  CA  . THR C  1 85  ? -28.178 -13.457 40.887 1.00 75.57  ? 76  THR C CA  1 
ATOM   4157  C  C   . THR C  1 85  ? -26.986 -14.409 41.055 1.00 68.78  ? 76  THR C C   1 
ATOM   4158  O  O   . THR C  1 85  ? -26.755 -14.924 42.144 1.00 62.43  ? 76  THR C O   1 
ATOM   4159  C  CB  . THR C  1 85  ? -29.487 -14.248 41.057 1.00 81.96  ? 76  THR C CB  1 
ATOM   4160  O  OG1 . THR C  1 85  ? -29.962 -14.682 39.771 1.00 72.17  ? 76  THR C OG1 1 
ATOM   4161  C  CG2 . THR C  1 85  ? -30.535 -13.370 41.728 1.00 86.38  ? 76  THR C CG2 1 
ATOM   4162  N  N   . ASP C  1 86  ? -26.235 -14.623 39.976 1.00 70.17  ? 77  ASP C N   1 
ATOM   4163  C  CA  . ASP C  1 86  ? -25.004 -15.414 40.016 1.00 64.68  ? 77  ASP C CA  1 
ATOM   4164  C  C   . ASP C  1 86  ? -24.217 -15.301 38.710 1.00 62.11  ? 77  ASP C C   1 
ATOM   4165  O  O   . ASP C  1 86  ? -24.687 -14.720 37.735 1.00 58.43  ? 77  ASP C O   1 
ATOM   4166  C  CB  . ASP C  1 86  ? -25.311 -16.890 40.315 1.00 67.66  ? 77  ASP C CB  1 
ATOM   4167  C  CG  . ASP C  1 86  ? -26.390 -17.473 39.405 1.00 71.87  ? 77  ASP C CG  1 
ATOM   4168  O  OD1 . ASP C  1 86  ? -26.349 -17.251 38.174 1.00 65.33  ? 77  ASP C OD1 1 
ATOM   4169  O  OD2 . ASP C  1 86  ? -27.290 -18.152 39.940 1.00 73.24  ? 77  ASP C OD2 1 
ATOM   4170  N  N   . PHE C  1 87  ? -23.034 -15.902 38.691 1.00 59.52  ? 78  PHE C N   1 
ATOM   4171  C  CA  . PHE C  1 87  ? -22.195 -15.910 37.505 1.00 58.62  ? 78  PHE C CA  1 
ATOM   4172  C  C   . PHE C  1 87  ? -21.172 -17.043 37.583 1.00 59.82  ? 78  PHE C C   1 
ATOM   4173  O  O   . PHE C  1 87  ? -20.825 -17.488 38.668 1.00 56.98  ? 78  PHE C O   1 
ATOM   4174  C  CB  . PHE C  1 87  ? -21.478 -14.565 37.367 1.00 55.94  ? 78  PHE C CB  1 
ATOM   4175  C  CG  . PHE C  1 87  ? -20.497 -14.287 38.472 1.00 55.97  ? 78  PHE C CG  1 
ATOM   4176  C  CD1 . PHE C  1 87  ? -19.165 -14.642 38.340 1.00 57.93  ? 78  PHE C CD1 1 
ATOM   4177  C  CD2 . PHE C  1 87  ? -20.910 -13.676 39.647 1.00 54.26  ? 78  PHE C CD2 1 
ATOM   4178  C  CE1 . PHE C  1 87  ? -18.265 -14.392 39.360 1.00 63.83  ? 78  PHE C CE1 1 
ATOM   4179  C  CE2 . PHE C  1 87  ? -20.019 -13.420 40.662 1.00 53.89  ? 78  PHE C CE2 1 
ATOM   4180  C  CZ  . PHE C  1 87  ? -18.695 -13.782 40.527 1.00 55.87  ? 78  PHE C CZ  1 
ATOM   4181  N  N   . ARG C  1 88  ? -20.642 -17.458 36.434 1.00 67.90  ? 79  ARG C N   1 
ATOM   4182  C  CA  . ARG C  1 88  ? -19.599 -18.484 36.374 1.00 62.53  ? 79  ARG C CA  1 
ATOM   4183  C  C   . ARG C  1 88  ? -18.250 -17.787 36.393 1.00 61.09  ? 79  ARG C C   1 
ATOM   4184  O  O   . ARG C  1 88  ? -18.121 -16.699 35.853 1.00 70.38  ? 79  ARG C O   1 
ATOM   4185  C  CB  . ARG C  1 88  ? -19.724 -19.289 35.078 1.00 61.30  ? 79  ARG C CB  1 
ATOM   4186  C  CG  . ARG C  1 88  ? -20.853 -20.317 35.058 1.00 67.94  ? 79  ARG C CG  1 
ATOM   4187  C  CD  . ARG C  1 88  ? -22.238 -19.694 34.985 1.00 70.34  ? 79  ARG C CD  1 
ATOM   4188  N  NE  . ARG C  1 88  ? -23.284 -20.708 35.134 1.00 75.31  ? 79  ARG C NE  1 
ATOM   4189  C  CZ  . ARG C  1 88  ? -24.589 -20.454 35.066 1.00 83.94  ? 79  ARG C CZ  1 
ATOM   4190  N  NH1 . ARG C  1 88  ? -25.014 -19.208 34.856 1.00 82.48  ? 79  ARG C NH1 1 
ATOM   4191  N  NH2 . ARG C  1 88  ? -25.470 -21.444 35.207 1.00 73.83  ? 79  ARG C NH2 1 
ATOM   4192  N  N   . THR C  1 89  ? -17.245 -18.366 37.028 1.00 52.05  ? 80  THR C N   1 
ATOM   4193  C  CA  . THR C  1 89  ? -15.920 -17.776 36.905 1.00 53.89  ? 80  THR C CA  1 
ATOM   4194  C  C   . THR C  1 89  ? -14.829 -18.822 36.961 1.00 55.91  ? 80  THR C C   1 
ATOM   4195  O  O   . THR C  1 89  ? -15.077 -19.960 37.323 1.00 55.09  ? 80  THR C O   1 
ATOM   4196  C  CB  . THR C  1 89  ? -15.663 -16.675 37.961 1.00 69.17  ? 80  THR C CB  1 
ATOM   4197  O  OG1 . THR C  1 89  ? -14.761 -15.684 37.426 1.00 68.34  ? 80  THR C OG1 1 
ATOM   4198  C  CG2 . THR C  1 89  ? -15.114 -17.281 39.278 1.00 60.52  ? 80  THR C CG2 1 
ATOM   4199  N  N   . SER C  1 90  ? -13.626 -18.453 36.543 1.00 63.81  ? 81  SER C N   1 
ATOM   4200  C  CA  . SER C  1 90  ? -12.486 -19.336 36.721 1.00 64.78  ? 81  SER C CA  1 
ATOM   4201  C  C   . SER C  1 90  ? -12.220 -19.494 38.210 1.00 62.14  ? 81  SER C C   1 
ATOM   4202  O  O   . SER C  1 90  ? -12.378 -18.546 38.967 1.00 63.86  ? 81  SER C O   1 
ATOM   4203  C  CB  . SER C  1 90  ? -11.246 -18.765 36.056 1.00 58.80  ? 81  SER C CB  1 
ATOM   4204  O  OG  . SER C  1 90  ? -10.111 -19.478 36.505 1.00 71.85  ? 81  SER C OG  1 
ATOM   4205  N  N   . ALA C  1 91  ? -11.807 -20.679 38.639 1.00 59.86  ? 82  ALA C N   1 
ATOM   4206  C  CA  . ALA C  1 91  ? -11.588 -20.910 40.063 1.00 60.60  ? 82  ALA C CA  1 
ATOM   4207  C  C   . ALA C  1 91  ? -10.212 -20.419 40.501 1.00 64.25  ? 82  ALA C C   1 
ATOM   4208  O  O   . ALA C  1 91  ? -9.834  -20.551 41.674 1.00 64.89  ? 82  ALA C O   1 
ATOM   4209  C  CB  . ALA C  1 91  ? -11.776 -22.379 40.417 1.00 58.50  ? 82  ALA C CB  1 
ATOM   4210  N  N   . ALA C  1 92  ? -9.451  -19.877 39.558 1.00 61.47  ? 83  ALA C N   1 
ATOM   4211  C  CA  . ALA C  1 92  ? -8.162  -19.309 39.898 1.00 64.20  ? 83  ALA C CA  1 
ATOM   4212  C  C   . ALA C  1 92  ? -8.356  -17.889 40.396 1.00 66.51  ? 83  ALA C C   1 
ATOM   4213  O  O   . ALA C  1 92  ? -7.461  -17.308 40.993 1.00 66.25  ? 83  ALA C O   1 
ATOM   4214  C  CB  . ALA C  1 92  ? -7.248  -19.329 38.705 1.00 64.96  ? 83  ALA C CB  1 
ATOM   4215  N  N   . ASP C  1 93  ? -9.535  -17.334 40.145 1.00 64.59  ? 84  ASP C N   1 
ATOM   4216  C  CA  . ASP C  1 93  ? -9.809  -15.952 40.507 1.00 67.03  ? 84  ASP C CA  1 
ATOM   4217  C  C   . ASP C  1 93  ? -10.420 -15.831 41.879 1.00 70.37  ? 84  ASP C C   1 
ATOM   4218  O  O   . ASP C  1 93  ? -10.519 -14.721 42.423 1.00 73.16  ? 84  ASP C O   1 
ATOM   4219  C  CB  . ASP C  1 93  ? -10.741 -15.302 39.486 1.00 69.67  ? 84  ASP C CB  1 
ATOM   4220  C  CG  . ASP C  1 93  ? -10.195 -15.384 38.079 1.00 76.43  ? 84  ASP C CG  1 
ATOM   4221  O  OD1 . ASP C  1 93  ? -8.951  -15.519 37.947 1.00 73.66  ? 84  ASP C OD1 1 
ATOM   4222  O  OD2 . ASP C  1 93  ? -11.003 -15.320 37.117 1.00 74.41  ? 84  ASP C OD2 1 
ATOM   4223  N  N   . ILE C  1 94  ? -10.827 -16.964 42.446 1.00 64.94  ? 85  ILE C N   1 
ATOM   4224  C  CA  . ILE C  1 94  ? -11.311 -16.952 43.817 1.00 62.36  ? 85  ILE C CA  1 
ATOM   4225  C  C   . ILE C  1 94  ? -10.511 -17.846 44.708 1.00 57.93  ? 85  ILE C C   1 
ATOM   4226  O  O   . ILE C  1 94  ? -9.629  -18.590 44.285 1.00 56.73  ? 85  ILE C O   1 
ATOM   4227  C  CB  . ILE C  1 94  ? -12.764 -17.432 43.966 1.00 52.68  ? 85  ILE C CB  1 
ATOM   4228  C  CG1 . ILE C  1 94  ? -13.008 -18.675 43.119 1.00 61.32  ? 85  ILE C CG1 1 
ATOM   4229  C  CG2 . ILE C  1 94  ? -13.730 -16.338 43.619 1.00 56.76  ? 85  ILE C CG2 1 
ATOM   4230  C  CD1 . ILE C  1 94  ? -14.279 -19.405 43.485 1.00 57.93  ? 85  ILE C CD1 1 
ATOM   4231  N  N   . TRP C  1 95  ? -10.881 -17.793 45.968 1.00 59.80  ? 86  TRP C N   1 
ATOM   4232  C  CA  . TRP C  1 95  ? -10.246 -18.627 46.938 1.00 60.59  ? 86  TRP C CA  1 
ATOM   4233  C  C   . TRP C  1 95  ? -10.869 -20.017 46.811 1.00 57.79  ? 86  TRP C C   1 
ATOM   4234  O  O   . TRP C  1 95  ? -12.056 -20.159 46.528 1.00 55.62  ? 86  TRP C O   1 
ATOM   4235  C  CB  . TRP C  1 95  ? -10.397 -18.014 48.336 1.00 62.00  ? 86  TRP C CB  1 
ATOM   4236  C  CG  . TRP C  1 95  ? -9.757  -18.852 49.357 1.00 56.35  ? 86  TRP C CG  1 
ATOM   4237  C  CD1 . TRP C  1 95  ? -8.462  -18.813 49.768 1.00 52.97  ? 86  TRP C CD1 1 
ATOM   4238  C  CD2 . TRP C  1 95  ? -10.382 -19.900 50.074 1.00 49.65  ? 86  TRP C CD2 1 
ATOM   4239  N  NE1 . TRP C  1 95  ? -8.248  -19.775 50.702 1.00 57.28  ? 86  TRP C NE1 1 
ATOM   4240  C  CE2 . TRP C  1 95  ? -9.412  -20.462 50.906 1.00 56.68  ? 86  TRP C CE2 1 
ATOM   4241  C  CE3 . TRP C  1 95  ? -11.677 -20.418 50.089 1.00 48.33  ? 86  TRP C CE3 1 
ATOM   4242  C  CZ2 . TRP C  1 95  ? -9.698  -21.522 51.756 1.00 59.45  ? 86  TRP C CZ2 1 
ATOM   4243  C  CZ3 . TRP C  1 95  ? -11.960 -21.465 50.928 1.00 46.94  ? 86  TRP C CZ3 1 
ATOM   4244  C  CH2 . TRP C  1 95  ? -10.979 -22.010 51.749 1.00 52.96  ? 86  TRP C CH2 1 
ATOM   4245  N  N   . THR C  1 96  ? -10.044 -21.044 46.944 1.00 52.69  ? 87  THR C N   1 
ATOM   4246  C  CA  . THR C  1 96  ? -10.556 -22.392 46.967 1.00 50.04  ? 87  THR C CA  1 
ATOM   4247  C  C   . THR C  1 96  ? -9.924  -23.075 48.157 1.00 52.35  ? 87  THR C C   1 
ATOM   4248  O  O   . THR C  1 96  ? -8.767  -22.812 48.485 1.00 51.75  ? 87  THR C O   1 
ATOM   4249  C  CB  . THR C  1 96  ? -10.248 -23.171 45.664 1.00 53.57  ? 87  THR C CB  1 
ATOM   4250  O  OG1 . THR C  1 96  ? -8.833  -23.239 45.454 1.00 54.33  ? 87  THR C OG1 1 
ATOM   4251  C  CG2 . THR C  1 96  ? -10.926 -22.515 44.460 1.00 52.08  ? 87  THR C CG2 1 
ATOM   4252  N  N   . PRO C  1 97  ? -10.695 -23.933 48.831 1.00 53.36  ? 88  PRO C N   1 
ATOM   4253  C  CA  . PRO C  1 97  ? -10.202 -24.701 49.985 1.00 53.24  ? 88  PRO C CA  1 
ATOM   4254  C  C   . PRO C  1 97  ? -9.111  -25.670 49.533 1.00 48.38  ? 88  PRO C C   1 
ATOM   4255  O  O   . PRO C  1 97  ? -9.133  -26.066 48.369 1.00 56.28  ? 88  PRO C O   1 
ATOM   4256  C  CB  . PRO C  1 97  ? -11.447 -25.452 50.464 1.00 48.91  ? 88  PRO C CB  1 
ATOM   4257  C  CG  . PRO C  1 97  ? -12.418 -25.400 49.286 1.00 50.72  ? 88  PRO C CG  1 
ATOM   4258  C  CD  . PRO C  1 97  ? -12.129 -24.144 48.573 1.00 45.34  ? 88  PRO C CD  1 
ATOM   4259  N  N   . ASP C  1 98  ? -8.184  -26.049 50.397 1.00 47.62  ? 89  ASP C N   1 
ATOM   4260  C  CA  . ASP C  1 98  ? -7.179  -26.994 49.959 1.00 50.23  ? 89  ASP C CA  1 
ATOM   4261  C  C   . ASP C  1 98  ? -7.789  -28.294 50.431 1.00 56.45  ? 89  ASP C C   1 
ATOM   4262  O  O   . ASP C  1 98  ? -7.871  -28.530 51.636 1.00 62.44  ? 89  ASP C O   1 
ATOM   4263  C  CB  . ASP C  1 98  ? -5.846  -26.737 50.655 1.00 53.82  ? 89  ASP C CB  1 
ATOM   4264  C  CG  . ASP C  1 98  ? -5.999  -26.527 52.149 1.00 56.54  ? 89  ASP C CG  1 
ATOM   4265  O  OD1 . ASP C  1 98  ? -4.997  -26.682 52.878 1.00 50.94  ? 89  ASP C OD1 1 
ATOM   4266  O  OD2 . ASP C  1 98  ? -7.120  -26.202 52.594 1.00 57.31  ? 89  ASP C OD2 1 
ATOM   4267  N  N   . ILE C  1 99  ? -8.232  -29.146 49.511 1.00 51.36  ? 90  ILE C N   1 
ATOM   4268  C  CA  . ILE C  1 99  ? -8.835  -30.376 49.988 1.00 54.00  ? 90  ILE C CA  1 
ATOM   4269  C  C   . ILE C  1 99  ? -8.183  -31.485 49.226 1.00 51.34  ? 90  ILE C C   1 
ATOM   4270  O  O   . ILE C  1 99  ? -8.141  -31.433 48.005 1.00 50.14  ? 90  ILE C O   1 
ATOM   4271  C  CB  . ILE C  1 99  ? -10.351 -30.408 49.770 1.00 52.35  ? 90  ILE C CB  1 
ATOM   4272  C  CG1 . ILE C  1 99  ? -11.023 -29.208 50.445 1.00 53.32  ? 90  ILE C CG1 1 
ATOM   4273  C  CG2 . ILE C  1 99  ? -10.918 -31.694 50.326 1.00 54.09  ? 90  ILE C CG2 1 
ATOM   4274  C  CD1 . ILE C  1 99  ? -11.231 -29.359 51.947 1.00 47.51  ? 90  ILE C CD1 1 
ATOM   4275  N  N   . THR C  1 100 ? -7.650  -32.459 49.954 1.00 48.86  ? 91  THR C N   1 
ATOM   4276  C  CA  . THR C  1 100 ? -6.804  -33.495 49.384 1.00 51.25  ? 91  THR C CA  1 
ATOM   4277  C  C   . THR C  1 100 ? -7.321  -34.868 49.805 1.00 55.85  ? 91  THR C C   1 
ATOM   4278  O  O   . THR C  1 100 ? -7.841  -35.028 50.909 1.00 57.42  ? 91  THR C O   1 
ATOM   4279  C  CB  . THR C  1 100 ? -5.338  -33.361 49.894 1.00 54.17  ? 91  THR C CB  1 
ATOM   4280  O  OG1 . THR C  1 100 ? -4.947  -31.990 49.903 1.00 58.04  ? 91  THR C OG1 1 
ATOM   4281  C  CG2 . THR C  1 100 ? -4.361  -34.156 49.025 1.00 54.59  ? 91  THR C CG2 1 
ATOM   4282  N  N   . ALA C  1 101 ? -7.195  -35.847 48.916 1.00 49.85  ? 92  ALA C N   1 
ATOM   4283  C  CA  . ALA C  1 101 ? -7.300  -37.246 49.294 1.00 51.32  ? 92  ALA C CA  1 
ATOM   4284  C  C   . ALA C  1 101 ? -6.001  -37.512 50.022 1.00 54.04  ? 92  ALA C C   1 
ATOM   4285  O  O   . ALA C  1 101 ? -4.937  -37.111 49.552 1.00 51.87  ? 92  ALA C O   1 
ATOM   4286  C  CB  . ALA C  1 101 ? -7.420  -38.115 48.072 1.00 50.84  ? 92  ALA C CB  1 
ATOM   4287  N  N   . TYR C  1 102 ? -6.095  -38.118 51.199 1.00 56.71  ? 93  TYR C N   1 
ATOM   4288  C  CA  . TYR C  1 102 ? -4.938  -38.307 52.064 1.00 52.50  ? 93  TYR C CA  1 
ATOM   4289  C  C   . TYR C  1 102 ? -4.107  -39.494 51.610 1.00 58.46  ? 93  TYR C C   1 
ATOM   4290  O  O   . TYR C  1 102 ? -2.890  -39.517 51.786 1.00 53.98  ? 93  TYR C O   1 
ATOM   4291  C  CB  . TYR C  1 102 ? -5.384  -38.504 53.507 1.00 57.03  ? 93  TYR C CB  1 
ATOM   4292  C  CG  . TYR C  1 102 ? -5.876  -37.251 54.191 1.00 67.45  ? 93  TYR C CG  1 
ATOM   4293  C  CD1 . TYR C  1 102 ? -5.439  -35.999 53.784 1.00 72.74  ? 93  TYR C CD1 1 
ATOM   4294  C  CD2 . TYR C  1 102 ? -6.776  -37.317 55.247 1.00 66.91  ? 93  TYR C CD2 1 
ATOM   4295  C  CE1 . TYR C  1 102 ? -5.880  -34.849 54.409 1.00 66.12  ? 93  TYR C CE1 1 
ATOM   4296  C  CE2 . TYR C  1 102 ? -7.224  -36.174 55.869 1.00 64.60  ? 93  TYR C CE2 1 
ATOM   4297  C  CZ  . TYR C  1 102 ? -6.770  -34.947 55.447 1.00 61.87  ? 93  TYR C CZ  1 
ATOM   4298  O  OH  . TYR C  1 102 ? -7.208  -33.812 56.066 1.00 55.73  ? 93  TYR C OH  1 
ATOM   4299  N  N   . SER C  1 103 ? -4.791  -40.484 51.045 1.00 60.04  ? 94  SER C N   1 
ATOM   4300  C  CA  . SER C  1 103 ? -4.178  -41.730 50.593 1.00 52.64  ? 94  SER C CA  1 
ATOM   4301  C  C   . SER C  1 103 ? -3.786  -41.755 49.100 1.00 57.51  ? 94  SER C C   1 
ATOM   4302  O  O   . SER C  1 103 ? -3.419  -42.809 48.572 1.00 57.31  ? 94  SER C O   1 
ATOM   4303  C  CB  . SER C  1 103 ? -5.015  -42.952 50.988 1.00 53.51  ? 94  SER C CB  1 
ATOM   4304  O  OG  . SER C  1 103 ? -6.394  -42.721 50.812 1.00 68.85  ? 94  SER C OG  1 
ATOM   4305  N  N   . SER C  1 104 ? -3.902  -40.624 48.407 1.00 50.85  ? 95  SER C N   1 
ATOM   4306  C  CA  . SER C  1 104 ? -3.474  -40.572 47.006 1.00 53.67  ? 95  SER C CA  1 
ATOM   4307  C  C   . SER C  1 104 ? -2.026  -41.063 46.799 1.00 53.92  ? 95  SER C C   1 
ATOM   4308  O  O   . SER C  1 104 ? -1.117  -40.673 47.541 1.00 47.92  ? 95  SER C O   1 
ATOM   4309  C  CB  . SER C  1 104 ? -3.669  -39.164 46.418 1.00 56.90  ? 95  SER C CB  1 
ATOM   4310  O  OG  . SER C  1 104 ? -2.581  -38.291 46.697 1.00 58.85  ? 95  SER C OG  1 
ATOM   4311  N  N   . THR C  1 105 ? -1.839  -41.974 45.837 1.00 50.48  ? 96  THR C N   1 
ATOM   4312  C  CA  . THR C  1 105 ? -0.504  -42.452 45.455 1.00 51.52  ? 96  THR C CA  1 
ATOM   4313  C  C   . THR C  1 105 ? 0.095   -41.795 44.221 1.00 48.78  ? 96  THR C C   1 
ATOM   4314  O  O   . THR C  1 105 ? 1.243   -42.080 43.876 1.00 46.50  ? 96  THR C O   1 
ATOM   4315  C  CB  . THR C  1 105 ? -0.490  -43.981 45.194 1.00 47.40  ? 96  THR C CB  1 
ATOM   4316  O  OG1 . THR C  1 105 ? -1.447  -44.290 44.180 1.00 49.83  ? 96  THR C OG1 1 
ATOM   4317  C  CG2 . THR C  1 105 ? -0.835  -44.745 46.446 1.00 45.33  ? 96  THR C CG2 1 
ATOM   4318  N  N   . ARG C  1 106 ? -0.707  -40.964 43.550 1.00 51.37  ? 97  ARG C N   1 
ATOM   4319  C  CA  A ARG C  1 106 ? -0.282  -40.207 42.367 0.50 48.70  ? 97  ARG C CA  1 
ATOM   4320  C  CA  B ARG C  1 106 ? -0.292  -40.215 42.358 0.50 48.48  ? 97  ARG C CA  1 
ATOM   4321  C  C   . ARG C  1 106 ? -1.061  -38.898 42.301 1.00 46.73  ? 97  ARG C C   1 
ATOM   4322  O  O   . ARG C  1 106 ? -2.199  -38.837 42.768 1.00 47.02  ? 97  ARG C O   1 
ATOM   4323  C  CB  A ARG C  1 106 ? -0.509  -41.006 41.081 0.50 47.89  ? 97  ARG C CB  1 
ATOM   4324  C  CB  B ARG C  1 106 ? -0.559  -41.030 41.090 0.50 47.95  ? 97  ARG C CB  1 
ATOM   4325  C  CG  A ARG C  1 106 ? 0.480   -42.137 40.837 0.50 50.36  ? 97  ARG C CG  1 
ATOM   4326  C  CG  B ARG C  1 106 ? 0.567   -41.973 40.696 0.50 50.32  ? 97  ARG C CG  1 
ATOM   4327  C  CD  A ARG C  1 106 ? 0.437   -42.560 39.382 0.50 53.22  ? 97  ARG C CD  1 
ATOM   4328  C  CD  B ARG C  1 106 ? 0.171   -42.840 39.506 0.50 53.36  ? 97  ARG C CD  1 
ATOM   4329  N  NE  A ARG C  1 106 ? 1.037   -43.865 39.108 0.50 56.75  ? 97  ARG C NE  1 
ATOM   4330  N  NE  B ARG C  1 106 ? -0.353  -44.152 39.890 0.50 54.98  ? 97  ARG C NE  1 
ATOM   4331  C  CZ  A ARG C  1 106 ? 2.331   -44.070 38.887 0.50 53.97  ? 97  ARG C CZ  1 
ATOM   4332  C  CZ  B ARG C  1 106 ? -0.904  -45.016 39.039 0.50 56.87  ? 97  ARG C CZ  1 
ATOM   4333  N  NH1 A ARG C  1 106 ? 3.189   -43.060 38.939 0.50 47.57  ? 97  ARG C NH1 1 
ATOM   4334  N  NH1 B ARG C  1 106 ? -1.024  -44.703 37.753 0.50 54.93  ? 97  ARG C NH1 1 
ATOM   4335  N  NH2 A ARG C  1 106 ? 2.766   -45.294 38.622 0.50 53.26  ? 97  ARG C NH2 1 
ATOM   4336  N  NH2 B ARG C  1 106 ? -1.351  -46.188 39.470 0.50 52.07  ? 97  ARG C NH2 1 
ATOM   4337  N  N   . PRO C  1 107 ? -0.457  -37.842 41.708 1.00 46.95  ? 98  PRO C N   1 
ATOM   4338  C  CA  . PRO C  1 107 ? -1.158  -36.547 41.709 1.00 43.75  ? 98  PRO C CA  1 
ATOM   4339  C  C   . PRO C  1 107 ? -2.528  -36.603 41.044 1.00 43.70  ? 98  PRO C C   1 
ATOM   4340  O  O   . PRO C  1 107 ? -2.669  -37.216 39.988 1.00 41.09  ? 98  PRO C O   1 
ATOM   4341  C  CB  . PRO C  1 107 ? -0.198  -35.600 40.978 1.00 26.80  ? 98  PRO C CB  1 
ATOM   4342  C  CG  . PRO C  1 107 ? 0.872   -36.414 40.441 1.00 33.12  ? 98  PRO C CG  1 
ATOM   4343  C  CD  . PRO C  1 107 ? 0.902   -37.726 41.157 1.00 45.48  ? 98  PRO C CD  1 
ATOM   4344  N  N   . VAL C  1 108 ? -3.532  -36.001 41.678 1.00 44.91  ? 99  VAL C N   1 
ATOM   4345  C  CA  . VAL C  1 108 ? -4.879  -36.037 41.137 1.00 43.89  ? 99  VAL C CA  1 
ATOM   4346  C  C   . VAL C  1 108 ? -4.872  -35.372 39.777 1.00 51.07  ? 99  VAL C C   1 
ATOM   4347  O  O   . VAL C  1 108 ? -4.215  -34.337 39.592 1.00 48.29  ? 99  VAL C O   1 
ATOM   4348  C  CB  . VAL C  1 108 ? -5.874  -35.360 42.070 1.00 37.15  ? 99  VAL C CB  1 
ATOM   4349  C  CG1 . VAL C  1 108 ? -7.237  -35.272 41.449 1.00 44.73  ? 99  VAL C CG1 1 
ATOM   4350  C  CG2 . VAL C  1 108 ? -5.980  -36.185 43.293 1.00 59.42  ? 99  VAL C CG2 1 
ATOM   4351  N  N   . GLN C  1 109 ? -5.566  -35.984 38.816 1.00 43.16  ? 100 GLN C N   1 
ATOM   4352  C  CA  . GLN C  1 109 ? -5.763  -35.357 37.521 1.00 44.26  ? 100 GLN C CA  1 
ATOM   4353  C  C   . GLN C  1 109 ? -7.176  -34.812 37.399 1.00 48.31  ? 100 GLN C C   1 
ATOM   4354  O  O   . GLN C  1 109 ? -8.146  -35.439 37.818 1.00 47.19  ? 100 GLN C O   1 
ATOM   4355  C  CB  . GLN C  1 109 ? -5.485  -36.341 36.401 1.00 47.85  ? 100 GLN C CB  1 
ATOM   4356  C  CG  . GLN C  1 109 ? -4.129  -36.971 36.474 1.00 46.88  ? 100 GLN C CG  1 
ATOM   4357  C  CD  . GLN C  1 109 ? -4.044  -38.209 35.622 1.00 51.94  ? 100 GLN C CD  1 
ATOM   4358  O  OE1 . GLN C  1 109 ? -4.472  -39.287 36.023 1.00 51.29  ? 100 GLN C OE1 1 
ATOM   4359  N  NE2 . GLN C  1 109 ? -3.505  -38.059 34.434 1.00 47.52  ? 100 GLN C NE2 1 
ATOM   4360  N  N   . VAL C  1 110 ? -7.276  -33.620 36.829 1.00 53.91  ? 101 VAL C N   1 
ATOM   4361  C  CA  . VAL C  1 110 ? -8.571  -32.988 36.628 1.00 56.01  ? 101 VAL C CA  1 
ATOM   4362  C  C   . VAL C  1 110 ? -9.077  -33.237 35.221 1.00 53.97  ? 101 VAL C C   1 
ATOM   4363  O  O   . VAL C  1 110 ? -8.347  -33.055 34.256 1.00 56.88  ? 101 VAL C O   1 
ATOM   4364  C  CB  . VAL C  1 110 ? -8.510  -31.496 36.891 1.00 56.84  ? 101 VAL C CB  1 
ATOM   4365  C  CG1 . VAL C  1 110 ? -9.898  -30.926 36.786 1.00 68.64  ? 101 VAL C CG1 1 
ATOM   4366  C  CG2 . VAL C  1 110 ? -7.950  -31.259 38.270 1.00 47.80  ? 101 VAL C CG2 1 
ATOM   4367  N  N   . LEU C  1 111 ? -10.302 -33.743 35.136 1.00 55.67  ? 102 LEU C N   1 
ATOM   4368  C  CA  . LEU C  1 111 ? -10.946 -34.089 33.873 1.00 48.99  ? 102 LEU C CA  1 
ATOM   4369  C  C   . LEU C  1 111 ? -11.929 -33.026 33.365 1.00 56.72  ? 102 LEU C C   1 
ATOM   4370  O  O   . LEU C  1 111 ? -12.569 -33.209 32.326 1.00 59.23  ? 102 LEU C O   1 
ATOM   4371  C  CB  . LEU C  1 111 ? -11.630 -35.447 33.996 1.00 46.79  ? 102 LEU C CB  1 
ATOM   4372  C  CG  . LEU C  1 111 ? -10.763 -36.473 34.718 1.00 52.12  ? 102 LEU C CG  1 
ATOM   4373  C  CD1 . LEU C  1 111 ? -11.551 -37.723 35.020 1.00 48.89  ? 102 LEU C CD1 1 
ATOM   4374  C  CD2 . LEU C  1 111 ? -9.499  -36.781 33.940 1.00 48.17  ? 102 LEU C CD2 1 
ATOM   4375  N  N   . SER C  1 112 ? -12.082 -31.940 34.115 1.00 57.44  ? 103 SER C N   1 
ATOM   4376  C  CA  . SER C  1 112 ? -12.985 -30.879 33.697 1.00 56.90  ? 103 SER C CA  1 
ATOM   4377  C  C   . SER C  1 112 ? -12.342 -29.501 33.804 1.00 55.49  ? 103 SER C C   1 
ATOM   4378  O  O   . SER C  1 112 ? -11.228 -29.353 34.312 1.00 52.81  ? 103 SER C O   1 
ATOM   4379  C  CB  . SER C  1 112 ? -14.261 -30.917 34.547 1.00 58.59  ? 103 SER C CB  1 
ATOM   4380  O  OG  . SER C  1 112 ? -13.963 -30.806 35.931 1.00 58.63  ? 103 SER C OG  1 
ATOM   4381  N  N   . PRO C  1 113 ? -13.087 -28.525 33.350 1.00 55.58  ? 104 PRO C N   1 
ATOM   4382  C  CA  . PRO C  1 113 ? -12.700 -27.146 33.424 1.00 56.06  ? 104 PRO C CA  1 
ATOM   4383  C  C   . PRO C  1 113 ? -12.838 -26.705 34.834 1.00 58.95  ? 104 PRO C C   1 
ATOM   4384  O  O   . PRO C  1 113 ? -13.775 -27.036 35.499 1.00 58.62  ? 104 PRO C O   1 
ATOM   4385  C  CB  . PRO C  1 113 ? -13.759 -26.486 32.594 1.00 56.27  ? 104 PRO C CB  1 
ATOM   4386  C  CG  . PRO C  1 113 ? -14.158 -27.492 31.671 1.00 52.46  ? 104 PRO C CG  1 
ATOM   4387  C  CD  . PRO C  1 113 ? -14.216 -28.696 32.448 1.00 55.73  ? 104 PRO C CD  1 
ATOM   4388  N  N   . GLN C  1 114 ? -11.873 -25.969 35.313 1.00 60.28  ? 105 GLN C N   1 
ATOM   4389  C  CA  . GLN C  1 114 ? -11.936 -25.501 36.659 1.00 63.08  ? 105 GLN C CA  1 
ATOM   4390  C  C   . GLN C  1 114 ? -12.595 -24.154 36.578 1.00 64.27  ? 105 GLN C C   1 
ATOM   4391  O  O   . GLN C  1 114 ? -11.942 -23.160 36.397 1.00 66.44  ? 105 GLN C O   1 
ATOM   4392  C  CB  . GLN C  1 114 ? -10.541 -25.520 37.243 1.00 57.33  ? 105 GLN C CB  1 
ATOM   4393  C  CG  . GLN C  1 114 ? -10.047 -26.930 37.343 1.00 61.78  ? 105 GLN C CG  1 
ATOM   4394  C  CD  . GLN C  1 114 ? -8.588  -27.010 37.476 1.00 64.21  ? 105 GLN C CD  1 
ATOM   4395  O  OE1 . GLN C  1 114 ? -7.875  -26.981 36.504 1.00 65.64  ? 105 GLN C OE1 1 
ATOM   4396  N  NE2 . GLN C  1 114 ? -8.121  -27.125 38.685 1.00 70.47  ? 105 GLN C NE2 1 
ATOM   4397  N  N   . ASN C  1 115 ? -13.904 -24.141 36.728 1.00 58.65  ? 106 ASN C N   1 
ATOM   4398  C  CA  . ASN C  1 115 ? -14.663 -22.931 36.772 1.00 53.93  ? 106 ASN C CA  1 
ATOM   4399  C  C   . ASN C  1 115 ? -15.625 -23.142 37.877 1.00 52.44  ? 106 ASN C C   1 
ATOM   4400  O  O   . ASN C  1 115 ? -16.027 -24.237 38.109 1.00 55.30  ? 106 ASN C O   1 
ATOM   4401  C  CB  . ASN C  1 115 ? -15.459 -22.740 35.490 1.00 65.84  ? 106 ASN C CB  1 
ATOM   4402  C  CG  . ASN C  1 115 ? -14.601 -22.630 34.253 1.00 68.88  ? 106 ASN C CG  1 
ATOM   4403  O  OD1 . ASN C  1 115 ? -13.652 -21.874 34.198 1.00 62.95  ? 106 ASN C OD1 1 
ATOM   4404  N  ND2 . ASN C  1 115 ? -14.977 -23.356 33.233 1.00 62.31  ? 106 ASN C ND2 1 
ATOM   4405  N  N   . ALA C  1 116 ? -16.007 -22.088 38.560 1.00 57.13  ? 107 ALA C N   1 
ATOM   4406  C  CA  . ALA C  1 116 ? -16.898 -22.212 39.682 1.00 49.99  ? 107 ALA C CA  1 
ATOM   4407  C  C   . ALA C  1 116 ? -18.040 -21.257 39.566 1.00 52.55  ? 107 ALA C C   1 
ATOM   4408  O  O   . ALA C  1 116 ? -17.936 -20.261 38.912 1.00 65.72  ? 107 ALA C O   1 
ATOM   4409  C  CB  . ALA C  1 116 ? -16.175 -21.957 40.904 1.00 46.35  ? 107 ALA C CB  1 
ATOM   4410  N  N   . LEU C  1 117 ? -19.140 -21.558 40.252 1.00 48.45  ? 108 LEU C N   1 
ATOM   4411  C  CA  . LEU C  1 117 ? -20.328 -20.703 40.234 1.00 54.40  ? 108 LEU C CA  1 
ATOM   4412  C  C   . LEU C  1 117 ? -20.536 -19.983 41.572 1.00 49.50  ? 108 LEU C C   1 
ATOM   4413  O  O   . LEU C  1 117 ? -20.482 -20.602 42.634 1.00 54.42  ? 108 LEU C O   1 
ATOM   4414  C  CB  . LEU C  1 117 ? -21.570 -21.524 39.883 1.00 49.88  ? 108 LEU C CB  1 
ATOM   4415  C  CG  . LEU C  1 117 ? -22.901 -20.769 39.862 1.00 66.31  ? 108 LEU C CG  1 
ATOM   4416  C  CD1 . LEU C  1 117 ? -22.877 -19.666 38.816 1.00 74.31  ? 108 LEU C CD1 1 
ATOM   4417  C  CD2 . LEU C  1 117 ? -24.057 -21.725 39.612 1.00 69.76  ? 108 LEU C CD2 1 
ATOM   4418  N  N   . VAL C  1 118 ? -20.747 -18.722 41.390 1.00 54.53  ? 109 VAL C N   1 
ATOM   4419  C  CA  . VAL C  1 118 ? -20.908 -17.855 42.561 1.00 57.28  ? 109 VAL C CA  1 
ATOM   4420  C  C   . VAL C  1 118 ? -22.290 -17.188 42.623 1.00 59.91  ? 109 VAL C C   1 
ATOM   4421  O  O   . VAL C  1 118 ? -22.757 -16.653 41.619 1.00 59.27  ? 109 VAL C O   1 
ATOM   4422  C  CB  . VAL C  1 118 ? -19.838 -16.754 42.602 1.00 49.85  ? 109 VAL C CB  1 
ATOM   4423  C  CG1 . VAL C  1 118 ? -19.879 -16.087 43.935 1.00 57.37  ? 109 VAL C CG1 1 
ATOM   4424  C  CG2 . VAL C  1 118 ? -18.446 -17.319 42.349 1.00 53.05  ? 109 VAL C CG2 1 
ATOM   4425  N  N   . ASN C  1 119 ? -22.911 -17.099 43.733 1.00 52.86  ? 110 ASN C N   1 
ATOM   4426  C  CA  . ASN C  1 119 ? -24.230 -16.461 43.800 1.00 64.26  ? 110 ASN C CA  1 
ATOM   4427  C  C   . ASN C  1 119 ? -24.370 -15.399 44.905 1.00 61.63  ? 110 ASN C C   1 
ATOM   4428  O  O   . ASN C  1 119 ? -23.567 -15.377 45.842 1.00 64.72  ? 110 ASN C O   1 
ATOM   4429  C  CB  . ASN C  1 119 ? -25.351 -17.405 43.727 1.00 66.61  ? 110 ASN C CB  1 
ATOM   4430  C  CG  . ASN C  1 119 ? -25.637 -17.958 45.017 1.00 68.89  ? 110 ASN C CG  1 
ATOM   4431  O  OD1 . ASN C  1 119 ? -25.028 -17.579 46.021 1.00 68.99  ? 110 ASN C OD1 1 
ATOM   4432  N  ND2 . ASN C  1 119 ? -26.565 -18.874 45.046 1.00 79.86  ? 110 ASN C ND2 1 
ATOM   4433  N  N   . SER C  1 120 ? -25.350 -14.527 44.773 1.00 60.13  ? 111 SER C N   1 
ATOM   4434  C  CA  . SER C  1 120 ? -25.454 -13.233 45.453 1.00 63.73  ? 111 SER C CA  1 
ATOM   4435  C  C   . SER C  1 120 ? -25.492 -13.344 46.961 1.00 65.85  ? 111 SER C C   1 
ATOM   4436  O  O   . SER C  1 120 ? -25.135 -12.400 47.661 1.00 70.12  ? 111 SER C O   1 
ATOM   4437  C  CB  . SER C  1 120 ? -26.664 -12.437 44.938 1.00 67.22  ? 111 SER C CB  1 
ATOM   4438  O  OG  . SER C  1 120 ? -27.872 -13.120 45.188 1.00 75.66  ? 111 SER C OG  1 
ATOM   4439  N  N   . SER C  1 121 ? -25.941 -14.502 47.440 1.00 74.92  ? 112 SER C N   1 
ATOM   4440  C  CA  . SER C  1 121 ? -25.906 -14.864 48.863 1.00 70.65  ? 112 SER C CA  1 
ATOM   4441  C  C   . SER C  1 121 ? -24.477 -15.052 49.368 1.00 68.44  ? 112 SER C C   1 
ATOM   4442  O  O   . SER C  1 121 ? -24.214 -15.010 50.560 1.00 70.58  ? 112 SER C O   1 
ATOM   4443  C  CB  . SER C  1 121 ? -26.678 -16.163 49.110 1.00 72.15  ? 112 SER C CB  1 
ATOM   4444  O  OG  . SER C  1 121 ? -27.993 -16.104 48.584 1.00 80.47  ? 112 SER C OG  1 
ATOM   4445  N  N   . GLY C  1 122 ? -23.554 -15.264 48.444 1.00 69.95  ? 113 GLY C N   1 
ATOM   4446  C  CA  . GLY C  1 122 ? -22.165 -15.513 48.778 1.00 67.77  ? 113 GLY C CA  1 
ATOM   4447  C  C   . GLY C  1 122 ? -21.732 -16.959 48.597 1.00 68.68  ? 113 GLY C C   1 
ATOM   4448  O  O   . GLY C  1 122 ? -20.566 -17.290 48.781 1.00 68.19  ? 113 GLY C O   1 
ATOM   4449  N  N   . HIS C  1 123 ? -22.645 -17.836 48.243 1.00 68.76  ? 114 HIS C N   1 
ATOM   4450  C  CA  . HIS C  1 123 ? -22.348 -19.251 48.146 1.00 63.33  ? 114 HIS C CA  1 
ATOM   4451  C  C   . HIS C  1 123 ? -21.469 -19.530 46.952 1.00 58.33  ? 114 HIS C C   1 
ATOM   4452  O  O   . HIS C  1 123 ? -21.658 -18.966 45.893 1.00 59.49  ? 114 HIS C O   1 
ATOM   4453  C  CB  . HIS C  1 123 ? -23.631 -20.064 48.088 1.00 68.94  ? 114 HIS C CB  1 
ATOM   4454  C  CG  . HIS C  1 123 ? -24.487 -19.898 49.302 1.00 81.56  ? 114 HIS C CG  1 
ATOM   4455  N  ND1 . HIS C  1 123 ? -25.612 -19.105 49.316 1.00 87.33  ? 114 HIS C ND1 1 
ATOM   4456  C  CD2 . HIS C  1 123 ? -24.356 -20.394 50.555 1.00 79.51  ? 114 HIS C CD2 1 
ATOM   4457  C  CE1 . HIS C  1 123 ? -26.154 -19.135 50.521 1.00 87.20  ? 114 HIS C CE1 1 
ATOM   4458  N  NE2 . HIS C  1 123 ? -25.411 -19.908 51.291 1.00 91.58  ? 114 HIS C NE2 1 
ATOM   4459  N  N   . VAL C  1 124 ? -20.478 -20.383 47.138 1.00 57.93  ? 115 VAL C N   1 
ATOM   4460  C  CA  . VAL C  1 124 ? -19.659 -20.814 46.026 1.00 51.69  ? 115 VAL C CA  1 
ATOM   4461  C  C   . VAL C  1 124 ? -19.806 -22.304 45.823 1.00 50.82  ? 115 VAL C C   1 
ATOM   4462  O  O   . VAL C  1 124 ? -19.880 -23.074 46.773 1.00 50.11  ? 115 VAL C O   1 
ATOM   4463  C  CB  . VAL C  1 124 ? -18.192 -20.442 46.205 1.00 51.88  ? 115 VAL C CB  1 
ATOM   4464  C  CG1 . VAL C  1 124 ? -17.366 -21.034 45.078 1.00 50.13  ? 115 VAL C CG1 1 
ATOM   4465  C  CG2 . VAL C  1 124 ? -18.048 -18.928 46.236 1.00 53.24  ? 115 VAL C CG2 1 
ATOM   4466  N  N   . GLN C  1 125 ? -19.887 -22.701 44.565 1.00 49.07  ? 116 GLN C N   1 
ATOM   4467  C  CA  . GLN C  1 125 ? -20.088 -24.092 44.243 1.00 53.73  ? 116 GLN C CA  1 
ATOM   4468  C  C   . GLN C  1 125 ? -19.081 -24.509 43.179 1.00 53.47  ? 116 GLN C C   1 
ATOM   4469  O  O   . GLN C  1 125 ? -19.069 -23.974 42.081 1.00 56.52  ? 116 GLN C O   1 
ATOM   4470  C  CB  . GLN C  1 125 ? -21.525 -24.301 43.782 1.00 55.21  ? 116 GLN C CB  1 
ATOM   4471  C  CG  . GLN C  1 125 ? -21.993 -25.729 43.821 1.00 66.82  ? 116 GLN C CG  1 
ATOM   4472  C  CD  . GLN C  1 125 ? -22.976 -26.006 42.711 1.00 82.70  ? 116 GLN C CD  1 
ATOM   4473  O  OE1 . GLN C  1 125 ? -23.935 -25.250 42.520 1.00 85.70  ? 116 GLN C OE1 1 
ATOM   4474  N  NE2 . GLN C  1 125 ? -22.728 -27.071 41.942 1.00 85.74  ? 116 GLN C NE2 1 
ATOM   4475  N  N   . TYR C  1 126 ? -18.228 -25.460 43.522 1.00 45.26  ? 117 TYR C N   1 
ATOM   4476  C  CA  . TYR C  1 126 ? -17.148 -25.884 42.651 1.00 48.39  ? 117 TYR C CA  1 
ATOM   4477  C  C   . TYR C  1 126 ? -17.195 -27.402 42.490 1.00 52.44  ? 117 TYR C C   1 
ATOM   4478  O  O   . TYR C  1 126 ? -17.314 -28.126 43.469 1.00 56.42  ? 117 TYR C O   1 
ATOM   4479  C  CB  . TYR C  1 126 ? -15.826 -25.426 43.252 1.00 48.33  ? 117 TYR C CB  1 
ATOM   4480  C  CG  . TYR C  1 126 ? -14.586 -25.844 42.507 1.00 52.79  ? 117 TYR C CG  1 
ATOM   4481  C  CD1 . TYR C  1 126 ? -14.450 -25.584 41.167 1.00 50.38  ? 117 TYR C CD1 1 
ATOM   4482  C  CD2 . TYR C  1 126 ? -13.533 -26.469 43.160 1.00 53.95  ? 117 TYR C CD2 1 
ATOM   4483  C  CE1 . TYR C  1 126 ? -13.323 -25.941 40.486 1.00 51.84  ? 117 TYR C CE1 1 
ATOM   4484  C  CE2 . TYR C  1 126 ? -12.393 -26.832 42.481 1.00 49.33  ? 117 TYR C CE2 1 
ATOM   4485  C  CZ  . TYR C  1 126 ? -12.294 -26.556 41.137 1.00 54.80  ? 117 TYR C CZ  1 
ATOM   4486  O  OH  . TYR C  1 126 ? -11.169 -26.897 40.418 1.00 50.98  ? 117 TYR C OH  1 
ATOM   4487  N  N   . LEU C  1 127 ? -17.127 -27.894 41.260 1.00 51.52  ? 118 LEU C N   1 
ATOM   4488  C  CA  . LEU C  1 127 ? -17.354 -29.320 41.026 1.00 53.29  ? 118 LEU C CA  1 
ATOM   4489  C  C   . LEU C  1 127 ? -16.455 -29.956 39.955 1.00 54.05  ? 118 LEU C C   1 
ATOM   4490  O  O   . LEU C  1 127 ? -16.895 -30.193 38.835 1.00 58.56  ? 118 LEU C O   1 
ATOM   4491  C  CB  . LEU C  1 127 ? -18.835 -29.559 40.702 1.00 54.02  ? 118 LEU C CB  1 
ATOM   4492  C  CG  . LEU C  1 127 ? -19.204 -30.965 40.219 1.00 68.50  ? 118 LEU C CG  1 
ATOM   4493  C  CD1 . LEU C  1 127 ? -19.022 -32.010 41.320 1.00 64.37  ? 118 LEU C CD1 1 
ATOM   4494  C  CD2 . LEU C  1 127 ? -20.612 -30.983 39.698 1.00 72.59  ? 118 LEU C CD2 1 
ATOM   4495  N  N   . PRO C  1 128 ? -15.182 -30.210 40.284 1.00 53.11  ? 119 PRO C N   1 
ATOM   4496  C  CA  . PRO C  1 128 ? -14.276 -30.864 39.333 1.00 56.18  ? 119 PRO C CA  1 
ATOM   4497  C  C   . PRO C  1 128 ? -14.462 -32.377 39.181 1.00 54.71  ? 119 PRO C C   1 
ATOM   4498  O  O   . PRO C  1 128 ? -14.762 -33.080 40.136 1.00 49.51  ? 119 PRO C O   1 
ATOM   4499  C  CB  . PRO C  1 128 ? -12.892 -30.577 39.918 1.00 53.43  ? 119 PRO C CB  1 
ATOM   4500  C  CG  . PRO C  1 128 ? -13.129 -30.396 41.347 1.00 52.24  ? 119 PRO C CG  1 
ATOM   4501  C  CD  . PRO C  1 128 ? -14.467 -29.731 41.474 1.00 51.26  ? 119 PRO C CD  1 
ATOM   4502  N  N   . ALA C  1 129 ? -14.258 -32.861 37.960 1.00 57.23  ? 120 ALA C N   1 
ATOM   4503  C  CA  . ALA C  1 129 ? -14.120 -34.284 37.710 1.00 54.70  ? 120 ALA C CA  1 
ATOM   4504  C  C   . ALA C  1 129 ? -12.653 -34.585 37.935 1.00 52.24  ? 120 ALA C C   1 
ATOM   4505  O  O   . ALA C  1 129 ? -11.786 -33.814 37.517 1.00 53.63  ? 120 ALA C O   1 
ATOM   4506  C  CB  . ALA C  1 129 ? -14.537 -34.630 36.277 1.00 42.08  ? 120 ALA C CB  1 
ATOM   4507  N  N   . GLN C  1 130 ? -12.361 -35.683 38.622 1.00 47.71  ? 121 GLN C N   1 
ATOM   4508  C  CA  . GLN C  1 130 ? -10.969 -36.048 38.850 1.00 52.35  ? 121 GLN C CA  1 
ATOM   4509  C  C   . GLN C  1 130 ? -10.723 -37.532 38.650 1.00 53.22  ? 121 GLN C C   1 
ATOM   4510  O  O   . GLN C  1 130 ? -11.641 -38.340 38.737 1.00 54.39  ? 121 GLN C O   1 
ATOM   4511  C  CB  . GLN C  1 130 ? -10.532 -35.601 40.246 1.00 49.54  ? 121 GLN C CB  1 
ATOM   4512  C  CG  . GLN C  1 130 ? -10.914 -34.153 40.508 1.00 55.01  ? 121 GLN C CG  1 
ATOM   4513  C  CD  . GLN C  1 130 ? -10.476 -33.649 41.845 1.00 51.00  ? 121 GLN C CD  1 
ATOM   4514  O  OE1 . GLN C  1 130 ? -10.324 -34.414 42.788 1.00 58.88  ? 121 GLN C OE1 1 
ATOM   4515  N  NE2 . GLN C  1 130 ? -10.260 -32.347 41.939 1.00 60.44  ? 121 GLN C NE2 1 
ATOM   4516  N  N   . ARG C  1 131 ? -9.483  -37.886 38.344 1.00 48.94  ? 122 ARG C N   1 
ATOM   4517  C  CA  . ARG C  1 131 ? -9.096  -39.281 38.379 1.00 47.19  ? 122 ARG C CA  1 
ATOM   4518  C  C   . ARG C  1 131 ? -8.030  -39.420 39.420 1.00 48.35  ? 122 ARG C C   1 
ATOM   4519  O  O   . ARG C  1 131 ? -7.003  -38.752 39.339 1.00 51.18  ? 122 ARG C O   1 
ATOM   4520  C  CB  . ARG C  1 131 ? -8.552  -39.780 37.040 1.00 50.99  ? 122 ARG C CB  1 
ATOM   4521  C  CG  . ARG C  1 131 ? -8.220  -41.267 37.053 1.00 47.81  ? 122 ARG C CG  1 
ATOM   4522  C  CD  . ARG C  1 131 ? -6.885  -41.546 36.410 1.00 53.49  ? 122 ARG C CD  1 
ATOM   4523  N  NE  . ARG C  1 131 ? -6.652  -42.981 36.244 1.00 62.89  ? 122 ARG C NE  1 
ATOM   4524  C  CZ  . ARG C  1 131 ? -6.979  -43.694 35.164 1.00 54.92  ? 122 ARG C CZ  1 
ATOM   4525  N  NH1 . ARG C  1 131 ? -7.572  -43.140 34.113 1.00 53.06  ? 122 ARG C NH1 1 
ATOM   4526  N  NH2 . ARG C  1 131 ? -6.713  -44.983 35.142 1.00 55.70  ? 122 ARG C NH2 1 
ATOM   4527  N  N   . LEU C  1 132 ? -8.280  -40.320 40.368 1.00 44.18  ? 123 LEU C N   1 
ATOM   4528  C  CA  . LEU C  1 132 ? -7.437  -40.528 41.527 1.00 45.04  ? 123 LEU C CA  1 
ATOM   4529  C  C   . LEU C  1 132 ? -6.895  -41.942 41.642 1.00 46.33  ? 123 LEU C C   1 
ATOM   4530  O  O   . LEU C  1 132 ? -7.654  -42.900 41.686 1.00 46.66  ? 123 LEU C O   1 
ATOM   4531  C  CB  . LEU C  1 132 ? -8.269  -40.234 42.773 1.00 51.54  ? 123 LEU C CB  1 
ATOM   4532  C  CG  . LEU C  1 132 ? -7.629  -40.297 44.157 1.00 51.30  ? 123 LEU C CG  1 
ATOM   4533  C  CD1 . LEU C  1 132 ? -6.586  -39.209 44.305 1.00 52.71  ? 123 LEU C CD1 1 
ATOM   4534  C  CD2 . LEU C  1 132 ? -8.709  -40.137 45.185 1.00 50.47  ? 123 LEU C CD2 1 
ATOM   4535  N  N   . SER C  1 133 ? -5.575  -42.064 41.713 1.00 52.30  ? 124 SER C N   1 
ATOM   4536  C  CA  . SER C  1 133 ? -4.943  -43.292 42.205 1.00 52.38  ? 124 SER C CA  1 
ATOM   4537  C  C   . SER C  1 133 ? -4.769  -43.231 43.735 1.00 51.96  ? 124 SER C C   1 
ATOM   4538  O  O   . SER C  1 133 ? -4.152  -42.306 44.273 1.00 57.17  ? 124 SER C O   1 
ATOM   4539  C  CB  . SER C  1 133 ? -3.594  -43.536 41.518 1.00 49.86  ? 124 SER C CB  1 
ATOM   4540  O  OG  . SER C  1 133 ? -3.789  -43.837 40.154 1.00 52.75  ? 124 SER C OG  1 
ATOM   4541  N  N   . PHE C  1 134 ? -5.320  -44.206 44.442 1.00 48.21  ? 125 PHE C N   1 
ATOM   4542  C  CA  . PHE C  1 134 ? -5.215  -44.184 45.891 1.00 48.98  ? 125 PHE C CA  1 
ATOM   4543  C  C   . PHE C  1 134 ? -4.936  -45.565 46.471 1.00 56.18  ? 125 PHE C C   1 
ATOM   4544  O  O   . PHE C  1 134 ? -5.076  -46.579 45.782 1.00 58.74  ? 125 PHE C O   1 
ATOM   4545  C  CB  . PHE C  1 134 ? -6.449  -43.544 46.505 1.00 48.28  ? 125 PHE C CB  1 
ATOM   4546  C  CG  . PHE C  1 134 ? -7.683  -44.390 46.425 1.00 51.91  ? 125 PHE C CG  1 
ATOM   4547  C  CD1 . PHE C  1 134 ? -7.982  -45.296 47.426 1.00 59.05  ? 125 PHE C CD1 1 
ATOM   4548  C  CD2 . PHE C  1 134 ? -8.569  -44.250 45.385 1.00 53.21  ? 125 PHE C CD2 1 
ATOM   4549  C  CE1 . PHE C  1 134 ? -9.120  -46.069 47.367 1.00 57.08  ? 125 PHE C CE1 1 
ATOM   4550  C  CE2 . PHE C  1 134 ? -9.711  -45.019 45.328 1.00 60.45  ? 125 PHE C CE2 1 
ATOM   4551  C  CZ  . PHE C  1 134 ? -9.980  -45.936 46.325 1.00 57.38  ? 125 PHE C CZ  1 
ATOM   4552  N  N   . MET C  1 135 ? -4.528  -45.627 47.731 1.00 57.18  ? 126 MET C N   1 
ATOM   4553  C  CA  . MET C  1 135 ? -4.133  -46.913 48.278 1.00 56.84  ? 126 MET C CA  1 
ATOM   4554  C  C   . MET C  1 135 ? -5.351  -47.756 48.646 1.00 53.59  ? 126 MET C C   1 
ATOM   4555  O  O   . MET C  1 135 ? -6.157  -47.381 49.497 1.00 52.95  ? 126 MET C O   1 
ATOM   4556  C  CB  . MET C  1 135 ? -3.209  -46.689 49.495 1.00 55.16  ? 126 MET C CB  1 
ATOM   4557  C  CG  . MET C  1 135 ? -1.994  -45.818 49.186 1.00 54.58  ? 126 MET C CG  1 
ATOM   4558  S  SD  . MET C  1 135 ? -1.119  -45.261 50.662 1.00 59.35  ? 126 MET C SD  1 
ATOM   4559  C  CE  . MET C  1 135 ? -2.417  -44.459 51.536 1.00 54.97  ? 126 MET C CE  1 
ATOM   4560  N  N   . CYS C  1 136 ? -5.462  -48.894 47.962 1.00 54.49  ? 127 CYS C N   1 
ATOM   4561  C  CA  . CYS C  1 136 ? -6.503  -49.884 48.220 1.00 58.77  ? 127 CYS C CA  1 
ATOM   4562  C  C   . CYS C  1 136 ? -6.036  -51.282 47.854 1.00 62.69  ? 127 CYS C C   1 
ATOM   4563  O  O   . CYS C  1 136 ? -5.318  -51.466 46.869 1.00 59.28  ? 127 CYS C O   1 
ATOM   4564  C  CB  . CYS C  1 136 ? -7.750  -49.516 47.433 1.00 62.05  ? 127 CYS C CB  1 
ATOM   4565  S  SG  . CYS C  1 136 ? -8.811  -50.864 46.999 1.00 69.83  ? 127 CYS C SG  1 
ATOM   4566  N  N   . ASP C  1 137 ? -6.447  -52.262 48.661 1.00 62.79  ? 128 ASP C N   1 
ATOM   4567  C  CA  . ASP C  1 137 ? -6.158  -53.659 48.378 1.00 61.27  ? 128 ASP C CA  1 
ATOM   4568  C  C   . ASP C  1 137 ? -7.415  -54.315 47.840 1.00 63.58  ? 128 ASP C C   1 
ATOM   4569  O  O   . ASP C  1 137 ? -8.404  -54.465 48.570 1.00 60.14  ? 128 ASP C O   1 
ATOM   4570  C  CB  . ASP C  1 137 ? -5.670  -54.396 49.626 1.00 64.33  ? 128 ASP C CB  1 
ATOM   4571  C  CG  . ASP C  1 137 ? -5.385  -55.881 49.357 1.00 70.45  ? 128 ASP C CG  1 
ATOM   4572  O  OD1 . ASP C  1 137 ? -5.495  -56.308 48.182 1.00 68.12  ? 128 ASP C OD1 1 
ATOM   4573  O  OD2 . ASP C  1 137 ? -5.039  -56.623 50.305 1.00 66.51  ? 128 ASP C OD2 1 
ATOM   4574  N  N   . PRO C  1 138 ? -7.379  -54.685 46.549 1.00 62.00  ? 129 PRO C N   1 
ATOM   4575  C  CA  . PRO C  1 138 ? -8.548  -55.204 45.839 1.00 66.80  ? 129 PRO C CA  1 
ATOM   4576  C  C   . PRO C  1 138 ? -8.964  -56.638 46.154 1.00 75.82  ? 129 PRO C C   1 
ATOM   4577  O  O   . PRO C  1 138 ? -9.877  -57.170 45.523 1.00 76.32  ? 129 PRO C O   1 
ATOM   4578  C  CB  . PRO C  1 138 ? -8.215  -54.864 44.384 1.00 62.14  ? 129 PRO C CB  1 
ATOM   4579  C  CG  . PRO C  1 138 ? -6.705  -54.960 44.315 1.00 57.00  ? 129 PRO C CG  1 
ATOM   4580  C  CD  . PRO C  1 138 ? -6.172  -54.676 45.702 1.00 60.63  ? 129 PRO C CD  1 
ATOM   4581  N  N   . THR C  1 139 ? -8.358  -57.216 47.182 1.00 70.77  ? 130 THR C N   1 
ATOM   4582  C  CA  . THR C  1 139 ? -8.598  -58.599 47.520 1.00 68.28  ? 130 THR C CA  1 
ATOM   4583  C  C   . THR C  1 139 ? -10.032 -59.079 47.631 1.00 71.14  ? 130 THR C C   1 
ATOM   4584  O  O   . THR C  1 139 ? -10.874 -58.414 48.238 1.00 62.87  ? 130 THR C O   1 
ATOM   4585  C  CB  . THR C  1 139 ? -7.819  -58.911 48.805 1.00 70.96  ? 130 THR C CB  1 
ATOM   4586  O  OG1 . THR C  1 139 ? -6.427  -59.042 48.492 1.00 71.26  ? 130 THR C OG1 1 
ATOM   4587  C  CG2 . THR C  1 139 ? -8.303  -60.201 49.433 1.00 60.77  ? 130 THR C CG2 1 
ATOM   4588  N  N   . GLY C  1 140 ? -10.309 -60.232 47.031 1.00 70.45  ? 131 GLY C N   1 
ATOM   4589  C  CA  . GLY C  1 140 ? -11.655 -60.767 47.040 1.00 76.96  ? 131 GLY C CA  1 
ATOM   4590  C  C   . GLY C  1 140 ? -12.597 -59.863 46.270 1.00 75.36  ? 131 GLY C C   1 
ATOM   4591  O  O   . GLY C  1 140 ? -13.793 -59.797 46.555 1.00 73.45  ? 131 GLY C O   1 
ATOM   4592  N  N   . VAL C  1 141 ? -12.038 -59.137 45.305 1.00 79.13  ? 132 VAL C N   1 
ATOM   4593  C  CA  . VAL C  1 141 ? -12.830 -58.456 44.290 1.00 72.27  ? 132 VAL C CA  1 
ATOM   4594  C  C   . VAL C  1 141 ? -13.373 -59.528 43.344 1.00 76.07  ? 132 VAL C C   1 
ATOM   4595  O  O   . VAL C  1 141 ? -14.335 -59.286 42.622 1.00 73.47  ? 132 VAL C O   1 
ATOM   4596  C  CB  . VAL C  1 141 ? -11.991 -57.414 43.513 1.00 63.37  ? 132 VAL C CB  1 
ATOM   4597  C  CG1 . VAL C  1 141 ? -11.040 -58.096 42.549 1.00 64.60  ? 132 VAL C CG1 1 
ATOM   4598  C  CG2 . VAL C  1 141 ? -12.894 -56.468 42.772 1.00 67.10  ? 132 VAL C CG2 1 
ATOM   4599  N  N   . ASP C  1 142 ? -12.733 -60.708 43.383 1.00 84.03  ? 133 ASP C N   1 
ATOM   4600  C  CA  . ASP C  1 142 ? -13.154 -61.941 42.702 1.00 80.51  ? 133 ASP C CA  1 
ATOM   4601  C  C   . ASP C  1 142 ? -14.389 -62.515 43.359 1.00 78.85  ? 133 ASP C C   1 
ATOM   4602  O  O   . ASP C  1 142 ? -15.284 -63.028 42.700 1.00 76.51  ? 133 ASP C O   1 
ATOM   4603  C  CB  . ASP C  1 142 ? -12.077 -63.018 42.833 1.00 82.78  ? 133 ASP C CB  1 
ATOM   4604  C  CG  . ASP C  1 142 ? -10.815 -62.690 42.074 1.00 98.35  ? 133 ASP C CG  1 
ATOM   4605  O  OD1 . ASP C  1 142 ? -10.415 -61.508 42.084 1.00 101.82 ? 133 ASP C OD1 1 
ATOM   4606  O  OD2 . ASP C  1 142 ? -10.219 -63.617 41.471 1.00 100.60 ? 133 ASP C OD2 1 
ATOM   4607  N  N   . SER C  1 143 ? -14.416 -62.439 44.680 1.00 78.84  ? 134 SER C N   1 
ATOM   4608  C  CA  . SER C  1 143 ? -15.525 -62.960 45.451 1.00 83.35  ? 134 SER C CA  1 
ATOM   4609  C  C   . SER C  1 143 ? -16.799 -62.284 45.005 1.00 81.35  ? 134 SER C C   1 
ATOM   4610  O  O   . SER C  1 143 ? -16.769 -61.176 44.494 1.00 82.02  ? 134 SER C O   1 
ATOM   4611  C  CB  . SER C  1 143 ? -15.301 -62.721 46.946 1.00 83.30  ? 134 SER C CB  1 
ATOM   4612  O  OG  . SER C  1 143 ? -14.233 -63.521 47.437 1.00 94.17  ? 134 SER C OG  1 
ATOM   4613  N  N   . GLU C  1 144 ? -17.916 -62.982 45.130 1.00 91.57  ? 135 GLU C N   1 
ATOM   4614  C  CA  . GLU C  1 144 ? -19.203 -62.349 44.921 1.00 91.87  ? 135 GLU C CA  1 
ATOM   4615  C  C   . GLU C  1 144 ? -19.356 -61.271 45.996 1.00 88.57  ? 135 GLU C C   1 
ATOM   4616  O  O   . GLU C  1 144 ? -20.178 -60.367 45.864 1.00 82.21  ? 135 GLU C O   1 
ATOM   4617  C  CB  . GLU C  1 144 ? -20.344 -63.379 44.982 1.00 94.59  ? 135 GLU C CB  1 
ATOM   4618  C  CG  . GLU C  1 144 ? -20.257 -64.503 43.929 1.00 102.35 ? 135 GLU C CG  1 
ATOM   4619  C  CD  . GLU C  1 144 ? -19.642 -65.810 44.461 1.00 113.42 ? 135 GLU C CD  1 
ATOM   4620  O  OE1 . GLU C  1 144 ? -18.736 -66.370 43.801 1.00 106.94 ? 135 GLU C OE1 1 
ATOM   4621  O  OE2 . GLU C  1 144 ? -20.076 -66.293 45.529 1.00 111.51 ? 135 GLU C OE2 1 
ATOM   4622  N  N   . GLU C  1 145 ? -18.535 -61.364 47.046 1.00 88.24  ? 136 GLU C N   1 
ATOM   4623  C  CA  . GLU C  1 145 ? -18.607 -60.441 48.187 1.00 88.49  ? 136 GLU C CA  1 
ATOM   4624  C  C   . GLU C  1 145 ? -17.808 -59.132 48.047 1.00 79.02  ? 136 GLU C C   1 
ATOM   4625  O  O   . GLU C  1 145 ? -18.013 -58.203 48.815 1.00 74.90  ? 136 GLU C O   1 
ATOM   4626  C  CB  . GLU C  1 145 ? -18.213 -61.159 49.486 1.00 86.69  ? 136 GLU C CB  1 
ATOM   4627  C  CG  . GLU C  1 145 ? -19.140 -62.297 49.885 0.00 94.71  ? 136 GLU C CG  1 
ATOM   4628  C  CD  . GLU C  1 145 ? -18.931 -63.548 49.051 0.00 97.20  ? 136 GLU C CD  1 
ATOM   4629  O  OE1 . GLU C  1 145 ? -18.051 -63.540 48.166 0.00 95.32  ? 136 GLU C OE1 1 
ATOM   4630  O  OE2 . GLU C  1 145 ? -19.646 -64.546 49.283 0.00 102.44 ? 136 GLU C OE2 1 
ATOM   4631  N  N   . GLY C  1 146 ? -16.905 -59.062 47.074 1.00 78.49  ? 137 GLY C N   1 
ATOM   4632  C  CA  . GLY C  1 146 ? -16.245 -57.815 46.722 1.00 68.07  ? 137 GLY C CA  1 
ATOM   4633  C  C   . GLY C  1 146 ? -15.089 -57.373 47.597 1.00 75.00  ? 137 GLY C C   1 
ATOM   4634  O  O   . GLY C  1 146 ? -14.764 -58.022 48.593 1.00 73.20  ? 137 GLY C O   1 
ATOM   4635  N  N   . ALA C  1 147 ? -14.456 -56.264 47.216 1.00 72.22  ? 138 ALA C N   1 
ATOM   4636  C  CA  . ALA C  1 147 ? -13.438 -55.661 48.065 1.00 72.21  ? 138 ALA C CA  1 
ATOM   4637  C  C   . ALA C  1 147 ? -14.023 -54.446 48.768 1.00 67.14  ? 138 ALA C C   1 
ATOM   4638  O  O   . ALA C  1 147 ? -15.130 -54.014 48.465 1.00 62.73  ? 138 ALA C O   1 
ATOM   4639  C  CB  . ALA C  1 147 ? -12.228 -55.250 47.230 1.00 60.48  ? 138 ALA C CB  1 
ATOM   4640  N  N   . THR C  1 148 ? -13.247 -53.861 49.672 1.00 69.85  ? 139 THR C N   1 
ATOM   4641  C  CA  . THR C  1 148 ? -13.660 -52.634 50.337 1.00 63.59  ? 139 THR C CA  1 
ATOM   4642  C  C   . THR C  1 148 ? -12.472 -51.709 50.461 1.00 57.61  ? 139 THR C C   1 
ATOM   4643  O  O   . THR C  1 148 ? -11.390 -52.105 50.888 1.00 52.59  ? 139 THR C O   1 
ATOM   4644  C  CB  . THR C  1 148 ? -14.263 -52.874 51.729 1.00 59.52  ? 139 THR C CB  1 
ATOM   4645  O  OG1 . THR C  1 148 ? -15.480 -53.605 51.598 1.00 74.43  ? 139 THR C OG1 1 
ATOM   4646  C  CG2 . THR C  1 148 ? -14.590 -51.554 52.386 1.00 57.78  ? 139 THR C CG2 1 
ATOM   4647  N  N   . CYS C  1 149 ? -12.683 -50.467 50.067 1.00 59.32  ? 140 CYS C N   1 
ATOM   4648  C  CA  . CYS C  1 149 ? -11.643 -49.473 50.180 1.00 60.82  ? 140 CYS C CA  1 
ATOM   4649  C  C   . CYS C  1 149 ? -12.186 -48.174 50.713 1.00 56.43  ? 140 CYS C C   1 
ATOM   4650  O  O   . CYS C  1 149 ? -13.387 -47.896 50.635 1.00 53.37  ? 140 CYS C O   1 
ATOM   4651  C  CB  . CYS C  1 149 ? -11.007 -49.236 48.819 1.00 65.99  ? 140 CYS C CB  1 
ATOM   4652  S  SG  . CYS C  1 149 ? -9.986  -50.606 48.271 1.00 71.50  ? 140 CYS C SG  1 
ATOM   4653  N  N   . ALA C  1 150 ? -11.287 -47.378 51.265 1.00 54.53  ? 141 ALA C N   1 
ATOM   4654  C  CA  . ALA C  1 150 ? -11.657 -46.057 51.722 1.00 55.28  ? 141 ALA C CA  1 
ATOM   4655  C  C   . ALA C  1 150 ? -10.533 -45.069 51.476 1.00 58.01  ? 141 ALA C C   1 
ATOM   4656  O  O   . ALA C  1 150 ? -9.354  -45.419 51.403 1.00 53.85  ? 141 ALA C O   1 
ATOM   4657  C  CB  . ALA C  1 150 ? -12.068 -46.077 53.185 1.00 48.96  ? 141 ALA C CB  1 
ATOM   4658  N  N   . VAL C  1 151 ? -10.928 -43.821 51.310 1.00 57.61  ? 142 VAL C N   1 
ATOM   4659  C  CA  . VAL C  1 151 ? -9.982  -42.750 51.105 1.00 56.86  ? 142 VAL C CA  1 
ATOM   4660  C  C   . VAL C  1 151 ? -10.494 -41.554 51.889 1.00 53.72  ? 142 VAL C C   1 
ATOM   4661  O  O   . VAL C  1 151 ? -11.685 -41.254 51.858 1.00 55.14  ? 142 VAL C O   1 
ATOM   4662  C  CB  . VAL C  1 151 ? -9.782  -42.466 49.567 1.00 61.31  ? 142 VAL C CB  1 
ATOM   4663  C  CG1 . VAL C  1 151 ? -11.095 -42.623 48.785 1.00 55.88  ? 142 VAL C CG1 1 
ATOM   4664  C  CG2 . VAL C  1 151 ? -9.119  -41.117 49.310 1.00 52.04  ? 142 VAL C CG2 1 
ATOM   4665  N  N   . LYS C  1 152 ? -9.586  -40.874 52.581 1.00 57.21  ? 143 LYS C N   1 
ATOM   4666  C  CA  A LYS C  1 152 ? -9.935  -39.696 53.367 0.50 57.86  ? 143 LYS C CA  1 
ATOM   4667  C  CA  B LYS C  1 152 ? -9.935  -39.694 53.364 0.50 57.86  ? 143 LYS C CA  1 
ATOM   4668  C  C   . LYS C  1 152 ? -9.705  -38.388 52.608 1.00 60.22  ? 143 LYS C C   1 
ATOM   4669  O  O   . LYS C  1 152 ? -8.733  -38.239 51.867 1.00 56.23  ? 143 LYS C O   1 
ATOM   4670  C  CB  A LYS C  1 152 ? -9.126  -39.666 54.666 0.50 65.51  ? 143 LYS C CB  1 
ATOM   4671  C  CB  B LYS C  1 152 ? -9.157  -39.679 54.682 0.50 65.51  ? 143 LYS C CB  1 
ATOM   4672  C  CG  A LYS C  1 152 ? -9.369  -40.859 55.576 0.50 72.37  ? 143 LYS C CG  1 
ATOM   4673  C  CG  B LYS C  1 152 ? -9.843  -40.422 55.816 0.50 71.00  ? 143 LYS C CG  1 
ATOM   4674  C  CD  A LYS C  1 152 ? -9.950  -40.426 56.912 0.50 75.00  ? 143 LYS C CD  1 
ATOM   4675  C  CD  B LYS C  1 152 ? -8.839  -40.885 56.860 0.50 77.84  ? 143 LYS C CD  1 
ATOM   4676  C  CE  A LYS C  1 152 ? -9.976  -41.578 57.903 0.50 79.68  ? 143 LYS C CE  1 
ATOM   4677  C  CE  B LYS C  1 152 ? -9.342  -42.110 57.605 0.50 81.63  ? 143 LYS C CE  1 
ATOM   4678  N  NZ  A LYS C  1 152 ? -11.170 -41.522 58.790 0.50 71.40  ? 143 LYS C NZ  1 
ATOM   4679  N  NZ  B LYS C  1 152 ? -8.342  -43.213 57.600 0.50 78.93  ? 143 LYS C NZ  1 
ATOM   4680  N  N   . PHE C  1 153 ? -10.615 -37.442 52.808 1.00 62.04  ? 144 PHE C N   1 
ATOM   4681  C  CA  . PHE C  1 153 ? -10.486 -36.107 52.252 1.00 53.31  ? 144 PHE C CA  1 
ATOM   4682  C  C   . PHE C  1 153 ? -10.601 -35.082 53.372 1.00 54.13  ? 144 PHE C C   1 
ATOM   4683  O  O   . PHE C  1 153 ? -11.486 -35.171 54.201 1.00 56.19  ? 144 PHE C O   1 
ATOM   4684  C  CB  . PHE C  1 153 ? -11.618 -35.863 51.263 1.00 53.81  ? 144 PHE C CB  1 
ATOM   4685  C  CG  . PHE C  1 153 ? -11.506 -36.662 50.009 1.00 52.42  ? 144 PHE C CG  1 
ATOM   4686  C  CD1 . PHE C  1 153 ? -11.039 -36.084 48.851 1.00 51.59  ? 144 PHE C CD1 1 
ATOM   4687  C  CD2 . PHE C  1 153 ? -11.862 -37.983 49.986 1.00 50.36  ? 144 PHE C CD2 1 
ATOM   4688  C  CE1 . PHE C  1 153 ? -10.925 -36.808 47.704 1.00 46.25  ? 144 PHE C CE1 1 
ATOM   4689  C  CE2 . PHE C  1 153 ? -11.751 -38.704 48.839 1.00 53.52  ? 144 PHE C CE2 1 
ATOM   4690  C  CZ  . PHE C  1 153 ? -11.280 -38.108 47.694 1.00 50.57  ? 144 PHE C CZ  1 
ATOM   4691  N  N   . GLY C  1 154 ? -9.721  -34.096 53.392 1.00 55.83  ? 145 GLY C N   1 
ATOM   4692  C  CA  . GLY C  1 154 ? -9.856  -32.999 54.333 1.00 57.08  ? 145 GLY C CA  1 
ATOM   4693  C  C   . GLY C  1 154 ? -8.977  -31.834 53.939 1.00 55.55  ? 145 GLY C C   1 
ATOM   4694  O  O   . GLY C  1 154 ? -8.341  -31.882 52.890 1.00 56.60  ? 145 GLY C O   1 
ATOM   4695  N  N   . SER C  1 155 ? -8.917  -30.787 54.753 1.00 46.37  ? 146 SER C N   1 
ATOM   4696  C  CA  . SER C  1 155 ? -7.954  -29.754 54.432 1.00 52.77  ? 146 SER C CA  1 
ATOM   4697  C  C   . SER C  1 155 ? -6.568  -30.296 54.686 1.00 49.15  ? 146 SER C C   1 
ATOM   4698  O  O   . SER C  1 155 ? -6.384  -31.152 55.527 1.00 54.54  ? 146 SER C O   1 
ATOM   4699  C  CB  . SER C  1 155 ? -8.180  -28.468 55.206 1.00 53.65  ? 146 SER C CB  1 
ATOM   4700  O  OG  . SER C  1 155 ? -7.441  -27.433 54.596 1.00 48.19  ? 146 SER C OG  1 
ATOM   4701  N  N   . TRP C  1 156 ? -5.603  -29.864 53.895 1.00 57.67  ? 147 TRP C N   1 
ATOM   4702  C  CA  . TRP C  1 156 ? -4.231  -30.244 54.149 1.00 54.22  ? 147 TRP C CA  1 
ATOM   4703  C  C   . TRP C  1 156 ? -3.594  -29.400 55.248 1.00 59.77  ? 147 TRP C C   1 
ATOM   4704  O  O   . TRP C  1 156 ? -2.929  -29.927 56.134 1.00 60.88  ? 147 TRP C O   1 
ATOM   4705  C  CB  . TRP C  1 156 ? -3.400  -30.158 52.869 1.00 53.49  ? 147 TRP C CB  1 
ATOM   4706  C  CG  . TRP C  1 156 ? -2.033  -30.711 53.059 1.00 54.38  ? 147 TRP C CG  1 
ATOM   4707  C  CD1 . TRP C  1 156 ? -0.865  -30.019 53.087 1.00 56.02  ? 147 TRP C CD1 1 
ATOM   4708  C  CD2 . TRP C  1 156 ? -1.694  -32.080 53.288 1.00 56.31  ? 147 TRP C CD2 1 
ATOM   4709  N  NE1 . TRP C  1 156 ? 0.187   -30.875 53.308 1.00 52.00  ? 147 TRP C NE1 1 
ATOM   4710  C  CE2 . TRP C  1 156 ? -0.298  -32.147 53.433 1.00 48.77  ? 147 TRP C CE2 1 
ATOM   4711  C  CE3 . TRP C  1 156 ? -2.436  -33.259 53.367 1.00 55.89  ? 147 TRP C CE3 1 
ATOM   4712  C  CZ2 . TRP C  1 156 ? 0.367   -33.332 53.649 1.00 49.25  ? 147 TRP C CZ2 1 
ATOM   4713  C  CZ3 . TRP C  1 156 ? -1.778  -34.431 53.582 1.00 53.55  ? 147 TRP C CZ3 1 
ATOM   4714  C  CH2 . TRP C  1 156 ? -0.389  -34.465 53.723 1.00 59.44  ? 147 TRP C CH2 1 
ATOM   4715  N  N   . SER C  1 157 ? -3.753  -28.081 55.139 1.00 60.28  ? 148 SER C N   1 
ATOM   4716  C  CA  . SER C  1 157 ? -3.156  -27.133 56.084 1.00 60.29  ? 148 SER C CA  1 
ATOM   4717  C  C   . SER C  1 157 ? -4.059  -26.556 57.192 1.00 62.93  ? 148 SER C C   1 
ATOM   4718  O  O   . SER C  1 157 ? -3.576  -25.848 58.064 1.00 60.89  ? 148 SER C O   1 
ATOM   4719  C  CB  . SER C  1 157 ? -2.502  -25.976 55.315 1.00 60.62  ? 148 SER C CB  1 
ATOM   4720  O  OG  . SER C  1 157 ? -1.573  -26.453 54.348 1.00 64.98  ? 148 SER C OG  1 
ATOM   4721  N  N   . TYR C  1 158 ? -5.348  -26.867 57.188 1.00 63.50  ? 149 TYR C N   1 
ATOM   4722  C  CA  . TYR C  1 158 ? -6.261  -26.210 58.113 1.00 55.24  ? 149 TYR C CA  1 
ATOM   4723  C  C   . TYR C  1 158 ? -6.904  -27.165 59.112 1.00 61.62  ? 149 TYR C C   1 
ATOM   4724  O  O   . TYR C  1 158 ? -7.272  -28.298 58.775 1.00 55.57  ? 149 TYR C O   1 
ATOM   4725  C  CB  . TYR C  1 158 ? -7.373  -25.484 57.355 1.00 56.76  ? 149 TYR C CB  1 
ATOM   4726  C  CG  . TYR C  1 158 ? -6.989  -24.205 56.627 1.00 65.42  ? 149 TYR C CG  1 
ATOM   4727  C  CD1 . TYR C  1 158 ? -6.900  -22.992 57.298 1.00 64.16  ? 149 TYR C CD1 1 
ATOM   4728  C  CD2 . TYR C  1 158 ? -6.769  -24.201 55.255 1.00 60.35  ? 149 TYR C CD2 1 
ATOM   4729  C  CE1 . TYR C  1 158 ? -6.578  -21.824 56.630 1.00 56.51  ? 149 TYR C CE1 1 
ATOM   4730  C  CE2 . TYR C  1 158 ? -6.446  -23.036 54.581 1.00 63.80  ? 149 TYR C CE2 1 
ATOM   4731  C  CZ  . TYR C  1 158 ? -6.349  -21.853 55.274 1.00 62.44  ? 149 TYR C CZ  1 
ATOM   4732  O  OH  . TYR C  1 158 ? -6.028  -20.697 54.605 1.00 62.14  ? 149 TYR C OH  1 
ATOM   4733  N  N   . GLY C  1 159 ? -7.068  -26.676 60.338 1.00 58.68  ? 150 GLY C N   1 
ATOM   4734  C  CA  . GLY C  1 159 ? -7.770  -27.415 61.368 1.00 63.87  ? 150 GLY C CA  1 
ATOM   4735  C  C   . GLY C  1 159 ? -9.232  -27.033 61.471 1.00 63.46  ? 150 GLY C C   1 
ATOM   4736  O  O   . GLY C  1 159 ? -9.675  -26.107 60.813 1.00 63.73  ? 150 GLY C O   1 
ATOM   4737  N  N   . GLY C  1 160 ? -9.972  -27.736 62.322 1.00 66.00  ? 151 GLY C N   1 
ATOM   4738  C  CA  . GLY C  1 160 ? -11.417 -27.607 62.404 1.00 59.13  ? 151 GLY C CA  1 
ATOM   4739  C  C   . GLY C  1 160 ? -11.945 -26.268 62.867 1.00 63.37  ? 151 GLY C C   1 
ATOM   4740  O  O   . GLY C  1 160 ? -13.114 -25.940 62.663 1.00 62.81  ? 151 GLY C O   1 
ATOM   4741  N  N   . TRP C  1 161 ? -11.111 -25.469 63.484 1.00 60.92  ? 152 TRP C N   1 
ATOM   4742  C  CA  . TRP C  1 161 ? -11.586 -24.191 63.940 1.00 63.46  ? 152 TRP C CA  1 
ATOM   4743  C  C   . TRP C  1 161 ? -11.413 -23.168 62.893 1.00 61.86  ? 152 TRP C C   1 
ATOM   4744  O  O   . TRP C  1 161 ? -11.750 -22.038 63.106 1.00 67.88  ? 152 TRP C O   1 
ATOM   4745  C  CB  . TRP C  1 161 ? -10.837 -23.705 65.154 1.00 77.16  ? 152 TRP C CB  1 
ATOM   4746  C  CG  . TRP C  1 161 ? -11.114 -24.417 66.392 1.00 78.95  ? 152 TRP C CG  1 
ATOM   4747  C  CD1 . TRP C  1 161 ? -12.237 -25.074 66.727 1.00 81.17  ? 152 TRP C CD1 1 
ATOM   4748  C  CD2 . TRP C  1 161 ? -10.249 -24.505 67.500 1.00 85.24  ? 152 TRP C CD2 1 
ATOM   4749  N  NE1 . TRP C  1 161 ? -12.118 -25.601 67.975 1.00 79.16  ? 152 TRP C NE1 1 
ATOM   4750  C  CE2 . TRP C  1 161 ? -10.897 -25.255 68.473 1.00 84.10  ? 152 TRP C CE2 1 
ATOM   4751  C  CE3 . TRP C  1 161 ? -8.970  -24.032 67.757 1.00 84.39  ? 152 TRP C CE3 1 
ATOM   4752  C  CZ2 . TRP C  1 161 ? -10.323 -25.539 69.678 1.00 85.98  ? 152 TRP C CZ2 1 
ATOM   4753  C  CZ3 . TRP C  1 161 ? -8.404  -24.317 68.937 1.00 87.70  ? 152 TRP C CZ3 1 
ATOM   4754  C  CH2 . TRP C  1 161 ? -9.071  -25.065 69.891 1.00 88.80  ? 152 TRP C CH2 1 
ATOM   4755  N  N   . GLU C  1 162 ? -10.830 -23.562 61.777 1.00 61.94  ? 153 GLU C N   1 
ATOM   4756  C  CA  . GLU C  1 162 ? -10.615 -22.665 60.661 1.00 63.69  ? 153 GLU C CA  1 
ATOM   4757  C  C   . GLU C  1 162 ? -11.438 -23.075 59.467 1.00 58.88  ? 153 GLU C C   1 
ATOM   4758  O  O   . GLU C  1 162 ? -12.015 -22.270 58.783 1.00 55.55  ? 153 GLU C O   1 
ATOM   4759  C  CB  . GLU C  1 162 ? -9.161  -22.704 60.227 1.00 60.78  ? 153 GLU C CB  1 
ATOM   4760  C  CG  . GLU C  1 162 ? -8.195  -22.256 61.268 1.00 61.04  ? 153 GLU C CG  1 
ATOM   4761  C  CD  . GLU C  1 162 ? -7.702  -23.390 62.086 1.00 72.21  ? 153 GLU C CD  1 
ATOM   4762  O  OE1 . GLU C  1 162 ? -7.970  -23.395 63.293 1.00 82.36  ? 153 GLU C OE1 1 
ATOM   4763  O  OE2 . GLU C  1 162 ? -7.039  -24.294 61.531 1.00 80.47  ? 153 GLU C OE2 1 
ATOM   4764  N  N   . ILE C  1 163 ? -11.500 -24.370 59.235 1.00 55.18  ? 154 ILE C N   1 
ATOM   4765  C  CA  . ILE C  1 163 ? -12.356 -24.929 58.226 1.00 60.13  ? 154 ILE C CA  1 
ATOM   4766  C  C   . ILE C  1 163 ? -13.024 -26.165 58.762 1.00 63.92  ? 154 ILE C C   1 
ATOM   4767  O  O   . ILE C  1 163 ? -12.380 -27.151 59.001 1.00 61.70  ? 154 ILE C O   1 
ATOM   4768  C  CB  . ILE C  1 163 ? -11.567 -25.415 57.031 1.00 68.26  ? 154 ILE C CB  1 
ATOM   4769  C  CG1 . ILE C  1 163 ? -10.554 -24.398 56.570 1.00 64.62  ? 154 ILE C CG1 1 
ATOM   4770  C  CG2 . ILE C  1 163 ? -12.465 -25.627 55.889 1.00 57.17  ? 154 ILE C CG2 1 
ATOM   4771  C  CD1 . ILE C  1 163 ? -10.227 -24.551 55.169 1.00 53.67  ? 154 ILE C CD1 1 
ATOM   4772  N  N   . ASP C  1 164 ? -14.325 -26.132 58.902 1.00 59.96  ? 155 ASP C N   1 
ATOM   4773  C  CA  . ASP C  1 164 ? -15.072 -27.281 59.391 1.00 61.41  ? 155 ASP C CA  1 
ATOM   4774  C  C   . ASP C  1 164 ? -15.655 -28.006 58.195 1.00 64.86  ? 155 ASP C C   1 
ATOM   4775  O  O   . ASP C  1 164 ? -16.229 -27.381 57.310 1.00 65.86  ? 155 ASP C O   1 
ATOM   4776  C  CB  . ASP C  1 164 ? -16.191 -26.837 60.333 1.00 63.89  ? 155 ASP C CB  1 
ATOM   4777  C  CG  . ASP C  1 164 ? -17.037 -27.996 60.824 1.00 72.36  ? 155 ASP C CG  1 
ATOM   4778  O  OD1 . ASP C  1 164 ? -16.465 -29.049 61.191 1.00 67.68  ? 155 ASP C OD1 1 
ATOM   4779  O  OD2 . ASP C  1 164 ? -18.280 -27.846 60.837 1.00 77.17  ? 155 ASP C OD2 1 
ATOM   4780  N  N   . LEU C  1 165 ? -15.507 -29.327 58.177 1.00 65.90  ? 156 LEU C N   1 
ATOM   4781  C  CA  . LEU C  1 165 ? -15.866 -30.136 57.020 1.00 58.55  ? 156 LEU C CA  1 
ATOM   4782  C  C   . LEU C  1 165 ? -17.178 -30.871 57.238 1.00 61.86  ? 156 LEU C C   1 
ATOM   4783  O  O   . LEU C  1 165 ? -17.365 -31.520 58.254 1.00 64.43  ? 156 LEU C O   1 
ATOM   4784  C  CB  . LEU C  1 165 ? -14.751 -31.138 56.758 1.00 58.88  ? 156 LEU C CB  1 
ATOM   4785  C  CG  . LEU C  1 165 ? -14.227 -31.243 55.337 1.00 59.84  ? 156 LEU C CG  1 
ATOM   4786  C  CD1 . LEU C  1 165 ? -14.399 -29.917 54.627 1.00 65.07  ? 156 LEU C CD1 1 
ATOM   4787  C  CD2 . LEU C  1 165 ? -12.777 -31.655 55.375 1.00 60.79  ? 156 LEU C CD2 1 
ATOM   4788  N  N   . LYS C  1 166 ? -18.087 -30.773 56.275 1.00 65.67  ? 157 LYS C N   1 
ATOM   4789  C  CA  . LYS C  1 166 ? -19.403 -31.398 56.389 1.00 66.38  ? 157 LYS C CA  1 
ATOM   4790  C  C   . LYS C  1 166 ? -19.860 -32.049 55.086 1.00 60.24  ? 157 LYS C C   1 
ATOM   4791  O  O   . LYS C  1 166 ? -19.281 -31.846 54.032 1.00 60.85  ? 157 LYS C O   1 
ATOM   4792  C  CB  . LYS C  1 166 ? -20.460 -30.401 56.891 1.00 64.03  ? 157 LYS C CB  1 
ATOM   4793  C  CG  . LYS C  1 166 ? -20.089 -29.720 58.202 1.00 67.59  ? 157 LYS C CG  1 
ATOM   4794  C  CD  . LYS C  1 166 ? -21.290 -29.135 58.926 1.00 68.49  ? 157 LYS C CD  1 
ATOM   4795  C  CE  . LYS C  1 166 ? -21.815 -30.104 59.986 1.00 85.32  ? 157 LYS C CE  1 
ATOM   4796  N  NZ  . LYS C  1 166 ? -22.883 -29.506 60.857 1.00 80.95  ? 157 LYS C NZ  1 
ATOM   4797  N  N   . THR C  1 167 ? -20.906 -32.850 55.193 1.00 68.48  ? 158 THR C N   1 
ATOM   4798  C  CA  . THR C  1 167 ? -21.433 -33.619 54.092 1.00 64.67  ? 158 THR C CA  1 
ATOM   4799  C  C   . THR C  1 167 ? -22.928 -33.427 54.110 1.00 80.67  ? 158 THR C C   1 
ATOM   4800  O  O   . THR C  1 167 ? -23.531 -33.354 55.194 1.00 79.32  ? 158 THR C O   1 
ATOM   4801  C  CB  . THR C  1 167 ? -21.188 -35.099 54.323 1.00 65.10  ? 158 THR C CB  1 
ATOM   4802  O  OG1 . THR C  1 167 ? -19.834 -35.421 54.003 1.00 68.19  ? 158 THR C OG1 1 
ATOM   4803  C  CG2 . THR C  1 167 ? -22.073 -35.898 53.454 1.00 72.70  ? 158 THR C CG2 1 
ATOM   4804  N  N   . ASP C  1 168 ? -23.535 -33.348 52.925 1.00 83.56  ? 159 ASP C N   1 
ATOM   4805  C  CA  A ASP C  1 168 ? -24.983 -33.165 52.891 0.60 88.86  ? 159 ASP C CA  1 
ATOM   4806  C  CA  B ASP C  1 168 ? -24.982 -33.183 52.758 0.40 88.69  ? 159 ASP C CA  1 
ATOM   4807  C  C   . ASP C  1 168 ? -25.747 -34.472 53.093 1.00 91.49  ? 159 ASP C C   1 
ATOM   4808  O  O   . ASP C  1 168 ? -26.828 -34.461 53.690 1.00 92.46  ? 159 ASP C O   1 
ATOM   4809  C  CB  A ASP C  1 168 ? -25.462 -32.404 51.649 0.60 89.03  ? 159 ASP C CB  1 
ATOM   4810  C  CB  B ASP C  1 168 ? -25.305 -32.782 51.307 0.40 87.25  ? 159 ASP C CB  1 
ATOM   4811  C  CG  A ASP C  1 168 ? -26.553 -31.386 51.981 0.60 91.38  ? 159 ASP C CG  1 
ATOM   4812  C  CG  B ASP C  1 168 ? -24.202 -31.952 50.655 0.40 82.96  ? 159 ASP C CG  1 
ATOM   4813  O  OD1 A ASP C  1 168 ? -27.489 -31.221 51.169 0.60 90.95  ? 159 ASP C OD1 1 
ATOM   4814  O  OD1 B ASP C  1 168 ? -23.014 -32.296 50.812 0.40 77.25  ? 159 ASP C OD1 1 
ATOM   4815  O  OD2 A ASP C  1 168 ? -26.475 -30.755 53.061 0.60 79.56  ? 159 ASP C OD2 1 
ATOM   4816  O  OD2 B ASP C  1 168 ? -24.525 -30.958 49.969 0.40 82.91  ? 159 ASP C OD2 1 
ATOM   4817  N  N   . THR C  1 169 ? -25.177 -35.587 52.652 1.00 82.12  ? 160 THR C N   1 
ATOM   4818  C  CA  . THR C  1 169 ? -25.791 -36.887 52.820 1.00 76.88  ? 160 THR C CA  1 
ATOM   4819  C  C   . THR C  1 169 ? -24.677 -37.860 53.049 1.00 75.57  ? 160 THR C C   1 
ATOM   4820  O  O   . THR C  1 169 ? -23.602 -37.687 52.501 1.00 79.74  ? 160 THR C O   1 
ATOM   4821  C  CB  . THR C  1 169 ? -26.515 -37.307 51.532 1.00 82.29  ? 160 THR C CB  1 
ATOM   4822  O  OG1 . THR C  1 169 ? -27.646 -36.452 51.328 1.00 92.25  ? 160 THR C OG1 1 
ATOM   4823  C  CG2 . THR C  1 169 ? -26.982 -38.769 51.600 1.00 73.52  ? 160 THR C CG2 1 
ATOM   4824  N  N   . ASP C  1 170 ? -24.930 -38.907 53.822 1.00 73.37  ? 161 ASP C N   1 
ATOM   4825  C  CA  . ASP C  1 170 ? -23.916 -39.939 54.027 1.00 73.17  ? 161 ASP C CA  1 
ATOM   4826  C  C   . ASP C  1 170 ? -23.947 -40.933 52.873 1.00 75.46  ? 161 ASP C C   1 
ATOM   4827  O  O   . ASP C  1 170 ? -23.200 -41.923 52.877 1.00 76.48  ? 161 ASP C O   1 
ATOM   4828  C  CB  . ASP C  1 170 ? -24.107 -40.665 55.361 1.00 75.22  ? 161 ASP C CB  1 
ATOM   4829  C  CG  . ASP C  1 170 ? -23.665 -39.823 56.552 1.00 86.53  ? 161 ASP C CG  1 
ATOM   4830  O  OD1 . ASP C  1 170 ? -23.505 -38.582 56.387 1.00 80.50  ? 161 ASP C OD1 1 
ATOM   4831  O  OD2 . ASP C  1 170 ? -23.486 -40.405 57.652 1.00 79.94  ? 161 ASP C OD2 1 
ATOM   4832  N  N   . GLN C  1 171 ? -24.829 -40.665 51.904 1.00 73.09  ? 162 GLN C N   1 
ATOM   4833  C  CA  . GLN C  1 171 ? -24.942 -41.469 50.693 1.00 65.70  ? 162 GLN C CA  1 
ATOM   4834  C  C   . GLN C  1 171 ? -24.201 -40.839 49.520 1.00 63.96  ? 162 GLN C C   1 
ATOM   4835  O  O   . GLN C  1 171 ? -24.510 -39.720 49.114 1.00 63.07  ? 162 GLN C O   1 
ATOM   4836  C  CB  . GLN C  1 171 ? -26.410 -41.687 50.340 1.00 67.29  ? 162 GLN C CB  1 
ATOM   4837  C  CG  . GLN C  1 171 ? -26.925 -43.047 50.760 1.00 73.33  ? 162 GLN C CG  1 
ATOM   4838  C  CD  . GLN C  1 171 ? -26.168 -44.177 50.082 1.00 83.49  ? 162 GLN C CD  1 
ATOM   4839  O  OE1 . GLN C  1 171 ? -25.936 -44.147 48.871 1.00 75.71  ? 162 GLN C OE1 1 
ATOM   4840  N  NE2 . GLN C  1 171 ? -25.774 -45.180 50.860 1.00 82.89  ? 162 GLN C NE2 1 
ATOM   4841  N  N   . VAL C  1 172 ? -23.207 -41.560 49.000 1.00 63.47  ? 163 VAL C N   1 
ATOM   4842  C  CA  . VAL C  1 172 ? -22.489 -41.175 47.779 1.00 57.69  ? 163 VAL C CA  1 
ATOM   4843  C  C   . VAL C  1 172 ? -23.448 -41.258 46.589 1.00 57.09  ? 163 VAL C C   1 
ATOM   4844  O  O   . VAL C  1 172 ? -24.242 -42.186 46.520 1.00 60.12  ? 163 VAL C O   1 
ATOM   4845  C  CB  . VAL C  1 172 ? -21.278 -42.122 47.526 1.00 49.92  ? 163 VAL C CB  1 
ATOM   4846  C  CG1 . VAL C  1 172 ? -20.764 -41.990 46.124 1.00 54.93  ? 163 VAL C CG1 1 
ATOM   4847  C  CG2 . VAL C  1 172 ? -20.170 -41.857 48.501 1.00 48.59  ? 163 VAL C CG2 1 
ATOM   4848  N  N   . ASP C  1 173 ? -23.397 -40.308 45.655 1.00 60.15  ? 164 ASP C N   1 
ATOM   4849  C  CA  . ASP C  1 173 ? -24.308 -40.364 44.519 1.00 52.90  ? 164 ASP C CA  1 
ATOM   4850  C  C   . ASP C  1 173 ? -23.779 -41.338 43.492 1.00 56.70  ? 164 ASP C C   1 
ATOM   4851  O  O   . ASP C  1 173 ? -22.664 -41.177 43.012 1.00 57.63  ? 164 ASP C O   1 
ATOM   4852  C  CB  . ASP C  1 173 ? -24.491 -38.992 43.885 1.00 50.64  ? 164 ASP C CB  1 
ATOM   4853  C  CG  . ASP C  1 173 ? -25.503 -39.016 42.757 1.00 61.97  ? 164 ASP C CG  1 
ATOM   4854  O  OD1 . ASP C  1 173 ? -26.229 -40.029 42.646 1.00 58.08  ? 164 ASP C OD1 1 
ATOM   4855  O  OD2 . ASP C  1 173 ? -25.573 -38.035 41.985 1.00 61.82  ? 164 ASP C OD2 1 
ATOM   4856  N  N   . LEU C  1 174 ? -24.556 -42.393 43.233 1.00 63.54  ? 165 LEU C N   1 
ATOM   4857  C  CA  . LEU C  1 174 ? -24.243 -43.398 42.203 1.00 60.84  ? 165 LEU C CA  1 
ATOM   4858  C  C   . LEU C  1 174 ? -24.976 -43.311 40.855 1.00 59.27  ? 165 LEU C C   1 
ATOM   4859  O  O   . LEU C  1 174 ? -24.681 -44.079 39.938 1.00 59.20  ? 165 LEU C O   1 
ATOM   4860  C  CB  . LEU C  1 174 ? -24.373 -44.805 42.784 1.00 51.06  ? 165 LEU C CB  1 
ATOM   4861  C  CG  . LEU C  1 174 ? -23.350 -45.061 43.884 1.00 53.04  ? 165 LEU C CG  1 
ATOM   4862  C  CD1 . LEU C  1 174 ? -23.682 -46.323 44.642 1.00 51.03  ? 165 LEU C CD1 1 
ATOM   4863  C  CD2 . LEU C  1 174 ? -21.961 -45.129 43.283 1.00 56.22  ? 165 LEU C CD2 1 
ATOM   4864  N  N   . SER C  1 175 ? -25.908 -42.376 40.726 1.00 60.35  ? 166 SER C N   1 
ATOM   4865  C  CA  . SER C  1 175 ? -26.774 -42.335 39.549 1.00 58.58  ? 166 SER C CA  1 
ATOM   4866  C  C   . SER C  1 175 ? -26.012 -42.167 38.228 1.00 57.15  ? 166 SER C C   1 
ATOM   4867  O  O   . SER C  1 175 ? -26.500 -42.561 37.178 1.00 58.04  ? 166 SER C O   1 
ATOM   4868  C  CB  . SER C  1 175 ? -27.831 -41.242 39.695 1.00 50.48  ? 166 SER C CB  1 
ATOM   4869  O  OG  . SER C  1 175 ? -27.220 -39.980 39.862 1.00 55.05  ? 166 SER C OG  1 
ATOM   4870  N  N   . SER C  1 176 ? -24.826 -41.573 38.279 1.00 60.82  ? 167 SER C N   1 
ATOM   4871  C  CA  . SER C  1 176 ? -24.026 -41.368 37.070 1.00 64.41  ? 167 SER C CA  1 
ATOM   4872  C  C   . SER C  1 176 ? -22.999 -42.464 36.811 1.00 67.16  ? 167 SER C C   1 
ATOM   4873  O  O   . SER C  1 176 ? -22.162 -42.330 35.911 1.00 63.63  ? 167 SER C O   1 
ATOM   4874  C  CB  . SER C  1 176 ? -23.344 -40.004 37.066 1.00 60.49  ? 167 SER C CB  1 
ATOM   4875  O  OG  . SER C  1 176 ? -24.299 -38.986 36.890 1.00 62.11  ? 167 SER C OG  1 
ATOM   4876  N  N   . TYR C  1 177 ? -23.025 -43.519 37.624 1.00 60.33  ? 168 TYR C N   1 
ATOM   4877  C  CA  . TYR C  1 177 ? -22.040 -44.588 37.485 1.00 59.35  ? 168 TYR C CA  1 
ATOM   4878  C  C   . TYR C  1 177 ? -22.112 -45.300 36.139 1.00 64.52  ? 168 TYR C C   1 
ATOM   4879  O  O   . TYR C  1 177 ? -23.199 -45.545 35.606 1.00 64.01  ? 168 TYR C O   1 
ATOM   4880  C  CB  . TYR C  1 177 ? -22.139 -45.604 38.618 1.00 54.50  ? 168 TYR C CB  1 
ATOM   4881  C  CG  . TYR C  1 177 ? -20.880 -46.428 38.751 1.00 54.44  ? 168 TYR C CG  1 
ATOM   4882  C  CD1 . TYR C  1 177 ? -19.738 -45.897 39.326 1.00 56.70  ? 168 TYR C CD1 1 
ATOM   4883  C  CD2 . TYR C  1 177 ? -20.826 -47.725 38.288 1.00 58.37  ? 168 TYR C CD2 1 
ATOM   4884  C  CE1 . TYR C  1 177 ? -18.582 -46.641 39.439 1.00 55.27  ? 168 TYR C CE1 1 
ATOM   4885  C  CE2 . TYR C  1 177 ? -19.676 -48.479 38.407 1.00 57.89  ? 168 TYR C CE2 1 
ATOM   4886  C  CZ  . TYR C  1 177 ? -18.563 -47.930 38.980 1.00 54.15  ? 168 TYR C CZ  1 
ATOM   4887  O  OH  . TYR C  1 177 ? -17.428 -48.681 39.091 1.00 53.40  ? 168 TYR C OH  1 
ATOM   4888  N  N   . TYR C  1 178 ? -20.944 -45.667 35.617 1.00 61.96  ? 169 TYR C N   1 
ATOM   4889  C  CA  . TYR C  1 178 ? -20.851 -46.218 34.277 1.00 59.22  ? 169 TYR C CA  1 
ATOM   4890  C  C   . TYR C  1 178 ? -21.312 -47.660 34.329 1.00 68.57  ? 169 TYR C C   1 
ATOM   4891  O  O   . TYR C  1 178 ? -20.713 -48.490 35.033 1.00 67.44  ? 169 TYR C O   1 
ATOM   4892  C  CB  . TYR C  1 178 ? -19.401 -46.151 33.815 1.00 55.16  ? 169 TYR C CB  1 
ATOM   4893  C  CG  . TYR C  1 178 ? -19.160 -46.740 32.453 1.00 55.26  ? 169 TYR C CG  1 
ATOM   4894  C  CD1 . TYR C  1 178 ? -20.002 -46.458 31.395 1.00 56.84  ? 169 TYR C CD1 1 
ATOM   4895  C  CD2 . TYR C  1 178 ? -18.072 -47.555 32.219 1.00 59.63  ? 169 TYR C CD2 1 
ATOM   4896  C  CE1 . TYR C  1 178 ? -19.776 -46.982 30.141 1.00 57.73  ? 169 TYR C CE1 1 
ATOM   4897  C  CE2 . TYR C  1 178 ? -17.835 -48.089 30.967 1.00 62.02  ? 169 TYR C CE2 1 
ATOM   4898  C  CZ  . TYR C  1 178 ? -18.689 -47.800 29.928 1.00 60.72  ? 169 TYR C CZ  1 
ATOM   4899  O  OH  . TYR C  1 178 ? -18.459 -48.346 28.677 1.00 66.18  ? 169 TYR C OH  1 
ATOM   4900  N  N   . ALA C  1 179 ? -22.366 -47.970 33.572 1.00 65.93  ? 170 ALA C N   1 
ATOM   4901  C  CA  . ALA C  1 179 ? -23.019 -49.272 33.701 1.00 57.93  ? 170 ALA C CA  1 
ATOM   4902  C  C   . ALA C  1 179 ? -22.185 -50.404 33.125 1.00 54.43  ? 170 ALA C C   1 
ATOM   4903  O  O   . ALA C  1 179 ? -22.325 -51.546 33.536 1.00 67.70  ? 170 ALA C O   1 
ATOM   4904  C  CB  . ALA C  1 179 ? -24.397 -49.246 33.083 1.00 55.13  ? 170 ALA C CB  1 
ATOM   4905  N  N   . SER C  1 180 ? -21.317 -50.079 32.177 1.00 56.31  ? 171 SER C N   1 
ATOM   4906  C  CA  . SER C  1 180 ? -20.461 -51.063 31.508 1.00 61.21  ? 171 SER C CA  1 
ATOM   4907  C  C   . SER C  1 180 ? -19.049 -51.207 32.108 1.00 62.02  ? 171 SER C C   1 
ATOM   4908  O  O   . SER C  1 180 ? -18.182 -51.843 31.521 1.00 58.37  ? 171 SER C O   1 
ATOM   4909  C  CB  . SER C  1 180 ? -20.432 -50.841 29.987 1.00 72.08  ? 171 SER C CB  1 
ATOM   4910  O  OG  . SER C  1 180 ? -21.739 -50.892 29.420 1.00 65.43  ? 171 SER C OG  1 
ATOM   4911  N  N   . SER C  1 181 ? -18.812 -50.548 33.241 1.00 64.32  ? 172 SER C N   1 
ATOM   4912  C  CA  . SER C  1 181 ? -17.538 -50.638 33.963 1.00 57.90  ? 172 SER C CA  1 
ATOM   4913  C  C   . SER C  1 181 ? -17.127 -52.051 34.361 1.00 61.71  ? 172 SER C C   1 
ATOM   4914  O  O   . SER C  1 181 ? -17.970 -52.881 34.698 1.00 59.23  ? 172 SER C O   1 
ATOM   4915  C  CB  . SER C  1 181 ? -17.580 -49.798 35.237 1.00 58.50  ? 172 SER C CB  1 
ATOM   4916  O  OG  . SER C  1 181 ? -16.424 -50.039 36.034 1.00 53.42  ? 172 SER C OG  1 
ATOM   4917  N  N   . LYS C  1 182 ? -15.816 -52.293 34.357 1.00 61.41  ? 173 LYS C N   1 
ATOM   4918  C  CA  . LYS C  1 182 ? -15.250 -53.573 34.756 1.00 56.23  ? 173 LYS C CA  1 
ATOM   4919  C  C   . LYS C  1 182 ? -15.666 -53.953 36.152 1.00 56.40  ? 173 LYS C C   1 
ATOM   4920  O  O   . LYS C  1 182 ? -15.644 -55.127 36.503 1.00 67.11  ? 173 LYS C O   1 
ATOM   4921  C  CB  . LYS C  1 182 ? -13.725 -53.541 34.719 1.00 57.58  ? 173 LYS C CB  1 
ATOM   4922  C  CG  . LYS C  1 182 ? -13.138 -53.406 33.353 1.00 61.78  ? 173 LYS C CG  1 
ATOM   4923  C  CD  . LYS C  1 182 ? -13.733 -54.415 32.400 1.00 69.41  ? 173 LYS C CD  1 
ATOM   4924  C  CE  . LYS C  1 182 ? -12.969 -55.723 32.412 1.00 67.81  ? 173 LYS C CE  1 
ATOM   4925  N  NZ  . LYS C  1 182 ? -13.256 -56.476 31.152 1.00 76.47  ? 173 LYS C NZ  1 
ATOM   4926  N  N   . TYR C  1 183 ? -16.016 -52.967 36.965 1.00 56.18  ? 174 TYR C N   1 
ATOM   4927  C  CA  . TYR C  1 183 ? -16.348 -53.249 38.356 1.00 66.04  ? 174 TYR C CA  1 
ATOM   4928  C  C   . TYR C  1 183 ? -17.706 -52.661 38.692 1.00 67.01  ? 174 TYR C C   1 
ATOM   4929  O  O   . TYR C  1 183 ? -18.072 -51.605 38.171 1.00 63.00  ? 174 TYR C O   1 
ATOM   4930  C  CB  . TYR C  1 183 ? -15.271 -52.700 39.300 1.00 55.60  ? 174 TYR C CB  1 
ATOM   4931  C  CG  . TYR C  1 183 ? -13.860 -53.193 39.010 1.00 54.79  ? 174 TYR C CG  1 
ATOM   4932  C  CD1 . TYR C  1 183 ? -13.322 -54.275 39.692 1.00 55.25  ? 174 TYR C CD1 1 
ATOM   4933  C  CD2 . TYR C  1 183 ? -13.064 -52.563 38.069 1.00 55.71  ? 174 TYR C CD2 1 
ATOM   4934  C  CE1 . TYR C  1 183 ? -12.038 -54.717 39.437 1.00 54.08  ? 174 TYR C CE1 1 
ATOM   4935  C  CE2 . TYR C  1 183 ? -11.778 -53.003 37.806 1.00 54.17  ? 174 TYR C CE2 1 
ATOM   4936  C  CZ  . TYR C  1 183 ? -11.273 -54.080 38.495 1.00 56.61  ? 174 TYR C CZ  1 
ATOM   4937  O  OH  . TYR C  1 183 ? -9.992  -54.511 38.241 1.00 56.51  ? 174 TYR C OH  1 
ATOM   4938  N  N   . GLU C  1 184 ? -18.444 -53.332 39.569 1.00 66.55  ? 175 GLU C N   1 
ATOM   4939  C  CA  . GLU C  1 184 ? -19.773 -52.861 39.947 1.00 67.67  ? 175 GLU C CA  1 
ATOM   4940  C  C   . GLU C  1 184 ? -19.750 -52.359 41.383 1.00 59.70  ? 175 GLU C C   1 
ATOM   4941  O  O   . GLU C  1 184 ? -18.882 -52.747 42.154 1.00 62.67  ? 175 GLU C O   1 
ATOM   4942  C  CB  . GLU C  1 184 ? -20.857 -53.927 39.721 1.00 61.68  ? 175 GLU C CB  1 
ATOM   4943  C  CG  . GLU C  1 184 ? -20.694 -55.188 40.528 1.00 77.39  ? 175 GLU C CG  1 
ATOM   4944  C  CD  . GLU C  1 184 ? -21.868 -56.137 40.355 1.00 87.99  ? 175 GLU C CD  1 
ATOM   4945  O  OE1 . GLU C  1 184 ? -23.004 -55.727 40.687 1.00 83.20  ? 175 GLU C OE1 1 
ATOM   4946  O  OE2 . GLU C  1 184 ? -21.653 -57.285 39.884 1.00 88.89  ? 175 GLU C OE2 1 
ATOM   4947  N  N   . ILE C  1 185 ? -20.646 -51.432 41.711 1.00 61.71  ? 176 ILE C N   1 
ATOM   4948  C  CA  . ILE C  1 185 ? -20.671 -50.821 43.047 1.00 65.85  ? 176 ILE C CA  1 
ATOM   4949  C  C   . ILE C  1 185 ? -21.725 -51.460 43.973 1.00 62.04  ? 176 ILE C C   1 
ATOM   4950  O  O   . ILE C  1 185 ? -22.937 -51.343 43.746 1.00 57.21  ? 176 ILE C O   1 
ATOM   4951  C  CB  . ILE C  1 185 ? -20.857 -49.260 42.971 1.00 62.56  ? 176 ILE C CB  1 
ATOM   4952  C  CG1 . ILE C  1 185 ? -19.706 -48.603 42.199 1.00 55.61  ? 176 ILE C CG1 1 
ATOM   4953  C  CG2 . ILE C  1 185 ? -20.986 -48.627 44.362 1.00 54.09  ? 176 ILE C CG2 1 
ATOM   4954  C  CD1 . ILE C  1 185 ? -18.373 -48.665 42.903 1.00 57.01  ? 176 ILE C CD1 1 
ATOM   4955  N  N   . LEU C  1 186 ? -21.245 -52.146 45.011 1.00 62.70  ? 177 LEU C N   1 
ATOM   4956  C  CA  . LEU C  1 186 ? -22.123 -52.745 46.017 1.00 60.05  ? 177 LEU C CA  1 
ATOM   4957  C  C   . LEU C  1 186 ? -22.636 -51.704 47.018 1.00 59.71  ? 177 LEU C C   1 
ATOM   4958  O  O   . LEU C  1 186 ? -23.830 -51.652 47.307 1.00 64.85  ? 177 LEU C O   1 
ATOM   4959  C  CB  . LEU C  1 186 ? -21.435 -53.936 46.700 1.00 56.13  ? 177 LEU C CB  1 
ATOM   4960  C  CG  . LEU C  1 186 ? -20.843 -54.954 45.706 1.00 59.85  ? 177 LEU C CG  1 
ATOM   4961  C  CD1 . LEU C  1 186 ? -20.042 -56.044 46.383 1.00 56.57  ? 177 LEU C CD1 1 
ATOM   4962  C  CD2 . LEU C  1 186 ? -21.910 -55.565 44.804 1.00 61.18  ? 177 LEU C CD2 1 
ATOM   4963  N  N   . SER C  1 187 ? -21.738 -50.871 47.537 1.00 59.88  ? 178 SER C N   1 
ATOM   4964  C  CA  . SER C  1 187 ? -22.140 -49.720 48.350 1.00 64.04  ? 178 SER C CA  1 
ATOM   4965  C  C   . SER C  1 187 ? -21.123 -48.588 48.295 1.00 60.22  ? 178 SER C C   1 
ATOM   4966  O  O   . SER C  1 187 ? -19.920 -48.823 48.147 1.00 60.11  ? 178 SER C O   1 
ATOM   4967  C  CB  . SER C  1 187 ? -22.354 -50.128 49.807 1.00 62.09  ? 178 SER C CB  1 
ATOM   4968  O  OG  . SER C  1 187 ? -21.187 -50.743 50.320 1.00 62.95  ? 178 SER C OG  1 
ATOM   4969  N  N   . ALA C  1 188 ? -21.604 -47.358 48.421 1.00 55.16  ? 179 ALA C N   1 
ATOM   4970  C  CA  . ALA C  1 188 ? -20.708 -46.238 48.648 1.00 50.08  ? 179 ALA C CA  1 
ATOM   4971  C  C   . ALA C  1 188 ? -21.273 -45.246 49.656 1.00 55.58  ? 179 ALA C C   1 
ATOM   4972  O  O   . ALA C  1 188 ? -22.398 -44.761 49.521 1.00 55.76  ? 179 ALA C O   1 
ATOM   4973  C  CB  . ALA C  1 188 ? -20.377 -45.558 47.359 1.00 52.01  ? 179 ALA C CB  1 
ATOM   4974  N  N   . THR C  1 189 ? -20.463 -44.955 50.668 1.00 54.38  ? 180 THR C N   1 
ATOM   4975  C  CA  . THR C  1 189 ? -20.821 -44.011 51.719 1.00 63.39  ? 180 THR C CA  1 
ATOM   4976  C  C   . THR C  1 189 ? -19.769 -42.920 51.833 1.00 60.39  ? 180 THR C C   1 
ATOM   4977  O  O   . THR C  1 189 ? -18.598 -43.138 51.497 1.00 54.16  ? 180 THR C O   1 
ATOM   4978  C  CB  . THR C  1 189 ? -20.943 -44.692 53.100 1.00 60.79  ? 180 THR C CB  1 
ATOM   4979  O  OG1 . THR C  1 189 ? -19.815 -45.546 53.309 1.00 62.48  ? 180 THR C OG1 1 
ATOM   4980  C  CG2 . THR C  1 189 ? -22.201 -45.524 53.183 1.00 62.52  ? 180 THR C CG2 1 
ATOM   4981  N  N   . GLN C  1 190 ? -20.213 -41.756 52.306 1.00 59.02  ? 181 GLN C N   1 
ATOM   4982  C  CA  . GLN C  1 190 ? -19.356 -40.612 52.583 1.00 54.14  ? 181 GLN C CA  1 
ATOM   4983  C  C   . GLN C  1 190 ? -19.685 -40.093 53.980 1.00 50.94  ? 181 GLN C C   1 
ATOM   4984  O  O   . GLN C  1 190 ? -20.798 -39.661 54.246 1.00 51.90  ? 181 GLN C O   1 
ATOM   4985  C  CB  . GLN C  1 190 ? -19.556 -39.522 51.524 1.00 57.03  ? 181 GLN C CB  1 
ATOM   4986  C  CG  . GLN C  1 190 ? -20.959 -38.934 51.466 1.00 55.92  ? 181 GLN C CG  1 
ATOM   4987  C  CD  . GLN C  1 190 ? -21.216 -38.183 50.181 1.00 59.27  ? 181 GLN C CD  1 
ATOM   4988  O  OE1 . GLN C  1 190 ? -20.388 -38.195 49.271 1.00 55.22  ? 181 GLN C OE1 1 
ATOM   4989  N  NE2 . GLN C  1 190 ? -22.364 -37.520 50.099 1.00 61.12  ? 181 GLN C NE2 1 
ATOM   4990  N  N   . THR C  1 191 ? -18.705 -40.157 54.873 1.00 54.78  ? 182 THR C N   1 
ATOM   4991  C  CA  . THR C  1 191 ? -18.950 -39.976 56.307 1.00 57.70  ? 182 THR C CA  1 
ATOM   4992  C  C   . THR C  1 191 ? -17.933 -39.061 56.983 1.00 54.13  ? 182 THR C C   1 
ATOM   4993  O  O   . THR C  1 191 ? -16.726 -39.222 56.826 1.00 50.48  ? 182 THR C O   1 
ATOM   4994  C  CB  . THR C  1 191 ? -19.032 -41.343 57.074 1.00 56.46  ? 182 THR C CB  1 
ATOM   4995  O  OG1 . THR C  1 191 ? -18.286 -42.353 56.374 1.00 55.73  ? 182 THR C OG1 1 
ATOM   4996  C  CG2 . THR C  1 191 ? -20.479 -41.803 57.202 1.00 55.52  ? 182 THR C CG2 1 
ATOM   4997  N  N   . ARG C  1 192 ? -18.445 -38.112 57.756 1.00 58.91  ? 183 ARG C N   1 
ATOM   4998  C  CA  . ARG C  1 192 ? -17.617 -37.143 58.461 1.00 55.23  ? 183 ARG C CA  1 
ATOM   4999  C  C   . ARG C  1 192 ? -16.927 -37.720 59.676 1.00 52.00  ? 183 ARG C C   1 
ATOM   5000  O  O   . ARG C  1 192 ? -17.580 -38.227 60.576 1.00 58.89  ? 183 ARG C O   1 
ATOM   5001  C  CB  . ARG C  1 192 ? -18.487 -35.977 58.912 1.00 59.74  ? 183 ARG C CB  1 
ATOM   5002  C  CG  . ARG C  1 192 ? -17.744 -34.878 59.627 1.00 54.89  ? 183 ARG C CG  1 
ATOM   5003  C  CD  . ARG C  1 192 ? -18.680 -33.728 59.870 1.00 56.11  ? 183 ARG C CD  1 
ATOM   5004  N  NE  . ARG C  1 192 ? -18.017 -32.658 60.595 1.00 65.95  ? 183 ARG C NE  1 
ATOM   5005  C  CZ  . ARG C  1 192 ? -17.721 -32.718 61.886 1.00 66.09  ? 183 ARG C CZ  1 
ATOM   5006  N  NH1 . ARG C  1 192 ? -18.032 -33.804 62.570 1.00 68.10  ? 183 ARG C NH1 1 
ATOM   5007  N  NH2 . ARG C  1 192 ? -17.118 -31.703 62.492 1.00 63.65  ? 183 ARG C NH2 1 
ATOM   5008  N  N   . SER C  1 193 ? -15.606 -37.619 59.718 1.00 58.79  ? 184 SER C N   1 
ATOM   5009  C  CA  . SER C  1 193 ? -14.848 -38.052 60.891 1.00 58.93  ? 184 SER C CA  1 
ATOM   5010  C  C   . SER C  1 193 ? -14.172 -36.846 61.536 1.00 59.90  ? 184 SER C C   1 
ATOM   5011  O  O   . SER C  1 193 ? -13.970 -35.827 60.884 1.00 62.91  ? 184 SER C O   1 
ATOM   5012  C  CB  . SER C  1 193 ? -13.836 -39.140 60.525 1.00 54.68  ? 184 SER C CB  1 
ATOM   5013  O  OG  . SER C  1 193 ? -14.494 -40.381 60.323 1.00 60.45  ? 184 SER C OG  1 
ATOM   5014  N  N   . GLU C  1 194 ? -13.884 -36.936 62.830 1.00 66.10  ? 185 GLU C N   1 
ATOM   5015  C  CA  . GLU C  1 194 ? -13.153 -35.882 63.535 1.00 62.17  ? 185 GLU C CA  1 
ATOM   5016  C  C   . GLU C  1 194 ? -12.046 -36.518 64.330 1.00 65.62  ? 185 GLU C C   1 
ATOM   5017  O  O   . GLU C  1 194 ? -12.261 -37.520 64.986 1.00 66.25  ? 185 GLU C O   1 
ATOM   5018  C  CB  . GLU C  1 194 ? -14.067 -35.142 64.466 1.00 53.52  ? 185 GLU C CB  1 
ATOM   5019  C  CG  . GLU C  1 194 ? -13.675 -33.733 64.637 1.00 63.18  ? 185 GLU C CG  1 
ATOM   5020  C  CD  . GLU C  1 194 ? -14.746 -32.962 65.376 1.00 87.22  ? 185 GLU C CD  1 
ATOM   5021  O  OE1 . GLU C  1 194 ? -15.589 -33.612 66.044 1.00 76.21  ? 185 GLU C OE1 1 
ATOM   5022  O  OE2 . GLU C  1 194 ? -14.751 -31.711 65.281 1.00 92.47  ? 185 GLU C OE2 1 
ATOM   5023  N  N   . ARG C  1 195 ? -10.853 -35.952 64.275 1.00 69.85  ? 186 ARG C N   1 
ATOM   5024  C  CA  A ARG C  1 195 ? -9.700  -36.602 64.882 0.50 69.56  ? 186 ARG C CA  1 
ATOM   5025  C  CA  B ARG C  1 195 ? -9.696  -36.602 64.875 0.50 69.55  ? 186 ARG C CA  1 
ATOM   5026  C  C   . ARG C  1 195 ? -8.877  -35.645 65.711 1.00 71.91  ? 186 ARG C C   1 
ATOM   5027  O  O   . ARG C  1 195 ? -8.464  -34.594 65.236 1.00 76.79  ? 186 ARG C O   1 
ATOM   5028  C  CB  A ARG C  1 195 ? -8.820  -37.235 63.814 0.50 74.02  ? 186 ARG C CB  1 
ATOM   5029  C  CB  B ARG C  1 195 ? -8.812  -37.221 63.797 0.50 74.01  ? 186 ARG C CB  1 
ATOM   5030  C  CG  A ARG C  1 195 ? -9.598  -38.044 62.807 0.50 75.62  ? 186 ARG C CG  1 
ATOM   5031  C  CG  B ARG C  1 195 ? -7.555  -37.891 64.311 0.50 75.43  ? 186 ARG C CG  1 
ATOM   5032  C  CD  A ARG C  1 195 ? -8.711  -39.071 62.182 0.50 78.52  ? 186 ARG C CD  1 
ATOM   5033  C  CD  B ARG C  1 195 ? -7.080  -38.896 63.286 0.50 84.06  ? 186 ARG C CD  1 
ATOM   5034  N  NE  A ARG C  1 195 ? -9.410  -40.323 61.933 0.50 77.75  ? 186 ARG C NE  1 
ATOM   5035  N  NE  B ARG C  1 195 ? -5.829  -39.554 63.644 0.50 87.68  ? 186 ARG C NE  1 
ATOM   5036  C  CZ  A ARG C  1 195 ? -8.793  -41.446 61.586 0.50 83.20  ? 186 ARG C CZ  1 
ATOM   5037  C  CZ  B ARG C  1 195 ? -4.940  -39.969 62.747 0.50 90.95  ? 186 ARG C CZ  1 
ATOM   5038  N  NH1 A ARG C  1 195 ? -7.474  -41.455 61.456 0.50 89.72  ? 186 ARG C NH1 1 
ATOM   5039  N  NH1 B ARG C  1 195 ? -5.169  -39.775 61.458 0.50 88.56  ? 186 ARG C NH1 1 
ATOM   5040  N  NH2 A ARG C  1 195 ? -9.485  -42.556 61.372 0.50 81.97  ? 186 ARG C NH2 1 
ATOM   5041  N  NH2 B ARG C  1 195 ? -3.821  -40.566 63.130 0.50 89.79  ? 186 ARG C NH2 1 
ATOM   5042  N  N   . PHE C  1 196 ? -8.642  -36.024 66.957 1.00 75.76  ? 187 PHE C N   1 
ATOM   5043  C  CA  . PHE C  1 196 ? -7.853  -35.214 67.853 1.00 75.25  ? 187 PHE C CA  1 
ATOM   5044  C  C   . PHE C  1 196 ? -6.452  -35.775 67.940 1.00 80.96  ? 187 PHE C C   1 
ATOM   5045  O  O   . PHE C  1 196 ? -6.240  -36.982 67.846 1.00 76.27  ? 187 PHE C O   1 
ATOM   5046  C  CB  . PHE C  1 196 ? -8.486  -35.173 69.231 1.00 66.69  ? 187 PHE C CB  1 
ATOM   5047  C  CG  . PHE C  1 196 ? -9.788  -34.449 69.279 1.00 63.31  ? 187 PHE C CG  1 
ATOM   5048  C  CD1 . PHE C  1 196 ? -9.832  -33.095 69.560 1.00 60.75  ? 187 PHE C CD1 1 
ATOM   5049  C  CD2 . PHE C  1 196 ? -10.974 -35.128 69.068 1.00 77.70  ? 187 PHE C CD2 1 
ATOM   5050  C  CE1 . PHE C  1 196 ? -11.030 -32.425 69.621 1.00 62.39  ? 187 PHE C CE1 1 
ATOM   5051  C  CE2 . PHE C  1 196 ? -12.184 -34.467 69.122 1.00 82.58  ? 187 PHE C CE2 1 
ATOM   5052  C  CZ  . PHE C  1 196 ? -12.211 -33.110 69.402 1.00 74.28  ? 187 PHE C CZ  1 
ATOM   5053  N  N   . TYR C  1 197 ? -5.497  -34.868 68.081 1.00 89.45  ? 188 TYR C N   1 
ATOM   5054  C  CA  . TYR C  1 197 ? -4.102  -35.217 68.276 1.00 90.78  ? 188 TYR C CA  1 
ATOM   5055  C  C   . TYR C  1 197 ? -3.672  -34.721 69.658 1.00 94.31  ? 188 TYR C C   1 
ATOM   5056  O  O   . TYR C  1 197 ? -4.303  -33.829 70.234 1.00 93.54  ? 188 TYR C O   1 
ATOM   5057  C  CB  . TYR C  1 197 ? -3.254  -34.584 67.171 1.00 96.32  ? 188 TYR C CB  1 
ATOM   5058  C  CG  . TYR C  1 197 ? -3.652  -35.037 65.782 1.00 87.37  ? 188 TYR C CG  1 
ATOM   5059  C  CD1 . TYR C  1 197 ? -3.000  -36.100 65.167 1.00 86.71  ? 188 TYR C CD1 1 
ATOM   5060  C  CD2 . TYR C  1 197 ? -4.683  -34.413 65.092 1.00 86.72  ? 188 TYR C CD2 1 
ATOM   5061  C  CE1 . TYR C  1 197 ? -3.355  -36.527 63.912 1.00 86.60  ? 188 TYR C CE1 1 
ATOM   5062  C  CE2 . TYR C  1 197 ? -5.050  -34.836 63.832 1.00 91.95  ? 188 TYR C CE2 1 
ATOM   5063  C  CZ  . TYR C  1 197 ? -4.380  -35.894 63.245 1.00 96.23  ? 188 TYR C CZ  1 
ATOM   5064  O  OH  . TYR C  1 197 ? -4.737  -36.312 61.979 1.00 94.94  ? 188 TYR C OH  1 
ATOM   5065  N  N   . GLU C  1 198 ? -2.638  -35.329 70.224 1.00 98.58  ? 189 GLU C N   1 
ATOM   5066  C  CA  . GLU C  1 198 ? -2.105  -34.840 71.494 1.00 105.12 ? 189 GLU C CA  1 
ATOM   5067  C  C   . GLU C  1 198 ? -1.668  -33.399 71.319 1.00 99.13  ? 189 GLU C C   1 
ATOM   5068  O  O   . GLU C  1 198 ? -1.882  -32.563 72.185 1.00 92.59  ? 189 GLU C O   1 
ATOM   5069  C  CB  . GLU C  1 198 ? -0.906  -35.672 71.939 1.00 100.18 ? 189 GLU C CB  1 
ATOM   5070  C  CG  . GLU C  1 198 ? -0.967  -36.162 73.370 1.00 101.21 ? 189 GLU C CG  1 
ATOM   5071  C  CD  . GLU C  1 198 ? -2.185  -37.038 73.633 1.00 112.80 ? 189 GLU C CD  1 
ATOM   5072  O  OE1 . GLU C  1 198 ? -3.308  -36.494 73.765 1.00 107.80 ? 189 GLU C OE1 1 
ATOM   5073  O  OE2 . GLU C  1 198 ? -2.017  -38.276 73.701 1.00 110.53 ? 189 GLU C OE2 1 
ATOM   5074  N  N   . CYS C  1 199 ? -1.085  -33.116 70.160 1.00 92.31  ? 190 CYS C N   1 
ATOM   5075  C  CA  . CYS C  1 199 ? -0.488  -31.812 69.908 1.00 93.94  ? 190 CYS C CA  1 
ATOM   5076  C  C   . CYS C  1 199 ? -1.422  -30.671 70.292 1.00 93.93  ? 190 CYS C C   1 
ATOM   5077  O  O   . CYS C  1 199 ? -1.011  -29.722 70.959 1.00 93.49  ? 190 CYS C O   1 
ATOM   5078  C  CB  . CYS C  1 199 ? -0.047  -31.665 68.457 1.00 102.83 ? 190 CYS C CB  1 
ATOM   5079  S  SG  . CYS C  1 199 ? -1.181  -30.843 67.324 1.00 104.16 ? 190 CYS C SG  1 
ATOM   5080  N  N   . CYS C  1 200 ? -2.674  -30.779 69.881 1.00 93.35  ? 191 CYS C N   1 
ATOM   5081  C  CA  . CYS C  1 200 ? -3.637  -29.702 70.081 1.00 92.47  ? 191 CYS C CA  1 
ATOM   5082  C  C   . CYS C  1 200 ? -5.036  -30.191 70.476 1.00 92.01  ? 191 CYS C C   1 
ATOM   5083  O  O   . CYS C  1 200 ? -5.369  -31.363 70.315 1.00 92.04  ? 191 CYS C O   1 
ATOM   5084  C  CB  . CYS C  1 200 ? -3.700  -28.827 68.828 1.00 91.22  ? 191 CYS C CB  1 
ATOM   5085  S  SG  . CYS C  1 200 ? -3.255  -29.664 67.298 1.00 108.73 ? 191 CYS C SG  1 
ATOM   5086  N  N   . LYS C  1 201 ? -5.856  -29.276 71.006 1.00 92.23  ? 192 LYS C N   1 
ATOM   5087  C  CA  . LYS C  1 201 ? -7.215  -29.604 71.429 1.00 93.48  ? 192 LYS C CA  1 
ATOM   5088  C  C   . LYS C  1 201 ? -8.208  -29.272 70.313 1.00 88.05  ? 192 LYS C C   1 
ATOM   5089  O  O   . LYS C  1 201 ? -9.416  -29.463 70.443 1.00 85.14  ? 192 LYS C O   1 
ATOM   5090  C  CB  . LYS C  1 201 ? -7.543  -28.860 72.738 1.00 94.73  ? 192 LYS C CB  1 
ATOM   5091  C  CG  . LYS C  1 201 ? -8.978  -28.438 72.929 0.00 89.76  ? 192 LYS C CG  1 
ATOM   5092  C  CD  . LYS C  1 201 ? -9.022  -27.112 73.665 0.00 89.57  ? 192 LYS C CD  1 
ATOM   5093  C  CE  . LYS C  1 201 ? -10.381 -26.460 73.545 0.00 87.96  ? 192 LYS C CE  1 
ATOM   5094  N  NZ  . LYS C  1 201 ? -10.440 -25.170 74.281 0.00 88.55  ? 192 LYS C NZ  1 
ATOM   5095  N  N   . GLU C  1 202 ? -7.667  -28.783 69.205 1.00 88.36  ? 193 GLU C N   1 
ATOM   5096  C  CA  . GLU C  1 202 ? -8.440  -28.480 68.007 1.00 78.30  ? 193 GLU C CA  1 
ATOM   5097  C  C   . GLU C  1 202 ? -8.747  -29.740 67.207 1.00 69.29  ? 193 GLU C C   1 
ATOM   5098  O  O   . GLU C  1 202 ? -7.874  -30.569 67.000 1.00 74.19  ? 193 GLU C O   1 
ATOM   5099  C  CB  . GLU C  1 202 ? -7.656  -27.504 67.127 1.00 80.69  ? 193 GLU C CB  1 
ATOM   5100  C  CG  . GLU C  1 202 ? -8.416  -26.997 65.910 1.00 77.32  ? 193 GLU C CG  1 
ATOM   5101  C  CD  . GLU C  1 202 ? -7.545  -26.205 64.972 1.00 73.89  ? 193 GLU C CD  1 
ATOM   5102  O  OE1 . GLU C  1 202 ? -6.307  -26.367 65.027 1.00 83.06  ? 193 GLU C OE1 1 
ATOM   5103  O  OE2 . GLU C  1 202 ? -8.101  -25.421 64.183 1.00 71.44  ? 193 GLU C OE2 1 
ATOM   5104  N  N   . PRO C  1 203 ? -9.997  -29.879 66.752 1.00 64.04  ? 194 PRO C N   1 
ATOM   5105  C  CA  . PRO C  1 203 ? -10.454 -30.995 65.924 1.00 69.07  ? 194 PRO C CA  1 
ATOM   5106  C  C   . PRO C  1 203 ? -9.923  -30.910 64.499 1.00 73.06  ? 194 PRO C C   1 
ATOM   5107  O  O   . PRO C  1 203 ? -9.790  -29.816 63.962 1.00 67.75  ? 194 PRO C O   1 
ATOM   5108  C  CB  . PRO C  1 203 ? -11.970 -30.798 65.873 1.00 64.72  ? 194 PRO C CB  1 
ATOM   5109  C  CG  . PRO C  1 203 ? -12.288 -29.728 66.812 1.00 65.13  ? 194 PRO C CG  1 
ATOM   5110  C  CD  . PRO C  1 203 ? -11.073 -28.916 67.008 1.00 69.86  ? 194 PRO C CD  1 
ATOM   5111  N  N   . TYR C  1 204 ? -9.614  -32.051 63.894 1.00 72.84  ? 195 TYR C N   1 
ATOM   5112  C  CA  . TYR C  1 204 ? -9.319  -32.080 62.475 1.00 63.53  ? 195 TYR C CA  1 
ATOM   5113  C  C   . TYR C  1 204 ? -10.340 -32.917 61.763 1.00 65.07  ? 195 TYR C C   1 
ATOM   5114  O  O   . TYR C  1 204 ? -10.340 -34.137 61.912 1.00 70.45  ? 195 TYR C O   1 
ATOM   5115  C  CB  . TYR C  1 204 ? -7.913  -32.609 62.239 1.00 74.37  ? 195 TYR C CB  1 
ATOM   5116  C  CG  . TYR C  1 204 ? -6.896  -31.640 62.769 1.00 84.37  ? 195 TYR C CG  1 
ATOM   5117  C  CD1 . TYR C  1 204 ? -6.203  -30.789 61.918 1.00 76.61  ? 195 TYR C CD1 1 
ATOM   5118  C  CD2 . TYR C  1 204 ? -6.673  -31.533 64.131 1.00 81.14  ? 195 TYR C CD2 1 
ATOM   5119  C  CE1 . TYR C  1 204 ? -5.293  -29.884 62.415 1.00 78.44  ? 195 TYR C CE1 1 
ATOM   5120  C  CE2 . TYR C  1 204 ? -5.772  -30.634 64.634 1.00 80.39  ? 195 TYR C CE2 1 
ATOM   5121  C  CZ  . TYR C  1 204 ? -5.082  -29.811 63.780 1.00 84.01  ? 195 TYR C CZ  1 
ATOM   5122  O  OH  . TYR C  1 204 ? -4.180  -28.915 64.314 1.00 93.15  ? 195 TYR C OH  1 
ATOM   5123  N  N   . PRO C  1 205 ? -11.226 -32.266 60.991 1.00 55.29  ? 196 PRO C N   1 
ATOM   5124  C  CA  . PRO C  1 205 ? -12.260 -32.986 60.247 1.00 52.72  ? 196 PRO C CA  1 
ATOM   5125  C  C   . PRO C  1 205 ? -11.725 -33.638 58.973 1.00 55.80  ? 196 PRO C C   1 
ATOM   5126  O  O   . PRO C  1 205 ? -10.703 -33.233 58.416 1.00 53.03  ? 196 PRO C O   1 
ATOM   5127  C  CB  . PRO C  1 205 ? -13.292 -31.900 59.919 1.00 52.63  ? 196 PRO C CB  1 
ATOM   5128  C  CG  . PRO C  1 205 ? -12.869 -30.697 60.668 1.00 59.47  ? 196 PRO C CG  1 
ATOM   5129  C  CD  . PRO C  1 205 ? -11.405 -30.816 60.887 1.00 55.02  ? 196 PRO C CD  1 
ATOM   5130  N  N   . ASP C  1 206 ? -12.419 -34.679 58.543 1.00 58.11  ? 197 ASP C N   1 
ATOM   5131  C  CA  . ASP C  1 206 ? -12.190 -35.287 57.252 1.00 53.63  ? 197 ASP C CA  1 
ATOM   5132  C  C   . ASP C  1 206 ? -13.483 -35.933 56.821 1.00 55.05  ? 197 ASP C C   1 
ATOM   5133  O  O   . ASP C  1 206 ? -14.347 -36.224 57.641 1.00 51.07  ? 197 ASP C O   1 
ATOM   5134  C  CB  . ASP C  1 206 ? -11.049 -36.315 57.287 1.00 52.46  ? 197 ASP C CB  1 
ATOM   5135  C  CG  . ASP C  1 206 ? -11.396 -37.574 58.070 1.00 62.28  ? 197 ASP C CG  1 
ATOM   5136  O  OD1 . ASP C  1 206 ? -12.530 -38.083 57.961 1.00 60.33  ? 197 ASP C OD1 1 
ATOM   5137  O  OD2 . ASP C  1 206 ? -10.511 -38.072 58.793 1.00 70.72  ? 197 ASP C OD2 1 
ATOM   5138  N  N   . VAL C  1 207 ? -13.627 -36.135 55.520 1.00 59.32  ? 198 VAL C N   1 
ATOM   5139  C  CA  . VAL C  1 207 ? -14.705 -36.963 55.014 1.00 56.70  ? 198 VAL C CA  1 
ATOM   5140  C  C   . VAL C  1 207 ? -14.120 -38.269 54.476 1.00 56.96  ? 198 VAL C C   1 
ATOM   5141  O  O   . VAL C  1 207 ? -13.126 -38.286 53.761 1.00 58.23  ? 198 VAL C O   1 
ATOM   5142  C  CB  . VAL C  1 207 ? -15.579 -36.218 53.996 1.00 56.15  ? 198 VAL C CB  1 
ATOM   5143  C  CG1 . VAL C  1 207 ? -16.631 -37.142 53.423 1.00 52.48  ? 198 VAL C CG1 1 
ATOM   5144  C  CG2 . VAL C  1 207 ? -16.239 -35.025 54.672 1.00 51.22  ? 198 VAL C CG2 1 
ATOM   5145  N  N   . ASN C  1 208 ? -14.705 -39.373 54.899 1.00 57.98  ? 199 ASN C N   1 
ATOM   5146  C  CA  . ASN C  1 208 ? -14.177 -40.666 54.553 1.00 55.79  ? 199 ASN C CA  1 
ATOM   5147  C  C   . ASN C  1 208 ? -15.061 -41.148 53.446 1.00 56.49  ? 199 ASN C C   1 
ATOM   5148  O  O   . ASN C  1 208 ? -16.275 -41.061 53.559 1.00 58.58  ? 199 ASN C O   1 
ATOM   5149  C  CB  . ASN C  1 208 ? -14.263 -41.599 55.758 1.00 61.57  ? 199 ASN C CB  1 
ATOM   5150  C  CG  . ASN C  1 208 ? -13.457 -42.872 55.579 1.00 69.19  ? 199 ASN C CG  1 
ATOM   5151  O  OD1 . ASN C  1 208 ? -12.361 -42.863 55.015 1.00 67.65  ? 199 ASN C OD1 1 
ATOM   5152  N  ND2 . ASN C  1 208 ? -13.996 -43.982 56.077 1.00 68.59  ? 199 ASN C ND2 1 
ATOM   5153  N  N   . LEU C  1 209 ? -14.457 -41.590 52.350 1.00 59.05  ? 200 LEU C N   1 
ATOM   5154  C  CA  . LEU C  1 209 ? -15.204 -42.193 51.262 1.00 51.68  ? 200 LEU C CA  1 
ATOM   5155  C  C   . LEU C  1 209 ? -14.954 -43.687 51.328 1.00 56.36  ? 200 LEU C C   1 
ATOM   5156  O  O   . LEU C  1 209 ? -13.817 -44.141 51.182 1.00 54.18  ? 200 LEU C O   1 
ATOM   5157  C  CB  . LEU C  1 209 ? -14.747 -41.631 49.919 1.00 52.95  ? 200 LEU C CB  1 
ATOM   5158  C  CG  . LEU C  1 209 ? -15.434 -42.086 48.626 1.00 53.53  ? 200 LEU C CG  1 
ATOM   5159  C  CD1 . LEU C  1 209 ? -16.880 -41.650 48.614 1.00 55.02  ? 200 LEU C CD1 1 
ATOM   5160  C  CD2 . LEU C  1 209 ? -14.715 -41.504 47.433 1.00 42.81  ? 200 LEU C CD2 1 
ATOM   5161  N  N   . VAL C  1 210 ? -16.014 -44.449 51.577 1.00 56.24  ? 201 VAL C N   1 
ATOM   5162  C  CA  . VAL C  1 210 ? -15.887 -45.897 51.698 1.00 52.43  ? 201 VAL C CA  1 
ATOM   5163  C  C   . VAL C  1 210 ? -16.651 -46.593 50.586 1.00 52.20  ? 201 VAL C C   1 
ATOM   5164  O  O   . VAL C  1 210 ? -17.843 -46.356 50.395 1.00 53.06  ? 201 VAL C O   1 
ATOM   5165  C  CB  . VAL C  1 210 ? -16.380 -46.407 53.057 1.00 54.37  ? 201 VAL C CB  1 
ATOM   5166  C  CG1 . VAL C  1 210 ? -16.339 -47.925 53.081 1.00 56.30  ? 201 VAL C CG1 1 
ATOM   5167  C  CG2 . VAL C  1 210 ? -15.534 -45.829 54.166 1.00 51.61  ? 201 VAL C CG2 1 
ATOM   5168  N  N   . VAL C  1 211 ? -15.953 -47.449 49.852 1.00 47.40  ? 202 VAL C N   1 
ATOM   5169  C  CA  . VAL C  1 211 ? -16.522 -48.033 48.647 1.00 52.06  ? 202 VAL C CA  1 
ATOM   5170  C  C   . VAL C  1 211 ? -16.357 -49.550 48.604 1.00 54.33  ? 202 VAL C C   1 
ATOM   5171  O  O   . VAL C  1 211 ? -15.242 -50.065 48.728 1.00 51.82  ? 202 VAL C O   1 
ATOM   5172  C  CB  . VAL C  1 211 ? -15.883 -47.404 47.386 1.00 49.80  ? 202 VAL C CB  1 
ATOM   5173  C  CG1 . VAL C  1 211 ? -16.447 -48.024 46.119 1.00 46.92  ? 202 VAL C CG1 1 
ATOM   5174  C  CG2 . VAL C  1 211 ? -16.085 -45.901 47.397 1.00 43.96  ? 202 VAL C CG2 1 
ATOM   5175  N  N   . LYS C  1 212 ? -17.479 -50.254 48.439 1.00 54.90  ? 203 LYS C N   1 
ATOM   5176  C  CA  . LYS C  1 212 ? -17.455 -51.706 48.241 1.00 67.18  ? 203 LYS C CA  1 
ATOM   5177  C  C   . LYS C  1 212 ? -17.861 -52.120 46.804 1.00 58.04  ? 203 LYS C C   1 
ATOM   5178  O  O   . LYS C  1 212 ? -18.973 -51.874 46.337 1.00 57.45  ? 203 LYS C O   1 
ATOM   5179  C  CB  . LYS C  1 212 ? -18.251 -52.457 49.335 1.00 64.26  ? 203 LYS C CB  1 
ATOM   5180  C  CG  . LYS C  1 212 ? -18.158 -53.995 49.230 1.00 67.48  ? 203 LYS C CG  1 
ATOM   5181  C  CD  . LYS C  1 212 ? -18.223 -54.736 50.583 1.00 82.53  ? 203 LYS C CD  1 
ATOM   5182  C  CE  . LYS C  1 212 ? -19.587 -54.621 51.288 1.00 87.27  ? 203 LYS C CE  1 
ATOM   5183  N  NZ  . LYS C  1 212 ? -19.805 -53.276 51.925 1.00 83.65  ? 203 LYS C NZ  1 
ATOM   5184  N  N   . PHE C  1 213 ? -16.926 -52.751 46.112 1.00 53.38  ? 204 PHE C N   1 
ATOM   5185  C  CA  . PHE C  1 213 ? -17.094 -53.062 44.714 1.00 58.32  ? 204 PHE C CA  1 
ATOM   5186  C  C   . PHE C  1 213 ? -16.613 -54.486 44.406 1.00 62.19  ? 204 PHE C C   1 
ATOM   5187  O  O   . PHE C  1 213 ? -15.858 -55.069 45.177 1.00 63.82  ? 204 PHE C O   1 
ATOM   5188  C  CB  . PHE C  1 213 ? -16.311 -52.035 43.889 1.00 61.12  ? 204 PHE C CB  1 
ATOM   5189  C  CG  . PHE C  1 213 ? -14.820 -52.052 44.142 1.00 54.18  ? 204 PHE C CG  1 
ATOM   5190  C  CD1 . PHE C  1 213 ? -13.948 -52.522 43.179 1.00 50.87  ? 204 PHE C CD1 1 
ATOM   5191  C  CD2 . PHE C  1 213 ? -14.298 -51.606 45.337 1.00 57.63  ? 204 PHE C CD2 1 
ATOM   5192  C  CE1 . PHE C  1 213 ? -12.593 -52.538 43.401 1.00 52.51  ? 204 PHE C CE1 1 
ATOM   5193  C  CE2 . PHE C  1 213 ? -12.934 -51.627 45.565 1.00 55.47  ? 204 PHE C CE2 1 
ATOM   5194  C  CZ  . PHE C  1 213 ? -12.084 -52.092 44.593 1.00 54.68  ? 204 PHE C CZ  1 
ATOM   5195  N  N   . ARG C  1 214 ? -17.071 -55.040 43.286 1.00 62.13  ? 205 ARG C N   1 
ATOM   5196  C  CA  . ARG C  1 214 ? -16.610 -56.340 42.801 1.00 66.09  ? 205 ARG C CA  1 
ATOM   5197  C  C   . ARG C  1 214 ? -16.557 -56.347 41.271 1.00 74.14  ? 205 ARG C C   1 
ATOM   5198  O  O   . ARG C  1 214 ? -17.139 -55.477 40.602 1.00 67.24  ? 205 ARG C O   1 
ATOM   5199  C  CB  . ARG C  1 214 ? -17.528 -57.466 43.286 1.00 63.20  ? 205 ARG C CB  1 
ATOM   5200  C  CG  . ARG C  1 214 ? -18.967 -57.263 42.881 1.00 69.03  ? 205 ARG C CG  1 
ATOM   5201  C  CD  . ARG C  1 214 ? -19.832 -58.475 43.148 1.00 72.25  ? 205 ARG C CD  1 
ATOM   5202  N  NE  . ARG C  1 214 ? -21.217 -58.207 42.769 1.00 70.28  ? 205 ARG C NE  1 
ATOM   5203  C  CZ  . ARG C  1 214 ? -22.270 -58.845 43.269 1.00 72.58  ? 205 ARG C CZ  1 
ATOM   5204  N  NH1 . ARG C  1 214 ? -22.106 -59.800 44.168 1.00 73.46  ? 205 ARG C NH1 1 
ATOM   5205  N  NH2 . ARG C  1 214 ? -23.491 -58.526 42.872 1.00 74.92  ? 205 ARG C NH2 1 
ATOM   5206  N  N   . GLU C  1 215 ? -15.852 -57.329 40.716 1.00 72.91  ? 206 GLU C N   1 
ATOM   5207  C  CA  . GLU C  1 215 ? -15.826 -57.495 39.274 1.00 69.25  ? 206 GLU C CA  1 
ATOM   5208  C  C   . GLU C  1 215 ? -17.261 -57.679 38.803 1.00 75.71  ? 206 GLU C C   1 
ATOM   5209  O  O   . GLU C  1 215 ? -17.982 -58.545 39.291 1.00 79.59  ? 206 GLU C O   1 
ATOM   5210  C  CB  . GLU C  1 215 ? -14.969 -58.694 38.884 1.00 74.41  ? 206 GLU C CB  1 
ATOM   5211  C  CG  . GLU C  1 215 ? -13.491 -58.511 39.196 1.00 72.85  ? 206 GLU C CG  1 
ATOM   5212  C  CD  . GLU C  1 215 ? -12.650 -59.744 38.878 1.00 89.04  ? 206 GLU C CD  1 
ATOM   5213  O  OE1 . GLU C  1 215 ? -13.219 -60.824 38.596 1.00 94.00  ? 206 GLU C OE1 1 
ATOM   5214  O  OE2 . GLU C  1 215 ? -11.407 -59.635 38.912 1.00 88.33  ? 206 GLU C OE2 1 
ATOM   5215  N  N   . ARG C  1 216 ? -17.666 -56.858 37.863 1.00 81.57  ? 207 ARG C N   1 
ATOM   5216  C  CA  . ARG C  1 216 ? -19.007 -56.907 37.348 1.00 88.35  ? 207 ARG C CA  1 
ATOM   5217  C  C   . ARG C  1 216 ? -19.276 -58.156 36.580 1.00 98.58  ? 207 ARG C C   1 
ATOM   5218  O  O   . ARG C  1 216 ? -18.425 -58.628 35.848 1.00 95.50  ? 207 ARG C O   1 
ATOM   5219  C  CB  . ARG C  1 216 ? -19.235 -55.735 36.407 1.00 79.85  ? 207 ARG C CB  1 
ATOM   5220  C  CG  . ARG C  1 216 ? -20.621 -55.622 35.862 1.00 76.11  ? 207 ARG C CG  1 
ATOM   5221  C  CD  . ARG C  1 216 ? -20.660 -54.668 34.701 1.00 79.94  ? 207 ARG C CD  1 
ATOM   5222  N  NE  . ARG C  1 216 ? -19.641 -55.002 33.711 1.00 89.44  ? 207 ARG C NE  1 
ATOM   5223  C  CZ  . ARG C  1 216 ? -19.802 -54.933 32.392 1.00 89.42  ? 207 ARG C CZ  1 
ATOM   5224  N  NH1 . ARG C  1 216 ? -20.952 -54.553 31.863 1.00 73.40  ? 207 ARG C NH1 1 
ATOM   5225  N  NH2 . ARG C  1 216 ? -18.803 -55.260 31.601 1.00 80.62  ? 207 ARG C NH2 1 
ATOM   5226  N  N   . ARG C  1 217 ? -20.480 -58.681 36.756 1.00 109.17 ? 208 ARG C N   1 
ATOM   5227  C  CA  . ARG C  1 217 ? -20.973 -59.808 35.988 1.00 115.28 ? 208 ARG C CA  1 
ATOM   5228  C  C   . ARG C  1 217 ? -22.291 -59.525 35.259 1.00 118.38 ? 208 ARG C C   1 
ATOM   5229  O  O   . ARG C  1 217 ? -22.685 -60.283 34.382 1.00 107.18 ? 208 ARG C O   1 
ATOM   5230  C  CB  . ARG C  1 217 ? -21.053 -61.023 36.881 1.00 104.93 ? 208 ARG C CB  1 
ATOM   5231  C  CG  . ARG C  1 217 ? -20.130 -62.023 36.343 1.00 113.36 ? 208 ARG C CG  1 
ATOM   5232  C  CD  . ARG C  1 217 ? -18.843 -61.287 36.234 1.00 107.18 ? 208 ARG C CD  1 
ATOM   5233  N  NE  . ARG C  1 217 ? -17.722 -62.172 36.034 1.00 120.66 ? 208 ARG C NE  1 
ATOM   5234  C  CZ  . ARG C  1 217 ? -16.473 -61.744 35.993 1.00 117.41 ? 208 ARG C CZ  1 
ATOM   5235  N  NH1 . ARG C  1 217 ? -16.230 -60.455 36.147 1.00 108.74 ? 208 ARG C NH1 1 
ATOM   5236  N  NH2 . ARG C  1 217 ? -15.474 -62.588 35.796 1.00 105.25 ? 208 ARG C NH2 1 
ATOM   5237  N  N   . ALA C  1 218 ? -22.950 -58.422 35.621 1.00 110.73 ? 209 ALA C N   1 
ATOM   5238  C  CA  . ALA C  1 218 ? -24.245 -57.991 34.962 1.00 101.14 ? 209 ALA C CA  1 
ATOM   5239  C  C   . ALA C  1 218 ? -25.321 -59.144 34.943 1.00 110.38 ? 209 ALA C C   1 
ATOM   5240  O  O   . ALA C  1 218 ? -25.095 -60.278 34.365 1.00 106.27 ? 209 ALA C O   1 
ATOM   5241  C  CB  . ALA C  1 218 ? -24.021 -57.408 33.500 1.00 83.95  ? 209 ALA C CB  1 
ATOM   5242  N  N   . LYS D  1 3   ? 6.497   1.436   -2.206 1.00 111.35 ? -6  LYS D N   1 
ATOM   5243  C  CA  . LYS D  1 3   ? 6.114   0.640   -3.360 1.00 110.75 ? -6  LYS D CA  1 
ATOM   5244  C  C   . LYS D  1 3   ? 4.862   -0.183  -3.096 1.00 100.70 ? -6  LYS D C   1 
ATOM   5245  O  O   . LYS D  1 3   ? 3.855   0.312   -2.598 1.00 97.15  ? -6  LYS D O   1 
ATOM   5246  C  CB  . LYS D  1 3   ? 7.250   -0.301  -3.747 1.00 109.97 ? -6  LYS D CB  1 
ATOM   5247  C  CG  . LYS D  1 3   ? 7.113   -0.861  -5.148 1.00 116.72 ? -6  LYS D CG  1 
ATOM   5248  C  CD  . LYS D  1 3   ? 7.961   -2.094  -5.318 1.00 117.24 ? -6  LYS D CD  1 
ATOM   5249  C  CE  . LYS D  1 3   ? 9.371   -1.840  -4.840 1.00 118.62 ? -6  LYS D CE  1 
ATOM   5250  N  NZ  . LYS D  1 3   ? 10.207  -3.042  -5.044 1.00 119.19 ? -6  LYS D NZ  1 
ATOM   5251  N  N   . ASP D  1 4   ? 4.931   -1.451  -3.465 1.00 104.34 ? -5  ASP D N   1 
ATOM   5252  C  CA  . ASP D  1 4   ? 3.841   -2.374  -3.222 1.00 112.22 ? -5  ASP D CA  1 
ATOM   5253  C  C   . ASP D  1 4   ? 3.924   -2.817  -1.778 1.00 102.03 ? -5  ASP D C   1 
ATOM   5254  O  O   . ASP D  1 4   ? 2.920   -3.142  -1.152 1.00 105.38 ? -5  ASP D O   1 
ATOM   5255  C  CB  . ASP D  1 4   ? 3.937   -3.581  -4.168 1.00 121.55 ? -5  ASP D CB  1 
ATOM   5256  C  CG  . ASP D  1 4   ? 5.367   -4.063  -4.352 1.00 120.28 ? -5  ASP D CG  1 
ATOM   5257  O  OD1 . ASP D  1 4   ? 6.212   -3.736  -3.490 1.00 126.22 ? -5  ASP D OD1 1 
ATOM   5258  O  OD2 . ASP D  1 4   ? 5.648   -4.759  -5.351 1.00 102.20 ? -5  ASP D OD2 1 
ATOM   5259  N  N   . ASP D  1 5   ? 5.139   -2.815  -1.251 1.00 101.62 ? -4  ASP D N   1 
ATOM   5260  C  CA  . ASP D  1 5   ? 5.393   -3.347  0.077  1.00 98.33  ? -4  ASP D CA  1 
ATOM   5261  C  C   . ASP D  1 5   ? 5.233   -2.303  1.189  1.00 96.09  ? -4  ASP D C   1 
ATOM   5262  O  O   . ASP D  1 5   ? 5.322   -2.625  2.371  1.00 95.67  ? -4  ASP D O   1 
ATOM   5263  C  CB  . ASP D  1 5   ? 6.782   -3.957  0.121  1.00 101.17 ? -4  ASP D CB  1 
ATOM   5264  C  CG  . ASP D  1 5   ? 7.860   -2.932  -0.090 1.00 111.07 ? -4  ASP D CG  1 
ATOM   5265  O  OD1 . ASP D  1 5   ? 7.522   -1.791  -0.478 1.00 110.89 ? -4  ASP D OD1 1 
ATOM   5266  O  OD2 . ASP D  1 5   ? 9.043   -3.270  0.128  1.00 110.40 ? -4  ASP D OD2 1 
ATOM   5267  N  N   . ASP D  1 6   ? 5.015   -1.049  0.822  1.00 91.95  ? -3  ASP D N   1 
ATOM   5268  C  CA  . ASP D  1 6   ? 4.495   -0.106  1.790  1.00 82.99  ? -3  ASP D CA  1 
ATOM   5269  C  C   . ASP D  1 6   ? 3.106   -0.622  2.156  1.00 82.49  ? -3  ASP D C   1 
ATOM   5270  O  O   . ASP D  1 6   ? 2.693   -0.563  3.313  1.00 82.55  ? -3  ASP D O   1 
ATOM   5271  C  CB  . ASP D  1 6   ? 4.426   1.307   1.204  1.00 88.60  ? -3  ASP D CB  1 
ATOM   5272  C  CG  . ASP D  1 6   ? 3.747   2.301   2.137  1.00 76.54  ? -3  ASP D CG  1 
ATOM   5273  O  OD1 . ASP D  1 6   ? 2.504   2.328   2.182  1.00 69.71  ? -3  ASP D OD1 1 
ATOM   5274  O  OD2 . ASP D  1 6   ? 4.451   3.068   2.815  1.00 71.51  ? -3  ASP D OD2 1 
ATOM   5275  N  N   . ASP D  1 7   ? 2.391   -1.142  1.160  1.00 84.45  ? -2  ASP D N   1 
ATOM   5276  C  CA  . ASP D  1 7   ? 1.089   -1.764  1.383  1.00 87.38  ? -2  ASP D CA  1 
ATOM   5277  C  C   . ASP D  1 7   ? 1.193   -2.912  2.376  1.00 91.04  ? -2  ASP D C   1 
ATOM   5278  O  O   . ASP D  1 7   ? 0.251   -3.179  3.127  1.00 87.36  ? -2  ASP D O   1 
ATOM   5279  C  CB  . ASP D  1 7   ? 0.495   -2.290  0.077  1.00 92.59  ? -2  ASP D CB  1 
ATOM   5280  C  CG  . ASP D  1 7   ? -0.212  -1.220  -0.716 1.00 103.32 ? -2  ASP D CG  1 
ATOM   5281  O  OD1 . ASP D  1 7   ? -0.395  -0.099  -0.193 1.00 97.16  ? -2  ASP D OD1 1 
ATOM   5282  O  OD2 . ASP D  1 7   ? -0.600  -1.512  -1.864 1.00 103.78 ? -2  ASP D OD2 1 
ATOM   5283  N  N   . LYS D  1 8   ? 2.330   -3.607  2.360  1.00 89.16  ? -1  LYS D N   1 
ATOM   5284  C  CA  . LYS D  1 8   ? 2.602   -4.645  3.350  1.00 82.26  ? -1  LYS D CA  1 
ATOM   5285  C  C   . LYS D  1 8   ? 2.628   -4.045  4.749  1.00 81.98  ? -1  LYS D C   1 
ATOM   5286  O  O   . LYS D  1 8   ? 2.121   -4.655  5.690  1.00 82.40  ? -1  LYS D O   1 
ATOM   5287  C  CB  . LYS D  1 8   ? 3.941   -5.330  3.088  1.00 86.06  ? -1  LYS D CB  1 
ATOM   5288  C  CG  . LYS D  1 8   ? 3.969   -6.296  1.930  1.00 92.93  ? -1  LYS D CG  1 
ATOM   5289  C  CD  . LYS D  1 8   ? 5.384   -6.818  1.746  1.00 93.66  ? -1  LYS D CD  1 
ATOM   5290  C  CE  . LYS D  1 8   ? 5.439   -7.961  0.750  1.00 101.44 ? -1  LYS D CE  1 
ATOM   5291  N  NZ  . LYS D  1 8   ? 5.050   -9.251  1.396  1.00 102.65 ? -1  LYS D NZ  1 
ATOM   5292  N  N   . LEU D  1 9   ? 3.229   -2.862  4.887  1.00 71.63  ? 0   LEU D N   1 
ATOM   5293  C  CA  . LEU D  1 9   ? 3.268   -2.183  6.175  1.00 68.50  ? 0   LEU D CA  1 
ATOM   5294  C  C   . LEU D  1 9   ? 1.884   -1.820  6.649  1.00 66.42  ? 0   LEU D C   1 
ATOM   5295  O  O   . LEU D  1 9   ? 1.489   -2.148  7.756  1.00 69.48  ? 0   LEU D O   1 
ATOM   5296  C  CB  . LEU D  1 9   ? 4.101   -0.919  6.111  1.00 70.91  ? 0   LEU D CB  1 
ATOM   5297  C  CG  . LEU D  1 9   ? 5.579   -1.100  6.393  1.00 71.13  ? 0   LEU D CG  1 
ATOM   5298  C  CD1 . LEU D  1 9   ? 6.186   -2.004  5.336  1.00 79.24  ? 0   LEU D CD1 1 
ATOM   5299  C  CD2 . LEU D  1 9   ? 6.232   0.247   6.397  1.00 53.20  ? 0   LEU D CD2 1 
ATOM   5300  N  N   . HIS D  1 10  ? 1.133   -1.132  5.816  1.00 63.07  ? 1   HIS D N   1 
ATOM   5301  C  CA  . HIS D  1 10  ? -0.155  -0.672  6.275  1.00 69.07  ? 1   HIS D CA  1 
ATOM   5302  C  C   . HIS D  1 10  ? -0.999  -1.830  6.749  1.00 70.13  ? 1   HIS D C   1 
ATOM   5303  O  O   . HIS D  1 10  ? -1.774  -1.697  7.688  1.00 73.89  ? 1   HIS D O   1 
ATOM   5304  C  CB  . HIS D  1 10  ? -0.851  0.110   5.186  1.00 74.02  ? 1   HIS D CB  1 
ATOM   5305  C  CG  . HIS D  1 10  ? -0.183  1.425   4.880  1.00 72.19  ? 1   HIS D CG  1 
ATOM   5306  N  ND1 . HIS D  1 10  ? -0.857  2.591   4.857  1.00 74.70  ? 1   HIS D ND1 1 
ATOM   5307  C  CD2 . HIS D  1 10  ? 1.126   1.685   4.627  1.00 71.09  ? 1   HIS D CD2 1 
ATOM   5308  C  CE1 . HIS D  1 10  ? 0.012   3.586   4.574  1.00 66.06  ? 1   HIS D CE1 1 
ATOM   5309  N  NE2 . HIS D  1 10  ? 1.192   3.050   4.446  1.00 65.62  ? 1   HIS D NE2 1 
ATOM   5310  N  N   . SER D  1 11  ? -0.833  -2.978  6.109  1.00 72.81  ? 2   SER D N   1 
ATOM   5311  C  CA  . SER D  1 11  ? -1.620  -4.146  6.474  1.00 75.84  ? 2   SER D CA  1 
ATOM   5312  C  C   . SER D  1 11  ? -1.176  -4.677  7.831  1.00 72.20  ? 2   SER D C   1 
ATOM   5313  O  O   . SER D  1 11  ? -2.012  -5.058  8.647  1.00 69.73  ? 2   SER D O   1 
ATOM   5314  C  CB  . SER D  1 11  ? -1.570  -5.235  5.389  1.00 72.80  ? 2   SER D CB  1 
ATOM   5315  O  OG  . SER D  1 11  ? -0.317  -5.885  5.372  1.00 72.43  ? 2   SER D OG  1 
ATOM   5316  N  N   . GLN D  1 12  ? 0.131   -4.696  8.079  1.00 70.42  ? 3   GLN D N   1 
ATOM   5317  C  CA  . GLN D  1 12  ? 0.622   -5.081  9.399  1.00 70.22  ? 3   GLN D CA  1 
ATOM   5318  C  C   . GLN D  1 12  ? 0.093   -4.098  10.420 1.00 70.68  ? 3   GLN D C   1 
ATOM   5319  O  O   . GLN D  1 12  ? -0.518  -4.491  11.404 1.00 72.41  ? 3   GLN D O   1 
ATOM   5320  C  CB  . GLN D  1 12  ? 2.145   -5.115  9.453  1.00 69.84  ? 3   GLN D CB  1 
ATOM   5321  C  CG  . GLN D  1 12  ? 2.758   -6.315  8.776  1.00 74.72  ? 3   GLN D CG  1 
ATOM   5322  C  CD  . GLN D  1 12  ? 4.266   -6.242  8.727  1.00 81.08  ? 3   GLN D CD  1 
ATOM   5323  O  OE1 . GLN D  1 12  ? 4.901   -5.634  9.588  1.00 83.79  ? 3   GLN D OE1 1 
ATOM   5324  N  NE2 . GLN D  1 12  ? 4.850   -6.857  7.711  1.00 85.66  ? 3   GLN D NE2 1 
ATOM   5325  N  N   . ALA D  1 13  ? 0.322   -2.814  10.172 1.00 67.64  ? 4   ALA D N   1 
ATOM   5326  C  CA  . ALA D  1 13  ? -0.161  -1.771  11.056 1.00 65.48  ? 4   ALA D CA  1 
ATOM   5327  C  C   . ALA D  1 13  ? -1.668  -1.867  11.287 1.00 68.48  ? 4   ALA D C   1 
ATOM   5328  O  O   . ALA D  1 13  ? -2.144  -1.714  12.415 1.00 67.08  ? 4   ALA D O   1 
ATOM   5329  C  CB  . ALA D  1 13  ? 0.196   -0.436  10.504 1.00 63.15  ? 4   ALA D CB  1 
ATOM   5330  N  N   . ASN D  1 14  ? -2.416  -2.117  10.220 1.00 61.89  ? 5   ASN D N   1 
ATOM   5331  C  CA  . ASN D  1 14  ? -3.865  -2.248  10.327 1.00 62.32  ? 5   ASN D CA  1 
ATOM   5332  C  C   . ASN D  1 14  ? -4.299  -3.415  11.194 1.00 64.19  ? 5   ASN D C   1 
ATOM   5333  O  O   . ASN D  1 14  ? -5.332  -3.373  11.846 1.00 64.98  ? 5   ASN D O   1 
ATOM   5334  C  CB  . ASN D  1 14  ? -4.487  -2.408  8.950  1.00 66.39  ? 5   ASN D CB  1 
ATOM   5335  C  CG  . ASN D  1 14  ? -4.628  -1.103  8.230  1.00 67.71  ? 5   ASN D CG  1 
ATOM   5336  O  OD1 . ASN D  1 14  ? -4.918  -0.077  8.842  1.00 65.01  ? 5   ASN D OD1 1 
ATOM   5337  N  ND2 . ASN D  1 14  ? -4.429  -1.129  6.917  1.00 67.94  ? 5   ASN D ND2 1 
ATOM   5338  N  N   . LEU D  1 15  ? -3.523  -4.481  11.170 1.00 65.49  ? 6   LEU D N   1 
ATOM   5339  C  CA  . LEU D  1 15  ? -3.874  -5.654  11.939 1.00 64.50  ? 6   LEU D CA  1 
ATOM   5340  C  C   . LEU D  1 15  ? -3.673  -5.336  13.400 1.00 65.08  ? 6   LEU D C   1 
ATOM   5341  O  O   . LEU D  1 15  ? -4.574  -5.524  14.199 1.00 72.84  ? 6   LEU D O   1 
ATOM   5342  C  CB  . LEU D  1 15  ? -3.008  -6.842  11.527 1.00 66.71  ? 6   LEU D CB  1 
ATOM   5343  C  CG  . LEU D  1 15  ? -3.362  -8.224  12.064 1.00 61.00  ? 6   LEU D CG  1 
ATOM   5344  C  CD1 . LEU D  1 15  ? -4.850  -8.489  11.928 1.00 61.86  ? 6   LEU D CD1 1 
ATOM   5345  C  CD2 . LEU D  1 15  ? -2.550  -9.261  11.323 1.00 57.97  ? 6   LEU D CD2 1 
ATOM   5346  N  N   . MET D  1 16  ? -2.485  -4.842  13.735 1.00 66.51  ? 7   MET D N   1 
ATOM   5347  C  CA  . MET D  1 16  ? -2.148  -4.499  15.104 1.00 63.80  ? 7   MET D CA  1 
ATOM   5348  C  C   . MET D  1 16  ? -3.258  -3.627  15.657 1.00 65.67  ? 7   MET D C   1 
ATOM   5349  O  O   . MET D  1 16  ? -3.810  -3.889  16.723 1.00 64.05  ? 7   MET D O   1 
ATOM   5350  C  CB  . MET D  1 16  ? -0.825  -3.738  15.143 1.00 68.77  ? 7   MET D CB  1 
ATOM   5351  C  CG  . MET D  1 16  ? 0.343   -4.437  14.456 1.00 72.62  ? 7   MET D CG  1 
ATOM   5352  S  SD  . MET D  1 16  ? 1.901   -4.273  15.365 1.00 108.09 ? 7   MET D SD  1 
ATOM   5353  C  CE  . MET D  1 16  ? 3.120   -4.678  14.121 1.00 86.56  ? 7   MET D CE  1 
ATOM   5354  N  N   . ARG D  1 17  ? -3.595  -2.600  14.891 1.00 65.93  ? 8   ARG D N   1 
ATOM   5355  C  CA  . ARG D  1 17  ? -4.635  -1.654  15.253 1.00 63.18  ? 8   ARG D CA  1 
ATOM   5356  C  C   . ARG D  1 17  ? -5.958  -2.352  15.548 1.00 59.79  ? 8   ARG D C   1 
ATOM   5357  O  O   . ARG D  1 17  ? -6.593  -2.084  16.556 1.00 62.68  ? 8   ARG D O   1 
ATOM   5358  C  CB  . ARG D  1 17  ? -4.800  -0.629  14.130 1.00 63.06  ? 8   ARG D CB  1 
ATOM   5359  C  CG  . ARG D  1 17  ? -5.399  0.688   14.567 1.00 63.75  ? 8   ARG D CG  1 
ATOM   5360  C  CD  . ARG D  1 17  ? -4.958  1.787   13.647 1.00 57.79  ? 8   ARG D CD  1 
ATOM   5361  N  NE  . ARG D  1 17  ? -5.285  1.446   12.275 1.00 63.73  ? 8   ARG D NE  1 
ATOM   5362  C  CZ  . ARG D  1 17  ? -6.517  1.497   11.775 1.00 67.34  ? 8   ARG D CZ  1 
ATOM   5363  N  NH1 . ARG D  1 17  ? -7.536  1.880   12.546 1.00 53.14  ? 8   ARG D NH1 1 
ATOM   5364  N  NH2 . ARG D  1 17  ? -6.730  1.153   10.506 1.00 55.87  ? 8   ARG D NH2 1 
ATOM   5365  N  N   . LEU D  1 18  ? -6.393  -3.253  14.701 1.00 61.67  ? 9   LEU D N   1 
ATOM   5366  C  CA  . LEU D  1 18  ? -7.649  -3.903  14.963 1.00 60.81  ? 9   LEU D CA  1 
ATOM   5367  C  C   . LEU D  1 18  ? -7.596  -4.681  16.237 1.00 65.50  ? 9   LEU D C   1 
ATOM   5368  O  O   . LEU D  1 18  ? -8.488  -4.640  17.066 1.00 73.01  ? 9   LEU D O   1 
ATOM   5369  C  CB  . LEU D  1 18  ? -7.937  -4.857  13.831 1.00 56.45  ? 9   LEU D CB  1 
ATOM   5370  C  CG  . LEU D  1 18  ? -9.089  -5.828  13.964 1.00 61.41  ? 9   LEU D CG  1 
ATOM   5371  C  CD1 . LEU D  1 18  ? -10.290 -5.138  14.447 1.00 63.32  ? 9   LEU D CD1 1 
ATOM   5372  C  CD2 . LEU D  1 18  ? -9.354  -6.380  12.643 1.00 55.33  ? 9   LEU D CD2 1 
ATOM   5373  N  N   . LYS D  1 19  ? -6.524  -5.402  16.414 1.00 65.22  ? 10  LYS D N   1 
ATOM   5374  C  CA  . LYS D  1 19  ? -6.430  -6.201  17.589 1.00 70.21  ? 10  LYS D CA  1 
ATOM   5375  C  C   . LYS D  1 19  ? -6.413  -5.310  18.788 1.00 69.29  ? 10  LYS D C   1 
ATOM   5376  O  O   . LYS D  1 19  ? -7.010  -5.606  19.789 1.00 71.38  ? 10  LYS D O   1 
ATOM   5377  C  CB  . LYS D  1 19  ? -5.204  -7.082  17.522 1.00 66.21  ? 10  LYS D CB  1 
ATOM   5378  C  CG  . LYS D  1 19  ? -5.400  -8.319  16.674 1.00 66.52  ? 10  LYS D CG  1 
ATOM   5379  C  CD  . LYS D  1 19  ? -4.091  -9.022  16.507 1.00 66.68  ? 10  LYS D CD  1 
ATOM   5380  C  CE  . LYS D  1 19  ? -4.238  -10.501 16.420 1.00 70.87  ? 10  LYS D CE  1 
ATOM   5381  N  NZ  . LYS D  1 19  ? -2.954  -11.174 16.705 1.00 76.02  ? 10  LYS D NZ  1 
ATOM   5382  N  N   . SER D  1 20  ? -5.719  -4.202  18.691 1.00 68.05  ? 11  SER D N   1 
ATOM   5383  C  CA  . SER D  1 20  ? -5.672  -3.311  19.811 1.00 78.33  ? 11  SER D CA  1 
ATOM   5384  C  C   . SER D  1 20  ? -7.050  -2.826  20.099 1.00 78.76  ? 11  SER D C   1 
ATOM   5385  O  O   . SER D  1 20  ? -7.450  -2.719  21.228 1.00 86.09  ? 11  SER D O   1 
ATOM   5386  C  CB  . SER D  1 20  ? -4.801  -2.118  19.503 1.00 78.29  ? 11  SER D CB  1 
ATOM   5387  O  OG  . SER D  1 20  ? -3.475  -2.356  19.895 1.00 84.34  ? 11  SER D OG  1 
ATOM   5388  N  N   . ASP D  1 21  ? -7.806  -2.519  19.077 1.00 72.29  ? 12  ASP D N   1 
ATOM   5389  C  CA  . ASP D  1 21  ? -9.090  -2.002  19.393 1.00 72.09  ? 12  ASP D CA  1 
ATOM   5390  C  C   . ASP D  1 21  ? -9.844  -3.027  20.159 1.00 76.32  ? 12  ASP D C   1 
ATOM   5391  O  O   . ASP D  1 21  ? -10.448 -2.722  21.157 1.00 93.45  ? 12  ASP D O   1 
ATOM   5392  C  CB  . ASP D  1 21  ? -9.862  -1.689  18.141 1.00 70.65  ? 12  ASP D CB  1 
ATOM   5393  C  CG  . ASP D  1 21  ? -9.313  -0.520  17.407 1.00 77.15  ? 12  ASP D CG  1 
ATOM   5394  O  OD1 . ASP D  1 21  ? -8.115  -0.269  17.503 1.00 80.14  ? 12  ASP D OD1 1 
ATOM   5395  O  OD2 . ASP D  1 21  ? -10.091 0.174   16.750 1.00 78.63  ? 12  ASP D OD2 1 
ATOM   5396  N  N   . LEU D  1 22  ? -9.821  -4.257  19.670 1.00 76.11  ? 13  LEU D N   1 
ATOM   5397  C  CA  . LEU D  1 22  ? -10.516 -5.395  20.277 1.00 77.38  ? 13  LEU D CA  1 
ATOM   5398  C  C   . LEU D  1 22  ? -10.127 -5.999  21.646 1.00 81.64  ? 13  LEU D C   1 
ATOM   5399  O  O   . LEU D  1 22  ? -11.005 -6.445  22.384 1.00 96.52  ? 13  LEU D O   1 
ATOM   5400  C  CB  . LEU D  1 22  ? -10.610 -6.534  19.252 1.00 79.32  ? 13  LEU D CB  1 
ATOM   5401  C  CG  . LEU D  1 22  ? -11.353 -6.216  17.952 1.00 62.88  ? 13  LEU D CG  1 
ATOM   5402  C  CD1 . LEU D  1 22  ? -11.330 -7.413  17.014 1.00 64.52  ? 13  LEU D CD1 1 
ATOM   5403  C  CD2 . LEU D  1 22  ? -12.782 -5.783  18.241 1.00 79.30  ? 13  LEU D CD2 1 
ATOM   5404  N  N   . PHE D  1 23  ? -8.836  -6.059  21.971 1.00 77.79  ? 14  PHE D N   1 
ATOM   5405  C  CA  . PHE D  1 23  ? -8.397  -6.731  23.200 1.00 85.23  ? 14  PHE D CA  1 
ATOM   5406  C  C   . PHE D  1 23  ? -7.817  -5.836  24.285 1.00 94.75  ? 14  PHE D C   1 
ATOM   5407  O  O   . PHE D  1 23  ? -7.452  -6.310  25.368 1.00 87.86  ? 14  PHE D O   1 
ATOM   5408  C  CB  . PHE D  1 23  ? -7.412  -7.845  22.868 1.00 90.52  ? 14  PHE D CB  1 
ATOM   5409  C  CG  . PHE D  1 23  ? -7.998  -8.926  22.007 1.00 90.06  ? 14  PHE D CG  1 
ATOM   5410  C  CD1 . PHE D  1 23  ? -9.231  -9.484  22.320 1.00 81.85  ? 14  PHE D CD1 1 
ATOM   5411  C  CD2 . PHE D  1 23  ? -7.326  -9.370  20.877 1.00 75.26  ? 14  PHE D CD2 1 
ATOM   5412  C  CE1 . PHE D  1 23  ? -9.770  -10.462 21.536 1.00 74.42  ? 14  PHE D CE1 1 
ATOM   5413  C  CE2 . PHE D  1 23  ? -7.859  -10.348 20.088 1.00 70.85  ? 14  PHE D CE2 1 
ATOM   5414  C  CZ  . PHE D  1 23  ? -9.082  -10.895 20.410 1.00 78.83  ? 14  PHE D CZ  1 
ATOM   5415  N  N   . ASN D  1 24  ? -7.745  -4.544  23.987 1.00 102.09 ? 15  ASN D N   1 
ATOM   5416  C  CA  . ASN D  1 24  ? -7.118  -3.552  24.864 1.00 107.54 ? 15  ASN D CA  1 
ATOM   5417  C  C   . ASN D  1 24  ? -8.081  -2.398  25.150 1.00 106.39 ? 15  ASN D C   1 
ATOM   5418  O  O   . ASN D  1 24  ? -8.391  -2.108  26.311 1.00 104.13 ? 15  ASN D O   1 
ATOM   5419  C  CB  . ASN D  1 24  ? -5.799  -3.040  24.266 1.00 105.89 ? 15  ASN D CB  1 
ATOM   5420  C  CG  . ASN D  1 24  ? -4.742  -4.131  24.154 1.00 103.20 ? 15  ASN D CG  1 
ATOM   5421  O  OD1 . ASN D  1 24  ? -5.027  -5.316  24.359 1.00 105.45 ? 15  ASN D OD1 1 
ATOM   5422  N  ND2 . ASN D  1 24  ? -3.517  -3.735  23.818 1.00 98.61  ? 15  ASN D ND2 1 
ATOM   5423  N  N   . ARG D  1 25  ? -8.480  -1.701  24.086 1.00 99.11  ? 16  ARG D N   1 
ATOM   5424  C  CA  . ARG D  1 25  ? -9.560  -0.720  24.141 1.00 99.06  ? 16  ARG D CA  1 
ATOM   5425  C  C   . ARG D  1 25  ? -10.802 -1.332  24.762 1.00 105.43 ? 16  ARG D C   1 
ATOM   5426  O  O   . ARG D  1 25  ? -11.534 -0.662  25.486 1.00 111.75 ? 16  ARG D O   1 
ATOM   5427  C  CB  . ARG D  1 25  ? -9.928  -0.218  22.747 1.00 101.57 ? 16  ARG D CB  1 
ATOM   5428  C  CG  . ARG D  1 25  ? -8.959  0.769   22.110 1.00 108.18 ? 16  ARG D CG  1 
ATOM   5429  C  CD  . ARG D  1 25  ? -7.518  0.282   22.176 1.00 116.59 ? 16  ARG D CD  1 
ATOM   5430  N  NE  . ARG D  1 25  ? -6.570  1.111   21.426 1.00 120.17 ? 16  ARG D NE  1 
ATOM   5431  C  CZ  . ARG D  1 25  ? -5.293  0.778   21.250 1.00 122.96 ? 16  ARG D CZ  1 
ATOM   5432  N  NH1 . ARG D  1 25  ? -4.836  -0.358  21.773 1.00 127.05 ? 16  ARG D NH1 1 
ATOM   5433  N  NH2 . ARG D  1 25  ? -4.473  1.563   20.558 1.00 112.64 ? 16  ARG D NH2 1 
ATOM   5434  N  N   . SER D  1 26  ? -11.062 -2.600  24.475 1.00 98.64  ? 17  SER D N   1 
ATOM   5435  C  CA  . SER D  1 26  ? -12.230 -3.239  25.078 1.00 110.27 ? 17  SER D CA  1 
ATOM   5436  C  C   . SER D  1 26  ? -11.901 -4.460  25.960 1.00 113.23 ? 17  SER D C   1 
ATOM   5437  O  O   . SER D  1 26  ? -10.907 -5.156  25.730 1.00 112.61 ? 17  SER D O   1 
ATOM   5438  C  CB  . SER D  1 26  ? -13.293 -3.547  24.017 1.00 104.05 ? 17  SER D CB  1 
ATOM   5439  O  OG  . SER D  1 26  ? -13.914 -2.350  23.579 1.00 86.83  ? 17  SER D OG  1 
ATOM   5440  N  N   . PRO D  1 27  ? -12.745 -4.713  26.978 1.00 117.14 ? 18  PRO D N   1 
ATOM   5441  C  CA  . PRO D  1 27  ? -12.530 -5.724  28.021 1.00 107.28 ? 18  PRO D CA  1 
ATOM   5442  C  C   . PRO D  1 27  ? -12.718 -7.103  27.440 1.00 111.67 ? 18  PRO D C   1 
ATOM   5443  O  O   . PRO D  1 27  ? -13.426 -7.229  26.440 1.00 107.34 ? 18  PRO D O   1 
ATOM   5444  C  CB  . PRO D  1 27  ? -13.682 -5.462  28.981 1.00 104.32 ? 18  PRO D CB  1 
ATOM   5445  C  CG  . PRO D  1 27  ? -14.790 -5.015  28.073 1.00 114.94 ? 18  PRO D CG  1 
ATOM   5446  C  CD  . PRO D  1 27  ? -14.110 -4.157  27.035 1.00 115.69 ? 18  PRO D CD  1 
ATOM   5447  N  N   . MET D  1 28  ? -12.122 -8.128  28.039 1.00 112.72 ? 19  MET D N   1 
ATOM   5448  C  CA  . MET D  1 28  ? -12.429 -9.471  27.573 1.00 107.62 ? 19  MET D CA  1 
ATOM   5449  C  C   . MET D  1 28  ? -13.846 -9.870  27.978 1.00 104.32 ? 19  MET D C   1 
ATOM   5450  O  O   . MET D  1 28  ? -14.344 -9.492  29.046 1.00 95.26  ? 19  MET D O   1 
ATOM   5451  C  CB  . MET D  1 28  ? -11.419 -10.521 28.032 1.00 99.60  ? 19  MET D CB  1 
ATOM   5452  C  CG  . MET D  1 28  ? -11.936 -11.937 27.774 1.00 95.81  ? 19  MET D CG  1 
ATOM   5453  S  SD  . MET D  1 28  ? -10.694 -13.146 27.337 1.00 97.86  ? 19  MET D SD  1 
ATOM   5454  C  CE  . MET D  1 28  ? -11.276 -14.570 28.277 1.00 81.93  ? 19  MET D CE  1 
ATOM   5455  N  N   . TYR D  1 29  ? -14.481 -10.630 27.093 1.00 96.27  ? 20  TYR D N   1 
ATOM   5456  C  CA  . TYR D  1 29  ? -15.846 -11.100 27.253 1.00 84.90  ? 20  TYR D CA  1 
ATOM   5457  C  C   . TYR D  1 29  ? -16.066 -11.863 28.575 1.00 87.91  ? 20  TYR D C   1 
ATOM   5458  O  O   . TYR D  1 29  ? -15.335 -12.808 28.895 1.00 87.56  ? 20  TYR D O   1 
ATOM   5459  C  CB  . TYR D  1 29  ? -16.166 -11.971 26.046 1.00 77.59  ? 20  TYR D CB  1 
ATOM   5460  C  CG  . TYR D  1 29  ? -17.588 -12.425 25.919 1.00 74.90  ? 20  TYR D CG  1 
ATOM   5461  C  CD1 . TYR D  1 29  ? -17.895 -13.777 25.917 1.00 72.48  ? 20  TYR D CD1 1 
ATOM   5462  C  CD2 . TYR D  1 29  ? -18.619 -11.514 25.779 1.00 70.10  ? 20  TYR D CD2 1 
ATOM   5463  C  CE1 . TYR D  1 29  ? -19.179 -14.211 25.788 1.00 71.14  ? 20  TYR D CE1 1 
ATOM   5464  C  CE2 . TYR D  1 29  ? -19.914 -11.937 25.652 1.00 74.73  ? 20  TYR D CE2 1 
ATOM   5465  C  CZ  . TYR D  1 29  ? -20.191 -13.292 25.654 1.00 77.21  ? 20  TYR D CZ  1 
ATOM   5466  O  OH  . TYR D  1 29  ? -21.487 -13.746 25.517 1.00 81.13  ? 20  TYR D OH  1 
ATOM   5467  N  N   . PRO D  1 30  ? -17.063 -11.429 29.359 1.00 79.94  ? 21  PRO D N   1 
ATOM   5468  C  CA  . PRO D  1 30  ? -17.459 -12.017 30.643 1.00 74.47  ? 21  PRO D CA  1 
ATOM   5469  C  C   . PRO D  1 30  ? -18.081 -13.392 30.473 1.00 76.27  ? 21  PRO D C   1 
ATOM   5470  O  O   . PRO D  1 30  ? -18.250 -14.118 31.452 1.00 83.06  ? 21  PRO D O   1 
ATOM   5471  C  CB  . PRO D  1 30  ? -18.492 -11.027 31.177 1.00 74.35  ? 21  PRO D CB  1 
ATOM   5472  C  CG  . PRO D  1 30  ? -19.045 -10.383 29.974 1.00 78.01  ? 21  PRO D CG  1 
ATOM   5473  C  CD  . PRO D  1 30  ? -17.907 -10.280 29.006 1.00 80.26  ? 21  PRO D CD  1 
ATOM   5474  N  N   . GLY D  1 31  ? -18.454 -13.729 29.246 1.00 71.19  ? 22  GLY D N   1 
ATOM   5475  C  CA  . GLY D  1 31  ? -19.070 -15.012 28.971 1.00 71.39  ? 22  GLY D CA  1 
ATOM   5476  C  C   . GLY D  1 31  ? -20.565 -14.829 28.909 1.00 77.34  ? 22  GLY D C   1 
ATOM   5477  O  O   . GLY D  1 31  ? -21.074 -13.811 29.371 1.00 79.65  ? 22  GLY D O   1 
ATOM   5478  N  N   . PRO D  1 32  ? -21.281 -15.812 28.346 1.00 75.34  ? 23  PRO D N   1 
ATOM   5479  C  CA  . PRO D  1 32  ? -22.731 -15.699 28.179 1.00 68.74  ? 23  PRO D CA  1 
ATOM   5480  C  C   . PRO D  1 32  ? -23.470 -15.652 29.510 1.00 76.01  ? 23  PRO D C   1 
ATOM   5481  O  O   . PRO D  1 32  ? -23.006 -16.166 30.533 1.00 70.85  ? 23  PRO D O   1 
ATOM   5482  C  CB  . PRO D  1 32  ? -23.094 -16.969 27.412 1.00 69.11  ? 23  PRO D CB  1 
ATOM   5483  C  CG  . PRO D  1 32  ? -22.040 -17.932 27.786 1.00 72.18  ? 23  PRO D CG  1 
ATOM   5484  C  CD  . PRO D  1 32  ? -20.782 -17.135 27.940 1.00 71.50  ? 23  PRO D CD  1 
ATOM   5485  N  N   . THR D  1 33  ? -24.632 -15.020 29.475 1.00 76.38  ? 24  THR D N   1 
ATOM   5486  C  CA  . THR D  1 33  ? -25.470 -14.828 30.643 1.00 77.15  ? 24  THR D CA  1 
ATOM   5487  C  C   . THR D  1 33  ? -26.872 -15.191 30.202 1.00 82.41  ? 24  THR D C   1 
ATOM   5488  O  O   . THR D  1 33  ? -27.110 -15.379 29.012 1.00 80.25  ? 24  THR D O   1 
ATOM   5489  C  CB  . THR D  1 33  ? -25.468 -13.359 31.105 1.00 82.47  ? 24  THR D CB  1 
ATOM   5490  O  OG1 . THR D  1 33  ? -26.269 -12.565 30.218 1.00 82.70  ? 24  THR D OG1 1 
ATOM   5491  C  CG2 . THR D  1 33  ? -24.051 -12.800 31.134 1.00 84.35  ? 24  THR D CG2 1 
ATOM   5492  N  N   . LYS D  1 34  ? -27.794 -15.320 31.147 1.00 86.81  ? 25  LYS D N   1 
ATOM   5493  C  CA  . LYS D  1 34  ? -29.190 -15.566 30.799 1.00 84.93  ? 25  LYS D CA  1 
ATOM   5494  C  C   . LYS D  1 34  ? -29.695 -14.499 29.820 1.00 84.52  ? 25  LYS D C   1 
ATOM   5495  O  O   . LYS D  1 34  ? -30.519 -14.794 28.952 1.00 81.17  ? 25  LYS D O   1 
ATOM   5496  C  CB  . LYS D  1 34  ? -30.061 -15.575 32.061 1.00 83.56  ? 25  LYS D CB  1 
ATOM   5497  C  CG  . LYS D  1 34  ? -30.103 -14.230 32.785 1.00 86.60  ? 25  LYS D CG  1 
ATOM   5498  C  CD  . LYS D  1 34  ? -30.732 -14.330 34.167 1.00 87.64  ? 25  LYS D CD  1 
ATOM   5499  C  CE  . LYS D  1 34  ? -30.566 -13.026 34.937 1.00 93.38  ? 25  LYS D CE  1 
ATOM   5500  N  NZ  . LYS D  1 34  ? -30.866 -13.178 36.386 1.00 77.84  ? 25  LYS D NZ  1 
ATOM   5501  N  N   . ASP D  1 35  ? -29.185 -13.272 29.965 1.00 75.69  ? 26  ASP D N   1 
ATOM   5502  C  CA  . ASP D  1 35  ? -29.624 -12.128 29.165 1.00 78.78  ? 26  ASP D CA  1 
ATOM   5503  C  C   . ASP D  1 35  ? -28.747 -11.919 27.939 1.00 84.00  ? 26  ASP D C   1 
ATOM   5504  O  O   . ASP D  1 35  ? -28.956 -11.004 27.142 1.00 84.76  ? 26  ASP D O   1 
ATOM   5505  C  CB  . ASP D  1 35  ? -29.656 -10.856 30.009 1.00 76.96  ? 26  ASP D CB  1 
ATOM   5506  C  CG  . ASP D  1 35  ? -30.485 -11.019 31.260 1.00 87.45  ? 26  ASP D CG  1 
ATOM   5507  O  OD1 . ASP D  1 35  ? -31.726 -11.111 31.144 1.00 86.49  ? 26  ASP D OD1 1 
ATOM   5508  O  OD2 . ASP D  1 35  ? -29.896 -11.059 32.361 1.00 88.93  ? 26  ASP D OD2 1 
ATOM   5509  N  N   . ASP D  1 36  ? -27.750 -12.778 27.806 1.00 85.59  ? 27  ASP D N   1 
ATOM   5510  C  CA  . ASP D  1 36  ? -26.913 -12.795 26.625 1.00 81.67  ? 27  ASP D CA  1 
ATOM   5511  C  C   . ASP D  1 36  ? -26.628 -14.247 26.261 1.00 77.78  ? 27  ASP D C   1 
ATOM   5512  O  O   . ASP D  1 36  ? -25.488 -14.693 26.319 1.00 78.22  ? 27  ASP D O   1 
ATOM   5513  C  CB  . ASP D  1 36  ? -25.607 -12.061 26.910 1.00 82.55  ? 27  ASP D CB  1 
ATOM   5514  C  CG  . ASP D  1 36  ? -25.087 -11.325 25.709 1.00 85.20  ? 27  ASP D CG  1 
ATOM   5515  O  OD1 . ASP D  1 36  ? -25.684 -11.481 24.625 1.00 94.07  ? 27  ASP D OD1 1 
ATOM   5516  O  OD2 . ASP D  1 36  ? -24.081 -10.599 25.846 1.00 79.46  ? 27  ASP D OD2 1 
ATOM   5517  N  N   . PRO D  1 37  ? -27.674 -14.998 25.889 1.00 79.57  ? 28  PRO D N   1 
ATOM   5518  C  CA  . PRO D  1 37  ? -27.433 -16.399 25.550 1.00 70.41  ? 28  PRO D CA  1 
ATOM   5519  C  C   . PRO D  1 37  ? -26.516 -16.482 24.346 1.00 66.92  ? 28  PRO D C   1 
ATOM   5520  O  O   . PRO D  1 37  ? -26.436 -15.545 23.566 1.00 72.62  ? 28  PRO D O   1 
ATOM   5521  C  CB  . PRO D  1 37  ? -28.826 -16.921 25.206 1.00 70.47  ? 28  PRO D CB  1 
ATOM   5522  C  CG  . PRO D  1 37  ? -29.584 -15.723 24.793 1.00 81.19  ? 28  PRO D CG  1 
ATOM   5523  C  CD  . PRO D  1 37  ? -29.069 -14.599 25.638 1.00 80.62  ? 28  PRO D CD  1 
ATOM   5524  N  N   . LEU D  1 38  ? -25.814 -17.596 24.217 1.00 68.63  ? 29  LEU D N   1 
ATOM   5525  C  CA  . LEU D  1 38  ? -24.861 -17.790 23.140 1.00 66.13  ? 29  LEU D CA  1 
ATOM   5526  C  C   . LEU D  1 38  ? -25.045 -19.174 22.528 1.00 69.73  ? 29  LEU D C   1 
ATOM   5527  O  O   . LEU D  1 38  ? -25.368 -20.131 23.226 1.00 69.85  ? 29  LEU D O   1 
ATOM   5528  C  CB  . LEU D  1 38  ? -23.450 -17.666 23.688 1.00 68.06  ? 29  LEU D CB  1 
ATOM   5529  C  CG  . LEU D  1 38  ? -22.372 -17.926 22.655 1.00 60.44  ? 29  LEU D CG  1 
ATOM   5530  C  CD1 . LEU D  1 38  ? -22.349 -16.772 21.691 1.00 68.86  ? 29  LEU D CD1 1 
ATOM   5531  C  CD2 . LEU D  1 38  ? -21.045 -18.072 23.347 1.00 70.99  ? 29  LEU D CD2 1 
ATOM   5532  N  N   . THR D  1 39  ? -24.850 -19.282 21.221 1.00 72.91  ? 30  THR D N   1 
ATOM   5533  C  CA  . THR D  1 39  ? -24.968 -20.570 20.557 1.00 65.56  ? 30  THR D CA  1 
ATOM   5534  C  C   . THR D  1 39  ? -23.597 -21.039 20.141 1.00 56.93  ? 30  THR D C   1 
ATOM   5535  O  O   . THR D  1 39  ? -22.842 -20.295 19.529 1.00 63.90  ? 30  THR D O   1 
ATOM   5536  C  CB  . THR D  1 39  ? -25.837 -20.487 19.295 1.00 79.61  ? 30  THR D CB  1 
ATOM   5537  O  OG1 . THR D  1 39  ? -27.039 -19.753 19.572 1.00 83.69  ? 30  THR D OG1 1 
ATOM   5538  C  CG2 . THR D  1 39  ? -26.190 -21.882 18.819 1.00 77.68  ? 30  THR D CG2 1 
ATOM   5539  N  N   . VAL D  1 40  ? -23.273 -22.275 20.478 1.00 55.59  ? 31  VAL D N   1 
ATOM   5540  C  CA  . VAL D  1 40  ? -21.999 -22.844 20.089 1.00 58.24  ? 31  VAL D CA  1 
ATOM   5541  C  C   . VAL D  1 40  ? -22.255 -24.010 19.163 1.00 58.94  ? 31  VAL D C   1 
ATOM   5542  O  O   . VAL D  1 40  ? -23.007 -24.914 19.496 1.00 62.32  ? 31  VAL D O   1 
ATOM   5543  C  CB  . VAL D  1 40  ? -21.195 -23.345 21.301 1.00 57.58  ? 31  VAL D CB  1 
ATOM   5544  C  CG1 . VAL D  1 40  ? -19.867 -23.927 20.846 1.00 55.66  ? 31  VAL D CG1 1 
ATOM   5545  C  CG2 . VAL D  1 40  ? -20.962 -22.216 22.283 1.00 62.00  ? 31  VAL D CG2 1 
ATOM   5546  N  N   . TYR D  1 41  ? -21.634 -23.985 17.995 1.00 56.84  ? 32  TYR D N   1 
ATOM   5547  C  CA  . TYR D  1 41  ? -21.792 -25.069 17.051 1.00 60.83  ? 32  TYR D CA  1 
ATOM   5548  C  C   . TYR D  1 41  ? -20.657 -26.057 17.202 1.00 61.59  ? 32  TYR D C   1 
ATOM   5549  O  O   . TYR D  1 41  ? -19.483 -25.685 17.262 1.00 59.36  ? 32  TYR D O   1 
ATOM   5550  C  CB  . TYR D  1 41  ? -21.938 -24.542 15.616 1.00 67.74  ? 32  TYR D CB  1 
ATOM   5551  C  CG  . TYR D  1 41  ? -23.363 -24.132 15.327 1.00 73.48  ? 32  TYR D CG  1 
ATOM   5552  C  CD1 . TYR D  1 41  ? -24.325 -25.093 15.013 1.00 79.80  ? 32  TYR D CD1 1 
ATOM   5553  C  CD2 . TYR D  1 41  ? -23.767 -22.803 15.413 1.00 68.08  ? 32  TYR D CD2 1 
ATOM   5554  C  CE1 . TYR D  1 41  ? -25.641 -24.747 14.764 1.00 76.60  ? 32  TYR D CE1 1 
ATOM   5555  C  CE2 . TYR D  1 41  ? -25.093 -22.446 15.169 1.00 77.62  ? 32  TYR D CE2 1 
ATOM   5556  C  CZ  . TYR D  1 41  ? -26.023 -23.431 14.845 1.00 79.92  ? 32  TYR D CZ  1 
ATOM   5557  O  OH  . TYR D  1 41  ? -27.341 -23.115 14.601 1.00 80.21  ? 32  TYR D OH  1 
ATOM   5558  N  N   . LEU D  1 42  ? -21.035 -27.325 17.291 1.00 62.05  ? 33  LEU D N   1 
ATOM   5559  C  CA  . LEU D  1 42  ? -20.104 -28.393 17.589 1.00 55.82  ? 33  LEU D CA  1 
ATOM   5560  C  C   . LEU D  1 42  ? -20.202 -29.478 16.528 1.00 62.68  ? 33  LEU D C   1 
ATOM   5561  O  O   . LEU D  1 42  ? -21.291 -29.946 16.190 1.00 65.90  ? 33  LEU D O   1 
ATOM   5562  C  CB  . LEU D  1 42  ? -20.419 -28.969 18.964 1.00 59.64  ? 33  LEU D CB  1 
ATOM   5563  C  CG  . LEU D  1 42  ? -19.369 -29.865 19.605 1.00 63.61  ? 33  LEU D CG  1 
ATOM   5564  C  CD1 . LEU D  1 42  ? -18.121 -29.061 19.906 1.00 64.40  ? 33  LEU D CD1 1 
ATOM   5565  C  CD2 . LEU D  1 42  ? -19.937 -30.492 20.864 1.00 55.72  ? 33  LEU D CD2 1 
ATOM   5566  N  N   . SER D  1 43  ? -19.051 -29.868 15.999 1.00 64.58  ? 34  SER D N   1 
ATOM   5567  C  CA  . SER D  1 43  ? -18.993 -30.859 14.946 1.00 63.63  ? 34  SER D CA  1 
ATOM   5568  C  C   . SER D  1 43  ? -17.729 -31.695 15.102 1.00 64.83  ? 34  SER D C   1 
ATOM   5569  O  O   . SER D  1 43  ? -16.689 -31.178 15.495 1.00 64.92  ? 34  SER D O   1 
ATOM   5570  C  CB  . SER D  1 43  ? -19.007 -30.163 13.595 1.00 64.39  ? 34  SER D CB  1 
ATOM   5571  O  OG  . SER D  1 43  ? -19.431 -31.064 12.594 1.00 85.72  ? 34  SER D OG  1 
ATOM   5572  N  N   . PHE D  1 44  ? -17.814 -32.989 14.806 1.00 63.15  ? 35  PHE D N   1 
ATOM   5573  C  CA  . PHE D  1 44  ? -16.663 -33.875 14.992 1.00 62.74  ? 35  PHE D CA  1 
ATOM   5574  C  C   . PHE D  1 44  ? -16.154 -34.509 13.699 1.00 60.14  ? 35  PHE D C   1 
ATOM   5575  O  O   . PHE D  1 44  ? -16.936 -34.911 12.844 1.00 63.44  ? 35  PHE D O   1 
ATOM   5576  C  CB  . PHE D  1 44  ? -16.976 -34.989 16.008 1.00 62.27  ? 35  PHE D CB  1 
ATOM   5577  C  CG  . PHE D  1 44  ? -17.213 -34.497 17.410 1.00 65.77  ? 35  PHE D CG  1 
ATOM   5578  C  CD1 . PHE D  1 44  ? -16.149 -34.231 18.257 1.00 61.84  ? 35  PHE D CD1 1 
ATOM   5579  C  CD2 . PHE D  1 44  ? -18.506 -34.312 17.884 1.00 63.96  ? 35  PHE D CD2 1 
ATOM   5580  C  CE1 . PHE D  1 44  ? -16.370 -33.779 19.544 1.00 61.84  ? 35  PHE D CE1 1 
ATOM   5581  C  CE2 . PHE D  1 44  ? -18.734 -33.861 19.167 1.00 62.36  ? 35  PHE D CE2 1 
ATOM   5582  C  CZ  . PHE D  1 44  ? -17.664 -33.593 19.997 1.00 65.75  ? 35  PHE D CZ  1 
ATOM   5583  N  N   . SER D  1 45  ? -14.833 -34.586 13.577 1.00 56.57  ? 36  SER D N   1 
ATOM   5584  C  CA  . SER D  1 45  ? -14.180 -35.381 12.548 1.00 57.23  ? 36  SER D CA  1 
ATOM   5585  C  C   . SER D  1 45  ? -13.240 -36.349 13.232 1.00 55.58  ? 36  SER D C   1 
ATOM   5586  O  O   . SER D  1 45  ? -12.330 -35.946 13.939 1.00 49.19  ? 36  SER D O   1 
ATOM   5587  C  CB  . SER D  1 45  ? -13.376 -34.516 11.578 1.00 54.90  ? 36  SER D CB  1 
ATOM   5588  O  OG  . SER D  1 45  ? -14.174 -33.512 10.995 1.00 65.99  ? 36  SER D OG  1 
ATOM   5589  N  N   . LEU D  1 46  ? -13.436 -37.634 12.972 1.00 64.17  ? 37  LEU D N   1 
ATOM   5590  C  CA  . LEU D  1 46  ? -12.727 -38.672 13.694 1.00 54.64  ? 37  LEU D CA  1 
ATOM   5591  C  C   . LEU D  1 46  ? -11.509 -39.212 12.943 1.00 52.33  ? 37  LEU D C   1 
ATOM   5592  O  O   . LEU D  1 46  ? -11.647 -39.885 11.941 1.00 61.39  ? 37  LEU D O   1 
ATOM   5593  C  CB  . LEU D  1 46  ? -13.719 -39.783 13.999 1.00 51.71  ? 37  LEU D CB  1 
ATOM   5594  C  CG  . LEU D  1 46  ? -13.138 -41.094 14.487 1.00 67.25  ? 37  LEU D CG  1 
ATOM   5595  C  CD1 . LEU D  1 46  ? -11.949 -40.820 15.385 1.00 66.96  ? 37  LEU D CD1 1 
ATOM   5596  C  CD2 . LEU D  1 46  ? -14.223 -41.882 15.210 1.00 69.74  ? 37  LEU D CD2 1 
ATOM   5597  N  N   . LEU D  1 47  ? -10.316 -38.915 13.452 1.00 56.61  ? 38  LEU D N   1 
ATOM   5598  C  CA  . LEU D  1 47  ? -9.060  -39.367 12.852 1.00 55.30  ? 38  LEU D CA  1 
ATOM   5599  C  C   . LEU D  1 47  ? -8.622  -40.801 13.126 1.00 56.98  ? 38  LEU D C   1 
ATOM   5600  O  O   . LEU D  1 47  ? -8.145  -41.480 12.232 1.00 65.56  ? 38  LEU D O   1 
ATOM   5601  C  CB  . LEU D  1 47  ? -7.908  -38.427 13.210 1.00 48.19  ? 38  LEU D CB  1 
ATOM   5602  C  CG  . LEU D  1 47  ? -7.784  -37.249 12.256 1.00 54.84  ? 38  LEU D CG  1 
ATOM   5603  C  CD1 . LEU D  1 47  ? -9.043  -36.415 12.311 1.00 54.99  ? 38  LEU D CD1 1 
ATOM   5604  C  CD2 . LEU D  1 47  ? -6.561  -36.419 12.569 1.00 58.43  ? 38  LEU D CD2 1 
ATOM   5605  N  N   . ASP D  1 48  ? -8.662  -41.234 14.372 1.00 54.55  ? 39  ASP D N   1 
ATOM   5606  C  CA  . ASP D  1 48  ? -8.205  -42.583 14.661 1.00 57.45  ? 39  ASP D CA  1 
ATOM   5607  C  C   . ASP D  1 48  ? -8.812  -43.162 15.947 1.00 60.98  ? 39  ASP D C   1 
ATOM   5608  O  O   . ASP D  1 48  ? -8.964  -42.447 16.941 1.00 62.21  ? 39  ASP D O   1 
ATOM   5609  C  CB  . ASP D  1 48  ? -6.677  -42.547 14.755 1.00 56.59  ? 39  ASP D CB  1 
ATOM   5610  C  CG  . ASP D  1 48  ? -6.045  -43.891 14.526 1.00 60.03  ? 39  ASP D CG  1 
ATOM   5611  O  OD1 . ASP D  1 48  ? -6.802  -44.873 14.406 1.00 59.28  ? 39  ASP D OD1 1 
ATOM   5612  O  OD2 . ASP D  1 48  ? -4.795  -43.967 14.479 1.00 54.71  ? 39  ASP D OD2 1 
ATOM   5613  N  N   . ILE D  1 49  ? -9.072  -44.466 15.971 1.00 54.12  ? 40  ILE D N   1 
ATOM   5614  C  CA  . ILE D  1 49  ? -9.277  -45.139 17.240 1.00 54.54  ? 40  ILE D CA  1 
ATOM   5615  C  C   . ILE D  1 49  ? -7.955  -45.828 17.476 1.00 54.91  ? 40  ILE D C   1 
ATOM   5616  O  O   . ILE D  1 49  ? -7.604  -46.740 16.753 1.00 60.54  ? 40  ILE D O   1 
ATOM   5617  C  CB  . ILE D  1 49  ? -10.431 -46.139 17.186 1.00 52.07  ? 40  ILE D CB  1 
ATOM   5618  C  CG1 . ILE D  1 49  ? -11.737 -45.389 16.954 1.00 53.99  ? 40  ILE D CG1 1 
ATOM   5619  C  CG2 . ILE D  1 49  ? -10.528 -46.936 18.484 1.00 46.25  ? 40  ILE D CG2 1 
ATOM   5620  C  CD1 . ILE D  1 49  ? -12.963 -46.149 17.404 1.00 53.32  ? 40  ILE D CD1 1 
ATOM   5621  N  N   . VAL D  1 50  ? -7.185  -45.337 18.439 1.00 54.83  ? 41  VAL D N   1 
ATOM   5622  C  CA  . VAL D  1 50  ? -5.826  -45.824 18.621 1.00 55.88  ? 41  VAL D CA  1 
ATOM   5623  C  C   . VAL D  1 50  ? -5.799  -47.131 19.406 1.00 56.46  ? 41  VAL D C   1 
ATOM   5624  O  O   . VAL D  1 50  ? -5.100  -48.074 19.040 1.00 58.96  ? 41  VAL D O   1 
ATOM   5625  C  CB  . VAL D  1 50  ? -4.920  -44.749 19.291 1.00 53.28  ? 41  VAL D CB  1 
ATOM   5626  C  CG1 . VAL D  1 50  ? -3.490  -45.239 19.410 1.00 51.20  ? 41  VAL D CG1 1 
ATOM   5627  C  CG2 . VAL D  1 50  ? -4.956  -43.463 18.496 1.00 50.69  ? 41  VAL D CG2 1 
ATOM   5628  N  N   . LYS D  1 51  ? -6.582  -47.179 20.479 1.00 56.39  ? 42  LYS D N   1 
ATOM   5629  C  CA  . LYS D  1 51  ? -6.528  -48.285 21.428 1.00 55.75  ? 42  LYS D CA  1 
ATOM   5630  C  C   . LYS D  1 51  ? -7.906  -48.577 22.002 1.00 57.70  ? 42  LYS D C   1 
ATOM   5631  O  O   . LYS D  1 51  ? -8.641  -47.662 22.360 1.00 60.59  ? 42  LYS D O   1 
ATOM   5632  C  CB  . LYS D  1 51  ? -5.557  -47.923 22.550 1.00 56.18  ? 42  LYS D CB  1 
ATOM   5633  C  CG  . LYS D  1 51  ? -4.961  -49.069 23.332 1.00 55.16  ? 42  LYS D CG  1 
ATOM   5634  C  CD  . LYS D  1 51  ? -3.938  -48.528 24.346 1.00 70.12  ? 42  LYS D CD  1 
ATOM   5635  C  CE  . LYS D  1 51  ? -4.545  -47.467 25.244 1.00 83.35  ? 42  LYS D CE  1 
ATOM   5636  N  NZ  . LYS D  1 51  ? -5.622  -48.030 26.098 1.00 82.99  ? 42  LYS D NZ  1 
ATOM   5637  N  N   . ALA D  1 52  ? -8.260  -49.852 22.083 1.00 58.13  ? 43  ALA D N   1 
ATOM   5638  C  CA  . ALA D  1 52  ? -9.440  -50.262 22.829 1.00 60.29  ? 43  ALA D CA  1 
ATOM   5639  C  C   . ALA D  1 52  ? -8.985  -51.230 23.910 1.00 67.20  ? 43  ALA D C   1 
ATOM   5640  O  O   . ALA D  1 52  ? -8.531  -52.328 23.605 1.00 69.38  ? 43  ALA D O   1 
ATOM   5641  C  CB  . ALA D  1 52  ? -10.433 -50.914 21.918 1.00 58.64  ? 43  ALA D CB  1 
ATOM   5642  N  N   . ASP D  1 53  ? -9.093  -50.826 25.173 1.00 70.16  ? 44  ASP D N   1 
ATOM   5643  C  CA  . ASP D  1 53  ? -8.534  -51.620 26.265 1.00 65.72  ? 44  ASP D CA  1 
ATOM   5644  C  C   . ASP D  1 53  ? -9.625  -52.342 27.050 1.00 62.89  ? 44  ASP D C   1 
ATOM   5645  O  O   . ASP D  1 53  ? -10.403 -51.725 27.759 1.00 59.63  ? 44  ASP D O   1 
ATOM   5646  C  CB  . ASP D  1 53  ? -7.695  -50.737 27.183 1.00 63.37  ? 44  ASP D CB  1 
ATOM   5647  C  CG  . ASP D  1 53  ? -6.841  -51.540 28.127 1.00 70.84  ? 44  ASP D CG  1 
ATOM   5648  O  OD1 . ASP D  1 53  ? -7.247  -52.668 28.454 1.00 74.84  ? 44  ASP D OD1 1 
ATOM   5649  O  OD2 . ASP D  1 53  ? -5.768  -51.057 28.543 1.00 74.14  ? 44  ASP D OD2 1 
ATOM   5650  N  N   . SER D  1 54  ? -9.675  -53.661 26.924 1.00 70.79  ? 45  SER D N   1 
ATOM   5651  C  CA  . SER D  1 54  ? -10.727 -54.431 27.583 1.00 73.27  ? 45  SER D CA  1 
ATOM   5652  C  C   . SER D  1 54  ? -10.379 -54.787 29.032 1.00 63.33  ? 45  SER D C   1 
ATOM   5653  O  O   . SER D  1 54  ? -11.217 -55.297 29.771 1.00 61.97  ? 45  SER D O   1 
ATOM   5654  C  CB  . SER D  1 54  ? -11.054 -55.682 26.772 1.00 62.32  ? 45  SER D CB  1 
ATOM   5655  O  OG  . SER D  1 54  ? -9.866  -56.348 26.398 1.00 68.47  ? 45  SER D OG  1 
ATOM   5656  N  N   . SER D  1 55  ? -9.140  -54.501 29.416 1.00 57.54  ? 46  SER D N   1 
ATOM   5657  C  CA  . SER D  1 55  ? -8.698  -54.604 30.796 1.00 60.06  ? 46  SER D CA  1 
ATOM   5658  C  C   . SER D  1 55  ? -9.163  -53.416 31.659 1.00 65.28  ? 46  SER D C   1 
ATOM   5659  O  O   . SER D  1 55  ? -9.545  -53.602 32.822 1.00 62.90  ? 46  SER D O   1 
ATOM   5660  C  CB  . SER D  1 55  ? -7.174  -54.725 30.844 1.00 61.41  ? 46  SER D CB  1 
ATOM   5661  O  OG  . SER D  1 55  ? -6.557  -53.445 30.849 1.00 73.64  ? 46  SER D OG  1 
ATOM   5662  N  N   . THR D  1 56  ? -9.058  -52.194 31.130 1.00 61.85  ? 47  THR D N   1 
ATOM   5663  C  CA  . THR D  1 56  ? -9.640  -51.017 31.795 1.00 60.81  ? 47  THR D CA  1 
ATOM   5664  C  C   . THR D  1 56  ? -11.007 -50.488 31.295 1.00 60.10  ? 47  THR D C   1 
ATOM   5665  O  O   . THR D  1 56  ? -11.582 -49.583 31.902 1.00 52.77  ? 47  THR D O   1 
ATOM   5666  C  CB  . THR D  1 56  ? -8.655  -49.836 31.826 1.00 60.03  ? 47  THR D CB  1 
ATOM   5667  O  OG1 . THR D  1 56  ? -8.338  -49.425 30.486 1.00 59.45  ? 47  THR D OG1 1 
ATOM   5668  C  CG2 . THR D  1 56  ? -7.382  -50.199 32.604 1.00 56.18  ? 47  THR D CG2 1 
ATOM   5669  N  N   . ASN D  1 57  ? -11.544 -51.070 30.231 1.00 59.70  ? 48  ASN D N   1 
ATOM   5670  C  CA  . ASN D  1 57  ? -12.691 -50.473 29.539 1.00 60.29  ? 48  ASN D CA  1 
ATOM   5671  C  C   . ASN D  1 57  ? -12.528 -48.988 29.167 1.00 55.90  ? 48  ASN D C   1 
ATOM   5672  O  O   . ASN D  1 57  ? -13.406 -48.168 29.405 1.00 51.83  ? 48  ASN D O   1 
ATOM   5673  C  CB  . ASN D  1 57  ? -13.995 -50.722 30.288 1.00 59.54  ? 48  ASN D CB  1 
ATOM   5674  C  CG  . ASN D  1 57  ? -14.563 -52.101 30.008 1.00 64.29  ? 48  ASN D CG  1 
ATOM   5675  O  OD1 . ASN D  1 57  ? -13.893 -52.955 29.417 1.00 64.79  ? 48  ASN D OD1 1 
ATOM   5676  N  ND2 . ASN D  1 57  ? -15.801 -52.326 30.432 1.00 67.05  ? 48  ASN D ND2 1 
ATOM   5677  N  N   . GLU D  1 58  ? -11.395 -48.676 28.554 1.00 55.00  ? 49  GLU D N   1 
ATOM   5678  C  CA  . GLU D  1 58  ? -11.109 -47.340 28.093 1.00 57.48  ? 49  GLU D CA  1 
ATOM   5679  C  C   . GLU D  1 58  ? -10.757 -47.358 26.611 1.00 60.20  ? 49  GLU D C   1 
ATOM   5680  O  O   . GLU D  1 58  ? -9.851  -48.074 26.210 1.00 64.86  ? 49  GLU D O   1 
ATOM   5681  C  CB  . GLU D  1 58  ? -9.909  -46.774 28.862 1.00 61.42  ? 49  GLU D CB  1 
ATOM   5682  C  CG  . GLU D  1 58  ? -10.006 -46.810 30.394 1.00 59.99  ? 49  GLU D CG  1 
ATOM   5683  C  CD  . GLU D  1 58  ? -8.807  -46.141 31.085 1.00 63.42  ? 49  GLU D CD  1 
ATOM   5684  O  OE1 . GLU D  1 58  ? -7.785  -46.826 31.333 1.00 55.97  ? 49  GLU D OE1 1 
ATOM   5685  O  OE2 . GLU D  1 58  ? -8.888  -44.924 31.378 1.00 60.92  ? 49  GLU D OE2 1 
ATOM   5686  N  N   . VAL D  1 59  ? -11.431 -46.551 25.797 1.00 55.01  ? 50  VAL D N   1 
ATOM   5687  C  CA  . VAL D  1 59  ? -10.978 -46.351 24.416 1.00 55.15  ? 50  VAL D CA  1 
ATOM   5688  C  C   . VAL D  1 59  ? -10.301 -44.980 24.214 1.00 58.79  ? 50  VAL D C   1 
ATOM   5689  O  O   . VAL D  1 59  ? -10.655 -43.998 24.866 1.00 58.77  ? 50  VAL D O   1 
ATOM   5690  C  CB  . VAL D  1 59  ? -12.122 -46.545 23.370 1.00 57.03  ? 50  VAL D CB  1 
ATOM   5691  C  CG1 . VAL D  1 59  ? -11.634 -46.205 21.982 1.00 62.05  ? 50  VAL D CG1 1 
ATOM   5692  C  CG2 . VAL D  1 59  ? -12.619 -47.967 23.376 1.00 63.38  ? 50  VAL D CG2 1 
ATOM   5693  N  N   . ASP D  1 60  ? -9.312  -44.940 23.323 1.00 58.08  ? 51  ASP D N   1 
ATOM   5694  C  CA  . ASP D  1 60  ? -8.584  -43.722 22.976 1.00 54.60  ? 51  ASP D CA  1 
ATOM   5695  C  C   . ASP D  1 60  ? -8.935  -43.256 21.570 1.00 55.21  ? 51  ASP D C   1 
ATOM   5696  O  O   . ASP D  1 60  ? -8.647  -43.946 20.600 1.00 55.55  ? 51  ASP D O   1 
ATOM   5697  C  CB  . ASP D  1 60  ? -7.079  -43.972 23.037 1.00 55.34  ? 51  ASP D CB  1 
ATOM   5698  C  CG  . ASP D  1 60  ? -6.588  -44.263 24.438 1.00 62.31  ? 51  ASP D CG  1 
ATOM   5699  O  OD1 . ASP D  1 60  ? -7.358  -44.815 25.250 1.00 68.55  ? 51  ASP D OD1 1 
ATOM   5700  O  OD2 . ASP D  1 60  ? -5.421  -43.942 24.729 1.00 65.83  ? 51  ASP D OD2 1 
ATOM   5701  N  N   . LEU D  1 61  ? -9.551  -42.080 21.474 1.00 54.85  ? 52  LEU D N   1 
ATOM   5702  C  CA  . LEU D  1 61  ? -9.905  -41.447 20.203 1.00 53.11  ? 52  LEU D CA  1 
ATOM   5703  C  C   . LEU D  1 61  ? -8.905  -40.365 19.851 1.00 53.30  ? 52  LEU D C   1 
ATOM   5704  O  O   . LEU D  1 61  ? -8.433  -39.660 20.725 1.00 57.64  ? 52  LEU D O   1 
ATOM   5705  C  CB  . LEU D  1 61  ? -11.254 -40.754 20.346 1.00 55.65  ? 52  LEU D CB  1 
ATOM   5706  C  CG  . LEU D  1 61  ? -12.517 -41.406 19.811 1.00 62.38  ? 52  LEU D CG  1 
ATOM   5707  C  CD1 . LEU D  1 61  ? -13.745 -40.625 20.252 1.00 58.90  ? 52  LEU D CD1 1 
ATOM   5708  C  CD2 . LEU D  1 61  ? -12.417 -41.427 18.316 1.00 65.86  ? 52  LEU D CD2 1 
ATOM   5709  N  N   . VAL D  1 62  ? -8.569  -40.223 18.581 1.00 53.54  ? 53  VAL D N   1 
ATOM   5710  C  CA  . VAL D  1 62  ? -7.947  -38.982 18.131 1.00 53.87  ? 53  VAL D CA  1 
ATOM   5711  C  C   . VAL D  1 62  ? -8.932  -38.294 17.193 1.00 56.50  ? 53  VAL D C   1 
ATOM   5712  O  O   . VAL D  1 62  ? -9.413  -38.893 16.244 1.00 52.86  ? 53  VAL D O   1 
ATOM   5713  C  CB  . VAL D  1 62  ? -6.598  -39.206 17.440 1.00 46.78  ? 53  VAL D CB  1 
ATOM   5714  C  CG1 . VAL D  1 62  ? -6.166  -37.954 16.723 1.00 40.44  ? 53  VAL D CG1 1 
ATOM   5715  C  CG2 . VAL D  1 62  ? -5.546  -39.616 18.460 1.00 49.25  ? 53  VAL D CG2 1 
ATOM   5716  N  N   . TYR D  1 63  ? -9.266  -37.044 17.468 1.00 56.13  ? 54  TYR D N   1 
ATOM   5717  C  CA  . TYR D  1 63  ? -10.289 -36.377 16.674 1.00 54.41  ? 54  TYR D CA  1 
ATOM   5718  C  C   . TYR D  1 63  ? -10.079 -34.859 16.594 1.00 55.90  ? 54  TYR D C   1 
ATOM   5719  O  O   . TYR D  1 63  ? -9.284  -34.287 17.335 1.00 51.63  ? 54  TYR D O   1 
ATOM   5720  C  CB  . TYR D  1 63  ? -11.681 -36.708 17.216 1.00 48.66  ? 54  TYR D CB  1 
ATOM   5721  C  CG  . TYR D  1 63  ? -11.876 -36.251 18.631 1.00 53.70  ? 54  TYR D CG  1 
ATOM   5722  C  CD1 . TYR D  1 63  ? -12.610 -35.119 18.909 1.00 55.81  ? 54  TYR D CD1 1 
ATOM   5723  C  CD2 . TYR D  1 63  ? -11.298 -36.938 19.695 1.00 56.57  ? 54  TYR D CD2 1 
ATOM   5724  C  CE1 . TYR D  1 63  ? -12.780 -34.676 20.208 1.00 59.97  ? 54  TYR D CE1 1 
ATOM   5725  C  CE2 . TYR D  1 63  ? -11.458 -36.501 20.999 1.00 56.91  ? 54  TYR D CE2 1 
ATOM   5726  C  CZ  . TYR D  1 63  ? -12.206 -35.366 21.251 1.00 61.85  ? 54  TYR D CZ  1 
ATOM   5727  O  OH  . TYR D  1 63  ? -12.394 -34.913 22.545 1.00 61.44  ? 54  TYR D OH  1 
ATOM   5728  N  N   . TRP D  1 64  ? -10.754 -34.236 15.637 1.00 54.54  ? 55  TRP D N   1 
ATOM   5729  C  CA  . TRP D  1 64  ? -10.864 -32.799 15.573 1.00 53.72  ? 55  TRP D CA  1 
ATOM   5730  C  C   . TRP D  1 64  ? -12.264 -32.447 16.043 1.00 59.12  ? 55  TRP D C   1 
ATOM   5731  O  O   . TRP D  1 64  ? -13.216 -33.190 15.814 1.00 59.38  ? 55  TRP D O   1 
ATOM   5732  C  CB  . TRP D  1 64  ? -10.656 -32.310 14.152 1.00 52.50  ? 55  TRP D CB  1 
ATOM   5733  C  CG  . TRP D  1 64  ? -9.353  -32.711 13.558 1.00 55.36  ? 55  TRP D CG  1 
ATOM   5734  C  CD1 . TRP D  1 64  ? -8.221  -33.081 14.225 1.00 57.92  ? 55  TRP D CD1 1 
ATOM   5735  C  CD2 . TRP D  1 64  ? -9.039  -32.791 12.165 1.00 62.51  ? 55  TRP D CD2 1 
ATOM   5736  N  NE1 . TRP D  1 64  ? -7.212  -33.370 13.333 1.00 58.34  ? 55  TRP D NE1 1 
ATOM   5737  C  CE2 . TRP D  1 64  ? -7.694  -33.202 12.054 1.00 64.58  ? 55  TRP D CE2 1 
ATOM   5738  C  CE3 . TRP D  1 64  ? -9.766  -32.554 10.986 1.00 60.12  ? 55  TRP D CE3 1 
ATOM   5739  C  CZ2 . TRP D  1 64  ? -7.064  -33.385 10.825 1.00 71.34  ? 55  TRP D CZ2 1 
ATOM   5740  C  CZ3 . TRP D  1 64  ? -9.138  -32.731 9.770  1.00 61.66  ? 55  TRP D CZ3 1 
ATOM   5741  C  CH2 . TRP D  1 64  ? -7.805  -33.143 9.696  1.00 64.76  ? 55  TRP D CH2 1 
ATOM   5742  N  N   . GLU D  1 65  ? -12.383 -31.326 16.735 1.00 63.15  ? 56  GLU D N   1 
ATOM   5743  C  CA  . GLU D  1 65  ? -13.658 -30.895 17.269 1.00 60.87  ? 56  GLU D CA  1 
ATOM   5744  C  C   . GLU D  1 65  ? -13.829 -29.469 16.792 1.00 65.08  ? 56  GLU D C   1 
ATOM   5745  O  O   . GLU D  1 65  ? -13.046 -28.595 17.158 1.00 68.25  ? 56  GLU D O   1 
ATOM   5746  C  CB  . GLU D  1 65  ? -13.602 -30.955 18.788 1.00 56.72  ? 56  GLU D CB  1 
ATOM   5747  C  CG  . GLU D  1 65  ? -14.889 -30.632 19.504 1.00 64.88  ? 56  GLU D CG  1 
ATOM   5748  C  CD  . GLU D  1 65  ? -14.705 -30.628 21.020 1.00 70.58  ? 56  GLU D CD  1 
ATOM   5749  O  OE1 . GLU D  1 65  ? -13.691 -31.181 21.503 1.00 65.65  ? 56  GLU D OE1 1 
ATOM   5750  O  OE2 . GLU D  1 65  ? -15.561 -30.060 21.733 1.00 71.85  ? 56  GLU D OE2 1 
ATOM   5751  N  N   . GLN D  1 66  ? -14.822 -29.229 15.945 1.00 61.97  ? 57  GLN D N   1 
ATOM   5752  C  CA  . GLN D  1 66  ? -15.026 -27.895 15.418 1.00 59.10  ? 57  GLN D CA  1 
ATOM   5753  C  C   . GLN D  1 66  ? -16.009 -27.140 16.292 1.00 62.25  ? 57  GLN D C   1 
ATOM   5754  O  O   . GLN D  1 66  ? -17.160 -27.542 16.447 1.00 63.90  ? 57  GLN D O   1 
ATOM   5755  C  CB  . GLN D  1 66  ? -15.515 -27.933 13.969 1.00 66.87  ? 57  GLN D CB  1 
ATOM   5756  C  CG  . GLN D  1 66  ? -15.991 -26.568 13.479 1.00 73.98  ? 57  GLN D CG  1 
ATOM   5757  C  CD  . GLN D  1 66  ? -16.377 -26.551 12.020 1.00 80.61  ? 57  GLN D CD  1 
ATOM   5758  O  OE1 . GLN D  1 66  ? -15.612 -26.982 11.159 1.00 91.10  ? 57  GLN D OE1 1 
ATOM   5759  N  NE2 . GLN D  1 66  ? -17.571 -26.047 11.730 1.00 87.12  ? 57  GLN D NE2 1 
ATOM   5760  N  N   . GLN D  1 67  ? -15.542 -26.043 16.872 1.00 59.87  ? 58  GLN D N   1 
ATOM   5761  C  CA  . GLN D  1 67  ? -16.382 -25.206 17.709 1.00 57.64  ? 58  GLN D CA  1 
ATOM   5762  C  C   . GLN D  1 67  ? -16.468 -23.836 17.089 1.00 56.76  ? 58  GLN D C   1 
ATOM   5763  O  O   . GLN D  1 67  ? -15.455 -23.257 16.714 1.00 58.93  ? 58  GLN D O   1 
ATOM   5764  C  CB  . GLN D  1 67  ? -15.790 -25.088 19.108 1.00 54.32  ? 58  GLN D CB  1 
ATOM   5765  C  CG  . GLN D  1 67  ? -15.559 -26.413 19.778 1.00 60.90  ? 58  GLN D CG  1 
ATOM   5766  C  CD  . GLN D  1 67  ? -14.824 -26.283 21.089 1.00 60.22  ? 58  GLN D CD  1 
ATOM   5767  O  OE1 . GLN D  1 67  ? -14.199 -25.261 21.370 1.00 56.32  ? 58  GLN D OE1 1 
ATOM   5768  N  NE2 . GLN D  1 67  ? -14.899 -27.323 21.907 1.00 60.90  ? 58  GLN D NE2 1 
ATOM   5769  N  N   . SER D  1 68  ? -17.681 -23.316 16.977 1.00 60.26  ? 59  SER D N   1 
ATOM   5770  C  CA  . SER D  1 68  ? -17.874 -21.974 16.454 1.00 58.73  ? 59  SER D CA  1 
ATOM   5771  C  C   . SER D  1 68  ? -19.039 -21.291 17.137 1.00 55.87  ? 59  SER D C   1 
ATOM   5772  O  O   . SER D  1 68  ? -19.941 -21.941 17.649 1.00 56.78  ? 59  SER D O   1 
ATOM   5773  C  CB  . SER D  1 68  ? -18.072 -21.997 14.937 1.00 58.08  ? 59  SER D CB  1 
ATOM   5774  O  OG  . SER D  1 68  ? -18.842 -23.115 14.524 1.00 66.69  ? 59  SER D OG  1 
ATOM   5775  N  N   . TRP D  1 69  ? -19.043 -19.970 17.074 1.00 53.65  ? 60  TRP D N   1 
ATOM   5776  C  CA  . TRP D  1 69  ? -20.010 -19.160 17.788 1.00 56.72  ? 60  TRP D CA  1 
ATOM   5777  C  C   . TRP D  1 69  ? -19.743 -17.743 17.335 1.00 58.87  ? 60  TRP D C   1 
ATOM   5778  O  O   . TRP D  1 69  ? -18.736 -17.485 16.673 1.00 55.85  ? 60  TRP D O   1 
ATOM   5779  C  CB  . TRP D  1 69  ? -19.816 -19.287 19.307 1.00 58.28  ? 60  TRP D CB  1 
ATOM   5780  C  CG  . TRP D  1 69  ? -18.483 -18.778 19.804 1.00 52.65  ? 60  TRP D CG  1 
ATOM   5781  C  CD1 . TRP D  1 69  ? -18.187 -17.505 20.169 1.00 56.47  ? 60  TRP D CD1 1 
ATOM   5782  C  CD2 . TRP D  1 69  ? -17.270 -19.535 19.975 1.00 53.97  ? 60  TRP D CD2 1 
ATOM   5783  N  NE1 . TRP D  1 69  ? -16.870 -17.414 20.559 1.00 56.07  ? 60  TRP D NE1 1 
ATOM   5784  C  CE2 . TRP D  1 69  ? -16.288 -18.642 20.449 1.00 47.43  ? 60  TRP D CE2 1 
ATOM   5785  C  CE3 . TRP D  1 69  ? -16.926 -20.877 19.777 1.00 56.09  ? 60  TRP D CE3 1 
ATOM   5786  C  CZ2 . TRP D  1 69  ? -14.987 -19.044 20.724 1.00 46.08  ? 60  TRP D CZ2 1 
ATOM   5787  C  CZ3 . TRP D  1 69  ? -15.626 -21.276 20.058 1.00 54.56  ? 60  TRP D CZ3 1 
ATOM   5788  C  CH2 . TRP D  1 69  ? -14.675 -20.360 20.528 1.00 50.02  ? 60  TRP D CH2 1 
ATOM   5789  N  N   . LYS D  1 70  ? -20.665 -16.836 17.641 1.00 63.54  ? 61  LYS D N   1 
ATOM   5790  C  CA  . LYS D  1 70  ? -20.526 -15.444 17.220 1.00 65.22  ? 61  LYS D CA  1 
ATOM   5791  C  C   . LYS D  1 70  ? -20.618 -14.491 18.409 1.00 64.10  ? 61  LYS D C   1 
ATOM   5792  O  O   . LYS D  1 70  ? -21.480 -14.635 19.276 1.00 63.23  ? 61  LYS D O   1 
ATOM   5793  C  CB  . LYS D  1 70  ? -21.557 -15.077 16.139 1.00 62.21  ? 61  LYS D CB  1 
ATOM   5794  C  CG  . LYS D  1 70  ? -21.803 -13.574 16.000 1.00 74.44  ? 61  LYS D CG  1 
ATOM   5795  C  CD  . LYS D  1 70  ? -23.071 -13.253 15.201 1.00 78.64  ? 61  LYS D CD  1 
ATOM   5796  C  CE  . LYS D  1 70  ? -22.745 -12.722 13.794 1.00 84.56  ? 61  LYS D CE  1 
ATOM   5797  N  NZ  . LYS D  1 70  ? -23.702 -11.664 13.334 1.00 75.45  ? 61  LYS D NZ  1 
ATOM   5798  N  N   . LEU D  1 71  ? -19.709 -13.527 18.449 1.00 62.47  ? 62  LEU D N   1 
ATOM   5799  C  CA  . LEU D  1 71  ? -19.752 -12.488 19.463 1.00 70.58  ? 62  LEU D CA  1 
ATOM   5800  C  C   . LEU D  1 71  ? -19.862 -11.123 18.796 1.00 75.82  ? 62  LEU D C   1 
ATOM   5801  O  O   . LEU D  1 71  ? -19.101 -10.812 17.886 1.00 75.26  ? 62  LEU D O   1 
ATOM   5802  C  CB  . LEU D  1 71  ? -18.513 -12.550 20.360 1.00 66.11  ? 62  LEU D CB  1 
ATOM   5803  C  CG  . LEU D  1 71  ? -18.432 -13.754 21.299 1.00 64.75  ? 62  LEU D CG  1 
ATOM   5804  C  CD1 . LEU D  1 71  ? -17.204 -13.659 22.193 1.00 62.86  ? 62  LEU D CD1 1 
ATOM   5805  C  CD2 . LEU D  1 71  ? -19.698 -13.863 22.122 1.00 58.54  ? 62  LEU D CD2 1 
ATOM   5806  N  N   . ASN D  1 72  ? -20.820 -10.313 19.234 1.00 77.56  ? 63  ASN D N   1 
ATOM   5807  C  CA  . ASN D  1 72  ? -20.936 -8.962  18.716 1.00 72.51  ? 63  ASN D CA  1 
ATOM   5808  C  C   . ASN D  1 72  ? -19.687 -8.187  19.093 1.00 70.50  ? 63  ASN D C   1 
ATOM   5809  O  O   . ASN D  1 72  ? -19.304 -7.244  18.410 1.00 70.55  ? 63  ASN D O   1 
ATOM   5810  C  CB  . ASN D  1 72  ? -22.183 -8.271  19.268 1.00 72.71  ? 63  ASN D CB  1 
ATOM   5811  C  CG  . ASN D  1 72  ? -23.456 -9.041  18.969 1.00 81.94  ? 63  ASN D CG  1 
ATOM   5812  O  OD1 . ASN D  1 72  ? -23.824 -9.961  19.702 1.00 86.08  ? 63  ASN D OD1 1 
ATOM   5813  N  ND2 . ASN D  1 72  ? -24.136 -8.670  17.894 1.00 68.24  ? 63  ASN D ND2 1 
ATOM   5814  N  N   . SER D  1 73  ? -19.045 -8.611  20.177 1.00 70.57  ? 64  SER D N   1 
ATOM   5815  C  CA  . SER D  1 73  ? -17.848 -7.951  20.678 1.00 61.67  ? 64  SER D CA  1 
ATOM   5816  C  C   . SER D  1 73  ? -16.726 -8.074  19.662 1.00 65.48  ? 64  SER D C   1 
ATOM   5817  O  O   . SER D  1 73  ? -15.793 -7.273  19.647 1.00 66.65  ? 64  SER D O   1 
ATOM   5818  C  CB  . SER D  1 73  ? -17.407 -8.581  22.000 1.00 71.14  ? 64  SER D CB  1 
ATOM   5819  O  OG  . SER D  1 73  ? -18.526 -8.960  22.780 1.00 72.89  ? 64  SER D OG  1 
ATOM   5820  N  N   . LEU D  1 74  ? -16.813 -9.098  18.820 1.00 67.71  ? 65  LEU D N   1 
ATOM   5821  C  CA  . LEU D  1 74  ? -15.762 -9.370  17.845 1.00 65.77  ? 65  LEU D CA  1 
ATOM   5822  C  C   . LEU D  1 74  ? -16.006 -8.813  16.436 1.00 67.39  ? 65  LEU D C   1 
ATOM   5823  O  O   . LEU D  1 74  ? -15.189 -9.014  15.543 1.00 67.22  ? 65  LEU D O   1 
ATOM   5824  C  CB  . LEU D  1 74  ? -15.472 -10.866 17.797 1.00 61.88  ? 65  LEU D CB  1 
ATOM   5825  C  CG  . LEU D  1 74  ? -14.866 -11.364 19.102 1.00 59.17  ? 65  LEU D CG  1 
ATOM   5826  C  CD1 . LEU D  1 74  ? -14.981 -12.861 19.189 1.00 53.20  ? 65  LEU D CD1 1 
ATOM   5827  C  CD2 . LEU D  1 74  ? -13.421 -10.903 19.219 1.00 56.03  ? 65  LEU D CD2 1 
ATOM   5828  N  N   . MET D  1 75  ? -17.120 -8.119  16.233 1.00 69.09  ? 66  MET D N   1 
ATOM   5829  C  CA  . MET D  1 75  ? -17.421 -7.554  14.924 1.00 65.57  ? 66  MET D CA  1 
ATOM   5830  C  C   . MET D  1 75  ? -16.606 -6.309  14.630 1.00 64.19  ? 66  MET D C   1 
ATOM   5831  O  O   . MET D  1 75  ? -16.210 -5.581  15.531 1.00 60.82  ? 66  MET D O   1 
ATOM   5832  C  CB  . MET D  1 75  ? -18.884 -7.179  14.831 1.00 60.55  ? 66  MET D CB  1 
ATOM   5833  C  CG  . MET D  1 75  ? -19.812 -8.313  15.033 1.00 69.33  ? 66  MET D CG  1 
ATOM   5834  S  SD  . MET D  1 75  ? -21.462 -7.647  15.104 1.00 74.86  ? 66  MET D SD  1 
ATOM   5835  C  CE  . MET D  1 75  ? -22.331 -8.759  14.001 1.00 74.55  ? 66  MET D CE  1 
ATOM   5836  N  N   . TRP D  1 76  ? -16.366 -6.076  13.348 1.00 68.90  ? 67  TRP D N   1 
ATOM   5837  C  CA  . TRP D  1 76  ? -15.784 -4.825  12.889 1.00 71.54  ? 67  TRP D CA  1 
ATOM   5838  C  C   . TRP D  1 76  ? -16.153 -4.606  11.418 1.00 71.90  ? 67  TRP D C   1 
ATOM   5839  O  O   . TRP D  1 76  ? -16.610 -5.535  10.752 1.00 63.54  ? 67  TRP D O   1 
ATOM   5840  C  CB  . TRP D  1 76  ? -14.268 -4.815  13.110 1.00 64.75  ? 67  TRP D CB  1 
ATOM   5841  C  CG  . TRP D  1 76  ? -13.483 -5.714  12.193 1.00 68.06  ? 67  TRP D CG  1 
ATOM   5842  C  CD1 . TRP D  1 76  ? -12.923 -5.371  10.995 1.00 64.36  ? 67  TRP D CD1 1 
ATOM   5843  C  CD2 . TRP D  1 76  ? -13.144 -7.094  12.411 1.00 68.66  ? 67  TRP D CD2 1 
ATOM   5844  N  NE1 . TRP D  1 76  ? -12.261 -6.446  10.456 1.00 59.78  ? 67  TRP D NE1 1 
ATOM   5845  C  CE2 . TRP D  1 76  ? -12.385 -7.517  11.303 1.00 66.28  ? 67  TRP D CE2 1 
ATOM   5846  C  CE3 . TRP D  1 76  ? -13.406 -8.010  13.434 1.00 67.54  ? 67  TRP D CE3 1 
ATOM   5847  C  CZ2 . TRP D  1 76  ? -11.886 -8.822  11.193 1.00 61.69  ? 67  TRP D CZ2 1 
ATOM   5848  C  CZ3 . TRP D  1 76  ? -12.911 -9.304  13.316 1.00 63.50  ? 67  TRP D CZ3 1 
ATOM   5849  C  CH2 . TRP D  1 76  ? -12.164 -9.694  12.206 1.00 59.12  ? 67  TRP D CH2 1 
ATOM   5850  N  N   . ASP D  1 77  ? -16.002 -3.374  10.932 1.00 73.28  ? 68  ASP D N   1 
ATOM   5851  C  CA  . ASP D  1 77  ? -16.177 -3.078  9.515  1.00 66.24  ? 68  ASP D CA  1 
ATOM   5852  C  C   . ASP D  1 77  ? -14.818 -3.083  8.843  1.00 68.18  ? 68  ASP D C   1 
ATOM   5853  O  O   . ASP D  1 77  ? -13.968 -2.256  9.153  1.00 71.27  ? 68  ASP D O   1 
ATOM   5854  C  CB  . ASP D  1 77  ? -16.850 -1.720  9.309  1.00 77.07  ? 68  ASP D CB  1 
ATOM   5855  C  CG  . ASP D  1 77  ? -16.985 -1.350  7.830  1.00 86.26  ? 68  ASP D CG  1 
ATOM   5856  O  OD1 . ASP D  1 77  ? -17.766 -2.016  7.118  1.00 85.69  ? 68  ASP D OD1 1 
ATOM   5857  O  OD2 . ASP D  1 77  ? -16.316 -0.394  7.379  1.00 84.30  ? 68  ASP D OD2 1 
ATOM   5858  N  N   . PRO D  1 78  ? -14.611 -4.014  7.904  1.00 67.74  ? 69  PRO D N   1 
ATOM   5859  C  CA  . PRO D  1 78  ? -13.284 -4.201  7.318  1.00 62.44  ? 69  PRO D CA  1 
ATOM   5860  C  C   . PRO D  1 78  ? -12.764 -2.972  6.615  1.00 67.00  ? 69  PRO D C   1 
ATOM   5861  O  O   . PRO D  1 78  ? -11.567 -2.923  6.356  1.00 69.58  ? 69  PRO D O   1 
ATOM   5862  C  CB  . PRO D  1 78  ? -13.502 -5.330  6.322  1.00 57.16  ? 69  PRO D CB  1 
ATOM   5863  C  CG  . PRO D  1 78  ? -14.678 -6.063  6.845  1.00 56.81  ? 69  PRO D CG  1 
ATOM   5864  C  CD  . PRO D  1 78  ? -15.571 -5.011  7.405  1.00 60.39  ? 69  PRO D CD  1 
ATOM   5865  N  N   . ASN D  1 79  ? -13.632 -2.011  6.306  1.00 70.60  ? 70  ASN D N   1 
ATOM   5866  C  CA  . ASN D  1 79  ? -13.198 -0.813  5.589  1.00 77.13  ? 70  ASN D CA  1 
ATOM   5867  C  C   . ASN D  1 79  ? -12.351 0.099   6.450  1.00 78.97  ? 70  ASN D C   1 
ATOM   5868  O  O   . ASN D  1 79  ? -11.445 0.774   5.949  1.00 78.77  ? 70  ASN D O   1 
ATOM   5869  C  CB  . ASN D  1 79  ? -14.382 -0.039  5.003  1.00 75.55  ? 70  ASN D CB  1 
ATOM   5870  C  CG  . ASN D  1 79  ? -15.021 -0.762  3.845  1.00 82.26  ? 70  ASN D CG  1 
ATOM   5871  O  OD1 . ASN D  1 79  ? -14.404 -0.921  2.787  1.00 75.57  ? 70  ASN D OD1 1 
ATOM   5872  N  ND2 . ASN D  1 79  ? -16.262 -1.214  4.035  1.00 73.56  ? 70  ASN D ND2 1 
ATOM   5873  N  N   . GLU D  1 80  ? -12.641 0.121   7.747  1.00 71.66  ? 71  GLU D N   1 
ATOM   5874  C  CA  . GLU D  1 80  ? -11.911 0.970   8.681  1.00 77.40  ? 71  GLU D CA  1 
ATOM   5875  C  C   . GLU D  1 80  ? -10.536 0.392   8.995  1.00 72.32  ? 71  GLU D C   1 
ATOM   5876  O  O   . GLU D  1 80  ? -9.684  1.068   9.570  1.00 69.72  ? 71  GLU D O   1 
ATOM   5877  C  CB  . GLU D  1 80  ? -12.710 1.155   9.972  1.00 80.53  ? 71  GLU D CB  1 
ATOM   5878  C  CG  . GLU D  1 80  ? -14.041 1.864   9.783  1.00 86.41  ? 71  GLU D CG  1 
ATOM   5879  C  CD  . GLU D  1 80  ? -14.922 1.787   11.014 1.00 96.99  ? 71  GLU D CD  1 
ATOM   5880  O  OE1 . GLU D  1 80  ? -14.699 0.888   11.851 1.00 97.96  ? 71  GLU D OE1 1 
ATOM   5881  O  OE2 . GLU D  1 80  ? -15.837 2.627   11.145 1.00 93.71  ? 71  GLU D OE2 1 
ATOM   5882  N  N   . TYR D  1 81  ? -10.326 -0.863  8.612  1.00 70.78  ? 72  TYR D N   1 
ATOM   5883  C  CA  . TYR D  1 81  ? -9.129  -1.594  9.011  1.00 70.05  ? 72  TYR D CA  1 
ATOM   5884  C  C   . TYR D  1 81  ? -8.413  -2.183  7.800  1.00 68.58  ? 72  TYR D C   1 
ATOM   5885  O  O   . TYR D  1 81  ? -7.773  -3.230  7.894  1.00 68.82  ? 72  TYR D O   1 
ATOM   5886  C  CB  . TYR D  1 81  ? -9.484  -2.703  10.003 1.00 62.32  ? 72  TYR D CB  1 
ATOM   5887  C  CG  . TYR D  1 81  ? -9.957  -2.193  11.346 1.00 60.50  ? 72  TYR D CG  1 
ATOM   5888  C  CD1 . TYR D  1 81  ? -11.306 -2.190  11.672 1.00 63.60  ? 72  TYR D CD1 1 
ATOM   5889  C  CD2 . TYR D  1 81  ? -9.054  -1.715  12.286 1.00 60.83  ? 72  TYR D CD2 1 
ATOM   5890  C  CE1 . TYR D  1 81  ? -11.743 -1.725  12.898 1.00 66.13  ? 72  TYR D CE1 1 
ATOM   5891  C  CE2 . TYR D  1 81  ? -9.482  -1.247  13.513 1.00 60.62  ? 72  TYR D CE2 1 
ATOM   5892  C  CZ  . TYR D  1 81  ? -10.827 -1.255  13.814 1.00 66.26  ? 72  TYR D CZ  1 
ATOM   5893  O  OH  . TYR D  1 81  ? -11.258 -0.790  15.036 1.00 62.32  ? 72  TYR D OH  1 
ATOM   5894  N  N   . GLY D  1 82  ? -8.527  -1.502  6.664  1.00 71.09  ? 73  GLY D N   1 
ATOM   5895  C  CA  . GLY D  1 82  ? -7.705  -1.807  5.508  1.00 68.44  ? 73  GLY D CA  1 
ATOM   5896  C  C   . GLY D  1 82  ? -8.171  -3.052  4.779  1.00 70.77  ? 73  GLY D C   1 
ATOM   5897  O  O   . GLY D  1 82  ? -7.381  -3.733  4.126  1.00 73.21  ? 73  GLY D O   1 
ATOM   5898  N  N   . ASN D  1 83  ? -9.461  -3.350  4.893  1.00 69.62  ? 74  ASN D N   1 
ATOM   5899  C  CA  . ASN D  1 83  ? -10.042 -4.500  4.218  1.00 73.14  ? 74  ASN D CA  1 
ATOM   5900  C  C   . ASN D  1 83  ? -9.594  -5.860  4.753  1.00 77.19  ? 74  ASN D C   1 
ATOM   5901  O  O   . ASN D  1 83  ? -9.473  -6.818  3.987  1.00 79.27  ? 74  ASN D O   1 
ATOM   5902  C  CB  . ASN D  1 83  ? -9.775  -4.415  2.710  1.00 78.29  ? 74  ASN D CB  1 
ATOM   5903  C  CG  . ASN D  1 83  ? -11.024 -4.654  1.883  1.00 91.13  ? 74  ASN D CG  1 
ATOM   5904  O  OD1 . ASN D  1 83  ? -11.359 -5.799  1.554  1.00 87.98  ? 74  ASN D OD1 1 
ATOM   5905  N  ND2 . ASN D  1 83  ? -11.725 -3.569  1.542  1.00 89.07  ? 74  ASN D ND2 1 
ATOM   5906  N  N   . ILE D  1 84  ? -9.371  -5.944  6.066  1.00 74.15  ? 75  ILE D N   1 
ATOM   5907  C  CA  . ILE D  1 84  ? -9.111  -7.217  6.741  1.00 64.93  ? 75  ILE D CA  1 
ATOM   5908  C  C   . ILE D  1 84  ? -10.446 -7.863  7.115  1.00 63.80  ? 75  ILE D C   1 
ATOM   5909  O  O   . ILE D  1 84  ? -11.224 -7.285  7.862  1.00 62.38  ? 75  ILE D O   1 
ATOM   5910  C  CB  . ILE D  1 84  ? -8.292  -6.994  8.034  1.00 64.66  ? 75  ILE D CB  1 
ATOM   5911  C  CG1 . ILE D  1 84  ? -6.809  -6.767  7.718  1.00 62.47  ? 75  ILE D CG1 1 
ATOM   5912  C  CG2 . ILE D  1 84  ? -8.457  -8.162  8.992  1.00 66.53  ? 75  ILE D CG2 1 
ATOM   5913  C  CD1 . ILE D  1 84  ? -5.945  -6.493  8.954  1.00 54.21  ? 75  ILE D CD1 1 
ATOM   5914  N  N   . THR D  1 85  ? -10.741 -9.033  6.556  1.00 67.99  ? 76  THR D N   1 
ATOM   5915  C  CA  . THR D  1 85  ? -11.962 -9.744  6.931  1.00 70.75  ? 76  THR D CA  1 
ATOM   5916  C  C   . THR D  1 85  ? -11.769 -10.855 7.969  1.00 71.94  ? 76  THR D C   1 
ATOM   5917  O  O   . THR D  1 85  ? -12.751 -11.432 8.446  1.00 72.52  ? 76  THR D O   1 
ATOM   5918  C  CB  . THR D  1 85  ? -12.679 -10.327 5.703  1.00 70.50  ? 76  THR D CB  1 
ATOM   5919  O  OG1 . THR D  1 85  ? -11.702 -10.844 4.793  1.00 65.88  ? 76  THR D OG1 1 
ATOM   5920  C  CG2 . THR D  1 85  ? -13.498 -9.254  5.020  1.00 60.75  ? 76  THR D CG2 1 
ATOM   5921  N  N   . ASP D  1 86  ? -10.521 -11.146 8.327  1.00 69.45  ? 77  ASP D N   1 
ATOM   5922  C  CA  . ASP D  1 86  ? -10.259 -12.021 9.466  1.00 63.00  ? 77  ASP D CA  1 
ATOM   5923  C  C   . ASP D  1 86  ? -8.820  -12.055 9.944  1.00 59.52  ? 77  ASP D C   1 
ATOM   5924  O  O   . ASP D  1 86  ? -7.925  -11.449 9.341  1.00 53.42  ? 77  ASP D O   1 
ATOM   5925  C  CB  . ASP D  1 86  ? -10.742 -13.453 9.203  1.00 59.91  ? 77  ASP D CB  1 
ATOM   5926  C  CG  . ASP D  1 86  ? -10.270 -14.013 7.877  1.00 66.83  ? 77  ASP D CG  1 
ATOM   5927  O  OD1 . ASP D  1 86  ? -9.250  -13.552 7.327  1.00 64.57  ? 77  ASP D OD1 1 
ATOM   5928  O  OD2 . ASP D  1 86  ? -10.932 -14.950 7.390  1.00 77.12  ? 77  ASP D OD2 1 
ATOM   5929  N  N   . PHE D  1 87  ? -8.626  -12.762 11.059 1.00 59.12  ? 78  PHE D N   1 
ATOM   5930  C  CA  . PHE D  1 87  ? -7.305  -12.982 11.644 1.00 62.11  ? 78  PHE D CA  1 
ATOM   5931  C  C   . PHE D  1 87  ? -7.213  -14.248 12.517 1.00 62.44  ? 78  PHE D C   1 
ATOM   5932  O  O   . PHE D  1 87  ? -8.167  -14.651 13.199 1.00 56.68  ? 78  PHE D O   1 
ATOM   5933  C  CB  . PHE D  1 87  ? -6.840  -11.742 12.422 1.00 58.11  ? 78  PHE D CB  1 
ATOM   5934  C  CG  . PHE D  1 87  ? -7.727  -11.389 13.560 1.00 57.51  ? 78  PHE D CG  1 
ATOM   5935  C  CD1 . PHE D  1 87  ? -7.417  -11.792 14.838 1.00 59.94  ? 78  PHE D CD1 1 
ATOM   5936  C  CD2 . PHE D  1 87  ? -8.890  -10.682 13.351 1.00 56.48  ? 78  PHE D CD2 1 
ATOM   5937  C  CE1 . PHE D  1 87  ? -8.244  -11.487 15.886 1.00 59.83  ? 78  PHE D CE1 1 
ATOM   5938  C  CE2 . PHE D  1 87  ? -9.719  -10.373 14.403 1.00 61.23  ? 78  PHE D CE2 1 
ATOM   5939  C  CZ  . PHE D  1 87  ? -9.397  -10.780 15.669 1.00 58.20  ? 78  PHE D CZ  1 
ATOM   5940  N  N   . ARG D  1 88  ? -6.040  -14.861 12.495 1.00 61.84  ? 79  ARG D N   1 
ATOM   5941  C  CA  . ARG D  1 88  ? -5.730  -15.947 13.398 1.00 57.52  ? 79  ARG D CA  1 
ATOM   5942  C  C   . ARG D  1 88  ? -5.267  -15.335 14.715 1.00 63.64  ? 79  ARG D C   1 
ATOM   5943  O  O   . ARG D  1 88  ? -4.719  -14.231 14.735 1.00 66.46  ? 79  ARG D O   1 
ATOM   5944  C  CB  . ARG D  1 88  ? -4.664  -16.855 12.791 1.00 59.01  ? 79  ARG D CB  1 
ATOM   5945  C  CG  . ARG D  1 88  ? -5.152  -17.719 11.619 1.00 53.58  ? 79  ARG D CG  1 
ATOM   5946  C  CD  . ARG D  1 88  ? -5.438  -16.935 10.371 1.00 55.90  ? 79  ARG D CD  1 
ATOM   5947  N  NE  . ARG D  1 88  ? -5.737  -17.806 9.235  1.00 69.69  ? 79  ARG D NE  1 
ATOM   5948  C  CZ  . ARG D  1 88  ? -6.110  -17.377 8.027  1.00 73.14  ? 79  ARG D CZ  1 
ATOM   5949  N  NH1 . ARG D  1 88  ? -6.358  -18.248 7.044  1.00 60.70  ? 79  ARG D NH1 1 
ATOM   5950  N  NH2 . ARG D  1 88  ? -6.235  -16.073 7.801  1.00 78.19  ? 79  ARG D NH2 1 
ATOM   5951  N  N   . THR D  1 89  ? -5.548  -16.013 15.821 1.00 64.31  ? 80  THR D N   1 
ATOM   5952  C  CA  . THR D  1 89  ? -5.106  -15.549 17.129 1.00 62.11  ? 80  THR D CA  1 
ATOM   5953  C  C   . THR D  1 89  ? -4.993  -16.714 18.101 1.00 60.59  ? 80  THR D C   1 
ATOM   5954  O  O   . THR D  1 89  ? -5.694  -17.715 17.958 1.00 59.02  ? 80  THR D O   1 
ATOM   5955  C  CB  . THR D  1 89  ? -6.106  -14.521 17.718 1.00 69.53  ? 80  THR D CB  1 
ATOM   5956  O  OG1 . THR D  1 89  ? -5.495  -13.782 18.792 1.00 78.11  ? 80  THR D OG1 1 
ATOM   5957  C  CG2 . THR D  1 89  ? -7.368  -15.229 18.222 1.00 59.94  ? 80  THR D CG2 1 
ATOM   5958  N  N   . SER D  1 90  ? -4.132  -16.572 19.106 1.00 63.03  ? 81  SER D N   1 
ATOM   5959  C  CA  A SER D  1 90  ? -4.056  -17.556 20.183 0.50 64.61  ? 81  SER D CA  1 
ATOM   5960  C  CA  B SER D  1 90  ? -4.051  -17.547 20.192 0.50 64.62  ? 81  SER D CA  1 
ATOM   5961  C  C   . SER D  1 90  ? -5.397  -17.637 20.904 1.00 63.20  ? 81  SER D C   1 
ATOM   5962  O  O   . SER D  1 90  ? -6.086  -16.629 21.068 1.00 63.67  ? 81  SER D O   1 
ATOM   5963  C  CB  A SER D  1 90  ? -2.931  -17.214 21.163 0.50 65.91  ? 81  SER D CB  1 
ATOM   5964  C  CB  B SER D  1 90  ? -2.964  -17.160 21.191 0.50 65.91  ? 81  SER D CB  1 
ATOM   5965  O  OG  A SER D  1 90  ? -1.665  -17.269 20.527 0.50 65.52  ? 81  SER D OG  1 
ATOM   5966  O  OG  B SER D  1 90  ? -2.905  -18.096 22.252 0.50 63.77  ? 81  SER D OG  1 
ATOM   5967  N  N   . ALA D  1 91  ? -5.773  -18.841 21.327 1.00 62.67  ? 82  ALA D N   1 
ATOM   5968  C  CA  . ALA D  1 91  ? -7.066  -19.025 21.980 1.00 60.53  ? 82  ALA D CA  1 
ATOM   5969  C  C   . ALA D  1 91  ? -7.070  -18.505 23.419 1.00 66.12  ? 82  ALA D C   1 
ATOM   5970  O  O   . ALA D  1 91  ? -8.101  -18.502 24.097 1.00 68.64  ? 82  ALA D O   1 
ATOM   5971  C  CB  . ALA D  1 91  ? -7.507  -20.492 21.917 1.00 53.06  ? 82  ALA D CB  1 
ATOM   5972  N  N   . ALA D  1 92  ? -5.906  -18.067 23.879 1.00 67.52  ? 83  ALA D N   1 
ATOM   5973  C  CA  . ALA D  1 92  ? -5.801  -17.477 25.197 1.00 63.00  ? 83  ALA D CA  1 
ATOM   5974  C  C   . ALA D  1 92  ? -6.369  -16.060 25.216 1.00 65.59  ? 83  ALA D C   1 
ATOM   5975  O  O   . ALA D  1 92  ? -6.819  -15.578 26.254 1.00 78.20  ? 83  ALA D O   1 
ATOM   5976  C  CB  . ALA D  1 92  ? -4.370  -17.480 25.651 1.00 61.99  ? 83  ALA D CB  1 
ATOM   5977  N  N   . ASP D  1 93  ? -6.365  -15.401 24.064 1.00 60.08  ? 84  ASP D N   1 
ATOM   5978  C  CA  . ASP D  1 93  ? -6.717  -13.986 23.978 1.00 62.79  ? 84  ASP D CA  1 
ATOM   5979  C  C   . ASP D  1 93  ? -8.208  -13.748 23.779 1.00 62.31  ? 84  ASP D C   1 
ATOM   5980  O  O   . ASP D  1 93  ? -8.670  -12.613 23.786 1.00 65.13  ? 84  ASP D O   1 
ATOM   5981  C  CB  . ASP D  1 93  ? -5.934  -13.313 22.847 1.00 69.05  ? 84  ASP D CB  1 
ATOM   5982  C  CG  . ASP D  1 93  ? -4.429  -13.562 22.939 1.00 74.35  ? 84  ASP D CG  1 
ATOM   5983  O  OD1 . ASP D  1 93  ? -3.933  -13.905 24.039 1.00 73.39  ? 84  ASP D OD1 1 
ATOM   5984  O  OD2 . ASP D  1 93  ? -3.742  -13.410 21.902 1.00 76.66  ? 84  ASP D OD2 1 
ATOM   5985  N  N   . ILE D  1 94  ? -8.959  -14.823 23.593 1.00 61.18  ? 85  ILE D N   1 
ATOM   5986  C  CA  . ILE D  1 94  ? -10.396 -14.717 23.398 1.00 58.43  ? 85  ILE D CA  1 
ATOM   5987  C  C   . ILE D  1 94  ? -11.123 -15.708 24.287 1.00 60.86  ? 85  ILE D C   1 
ATOM   5988  O  O   . ILE D  1 94  ? -10.574 -16.742 24.691 1.00 58.44  ? 85  ILE D O   1 
ATOM   5989  C  CB  . ILE D  1 94  ? -10.810 -14.989 21.939 1.00 57.91  ? 85  ILE D CB  1 
ATOM   5990  C  CG1 . ILE D  1 94  ? -10.311 -16.364 21.488 1.00 54.63  ? 85  ILE D CG1 1 
ATOM   5991  C  CG2 . ILE D  1 94  ? -10.284 -13.914 21.020 1.00 60.75  ? 85  ILE D CG2 1 
ATOM   5992  C  CD1 . ILE D  1 94  ? -11.053 -16.895 20.311 1.00 55.79  ? 85  ILE D CD1 1 
ATOM   5993  N  N   . TRP D  1 95  ? -12.367 -15.377 24.598 1.00 60.16  ? 86  TRP D N   1 
ATOM   5994  C  CA  . TRP D  1 95  ? -13.185 -16.236 25.420 1.00 60.29  ? 86  TRP D CA  1 
ATOM   5995  C  C   . TRP D  1 95  ? -13.454 -17.509 24.647 1.00 59.52  ? 86  TRP D C   1 
ATOM   5996  O  O   . TRP D  1 95  ? -13.874 -17.467 23.495 1.00 59.73  ? 86  TRP D O   1 
ATOM   5997  C  CB  . TRP D  1 95  ? -14.495 -15.539 25.757 1.00 57.99  ? 86  TRP D CB  1 
ATOM   5998  C  CG  . TRP D  1 95  ? -15.421 -16.392 26.522 1.00 58.50  ? 86  TRP D CG  1 
ATOM   5999  C  CD1 . TRP D  1 95  ? -15.571 -16.422 27.868 1.00 60.41  ? 86  TRP D CD1 1 
ATOM   6000  C  CD2 . TRP D  1 95  ? -16.335 -17.356 25.995 1.00 61.39  ? 86  TRP D CD2 1 
ATOM   6001  N  NE1 . TRP D  1 95  ? -16.530 -17.332 28.221 1.00 59.46  ? 86  TRP D NE1 1 
ATOM   6002  C  CE2 . TRP D  1 95  ? -17.012 -17.927 27.085 1.00 64.35  ? 86  TRP D CE2 1 
ATOM   6003  C  CE3 . TRP D  1 95  ? -16.654 -17.790 24.701 1.00 56.86  ? 86  TRP D CE3 1 
ATOM   6004  C  CZ2 . TRP D  1 95  ? -17.985 -18.906 26.930 1.00 66.50  ? 86  TRP D CZ2 1 
ATOM   6005  C  CZ3 . TRP D  1 95  ? -17.618 -18.755 24.544 1.00 49.78  ? 86  TRP D CZ3 1 
ATOM   6006  C  CH2 . TRP D  1 95  ? -18.272 -19.307 25.649 1.00 62.82  ? 86  TRP D CH2 1 
ATOM   6007  N  N   . THR D  1 96  ? -13.252 -18.651 25.268 1.00 59.34  ? 87  THR D N   1 
ATOM   6008  C  CA  . THR D  1 96  ? -13.508 -19.911 24.632 1.00 61.03  ? 87  THR D CA  1 
ATOM   6009  C  C   . THR D  1 96  ? -14.417 -20.625 25.574 1.00 62.82  ? 87  THR D C   1 
ATOM   6010  O  O   . THR D  1 96  ? -14.301 -20.469 26.758 1.00 60.94  ? 87  THR D O   1 
ATOM   6011  C  CB  . THR D  1 96  ? -12.285 -20.726 24.534 1.00 57.58  ? 87  THR D CB  1 
ATOM   6012  O  OG1 . THR D  1 96  ? -12.063 -21.338 25.790 1.00 61.24  ? 87  THR D OG1 1 
ATOM   6013  C  CG2 . THR D  1 96  ? -11.139 -19.864 24.251 1.00 61.59  ? 87  THR D CG2 1 
ATOM   6014  N  N   . PRO D  1 97  ? -15.331 -21.405 25.033 1.00 66.96  ? 88  PRO D N   1 
ATOM   6015  C  CA  . PRO D  1 97  ? -16.310 -22.179 25.787 1.00 64.40  ? 88  PRO D CA  1 
ATOM   6016  C  C   . PRO D  1 97  ? -15.804 -23.394 26.522 1.00 57.73  ? 88  PRO D C   1 
ATOM   6017  O  O   . PRO D  1 97  ? -14.841 -24.000 26.128 1.00 52.62  ? 88  PRO D O   1 
ATOM   6018  C  CB  . PRO D  1 97  ? -17.272 -22.646 24.700 1.00 62.89  ? 88  PRO D CB  1 
ATOM   6019  C  CG  . PRO D  1 97  ? -16.702 -22.226 23.448 1.00 55.87  ? 88  PRO D CG  1 
ATOM   6020  C  CD  . PRO D  1 97  ? -15.860 -21.067 23.722 1.00 64.59  ? 88  PRO D CD  1 
ATOM   6021  N  N   . ASP D  1 98  ? -16.470 -23.742 27.603 1.00 53.46  ? 89  ASP D N   1 
ATOM   6022  C  CA  . ASP D  1 98  ? -16.066 -24.889 28.354 1.00 55.60  ? 89  ASP D CA  1 
ATOM   6023  C  C   . ASP D  1 98  ? -16.710 -26.183 27.939 1.00 57.07  ? 89  ASP D C   1 
ATOM   6024  O  O   . ASP D  1 98  ? -17.389 -26.776 28.722 1.00 59.73  ? 89  ASP D O   1 
ATOM   6025  C  CB  . ASP D  1 98  ? -16.313 -24.655 29.824 1.00 58.69  ? 89  ASP D CB  1 
ATOM   6026  C  CG  . ASP D  1 98  ? -17.729 -24.594 30.146 1.00 62.13  ? 89  ASP D CG  1 
ATOM   6027  O  OD1 . ASP D  1 98  ? -18.072 -24.577 31.323 1.00 61.39  ? 89  ASP D OD1 1 
ATOM   6028  O  OD2 . ASP D  1 98  ? -18.510 -24.570 29.214 1.00 61.09  ? 89  ASP D OD2 1 
ATOM   6029  N  N   . ILE D  1 99  ? -16.489 -26.633 26.718 1.00 54.90  ? 90  ILE D N   1 
ATOM   6030  C  CA  . ILE D  1 99  ? -17.051 -27.885 26.268 1.00 63.00  ? 90  ILE D CA  1 
ATOM   6031  C  C   . ILE D  1 99  ? -16.106 -28.912 26.785 1.00 59.02  ? 90  ILE D C   1 
ATOM   6032  O  O   . ILE D  1 99  ? -14.917 -28.699 26.781 1.00 56.42  ? 90  ILE D O   1 
ATOM   6033  C  CB  . ILE D  1 99  ? -17.057 -28.037 24.759 1.00 65.60  ? 90  ILE D CB  1 
ATOM   6034  C  CG1 . ILE D  1 99  ? -17.918 -26.983 24.106 1.00 60.75  ? 90  ILE D CG1 1 
ATOM   6035  C  CG2 . ILE D  1 99  ? -17.533 -29.394 24.389 1.00 53.81  ? 90  ILE D CG2 1 
ATOM   6036  C  CD1 . ILE D  1 99  ? -19.103 -26.658 24.868 1.00 59.14  ? 90  ILE D CD1 1 
ATOM   6037  N  N   . THR D  1 100 ? -16.632 -30.031 27.230 1.00 48.53  ? 91  THR D N   1 
ATOM   6038  C  CA  . THR D  1 100 ? -15.793 -31.082 27.774 1.00 58.63  ? 91  THR D CA  1 
ATOM   6039  C  C   . THR D  1 100 ? -16.452 -32.442 27.562 1.00 57.37  ? 91  THR D C   1 
ATOM   6040  O  O   . THR D  1 100 ? -17.676 -32.535 27.515 1.00 57.81  ? 91  THR D O   1 
ATOM   6041  C  CB  . THR D  1 100 ? -15.504 -30.852 29.291 1.00 56.38  ? 91  THR D CB  1 
ATOM   6042  O  OG1 . THR D  1 100 ? -14.823 -31.991 29.840 1.00 55.87  ? 91  THR D OG1 1 
ATOM   6043  C  CG2 . THR D  1 100 ? -16.789 -30.628 30.052 1.00 55.24  ? 91  THR D CG2 1 
ATOM   6044  N  N   . ALA D  1 101 ? -15.643 -33.486 27.408 1.00 52.05  ? 92  ALA D N   1 
ATOM   6045  C  CA  . ALA D  1 101 ? -16.162 -34.849 27.437 1.00 60.14  ? 92  ALA D CA  1 
ATOM   6046  C  C   . ALA D  1 101 ? -16.616 -35.203 28.854 1.00 63.42  ? 92  ALA D C   1 
ATOM   6047  O  O   . ALA D  1 101 ? -15.863 -35.040 29.820 1.00 68.26  ? 92  ALA D O   1 
ATOM   6048  C  CB  . ALA D  1 101 ? -15.110 -35.840 26.960 1.00 59.68  ? 92  ALA D CB  1 
ATOM   6049  N  N   . TYR D  1 102 ? -17.848 -35.687 28.970 1.00 57.67  ? 93  TYR D N   1 
ATOM   6050  C  CA  . TYR D  1 102 ? -18.453 -35.939 30.272 1.00 57.38  ? 93  TYR D CA  1 
ATOM   6051  C  C   . TYR D  1 102 ? -17.934 -37.238 30.879 1.00 52.24  ? 93  TYR D C   1 
ATOM   6052  O  O   . TYR D  1 102 ? -17.921 -37.403 32.098 1.00 68.37  ? 93  TYR D O   1 
ATOM   6053  C  CB  . TYR D  1 102 ? -19.978 -35.989 30.153 1.00 65.65  ? 93  TYR D CB  1 
ATOM   6054  C  CG  . TYR D  1 102 ? -20.619 -34.639 29.924 1.00 67.31  ? 93  TYR D CG  1 
ATOM   6055  C  CD1 . TYR D  1 102 ? -19.914 -33.466 30.154 1.00 67.83  ? 93  TYR D CD1 1 
ATOM   6056  C  CD2 . TYR D  1 102 ? -21.929 -34.539 29.476 1.00 67.29  ? 93  TYR D CD2 1 
ATOM   6057  C  CE1 . TYR D  1 102 ? -20.496 -32.230 29.946 1.00 66.82  ? 93  TYR D CE1 1 
ATOM   6058  C  CE2 . TYR D  1 102 ? -22.520 -33.308 29.265 1.00 69.71  ? 93  TYR D CE2 1 
ATOM   6059  C  CZ  . TYR D  1 102 ? -21.799 -32.157 29.501 1.00 70.09  ? 93  TYR D CZ  1 
ATOM   6060  O  OH  . TYR D  1 102 ? -22.383 -30.929 29.292 1.00 63.54  ? 93  TYR D OH  1 
ATOM   6061  N  N   . SER D  1 103 ? -17.507 -38.157 30.019 1.00 49.12  ? 94  SER D N   1 
ATOM   6062  C  CA  . SER D  1 103 ? -17.019 -39.456 30.467 1.00 55.24  ? 94  SER D CA  1 
ATOM   6063  C  C   . SER D  1 103 ? -15.580 -39.688 30.020 1.00 57.79  ? 94  SER D C   1 
ATOM   6064  O  O   . SER D  1 103 ? -15.181 -40.820 29.747 1.00 53.62  ? 94  SER D O   1 
ATOM   6065  C  CB  . SER D  1 103 ? -17.920 -40.576 29.944 1.00 55.00  ? 94  SER D CB  1 
ATOM   6066  O  OG  . SER D  1 103 ? -18.271 -40.357 28.588 1.00 53.22  ? 94  SER D OG  1 
ATOM   6067  N  N   . SER D  1 104 ? -14.807 -38.610 29.948 1.00 59.18  ? 95  SER D N   1 
ATOM   6068  C  CA  . SER D  1 104 ? -13.354 -38.705 30.024 1.00 53.24  ? 95  SER D CA  1 
ATOM   6069  C  C   . SER D  1 104 ? -12.920 -39.522 31.236 1.00 52.28  ? 95  SER D C   1 
ATOM   6070  O  O   . SER D  1 104 ? -13.405 -39.309 32.347 1.00 48.95  ? 95  SER D O   1 
ATOM   6071  C  CB  . SER D  1 104 ? -12.728 -37.310 30.079 1.00 51.61  ? 95  SER D CB  1 
ATOM   6072  O  OG  . SER D  1 104 ? -13.326 -36.521 31.092 1.00 69.23  ? 95  SER D OG  1 
ATOM   6073  N  N   . THR D  1 105 ? -12.003 -40.458 31.014 1.00 51.57  ? 96  THR D N   1 
ATOM   6074  C  CA  . THR D  1 105 ? -11.258 -41.069 32.100 1.00 50.92  ? 96  THR D CA  1 
ATOM   6075  C  C   . THR D  1 105 ? -9.834  -40.529 32.269 1.00 49.16  ? 96  THR D C   1 
ATOM   6076  O  O   . THR D  1 105 ? -9.115  -40.937 33.176 1.00 57.03  ? 96  THR D O   1 
ATOM   6077  C  CB  . THR D  1 105 ? -11.181 -42.600 31.933 1.00 52.25  ? 96  THR D CB  1 
ATOM   6078  O  OG1 . THR D  1 105 ? -10.522 -42.919 30.700 1.00 56.19  ? 96  THR D OG1 1 
ATOM   6079  C  CG2 . THR D  1 105 ? -12.564 -43.193 31.943 1.00 51.35  ? 96  THR D CG2 1 
ATOM   6080  N  N   . ARG D  1 106 ? -9.401  -39.651 31.387 1.00 44.62  ? 97  ARG D N   1 
ATOM   6081  C  CA  A ARG D  1 106 ? -8.070  -39.071 31.502 0.60 48.78  ? 97  ARG D CA  1 
ATOM   6082  C  CA  B ARG D  1 106 ? -8.072  -39.068 31.507 0.40 48.78  ? 97  ARG D CA  1 
ATOM   6083  C  C   . ARG D  1 106 ? -8.062  -37.613 31.062 1.00 46.90  ? 97  ARG D C   1 
ATOM   6084  O  O   . ARG D  1 106 ? -9.000  -37.149 30.420 1.00 52.22  ? 97  ARG D O   1 
ATOM   6085  C  CB  A ARG D  1 106 ? -7.055  -39.888 30.712 0.60 50.50  ? 97  ARG D CB  1 
ATOM   6086  C  CB  B ARG D  1 106 ? -7.044  -39.903 30.750 0.40 50.52  ? 97  ARG D CB  1 
ATOM   6087  C  CG  A ARG D  1 106 ? -5.986  -40.519 31.568 0.60 52.91  ? 97  ARG D CG  1 
ATOM   6088  C  CG  B ARG D  1 106 ? -7.020  -41.348 31.208 0.40 54.71  ? 97  ARG D CG  1 
ATOM   6089  C  CD  A ARG D  1 106 ? -5.088  -41.412 30.731 0.60 59.62  ? 97  ARG D CD  1 
ATOM   6090  C  CD  B ARG D  1 106 ? -5.695  -42.004 30.917 0.40 58.38  ? 97  ARG D CD  1 
ATOM   6091  N  NE  A ARG D  1 106 ? -5.555  -42.797 30.678 0.60 60.23  ? 97  ARG D NE  1 
ATOM   6092  N  NE  B ARG D  1 106 ? -4.578  -41.182 31.371 0.40 59.52  ? 97  ARG D NE  1 
ATOM   6093  C  CZ  A ARG D  1 106 ? -5.223  -43.661 29.722 0.60 60.86  ? 97  ARG D CZ  1 
ATOM   6094  C  CZ  B ARG D  1 106 ? -3.905  -41.376 32.501 0.40 58.14  ? 97  ARG D CZ  1 
ATOM   6095  N  NH1 A ARG D  1 106 ? -4.431  -43.281 28.721 0.60 58.13  ? 97  ARG D NH1 1 
ATOM   6096  N  NH1 B ARG D  1 106 ? -4.229  -42.372 33.317 0.40 50.92  ? 97  ARG D NH1 1 
ATOM   6097  N  NH2 A ARG D  1 106 ? -5.696  -44.899 29.761 0.60 56.08  ? 97  ARG D NH2 1 
ATOM   6098  N  NH2 B ARG D  1 106 ? -2.900  -40.568 32.807 0.40 55.87  ? 97  ARG D NH2 1 
ATOM   6099  N  N   . PRO D  1 107 ? -7.022  -36.867 31.438 1.00 49.23  ? 98  PRO D N   1 
ATOM   6100  C  CA  . PRO D  1 107 ? -6.982  -35.496 30.930 1.00 49.35  ? 98  PRO D CA  1 
ATOM   6101  C  C   . PRO D  1 107 ? -6.784  -35.542 29.427 1.00 49.21  ? 98  PRO D C   1 
ATOM   6102  O  O   . PRO D  1 107 ? -6.025  -36.382 28.945 1.00 58.40  ? 98  PRO D O   1 
ATOM   6103  C  CB  . PRO D  1 107 ? -5.739  -34.912 31.608 1.00 42.09  ? 98  PRO D CB  1 
ATOM   6104  C  CG  . PRO D  1 107 ? -5.544  -35.731 32.812 1.00 47.32  ? 98  PRO D CG  1 
ATOM   6105  C  CD  . PRO D  1 107 ? -5.973  -37.113 32.436 1.00 53.43  ? 98  PRO D CD  1 
ATOM   6106  N  N   . VAL D  1 108 ? -7.460  -34.664 28.698 1.00 44.62  ? 99  VAL D N   1 
ATOM   6107  C  CA  . VAL D  1 108 ? -7.349  -34.625 27.239 1.00 48.46  ? 99  VAL D CA  1 
ATOM   6108  C  C   . VAL D  1 108 ? -5.999  -34.093 26.786 1.00 46.11  ? 99  VAL D C   1 
ATOM   6109  O  O   . VAL D  1 108 ? -5.553  -33.055 27.257 1.00 49.74  ? 99  VAL D O   1 
ATOM   6110  C  CB  . VAL D  1 108 ? -8.419  -33.717 26.638 1.00 44.32  ? 99  VAL D CB  1 
ATOM   6111  C  CG1 . VAL D  1 108 ? -8.225  -33.622 25.169 1.00 54.20  ? 99  VAL D CG1 1 
ATOM   6112  C  CG2 . VAL D  1 108 ? -9.789  -34.255 26.950 1.00 51.20  ? 99  VAL D CG2 1 
ATOM   6113  N  N   . GLN D  1 109 ? -5.349  -34.792 25.867 1.00 48.25  ? 100 GLN D N   1 
ATOM   6114  C  CA  . GLN D  1 109 ? -4.115  -34.273 25.279 1.00 53.15  ? 100 GLN D CA  1 
ATOM   6115  C  C   . GLN D  1 109 ? -4.344  -33.444 23.998 1.00 55.40  ? 100 GLN D C   1 
ATOM   6116  O  O   . GLN D  1 109 ? -4.945  -33.917 23.031 1.00 54.60  ? 100 GLN D O   1 
ATOM   6117  C  CB  . GLN D  1 109 ? -3.127  -35.402 24.999 1.00 49.97  ? 100 GLN D CB  1 
ATOM   6118  C  CG  . GLN D  1 109 ? -2.515  -36.036 26.234 1.00 45.17  ? 100 GLN D CG  1 
ATOM   6119  C  CD  . GLN D  1 109 ? -2.364  -37.516 26.057 1.00 56.22  ? 100 GLN D CD  1 
ATOM   6120  O  OE1 . GLN D  1 109 ? -1.264  -38.026 25.850 1.00 58.84  ? 100 GLN D OE1 1 
ATOM   6121  N  NE2 . GLN D  1 109 ? -3.487  -38.225 26.103 1.00 60.13  ? 100 GLN D NE2 1 
ATOM   6122  N  N   . VAL D  1 110 ? -3.835  -32.214 23.995 1.00 55.50  ? 101 VAL D N   1 
ATOM   6123  C  CA  . VAL D  1 110 ? -3.969  -31.329 22.848 1.00 52.92  ? 101 VAL D CA  1 
ATOM   6124  C  C   . VAL D  1 110 ? -2.873  -31.583 21.810 1.00 52.09  ? 101 VAL D C   1 
ATOM   6125  O  O   . VAL D  1 110 ? -1.680  -31.425 22.083 1.00 43.02  ? 101 VAL D O   1 
ATOM   6126  C  CB  . VAL D  1 110 ? -3.930  -29.864 23.295 1.00 60.70  ? 101 VAL D CB  1 
ATOM   6127  C  CG1 . VAL D  1 110 ? -3.889  -28.943 22.092 1.00 56.19  ? 101 VAL D CG1 1 
ATOM   6128  C  CG2 . VAL D  1 110 ? -5.132  -29.562 24.178 1.00 66.39  ? 101 VAL D CG2 1 
ATOM   6129  N  N   . LEU D  1 111 ? -3.308  -31.987 20.616 1.00 57.70  ? 102 LEU D N   1 
ATOM   6130  C  CA  . LEU D  1 111 ? -2.413  -32.399 19.526 1.00 55.38  ? 102 LEU D CA  1 
ATOM   6131  C  C   . LEU D  1 111 ? -2.114  -31.330 18.498 1.00 53.81  ? 102 LEU D C   1 
ATOM   6132  O  O   . LEU D  1 111 ? -1.358  -31.591 17.566 1.00 54.41  ? 102 LEU D O   1 
ATOM   6133  C  CB  . LEU D  1 111 ? -2.987  -33.603 18.792 1.00 51.02  ? 102 LEU D CB  1 
ATOM   6134  C  CG  . LEU D  1 111 ? -3.378  -34.764 19.684 1.00 53.56  ? 102 LEU D CG  1 
ATOM   6135  C  CD1 . LEU D  1 111 ? -4.304  -35.683 18.923 1.00 51.58  ? 102 LEU D CD1 1 
ATOM   6136  C  CD2 . LEU D  1 111 ? -2.123  -35.468 20.165 1.00 51.28  ? 102 LEU D CD2 1 
ATOM   6137  N  N   . SER D  1 112 ? -2.718  -30.150 18.660 1.00 53.67  ? 103 SER D N   1 
ATOM   6138  C  CA  . SER D  1 112 ? -2.601  -29.055 17.694 1.00 50.93  ? 103 SER D CA  1 
ATOM   6139  C  C   . SER D  1 112 ? -2.343  -27.714 18.373 1.00 52.24  ? 103 SER D C   1 
ATOM   6140  O  O   . SER D  1 112 ? -2.729  -27.507 19.529 1.00 53.49  ? 103 SER D O   1 
ATOM   6141  C  CB  . SER D  1 112 ? -3.877  -28.946 16.862 1.00 52.12  ? 103 SER D CB  1 
ATOM   6142  O  OG  . SER D  1 112 ? -4.972  -28.511 17.653 1.00 53.05  ? 103 SER D OG  1 
ATOM   6143  N  N   . PRO D  1 113 ? -1.693  -26.789 17.652 1.00 50.30  ? 104 PRO D N   1 
ATOM   6144  C  CA  . PRO D  1 113 ? -1.524  -25.439 18.186 1.00 53.17  ? 104 PRO D CA  1 
ATOM   6145  C  C   . PRO D  1 113 ? -2.897  -24.909 18.556 1.00 56.75  ? 104 PRO D C   1 
ATOM   6146  O  O   . PRO D  1 113 ? -3.867  -25.236 17.876 1.00 58.09  ? 104 PRO D O   1 
ATOM   6147  C  CB  . PRO D  1 113 ? -0.947  -24.667 16.998 1.00 50.22  ? 104 PRO D CB  1 
ATOM   6148  C  CG  . PRO D  1 113 ? -0.245  -25.705 16.194 1.00 52.83  ? 104 PRO D CG  1 
ATOM   6149  C  CD  . PRO D  1 113 ? -1.126  -26.917 16.299 1.00 57.86  ? 104 PRO D CD  1 
ATOM   6150  N  N   . GLN D  1 114 ? -3.012  -24.145 19.634 1.00 58.96  ? 105 GLN D N   1 
ATOM   6151  C  CA  . GLN D  1 114 ? -4.345  -23.711 19.989 1.00 62.16  ? 105 GLN D CA  1 
ATOM   6152  C  C   . GLN D  1 114 ? -4.484  -22.280 19.557 1.00 63.13  ? 105 GLN D C   1 
ATOM   6153  O  O   . GLN D  1 114 ? -4.048  -21.348 20.251 1.00 62.66  ? 105 GLN D O   1 
ATOM   6154  C  CB  . GLN D  1 114 ? -4.559  -23.858 21.486 1.00 56.21  ? 105 GLN D CB  1 
ATOM   6155  C  CG  . GLN D  1 114 ? -4.158  -25.232 21.983 1.00 60.42  ? 105 GLN D CG  1 
ATOM   6156  C  CD  . GLN D  1 114 ? -4.380  -25.420 23.471 1.00 65.34  ? 105 GLN D CD  1 
ATOM   6157  O  OE1 . GLN D  1 114 ? -5.439  -25.869 23.886 1.00 63.38  ? 105 GLN D OE1 1 
ATOM   6158  N  NE2 . GLN D  1 114 ? -3.374  -25.094 24.275 1.00 57.40  ? 105 GLN D NE2 1 
ATOM   6159  N  N   . ASN D  1 115 ? -5.215  -22.135 18.457 1.00 54.19  ? 106 ASN D N   1 
ATOM   6160  C  CA  . ASN D  1 115 ? -5.286  -20.912 17.692 1.00 51.62  ? 106 ASN D CA  1 
ATOM   6161  C  C   . ASN D  1 115 ? -6.668  -20.911 17.134 1.00 55.72  ? 106 ASN D C   1 
ATOM   6162  O  O   . ASN D  1 115 ? -7.194  -21.964 16.784 1.00 60.63  ? 106 ASN D O   1 
ATOM   6163  C  CB  . ASN D  1 115 ? -4.308  -20.947 16.531 1.00 53.00  ? 106 ASN D CB  1 
ATOM   6164  C  CG  . ASN D  1 115 ? -2.900  -20.626 16.946 1.00 55.12  ? 106 ASN D CG  1 
ATOM   6165  O  OD1 . ASN D  1 115 ? -2.692  -19.864 17.875 1.00 50.23  ? 106 ASN D OD1 1 
ATOM   6166  N  ND2 . ASN D  1 115 ? -1.916  -21.205 16.252 1.00 55.97  ? 106 ASN D ND2 1 
ATOM   6167  N  N   . ALA D  1 116 ? -7.265  -19.736 17.045 1.00 60.97  ? 107 ALA D N   1 
ATOM   6168  C  CA  . ALA D  1 116 ? -8.610  -19.625 16.512 1.00 65.09  ? 107 ALA D CA  1 
ATOM   6169  C  C   . ALA D  1 116 ? -8.635  -18.672 15.322 1.00 60.85  ? 107 ALA D C   1 
ATOM   6170  O  O   . ALA D  1 116 ? -7.707  -17.893 15.105 1.00 59.01  ? 107 ALA D O   1 
ATOM   6171  C  CB  . ALA D  1 116 ? -9.581  -19.162 17.603 1.00 63.43  ? 107 ALA D CB  1 
ATOM   6172  N  N   . LEU D  1 117 ? -9.698  -18.756 14.540 1.00 60.50  ? 108 LEU D N   1 
ATOM   6173  C  CA  . LEU D  1 117 ? -9.898  -17.833 13.446 1.00 58.92  ? 108 LEU D CA  1 
ATOM   6174  C  C   . LEU D  1 117 ? -11.069 -16.958 13.828 1.00 59.79  ? 108 LEU D C   1 
ATOM   6175  O  O   . LEU D  1 117 ? -12.128 -17.462 14.192 1.00 61.80  ? 108 LEU D O   1 
ATOM   6176  C  CB  . LEU D  1 117 ? -10.214 -18.602 12.168 1.00 57.47  ? 108 LEU D CB  1 
ATOM   6177  C  CG  . LEU D  1 117 ? -10.254 -17.791 10.875 1.00 71.24  ? 108 LEU D CG  1 
ATOM   6178  C  CD1 . LEU D  1 117 ? -8.843  -17.385 10.461 1.00 69.12  ? 108 LEU D CD1 1 
ATOM   6179  C  CD2 . LEU D  1 117 ? -10.944 -18.572 9.759  1.00 69.42  ? 108 LEU D CD2 1 
ATOM   6180  N  N   . VAL D  1 118 ? -10.873 -15.647 13.785 1.00 59.50  ? 109 VAL D N   1 
ATOM   6181  C  CA  . VAL D  1 118 ? -11.975 -14.715 14.013 1.00 67.30  ? 109 VAL D CA  1 
ATOM   6182  C  C   . VAL D  1 118 ? -12.181 -13.908 12.735 1.00 66.79  ? 109 VAL D C   1 
ATOM   6183  O  O   . VAL D  1 118 ? -11.210 -13.618 12.033 1.00 65.01  ? 109 VAL D O   1 
ATOM   6184  C  CB  . VAL D  1 118 ? -11.683 -13.753 15.197 1.00 61.15  ? 109 VAL D CB  1 
ATOM   6185  C  CG1 . VAL D  1 118 ? -12.936 -12.965 15.574 1.00 59.54  ? 109 VAL D CG1 1 
ATOM   6186  C  CG2 . VAL D  1 118 ? -11.189 -14.529 16.387 1.00 60.08  ? 109 VAL D CG2 1 
ATOM   6187  N  N   . ASN D  1 119 ? -13.427 -13.555 12.419 1.00 64.99  ? 110 ASN D N   1 
ATOM   6188  C  CA  . ASN D  1 119 ? -13.677 -12.686 11.264 1.00 72.16  ? 110 ASN D CA  1 
ATOM   6189  C  C   . ASN D  1 119 ? -14.763 -11.613 11.405 1.00 72.10  ? 110 ASN D C   1 
ATOM   6190  O  O   . ASN D  1 119 ? -15.551 -11.631 12.353 1.00 75.05  ? 110 ASN D O   1 
ATOM   6191  C  CB  . ASN D  1 119 ? -13.861 -13.490 9.986  1.00 74.55  ? 110 ASN D CB  1 
ATOM   6192  C  CG  . ASN D  1 119 ? -15.221 -14.099 9.870  1.00 79.28  ? 110 ASN D CG  1 
ATOM   6193  O  OD1 . ASN D  1 119 ? -16.098 -13.897 10.711 1.00 71.01  ? 110 ASN D OD1 1 
ATOM   6194  N  ND2 . ASN D  1 119 ? -15.417 -14.852 8.806  1.00 89.55  ? 110 ASN D ND2 1 
ATOM   6195  N  N   . SER D  1 120 ? -14.800 -10.700 10.436 1.00 69.08  ? 111 SER D N   1 
ATOM   6196  C  CA  . SER D  1 120 ? -15.500 -9.420  10.574 1.00 67.99  ? 111 SER D CA  1 
ATOM   6197  C  C   . SER D  1 120 ? -16.951 -9.526  11.038 1.00 66.78  ? 111 SER D C   1 
ATOM   6198  O  O   . SER D  1 120 ? -17.459 -8.600  11.662 1.00 67.43  ? 111 SER D O   1 
ATOM   6199  C  CB  . SER D  1 120 ? -15.418 -8.618  9.271  1.00 67.17  ? 111 SER D CB  1 
ATOM   6200  O  OG  . SER D  1 120 ? -16.321 -9.121  8.302  1.00 69.76  ? 111 SER D OG  1 
ATOM   6201  N  N   . SER D  1 121 ? -17.617 -10.639 10.744 1.00 70.60  ? 112 SER D N   1 
ATOM   6202  C  CA  . SER D  1 121 ? -18.995 -10.838 11.193 1.00 66.87  ? 112 SER D CA  1 
ATOM   6203  C  C   . SER D  1 121 ? -19.081 -11.130 12.683 1.00 73.64  ? 112 SER D C   1 
ATOM   6204  O  O   . SER D  1 121 ? -20.172 -11.198 13.246 1.00 71.91  ? 112 SER D O   1 
ATOM   6205  C  CB  . SER D  1 121 ? -19.652 -11.971 10.422 1.00 75.37  ? 112 SER D CB  1 
ATOM   6206  O  OG  . SER D  1 121 ? -19.696 -11.666 9.041  1.00 93.73  ? 112 SER D OG  1 
ATOM   6207  N  N   . GLY D  1 122 ? -17.922 -11.315 13.309 1.00 70.57  ? 113 GLY D N   1 
ATOM   6208  C  CA  . GLY D  1 122 ? -17.851 -11.656 14.713 1.00 67.35  ? 113 GLY D CA  1 
ATOM   6209  C  C   . GLY D  1 122 ? -17.962 -13.146 14.996 1.00 69.08  ? 113 GLY D C   1 
ATOM   6210  O  O   . GLY D  1 122 ? -18.299 -13.546 16.107 1.00 65.59  ? 113 GLY D O   1 
ATOM   6211  N  N   . HIS D  1 123 ? -17.682 -13.968 13.989 1.00 72.55  ? 114 HIS D N   1 
ATOM   6212  C  CA  . HIS D  1 123 ? -17.714 -15.420 14.144 1.00 68.97  ? 114 HIS D CA  1 
ATOM   6213  C  C   . HIS D  1 123 ? -16.329 -15.946 14.480 1.00 61.94  ? 114 HIS D C   1 
ATOM   6214  O  O   . HIS D  1 123 ? -15.317 -15.445 13.983 1.00 59.36  ? 114 HIS D O   1 
ATOM   6215  C  CB  . HIS D  1 123 ? -18.200 -16.115 12.866 1.00 73.77  ? 114 HIS D CB  1 
ATOM   6216  C  CG  . HIS D  1 123 ? -19.640 -15.871 12.540 1.00 76.64  ? 114 HIS D CG  1 
ATOM   6217  N  ND1 . HIS D  1 123 ? -20.050 -14.863 11.696 1.00 80.90  ? 114 HIS D ND1 1 
ATOM   6218  C  CD2 . HIS D  1 123 ? -20.764 -16.520 12.923 1.00 77.00  ? 114 HIS D CD2 1 
ATOM   6219  C  CE1 . HIS D  1 123 ? -21.365 -14.893 11.584 1.00 79.69  ? 114 HIS D CE1 1 
ATOM   6220  N  NE2 . HIS D  1 123 ? -21.823 -15.888 12.320 1.00 76.73  ? 114 HIS D NE2 1 
ATOM   6221  N  N   . VAL D  1 124 ? -16.297 -16.968 15.328 1.00 63.36  ? 115 VAL D N   1 
ATOM   6222  C  CA  . VAL D  1 124 ? -15.050 -17.607 15.734 1.00 59.57  ? 115 VAL D CA  1 
ATOM   6223  C  C   . VAL D  1 124 ? -15.035 -19.103 15.410 1.00 58.34  ? 115 VAL D C   1 
ATOM   6224  O  O   . VAL D  1 124 ? -15.987 -19.818 15.717 1.00 55.90  ? 115 VAL D O   1 
ATOM   6225  C  CB  . VAL D  1 124 ? -14.834 -17.432 17.224 1.00 51.27  ? 115 VAL D CB  1 
ATOM   6226  C  CG1 . VAL D  1 124 ? -13.508 -18.052 17.638 1.00 57.77  ? 115 VAL D CG1 1 
ATOM   6227  C  CG2 . VAL D  1 124 ? -14.892 -15.964 17.578 1.00 52.95  ? 115 VAL D CG2 1 
ATOM   6228  N  N   . GLN D  1 125 ? -13.961 -19.567 14.772 1.00 58.68  ? 116 GLN D N   1 
ATOM   6229  C  CA  . GLN D  1 125 ? -13.771 -20.993 14.521 1.00 58.97  ? 116 GLN D CA  1 
ATOM   6230  C  C   . GLN D  1 125 ? -12.594 -21.511 15.339 1.00 61.80  ? 116 GLN D C   1 
ATOM   6231  O  O   . GLN D  1 125 ? -11.448 -21.126 15.100 1.00 63.17  ? 116 GLN D O   1 
ATOM   6232  C  CB  . GLN D  1 125 ? -13.512 -21.286 13.034 1.00 64.84  ? 116 GLN D CB  1 
ATOM   6233  C  CG  . GLN D  1 125 ? -14.637 -20.921 12.070 1.00 70.77  ? 116 GLN D CG  1 
ATOM   6234  C  CD  . GLN D  1 125 ? -15.913 -21.674 12.346 0.00 68.45  ? 116 GLN D CD  1 
ATOM   6235  O  OE1 . GLN D  1 125 ? -15.951 -22.571 13.187 0.00 67.27  ? 116 GLN D OE1 1 
ATOM   6236  N  NE2 . GLN D  1 125 ? -16.974 -21.315 11.633 0.00 72.13  ? 116 GLN D NE2 1 
ATOM   6237  N  N   . TYR D  1 126 ? -12.883 -22.381 16.303 1.00 56.34  ? 117 TYR D N   1 
ATOM   6238  C  CA  . TYR D  1 126 ? -11.850 -23.078 17.056 1.00 53.40  ? 117 TYR D CA  1 
ATOM   6239  C  C   . TYR D  1 126 ? -11.880 -24.561 16.685 1.00 59.96  ? 117 TYR D C   1 
ATOM   6240  O  O   . TYR D  1 126 ? -12.922 -25.216 16.765 1.00 59.44  ? 117 TYR D O   1 
ATOM   6241  C  CB  . TYR D  1 126 ? -12.072 -22.886 18.551 1.00 54.98  ? 117 TYR D CB  1 
ATOM   6242  C  CG  . TYR D  1 126 ? -10.952 -23.404 19.421 1.00 60.73  ? 117 TYR D CG  1 
ATOM   6243  C  CD1 . TYR D  1 126 ? -9.627  -23.246 19.042 1.00 66.69  ? 117 TYR D CD1 1 
ATOM   6244  C  CD2 . TYR D  1 126 ? -11.216 -24.033 20.632 1.00 53.01  ? 117 TYR D CD2 1 
ATOM   6245  C  CE1 . TYR D  1 126 ? -8.590  -23.712 19.841 1.00 62.49  ? 117 TYR D CE1 1 
ATOM   6246  C  CE2 . TYR D  1 126 ? -10.191 -24.495 21.435 1.00 53.12  ? 117 TYR D CE2 1 
ATOM   6247  C  CZ  . TYR D  1 126 ? -8.875  -24.337 21.036 1.00 56.40  ? 117 TYR D CZ  1 
ATOM   6248  O  OH  . TYR D  1 126 ? -7.834  -24.803 21.823 1.00 53.55  ? 117 TYR D OH  1 
ATOM   6249  N  N   . LEU D  1 127 ? -10.758 -25.074 16.233 1.00 60.14  ? 118 LEU D N   1 
ATOM   6250  C  CA  . LEU D  1 127 ? -10.686 -26.435 15.793 1.00 54.48  ? 118 LEU D CA  1 
ATOM   6251  C  C   . LEU D  1 127 ? -9.465  -27.071 16.371 1.00 55.71  ? 118 LEU D C   1 
ATOM   6252  O  O   . LEU D  1 127 ? -8.465  -27.180 15.708 1.00 59.33  ? 118 LEU D O   1 
ATOM   6253  C  CB  . LEU D  1 127 ? -10.577 -26.436 14.296 1.00 57.79  ? 118 LEU D CB  1 
ATOM   6254  C  CG  . LEU D  1 127 ? -11.638 -27.225 13.581 1.00 64.85  ? 118 LEU D CG  1 
ATOM   6255  C  CD1 . LEU D  1 127 ? -11.506 -27.030 12.124 1.00 65.48  ? 118 LEU D CD1 1 
ATOM   6256  C  CD2 . LEU D  1 127 ? -11.474 -28.639 13.908 1.00 73.58  ? 118 LEU D CD2 1 
ATOM   6257  N  N   . PRO D  1 128 ? -9.566  -27.498 17.607 1.00 56.33  ? 119 PRO D N   1 
ATOM   6258  C  CA  . PRO D  1 128 ? -8.524  -28.250 18.320 1.00 56.29  ? 119 PRO D CA  1 
ATOM   6259  C  C   . PRO D  1 128 ? -8.477  -29.745 18.013 1.00 56.35  ? 119 PRO D C   1 
ATOM   6260  O  O   . PRO D  1 128 ? -9.481  -30.448 18.146 1.00 52.41  ? 119 PRO D O   1 
ATOM   6261  C  CB  . PRO D  1 128 ? -8.924  -28.066 19.781 1.00 50.31  ? 119 PRO D CB  1 
ATOM   6262  C  CG  . PRO D  1 128 ? -10.403 -27.956 19.731 1.00 55.56  ? 119 PRO D CG  1 
ATOM   6263  C  CD  . PRO D  1 128 ? -10.717 -27.200 18.479 1.00 58.39  ? 119 PRO D CD  1 
ATOM   6264  N  N   . ALA D  1 129 ? -7.282  -30.238 17.720 1.00 56.20  ? 120 ALA D N   1 
ATOM   6265  C  CA  . ALA D  1 129 ? -7.072  -31.668 17.551 1.00 58.43  ? 120 ALA D CA  1 
ATOM   6266  C  C   . ALA D  1 129 ? -6.684  -32.260 18.904 1.00 56.72  ? 120 ALA D C   1 
ATOM   6267  O  O   . ALA D  1 129 ? -5.848  -31.698 19.619 1.00 55.64  ? 120 ALA D O   1 
ATOM   6268  C  CB  . ALA D  1 129 ? -5.987  -31.947 16.499 1.00 48.67  ? 120 ALA D CB  1 
ATOM   6269  N  N   . GLN D  1 130 ? -7.286  -33.390 19.258 1.00 54.30  ? 121 GLN D N   1 
ATOM   6270  C  CA  . GLN D  1 130 ? -7.053  -33.946 20.576 1.00 52.01  ? 121 GLN D CA  1 
ATOM   6271  C  C   . GLN D  1 130 ? -7.137  -35.467 20.694 1.00 54.00  ? 121 GLN D C   1 
ATOM   6272  O  O   . GLN D  1 130 ? -7.801  -36.132 19.898 1.00 56.83  ? 121 GLN D O   1 
ATOM   6273  C  CB  . GLN D  1 130 ? -7.983  -33.277 21.587 1.00 55.42  ? 121 GLN D CB  1 
ATOM   6274  C  CG  . GLN D  1 130 ? -9.428  -33.108 21.166 1.00 54.54  ? 121 GLN D CG  1 
ATOM   6275  C  CD  . GLN D  1 130 ? -10.142 -32.185 22.137 1.00 63.18  ? 121 GLN D CD  1 
ATOM   6276  O  OE1 . GLN D  1 130 ? -9.625  -31.118 22.465 1.00 57.84  ? 121 GLN D OE1 1 
ATOM   6277  N  NE2 . GLN D  1 130 ? -11.304 -32.606 22.641 1.00 65.58  ? 121 GLN D NE2 1 
ATOM   6278  N  N   . ARG D  1 131 ? -6.452  -36.003 21.703 1.00 51.65  ? 122 ARG D N   1 
ATOM   6279  C  CA  . ARG D  1 131 ? -6.587  -37.413 22.072 1.00 53.46  ? 122 ARG D CA  1 
ATOM   6280  C  C   . ARG D  1 131 ? -7.349  -37.593 23.372 1.00 48.40  ? 122 ARG D C   1 
ATOM   6281  O  O   . ARG D  1 131 ? -6.892  -37.162 24.421 1.00 57.29  ? 122 ARG D O   1 
ATOM   6282  C  CB  . ARG D  1 131 ? -5.227  -38.090 22.199 1.00 48.19  ? 122 ARG D CB  1 
ATOM   6283  C  CG  . ARG D  1 131 ? -5.354  -39.533 22.560 1.00 46.62  ? 122 ARG D CG  1 
ATOM   6284  C  CD  . ARG D  1 131 ? -4.097  -40.271 22.242 1.00 53.57  ? 122 ARG D CD  1 
ATOM   6285  N  NE  . ARG D  1 131 ? -4.154  -41.652 22.699 1.00 53.08  ? 122 ARG D NE  1 
ATOM   6286  C  CZ  . ARG D  1 131 ? -3.172  -42.521 22.513 1.00 53.63  ? 122 ARG D CZ  1 
ATOM   6287  N  NH1 . ARG D  1 131 ? -2.073  -42.138 21.874 1.00 56.24  ? 122 ARG D NH1 1 
ATOM   6288  N  NH2 . ARG D  1 131 ? -3.293  -43.764 22.950 1.00 51.31  ? 122 ARG D NH2 1 
ATOM   6289  N  N   . LEU D  1 132 ? -8.495  -38.257 23.296 1.00 42.01  ? 123 LEU D N   1 
ATOM   6290  C  CA  . LEU D  1 132 ? -9.338  -38.478 24.454 1.00 49.22  ? 123 LEU D CA  1 
ATOM   6291  C  C   . LEU D  1 132 ? -9.363  -39.935 24.843 1.00 48.65  ? 123 LEU D C   1 
ATOM   6292  O  O   . LEU D  1 132 ? -9.411  -40.790 23.971 1.00 50.93  ? 123 LEU D O   1 
ATOM   6293  C  CB  . LEU D  1 132 ? -10.765 -38.047 24.157 1.00 53.11  ? 123 LEU D CB  1 
ATOM   6294  C  CG  . LEU D  1 132 ? -11.761 -38.260 25.293 1.00 52.83  ? 123 LEU D CG  1 
ATOM   6295  C  CD1 . LEU D  1 132 ? -11.609 -37.163 26.334 1.00 50.10  ? 123 LEU D CD1 1 
ATOM   6296  C  CD2 . LEU D  1 132 ? -13.177 -38.295 24.754 1.00 54.92  ? 123 LEU D CD2 1 
ATOM   6297  N  N   . SER D  1 133 ? -9.316  -40.204 26.152 1.00 52.75  ? 124 SER D N   1 
ATOM   6298  C  CA  . SER D  1 133 ? -9.606  -41.529 26.709 1.00 52.71  ? 124 SER D CA  1 
ATOM   6299  C  C   . SER D  1 133 ? -10.954 -41.455 27.382 1.00 52.83  ? 124 SER D C   1 
ATOM   6300  O  O   . SER D  1 133 ? -11.174 -40.578 28.196 1.00 53.42  ? 124 SER D O   1 
ATOM   6301  C  CB  . SER D  1 133 ? -8.560  -41.941 27.738 1.00 49.85  ? 124 SER D CB  1 
ATOM   6302  O  OG  . SER D  1 133 ? -7.372  -42.359 27.104 1.00 53.54  ? 124 SER D OG  1 
ATOM   6303  N  N   . PHE D  1 134 ? -11.872 -42.345 27.035 1.00 52.54  ? 125 PHE D N   1 
ATOM   6304  C  CA  . PHE D  1 134 ? -13.183 -42.286 27.655 1.00 55.61  ? 125 PHE D CA  1 
ATOM   6305  C  C   . PHE D  1 134 ? -13.665 -43.675 28.033 1.00 58.61  ? 125 PHE D C   1 
ATOM   6306  O  O   . PHE D  1 134 ? -13.134 -44.670 27.543 1.00 56.67  ? 125 PHE D O   1 
ATOM   6307  C  CB  . PHE D  1 134 ? -14.195 -41.570 26.750 1.00 51.24  ? 125 PHE D CB  1 
ATOM   6308  C  CG  . PHE D  1 134 ? -14.411 -42.239 25.420 1.00 60.26  ? 125 PHE D CG  1 
ATOM   6309  C  CD1 . PHE D  1 134 ? -15.507 -43.069 25.217 1.00 61.38  ? 125 PHE D CD1 1 
ATOM   6310  C  CD2 . PHE D  1 134 ? -13.524 -42.035 24.366 1.00 57.83  ? 125 PHE D CD2 1 
ATOM   6311  C  CE1 . PHE D  1 134 ? -15.709 -43.677 23.992 1.00 63.72  ? 125 PHE D CE1 1 
ATOM   6312  C  CE2 . PHE D  1 134 ? -13.721 -42.642 23.144 1.00 51.96  ? 125 PHE D CE2 1 
ATOM   6313  C  CZ  . PHE D  1 134 ? -14.810 -43.462 22.957 1.00 58.18  ? 125 PHE D CZ  1 
ATOM   6314  N  N   . MET D  1 135 ? -14.716 -43.747 28.849 1.00 56.19  ? 126 MET D N   1 
ATOM   6315  C  CA  . MET D  1 135 ? -15.136 -45.040 29.359 1.00 52.74  ? 126 MET D CA  1 
ATOM   6316  C  C   . MET D  1 135 ? -15.889 -45.738 28.253 1.00 53.96  ? 126 MET D C   1 
ATOM   6317  O  O   . MET D  1 135 ? -16.961 -45.305 27.856 1.00 64.51  ? 126 MET D O   1 
ATOM   6318  C  CB  . MET D  1 135 ? -16.101 -44.832 30.500 1.00 51.95  ? 126 MET D CB  1 
ATOM   6319  C  CG  . MET D  1 135 ? -15.627 -43.882 31.564 1.00 57.05  ? 126 MET D CG  1 
ATOM   6320  S  SD  . MET D  1 135 ? -16.972 -43.292 32.572 1.00 58.97  ? 126 MET D SD  1 
ATOM   6321  C  CE  . MET D  1 135 ? -16.092 -42.088 33.557 1.00 59.94  ? 126 MET D CE  1 
ATOM   6322  N  N   . CYS D  1 136 ? -15.336 -46.850 27.790 1.00 61.38  ? 127 CYS D N   1 
ATOM   6323  C  CA  . CYS D  1 136 ? -15.934 -47.642 26.715 1.00 67.21  ? 127 CYS D CA  1 
ATOM   6324  C  C   . CYS D  1 136 ? -15.694 -49.118 26.986 1.00 59.57  ? 127 CYS D C   1 
ATOM   6325  O  O   . CYS D  1 136 ? -14.571 -49.518 27.273 1.00 61.81  ? 127 CYS D O   1 
ATOM   6326  C  CB  . CYS D  1 136 ? -15.329 -47.235 25.357 1.00 64.35  ? 127 CYS D CB  1 
ATOM   6327  S  SG  . CYS D  1 136 ? -15.491 -48.391 23.942 1.00 70.35  ? 127 CYS D SG  1 
ATOM   6328  N  N   . ASP D  1 137 ? -16.743 -49.921 26.884 1.00 56.37  ? 128 ASP D N   1 
ATOM   6329  C  CA  . ASP D  1 137 ? -16.583 -51.363 26.935 1.00 66.92  ? 128 ASP D CA  1 
ATOM   6330  C  C   . ASP D  1 137 ? -16.604 -51.953 25.518 1.00 64.78  ? 128 ASP D C   1 
ATOM   6331  O  O   . ASP D  1 137 ? -17.654 -52.039 24.903 1.00 61.00  ? 128 ASP D O   1 
ATOM   6332  C  CB  . ASP D  1 137 ? -17.714 -51.948 27.768 1.00 64.95  ? 128 ASP D CB  1 
ATOM   6333  C  CG  . ASP D  1 137 ? -17.810 -53.453 27.647 1.00 70.50  ? 128 ASP D CG  1 
ATOM   6334  O  OD1 . ASP D  1 137 ? -16.774 -54.113 27.425 1.00 67.52  ? 128 ASP D OD1 1 
ATOM   6335  O  OD2 . ASP D  1 137 ? -18.925 -53.983 27.795 1.00 77.61  ? 128 ASP D OD2 1 
ATOM   6336  N  N   . PRO D  1 138 ? -15.477 -52.389 25.003 1.00 62.25  ? 129 PRO D N   1 
ATOM   6337  C  CA  . PRO D  1 138 ? -15.470 -52.902 23.644 1.00 65.56  ? 129 PRO D CA  1 
ATOM   6338  C  C   . PRO D  1 138 ? -15.959 -54.306 23.314 1.00 72.18  ? 129 PRO D C   1 
ATOM   6339  O  O   . PRO D  1 138 ? -15.486 -54.869 22.356 1.00 71.58  ? 129 PRO D O   1 
ATOM   6340  C  CB  . PRO D  1 138 ? -14.048 -52.621 23.210 1.00 65.63  ? 129 PRO D CB  1 
ATOM   6341  C  CG  . PRO D  1 138 ? -13.287 -52.678 24.424 1.00 63.99  ? 129 PRO D CG  1 
ATOM   6342  C  CD  . PRO D  1 138 ? -14.121 -52.178 25.510 1.00 63.36  ? 129 PRO D CD  1 
ATOM   6343  N  N   . THR D  1 139 ? -16.725 -54.962 24.125 1.00 73.92  ? 130 THR D N   1 
ATOM   6344  C  CA  . THR D  1 139 ? -17.174 -56.296 23.791 1.00 77.35  ? 130 THR D CA  1 
ATOM   6345  C  C   . THR D  1 139 ? -17.711 -56.531 22.405 1.00 82.24  ? 130 THR D C   1 
ATOM   6346  O  O   . THR D  1 139 ? -18.609 -55.846 21.975 1.00 82.32  ? 130 THR D O   1 
ATOM   6347  C  CB  . THR D  1 139 ? -18.194 -56.768 24.797 1.00 86.75  ? 130 THR D CB  1 
ATOM   6348  O  OG1 . THR D  1 139 ? -17.536 -57.073 26.023 1.00 79.08  ? 130 THR D OG1 1 
ATOM   6349  C  CG2 . THR D  1 139 ? -18.856 -57.993 24.310 1.00 77.91  ? 130 THR D CG2 1 
ATOM   6350  N  N   . GLY D  1 140 ? -17.167 -57.505 21.700 1.00 73.11  ? 131 GLY D N   1 
ATOM   6351  C  CA  . GLY D  1 140 ? -17.594 -57.761 20.335 1.00 79.68  ? 131 GLY D CA  1 
ATOM   6352  C  C   . GLY D  1 140 ? -16.883 -56.913 19.287 1.00 78.93  ? 131 GLY D C   1 
ATOM   6353  O  O   . GLY D  1 140 ? -17.339 -56.789 18.155 1.00 79.01  ? 131 GLY D O   1 
ATOM   6354  N  N   . VAL D  1 141 ? -15.758 -56.321 19.662 1.00 81.87  ? 132 VAL D N   1 
ATOM   6355  C  CA  . VAL D  1 141 ? -14.978 -55.532 18.722 1.00 78.57  ? 132 VAL D CA  1 
ATOM   6356  C  C   . VAL D  1 141 ? -14.382 -56.493 17.711 1.00 71.97  ? 132 VAL D C   1 
ATOM   6357  O  O   . VAL D  1 141 ? -14.056 -56.122 16.592 1.00 67.51  ? 132 VAL D O   1 
ATOM   6358  C  CB  . VAL D  1 141 ? -13.855 -54.722 19.443 1.00 76.74  ? 132 VAL D CB  1 
ATOM   6359  C  CG1 . VAL D  1 141 ? -12.846 -55.648 20.120 1.00 67.71  ? 132 VAL D CG1 1 
ATOM   6360  C  CG2 . VAL D  1 141 ? -13.152 -53.792 18.467 1.00 74.70  ? 132 VAL D CG2 1 
ATOM   6361  N  N   . ASP D  1 142 ? -14.238 -57.742 18.133 1.00 76.50  ? 133 ASP D N   1 
ATOM   6362  C  CA  . ASP D  1 142 ? -13.646 -58.777 17.305 1.00 78.12  ? 133 ASP D CA  1 
ATOM   6363  C  C   . ASP D  1 142 ? -14.689 -59.553 16.487 1.00 90.69  ? 133 ASP D C   1 
ATOM   6364  O  O   . ASP D  1 142 ? -14.321 -60.373 15.640 1.00 102.43 ? 133 ASP D O   1 
ATOM   6365  C  CB  . ASP D  1 142 ? -12.796 -59.723 18.160 1.00 80.84  ? 133 ASP D CB  1 
ATOM   6366  C  CG  . ASP D  1 142 ? -13.578 -60.331 19.317 1.00 85.40  ? 133 ASP D CG  1 
ATOM   6367  O  OD1 . ASP D  1 142 ? -14.500 -59.660 19.834 1.00 71.18  ? 133 ASP D OD1 1 
ATOM   6368  O  OD2 . ASP D  1 142 ? -13.272 -61.482 19.708 1.00 86.75  ? 133 ASP D OD2 1 
ATOM   6369  N  N   . SER D  1 143 ? -15.979 -59.303 16.732 1.00 88.20  ? 134 SER D N   1 
ATOM   6370  C  CA  . SER D  1 143 ? -17.043 -59.890 15.907 1.00 82.62  ? 134 SER D CA  1 
ATOM   6371  C  C   . SER D  1 143 ? -17.301 -59.025 14.668 1.00 80.94  ? 134 SER D C   1 
ATOM   6372  O  O   . SER D  1 143 ? -16.623 -58.020 14.458 1.00 86.84  ? 134 SER D O   1 
ATOM   6373  C  CB  . SER D  1 143 ? -18.328 -60.104 16.719 1.00 79.36  ? 134 SER D CB  1 
ATOM   6374  O  OG  . SER D  1 143 ? -19.107 -58.929 16.801 1.00 84.13  ? 134 SER D OG  1 
ATOM   6375  N  N   . GLU D  1 144 ? -18.239 -59.424 13.817 1.00 87.97  ? 135 GLU D N   1 
ATOM   6376  C  CA  . GLU D  1 144 ? -18.592 -58.562 12.686 1.00 96.84  ? 135 GLU D CA  1 
ATOM   6377  C  C   . GLU D  1 144 ? -19.557 -57.444 13.079 1.00 90.68  ? 135 GLU D C   1 
ATOM   6378  O  O   . GLU D  1 144 ? -19.420 -56.305 12.624 1.00 82.27  ? 135 GLU D O   1 
ATOM   6379  C  CB  . GLU D  1 144 ? -19.098 -59.364 11.479 1.00 94.67  ? 135 GLU D CB  1 
ATOM   6380  C  CG  . GLU D  1 144 ? -18.006 -59.616 10.454 1.00 92.26  ? 135 GLU D CG  1 
ATOM   6381  C  CD  . GLU D  1 144 ? -18.467 -60.477 9.303  1.00 109.75 ? 135 GLU D CD  1 
ATOM   6382  O  OE1 . GLU D  1 144 ? -18.990 -61.588 9.555  1.00 119.33 ? 135 GLU D OE1 1 
ATOM   6383  O  OE2 . GLU D  1 144 ? -18.299 -60.042 8.144  1.00 105.25 ? 135 GLU D OE2 1 
ATOM   6384  N  N   . GLU D  1 145 ? -20.517 -57.772 13.939 1.00 89.95  ? 136 GLU D N   1 
ATOM   6385  C  CA  A GLU D  1 145 ? -21.479 -56.797 14.435 0.40 93.42  ? 136 GLU D CA  1 
ATOM   6386  C  CA  B GLU D  1 145 ? -21.475 -56.780 14.406 0.60 93.42  ? 136 GLU D CA  1 
ATOM   6387  C  C   . GLU D  1 145 ? -20.762 -55.591 15.048 1.00 91.26  ? 136 GLU D C   1 
ATOM   6388  O  O   . GLU D  1 145 ? -21.261 -54.464 15.003 1.00 85.94  ? 136 GLU D O   1 
ATOM   6389  C  CB  A GLU D  1 145 ? -22.392 -57.461 15.465 0.40 94.75  ? 136 GLU D CB  1 
ATOM   6390  C  CB  B GLU D  1 145 ? -22.484 -57.392 15.379 0.60 94.75  ? 136 GLU D CB  1 
ATOM   6391  C  CG  A GLU D  1 145 ? -22.534 -58.964 15.257 0.40 95.54  ? 136 GLU D CG  1 
ATOM   6392  C  CG  B GLU D  1 145 ? -23.540 -56.399 15.840 0.60 94.08  ? 136 GLU D CG  1 
ATOM   6393  C  CD  A GLU D  1 145 ? -23.554 -59.596 16.182 0.40 100.02 ? 136 GLU D CD  1 
ATOM   6394  C  CD  B GLU D  1 145 ? -24.554 -57.008 16.782 0.60 102.93 ? 136 GLU D CD  1 
ATOM   6395  O  OE1 A GLU D  1 145 ? -24.748 -59.620 15.819 0.40 97.73  ? 136 GLU D OE1 1 
ATOM   6396  O  OE1 B GLU D  1 145 ? -24.424 -58.211 17.104 0.60 109.78 ? 136 GLU D OE1 1 
ATOM   6397  O  OE2 A GLU D  1 145 ? -23.163 -60.074 17.267 0.40 97.58  ? 136 GLU D OE2 1 
ATOM   6398  O  OE2 B GLU D  1 145 ? -25.483 -56.279 17.197 0.60 95.45  ? 136 GLU D OE2 1 
ATOM   6399  N  N   . GLY D  1 146 ? -19.590 -55.843 15.628 1.00 83.52  ? 137 GLY D N   1 
ATOM   6400  C  CA  . GLY D  1 146 ? -18.770 -54.792 16.205 1.00 82.30  ? 137 GLY D CA  1 
ATOM   6401  C  C   . GLY D  1 146 ? -19.189 -54.333 17.594 1.00 88.68  ? 137 GLY D C   1 
ATOM   6402  O  O   . GLY D  1 146 ? -20.117 -54.875 18.191 1.00 96.32  ? 137 GLY D O   1 
ATOM   6403  N  N   . ALA D  1 147 ? -18.516 -53.308 18.104 1.00 73.52  ? 138 ALA D N   1 
ATOM   6404  C  CA  . ALA D  1 147 ? -18.787 -52.807 19.442 1.00 74.62  ? 138 ALA D CA  1 
ATOM   6405  C  C   . ALA D  1 147 ? -19.259 -51.368 19.325 1.00 74.07  ? 138 ALA D C   1 
ATOM   6406  O  O   . ALA D  1 147 ? -19.065 -50.742 18.282 1.00 74.28  ? 138 ALA D O   1 
ATOM   6407  C  CB  . ALA D  1 147 ? -17.543 -52.892 20.296 1.00 75.79  ? 138 ALA D CB  1 
ATOM   6408  N  N   . THR D  1 148 ? -19.922 -50.858 20.360 1.00 65.01  ? 139 THR D N   1 
ATOM   6409  C  CA  . THR D  1 148 ? -20.408 -49.480 20.326 1.00 67.62  ? 139 THR D CA  1 
ATOM   6410  C  C   . THR D  1 148 ? -20.158 -48.731 21.613 1.00 66.50  ? 139 THR D C   1 
ATOM   6411  O  O   . THR D  1 148 ? -20.484 -49.215 22.696 1.00 71.63  ? 139 THR D O   1 
ATOM   6412  C  CB  . THR D  1 148 ? -21.916 -49.410 20.073 1.00 72.10  ? 139 THR D CB  1 
ATOM   6413  O  OG1 . THR D  1 148 ? -22.262 -50.274 18.987 1.00 73.51  ? 139 THR D OG1 1 
ATOM   6414  C  CG2 . THR D  1 148 ? -22.326 -47.975 19.745 1.00 73.67  ? 139 THR D CG2 1 
ATOM   6415  N  N   . CYS D  1 149 ? -19.606 -47.532 21.490 1.00 67.19  ? 140 CYS D N   1 
ATOM   6416  C  CA  . CYS D  1 149 ? -19.378 -46.679 22.651 1.00 74.98  ? 140 CYS D CA  1 
ATOM   6417  C  C   . CYS D  1 149 ? -19.880 -45.258 22.461 1.00 72.30  ? 140 CYS D C   1 
ATOM   6418  O  O   . CYS D  1 149 ? -19.742 -44.684 21.388 1.00 79.63  ? 140 CYS D O   1 
ATOM   6419  C  CB  . CYS D  1 149 ? -17.902 -46.672 23.023 1.00 74.82  ? 140 CYS D CB  1 
ATOM   6420  S  SG  . CYS D  1 149 ? -17.487 -48.106 23.995 1.00 84.40  ? 140 CYS D SG  1 
ATOM   6421  N  N   . ALA D  1 150 ? -20.469 -44.693 23.505 1.00 66.28  ? 141 ALA D N   1 
ATOM   6422  C  CA  . ALA D  1 150 ? -20.973 -43.332 23.428 1.00 67.75  ? 141 ALA D CA  1 
ATOM   6423  C  C   . ALA D  1 150 ? -20.199 -42.419 24.366 1.00 67.83  ? 141 ALA D C   1 
ATOM   6424  O  O   . ALA D  1 150 ? -19.740 -42.840 25.439 1.00 72.66  ? 141 ALA D O   1 
ATOM   6425  C  CB  . ALA D  1 150 ? -22.470 -43.284 23.739 1.00 67.50  ? 141 ALA D CB  1 
ATOM   6426  N  N   . VAL D  1 151 ? -20.047 -41.168 23.935 1.00 68.43  ? 142 VAL D N   1 
ATOM   6427  C  CA  . VAL D  1 151 ? -19.428 -40.125 24.741 1.00 60.20  ? 142 VAL D CA  1 
ATOM   6428  C  C   . VAL D  1 151 ? -20.191 -38.829 24.536 1.00 57.27  ? 142 VAL D C   1 
ATOM   6429  O  O   . VAL D  1 151 ? -20.473 -38.447 23.411 1.00 59.46  ? 142 VAL D O   1 
ATOM   6430  C  CB  . VAL D  1 151 ? -17.933 -39.952 24.386 1.00 56.73  ? 142 VAL D CB  1 
ATOM   6431  C  CG1 . VAL D  1 151 ? -17.768 -39.473 22.970 1.00 59.59  ? 142 VAL D CG1 1 
ATOM   6432  C  CG2 . VAL D  1 151 ? -17.243 -39.022 25.366 1.00 55.62  ? 142 VAL D CG2 1 
ATOM   6433  N  N   . LYS D  1 152 ? -20.540 -38.162 25.631 1.00 60.12  ? 143 LYS D N   1 
ATOM   6434  C  CA  . LYS D  1 152 ? -21.269 -36.904 25.554 1.00 59.62  ? 143 LYS D CA  1 
ATOM   6435  C  C   . LYS D  1 152 ? -20.378 -35.695 25.793 1.00 59.18  ? 143 LYS D C   1 
ATOM   6436  O  O   . LYS D  1 152 ? -19.442 -35.745 26.583 1.00 56.43  ? 143 LYS D O   1 
ATOM   6437  C  CB  . LYS D  1 152 ? -22.441 -36.897 26.522 1.00 65.38  ? 143 LYS D CB  1 
ATOM   6438  C  CG  . LYS D  1 152 ? -23.433 -37.995 26.254 1.00 73.78  ? 143 LYS D CG  1 
ATOM   6439  C  CD  . LYS D  1 152 ? -24.779 -37.675 26.860 1.00 79.31  ? 143 LYS D CD  1 
ATOM   6440  C  CE  . LYS D  1 152 ? -25.537 -38.949 27.121 1.00 80.99  ? 143 LYS D CE  1 
ATOM   6441  N  NZ  . LYS D  1 152 ? -24.907 -40.079 26.375 1.00 80.69  ? 143 LYS D NZ  1 
ATOM   6442  N  N   . PHE D  1 153 ? -20.675 -34.616 25.077 1.00 58.84  ? 144 PHE D N   1 
ATOM   6443  C  CA  . PHE D  1 153 ? -19.937 -33.369 25.187 1.00 55.47  ? 144 PHE D CA  1 
ATOM   6444  C  C   . PHE D  1 153 ? -20.907 -32.227 25.508 1.00 58.65  ? 144 PHE D C   1 
ATOM   6445  O  O   . PHE D  1 153 ? -22.069 -32.253 25.111 1.00 62.92  ? 144 PHE D O   1 
ATOM   6446  C  CB  . PHE D  1 153 ? -19.218 -33.056 23.876 1.00 54.13  ? 144 PHE D CB  1 
ATOM   6447  C  CG  . PHE D  1 153 ? -18.054 -33.944 23.576 1.00 51.49  ? 144 PHE D CG  1 
ATOM   6448  C  CD1 . PHE D  1 153 ? -16.773 -33.559 23.914 1.00 53.24  ? 144 PHE D CD1 1 
ATOM   6449  C  CD2 . PHE D  1 153 ? -18.232 -35.140 22.910 1.00 57.48  ? 144 PHE D CD2 1 
ATOM   6450  C  CE1 . PHE D  1 153 ? -15.692 -34.359 23.623 1.00 57.75  ? 144 PHE D CE1 1 
ATOM   6451  C  CE2 . PHE D  1 153 ? -17.157 -35.946 22.612 1.00 57.36  ? 144 PHE D CE2 1 
ATOM   6452  C  CZ  . PHE D  1 153 ? -15.885 -35.558 22.969 1.00 60.29  ? 144 PHE D CZ  1 
ATOM   6453  N  N   . GLY D  1 154 ? -20.426 -31.215 26.218 1.00 58.15  ? 145 GLY D N   1 
ATOM   6454  C  CA  . GLY D  1 154 ? -21.255 -30.070 26.532 1.00 56.73  ? 145 GLY D CA  1 
ATOM   6455  C  C   . GLY D  1 154 ? -20.544 -29.141 27.480 1.00 56.30  ? 145 GLY D C   1 
ATOM   6456  O  O   . GLY D  1 154 ? -19.444 -29.431 27.946 1.00 54.33  ? 145 GLY D O   1 
ATOM   6457  N  N   . SER D  1 155 ? -21.173 -28.011 27.757 1.00 54.85  ? 146 SER D N   1 
ATOM   6458  C  CA  . SER D  1 155 ? -20.630 -27.059 28.715 1.00 59.73  ? 146 SER D CA  1 
ATOM   6459  C  C   . SER D  1 155 ? -20.577 -27.715 30.075 1.00 59.36  ? 146 SER D C   1 
ATOM   6460  O  O   . SER D  1 155 ? -21.508 -28.423 30.453 1.00 63.89  ? 146 SER D O   1 
ATOM   6461  C  CB  . SER D  1 155 ? -21.515 -25.810 28.782 1.00 60.39  ? 146 SER D CB  1 
ATOM   6462  O  OG  . SER D  1 155 ? -21.054 -24.908 29.767 1.00 59.23  ? 146 SER D OG  1 
ATOM   6463  N  N   . TRP D  1 156 ? -19.488 -27.504 30.805 1.00 62.08  ? 147 TRP D N   1 
ATOM   6464  C  CA  . TRP D  1 156 ? -19.416 -27.993 32.179 1.00 69.01  ? 147 TRP D CA  1 
ATOM   6465  C  C   . TRP D  1 156 ? -20.210 -27.076 33.101 1.00 63.46  ? 147 TRP D C   1 
ATOM   6466  O  O   . TRP D  1 156 ? -20.994 -27.534 33.915 1.00 65.73  ? 147 TRP D O   1 
ATOM   6467  C  CB  . TRP D  1 156 ? -17.960 -28.133 32.654 1.00 65.32  ? 147 TRP D CB  1 
ATOM   6468  C  CG  . TRP D  1 156 ? -17.811 -28.923 33.926 1.00 61.33  ? 147 TRP D CG  1 
ATOM   6469  C  CD1 . TRP D  1 156 ? -17.476 -28.438 35.150 1.00 65.81  ? 147 TRP D CD1 1 
ATOM   6470  C  CD2 . TRP D  1 156 ? -18.006 -30.335 34.096 1.00 63.97  ? 147 TRP D CD2 1 
ATOM   6471  N  NE1 . TRP D  1 156 ? -17.445 -29.455 36.075 1.00 62.44  ? 147 TRP D NE1 1 
ATOM   6472  C  CE2 . TRP D  1 156 ? -17.766 -30.628 35.453 1.00 63.90  ? 147 TRP D CE2 1 
ATOM   6473  C  CE3 . TRP D  1 156 ? -18.364 -31.374 33.236 1.00 66.36  ? 147 TRP D CE3 1 
ATOM   6474  C  CZ2 . TRP D  1 156 ? -17.871 -31.919 35.966 1.00 62.17  ? 147 TRP D CZ2 1 
ATOM   6475  C  CZ3 . TRP D  1 156 ? -18.467 -32.652 33.748 1.00 67.56  ? 147 TRP D CZ3 1 
ATOM   6476  C  CH2 . TRP D  1 156 ? -18.221 -32.914 35.101 1.00 66.87  ? 147 TRP D CH2 1 
ATOM   6477  N  N   . SER D  1 157 ? -19.996 -25.775 32.969 1.00 65.11  ? 148 SER D N   1 
ATOM   6478  C  CA  . SER D  1 157 ? -20.599 -24.827 33.897 1.00 65.96  ? 148 SER D CA  1 
ATOM   6479  C  C   . SER D  1 157 ? -21.871 -24.100 33.479 1.00 64.76  ? 148 SER D C   1 
ATOM   6480  O  O   . SER D  1 157 ? -22.415 -23.347 34.280 1.00 63.62  ? 148 SER D O   1 
ATOM   6481  C  CB  . SER D  1 157 ? -19.548 -23.834 34.394 1.00 66.83  ? 148 SER D CB  1 
ATOM   6482  O  OG  . SER D  1 157 ? -18.593 -24.518 35.196 1.00 70.18  ? 148 SER D OG  1 
ATOM   6483  N  N   . TYR D  1 158 ? -22.355 -24.325 32.257 1.00 65.32  ? 149 TYR D N   1 
ATOM   6484  C  CA  . TYR D  1 158 ? -23.454 -23.517 31.705 1.00 59.05  ? 149 TYR D CA  1 
ATOM   6485  C  C   . TYR D  1 158 ? -24.632 -24.320 31.191 1.00 65.10  ? 149 TYR D C   1 
ATOM   6486  O  O   . TYR D  1 158 ? -24.465 -25.328 30.508 1.00 70.48  ? 149 TYR D O   1 
ATOM   6487  C  CB  . TYR D  1 158 ? -22.975 -22.682 30.540 1.00 57.63  ? 149 TYR D CB  1 
ATOM   6488  C  CG  . TYR D  1 158 ? -22.068 -21.535 30.861 1.00 63.01  ? 149 TYR D CG  1 
ATOM   6489  C  CD1 . TYR D  1 158 ? -22.567 -20.366 31.403 1.00 66.66  ? 149 TYR D CD1 1 
ATOM   6490  C  CD2 . TYR D  1 158 ? -20.715 -21.597 30.561 1.00 65.26  ? 149 TYR D CD2 1 
ATOM   6491  C  CE1 . TYR D  1 158 ? -21.737 -19.298 31.661 1.00 75.05  ? 149 TYR D CE1 1 
ATOM   6492  C  CE2 . TYR D  1 158 ? -19.877 -20.542 30.811 1.00 64.77  ? 149 TYR D CE2 1 
ATOM   6493  C  CZ  . TYR D  1 158 ? -20.387 -19.391 31.362 1.00 71.39  ? 149 TYR D CZ  1 
ATOM   6494  O  OH  . TYR D  1 158 ? -19.555 -18.319 31.614 1.00 68.40  ? 149 TYR D OH  1 
ATOM   6495  N  N   . GLY D  1 159 ? -25.830 -23.839 31.479 1.00 63.86  ? 150 GLY D N   1 
ATOM   6496  C  CA  . GLY D  1 159 ? -27.027 -24.506 31.018 1.00 72.37  ? 150 GLY D CA  1 
ATOM   6497  C  C   . GLY D  1 159 ? -27.507 -23.942 29.699 1.00 68.80  ? 150 GLY D C   1 
ATOM   6498  O  O   . GLY D  1 159 ? -26.920 -23.002 29.178 1.00 64.52  ? 150 GLY D O   1 
ATOM   6499  N  N   . GLY D  1 160 ? -28.592 -24.510 29.180 1.00 71.62  ? 151 GLY D N   1 
ATOM   6500  C  CA  . GLY D  1 160 ? -29.141 -24.129 27.889 1.00 70.94  ? 151 GLY D CA  1 
ATOM   6501  C  C   . GLY D  1 160 ? -29.517 -22.665 27.728 1.00 76.72  ? 151 GLY D C   1 
ATOM   6502  O  O   . GLY D  1 160 ? -29.493 -22.141 26.611 1.00 64.39  ? 151 GLY D O   1 
ATOM   6503  N  N   . TRP D  1 161 ? -29.861 -22.000 28.832 1.00 79.93  ? 152 TRP D N   1 
ATOM   6504  C  CA  . TRP D  1 161 ? -30.289 -20.597 28.770 1.00 80.64  ? 152 TRP D CA  1 
ATOM   6505  C  C   . TRP D  1 161 ? -29.121 -19.619 28.673 1.00 78.56  ? 152 TRP D C   1 
ATOM   6506  O  O   . TRP D  1 161 ? -29.313 -18.424 28.450 1.00 79.53  ? 152 TRP D O   1 
ATOM   6507  C  CB  . TRP D  1 161 ? -31.191 -20.240 29.950 1.00 82.97  ? 152 TRP D CB  1 
ATOM   6508  C  CG  . TRP D  1 161 ? -32.561 -20.813 29.827 1.00 83.63  ? 152 TRP D CG  1 
ATOM   6509  C  CD1 . TRP D  1 161 ? -33.168 -21.241 28.686 1.00 78.75  ? 152 TRP D CD1 1 
ATOM   6510  C  CD2 . TRP D  1 161 ? -33.495 -21.033 30.885 1.00 86.88  ? 152 TRP D CD2 1 
ATOM   6511  N  NE1 . TRP D  1 161 ? -34.426 -21.710 28.964 1.00 82.32  ? 152 TRP D NE1 1 
ATOM   6512  C  CE2 . TRP D  1 161 ? -34.653 -21.596 30.308 1.00 83.46  ? 152 TRP D CE2 1 
ATOM   6513  C  CE3 . TRP D  1 161 ? -33.465 -20.810 32.265 1.00 85.59  ? 152 TRP D CE3 1 
ATOM   6514  C  CZ2 . TRP D  1 161 ? -35.771 -21.934 31.059 1.00 83.43  ? 152 TRP D CZ2 1 
ATOM   6515  C  CZ3 . TRP D  1 161 ? -34.573 -21.150 33.014 1.00 88.71  ? 152 TRP D CZ3 1 
ATOM   6516  C  CH2 . TRP D  1 161 ? -35.713 -21.706 32.409 1.00 98.01  ? 152 TRP D CH2 1 
ATOM   6517  N  N   . GLU D  1 162 ? -27.913 -20.145 28.838 1.00 75.13  ? 153 GLU D N   1 
ATOM   6518  C  CA  . GLU D  1 162 ? -26.684 -19.374 28.680 1.00 69.71  ? 153 GLU D CA  1 
ATOM   6519  C  C   . GLU D  1 162 ? -25.909 -19.831 27.441 1.00 67.54  ? 153 GLU D C   1 
ATOM   6520  O  O   . GLU D  1 162 ? -25.604 -19.027 26.564 1.00 67.57  ? 153 GLU D O   1 
ATOM   6521  C  CB  . GLU D  1 162 ? -25.832 -19.413 29.942 1.00 74.20  ? 153 GLU D CB  1 
ATOM   6522  C  CG  . GLU D  1 162 ? -26.529 -18.853 31.173 1.00 78.29  ? 153 GLU D CG  1 
ATOM   6523  C  CD  . GLU D  1 162 ? -27.059 -19.940 32.094 1.00 87.01  ? 153 GLU D CD  1 
ATOM   6524  O  OE1 . GLU D  1 162 ? -26.708 -21.125 31.887 1.00 88.01  ? 153 GLU D OE1 1 
ATOM   6525  O  OE2 . GLU D  1 162 ? -27.823 -19.613 33.031 1.00 93.23  ? 153 GLU D OE2 1 
ATOM   6526  N  N   . ILE D  1 163 ? -25.515 -21.101 27.414 1.00 70.44  ? 154 ILE D N   1 
ATOM   6527  C  CA  . ILE D  1 163 ? -24.971 -21.712 26.200 1.00 66.68  ? 154 ILE D CA  1 
ATOM   6528  C  C   . ILE D  1 163 ? -25.942 -22.703 25.571 1.00 64.33  ? 154 ILE D C   1 
ATOM   6529  O  O   . ILE D  1 163 ? -26.587 -23.477 26.257 1.00 64.38  ? 154 ILE D O   1 
ATOM   6530  C  CB  . ILE D  1 163 ? -23.665 -22.455 26.475 1.00 62.89  ? 154 ILE D CB  1 
ATOM   6531  C  CG1 . ILE D  1 163 ? -22.580 -21.473 26.912 1.00 64.10  ? 154 ILE D CG1 1 
ATOM   6532  C  CG2 . ILE D  1 163 ? -23.227 -23.222 25.244 1.00 59.52  ? 154 ILE D CG2 1 
ATOM   6533  C  CD1 . ILE D  1 163 ? -21.332 -22.130 27.443 1.00 58.89  ? 154 ILE D CD1 1 
ATOM   6534  N  N   . ASP D  1 164 ? -26.031 -22.682 24.250 1.00 72.02  ? 155 ASP D N   1 
ATOM   6535  C  CA  . ASP D  1 164 ? -26.870 -23.629 23.525 1.00 74.00  ? 155 ASP D CA  1 
ATOM   6536  C  C   . ASP D  1 164 ? -26.044 -24.430 22.529 1.00 73.02  ? 155 ASP D C   1 
ATOM   6537  O  O   . ASP D  1 164 ? -25.395 -23.864 21.652 1.00 72.82  ? 155 ASP D O   1 
ATOM   6538  C  CB  . ASP D  1 164 ? -28.003 -22.904 22.789 1.00 76.38  ? 155 ASP D CB  1 
ATOM   6539  C  CG  . ASP D  1 164 ? -29.075 -23.859 22.280 1.00 85.89  ? 155 ASP D CG  1 
ATOM   6540  O  OD1 . ASP D  1 164 ? -29.281 -24.926 22.903 1.00 82.85  ? 155 ASP D OD1 1 
ATOM   6541  O  OD2 . ASP D  1 164 ? -29.713 -23.541 21.254 1.00 90.48  ? 155 ASP D OD2 1 
ATOM   6542  N  N   . LEU D  1 165 ? -26.073 -25.750 22.670 1.00 70.81  ? 156 LEU D N   1 
ATOM   6543  C  CA  . LEU D  1 165 ? -25.392 -26.629 21.739 1.00 64.52  ? 156 LEU D CA  1 
ATOM   6544  C  C   . LEU D  1 165 ? -26.284 -26.928 20.564 1.00 72.79  ? 156 LEU D C   1 
ATOM   6545  O  O   . LEU D  1 165 ? -27.480 -27.154 20.736 1.00 76.16  ? 156 LEU D O   1 
ATOM   6546  C  CB  . LEU D  1 165 ? -25.047 -27.947 22.409 1.00 69.30  ? 156 LEU D CB  1 
ATOM   6547  C  CG  . LEU D  1 165 ? -23.909 -27.900 23.408 1.00 71.63  ? 156 LEU D CG  1 
ATOM   6548  C  CD1 . LEU D  1 165 ? -23.736 -29.272 24.018 1.00 76.29  ? 156 LEU D CD1 1 
ATOM   6549  C  CD2 . LEU D  1 165 ? -22.642 -27.448 22.723 1.00 65.42  ? 156 LEU D CD2 1 
ATOM   6550  N  N   . LYS D  1 166 ? -25.685 -26.922 19.374 1.00 79.33  ? 157 LYS D N   1 
ATOM   6551  C  CA  . LYS D  1 166 ? -26.312 -27.385 18.139 1.00 67.46  ? 157 LYS D CA  1 
ATOM   6552  C  C   . LYS D  1 166 ? -25.255 -28.088 17.300 1.00 68.76  ? 157 LYS D C   1 
ATOM   6553  O  O   . LYS D  1 166 ? -24.080 -27.741 17.344 1.00 64.51  ? 157 LYS D O   1 
ATOM   6554  C  CB  . LYS D  1 166 ? -26.909 -26.222 17.346 1.00 64.95  ? 157 LYS D CB  1 
ATOM   6555  C  CG  . LYS D  1 166 ? -28.144 -25.602 17.964 1.00 72.44  ? 157 LYS D CG  1 
ATOM   6556  C  CD  . LYS D  1 166 ? -28.679 -24.465 17.113 1.00 75.13  ? 157 LYS D CD  1 
ATOM   6557  C  CE  . LYS D  1 166 ? -29.859 -23.789 17.786 1.00 85.02  ? 157 LYS D CE  1 
ATOM   6558  N  NZ  . LYS D  1 166 ? -30.913 -24.790 18.124 1.00 93.99  ? 157 LYS D NZ  1 
ATOM   6559  N  N   . THR D  1 167 ? -25.687 -29.091 16.549 1.00 83.24  ? 158 THR D N   1 
ATOM   6560  C  CA  . THR D  1 167 ? -24.866 -29.746 15.540 1.00 75.65  ? 158 THR D CA  1 
ATOM   6561  C  C   . THR D  1 167 ? -25.355 -29.281 14.177 1.00 78.61  ? 158 THR D C   1 
ATOM   6562  O  O   . THR D  1 167 ? -26.554 -29.333 13.904 1.00 78.17  ? 158 THR D O   1 
ATOM   6563  C  CB  . THR D  1 167 ? -25.078 -31.251 15.603 1.00 85.89  ? 158 THR D CB  1 
ATOM   6564  O  OG1 . THR D  1 167 ? -26.482 -31.511 15.746 1.00 86.85  ? 158 THR D OG1 1 
ATOM   6565  C  CG2 . THR D  1 167 ? -24.341 -31.859 16.792 1.00 79.68  ? 158 THR D CG2 1 
ATOM   6566  N  N   . ASP D  1 168 ? -24.440 -28.813 13.329 1.00 93.96  ? 159 ASP D N   1 
ATOM   6567  C  CA  . ASP D  1 168 ? -24.794 -28.389 11.958 1.00 100.58 ? 159 ASP D CA  1 
ATOM   6568  C  C   . ASP D  1 168 ? -25.173 -29.581 11.079 1.00 91.00  ? 159 ASP D C   1 
ATOM   6569  O  O   . ASP D  1 168 ? -26.082 -29.494 10.258 1.00 86.29  ? 159 ASP D O   1 
ATOM   6570  C  CB  . ASP D  1 168 ? -23.673 -27.562 11.297 1.00 92.60  ? 159 ASP D CB  1 
ATOM   6571  C  CG  . ASP D  1 168 ? -22.380 -28.348 11.112 1.00 103.44 ? 159 ASP D CG  1 
ATOM   6572  O  OD1 . ASP D  1 168 ? -22.225 -29.428 11.727 1.00 109.24 ? 159 ASP D OD1 1 
ATOM   6573  O  OD2 . ASP D  1 168 ? -21.506 -27.871 10.359 1.00 93.12  ? 159 ASP D OD2 1 
ATOM   6574  N  N   . THR D  1 169 ? -24.462 -30.688 11.272 1.00 90.85  ? 160 THR D N   1 
ATOM   6575  C  CA  . THR D  1 169 ? -24.784 -31.958 10.638 1.00 90.31  ? 160 THR D CA  1 
ATOM   6576  C  C   . THR D  1 169 ? -24.864 -33.066 11.678 1.00 90.45  ? 160 THR D C   1 
ATOM   6577  O  O   . THR D  1 169 ? -24.084 -33.102 12.629 1.00 87.06  ? 160 THR D O   1 
ATOM   6578  C  CB  . THR D  1 169 ? -23.713 -32.381 9.626  1.00 91.57  ? 160 THR D CB  1 
ATOM   6579  O  OG1 . THR D  1 169 ? -23.912 -33.760 9.290  1.00 84.45  ? 160 THR D OG1 1 
ATOM   6580  C  CG2 . THR D  1 169 ? -22.317 -32.215 10.223 1.00 92.79  ? 160 THR D CG2 1 
ATOM   6581  N  N   . ASP D  1 170 ? -25.803 -33.980 11.477 1.00 87.97  ? 161 ASP D N   1 
ATOM   6582  C  CA  . ASP D  1 170 ? -25.931 -35.166 12.317 1.00 88.30  ? 161 ASP D CA  1 
ATOM   6583  C  C   . ASP D  1 170 ? -24.888 -36.245 11.964 1.00 84.05  ? 161 ASP D C   1 
ATOM   6584  O  O   . ASP D  1 170 ? -24.621 -37.171 12.731 1.00 81.22  ? 161 ASP D O   1 
ATOM   6585  C  CB  . ASP D  1 170 ? -27.342 -35.730 12.162 1.00 97.35  ? 161 ASP D CB  1 
ATOM   6586  C  CG  . ASP D  1 170 ? -27.530 -37.066 12.860 1.00 110.47 ? 161 ASP D CG  1 
ATOM   6587  O  OD1 . ASP D  1 170 ? -26.573 -37.580 13.476 1.00 106.42 ? 161 ASP D OD1 1 
ATOM   6588  O  OD2 . ASP D  1 170 ? -28.649 -37.614 12.785 1.00 122.72 ? 161 ASP D OD2 1 
ATOM   6589  N  N   . GLN D  1 171 ? -24.284 -36.142 10.796 1.00 86.95  ? 162 GLN D N   1 
ATOM   6590  C  CA  . GLN D  1 171 ? -23.326 -37.172 10.421 1.00 88.78  ? 162 GLN D CA  1 
ATOM   6591  C  C   . GLN D  1 171 ? -21.916 -36.776 10.863 1.00 79.42  ? 162 GLN D C   1 
ATOM   6592  O  O   . GLN D  1 171 ? -21.482 -35.643 10.647 1.00 76.70  ? 162 GLN D O   1 
ATOM   6593  C  CB  . GLN D  1 171 ? -23.393 -37.456 8.914  1.00 89.11  ? 162 GLN D CB  1 
ATOM   6594  C  CG  . GLN D  1 171 ? -22.449 -38.550 8.447  1.00 86.27  ? 162 GLN D CG  1 
ATOM   6595  C  CD  . GLN D  1 171 ? -22.786 -39.905 9.050  1.00 94.50  ? 162 GLN D CD  1 
ATOM   6596  O  OE1 . GLN D  1 171 ? -21.948 -40.819 9.091  1.00 92.21  ? 162 GLN D OE1 1 
ATOM   6597  N  NE2 . GLN D  1 171 ? -24.022 -40.043 9.524  1.00 87.25  ? 162 GLN D NE2 1 
ATOM   6598  N  N   . VAL D  1 172 ? -21.212 -37.698 11.513 1.00 70.25  ? 163 VAL D N   1 
ATOM   6599  C  CA  . VAL D  1 172 ? -19.835 -37.435 11.911 1.00 71.30  ? 163 VAL D CA  1 
ATOM   6600  C  C   . VAL D  1 172 ? -18.976 -37.464 10.663 1.00 70.02  ? 163 VAL D C   1 
ATOM   6601  O  O   . VAL D  1 172 ? -19.234 -38.259 9.776  1.00 70.29  ? 163 VAL D O   1 
ATOM   6602  C  CB  . VAL D  1 172 ? -19.311 -38.492 12.915 1.00 69.01  ? 163 VAL D CB  1 
ATOM   6603  C  CG1 . VAL D  1 172 ? -17.800 -38.345 13.138 1.00 61.26  ? 163 VAL D CG1 1 
ATOM   6604  C  CG2 . VAL D  1 172 ? -20.051 -38.385 14.231 1.00 67.33  ? 163 VAL D CG2 1 
ATOM   6605  N  N   . ASP D  1 173 ? -17.940 -36.632 10.599 1.00 66.00  ? 164 ASP D N   1 
ATOM   6606  C  CA  . ASP D  1 173 ? -17.104 -36.603 9.410  1.00 62.76  ? 164 ASP D CA  1 
ATOM   6607  C  C   . ASP D  1 173 ? -16.039 -37.701 9.473  1.00 66.62  ? 164 ASP D C   1 
ATOM   6608  O  O   . ASP D  1 173 ? -15.145 -37.683 10.323 1.00 64.08  ? 164 ASP D O   1 
ATOM   6609  C  CB  . ASP D  1 173 ? -16.443 -35.229 9.273  1.00 56.85  ? 164 ASP D CB  1 
ATOM   6610  C  CG  . ASP D  1 173 ? -15.561 -35.120 8.041  1.00 66.35  ? 164 ASP D CG  1 
ATOM   6611  O  OD1 . ASP D  1 173 ? -15.648 -35.997 7.150  1.00 67.20  ? 164 ASP D OD1 1 
ATOM   6612  O  OD2 . ASP D  1 173 ? -14.782 -34.147 7.958  1.00 65.10  ? 164 ASP D OD2 1 
ATOM   6613  N  N   . LEU D  1 174 ? -16.149 -38.653 8.547  1.00 67.56  ? 165 LEU D N   1 
ATOM   6614  C  CA  . LEU D  1 174 ? -15.254 -39.807 8.489  1.00 64.00  ? 165 LEU D CA  1 
ATOM   6615  C  C   . LEU D  1 174 ? -14.128 -39.674 7.466  1.00 63.42  ? 165 LEU D C   1 
ATOM   6616  O  O   . LEU D  1 174 ? -13.291 -40.569 7.349  1.00 56.73  ? 165 LEU D O   1 
ATOM   6617  C  CB  . LEU D  1 174 ? -16.049 -41.107 8.320  1.00 50.01  ? 165 LEU D CB  1 
ATOM   6618  C  CG  . LEU D  1 174 ? -16.885 -41.397 9.574  1.00 61.21  ? 165 LEU D CG  1 
ATOM   6619  C  CD1 . LEU D  1 174 ? -17.722 -42.655 9.449  1.00 55.45  ? 165 LEU D CD1 1 
ATOM   6620  C  CD2 . LEU D  1 174 ? -15.968 -41.496 10.774 1.00 58.34  ? 165 LEU D CD2 1 
ATOM   6621  N  N   . SER D  1 175 ? -14.105 -38.550 6.749  1.00 59.84  ? 166 SER D N   1 
ATOM   6622  C  CA  . SER D  1 175 ? -13.236 -38.389 5.577  1.00 58.61  ? 166 SER D CA  1 
ATOM   6623  C  C   . SER D  1 175 ? -11.713 -38.429 5.813  1.00 62.50  ? 166 SER D C   1 
ATOM   6624  O  O   . SER D  1 175 ? -10.970 -38.885 4.946  1.00 65.72  ? 166 SER D O   1 
ATOM   6625  C  CB  . SER D  1 175 ? -13.623 -37.142 4.779  1.00 56.03  ? 166 SER D CB  1 
ATOM   6626  O  OG  . SER D  1 175 ? -13.495 -35.968 5.556  1.00 65.42  ? 166 SER D OG  1 
ATOM   6627  N  N   . SER D  1 176 ? -11.241 -37.937 6.954  1.00 64.68  ? 167 SER D N   1 
ATOM   6628  C  CA  . SER D  1 176 ? -9.802  -37.970 7.259  1.00 67.23  ? 167 SER D CA  1 
ATOM   6629  C  C   . SER D  1 176 ? -9.348  -39.155 8.123  1.00 64.45  ? 167 SER D C   1 
ATOM   6630  O  O   . SER D  1 176 ? -8.171  -39.278 8.474  1.00 58.68  ? 167 SER D O   1 
ATOM   6631  C  CB  . SER D  1 176 ? -9.340  -36.651 7.864  1.00 66.77  ? 167 SER D CB  1 
ATOM   6632  O  OG  . SER D  1 176 ? -9.220  -35.671 6.857  1.00 73.47  ? 167 SER D OG  1 
ATOM   6633  N  N   . TYR D  1 177 ? -10.288 -40.034 8.438  1.00 61.59  ? 168 TYR D N   1 
ATOM   6634  C  CA  . TYR D  1 177 ? -10.003 -41.177 9.278  1.00 58.02  ? 168 TYR D CA  1 
ATOM   6635  C  C   . TYR D  1 177 ? -8.888  -42.045 8.689  1.00 66.83  ? 168 TYR D C   1 
ATOM   6636  O  O   . TYR D  1 177 ? -8.705  -42.105 7.481  1.00 66.72  ? 168 TYR D O   1 
ATOM   6637  C  CB  . TYR D  1 177 ? -11.261 -42.004 9.486  1.00 50.96  ? 168 TYR D CB  1 
ATOM   6638  C  CG  . TYR D  1 177 ? -11.085 -43.038 10.554 1.00 59.06  ? 168 TYR D CG  1 
ATOM   6639  C  CD1 . TYR D  1 177 ? -11.414 -42.761 11.881 1.00 61.08  ? 168 TYR D CD1 1 
ATOM   6640  C  CD2 . TYR D  1 177 ? -10.558 -44.283 10.254 1.00 54.89  ? 168 TYR D CD2 1 
ATOM   6641  C  CE1 . TYR D  1 177 ? -11.242 -43.704 12.866 1.00 57.38  ? 168 TYR D CE1 1 
ATOM   6642  C  CE2 . TYR D  1 177 ? -10.387 -45.232 11.231 1.00 56.58  ? 168 TYR D CE2 1 
ATOM   6643  C  CZ  . TYR D  1 177 ? -10.725 -44.942 12.534 1.00 56.27  ? 168 TYR D CZ  1 
ATOM   6644  O  OH  . TYR D  1 177 ? -10.545 -45.903 13.502 1.00 58.82  ? 168 TYR D OH  1 
ATOM   6645  N  N   . TYR D  1 178 ? -8.124  -42.694 9.558  1.00 66.06  ? 169 TYR D N   1 
ATOM   6646  C  CA  . TYR D  1 178 ? -6.947  -43.458 9.154  1.00 63.07  ? 169 TYR D CA  1 
ATOM   6647  C  C   . TYR D  1 178 ? -7.339  -44.831 8.629  1.00 66.41  ? 169 TYR D C   1 
ATOM   6648  O  O   . TYR D  1 178 ? -7.921  -45.641 9.366  1.00 60.07  ? 169 TYR D O   1 
ATOM   6649  C  CB  . TYR D  1 178 ? -6.032  -43.609 10.370 1.00 63.02  ? 169 TYR D CB  1 
ATOM   6650  C  CG  . TYR D  1 178 ? -4.707  -44.277 10.120 1.00 61.52  ? 169 TYR D CG  1 
ATOM   6651  C  CD1 . TYR D  1 178 ? -3.907  -43.899 9.054  1.00 63.22  ? 169 TYR D CD1 1 
ATOM   6652  C  CD2 . TYR D  1 178 ? -4.238  -45.256 10.976 1.00 57.19  ? 169 TYR D CD2 1 
ATOM   6653  C  CE1 . TYR D  1 178 ? -2.685  -44.493 8.835  1.00 62.76  ? 169 TYR D CE1 1 
ATOM   6654  C  CE2 . TYR D  1 178 ? -3.017  -45.861 10.766 1.00 58.02  ? 169 TYR D CE2 1 
ATOM   6655  C  CZ  . TYR D  1 178 ? -2.244  -45.471 9.693  1.00 64.16  ? 169 TYR D CZ  1 
ATOM   6656  O  OH  . TYR D  1 178 ? -1.028  -46.061 9.454  1.00 64.37  ? 169 TYR D OH  1 
ATOM   6657  N  N   . ALA D  1 179 ? -6.994  -45.103 7.369  1.00 73.36  ? 170 ALA D N   1 
ATOM   6658  C  CA  . ALA D  1 179 ? -7.399  -46.353 6.703  1.00 71.36  ? 170 ALA D CA  1 
ATOM   6659  C  C   . ALA D  1 179 ? -6.668  -47.586 7.238  1.00 69.30  ? 170 ALA D C   1 
ATOM   6660  O  O   . ALA D  1 179 ? -7.237  -48.675 7.334  1.00 69.64  ? 170 ALA D O   1 
ATOM   6661  C  CB  . ALA D  1 179 ? -7.215  -46.244 5.212  1.00 56.32  ? 170 ALA D CB  1 
ATOM   6662  N  N   . SER D  1 180 ? -5.407  -47.394 7.604  1.00 69.02  ? 171 SER D N   1 
ATOM   6663  C  CA  . SER D  1 180 ? -4.576  -48.466 8.158  1.00 73.60  ? 171 SER D CA  1 
ATOM   6664  C  C   . SER D  1 180 ? -4.662  -48.589 9.688  1.00 64.93  ? 171 SER D C   1 
ATOM   6665  O  O   . SER D  1 180 ? -3.862  -49.281 10.284 1.00 68.38  ? 171 SER D O   1 
ATOM   6666  C  CB  . SER D  1 180 ? -3.119  -48.358 7.678  1.00 75.57  ? 171 SER D CB  1 
ATOM   6667  O  OG  . SER D  1 180 ? -3.012  -48.631 6.282  1.00 61.56  ? 171 SER D OG  1 
ATOM   6668  N  N   . SER D  1 181 ? -5.573  -47.842 10.312 1.00 66.29  ? 172 SER D N   1 
ATOM   6669  C  CA  . SER D  1 181 ? -5.886  -47.982 11.737 1.00 61.42  ? 172 SER D CA  1 
ATOM   6670  C  C   . SER D  1 181 ? -6.338  -49.382 12.130 1.00 58.99  ? 172 SER D C   1 
ATOM   6671  O  O   . SER D  1 181 ? -7.061  -50.027 11.395 1.00 62.16  ? 172 SER D O   1 
ATOM   6672  C  CB  . SER D  1 181 ? -6.990  -47.000 12.145 1.00 59.41  ? 172 SER D CB  1 
ATOM   6673  O  OG  . SER D  1 181 ? -7.759  -47.523 13.228 1.00 57.00  ? 172 SER D OG  1 
ATOM   6674  N  N   . LYS D  1 182 ? -5.939  -49.829 13.313 1.00 57.72  ? 173 LYS D N   1 
ATOM   6675  C  CA  . LYS D  1 182 ? -6.335  -51.140 13.803 1.00 64.75  ? 173 LYS D CA  1 
ATOM   6676  C  C   . LYS D  1 182 ? -7.847  -51.323 13.827 1.00 63.93  ? 173 LYS D C   1 
ATOM   6677  O  O   . LYS D  1 182 ? -8.344  -52.449 13.778 1.00 64.60  ? 173 LYS D O   1 
ATOM   6678  C  CB  . LYS D  1 182 ? -5.783  -51.381 15.216 1.00 66.52  ? 173 LYS D CB  1 
ATOM   6679  C  CG  . LYS D  1 182 ? -4.282  -51.579 15.278 1.00 65.68  ? 173 LYS D CG  1 
ATOM   6680  C  CD  . LYS D  1 182 ? -3.848  -52.780 14.456 1.00 63.47  ? 173 LYS D CD  1 
ATOM   6681  C  CE  . LYS D  1 182 ? -4.340  -54.063 15.067 1.00 66.20  ? 173 LYS D CE  1 
ATOM   6682  N  NZ  . LYS D  1 182 ? -3.342  -54.614 16.011 1.00 71.87  ? 173 LYS D NZ  1 
ATOM   6683  N  N   . TYR D  1 183 ? -8.588  -50.232 13.934 1.00 58.14  ? 174 TYR D N   1 
ATOM   6684  C  CA  . TYR D  1 183 ? -10.030 -50.373 13.999 1.00 61.58  ? 174 TYR D CA  1 
ATOM   6685  C  C   . TYR D  1 183 ? -10.674 -49.645 12.842 1.00 63.61  ? 174 TYR D C   1 
ATOM   6686  O  O   . TYR D  1 183 ? -10.167 -48.631 12.382 1.00 61.93  ? 174 TYR D O   1 
ATOM   6687  C  CB  . TYR D  1 183 ? -10.581 -49.887 15.337 1.00 55.23  ? 174 TYR D CB  1 
ATOM   6688  C  CG  . TYR D  1 183 ? -9.964  -50.587 16.510 1.00 60.00  ? 174 TYR D CG  1 
ATOM   6689  C  CD1 . TYR D  1 183 ? -8.719  -50.198 16.987 1.00 60.97  ? 174 TYR D CD1 1 
ATOM   6690  C  CD2 . TYR D  1 183 ? -10.605 -51.642 17.136 1.00 62.11  ? 174 TYR D CD2 1 
ATOM   6691  C  CE1 . TYR D  1 183 ? -8.126  -50.833 18.057 1.00 62.40  ? 174 TYR D CE1 1 
ATOM   6692  C  CE2 . TYR D  1 183 ? -10.017 -52.292 18.222 1.00 66.46  ? 174 TYR D CE2 1 
ATOM   6693  C  CZ  . TYR D  1 183 ? -8.777  -51.877 18.674 1.00 66.57  ? 174 TYR D CZ  1 
ATOM   6694  O  OH  . TYR D  1 183 ? -8.174  -52.491 19.742 1.00 57.74  ? 174 TYR D OH  1 
ATOM   6695  N  N   . GLU D  1 184 ? -11.786 -50.185 12.364 1.00 62.45  ? 175 GLU D N   1 
ATOM   6696  C  CA  . GLU D  1 184 ? -12.491 -49.581 11.258 1.00 70.28  ? 175 GLU D CA  1 
ATOM   6697  C  C   . GLU D  1 184 ? -13.843 -49.106 11.755 1.00 71.80  ? 175 GLU D C   1 
ATOM   6698  O  O   . GLU D  1 184 ? -14.450 -49.737 12.622 1.00 63.96  ? 175 GLU D O   1 
ATOM   6699  C  CB  . GLU D  1 184 ? -12.628 -50.568 10.083 1.00 76.45  ? 175 GLU D CB  1 
ATOM   6700  C  CG  . GLU D  1 184 ? -13.851 -51.479 10.124 1.00 75.93  ? 175 GLU D CG  1 
ATOM   6701  C  CD  . GLU D  1 184 ? -13.802 -52.566 9.064  1.00 81.92  ? 175 GLU D CD  1 
ATOM   6702  O  OE1 . GLU D  1 184 ? -12.888 -53.417 9.124  1.00 84.45  ? 175 GLU D OE1 1 
ATOM   6703  O  OE2 . GLU D  1 184 ? -14.678 -52.567 8.172  1.00 83.70  ? 175 GLU D OE2 1 
ATOM   6704  N  N   . ILE D  1 185 ? -14.303 -47.979 11.216 1.00 74.24  ? 176 ILE D N   1 
ATOM   6705  C  CA  . ILE D  1 185 ? -15.566 -47.415 11.662 1.00 72.15  ? 176 ILE D CA  1 
ATOM   6706  C  C   . ILE D  1 185 ? -16.744 -47.936 10.845 1.00 68.93  ? 176 ILE D C   1 
ATOM   6707  O  O   . ILE D  1 185 ? -16.809 -47.729 9.627  1.00 62.15  ? 176 ILE D O   1 
ATOM   6708  C  CB  . ILE D  1 185 ? -15.555 -45.876 11.631 1.00 67.93  ? 176 ILE D CB  1 
ATOM   6709  C  CG1 . ILE D  1 185 ? -14.299 -45.337 12.323 1.00 64.92  ? 176 ILE D CG1 1 
ATOM   6710  C  CG2 . ILE D  1 185 ? -16.827 -45.327 12.283 1.00 65.80  ? 176 ILE D CG2 1 
ATOM   6711  C  CD1 . ILE D  1 185 ? -14.269 -45.584 13.807 1.00 56.64  ? 176 ILE D CD1 1 
ATOM   6712  N  N   . LEU D  1 186 ? -17.651 -48.637 11.527 1.00 65.74  ? 177 LEU D N   1 
ATOM   6713  C  CA  . LEU D  1 186 ? -18.930 -49.013 10.943 1.00 64.26  ? 177 LEU D CA  1 
ATOM   6714  C  C   . LEU D  1 186 ? -19.819 -47.790 10.798 1.00 62.87  ? 177 LEU D C   1 
ATOM   6715  O  O   . LEU D  1 186 ? -20.250 -47.467 9.695  1.00 72.43  ? 177 LEU D O   1 
ATOM   6716  C  CB  . LEU D  1 186 ? -19.617 -50.075 11.794 1.00 65.64  ? 177 LEU D CB  1 
ATOM   6717  C  CG  . LEU D  1 186 ? -18.750 -51.322 11.969 1.00 69.44  ? 177 LEU D CG  1 
ATOM   6718  C  CD1 . LEU D  1 186 ? -19.500 -52.459 12.672 1.00 62.43  ? 177 LEU D CD1 1 
ATOM   6719  C  CD2 . LEU D  1 186 ? -18.217 -51.756 10.617 1.00 60.65  ? 177 LEU D CD2 1 
ATOM   6720  N  N   . SER D  1 187 ? -20.047 -47.084 11.901 1.00 67.93  ? 178 SER D N   1 
ATOM   6721  C  CA  . SER D  1 187 ? -20.801 -45.826 11.883 1.00 72.21  ? 178 SER D CA  1 
ATOM   6722  C  C   . SER D  1 187 ? -20.357 -44.870 12.990 1.00 66.22  ? 178 SER D C   1 
ATOM   6723  O  O   . SER D  1 187 ? -19.866 -45.292 14.019 1.00 72.05  ? 178 SER D O   1 
ATOM   6724  C  CB  . SER D  1 187 ? -22.302 -46.091 12.010 1.00 70.78  ? 178 SER D CB  1 
ATOM   6725  O  OG  . SER D  1 187 ? -22.745 -45.928 13.345 1.00 72.99  ? 178 SER D OG  1 
ATOM   6726  N  N   . ALA D  1 188 ? -20.513 -43.574 12.758 1.00 72.56  ? 179 ALA D N   1 
ATOM   6727  C  CA  . ALA D  1 188 ? -20.308 -42.572 13.798 1.00 63.66  ? 179 ALA D CA  1 
ATOM   6728  C  C   . ALA D  1 188 ? -21.315 -41.455 13.594 1.00 67.52  ? 179 ALA D C   1 
ATOM   6729  O  O   . ALA D  1 188 ? -21.497 -40.971 12.479 1.00 79.41  ? 179 ALA D O   1 
ATOM   6730  C  CB  . ALA D  1 188 ? -18.891 -42.032 13.748 1.00 59.09  ? 179 ALA D CB  1 
ATOM   6731  N  N   . THR D  1 189 ? -21.961 -41.025 14.666 1.00 67.31  ? 180 THR D N   1 
ATOM   6732  C  CA  . THR D  1 189 ? -23.004 -40.023 14.546 1.00 73.51  ? 180 THR D CA  1 
ATOM   6733  C  C   . THR D  1 189 ? -23.003 -39.046 15.710 1.00 70.10  ? 180 THR D C   1 
ATOM   6734  O  O   . THR D  1 189 ? -22.956 -39.453 16.865 1.00 69.22  ? 180 THR D O   1 
ATOM   6735  C  CB  . THR D  1 189 ? -24.368 -40.702 14.477 1.00 74.33  ? 180 THR D CB  1 
ATOM   6736  O  OG1 . THR D  1 189 ? -24.639 -41.356 15.722 1.00 77.30  ? 180 THR D OG1 1 
ATOM   6737  C  CG2 . THR D  1 189 ? -24.364 -41.738 13.377 1.00 76.19  ? 180 THR D CG2 1 
ATOM   6738  N  N   . GLN D  1 190 ? -23.100 -37.758 15.405 1.00 67.80  ? 181 GLN D N   1 
ATOM   6739  C  CA  . GLN D  1 190 ? -23.156 -36.755 16.449 1.00 66.73  ? 181 GLN D CA  1 
ATOM   6740  C  C   . GLN D  1 190 ? -24.572 -36.194 16.576 1.00 71.60  ? 181 GLN D C   1 
ATOM   6741  O  O   . GLN D  1 190 ? -25.029 -35.432 15.731 1.00 76.36  ? 181 GLN D O   1 
ATOM   6742  C  CB  . GLN D  1 190 ? -22.147 -35.647 16.156 1.00 68.76  ? 181 GLN D CB  1 
ATOM   6743  C  CG  . GLN D  1 190 ? -22.407 -34.880 14.875 1.00 68.51  ? 181 GLN D CG  1 
ATOM   6744  C  CD  . GLN D  1 190 ? -21.180 -34.152 14.367 1.00 66.40  ? 181 GLN D CD  1 
ATOM   6745  O  OE1 . GLN D  1 190 ? -20.055 -34.513 14.686 1.00 63.19  ? 181 GLN D OE1 1 
ATOM   6746  N  NE2 . GLN D  1 190 ? -21.396 -33.125 13.563 1.00 75.79  ? 181 GLN D NE2 1 
ATOM   6747  N  N   . THR D  1 191 ? -25.243 -36.551 17.666 1.00 69.48  ? 182 THR D N   1 
ATOM   6748  C  CA  . THR D  1 191 ? -26.630 -36.160 17.902 1.00 69.30  ? 182 THR D CA  1 
ATOM   6749  C  C   . THR D  1 191 ? -26.740 -35.186 19.066 1.00 63.90  ? 182 THR D C   1 
ATOM   6750  O  O   . THR D  1 191 ? -26.033 -35.305 20.054 1.00 60.83  ? 182 THR D O   1 
ATOM   6751  C  CB  . THR D  1 191 ? -27.502 -37.378 18.261 1.00 71.05  ? 182 THR D CB  1 
ATOM   6752  O  OG1 . THR D  1 191 ? -27.073 -38.528 17.518 1.00 74.07  ? 182 THR D OG1 1 
ATOM   6753  C  CG2 . THR D  1 191 ? -28.970 -37.087 17.996 1.00 59.60  ? 182 THR D CG2 1 
ATOM   6754  N  N   . ARG D  1 192 ? -27.649 -34.234 18.950 1.00 66.29  ? 183 ARG D N   1 
ATOM   6755  C  CA  . ARG D  1 192 ? -27.905 -33.300 20.030 1.00 70.50  ? 183 ARG D CA  1 
ATOM   6756  C  C   . ARG D  1 192 ? -29.066 -33.777 20.888 1.00 69.58  ? 183 ARG D C   1 
ATOM   6757  O  O   . ARG D  1 192 ? -30.004 -34.382 20.384 1.00 74.75  ? 183 ARG D O   1 
ATOM   6758  C  CB  . ARG D  1 192 ? -28.216 -31.916 19.476 1.00 73.15  ? 183 ARG D CB  1 
ATOM   6759  C  CG  . ARG D  1 192 ? -28.725 -30.947 20.519 1.00 66.74  ? 183 ARG D CG  1 
ATOM   6760  C  CD  . ARG D  1 192 ? -29.501 -29.858 19.854 1.00 64.20  ? 183 ARG D CD  1 
ATOM   6761  N  NE  . ARG D  1 192 ? -29.568 -28.656 20.666 1.00 73.07  ? 183 ARG D NE  1 
ATOM   6762  C  CZ  . ARG D  1 192 ? -30.605 -28.324 21.424 1.00 79.33  ? 183 ARG D CZ  1 
ATOM   6763  N  NH1 . ARG D  1 192 ? -31.665 -29.119 21.476 1.00 80.65  ? 183 ARG D NH1 1 
ATOM   6764  N  NH2 . ARG D  1 192 ? -30.579 -27.196 22.123 1.00 75.69  ? 183 ARG D NH2 1 
ATOM   6765  N  N   . SER D  1 193 ? -28.993 -33.527 22.189 1.00 71.34  ? 184 SER D N   1 
ATOM   6766  C  CA  . SER D  1 193 ? -30.077 -33.902 23.090 1.00 73.63  ? 184 SER D CA  1 
ATOM   6767  C  C   . SER D  1 193 ? -30.355 -32.787 24.073 1.00 70.30  ? 184 SER D C   1 
ATOM   6768  O  O   . SER D  1 193 ? -29.548 -31.879 24.220 1.00 74.43  ? 184 SER D O   1 
ATOM   6769  C  CB  . SER D  1 193 ? -29.730 -35.185 23.844 1.00 71.73  ? 184 SER D CB  1 
ATOM   6770  O  OG  . SER D  1 193 ? -29.823 -36.318 22.996 1.00 73.10  ? 184 SER D OG  1 
ATOM   6771  N  N   . GLU D  1 194 ? -31.509 -32.844 24.726 1.00 75.74  ? 185 GLU D N   1 
ATOM   6772  C  CA  . GLU D  1 194 ? -31.803 -31.935 25.833 1.00 87.02  ? 185 GLU D CA  1 
ATOM   6773  C  C   . GLU D  1 194 ? -32.208 -32.722 27.078 1.00 86.83  ? 185 GLU D C   1 
ATOM   6774  O  O   . GLU D  1 194 ? -33.022 -33.643 27.011 1.00 84.59  ? 185 GLU D O   1 
ATOM   6775  C  CB  . GLU D  1 194 ? -32.879 -30.909 25.456 1.00 78.60  ? 185 GLU D CB  1 
ATOM   6776  C  CG  . GLU D  1 194 ? -32.329 -29.638 24.808 1.00 80.81  ? 185 GLU D CG  1 
ATOM   6777  C  CD  . GLU D  1 194 ? -33.427 -28.754 24.230 1.00 92.66  ? 185 GLU D CD  1 
ATOM   6778  O  OE1 . GLU D  1 194 ? -34.606 -28.985 24.564 1.00 98.39  ? 185 GLU D OE1 1 
ATOM   6779  O  OE2 . GLU D  1 194 ? -33.120 -27.837 23.437 1.00 87.12  ? 185 GLU D OE2 1 
ATOM   6780  N  N   . ARG D  1 195 ? -31.625 -32.369 28.214 1.00 82.08  ? 186 ARG D N   1 
ATOM   6781  C  CA  . ARG D  1 195 ? -31.927 -33.083 29.438 1.00 91.60  ? 186 ARG D CA  1 
ATOM   6782  C  C   . ARG D  1 195 ? -32.514 -32.129 30.475 1.00 91.99  ? 186 ARG D C   1 
ATOM   6783  O  O   . ARG D  1 195 ? -32.214 -30.937 30.468 1.00 88.79  ? 186 ARG D O   1 
ATOM   6784  C  CB  . ARG D  1 195 ? -30.680 -33.806 29.966 1.00 91.78  ? 186 ARG D CB  1 
ATOM   6785  C  CG  . ARG D  1 195 ? -30.804 -34.216 31.419 1.00 105.85 ? 186 ARG D CG  1 
ATOM   6786  C  CD  . ARG D  1 195 ? -30.057 -35.498 31.777 1.00 110.85 ? 186 ARG D CD  1 
ATOM   6787  N  NE  . ARG D  1 195 ? -30.388 -35.908 33.143 1.00 111.24 ? 186 ARG D NE  1 
ATOM   6788  C  CZ  . ARG D  1 195 ? -31.360 -36.760 33.456 1.00 107.90 ? 186 ARG D CZ  1 
ATOM   6789  N  NH1 . ARG D  1 195 ? -32.088 -37.319 32.500 1.00 107.78 ? 186 ARG D NH1 1 
ATOM   6790  N  NH2 . ARG D  1 195 ? -31.599 -37.062 34.726 1.00 108.07 ? 186 ARG D NH2 1 
ATOM   6791  N  N   . PHE D  1 196 ? -33.368 -32.655 31.348 1.00 95.81  ? 187 PHE D N   1 
ATOM   6792  C  CA  . PHE D  1 196 ? -33.974 -31.855 32.412 1.00 99.54  ? 187 PHE D CA  1 
ATOM   6793  C  C   . PHE D  1 196 ? -33.725 -32.387 33.833 1.00 108.05 ? 187 PHE D C   1 
ATOM   6794  O  O   . PHE D  1 196 ? -33.467 -33.578 34.034 1.00 107.33 ? 187 PHE D O   1 
ATOM   6795  C  CB  . PHE D  1 196 ? -35.470 -31.721 32.171 1.00 91.93  ? 187 PHE D CB  1 
ATOM   6796  C  CG  . PHE D  1 196 ? -35.819 -30.689 31.154 1.00 92.64  ? 187 PHE D CG  1 
ATOM   6797  C  CD1 . PHE D  1 196 ? -36.140 -29.405 31.541 1.00 93.89  ? 187 PHE D CD1 1 
ATOM   6798  C  CD2 . PHE D  1 196 ? -35.824 -30.998 29.811 1.00 92.29  ? 187 PHE D CD2 1 
ATOM   6799  C  CE1 . PHE D  1 196 ? -36.468 -28.448 30.612 1.00 91.60  ? 187 PHE D CE1 1 
ATOM   6800  C  CE2 . PHE D  1 196 ? -36.150 -30.042 28.875 1.00 94.10  ? 187 PHE D CE2 1 
ATOM   6801  C  CZ  . PHE D  1 196 ? -36.472 -28.765 29.278 1.00 92.67  ? 187 PHE D CZ  1 
ATOM   6802  N  N   . TYR D  1 197 ? -33.806 -31.491 34.815 1.00 102.98 ? 188 TYR D N   1 
ATOM   6803  C  CA  . TYR D  1 197 ? -33.681 -31.862 36.221 1.00 104.21 ? 188 TYR D CA  1 
ATOM   6804  C  C   . TYR D  1 197 ? -34.786 -31.171 37.025 1.00 112.26 ? 188 TYR D C   1 
ATOM   6805  O  O   . TYR D  1 197 ? -35.166 -30.048 36.703 1.00 116.85 ? 188 TYR D O   1 
ATOM   6806  C  CB  . TYR D  1 197 ? -32.315 -31.437 36.769 1.00 109.05 ? 188 TYR D CB  1 
ATOM   6807  C  CG  . TYR D  1 197 ? -31.108 -31.933 35.998 1.00 106.05 ? 188 TYR D CG  1 
ATOM   6808  C  CD1 . TYR D  1 197 ? -30.653 -33.237 36.142 1.00 100.38 ? 188 TYR D CD1 1 
ATOM   6809  C  CD2 . TYR D  1 197 ? -30.398 -31.081 35.156 1.00 103.18 ? 188 TYR D CD2 1 
ATOM   6810  C  CE1 . TYR D  1 197 ? -29.542 -33.688 35.453 1.00 98.94  ? 188 TYR D CE1 1 
ATOM   6811  C  CE2 . TYR D  1 197 ? -29.283 -31.522 34.461 1.00 97.88  ? 188 TYR D CE2 1 
ATOM   6812  C  CZ  . TYR D  1 197 ? -28.860 -32.827 34.614 1.00 101.62 ? 188 TYR D CZ  1 
ATOM   6813  O  OH  . TYR D  1 197 ? -27.753 -33.275 33.927 1.00 97.89  ? 188 TYR D OH  1 
ATOM   6814  N  N   . GLU D  1 198 ? -35.293 -31.828 38.068 1.00 116.89 ? 189 GLU D N   1 
ATOM   6815  C  CA  . GLU D  1 198 ? -36.287 -31.214 38.959 1.00 120.33 ? 189 GLU D CA  1 
ATOM   6816  C  C   . GLU D  1 198 ? -35.724 -30.005 39.701 1.00 111.07 ? 189 GLU D C   1 
ATOM   6817  O  O   . GLU D  1 198 ? -36.454 -29.085 40.063 1.00 105.86 ? 189 GLU D O   1 
ATOM   6818  C  CB  . GLU D  1 198 ? -36.811 -32.226 39.984 1.00 108.39 ? 189 GLU D CB  1 
ATOM   6819  C  CG  . GLU D  1 198 ? -37.524 -33.435 39.412 1.00 112.98 ? 189 GLU D CG  1 
ATOM   6820  C  CD  . GLU D  1 198 ? -38.473 -33.099 38.258 1.00 123.25 ? 189 GLU D CD  1 
ATOM   6821  O  OE1 . GLU D  1 198 ? -39.021 -31.975 38.221 1.00 117.58 ? 189 GLU D OE1 1 
ATOM   6822  O  OE2 . GLU D  1 198 ? -38.665 -33.962 37.372 1.00 110.35 ? 189 GLU D OE2 1 
ATOM   6823  N  N   . CYS D  1 199 ? -34.413 -30.020 39.912 1.00 108.05 ? 190 CYS D N   1 
ATOM   6824  C  CA  . CYS D  1 199 ? -33.702 -28.904 40.524 1.00 105.57 ? 190 CYS D CA  1 
ATOM   6825  C  C   . CYS D  1 199 ? -34.061 -27.555 39.905 1.00 117.59 ? 190 CYS D C   1 
ATOM   6826  O  O   . CYS D  1 199 ? -34.278 -26.579 40.630 1.00 115.10 ? 190 CYS D O   1 
ATOM   6827  C  CB  . CYS D  1 199 ? -32.189 -29.104 40.399 1.00 104.51 ? 190 CYS D CB  1 
ATOM   6828  S  SG  . CYS D  1 199 ? -31.407 -28.391 38.931 1.00 122.78 ? 190 CYS D SG  1 
ATOM   6829  N  N   . CYS D  1 200 ? -34.114 -27.519 38.570 1.00 112.88 ? 191 CYS D N   1 
ATOM   6830  C  CA  . CYS D  1 200 ? -34.295 -26.289 37.808 1.00 107.18 ? 191 CYS D CA  1 
ATOM   6831  C  C   . CYS D  1 200 ? -34.977 -26.578 36.474 1.00 106.89 ? 191 CYS D C   1 
ATOM   6832  O  O   . CYS D  1 200 ? -34.929 -27.700 35.991 1.00 101.09 ? 191 CYS D O   1 
ATOM   6833  C  CB  . CYS D  1 200 ? -32.953 -25.588 37.602 1.00 100.53 ? 191 CYS D CB  1 
ATOM   6834  S  SG  . CYS D  1 200 ? -31.544 -26.668 37.770 1.00 113.35 ? 191 CYS D SG  1 
ATOM   6835  N  N   . LYS D  1 201 ? -35.687 -25.579 35.914 1.00 112.85 ? 192 LYS D N   1 
ATOM   6836  C  CA  . LYS D  1 201 ? -36.466 -25.756 34.692 1.00 102.28 ? 192 LYS D CA  1 
ATOM   6837  C  C   . LYS D  1 201 ? -35.621 -25.549 33.441 1.00 95.00  ? 192 LYS D C   1 
ATOM   6838  O  O   . LYS D  1 201 ? -36.084 -25.780 32.324 1.00 91.31  ? 192 LYS D O   1 
ATOM   6839  C  CB  . LYS D  1 201 ? -37.664 -24.804 34.680 1.00 102.60 ? 192 LYS D CB  1 
ATOM   6840  C  CG  . LYS D  1 201 ? -37.961 -24.164 36.026 1.00 111.18 ? 192 LYS D CG  1 
ATOM   6841  C  CD  . LYS D  1 201 ? -39.164 -24.812 36.692 1.00 116.01 ? 192 LYS D CD  1 
ATOM   6842  C  CE  . LYS D  1 201 ? -39.539 -24.091 37.977 1.00 119.12 ? 192 LYS D CE  1 
ATOM   6843  N  NZ  . LYS D  1 201 ? -38.956 -24.754 39.176 1.00 108.64 ? 192 LYS D NZ  1 
ATOM   6844  N  N   . GLU D  1 202 ? -34.356 -25.037 33.606 1.00 93.25  ? 193 GLU D N   1 
ATOM   6845  C  CA  . GLU D  1 202 ? -33.428 -24.862 32.508 1.00 89.11  ? 193 GLU D CA  1 
ATOM   6846  C  C   . GLU D  1 202 ? -33.059 -26.203 31.886 1.00 89.24  ? 193 GLU D C   1 
ATOM   6847  O  O   . GLU D  1 202 ? -32.745 -27.159 32.606 1.00 87.43  ? 193 GLU D O   1 
ATOM   6848  C  CB  . GLU D  1 202 ? -32.175 -24.140 32.985 1.00 87.66  ? 193 GLU D CB  1 
ATOM   6849  C  CG  . GLU D  1 202 ? -31.418 -23.484 31.865 1.00 85.95  ? 193 GLU D CG  1 
ATOM   6850  C  CD  . GLU D  1 202 ? -30.244 -22.670 32.351 1.00 88.16  ? 193 GLU D CD  1 
ATOM   6851  O  OE1 . GLU D  1 202 ? -29.852 -22.801 33.537 1.00 75.99  ? 193 GLU D OE1 1 
ATOM   6852  O  OE2 . GLU D  1 202 ? -29.711 -21.895 31.531 1.00 85.08  ? 193 GLU D OE2 1 
ATOM   6853  N  N   . PRO D  1 203 ? -33.138 -26.283 30.543 1.00 86.80  ? 194 PRO D N   1 
ATOM   6854  C  CA  . PRO D  1 203 ? -32.721 -27.426 29.727 1.00 86.29  ? 194 PRO D CA  1 
ATOM   6855  C  C   . PRO D  1 203 ? -31.205 -27.501 29.636 1.00 78.21  ? 194 PRO D C   1 
ATOM   6856  O  O   . PRO D  1 203 ? -30.548 -26.469 29.542 1.00 74.72  ? 194 PRO D O   1 
ATOM   6857  C  CB  . PRO D  1 203 ? -33.305 -27.091 28.356 1.00 83.86  ? 194 PRO D CB  1 
ATOM   6858  C  CG  . PRO D  1 203 ? -33.304 -25.616 28.324 1.00 71.33  ? 194 PRO D CG  1 
ATOM   6859  C  CD  . PRO D  1 203 ? -33.680 -25.197 29.707 1.00 83.33  ? 194 PRO D CD  1 
ATOM   6860  N  N   . TYR D  1 204 ? -30.659 -28.710 29.676 1.00 79.83  ? 195 TYR D N   1 
ATOM   6861  C  CA  . TYR D  1 204 ? -29.224 -28.898 29.532 1.00 76.92  ? 195 TYR D CA  1 
ATOM   6862  C  C   . TYR D  1 204 ? -28.898 -29.701 28.279 1.00 74.00  ? 195 TYR D C   1 
ATOM   6863  O  O   . TYR D  1 204 ? -29.163 -30.901 28.218 1.00 72.68  ? 195 TYR D O   1 
ATOM   6864  C  CB  . TYR D  1 204 ? -28.647 -29.552 30.794 1.00 79.26  ? 195 TYR D CB  1 
ATOM   6865  C  CG  . TYR D  1 204 ? -28.707 -28.632 31.997 1.00 83.81  ? 195 TYR D CG  1 
ATOM   6866  C  CD1 . TYR D  1 204 ? -27.569 -27.994 32.466 1.00 78.82  ? 195 TYR D CD1 1 
ATOM   6867  C  CD2 . TYR D  1 204 ? -29.911 -28.372 32.636 1.00 84.16  ? 195 TYR D CD2 1 
ATOM   6868  C  CE1 . TYR D  1 204 ? -27.627 -27.144 33.536 1.00 73.53  ? 195 TYR D CE1 1 
ATOM   6869  C  CE2 . TYR D  1 204 ? -29.973 -27.522 33.710 1.00 78.70  ? 195 TYR D CE2 1 
ATOM   6870  C  CZ  . TYR D  1 204 ? -28.830 -26.912 34.150 1.00 74.70  ? 195 TYR D CZ  1 
ATOM   6871  O  OH  . TYR D  1 204 ? -28.891 -26.062 35.219 1.00 81.89  ? 195 TYR D OH  1 
ATOM   6872  N  N   . PRO D  1 205 ? -28.341 -29.029 27.259 1.00 72.60  ? 196 PRO D N   1 
ATOM   6873  C  CA  . PRO D  1 205 ? -27.941 -29.705 26.022 1.00 72.13  ? 196 PRO D CA  1 
ATOM   6874  C  C   . PRO D  1 205 ? -26.627 -30.481 26.122 1.00 66.84  ? 196 PRO D C   1 
ATOM   6875  O  O   . PRO D  1 205 ? -25.666 -30.034 26.739 1.00 71.63  ? 196 PRO D O   1 
ATOM   6876  C  CB  . PRO D  1 205 ? -27.791 -28.551 25.019 1.00 66.17  ? 196 PRO D CB  1 
ATOM   6877  C  CG  . PRO D  1 205 ? -27.964 -27.275 25.811 1.00 66.38  ? 196 PRO D CG  1 
ATOM   6878  C  CD  . PRO D  1 205 ? -27.950 -27.612 27.255 1.00 60.84  ? 196 PRO D CD  1 
ATOM   6879  N  N   . ASP D  1 206 ? -26.578 -31.618 25.455 1.00 61.56  ? 197 ASP D N   1 
ATOM   6880  C  CA  . ASP D  1 206 ? -25.327 -32.310 25.232 1.00 64.10  ? 197 ASP D CA  1 
ATOM   6881  C  C   . ASP D  1 206 ? -25.285 -32.742 23.769 1.00 65.50  ? 197 ASP D C   1 
ATOM   6882  O  O   . ASP D  1 206 ? -26.314 -32.771 23.095 1.00 65.45  ? 197 ASP D O   1 
ATOM   6883  C  CB  . ASP D  1 206 ? -25.174 -33.511 26.174 1.00 66.44  ? 197 ASP D CB  1 
ATOM   6884  C  CG  . ASP D  1 206 ? -26.333 -34.501 26.073 1.00 74.20  ? 197 ASP D CG  1 
ATOM   6885  O  OD1 . ASP D  1 206 ? -27.299 -34.378 26.863 1.00 79.33  ? 197 ASP D OD1 1 
ATOM   6886  O  OD2 . ASP D  1 206 ? -26.271 -35.415 25.219 1.00 66.15  ? 197 ASP D OD2 1 
ATOM   6887  N  N   . VAL D  1 207 ? -24.091 -33.033 23.269 1.00 59.94  ? 198 VAL D N   1 
ATOM   6888  C  CA  . VAL D  1 207 ? -23.950 -33.651 21.964 1.00 61.05  ? 198 VAL D CA  1 
ATOM   6889  C  C   . VAL D  1 207 ? -23.377 -35.034 22.156 1.00 62.77  ? 198 VAL D C   1 
ATOM   6890  O  O   . VAL D  1 207 ? -22.236 -35.181 22.580 1.00 65.59  ? 198 VAL D O   1 
ATOM   6891  C  CB  . VAL D  1 207 ? -23.020 -32.865 21.035 1.00 64.22  ? 198 VAL D CB  1 
ATOM   6892  C  CG1 . VAL D  1 207 ? -22.651 -33.721 19.824 1.00 61.61  ? 198 VAL D CG1 1 
ATOM   6893  C  CG2 . VAL D  1 207 ? -23.675 -31.557 20.604 1.00 61.99  ? 198 VAL D CG2 1 
ATOM   6894  N  N   . ASN D  1 208 ? -24.174 -36.046 21.842 1.00 63.58  ? 199 ASN D N   1 
ATOM   6895  C  CA  . ASN D  1 208 ? -23.801 -37.422 22.110 1.00 61.62  ? 199 ASN D CA  1 
ATOM   6896  C  C   . ASN D  1 208 ? -23.064 -38.041 20.934 1.00 61.03  ? 199 ASN D C   1 
ATOM   6897  O  O   . ASN D  1 208 ? -23.606 -38.130 19.843 1.00 69.23  ? 199 ASN D O   1 
ATOM   6898  C  CB  . ASN D  1 208 ? -25.058 -38.222 22.426 1.00 65.51  ? 199 ASN D CB  1 
ATOM   6899  C  CG  . ASN D  1 208 ? -24.761 -39.665 22.737 1.00 72.29  ? 199 ASN D CG  1 
ATOM   6900  O  OD1 . ASN D  1 208 ? -23.713 -39.984 23.296 1.00 74.06  ? 199 ASN D OD1 1 
ATOM   6901  N  ND2 . ASN D  1 208 ? -25.685 -40.554 22.377 1.00 72.10  ? 199 ASN D ND2 1 
ATOM   6902  N  N   . LEU D  1 209 ? -21.824 -38.458 21.134 1.00 57.84  ? 200 LEU D N   1 
ATOM   6903  C  CA  . LEU D  1 209 ? -21.088 -39.077 20.038 1.00 62.89  ? 200 LEU D CA  1 
ATOM   6904  C  C   . LEU D  1 209 ? -21.156 -40.600 20.134 1.00 68.02  ? 200 LEU D C   1 
ATOM   6905  O  O   . LEU D  1 209 ? -20.682 -41.192 21.111 1.00 62.26  ? 200 LEU D O   1 
ATOM   6906  C  CB  . LEU D  1 209 ? -19.636 -38.590 19.994 1.00 64.76  ? 200 LEU D CB  1 
ATOM   6907  C  CG  . LEU D  1 209 ? -18.733 -39.191 18.911 1.00 61.82  ? 200 LEU D CG  1 
ATOM   6908  C  CD1 . LEU D  1 209 ? -19.182 -38.754 17.559 1.00 62.39  ? 200 LEU D CD1 1 
ATOM   6909  C  CD2 . LEU D  1 209 ? -17.288 -38.791 19.124 1.00 57.93  ? 200 LEU D CD2 1 
ATOM   6910  N  N   . VAL D  1 210 ? -21.762 -41.228 19.123 1.00 68.95  ? 201 VAL D N   1 
ATOM   6911  C  CA  . VAL D  1 210 ? -21.917 -42.681 19.114 1.00 67.13  ? 201 VAL D CA  1 
ATOM   6912  C  C   . VAL D  1 210 ? -21.060 -43.300 18.035 1.00 64.52  ? 201 VAL D C   1 
ATOM   6913  O  O   . VAL D  1 210 ? -21.208 -42.976 16.874 1.00 64.70  ? 201 VAL D O   1 
ATOM   6914  C  CB  . VAL D  1 210 ? -23.372 -43.131 18.876 1.00 59.56  ? 201 VAL D CB  1 
ATOM   6915  C  CG1 . VAL D  1 210 ? -23.462 -44.639 19.037 1.00 59.51  ? 201 VAL D CG1 1 
ATOM   6916  C  CG2 . VAL D  1 210 ? -24.327 -42.442 19.847 1.00 57.62  ? 201 VAL D CG2 1 
ATOM   6917  N  N   . VAL D  1 211 ? -20.170 -44.206 18.414 1.00 67.69  ? 202 VAL D N   1 
ATOM   6918  C  CA  . VAL D  1 211 ? -19.338 -44.870 17.420 1.00 64.92  ? 202 VAL D CA  1 
ATOM   6919  C  C   . VAL D  1 211 ? -19.444 -46.398 17.478 1.00 69.79  ? 202 VAL D C   1 
ATOM   6920  O  O   . VAL D  1 211 ? -19.359 -46.999 18.549 1.00 69.15  ? 202 VAL D O   1 
ATOM   6921  C  CB  . VAL D  1 211 ? -17.882 -44.411 17.518 1.00 65.05  ? 202 VAL D CB  1 
ATOM   6922  C  CG1 . VAL D  1 211 ? -17.027 -45.084 16.453 1.00 60.32  ? 202 VAL D CG1 1 
ATOM   6923  C  CG2 . VAL D  1 211 ? -17.818 -42.892 17.395 1.00 65.78  ? 202 VAL D CG2 1 
ATOM   6924  N  N   . LYS D  1 212 ? -19.678 -47.000 16.309 1.00 73.37  ? 203 LYS D N   1 
ATOM   6925  C  CA  . LYS D  1 212 ? -19.712 -48.447 16.125 1.00 64.41  ? 203 LYS D CA  1 
ATOM   6926  C  C   . LYS D  1 212 ? -18.444 -48.845 15.391 1.00 61.72  ? 203 LYS D C   1 
ATOM   6927  O  O   . LYS D  1 212 ? -18.083 -48.242 14.395 1.00 64.06  ? 203 LYS D O   1 
ATOM   6928  C  CB  . LYS D  1 212 ? -20.945 -48.860 15.316 1.00 69.64  ? 203 LYS D CB  1 
ATOM   6929  C  CG  . LYS D  1 212 ? -22.267 -48.610 16.018 1.00 79.24  ? 203 LYS D CG  1 
ATOM   6930  C  CD  . LYS D  1 212 ? -23.244 -49.748 15.805 1.00 92.64  ? 203 LYS D CD  1 
ATOM   6931  C  CE  . LYS D  1 212 ? -24.442 -49.612 16.731 1.00 93.53  ? 203 LYS D CE  1 
ATOM   6932  N  NZ  . LYS D  1 212 ? -25.410 -50.730 16.564 1.00 89.48  ? 203 LYS D NZ  1 
ATOM   6933  N  N   . PHE D  1 213 ? -17.741 -49.844 15.889 1.00 61.40  ? 204 PHE D N   1 
ATOM   6934  C  CA  . PHE D  1 213 ? -16.468 -50.186 15.283 1.00 61.86  ? 204 PHE D CA  1 
ATOM   6935  C  C   . PHE D  1 213 ? -16.060 -51.634 15.557 1.00 65.91  ? 204 PHE D C   1 
ATOM   6936  O  O   . PHE D  1 213 ? -16.529 -52.269 16.505 1.00 66.74  ? 204 PHE D O   1 
ATOM   6937  C  CB  . PHE D  1 213 ? -15.386 -49.209 15.763 1.00 64.31  ? 204 PHE D CB  1 
ATOM   6938  C  CG  . PHE D  1 213 ? -15.120 -49.276 17.246 1.00 61.06  ? 204 PHE D CG  1 
ATOM   6939  C  CD1 . PHE D  1 213 ? -13.913 -49.766 17.727 1.00 63.21  ? 204 PHE D CD1 1 
ATOM   6940  C  CD2 . PHE D  1 213 ? -16.081 -48.875 18.155 1.00 60.29  ? 204 PHE D CD2 1 
ATOM   6941  C  CE1 . PHE D  1 213 ? -13.669 -49.848 19.089 1.00 60.53  ? 204 PHE D CE1 1 
ATOM   6942  C  CE2 . PHE D  1 213 ? -15.846 -48.958 19.516 1.00 64.72  ? 204 PHE D CE2 1 
ATOM   6943  C  CZ  . PHE D  1 213 ? -14.637 -49.446 19.983 1.00 61.97  ? 204 PHE D CZ  1 
ATOM   6944  N  N   . ARG D  1 214 ? -15.176 -52.150 14.720 1.00 62.12  ? 205 ARG D N   1 
ATOM   6945  C  CA  . ARG D  1 214 ? -14.711 -53.504 14.886 1.00 69.38  ? 205 ARG D CA  1 
ATOM   6946  C  C   . ARG D  1 214 ? -13.226 -53.544 14.609 1.00 69.70  ? 205 ARG D C   1 
ATOM   6947  O  O   . ARG D  1 214 ? -12.681 -52.623 14.014 1.00 67.41  ? 205 ARG D O   1 
ATOM   6948  C  CB  . ARG D  1 214 ? -15.454 -54.449 13.939 1.00 73.78  ? 205 ARG D CB  1 
ATOM   6949  C  CG  . ARG D  1 214 ? -15.231 -54.186 12.459 1.00 72.59  ? 205 ARG D CG  1 
ATOM   6950  C  CD  . ARG D  1 214 ? -15.782 -55.338 11.646 1.00 79.72  ? 205 ARG D CD  1 
ATOM   6951  N  NE  . ARG D  1 214 ? -15.971 -54.999 10.238 1.00 84.88  ? 205 ARG D NE  1 
ATOM   6952  C  CZ  . ARG D  1 214 ? -17.096 -55.229 9.564  1.00 83.88  ? 205 ARG D CZ  1 
ATOM   6953  N  NH1 . ARG D  1 214 ? -18.126 -55.793 10.180 1.00 83.52  ? 205 ARG D NH1 1 
ATOM   6954  N  NH2 . ARG D  1 214 ? -17.194 -54.892 8.283  1.00 65.86  ? 205 ARG D NH2 1 
ATOM   6955  N  N   . GLU D  1 215 ? -12.577 -54.624 15.021 1.00 70.64  ? 206 GLU D N   1 
ATOM   6956  C  CA  . GLU D  1 215 ? -11.171 -54.803 14.728 1.00 65.64  ? 206 GLU D CA  1 
ATOM   6957  C  C   . GLU D  1 215 ? -11.077 -54.872 13.216 1.00 76.05  ? 206 GLU D C   1 
ATOM   6958  O  O   . GLU D  1 215 ? -12.069 -55.134 12.526 1.00 75.64  ? 206 GLU D O   1 
ATOM   6959  C  CB  . GLU D  1 215 ? -10.646 -56.106 15.338 1.00 70.37  ? 206 GLU D CB  1 
ATOM   6960  C  CG  . GLU D  1 215 ? -10.533 -56.122 16.868 1.00 87.47  ? 206 GLU D CG  1 
ATOM   6961  C  CD  . GLU D  1 215 ? -9.688  -57.288 17.379 1.00 94.80  ? 206 GLU D CD  1 
ATOM   6962  O  OE1 . GLU D  1 215 ? -9.296  -57.276 18.571 1.00 87.97  ? 206 GLU D OE1 1 
ATOM   6963  O  OE2 . GLU D  1 215 ? -9.417  -58.212 16.578 1.00 92.20  ? 206 GLU D OE2 1 
ATOM   6964  N  N   . ARG D  1 216 ? -9.903  -54.591 12.678 1.00 74.91  ? 207 ARG D N   1 
ATOM   6965  C  CA  . ARG D  1 216 ? -9.747  -54.650 11.231 1.00 74.84  ? 207 ARG D CA  1 
ATOM   6966  C  C   . ARG D  1 216 ? -8.545  -55.481 10.829 1.00 84.07  ? 207 ARG D C   1 
ATOM   6967  O  O   . ARG D  1 216 ? -8.555  -56.105 9.772  1.00 90.76  ? 207 ARG D O   1 
ATOM   6968  C  CB  . ARG D  1 216 ? -9.640  -53.245 10.648 1.00 71.25  ? 207 ARG D CB  1 
ATOM   6969  C  CG  . ARG D  1 216 ? -8.735  -53.130 9.451  1.00 61.52  ? 207 ARG D CG  1 
ATOM   6970  C  CD  . ARG D  1 216 ? -8.393  -51.675 9.162  1.00 61.57  ? 207 ARG D CD  1 
ATOM   6971  N  NE  . ARG D  1 216 ? -7.550  -51.558 7.976  1.00 80.11  ? 207 ARG D NE  1 
ATOM   6972  C  CZ  . ARG D  1 216 ? -6.233  -51.779 7.947  1.00 89.42  ? 207 ARG D CZ  1 
ATOM   6973  N  NH1 . ARG D  1 216 ? -5.582  -52.124 9.054  1.00 74.41  ? 207 ARG D NH1 1 
ATOM   6974  N  NH2 . ARG D  1 216 ? -5.560  -51.654 6.802  1.00 86.87  ? 207 ARG D NH2 1 
ATOM   6975  N  N   . LYS E  1 3   ? 42.153  -1.527  23.933 1.00 106.92 ? -6  LYS E N   1 
ATOM   6976  C  CA  . LYS E  1 3   ? 42.036  -2.553  24.964 1.00 109.29 ? -6  LYS E CA  1 
ATOM   6977  C  C   . LYS E  1 3   ? 41.106  -3.686  24.545 1.00 115.40 ? -6  LYS E C   1 
ATOM   6978  O  O   . LYS E  1 3   ? 40.049  -3.456  23.946 1.00 108.10 ? -6  LYS E O   1 
ATOM   6979  C  CB  . LYS E  1 3   ? 41.544  -1.960  26.281 1.00 98.51  ? -6  LYS E CB  1 
ATOM   6980  C  CG  . LYS E  1 3   ? 41.593  -2.957  27.405 1.00 104.07 ? -6  LYS E CG  1 
ATOM   6981  C  CD  . LYS E  1 3   ? 42.861  -3.781  27.273 1.00 109.59 ? -6  LYS E CD  1 
ATOM   6982  C  CE  . LYS E  1 3   ? 43.429  -4.172  28.617 1.00 108.02 ? -6  LYS E CE  1 
ATOM   6983  N  NZ  . LYS E  1 3   ? 44.828  -4.663  28.474 1.00 107.39 ? -6  LYS E NZ  1 
ATOM   6984  N  N   . ASP E  1 4   ? 41.508  -4.909  24.874 1.00 116.48 ? -5  ASP E N   1 
ATOM   6985  C  CA  . ASP E  1 4   ? 40.728  -6.089  24.530 1.00 115.58 ? -5  ASP E CA  1 
ATOM   6986  C  C   . ASP E  1 4   ? 39.385  -6.082  25.249 1.00 109.71 ? -5  ASP E C   1 
ATOM   6987  O  O   . ASP E  1 4   ? 38.347  -6.371  24.649 1.00 101.68 ? -5  ASP E O   1 
ATOM   6988  C  CB  . ASP E  1 4   ? 41.513  -7.355  24.875 1.00 118.71 ? -5  ASP E CB  1 
ATOM   6989  C  CG  . ASP E  1 4   ? 42.709  -7.559  23.966 1.00 123.13 ? -5  ASP E CG  1 
ATOM   6990  O  OD1 . ASP E  1 4   ? 42.721  -6.967  22.863 1.00 126.50 ? -5  ASP E OD1 1 
ATOM   6991  O  OD2 . ASP E  1 4   ? 43.630  -8.312  24.348 1.00 115.11 ? -5  ASP E OD2 1 
ATOM   6992  N  N   . ASP E  1 5   ? 39.420  -5.732  26.533 1.00 108.93 ? -4  ASP E N   1 
ATOM   6993  C  CA  . ASP E  1 5   ? 38.227  -5.703  27.376 1.00 102.93 ? -4  ASP E CA  1 
ATOM   6994  C  C   . ASP E  1 5   ? 37.182  -4.709  26.889 1.00 100.99 ? -4  ASP E C   1 
ATOM   6995  O  O   . ASP E  1 5   ? 35.987  -5.012  26.850 1.00 96.88  ? -4  ASP E O   1 
ATOM   6996  C  CB  . ASP E  1 5   ? 38.606  -5.363  28.815 1.00 102.05 ? -4  ASP E CB  1 
ATOM   6997  C  CG  . ASP E  1 5   ? 39.548  -6.375  29.417 1.00 108.15 ? -4  ASP E CG  1 
ATOM   6998  O  OD1 . ASP E  1 5   ? 39.072  -7.453  29.840 1.00 101.76 ? -4  ASP E OD1 1 
ATOM   6999  O  OD2 . ASP E  1 5   ? 40.763  -6.090  29.464 1.00 112.16 ? -4  ASP E OD2 1 
ATOM   7000  N  N   . ASP E  1 6   ? 37.636  -3.515  26.532 1.00 101.73 ? -3  ASP E N   1 
ATOM   7001  C  CA  . ASP E  1 6   ? 36.736  -2.473  26.057 1.00 96.24  ? -3  ASP E CA  1 
ATOM   7002  C  C   . ASP E  1 6   ? 35.938  -2.954  24.848 1.00 85.93  ? -3  ASP E C   1 
ATOM   7003  O  O   . ASP E  1 6   ? 34.788  -2.569  24.661 1.00 80.85  ? -3  ASP E O   1 
ATOM   7004  C  CB  . ASP E  1 6   ? 37.528  -1.211  25.721 1.00 94.22  ? -3  ASP E CB  1 
ATOM   7005  C  CG  . ASP E  1 6   ? 36.642  -0.048  25.355 1.00 82.25  ? -3  ASP E CG  1 
ATOM   7006  O  OD1 . ASP E  1 6   ? 37.130  0.861   24.658 1.00 85.21  ? -3  ASP E OD1 1 
ATOM   7007  O  OD2 . ASP E  1 6   ? 35.463  -0.040  25.756 1.00 78.22  ? -3  ASP E OD2 1 
ATOM   7008  N  N   . ASP E  1 7   ? 36.545  -3.809  24.036 1.00 84.22  ? -2  ASP E N   1 
ATOM   7009  C  CA  . ASP E  1 7   ? 35.861  -4.338  22.861 1.00 90.27  ? -2  ASP E CA  1 
ATOM   7010  C  C   . ASP E  1 7   ? 34.761  -5.314  23.258 1.00 83.77  ? -2  ASP E C   1 
ATOM   7011  O  O   . ASP E  1 7   ? 33.644  -5.250  22.741 1.00 76.23  ? -2  ASP E O   1 
ATOM   7012  C  CB  . ASP E  1 7   ? 36.859  -4.997  21.907 1.00 100.71 ? -2  ASP E CB  1 
ATOM   7013  C  CG  . ASP E  1 7   ? 37.855  -4.003  21.327 1.00 111.83 ? -2  ASP E CG  1 
ATOM   7014  O  OD1 . ASP E  1 7   ? 38.619  -4.386  20.419 1.00 116.11 ? -2  ASP E OD1 1 
ATOM   7015  O  OD2 . ASP E  1 7   ? 37.875  -2.836  21.773 1.00 116.02 ? -2  ASP E OD2 1 
ATOM   7016  N  N   . LYS E  1 8   ? 35.085  -6.210  24.185 1.00 87.51  ? -1  LYS E N   1 
ATOM   7017  C  CA  . LYS E  1 8   ? 34.108  -7.134  24.749 1.00 84.84  ? -1  LYS E CA  1 
ATOM   7018  C  C   . LYS E  1 8   ? 32.905  -6.371  25.313 1.00 81.08  ? -1  LYS E C   1 
ATOM   7019  O  O   . LYS E  1 8   ? 31.759  -6.811  25.212 1.00 82.88  ? -1  LYS E O   1 
ATOM   7020  C  CB  . LYS E  1 8   ? 34.767  -8.009  25.825 1.00 79.16  ? -1  LYS E CB  1 
ATOM   7021  C  CG  . LYS E  1 8   ? 35.780  -9.022  25.283 1.00 83.04  ? -1  LYS E CG  1 
ATOM   7022  C  CD  . LYS E  1 8   ? 36.339  -9.906  26.383 1.00 91.34  ? -1  LYS E CD  1 
ATOM   7023  C  CE  . LYS E  1 8   ? 37.131  -11.071 25.816 1.00 100.69 ? -1  LYS E CE  1 
ATOM   7024  N  NZ  . LYS E  1 8   ? 38.355  -10.623 25.101 1.00 92.55  ? -1  LYS E NZ  1 
ATOM   7025  N  N   . LEU E  1 9   ? 33.165  -5.184  25.835 1.00 80.57  ? 0   LEU E N   1 
ATOM   7026  C  CA  . LEU E  1 9   ? 32.139  -4.385  26.482 1.00 79.34  ? 0   LEU E CA  1 
ATOM   7027  C  C   . LEU E  1 9   ? 31.195  -3.822  25.427 1.00 78.23  ? 0   LEU E C   1 
ATOM   7028  O  O   . LEU E  1 9   ? 29.991  -4.088  25.466 1.00 75.89  ? 0   LEU E O   1 
ATOM   7029  C  CB  . LEU E  1 9   ? 32.780  -3.260  27.289 1.00 85.51  ? 0   LEU E CB  1 
ATOM   7030  C  CG  . LEU E  1 9   ? 32.064  -2.833  28.565 1.00 84.76  ? 0   LEU E CG  1 
ATOM   7031  C  CD1 . LEU E  1 9   ? 31.693  -4.054  29.387 1.00 76.35  ? 0   LEU E CD1 1 
ATOM   7032  C  CD2 . LEU E  1 9   ? 32.966  -1.910  29.347 1.00 89.33  ? 0   LEU E CD2 1 
ATOM   7033  N  N   . HIS E  1 10  ? 31.744  -3.007  24.525 1.00 74.69  ? 1   HIS E N   1 
ATOM   7034  C  CA  . HIS E  1 10  ? 31.005  -2.473  23.382 1.00 71.50  ? 1   HIS E CA  1 
ATOM   7035  C  C   . HIS E  1 10  ? 30.242  -3.551  22.620 1.00 69.60  ? 1   HIS E C   1 
ATOM   7036  O  O   . HIS E  1 10  ? 29.100  -3.343  22.218 1.00 67.89  ? 1   HIS E O   1 
ATOM   7037  C  CB  . HIS E  1 10  ? 31.955  -1.755  22.413 1.00 78.95  ? 1   HIS E CB  1 
ATOM   7038  C  CG  . HIS E  1 10  ? 32.485  -0.448  22.924 1.00 79.35  ? 1   HIS E CG  1 
ATOM   7039  N  ND1 . HIS E  1 10  ? 31.765  0.723   22.855 1.00 64.38  ? 1   HIS E ND1 1 
ATOM   7040  C  CD2 . HIS E  1 10  ? 33.672  -0.131  23.492 1.00 78.26  ? 1   HIS E CD2 1 
ATOM   7041  C  CE1 . HIS E  1 10  ? 32.481  1.705   23.374 1.00 73.77  ? 1   HIS E CE1 1 
ATOM   7042  N  NE2 . HIS E  1 10  ? 33.638  1.212   23.767 1.00 68.84  ? 1   HIS E NE2 1 
ATOM   7043  N  N   . SER E  1 11  ? 30.884  -4.696  22.409 1.00 73.81  ? 2   SER E N   1 
ATOM   7044  C  CA  . SER E  1 11  ? 30.242  -5.823  21.738 1.00 72.57  ? 2   SER E CA  1 
ATOM   7045  C  C   . SER E  1 11  ? 28.901  -6.162  22.383 1.00 69.77  ? 2   SER E C   1 
ATOM   7046  O  O   . SER E  1 11  ? 27.877  -6.214  21.707 1.00 66.29  ? 2   SER E O   1 
ATOM   7047  C  CB  . SER E  1 11  ? 31.159  -7.048  21.764 1.00 80.49  ? 2   SER E CB  1 
ATOM   7048  O  OG  . SER E  1 11  ? 30.416  -8.250  21.639 1.00 80.30  ? 2   SER E OG  1 
ATOM   7049  N  N   . GLN E  1 12  ? 28.924  -6.386  23.696 1.00 70.58  ? 3   GLN E N   1 
ATOM   7050  C  CA  . GLN E  1 12  ? 27.729  -6.710  24.468 1.00 66.17  ? 3   GLN E CA  1 
ATOM   7051  C  C   . GLN E  1 12  ? 26.640  -5.648  24.360 1.00 66.75  ? 3   GLN E C   1 
ATOM   7052  O  O   . GLN E  1 12  ? 25.507  -5.931  23.966 1.00 60.76  ? 3   GLN E O   1 
ATOM   7053  C  CB  . GLN E  1 12  ? 28.105  -6.870  25.937 1.00 70.54  ? 3   GLN E CB  1 
ATOM   7054  C  CG  . GLN E  1 12  ? 28.836  -8.145  26.255 1.00 72.73  ? 3   GLN E CG  1 
ATOM   7055  C  CD  . GLN E  1 12  ? 29.043  -8.329  27.742 1.00 76.78  ? 3   GLN E CD  1 
ATOM   7056  O  OE1 . GLN E  1 12  ? 29.103  -9.454  28.230 1.00 89.32  ? 3   GLN E OE1 1 
ATOM   7057  N  NE2 . GLN E  1 12  ? 29.153  -7.225  28.473 1.00 76.76  ? 3   GLN E NE2 1 
ATOM   7058  N  N   . ALA E  1 13  ? 26.996  -4.424  24.736 1.00 67.73  ? 4   ALA E N   1 
ATOM   7059  C  CA  . ALA E  1 13  ? 26.070  -3.305  24.704 1.00 64.81  ? 4   ALA E CA  1 
ATOM   7060  C  C   . ALA E  1 13  ? 25.407  -3.208  23.341 1.00 62.96  ? 4   ALA E C   1 
ATOM   7061  O  O   . ALA E  1 13  ? 24.203  -2.993  23.237 1.00 60.44  ? 4   ALA E O   1 
ATOM   7062  C  CB  . ALA E  1 13  ? 26.802  -2.016  25.034 1.00 46.46  ? 4   ALA E CB  1 
ATOM   7063  N  N   . ASN E  1 14  ? 26.213  -3.367  22.300 1.00 59.60  ? 5   ASN E N   1 
ATOM   7064  C  CA  . ASN E  1 14  ? 25.727  -3.351  20.930 1.00 67.52  ? 5   ASN E CA  1 
ATOM   7065  C  C   . ASN E  1 14  ? 24.593  -4.345  20.686 1.00 66.12  ? 5   ASN E C   1 
ATOM   7066  O  O   . ASN E  1 14  ? 23.539  -3.990  20.150 1.00 65.60  ? 5   ASN E O   1 
ATOM   7067  C  CB  . ASN E  1 14  ? 26.878  -3.646  19.972 1.00 67.70  ? 5   ASN E CB  1 
ATOM   7068  C  CG  . ASN E  1 14  ? 27.594  -2.396  19.514 1.00 68.56  ? 5   ASN E CG  1 
ATOM   7069  O  OD1 . ASN E  1 14  ? 26.993  -1.328  19.383 1.00 69.06  ? 5   ASN E OD1 1 
ATOM   7070  N  ND2 . ASN E  1 14  ? 28.888  -2.528  19.252 1.00 69.52  ? 5   ASN E ND2 1 
ATOM   7071  N  N   . LEU E  1 15  ? 24.835  -5.595  21.069 1.00 68.07  ? 6   LEU E N   1 
ATOM   7072  C  CA  . LEU E  1 15  ? 23.846  -6.667  20.984 1.00 66.38  ? 6   LEU E CA  1 
ATOM   7073  C  C   . LEU E  1 15  ? 22.575  -6.363  21.798 1.00 67.53  ? 6   LEU E C   1 
ATOM   7074  O  O   . LEU E  1 15  ? 21.458  -6.528  21.311 1.00 63.62  ? 6   LEU E O   1 
ATOM   7075  C  CB  . LEU E  1 15  ? 24.488  -7.987  21.430 1.00 61.87  ? 6   LEU E CB  1 
ATOM   7076  C  CG  . LEU E  1 15  ? 23.687  -9.287  21.433 1.00 51.56  ? 6   LEU E CG  1 
ATOM   7077  C  CD1 . LEU E  1 15  ? 22.991  -9.490  20.124 1.00 55.77  ? 6   LEU E CD1 1 
ATOM   7078  C  CD2 . LEU E  1 15  ? 24.610  -10.434 21.718 1.00 52.89  ? 6   LEU E CD2 1 
ATOM   7079  N  N   . MET E  1 16  ? 22.745  -5.909  23.036 1.00 67.88  ? 7   MET E N   1 
ATOM   7080  C  CA  . MET E  1 16  ? 21.601  -5.514  23.851 1.00 65.57  ? 7   MET E CA  1 
ATOM   7081  C  C   . MET E  1 16  ? 20.754  -4.421  23.184 1.00 62.74  ? 7   MET E C   1 
ATOM   7082  O  O   . MET E  1 16  ? 19.523  -4.493  23.163 1.00 61.85  ? 7   MET E O   1 
ATOM   7083  C  CB  . MET E  1 16  ? 22.072  -5.075  25.234 1.00 67.62  ? 7   MET E CB  1 
ATOM   7084  C  CG  . MET E  1 16  ? 22.563  -6.214  26.111 1.00 70.22  ? 7   MET E CG  1 
ATOM   7085  S  SD  . MET E  1 16  ? 23.101  -5.585  27.710 1.00 112.65 ? 7   MET E SD  1 
ATOM   7086  C  CE  . MET E  1 16  ? 23.794  -7.055  28.471 1.00 99.77  ? 7   MET E CE  1 
ATOM   7087  N  N   . ARG E  1 17  ? 21.432  -3.419  22.636 1.00 64.76  ? 8   ARG E N   1 
ATOM   7088  C  CA  . ARG E  1 17  ? 20.791  -2.318  21.928 1.00 67.11  ? 8   ARG E CA  1 
ATOM   7089  C  C   . ARG E  1 17  ? 20.054  -2.832  20.706 1.00 69.54  ? 8   ARG E C   1 
ATOM   7090  O  O   . ARG E  1 17  ? 18.974  -2.350  20.367 1.00 76.76  ? 8   ARG E O   1 
ATOM   7091  C  CB  . ARG E  1 17  ? 21.848  -1.296  21.498 1.00 65.54  ? 8   ARG E CB  1 
ATOM   7092  C  CG  . ARG E  1 17  ? 21.306  0.025   20.981 1.00 64.00  ? 8   ARG E CG  1 
ATOM   7093  C  CD  . ARG E  1 17  ? 22.416  1.061   20.958 1.00 62.27  ? 8   ARG E CD  1 
ATOM   7094  N  NE  . ARG E  1 17  ? 23.613  0.527   20.317 1.00 67.51  ? 8   ARG E NE  1 
ATOM   7095  C  CZ  . ARG E  1 17  ? 23.854  0.613   19.010 1.00 78.03  ? 8   ARG E CZ  1 
ATOM   7096  N  NH1 . ARG E  1 17  ? 22.981  1.220   18.215 1.00 68.01  ? 8   ARG E NH1 1 
ATOM   7097  N  NH2 . ARG E  1 17  ? 24.962  0.094   18.489 1.00 76.55  ? 8   ARG E NH2 1 
ATOM   7098  N  N   . LEU E  1 18  ? 20.655  -3.814  20.044 1.00 68.33  ? 9   LEU E N   1 
ATOM   7099  C  CA  . LEU E  1 18  ? 20.109  -4.376  18.815 1.00 65.26  ? 9   LEU E CA  1 
ATOM   7100  C  C   . LEU E  1 18  ? 18.835  -5.168  19.060 1.00 66.15  ? 9   LEU E C   1 
ATOM   7101  O  O   . LEU E  1 18  ? 17.861  -5.032  18.324 1.00 63.57  ? 9   LEU E O   1 
ATOM   7102  C  CB  . LEU E  1 18  ? 21.151  -5.269  18.166 1.00 61.38  ? 9   LEU E CB  1 
ATOM   7103  C  CG  . LEU E  1 18  ? 20.656  -6.175  17.059 1.00 58.94  ? 9   LEU E CG  1 
ATOM   7104  C  CD1 . LEU E  1 18  ? 20.132  -5.342  15.908 1.00 58.38  ? 9   LEU E CD1 1 
ATOM   7105  C  CD2 . LEU E  1 18  ? 21.792  -7.079  16.625 1.00 63.99  ? 9   LEU E CD2 1 
ATOM   7106  N  N   . LYS E  1 19  ? 18.858  -6.003  20.095 1.00 69.51  ? 10  LYS E N   1 
ATOM   7107  C  CA  . LYS E  1 19  ? 17.695  -6.783  20.486 1.00 68.83  ? 10  LYS E CA  1 
ATOM   7108  C  C   . LYS E  1 19  ? 16.638  -5.839  21.005 1.00 72.66  ? 10  LYS E C   1 
ATOM   7109  O  O   . LYS E  1 19  ? 15.456  -6.020  20.738 1.00 76.28  ? 10  LYS E O   1 
ATOM   7110  C  CB  . LYS E  1 19  ? 18.058  -7.807  21.561 1.00 70.01  ? 10  LYS E CB  1 
ATOM   7111  C  CG  . LYS E  1 19  ? 19.046  -8.860  21.092 1.00 68.60  ? 10  LYS E CG  1 
ATOM   7112  C  CD  . LYS E  1 19  ? 19.388  -9.849  22.187 1.00 68.15  ? 10  LYS E CD  1 
ATOM   7113  C  CE  . LYS E  1 19  ? 18.421  -11.020 22.211 1.00 67.40  ? 10  LYS E CE  1 
ATOM   7114  N  NZ  . LYS E  1 19  ? 18.944  -12.163 23.029 1.00 71.14  ? 10  LYS E NZ  1 
ATOM   7115  N  N   . SER E  1 20  ? 17.079  -4.821  21.740 1.00 74.81  ? 11  SER E N   1 
ATOM   7116  C  CA  . SER E  1 20  ? 16.194  -3.771  22.246 1.00 83.94  ? 11  SER E CA  1 
ATOM   7117  C  C   . SER E  1 20  ? 15.452  -3.009  21.139 1.00 80.47  ? 11  SER E C   1 
ATOM   7118  O  O   . SER E  1 20  ? 14.242  -2.784  21.233 1.00 83.14  ? 11  SER E O   1 
ATOM   7119  C  CB  . SER E  1 20  ? 16.974  -2.786  23.116 1.00 83.89  ? 11  SER E CB  1 
ATOM   7120  O  OG  . SER E  1 20  ? 16.089  -1.912  23.799 1.00 89.69  ? 11  SER E OG  1 
ATOM   7121  N  N   . ASP E  1 21  ? 16.161  -2.630  20.088 1.00 74.18  ? 12  ASP E N   1 
ATOM   7122  C  CA  . ASP E  1 21  ? 15.520  -1.988  18.945 1.00 77.84  ? 12  ASP E CA  1 
ATOM   7123  C  C   . ASP E  1 21  ? 14.398  -2.839  18.339 1.00 85.74  ? 12  ASP E C   1 
ATOM   7124  O  O   . ASP E  1 21  ? 13.270  -2.369  18.198 1.00 91.51  ? 12  ASP E O   1 
ATOM   7125  C  CB  . ASP E  1 21  ? 16.561  -1.644  17.885 1.00 76.82  ? 12  ASP E CB  1 
ATOM   7126  C  CG  . ASP E  1 21  ? 17.207  -0.287  18.107 1.00 81.41  ? 12  ASP E CG  1 
ATOM   7127  O  OD1 . ASP E  1 21  ? 16.847  0.390   19.092 1.00 84.90  ? 12  ASP E OD1 1 
ATOM   7128  O  OD2 . ASP E  1 21  ? 18.071  0.111   17.306 1.00 84.72  ? 12  ASP E OD2 1 
ATOM   7129  N  N   . LEU E  1 22  ? 14.696  -4.108  18.038 1.00 78.53  ? 13  LEU E N   1 
ATOM   7130  C  CA  . LEU E  1 22  ? 13.705  -5.032  17.497 1.00 70.32  ? 13  LEU E CA  1 
ATOM   7131  C  C   . LEU E  1 22  ? 12.536  -5.385  18.446 1.00 81.94  ? 13  LEU E C   1 
ATOM   7132  O  O   . LEU E  1 22  ? 11.378  -5.166  18.103 1.00 83.85  ? 13  LEU E O   1 
ATOM   7133  C  CB  . LEU E  1 22  ? 14.416  -6.304  17.050 1.00 74.46  ? 13  LEU E CB  1 
ATOM   7134  C  CG  . LEU E  1 22  ? 15.641  -6.134  16.142 1.00 65.58  ? 13  LEU E CG  1 
ATOM   7135  C  CD1 . LEU E  1 22  ? 16.507  -7.389  16.076 1.00 55.59  ? 13  LEU E CD1 1 
ATOM   7136  C  CD2 . LEU E  1 22  ? 15.205  -5.738  14.752 1.00 65.81  ? 13  LEU E CD2 1 
ATOM   7137  N  N   . PHE E  1 23  ? 12.864  -6.059  19.561 1.00 88.21  ? 14  PHE E N   1 
ATOM   7138  C  CA  . PHE E  1 23  ? 11.899  -6.531  20.588 1.00 89.15  ? 14  PHE E CA  1 
ATOM   7139  C  C   . PHE E  1 23  ? 11.148  -5.562  21.541 1.00 87.66  ? 14  PHE E C   1 
ATOM   7140  O  O   . PHE E  1 23  ? 9.931   -5.670  21.691 1.00 92.38  ? 14  PHE E O   1 
ATOM   7141  C  CB  . PHE E  1 23  ? 12.548  -7.640  21.426 1.00 84.72  ? 14  PHE E CB  1 
ATOM   7142  C  CG  . PHE E  1 23  ? 13.138  -8.753  20.607 1.00 84.72  ? 14  PHE E CG  1 
ATOM   7143  C  CD1 . PHE E  1 23  ? 12.507  -9.192  19.455 1.00 80.41  ? 14  PHE E CD1 1 
ATOM   7144  C  CD2 . PHE E  1 23  ? 14.323  -9.359  20.988 1.00 81.07  ? 14  PHE E CD2 1 
ATOM   7145  C  CE1 . PHE E  1 23  ? 13.047  -10.215 18.699 1.00 76.43  ? 14  PHE E CE1 1 
ATOM   7146  C  CE2 . PHE E  1 23  ? 14.868  -10.382 20.236 1.00 80.50  ? 14  PHE E CE2 1 
ATOM   7147  C  CZ  . PHE E  1 23  ? 14.229  -10.811 19.090 1.00 82.31  ? 14  PHE E CZ  1 
ATOM   7148  N  N   . ASN E  1 24  ? 11.860  -4.620  22.163 1.00 96.53  ? 15  ASN E N   1 
ATOM   7149  C  CA  . ASN E  1 24  ? 11.242  -3.603  23.019 1.00 110.47 ? 15  ASN E CA  1 
ATOM   7150  C  C   . ASN E  1 24  ? 10.540  -2.482  22.235 1.00 112.47 ? 15  ASN E C   1 
ATOM   7151  O  O   . ASN E  1 24  ? 9.414   -2.097  22.566 1.00 113.59 ? 15  ASN E O   1 
ATOM   7152  C  CB  . ASN E  1 24  ? 12.252  -2.985  24.007 1.00 112.11 ? 15  ASN E CB  1 
ATOM   7153  C  CG  . ASN E  1 24  ? 12.784  -3.992  25.030 1.00 115.54 ? 15  ASN E CG  1 
ATOM   7154  O  OD1 . ASN E  1 24  ? 12.169  -5.031  25.287 1.00 118.07 ? 15  ASN E OD1 1 
ATOM   7155  N  ND2 . ASN E  1 24  ? 13.933  -3.678  25.619 1.00 108.42 ? 15  ASN E ND2 1 
ATOM   7156  N  N   . ARG E  1 25  ? 11.217  -1.956  21.210 1.00 112.44 ? 16  ARG E N   1 
ATOM   7157  C  CA  . ARG E  1 25  ? 10.783  -0.726  20.522 1.00 113.61 ? 16  ARG E CA  1 
ATOM   7158  C  C   . ARG E  1 25  ? 9.678   -0.931  19.501 1.00 113.07 ? 16  ARG E C   1 
ATOM   7159  O  O   . ARG E  1 25  ? 8.850   -0.051  19.291 1.00 117.89 ? 16  ARG E O   1 
ATOM   7160  C  CB  . ARG E  1 25  ? 11.951  -0.044  19.825 1.00 110.34 ? 16  ARG E CB  1 
ATOM   7161  C  CG  . ARG E  1 25  ? 13.213  0.045   20.647 1.00 109.27 ? 16  ARG E CG  1 
ATOM   7162  C  CD  . ARG E  1 25  ? 14.225  0.858   19.885 1.00 105.75 ? 16  ARG E CD  1 
ATOM   7163  N  NE  . ARG E  1 25  ? 13.691  2.181   19.615 1.00 108.72 ? 16  ARG E NE  1 
ATOM   7164  C  CZ  . ARG E  1 25  ? 14.376  3.174   19.062 1.00 111.34 ? 16  ARG E CZ  1 
ATOM   7165  N  NH1 . ARG E  1 25  ? 15.656  3.010   18.717 1.00 110.79 ? 16  ARG E NH1 1 
ATOM   7166  N  NH2 . ARG E  1 25  ? 13.770  4.335   18.867 1.00 96.20  ? 16  ARG E NH2 1 
ATOM   7167  N  N   . SER E  1 26  ? 9.657   -2.094  18.869 1.00 111.13 ? 17  SER E N   1 
ATOM   7168  C  CA  . SER E  1 26  ? 8.584   -2.379  17.937 1.00 118.00 ? 17  SER E CA  1 
ATOM   7169  C  C   . SER E  1 26  ? 7.774   -3.523  18.528 1.00 118.59 ? 17  SER E C   1 
ATOM   7170  O  O   . SER E  1 26  ? 8.319   -4.383  19.228 1.00 108.77 ? 17  SER E O   1 
ATOM   7171  C  CB  . SER E  1 26  ? 9.132   -2.757  16.558 1.00 112.01 ? 17  SER E CB  1 
ATOM   7172  O  OG  . SER E  1 26  ? 9.488   -1.611  15.814 1.00 99.29  ? 17  SER E OG  1 
ATOM   7173  N  N   . PRO E  1 27  ? 6.457   -3.505  18.282 1.00 119.86 ? 18  PRO E N   1 
ATOM   7174  C  CA  . PRO E  1 27  ? 5.501   -4.523  18.735 1.00 111.73 ? 18  PRO E CA  1 
ATOM   7175  C  C   . PRO E  1 27  ? 5.718   -5.814  17.972 1.00 107.82 ? 18  PRO E C   1 
ATOM   7176  O  O   . PRO E  1 27  ? 5.958   -5.745  16.762 1.00 103.42 ? 18  PRO E O   1 
ATOM   7177  C  CB  . PRO E  1 27  ? 4.143   -3.913  18.373 1.00 109.99 ? 18  PRO E CB  1 
ATOM   7178  C  CG  . PRO E  1 27  ? 4.439   -2.910  17.313 1.00 115.18 ? 18  PRO E CG  1 
ATOM   7179  C  CD  . PRO E  1 27  ? 5.798   -2.373  17.613 1.00 113.25 ? 18  PRO E CD  1 
ATOM   7180  N  N   . MET E  1 28  ? 5.642   -6.960  18.651 1.00 101.55 ? 19  MET E N   1 
ATOM   7181  C  CA  . MET E  1 28  ? 5.934   -8.226  17.987 1.00 94.94  ? 19  MET E CA  1 
ATOM   7182  C  C   . MET E  1 28  ? 4.998   -8.448  16.798 1.00 100.58 ? 19  MET E C   1 
ATOM   7183  O  O   . MET E  1 28  ? 3.815   -8.106  16.852 1.00 97.38  ? 19  MET E O   1 
ATOM   7184  C  CB  . MET E  1 28  ? 5.873   -9.422  18.942 1.00 92.65  ? 19  MET E CB  1 
ATOM   7185  C  CG  . MET E  1 28  ? 6.219   -10.745 18.237 1.00 88.77  ? 19  MET E CG  1 
ATOM   7186  S  SD  . MET E  1 28  ? 5.846   -12.247 19.170 1.00 97.17  ? 19  MET E SD  1 
ATOM   7187  C  CE  . MET E  1 28  ? 7.247   -12.373 20.287 1.00 67.07  ? 19  MET E CE  1 
ATOM   7188  N  N   . TYR E  1 29  ? 5.555   -9.031  15.737 1.00 94.57  ? 20  TYR E N   1 
ATOM   7189  C  CA  . TYR E  1 29  ? 4.871   -9.288  14.467 1.00 84.39  ? 20  TYR E CA  1 
ATOM   7190  C  C   . TYR E  1 29  ? 3.535   -10.048 14.672 1.00 83.26  ? 20  TYR E C   1 
ATOM   7191  O  O   . TYR E  1 29  ? 3.492   -11.082 15.349 1.00 79.61  ? 20  TYR E O   1 
ATOM   7192  C  CB  . TYR E  1 29  ? 5.880   -10.013 13.551 1.00 75.75  ? 20  TYR E CB  1 
ATOM   7193  C  CG  . TYR E  1 29  ? 5.377   -10.703 12.302 1.00 69.78  ? 20  TYR E CG  1 
ATOM   7194  C  CD1 . TYR E  1 29  ? 5.337   -10.043 11.081 1.00 70.45  ? 20  TYR E CD1 1 
ATOM   7195  C  CD2 . TYR E  1 29  ? 5.018   -12.045 12.330 1.00 67.98  ? 20  TYR E CD2 1 
ATOM   7196  C  CE1 . TYR E  1 29  ? 4.904   -10.695 9.937  1.00 73.43  ? 20  TYR E CE1 1 
ATOM   7197  C  CE2 . TYR E  1 29  ? 4.585   -12.701 11.196 1.00 63.81  ? 20  TYR E CE2 1 
ATOM   7198  C  CZ  . TYR E  1 29  ? 4.528   -12.030 10.007 1.00 68.20  ? 20  TYR E CZ  1 
ATOM   7199  O  OH  . TYR E  1 29  ? 4.097   -12.709 8.891  1.00 73.09  ? 20  TYR E OH  1 
ATOM   7200  N  N   . PRO E  1 30  ? 2.433   -9.493  14.123 1.00 76.67  ? 21  PRO E N   1 
ATOM   7201  C  CA  . PRO E  1 30  ? 1.038   -9.919  14.321 1.00 67.45  ? 21  PRO E CA  1 
ATOM   7202  C  C   . PRO E  1 30  ? 0.710   -11.256 13.693 1.00 66.57  ? 21  PRO E C   1 
ATOM   7203  O  O   . PRO E  1 30  ? -0.356  -11.806 13.963 1.00 67.96  ? 21  PRO E O   1 
ATOM   7204  C  CB  . PRO E  1 30  ? 0.237   -8.815  13.646 1.00 63.71  ? 21  PRO E CB  1 
ATOM   7205  C  CG  . PRO E  1 30  ? 1.146   -8.313  12.588 1.00 68.85  ? 21  PRO E CG  1 
ATOM   7206  C  CD  . PRO E  1 30  ? 2.527   -8.387  13.153 1.00 69.99  ? 21  PRO E CD  1 
ATOM   7207  N  N   . GLY E  1 31  ? 1.592   -11.735 12.821 1.00 68.38  ? 22  GLY E N   1 
ATOM   7208  C  CA  . GLY E  1 31  ? 1.333   -12.918 12.013 1.00 71.31  ? 22  GLY E CA  1 
ATOM   7209  C  C   . GLY E  1 31  ? 1.101   -12.567 10.553 1.00 64.71  ? 22  GLY E C   1 
ATOM   7210  O  O   . GLY E  1 31  ? 0.790   -11.429 10.225 1.00 65.77  ? 22  GLY E O   1 
ATOM   7211  N  N   . PRO E  1 32  ? 1.272   -13.542 9.658  1.00 60.58  ? 23  PRO E N   1 
ATOM   7212  C  CA  . PRO E  1 32  ? 1.105   -13.295 8.225  1.00 60.01  ? 23  PRO E CA  1 
ATOM   7213  C  C   . PRO E  1 32  ? -0.335  -12.978 7.871  1.00 65.06  ? 23  PRO E C   1 
ATOM   7214  O  O   . PRO E  1 32  ? -1.260  -13.373 8.583  1.00 66.42  ? 23  PRO E O   1 
ATOM   7215  C  CB  . PRO E  1 32  ? 1.491   -14.633 7.595  1.00 64.68  ? 23  PRO E CB  1 
ATOM   7216  C  CG  . PRO E  1 32  ? 2.313   -15.315 8.600  1.00 62.11  ? 23  PRO E CG  1 
ATOM   7217  C  CD  . PRO E  1 32  ? 1.758   -14.900 9.927  1.00 64.01  ? 23  PRO E CD  1 
ATOM   7218  N  N   . THR E  1 33  ? -0.519  -12.264 6.769  1.00 66.27  ? 24  THR E N   1 
ATOM   7219  C  CA  . THR E  1 33  ? -1.845  -12.040 6.221  1.00 67.03  ? 24  THR E CA  1 
ATOM   7220  C  C   . THR E  1 33  ? -1.837  -12.368 4.724  1.00 67.48  ? 24  THR E C   1 
ATOM   7221  O  O   . THR E  1 33  ? -0.807  -12.763 4.170  1.00 67.22  ? 24  THR E O   1 
ATOM   7222  C  CB  . THR E  1 33  ? -2.337  -10.597 6.493  1.00 73.96  ? 24  THR E CB  1 
ATOM   7223  O  OG1 . THR E  1 33  ? -1.254  -9.674  6.325  1.00 75.13  ? 24  THR E OG1 1 
ATOM   7224  C  CG2 . THR E  1 33  ? -2.848  -10.477 7.931  1.00 72.50  ? 24  THR E CG2 1 
ATOM   7225  N  N   . LYS E  1 34  ? -2.991  -12.231 4.080  1.00 74.66  ? 25  LYS E N   1 
ATOM   7226  C  CA  . LYS E  1 34  ? -3.101  -12.444 2.638  1.00 68.67  ? 25  LYS E CA  1 
ATOM   7227  C  C   . LYS E  1 34  ? -2.366  -11.328 1.911  1.00 68.28  ? 25  LYS E C   1 
ATOM   7228  O  O   . LYS E  1 34  ? -1.760  -11.548 0.861  1.00 64.47  ? 25  LYS E O   1 
ATOM   7229  C  CB  . LYS E  1 34  ? -4.571  -12.509 2.210  1.00 55.44  ? 25  LYS E CB  1 
ATOM   7230  C  CG  . LYS E  1 34  ? -5.345  -11.225 2.384  1.00 57.59  ? 25  LYS E CG  1 
ATOM   7231  C  CD  . LYS E  1 34  ? -6.850  -11.463 2.254  1.00 66.96  ? 25  LYS E CD  1 
ATOM   7232  C  CE  . LYS E  1 34  ? -7.611  -10.146 2.033  1.00 76.43  ? 25  LYS E CE  1 
ATOM   7233  N  NZ  . LYS E  1 34  ? -8.253  -9.610  3.269  1.00 69.35  ? 25  LYS E NZ  1 
ATOM   7234  N  N   . ASP E  1 35  ? -2.404  -10.140 2.509  1.00 70.40  ? 26  ASP E N   1 
ATOM   7235  C  CA  . ASP E  1 35  ? -1.780  -8.947  1.951  1.00 69.35  ? 26  ASP E CA  1 
ATOM   7236  C  C   . ASP E  1 35  ? -0.295  -8.907  2.262  1.00 68.06  ? 26  ASP E C   1 
ATOM   7237  O  O   . ASP E  1 35  ? 0.444   -8.070  1.732  1.00 67.15  ? 26  ASP E O   1 
ATOM   7238  C  CB  . ASP E  1 35  ? -2.468  -7.688  2.488  1.00 72.45  ? 26  ASP E CB  1 
ATOM   7239  C  CG  . ASP E  1 35  ? -3.802  -7.415  1.806  1.00 81.86  ? 26  ASP E CG  1 
ATOM   7240  O  OD1 . ASP E  1 35  ? -3.851  -7.505  0.561  1.00 84.89  ? 26  ASP E OD1 1 
ATOM   7241  O  OD2 . ASP E  1 35  ? -4.801  -7.116  2.503  1.00 76.17  ? 26  ASP E OD2 1 
ATOM   7242  N  N   . ASP E  1 36  ? 0.126   -9.793  3.157  1.00 65.66  ? 27  ASP E N   1 
ATOM   7243  C  CA  . ASP E  1 36  ? 1.526   -9.914  3.523  1.00 63.67  ? 27  ASP E CA  1 
ATOM   7244  C  C   . ASP E  1 36  ? 1.881   -11.376 3.768  1.00 64.79  ? 27  ASP E C   1 
ATOM   7245  O  O   . ASP E  1 36  ? 2.033   -11.797 4.910  1.00 61.83  ? 27  ASP E O   1 
ATOM   7246  C  CB  . ASP E  1 36  ? 1.814   -9.068  4.761  1.00 69.00  ? 27  ASP E CB  1 
ATOM   7247  C  CG  . ASP E  1 36  ? 3.277   -9.043  5.120  1.00 78.89  ? 27  ASP E CG  1 
ATOM   7248  O  OD1 . ASP E  1 36  ? 4.106   -9.320  4.226  1.00 82.03  ? 27  ASP E OD1 1 
ATOM   7249  O  OD2 . ASP E  1 36  ? 3.595   -8.752  6.295  1.00 77.45  ? 27  ASP E OD2 1 
ATOM   7250  N  N   . PRO E  1 37  ? 2.007   -12.162 2.692  1.00 67.30  ? 28  PRO E N   1 
ATOM   7251  C  CA  . PRO E  1 37  ? 2.222   -13.608 2.817  1.00 61.72  ? 28  PRO E CA  1 
ATOM   7252  C  C   . PRO E  1 37  ? 3.599   -13.938 3.385  1.00 59.06  ? 28  PRO E C   1 
ATOM   7253  O  O   . PRO E  1 37  ? 4.519   -13.127 3.272  1.00 60.95  ? 28  PRO E O   1 
ATOM   7254  C  CB  . PRO E  1 37  ? 2.148   -14.095 1.367  1.00 53.88  ? 28  PRO E CB  1 
ATOM   7255  C  CG  . PRO E  1 37  ? 1.532   -12.979 0.602  1.00 64.81  ? 28  PRO E CG  1 
ATOM   7256  C  CD  . PRO E  1 37  ? 1.952   -11.738 1.286  1.00 63.36  ? 28  PRO E CD  1 
ATOM   7257  N  N   . LEU E  1 38  ? 3.733   -15.122 3.976  1.00 49.90  ? 29  LEU E N   1 
ATOM   7258  C  CA  . LEU E  1 38  ? 5.030   -15.604 4.432  1.00 53.78  ? 29  LEU E CA  1 
ATOM   7259  C  C   . LEU E  1 38  ? 5.386   -16.981 3.869  1.00 60.07  ? 29  LEU E C   1 
ATOM   7260  O  O   . LEU E  1 38  ? 4.534   -17.871 3.751  1.00 60.31  ? 29  LEU E O   1 
ATOM   7261  C  CB  . LEU E  1 38  ? 5.079   -15.650 5.954  1.00 63.88  ? 29  LEU E CB  1 
ATOM   7262  C  CG  . LEU E  1 38  ? 6.440   -16.008 6.537  1.00 62.30  ? 29  LEU E CG  1 
ATOM   7263  C  CD1 . LEU E  1 38  ? 7.439   -14.906 6.233  1.00 62.61  ? 29  LEU E CD1 1 
ATOM   7264  C  CD2 . LEU E  1 38  ? 6.319   -16.237 8.024  1.00 61.21  ? 29  LEU E CD2 1 
ATOM   7265  N  N   . THR E  1 39  ? 6.656   -17.149 3.522  1.00 54.78  ? 30  THR E N   1 
ATOM   7266  C  CA  . THR E  1 39  ? 7.148   -18.427 3.039  1.00 60.22  ? 30  THR E CA  1 
ATOM   7267  C  C   . THR E  1 39  ? 7.999   -19.070 4.117  1.00 63.99  ? 30  THR E C   1 
ATOM   7268  O  O   . THR E  1 39  ? 8.960   -18.462 4.593  1.00 63.80  ? 30  THR E O   1 
ATOM   7269  C  CB  . THR E  1 39  ? 8.013   -18.267 1.774  1.00 58.84  ? 30  THR E CB  1 
ATOM   7270  O  OG1 . THR E  1 39  ? 7.166   -18.145 0.632  1.00 67.48  ? 30  THR E OG1 1 
ATOM   7271  C  CG2 . THR E  1 39  ? 8.923   -19.471 1.581  1.00 60.59  ? 30  THR E CG2 1 
ATOM   7272  N  N   . VAL E  1 40  ? 7.637   -20.300 4.482  1.00 57.39  ? 31  VAL E N   1 
ATOM   7273  C  CA  . VAL E  1 40  ? 8.370   -21.095 5.450  1.00 51.94  ? 31  VAL E CA  1 
ATOM   7274  C  C   . VAL E  1 40  ? 9.008   -22.278 4.764  1.00 54.91  ? 31  VAL E C   1 
ATOM   7275  O  O   . VAL E  1 40  ? 8.317   -23.055 4.119  1.00 55.87  ? 31  VAL E O   1 
ATOM   7276  C  CB  . VAL E  1 40  ? 7.424   -21.689 6.486  1.00 58.71  ? 31  VAL E CB  1 
ATOM   7277  C  CG1 . VAL E  1 40  ? 8.220   -22.435 7.545  1.00 55.24  ? 31  VAL E CG1 1 
ATOM   7278  C  CG2 . VAL E  1 40  ? 6.567   -20.606 7.107  1.00 60.14  ? 31  VAL E CG2 1 
ATOM   7279  N  N   . TYR E  1 41  ? 10.318  -22.430 4.924  1.00 60.10  ? 32  TYR E N   1 
ATOM   7280  C  CA  . TYR E  1 41  ? 11.031  -23.594 4.404  1.00 58.75  ? 32  TYR E CA  1 
ATOM   7281  C  C   . TYR E  1 41  ? 11.176  -24.672 5.475  1.00 56.98  ? 32  TYR E C   1 
ATOM   7282  O  O   . TYR E  1 41  ? 11.729  -24.414 6.530  1.00 57.14  ? 32  TYR E O   1 
ATOM   7283  C  CB  . TYR E  1 41  ? 12.409  -23.186 3.873  1.00 63.39  ? 32  TYR E CB  1 
ATOM   7284  C  CG  . TYR E  1 41  ? 12.358  -22.346 2.605  1.00 72.09  ? 32  TYR E CG  1 
ATOM   7285  C  CD1 . TYR E  1 41  ? 12.414  -22.958 1.346  1.00 78.32  ? 32  TYR E CD1 1 
ATOM   7286  C  CD2 . TYR E  1 41  ? 12.245  -20.945 2.659  1.00 58.97  ? 32  TYR E CD2 1 
ATOM   7287  C  CE1 . TYR E  1 41  ? 12.359  -22.209 0.174  1.00 78.73  ? 32  TYR E CE1 1 
ATOM   7288  C  CE2 . TYR E  1 41  ? 12.193  -20.182 1.496  1.00 72.07  ? 32  TYR E CE2 1 
ATOM   7289  C  CZ  . TYR E  1 41  ? 12.250  -20.825 0.251  1.00 87.72  ? 32  TYR E CZ  1 
ATOM   7290  O  OH  . TYR E  1 41  ? 12.198  -20.111 -0.932 1.00 75.97  ? 32  TYR E OH  1 
ATOM   7291  N  N   . LEU E  1 42  ? 10.654  -25.869 5.209  1.00 62.77  ? 33  LEU E N   1 
ATOM   7292  C  CA  . LEU E  1 42  ? 10.842  -27.009 6.100  1.00 63.55  ? 33  LEU E CA  1 
ATOM   7293  C  C   . LEU E  1 42  ? 11.958  -27.909 5.591  1.00 68.29  ? 33  LEU E C   1 
ATOM   7294  O  O   . LEU E  1 42  ? 12.404  -27.778 4.453  1.00 74.99  ? 33  LEU E O   1 
ATOM   7295  C  CB  . LEU E  1 42  ? 9.575   -27.863 6.128  1.00 56.18  ? 33  LEU E CB  1 
ATOM   7296  C  CG  . LEU E  1 42  ? 8.323   -27.403 6.850  1.00 54.95  ? 33  LEU E CG  1 
ATOM   7297  C  CD1 . LEU E  1 42  ? 7.375   -28.578 6.983  1.00 52.55  ? 33  LEU E CD1 1 
ATOM   7298  C  CD2 . LEU E  1 42  ? 8.694   -26.874 8.208  1.00 56.04  ? 33  LEU E CD2 1 
ATOM   7299  N  N   . SER E  1 43  ? 12.306  -28.913 6.383  1.00 65.16  ? 34  SER E N   1 
ATOM   7300  C  CA  . SER E  1 43  ? 13.301  -29.899 5.986  1.00 67.14  ? 34  SER E CA  1 
ATOM   7301  C  C   . SER E  1 43  ? 13.429  -30.886 7.147  1.00 65.57  ? 34  SER E C   1 
ATOM   7302  O  O   . SER E  1 43  ? 13.167  -30.516 8.286  1.00 65.21  ? 34  SER E O   1 
ATOM   7303  C  CB  . SER E  1 43  ? 14.635  -29.173 5.754  1.00 65.21  ? 34  SER E CB  1 
ATOM   7304  O  OG  . SER E  1 43  ? 15.514  -29.922 4.933  1.00 69.63  ? 34  SER E OG  1 
ATOM   7305  N  N   . PHE E  1 44  ? 13.908  -32.102 6.898  1.00 62.32  ? 35  PHE E N   1 
ATOM   7306  C  CA  . PHE E  1 44  ? 13.968  -33.101 7.971  1.00 53.54  ? 35  PHE E CA  1 
ATOM   7307  C  C   . PHE E  1 44  ? 15.273  -33.859 7.992  1.00 54.46  ? 35  PHE E C   1 
ATOM   7308  O  O   . PHE E  1 44  ? 15.865  -34.153 6.965  1.00 58.67  ? 35  PHE E O   1 
ATOM   7309  C  CB  . PHE E  1 44  ? 12.786  -34.061 7.926  1.00 44.71  ? 35  PHE E CB  1 
ATOM   7310  C  CG  . PHE E  1 44  ? 11.456  -33.384 8.072  1.00 49.82  ? 35  PHE E CG  1 
ATOM   7311  C  CD1 . PHE E  1 44  ? 10.789  -33.398 9.272  1.00 53.78  ? 35  PHE E CD1 1 
ATOM   7312  C  CD2 . PHE E  1 44  ? 10.871  -32.727 7.005  1.00 58.40  ? 35  PHE E CD2 1 
ATOM   7313  C  CE1 . PHE E  1 44  ? 9.561   -32.781 9.417  1.00 53.77  ? 35  PHE E CE1 1 
ATOM   7314  C  CE2 . PHE E  1 44  ? 9.638   -32.105 7.140  1.00 58.18  ? 35  PHE E CE2 1 
ATOM   7315  C  CZ  . PHE E  1 44  ? 8.987   -32.133 8.352  1.00 58.80  ? 35  PHE E CZ  1 
ATOM   7316  N  N   . SER E  1 45  ? 15.734  -34.137 9.194  1.00 55.79  ? 36  SER E N   1 
ATOM   7317  C  CA  . SER E  1 45  ? 16.982  -34.836 9.392  1.00 60.31  ? 36  SER E CA  1 
ATOM   7318  C  C   . SER E  1 45  ? 16.623  -35.974 10.327 1.00 68.00  ? 36  SER E C   1 
ATOM   7319  O  O   . SER E  1 45  ? 16.149  -35.737 11.444 1.00 65.40  ? 36  SER E O   1 
ATOM   7320  C  CB  . SER E  1 45  ? 18.018  -33.902 10.023 1.00 63.24  ? 36  SER E CB  1 
ATOM   7321  O  OG  . SER E  1 45  ? 19.324  -34.448 9.962  1.00 68.34  ? 36  SER E OG  1 
ATOM   7322  N  N   . LEU E  1 46  ? 16.807  -37.207 9.855  1.00 68.92  ? 37  LEU E N   1 
ATOM   7323  C  CA  . LEU E  1 46  ? 16.397  -38.381 10.613 1.00 57.24  ? 37  LEU E CA  1 
ATOM   7324  C  C   . LEU E  1 46  ? 17.468  -38.971 11.501 1.00 64.73  ? 37  LEU E C   1 
ATOM   7325  O  O   . LEU E  1 46  ? 18.632  -39.123 11.099 1.00 65.60  ? 37  LEU E O   1 
ATOM   7326  C  CB  . LEU E  1 46  ? 15.822  -39.451 9.709  1.00 63.41  ? 37  LEU E CB  1 
ATOM   7327  C  CG  . LEU E  1 46  ? 14.391  -39.558 10.190 1.00 71.96  ? 37  LEU E CG  1 
ATOM   7328  C  CD1 . LEU E  1 46  ? 13.932  -38.141 10.391 1.00 75.42  ? 37  LEU E CD1 1 
ATOM   7329  C  CD2 . LEU E  1 46  ? 13.500  -40.277 9.207  1.00 67.64  ? 37  LEU E CD2 1 
ATOM   7330  N  N   . LEU E  1 47  ? 17.023  -39.307 12.711 1.00 65.00  ? 38  LEU E N   1 
ATOM   7331  C  CA  . LEU E  1 47  ? 17.864  -39.718 13.833 1.00 57.77  ? 38  LEU E CA  1 
ATOM   7332  C  C   . LEU E  1 47  ? 17.515  -41.109 14.340 1.00 53.86  ? 38  LEU E C   1 
ATOM   7333  O  O   . LEU E  1 47  ? 18.373  -41.981 14.358 1.00 59.87  ? 38  LEU E O   1 
ATOM   7334  C  CB  . LEU E  1 47  ? 17.824  -38.682 14.941 1.00 58.77  ? 38  LEU E CB  1 
ATOM   7335  C  CG  . LEU E  1 47  ? 18.743  -37.527 14.576 1.00 60.63  ? 38  LEU E CG  1 
ATOM   7336  C  CD1 . LEU E  1 47  ? 17.983  -36.235 14.526 1.00 60.90  ? 38  LEU E CD1 1 
ATOM   7337  C  CD2 . LEU E  1 47  ? 19.860  -37.459 15.575 1.00 70.01  ? 38  LEU E CD2 1 
ATOM   7338  N  N   . ASP E  1 48  ? 16.290  -41.313 14.815 1.00 49.99  ? 39  ASP E N   1 
ATOM   7339  C  CA  . ASP E  1 48  ? 15.894  -42.667 15.203 1.00 54.98  ? 39  ASP E CA  1 
ATOM   7340  C  C   . ASP E  1 48  ? 14.409  -43.046 15.038 1.00 54.48  ? 39  ASP E C   1 
ATOM   7341  O  O   . ASP E  1 48  ? 13.513  -42.287 15.414 1.00 49.99  ? 39  ASP E O   1 
ATOM   7342  C  CB  . ASP E  1 48  ? 16.320  -42.905 16.649 1.00 51.39  ? 39  ASP E CB  1 
ATOM   7343  C  CG  . ASP E  1 48  ? 16.398  -44.341 16.983 1.00 56.48  ? 39  ASP E CG  1 
ATOM   7344  O  OD1 . ASP E  1 48  ? 16.414  -45.139 16.036 1.00 59.98  ? 39  ASP E OD1 1 
ATOM   7345  O  OD2 . ASP E  1 48  ? 16.431  -44.677 18.181 1.00 62.12  ? 39  ASP E OD2 1 
ATOM   7346  N  N   . ILE E  1 49  ? 14.150  -44.260 14.554 1.00 51.33  ? 40  ILE E N   1 
ATOM   7347  C  CA  . ILE E  1 49  ? 12.832  -44.841 14.751 1.00 53.84  ? 40  ILE E CA  1 
ATOM   7348  C  C   . ILE E  1 49  ? 12.964  -45.690 16.004 1.00 60.88  ? 40  ILE E C   1 
ATOM   7349  O  O   . ILE E  1 49  ? 13.589  -46.755 16.003 1.00 62.14  ? 40  ILE E O   1 
ATOM   7350  C  CB  . ILE E  1 49  ? 12.413  -45.754 13.592 1.00 56.26  ? 40  ILE E CB  1 
ATOM   7351  C  CG1 . ILE E  1 49  ? 12.343  -44.979 12.281 1.00 54.37  ? 40  ILE E CG1 1 
ATOM   7352  C  CG2 . ILE E  1 49  ? 11.070  -46.418 13.887 1.00 58.43  ? 40  ILE E CG2 1 
ATOM   7353  C  CD1 . ILE E  1 49  ? 11.255  -45.462 11.374 1.00 50.37  ? 40  ILE E CD1 1 
ATOM   7354  N  N   . VAL E  1 50  ? 12.359  -45.205 17.077 1.00 62.01  ? 41  VAL E N   1 
ATOM   7355  C  CA  . VAL E  1 50  ? 12.568  -45.774 18.393 1.00 56.48  ? 41  VAL E CA  1 
ATOM   7356  C  C   . VAL E  1 50  ? 11.683  -46.990 18.634 1.00 63.69  ? 41  VAL E C   1 
ATOM   7357  O  O   . VAL E  1 50  ? 12.118  -47.971 19.238 1.00 64.85  ? 41  VAL E O   1 
ATOM   7358  C  CB  . VAL E  1 50  ? 12.387  -44.714 19.481 1.00 51.88  ? 41  VAL E CB  1 
ATOM   7359  C  CG1 . VAL E  1 50  ? 13.288  -45.013 20.653 1.00 60.36  ? 41  VAL E CG1 1 
ATOM   7360  C  CG2 . VAL E  1 50  ? 12.737  -43.365 18.924 1.00 53.88  ? 41  VAL E CG2 1 
ATOM   7361  N  N   . LYS E  1 51  ? 10.434  -46.916 18.184 1.00 57.79  ? 42  LYS E N   1 
ATOM   7362  C  CA  . LYS E  1 51  ? 9.483   -47.983 18.464 1.00 61.68  ? 42  LYS E CA  1 
ATOM   7363  C  C   . LYS E  1 51  ? 8.458   -48.112 17.350 1.00 63.94  ? 42  LYS E C   1 
ATOM   7364  O  O   . LYS E  1 51  ? 8.034   -47.108 16.780 1.00 69.71  ? 42  LYS E O   1 
ATOM   7365  C  CB  . LYS E  1 51  ? 8.778   -47.728 19.805 1.00 56.86  ? 42  LYS E CB  1 
ATOM   7366  C  CG  . LYS E  1 51  ? 7.765   -48.790 20.189 1.00 56.50  ? 42  LYS E CG  1 
ATOM   7367  C  CD  . LYS E  1 51  ? 7.335   -48.687 21.655 1.00 56.88  ? 42  LYS E CD  1 
ATOM   7368  C  CE  . LYS E  1 51  ? 6.656   -47.374 21.921 1.00 61.89  ? 42  LYS E CE  1 
ATOM   7369  N  NZ  . LYS E  1 51  ? 5.898   -46.942 20.707 1.00 77.92  ? 42  LYS E NZ  1 
ATOM   7370  N  N   . ALA E  1 52  ? 8.055   -49.342 17.039 1.00 63.82  ? 43  ALA E N   1 
ATOM   7371  C  CA  . ALA E  1 52  ? 6.936   -49.571 16.120 1.00 58.68  ? 43  ALA E CA  1 
ATOM   7372  C  C   . ALA E  1 52  ? 5.920   -50.454 16.820 1.00 64.82  ? 43  ALA E C   1 
ATOM   7373  O  O   . ALA E  1 52  ? 6.218   -51.594 17.187 1.00 60.43  ? 43  ALA E O   1 
ATOM   7374  C  CB  . ALA E  1 52  ? 7.408   -50.209 14.832 1.00 55.15  ? 43  ALA E CB  1 
ATOM   7375  N  N   . ASP E  1 53  ? 4.719   -49.933 17.027 1.00 64.22  ? 44  ASP E N   1 
ATOM   7376  C  CA  . ASP E  1 53  ? 3.795   -50.619 17.912 1.00 63.25  ? 44  ASP E CA  1 
ATOM   7377  C  C   . ASP E  1 53  ? 2.667   -51.258 17.131 1.00 64.22  ? 44  ASP E C   1 
ATOM   7378  O  O   . ASP E  1 53  ? 1.778   -50.566 16.651 1.00 66.75  ? 44  ASP E O   1 
ATOM   7379  C  CB  . ASP E  1 53  ? 3.241   -49.638 18.938 1.00 63.55  ? 44  ASP E CB  1 
ATOM   7380  C  CG  . ASP E  1 53  ? 2.611   -50.335 20.116 1.00 68.24  ? 44  ASP E CG  1 
ATOM   7381  O  OD1 . ASP E  1 53  ? 2.105   -51.460 19.936 1.00 66.39  ? 44  ASP E OD1 1 
ATOM   7382  O  OD2 . ASP E  1 53  ? 2.619   -49.758 21.223 1.00 66.46  ? 44  ASP E OD2 1 
ATOM   7383  N  N   . SER E  1 54  ? 2.685   -52.586 17.049 1.00 63.41  ? 45  SER E N   1 
ATOM   7384  C  CA  . SER E  1 54  ? 1.794   -53.302 16.144 1.00 60.28  ? 45  SER E CA  1 
ATOM   7385  C  C   . SER E  1 54  ? 0.383   -53.374 16.697 1.00 64.72  ? 45  SER E C   1 
ATOM   7386  O  O   . SER E  1 54  ? -0.568  -53.575 15.948 1.00 65.99  ? 45  SER E O   1 
ATOM   7387  C  CB  . SER E  1 54  ? 2.318   -54.709 15.879 1.00 56.57  ? 45  SER E CB  1 
ATOM   7388  O  OG  . SER E  1 54  ? 3.725   -54.692 15.714 1.00 65.85  ? 45  SER E OG  1 
ATOM   7389  N  N   . SER E  1 55  ? 0.257   -53.219 18.011 1.00 62.44  ? 46  SER E N   1 
ATOM   7390  C  CA  . SER E  1 55  ? -1.034  -53.327 18.688 1.00 60.34  ? 46  SER E CA  1 
ATOM   7391  C  C   . SER E  1 55  ? -1.861  -52.062 18.590 1.00 62.53  ? 46  SER E C   1 
ATOM   7392  O  O   . SER E  1 55  ? -3.092  -52.120 18.582 1.00 61.67  ? 46  SER E O   1 
ATOM   7393  C  CB  . SER E  1 55  ? -0.844  -53.689 20.157 1.00 57.05  ? 46  SER E CB  1 
ATOM   7394  O  OG  . SER E  1 55  ? -0.006  -52.736 20.779 1.00 70.38  ? 46  SER E OG  1 
ATOM   7395  N  N   . THR E  1 56  ? -1.191  -50.919 18.678 1.00 60.12  ? 47  THR E N   1 
ATOM   7396  C  CA  . THR E  1 56  ? -1.835  -49.633 18.436 1.00 58.91  ? 47  THR E CA  1 
ATOM   7397  C  C   . THR E  1 56  ? -1.678  -49.020 17.031 1.00 59.28  ? 47  THR E C   1 
ATOM   7398  O  O   . THR E  1 56  ? -2.361  -48.052 16.684 1.00 55.92  ? 47  THR E O   1 
ATOM   7399  C  CB  . THR E  1 56  ? -1.388  -48.634 19.496 1.00 67.55  ? 47  THR E CB  1 
ATOM   7400  O  OG1 . THR E  1 56  ? 0.043   -48.500 19.452 1.00 65.84  ? 47  THR E OG1 1 
ATOM   7401  C  CG2 . THR E  1 56  ? -1.824  -49.131 20.871 1.00 54.08  ? 47  THR E CG2 1 
ATOM   7402  N  N   . ASN E  1 57  ? -0.795  -49.596 16.224 1.00 65.47  ? 48  ASN E N   1 
ATOM   7403  C  CA  . ASN E  1 57  ? -0.393  -48.977 14.961 1.00 57.21  ? 48  ASN E CA  1 
ATOM   7404  C  C   . ASN E  1 57  ? 0.142   -47.554 15.095 1.00 55.10  ? 48  ASN E C   1 
ATOM   7405  O  O   . ASN E  1 57  ? -0.291  -46.674 14.360 1.00 57.58  ? 48  ASN E O   1 
ATOM   7406  C  CB  . ASN E  1 57  ? -1.556  -48.973 13.976 1.00 66.82  ? 48  ASN E CB  1 
ATOM   7407  C  CG  . ASN E  1 57  ? -1.657  -50.260 13.195 1.00 65.08  ? 48  ASN E CG  1 
ATOM   7408  O  OD1 . ASN E  1 57  ? -0.742  -51.083 13.209 1.00 68.39  ? 48  ASN E OD1 1 
ATOM   7409  N  ND2 . ASN E  1 57  ? -2.767  -50.436 12.501 1.00 54.77  ? 48  ASN E ND2 1 
ATOM   7410  N  N   . GLU E  1 58  ? 1.064   -47.335 16.036 1.00 63.87  ? 49  GLU E N   1 
ATOM   7411  C  CA  . GLU E  1 58  ? 1.778   -46.064 16.184 1.00 55.70  ? 49  GLU E CA  1 
ATOM   7412  C  C   . GLU E  1 58  ? 3.281   -46.297 16.050 1.00 55.54  ? 49  GLU E C   1 
ATOM   7413  O  O   . GLU E  1 58  ? 3.790   -47.352 16.409 1.00 58.80  ? 49  GLU E O   1 
ATOM   7414  C  CB  . GLU E  1 58  ? 1.530   -45.431 17.557 1.00 54.20  ? 49  GLU E CB  1 
ATOM   7415  C  CG  . GLU E  1 58  ? 0.092   -45.375 18.037 1.00 55.41  ? 49  GLU E CG  1 
ATOM   7416  C  CD  . GLU E  1 58  ? -0.006  -45.009 19.521 1.00 61.95  ? 49  GLU E CD  1 
ATOM   7417  O  OE1 . GLU E  1 58  ? -0.090  -45.932 20.356 1.00 56.10  ? 49  GLU E OE1 1 
ATOM   7418  O  OE2 . GLU E  1 58  ? 0.010   -43.803 19.861 1.00 59.13  ? 49  GLU E OE2 1 
ATOM   7419  N  N   . VAL E  1 59  ? 3.999   -45.297 15.561 1.00 57.99  ? 50  VAL E N   1 
ATOM   7420  C  CA  . VAL E  1 59  ? 5.457   -45.360 15.512 1.00 55.21  ? 50  VAL E CA  1 
ATOM   7421  C  C   . VAL E  1 59  ? 6.066   -44.125 16.175 1.00 55.99  ? 50  VAL E C   1 
ATOM   7422  O  O   . VAL E  1 59  ? 5.494   -43.033 16.130 1.00 49.35  ? 50  VAL E O   1 
ATOM   7423  C  CB  . VAL E  1 59  ? 5.970   -45.453 14.051 1.00 65.31  ? 50  VAL E CB  1 
ATOM   7424  C  CG1 . VAL E  1 59  ? 7.506   -45.469 13.987 1.00 55.40  ? 50  VAL E CG1 1 
ATOM   7425  C  CG2 . VAL E  1 59  ? 5.400   -46.664 13.373 1.00 63.60  ? 50  VAL E CG2 1 
ATOM   7426  N  N   . ASP E  1 60  ? 7.236   -44.318 16.777 1.00 57.12  ? 51  ASP E N   1 
ATOM   7427  C  CA  . ASP E  1 60  ? 7.955   -43.263 17.480 1.00 55.93  ? 51  ASP E CA  1 
ATOM   7428  C  C   . ASP E  1 60  ? 9.193   -42.858 16.701 1.00 55.21  ? 51  ASP E C   1 
ATOM   7429  O  O   . ASP E  1 60  ? 10.094  -43.662 16.466 1.00 54.25  ? 51  ASP E O   1 
ATOM   7430  C  CB  . ASP E  1 60  ? 8.335   -43.718 18.896 1.00 57.60  ? 51  ASP E CB  1 
ATOM   7431  C  CG  . ASP E  1 60  ? 7.127   -43.826 19.809 1.00 64.77  ? 51  ASP E CG  1 
ATOM   7432  O  OD1 . ASP E  1 60  ? 5.999   -43.719 19.287 1.00 64.40  ? 51  ASP E OD1 1 
ATOM   7433  O  OD2 . ASP E  1 60  ? 7.290   -44.023 21.037 1.00 68.96  ? 51  ASP E OD2 1 
ATOM   7434  N  N   . LEU E  1 61  ? 9.232   -41.600 16.300 1.00 48.35  ? 52  LEU E N   1 
ATOM   7435  C  CA  . LEU E  1 61  ? 10.318  -41.130 15.479 1.00 48.34  ? 52  LEU E CA  1 
ATOM   7436  C  C   . LEU E  1 61  ? 10.992  -39.972 16.178 1.00 48.31  ? 52  LEU E C   1 
ATOM   7437  O  O   . LEU E  1 61  ? 10.327  -39.134 16.775 1.00 54.70  ? 52  LEU E O   1 
ATOM   7438  C  CB  . LEU E  1 61  ? 9.765   -40.719 14.108 1.00 61.13  ? 52  LEU E CB  1 
ATOM   7439  C  CG  . LEU E  1 61  ? 10.613  -40.048 13.021 1.00 65.49  ? 52  LEU E CG  1 
ATOM   7440  C  CD1 . LEU E  1 61  ? 11.785  -40.896 12.551 1.00 63.09  ? 52  LEU E CD1 1 
ATOM   7441  C  CD2 . LEU E  1 61  ? 9.696   -39.776 11.876 1.00 62.26  ? 52  LEU E CD2 1 
ATOM   7442  N  N   . VAL E  1 62  ? 12.318  -39.956 16.135 1.00 49.61  ? 53  VAL E N   1 
ATOM   7443  C  CA  . VAL E  1 62  ? 13.119  -38.870 16.703 1.00 56.36  ? 53  VAL E CA  1 
ATOM   7444  C  C   . VAL E  1 62  ? 13.878  -38.222 15.549 1.00 59.75  ? 53  VAL E C   1 
ATOM   7445  O  O   . VAL E  1 62  ? 14.614  -38.902 14.822 1.00 58.21  ? 53  VAL E O   1 
ATOM   7446  C  CB  . VAL E  1 62  ? 14.140  -39.379 17.774 1.00 49.06  ? 53  VAL E CB  1 
ATOM   7447  C  CG1 . VAL E  1 62  ? 15.200  -38.327 18.056 1.00 46.16  ? 53  VAL E CG1 1 
ATOM   7448  C  CG2 . VAL E  1 62  ? 13.434  -39.809 19.043 1.00 44.14  ? 53  VAL E CG2 1 
ATOM   7449  N  N   . TYR E  1 63  ? 13.699  -36.913 15.376 1.00 57.79  ? 54  TYR E N   1 
ATOM   7450  C  CA  . TYR E  1 63  ? 14.218  -36.231 14.200 1.00 56.03  ? 54  TYR E CA  1 
ATOM   7451  C  C   . TYR E  1 63  ? 14.438  -34.761 14.456 1.00 54.87  ? 54  TYR E C   1 
ATOM   7452  O  O   . TYR E  1 63  ? 13.841  -34.193 15.357 1.00 53.91  ? 54  TYR E O   1 
ATOM   7453  C  CB  . TYR E  1 63  ? 13.211  -36.359 13.066 1.00 58.24  ? 54  TYR E CB  1 
ATOM   7454  C  CG  . TYR E  1 63  ? 11.893  -35.682 13.375 1.00 58.61  ? 54  TYR E CG  1 
ATOM   7455  C  CD1 . TYR E  1 63  ? 11.680  -34.348 13.057 1.00 54.13  ? 54  TYR E CD1 1 
ATOM   7456  C  CD2 . TYR E  1 63  ? 10.868  -36.376 13.989 1.00 61.07  ? 54  TYR E CD2 1 
ATOM   7457  C  CE1 . TYR E  1 63  ? 10.498  -33.733 13.342 1.00 52.11  ? 54  TYR E CE1 1 
ATOM   7458  C  CE2 . TYR E  1 63  ? 9.680   -35.764 14.276 1.00 56.43  ? 54  TYR E CE2 1 
ATOM   7459  C  CZ  . TYR E  1 63  ? 9.501   -34.447 13.945 1.00 54.99  ? 54  TYR E CZ  1 
ATOM   7460  O  OH  . TYR E  1 63  ? 8.307   -33.845 14.233 1.00 63.59  ? 54  TYR E OH  1 
ATOM   7461  N  N   . TRP E  1 64  ? 15.278  -34.139 13.634 1.00 60.83  ? 55  TRP E N   1 
ATOM   7462  C  CA  . TRP E  1 64  ? 15.357  -32.676 13.584 1.00 60.69  ? 55  TRP E CA  1 
ATOM   7463  C  C   . TRP E  1 64  ? 14.444  -32.119 12.472 1.00 55.88  ? 55  TRP E C   1 
ATOM   7464  O  O   . TRP E  1 64  ? 14.474  -32.554 11.328 1.00 49.92  ? 55  TRP E O   1 
ATOM   7465  C  CB  . TRP E  1 64  ? 16.806  -32.198 13.397 1.00 60.00  ? 55  TRP E CB  1 
ATOM   7466  C  CG  . TRP E  1 64  ? 17.793  -32.802 14.371 1.00 64.04  ? 55  TRP E CG  1 
ATOM   7467  C  CD1 . TRP E  1 64  ? 17.542  -33.216 15.653 1.00 61.71  ? 55  TRP E CD1 1 
ATOM   7468  C  CD2 . TRP E  1 64  ? 19.183  -33.073 14.131 1.00 67.12  ? 55  TRP E CD2 1 
ATOM   7469  N  NE1 . TRP E  1 64  ? 18.692  -33.714 16.226 1.00 66.79  ? 55  TRP E NE1 1 
ATOM   7470  C  CE2 . TRP E  1 64  ? 19.709  -33.642 15.311 1.00 70.89  ? 55  TRP E CE2 1 
ATOM   7471  C  CE3 . TRP E  1 64  ? 20.031  -32.883 13.039 1.00 71.27  ? 55  TRP E CE3 1 
ATOM   7472  C  CZ2 . TRP E  1 64  ? 21.046  -34.025 15.422 1.00 72.43  ? 55  TRP E CZ2 1 
ATOM   7473  C  CZ3 . TRP E  1 64  ? 21.356  -33.271 13.156 1.00 79.78  ? 55  TRP E CZ3 1 
ATOM   7474  C  CH2 . TRP E  1 64  ? 21.849  -33.832 14.338 1.00 73.64  ? 55  TRP E CH2 1 
ATOM   7475  N  N   . GLU E  1 65  ? 13.604  -31.171 12.837 1.00 53.72  ? 56  GLU E N   1 
ATOM   7476  C  CA  . GLU E  1 65  ? 12.799  -30.473 11.865 1.00 55.41  ? 56  GLU E CA  1 
ATOM   7477  C  C   . GLU E  1 65  ? 13.347  -29.055 11.711 1.00 58.41  ? 56  GLU E C   1 
ATOM   7478  O  O   . GLU E  1 65  ? 13.322  -28.275 12.658 1.00 60.39  ? 56  GLU E O   1 
ATOM   7479  C  CB  . GLU E  1 65  ? 11.357  -30.447 12.343 1.00 57.80  ? 56  GLU E CB  1 
ATOM   7480  C  CG  . GLU E  1 65  ? 10.479  -29.399 11.713 1.00 56.81  ? 56  GLU E CG  1 
ATOM   7481  C  CD  . GLU E  1 65  ? 9.051   -29.592 12.142 1.00 62.98  ? 56  GLU E CD  1 
ATOM   7482  O  OE1 . GLU E  1 65  ? 8.830   -30.482 12.989 1.00 62.57  ? 56  GLU E OE1 1 
ATOM   7483  O  OE2 . GLU E  1 65  ? 8.154   -28.878 11.644 1.00 66.45  ? 56  GLU E OE2 1 
ATOM   7484  N  N   . GLN E  1 66  ? 13.868  -28.729 10.530 1.00 57.76  ? 57  GLN E N   1 
ATOM   7485  C  CA  . GLN E  1 66  ? 14.344  -27.379 10.282 1.00 58.92  ? 57  GLN E CA  1 
ATOM   7486  C  C   . GLN E  1 66  ? 13.287  -26.470 9.650  1.00 57.07  ? 57  GLN E C   1 
ATOM   7487  O  O   . GLN E  1 66  ? 12.678  -26.808 8.642  1.00 57.73  ? 57  GLN E O   1 
ATOM   7488  C  CB  . GLN E  1 66  ? 15.618  -27.369 9.446  1.00 63.05  ? 57  GLN E CB  1 
ATOM   7489  C  CG  . GLN E  1 66  ? 16.140  -25.958 9.264  1.00 70.33  ? 57  GLN E CG  1 
ATOM   7490  C  CD  . GLN E  1 66  ? 17.368  -25.873 8.393  1.00 85.38  ? 57  GLN E CD  1 
ATOM   7491  O  OE1 . GLN E  1 66  ? 17.992  -24.811 8.287  1.00 85.46  ? 57  GLN E OE1 1 
ATOM   7492  N  NE2 . GLN E  1 66  ? 17.723  -26.987 7.750  1.00 86.12  ? 57  GLN E NE2 1 
ATOM   7493  N  N   . GLN E  1 67  ? 13.102  -25.310 10.273 1.00 55.04  ? 58  GLN E N   1 
ATOM   7494  C  CA  . GLN E  1 67  ? 12.183  -24.277 9.829  1.00 52.58  ? 58  GLN E CA  1 
ATOM   7495  C  C   . GLN E  1 67  ? 12.956  -22.994 9.554  1.00 55.30  ? 58  GLN E C   1 
ATOM   7496  O  O   . GLN E  1 67  ? 13.851  -22.630 10.312 1.00 56.90  ? 58  GLN E O   1 
ATOM   7497  C  CB  . GLN E  1 67  ? 11.139  -24.018 10.908 1.00 52.84  ? 58  GLN E CB  1 
ATOM   7498  C  CG  . GLN E  1 67  ? 10.440  -25.269 11.380 1.00 50.84  ? 58  GLN E CG  1 
ATOM   7499  C  CD  . GLN E  1 67  ? 9.301   -24.966 12.319 1.00 55.56  ? 58  GLN E CD  1 
ATOM   7500  O  OE1 . GLN E  1 67  ? 9.103   -23.822 12.724 1.00 50.56  ? 58  GLN E OE1 1 
ATOM   7501  N  NE2 . GLN E  1 67  ? 8.538   -25.994 12.675 1.00 56.57  ? 58  GLN E NE2 1 
ATOM   7502  N  N   . SER E  1 68  ? 12.620  -22.324 8.454  1.00 58.34  ? 59  SER E N   1 
ATOM   7503  C  CA  . SER E  1 68  ? 13.236  -21.049 8.094  1.00 58.87  ? 59  SER E CA  1 
ATOM   7504  C  C   . SER E  1 68  ? 12.186  -20.147 7.478  1.00 61.56  ? 59  SER E C   1 
ATOM   7505  O  O   . SER E  1 68  ? 11.227  -20.621 6.872  1.00 56.58  ? 59  SER E O   1 
ATOM   7506  C  CB  . SER E  1 68  ? 14.376  -21.238 7.097  1.00 59.00  ? 59  SER E CB  1 
ATOM   7507  O  OG  . SER E  1 68  ? 14.973  -22.513 7.243  1.00 68.41  ? 59  SER E OG  1 
ATOM   7508  N  N   . TRP E  1 69  ? 12.374  -18.846 7.659  1.00 60.53  ? 60  TRP E N   1 
ATOM   7509  C  CA  . TRP E  1 69  ? 11.500  -17.831 7.101  1.00 54.30  ? 60  TRP E CA  1 
ATOM   7510  C  C   . TRP E  1 69  ? 12.243  -16.526 7.210  1.00 54.13  ? 60  TRP E C   1 
ATOM   7511  O  O   . TRP E  1 69  ? 13.352  -16.495 7.728  1.00 56.78  ? 60  TRP E O   1 
ATOM   7512  C  CB  . TRP E  1 69  ? 10.142  -17.771 7.829  1.00 57.05  ? 60  TRP E CB  1 
ATOM   7513  C  CG  . TRP E  1 69  ? 10.194  -17.390 9.285  1.00 59.82  ? 60  TRP E CG  1 
ATOM   7514  C  CD1 . TRP E  1 69  ? 10.078  -16.136 9.803  1.00 59.23  ? 60  TRP E CD1 1 
ATOM   7515  C  CD2 . TRP E  1 69  ? 10.356  -18.276 10.416 1.00 65.19  ? 60  TRP E CD2 1 
ATOM   7516  N  NE1 . TRP E  1 69  ? 10.173  -16.179 11.183 1.00 64.16  ? 60  TRP E NE1 1 
ATOM   7517  C  CE2 . TRP E  1 69  ? 10.345  -17.478 11.579 1.00 58.48  ? 60  TRP E CE2 1 
ATOM   7518  C  CE3 . TRP E  1 69  ? 10.515  -19.659 10.553 1.00 55.85  ? 60  TRP E CE3 1 
ATOM   7519  C  CZ2 . TRP E  1 69  ? 10.477  -18.017 12.852 1.00 55.27  ? 60  TRP E CZ2 1 
ATOM   7520  C  CZ3 . TRP E  1 69  ? 10.646  -20.186 11.820 1.00 57.36  ? 60  TRP E CZ3 1 
ATOM   7521  C  CH2 . TRP E  1 69  ? 10.625  -19.371 12.951 1.00 55.43  ? 60  TRP E CH2 1 
ATOM   7522  N  N   . LYS E  1 70  ? 11.642  -15.452 6.717  1.00 54.19  ? 61  LYS E N   1 
ATOM   7523  C  CA  . LYS E  1 70  ? 12.277  -14.144 6.758  1.00 56.34  ? 61  LYS E CA  1 
ATOM   7524  C  C   . LYS E  1 70  ? 11.224  -13.116 7.084  1.00 57.73  ? 61  LYS E C   1 
ATOM   7525  O  O   . LYS E  1 70  ? 10.107  -13.228 6.610  1.00 58.75  ? 61  LYS E O   1 
ATOM   7526  C  CB  . LYS E  1 70  ? 12.955  -13.815 5.426  1.00 55.36  ? 61  LYS E CB  1 
ATOM   7527  C  CG  . LYS E  1 70  ? 13.047  -12.329 5.117  1.00 59.76  ? 61  LYS E CG  1 
ATOM   7528  C  CD  . LYS E  1 70  ? 14.109  -12.039 4.063  1.00 70.33  ? 61  LYS E CD  1 
ATOM   7529  C  CE  . LYS E  1 70  ? 14.117  -10.563 3.662  1.00 89.01  ? 61  LYS E CE  1 
ATOM   7530  N  NZ  . LYS E  1 70  ? 15.222  -10.241 2.716  1.00 85.64  ? 61  LYS E NZ  1 
ATOM   7531  N  N   . LEU E  1 71  ? 11.575  -12.146 7.928  1.00 59.11  ? 62  LEU E N   1 
ATOM   7532  C  CA  . LEU E  1 71  ? 10.702  -11.017 8.243  1.00 60.85  ? 62  LEU E CA  1 
ATOM   7533  C  C   . LEU E  1 71  ? 11.461  -9.707  8.042  1.00 65.96  ? 62  LEU E C   1 
ATOM   7534  O  O   . LEU E  1 71  ? 12.610  -9.586  8.458  1.00 68.07  ? 62  LEU E O   1 
ATOM   7535  C  CB  . LEU E  1 71  ? 10.205  -11.110 9.680  1.00 59.24  ? 62  LEU E CB  1 
ATOM   7536  C  CG  . LEU E  1 71  ? 9.287   -12.277 10.010 1.00 56.28  ? 62  LEU E CG  1 
ATOM   7537  C  CD1 . LEU E  1 71  ? 8.912   -12.240 11.474 1.00 57.81  ? 62  LEU E CD1 1 
ATOM   7538  C  CD2 . LEU E  1 71  ? 8.051   -12.239 9.154  1.00 58.73  ? 62  LEU E CD2 1 
ATOM   7539  N  N   . ASN E  1 72  ? 10.841  -8.729  7.392  1.00 66.44  ? 63  ASN E N   1 
ATOM   7540  C  CA  . ASN E  1 72  ? 11.522  -7.452  7.216  1.00 70.86  ? 63  ASN E CA  1 
ATOM   7541  C  C   . ASN E  1 72  ? 11.752  -6.827  8.585  1.00 68.73  ? 63  ASN E C   1 
ATOM   7542  O  O   . ASN E  1 72  ? 12.699  -6.067  8.788  1.00 75.16  ? 63  ASN E O   1 
ATOM   7543  C  CB  . ASN E  1 72  ? 10.741  -6.498  6.294  1.00 76.44  ? 63  ASN E CB  1 
ATOM   7544  C  CG  . ASN E  1 72  ? 10.559  -7.057  4.887  1.00 82.43  ? 63  ASN E CG  1 
ATOM   7545  O  OD1 . ASN E  1 72  ? 11.410  -7.790  4.384  1.00 84.87  ? 63  ASN E OD1 1 
ATOM   7546  N  ND2 . ASN E  1 72  ? 9.438   -6.720  4.253  1.00 77.53  ? 63  ASN E ND2 1 
ATOM   7547  N  N   . SER E  1 73  ? 10.890  -7.169  9.534  1.00 66.15  ? 64  SER E N   1 
ATOM   7548  C  CA  . SER E  1 73  ? 10.971  -6.594  10.867 1.00 60.70  ? 64  SER E CA  1 
ATOM   7549  C  C   . SER E  1 73  ? 12.253  -7.009  11.567 1.00 64.87  ? 64  SER E C   1 
ATOM   7550  O  O   . SER E  1 73  ? 12.739  -6.299  12.441 1.00 68.73  ? 64  SER E O   1 
ATOM   7551  C  CB  . SER E  1 73  ? 9.766   -7.013  11.691 1.00 57.14  ? 64  SER E CB  1 
ATOM   7552  O  OG  . SER E  1 73  ? 8.704   -7.389  10.833 1.00 72.35  ? 64  SER E OG  1 
ATOM   7553  N  N   . LEU E  1 74  ? 12.804  -8.158  11.183 1.00 61.48  ? 65  LEU E N   1 
ATOM   7554  C  CA  . LEU E  1 74  ? 14.006  -8.678  11.832 1.00 62.69  ? 65  LEU E CA  1 
ATOM   7555  C  C   . LEU E  1 74  ? 15.301  -8.187  11.195 1.00 64.22  ? 65  LEU E C   1 
ATOM   7556  O  O   . LEU E  1 74  ? 16.393  -8.535  11.659 1.00 64.76  ? 65  LEU E O   1 
ATOM   7557  C  CB  . LEU E  1 74  ? 13.978  -10.206 11.879 1.00 60.72  ? 65  LEU E CB  1 
ATOM   7558  C  CG  . LEU E  1 74  ? 12.863  -10.751 12.768 1.00 57.85  ? 65  LEU E CG  1 
ATOM   7559  C  CD1 . LEU E  1 74  ? 13.038  -12.231 12.978 1.00 60.48  ? 65  LEU E CD1 1 
ATOM   7560  C  CD2 . LEU E  1 74  ? 12.868  -10.039 14.104 1.00 52.42  ? 65  LEU E CD2 1 
ATOM   7561  N  N   . MET E  1 75  ? 15.165  -7.367  10.149 1.00 66.21  ? 66  MET E N   1 
ATOM   7562  C  CA  . MET E  1 75  ? 16.300  -6.827  9.404  1.00 59.51  ? 66  MET E CA  1 
ATOM   7563  C  C   . MET E  1 75  ? 16.991  -5.676  10.108 1.00 61.51  ? 66  MET E C   1 
ATOM   7564  O  O   . MET E  1 75  ? 16.352  -4.851  10.761 1.00 60.57  ? 66  MET E O   1 
ATOM   7565  C  CB  . MET E  1 75  ? 15.851  -6.315  8.052  1.00 61.26  ? 66  MET E CB  1 
ATOM   7566  C  CG  . MET E  1 75  ? 15.055  -7.292  7.225  1.00 71.06  ? 66  MET E CG  1 
ATOM   7567  S  SD  . MET E  1 75  ? 14.864  -6.611  5.569  1.00 63.51  ? 66  MET E SD  1 
ATOM   7568  C  CE  . MET E  1 75  ? 16.583  -6.628  5.048  1.00 59.82  ? 66  MET E CE  1 
ATOM   7569  N  N   . TRP E  1 76  ? 18.307  -5.617  9.944  1.00 62.79  ? 67  TRP E N   1 
ATOM   7570  C  CA  . TRP E  1 76  ? 19.097  -4.511  10.461 1.00 65.41  ? 67  TRP E CA  1 
ATOM   7571  C  C   . TRP E  1 76  ? 20.389  -4.336  9.653  1.00 70.72  ? 67  TRP E C   1 
ATOM   7572  O  O   . TRP E  1 76  ? 20.777  -5.220  8.875  1.00 60.08  ? 67  TRP E O   1 
ATOM   7573  C  CB  . TRP E  1 76  ? 19.401  -4.701  11.943 1.00 55.32  ? 67  TRP E CB  1 
ATOM   7574  C  CG  . TRP E  1 76  ? 20.467  -5.724  12.222 1.00 66.35  ? 67  TRP E CG  1 
ATOM   7575  C  CD1 . TRP E  1 76  ? 21.817  -5.514  12.281 1.00 61.65  ? 67  TRP E CD1 1 
ATOM   7576  C  CD2 . TRP E  1 76  ? 20.268  -7.114  12.493 1.00 64.33  ? 67  TRP E CD2 1 
ATOM   7577  N  NE1 . TRP E  1 76  ? 22.466  -6.690  12.559 1.00 61.53  ? 67  TRP E NE1 1 
ATOM   7578  C  CE2 . TRP E  1 76  ? 21.534  -7.689  12.704 1.00 60.68  ? 67  TRP E CE2 1 
ATOM   7579  C  CE3 . TRP E  1 76  ? 19.136  -7.933  12.585 1.00 56.53  ? 67  TRP E CE3 1 
ATOM   7580  C  CZ2 . TRP E  1 76  ? 21.703  -9.025  13.002 1.00 59.70  ? 67  TRP E CZ2 1 
ATOM   7581  C  CZ3 . TRP E  1 76  ? 19.304  -9.251  12.867 1.00 54.02  ? 67  TRP E CZ3 1 
ATOM   7582  C  CH2 . TRP E  1 76  ? 20.576  -9.789  13.081 1.00 59.06  ? 67  TRP E CH2 1 
ATOM   7583  N  N   . ASP E  1 77  ? 21.022  -3.174  9.823  1.00 71.83  ? 68  ASP E N   1 
ATOM   7584  C  CA  . ASP E  1 77  ? 22.299  -2.879  9.187  1.00 70.90  ? 68  ASP E CA  1 
ATOM   7585  C  C   . ASP E  1 77  ? 23.423  -3.211  10.146 1.00 70.45  ? 68  ASP E C   1 
ATOM   7586  O  O   . ASP E  1 77  ? 23.532  -2.604  11.199 1.00 76.91  ? 68  ASP E O   1 
ATOM   7587  C  CB  . ASP E  1 77  ? 22.374  -1.400  8.799  1.00 78.24  ? 68  ASP E CB  1 
ATOM   7588  C  CG  . ASP E  1 77  ? 23.567  -1.085  7.900  1.00 82.37  ? 68  ASP E CG  1 
ATOM   7589  O  OD1 . ASP E  1 77  ? 24.214  -2.031  7.390  1.00 78.24  ? 68  ASP E OD1 1 
ATOM   7590  O  OD2 . ASP E  1 77  ? 23.847  0.117   7.693  1.00 85.78  ? 68  ASP E OD2 1 
ATOM   7591  N  N   . PRO E  1 78  ? 24.264  -4.189  9.794  1.00 74.72  ? 69  PRO E N   1 
ATOM   7592  C  CA  . PRO E  1 78  ? 25.356  -4.558  10.705 1.00 70.83  ? 69  PRO E CA  1 
ATOM   7593  C  C   . PRO E  1 78  ? 26.292  -3.397  11.068 1.00 72.34  ? 69  PRO E C   1 
ATOM   7594  O  O   . PRO E  1 78  ? 26.881  -3.430  12.129 1.00 75.92  ? 69  PRO E O   1 
ATOM   7595  C  CB  . PRO E  1 78  ? 26.103  -5.650  9.931  1.00 73.81  ? 69  PRO E CB  1 
ATOM   7596  C  CG  . PRO E  1 78  ? 25.053  -6.256  9.043  1.00 68.96  ? 69  PRO E CG  1 
ATOM   7597  C  CD  . PRO E  1 78  ? 24.151  -5.113  8.650  1.00 66.89  ? 69  PRO E CD  1 
ATOM   7598  N  N   . ASN E  1 79  ? 26.435  -2.393  10.212 1.00 74.07  ? 70  ASN E N   1 
ATOM   7599  C  CA  . ASN E  1 79  ? 27.302  -1.270  10.539 1.00 73.99  ? 70  ASN E CA  1 
ATOM   7600  C  C   . ASN E  1 79  ? 26.699  -0.442  11.661 1.00 81.54  ? 70  ASN E C   1 
ATOM   7601  O  O   . ASN E  1 79  ? 27.417  0.148   12.479 1.00 80.53  ? 70  ASN E O   1 
ATOM   7602  C  CB  . ASN E  1 79  ? 27.571  -0.403  9.308  1.00 80.77  ? 70  ASN E CB  1 
ATOM   7603  C  CG  . ASN E  1 79  ? 28.782  -0.870  8.527  1.00 97.00  ? 70  ASN E CG  1 
ATOM   7604  O  OD1 . ASN E  1 79  ? 28.678  -1.262  7.360  1.00 103.62 ? 70  ASN E OD1 1 
ATOM   7605  N  ND2 . ASN E  1 79  ? 29.944  -0.843  9.173  1.00 99.04  ? 70  ASN E ND2 1 
ATOM   7606  N  N   . GLU E  1 80  ? 25.371  -0.415  11.698 1.00 78.29  ? 71  GLU E N   1 
ATOM   7607  C  CA  . GLU E  1 80  ? 24.643  0.281   12.754 1.00 80.58  ? 71  GLU E CA  1 
ATOM   7608  C  C   . GLU E  1 80  ? 24.928  -0.269  14.164 1.00 81.94  ? 71  GLU E C   1 
ATOM   7609  O  O   . GLU E  1 80  ? 25.129  0.525   15.086 1.00 79.59  ? 71  GLU E O   1 
ATOM   7610  C  CB  . GLU E  1 80  ? 23.138  0.292   12.468 1.00 88.44  ? 71  GLU E CB  1 
ATOM   7611  C  CG  . GLU E  1 80  ? 22.575  1.638   12.002 1.00 96.87  ? 71  GLU E CG  1 
ATOM   7612  C  CD  . GLU E  1 80  ? 21.048  1.645   11.960 1.00 103.67 ? 71  GLU E CD  1 
ATOM   7613  O  OE1 . GLU E  1 80  ? 20.421  2.440   12.711 1.00 93.96  ? 71  GLU E OE1 1 
ATOM   7614  O  OE2 . GLU E  1 80  ? 20.482  0.845   11.174 1.00 102.51 ? 71  GLU E OE2 1 
ATOM   7615  N  N   . TYR E  1 81  ? 25.085  -1.596  14.295 1.00 80.53  ? 72  TYR E N   1 
ATOM   7616  C  CA  . TYR E  1 81  ? 25.295  -2.242  15.617 1.00 78.90  ? 72  TYR E CA  1 
ATOM   7617  C  C   . TYR E  1 81  ? 26.573  -3.092  15.972 1.00 77.93  ? 72  TYR E C   1 
ATOM   7618  O  O   . TYR E  1 81  ? 26.435  -4.057  16.723 1.00 89.16  ? 72  TYR E O   1 
ATOM   7619  C  CB  . TYR E  1 81  ? 24.155  -3.239  15.870 1.00 70.03  ? 72  TYR E CB  1 
ATOM   7620  C  CG  . TYR E  1 81  ? 22.777  -2.626  15.776 1.00 71.94  ? 72  TYR E CG  1 
ATOM   7621  C  CD1 . TYR E  1 81  ? 22.149  -2.107  16.900 1.00 63.82  ? 72  TYR E CD1 1 
ATOM   7622  C  CD2 . TYR E  1 81  ? 22.104  -2.563  14.563 1.00 71.61  ? 72  TYR E CD2 1 
ATOM   7623  C  CE1 . TYR E  1 81  ? 20.889  -1.545  16.820 1.00 62.99  ? 72  TYR E CE1 1 
ATOM   7624  C  CE2 . TYR E  1 81  ? 20.844  -2.003  14.473 1.00 69.72  ? 72  TYR E CE2 1 
ATOM   7625  C  CZ  . TYR E  1 81  ? 20.242  -1.495  15.604 1.00 66.54  ? 72  TYR E CZ  1 
ATOM   7626  O  OH  . TYR E  1 81  ? 18.988  -0.936  15.519 1.00 62.48  ? 72  TYR E OH  1 
ATOM   7627  N  N   . GLY E  1 82  ? 27.770  -2.781  15.487 1.00 77.35  ? 73  GLY E N   1 
ATOM   7628  C  CA  . GLY E  1 82  ? 28.953  -3.571  15.829 1.00 81.74  ? 73  GLY E CA  1 
ATOM   7629  C  C   . GLY E  1 82  ? 29.316  -4.628  14.780 1.00 79.84  ? 73  GLY E C   1 
ATOM   7630  O  O   . GLY E  1 82  ? 30.015  -5.568  15.125 1.00 78.13  ? 73  GLY E O   1 
ATOM   7631  N  N   . ASN E  1 83  ? 28.890  -4.470  13.521 1.00 87.56  ? 74  ASN E N   1 
ATOM   7632  C  CA  A ASN E  1 83  ? 28.981  -5.489  12.477 0.50 87.22  ? 74  ASN E CA  1 
ATOM   7633  C  CA  B ASN E  1 83  ? 29.091  -5.529  12.499 0.50 87.27  ? 74  ASN E CA  1 
ATOM   7634  C  C   . ASN E  1 83  ? 28.499  -6.871  12.952 1.00 82.93  ? 74  ASN E C   1 
ATOM   7635  O  O   . ASN E  1 83  ? 29.048  -7.917  12.615 1.00 85.31  ? 74  ASN E O   1 
ATOM   7636  C  CB  A ASN E  1 83  ? 30.366  -5.461  11.819 0.50 92.01  ? 74  ASN E CB  1 
ATOM   7637  C  CB  B ASN E  1 83  ? 30.596  -5.695  12.100 0.50 91.82  ? 74  ASN E CB  1 
ATOM   7638  C  CG  A ASN E  1 83  ? 30.866  -4.027  11.599 0.50 93.17  ? 74  ASN E CG  1 
ATOM   7639  C  CG  B ASN E  1 83  ? 30.814  -6.629  10.861 0.50 94.40  ? 74  ASN E CG  1 
ATOM   7640  O  OD1 A ASN E  1 83  ? 30.635  -3.401  10.555 0.50 78.88  ? 74  ASN E OD1 1 
ATOM   7641  O  OD1 B ASN E  1 83  ? 29.860  -6.972  10.173 0.50 94.99  ? 74  ASN E OD1 1 
ATOM   7642  N  ND2 A ASN E  1 83  ? 31.548  -3.503  12.602 0.50 99.50  ? 74  ASN E ND2 1 
ATOM   7643  N  ND2 B ASN E  1 83  ? 32.080  -7.044  10.605 0.50 100.63 ? 74  ASN E ND2 1 
ATOM   7644  N  N   . ILE E  1 84  ? 27.407  -6.849  13.731 1.00 80.79  ? 75  ILE E N   1 
ATOM   7645  C  CA  . ILE E  1 84  ? 26.764  -8.086  14.165 1.00 74.33  ? 75  ILE E CA  1 
ATOM   7646  C  C   . ILE E  1 84  ? 25.912  -8.562  13.002 1.00 73.48  ? 75  ILE E C   1 
ATOM   7647  O  O   . ILE E  1 84  ? 24.967  -7.891  12.573 1.00 68.92  ? 75  ILE E O   1 
ATOM   7648  C  CB  . ILE E  1 84  ? 25.831  -7.867  15.392 1.00 70.63  ? 75  ILE E CB  1 
ATOM   7649  C  CG1 . ILE E  1 84  ? 26.624  -7.402  16.609 1.00 67.22  ? 75  ILE E CG1 1 
ATOM   7650  C  CG2 . ILE E  1 84  ? 25.036  -9.134  15.724 1.00 57.79  ? 75  ILE E CG2 1 
ATOM   7651  C  CD1 . ILE E  1 84  ? 25.807  -7.373  17.877 1.00 60.78  ? 75  ILE E CD1 1 
ATOM   7652  N  N   . THR E  1 85  ? 26.269  -9.721  12.472 1.00 72.68  ? 76  THR E N   1 
ATOM   7653  C  CA  . THR E  1 85  ? 25.522  -10.286 11.369 1.00 72.46  ? 76  THR E CA  1 
ATOM   7654  C  C   . THR E  1 85  ? 24.422  -11.275 11.785 1.00 72.35  ? 76  THR E C   1 
ATOM   7655  O  O   . THR E  1 85  ? 23.551  -11.607 10.986 1.00 71.75  ? 76  THR E O   1 
ATOM   7656  C  CB  . THR E  1 85  ? 26.498  -10.935 10.373 1.00 74.53  ? 76  THR E CB  1 
ATOM   7657  O  OG1 . THR E  1 85  ? 27.430  -11.751 11.093 1.00 74.39  ? 76  THR E OG1 1 
ATOM   7658  C  CG2 . THR E  1 85  ? 27.274  -9.854  9.625  1.00 68.33  ? 76  THR E CG2 1 
ATOM   7659  N  N   . ASP E  1 86  ? 24.468  -11.740 13.033 1.00 70.96  ? 77  ASP E N   1 
ATOM   7660  C  CA  . ASP E  1 86  ? 23.489  -12.706 13.547 1.00 67.50  ? 77  ASP E CA  1 
ATOM   7661  C  C   . ASP E  1 86  ? 23.463  -12.758 15.089 1.00 64.51  ? 77  ASP E C   1 
ATOM   7662  O  O   . ASP E  1 86  ? 24.441  -12.388 15.748 1.00 60.91  ? 77  ASP E O   1 
ATOM   7663  C  CB  . ASP E  1 86  ? 23.783  -14.097 12.974 1.00 70.81  ? 77  ASP E CB  1 
ATOM   7664  C  CG  . ASP E  1 86  ? 25.214  -14.538 13.230 1.00 69.84  ? 77  ASP E CG  1 
ATOM   7665  O  OD1 . ASP E  1 86  ? 25.566  -14.741 14.413 1.00 76.46  ? 77  ASP E OD1 1 
ATOM   7666  O  OD2 . ASP E  1 86  ? 25.987  -14.674 12.258 1.00 67.96  ? 77  ASP E OD2 1 
ATOM   7667  N  N   . PHE E  1 87  ? 22.369  -13.255 15.662 1.00 58.18  ? 78  PHE E N   1 
ATOM   7668  C  CA  . PHE E  1 87  ? 22.301  -13.474 17.108 1.00 59.30  ? 78  PHE E CA  1 
ATOM   7669  C  C   . PHE E  1 87  ? 21.343  -14.624 17.460 1.00 54.24  ? 78  PHE E C   1 
ATOM   7670  O  O   . PHE E  1 87  ? 20.369  -14.854 16.762 1.00 45.10  ? 78  PHE E O   1 
ATOM   7671  C  CB  . PHE E  1 87  ? 21.897  -12.181 17.834 1.00 54.15  ? 78  PHE E CB  1 
ATOM   7672  C  CG  . PHE E  1 87  ? 20.471  -11.787 17.602 1.00 59.05  ? 78  PHE E CG  1 
ATOM   7673  C  CD1 . PHE E  1 87  ? 19.458  -12.280 18.415 1.00 56.96  ? 78  PHE E CD1 1 
ATOM   7674  C  CD2 . PHE E  1 87  ? 20.134  -10.943 16.554 1.00 58.02  ? 78  PHE E CD2 1 
ATOM   7675  C  CE1 . PHE E  1 87  ? 18.137  -11.932 18.189 1.00 59.19  ? 78  PHE E CE1 1 
ATOM   7676  C  CE2 . PHE E  1 87  ? 18.814  -10.584 16.322 1.00 51.29  ? 78  PHE E CE2 1 
ATOM   7677  C  CZ  . PHE E  1 87  ? 17.814  -11.081 17.139 1.00 55.33  ? 78  PHE E CZ  1 
ATOM   7678  N  N   . ARG E  1 88  ? 21.637  -15.349 18.540 1.00 61.46  ? 79  ARG E N   1 
ATOM   7679  C  CA  . ARG E  1 88  ? 20.757  -16.406 19.049 1.00 54.25  ? 79  ARG E CA  1 
ATOM   7680  C  C   . ARG E  1 88  ? 19.675  -15.809 19.919 1.00 54.55  ? 79  ARG E C   1 
ATOM   7681  O  O   . ARG E  1 88  ? 19.911  -14.819 20.595 1.00 58.64  ? 79  ARG E O   1 
ATOM   7682  C  CB  . ARG E  1 88  ? 21.545  -17.421 19.868 1.00 58.36  ? 79  ARG E CB  1 
ATOM   7683  C  CG  . ARG E  1 88  ? 22.273  -18.462 19.047 1.00 64.86  ? 79  ARG E CG  1 
ATOM   7684  C  CD  . ARG E  1 88  ? 23.553  -17.898 18.439 1.00 71.25  ? 79  ARG E CD  1 
ATOM   7685  N  NE  . ARG E  1 88  ? 24.081  -18.750 17.370 1.00 76.68  ? 79  ARG E NE  1 
ATOM   7686  C  CZ  . ARG E  1 88  ? 25.228  -18.531 16.731 1.00 79.27  ? 79  ARG E CZ  1 
ATOM   7687  N  NH1 . ARG E  1 88  ? 25.983  -17.479 17.052 1.00 77.01  ? 79  ARG E NH1 1 
ATOM   7688  N  NH2 . ARG E  1 88  ? 25.617  -19.366 15.772 1.00 71.00  ? 79  ARG E NH2 1 
ATOM   7689  N  N   . THR E  1 89  ? 18.486  -16.390 19.908 1.00 49.83  ? 80  THR E N   1 
ATOM   7690  C  CA  . THR E  1 89  ? 17.451  -15.896 20.799 1.00 57.37  ? 80  THR E CA  1 
ATOM   7691  C  C   . THR E  1 89  ? 16.494  -16.986 21.212 1.00 56.80  ? 80  THR E C   1 
ATOM   7692  O  O   . THR E  1 89  ? 16.301  -17.949 20.489 1.00 55.79  ? 80  THR E O   1 
ATOM   7693  C  CB  . THR E  1 89  ? 16.640  -14.773 20.163 1.00 53.66  ? 80  THR E CB  1 
ATOM   7694  O  OG1 . THR E  1 89  ? 15.880  -14.103 21.180 1.00 66.10  ? 80  THR E OG1 1 
ATOM   7695  C  CG2 . THR E  1 89  ? 15.694  -15.339 19.143 1.00 56.39  ? 80  THR E CG2 1 
ATOM   7696  N  N   . SER E  1 90  ? 15.897  -16.835 22.385 1.00 56.07  ? 81  SER E N   1 
ATOM   7697  C  CA  . SER E  1 90  ? 14.842  -17.744 22.786 1.00 58.08  ? 81  SER E CA  1 
ATOM   7698  C  C   . SER E  1 90  ? 13.684  -17.701 21.799 1.00 58.27  ? 81  SER E C   1 
ATOM   7699  O  O   . SER E  1 90  ? 13.260  -16.631 21.382 1.00 59.10  ? 81  SER E O   1 
ATOM   7700  C  CB  . SER E  1 90  ? 14.307  -17.380 24.154 1.00 58.34  ? 81  SER E CB  1 
ATOM   7701  O  OG  . SER E  1 90  ? 12.985  -17.876 24.279 1.00 60.57  ? 81  SER E OG  1 
ATOM   7702  N  N   . ALA E  1 91  ? 13.147  -18.865 21.461 1.00 51.36  ? 82  ALA E N   1 
ATOM   7703  C  CA  . ALA E  1 91  ? 12.087  -18.941 20.473 1.00 56.68  ? 82  ALA E CA  1 
ATOM   7704  C  C   . ALA E  1 91  ? 10.781  -18.284 20.925 1.00 58.82  ? 82  ALA E C   1 
ATOM   7705  O  O   . ALA E  1 91  ? 9.900   -18.000 20.106 1.00 57.78  ? 82  ALA E O   1 
ATOM   7706  C  CB  . ALA E  1 91  ? 11.855  -20.399 20.042 1.00 60.00  ? 82  ALA E CB  1 
ATOM   7707  N  N   . ALA E  1 92  ? 10.639  -18.046 22.222 1.00 60.72  ? 83  ALA E N   1 
ATOM   7708  C  CA  . ALA E  1 92  ? 9.449   -17.349 22.697 1.00 65.51  ? 83  ALA E CA  1 
ATOM   7709  C  C   . ALA E  1 92  ? 9.563   -15.837 22.469 1.00 65.04  ? 83  ALA E C   1 
ATOM   7710  O  O   . ALA E  1 92  ? 8.565   -15.118 22.505 1.00 67.60  ? 83  ALA E O   1 
ATOM   7711  C  CB  . ALA E  1 92  ? 9.179   -17.661 24.145 1.00 68.28  ? 83  ALA E CB  1 
ATOM   7712  N  N   . ASP E  1 93  ? 10.778  -15.367 22.203 1.00 62.09  ? 84  ASP E N   1 
ATOM   7713  C  CA  . ASP E  1 93  ? 11.006  -13.954 21.888 1.00 67.26  ? 84  ASP E CA  1 
ATOM   7714  C  C   . ASP E  1 93  ? 10.520  -13.547 20.491 1.00 64.34  ? 84  ASP E C   1 
ATOM   7715  O  O   . ASP E  1 93  ? 10.269  -12.374 20.240 1.00 63.75  ? 84  ASP E O   1 
ATOM   7716  C  CB  . ASP E  1 93  ? 12.495  -13.590 22.004 1.00 73.22  ? 84  ASP E CB  1 
ATOM   7717  C  CG  . ASP E  1 93  ? 13.026  -13.670 23.433 1.00 79.30  ? 84  ASP E CG  1 
ATOM   7718  O  OD1 . ASP E  1 93  ? 12.230  -13.933 24.376 1.00 74.35  ? 84  ASP E OD1 1 
ATOM   7719  O  OD2 . ASP E  1 93  ? 14.256  -13.455 23.594 1.00 79.15  ? 84  ASP E OD2 1 
ATOM   7720  N  N   . ILE E  1 94  ? 10.419  -14.513 19.583 1.00 62.01  ? 85  ILE E N   1 
ATOM   7721  C  CA  . ILE E  1 94  ? 10.018  -14.243 18.207 1.00 52.02  ? 85  ILE E CA  1 
ATOM   7722  C  C   . ILE E  1 94  ? 8.758   -14.985 17.857 1.00 54.44  ? 85  ILE E C   1 
ATOM   7723  O  O   . ILE E  1 94  ? 8.389   -15.962 18.506 1.00 52.26  ? 85  ILE E O   1 
ATOM   7724  C  CB  . ILE E  1 94  ? 11.075  -14.675 17.183 1.00 54.16  ? 85  ILE E CB  1 
ATOM   7725  C  CG1 . ILE E  1 94  ? 11.457  -16.144 17.395 1.00 55.75  ? 85  ILE E CG1 1 
ATOM   7726  C  CG2 . ILE E  1 94  ? 12.270  -13.761 17.231 1.00 55.85  ? 85  ILE E CG2 1 
ATOM   7727  C  CD1 . ILE E  1 94  ? 12.727  -16.558 16.714 1.00 49.56  ? 85  ILE E CD1 1 
ATOM   7728  N  N   . TRP E  1 95  ? 8.097   -14.500 16.816 1.00 55.67  ? 86  TRP E N   1 
ATOM   7729  C  CA  . TRP E  1 95  ? 6.924   -15.163 16.290 1.00 55.33  ? 86  TRP E CA  1 
ATOM   7730  C  C   . TRP E  1 95  ? 7.389   -16.449 15.622 1.00 56.90  ? 86  TRP E C   1 
ATOM   7731  O  O   . TRP E  1 95  ? 8.404   -16.467 14.934 1.00 58.08  ? 86  TRP E O   1 
ATOM   7732  C  CB  . TRP E  1 95  ? 6.206   -14.245 15.302 1.00 52.41  ? 86  TRP E CB  1 
ATOM   7733  C  CG  . TRP E  1 95  ? 5.101   -14.916 14.605 1.00 50.26  ? 86  TRP E CG  1 
ATOM   7734  C  CD1 . TRP E  1 95  ? 3.779   -14.883 14.930 1.00 60.82  ? 86  TRP E CD1 1 
ATOM   7735  C  CD2 . TRP E  1 95  ? 5.215   -15.756 13.462 1.00 50.03  ? 86  TRP E CD2 1 
ATOM   7736  N  NE1 . TRP E  1 95  ? 3.055   -15.646 14.046 1.00 59.04  ? 86  TRP E NE1 1 
ATOM   7737  C  CE2 . TRP E  1 95  ? 3.918   -16.201 13.141 1.00 53.03  ? 86  TRP E CE2 1 
ATOM   7738  C  CE3 . TRP E  1 95  ? 6.292   -16.184 12.680 1.00 55.76  ? 86  TRP E CE3 1 
ATOM   7739  C  CZ2 . TRP E  1 95  ? 3.671   -17.053 12.073 1.00 56.85  ? 86  TRP E CZ2 1 
ATOM   7740  C  CZ3 . TRP E  1 95  ? 6.043   -17.029 11.616 1.00 54.60  ? 86  TRP E CZ3 1 
ATOM   7741  C  CH2 . TRP E  1 95  ? 4.743   -17.454 11.322 1.00 52.85  ? 86  TRP E CH2 1 
ATOM   7742  N  N   . THR E  1 96  ? 6.685   -17.544 15.859 1.00 54.61  ? 87  THR E N   1 
ATOM   7743  C  CA  . THR E  1 96  ? 7.041   -18.774 15.174 1.00 51.92  ? 87  THR E CA  1 
ATOM   7744  C  C   . THR E  1 96  ? 5.811   -19.338 14.486 1.00 54.39  ? 87  THR E C   1 
ATOM   7745  O  O   . THR E  1 96  ? 4.676   -19.035 14.856 1.00 55.25  ? 87  THR E O   1 
ATOM   7746  C  CB  . THR E  1 96  ? 7.703   -19.835 16.103 1.00 55.94  ? 87  THR E CB  1 
ATOM   7747  O  OG1 . THR E  1 96  ? 6.765   -20.289 17.091 1.00 57.34  ? 87  THR E OG1 1 
ATOM   7748  C  CG2 . THR E  1 96  ? 8.957   -19.275 16.778 1.00 51.14  ? 87  THR E CG2 1 
ATOM   7749  N  N   . PRO E  1 97  ? 6.040   -20.168 13.474 1.00 53.53  ? 88  PRO E N   1 
ATOM   7750  C  CA  . PRO E  1 97  ? 4.951   -20.684 12.639 1.00 52.42  ? 88  PRO E CA  1 
ATOM   7751  C  C   . PRO E  1 97  ? 4.293   -21.912 13.260 1.00 46.86  ? 88  PRO E C   1 
ATOM   7752  O  O   . PRO E  1 97  ? 4.980   -22.753 13.839 1.00 49.96  ? 88  PRO E O   1 
ATOM   7753  C  CB  . PRO E  1 97  ? 5.664   -21.070 11.341 1.00 51.28  ? 88  PRO E CB  1 
ATOM   7754  C  CG  . PRO E  1 97  ? 7.058   -21.372 11.758 1.00 55.41  ? 88  PRO E CG  1 
ATOM   7755  C  CD  . PRO E  1 97  ? 7.364   -20.422 12.879 1.00 49.81  ? 88  PRO E CD  1 
ATOM   7756  N  N   . ASP E  1 98  ? 2.973   -22.007 13.136 1.00 43.65  ? 89  ASP E N   1 
ATOM   7757  C  CA  . ASP E  1 98  ? 2.214   -23.049 13.818 1.00 41.80  ? 89  ASP E CA  1 
ATOM   7758  C  C   . ASP E  1 98  ? 2.208   -24.344 13.014 1.00 45.20  ? 89  ASP E C   1 
ATOM   7759  O  O   . ASP E  1 98  ? 1.153   -24.930 12.771 1.00 44.90  ? 89  ASP E O   1 
ATOM   7760  C  CB  . ASP E  1 98  ? 0.779   -22.584 14.078 1.00 45.10  ? 89  ASP E CB  1 
ATOM   7761  C  CG  . ASP E  1 98  ? -0.004  -22.367 12.798 1.00 55.05  ? 89  ASP E CG  1 
ATOM   7762  O  OD1 . ASP E  1 98  ? 0.617   -22.023 11.771 1.00 54.86  ? 89  ASP E OD1 1 
ATOM   7763  O  OD2 . ASP E  1 98  ? -1.240  -22.542 12.820 1.00 54.64  ? 89  ASP E OD2 1 
ATOM   7764  N  N   . ILE E  1 99  ? 3.392   -24.787 12.606 1.00 40.81  ? 90  ILE E N   1 
ATOM   7765  C  CA  . ILE E  1 99  ? 3.530   -26.034 11.864 1.00 48.34  ? 90  ILE E CA  1 
ATOM   7766  C  C   . ILE E  1 99  ? 3.311   -27.242 12.769 1.00 51.10  ? 90  ILE E C   1 
ATOM   7767  O  O   . ILE E  1 99  ? 3.863   -27.314 13.867 1.00 54.07  ? 90  ILE E O   1 
ATOM   7768  C  CB  . ILE E  1 99  ? 4.915   -26.146 11.202 1.00 47.62  ? 90  ILE E CB  1 
ATOM   7769  C  CG1 . ILE E  1 99  ? 5.185   -24.926 10.320 1.00 52.05  ? 90  ILE E CG1 1 
ATOM   7770  C  CG2 . ILE E  1 99  ? 5.015   -27.428 10.390 1.00 52.08  ? 90  ILE E CG2 1 
ATOM   7771  C  CD1 . ILE E  1 99  ? 4.096   -24.653 9.306  1.00 60.51  ? 90  ILE E CD1 1 
ATOM   7772  N  N   . THR E  1 100 ? 2.504   -28.188 12.301 1.00 49.15  ? 91  THR E N   1 
ATOM   7773  C  CA  . THR E  1 100 ? 2.100   -29.323 13.119 1.00 45.67  ? 91  THR E CA  1 
ATOM   7774  C  C   . THR E  1 100 ? 1.979   -30.575 12.227 1.00 56.18  ? 91  THR E C   1 
ATOM   7775  O  O   . THR E  1 100 ? 1.539   -30.492 11.068 1.00 54.08  ? 91  THR E O   1 
ATOM   7776  C  CB  . THR E  1 100 ? 0.728   -29.049 13.820 1.00 44.64  ? 91  THR E CB  1 
ATOM   7777  O  OG1 . THR E  1 100 ? 0.318   -30.187 14.579 1.00 47.81  ? 91  THR E OG1 1 
ATOM   7778  C  CG2 . THR E  1 100 ? -0.339  -28.783 12.810 1.00 51.72  ? 91  THR E CG2 1 
ATOM   7779  N  N   . ALA E  1 101 ? 2.376   -31.730 12.756 1.00 48.59  ? 92  ALA E N   1 
ATOM   7780  C  CA  . ALA E  1 101 ? 2.121   -32.990 12.081 1.00 48.34  ? 92  ALA E CA  1 
ATOM   7781  C  C   . ALA E  1 101 ? 0.649   -33.345 12.256 1.00 48.08  ? 92  ALA E C   1 
ATOM   7782  O  O   . ALA E  1 101 ? 0.151   -33.389 13.366 1.00 52.87  ? 92  ALA E O   1 
ATOM   7783  C  CB  . ALA E  1 101 ? 3.000   -34.060 12.633 1.00 49.61  ? 92  ALA E CB  1 
ATOM   7784  N  N   . TYR E  1 102 ? -0.049  -33.562 11.148 1.00 49.80  ? 93  TYR E N   1 
ATOM   7785  C  CA  . TYR E  1 102 ? -1.506  -33.693 11.143 1.00 50.85  ? 93  TYR E CA  1 
ATOM   7786  C  C   . TYR E  1 102 ? -1.908  -35.074 11.604 1.00 54.08  ? 93  TYR E C   1 
ATOM   7787  O  O   . TYR E  1 102 ? -3.091  -35.362 11.809 1.00 51.43  ? 93  TYR E O   1 
ATOM   7788  C  CB  . TYR E  1 102 ? -2.023  -33.511 9.725  1.00 49.55  ? 93  TYR E CB  1 
ATOM   7789  C  CG  . TYR E  1 102 ? -1.770  -32.159 9.129  1.00 58.41  ? 93  TYR E CG  1 
ATOM   7790  C  CD1 . TYR E  1 102 ? -1.994  -31.005 9.862  1.00 63.96  ? 93  TYR E CD1 1 
ATOM   7791  C  CD2 . TYR E  1 102 ? -1.318  -32.032 7.833  1.00 61.50  ? 93  TYR E CD2 1 
ATOM   7792  C  CE1 . TYR E  1 102 ? -1.781  -29.761 9.319  1.00 61.77  ? 93  TYR E CE1 1 
ATOM   7793  C  CE2 . TYR E  1 102 ? -1.099  -30.796 7.282  1.00 65.14  ? 93  TYR E CE2 1 
ATOM   7794  C  CZ  . TYR E  1 102 ? -1.335  -29.661 8.028  1.00 65.15  ? 93  TYR E CZ  1 
ATOM   7795  O  OH  . TYR E  1 102 ? -1.120  -28.419 7.488  1.00 60.26  ? 93  TYR E OH  1 
ATOM   7796  N  N   . SER E  1 103 ? -0.902  -35.939 11.650 1.00 52.96  ? 94  SER E N   1 
ATOM   7797  C  CA  . SER E  1 103 ? -1.062  -37.358 11.889 1.00 47.78  ? 94  SER E CA  1 
ATOM   7798  C  C   . SER E  1 103 ? -0.762  -37.845 13.321 1.00 58.84  ? 94  SER E C   1 
ATOM   7799  O  O   . SER E  1 103 ? -0.956  -39.029 13.620 1.00 64.79  ? 94  SER E O   1 
ATOM   7800  C  CB  . SER E  1 103 ? -0.205  -38.093 10.849 1.00 50.93  ? 94  SER E CB  1 
ATOM   7801  O  OG  . SER E  1 103 ? -0.471  -39.475 10.820 1.00 65.02  ? 94  SER E OG  1 
ATOM   7802  N  N   . SER E  1 104 ? -0.308  -36.950 14.204 1.00 52.92  ? 95  SER E N   1 
ATOM   7803  C  CA  . SER E  1 104 ? 0.156   -37.345 15.545 1.00 52.50  ? 95  SER E CA  1 
ATOM   7804  C  C   . SER E  1 104 ? -0.903  -37.969 16.475 1.00 57.29  ? 95  SER E C   1 
ATOM   7805  O  O   . SER E  1 104 ? -2.067  -37.563 16.503 1.00 57.28  ? 95  SER E O   1 
ATOM   7806  C  CB  . SER E  1 104 ? 0.826   -36.172 16.245 1.00 51.28  ? 95  SER E CB  1 
ATOM   7807  O  OG  . SER E  1 104 ? -0.113  -35.141 16.487 1.00 54.88  ? 95  SER E OG  1 
ATOM   7808  N  N   . THR E  1 105 ? -0.499  -39.019 17.179 1.00 58.29  ? 96  THR E N   1 
ATOM   7809  C  CA  . THR E  1 105 ? -1.308  -39.612 18.247 1.00 61.66  ? 96  THR E CA  1 
ATOM   7810  C  C   . THR E  1 105 ? -0.991  -39.142 19.685 1.00 58.54  ? 96  THR E C   1 
ATOM   7811  O  O   . THR E  1 105 ? -1.747  -39.430 20.616 1.00 55.83  ? 96  THR E O   1 
ATOM   7812  C  CB  . THR E  1 105 ? -1.205  -41.153 18.194 1.00 62.56  ? 96  THR E CB  1 
ATOM   7813  O  OG1 . THR E  1 105 ? 0.110   -41.560 18.620 1.00 59.28  ? 96  THR E OG1 1 
ATOM   7814  C  CG2 . THR E  1 105 ? -1.490  -41.648 16.764 1.00 48.55  ? 96  THR E CG2 1 
ATOM   7815  N  N   A ARG E  1 106 ? 0.114   -38.421 19.849 0.50 54.54  ? 97  ARG E N   1 
ATOM   7816  N  N   B ARG E  1 106 ? 0.119   -38.431 19.860 0.50 55.29  ? 97  ARG E N   1 
ATOM   7817  C  CA  A ARG E  1 106 ? 0.533   -37.945 21.164 0.50 55.17  ? 97  ARG E CA  1 
ATOM   7818  C  CA  B ARG E  1 106 ? 0.518   -37.959 21.185 0.50 54.93  ? 97  ARG E CA  1 
ATOM   7819  C  C   A ARG E  1 106 ? 1.160   -36.565 21.073 0.50 53.83  ? 97  ARG E C   1 
ATOM   7820  C  C   B ARG E  1 106 ? 1.156   -36.580 21.083 0.50 53.16  ? 97  ARG E C   1 
ATOM   7821  O  O   A ARG E  1 106 ? 1.817   -36.244 20.087 0.50 54.54  ? 97  ARG E O   1 
ATOM   7822  O  O   B ARG E  1 106 ? 1.815   -36.275 20.094 0.50 54.20  ? 97  ARG E O   1 
ATOM   7823  C  CB  A ARG E  1 106 ? 1.539   -38.908 21.792 0.50 53.68  ? 97  ARG E CB  1 
ATOM   7824  C  CB  B ARG E  1 106 ? 1.510   -38.924 21.846 0.50 53.25  ? 97  ARG E CB  1 
ATOM   7825  C  CG  A ARG E  1 106 ? 0.907   -40.096 22.468 0.50 55.58  ? 97  ARG E CG  1 
ATOM   7826  C  CG  B ARG E  1 106 ? 1.216   -40.398 21.633 0.50 56.21  ? 97  ARG E CG  1 
ATOM   7827  C  CD  A ARG E  1 106 ? 1.837   -41.294 22.437 0.50 55.64  ? 97  ARG E CD  1 
ATOM   7828  C  CD  B ARG E  1 106 ? 1.105   -41.161 22.951 0.50 56.42  ? 97  ARG E CD  1 
ATOM   7829  N  NE  A ARG E  1 106 ? 1.130   -42.520 22.785 0.50 53.70  ? 97  ARG E NE  1 
ATOM   7830  N  NE  B ARG E  1 106 ? -0.069  -40.755 23.725 0.50 54.80  ? 97  ARG E NE  1 
ATOM   7831  C  CZ  A ARG E  1 106 ? 1.689   -43.721 22.810 0.50 54.80  ? 97  ARG E CZ  1 
ATOM   7832  C  CZ  B ARG E  1 106 ? -0.760  -41.565 24.524 0.50 49.68  ? 97  ARG E CZ  1 
ATOM   7833  N  NH1 A ARG E  1 106 ? 0.958   -44.774 23.143 0.50 60.72  ? 97  ARG E NH1 1 
ATOM   7834  N  NH1 B ARG E  1 106 ? -1.811  -41.096 25.181 0.50 48.06  ? 97  ARG E NH1 1 
ATOM   7835  N  NH2 A ARG E  1 106 ? 2.973   -43.867 22.509 0.50 53.64  ? 97  ARG E NH2 1 
ATOM   7836  N  NH2 B ARG E  1 106 ? -0.406  -42.837 24.663 0.50 40.84  ? 97  ARG E NH2 1 
ATOM   7837  N  N   . PRO E  1 107 ? 0.970   -35.743 22.113 1.00 50.83  ? 98  PRO E N   1 
ATOM   7838  C  CA  . PRO E  1 107 ? 1.604   -34.432 22.092 1.00 47.07  ? 98  PRO E CA  1 
ATOM   7839  C  C   . PRO E  1 107 ? 3.086   -34.587 21.802 1.00 46.77  ? 98  PRO E C   1 
ATOM   7840  O  O   . PRO E  1 107 ? 3.737   -35.440 22.381 1.00 52.32  ? 98  PRO E O   1 
ATOM   7841  C  CB  . PRO E  1 107 ? 1.375   -33.935 23.508 1.00 34.09  ? 98  PRO E CB  1 
ATOM   7842  C  CG  . PRO E  1 107 ? 0.107   -34.584 23.902 1.00 38.67  ? 98  PRO E CG  1 
ATOM   7843  C  CD  . PRO E  1 107 ? 0.123   -35.932 23.299 1.00 41.64  ? 98  PRO E CD  1 
ATOM   7844  N  N   . VAL E  1 108 ? 3.603   -33.785 20.886 1.00 49.93  ? 99  VAL E N   1 
ATOM   7845  C  CA  . VAL E  1 108 ? 5.014   -33.830 20.517 1.00 55.45  ? 99  VAL E CA  1 
ATOM   7846  C  C   . VAL E  1 108 ? 5.883   -33.441 21.713 1.00 49.87  ? 99  VAL E C   1 
ATOM   7847  O  O   . VAL E  1 108 ? 5.486   -32.605 22.522 1.00 53.85  ? 99  VAL E O   1 
ATOM   7848  C  CB  . VAL E  1 108 ? 5.287   -32.881 19.318 1.00 57.64  ? 99  VAL E CB  1 
ATOM   7849  C  CG1 . VAL E  1 108 ? 6.721   -33.005 18.820 1.00 51.73  ? 99  VAL E CG1 1 
ATOM   7850  C  CG2 . VAL E  1 108 ? 4.319   -33.192 18.194 1.00 61.26  ? 99  VAL E CG2 1 
ATOM   7851  N  N   . GLN E  1 109 ? 7.061   -34.043 21.835 1.00 48.77  ? 100 GLN E N   1 
ATOM   7852  C  CA  . GLN E  1 109 ? 7.956   -33.722 22.944 1.00 54.58  ? 100 GLN E CA  1 
ATOM   7853  C  C   . GLN E  1 109 ? 9.205   -33.069 22.403 1.00 55.89  ? 100 GLN E C   1 
ATOM   7854  O  O   . GLN E  1 109 ? 9.730   -33.513 21.390 1.00 52.29  ? 100 GLN E O   1 
ATOM   7855  C  CB  . GLN E  1 109 ? 8.316   -34.979 23.724 1.00 51.19  ? 100 GLN E CB  1 
ATOM   7856  C  CG  . GLN E  1 109 ? 7.104   -35.698 24.283 1.00 56.08  ? 100 GLN E CG  1 
ATOM   7857  C  CD  . GLN E  1 109 ? 7.444   -37.049 24.847 1.00 58.49  ? 100 GLN E CD  1 
ATOM   7858  O  OE1 . GLN E  1 109 ? 8.550   -37.269 25.320 1.00 61.49  ? 100 GLN E OE1 1 
ATOM   7859  N  NE2 . GLN E  1 109 ? 6.497   -37.971 24.793 1.00 57.14  ? 100 GLN E NE2 1 
ATOM   7860  N  N   . VAL E  1 110 ? 9.678   -32.005 23.050 1.00 59.21  ? 101 VAL E N   1 
ATOM   7861  C  CA  . VAL E  1 110 ? 10.835  -31.304 22.507 1.00 55.73  ? 101 VAL E CA  1 
ATOM   7862  C  C   . VAL E  1 110 ? 12.103  -31.734 23.182 1.00 50.93  ? 101 VAL E C   1 
ATOM   7863  O  O   . VAL E  1 110 ? 12.174  -31.718 24.388 1.00 58.58  ? 101 VAL E O   1 
ATOM   7864  C  CB  . VAL E  1 110 ? 10.715  -29.802 22.577 1.00 58.17  ? 101 VAL E CB  1 
ATOM   7865  C  CG1 . VAL E  1 110 ? 12.091  -29.196 22.426 1.00 58.59  ? 101 VAL E CG1 1 
ATOM   7866  C  CG2 . VAL E  1 110 ? 9.794   -29.314 21.450 1.00 60.24  ? 101 VAL E CG2 1 
ATOM   7867  N  N   . LEU E  1 111 ? 13.080  -32.167 22.391 1.00 51.63  ? 102 LEU E N   1 
ATOM   7868  C  CA  . LEU E  1 111 ? 14.285  -32.774 22.937 1.00 48.76  ? 102 LEU E CA  1 
ATOM   7869  C  C   . LEU E  1 111 ? 15.458  -31.816 23.056 1.00 53.00  ? 102 LEU E C   1 
ATOM   7870  O  O   . LEU E  1 111 ? 16.511  -32.194 23.586 1.00 53.66  ? 102 LEU E O   1 
ATOM   7871  C  CB  . LEU E  1 111 ? 14.694  -34.019 22.142 1.00 48.94  ? 102 LEU E CB  1 
ATOM   7872  C  CG  . LEU E  1 111 ? 13.571  -34.956 21.704 1.00 52.71  ? 102 LEU E CG  1 
ATOM   7873  C  CD1 . LEU E  1 111 ? 14.126  -36.232 21.142 1.00 55.17  ? 102 LEU E CD1 1 
ATOM   7874  C  CD2 . LEU E  1 111 ? 12.664  -35.249 22.861 1.00 52.52  ? 102 LEU E CD2 1 
ATOM   7875  N  N   . SER E  1 112 ? 15.283  -30.581 22.584 1.00 55.44  ? 103 SER E N   1 
ATOM   7876  C  CA  . SER E  1 112 ? 16.373  -29.592 22.618 1.00 55.20  ? 103 SER E CA  1 
ATOM   7877  C  C   . SER E  1 112 ? 15.933  -28.242 23.143 1.00 52.28  ? 103 SER E C   1 
ATOM   7878  O  O   . SER E  1 112 ? 14.748  -27.987 23.272 1.00 54.63  ? 103 SER E O   1 
ATOM   7879  C  CB  . SER E  1 112 ? 17.018  -29.428 21.246 1.00 57.63  ? 103 SER E CB  1 
ATOM   7880  O  OG  . SER E  1 112 ? 16.036  -29.319 20.239 1.00 63.45  ? 103 SER E OG  1 
ATOM   7881  N  N   . PRO E  1 113 ? 16.898  -27.387 23.487 1.00 52.31  ? 104 PRO E N   1 
ATOM   7882  C  CA  . PRO E  1 113 ? 16.606  -25.998 23.848 1.00 57.11  ? 104 PRO E CA  1 
ATOM   7883  C  C   . PRO E  1 113 ? 15.765  -25.343 22.754 1.00 58.29  ? 104 PRO E C   1 
ATOM   7884  O  O   . PRO E  1 113 ? 15.915  -25.686 21.579 1.00 58.65  ? 104 PRO E O   1 
ATOM   7885  C  CB  . PRO E  1 113 ? 17.990  -25.350 23.870 1.00 51.00  ? 104 PRO E CB  1 
ATOM   7886  C  CG  . PRO E  1 113 ? 18.919  -26.455 24.135 1.00 51.95  ? 104 PRO E CG  1 
ATOM   7887  C  CD  . PRO E  1 113 ? 18.342  -27.656 23.458 1.00 55.30  ? 104 PRO E CD  1 
ATOM   7888  N  N   . GLN E  1 114 ? 14.893  -24.411 23.103 1.00 53.54  ? 105 GLN E N   1 
ATOM   7889  C  CA  . GLN E  1 114 ? 14.170  -23.759 22.036 1.00 61.05  ? 105 GLN E CA  1 
ATOM   7890  C  C   . GLN E  1 114 ? 14.795  -22.396 21.765 1.00 53.40  ? 105 GLN E C   1 
ATOM   7891  O  O   . GLN E  1 114 ? 14.595  -21.421 22.476 1.00 52.43  ? 105 GLN E O   1 
ATOM   7892  C  CB  . GLN E  1 114 ? 12.691  -23.674 22.391 1.00 65.06  ? 105 GLN E CB  1 
ATOM   7893  C  CG  . GLN E  1 114 ? 12.250  -24.896 23.164 1.00 69.21  ? 105 GLN E CG  1 
ATOM   7894  C  CD  . GLN E  1 114 ? 10.782  -25.194 23.012 1.00 77.15  ? 105 GLN E CD  1 
ATOM   7895  O  OE1 . GLN E  1 114 ? 10.009  -25.029 23.957 1.00 75.92  ? 105 GLN E OE1 1 
ATOM   7896  N  NE2 . GLN E  1 114 ? 10.388  -25.652 21.826 1.00 61.87  ? 105 GLN E NE2 1 
ATOM   7897  N  N   . ASN E  1 115 ? 15.508  -22.348 20.657 1.00 53.29  ? 106 ASN E N   1 
ATOM   7898  C  CA  . ASN E  1 115 ? 16.306  -21.209 20.299 1.00 51.54  ? 106 ASN E CA  1 
ATOM   7899  C  C   . ASN E  1 115 ? 16.302  -21.123 18.807 1.00 55.19  ? 106 ASN E C   1 
ATOM   7900  O  O   . ASN E  1 115 ? 16.096  -22.110 18.113 1.00 56.43  ? 106 ASN E O   1 
ATOM   7901  C  CB  . ASN E  1 115 ? 17.725  -21.381 20.796 1.00 50.28  ? 106 ASN E CB  1 
ATOM   7902  C  CG  . ASN E  1 115 ? 17.810  -21.343 22.310 1.00 64.00  ? 106 ASN E CG  1 
ATOM   7903  O  OD1 . ASN E  1 115 ? 17.083  -20.588 22.959 1.00 58.33  ? 106 ASN E OD1 1 
ATOM   7904  N  ND2 . ASN E  1 115 ? 18.693  -22.165 22.885 1.00 68.05  ? 106 ASN E ND2 1 
ATOM   7905  N  N   . ALA E  1 116 ? 16.526  -19.927 18.314 1.00 54.60  ? 107 ALA E N   1 
ATOM   7906  C  CA  . ALA E  1 116 ? 16.433  -19.679 16.910 1.00 49.10  ? 107 ALA E CA  1 
ATOM   7907  C  C   . ALA E  1 116 ? 17.627  -18.814 16.560 1.00 57.14  ? 107 ALA E C   1 
ATOM   7908  O  O   . ALA E  1 116 ? 18.016  -17.960 17.352 1.00 61.55  ? 107 ALA E O   1 
ATOM   7909  C  CB  . ALA E  1 116 ? 15.151  -18.960 16.637 1.00 53.08  ? 107 ALA E CB  1 
ATOM   7910  N  N   . LEU E  1 117 ? 18.241  -19.048 15.406 1.00 58.62  ? 108 LEU E N   1 
ATOM   7911  C  CA  . LEU E  1 117 ? 19.246  -18.116 14.922 1.00 56.94  ? 108 LEU E CA  1 
ATOM   7912  C  C   . LEU E  1 117 ? 18.510  -17.041 14.145 1.00 52.09  ? 108 LEU E C   1 
ATOM   7913  O  O   . LEU E  1 117 ? 17.546  -17.349 13.447 1.00 58.58  ? 108 LEU E O   1 
ATOM   7914  C  CB  . LEU E  1 117 ? 20.279  -18.817 14.040 1.00 55.69  ? 108 LEU E CB  1 
ATOM   7915  C  CG  . LEU E  1 117 ? 21.509  -17.945 13.771 1.00 59.33  ? 108 LEU E CG  1 
ATOM   7916  C  CD1 . LEU E  1 117 ? 22.212  -17.621 15.080 1.00 60.69  ? 108 LEU E CD1 1 
ATOM   7917  C  CD2 . LEU E  1 117 ? 22.477  -18.606 12.795 1.00 59.89  ? 108 LEU E CD2 1 
ATOM   7918  N  N   . VAL E  1 118 ? 18.930  -15.785 14.286 1.00 52.94  ? 109 VAL E N   1 
ATOM   7919  C  CA  . VAL E  1 118 ? 18.384  -14.690 13.472 1.00 59.23  ? 109 VAL E CA  1 
ATOM   7920  C  C   . VAL E  1 118 ? 19.526  -13.893 12.853 1.00 58.39  ? 109 VAL E C   1 
ATOM   7921  O  O   . VAL E  1 118 ? 20.543  -13.665 13.511 1.00 59.42  ? 109 VAL E O   1 
ATOM   7922  C  CB  . VAL E  1 118 ? 17.549  -13.699 14.314 1.00 56.22  ? 109 VAL E CB  1 
ATOM   7923  C  CG1 . VAL E  1 118 ? 16.843  -12.705 13.410 1.00 55.86  ? 109 VAL E CG1 1 
ATOM   7924  C  CG2 . VAL E  1 118 ? 16.547  -14.430 15.209 1.00 50.60  ? 109 VAL E CG2 1 
ATOM   7925  N  N   . ASN E  1 119 ? 19.390  -13.447 11.607 1.00 54.88  ? 110 ASN E N   1 
ATOM   7926  C  CA  . ASN E  1 119 ? 20.404  -12.505 11.122 1.00 66.97  ? 110 ASN E CA  1 
ATOM   7927  C  C   . ASN E  1 119 ? 19.980  -11.275 10.331 1.00 63.35  ? 110 ASN E C   1 
ATOM   7928  O  O   . ASN E  1 119 ? 18.796  -11.037 10.125 1.00 66.88  ? 110 ASN E O   1 
ATOM   7929  C  CB  . ASN E  1 119 ? 21.540  -13.223 10.418 1.00 71.48  ? 110 ASN E CB  1 
ATOM   7930  C  CG  . ASN E  1 119 ? 21.118  -13.834 9.122  1.00 78.17  ? 110 ASN E CG  1 
ATOM   7931  O  OD1 . ASN E  1 119 ? 20.096  -13.518 8.592  1.00 68.83  ? 110 ASN E OD1 1 
ATOM   7932  N  ND2 . ASN E  1 119 ? 21.933  -14.690 8.592  1.00 89.49  ? 110 ASN E ND2 1 
ATOM   7933  N  N   . SER E  1 120 ? 20.981  -10.498 9.914  1.00 63.62  ? 111 SER E N   1 
ATOM   7934  C  CA  . SER E  1 120 ? 20.792  -9.112  9.474  1.00 67.65  ? 111 SER E CA  1 
ATOM   7935  C  C   . SER E  1 120 ? 19.683  -8.924  8.430  1.00 65.74  ? 111 SER E C   1 
ATOM   7936  O  O   . SER E  1 120 ? 18.936  -7.953  8.493  1.00 65.16  ? 111 SER E O   1 
ATOM   7937  C  CB  . SER E  1 120 ? 22.116  -8.521  8.980  1.00 65.72  ? 111 SER E CB  1 
ATOM   7938  O  OG  . SER E  1 120 ? 22.554  -9.161  7.795  1.00 67.03  ? 111 SER E OG  1 
ATOM   7939  N  N   . SER E  1 121 ? 19.537  -9.874  7.512  1.00 63.23  ? 112 SER E N   1 
ATOM   7940  C  CA  . SER E  1 121 ? 18.522  -9.780  6.462  1.00 71.36  ? 112 SER E CA  1 
ATOM   7941  C  C   . SER E  1 121 ? 17.154  -10.269 6.946  1.00 69.94  ? 112 SER E C   1 
ATOM   7942  O  O   . SER E  1 121 ? 16.195  -10.347 6.179  1.00 70.04  ? 112 SER E O   1 
ATOM   7943  C  CB  . SER E  1 121 ? 18.963  -10.524 5.193  1.00 69.05  ? 112 SER E CB  1 
ATOM   7944  O  OG  . SER E  1 121 ? 19.591  -11.755 5.503  1.00 71.02  ? 112 SER E OG  1 
ATOM   7945  N  N   . GLY E  1 122 ? 17.083  -10.631 8.217  1.00 61.88  ? 113 GLY E N   1 
ATOM   7946  C  CA  . GLY E  1 122 ? 15.823  -10.979 8.829  1.00 61.76  ? 113 GLY E CA  1 
ATOM   7947  C  C   . GLY E  1 122 ? 15.422  -12.419 8.602  1.00 62.78  ? 113 GLY E C   1 
ATOM   7948  O  O   . GLY E  1 122 ? 14.236  -12.738 8.661  1.00 58.83  ? 113 GLY E O   1 
ATOM   7949  N  N   . HIS E  1 123 ? 16.399  -13.289 8.347  1.00 61.31  ? 114 HIS E N   1 
ATOM   7950  C  CA  . HIS E  1 123 ? 16.142  -14.727 8.259  1.00 59.87  ? 114 HIS E CA  1 
ATOM   7951  C  C   . HIS E  1 123 ? 16.185  -15.407 9.619  1.00 65.46  ? 114 HIS E C   1 
ATOM   7952  O  O   . HIS E  1 123 ? 17.126  -15.223 10.395 1.00 69.36  ? 114 HIS E O   1 
ATOM   7953  C  CB  . HIS E  1 123 ? 17.142  -15.406 7.336  1.00 67.07  ? 114 HIS E CB  1 
ATOM   7954  C  CG  . HIS E  1 123 ? 16.820  -15.243 5.884  1.00 79.59  ? 114 HIS E CG  1 
ATOM   7955  N  ND1 . HIS E  1 123 ? 17.388  -14.259 5.103  1.00 80.35  ? 114 HIS E ND1 1 
ATOM   7956  C  CD2 . HIS E  1 123 ? 15.984  -15.932 5.074  1.00 66.50  ? 114 HIS E CD2 1 
ATOM   7957  C  CE1 . HIS E  1 123 ? 16.914  -14.345 3.876  1.00 75.67  ? 114 HIS E CE1 1 
ATOM   7958  N  NE2 . HIS E  1 123 ? 16.061  -15.353 3.832  1.00 84.07  ? 114 HIS E NE2 1 
ATOM   7959  N  N   . VAL E  1 124 ? 15.161  -16.194 9.910  1.00 60.03  ? 115 VAL E N   1 
ATOM   7960  C  CA  . VAL E  1 124 ? 15.111  -16.908 11.172 1.00 60.54  ? 115 VAL E CA  1 
ATOM   7961  C  C   . VAL E  1 124 ? 15.346  -18.372 10.893 1.00 64.50  ? 115 VAL E C   1 
ATOM   7962  O  O   . VAL E  1 124 ? 14.746  -18.939 9.977  1.00 64.30  ? 115 VAL E O   1 
ATOM   7963  C  CB  . VAL E  1 124 ? 13.744  -16.785 11.842 1.00 54.84  ? 115 VAL E CB  1 
ATOM   7964  C  CG1 . VAL E  1 124 ? 13.763  -17.490 13.191 1.00 55.12  ? 115 VAL E CG1 1 
ATOM   7965  C  CG2 . VAL E  1 124 ? 13.368  -15.340 11.979 1.00 52.22  ? 115 VAL E CG2 1 
ATOM   7966  N  N   . GLN E  1 125 ? 16.207  -18.995 11.683 1.00 62.48  ? 116 GLN E N   1 
ATOM   7967  C  CA  . GLN E  1 125 ? 16.461  -20.413 11.510 1.00 63.36  ? 116 GLN E CA  1 
ATOM   7968  C  C   . GLN E  1 125 ? 16.170  -21.136 12.812 1.00 61.07  ? 116 GLN E C   1 
ATOM   7969  O  O   . GLN E  1 125 ? 16.799  -20.872 13.822 1.00 59.53  ? 116 GLN E O   1 
ATOM   7970  C  CB  . GLN E  1 125 ? 17.904  -20.626 11.090 1.00 63.61  ? 116 GLN E CB  1 
ATOM   7971  C  CG  . GLN E  1 125 ? 18.142  -21.898 10.337 1.00 70.04  ? 116 GLN E CG  1 
ATOM   7972  C  CD  . GLN E  1 125 ? 19.543  -21.946 9.786  1.00 88.00  ? 116 GLN E CD  1 
ATOM   7973  O  OE1 . GLN E  1 125 ? 20.117  -20.907 9.447  1.00 88.98  ? 116 GLN E OE1 1 
ATOM   7974  N  NE2 . GLN E  1 125 ? 20.115  -23.145 9.706  1.00 88.06  ? 116 GLN E NE2 1 
ATOM   7975  N  N   . TYR E  1 126 ? 15.209  -22.044 12.777 1.00 56.68  ? 117 TYR E N   1 
ATOM   7976  C  CA  . TYR E  1 126 ? 14.752  -22.737 13.967 1.00 54.09  ? 117 TYR E CA  1 
ATOM   7977  C  C   . TYR E  1 126 ? 14.842  -24.242 13.722 1.00 60.23  ? 117 TYR E C   1 
ATOM   7978  O  O   . TYR E  1 126 ? 14.422  -24.738 12.688 1.00 63.13  ? 117 TYR E O   1 
ATOM   7979  C  CB  . TYR E  1 126 ? 13.324  -22.295 14.253 1.00 58.09  ? 117 TYR E CB  1 
ATOM   7980  C  CG  . TYR E  1 126 ? 12.682  -22.901 15.471 1.00 57.62  ? 117 TYR E CG  1 
ATOM   7981  C  CD1 . TYR E  1 126 ? 13.314  -22.881 16.704 1.00 57.86  ? 117 TYR E CD1 1 
ATOM   7982  C  CD2 . TYR E  1 126 ? 11.411  -23.448 15.396 1.00 61.94  ? 117 TYR E CD2 1 
ATOM   7983  C  CE1 . TYR E  1 126 ? 12.705  -23.421 17.821 1.00 61.61  ? 117 TYR E CE1 1 
ATOM   7984  C  CE2 . TYR E  1 126 ? 10.794  -23.984 16.500 1.00 53.82  ? 117 TYR E CE2 1 
ATOM   7985  C  CZ  . TYR E  1 126 ? 11.442  -23.970 17.705 1.00 64.84  ? 117 TYR E CZ  1 
ATOM   7986  O  OH  . TYR E  1 126 ? 10.818  -24.519 18.797 1.00 84.50  ? 117 TYR E OH  1 
ATOM   7987  N  N   . LEU E  1 127 ? 15.421  -24.970 14.663 1.00 63.17  ? 118 LEU E N   1 
ATOM   7988  C  CA  . LEU E  1 127 ? 15.763  -26.365 14.420 1.00 60.39  ? 118 LEU E CA  1 
ATOM   7989  C  C   . LEU E  1 127 ? 15.523  -27.233 15.657 1.00 61.08  ? 118 LEU E C   1 
ATOM   7990  O  O   . LEU E  1 127 ? 16.471  -27.730 16.261 1.00 62.50  ? 118 LEU E O   1 
ATOM   7991  C  CB  . LEU E  1 127 ? 17.233  -26.436 13.999 1.00 64.10  ? 118 LEU E CB  1 
ATOM   7992  C  CG  . LEU E  1 127 ? 17.737  -27.620 13.187 1.00 73.30  ? 118 LEU E CG  1 
ATOM   7993  C  CD1 . LEU E  1 127 ? 19.069  -27.266 12.564 1.00 83.53  ? 118 LEU E CD1 1 
ATOM   7994  C  CD2 . LEU E  1 127 ? 17.863  -28.847 14.053 1.00 68.91  ? 118 LEU E CD2 1 
ATOM   7995  N  N   . PRO E  1 128 ? 14.253  -27.388 16.058 1.00 58.54  ? 119 PRO E N   1 
ATOM   7996  C  CA  . PRO E  1 128 ? 13.913  -28.234 17.213 1.00 55.59  ? 119 PRO E CA  1 
ATOM   7997  C  C   . PRO E  1 128 ? 14.078  -29.749 16.988 1.00 56.75  ? 119 PRO E C   1 
ATOM   7998  O  O   . PRO E  1 128 ? 13.599  -30.306 16.002 1.00 60.52  ? 119 PRO E O   1 
ATOM   7999  C  CB  . PRO E  1 128 ? 12.447  -27.894 17.474 1.00 55.76  ? 119 PRO E CB  1 
ATOM   8000  C  CG  . PRO E  1 128 ? 11.929  -27.382 16.154 1.00 56.73  ? 119 PRO E CG  1 
ATOM   8001  C  CD  . PRO E  1 128 ? 13.075  -26.748 15.445 1.00 53.57  ? 119 PRO E CD  1 
ATOM   8002  N  N   . ALA E  1 129 ? 14.718  -30.422 17.937 1.00 59.83  ? 120 ALA E N   1 
ATOM   8003  C  CA  . ALA E  1 129 ? 14.750  -31.877 17.949 1.00 55.63  ? 120 ALA E CA  1 
ATOM   8004  C  C   . ALA E  1 129 ? 13.421  -32.292 18.558 1.00 55.31  ? 120 ALA E C   1 
ATOM   8005  O  O   . ALA E  1 129 ? 12.887  -31.579 19.387 1.00 65.93  ? 120 ALA E O   1 
ATOM   8006  C  CB  . ALA E  1 129 ? 15.915  -32.365 18.780 1.00 47.87  ? 120 ALA E CB  1 
ATOM   8007  N  N   . GLN E  1 130 ? 12.851  -33.405 18.131 1.00 51.77  ? 121 GLN E N   1 
ATOM   8008  C  CA  . GLN E  1 130 ? 11.539  -33.804 18.633 1.00 52.36  ? 121 GLN E CA  1 
ATOM   8009  C  C   . GLN E  1 130 ? 11.318  -35.315 18.606 1.00 59.17  ? 121 GLN E C   1 
ATOM   8010  O  O   . GLN E  1 130 ? 11.907  -36.036 17.798 1.00 59.09  ? 121 GLN E O   1 
ATOM   8011  C  CB  . GLN E  1 130 ? 10.430  -33.143 17.814 1.00 54.53  ? 121 GLN E CB  1 
ATOM   8012  C  CG  . GLN E  1 130 ? 10.533  -31.639 17.698 1.00 53.95  ? 121 GLN E CG  1 
ATOM   8013  C  CD  . GLN E  1 130 ? 9.335   -31.056 17.002 1.00 57.17  ? 121 GLN E CD  1 
ATOM   8014  O  OE1 . GLN E  1 130 ? 8.747   -31.683 16.123 1.00 57.50  ? 121 GLN E OE1 1 
ATOM   8015  N  NE2 . GLN E  1 130 ? 8.957   -29.855 17.395 1.00 60.16  ? 121 GLN E NE2 1 
ATOM   8016  N  N   . ARG E  1 131 ? 10.450  -35.797 19.482 1.00 52.35  ? 122 ARG E N   1 
ATOM   8017  C  CA  . ARG E  1 131 ? 10.031  -37.170 19.391 1.00 45.60  ? 122 ARG E CA  1 
ATOM   8018  C  C   . ARG E  1 131 ? 8.548   -37.183 19.152 1.00 49.03  ? 122 ARG E C   1 
ATOM   8019  O  O   . ARG E  1 131 ? 7.790   -36.610 19.938 1.00 45.99  ? 122 ARG E O   1 
ATOM   8020  C  CB  . ARG E  1 131 ? 10.340  -37.933 20.657 1.00 54.60  ? 122 ARG E CB  1 
ATOM   8021  C  CG  . ARG E  1 131 ? 9.575   -39.245 20.718 1.00 60.37  ? 122 ARG E CG  1 
ATOM   8022  C  CD  . ARG E  1 131 ? 10.206  -40.156 21.702 1.00 55.49  ? 122 ARG E CD  1 
ATOM   8023  N  NE  . ARG E  1 131 ? 9.539   -41.439 21.819 1.00 52.13  ? 122 ARG E NE  1 
ATOM   8024  C  CZ  . ARG E  1 131 ? 10.117  -42.474 22.414 1.00 57.37  ? 122 ARG E CZ  1 
ATOM   8025  N  NH1 . ARG E  1 131 ? 11.348  -42.345 22.902 1.00 57.52  ? 122 ARG E NH1 1 
ATOM   8026  N  NH2 . ARG E  1 131 ? 9.487   -43.628 22.517 1.00 55.06  ? 122 ARG E NH2 1 
ATOM   8027  N  N   . LEU E  1 132 ? 8.151   -37.840 18.055 1.00 53.61  ? 123 LEU E N   1 
ATOM   8028  C  CA  . LEU E  1 132 ? 6.764   -37.870 17.594 1.00 47.62  ? 123 LEU E CA  1 
ATOM   8029  C  C   . LEU E  1 132 ? 6.223   -39.301 17.519 1.00 44.56  ? 123 LEU E C   1 
ATOM   8030  O  O   . LEU E  1 132 ? 6.935   -40.232 17.150 1.00 42.55  ? 123 LEU E O   1 
ATOM   8031  C  CB  . LEU E  1 132 ? 6.616   -37.121 16.247 1.00 44.30  ? 123 LEU E CB  1 
ATOM   8032  C  CG  . LEU E  1 132 ? 5.278   -37.096 15.460 1.00 49.68  ? 123 LEU E CG  1 
ATOM   8033  C  CD1 . LEU E  1 132 ? 4.181   -36.294 16.138 1.00 51.62  ? 123 LEU E CD1 1 
ATOM   8034  C  CD2 . LEU E  1 132 ? 5.470   -36.576 14.047 1.00 48.87  ? 123 LEU E CD2 1 
ATOM   8035  N  N   . SER E  1 133 ? 4.969   -39.452 17.932 1.00 46.69  ? 124 SER E N   1 
ATOM   8036  C  CA  . SER E  1 133 ? 4.187   -40.656 17.712 1.00 49.05  ? 124 SER E CA  1 
ATOM   8037  C  C   . SER E  1 133 ? 3.088   -40.341 16.726 1.00 51.87  ? 124 SER E C   1 
ATOM   8038  O  O   . SER E  1 133 ? 2.297   -39.426 16.941 1.00 53.30  ? 124 SER E O   1 
ATOM   8039  C  CB  . SER E  1 133 ? 3.549   -41.133 19.009 1.00 50.16  ? 124 SER E CB  1 
ATOM   8040  O  OG  . SER E  1 133 ? 4.541   -41.577 19.907 1.00 53.34  ? 124 SER E OG  1 
ATOM   8041  N  N   . PHE E  1 134 ? 3.032   -41.100 15.639 1.00 59.58  ? 125 PHE E N   1 
ATOM   8042  C  CA  . PHE E  1 134 ? 2.000   -40.875 14.632 1.00 58.06  ? 125 PHE E CA  1 
ATOM   8043  C  C   . PHE E  1 134 ? 1.405   -42.174 14.172 1.00 58.41  ? 125 PHE E C   1 
ATOM   8044  O  O   . PHE E  1 134 ? 1.991   -43.240 14.391 1.00 57.70  ? 125 PHE E O   1 
ATOM   8045  C  CB  . PHE E  1 134 ? 2.549   -40.103 13.436 1.00 54.35  ? 125 PHE E CB  1 
ATOM   8046  C  CG  . PHE E  1 134 ? 3.724   -40.760 12.748 1.00 62.02  ? 125 PHE E CG  1 
ATOM   8047  C  CD1 . PHE E  1 134 ? 3.549   -41.444 11.543 1.00 62.08  ? 125 PHE E CD1 1 
ATOM   8048  C  CD2 . PHE E  1 134 ? 5.011   -40.651 13.276 1.00 63.65  ? 125 PHE E CD2 1 
ATOM   8049  C  CE1 . PHE E  1 134 ? 4.624   -42.029 10.891 1.00 59.94  ? 125 PHE E CE1 1 
ATOM   8050  C  CE2 . PHE E  1 134 ? 6.096   -41.236 12.631 1.00 66.48  ? 125 PHE E CE2 1 
ATOM   8051  C  CZ  . PHE E  1 134 ? 5.898   -41.924 11.434 1.00 64.24  ? 125 PHE E CZ  1 
ATOM   8052  N  N   . MET E  1 135 ? 0.257   -42.075 13.506 1.00 58.49  ? 126 MET E N   1 
ATOM   8053  C  CA  . MET E  1 135 ? -0.381  -43.256 12.953 1.00 59.97  ? 126 MET E CA  1 
ATOM   8054  C  C   . MET E  1 135 ? 0.482   -43.780 11.813 1.00 57.47  ? 126 MET E C   1 
ATOM   8055  O  O   . MET E  1 135 ? 0.788   -43.057 10.851 1.00 55.65  ? 126 MET E O   1 
ATOM   8056  C  CB  . MET E  1 135 ? -1.772  -42.912 12.424 1.00 54.96  ? 126 MET E CB  1 
ATOM   8057  C  CG  . MET E  1 135 ? -2.633  -42.188 13.400 1.00 53.52  ? 126 MET E CG  1 
ATOM   8058  S  SD  . MET E  1 135 ? -3.691  -41.109 12.487 1.00 52.69  ? 126 MET E SD  1 
ATOM   8059  C  CE  . MET E  1 135 ? -4.658  -40.344 13.764 1.00 57.60  ? 126 MET E CE  1 
ATOM   8060  N  N   . CYS E  1 136 ? 0.888   -45.039 11.955 1.00 59.45  ? 127 CYS E N   1 
ATOM   8061  C  CA  . CYS E  1 136 ? 1.570   -45.795 10.912 1.00 63.87  ? 127 CYS E CA  1 
ATOM   8062  C  C   . CYS E  1 136 ? 1.333   -47.270 11.156 1.00 62.30  ? 127 CYS E C   1 
ATOM   8063  O  O   . CYS E  1 136 ? 1.101   -47.692 12.295 1.00 56.82  ? 127 CYS E O   1 
ATOM   8064  C  CB  . CYS E  1 136 ? 3.067   -45.507 10.877 1.00 65.11  ? 127 CYS E CB  1 
ATOM   8065  S  SG  . CYS E  1 136 ? 4.078   -46.815 10.171 1.00 71.50  ? 127 CYS E SG  1 
ATOM   8066  N  N   . ASP E  1 137 ? 1.398   -48.049 10.082 1.00 66.86  ? 128 ASP E N   1 
ATOM   8067  C  CA  . ASP E  1 137 ? 1.264   -49.492 10.176 1.00 67.60  ? 128 ASP E CA  1 
ATOM   8068  C  C   . ASP E  1 137 ? 2.612   -50.163 9.956  1.00 70.07  ? 128 ASP E C   1 
ATOM   8069  O  O   . ASP E  1 137 ? 3.151   -50.145 8.850  1.00 73.43  ? 128 ASP E O   1 
ATOM   8070  C  CB  . ASP E  1 137 ? 0.243   -50.009 9.167  1.00 70.08  ? 128 ASP E CB  1 
ATOM   8071  C  CG  . ASP E  1 137 ? -0.182  -51.435 9.452  1.00 72.67  ? 128 ASP E CG  1 
ATOM   8072  O  OD1 . ASP E  1 137 ? 0.682   -52.243 9.846  1.00 68.59  ? 128 ASP E OD1 1 
ATOM   8073  O  OD2 . ASP E  1 137 ? -1.382  -51.740 9.287  1.00 69.92  ? 128 ASP E OD2 1 
ATOM   8074  N  N   . PRO E  1 138 ? 3.164   -50.745 11.023 1.00 66.13  ? 129 PRO E N   1 
ATOM   8075  C  CA  . PRO E  1 138 ? 4.457   -51.423 11.015 1.00 71.45  ? 129 PRO E CA  1 
ATOM   8076  C  C   . PRO E  1 138 ? 4.428   -52.695 10.159 1.00 69.95  ? 129 PRO E C   1 
ATOM   8077  O  O   . PRO E  1 138 ? 5.492   -53.243 9.866  1.00 64.34  ? 129 PRO E O   1 
ATOM   8078  C  CB  . PRO E  1 138 ? 4.699   -51.730 12.496 1.00 71.00  ? 129 PRO E CB  1 
ATOM   8079  C  CG  . PRO E  1 138 ? 3.345   -51.787 13.093 1.00 68.40  ? 129 PRO E CG  1 
ATOM   8080  C  CD  . PRO E  1 138 ? 2.524   -50.790 12.349 1.00 69.03  ? 129 PRO E CD  1 
ATOM   8081  N  N   . THR E  1 139 ? 3.232   -53.156 9.780  1.00 74.11  ? 130 THR E N   1 
ATOM   8082  C  CA  . THR E  1 139 ? 3.086   -54.467 9.135  1.00 79.28  ? 130 THR E CA  1 
ATOM   8083  C  C   . THR E  1 139 ? 4.011   -54.644 7.948  1.00 71.72  ? 130 THR E C   1 
ATOM   8084  O  O   . THR E  1 139 ? 4.044   -53.815 7.033  1.00 62.45  ? 130 THR E O   1 
ATOM   8085  C  CB  . THR E  1 139 ? 1.654   -54.757 8.629  1.00 71.43  ? 130 THR E CB  1 
ATOM   8086  O  OG1 . THR E  1 139 ? 0.733   -54.782 9.727  1.00 81.28  ? 130 THR E OG1 1 
ATOM   8087  C  CG2 . THR E  1 139 ? 1.633   -56.110 7.971  1.00 67.44  ? 130 THR E CG2 1 
ATOM   8088  N  N   . GLY E  1 140 ? 4.745   -55.751 7.972  1.00 61.13  ? 131 GLY E N   1 
ATOM   8089  C  CA  . GLY E  1 140 ? 5.711   -56.048 6.937  1.00 73.68  ? 131 GLY E CA  1 
ATOM   8090  C  C   . GLY E  1 140 ? 7.099   -55.524 7.231  1.00 72.78  ? 131 GLY E C   1 
ATOM   8091  O  O   . GLY E  1 140 ? 7.959   -55.503 6.357  1.00 75.90  ? 131 GLY E O   1 
ATOM   8092  N  N   . VAL E  1 141 ? 7.329   -55.105 8.465  1.00 69.16  ? 132 VAL E N   1 
ATOM   8093  C  CA  . VAL E  1 141 ? 8.602   -54.503 8.812  1.00 70.44  ? 132 VAL E CA  1 
ATOM   8094  C  C   . VAL E  1 141 ? 9.626   -55.609 9.090  1.00 77.49  ? 132 VAL E C   1 
ATOM   8095  O  O   . VAL E  1 141 ? 10.840  -55.383 9.084  1.00 77.44  ? 132 VAL E O   1 
ATOM   8096  C  CB  . VAL E  1 141 ? 8.432   -53.531 10.006 1.00 74.13  ? 132 VAL E CB  1 
ATOM   8097  C  CG1 . VAL E  1 141 ? 8.157   -54.295 11.298 1.00 66.17  ? 132 VAL E CG1 1 
ATOM   8098  C  CG2 . VAL E  1 141 ? 9.641   -52.618 10.140 1.00 72.19  ? 132 VAL E CG2 1 
ATOM   8099  N  N   . ASP E  1 142 ? 9.113   -56.818 9.290  1.00 77.47  ? 133 ASP E N   1 
ATOM   8100  C  CA  . ASP E  1 142 ? 9.922   -58.006 9.563  1.00 79.60  ? 133 ASP E CA  1 
ATOM   8101  C  C   . ASP E  1 142 ? 10.320  -58.769 8.288  1.00 84.95  ? 133 ASP E C   1 
ATOM   8102  O  O   . ASP E  1 142 ? 10.866  -59.875 8.351  1.00 81.13  ? 133 ASP E O   1 
ATOM   8103  C  CB  . ASP E  1 142 ? 9.230   -58.922 10.576 1.00 82.94  ? 133 ASP E CB  1 
ATOM   8104  C  CG  . ASP E  1 142 ? 7.815   -59.281 10.171 1.00 80.35  ? 133 ASP E CG  1 
ATOM   8105  O  OD1 . ASP E  1 142 ? 7.352   -58.777 9.131  1.00 78.83  ? 133 ASP E OD1 1 
ATOM   8106  O  OD2 . ASP E  1 142 ? 7.163   -60.059 10.906 1.00 76.52  ? 133 ASP E OD2 1 
ATOM   8107  N  N   . SER E  1 143 ? 9.996   -58.189 7.135  1.00 85.14  ? 134 SER E N   1 
ATOM   8108  C  CA  . SER E  1 143 ? 10.376  -58.746 5.844  1.00 80.70  ? 134 SER E CA  1 
ATOM   8109  C  C   . SER E  1 143 ? 11.388  -57.843 5.141  1.00 78.59  ? 134 SER E C   1 
ATOM   8110  O  O   . SER E  1 143 ? 11.820  -56.849 5.701  1.00 84.25  ? 134 SER E O   1 
ATOM   8111  C  CB  . SER E  1 143 ? 9.138   -58.937 4.973  1.00 83.00  ? 134 SER E CB  1 
ATOM   8112  O  OG  . SER E  1 143 ? 8.592   -57.692 4.589  1.00 78.76  ? 134 SER E OG  1 
ATOM   8113  N  N   . GLU E  1 144 ? 11.777  -58.195 3.921  1.00 89.47  ? 135 GLU E N   1 
ATOM   8114  C  CA  . GLU E  1 144 ? 12.782  -57.419 3.196  1.00 93.80  ? 135 GLU E CA  1 
ATOM   8115  C  C   . GLU E  1 144 ? 12.231  -56.095 2.660  1.00 89.55  ? 135 GLU E C   1 
ATOM   8116  O  O   . GLU E  1 144 ? 12.938  -55.083 2.642  1.00 76.48  ? 135 GLU E O   1 
ATOM   8117  C  CB  . GLU E  1 144 ? 13.404  -58.243 2.053  1.00 94.98  ? 135 GLU E CB  1 
ATOM   8118  C  CG  . GLU E  1 144 ? 14.593  -59.120 2.468  1.00 97.99  ? 135 GLU E CG  1 
ATOM   8119  C  CD  . GLU E  1 144 ? 15.657  -59.228 1.379  1.00 98.59  ? 135 GLU E CD  1 
ATOM   8120  O  OE1 . GLU E  1 144 ? 15.459  -58.629 0.300  1.00 87.09  ? 135 GLU E OE1 1 
ATOM   8121  O  OE2 . GLU E  1 144 ? 16.689  -59.906 1.603  1.00 93.72  ? 135 GLU E OE2 1 
ATOM   8122  N  N   . GLU E  1 145 ? 10.969  -56.120 2.230  1.00 93.78  ? 136 GLU E N   1 
ATOM   8123  C  CA  . GLU E  1 145 ? 10.309  -54.966 1.609  1.00 96.64  ? 136 GLU E CA  1 
ATOM   8124  C  C   . GLU E  1 145 ? 10.141  -53.831 2.597  1.00 94.10  ? 136 GLU E C   1 
ATOM   8125  O  O   . GLU E  1 145 ? 10.136  -52.646 2.234  1.00 94.12  ? 136 GLU E O   1 
ATOM   8126  C  CB  . GLU E  1 145 ? 8.924   -55.355 1.076  1.00 100.51 ? 136 GLU E CB  1 
ATOM   8127  C  CG  . GLU E  1 145 ? 8.932   -56.113 -0.240 1.00 108.57 ? 136 GLU E CG  1 
ATOM   8128  C  CD  . GLU E  1 145 ? 9.588   -55.324 -1.352 1.00 114.75 ? 136 GLU E CD  1 
ATOM   8129  O  OE1 . GLU E  1 145 ? 9.994   -54.168 -1.098 1.00 104.12 ? 136 GLU E OE1 1 
ATOM   8130  O  OE2 . GLU E  1 145 ? 9.700   -55.862 -2.475 1.00 117.85 ? 136 GLU E OE2 1 
ATOM   8131  N  N   . GLY E  1 146 ? 9.982   -54.214 3.856  1.00 85.06  ? 137 GLY E N   1 
ATOM   8132  C  CA  . GLY E  1 146 ? 9.812   -53.259 4.922  1.00 79.98  ? 137 GLY E CA  1 
ATOM   8133  C  C   . GLY E  1 146 ? 8.395   -52.738 4.989  1.00 81.21  ? 137 GLY E C   1 
ATOM   8134  O  O   . GLY E  1 146 ? 7.517   -53.157 4.226  1.00 76.79  ? 137 GLY E O   1 
ATOM   8135  N  N   . ALA E  1 147 ? 8.185   -51.822 5.928  1.00 77.09  ? 138 ALA E N   1 
ATOM   8136  C  CA  . ALA E  1 147 ? 6.920   -51.130 6.077  1.00 73.64  ? 138 ALA E CA  1 
ATOM   8137  C  C   . ALA E  1 147 ? 7.111   -49.714 5.566  1.00 70.06  ? 138 ALA E C   1 
ATOM   8138  O  O   . ALA E  1 147 ? 8.197   -49.138 5.685  1.00 67.33  ? 138 ALA E O   1 
ATOM   8139  C  CB  . ALA E  1 147 ? 6.489   -51.124 7.535  1.00 68.75  ? 138 ALA E CB  1 
ATOM   8140  N  N   . THR E  1 148 ? 6.072   -49.158 4.964  1.00 68.18  ? 139 THR E N   1 
ATOM   8141  C  CA  . THR E  1 148 ? 6.133   -47.765 4.574  1.00 67.00  ? 139 THR E CA  1 
ATOM   8142  C  C   . THR E  1 148 ? 5.135   -47.002 5.415  1.00 62.67  ? 139 THR E C   1 
ATOM   8143  O  O   . THR E  1 148 ? 4.008   -47.453 5.594  1.00 65.77  ? 139 THR E O   1 
ATOM   8144  C  CB  . THR E  1 148 ? 5.836   -47.571 3.079  1.00 70.77  ? 139 THR E CB  1 
ATOM   8145  O  OG1 . THR E  1 148 ? 6.949   -48.044 2.311  1.00 75.56  ? 139 THR E OG1 1 
ATOM   8146  C  CG2 . THR E  1 148 ? 5.601   -46.094 2.761  1.00 59.26  ? 139 THR E CG2 1 
ATOM   8147  N  N   . CYS E  1 149 ? 5.562   -45.865 5.956  1.00 62.54  ? 140 CYS E N   1 
ATOM   8148  C  CA  . CYS E  1 149 ? 4.658   -44.979 6.683  1.00 64.69  ? 140 CYS E CA  1 
ATOM   8149  C  C   . CYS E  1 149 ? 4.798   -43.544 6.212  1.00 57.85  ? 140 CYS E C   1 
ATOM   8150  O  O   . CYS E  1 149 ? 5.789   -43.193 5.566  1.00 59.98  ? 140 CYS E O   1 
ATOM   8151  C  CB  . CYS E  1 149 ? 4.903   -45.075 8.186  1.00 61.15  ? 140 CYS E CB  1 
ATOM   8152  S  SG  . CYS E  1 149 ? 4.953   -46.770 8.773  1.00 84.53  ? 140 CYS E SG  1 
ATOM   8153  N  N   . ALA E  1 150 ? 3.807   -42.714 6.517  1.00 52.15  ? 141 ALA E N   1 
ATOM   8154  C  CA  . ALA E  1 150 ? 3.894   -41.301 6.141  1.00 61.34  ? 141 ALA E CA  1 
ATOM   8155  C  C   . ALA E  1 150 ? 3.138   -40.384 7.102  1.00 60.06  ? 141 ALA E C   1 
ATOM   8156  O  O   . ALA E  1 150 ? 2.153   -40.796 7.720  1.00 63.96  ? 141 ALA E O   1 
ATOM   8157  C  CB  . ALA E  1 150 ? 3.429   -41.085 4.682  1.00 58.17  ? 141 ALA E CB  1 
ATOM   8158  N  N   . VAL E  1 151 ? 3.620   -39.148 7.232  1.00 56.88  ? 142 VAL E N   1 
ATOM   8159  C  CA  . VAL E  1 151 ? 2.997   -38.142 8.088  1.00 52.29  ? 142 VAL E CA  1 
ATOM   8160  C  C   . VAL E  1 151 ? 3.082   -36.780 7.419  1.00 54.99  ? 142 VAL E C   1 
ATOM   8161  O  O   . VAL E  1 151 ? 4.136   -36.399 6.904  1.00 54.82  ? 142 VAL E O   1 
ATOM   8162  C  CB  . VAL E  1 151 ? 3.673   -38.092 9.500  1.00 62.84  ? 142 VAL E CB  1 
ATOM   8163  C  CG1 . VAL E  1 151 ? 5.161   -37.760 9.381  1.00 62.15  ? 142 VAL E CG1 1 
ATOM   8164  C  CG2 . VAL E  1 151 ? 2.963   -37.108 10.436 1.00 52.26  ? 142 VAL E CG2 1 
ATOM   8165  N  N   . LYS E  1 152 ? 1.974   -36.044 7.435  1.00 57.32  ? 143 LYS E N   1 
ATOM   8166  C  CA  . LYS E  1 152 ? 1.929   -34.715 6.826  1.00 60.29  ? 143 LYS E CA  1 
ATOM   8167  C  C   . LYS E  1 152 ? 2.131   -33.580 7.831  1.00 59.67  ? 143 LYS E C   1 
ATOM   8168  O  O   . LYS E  1 152 ? 1.615   -33.627 8.937  1.00 57.87  ? 143 LYS E O   1 
ATOM   8169  C  CB  . LYS E  1 152 ? 0.623   -34.525 6.062  1.00 58.54  ? 143 LYS E CB  1 
ATOM   8170  C  CG  . LYS E  1 152 ? 0.723   -34.974 4.626  1.00 62.71  ? 143 LYS E CG  1 
ATOM   8171  C  CD  . LYS E  1 152 ? -0.626  -35.184 4.005  1.00 64.65  ? 143 LYS E CD  1 
ATOM   8172  C  CE  . LYS E  1 152 ? -0.795  -36.628 3.625  1.00 69.65  ? 143 LYS E CE  1 
ATOM   8173  N  NZ  . LYS E  1 152 ? 0.497   -37.152 3.105  1.00 63.17  ? 143 LYS E NZ  1 
ATOM   8174  N  N   . PHE E  1 153 ? 2.894   -32.567 7.429  1.00 55.49  ? 144 PHE E N   1 
ATOM   8175  C  CA  . PHE E  1 153 ? 3.175   -31.410 8.265  1.00 51.56  ? 144 PHE E CA  1 
ATOM   8176  C  C   . PHE E  1 153 ? 2.696   -30.205 7.512  1.00 53.40  ? 144 PHE E C   1 
ATOM   8177  O  O   . PHE E  1 153 ? 2.823   -30.161 6.310  1.00 61.85  ? 144 PHE E O   1 
ATOM   8178  C  CB  . PHE E  1 153 ? 4.681   -31.240 8.479  1.00 53.11  ? 144 PHE E CB  1 
ATOM   8179  C  CG  . PHE E  1 153 ? 5.297   -32.271 9.374  1.00 56.55  ? 144 PHE E CG  1 
ATOM   8180  C  CD1 . PHE E  1 153 ? 5.490   -32.011 10.727 1.00 55.62  ? 144 PHE E CD1 1 
ATOM   8181  C  CD2 . PHE E  1 153 ? 5.698   -33.498 8.864  1.00 53.11  ? 144 PHE E CD2 1 
ATOM   8182  C  CE1 . PHE E  1 153 ? 6.064   -32.959 11.554 1.00 52.09  ? 144 PHE E CE1 1 
ATOM   8183  C  CE2 . PHE E  1 153 ? 6.270   -34.449 9.680  1.00 60.09  ? 144 PHE E CE2 1 
ATOM   8184  C  CZ  . PHE E  1 153 ? 6.455   -34.175 11.036 1.00 58.61  ? 144 PHE E CZ  1 
ATOM   8185  N  N   . GLY E  1 154 ? 2.173   -29.216 8.219  1.00 53.50  ? 145 GLY E N   1 
ATOM   8186  C  CA  . GLY E  1 154 ? 1.788   -27.960 7.615  1.00 46.56  ? 145 GLY E CA  1 
ATOM   8187  C  C   . GLY E  1 154 ? 1.228   -27.064 8.691  1.00 53.21  ? 145 GLY E C   1 
ATOM   8188  O  O   . GLY E  1 154 ? 1.027   -27.507 9.817  1.00 49.01  ? 145 GLY E O   1 
ATOM   8189  N  N   . SER E  1 155 ? 0.980   -25.803 8.363  1.00 53.65  ? 146 SER E N   1 
ATOM   8190  C  CA  . SER E  1 155 ? 0.378   -24.895 9.331  1.00 50.76  ? 146 SER E CA  1 
ATOM   8191  C  C   . SER E  1 155 ? -1.038  -25.339 9.680  1.00 49.64  ? 146 SER E C   1 
ATOM   8192  O  O   . SER E  1 155 ? -1.772  -25.815 8.833  1.00 48.00  ? 146 SER E O   1 
ATOM   8193  C  CB  . SER E  1 155 ? 0.394   -23.459 8.826  1.00 52.88  ? 146 SER E CB  1 
ATOM   8194  O  OG  . SER E  1 155 ? -0.633  -22.712 9.427  1.00 49.01  ? 146 SER E OG  1 
ATOM   8195  N  N   . TRP E  1 156 ? -1.392  -25.236 10.953 1.00 53.22  ? 147 TRP E N   1 
ATOM   8196  C  CA  . TRP E  1 156 ? -2.712  -25.649 11.402 1.00 52.28  ? 147 TRP E CA  1 
ATOM   8197  C  C   . TRP E  1 156 ? -3.795  -24.602 11.152 1.00 54.08  ? 147 TRP E C   1 
ATOM   8198  O  O   . TRP E  1 156 ? -4.916  -24.934 10.814 1.00 57.63  ? 147 TRP E O   1 
ATOM   8199  C  CB  . TRP E  1 156 ? -2.678  -26.009 12.887 1.00 48.42  ? 147 TRP E CB  1 
ATOM   8200  C  CG  . TRP E  1 156 ? -3.967  -26.586 13.359 1.00 52.20  ? 147 TRP E CG  1 
ATOM   8201  C  CD1 . TRP E  1 156 ? -4.941  -25.953 14.064 1.00 49.98  ? 147 TRP E CD1 1 
ATOM   8202  C  CD2 . TRP E  1 156 ? -4.434  -27.917 13.135 1.00 55.24  ? 147 TRP E CD2 1 
ATOM   8203  N  NE1 . TRP E  1 156 ? -5.986  -26.804 14.300 1.00 48.62  ? 147 TRP E NE1 1 
ATOM   8204  C  CE2 . TRP E  1 156 ? -5.694  -28.022 13.748 1.00 52.34  ? 147 TRP E CE2 1 
ATOM   8205  C  CE3 . TRP E  1 156 ? -3.900  -29.038 12.485 1.00 49.01  ? 147 TRP E CE3 1 
ATOM   8206  C  CZ2 . TRP E  1 156 ? -6.430  -29.196 13.728 1.00 53.25  ? 147 TRP E CZ2 1 
ATOM   8207  C  CZ3 . TRP E  1 156 ? -4.622  -30.197 12.475 1.00 48.21  ? 147 TRP E CZ3 1 
ATOM   8208  C  CH2 . TRP E  1 156 ? -5.877  -30.270 13.083 1.00 55.45  ? 147 TRP E CH2 1 
ATOM   8209  N  N   . SER E  1 157 ? -3.479  -23.343 11.418 1.00 54.75  ? 148 SER E N   1 
ATOM   8210  C  CA  . SER E  1 157 ? -4.449  -22.263 11.285 1.00 53.82  ? 148 SER E CA  1 
ATOM   8211  C  C   . SER E  1 157 ? -4.377  -21.426 9.990  1.00 55.96  ? 148 SER E C   1 
ATOM   8212  O  O   . SER E  1 157 ? -5.267  -20.624 9.727  1.00 48.92  ? 148 SER E O   1 
ATOM   8213  C  CB  . SER E  1 157 ? -4.322  -21.341 12.507 1.00 51.30  ? 148 SER E CB  1 
ATOM   8214  O  OG  . SER E  1 157 ? -4.546  -22.061 13.709 1.00 56.94  ? 148 SER E OG  1 
ATOM   8215  N  N   . TYR E  1 158 ? -3.364  -21.656 9.158  1.00 57.81  ? 149 TYR E N   1 
ATOM   8216  C  CA  . TYR E  1 158 ? -3.084  -20.763 8.030  1.00 56.68  ? 149 TYR E CA  1 
ATOM   8217  C  C   . TYR E  1 158 ? -3.092  -21.456 6.665  1.00 63.48  ? 149 TYR E C   1 
ATOM   8218  O  O   . TYR E  1 158 ? -2.529  -22.542 6.494  1.00 55.27  ? 149 TYR E O   1 
ATOM   8219  C  CB  . TYR E  1 158 ? -1.729  -20.078 8.198  1.00 50.17  ? 149 TYR E CB  1 
ATOM   8220  C  CG  . TYR E  1 158 ? -1.645  -19.014 9.274  1.00 64.43  ? 149 TYR E CG  1 
ATOM   8221  C  CD1 . TYR E  1 158 ? -2.038  -17.701 9.025  1.00 64.86  ? 149 TYR E CD1 1 
ATOM   8222  C  CD2 . TYR E  1 158 ? -1.135  -19.311 10.532 1.00 60.59  ? 149 TYR E CD2 1 
ATOM   8223  C  CE1 . TYR E  1 158 ? -1.940  -16.725 10.007 1.00 58.87  ? 149 TYR E CE1 1 
ATOM   8224  C  CE2 . TYR E  1 158 ? -1.030  -18.340 11.510 1.00 59.48  ? 149 TYR E CE2 1 
ATOM   8225  C  CZ  . TYR E  1 158 ? -1.429  -17.051 11.249 1.00 57.62  ? 149 TYR E CZ  1 
ATOM   8226  O  OH  . TYR E  1 158 ? -1.307  -16.105 12.245 1.00 55.81  ? 149 TYR E OH  1 
ATOM   8227  N  N   . GLY E  1 159 ? -3.700  -20.799 5.683  1.00 61.69  ? 150 GLY E N   1 
ATOM   8228  C  CA  . GLY E  1 159 ? -3.654  -21.281 4.323  1.00 58.73  ? 150 GLY E CA  1 
ATOM   8229  C  C   . GLY E  1 159 ? -2.465  -20.763 3.546  1.00 56.28  ? 150 GLY E C   1 
ATOM   8230  O  O   . GLY E  1 159 ? -1.726  -19.893 4.003  1.00 54.55  ? 150 GLY E O   1 
ATOM   8231  N  N   . GLY E  1 160 ? -2.314  -21.297 2.342  1.00 60.65  ? 151 GLY E N   1 
ATOM   8232  C  CA  . GLY E  1 160 ? -1.199  -20.992 1.464  1.00 66.20  ? 151 GLY E CA  1 
ATOM   8233  C  C   . GLY E  1 160 ? -1.070  -19.557 0.997  1.00 62.94  ? 151 GLY E C   1 
ATOM   8234  O  O   . GLY E  1 160 ? 0.017   -19.150 0.580  1.00 61.75  ? 151 GLY E O   1 
ATOM   8235  N  N   . TRP E  1 161 ? -2.168  -18.801 1.059  1.00 65.96  ? 152 TRP E N   1 
ATOM   8236  C  CA  . TRP E  1 161 ? -2.150  -17.358 0.775  1.00 66.93  ? 152 TRP E CA  1 
ATOM   8237  C  C   . TRP E  1 161 ? -1.589  -16.484 1.885  1.00 64.19  ? 152 TRP E C   1 
ATOM   8238  O  O   . TRP E  1 161 ? -1.301  -15.310 1.653  1.00 63.60  ? 152 TRP E O   1 
ATOM   8239  C  CB  . TRP E  1 161 ? -3.542  -16.859 0.448  1.00 69.49  ? 152 TRP E CB  1 
ATOM   8240  C  CG  . TRP E  1 161 ? -4.000  -17.288 -0.888 1.00 73.07  ? 152 TRP E CG  1 
ATOM   8241  C  CD1 . TRP E  1 161 ? -3.226  -17.741 -1.921 1.00 72.20  ? 152 TRP E CD1 1 
ATOM   8242  C  CD2 . TRP E  1 161 ? -5.348  -17.314 -1.349 1.00 72.84  ? 152 TRP E CD2 1 
ATOM   8243  N  NE1 . TRP E  1 161 ? -4.016  -18.042 -2.999 1.00 77.57  ? 152 TRP E NE1 1 
ATOM   8244  C  CE2 . TRP E  1 161 ? -5.323  -17.794 -2.673 1.00 78.89  ? 152 TRP E CE2 1 
ATOM   8245  C  CE3 . TRP E  1 161 ? -6.576  -16.985 -0.767 1.00 70.69  ? 152 TRP E CE3 1 
ATOM   8246  C  CZ2 . TRP E  1 161 ? -6.485  -17.953 -3.426 1.00 76.42  ? 152 TRP E CZ2 1 
ATOM   8247  C  CZ3 . TRP E  1 161 ? -7.725  -17.139 -1.513 1.00 78.09  ? 152 TRP E CZ3 1 
ATOM   8248  C  CH2 . TRP E  1 161 ? -7.674  -17.618 -2.831 1.00 78.51  ? 152 TRP E CH2 1 
ATOM   8249  N  N   . GLU E  1 162 ? -1.463  -17.062 3.083  1.00 65.84  ? 153 GLU E N   1 
ATOM   8250  C  CA  . GLU E  1 162 ? -0.816  -16.444 4.250  1.00 61.24  ? 153 GLU E CA  1 
ATOM   8251  C  C   . GLU E  1 162 ? 0.564   -17.057 4.502  1.00 58.50  ? 153 GLU E C   1 
ATOM   8252  O  O   . GLU E  1 162 ? 1.568   -16.347 4.587  1.00 51.54  ? 153 GLU E O   1 
ATOM   8253  C  CB  . GLU E  1 162 ? -1.704  -16.513 5.484  1.00 60.53  ? 153 GLU E CB  1 
ATOM   8254  C  CG  . GLU E  1 162 ? -3.019  -15.764 5.337  1.00 63.78  ? 153 GLU E CG  1 
ATOM   8255  C  CD  . GLU E  1 162 ? -4.161  -16.657 4.858  1.00 74.59  ? 153 GLU E CD  1 
ATOM   8256  O  OE1 . GLU E  1 162 ? -4.052  -17.902 4.976  1.00 70.33  ? 153 GLU E OE1 1 
ATOM   8257  O  OE2 . GLU E  1 162 ? -5.176  -16.110 4.374  1.00 77.65  ? 153 GLU E OE2 1 
ATOM   8258  N  N   . ILE E  1 163 ? 0.577   -18.369 4.723  1.00 57.84  ? 154 ILE E N   1 
ATOM   8259  C  CA  . ILE E  1 163 ? 1.815   -19.152 4.856  1.00 63.56  ? 154 ILE E CA  1 
ATOM   8260  C  C   . ILE E  1 163 ? 1.988   -20.163 3.715  1.00 67.03  ? 154 ILE E C   1 
ATOM   8261  O  O   . ILE E  1 163 ? 1.141   -21.044 3.481  1.00 60.34  ? 154 ILE E O   1 
ATOM   8262  C  CB  . ILE E  1 163 ? 1.859   -19.959 6.196  1.00 65.84  ? 154 ILE E CB  1 
ATOM   8263  C  CG1 . ILE E  1 163 ? 1.611   -19.051 7.395  1.00 60.02  ? 154 ILE E CG1 1 
ATOM   8264  C  CG2 . ILE E  1 163 ? 3.178   -20.717 6.356  1.00 55.20  ? 154 ILE E CG2 1 
ATOM   8265  C  CD1 . ILE E  1 163 ? 1.590   -19.805 8.679  1.00 65.94  ? 154 ILE E CD1 1 
ATOM   8266  N  N   . ASP E  1 164 ? 3.108   -20.058 3.018  1.00 67.33  ? 155 ASP E N   1 
ATOM   8267  C  CA  . ASP E  1 164 ? 3.380   -21.002 1.949  1.00 72.26  ? 155 ASP E CA  1 
ATOM   8268  C  C   . ASP E  1 164 ? 4.539   -21.931 2.296  1.00 66.13  ? 155 ASP E C   1 
ATOM   8269  O  O   . ASP E  1 164 ? 5.635   -21.466 2.590  1.00 69.77  ? 155 ASP E O   1 
ATOM   8270  C  CB  . ASP E  1 164 ? 3.679   -20.263 0.649  1.00 68.78  ? 155 ASP E CB  1 
ATOM   8271  C  CG  . ASP E  1 164 ? 4.024   -21.206 -0.471 1.00 71.49  ? 155 ASP E CG  1 
ATOM   8272  O  OD1 . ASP E  1 164 ? 3.298   -22.219 -0.649 1.00 58.97  ? 155 ASP E OD1 1 
ATOM   8273  O  OD2 . ASP E  1 164 ? 5.034   -20.940 -1.154 1.00 75.02  ? 155 ASP E OD2 1 
ATOM   8274  N  N   . LEU E  1 165 ? 4.293   -23.237 2.247  1.00 56.09  ? 156 LEU E N   1 
ATOM   8275  C  CA  . LEU E  1 165 ? 5.318   -24.228 2.570  1.00 62.98  ? 156 LEU E CA  1 
ATOM   8276  C  C   . LEU E  1 165 ? 6.233   -24.559 1.399  1.00 61.66  ? 156 LEU E C   1 
ATOM   8277  O  O   . LEU E  1 165 ? 5.757   -24.782 0.308  1.00 68.20  ? 156 LEU E O   1 
ATOM   8278  C  CB  . LEU E  1 165 ? 4.657   -25.523 3.040  1.00 65.85  ? 156 LEU E CB  1 
ATOM   8279  C  CG  . LEU E  1 165 ? 4.146   -25.595 4.475  1.00 55.64  ? 156 LEU E CG  1 
ATOM   8280  C  CD1 . LEU E  1 165 ? 3.321   -26.853 4.651  1.00 52.80  ? 156 LEU E CD1 1 
ATOM   8281  C  CD2 . LEU E  1 165 ? 5.322   -25.537 5.452  1.00 57.25  ? 156 LEU E CD2 1 
ATOM   8282  N  N   . LYS E  1 166 ? 7.541   -24.616 1.633  1.00 60.22  ? 157 LYS E N   1 
ATOM   8283  C  CA  . LYS E  1 166 ? 8.498   -24.987 0.588  1.00 67.24  ? 157 LYS E CA  1 
ATOM   8284  C  C   . LYS E  1 166 ? 9.539   -25.945 1.154  1.00 66.30  ? 157 LYS E C   1 
ATOM   8285  O  O   . LYS E  1 166 ? 9.664   -26.060 2.359  1.00 68.35  ? 157 LYS E O   1 
ATOM   8286  C  CB  . LYS E  1 166 ? 9.204   -23.748 0.028  1.00 63.06  ? 157 LYS E CB  1 
ATOM   8287  C  CG  . LYS E  1 166 ? 8.299   -22.757 -0.687 1.00 72.40  ? 157 LYS E CG  1 
ATOM   8288  C  CD  . LYS E  1 166 ? 7.750   -23.334 -1.994 1.00 81.45  ? 157 LYS E CD  1 
ATOM   8289  C  CE  . LYS E  1 166 ? 7.291   -22.251 -2.973 1.00 75.17  ? 157 LYS E CE  1 
ATOM   8290  N  NZ  . LYS E  1 166 ? 6.952   -22.862 -4.298 1.00 74.77  ? 157 LYS E NZ  1 
ATOM   8291  N  N   . THR E  1 167 ? 10.293  -26.623 0.293  1.00 69.12  ? 158 THR E N   1 
ATOM   8292  C  CA  . THR E  1 167 ? 11.366  -27.498 0.757  1.00 74.19  ? 158 THR E CA  1 
ATOM   8293  C  C   . THR E  1 167 ? 12.637  -27.380 -0.093 1.00 82.39  ? 158 THR E C   1 
ATOM   8294  O  O   . THR E  1 167 ? 12.575  -27.247 -1.317 1.00 73.73  ? 158 THR E O   1 
ATOM   8295  C  CB  . THR E  1 167 ? 10.937  -28.982 0.771  1.00 77.61  ? 158 THR E CB  1 
ATOM   8296  O  OG1 . THR E  1 167 ? 11.048  -29.519 -0.550 1.00 82.05  ? 158 THR E OG1 1 
ATOM   8297  C  CG2 . THR E  1 167 ? 9.510   -29.141 1.256  1.00 64.38  ? 158 THR E CG2 1 
ATOM   8298  N  N   . ASP E  1 168 ? 13.790  -27.454 0.571  1.00 95.20  ? 159 ASP E N   1 
ATOM   8299  C  CA  . ASP E  1 168 ? 15.087  -27.463 -0.109 1.00 94.61  ? 159 ASP E CA  1 
ATOM   8300  C  C   . ASP E  1 168 ? 15.172  -28.584 -1.145 1.00 89.40  ? 159 ASP E C   1 
ATOM   8301  O  O   . ASP E  1 168 ? 15.435  -28.319 -2.319 1.00 88.37  ? 159 ASP E O   1 
ATOM   8302  C  CB  . ASP E  1 168 ? 16.232  -27.624 0.904  1.00 100.30 ? 159 ASP E CB  1 
ATOM   8303  C  CG  . ASP E  1 168 ? 16.506  -26.351 1.700  1.00 107.54 ? 159 ASP E CG  1 
ATOM   8304  O  OD1 . ASP E  1 168 ? 16.030  -25.271 1.283  1.00 103.69 ? 159 ASP E OD1 1 
ATOM   8305  O  OD2 . ASP E  1 168 ? 17.214  -26.432 2.735  1.00 97.47  ? 159 ASP E OD2 1 
ATOM   8306  N  N   . THR E  1 169 ? 14.950  -29.824 -0.697 1.00 79.70  ? 160 THR E N   1 
ATOM   8307  C  CA  . THR E  1 169 ? 15.010  -31.010 -1.556 1.00 84.16  ? 160 THR E CA  1 
ATOM   8308  C  C   . THR E  1 169 ? 13.889  -31.993 -1.191 1.00 83.72  ? 160 THR E C   1 
ATOM   8309  O  O   . THR E  1 169 ? 13.130  -31.726 -0.265 1.00 81.25  ? 160 THR E O   1 
ATOM   8310  C  CB  . THR E  1 169 ? 16.413  -31.670 -1.475 1.00 89.71  ? 160 THR E CB  1 
ATOM   8311  O  OG1 . THR E  1 169 ? 17.268  -31.064 -2.448 1.00 105.36 ? 160 THR E OG1 1 
ATOM   8312  C  CG2 . THR E  1 169 ? 16.368  -33.138 -1.775 1.00 80.39  ? 160 THR E CG2 1 
ATOM   8313  N  N   . ASP E  1 170 ? 13.762  -33.096 -1.934 1.00 79.22  ? 161 ASP E N   1 
ATOM   8314  C  CA  . ASP E  1 170 ? 12.788  -34.146 -1.636 1.00 70.30  ? 161 ASP E CA  1 
ATOM   8315  C  C   . ASP E  1 170 ? 13.488  -35.228 -0.818 1.00 78.57  ? 161 ASP E C   1 
ATOM   8316  O  O   . ASP E  1 170 ? 12.890  -36.240 -0.435 1.00 75.93  ? 161 ASP E O   1 
ATOM   8317  C  CB  . ASP E  1 170 ? 12.214  -34.756 -2.923 1.00 84.05  ? 161 ASP E CB  1 
ATOM   8318  C  CG  . ASP E  1 170 ? 13.288  -35.458 -3.782 1.00 100.27 ? 161 ASP E CG  1 
ATOM   8319  O  OD1 . ASP E  1 170 ? 14.383  -34.860 -3.947 1.00 97.71  ? 161 ASP E OD1 1 
ATOM   8320  O  OD2 . ASP E  1 170 ? 13.049  -36.599 -4.283 1.00 90.25  ? 161 ASP E OD2 1 
ATOM   8321  N  N   . GLN E  1 171 ? 14.772  -35.010 -0.568 1.00 74.32  ? 162 GLN E N   1 
ATOM   8322  C  CA  . GLN E  1 171 ? 15.585  -35.965 0.158  1.00 78.05  ? 162 GLN E CA  1 
ATOM   8323  C  C   . GLN E  1 171 ? 15.678  -35.599 1.632  1.00 77.21  ? 162 GLN E C   1 
ATOM   8324  O  O   . GLN E  1 171 ? 16.229  -34.553 1.996  1.00 75.80  ? 162 GLN E O   1 
ATOM   8325  C  CB  . GLN E  1 171 ? 16.989  -36.042 -0.443 1.00 81.93  ? 162 GLN E CB  1 
ATOM   8326  C  CG  . GLN E  1 171 ? 17.073  -36.788 -1.761 1.00 82.82  ? 162 GLN E CG  1 
ATOM   8327  C  CD  . GLN E  1 171 ? 16.961  -38.274 -1.566 1.00 86.12  ? 162 GLN E CD  1 
ATOM   8328  O  OE1 . GLN E  1 171 ? 16.148  -38.737 -0.770 1.00 85.15  ? 162 GLN E OE1 1 
ATOM   8329  N  NE2 . GLN E  1 171 ? 17.793  -39.037 -2.273 1.00 95.24  ? 162 GLN E NE2 1 
ATOM   8330  N  N   . VAL E  1 172 ? 15.131  -36.467 2.472  1.00 66.27  ? 163 VAL E N   1 
ATOM   8331  C  CA  . VAL E  1 172 ? 15.327  -36.364 3.902  1.00 66.40  ? 163 VAL E CA  1 
ATOM   8332  C  C   . VAL E  1 172 ? 16.805  -36.606 4.239  1.00 65.94  ? 163 VAL E C   1 
ATOM   8333  O  O   . VAL E  1 172 ? 17.477  -37.369 3.553  1.00 65.69  ? 163 VAL E O   1 
ATOM   8334  C  CB  . VAL E  1 172 ? 14.447  -37.386 4.616  1.00 63.50  ? 163 VAL E CB  1 
ATOM   8335  C  CG1 . VAL E  1 172 ? 14.845  -37.508 6.074  1.00 65.35  ? 163 VAL E CG1 1 
ATOM   8336  C  CG2 . VAL E  1 172 ? 13.003  -36.995 4.478  1.00 58.14  ? 163 VAL E CG2 1 
ATOM   8337  N  N   . ASP E  1 173 ? 17.317  -35.976 5.293  1.00 62.51  ? 164 ASP E N   1 
ATOM   8338  C  CA  . ASP E  1 173 ? 18.720  -36.157 5.628  1.00 59.58  ? 164 ASP E CA  1 
ATOM   8339  C  C   . ASP E  1 173 ? 18.897  -37.306 6.618  1.00 61.86  ? 164 ASP E C   1 
ATOM   8340  O  O   . ASP E  1 173 ? 18.445  -37.222 7.752  1.00 66.19  ? 164 ASP E O   1 
ATOM   8341  C  CB  . ASP E  1 173 ? 19.307  -34.878 6.204  1.00 51.02  ? 164 ASP E CB  1 
ATOM   8342  C  CG  . ASP E  1 173 ? 20.764  -35.035 6.563  1.00 56.63  ? 164 ASP E CG  1 
ATOM   8343  O  OD1 . ASP E  1 173 ? 21.417  -35.954 6.035  1.00 59.92  ? 164 ASP E OD1 1 
ATOM   8344  O  OD2 . ASP E  1 173 ? 21.266  -34.253 7.383  1.00 67.02  ? 164 ASP E OD2 1 
ATOM   8345  N  N   . LEU E  1 174 ? 19.514  -38.394 6.151  1.00 63.66  ? 165 LEU E N   1 
ATOM   8346  C  CA  . LEU E  1 174 ? 19.799  -39.593 6.948  1.00 57.89  ? 165 LEU E CA  1 
ATOM   8347  C  C   . LEU E  1 174 ? 21.228  -39.694 7.481  1.00 60.66  ? 165 LEU E C   1 
ATOM   8348  O  O   . LEU E  1 174 ? 21.579  -40.683 8.129  1.00 55.42  ? 165 LEU E O   1 
ATOM   8349  C  CB  . LEU E  1 174 ? 19.491  -40.860 6.148  1.00 52.73  ? 165 LEU E CB  1 
ATOM   8350  C  CG  . LEU E  1 174 ? 18.115  -41.043 5.519  1.00 54.34  ? 165 LEU E CG  1 
ATOM   8351  C  CD1 . LEU E  1 174 ? 17.913  -42.520 5.255  1.00 63.29  ? 165 LEU E CD1 1 
ATOM   8352  C  CD2 . LEU E  1 174 ? 17.051  -40.539 6.446  1.00 60.54  ? 165 LEU E CD2 1 
ATOM   8353  N  N   . SER E  1 175 ? 22.069  -38.713 7.166  1.00 57.15  ? 166 SER E N   1 
ATOM   8354  C  CA  . SER E  1 175 ? 23.476  -38.803 7.547  1.00 59.94  ? 166 SER E CA  1 
ATOM   8355  C  C   . SER E  1 175 ? 23.650  -38.882 9.059  1.00 59.35  ? 166 SER E C   1 
ATOM   8356  O  O   . SER E  1 175 ? 24.689  -39.304 9.546  1.00 64.10  ? 166 SER E O   1 
ATOM   8357  C  CB  . SER E  1 175 ? 24.285  -37.635 6.978  1.00 64.44  ? 166 SER E CB  1 
ATOM   8358  O  OG  . SER E  1 175 ? 24.035  -36.431 7.687  1.00 68.03  ? 166 SER E OG  1 
ATOM   8359  N  N   . SER E  1 176 ? 22.645  -38.430 9.797  1.00 62.50  ? 167 SER E N   1 
ATOM   8360  C  CA  . SER E  1 176 ? 22.669  -38.509 11.247 1.00 56.39  ? 167 SER E CA  1 
ATOM   8361  C  C   . SER E  1 176 ? 21.912  -39.690 11.839 1.00 59.28  ? 167 SER E C   1 
ATOM   8362  O  O   . SER E  1 176 ? 21.785  -39.786 13.050 1.00 62.28  ? 167 SER E O   1 
ATOM   8363  C  CB  . SER E  1 176 ? 22.210  -37.197 11.867 1.00 63.18  ? 167 SER E CB  1 
ATOM   8364  O  OG  . SER E  1 176 ? 23.320  -36.349 12.097 1.00 67.60  ? 167 SER E OG  1 
ATOM   8365  N  N   . TYR E  1 177 ? 21.372  -40.566 11.002 1.00 57.32  ? 168 TYR E N   1 
ATOM   8366  C  CA  . TYR E  1 177 ? 20.583  -41.683 11.516 1.00 56.02  ? 168 TYR E CA  1 
ATOM   8367  C  C   . TYR E  1 177 ? 21.395  -42.667 12.348 1.00 62.23  ? 168 TYR E C   1 
ATOM   8368  O  O   . TYR E  1 177 ? 22.551  -42.956 12.035 1.00 63.48  ? 168 TYR E O   1 
ATOM   8369  C  CB  . TYR E  1 177 ? 19.876  -42.436 10.402 1.00 55.89  ? 168 TYR E CB  1 
ATOM   8370  C  CG  . TYR E  1 177 ? 18.760  -43.291 10.931 1.00 57.46  ? 168 TYR E CG  1 
ATOM   8371  C  CD1 . TYR E  1 177 ? 17.508  -42.751 11.153 1.00 57.11  ? 168 TYR E CD1 1 
ATOM   8372  C  CD2 . TYR E  1 177 ? 18.961  -44.627 11.232 1.00 60.35  ? 168 TYR E CD2 1 
ATOM   8373  C  CE1 . TYR E  1 177 ? 16.486  -43.515 11.641 1.00 60.92  ? 168 TYR E CE1 1 
ATOM   8374  C  CE2 . TYR E  1 177 ? 17.935  -45.406 11.730 1.00 58.31  ? 168 TYR E CE2 1 
ATOM   8375  C  CZ  . TYR E  1 177 ? 16.701  -44.838 11.930 1.00 58.06  ? 168 TYR E CZ  1 
ATOM   8376  O  OH  . TYR E  1 177 ? 15.658  -45.578 12.414 1.00 59.22  ? 168 TYR E OH  1 
ATOM   8377  N  N   . TYR E  1 178 ? 20.761  -43.204 13.392 1.00 64.20  ? 169 TYR E N   1 
ATOM   8378  C  CA  . TYR E  1 178 ? 21.461  -43.973 14.417 1.00 63.05  ? 169 TYR E CA  1 
ATOM   8379  C  C   . TYR E  1 178 ? 21.792  -45.342 13.855 1.00 64.08  ? 169 TYR E C   1 
ATOM   8380  O  O   . TYR E  1 178 ? 20.899  -46.134 13.524 1.00 58.22  ? 169 TYR E O   1 
ATOM   8381  C  CB  . TYR E  1 178 ? 20.597  -44.074 15.703 1.00 64.86  ? 169 TYR E CB  1 
ATOM   8382  C  CG  . TYR E  1 178 ? 21.165  -44.949 16.822 1.00 66.76  ? 169 TYR E CG  1 
ATOM   8383  C  CD1 . TYR E  1 178 ? 22.489  -44.808 17.235 1.00 66.92  ? 169 TYR E CD1 1 
ATOM   8384  C  CD2 . TYR E  1 178 ? 20.372  -45.888 17.483 1.00 58.50  ? 169 TYR E CD2 1 
ATOM   8385  C  CE1 . TYR E  1 178 ? 23.018  -45.586 18.242 1.00 55.46  ? 169 TYR E CE1 1 
ATOM   8386  C  CE2 . TYR E  1 178 ? 20.898  -46.675 18.501 1.00 61.28  ? 169 TYR E CE2 1 
ATOM   8387  C  CZ  . TYR E  1 178 ? 22.231  -46.514 18.872 1.00 60.76  ? 169 TYR E CZ  1 
ATOM   8388  O  OH  . TYR E  1 178 ? 22.803  -47.276 19.872 1.00 57.23  ? 169 TYR E OH  1 
ATOM   8389  N  N   . ALA E  1 179 ? 23.092  -45.621 13.806 1.00 69.52  ? 170 ALA E N   1 
ATOM   8390  C  CA  . ALA E  1 179 ? 23.618  -46.810 13.143 1.00 67.14  ? 170 ALA E CA  1 
ATOM   8391  C  C   . ALA E  1 179 ? 23.060  -48.093 13.753 1.00 67.09  ? 170 ALA E C   1 
ATOM   8392  O  O   . ALA E  1 179 ? 22.772  -49.068 13.054 1.00 70.84  ? 170 ALA E O   1 
ATOM   8393  C  CB  . ALA E  1 179 ? 25.146  -46.796 13.211 1.00 56.69  ? 170 ALA E CB  1 
ATOM   8394  N  N   . SER E  1 180 ? 22.913  -48.068 15.070 1.00 64.06  ? 171 SER E N   1 
ATOM   8395  C  CA  . SER E  1 180 ? 22.512  -49.227 15.848 1.00 65.33  ? 171 SER E CA  1 
ATOM   8396  C  C   . SER E  1 180 ? 21.023  -49.346 16.136 1.00 66.55  ? 171 SER E C   1 
ATOM   8397  O  O   . SER E  1 180 ? 20.625  -50.156 16.960 1.00 66.86  ? 171 SER E O   1 
ATOM   8398  C  CB  . SER E  1 180 ? 23.329  -49.310 17.118 1.00 63.49  ? 171 SER E CB  1 
ATOM   8399  O  OG  . SER E  1 180 ? 24.698  -49.201 16.787 1.00 68.57  ? 171 SER E OG  1 
ATOM   8400  N  N   . SER E  1 181 ? 20.215  -48.488 15.525 1.00 64.89  ? 172 SER E N   1 
ATOM   8401  C  CA  . SER E  1 181 ? 18.770  -48.495 15.751 1.00 64.23  ? 172 SER E CA  1 
ATOM   8402  C  C   . SER E  1 181 ? 18.096  -49.838 15.460 1.00 64.18  ? 172 SER E C   1 
ATOM   8403  O  O   . SER E  1 181 ? 18.527  -50.560 14.568 1.00 67.78  ? 172 SER E O   1 
ATOM   8404  C  CB  . SER E  1 181 ? 18.112  -47.416 14.896 1.00 62.89  ? 172 SER E CB  1 
ATOM   8405  O  OG  . SER E  1 181 ? 16.699  -47.516 14.962 1.00 62.53  ? 172 SER E OG  1 
ATOM   8406  N  N   . LYS E  1 182 ? 17.035  -50.163 16.203 1.00 60.66  ? 173 LYS E N   1 
ATOM   8407  C  CA  . LYS E  1 182 ? 16.246  -51.374 15.939 1.00 62.68  ? 173 LYS E CA  1 
ATOM   8408  C  C   . LYS E  1 182 ? 15.709  -51.435 14.508 1.00 63.87  ? 173 LYS E C   1 
ATOM   8409  O  O   . LYS E  1 182 ? 15.392  -52.507 13.996 1.00 66.19  ? 173 LYS E O   1 
ATOM   8410  C  CB  . LYS E  1 182 ? 15.073  -51.511 16.915 1.00 61.79  ? 173 LYS E CB  1 
ATOM   8411  C  CG  . LYS E  1 182 ? 15.471  -51.691 18.361 1.00 68.57  ? 173 LYS E CG  1 
ATOM   8412  C  CD  . LYS E  1 182 ? 16.289  -52.951 18.583 1.00 75.23  ? 173 LYS E CD  1 
ATOM   8413  C  CE  . LYS E  1 182 ? 15.489  -54.218 18.324 1.00 71.58  ? 173 LYS E CE  1 
ATOM   8414  N  NZ  . LYS E  1 182 ? 16.223  -55.420 18.822 1.00 64.91  ? 173 LYS E NZ  1 
ATOM   8415  N  N   . TYR E  1 183 ? 15.591  -50.280 13.869 1.00 63.74  ? 174 TYR E N   1 
ATOM   8416  C  CA  . TYR E  1 183 ? 15.115  -50.231 12.503 1.00 61.64  ? 174 TYR E CA  1 
ATOM   8417  C  C   . TYR E  1 183 ? 16.118  -49.545 11.614 1.00 65.77  ? 174 TYR E C   1 
ATOM   8418  O  O   . TYR E  1 183 ? 16.720  -48.552 12.026 1.00 63.60  ? 174 TYR E O   1 
ATOM   8419  C  CB  . TYR E  1 183 ? 13.795  -49.492 12.461 1.00 54.19  ? 174 TYR E CB  1 
ATOM   8420  C  CG  . TYR E  1 183 ? 12.784  -50.141 13.346 1.00 57.07  ? 174 TYR E CG  1 
ATOM   8421  C  CD1 . TYR E  1 183 ? 12.070  -51.233 12.910 1.00 59.35  ? 174 TYR E CD1 1 
ATOM   8422  C  CD2 . TYR E  1 183 ? 12.558  -49.682 14.625 1.00 61.48  ? 174 TYR E CD2 1 
ATOM   8423  C  CE1 . TYR E  1 183 ? 11.148  -51.848 13.708 1.00 60.91  ? 174 TYR E CE1 1 
ATOM   8424  C  CE2 . TYR E  1 183 ? 11.630  -50.295 15.439 1.00 66.97  ? 174 TYR E CE2 1 
ATOM   8425  C  CZ  . TYR E  1 183 ? 10.927  -51.382 14.969 1.00 60.99  ? 174 TYR E CZ  1 
ATOM   8426  O  OH  . TYR E  1 183 ? 9.992   -52.007 15.757 1.00 57.34  ? 174 TYR E OH  1 
ATOM   8427  N  N   . GLU E  1 184 ? 16.290  -50.070 10.399 1.00 69.93  ? 175 GLU E N   1 
ATOM   8428  C  CA  . GLU E  1 184 ? 17.099  -49.406 9.370  1.00 68.43  ? 175 GLU E CA  1 
ATOM   8429  C  C   . GLU E  1 184 ? 16.210  -48.737 8.311  1.00 66.36  ? 175 GLU E C   1 
ATOM   8430  O  O   . GLU E  1 184 ? 15.106  -49.207 8.015  1.00 66.40  ? 175 GLU E O   1 
ATOM   8431  C  CB  . GLU E  1 184 ? 18.133  -50.358 8.731  1.00 74.43  ? 175 GLU E CB  1 
ATOM   8432  C  CG  . GLU E  1 184 ? 17.564  -51.644 8.126  1.00 83.63  ? 175 GLU E CG  1 
ATOM   8433  C  CD  . GLU E  1 184 ? 18.492  -52.293 7.097  1.00 84.63  ? 175 GLU E CD  1 
ATOM   8434  O  OE1 . GLU E  1 184 ? 18.812  -53.498 7.245  1.00 81.49  ? 175 GLU E OE1 1 
ATOM   8435  O  OE2 . GLU E  1 184 ? 18.880  -51.601 6.128  1.00 81.09  ? 175 GLU E OE2 1 
ATOM   8436  N  N   . ILE E  1 185 ? 16.686  -47.618 7.777  1.00 64.11  ? 176 ILE E N   1 
ATOM   8437  C  CA  . ILE E  1 185 ? 15.901  -46.818 6.837  1.00 70.70  ? 176 ILE E CA  1 
ATOM   8438  C  C   . ILE E  1 185 ? 16.222  -47.154 5.382  1.00 71.87  ? 176 ILE E C   1 
ATOM   8439  O  O   . ILE E  1 185 ? 17.380  -47.095 4.973  1.00 79.33  ? 176 ILE E O   1 
ATOM   8440  C  CB  . ILE E  1 185 ? 16.110  -45.298 7.100  1.00 68.60  ? 176 ILE E CB  1 
ATOM   8441  C  CG1 . ILE E  1 185 ? 15.711  -44.975 8.541  1.00 64.49  ? 176 ILE E CG1 1 
ATOM   8442  C  CG2 . ILE E  1 185 ? 15.344  -44.427 6.086  1.00 61.14  ? 176 ILE E CG2 1 
ATOM   8443  C  CD1 . ILE E  1 185 ? 14.437  -45.688 9.002  1.00 68.89  ? 176 ILE E CD1 1 
ATOM   8444  N  N   . LEU E  1 186 ? 15.200  -47.507 4.603  1.00 70.14  ? 177 LEU E N   1 
ATOM   8445  C  CA  . LEU E  1 186 ? 15.397  -47.850 3.188  1.00 68.71  ? 177 LEU E CA  1 
ATOM   8446  C  C   . LEU E  1 186 ? 15.301  -46.597 2.321  1.00 70.60  ? 177 LEU E C   1 
ATOM   8447  O  O   . LEU E  1 186 ? 16.289  -46.176 1.718  1.00 71.20  ? 177 LEU E O   1 
ATOM   8448  C  CB  . LEU E  1 186 ? 14.408  -48.937 2.745  1.00 69.92  ? 177 LEU E CB  1 
ATOM   8449  C  CG  . LEU E  1 186 ? 14.351  -50.210 3.624  1.00 76.32  ? 177 LEU E CG  1 
ATOM   8450  C  CD1 . LEU E  1 186 ? 13.143  -51.088 3.297  1.00 75.97  ? 177 LEU E CD1 1 
ATOM   8451  C  CD2 . LEU E  1 186 ? 15.640  -51.033 3.574  1.00 64.35  ? 177 LEU E CD2 1 
ATOM   8452  N  N   . SER E  1 187 ? 14.114  -45.993 2.280  1.00 77.38  ? 178 SER E N   1 
ATOM   8453  C  CA  . SER E  1 187 ? 13.926  -44.678 1.655  1.00 75.28  ? 178 SER E CA  1 
ATOM   8454  C  C   . SER E  1 187 ? 13.283  -43.661 2.610  1.00 70.32  ? 178 SER E C   1 
ATOM   8455  O  O   . SER E  1 187 ? 12.500  -44.022 3.494  1.00 61.70  ? 178 SER E O   1 
ATOM   8456  C  CB  . SER E  1 187 ? 13.116  -44.784 0.356  1.00 70.42  ? 178 SER E CB  1 
ATOM   8457  O  OG  . SER E  1 187 ? 12.073  -45.744 0.453  1.00 68.37  ? 178 SER E OG  1 
ATOM   8458  N  N   . ALA E  1 188 ? 13.666  -42.396 2.445  1.00 70.38  ? 179 ALA E N   1 
ATOM   8459  C  CA  . ALA E  1 188 ? 13.043  -41.277 3.145  1.00 65.16  ? 179 ALA E CA  1 
ATOM   8460  C  C   . ALA E  1 188 ? 12.918  -40.078 2.212  1.00 67.10  ? 179 ALA E C   1 
ATOM   8461  O  O   . ALA E  1 188 ? 13.893  -39.639 1.592  1.00 61.03  ? 179 ALA E O   1 
ATOM   8462  C  CB  . ALA E  1 188 ? 13.837  -40.901 4.392  1.00 64.86  ? 179 ALA E CB  1 
ATOM   8463  N  N   . THR E  1 189 ? 11.713  -39.533 2.133  1.00 68.01  ? 180 THR E N   1 
ATOM   8464  C  CA  . THR E  1 189 ? 11.462  -38.391 1.271  1.00 67.32  ? 180 THR E CA  1 
ATOM   8465  C  C   . THR E  1 189 ? 10.603  -37.305 1.938  1.00 65.01  ? 180 THR E C   1 
ATOM   8466  O  O   . THR E  1 189 ? 9.703   -37.602 2.723  1.00 62.27  ? 180 THR E O   1 
ATOM   8467  C  CB  . THR E  1 189 ? 10.756  -38.862 0.014  1.00 65.34  ? 180 THR E CB  1 
ATOM   8468  O  OG1 . THR E  1 189 ? 9.426   -39.289 0.349  1.00 65.99  ? 180 THR E OG1 1 
ATOM   8469  C  CG2 . THR E  1 189 ? 11.521  -40.020 -0.581 1.00 60.29  ? 180 THR E CG2 1 
ATOM   8470  N  N   . GLN E  1 190 ? 10.893  -36.048 1.625  1.00 58.65  ? 181 GLN E N   1 
ATOM   8471  C  CA  . GLN E  1 190 ? 9.993   -34.952 1.957  1.00 59.00  ? 181 GLN E CA  1 
ATOM   8472  C  C   . GLN E  1 190 ? 9.367   -34.380 0.679  1.00 69.13  ? 181 GLN E C   1 
ATOM   8473  O  O   . GLN E  1 190 ? 10.070  -33.834 -0.173 1.00 75.37  ? 181 GLN E O   1 
ATOM   8474  C  CB  . GLN E  1 190 ? 10.726  -33.874 2.763  1.00 63.68  ? 181 GLN E CB  1 
ATOM   8475  C  CG  . GLN E  1 190 ? 11.924  -33.253 2.079  1.00 66.45  ? 181 GLN E CG  1 
ATOM   8476  C  CD  . GLN E  1 190 ? 12.988  -32.778 3.055  1.00 63.55  ? 181 GLN E CD  1 
ATOM   8477  O  OE1 . GLN E  1 190 ? 13.146  -33.331 4.127  1.00 62.85  ? 181 GLN E OE1 1 
ATOM   8478  N  NE2 . GLN E  1 190 ? 13.723  -31.748 2.676  1.00 74.22  ? 181 GLN E NE2 1 
ATOM   8479  N  N   . THR E  1 191 ? 8.049   -34.523 0.535  1.00 71.27  ? 182 THR E N   1 
ATOM   8480  C  CA  . THR E  1 191 ? 7.349   -34.107 -0.696 1.00 75.56  ? 182 THR E CA  1 
ATOM   8481  C  C   . THR E  1 191 ? 6.260   -33.043 -0.477 1.00 62.26  ? 182 THR E C   1 
ATOM   8482  O  O   . THR E  1 191 ? 5.293   -33.249 0.256  1.00 55.52  ? 182 THR E O   1 
ATOM   8483  C  CB  . THR E  1 191 ? 6.747   -35.328 -1.455 1.00 72.69  ? 182 THR E CB  1 
ATOM   8484  O  OG1 . THR E  1 191 ? 7.750   -35.919 -2.285 1.00 76.65  ? 182 THR E OG1 1 
ATOM   8485  C  CG2 . THR E  1 191 ? 5.596   -34.903 -2.331 1.00 69.17  ? 182 THR E CG2 1 
ATOM   8486  N  N   . ARG E  1 192 ? 6.420   -31.903 -1.130 1.00 59.13  ? 183 ARG E N   1 
ATOM   8487  C  CA  . ARG E  1 192 ? 5.439   -30.843 -0.989 1.00 60.65  ? 183 ARG E CA  1 
ATOM   8488  C  C   . ARG E  1 192 ? 4.175   -31.121 -1.799 1.00 58.07  ? 183 ARG E C   1 
ATOM   8489  O  O   . ARG E  1 192 ? 4.227   -31.771 -2.825 1.00 67.92  ? 183 ARG E O   1 
ATOM   8490  C  CB  . ARG E  1 192 ? 6.041   -29.510 -1.416 1.00 58.83  ? 183 ARG E CB  1 
ATOM   8491  C  CG  . ARG E  1 192 ? 5.045   -28.385 -1.341 1.00 60.21  ? 183 ARG E CG  1 
ATOM   8492  C  CD  . ARG E  1 192 ? 5.566   -27.085 -1.868 1.00 53.38  ? 183 ARG E CD  1 
ATOM   8493  N  NE  . ARG E  1 192 ? 4.589   -26.050 -1.563 1.00 67.29  ? 183 ARG E NE  1 
ATOM   8494  C  CZ  . ARG E  1 192 ? 3.912   -25.340 -2.461 1.00 70.25  ? 183 ARG E CZ  1 
ATOM   8495  N  NH1 . ARG E  1 192 ? 4.105   -25.526 -3.757 1.00 72.88  ? 183 ARG E NH1 1 
ATOM   8496  N  NH2 . ARG E  1 192 ? 3.046   -24.425 -2.051 1.00 65.71  ? 183 ARG E NH2 1 
ATOM   8497  N  N   . SER E  1 193 ? 3.028   -30.654 -1.332 1.00 58.64  ? 184 SER E N   1 
ATOM   8498  C  CA  . SER E  1 193 ? 1.845   -30.632 -2.189 1.00 58.25  ? 184 SER E CA  1 
ATOM   8499  C  C   . SER E  1 193 ? 0.834   -29.614 -1.675 1.00 59.75  ? 184 SER E C   1 
ATOM   8500  O  O   . SER E  1 193 ? 0.899   -29.204 -0.520 1.00 63.64  ? 184 SER E O   1 
ATOM   8501  C  CB  . SER E  1 193 ? 1.222   -32.022 -2.303 1.00 60.93  ? 184 SER E CB  1 
ATOM   8502  O  OG  . SER E  1 193 ? 0.174   -32.190 -1.369 1.00 63.61  ? 184 SER E OG  1 
ATOM   8503  N  N   . GLU E  1 194 ? -0.091  -29.194 -2.529 1.00 57.04  ? 185 GLU E N   1 
ATOM   8504  C  CA  . GLU E  1 194 ? -1.105  -28.237 -2.117 1.00 58.66  ? 185 GLU E CA  1 
ATOM   8505  C  C   . GLU E  1 194 ? -2.461  -28.874 -2.160 1.00 56.97  ? 185 GLU E C   1 
ATOM   8506  O  O   . GLU E  1 194 ? -2.797  -29.527 -3.121 1.00 64.74  ? 185 GLU E O   1 
ATOM   8507  C  CB  . GLU E  1 194 ? -1.110  -27.047 -3.043 1.00 60.66  ? 185 GLU E CB  1 
ATOM   8508  C  CG  . GLU E  1 194 ? 0.256   -26.528 -3.334 1.00 66.89  ? 185 GLU E CG  1 
ATOM   8509  C  CD  . GLU E  1 194 ? 0.199   -25.236 -4.092 1.00 69.89  ? 185 GLU E CD  1 
ATOM   8510  O  OE1 . GLU E  1 194 ? 1.229   -24.852 -4.677 1.00 72.19  ? 185 GLU E OE1 1 
ATOM   8511  O  OE2 . GLU E  1 194 ? -0.878  -24.601 -4.094 1.00 65.54  ? 185 GLU E OE2 1 
ATOM   8512  N  N   . ARG E  1 195 ? -3.252  -28.685 -1.121 1.00 61.75  ? 186 ARG E N   1 
ATOM   8513  C  CA  . ARG E  1 195 ? -4.575  -29.274 -1.111 1.00 62.72  ? 186 ARG E CA  1 
ATOM   8514  C  C   . ARG E  1 195 ? -5.622  -28.228 -1.429 1.00 63.71  ? 186 ARG E C   1 
ATOM   8515  O  O   . ARG E  1 195 ? -5.443  -27.053 -1.133 1.00 67.66  ? 186 ARG E O   1 
ATOM   8516  C  CB  . ARG E  1 195 ? -4.849  -30.044 0.187  1.00 71.50  ? 186 ARG E CB  1 
ATOM   8517  C  CG  . ARG E  1 195 ? -4.332  -31.487 0.097  1.00 75.77  ? 186 ARG E CG  1 
ATOM   8518  C  CD  . ARG E  1 195 ? -4.692  -32.387 1.289  1.00 96.02  ? 186 ARG E CD  1 
ATOM   8519  N  NE  . ARG E  1 195 ? -6.130  -32.595 1.495  1.00 103.11 ? 186 ARG E NE  1 
ATOM   8520  C  CZ  . ARG E  1 195 ? -6.650  -33.556 2.265  1.00 104.47 ? 186 ARG E CZ  1 
ATOM   8521  N  NH1 . ARG E  1 195 ? -5.852  -34.418 2.889  1.00 99.30  ? 186 ARG E NH1 1 
ATOM   8522  N  NH2 . ARG E  1 195 ? -7.971  -33.665 2.401  1.00 99.51  ? 186 ARG E NH2 1 
ATOM   8523  N  N   . PHE E  1 196 ? -6.673  -28.655 -2.113 1.00 64.74  ? 187 PHE E N   1 
ATOM   8524  C  CA  . PHE E  1 196 ? -7.745  -27.768 -2.533 1.00 70.07  ? 187 PHE E CA  1 
ATOM   8525  C  C   . PHE E  1 196 ? -9.059  -28.415 -2.143 1.00 74.25  ? 187 PHE E C   1 
ATOM   8526  O  O   . PHE E  1 196 ? -9.226  -29.624 -2.298 1.00 78.37  ? 187 PHE E O   1 
ATOM   8527  C  CB  . PHE E  1 196 ? -7.718  -27.566 -4.050 1.00 69.06  ? 187 PHE E CB  1 
ATOM   8528  C  CG  . PHE E  1 196 ? -6.583  -26.701 -4.549 1.00 65.61  ? 187 PHE E CG  1 
ATOM   8529  C  CD1 . PHE E  1 196 ? -6.720  -25.319 -4.597 1.00 62.58  ? 187 PHE E CD1 1 
ATOM   8530  C  CD2 . PHE E  1 196 ? -5.399  -27.277 -5.011 1.00 62.77  ? 187 PHE E CD2 1 
ATOM   8531  C  CE1 . PHE E  1 196 ? -5.691  -24.521 -5.068 1.00 64.99  ? 187 PHE E CE1 1 
ATOM   8532  C  CE2 . PHE E  1 196 ? -4.363  -26.486 -5.485 1.00 65.93  ? 187 PHE E CE2 1 
ATOM   8533  C  CZ  . PHE E  1 196 ? -4.510  -25.102 -5.516 1.00 65.81  ? 187 PHE E CZ  1 
ATOM   8534  N  N   . TYR E  1 197 ? -9.993  -27.615 -1.645 1.00 76.83  ? 188 TYR E N   1 
ATOM   8535  C  CA  . TYR E  1 197 ? -11.274 -28.141 -1.190 1.00 83.70  ? 188 TYR E CA  1 
ATOM   8536  C  C   . TYR E  1 197 ? -12.435 -27.624 -2.039 1.00 91.03  ? 188 TYR E C   1 
ATOM   8537  O  O   . TYR E  1 197 ? -12.319 -26.605 -2.725 1.00 89.69  ? 188 TYR E O   1 
ATOM   8538  C  CB  . TYR E  1 197 ? -11.487 -27.851 0.304  1.00 84.18  ? 188 TYR E CB  1 
ATOM   8539  C  CG  . TYR E  1 197 ? -10.530 -28.611 1.202  1.00 84.23  ? 188 TYR E CG  1 
ATOM   8540  C  CD1 . TYR E  1 197 ? -10.738 -29.959 1.477  1.00 89.04  ? 188 TYR E CD1 1 
ATOM   8541  C  CD2 . TYR E  1 197 ? -9.417  -27.991 1.767  1.00 79.55  ? 188 TYR E CD2 1 
ATOM   8542  C  CE1 . TYR E  1 197 ? -9.872  -30.674 2.280  1.00 81.98  ? 188 TYR E CE1 1 
ATOM   8543  C  CE2 . TYR E  1 197 ? -8.542  -28.702 2.582  1.00 82.97  ? 188 TYR E CE2 1 
ATOM   8544  C  CZ  . TYR E  1 197 ? -8.782  -30.046 2.830  1.00 86.98  ? 188 TYR E CZ  1 
ATOM   8545  O  OH  . TYR E  1 197 ? -7.941  -30.783 3.626  1.00 92.65  ? 188 TYR E OH  1 
ATOM   8546  N  N   . GLU E  1 198 ? -13.534 -28.369 -2.036 1.00 94.36  ? 189 GLU E N   1 
ATOM   8547  C  CA  . GLU E  1 198 ? -14.740 -27.925 -2.706 1.00 95.83  ? 189 GLU E CA  1 
ATOM   8548  C  C   . GLU E  1 198 ? -15.032 -26.494 -2.280 1.00 95.37  ? 189 GLU E C   1 
ATOM   8549  O  O   . GLU E  1 198 ? -15.232 -25.619 -3.114 1.00 92.71  ? 189 GLU E O   1 
ATOM   8550  C  CB  . GLU E  1 198 ? -15.915 -28.827 -2.329 1.00 103.60 ? 189 GLU E CB  1 
ATOM   8551  C  CG  . GLU E  1 198 ? -16.562 -28.474 -0.996 0.00 108.17 ? 189 GLU E CG  1 
ATOM   8552  C  CD  . GLU E  1 198 ? -17.401 -29.596 -0.429 0.00 115.21 ? 189 GLU E CD  1 
ATOM   8553  O  OE1 . GLU E  1 198 ? -18.610 -29.383 -0.194 0.00 118.47 ? 189 GLU E OE1 1 
ATOM   8554  O  OE2 . GLU E  1 198 ? -16.846 -30.691 -0.209 0.00 116.92 ? 189 GLU E OE2 1 
ATOM   8555  N  N   . CYS E  1 199 ? -14.993 -26.267 -0.970 1.00 100.21 ? 190 CYS E N   1 
ATOM   8556  C  CA  . CYS E  1 199 ? -15.442 -25.026 -0.341 1.00 96.35  ? 190 CYS E CA  1 
ATOM   8557  C  C   . CYS E  1 199 ? -14.681 -23.745 -0.724 1.00 92.61  ? 190 CYS E C   1 
ATOM   8558  O  O   . CYS E  1 199 ? -15.293 -22.678 -0.876 1.00 93.02  ? 190 CYS E O   1 
ATOM   8559  C  CB  . CYS E  1 199 ? -15.410 -25.183 1.182  1.00 98.00  ? 190 CYS E CB  1 
ATOM   8560  S  SG  . CYS E  1 199 ? -13.790 -24.957 1.964  1.00 112.17 ? 190 CYS E SG  1 
ATOM   8561  N  N   . CYS E  1 200 ? -13.359 -23.841 -0.869 1.00 90.18  ? 191 CYS E N   1 
ATOM   8562  C  CA  . CYS E  1 200 ? -12.523 -22.642 -0.927 1.00 96.24  ? 191 CYS E CA  1 
ATOM   8563  C  C   . CYS E  1 200 ? -11.446 -22.637 -2.012 1.00 86.81  ? 191 CYS E C   1 
ATOM   8564  O  O   . CYS E  1 200 ? -10.813 -23.650 -2.290 1.00 89.27  ? 191 CYS E O   1 
ATOM   8565  C  CB  . CYS E  1 200 ? -11.903 -22.369 0.450  1.00 96.46  ? 191 CYS E CB  1 
ATOM   8566  S  SG  . CYS E  1 200 ? -11.850 -23.812 1.553  1.00 114.82 ? 191 CYS E SG  1 
ATOM   8567  N  N   . LYS E  1 201 ? -11.231 -21.465 -2.593 1.00 78.50  ? 192 LYS E N   1 
ATOM   8568  C  CA  . LYS E  1 201 ? -10.264 -21.286 -3.666 1.00 75.34  ? 192 LYS E CA  1 
ATOM   8569  C  C   . LYS E  1 201 ? -8.812  -21.287 -3.193 1.00 79.40  ? 192 LYS E C   1 
ATOM   8570  O  O   . LYS E  1 201 ? -7.898  -21.291 -4.014 1.00 81.54  ? 192 LYS E O   1 
ATOM   8571  C  CB  . LYS E  1 201 ? -10.542 -19.984 -4.428 0.00 88.29  ? 192 LYS E CB  1 
ATOM   8572  C  CG  . LYS E  1 201 ? -11.651 -20.082 -5.481 0.00 95.53  ? 192 LYS E CG  1 
ATOM   8573  C  CD  . LYS E  1 201 ? -11.195 -20.882 -6.714 0.00 102.61 ? 192 LYS E CD  1 
ATOM   8574  C  CE  . LYS E  1 201 ? -12.312 -21.040 -7.744 0.00 104.12 ? 192 LYS E CE  1 
ATOM   8575  N  NZ  . LYS E  1 201 ? -13.498 -21.761 -7.187 0.00 102.50 ? 192 LYS E NZ  1 
ATOM   8576  N  N   . GLU E  1 202 ? -8.594  -21.275 -1.880 1.00 82.73  ? 193 GLU E N   1 
ATOM   8577  C  CA  . GLU E  1 202 ? -7.240  -21.138 -1.341 1.00 75.69  ? 193 GLU E CA  1 
ATOM   8578  C  C   . GLU E  1 202 ? -6.512  -22.462 -1.205 1.00 70.49  ? 193 GLU E C   1 
ATOM   8579  O  O   . GLU E  1 202 ? -7.071  -23.445 -0.716 1.00 68.71  ? 193 GLU E O   1 
ATOM   8580  C  CB  . GLU E  1 202 ? -7.238  -20.416 0.009  1.00 78.06  ? 193 GLU E CB  1 
ATOM   8581  C  CG  . GLU E  1 202 ? -5.833  -20.061 0.455  1.00 72.63  ? 193 GLU E CG  1 
ATOM   8582  C  CD  . GLU E  1 202 ? -5.771  -19.567 1.856  1.00 70.07  ? 193 GLU E CD  1 
ATOM   8583  O  OE1 . GLU E  1 202 ? -6.797  -19.621 2.568  1.00 72.18  ? 193 GLU E OE1 1 
ATOM   8584  O  OE2 . GLU E  1 202 ? -4.675  -19.128 2.236  1.00 70.98  ? 193 GLU E OE2 1 
ATOM   8585  N  N   . PRO E  1 203 ? -5.248  -22.484 -1.646 1.00 67.45  ? 194 PRO E N   1 
ATOM   8586  C  CA  . PRO E  1 203 ? -4.356  -23.633 -1.485 1.00 68.22  ? 194 PRO E CA  1 
ATOM   8587  C  C   . PRO E  1 203 ? -4.007  -23.890 -0.022 1.00 65.52  ? 194 PRO E C   1 
ATOM   8588  O  O   . PRO E  1 203 ? -3.870  -22.952 0.743  1.00 58.28  ? 194 PRO E O   1 
ATOM   8589  C  CB  . PRO E  1 203 ? -3.093  -23.201 -2.242 1.00 61.02  ? 194 PRO E CB  1 
ATOM   8590  C  CG  . PRO E  1 203 ? -3.187  -21.731 -2.322 1.00 62.29  ? 194 PRO E CG  1 
ATOM   8591  C  CD  . PRO E  1 203 ? -4.627  -21.432 -2.461 1.00 62.12  ? 194 PRO E CD  1 
ATOM   8592  N  N   . TYR E  1 204 ? -3.869  -25.162 0.340  1.00 67.19  ? 195 TYR E N   1 
ATOM   8593  C  CA  . TYR E  1 204 ? -3.447  -25.593 1.661  1.00 57.40  ? 195 TYR E CA  1 
ATOM   8594  C  C   . TYR E  1 204 ? -2.268  -26.539 1.556  1.00 56.12  ? 195 TYR E C   1 
ATOM   8595  O  O   . TYR E  1 204 ? -2.452  -27.741 1.395  1.00 65.96  ? 195 TYR E O   1 
ATOM   8596  C  CB  . TYR E  1 204 ? -4.600  -26.299 2.354  1.00 61.50  ? 195 TYR E CB  1 
ATOM   8597  C  CG  . TYR E  1 204 ? -5.660  -25.338 2.715  1.00 63.31  ? 195 TYR E CG  1 
ATOM   8598  C  CD1 . TYR E  1 204 ? -5.495  -24.496 3.794  1.00 68.43  ? 195 TYR E CD1 1 
ATOM   8599  C  CD2 . TYR E  1 204 ? -6.800  -25.222 1.953  1.00 66.84  ? 195 TYR E CD2 1 
ATOM   8600  C  CE1 . TYR E  1 204 ? -6.451  -23.571 4.122  1.00 76.12  ? 195 TYR E CE1 1 
ATOM   8601  C  CE2 . TYR E  1 204 ? -7.771  -24.297 2.268  1.00 74.26  ? 195 TYR E CE2 1 
ATOM   8602  C  CZ  . TYR E  1 204 ? -7.589  -23.470 3.356  1.00 77.31  ? 195 TYR E CZ  1 
ATOM   8603  O  OH  . TYR E  1 204 ? -8.540  -22.537 3.695  1.00 77.43  ? 195 TYR E OH  1 
ATOM   8604  N  N   . PRO E  1 205 ? -1.049  -26.003 1.625  1.00 42.71  ? 196 PRO E N   1 
ATOM   8605  C  CA  . PRO E  1 205 ? 0.157   -26.806 1.434  1.00 46.65  ? 196 PRO E CA  1 
ATOM   8606  C  C   . PRO E  1 205 ? 0.462   -27.717 2.612  1.00 57.38  ? 196 PRO E C   1 
ATOM   8607  O  O   . PRO E  1 205 ? 0.016   -27.493 3.745  1.00 61.61  ? 196 PRO E O   1 
ATOM   8608  C  CB  . PRO E  1 205 ? 1.262   -25.764 1.332  1.00 48.05  ? 196 PRO E CB  1 
ATOM   8609  C  CG  . PRO E  1 205 ? 0.591   -24.448 1.308  1.00 56.58  ? 196 PRO E CG  1 
ATOM   8610  C  CD  . PRO E  1 205 ? -0.735  -24.610 1.933  1.00 45.70  ? 196 PRO E CD  1 
ATOM   8611  N  N   . ASP E  1 206 ? 1.240   -28.755 2.336  1.00 61.61  ? 197 ASP E N   1 
ATOM   8612  C  CA  . ASP E  1 206 ? 1.822   -29.587 3.374  1.00 55.15  ? 197 ASP E CA  1 
ATOM   8613  C  C   . ASP E  1 206 ? 3.119   -30.159 2.855  1.00 58.75  ? 197 ASP E C   1 
ATOM   8614  O  O   . ASP E  1 206 ? 3.317   -30.251 1.643  1.00 58.28  ? 197 ASP E O   1 
ATOM   8615  C  CB  . ASP E  1 206 ? 0.880   -30.725 3.777  1.00 59.90  ? 197 ASP E CB  1 
ATOM   8616  C  CG  . ASP E  1 206 ? 0.429   -31.563 2.601  1.00 62.38  ? 197 ASP E CG  1 
ATOM   8617  O  OD1 . ASP E  1 206 ? 1.147   -32.513 2.212  1.00 57.59  ? 197 ASP E OD1 1 
ATOM   8618  O  OD2 . ASP E  1 206 ? -0.665  -31.272 2.078  1.00 70.99  ? 197 ASP E OD2 1 
ATOM   8619  N  N   . VAL E  1 207 ? 4.010   -30.525 3.769  1.00 53.71  ? 198 VAL E N   1 
ATOM   8620  C  CA  . VAL E  1 207 ? 5.134   -31.368 3.409  1.00 54.84  ? 198 VAL E CA  1 
ATOM   8621  C  C   . VAL E  1 207 ? 4.843   -32.780 3.879  1.00 57.85  ? 198 VAL E C   1 
ATOM   8622  O  O   . VAL E  1 207 ? 4.338   -32.989 4.973  1.00 53.99  ? 198 VAL E O   1 
ATOM   8623  C  CB  . VAL E  1 207 ? 6.456   -30.860 3.955  1.00 48.65  ? 198 VAL E CB  1 
ATOM   8624  C  CG1 . VAL E  1 207 ? 7.538   -31.874 3.707  1.00 53.72  ? 198 VAL E CG1 1 
ATOM   8625  C  CG2 . VAL E  1 207 ? 6.805   -29.555 3.288  1.00 51.71  ? 198 VAL E CG2 1 
ATOM   8626  N  N   . ASN E  1 208 ? 5.108   -33.743 3.009  1.00 62.52  ? 199 ASN E N   1 
ATOM   8627  C  CA  . ASN E  1 208 ? 4.770   -35.127 3.284  1.00 64.97  ? 199 ASN E CA  1 
ATOM   8628  C  C   . ASN E  1 208 ? 6.074   -35.853 3.496  1.00 61.59  ? 199 ASN E C   1 
ATOM   8629  O  O   . ASN E  1 208 ? 6.938   -35.862 2.626  1.00 66.06  ? 199 ASN E O   1 
ATOM   8630  C  CB  . ASN E  1 208 ? 3.972   -35.736 2.115  1.00 63.05  ? 199 ASN E CB  1 
ATOM   8631  C  CG  . ASN E  1 208 ? 3.272   -37.038 2.485  1.00 58.85  ? 199 ASN E CG  1 
ATOM   8632  O  OD1 . ASN E  1 208 ? 2.996   -37.300 3.644  1.00 57.31  ? 199 ASN E OD1 1 
ATOM   8633  N  ND2 . ASN E  1 208 ? 2.983   -37.855 1.489  1.00 63.40  ? 199 ASN E ND2 1 
ATOM   8634  N  N   . LEU E  1 209 ? 6.238   -36.418 4.680  1.00 59.85  ? 200 LEU E N   1 
ATOM   8635  C  CA  . LEU E  1 209 ? 7.439   -37.154 4.992  1.00 54.84  ? 200 LEU E CA  1 
ATOM   8636  C  C   . LEU E  1 209 ? 7.081   -38.608 4.804  1.00 62.40  ? 200 LEU E C   1 
ATOM   8637  O  O   . LEU E  1 209 ? 6.157   -39.113 5.440  1.00 59.67  ? 200 LEU E O   1 
ATOM   8638  C  CB  . LEU E  1 209 ? 7.874   -36.863 6.426  1.00 55.42  ? 200 LEU E CB  1 
ATOM   8639  C  CG  . LEU E  1 209 ? 9.142   -37.529 6.964  1.00 65.26  ? 200 LEU E CG  1 
ATOM   8640  C  CD1 . LEU E  1 209 ? 10.290  -37.386 5.997  1.00 60.39  ? 200 LEU E CD1 1 
ATOM   8641  C  CD2 . LEU E  1 209 ? 9.511   -36.947 8.326  1.00 66.99  ? 200 LEU E CD2 1 
ATOM   8642  N  N   . VAL E  1 210 ? 7.777   -39.277 3.893  1.00 66.70  ? 201 VAL E N   1 
ATOM   8643  C  CA  . VAL E  1 210 ? 7.516   -40.691 3.659  1.00 64.81  ? 201 VAL E CA  1 
ATOM   8644  C  C   . VAL E  1 210 ? 8.743   -41.541 3.977  1.00 63.47  ? 201 VAL E C   1 
ATOM   8645  O  O   . VAL E  1 210 ? 9.841   -41.319 3.453  1.00 64.05  ? 201 VAL E O   1 
ATOM   8646  C  CB  . VAL E  1 210 ? 7.005   -40.965 2.234  1.00 62.13  ? 201 VAL E CB  1 
ATOM   8647  C  CG1 . VAL E  1 210 ? 6.584   -42.420 2.115  1.00 60.10  ? 201 VAL E CG1 1 
ATOM   8648  C  CG2 . VAL E  1 210 ? 5.835   -40.041 1.893  1.00 57.88  ? 201 VAL E CG2 1 
ATOM   8649  N  N   . VAL E  1 211 ? 8.543   -42.513 4.857  1.00 60.34  ? 202 VAL E N   1 
ATOM   8650  C  CA  . VAL E  1 211 ? 9.646   -43.325 5.344  1.00 69.23  ? 202 VAL E CA  1 
ATOM   8651  C  C   . VAL E  1 211 ? 9.381   -44.796 5.055  1.00 67.84  ? 202 VAL E C   1 
ATOM   8652  O  O   . VAL E  1 211 ? 8.284   -45.298 5.308  1.00 70.58  ? 202 VAL E O   1 
ATOM   8653  C  CB  . VAL E  1 211 ? 9.912   -43.091 6.867  1.00 62.37  ? 202 VAL E CB  1 
ATOM   8654  C  CG1 . VAL E  1 211 ? 11.187  -43.771 7.300  1.00 56.69  ? 202 VAL E CG1 1 
ATOM   8655  C  CG2 . VAL E  1 211 ? 10.023  -41.624 7.152  1.00 58.83  ? 202 VAL E CG2 1 
ATOM   8656  N  N   . LYS E  1 212 ? 10.391  -45.465 4.499  1.00 67.40  ? 203 LYS E N   1 
ATOM   8657  C  CA  . LYS E  1 212 ? 10.364  -46.907 4.252  1.00 70.72  ? 203 LYS E CA  1 
ATOM   8658  C  C   . LYS E  1 212 ? 11.402  -47.565 5.181  1.00 67.26  ? 203 LYS E C   1 
ATOM   8659  O  O   . LYS E  1 212 ? 12.593  -47.244 5.133  1.00 63.96  ? 203 LYS E O   1 
ATOM   8660  C  CB  . LYS E  1 212 ? 10.678  -47.180 2.772  1.00 72.00  ? 203 LYS E CB  1 
ATOM   8661  C  CG  . LYS E  1 212 ? 10.078  -48.458 2.182  1.00 85.75  ? 203 LYS E CG  1 
ATOM   8662  C  CD  . LYS E  1 212 ? 10.380  -48.571 0.676  1.00 93.99  ? 203 LYS E CD  1 
ATOM   8663  C  CE  . LYS E  1 212 ? 10.429  -50.028 0.206  1.00 90.05  ? 203 LYS E CE  1 
ATOM   8664  N  NZ  . LYS E  1 212 ? 11.509  -50.226 -0.807 1.00 78.52  ? 203 LYS E NZ  1 
ATOM   8665  N  N   . PHE E  1 213 ? 10.958  -48.462 6.051  1.00 62.95  ? 204 PHE E N   1 
ATOM   8666  C  CA  . PHE E  1 213 ? 11.854  -48.962 7.093  1.00 69.41  ? 204 PHE E CA  1 
ATOM   8667  C  C   . PHE E  1 213 ? 11.621  -50.430 7.422  1.00 64.49  ? 204 PHE E C   1 
ATOM   8668  O  O   . PHE E  1 213 ? 10.524  -50.951 7.243  1.00 65.18  ? 204 PHE E O   1 
ATOM   8669  C  CB  . PHE E  1 213 ? 11.746  -48.092 8.362  1.00 65.72  ? 204 PHE E CB  1 
ATOM   8670  C  CG  . PHE E  1 213 ? 10.391  -48.141 9.023  1.00 61.00  ? 204 PHE E CG  1 
ATOM   8671  C  CD1 . PHE E  1 213 ? 10.214  -48.795 10.232 1.00 59.64  ? 204 PHE E CD1 1 
ATOM   8672  C  CD2 . PHE E  1 213 ? 9.295   -47.544 8.431  1.00 62.65  ? 204 PHE E CD2 1 
ATOM   8673  C  CE1 . PHE E  1 213 ? 8.970   -48.850 10.835 1.00 59.65  ? 204 PHE E CE1 1 
ATOM   8674  C  CE2 . PHE E  1 213 ? 8.049   -47.594 9.033  1.00 64.47  ? 204 PHE E CE2 1 
ATOM   8675  C  CZ  . PHE E  1 213 ? 7.890   -48.247 10.238 1.00 57.07  ? 204 PHE E CZ  1 
ATOM   8676  N  N   . ARG E  1 214 ? 12.663  -51.093 7.905  1.00 64.97  ? 205 ARG E N   1 
ATOM   8677  C  CA  . ARG E  1 214 ? 12.559  -52.498 8.281  1.00 70.17  ? 205 ARG E CA  1 
ATOM   8678  C  C   . ARG E  1 214 ? 13.471  -52.828 9.465  1.00 73.47  ? 205 ARG E C   1 
ATOM   8679  O  O   . ARG E  1 214 ? 14.443  -52.113 9.726  1.00 68.30  ? 205 ARG E O   1 
ATOM   8680  C  CB  . ARG E  1 214 ? 12.926  -53.389 7.095  1.00 73.11  ? 205 ARG E CB  1 
ATOM   8681  C  CG  . ARG E  1 214 ? 14.377  -53.270 6.684  1.00 71.85  ? 205 ARG E CG  1 
ATOM   8682  C  CD  . ARG E  1 214 ? 14.818  -54.486 5.912  1.00 75.02  ? 205 ARG E CD  1 
ATOM   8683  N  NE  . ARG E  1 214 ? 16.189  -54.347 5.440  1.00 80.16  ? 205 ARG E NE  1 
ATOM   8684  C  CZ  . ARG E  1 214 ? 16.562  -54.576 4.187  1.00 77.11  ? 205 ARG E CZ  1 
ATOM   8685  N  NH1 . ARG E  1 214 ? 15.655  -54.968 3.295  1.00 74.34  ? 205 ARG E NH1 1 
ATOM   8686  N  NH2 . ARG E  1 214 ? 17.836  -54.420 3.833  1.00 61.92  ? 205 ARG E NH2 1 
ATOM   8687  N  N   . GLU E  1 215 ? 13.166  -53.927 10.156 1.00 71.85  ? 206 GLU E N   1 
ATOM   8688  C  CA  . GLU E  1 215 ? 13.974  -54.396 11.265 1.00 63.02  ? 206 GLU E CA  1 
ATOM   8689  C  C   . GLU E  1 215 ? 15.431  -54.573 10.838 1.00 71.97  ? 206 GLU E C   1 
ATOM   8690  O  O   . GLU E  1 215 ? 15.715  -55.013 9.716  1.00 74.56  ? 206 GLU E O   1 
ATOM   8691  C  CB  . GLU E  1 215 ? 13.405  -55.706 11.784 1.00 70.77  ? 206 GLU E CB  1 
ATOM   8692  C  CG  . GLU E  1 215 ? 11.914  -55.648 12.143 1.00 77.72  ? 206 GLU E CG  1 
ATOM   8693  C  CD  . GLU E  1 215 ? 11.471  -56.820 13.031 1.00 91.78  ? 206 GLU E CD  1 
ATOM   8694  O  OE1 . GLU E  1 215 ? 12.237  -57.810 13.151 1.00 85.84  ? 206 GLU E OE1 1 
ATOM   8695  O  OE2 . GLU E  1 215 ? 10.361  -56.747 13.613 1.00 84.62  ? 206 GLU E OE2 1 
ATOM   8696  N  N   . ARG E  1 216 ? 16.347  -54.223 11.744 1.00 72.48  ? 207 ARG E N   1 
ATOM   8697  C  CA  . ARG E  1 216 ? 17.790  -54.258 11.453 1.00 78.74  ? 207 ARG E CA  1 
ATOM   8698  C  C   . ARG E  1 216 ? 18.403  -55.656 11.201 1.00 93.13  ? 207 ARG E C   1 
ATOM   8699  O  O   . ARG E  1 216 ? 19.449  -55.784 10.573 1.00 101.12 ? 207 ARG E O   1 
ATOM   8700  C  CB  . ARG E  1 216 ? 18.615  -53.522 12.511 1.00 76.29  ? 207 ARG E CB  1 
ATOM   8701  C  CG  . ARG E  1 216 ? 19.971  -53.008 12.008 1.00 78.16  ? 207 ARG E CG  1 
ATOM   8702  C  CD  . ARG E  1 216 ? 20.578  -52.062 13.042 1.00 87.39  ? 207 ARG E CD  1 
ATOM   8703  N  NE  . ARG E  1 216 ? 20.461  -52.601 14.400 1.00 80.11  ? 207 ARG E NE  1 
ATOM   8704  C  CZ  . ARG E  1 216 ? 21.490  -52.839 15.203 0.00 76.90  ? 207 ARG E CZ  1 
ATOM   8705  N  NH1 . ARG E  1 216 ? 22.722  -52.575 14.794 0.00 76.49  ? 207 ARG E NH1 1 
ATOM   8706  N  NH2 . ARG E  1 216 ? 21.287  -53.332 16.416 0.00 77.47  ? 207 ARG E NH2 1 
ATOM   8707  N  N   . ARG E  1 217 ? 17.732  -56.688 11.702 1.00 90.89  ? 208 ARG E N   1 
ATOM   8708  C  CA  A ARG E  1 217 ? 18.202  -58.057 11.535 0.50 95.82  ? 208 ARG E CA  1 
ATOM   8709  C  CA  B ARG E  1 217 ? 18.206  -58.056 11.543 0.50 95.83  ? 208 ARG E CA  1 
ATOM   8710  C  C   . ARG E  1 217 ? 17.061  -59.056 11.694 1.00 102.29 ? 208 ARG E C   1 
ATOM   8711  O  O   . ARG E  1 217 ? 16.833  -59.686 10.661 1.00 99.58  ? 208 ARG E O   1 
ATOM   8712  C  CB  A ARG E  1 217 ? 19.316  -58.368 12.537 0.50 98.00  ? 208 ARG E CB  1 
ATOM   8713  C  CB  B ARG E  1 217 ? 18.920  -58.522 12.813 0.50 98.65  ? 208 ARG E CB  1 
ATOM   8714  C  CG  A ARG E  1 217 ? 19.940  -59.742 12.364 0.50 92.93  ? 208 ARG E CG  1 
ATOM   8715  C  CG  B ARG E  1 217 ? 19.566  -59.892 12.697 0.50 93.15  ? 208 ARG E CG  1 
ATOM   8716  C  CD  A ARG E  1 217 ? 20.582  -59.886 10.995 0.50 90.26  ? 208 ARG E CD  1 
ATOM   8717  C  CD  B ARG E  1 217 ? 20.244  -60.286 13.999 0.50 83.13  ? 208 ARG E CD  1 
ATOM   8718  N  NE  A ARG E  1 217 ? 19.622  -59.666 9.916  0.50 93.30  ? 208 ARG E NE  1 
ATOM   8719  N  NE  B ARG E  1 217 ? 21.202  -59.276 14.439 0.50 90.83  ? 208 ARG E NE  1 
ATOM   8720  C  CZ  A ARG E  1 217 ? 19.926  -59.722 8.624  0.50 98.01  ? 208 ARG E CZ  1 
ATOM   8721  C  CZ  B ARG E  1 217 ? 20.885  -58.219 15.180 0.50 87.30  ? 208 ARG E CZ  1 
ATOM   8722  N  NH1 A ARG E  1 217 ? 21.167  -59.991 8.243  0.50 94.94  ? 208 ARG E NH1 1 
ATOM   8723  N  NH1 B ARG E  1 217 ? 19.631  -58.030 15.566 0.50 83.36  ? 208 ARG E NH1 1 
ATOM   8724  N  NH2 A ARG E  1 217 ? 18.988  -59.508 7.711  0.50 94.56  ? 208 ARG E NH2 1 
ATOM   8725  N  NH2 B ARG E  1 217 ? 21.822  -57.350 15.535 0.50 78.05  ? 208 ARG E NH2 1 
ATOM   8726  N  N   . LYS F  1 3   ? -17.144 0.417   70.534 1.00 106.54 ? -6  LYS F N   1 
ATOM   8727  C  CA  . LYS F  1 3   ? -16.175 1.268   71.218 1.00 103.63 ? -6  LYS F CA  1 
ATOM   8728  C  C   . LYS F  1 3   ? -15.985 2.529   70.407 1.00 105.73 ? -6  LYS F C   1 
ATOM   8729  O  O   . LYS F  1 3   ? -16.080 2.516   69.177 1.00 105.60 ? -6  LYS F O   1 
ATOM   8730  C  CB  . LYS F  1 3   ? -14.829 0.557   71.409 1.00 98.29  ? -6  LYS F CB  1 
ATOM   8731  C  CG  . LYS F  1 3   ? -14.151 0.888   72.723 1.00 101.75 ? -6  LYS F CG  1 
ATOM   8732  C  CD  . LYS F  1 3   ? -12.815 1.576   72.530 1.00 103.36 ? -6  LYS F CD  1 
ATOM   8733  C  CE  . LYS F  1 3   ? -12.398 2.332   73.798 1.00 97.93  ? -6  LYS F CE  1 
ATOM   8734  N  NZ  . LYS F  1 3   ? -13.327 3.460   74.158 1.00 83.52  ? -6  LYS F NZ  1 
ATOM   8735  N  N   . ASP F  1 4   ? -15.718 3.625   71.100 1.00 110.38 ? -5  ASP F N   1 
ATOM   8736  C  CA  . ASP F  1 4   ? -15.690 4.926   70.452 1.00 112.47 ? -5  ASP F CA  1 
ATOM   8737  C  C   . ASP F  1 4   ? -14.468 5.082   69.540 1.00 102.06 ? -5  ASP F C   1 
ATOM   8738  O  O   . ASP F  1 4   ? -14.509 5.851   68.580 1.00 98.71  ? -5  ASP F O   1 
ATOM   8739  C  CB  . ASP F  1 4   ? -15.777 6.050   71.500 1.00 116.76 ? -5  ASP F CB  1 
ATOM   8740  C  CG  . ASP F  1 4   ? -16.603 5.648   72.726 1.00 113.68 ? -5  ASP F CG  1 
ATOM   8741  O  OD1 . ASP F  1 4   ? -17.844 5.508   72.611 1.00 101.12 ? -5  ASP F OD1 1 
ATOM   8742  O  OD2 . ASP F  1 4   ? -16.001 5.472   73.808 1.00 105.96 ? -5  ASP F OD2 1 
ATOM   8743  N  N   . ASP F  1 5   ? -13.393 4.348   69.830 1.00 99.85  ? -4  ASP F N   1 
ATOM   8744  C  CA  . ASP F  1 5   ? -12.172 4.438   69.026 1.00 96.02  ? -4  ASP F CA  1 
ATOM   8745  C  C   . ASP F  1 5   ? -12.325 3.644   67.743 1.00 91.33  ? -4  ASP F C   1 
ATOM   8746  O  O   . ASP F  1 5   ? -11.746 3.983   66.712 1.00 82.57  ? -4  ASP F O   1 
ATOM   8747  C  CB  . ASP F  1 5   ? -10.949 3.929   69.791 1.00 95.36  ? -4  ASP F CB  1 
ATOM   8748  C  CG  . ASP F  1 5   ? -10.791 4.580   71.153 1.00 107.06 ? -4  ASP F CG  1 
ATOM   8749  O  OD1 . ASP F  1 5   ? -10.291 3.892   72.068 1.00 114.48 ? -4  ASP F OD1 1 
ATOM   8750  O  OD2 . ASP F  1 5   ? -11.163 5.765   71.316 1.00 96.94  ? -4  ASP F OD2 1 
ATOM   8751  N  N   . ASP F  1 6   ? -13.100 2.572   67.816 1.00 95.55  ? -3  ASP F N   1 
ATOM   8752  C  CA  . ASP F  1 6   ? -13.328 1.736   66.651 1.00 85.60  ? -3  ASP F CA  1 
ATOM   8753  C  C   . ASP F  1 6   ? -14.359 2.366   65.724 1.00 78.33  ? -3  ASP F C   1 
ATOM   8754  O  O   . ASP F  1 6   ? -14.355 2.120   64.529 1.00 79.10  ? -3  ASP F O   1 
ATOM   8755  C  CB  . ASP F  1 6   ? -13.752 0.330   67.074 1.00 90.97  ? -3  ASP F CB  1 
ATOM   8756  C  CG  . ASP F  1 6   ? -13.902 -0.611  65.900 1.00 83.75  ? -3  ASP F CG  1 
ATOM   8757  O  OD1 . ASP F  1 6   ? -12.864 -1.051  65.344 1.00 78.72  ? -3  ASP F OD1 1 
ATOM   8758  O  OD2 . ASP F  1 6   ? -15.065 -0.915  65.543 1.00 77.86  ? -3  ASP F OD2 1 
ATOM   8759  N  N   . ASP F  1 7   ? -15.244 3.184   66.273 1.00 85.52  ? -2  ASP F N   1 
ATOM   8760  C  CA  . ASP F  1 7   ? -16.200 3.888   65.437 1.00 83.96  ? -2  ASP F CA  1 
ATOM   8761  C  C   . ASP F  1 7   ? -15.491 4.916   64.565 1.00 79.72  ? -2  ASP F C   1 
ATOM   8762  O  O   . ASP F  1 7   ? -15.785 5.042   63.376 1.00 75.88  ? -2  ASP F O   1 
ATOM   8763  C  CB  . ASP F  1 7   ? -17.282 4.540   66.287 1.00 88.51  ? -2  ASP F CB  1 
ATOM   8764  C  CG  . ASP F  1 7   ? -18.465 3.631   66.501 1.00 100.83 ? -2  ASP F CG  1 
ATOM   8765  O  OD1 . ASP F  1 7   ? -18.309 2.398   66.332 1.00 96.82  ? -2  ASP F OD1 1 
ATOM   8766  O  OD2 . ASP F  1 7   ? -19.551 4.152   66.833 1.00 103.28 ? -2  ASP F OD2 1 
ATOM   8767  N  N   . LYS F  1 8   ? -14.550 5.641   65.161 1.00 80.86  ? -1  LYS F N   1 
ATOM   8768  C  CA  . LYS F  1 8   ? -13.743 6.613   64.433 1.00 74.78  ? -1  LYS F CA  1 
ATOM   8769  C  C   . LYS F  1 8   ? -13.057 5.907   63.286 1.00 71.97  ? -1  LYS F C   1 
ATOM   8770  O  O   . LYS F  1 8   ? -13.028 6.404   62.172 1.00 76.85  ? -1  LYS F O   1 
ATOM   8771  C  CB  . LYS F  1 8   ? -12.684 7.238   65.347 1.00 77.18  ? -1  LYS F CB  1 
ATOM   8772  C  CG  . LYS F  1 8   ? -13.222 8.101   66.489 1.00 80.58  ? -1  LYS F CG  1 
ATOM   8773  C  CD  . LYS F  1 8   ? -12.175 8.269   67.603 1.00 82.64  ? -1  LYS F CD  1 
ATOM   8774  C  CE  . LYS F  1 8   ? -12.445 9.492   68.486 1.00 79.41  ? -1  LYS F CE  1 
ATOM   8775  N  NZ  . LYS F  1 8   ? -12.250 10.791  67.752 1.00 86.42  ? -1  LYS F NZ  1 
ATOM   8776  N  N   . LEU F  1 9   ? -12.514 4.734   63.580 1.00 71.88  ? 0   LEU F N   1 
ATOM   8777  C  CA  . LEU F  1 9   ? -11.774 3.916   62.627 1.00 68.89  ? 0   LEU F CA  1 
ATOM   8778  C  C   . LEU F  1 9   ? -12.670 3.415   61.492 1.00 69.92  ? 0   LEU F C   1 
ATOM   8779  O  O   . LEU F  1 9   ? -12.332 3.519   60.318 1.00 60.71  ? 0   LEU F O   1 
ATOM   8780  C  CB  . LEU F  1 9   ? -11.185 2.722   63.374 1.00 71.12  ? 0   LEU F CB  1 
ATOM   8781  C  CG  . LEU F  1 9   ? -10.014 1.958   62.778 1.00 71.74  ? 0   LEU F CG  1 
ATOM   8782  C  CD1 . LEU F  1 9   ? -8.867  2.919   62.525 1.00 60.12  ? 0   LEU F CD1 1 
ATOM   8783  C  CD2 . LEU F  1 9   ? -9.606  0.834   63.721 1.00 65.48  ? 0   LEU F CD2 1 
ATOM   8784  N  N   . HIS F  1 10  ? -13.817 2.855   61.850 1.00 72.71  ? 1   HIS F N   1 
ATOM   8785  C  CA  . HIS F  1 10  ? -14.743 2.355   60.850 1.00 69.10  ? 1   HIS F CA  1 
ATOM   8786  C  C   . HIS F  1 10  ? -15.238 3.484   59.957 1.00 66.95  ? 1   HIS F C   1 
ATOM   8787  O  O   . HIS F  1 10  ? -15.538 3.272   58.790 1.00 68.79  ? 1   HIS F O   1 
ATOM   8788  C  CB  . HIS F  1 10  ? -15.927 1.630   61.505 1.00 70.90  ? 1   HIS F CB  1 
ATOM   8789  C  CG  . HIS F  1 10  ? -15.605 0.250   61.978 1.00 76.79  ? 1   HIS F CG  1 
ATOM   8790  N  ND1 . HIS F  1 10  ? -16.130 -0.885  61.387 1.00 74.97  ? 1   HIS F ND1 1 
ATOM   8791  C  CD2 . HIS F  1 10  ? -14.810 -0.193  62.979 1.00 82.21  ? 1   HIS F CD2 1 
ATOM   8792  C  CE1 . HIS F  1 10  ? -15.677 -1.953  62.010 1.00 75.97  ? 1   HIS F CE1 1 
ATOM   8793  N  NE2 . HIS F  1 10  ? -14.868 -1.562  62.982 1.00 64.45  ? 1   HIS F NE2 1 
ATOM   8794  N  N   . SER F  1 11  ? -15.344 4.689   60.502 1.00 78.03  ? 2   SER F N   1 
ATOM   8795  C  CA  . SER F  1 11  ? -15.859 5.814   59.714 1.00 74.87  ? 2   SER F CA  1 
ATOM   8796  C  C   . SER F  1 11  ? -14.792 6.502   58.846 1.00 71.97  ? 2   SER F C   1 
ATOM   8797  O  O   . SER F  1 11  ? -15.130 7.222   57.919 1.00 73.90  ? 2   SER F O   1 
ATOM   8798  C  CB  . SER F  1 11  ? -16.569 6.834   60.616 1.00 71.26  ? 2   SER F CB  1 
ATOM   8799  O  OG  . SER F  1 11  ? -15.636 7.712   61.216 1.00 68.25  ? 2   SER F OG  1 
ATOM   8800  N  N   . GLN F  1 12  ? -13.513 6.279   59.151 1.00 75.75  ? 3   GLN F N   1 
ATOM   8801  C  CA  . GLN F  1 12  ? -12.414 6.768   58.317 1.00 65.57  ? 3   GLN F CA  1 
ATOM   8802  C  C   . GLN F  1 12  ? -12.351 5.923   57.063 1.00 63.67  ? 3   GLN F C   1 
ATOM   8803  O  O   . GLN F  1 12  ? -12.059 6.423   55.985 1.00 66.00  ? 3   GLN F O   1 
ATOM   8804  C  CB  . GLN F  1 12  ? -11.070 6.672   59.051 1.00 65.18  ? 3   GLN F CB  1 
ATOM   8805  C  CG  . GLN F  1 12  ? -10.561 7.979   59.635 1.00 72.93  ? 3   GLN F CG  1 
ATOM   8806  C  CD  . GLN F  1 12  ? -9.337  7.798   60.535 1.00 76.72  ? 3   GLN F CD  1 
ATOM   8807  O  OE1 . GLN F  1 12  ? -8.576  6.839   60.393 1.00 70.56  ? 3   GLN F OE1 1 
ATOM   8808  N  NE2 . GLN F  1 12  ? -9.150  8.727   61.470 1.00 75.61  ? 3   GLN F NE2 1 
ATOM   8809  N  N   . ALA F  1 13  ? -12.625 4.632   57.225 1.00 65.52  ? 4   ALA F N   1 
ATOM   8810  C  CA  . ALA F  1 13  ? -12.531 3.661   56.142 1.00 63.56  ? 4   ALA F CA  1 
ATOM   8811  C  C   . ALA F  1 13  ? -13.735 3.743   55.216 1.00 59.12  ? 4   ALA F C   1 
ATOM   8812  O  O   . ALA F  1 13  ? -13.618 3.555   54.007 1.00 59.50  ? 4   ALA F O   1 
ATOM   8813  C  CB  . ALA F  1 13  ? -12.379 2.258   56.705 1.00 45.28  ? 4   ALA F CB  1 
ATOM   8814  N  N   . ASN F  1 14  ? -14.893 4.028   55.791 1.00 58.01  ? 5   ASN F N   1 
ATOM   8815  C  CA  . ASN F  1 14  ? -16.091 4.233   55.000 1.00 62.23  ? 5   ASN F CA  1 
ATOM   8816  C  C   . ASN F  1 14  ? -15.963 5.425   54.071 1.00 62.82  ? 5   ASN F C   1 
ATOM   8817  O  O   . ASN F  1 14  ? -16.482 5.417   52.959 1.00 64.34  ? 5   ASN F O   1 
ATOM   8818  C  CB  . ASN F  1 14  ? -17.300 4.440   55.898 1.00 65.46  ? 5   ASN F CB  1 
ATOM   8819  C  CG  . ASN F  1 14  ? -17.749 3.174   56.555 1.00 71.03  ? 5   ASN F CG  1 
ATOM   8820  O  OD1 . ASN F  1 14  ? -17.402 2.074   56.111 1.00 67.97  ? 5   ASN F OD1 1 
ATOM   8821  N  ND2 . ASN F  1 14  ? -18.536 3.312   57.621 1.00 67.73  ? 5   ASN F ND2 1 
ATOM   8822  N  N   . LEU F  1 15  ? -15.295 6.468   54.535 1.00 59.78  ? 6   LEU F N   1 
ATOM   8823  C  CA  . LEU F  1 15  ? -15.158 7.661   53.730 1.00 62.14  ? 6   LEU F CA  1 
ATOM   8824  C  C   . LEU F  1 15  ? -14.080 7.507   52.675 1.00 64.69  ? 6   LEU F C   1 
ATOM   8825  O  O   . LEU F  1 15  ? -14.224 8.010   51.563 1.00 65.55  ? 6   LEU F O   1 
ATOM   8826  C  CB  . LEU F  1 15  ? -14.855 8.869   54.598 1.00 65.06  ? 6   LEU F CB  1 
ATOM   8827  C  CG  . LEU F  1 15  ? -14.675 10.139  53.779 1.00 56.92  ? 6   LEU F CG  1 
ATOM   8828  C  CD1 . LEU F  1 15  ? -16.010 10.561  53.221 1.00 53.59  ? 6   LEU F CD1 1 
ATOM   8829  C  CD2 . LEU F  1 15  ? -14.076 11.205  54.646 1.00 51.19  ? 6   LEU F CD2 1 
ATOM   8830  N  N   . MET F  1 16  ? -12.991 6.834   53.023 1.00 61.34  ? 7   MET F N   1 
ATOM   8831  C  CA  . MET F  1 16  ? -11.964 6.549   52.037 1.00 63.09  ? 7   MET F CA  1 
ATOM   8832  C  C   . MET F  1 16  ? -12.557 5.661   50.955 1.00 63.47  ? 7   MET F C   1 
ATOM   8833  O  O   . MET F  1 16  ? -12.247 5.796   49.775 1.00 65.37  ? 7   MET F O   1 
ATOM   8834  C  CB  . MET F  1 16  ? -10.770 5.866   52.681 1.00 62.47  ? 7   MET F CB  1 
ATOM   8835  C  CG  . MET F  1 16  ? -9.725  6.815   53.230 1.00 73.12  ? 7   MET F CG  1 
ATOM   8836  S  SD  . MET F  1 16  ? -8.533  5.935   54.270 1.00 93.88  ? 7   MET F SD  1 
ATOM   8837  C  CE  . MET F  1 16  ? -7.077  6.948   54.055 1.00 95.67  ? 7   MET F CE  1 
ATOM   8838  N  N   . ARG F  1 17  ? -13.433 4.758   51.370 1.00 68.05  ? 8   ARG F N   1 
ATOM   8839  C  CA  . ARG F  1 17  ? -14.062 3.810   50.455 1.00 69.59  ? 8   ARG F CA  1 
ATOM   8840  C  C   . ARG F  1 17  ? -15.077 4.480   49.540 1.00 65.46  ? 8   ARG F C   1 
ATOM   8841  O  O   . ARG F  1 17  ? -15.143 4.166   48.361 1.00 65.35  ? 8   ARG F O   1 
ATOM   8842  C  CB  . ARG F  1 17  ? -14.722 2.690   51.250 1.00 66.32  ? 8   ARG F CB  1 
ATOM   8843  C  CG  . ARG F  1 17  ? -15.449 1.684   50.425 1.00 64.92  ? 8   ARG F CG  1 
ATOM   8844  C  CD  . ARG F  1 17  ? -15.826 0.509   51.292 1.00 69.82  ? 8   ARG F CD  1 
ATOM   8845  N  NE  . ARG F  1 17  ? -17.243 0.548   51.598 1.00 55.62  ? 8   ARG F NE  1 
ATOM   8846  C  CZ  . ARG F  1 17  ? -17.736 0.671   52.818 1.00 72.07  ? 8   ARG F CZ  1 
ATOM   8847  N  NH1 . ARG F  1 17  ? -16.918 0.757   53.860 1.00 74.96  ? 8   ARG F NH1 1 
ATOM   8848  N  NH2 . ARG F  1 17  ? -19.048 0.701   52.985 1.00 74.05  ? 8   ARG F NH2 1 
ATOM   8849  N  N   . LEU F  1 18  ? -15.863 5.405   50.088 1.00 66.11  ? 9   LEU F N   1 
ATOM   8850  C  CA  . LEU F  1 18  ? -16.812 6.175   49.290 1.00 62.88  ? 9   LEU F CA  1 
ATOM   8851  C  C   . LEU F  1 18  ? -16.085 6.953   48.208 1.00 67.52  ? 9   LEU F C   1 
ATOM   8852  O  O   . LEU F  1 18  ? -16.560 7.070   47.085 1.00 65.71  ? 9   LEU F O   1 
ATOM   8853  C  CB  . LEU F  1 18  ? -17.610 7.134   50.169 1.00 57.73  ? 9   LEU F CB  1 
ATOM   8854  C  CG  . LEU F  1 18  ? -18.520 8.120   49.437 1.00 55.78  ? 9   LEU F CG  1 
ATOM   8855  C  CD1 . LEU F  1 18  ? -19.397 7.424   48.424 1.00 54.97  ? 9   LEU F CD1 1 
ATOM   8856  C  CD2 . LEU F  1 18  ? -19.368 8.847   50.431 1.00 55.65  ? 9   LEU F CD2 1 
ATOM   8857  N  N   . LYS F  1 19  ? -14.913 7.467   48.553 1.00 72.39  ? 10  LYS F N   1 
ATOM   8858  C  CA  . LYS F  1 19  ? -14.147 8.309   47.644 1.00 69.81  ? 10  LYS F CA  1 
ATOM   8859  C  C   . LYS F  1 19  ? -13.528 7.574   46.470 1.00 68.28  ? 10  LYS F C   1 
ATOM   8860  O  O   . LYS F  1 19  ? -13.496 8.106   45.370 1.00 75.49  ? 10  LYS F O   1 
ATOM   8861  C  CB  . LYS F  1 19  ? -13.071 9.071   48.403 1.00 66.88  ? 10  LYS F CB  1 
ATOM   8862  C  CG  . LYS F  1 19  ? -13.580 10.333  49.011 1.00 62.86  ? 10  LYS F CG  1 
ATOM   8863  C  CD  . LYS F  1 19  ? -12.436 11.078  49.591 1.00 72.09  ? 10  LYS F CD  1 
ATOM   8864  C  CE  . LYS F  1 19  ? -12.704 12.551  49.610 1.00 66.72  ? 10  LYS F CE  1 
ATOM   8865  N  NZ  . LYS F  1 19  ? -11.506 13.245  50.143 1.00 76.07  ? 10  LYS F NZ  1 
ATOM   8866  N  N   . SER F  1 20  ? -13.023 6.365   46.688 1.00 69.16  ? 11  SER F N   1 
ATOM   8867  C  CA  . SER F  1 20  ? -12.483 5.612   45.564 1.00 78.62  ? 11  SER F CA  1 
ATOM   8868  C  C   . SER F  1 20  ? -13.626 5.025   44.739 1.00 76.06  ? 11  SER F C   1 
ATOM   8869  O  O   . SER F  1 20  ? -13.534 4.963   43.518 1.00 86.03  ? 11  SER F O   1 
ATOM   8870  C  CB  . SER F  1 20  ? -11.463 4.549   45.994 1.00 72.02  ? 11  SER F CB  1 
ATOM   8871  O  OG  . SER F  1 20  ? -12.093 3.422   46.549 1.00 69.37  ? 11  SER F OG  1 
ATOM   8872  N  N   . ASP F  1 21  ? -14.718 4.644   45.396 1.00 68.65  ? 12  ASP F N   1 
ATOM   8873  C  CA  . ASP F  1 21  ? -15.898 4.159   44.684 1.00 68.29  ? 12  ASP F CA  1 
ATOM   8874  C  C   . ASP F  1 21  ? -16.512 5.221   43.752 1.00 76.09  ? 12  ASP F C   1 
ATOM   8875  O  O   . ASP F  1 21  ? -17.333 4.898   42.895 1.00 75.66  ? 12  ASP F O   1 
ATOM   8876  C  CB  . ASP F  1 21  ? -16.938 3.598   45.660 1.00 57.91  ? 12  ASP F CB  1 
ATOM   8877  C  CG  . ASP F  1 21  ? -16.570 2.199   46.176 1.00 75.80  ? 12  ASP F CG  1 
ATOM   8878  O  OD1 . ASP F  1 21  ? -15.440 1.717   45.905 1.00 73.58  ? 12  ASP F OD1 1 
ATOM   8879  O  OD2 . ASP F  1 21  ? -17.414 1.580   46.864 1.00 69.67  ? 12  ASP F OD2 1 
ATOM   8880  N  N   . LEU F  1 22  ? -16.105 6.478   43.920 1.00 72.32  ? 13  LEU F N   1 
ATOM   8881  C  CA  . LEU F  1 22  ? -16.533 7.576   43.046 1.00 70.94  ? 13  LEU F CA  1 
ATOM   8882  C  C   . LEU F  1 22  ? -15.512 8.187   42.073 1.00 79.37  ? 13  LEU F C   1 
ATOM   8883  O  O   . LEU F  1 22  ? -15.810 8.407   40.901 1.00 76.41  ? 13  LEU F O   1 
ATOM   8884  C  CB  . LEU F  1 22  ? -17.011 8.780   43.864 1.00 69.54  ? 13  LEU F CB  1 
ATOM   8885  C  CG  . LEU F  1 22  ? -18.244 8.665   44.775 1.00 64.81  ? 13  LEU F CG  1 
ATOM   8886  C  CD1 . LEU F  1 22  ? -18.303 9.847   45.729 1.00 59.88  ? 13  LEU F CD1 1 
ATOM   8887  C  CD2 . LEU F  1 22  ? -19.555 8.538   44.014 1.00 55.67  ? 13  LEU F CD2 1 
ATOM   8888  N  N   . PHE F  1 23  ? -14.321 8.485   42.586 1.00 78.34  ? 14  PHE F N   1 
ATOM   8889  C  CA  . PHE F  1 23  ? -13.241 9.095   41.797 1.00 86.61  ? 14  PHE F CA  1 
ATOM   8890  C  C   . PHE F  1 23  ? -12.249 8.164   41.107 1.00 85.88  ? 14  PHE F C   1 
ATOM   8891  O  O   . PHE F  1 23  ? -11.630 8.530   40.108 1.00 87.31  ? 14  PHE F O   1 
ATOM   8892  C  CB  . PHE F  1 23  ? -12.452 10.061  42.678 1.00 87.47  ? 14  PHE F CB  1 
ATOM   8893  C  CG  . PHE F  1 23  ? -13.302 11.109  43.326 1.00 80.20  ? 14  PHE F CG  1 
ATOM   8894  C  CD1 . PHE F  1 23  ? -14.387 11.649  42.651 1.00 76.30  ? 14  PHE F CD1 1 
ATOM   8895  C  CD2 . PHE F  1 23  ? -13.035 11.532  44.611 1.00 70.79  ? 14  PHE F CD2 1 
ATOM   8896  C  CE1 . PHE F  1 23  ? -15.175 12.593  43.243 1.00 79.19  ? 14  PHE F CE1 1 
ATOM   8897  C  CE2 . PHE F  1 23  ? -13.817 12.477  45.212 1.00 75.68  ? 14  PHE F CE2 1 
ATOM   8898  C  CZ  . PHE F  1 23  ? -14.887 13.013  44.535 1.00 81.30  ? 14  PHE F CZ  1 
ATOM   8899  N  N   . ASN F  1 24  ? -12.066 6.978   41.659 1.00 96.10  ? 15  ASN F N   1 
ATOM   8900  C  CA  . ASN F  1 24  ? -11.026 6.076   41.172 1.00 105.04 ? 15  ASN F CA  1 
ATOM   8901  C  C   . ASN F  1 24  ? -11.462 4.829   40.402 1.00 98.32  ? 15  ASN F C   1 
ATOM   8902  O  O   . ASN F  1 24  ? -10.902 4.515   39.356 1.00 105.27 ? 15  ASN F O   1 
ATOM   8903  C  CB  . ASN F  1 24  ? -10.105 5.636   42.306 1.00 101.08 ? 15  ASN F CB  1 
ATOM   8904  C  CG  . ASN F  1 24  ? -9.435  6.820   42.985 1.00 106.06 ? 15  ASN F CG  1 
ATOM   8905  O  OD1 . ASN F  1 24  ? -9.894  7.957   42.863 1.00 105.05 ? 15  ASN F OD1 1 
ATOM   8906  N  ND2 . ASN F  1 24  ? -8.344  6.562   43.696 1.00 101.13 ? 15  ASN F ND2 1 
ATOM   8907  N  N   . ARG F  1 25  ? -12.418 4.092   40.945 1.00 89.97  ? 16  ARG F N   1 
ATOM   8908  C  CA  . ARG F  1 25  ? -13.137 3.068   40.198 1.00 99.82  ? 16  ARG F CA  1 
ATOM   8909  C  C   . ARG F  1 25  ? -13.884 3.603   38.959 1.00 115.71 ? 16  ARG F C   1 
ATOM   8910  O  O   . ARG F  1 25  ? -13.556 3.225   37.828 1.00 114.22 ? 16  ARG F O   1 
ATOM   8911  C  CB  . ARG F  1 25  ? -14.038 2.278   41.134 1.00 94.09  ? 16  ARG F CB  1 
ATOM   8912  C  CG  . ARG F  1 25  ? -13.248 1.766   42.348 1.00 98.15  ? 16  ARG F CG  1 
ATOM   8913  C  CD  . ARG F  1 25  ? -14.083 0.860   43.212 1.00 89.06  ? 16  ARG F CD  1 
ATOM   8914  N  NE  . ARG F  1 25  ? -14.898 0.010   42.359 1.00 97.38  ? 16  ARG F NE  1 
ATOM   8915  C  CZ  . ARG F  1 25  ? -14.396 -0.909  41.542 1.00 100.16 ? 16  ARG F CZ  1 
ATOM   8916  N  NH1 . ARG F  1 25  ? -15.200 -1.624  40.773 1.00 89.25  ? 16  ARG F NH1 1 
ATOM   8917  N  NH2 . ARG F  1 25  ? -13.085 -1.111  41.485 1.00 99.04  ? 16  ARG F NH2 1 
ATOM   8918  N  N   . SER F  1 26  ? -14.879 4.469   39.148 1.00 112.68 ? 17  SER F N   1 
ATOM   8919  C  CA  . SER F  1 26  ? -15.532 5.097   37.988 1.00 118.01 ? 17  SER F CA  1 
ATOM   8920  C  C   . SER F  1 26  ? -14.796 6.382   37.517 1.00 115.82 ? 17  SER F C   1 
ATOM   8921  O  O   . SER F  1 26  ? -14.255 7.128   38.341 1.00 109.08 ? 17  SER F O   1 
ATOM   8922  C  CB  . SER F  1 26  ? -17.018 5.352   38.273 1.00 113.17 ? 17  SER F CB  1 
ATOM   8923  O  OG  . SER F  1 26  ? -17.707 4.132   38.499 1.00 101.07 ? 17  SER F OG  1 
ATOM   8924  N  N   . PRO F  1 27  ? -14.777 6.637   36.188 1.00 117.68 ? 18  PRO F N   1 
ATOM   8925  C  CA  . PRO F  1 27  ? -13.981 7.699   35.540 1.00 112.78 ? 18  PRO F CA  1 
ATOM   8926  C  C   . PRO F  1 27  ? -14.568 9.099   35.729 1.00 111.54 ? 18  PRO F C   1 
ATOM   8927  O  O   . PRO F  1 27  ? -15.786 9.222   35.859 1.00 110.55 ? 18  PRO F O   1 
ATOM   8928  C  CB  . PRO F  1 27  ? -14.056 7.323   34.061 1.00 99.81  ? 18  PRO F CB  1 
ATOM   8929  C  CG  . PRO F  1 27  ? -15.413 6.718   33.923 1.00 107.42 ? 18  PRO F CG  1 
ATOM   8930  C  CD  . PRO F  1 27  ? -15.661 5.959   35.221 1.00 114.24 ? 18  PRO F CD  1 
ATOM   8931  N  N   . MET F  1 28  ? -13.729 10.137  35.715 1.00 110.66 ? 19  MET F N   1 
ATOM   8932  C  CA  . MET F  1 28  ? -14.221 11.495  35.978 1.00 105.85 ? 19  MET F CA  1 
ATOM   8933  C  C   . MET F  1 28  ? -15.133 12.035  34.873 1.00 103.20 ? 19  MET F C   1 
ATOM   8934  O  O   . MET F  1 28  ? -14.836 11.910  33.679 1.00 94.06  ? 19  MET F O   1 
ATOM   8935  C  CB  . MET F  1 28  ? -13.092 12.498  36.263 1.00 106.11 ? 19  MET F CB  1 
ATOM   8936  C  CG  . MET F  1 28  ? -13.621 13.810  36.883 1.00 94.42  ? 19  MET F CG  1 
ATOM   8937  S  SD  . MET F  1 28  ? -12.616 15.296  36.621 1.00 100.67 ? 19  MET F SD  1 
ATOM   8938  C  CE  . MET F  1 28  ? -11.141 14.889  37.567 1.00 93.15  ? 19  MET F CE  1 
ATOM   8939  N  N   . TYR F  1 29  ? -16.224 12.663  35.314 1.00 94.03  ? 20  TYR F N   1 
ATOM   8940  C  CA  . TYR F  1 29  ? -17.311 13.168  34.469 1.00 79.04  ? 20  TYR F CA  1 
ATOM   8941  C  C   . TYR F  1 29  ? -16.857 14.149  33.372 1.00 72.21  ? 20  TYR F C   1 
ATOM   8942  O  O   . TYR F  1 29  ? -16.184 15.148  33.638 1.00 69.72  ? 20  TYR F O   1 
ATOM   8943  C  CB  . TYR F  1 29  ? -18.393 13.744  35.393 1.00 70.69  ? 20  TYR F CB  1 
ATOM   8944  C  CG  . TYR F  1 29  ? -19.446 14.659  34.808 1.00 71.30  ? 20  TYR F CG  1 
ATOM   8945  C  CD1 . TYR F  1 29  ? -20.723 14.194  34.515 1.00 65.25  ? 20  TYR F CD1 1 
ATOM   8946  C  CD2 . TYR F  1 29  ? -19.189 16.011  34.630 1.00 71.17  ? 20  TYR F CD2 1 
ATOM   8947  C  CE1 . TYR F  1 29  ? -21.700 15.048  34.022 1.00 64.23  ? 20  TYR F CE1 1 
ATOM   8948  C  CE2 . TYR F  1 29  ? -20.153 16.869  34.138 1.00 66.43  ? 20  TYR F CE2 1 
ATOM   8949  C  CZ  . TYR F  1 29  ? -21.404 16.392  33.834 1.00 69.06  ? 20  TYR F CZ  1 
ATOM   8950  O  OH  . TYR F  1 29  ? -22.345 17.277  33.345 1.00 67.25  ? 20  TYR F OH  1 
ATOM   8951  N  N   . PRO F  1 30  ? -17.234 13.842  32.121 1.00 75.26  ? 21  PRO F N   1 
ATOM   8952  C  CA  . PRO F  1 30  ? -16.730 14.467  30.891 1.00 66.93  ? 21  PRO F CA  1 
ATOM   8953  C  C   . PRO F  1 30  ? -17.134 15.932  30.733 1.00 65.45  ? 21  PRO F C   1 
ATOM   8954  O  O   . PRO F  1 30  ? -16.548 16.640  29.912 1.00 67.86  ? 21  PRO F O   1 
ATOM   8955  C  CB  . PRO F  1 30  ? -17.362 13.613  29.797 1.00 58.07  ? 21  PRO F CB  1 
ATOM   8956  C  CG  . PRO F  1 30  ? -18.621 13.103  30.414 1.00 64.27  ? 21  PRO F CG  1 
ATOM   8957  C  CD  . PRO F  1 30  ? -18.292 12.851  31.840 1.00 70.18  ? 21  PRO F CD  1 
ATOM   8958  N  N   . GLY F  1 31  ? -18.118 16.373  31.511 1.00 58.56  ? 22  GLY F N   1 
ATOM   8959  C  CA  . GLY F  1 31  ? -18.712 17.682  31.342 1.00 61.19  ? 22  GLY F CA  1 
ATOM   8960  C  C   . GLY F  1 31  ? -20.098 17.519  30.757 1.00 63.40  ? 22  GLY F C   1 
ATOM   8961  O  O   . GLY F  1 31  ? -20.445 16.447  30.291 1.00 64.53  ? 22  GLY F O   1 
ATOM   8962  N  N   . PRO F  1 32  ? -20.915 18.574  30.785 1.00 65.99  ? 23  PRO F N   1 
ATOM   8963  C  CA  . PRO F  1 32  ? -22.239 18.325  30.204 1.00 66.65  ? 23  PRO F CA  1 
ATOM   8964  C  C   . PRO F  1 32  ? -22.194 18.316  28.677 1.00 67.15  ? 23  PRO F C   1 
ATOM   8965  O  O   . PRO F  1 32  ? -21.149 18.590  28.087 1.00 63.52  ? 23  PRO F O   1 
ATOM   8966  C  CB  . PRO F  1 32  ? -23.065 19.518  30.704 1.00 72.68  ? 23  PRO F CB  1 
ATOM   8967  C  CG  . PRO F  1 32  ? -22.054 20.609  30.955 1.00 63.46  ? 23  PRO F CG  1 
ATOM   8968  C  CD  . PRO F  1 32  ? -20.787 19.920  31.377 1.00 61.43  ? 23  PRO F CD  1 
ATOM   8969  N  N   . THR F  1 33  ? -23.333 18.024  28.058 1.00 69.37  ? 24  THR F N   1 
ATOM   8970  C  CA  . THR F  1 33  ? -23.483 18.033  26.606 1.00 70.60  ? 24  THR F CA  1 
ATOM   8971  C  C   . THR F  1 33  ? -24.925 18.393  26.382 1.00 71.35  ? 24  THR F C   1 
ATOM   8972  O  O   . THR F  1 33  ? -25.669 18.532  27.346 1.00 74.25  ? 24  THR F O   1 
ATOM   8973  C  CB  . THR F  1 33  ? -23.266 16.645  25.985 1.00 76.17  ? 24  THR F CB  1 
ATOM   8974  O  OG1 . THR F  1 33  ? -24.033 15.680  26.709 1.00 74.57  ? 24  THR F OG1 1 
ATOM   8975  C  CG2 . THR F  1 33  ? -21.799 16.242  26.026 1.00 75.19  ? 24  THR F CG2 1 
ATOM   8976  N  N   . LYS F  1 34  ? -25.340 18.517  25.129 1.00 77.88  ? 25  LYS F N   1 
ATOM   8977  C  CA  . LYS F  1 34  ? -26.730 18.862  24.844 1.00 77.20  ? 25  LYS F CA  1 
ATOM   8978  C  C   . LYS F  1 34  ? -27.685 17.741  25.270 1.00 78.92  ? 25  LYS F C   1 
ATOM   8979  O  O   . LYS F  1 34  ? -28.858 17.997  25.557 1.00 79.33  ? 25  LYS F O   1 
ATOM   8980  C  CB  . LYS F  1 34  ? -26.904 19.229  23.372 1.00 68.51  ? 25  LYS F CB  1 
ATOM   8981  C  CG  . LYS F  1 34  ? -26.565 20.687  23.070 1.00 88.15  ? 25  LYS F CG  1 
ATOM   8982  C  CD  . LYS F  1 34  ? -26.230 20.917  21.603 1.00 88.71  ? 25  LYS F CD  1 
ATOM   8983  C  CE  . LYS F  1 34  ? -24.904 20.272  21.239 1.00 94.39  ? 25  LYS F CE  1 
ATOM   8984  N  NZ  . LYS F  1 34  ? -23.759 20.948  21.906 1.00 91.19  ? 25  LYS F NZ  1 
ATOM   8985  N  N   . ASP F  1 35  ? -27.164 16.513  25.328 1.00 74.61  ? 26  ASP F N   1 
ATOM   8986  C  CA  . ASP F  1 35  ? -27.937 15.328  25.722 1.00 80.12  ? 26  ASP F CA  1 
ATOM   8987  C  C   . ASP F  1 35  ? -27.895 15.092  27.214 1.00 77.09  ? 26  ASP F C   1 
ATOM   8988  O  O   . ASP F  1 35  ? -28.578 14.208  27.731 1.00 80.89  ? 26  ASP F O   1 
ATOM   8989  C  CB  . ASP F  1 35  ? -27.378 14.063  25.067 1.00 81.49  ? 26  ASP F CB  1 
ATOM   8990  C  CG  . ASP F  1 35  ? -27.528 14.063  23.579 1.00 82.30  ? 26  ASP F CG  1 
ATOM   8991  O  OD1 . ASP F  1 35  ? -28.680 14.150  23.101 1.00 84.63  ? 26  ASP F OD1 1 
ATOM   8992  O  OD2 . ASP F  1 35  ? -26.485 13.975  22.898 1.00 82.55  ? 26  ASP F OD2 1 
ATOM   8993  N  N   . ASP F  1 36  ? -27.024 15.827  27.889 1.00 78.99  ? 27  ASP F N   1 
ATOM   8994  C  CA  . ASP F  1 36  ? -26.876 15.721  29.331 1.00 75.15  ? 27  ASP F CA  1 
ATOM   8995  C  C   . ASP F  1 36  ? -26.599 17.115  29.867 1.00 71.50  ? 27  ASP F C   1 
ATOM   8996  O  O   . ASP F  1 36  ? -25.469 17.422  30.243 1.00 68.64  ? 27  ASP F O   1 
ATOM   8997  C  CB  . ASP F  1 36  ? -25.734 14.763  29.662 1.00 76.38  ? 27  ASP F CB  1 
ATOM   8998  C  CG  . ASP F  1 36  ? -25.694 14.382  31.126 1.00 82.98  ? 27  ASP F CG  1 
ATOM   8999  O  OD1 . ASP F  1 36  ? -26.748 14.459  31.798 1.00 84.37  ? 27  ASP F OD1 1 
ATOM   9000  O  OD2 . ASP F  1 36  ? -24.601 13.998  31.596 1.00 76.12  ? 27  ASP F OD2 1 
ATOM   9001  N  N   . PRO F  1 37  ? -27.624 17.978  29.856 1.00 73.75  ? 28  PRO F N   1 
ATOM   9002  C  CA  . PRO F  1 37  ? -27.504 19.398  30.211 1.00 72.89  ? 28  PRO F CA  1 
ATOM   9003  C  C   . PRO F  1 37  ? -27.454 19.580  31.712 1.00 64.27  ? 28  PRO F C   1 
ATOM   9004  O  O   . PRO F  1 37  ? -28.013 18.777  32.445 1.00 65.29  ? 28  PRO F O   1 
ATOM   9005  C  CB  . PRO F  1 37  ? -28.791 19.999  29.656 1.00 76.29  ? 28  PRO F CB  1 
ATOM   9006  C  CG  . PRO F  1 37  ? -29.788 18.892  29.801 1.00 86.07  ? 28  PRO F CG  1 
ATOM   9007  C  CD  . PRO F  1 37  ? -29.027 17.587  29.632 1.00 75.73  ? 28  PRO F CD  1 
ATOM   9008  N  N   . LEU F  1 38  ? -26.808 20.641  32.161 1.00 63.50  ? 29  LEU F N   1 
ATOM   9009  C  CA  . LEU F  1 38  ? -26.599 20.846  33.583 1.00 60.10  ? 29  LEU F CA  1 
ATOM   9010  C  C   . LEU F  1 38  ? -26.963 22.256  34.029 1.00 63.25  ? 29  LEU F C   1 
ATOM   9011  O  O   . LEU F  1 38  ? -26.582 23.238  33.393 1.00 63.36  ? 29  LEU F O   1 
ATOM   9012  C  CB  . LEU F  1 38  ? -25.137 20.591  33.899 1.00 61.18  ? 29  LEU F CB  1 
ATOM   9013  C  CG  . LEU F  1 38  ? -24.670 20.844  35.318 1.00 55.25  ? 29  LEU F CG  1 
ATOM   9014  C  CD1 . LEU F  1 38  ? -25.066 19.683  36.191 1.00 61.79  ? 29  LEU F CD1 1 
ATOM   9015  C  CD2 . LEU F  1 38  ? -23.180 20.988  35.277 1.00 62.08  ? 29  LEU F CD2 1 
ATOM   9016  N  N   . THR F  1 39  ? -27.694 22.365  35.131 1.00 67.38  ? 30  THR F N   1 
ATOM   9017  C  CA  . THR F  1 39  ? -27.952 23.682  35.696 1.00 63.65  ? 30  THR F CA  1 
ATOM   9018  C  C   . THR F  1 39  ? -26.980 23.982  36.830 1.00 60.58  ? 30  THR F C   1 
ATOM   9019  O  O   . THR F  1 39  ? -26.834 23.198  37.774 1.00 59.44  ? 30  THR F O   1 
ATOM   9020  C  CB  . THR F  1 39  ? -29.391 23.846  36.200 1.00 61.74  ? 30  THR F CB  1 
ATOM   9021  O  OG1 . THR F  1 39  ? -30.309 23.299  35.251 1.00 77.39  ? 30  THR F OG1 1 
ATOM   9022  C  CG2 . THR F  1 39  ? -29.699 25.295  36.355 1.00 67.02  ? 30  THR F CG2 1 
ATOM   9023  N  N   . VAL F  1 40  ? -26.300 25.114  36.697 1.00 60.77  ? 31  VAL F N   1 
ATOM   9024  C  CA  . VAL F  1 40  ? -25.456 25.669  37.744 1.00 61.88  ? 31  VAL F CA  1 
ATOM   9025  C  C   . VAL F  1 40  ? -26.166 26.869  38.368 1.00 59.61  ? 31  VAL F C   1 
ATOM   9026  O  O   . VAL F  1 40  ? -26.613 27.766  37.659 1.00 59.17  ? 31  VAL F O   1 
ATOM   9027  C  CB  . VAL F  1 40  ? -24.119 26.162  37.171 1.00 59.98  ? 31  VAL F CB  1 
ATOM   9028  C  CG1 . VAL F  1 40  ? -23.291 26.809  38.265 1.00 58.52  ? 31  VAL F CG1 1 
ATOM   9029  C  CG2 . VAL F  1 40  ? -23.361 25.028  36.496 1.00 59.25  ? 31  VAL F CG2 1 
ATOM   9030  N  N   . TYR F  1 41  ? -26.283 26.893  39.688 1.00 59.14  ? 32  TYR F N   1 
ATOM   9031  C  CA  . TYR F  1 41  ? -26.844 28.066  40.343 1.00 63.53  ? 32  TYR F CA  1 
ATOM   9032  C  C   . TYR F  1 41  ? -25.739 29.029  40.747 1.00 62.24  ? 32  TYR F C   1 
ATOM   9033  O  O   . TYR F  1 41  ? -24.674 28.596  41.179 1.00 61.80  ? 32  TYR F O   1 
ATOM   9034  C  CB  . TYR F  1 41  ? -27.682 27.661  41.548 1.00 68.14  ? 32  TYR F CB  1 
ATOM   9035  C  CG  . TYR F  1 41  ? -29.014 27.078  41.162 1.00 74.05  ? 32  TYR F CG  1 
ATOM   9036  C  CD1 . TYR F  1 41  ? -30.148 27.884  41.090 1.00 76.68  ? 32  TYR F CD1 1 
ATOM   9037  C  CD2 . TYR F  1 41  ? -29.141 25.729  40.849 1.00 66.87  ? 32  TYR F CD2 1 
ATOM   9038  C  CE1 . TYR F  1 41  ? -31.376 27.361  40.727 1.00 78.03  ? 32  TYR F CE1 1 
ATOM   9039  C  CE2 . TYR F  1 41  ? -30.367 25.194  40.483 1.00 76.94  ? 32  TYR F CE2 1 
ATOM   9040  C  CZ  . TYR F  1 41  ? -31.482 26.016  40.424 1.00 87.46  ? 32  TYR F CZ  1 
ATOM   9041  O  OH  . TYR F  1 41  ? -32.706 25.494  40.059 1.00 93.93  ? 32  TYR F OH  1 
ATOM   9042  N  N   . LEU F  1 42  ? -25.982 30.329  40.574 1.00 60.09  ? 33  LEU F N   1 
ATOM   9043  C  CA  . LEU F  1 42  ? -25.043 31.361  41.028 1.00 57.35  ? 33  LEU F CA  1 
ATOM   9044  C  C   . LEU F  1 42  ? -25.645 32.261  42.087 1.00 60.58  ? 33  LEU F C   1 
ATOM   9045  O  O   . LEU F  1 42  ? -26.825 32.597  42.039 1.00 64.55  ? 33  LEU F O   1 
ATOM   9046  C  CB  . LEU F  1 42  ? -24.574 32.248  39.885 1.00 54.33  ? 33  LEU F CB  1 
ATOM   9047  C  CG  . LEU F  1 42  ? -23.463 31.785  38.953 1.00 64.26  ? 33  LEU F CG  1 
ATOM   9048  C  CD1 . LEU F  1 42  ? -22.878 33.025  38.320 1.00 64.72  ? 33  LEU F CD1 1 
ATOM   9049  C  CD2 . LEU F  1 42  ? -22.382 30.988  39.673 1.00 58.55  ? 33  LEU F CD2 1 
ATOM   9050  N  N   . SER F  1 43  ? -24.816 32.631  43.054 1.00 66.32  ? 34  SER F N   1 
ATOM   9051  C  CA  . SER F  1 43  ? -25.174 33.631  44.052 1.00 66.29  ? 34  SER F CA  1 
ATOM   9052  C  C   . SER F  1 43  ? -23.928 34.416  44.444 1.00 58.71  ? 34  SER F C   1 
ATOM   9053  O  O   . SER F  1 43  ? -22.849 33.848  44.572 1.00 54.39  ? 34  SER F O   1 
ATOM   9054  C  CB  . SER F  1 43  ? -25.808 32.974  45.279 1.00 65.15  ? 34  SER F CB  1 
ATOM   9055  O  OG  . SER F  1 43  ? -26.553 33.931  46.019 1.00 66.95  ? 34  SER F OG  1 
ATOM   9056  N  N   . PHE F  1 44  ? -24.072 35.720  44.634 1.00 59.78  ? 35  PHE F N   1 
ATOM   9057  C  CA  . PHE F  1 44  ? -22.924 36.544  45.008 1.00 57.06  ? 35  PHE F CA  1 
ATOM   9058  C  C   . PHE F  1 44  ? -23.050 37.056  46.426 1.00 62.22  ? 35  PHE F C   1 
ATOM   9059  O  O   . PHE F  1 44  ? -24.153 37.324  46.899 1.00 68.81  ? 35  PHE F O   1 
ATOM   9060  C  CB  . PHE F  1 44  ? -22.727 37.701  44.018 1.00 54.69  ? 35  PHE F CB  1 
ATOM   9061  C  CG  . PHE F  1 44  ? -22.145 37.262  42.724 1.00 63.38  ? 35  PHE F CG  1 
ATOM   9062  C  CD1 . PHE F  1 44  ? -20.767 37.219  42.558 1.00 59.03  ? 35  PHE F CD1 1 
ATOM   9063  C  CD2 . PHE F  1 44  ? -22.968 36.823  41.691 1.00 59.93  ? 35  PHE F CD2 1 
ATOM   9064  C  CE1 . PHE F  1 44  ? -20.214 36.769  41.378 1.00 60.41  ? 35  PHE F CE1 1 
ATOM   9065  C  CE2 . PHE F  1 44  ? -22.427 36.369  40.507 1.00 57.49  ? 35  PHE F CE2 1 
ATOM   9066  C  CZ  . PHE F  1 44  ? -21.046 36.341  40.348 1.00 65.79  ? 35  PHE F CZ  1 
ATOM   9067  N  N   . SER F  1 45  ? -21.917 37.157  47.109 1.00 64.15  ? 36  SER F N   1 
ATOM   9068  C  CA  . SER F  1 45  ? -21.855 37.848  48.385 1.00 60.68  ? 36  SER F CA  1 
ATOM   9069  C  C   . SER F  1 45  ? -20.748 38.896  48.337 1.00 54.94  ? 36  SER F C   1 
ATOM   9070  O  O   . SER F  1 45  ? -19.562 38.579  48.266 1.00 49.08  ? 36  SER F O   1 
ATOM   9071  C  CB  . SER F  1 45  ? -21.612 36.855  49.516 1.00 58.16  ? 36  SER F CB  1 
ATOM   9072  O  OG  . SER F  1 45  ? -21.714 37.493  50.775 1.00 68.60  ? 36  SER F OG  1 
ATOM   9073  N  N   . LEU F  1 46  ? -21.145 40.156  48.391 1.00 58.73  ? 37  LEU F N   1 
ATOM   9074  C  CA  . LEU F  1 46  ? -20.175 41.237  48.375 1.00 59.19  ? 37  LEU F CA  1 
ATOM   9075  C  C   . LEU F  1 46  ? -19.495 41.381  49.715 1.00 59.21  ? 37  LEU F C   1 
ATOM   9076  O  O   . LEU F  1 46  ? -20.125 41.203  50.765 1.00 64.82  ? 37  LEU F O   1 
ATOM   9077  C  CB  . LEU F  1 46  ? -20.834 42.551  48.002 1.00 65.02  ? 37  LEU F CB  1 
ATOM   9078  C  CG  . LEU F  1 46  ? -20.106 43.170  46.825 1.00 67.77  ? 37  LEU F CG  1 
ATOM   9079  C  CD1 . LEU F  1 46  ? -19.805 42.055  45.831 1.00 68.57  ? 37  LEU F CD1 1 
ATOM   9080  C  CD2 . LEU F  1 46  ? -20.957 44.268  46.201 1.00 72.04  ? 37  LEU F CD2 1 
ATOM   9081  N  N   . LEU F  1 47  ? -18.208 41.713  49.664 1.00 55.32  ? 38  LEU F N   1 
ATOM   9082  C  CA  . LEU F  1 47  ? -17.342 41.751  50.841 1.00 56.01  ? 38  LEU F CA  1 
ATOM   9083  C  C   . LEU F  1 47  ? -16.693 43.118  51.025 1.00 56.56  ? 38  LEU F C   1 
ATOM   9084  O  O   . LEU F  1 47  ? -16.836 43.749  52.068 1.00 62.45  ? 38  LEU F O   1 
ATOM   9085  C  CB  . LEU F  1 47  ? -16.269 40.669  50.765 1.00 50.44  ? 38  LEU F CB  1 
ATOM   9086  C  CG  . LEU F  1 47  ? -16.410 39.576  51.807 1.00 57.37  ? 38  LEU F CG  1 
ATOM   9087  C  CD1 . LEU F  1 47  ? -17.729 38.850  51.646 1.00 60.21  ? 38  LEU F CD1 1 
ATOM   9088  C  CD2 . LEU F  1 47  ? -15.244 38.616  51.728 1.00 65.86  ? 38  LEU F CD2 1 
ATOM   9089  N  N   . ASP F  1 48  ? -15.901 43.523  50.043 1.00 50.11  ? 39  ASP F N   1 
ATOM   9090  C  CA  . ASP F  1 48  ? -15.253 44.809  50.072 1.00 50.38  ? 39  ASP F CA  1 
ATOM   9091  C  C   . ASP F  1 48  ? -15.053 45.292  48.645 1.00 57.33  ? 39  ASP F C   1 
ATOM   9092  O  O   . ASP F  1 48  ? -14.735 44.489  47.770 1.00 55.60  ? 39  ASP F O   1 
ATOM   9093  C  CB  . ASP F  1 48  ? -13.898 44.657  50.756 1.00 53.46  ? 39  ASP F CB  1 
ATOM   9094  C  CG  . ASP F  1 48  ? -13.290 45.979  51.145 1.00 60.63  ? 39  ASP F CG  1 
ATOM   9095  O  OD1 . ASP F  1 48  ? -14.046 46.963  51.212 1.00 64.87  ? 39  ASP F OD1 1 
ATOM   9096  O  OD2 . ASP F  1 48  ? -12.070 46.043  51.401 1.00 65.15  ? 39  ASP F OD2 1 
ATOM   9097  N  N   . ILE F  1 49  ? -15.207 46.598  48.411 1.00 60.44  ? 40  ILE F N   1 
ATOM   9098  C  CA  . ILE F  1 49  ? -14.723 47.206  47.170 1.00 56.42  ? 40  ILE F CA  1 
ATOM   9099  C  C   . ILE F  1 49  ? -13.422 47.868  47.546 1.00 55.48  ? 40  ILE F C   1 
ATOM   9100  O  O   . ILE F  1 49  ? -13.416 48.895  48.204 1.00 62.01  ? 40  ILE F O   1 
ATOM   9101  C  CB  . ILE F  1 49  ? -15.654 48.316  46.638 1.00 50.42  ? 40  ILE F CB  1 
ATOM   9102  C  CG1 . ILE F  1 49  ? -16.968 47.732  46.140 1.00 47.75  ? 40  ILE F CG1 1 
ATOM   9103  C  CG2 . ILE F  1 49  ? -14.983 49.090  45.512 1.00 48.65  ? 40  ILE F CG2 1 
ATOM   9104  C  CD1 . ILE F  1 49  ? -17.776 48.703  45.324 1.00 51.89  ? 40  ILE F CD1 1 
ATOM   9105  N  N   . VAL F  1 50  ? -12.315 47.298  47.105 1.00 54.61  ? 41  VAL F N   1 
ATOM   9106  C  CA  . VAL F  1 50  ? -11.031 47.701  47.633 1.00 57.47  ? 41  VAL F CA  1 
ATOM   9107  C  C   . VAL F  1 50  ? -10.538 49.018  47.049 1.00 57.92  ? 41  VAL F C   1 
ATOM   9108  O  O   . VAL F  1 50  ? -10.077 49.898  47.778 1.00 62.70  ? 41  VAL F O   1 
ATOM   9109  C  CB  . VAL F  1 50  ? -10.009 46.591  47.474 1.00 52.71  ? 41  VAL F CB  1 
ATOM   9110  C  CG1 . VAL F  1 50  ? -8.643  47.076  47.908 1.00 52.73  ? 41  VAL F CG1 1 
ATOM   9111  C  CG2 . VAL F  1 50  ? -10.459 45.392  48.286 1.00 48.70  ? 41  VAL F CG2 1 
ATOM   9112  N  N   . LYS F  1 51  ? -10.640 49.170  45.736 1.00 55.58  ? 42  LYS F N   1 
ATOM   9113  C  CA  . LYS F  1 51  ? -10.316 50.456  45.130 1.00 62.59  ? 42  LYS F CA  1 
ATOM   9114  C  C   . LYS F  1 51  ? -11.047 50.630  43.824 1.00 62.09  ? 42  LYS F C   1 
ATOM   9115  O  O   . LYS F  1 51  ? -11.440 49.648  43.201 1.00 55.20  ? 42  LYS F O   1 
ATOM   9116  C  CB  . LYS F  1 51  ? -8.818  50.585  44.875 1.00 61.55  ? 42  LYS F CB  1 
ATOM   9117  C  CG  . LYS F  1 51  ? -8.343  49.723  43.750 1.00 58.25  ? 42  LYS F CG  1 
ATOM   9118  C  CD  . LYS F  1 51  ? -7.189  50.366  43.028 1.00 69.57  ? 42  LYS F CD  1 
ATOM   9119  C  CE  . LYS F  1 51  ? -6.062  50.718  43.965 1.00 65.17  ? 42  LYS F CE  1 
ATOM   9120  N  NZ  . LYS F  1 51  ? -4.960  51.329  43.180 1.00 76.14  ? 42  LYS F NZ  1 
ATOM   9121  N  N   . ALA F  1 52  ? -11.226 51.891  43.423 1.00 65.16  ? 43  ALA F N   1 
ATOM   9122  C  CA  . ALA F  1 52  ? -11.716 52.227  42.089 1.00 64.11  ? 43  ALA F CA  1 
ATOM   9123  C  C   . ALA F  1 52  ? -10.716 53.171  41.432 1.00 61.97  ? 43  ALA F C   1 
ATOM   9124  O  O   . ALA F  1 52  ? -10.596 54.311  41.845 1.00 68.20  ? 43  ALA F O   1 
ATOM   9125  C  CB  . ALA F  1 52  ? -13.085 52.882  42.187 1.00 52.00  ? 43  ALA F CB  1 
ATOM   9126  N  N   . ASP F  1 53  ? -10.023 52.721  40.389 1.00 63.33  ? 44  ASP F N   1 
ATOM   9127  C  CA  . ASP F  1 53  ? -8.976  53.541  39.772 1.00 63.87  ? 44  ASP F CA  1 
ATOM   9128  C  C   . ASP F  1 53  ? -9.553  54.349  38.614 1.00 69.21  ? 44  ASP F C   1 
ATOM   9129  O  O   . ASP F  1 53  ? -9.915  53.797  37.574 1.00 68.64  ? 44  ASP F O   1 
ATOM   9130  C  CB  . ASP F  1 53  ? -7.813  52.667  39.284 1.00 65.03  ? 44  ASP F CB  1 
ATOM   9131  C  CG  . ASP F  1 53  ? -6.583  53.483  38.881 1.00 68.50  ? 44  ASP F CG  1 
ATOM   9132  O  OD1 . ASP F  1 53  ? -6.742  54.663  38.493 1.00 72.28  ? 44  ASP F OD1 1 
ATOM   9133  O  OD2 . ASP F  1 53  ? -5.452  52.943  38.946 1.00 64.45  ? 44  ASP F OD2 1 
ATOM   9134  N  N   . SER F  1 54  ? -9.617  55.666  38.787 1.00 74.27  ? 45  SER F N   1 
ATOM   9135  C  CA  . SER F  1 54  ? -10.296 56.517  37.816 1.00 70.25  ? 45  SER F CA  1 
ATOM   9136  C  C   . SER F  1 54  ? -9.391  56.840  36.639 1.00 67.00  ? 45  SER F C   1 
ATOM   9137  O  O   . SER F  1 54  ? -9.849  57.354  35.621 1.00 67.89  ? 45  SER F O   1 
ATOM   9138  C  CB  . SER F  1 54  ? -10.793 57.802  38.477 1.00 70.93  ? 45  SER F CB  1 
ATOM   9139  O  OG  . SER F  1 54  ? -9.711  58.566  38.982 1.00 79.59  ? 45  SER F OG  1 
ATOM   9140  N  N   . SER F  1 55  ? -8.105  56.548  36.795 1.00 60.88  ? 46  SER F N   1 
ATOM   9141  C  CA  . SER F  1 55  ? -7.145  56.749  35.725 1.00 61.88  ? 46  SER F CA  1 
ATOM   9142  C  C   . SER F  1 55  ? -7.176  55.617  34.700 1.00 62.07  ? 46  SER F C   1 
ATOM   9143  O  O   . SER F  1 55  ? -6.940  55.833  33.517 1.00 62.83  ? 46  SER F O   1 
ATOM   9144  C  CB  . SER F  1 55  ? -5.740  56.890  36.296 1.00 59.45  ? 46  SER F CB  1 
ATOM   9145  O  OG  . SER F  1 55  ? -5.199  55.622  36.583 1.00 61.48  ? 46  SER F OG  1 
ATOM   9146  N  N   . THR F  1 56  ? -7.339  54.392  35.178 1.00 65.80  ? 47  THR F N   1 
ATOM   9147  C  CA  . THR F  1 56  ? -7.523  53.231  34.308 1.00 62.72  ? 47  THR F CA  1 
ATOM   9148  C  C   . THR F  1 56  ? -8.958  52.735  34.144 1.00 58.01  ? 47  THR F C   1 
ATOM   9149  O  O   . THR F  1 56  ? -9.205  51.790  33.410 1.00 58.62  ? 47  THR F O   1 
ATOM   9150  C  CB  . THR F  1 56  ? -6.657  52.076  34.788 1.00 65.10  ? 47  THR F CB  1 
ATOM   9151  O  OG1 . THR F  1 56  ? -6.974  51.788  36.162 1.00 68.09  ? 47  THR F OG1 1 
ATOM   9152  C  CG2 . THR F  1 56  ? -5.182  52.449  34.665 1.00 59.92  ? 47  THR F CG2 1 
ATOM   9153  N  N   . ASN F  1 57  ? -9.900  53.348  34.839 1.00 60.90  ? 48  ASN F N   1 
ATOM   9154  C  CA  . ASN F  1 57  ? -11.258 52.821  34.861 1.00 63.82  ? 48  ASN F CA  1 
ATOM   9155  C  C   . ASN F  1 57  ? -11.342 51.329  35.162 1.00 64.21  ? 48  ASN F C   1 
ATOM   9156  O  O   . ASN F  1 57  ? -12.019 50.579  34.459 1.00 58.17  ? 48  ASN F O   1 
ATOM   9157  C  CB  . ASN F  1 57  ? -11.966 53.113  33.549 1.00 63.43  ? 48  ASN F CB  1 
ATOM   9158  C  CG  . ASN F  1 57  ? -12.628 54.456  33.544 1.00 65.41  ? 48  ASN F CG  1 
ATOM   9159  O  OD1 . ASN F  1 57  ? -12.351 55.299  34.386 1.00 72.53  ? 48  ASN F OD1 1 
ATOM   9160  N  ND2 . ASN F  1 57  ? -13.518 54.663  32.600 1.00 68.17  ? 48  ASN F ND2 1 
ATOM   9161  N  N   . GLU F  1 58  ? -10.651 50.902  36.213 1.00 63.27  ? 49  GLU F N   1 
ATOM   9162  C  CA  . GLU F  1 58  ? -10.827 49.553  36.722 1.00 61.47  ? 49  GLU F CA  1 
ATOM   9163  C  C   . GLU F  1 58  ? -11.226 49.627  38.189 1.00 65.73  ? 49  GLU F C   1 
ATOM   9164  O  O   . GLU F  1 58  ? -10.896 50.578  38.887 1.00 64.41  ? 49  GLU F O   1 
ATOM   9165  C  CB  . GLU F  1 58  ? -9.547  48.729  36.596 1.00 65.36  ? 49  GLU F CB  1 
ATOM   9166  C  CG  . GLU F  1 58  ? -8.698  48.983  35.366 1.00 64.47  ? 49  GLU F CG  1 
ATOM   9167  C  CD  . GLU F  1 58  ? -7.426  48.155  35.382 1.00 63.94  ? 49  GLU F CD  1 
ATOM   9168  O  OE1 . GLU F  1 58  ? -6.322  48.701  35.620 1.00 64.82  ? 49  GLU F OE1 1 
ATOM   9169  O  OE2 . GLU F  1 58  ? -7.536  46.936  35.171 1.00 65.55  ? 49  GLU F OE2 1 
ATOM   9170  N  N   . VAL F  1 59  ? -11.923 48.604  38.659 1.00 65.54  ? 50  VAL F N   1 
ATOM   9171  C  CA  . VAL F  1 59  ? -12.352 48.546  40.041 1.00 54.36  ? 50  VAL F CA  1 
ATOM   9172  C  C   . VAL F  1 59  ? -12.037 47.158  40.585 1.00 57.20  ? 50  VAL F C   1 
ATOM   9173  O  O   . VAL F  1 59  ? -12.245 46.154  39.914 1.00 55.45  ? 50  VAL F O   1 
ATOM   9174  C  CB  . VAL F  1 59  ? -13.847 48.871  40.151 1.00 52.12  ? 50  VAL F CB  1 
ATOM   9175  C  CG1 . VAL F  1 59  ? -14.400 48.412  41.448 1.00 59.54  ? 50  VAL F CG1 1 
ATOM   9176  C  CG2 . VAL F  1 59  ? -14.050 50.356  40.007 1.00 58.93  ? 50  VAL F CG2 1 
ATOM   9177  N  N   . ASP F  1 60  ? -11.493 47.115  41.792 1.00 55.86  ? 51  ASP F N   1 
ATOM   9178  C  CA  . ASP F  1 60  ? -11.145 45.863  42.437 1.00 50.28  ? 51  ASP F CA  1 
ATOM   9179  C  C   . ASP F  1 60  ? -12.168 45.510  43.489 1.00 49.96  ? 51  ASP F C   1 
ATOM   9180  O  O   . ASP F  1 60  ? -12.391 46.255  44.425 1.00 57.42  ? 51  ASP F O   1 
ATOM   9181  C  CB  . ASP F  1 60  ? -9.754  45.943  43.053 1.00 49.38  ? 51  ASP F CB  1 
ATOM   9182  C  CG  . ASP F  1 60  ? -8.691  46.254  42.027 1.00 55.56  ? 51  ASP F CG  1 
ATOM   9183  O  OD1 . ASP F  1 60  ? -9.049  46.516  40.861 1.00 62.80  ? 51  ASP F OD1 1 
ATOM   9184  O  OD2 . ASP F  1 60  ? -7.497  46.259  42.373 1.00 62.61  ? 51  ASP F OD2 1 
ATOM   9185  N  N   . LEU F  1 61  ? -12.770 44.344  43.332 1.00 54.14  ? 52  LEU F N   1 
ATOM   9186  C  CA  . LEU F  1 61  ? -13.814 43.869  44.217 1.00 54.51  ? 52  LEU F CA  1 
ATOM   9187  C  C   . LEU F  1 61  ? -13.403 42.547  44.930 1.00 52.13  ? 52  LEU F C   1 
ATOM   9188  O  O   . LEU F  1 61  ? -12.786 41.682  44.324 1.00 52.62  ? 52  LEU F O   1 
ATOM   9189  C  CB  . LEU F  1 61  ? -15.081 43.725  43.366 1.00 57.45  ? 52  LEU F CB  1 
ATOM   9190  C  CG  . LEU F  1 61  ? -16.371 43.074  43.858 1.00 68.59  ? 52  LEU F CG  1 
ATOM   9191  C  CD1 . LEU F  1 61  ? -16.728 43.555  45.258 1.00 70.92  ? 52  LEU F CD1 1 
ATOM   9192  C  CD2 . LEU F  1 61  ? -17.502 43.374  42.873 1.00 60.50  ? 52  LEU F CD2 1 
ATOM   9193  N  N   . VAL F  1 62  ? -13.689 42.410  46.225 1.00 52.26  ? 53  VAL F N   1 
ATOM   9194  C  CA  . VAL F  1 62  ? -13.535 41.111  46.899 1.00 49.51  ? 53  VAL F CA  1 
ATOM   9195  C  C   . VAL F  1 62  ? -14.916 40.530  47.174 1.00 49.56  ? 53  VAL F C   1 
ATOM   9196  O  O   . VAL F  1 62  ? -15.801 41.238  47.616 1.00 54.23  ? 53  VAL F O   1 
ATOM   9197  C  CB  . VAL F  1 62  ? -12.755 41.205  48.234 1.00 50.26  ? 53  VAL F CB  1 
ATOM   9198  C  CG1 . VAL F  1 62  ? -12.865 39.912  48.990 1.00 46.53  ? 53  VAL F CG1 1 
ATOM   9199  C  CG2 . VAL F  1 62  ? -11.289 41.539  48.003 1.00 48.32  ? 53  VAL F CG2 1 
ATOM   9200  N  N   . TYR F  1 63  ? -15.123 39.257  46.871 1.00 50.15  ? 54  TYR F N   1 
ATOM   9201  C  CA  . TYR F  1 63  ? -16.450 38.657  47.033 1.00 52.37  ? 54  TYR F CA  1 
ATOM   9202  C  C   . TYR F  1 63  ? -16.391 37.145  47.134 1.00 53.22  ? 54  TYR F C   1 
ATOM   9203  O  O   . TYR F  1 63  ? -15.394 36.524  46.767 1.00 53.69  ? 54  TYR F O   1 
ATOM   9204  C  CB  . TYR F  1 63  ? -17.373 39.043  45.869 1.00 54.62  ? 54  TYR F CB  1 
ATOM   9205  C  CG  . TYR F  1 63  ? -16.847 38.592  44.535 1.00 51.92  ? 54  TYR F CG  1 
ATOM   9206  C  CD1 . TYR F  1 63  ? -17.386 37.497  43.887 1.00 54.71  ? 54  TYR F CD1 1 
ATOM   9207  C  CD2 . TYR F  1 63  ? -15.783 39.248  43.941 1.00 55.93  ? 54  TYR F CD2 1 
ATOM   9208  C  CE1 . TYR F  1 63  ? -16.884 37.070  42.674 1.00 57.03  ? 54  TYR F CE1 1 
ATOM   9209  C  CE2 . TYR F  1 63  ? -15.274 38.832  42.736 1.00 55.32  ? 54  TYR F CE2 1 
ATOM   9210  C  CZ  . TYR F  1 63  ? -15.829 37.746  42.105 1.00 56.11  ? 54  TYR F CZ  1 
ATOM   9211  O  OH  . TYR F  1 63  ? -15.311 37.345  40.900 1.00 61.58  ? 54  TYR F OH  1 
ATOM   9212  N  N   . TRP F  1 64  ? -17.469 36.561  47.647 1.00 57.80  ? 55  TRP F N   1 
ATOM   9213  C  CA  . TRP F  1 64  ? -17.682 35.122  47.568 1.00 58.10  ? 55  TRP F CA  1 
ATOM   9214  C  C   . TRP F  1 64  ? -18.673 34.846  46.441 1.00 59.52  ? 55  TRP F C   1 
ATOM   9215  O  O   . TRP F  1 64  ? -19.694 35.522  46.300 1.00 54.47  ? 55  TRP F O   1 
ATOM   9216  C  CB  . TRP F  1 64  ? -18.200 34.552  48.892 1.00 56.79  ? 55  TRP F CB  1 
ATOM   9217  C  CG  . TRP F  1 64  ? -17.374 34.952  50.072 1.00 60.07  ? 55  TRP F CG  1 
ATOM   9218  C  CD1 . TRP F  1 64  ? -16.051 35.301  50.072 1.00 60.76  ? 55  TRP F CD1 1 
ATOM   9219  C  CD2 . TRP F  1 64  ? -17.816 35.064  51.429 1.00 69.34  ? 55  TRP F CD2 1 
ATOM   9220  N  NE1 . TRP F  1 64  ? -15.640 35.618  51.347 1.00 62.88  ? 55  TRP F NE1 1 
ATOM   9221  C  CE2 . TRP F  1 64  ? -16.708 35.484  52.199 1.00 71.92  ? 55  TRP F CE2 1 
ATOM   9222  C  CE3 . TRP F  1 64  ? -19.042 34.846  52.073 1.00 71.36  ? 55  TRP F CE3 1 
ATOM   9223  C  CZ2 . TRP F  1 64  ? -16.793 35.695  53.576 1.00 74.09  ? 55  TRP F CZ2 1 
ATOM   9224  C  CZ3 . TRP F  1 64  ? -19.123 35.057  53.439 1.00 73.70  ? 55  TRP F CZ3 1 
ATOM   9225  C  CH2 . TRP F  1 64  ? -18.006 35.476  54.175 1.00 72.64  ? 55  TRP F CH2 1 
ATOM   9226  N  N   . GLU F  1 65  ? -18.342 33.870  45.610 1.00 59.83  ? 56  GLU F N   1 
ATOM   9227  C  CA  . GLU F  1 65  ? -19.223 33.473  44.528 1.00 61.68  ? 56  GLU F CA  1 
ATOM   9228  C  C   . GLU F  1 65  ? -19.696 32.055  44.782 1.00 60.98  ? 56  GLU F C   1 
ATOM   9229  O  O   . GLU F  1 65  ? -18.910 31.125  44.722 1.00 65.72  ? 56  GLU F O   1 
ATOM   9230  C  CB  . GLU F  1 65  ? -18.474 33.585  43.203 1.00 59.85  ? 56  GLU F CB  1 
ATOM   9231  C  CG  . GLU F  1 65  ? -18.940 32.688  42.091 1.00 59.38  ? 56  GLU F CG  1 
ATOM   9232  C  CD  . GLU F  1 65  ? -18.163 32.952  40.814 1.00 69.06  ? 56  GLU F CD  1 
ATOM   9233  O  OE1 . GLU F  1 65  ? -17.318 33.873  40.798 1.00 69.85  ? 56  GLU F OE1 1 
ATOM   9234  O  OE2 . GLU F  1 65  ? -18.389 32.244  39.818 1.00 77.32  ? 56  GLU F OE2 1 
ATOM   9235  N  N   . GLN F  1 66  ? -20.974 31.887  45.091 1.00 57.57  ? 57  GLN F N   1 
ATOM   9236  C  CA  . GLN F  1 66  ? -21.484 30.548  45.291 1.00 59.62  ? 57  GLN F CA  1 
ATOM   9237  C  C   . GLN F  1 66  ? -21.876 29.896  43.972 1.00 69.11  ? 57  GLN F C   1 
ATOM   9238  O  O   . GLN F  1 66  ? -22.613 30.471  43.169 1.00 63.90  ? 57  GLN F O   1 
ATOM   9239  C  CB  . GLN F  1 66  ? -22.664 30.529  46.243 1.00 65.13  ? 57  GLN F CB  1 
ATOM   9240  C  CG  . GLN F  1 66  ? -22.704 29.231  47.035 1.00 80.24  ? 57  GLN F CG  1 
ATOM   9241  C  CD  . GLN F  1 66  ? -24.074 28.909  47.580 1.00 88.36  ? 57  GLN F CD  1 
ATOM   9242  O  OE1 . GLN F  1 66  ? -25.036 29.642  47.349 1.00 97.39  ? 57  GLN F OE1 1 
ATOM   9243  N  NE2 . GLN F  1 66  ? -24.174 27.802  48.305 1.00 84.75  ? 57  GLN F NE2 1 
ATOM   9244  N  N   . GLN F  1 67  ? -21.362 28.690  43.758 1.00 69.05  ? 58  GLN F N   1 
ATOM   9245  C  CA  . GLN F  1 67  ? -21.682 27.900  42.581 1.00 57.10  ? 58  GLN F CA  1 
ATOM   9246  C  C   . GLN F  1 67  ? -22.269 26.590  43.056 1.00 61.47  ? 58  GLN F C   1 
ATOM   9247  O  O   . GLN F  1 67  ? -21.678 25.903  43.892 1.00 61.61  ? 58  GLN F O   1 
ATOM   9248  C  CB  . GLN F  1 67  ? -20.424 27.636  41.769 1.00 52.89  ? 58  GLN F CB  1 
ATOM   9249  C  CG  . GLN F  1 67  ? -19.617 28.872  41.495 1.00 53.28  ? 58  GLN F CG  1 
ATOM   9250  C  CD  . GLN F  1 67  ? -18.447 28.574  40.615 1.00 60.42  ? 58  GLN F CD  1 
ATOM   9251  O  OE1 . GLN F  1 67  ? -18.269 27.437  40.177 1.00 63.49  ? 58  GLN F OE1 1 
ATOM   9252  N  NE2 . GLN F  1 67  ? -17.633 29.584  40.343 1.00 61.37  ? 58  GLN F NE2 1 
ATOM   9253  N  N   . SER F  1 68  ? -23.437 26.233  42.541 1.00 58.49  ? 59  SER F N   1 
ATOM   9254  C  CA  . SER F  1 68  ? -24.065 24.972  42.918 1.00 61.32  ? 59  SER F CA  1 
ATOM   9255  C  C   . SER F  1 68  ? -24.475 24.183  41.682 1.00 61.39  ? 59  SER F C   1 
ATOM   9256  O  O   . SER F  1 68  ? -24.859 24.757  40.664 1.00 57.32  ? 59  SER F O   1 
ATOM   9257  C  CB  . SER F  1 68  ? -25.281 25.200  43.827 1.00 59.78  ? 59  SER F CB  1 
ATOM   9258  O  OG  . SER F  1 68  ? -25.202 26.439  44.510 1.00 72.94  ? 59  SER F OG  1 
ATOM   9259  N  N   . TRP F  1 69  ? -24.365 22.879  41.771 1.00 59.18  ? 60  TRP F N   1 
ATOM   9260  C  CA  . TRP F  1 69  ? -24.853 22.017  40.705 1.00 62.33  ? 60  TRP F CA  1 
ATOM   9261  C  C   . TRP F  1 69  ? -25.109 20.597  41.201 1.00 60.64  ? 60  TRP F C   1 
ATOM   9262  O  O   . TRP F  1 69  ? -24.594 20.200  42.241 1.00 55.15  ? 60  TRP F O   1 
ATOM   9263  C  CB  . TRP F  1 69  ? -23.899 22.030  39.499 1.00 60.56  ? 60  TRP F CB  1 
ATOM   9264  C  CG  . TRP F  1 69  ? -22.566 21.438  39.774 1.00 55.81  ? 60  TRP F CG  1 
ATOM   9265  C  CD1 . TRP F  1 69  ? -22.202 20.138  39.614 1.00 59.17  ? 60  TRP F CD1 1 
ATOM   9266  C  CD2 . TRP F  1 69  ? -21.410 22.123  40.256 1.00 54.33  ? 60  TRP F CD2 1 
ATOM   9267  N  NE1 . TRP F  1 69  ? -20.888 19.965  39.977 1.00 63.57  ? 60  TRP F NE1 1 
ATOM   9268  C  CE2 . TRP F  1 69  ? -20.381 21.172  40.375 1.00 57.18  ? 60  TRP F CE2 1 
ATOM   9269  C  CE3 . TRP F  1 69  ? -21.147 23.444  40.608 1.00 57.95  ? 60  TRP F CE3 1 
ATOM   9270  C  CZ2 . TRP F  1 69  ? -19.112 21.501  40.821 1.00 55.93  ? 60  TRP F CZ2 1 
ATOM   9271  C  CZ3 . TRP F  1 69  ? -19.889 23.767  41.054 1.00 57.58  ? 60  TRP F CZ3 1 
ATOM   9272  C  CH2 . TRP F  1 69  ? -18.885 22.800  41.153 1.00 52.99  ? 60  TRP F CH2 1 
ATOM   9273  N  N   . LYS F  1 70  ? -25.919 19.843  40.460 1.00 62.71  ? 61  LYS F N   1 
ATOM   9274  C  CA  . LYS F  1 70  ? -26.151 18.440  40.790 1.00 64.96  ? 61  LYS F CA  1 
ATOM   9275  C  C   . LYS F  1 70  ? -25.613 17.511  39.701 1.00 59.43  ? 61  LYS F C   1 
ATOM   9276  O  O   . LYS F  1 70  ? -25.657 17.837  38.531 1.00 58.41  ? 61  LYS F O   1 
ATOM   9277  C  CB  . LYS F  1 70  ? -27.631 18.155  41.039 1.00 60.89  ? 61  LYS F CB  1 
ATOM   9278  C  CG  . LYS F  1 70  ? -27.949 16.694  40.834 1.00 71.21  ? 61  LYS F CG  1 
ATOM   9279  C  CD  . LYS F  1 70  ? -29.338 16.298  41.279 1.00 85.85  ? 61  LYS F CD  1 
ATOM   9280  C  CE  . LYS F  1 70  ? -29.546 14.794  41.044 1.00 91.21  ? 61  LYS F CE  1 
ATOM   9281  N  NZ  . LYS F  1 70  ? -30.813 14.260  41.628 1.00 95.66  ? 61  LYS F NZ  1 
ATOM   9282  N  N   . LEU F  1 71  ? -25.079 16.367  40.108 1.00 62.42  ? 62  LEU F N   1 
ATOM   9283  C  CA  . LEU F  1 71  ? -24.627 15.336  39.187 1.00 61.50  ? 62  LEU F CA  1 
ATOM   9284  C  C   . LEU F  1 71  ? -25.112 13.981  39.682 1.00 68.84  ? 62  LEU F C   1 
ATOM   9285  O  O   . LEU F  1 71  ? -24.901 13.625  40.839 1.00 68.30  ? 62  LEU F O   1 
ATOM   9286  C  CB  . LEU F  1 71  ? -23.099 15.317  39.081 1.00 60.60  ? 62  LEU F CB  1 
ATOM   9287  C  CG  . LEU F  1 71  ? -22.364 16.465  38.388 1.00 63.30  ? 62  LEU F CG  1 
ATOM   9288  C  CD1 . LEU F  1 71  ? -20.905 16.103  38.179 1.00 62.40  ? 62  LEU F CD1 1 
ATOM   9289  C  CD2 . LEU F  1 71  ? -23.009 16.832  37.058 1.00 66.77  ? 62  LEU F CD2 1 
ATOM   9290  N  N   . ASN F  1 72  ? -25.764 13.220  38.811 1.00 75.74  ? 63  ASN F N   1 
ATOM   9291  C  CA  . ASN F  1 72  ? -26.183 11.872  39.179 1.00 79.06  ? 63  ASN F CA  1 
ATOM   9292  C  C   . ASN F  1 72  ? -24.968 11.019  39.499 1.00 72.10  ? 63  ASN F C   1 
ATOM   9293  O  O   . ASN F  1 72  ? -25.063 10.039  40.230 1.00 66.26  ? 63  ASN F O   1 
ATOM   9294  C  CB  . ASN F  1 72  ? -27.016 11.218  38.067 1.00 79.65  ? 63  ASN F CB  1 
ATOM   9295  C  CG  . ASN F  1 72  ? -28.438 11.746  38.016 1.00 88.47  ? 63  ASN F CG  1 
ATOM   9296  O  OD1 . ASN F  1 72  ? -28.989 12.171  39.038 1.00 90.53  ? 63  ASN F OD1 1 
ATOM   9297  N  ND2 . ASN F  1 72  ? -29.041 11.720  36.829 1.00 75.48  ? 63  ASN F ND2 1 
ATOM   9298  N  N   . SER F  1 73  ? -23.821 11.409  38.952 1.00 71.07  ? 64  SER F N   1 
ATOM   9299  C  CA  . SER F  1 73  ? -22.605 10.620  39.121 1.00 68.53  ? 64  SER F CA  1 
ATOM   9300  C  C   . SER F  1 73  ? -21.975 10.682  40.523 1.00 67.95  ? 64  SER F C   1 
ATOM   9301  O  O   . SER F  1 73  ? -21.318 9.721   40.937 1.00 63.99  ? 64  SER F O   1 
ATOM   9302  C  CB  . SER F  1 73  ? -21.581 10.899  38.006 1.00 63.22  ? 64  SER F CB  1 
ATOM   9303  O  OG  . SER F  1 73  ? -21.470 12.280  37.740 1.00 72.64  ? 64  SER F OG  1 
ATOM   9304  N  N   . LEU F  1 74  ? -22.155 11.782  41.259 1.00 68.38  ? 65  LEU F N   1 
ATOM   9305  C  CA  . LEU F  1 74  ? -21.795 11.725  42.671 1.00 70.98  ? 65  LEU F CA  1 
ATOM   9306  C  C   . LEU F  1 74  ? -23.085 11.596  43.450 1.00 68.44  ? 65  LEU F C   1 
ATOM   9307  O  O   . LEU F  1 74  ? -23.705 12.579  43.793 1.00 79.92  ? 65  LEU F O   1 
ATOM   9308  C  CB  . LEU F  1 74  ? -21.171 13.062  43.055 1.00 64.51  ? 65  LEU F CB  1 
ATOM   9309  C  CG  . LEU F  1 74  ? -20.145 13.623  42.085 1.00 56.99  ? 65  LEU F CG  1 
ATOM   9310  C  CD1 . LEU F  1 74  ? -20.264 15.125  41.986 1.00 53.59  ? 65  LEU F CD1 1 
ATOM   9311  C  CD2 . LEU F  1 74  ? -18.761 13.204  42.543 1.00 62.56  ? 65  LEU F CD2 1 
ATOM   9312  N  N   . MET F  1 75  ? -23.415 10.387  43.845 1.00 63.46  ? 66  MET F N   1 
ATOM   9313  C  CA  . MET F  1 75  ? -24.665 10.136  44.515 1.00 63.34  ? 66  MET F CA  1 
ATOM   9314  C  C   . MET F  1 75  ? -24.332 8.868   45.241 1.00 69.35  ? 66  MET F C   1 
ATOM   9315  O  O   . MET F  1 75  ? -23.605 8.031   44.703 1.00 62.76  ? 66  MET F O   1 
ATOM   9316  C  CB  . MET F  1 75  ? -25.758 9.886   43.477 1.00 65.43  ? 66  MET F CB  1 
ATOM   9317  C  CG  . MET F  1 75  ? -27.152 10.431  43.799 1.00 73.36  ? 66  MET F CG  1 
ATOM   9318  S  SD  . MET F  1 75  ? -28.134 10.802  42.300 1.00 81.20  ? 66  MET F SD  1 
ATOM   9319  C  CE  . MET F  1 75  ? -29.751 11.164  42.986 1.00 71.09  ? 66  MET F CE  1 
ATOM   9320  N  N   . TRP F  1 76  ? -24.874 8.674   46.428 1.00 65.06  ? 67  TRP F N   1 
ATOM   9321  C  CA  . TRP F  1 76  ? -24.657 7.411   47.084 1.00 57.75  ? 67  TRP F CA  1 
ATOM   9322  C  C   . TRP F  1 76  ? -25.749 7.187   48.077 1.00 65.14  ? 67  TRP F C   1 
ATOM   9323  O  O   . TRP F  1 76  ? -26.442 8.117   48.473 1.00 64.82  ? 67  TRP F O   1 
ATOM   9324  C  CB  . TRP F  1 76  ? -23.281 7.344   47.734 1.00 52.52  ? 67  TRP F CB  1 
ATOM   9325  C  CG  . TRP F  1 76  ? -23.071 8.318   48.825 1.00 63.18  ? 67  TRP F CG  1 
ATOM   9326  C  CD1 . TRP F  1 76  ? -23.247 8.102   50.158 1.00 63.46  ? 67  TRP F CD1 1 
ATOM   9327  C  CD2 . TRP F  1 76  ? -22.622 9.673   48.694 1.00 67.52  ? 67  TRP F CD2 1 
ATOM   9328  N  NE1 . TRP F  1 76  ? -22.941 9.236   50.867 1.00 62.44  ? 67  TRP F NE1 1 
ATOM   9329  C  CE2 . TRP F  1 76  ? -22.557 10.219  49.992 1.00 61.55  ? 67  TRP F CE2 1 
ATOM   9330  C  CE3 . TRP F  1 76  ? -22.272 10.482  47.604 1.00 66.37  ? 67  TRP F CE3 1 
ATOM   9331  C  CZ2 . TRP F  1 76  ? -22.150 11.525  50.233 1.00 60.00  ? 67  TRP F CZ2 1 
ATOM   9332  C  CZ3 . TRP F  1 76  ? -21.873 11.782  47.843 1.00 64.23  ? 67  TRP F CZ3 1 
ATOM   9333  C  CH2 . TRP F  1 76  ? -21.815 12.291  49.147 1.00 64.73  ? 67  TRP F CH2 1 
ATOM   9334  N  N   . ASP F  1 77  ? -25.923 5.927   48.440 1.00 74.27  ? 68  ASP F N   1 
ATOM   9335  C  CA  . ASP F  1 77  ? -26.854 5.553   49.482 1.00 80.60  ? 68  ASP F CA  1 
ATOM   9336  C  C   . ASP F  1 77  ? -26.064 5.633   50.785 1.00 77.59  ? 68  ASP F C   1 
ATOM   9337  O  O   . ASP F  1 77  ? -25.140 4.843   51.003 1.00 78.27  ? 68  ASP F O   1 
ATOM   9338  C  CB  . ASP F  1 77  ? -27.362 4.132   49.211 1.00 86.93  ? 68  ASP F CB  1 
ATOM   9339  C  CG  . ASP F  1 77  ? -28.362 3.648   50.246 1.00 90.87  ? 68  ASP F CG  1 
ATOM   9340  O  OD1 . ASP F  1 77  ? -28.867 4.485   51.033 1.00 87.97  ? 68  ASP F OD1 1 
ATOM   9341  O  OD2 . ASP F  1 77  ? -28.640 2.422   50.257 1.00 90.10  ? 68  ASP F OD2 1 
ATOM   9342  N  N   . PRO F  1 78  ? -26.393 6.614   51.641 1.00 74.75  ? 69  PRO F N   1 
ATOM   9343  C  CA  . PRO F  1 78  ? -25.636 6.757   52.887 1.00 74.42  ? 69  PRO F CA  1 
ATOM   9344  C  C   . PRO F  1 78  ? -25.561 5.444   53.661 1.00 79.33  ? 69  PRO F C   1 
ATOM   9345  O  O   . PRO F  1 78  ? -24.569 5.216   54.359 1.00 75.37  ? 69  PRO F O   1 
ATOM   9346  C  CB  . PRO F  1 78  ? -26.440 7.806   53.664 1.00 71.70  ? 69  PRO F CB  1 
ATOM   9347  C  CG  . PRO F  1 78  ? -27.065 8.646   52.610 1.00 68.73  ? 69  PRO F CG  1 
ATOM   9348  C  CD  . PRO F  1 78  ? -27.365 7.707   51.455 1.00 75.34  ? 69  PRO F CD  1 
ATOM   9349  N  N   . ASN F  1 79  ? -26.580 4.594   53.516 1.00 82.45  ? 70  ASN F N   1 
ATOM   9350  C  CA  . ASN F  1 79  ? -26.665 3.331   54.258 1.00 85.72  ? 70  ASN F CA  1 
ATOM   9351  C  C   . ASN F  1 79  ? -25.485 2.399   54.029 1.00 77.38  ? 70  ASN F C   1 
ATOM   9352  O  O   . ASN F  1 79  ? -25.019 1.732   54.951 1.00 68.81  ? 70  ASN F O   1 
ATOM   9353  C  CB  . ASN F  1 79  ? -27.971 2.602   53.931 1.00 89.16  ? 70  ASN F CB  1 
ATOM   9354  C  CG  . ASN F  1 79  ? -29.169 3.212   54.633 1.00 99.97  ? 70  ASN F CG  1 
ATOM   9355  O  OD1 . ASN F  1 79  ? -29.193 3.310   55.860 1.00 89.69  ? 70  ASN F OD1 1 
ATOM   9356  N  ND2 . ASN F  1 79  ? -30.163 3.643   53.856 1.00 100.10 ? 70  ASN F ND2 1 
ATOM   9357  N  N   . GLU F  1 80  ? -25.001 2.360   52.792 1.00 78.06  ? 71  GLU F N   1 
ATOM   9358  C  CA  . GLU F  1 80  ? -23.922 1.453   52.419 1.00 77.25  ? 71  GLU F CA  1 
ATOM   9359  C  C   . GLU F  1 80  ? -22.576 1.953   52.931 1.00 72.40  ? 71  GLU F C   1 
ATOM   9360  O  O   . GLU F  1 80  ? -21.570 1.249   52.849 1.00 67.95  ? 71  GLU F O   1 
ATOM   9361  C  CB  . GLU F  1 80  ? -23.874 1.275   50.901 1.00 76.78  ? 71  GLU F CB  1 
ATOM   9362  C  CG  . GLU F  1 80  ? -25.235 1.072   50.256 1.00 86.76  ? 71  GLU F CG  1 
ATOM   9363  C  CD  . GLU F  1 80  ? -25.144 0.387   48.907 1.00 97.77  ? 71  GLU F CD  1 
ATOM   9364  O  OE1 . GLU F  1 80  ? -24.021 0.030   48.494 1.00 93.69  ? 71  GLU F OE1 1 
ATOM   9365  O  OE2 . GLU F  1 80  ? -26.196 0.205   48.259 1.00 103.35 ? 71  GLU F OE2 1 
ATOM   9366  N  N   . TYR F  1 81  ? -22.564 3.173   53.459 1.00 78.88  ? 72  TYR F N   1 
ATOM   9367  C  CA  . TYR F  1 81  ? -21.342 3.967   53.520 1.00 73.16  ? 72  TYR F CA  1 
ATOM   9368  C  C   . TYR F  1 81  ? -21.196 4.654   54.874 1.00 75.75  ? 72  TYR F C   1 
ATOM   9369  O  O   . TYR F  1 81  ? -20.505 5.665   54.996 1.00 69.80  ? 72  TYR F O   1 
ATOM   9370  C  CB  . TYR F  1 81  ? -21.322 5.007   52.398 1.00 60.14  ? 72  TYR F CB  1 
ATOM   9371  C  CG  . TYR F  1 81  ? -20.811 4.475   51.079 1.00 59.29  ? 72  TYR F CG  1 
ATOM   9372  C  CD1 . TYR F  1 81  ? -19.470 4.158   50.908 1.00 55.39  ? 72  TYR F CD1 1 
ATOM   9373  C  CD2 . TYR F  1 81  ? -21.670 4.290   50.004 1.00 65.48  ? 72  TYR F CD2 1 
ATOM   9374  C  CE1 . TYR F  1 81  ? -18.999 3.672   49.704 1.00 61.74  ? 72  TYR F CE1 1 
ATOM   9375  C  CE2 . TYR F  1 81  ? -21.207 3.804   48.796 1.00 63.18  ? 72  TYR F CE2 1 
ATOM   9376  C  CZ  . TYR F  1 81  ? -19.871 3.496   48.651 1.00 65.43  ? 72  TYR F CZ  1 
ATOM   9377  O  OH  . TYR F  1 81  ? -19.406 3.012   47.450 1.00 56.40  ? 72  TYR F OH  1 
ATOM   9378  N  N   . GLY F  1 82  ? -21.849 4.098   55.888 1.00 75.16  ? 73  GLY F N   1 
ATOM   9379  C  CA  . GLY F  1 82  ? -21.639 4.528   57.258 1.00 61.27  ? 73  GLY F CA  1 
ATOM   9380  C  C   . GLY F  1 82  ? -22.586 5.639   57.668 1.00 71.84  ? 73  GLY F C   1 
ATOM   9381  O  O   . GLY F  1 82  ? -22.402 6.273   58.706 1.00 66.70  ? 73  GLY F O   1 
ATOM   9382  N  N   . ASN F  1 83  ? -23.604 5.874   56.847 1.00 73.38  ? 74  ASN F N   1 
ATOM   9383  C  CA  . ASN F  1 83  ? -24.478 7.025   57.021 1.00 77.43  ? 74  ASN F CA  1 
ATOM   9384  C  C   . ASN F  1 83  ? -23.713 8.338   56.887 1.00 75.49  ? 74  ASN F C   1 
ATOM   9385  O  O   . ASN F  1 83  ? -23.995 9.310   57.579 1.00 81.34  ? 74  ASN F O   1 
ATOM   9386  C  CB  . ASN F  1 83  ? -25.267 6.941   58.337 1.00 83.78  ? 74  ASN F CB  1 
ATOM   9387  C  CG  . ASN F  1 83  ? -26.382 5.886   58.286 1.00 99.67  ? 74  ASN F CG  1 
ATOM   9388  O  OD1 . ASN F  1 83  ? -27.313 5.981   57.470 1.00 86.90  ? 74  ASN F OD1 1 
ATOM   9389  N  ND2 . ASN F  1 83  ? -26.293 4.877   59.164 1.00 94.92  ? 74  ASN F ND2 1 
ATOM   9390  N  N   . ILE F  1 84  ? -22.740 8.351   55.980 1.00 71.77  ? 75  ILE F N   1 
ATOM   9391  C  CA  . ILE F  1 84  ? -22.071 9.579   55.603 1.00 64.20  ? 75  ILE F CA  1 
ATOM   9392  C  C   . ILE F  1 84  ? -22.995 10.279  54.613 1.00 67.98  ? 75  ILE F C   1 
ATOM   9393  O  O   . ILE F  1 84  ? -23.274 9.750   53.543 1.00 62.51  ? 75  ILE F O   1 
ATOM   9394  C  CB  . ILE F  1 84  ? -20.755 9.248   54.892 1.00 55.72  ? 75  ILE F CB  1 
ATOM   9395  C  CG1 . ILE F  1 84  ? -19.782 8.588   55.863 1.00 52.98  ? 75  ILE F CG1 1 
ATOM   9396  C  CG2 . ILE F  1 84  ? -20.145 10.481  54.280 1.00 52.31  ? 75  ILE F CG2 1 
ATOM   9397  C  CD1 . ILE F  1 84  ? -18.422 8.365   55.279 1.00 54.30  ? 75  ILE F CD1 1 
ATOM   9398  N  N   . THR F  1 85  ? -23.492 11.457  54.981 1.00 72.69  ? 76  THR F N   1 
ATOM   9399  C  CA  . THR F  1 85  ? -24.406 12.191  54.113 1.00 68.45  ? 76  THR F CA  1 
ATOM   9400  C  C   . THR F  1 85  ? -23.719 13.247  53.234 1.00 72.24  ? 76  THR F C   1 
ATOM   9401  O  O   . THR F  1 85  ? -24.335 13.795  52.308 1.00 67.56  ? 76  THR F O   1 
ATOM   9402  C  CB  . THR F  1 85  ? -25.558 12.833  54.917 1.00 73.83  ? 76  THR F CB  1 
ATOM   9403  O  OG1 . THR F  1 85  ? -25.072 13.976  55.625 1.00 75.12  ? 76  THR F OG1 1 
ATOM   9404  C  CG2 . THR F  1 85  ? -26.145 11.844  55.908 1.00 76.51  ? 76  THR F CG2 1 
ATOM   9405  N  N   . ASP F  1 86  ? -22.448 13.527  53.518 1.00 66.59  ? 77  ASP F N   1 
ATOM   9406  C  CA  . ASP F  1 86  ? -21.680 14.422  52.664 1.00 64.21  ? 77  ASP F CA  1 
ATOM   9407  C  C   . ASP F  1 86  ? -20.187 14.385  52.961 1.00 60.67  ? 77  ASP F C   1 
ATOM   9408  O  O   . ASP F  1 86  ? -19.760 13.765  53.933 1.00 52.88  ? 77  ASP F O   1 
ATOM   9409  C  CB  . ASP F  1 86  ? -22.189 15.837  52.855 1.00 64.54  ? 77  ASP F CB  1 
ATOM   9410  C  CG  . ASP F  1 86  ? -22.138 16.268  54.293 1.00 69.34  ? 77  ASP F CG  1 
ATOM   9411  O  OD1 . ASP F  1 86  ? -21.175 15.863  54.974 1.00 71.31  ? 77  ASP F OD1 1 
ATOM   9412  O  OD2 . ASP F  1 86  ? -23.054 16.995  54.742 1.00 72.00  ? 77  ASP F OD2 1 
ATOM   9413  N  N   . PHE F  1 87  ? -19.404 15.086  52.139 1.00 56.57  ? 78  PHE F N   1 
ATOM   9414  C  CA  . PHE F  1 87  ? -17.951 15.127  52.305 1.00 56.11  ? 78  PHE F CA  1 
ATOM   9415  C  C   . PHE F  1 87  ? -17.300 16.324  51.626 1.00 51.71  ? 78  PHE F C   1 
ATOM   9416  O  O   . PHE F  1 87  ? -17.871 16.901  50.709 1.00 55.67  ? 78  PHE F O   1 
ATOM   9417  C  CB  . PHE F  1 87  ? -17.286 13.808  51.858 1.00 58.17  ? 78  PHE F CB  1 
ATOM   9418  C  CG  . PHE F  1 87  ? -17.341 13.549  50.374 1.00 58.97  ? 78  PHE F CG  1 
ATOM   9419  C  CD1 . PHE F  1 87  ? -16.382 14.075  49.526 1.00 59.99  ? 78  PHE F CD1 1 
ATOM   9420  C  CD2 . PHE F  1 87  ? -18.333 12.748  49.831 1.00 60.08  ? 78  PHE F CD2 1 
ATOM   9421  C  CE1 . PHE F  1 87  ? -16.427 13.831  48.163 1.00 58.02  ? 78  PHE F CE1 1 
ATOM   9422  C  CE2 . PHE F  1 87  ? -18.378 12.499  48.462 1.00 61.31  ? 78  PHE F CE2 1 
ATOM   9423  C  CZ  . PHE F  1 87  ? -17.421 13.042  47.632 1.00 60.35  ? 78  PHE F CZ  1 
ATOM   9424  N  N   . ARG F  1 88  ? -16.092 16.667  52.068 1.00 53.07  ? 79  ARG F N   1 
ATOM   9425  C  CA  . ARG F  1 88  ? -15.312 17.759  51.487 1.00 55.83  ? 79  ARG F CA  1 
ATOM   9426  C  C   . ARG F  1 88  ? -14.161 17.215  50.652 1.00 56.22  ? 79  ARG F C   1 
ATOM   9427  O  O   . ARG F  1 88  ? -13.578 16.200  50.998 1.00 58.89  ? 79  ARG F O   1 
ATOM   9428  C  CB  . ARG F  1 88  ? -14.754 18.669  52.584 1.00 50.47  ? 79  ARG F CB  1 
ATOM   9429  C  CG  . ARG F  1 88  ? -15.775 19.579  53.248 1.00 55.76  ? 79  ARG F CG  1 
ATOM   9430  C  CD  . ARG F  1 88  ? -16.454 18.916  54.427 1.00 59.10  ? 79  ARG F CD  1 
ATOM   9431  N  NE  . ARG F  1 88  ? -17.262 19.849  55.207 1.00 62.00  ? 79  ARG F NE  1 
ATOM   9432  C  CZ  . ARG F  1 88  ? -18.087 19.487  56.187 1.00 72.18  ? 79  ARG F CZ  1 
ATOM   9433  N  NH1 . ARG F  1 88  ? -18.790 20.409  56.848 1.00 70.62  ? 79  ARG F NH1 1 
ATOM   9434  N  NH2 . ARG F  1 88  ? -18.216 18.201  56.503 1.00 70.83  ? 79  ARG F NH2 1 
ATOM   9435  N  N   . THR F  1 89  ? -13.840 17.886  49.550 1.00 54.50  ? 80  THR F N   1 
ATOM   9436  C  CA  . THR F  1 89  ? -12.697 17.494  48.726 1.00 55.31  ? 80  THR F CA  1 
ATOM   9437  C  C   . THR F  1 89  ? -12.081 18.665  48.018 1.00 57.68  ? 80  THR F C   1 
ATOM   9438  O  O   . THR F  1 89  ? -12.720 19.706  47.838 1.00 52.11  ? 80  THR F O   1 
ATOM   9439  C  CB  . THR F  1 89  ? -13.077 16.525  47.588 1.00 66.50  ? 80  THR F CB  1 
ATOM   9440  O  OG1 . THR F  1 89  ? -14.170 17.060  46.809 1.00 62.93  ? 80  THR F OG1 1 
ATOM   9441  C  CG2 . THR F  1 89  ? -13.419 15.152  48.134 1.00 74.85  ? 80  THR F CG2 1 
ATOM   9442  N  N   . SER F  1 90  ? -10.845 18.466  47.572 1.00 58.08  ? 81  SER F N   1 
ATOM   9443  C  CA  . SER F  1 90  ? -10.193 19.445  46.727 1.00 62.81  ? 81  SER F CA  1 
ATOM   9444  C  C   . SER F  1 90  ? -11.007 19.619  45.465 1.00 64.14  ? 81  SER F C   1 
ATOM   9445  O  O   . SER F  1 90  ? -11.533 18.643  44.934 1.00 63.78  ? 81  SER F O   1 
ATOM   9446  C  CB  . SER F  1 90  ? -8.803  18.976  46.343 1.00 67.93  ? 81  SER F CB  1 
ATOM   9447  O  OG  . SER F  1 90  ? -8.231  19.886  45.419 1.00 70.84  ? 81  SER F OG  1 
ATOM   9448  N  N   . ALA F  1 91  ? -11.107 20.849  44.972 1.00 59.65  ? 82  ALA F N   1 
ATOM   9449  C  CA  . ALA F  1 91  ? -11.895 21.087  43.770 1.00 58.21  ? 82  ALA F CA  1 
ATOM   9450  C  C   . ALA F  1 91  ? -11.238 20.480  42.544 1.00 62.09  ? 82  ALA F C   1 
ATOM   9451  O  O   . ALA F  1 91  ? -11.899 20.274  41.532 1.00 71.15  ? 82  ALA F O   1 
ATOM   9452  C  CB  . ALA F  1 91  ? -12.152 22.568  43.561 1.00 56.43  ? 82  ALA F CB  1 
ATOM   9453  N  N   . ALA F  1 92  ? -9.943  20.193  42.624 1.00 60.53  ? 83  ALA F N   1 
ATOM   9454  C  CA  . ALA F  1 92  ? -9.257  19.550  41.507 1.00 65.22  ? 83  ALA F CA  1 
ATOM   9455  C  C   . ALA F  1 92  ? -9.749  18.117  41.220 1.00 63.77  ? 83  ALA F C   1 
ATOM   9456  O  O   . ALA F  1 92  ? -9.569  17.610  40.113 1.00 70.08  ? 83  ALA F O   1 
ATOM   9457  C  CB  . ALA F  1 92  ? -7.754  19.579  41.712 1.00 61.78  ? 83  ALA F CB  1 
ATOM   9458  N  N   . ASP F  1 93  ? -10.382 17.487  42.206 1.00 55.55  ? 84  ASP F N   1 
ATOM   9459  C  CA  . ASP F  1 93  ? -10.846 16.105  42.086 1.00 64.01  ? 84  ASP F CA  1 
ATOM   9460  C  C   . ASP F  1 93  ? -12.209 15.991  41.455 1.00 64.69  ? 84  ASP F C   1 
ATOM   9461  O  O   . ASP F  1 93  ? -12.660 14.896  41.127 1.00 69.04  ? 84  ASP F O   1 
ATOM   9462  C  CB  . ASP F  1 93  ? -10.935 15.435  43.453 1.00 68.67  ? 84  ASP F CB  1 
ATOM   9463  C  CG  . ASP F  1 93  ? -9.601  15.344  44.138 1.00 79.42  ? 84  ASP F CG  1 
ATOM   9464  O  OD1 . ASP F  1 93  ? -8.586  15.758  43.520 1.00 77.51  ? 84  ASP F OD1 1 
ATOM   9465  O  OD2 . ASP F  1 93  ? -9.575  14.850  45.290 1.00 80.76  ? 84  ASP F OD2 1 
ATOM   9466  N  N   . ILE F  1 94  ? -12.894 17.113  41.322 1.00 60.38  ? 85  ILE F N   1 
ATOM   9467  C  CA  . ILE F  1 94  ? -14.226 17.072  40.754 1.00 57.87  ? 85  ILE F CA  1 
ATOM   9468  C  C   . ILE F  1 94  ? -14.315 17.992  39.565 1.00 57.04  ? 85  ILE F C   1 
ATOM   9469  O  O   . ILE F  1 94  ? -13.549 18.945  39.421 1.00 58.41  ? 85  ILE F O   1 
ATOM   9470  C  CB  . ILE F  1 94  ? -15.331 17.422  41.778 1.00 52.04  ? 85  ILE F CB  1 
ATOM   9471  C  CG1 . ILE F  1 94  ? -15.015 18.741  42.498 1.00 54.09  ? 85  ILE F CG1 1 
ATOM   9472  C  CG2 . ILE F  1 94  ? -15.516 16.279  42.763 1.00 57.39  ? 85  ILE F CG2 1 
ATOM   9473  C  CD1 . ILE F  1 94  ? -16.195 19.341  43.210 1.00 45.02  ? 85  ILE F CD1 1 
ATOM   9474  N  N   . TRP F  1 95  ? -15.249 17.687  38.687 1.00 54.96  ? 86  TRP F N   1 
ATOM   9475  C  CA  . TRP F  1 95  ? -15.520 18.610  37.628 1.00 59.51  ? 86  TRP F CA  1 
ATOM   9476  C  C   . TRP F  1 95  ? -16.080 19.879  38.254 1.00 57.80  ? 86  TRP F C   1 
ATOM   9477  O  O   . TRP F  1 95  ? -16.865 19.836  39.204 1.00 58.09  ? 86  TRP F O   1 
ATOM   9478  C  CB  . TRP F  1 95  ? -16.475 18.006  36.610 1.00 57.28  ? 86  TRP F CB  1 
ATOM   9479  C  CG  . TRP F  1 95  ? -16.741 18.911  35.471 1.00 57.99  ? 86  TRP F CG  1 
ATOM   9480  C  CD1 . TRP F  1 95  ? -16.067 18.972  34.287 1.00 62.50  ? 86  TRP F CD1 1 
ATOM   9481  C  CD2 . TRP F  1 95  ? -17.763 19.895  35.403 1.00 57.53  ? 86  TRP F CD2 1 
ATOM   9482  N  NE1 . TRP F  1 95  ? -16.618 19.937  33.481 1.00 57.68  ? 86  TRP F NE1 1 
ATOM   9483  C  CE2 . TRP F  1 95  ? -17.663 20.519  34.146 1.00 56.20  ? 86  TRP F CE2 1 
ATOM   9484  C  CE3 . TRP F  1 95  ? -18.759 20.310  36.288 1.00 54.01  ? 86  TRP F CE3 1 
ATOM   9485  C  CZ2 . TRP F  1 95  ? -18.516 21.536  33.752 1.00 55.87  ? 86  TRP F CZ2 1 
ATOM   9486  C  CZ3 . TRP F  1 95  ? -19.606 21.311  35.895 1.00 58.09  ? 86  TRP F CZ3 1 
ATOM   9487  C  CH2 . TRP F  1 95  ? -19.484 21.916  34.634 1.00 54.31  ? 86  TRP F CH2 1 
ATOM   9488  N  N   . THR F  1 96  ? -15.612 21.006  37.743 1.00 55.07  ? 87  THR F N   1 
ATOM   9489  C  CA  . THR F  1 96  ? -16.124 22.301  38.127 1.00 57.19  ? 87  THR F CA  1 
ATOM   9490  C  C   . THR F  1 96  ? -16.442 23.073  36.849 1.00 57.10  ? 87  THR F C   1 
ATOM   9491  O  O   . THR F  1 96  ? -15.734 22.953  35.850 1.00 52.94  ? 87  THR F O   1 
ATOM   9492  C  CB  . THR F  1 96  ? -15.120 23.067  39.017 1.00 55.52  ? 87  THR F CB  1 
ATOM   9493  O  OG1 . THR F  1 96  ? -13.794 22.901  38.502 1.00 60.65  ? 87  THR F OG1 1 
ATOM   9494  C  CG2 . THR F  1 96  ? -15.170 22.536  40.453 1.00 58.20  ? 87  THR F CG2 1 
ATOM   9495  N  N   . PRO F  1 97  ? -17.525 23.853  36.875 1.00 55.72  ? 88  PRO F N   1 
ATOM   9496  C  CA  . PRO F  1 97  ? -18.002 24.632  35.722 1.00 53.09  ? 88  PRO F CA  1 
ATOM   9497  C  C   . PRO F  1 97  ? -17.037 25.750  35.364 1.00 53.29  ? 88  PRO F C   1 
ATOM   9498  O  O   . PRO F  1 97  ? -16.391 26.277  36.262 1.00 53.75  ? 88  PRO F O   1 
ATOM   9499  C  CB  . PRO F  1 97  ? -19.320 25.222  36.226 1.00 55.72  ? 88  PRO F CB  1 
ATOM   9500  C  CG  . PRO F  1 97  ? -19.164 25.240  37.736 1.00 59.53  ? 88  PRO F CG  1 
ATOM   9501  C  CD  . PRO F  1 97  ? -18.372 24.025  38.067 1.00 51.24  ? 88  PRO F CD  1 
ATOM   9502  N  N   . ASP F  1 98  ? -16.938 26.148  34.099 1.00 55.24  ? 89  ASP F N   1 
ATOM   9503  C  CA  . ASP F  1 98  ? -15.980 27.203  33.848 1.00 60.13  ? 89  ASP F CA  1 
ATOM   9504  C  C   . ASP F  1 98  ? -16.754 28.494  33.751 1.00 62.25  ? 89  ASP F C   1 
ATOM   9505  O  O   . ASP F  1 98  ? -17.216 28.887  32.686 1.00 64.86  ? 89  ASP F O   1 
ATOM   9506  C  CB  . ASP F  1 98  ? -15.258 26.936  32.520 1.00 61.08  ? 89  ASP F CB  1 
ATOM   9507  C  CG  . ASP F  1 98  ? -16.211 26.917  31.310 1.00 60.89  ? 89  ASP F CG  1 
ATOM   9508  O  OD1 . ASP F  1 98  ? -17.411 26.627  31.501 1.00 57.25  ? 89  ASP F OD1 1 
ATOM   9509  O  OD2 . ASP F  1 98  ? -15.753 27.189  30.173 1.00 55.10  ? 89  ASP F OD2 1 
ATOM   9510  N  N   . ILE F  1 99  ? -16.719 29.252  34.832 1.00 54.95  ? 90  ILE F N   1 
ATOM   9511  C  CA  . ILE F  1 99  ? -17.562 30.419  34.936 1.00 55.70  ? 90  ILE F CA  1 
ATOM   9512  C  C   . ILE F  1 99  ? -16.581 31.529  35.108 1.00 56.52  ? 90  ILE F C   1 
ATOM   9513  O  O   . ILE F  1 99  ? -15.658 31.407  35.905 1.00 59.96  ? 90  ILE F O   1 
ATOM   9514  C  CB  . ILE F  1 99  ? -18.485 30.359  36.150 1.00 56.81  ? 90  ILE F CB  1 
ATOM   9515  C  CG1 . ILE F  1 99  ? -19.335 29.086  36.115 1.00 56.43  ? 90  ILE F CG1 1 
ATOM   9516  C  CG2 . ILE F  1 99  ? -19.362 31.601  36.201 1.00 46.65  ? 90  ILE F CG2 1 
ATOM   9517  C  CD1 . ILE F  1 99  ? -20.550 29.196  35.238 1.00 52.42  ? 90  ILE F CD1 1 
ATOM   9518  N  N   . THR F  1 100 ? -16.760 32.593  34.339 1.00 55.49  ? 91  THR F N   1 
ATOM   9519  C  CA  . THR F  1 100 ? -15.791 33.661  34.291 1.00 50.77  ? 91  THR F CA  1 
ATOM   9520  C  C   . THR F  1 100 ? -16.523 34.970  34.397 1.00 57.37  ? 91  THR F C   1 
ATOM   9521  O  O   . THR F  1 100 ? -17.714 35.051  34.098 1.00 60.76  ? 91  THR F O   1 
ATOM   9522  C  CB  . THR F  1 100 ? -15.046 33.650  32.953 1.00 57.04  ? 91  THR F CB  1 
ATOM   9523  O  OG1 . THR F  1 100 ? -14.757 32.300  32.586 1.00 62.84  ? 91  THR F OG1 1 
ATOM   9524  C  CG2 . THR F  1 100 ? -13.751 34.443  33.041 1.00 55.47  ? 91  THR F CG2 1 
ATOM   9525  N  N   . ALA F  1 101 ? -15.802 35.992  34.836 1.00 53.57  ? 92  ALA F N   1 
ATOM   9526  C  CA  . ALA F  1 101 ? -16.238 37.371  34.682 1.00 59.53  ? 92  ALA F CA  1 
ATOM   9527  C  C   . ALA F  1 101 ? -15.828 37.856  33.290 1.00 58.04  ? 92  ALA F C   1 
ATOM   9528  O  O   . ALA F  1 101 ? -14.657 37.788  32.926 1.00 63.26  ? 92  ALA F O   1 
ATOM   9529  C  CB  . ALA F  1 101 ? -15.599 38.233  35.747 1.00 61.34  ? 92  ALA F CB  1 
ATOM   9530  N  N   . TYR F  1 102 ? -16.784 38.342  32.509 1.00 60.13  ? 93  TYR F N   1 
ATOM   9531  C  CA  . TYR F  1 102 ? -16.495 38.721  31.128 1.00 61.82  ? 93  TYR F CA  1 
ATOM   9532  C  C   . TYR F  1 102 ? -15.629 39.980  31.008 1.00 63.78  ? 93  TYR F C   1 
ATOM   9533  O  O   . TYR F  1 102 ? -14.850 40.113  30.065 1.00 59.11  ? 93  TYR F O   1 
ATOM   9534  C  CB  . TYR F  1 102 ? -17.793 38.841  30.337 1.00 58.54  ? 93  TYR F CB  1 
ATOM   9535  C  CG  . TYR F  1 102 ? -18.476 37.505  30.166 1.00 64.26  ? 93  TYR F CG  1 
ATOM   9536  C  CD1 . TYR F  1 102 ? -17.734 36.338  30.086 1.00 66.79  ? 93  TYR F CD1 1 
ATOM   9537  C  CD2 . TYR F  1 102 ? -19.856 37.403  30.102 1.00 67.85  ? 93  TYR F CD2 1 
ATOM   9538  C  CE1 . TYR F  1 102 ? -18.348 35.107  29.939 1.00 64.77  ? 93  TYR F CE1 1 
ATOM   9539  C  CE2 . TYR F  1 102 ? -20.477 36.173  29.958 1.00 62.13  ? 93  TYR F CE2 1 
ATOM   9540  C  CZ  . TYR F  1 102 ? -19.716 35.032  29.874 1.00 60.62  ? 93  TYR F CZ  1 
ATOM   9541  O  OH  . TYR F  1 102 ? -20.317 33.808  29.720 1.00 58.01  ? 93  TYR F OH  1 
ATOM   9542  N  N   . SER F  1 103 ? -15.747 40.873  31.988 1.00 62.29  ? 94  SER F N   1 
ATOM   9543  C  CA  . SER F  1 103 ? -15.078 42.176  31.985 1.00 56.43  ? 94  SER F CA  1 
ATOM   9544  C  C   . SER F  1 103 ? -13.727 42.228  32.711 1.00 60.05  ? 94  SER F C   1 
ATOM   9545  O  O   . SER F  1 103 ? -13.192 43.313  32.910 1.00 61.66  ? 94  SER F O   1 
ATOM   9546  C  CB  . SER F  1 103 ? -16.001 43.242  32.575 1.00 62.95  ? 94  SER F CB  1 
ATOM   9547  O  OG  . SER F  1 103 ? -17.354 42.843  32.468 1.00 72.47  ? 94  SER F OG  1 
ATOM   9548  N  N   . SER F  1 104 ? -13.207 41.090  33.170 1.00 52.58  ? 95  SER F N   1 
ATOM   9549  C  CA  . SER F  1 104 ? -11.965 41.096  33.952 1.00 48.16  ? 95  SER F CA  1 
ATOM   9550  C  C   . SER F  1 104 ? -10.741 41.693  33.222 1.00 53.09  ? 95  SER F C   1 
ATOM   9551  O  O   . SER F  1 104 ? -10.538 41.459  32.034 1.00 55.17  ? 95  SER F O   1 
ATOM   9552  C  CB  . SER F  1 104 ? -11.691 39.720  34.578 1.00 48.81  ? 95  SER F CB  1 
ATOM   9553  O  OG  . SER F  1 104 ? -10.923 38.858  33.770 1.00 51.93  ? 95  SER F OG  1 
ATOM   9554  N  N   . THR F  1 105 ? -10.017 42.579  33.907 1.00 55.61  ? 96  THR F N   1 
ATOM   9555  C  CA  . THR F  1 105 ? -8.766  43.165  33.398 1.00 51.35  ? 96  THR F CA  1 
ATOM   9556  C  C   . THR F  1 105 ? -7.463  42.557  33.941 1.00 47.17  ? 96  THR F C   1 
ATOM   9557  O  O   . THR F  1 105 ? -6.375  42.937  33.521 1.00 46.55  ? 96  THR F O   1 
ATOM   9558  C  CB  . THR F  1 105 ? -8.742  44.674  33.649 1.00 50.77  ? 96  THR F CB  1 
ATOM   9559  O  OG1 . THR F  1 105 ? -8.881  44.911  35.054 1.00 56.40  ? 96  THR F OG1 1 
ATOM   9560  C  CG2 . THR F  1 105 ? -9.892  45.337  32.928 1.00 48.70  ? 96  THR F CG2 1 
ATOM   9561  N  N   A ARG F  1 106 ? -7.592  41.636  34.890 0.50 48.02  ? 97  ARG F N   1 
ATOM   9562  N  N   B ARG F  1 106 ? -7.593  41.629  34.882 0.50 47.83  ? 97  ARG F N   1 
ATOM   9563  C  CA  A ARG F  1 106 ? -6.455  40.910  35.456 0.50 48.06  ? 97  ARG F CA  1 
ATOM   9564  C  CA  B ARG F  1 106 ? -6.453  40.922  35.462 0.50 48.07  ? 97  ARG F CA  1 
ATOM   9565  C  C   A ARG F  1 106 ? -6.918  39.503  35.750 0.50 47.88  ? 97  ARG F C   1 
ATOM   9566  C  C   B ARG F  1 106 ? -6.913  39.517  35.795 0.50 48.22  ? 97  ARG F C   1 
ATOM   9567  O  O   A ARG F  1 106 ? -8.117  39.258  35.872 0.50 48.93  ? 97  ARG F O   1 
ATOM   9568  O  O   B ARG F  1 106 ? -8.107  39.288  35.983 0.50 48.92  ? 97  ARG F O   1 
ATOM   9569  C  CB  A ARG F  1 106 ? -5.975  41.531  36.771 0.50 49.31  ? 97  ARG F CB  1 
ATOM   9570  C  CB  B ARG F  1 106 ? -5.968  41.606  36.745 0.50 49.49  ? 97  ARG F CB  1 
ATOM   9571  C  CG  A ARG F  1 106 ? -5.402  42.929  36.678 0.50 54.15  ? 97  ARG F CG  1 
ATOM   9572  C  CG  B ARG F  1 106 ? -5.278  42.952  36.550 0.50 54.15  ? 97  ARG F CG  1 
ATOM   9573  C  CD  A ARG F  1 106 ? -4.004  42.955  36.084 0.50 51.62  ? 97  ARG F CD  1 
ATOM   9574  C  CD  B ARG F  1 106 ? -5.401  43.816  37.802 0.50 53.54  ? 97  ARG F CD  1 
ATOM   9575  N  NE  A ARG F  1 106 ? -3.362  44.232  36.379 0.50 53.26  ? 97  ARG F NE  1 
ATOM   9576  N  NE  B ARG F  1 106 ? -4.549  45.002  37.759 0.50 54.16  ? 97  ARG F NE  1 
ATOM   9577  C  CZ  A ARG F  1 106 ? -2.209  44.626  35.859 0.50 51.02  ? 97  ARG F CZ  1 
ATOM   9578  C  CZ  B ARG F  1 106 ? -4.882  46.174  38.287 0.50 56.42  ? 97  ARG F CZ  1 
ATOM   9579  N  NH1 A ARG F  1 106 ? -1.572  43.841  35.003 0.50 49.68  ? 97  ARG F NH1 1 
ATOM   9580  N  NH1 B ARG F  1 106 ? -6.056  46.326  38.881 0.50 57.28  ? 97  ARG F NH1 1 
ATOM   9581  N  NH2 A ARG F  1 106 ? -1.699  45.803  36.196 0.50 42.66  ? 97  ARG F NH2 1 
ATOM   9582  N  NH2 B ARG F  1 106 ? -4.047  47.198  38.215 0.50 57.36  ? 97  ARG F NH2 1 
ATOM   9583  N  N   . PRO F  1 107 ? -5.971  38.568  35.877 1.00 48.26  ? 98  PRO F N   1 
ATOM   9584  C  CA  . PRO F  1 107 ? -6.339  37.225  36.316 1.00 42.44  ? 98  PRO F CA  1 
ATOM   9585  C  C   . PRO F  1 107 ? -7.032  37.321  37.684 1.00 47.18  ? 98  PRO F C   1 
ATOM   9586  O  O   . PRO F  1 107 ? -6.565  38.060  38.546 1.00 45.95  ? 98  PRO F O   1 
ATOM   9587  C  CB  . PRO F  1 107 ? -4.992  36.526  36.456 1.00 35.23  ? 98  PRO F CB  1 
ATOM   9588  C  CG  . PRO F  1 107 ? -4.048  37.305  35.669 1.00 47.21  ? 98  PRO F CG  1 
ATOM   9589  C  CD  . PRO F  1 107 ? -4.524  38.714  35.660 1.00 48.92  ? 98  PRO F CD  1 
ATOM   9590  N  N   . VAL F  1 108 ? -8.141  36.613  37.873 1.00 49.60  ? 99  VAL F N   1 
ATOM   9591  C  CA  . VAL F  1 108 ? -8.790  36.559  39.174 1.00 46.96  ? 99  VAL F CA  1 
ATOM   9592  C  C   . VAL F  1 108 ? -7.820  35.976  40.192 1.00 52.10  ? 99  VAL F C   1 
ATOM   9593  O  O   . VAL F  1 108 ? -6.955  35.170  39.851 1.00 52.79  ? 99  VAL F O   1 
ATOM   9594  C  CB  . VAL F  1 108 ? -10.064 35.701  39.145 1.00 44.29  ? 99  VAL F CB  1 
ATOM   9595  C  CG1 . VAL F  1 108 ? -10.342 35.137  40.501 1.00 59.02  ? 99  VAL F CG1 1 
ATOM   9596  C  CG2 . VAL F  1 108 ? -11.236 36.519  38.712 1.00 51.31  ? 99  VAL F CG2 1 
ATOM   9597  N  N   . GLN F  1 109 ? -7.947  36.398  41.443 1.00 52.17  ? 100 GLN F N   1 
ATOM   9598  C  CA  . GLN F  1 109 ? -7.107  35.865  42.503 1.00 51.74  ? 100 GLN F CA  1 
ATOM   9599  C  C   . GLN F  1 109 ? -7.930  35.120  43.546 1.00 58.12  ? 100 GLN F C   1 
ATOM   9600  O  O   . GLN F  1 109 ? -8.879  35.671  44.102 1.00 57.24  ? 100 GLN F O   1 
ATOM   9601  C  CB  . GLN F  1 109 ? -6.305  36.991  43.137 1.00 46.00  ? 100 GLN F CB  1 
ATOM   9602  C  CG  . GLN F  1 109 ? -5.410  37.629  42.144 1.00 43.40  ? 100 GLN F CG  1 
ATOM   9603  C  CD  . GLN F  1 109 ? -4.516  38.655  42.741 1.00 49.98  ? 100 GLN F CD  1 
ATOM   9604  O  OE1 . GLN F  1 109 ? -4.845  39.837  42.771 1.00 54.38  ? 100 GLN F OE1 1 
ATOM   9605  N  NE2 . GLN F  1 109 ? -3.358  38.218  43.214 1.00 54.45  ? 100 GLN F NE2 1 
ATOM   9606  N  N   . VAL F  1 110 ? -7.566  33.863  43.798 1.00 56.98  ? 101 VAL F N   1 
ATOM   9607  C  CA  . VAL F  1 110 ? -8.271  33.046  44.787 1.00 57.89  ? 101 VAL F CA  1 
ATOM   9608  C  C   . VAL F  1 110 ? -7.765  33.344  46.192 1.00 52.78  ? 101 VAL F C   1 
ATOM   9609  O  O   . VAL F  1 110 ? -6.580  33.182  46.481 1.00 50.21  ? 101 VAL F O   1 
ATOM   9610  C  CB  . VAL F  1 110 ? -8.124  31.534  44.501 1.00 57.61  ? 101 VAL F CB  1 
ATOM   9611  C  CG1 . VAL F  1 110 ? -9.119  30.754  45.324 1.00 59.09  ? 101 VAL F CG1 1 
ATOM   9612  C  CG2 . VAL F  1 110 ? -8.346  31.252  43.039 1.00 51.83  ? 101 VAL F CG2 1 
ATOM   9613  N  N   . LEU F  1 111 ? -8.681  33.782  47.051 1.00 53.37  ? 102 LEU F N   1 
ATOM   9614  C  CA  . LEU F  1 111 ? -8.359  34.201  48.416 1.00 51.91  ? 102 LEU F CA  1 
ATOM   9615  C  C   . LEU F  1 111 ? -8.568  33.132  49.502 1.00 51.02  ? 102 LEU F C   1 
ATOM   9616  O  O   . LEU F  1 111 ? -8.315  33.394  50.671 1.00 52.11  ? 102 LEU F O   1 
ATOM   9617  C  CB  . LEU F  1 111 ? -9.172  35.446  48.777 1.00 50.15  ? 102 LEU F CB  1 
ATOM   9618  C  CG  . LEU F  1 111 ? -9.020  36.628  47.837 1.00 50.82  ? 102 LEU F CG  1 
ATOM   9619  C  CD1 . LEU F  1 111 ? -9.987  37.721  48.214 1.00 48.28  ? 102 LEU F CD1 1 
ATOM   9620  C  CD2 . LEU F  1 111 ? -7.592  37.106  47.882 1.00 48.49  ? 102 LEU F CD2 1 
ATOM   9621  N  N   . SER F  1 112 ? -9.026  31.950  49.101 1.00 49.68  ? 103 SER F N   1 
ATOM   9622  C  CA  . SER F  1 112 ? -9.521  30.925  50.004 1.00 47.53  ? 103 SER F CA  1 
ATOM   9623  C  C   . SER F  1 112 ? -9.139  29.535  49.501 1.00 53.80  ? 103 SER F C   1 
ATOM   9624  O  O   . SER F  1 112 ? -8.960  29.329  48.296 1.00 52.98  ? 103 SER F O   1 
ATOM   9625  C  CB  . SER F  1 112 ? -11.050 30.999  50.069 1.00 53.97  ? 103 SER F CB  1 
ATOM   9626  O  OG  . SER F  1 112 ? -11.647 30.297  48.979 1.00 55.69  ? 103 SER F OG  1 
ATOM   9627  N  N   . PRO F  1 113 ? -9.061  28.556  50.417 1.00 53.15  ? 104 PRO F N   1 
ATOM   9628  C  CA  . PRO F  1 113 ? -8.787  27.170  50.020 1.00 51.68  ? 104 PRO F CA  1 
ATOM   9629  C  C   . PRO F  1 113 ? -9.739  26.740  48.917 1.00 57.01  ? 104 PRO F C   1 
ATOM   9630  O  O   . PRO F  1 113 ? -10.911 27.138  48.956 1.00 59.38  ? 104 PRO F O   1 
ATOM   9631  C  CB  . PRO F  1 113 ? -9.109  26.393  51.289 1.00 45.90  ? 104 PRO F CB  1 
ATOM   9632  C  CG  . PRO F  1 113 ? -8.842  27.365  52.385 1.00 54.28  ? 104 PRO F CG  1 
ATOM   9633  C  CD  . PRO F  1 113 ? -9.311  28.677  51.862 1.00 45.66  ? 104 PRO F CD  1 
ATOM   9634  N  N   . GLN F  1 114 ? -9.282  25.950  47.948 1.00 59.83  ? 105 GLN F N   1 
ATOM   9635  C  CA  . GLN F  1 114 ? -10.218 25.567  46.901 1.00 58.13  ? 105 GLN F CA  1 
ATOM   9636  C  C   . GLN F  1 114 ? -10.685 24.164  47.190 1.00 58.50  ? 105 GLN F C   1 
ATOM   9637  O  O   . GLN F  1 114 ? -10.027 23.193  46.843 1.00 64.86  ? 105 GLN F O   1 
ATOM   9638  C  CB  . GLN F  1 114 ? -9.532  25.638  45.534 1.00 50.09  ? 105 GLN F CB  1 
ATOM   9639  C  CG  . GLN F  1 114 ? -9.454  27.064  44.974 1.00 61.40  ? 105 GLN F CG  1 
ATOM   9640  C  CD  . GLN F  1 114 ? -8.425  27.231  43.869 1.00 63.47  ? 105 GLN F CD  1 
ATOM   9641  O  OE1 . GLN F  1 114 ? -7.243  26.944  44.053 1.00 68.30  ? 105 GLN F OE1 1 
ATOM   9642  N  NE2 . GLN F  1 114 ? -8.869  27.708  42.721 1.00 60.12  ? 105 GLN F NE2 1 
ATOM   9643  N  N   . ASN F  1 115 ? -11.905 24.078  47.705 1.00 55.69  ? 106 ASN F N   1 
ATOM   9644  C  CA  . ASN F  1 115 ? -12.448 22.844  48.233 1.00 53.49  ? 106 ASN F CA  1 
ATOM   9645  C  C   . ASN F  1 115 ? -13.942 22.936  48.066 1.00 56.31  ? 106 ASN F C   1 
ATOM   9646  O  O   . ASN F  1 115 ? -14.506 24.017  48.179 1.00 56.08  ? 106 ASN F O   1 
ATOM   9647  C  CB  . ASN F  1 115 ? -12.156 22.712  49.728 1.00 58.23  ? 106 ASN F CB  1 
ATOM   9648  C  CG  . ASN F  1 115 ? -10.705 22.371  50.044 1.00 57.45  ? 106 ASN F CG  1 
ATOM   9649  O  OD1 . ASN F  1 115 ? -10.015 21.696  49.283 1.00 54.14  ? 106 ASN F OD1 1 
ATOM   9650  N  ND2 . ASN F  1 115 ? -10.249 22.827  51.203 1.00 57.73  ? 106 ASN F ND2 1 
ATOM   9651  N  N   . ALA F  1 116 ? -14.596 21.807  47.833 1.00 57.08  ? 107 ALA F N   1 
ATOM   9652  C  CA  . ALA F  1 116 ? -16.035 21.822  47.659 1.00 49.08  ? 107 ALA F CA  1 
ATOM   9653  C  C   . ALA F  1 116 ? -16.745 20.840  48.582 1.00 55.51  ? 107 ALA F C   1 
ATOM   9654  O  O   . ALA F  1 116 ? -16.164 19.853  49.044 1.00 54.34  ? 107 ALA F O   1 
ATOM   9655  C  CB  . ALA F  1 116 ? -16.371 21.534  46.235 1.00 51.24  ? 107 ALA F CB  1 
ATOM   9656  N  N   . LEU F  1 117 ? -18.012 21.122  48.850 1.00 53.43  ? 108 LEU F N   1 
ATOM   9657  C  CA  . LEU F  1 117 ? -18.815 20.236  49.671 1.00 56.57  ? 108 LEU F CA  1 
ATOM   9658  C  C   . LEU F  1 117 ? -19.735 19.391  48.800 1.00 56.04  ? 108 LEU F C   1 
ATOM   9659  O  O   . LEU F  1 117 ? -20.644 19.904  48.157 1.00 57.47  ? 108 LEU F O   1 
ATOM   9660  C  CB  . LEU F  1 117 ? -19.622 21.048  50.677 1.00 54.59  ? 108 LEU F CB  1 
ATOM   9661  C  CG  . LEU F  1 117 ? -20.560 20.333  51.645 1.00 60.06  ? 108 LEU F CG  1 
ATOM   9662  C  CD1 . LEU F  1 117 ? -19.818 19.382  52.577 1.00 60.94  ? 108 LEU F CD1 1 
ATOM   9663  C  CD2 . LEU F  1 117 ? -21.305 21.383  52.453 1.00 71.37  ? 108 LEU F CD2 1 
ATOM   9664  N  N   . VAL F  1 118 ? -19.480 18.089  48.775 1.00 55.09  ? 109 VAL F N   1 
ATOM   9665  C  CA  . VAL F  1 118 ? -20.290 17.156  48.002 1.00 56.60  ? 109 VAL F CA  1 
ATOM   9666  C  C   . VAL F  1 118 ? -21.206 16.352  48.928 1.00 59.38  ? 109 VAL F C   1 
ATOM   9667  O  O   . VAL F  1 118 ? -20.758 15.855  49.950 1.00 56.03  ? 109 VAL F O   1 
ATOM   9668  C  CB  . VAL F  1 118 ? -19.389 16.167  47.217 1.00 53.26  ? 109 VAL F CB  1 
ATOM   9669  C  CG1 . VAL F  1 118 ? -20.229 15.137  46.487 1.00 54.22  ? 109 VAL F CG1 1 
ATOM   9670  C  CG2 . VAL F  1 118 ? -18.469 16.904  46.250 1.00 50.20  ? 109 VAL F CG2 1 
ATOM   9671  N  N   . ASN F  1 119 ? -22.474 16.186  48.560 1.00 63.34  ? 110 ASN F N   1 
ATOM   9672  C  CA  . ASN F  1 119 ? -23.410 15.416  49.394 1.00 67.67  ? 110 ASN F CA  1 
ATOM   9673  C  C   . ASN F  1 119 ? -24.189 14.308  48.676 1.00 63.81  ? 110 ASN F C   1 
ATOM   9674  O  O   . ASN F  1 119 ? -24.182 14.221  47.454 1.00 67.12  ? 110 ASN F O   1 
ATOM   9675  C  CB  . ASN F  1 119 ? -24.371 16.336  50.145 1.00 71.93  ? 110 ASN F CB  1 
ATOM   9676  C  CG  . ASN F  1 119 ? -25.485 16.863  49.267 1.00 77.81  ? 110 ASN F CG  1 
ATOM   9677  O  OD1 . ASN F  1 119 ? -25.976 16.181  48.392 1.00 75.44  ? 110 ASN F OD1 1 
ATOM   9678  N  ND2 . ASN F  1 119 ? -25.903 18.078  49.522 1.00 88.08  ? 110 ASN F ND2 1 
ATOM   9679  N  N   . SER F  1 120 ? -24.842 13.460  49.466 1.00 68.22  ? 111 SER F N   1 
ATOM   9680  C  CA  . SER F  1 120 ? -25.355 12.165  49.005 1.00 66.57  ? 111 SER F CA  1 
ATOM   9681  C  C   . SER F  1 120 ? -26.408 12.206  47.899 1.00 66.69  ? 111 SER F C   1 
ATOM   9682  O  O   . SER F  1 120 ? -26.600 11.216  47.191 1.00 69.61  ? 111 SER F O   1 
ATOM   9683  C  CB  . SER F  1 120 ? -25.849 11.313  50.186 1.00 66.22  ? 111 SER F CB  1 
ATOM   9684  O  OG  . SER F  1 120 ? -27.082 11.784  50.701 1.00 68.72  ? 111 SER F OG  1 
ATOM   9685  N  N   . SER F  1 121 ? -27.080 13.340  47.743 1.00 68.90  ? 112 SER F N   1 
ATOM   9686  C  CA  . SER F  1 121 ? -28.028 13.508  46.642 1.00 70.86  ? 112 SER F CA  1 
ATOM   9687  C  C   . SER F  1 121 ? -27.341 13.988  45.345 1.00 72.46  ? 112 SER F C   1 
ATOM   9688  O  O   . SER F  1 121 ? -27.995 14.201  44.318 1.00 71.12  ? 112 SER F O   1 
ATOM   9689  C  CB  . SER F  1 121 ? -29.147 14.461  47.052 1.00 65.39  ? 112 SER F CB  1 
ATOM   9690  O  OG  . SER F  1 121 ? -28.626 15.744  47.335 1.00 74.55  ? 112 SER F OG  1 
ATOM   9691  N  N   . GLY F  1 122 ? -26.024 14.161  45.399 1.00 65.11  ? 113 GLY F N   1 
ATOM   9692  C  CA  . GLY F  1 122 ? -25.257 14.521  44.225 1.00 65.30  ? 113 GLY F CA  1 
ATOM   9693  C  C   . GLY F  1 122 ? -24.976 15.996  44.045 1.00 70.59  ? 113 GLY F C   1 
ATOM   9694  O  O   . GLY F  1 122 ? -24.275 16.382  43.106 1.00 65.04  ? 113 GLY F O   1 
ATOM   9695  N  N   . HIS F  1 123 ? -25.534 16.819  44.930 1.00 70.79  ? 114 HIS F N   1 
ATOM   9696  C  CA  . HIS F  1 123 ? -25.331 18.257  44.870 1.00 64.83  ? 114 HIS F CA  1 
ATOM   9697  C  C   . HIS F  1 123 ? -23.904 18.603  45.252 1.00 62.12  ? 114 HIS F C   1 
ATOM   9698  O  O   . HIS F  1 123 ? -23.365 18.075  46.213 1.00 64.12  ? 114 HIS F O   1 
ATOM   9699  C  CB  . HIS F  1 123 ? -26.316 18.975  45.790 1.00 73.63  ? 114 HIS F CB  1 
ATOM   9700  C  CG  . HIS F  1 123 ? -27.728 18.960  45.293 1.00 79.27  ? 114 HIS F CG  1 
ATOM   9701  N  ND1 . HIS F  1 123 ? -28.557 17.865  45.435 1.00 78.46  ? 114 HIS F ND1 1 
ATOM   9702  C  CD2 . HIS F  1 123 ? -28.456 19.901  44.646 1.00 78.97  ? 114 HIS F CD2 1 
ATOM   9703  C  CE1 . HIS F  1 123 ? -29.732 18.134  44.896 1.00 84.99  ? 114 HIS F CE1 1 
ATOM   9704  N  NE2 . HIS F  1 123 ? -29.698 19.363  44.409 1.00 88.66  ? 114 HIS F NE2 1 
ATOM   9705  N  N   . VAL F  1 124 ? -23.280 19.468  44.468 1.00 61.79  ? 115 VAL F N   1 
ATOM   9706  C  CA  . VAL F  1 124 ? -21.966 19.994  44.795 1.00 59.03  ? 115 VAL F CA  1 
ATOM   9707  C  C   . VAL F  1 124 ? -22.133 21.458  45.188 1.00 59.68  ? 115 VAL F C   1 
ATOM   9708  O  O   . VAL F  1 124 ? -22.891 22.198  44.553 1.00 60.87  ? 115 VAL F O   1 
ATOM   9709  C  CB  . VAL F  1 124 ? -21.006 19.906  43.589 1.00 52.70  ? 115 VAL F CB  1 
ATOM   9710  C  CG1 . VAL F  1 124 ? -19.639 20.453  43.950 1.00 50.82  ? 115 VAL F CG1 1 
ATOM   9711  C  CG2 . VAL F  1 124 ? -20.887 18.492  43.119 1.00 52.43  ? 115 VAL F CG2 1 
ATOM   9712  N  N   . GLN F  1 125 ? -21.446 21.887  46.236 1.00 55.60  ? 116 GLN F N   1 
ATOM   9713  C  CA  . GLN F  1 125 ? -21.454 23.302  46.569 1.00 61.63  ? 116 GLN F CA  1 
ATOM   9714  C  C   . GLN F  1 125 ? -20.018 23.815  46.588 1.00 59.59  ? 116 GLN F C   1 
ATOM   9715  O  O   . GLN F  1 125 ? -19.187 23.328  47.353 1.00 63.59  ? 116 GLN F O   1 
ATOM   9716  C  CB  . GLN F  1 125 ? -22.157 23.531  47.910 1.00 64.82  ? 116 GLN F CB  1 
ATOM   9717  C  CG  . GLN F  1 125 ? -22.228 24.989  48.346 1.00 80.41  ? 116 GLN F CG  1 
ATOM   9718  C  CD  . GLN F  1 125 ? -22.522 25.147  49.835 1.00 93.32  ? 116 GLN F CD  1 
ATOM   9719  O  OE1 . GLN F  1 125 ? -21.928 25.993  50.516 1.00 96.18  ? 116 GLN F OE1 1 
ATOM   9720  N  NE2 . GLN F  1 125 ? -23.442 24.332  50.346 1.00 96.88  ? 116 GLN F NE2 1 
ATOM   9721  N  N   . TYR F  1 126 ? -19.716 24.781  45.734 1.00 51.35  ? 117 TYR F N   1 
ATOM   9722  C  CA  . TYR F  1 126 ? -18.366 25.331  45.672 1.00 55.66  ? 117 TYR F CA  1 
ATOM   9723  C  C   . TYR F  1 126 ? -18.356 26.840  45.924 1.00 60.40  ? 117 TYR F C   1 
ATOM   9724  O  O   . TYR F  1 126 ? -19.108 27.585  45.300 1.00 56.15  ? 117 TYR F O   1 
ATOM   9725  C  CB  . TYR F  1 126 ? -17.738 25.020  44.319 1.00 51.54  ? 117 TYR F CB  1 
ATOM   9726  C  CG  . TYR F  1 126 ? -16.331 25.531  44.161 1.00 54.92  ? 117 TYR F CG  1 
ATOM   9727  C  CD1 . TYR F  1 126 ? -15.377 25.304  45.141 1.00 58.04  ? 117 TYR F CD1 1 
ATOM   9728  C  CD2 . TYR F  1 126 ? -15.948 26.221  43.024 1.00 51.22  ? 117 TYR F CD2 1 
ATOM   9729  C  CE1 . TYR F  1 126 ? -14.079 25.761  44.997 1.00 55.93  ? 117 TYR F CE1 1 
ATOM   9730  C  CE2 . TYR F  1 126 ? -14.654 26.683  42.870 1.00 54.04  ? 117 TYR F CE2 1 
ATOM   9731  C  CZ  . TYR F  1 126 ? -13.724 26.449  43.863 1.00 59.17  ? 117 TYR F CZ  1 
ATOM   9732  O  OH  . TYR F  1 126 ? -12.435 26.904  43.720 1.00 57.02  ? 117 TYR F OH  1 
ATOM   9733  N  N   . LEU F  1 127 ? -17.508 27.297  46.839 1.00 58.58  ? 118 LEU F N   1 
ATOM   9734  C  CA  . LEU F  1 127 ? -17.540 28.708  47.218 1.00 64.14  ? 118 LEU F CA  1 
ATOM   9735  C  C   . LEU F  1 127 ? -16.178 29.391  47.262 1.00 60.44  ? 118 LEU F C   1 
ATOM   9736  O  O   . LEU F  1 127 ? -15.594 29.544  48.324 1.00 63.96  ? 118 LEU F O   1 
ATOM   9737  C  CB  . LEU F  1 127 ? -18.256 28.892  48.561 1.00 61.36  ? 118 LEU F CB  1 
ATOM   9738  C  CG  . LEU F  1 127 ? -18.516 30.361  48.891 1.00 70.91  ? 118 LEU F CG  1 
ATOM   9739  C  CD1 . LEU F  1 127 ? -19.905 30.793  48.450 1.00 70.66  ? 118 LEU F CD1 1 
ATOM   9740  C  CD2 . LEU F  1 127 ? -18.324 30.614  50.375 1.00 83.58  ? 118 LEU F CD2 1 
ATOM   9741  N  N   . PRO F  1 128 ? -15.662 29.793  46.101 1.00 51.66  ? 119 PRO F N   1 
ATOM   9742  C  CA  . PRO F  1 128 ? -14.412 30.550  46.014 1.00 57.35  ? 119 PRO F CA  1 
ATOM   9743  C  C   . PRO F  1 128 ? -14.511 32.004  46.495 1.00 61.52  ? 119 PRO F C   1 
ATOM   9744  O  O   . PRO F  1 128 ? -15.397 32.733  46.032 1.00 60.48  ? 119 PRO F O   1 
ATOM   9745  C  CB  . PRO F  1 128 ? -14.107 30.553  44.514 1.00 51.78  ? 119 PRO F CB  1 
ATOM   9746  C  CG  . PRO F  1 128 ? -15.134 29.712  43.874 1.00 60.82  ? 119 PRO F CG  1 
ATOM   9747  C  CD  . PRO F  1 128 ? -16.284 29.604  44.792 1.00 57.40  ? 119 PRO F CD  1 
ATOM   9748  N  N   . ALA F  1 129 ? -13.567 32.447  47.324 1.00 52.61  ? 120 ALA F N   1 
ATOM   9749  C  CA  . ALA F  1 129 ? -13.492 33.853  47.684 1.00 52.43  ? 120 ALA F CA  1 
ATOM   9750  C  C   . ALA F  1 129 ? -12.427 34.428  46.797 1.00 54.58  ? 120 ALA F C   1 
ATOM   9751  O  O   . ALA F  1 129 ? -11.326 33.880  46.728 1.00 52.60  ? 120 ALA F O   1 
ATOM   9752  C  CB  . ALA F  1 129 ? -13.126 34.025  49.136 1.00 48.11  ? 120 ALA F CB  1 
ATOM   9753  N  N   . GLN F  1 130 ? -12.768 35.518  46.108 1.00 53.90  ? 121 GLN F N   1 
ATOM   9754  C  CA  . GLN F  1 130 ? -11.904 36.088  45.071 1.00 53.88  ? 121 GLN F CA  1 
ATOM   9755  C  C   . GLN F  1 130 ? -11.738 37.609  45.090 1.00 52.11  ? 121 GLN F C   1 
ATOM   9756  O  O   . GLN F  1 130 ? -12.594 38.354  45.566 1.00 52.81  ? 121 GLN F O   1 
ATOM   9757  C  CB  . GLN F  1 130 ? -12.390 35.689  43.668 1.00 52.95  ? 121 GLN F CB  1 
ATOM   9758  C  CG  . GLN F  1 130 ? -13.364 34.532  43.625 1.00 57.49  ? 121 GLN F CG  1 
ATOM   9759  C  CD  . GLN F  1 130 ? -13.702 34.078  42.213 1.00 55.09  ? 121 GLN F CD  1 
ATOM   9760  O  OE1 . GLN F  1 130 ? -13.247 34.646  41.226 1.00 58.17  ? 121 GLN F OE1 1 
ATOM   9761  N  NE2 . GLN F  1 130 ? -14.514 33.046  42.118 1.00 63.59  ? 121 GLN F NE2 1 
ATOM   9762  N  N   . ARG F  1 131 ? -10.625 38.059  44.533 1.00 46.48  ? 122 ARG F N   1 
ATOM   9763  C  CA  . ARG F  1 131 ? -10.487 39.452  44.182 1.00 46.41  ? 122 ARG F CA  1 
ATOM   9764  C  C   . ARG F  1 131 ? -10.342 39.596  42.665 1.00 48.43  ? 122 ARG F C   1 
ATOM   9765  O  O   . ARG F  1 131 ? -9.405  39.080  42.047 1.00 41.51  ? 122 ARG F O   1 
ATOM   9766  C  CB  . ARG F  1 131 ? -9.309  40.079  44.911 1.00 49.86  ? 122 ARG F CB  1 
ATOM   9767  C  CG  . ARG F  1 131 ? -9.172  41.570  44.726 1.00 45.43  ? 122 ARG F CG  1 
ATOM   9768  C  CD  . ARG F  1 131 ? -7.712  41.915  44.782 1.00 48.57  ? 122 ARG F CD  1 
ATOM   9769  N  NE  . ARG F  1 131 ? -7.467  43.326  44.541 1.00 61.13  ? 122 ARG F NE  1 
ATOM   9770  C  CZ  . ARG F  1 131 ? -7.120  44.177  45.493 1.00 57.26  ? 122 ARG F CZ  1 
ATOM   9771  N  NH1 . ARG F  1 131 ? -6.988  43.739  46.736 1.00 60.34  ? 122 ARG F NH1 1 
ATOM   9772  N  NH2 . ARG F  1 131 ? -6.897  45.449  45.210 1.00 48.49  ? 122 ARG F NH2 1 
ATOM   9773  N  N   . LEU F  1 132 ? -11.306 40.319  42.102 1.00 47.24  ? 123 LEU F N   1 
ATOM   9774  C  CA  . LEU F  1 132 ? -11.436 40.595  40.685 1.00 46.33  ? 123 LEU F CA  1 
ATOM   9775  C  C   . LEU F  1 132 ? -11.201 42.072  40.379 1.00 49.63  ? 123 LEU F C   1 
ATOM   9776  O  O   . LEU F  1 132 ? -11.824 42.913  40.997 1.00 51.05  ? 123 LEU F O   1 
ATOM   9777  C  CB  . LEU F  1 132 ? -12.867 40.250  40.268 1.00 46.98  ? 123 LEU F CB  1 
ATOM   9778  C  CG  . LEU F  1 132 ? -13.309 40.559  38.839 1.00 51.86  ? 123 LEU F CG  1 
ATOM   9779  C  CD1 . LEU F  1 132 ? -12.622 39.589  37.901 1.00 43.72  ? 123 LEU F CD1 1 
ATOM   9780  C  CD2 . LEU F  1 132 ? -14.824 40.510  38.682 1.00 46.93  ? 123 LEU F CD2 1 
ATOM   9781  N  N   . SER F  1 133 ? -10.315 42.385  39.431 1.00 48.98  ? 124 SER F N   1 
ATOM   9782  C  CA  . SER F  1 133 ? -10.274 43.718  38.827 1.00 47.10  ? 124 SER F CA  1 
ATOM   9783  C  C   . SER F  1 133 ? -11.033 43.656  37.508 1.00 49.18  ? 124 SER F C   1 
ATOM   9784  O  O   . SER F  1 133 ? -10.703 42.882  36.626 1.00 48.29  ? 124 SER F O   1 
ATOM   9785  C  CB  . SER F  1 133 ? -8.844  44.172  38.547 1.00 51.21  ? 124 SER F CB  1 
ATOM   9786  O  OG  . SER F  1 133 ? -8.083  44.324  39.730 1.00 58.86  ? 124 SER F OG  1 
ATOM   9787  N  N   . PHE F  1 134 ? -12.055 44.475  37.370 1.00 54.68  ? 125 PHE F N   1 
ATOM   9788  C  CA  . PHE F  1 134 ? -12.876 44.429  36.176 1.00 60.17  ? 125 PHE F CA  1 
ATOM   9789  C  C   . PHE F  1 134 ? -13.097 45.841  35.610 1.00 66.66  ? 125 PHE F C   1 
ATOM   9790  O  O   . PHE F  1 134 ? -12.756 46.840  36.263 1.00 63.76  ? 125 PHE F O   1 
ATOM   9791  C  CB  . PHE F  1 134 ? -14.186 43.685  36.454 1.00 60.13  ? 125 PHE F CB  1 
ATOM   9792  C  CG  . PHE F  1 134 ? -15.154 44.454  37.293 1.00 63.88  ? 125 PHE F CG  1 
ATOM   9793  C  CD1 . PHE F  1 134 ? -16.128 45.243  36.704 1.00 71.61  ? 125 PHE F CD1 1 
ATOM   9794  C  CD2 . PHE F  1 134 ? -15.092 44.394  38.667 1.00 63.76  ? 125 PHE F CD2 1 
ATOM   9795  C  CE1 . PHE F  1 134 ? -17.024 45.957  37.473 1.00 72.65  ? 125 PHE F CE1 1 
ATOM   9796  C  CE2 . PHE F  1 134 ? -15.981 45.110  39.445 1.00 70.20  ? 125 PHE F CE2 1 
ATOM   9797  C  CZ  . PHE F  1 134 ? -16.949 45.891  38.847 1.00 74.83  ? 125 PHE F CZ  1 
ATOM   9798  N  N   . MET F  1 135 ? -13.641 45.929  34.394 1.00 64.90  ? 126 MET F N   1 
ATOM   9799  C  CA  . MET F  1 135 ? -13.714 47.218  33.711 1.00 62.62  ? 126 MET F CA  1 
ATOM   9800  C  C   . MET F  1 135 ? -14.845 48.041  34.281 1.00 63.99  ? 126 MET F C   1 
ATOM   9801  O  O   . MET F  1 135 ? -16.004 47.650  34.200 1.00 66.76  ? 126 MET F O   1 
ATOM   9802  C  CB  . MET F  1 135 ? -13.979 46.999  32.234 1.00 51.94  ? 126 MET F CB  1 
ATOM   9803  C  CG  . MET F  1 135 ? -12.892 46.233  31.526 1.00 55.69  ? 126 MET F CG  1 
ATOM   9804  S  SD  . MET F  1 135 ? -13.431 45.656  29.917 1.00 60.07  ? 126 MET F SD  1 
ATOM   9805  C  CE  . MET F  1 135 ? -12.357 44.238  29.671 1.00 57.12  ? 126 MET F CE  1 
ATOM   9806  N  N   . CYS F  1 136 ? -14.501 49.188  34.853 1.00 60.31  ? 127 CYS F N   1 
ATOM   9807  C  CA  . CYS F  1 136 ? -15.503 50.045  35.457 1.00 61.66  ? 127 CYS F CA  1 
ATOM   9808  C  C   . CYS F  1 136 ? -15.068 51.498  35.406 1.00 63.06  ? 127 CYS F C   1 
ATOM   9809  O  O   . CYS F  1 136 ? -13.898 51.798  35.607 1.00 65.60  ? 127 CYS F O   1 
ATOM   9810  C  CB  . CYS F  1 136 ? -15.738 49.583  36.894 1.00 71.06  ? 127 CYS F CB  1 
ATOM   9811  S  SG  . CYS F  1 136 ? -16.550 50.732  38.015 1.00 77.35  ? 127 CYS F SG  1 
ATOM   9812  N  N   . ASP F  1 137 ? -16.013 52.400  35.158 1.00 67.36  ? 128 ASP F N   1 
ATOM   9813  C  CA  . ASP F  1 137 ? -15.728 53.835  35.165 1.00 70.59  ? 128 ASP F CA  1 
ATOM   9814  C  C   . ASP F  1 137 ? -16.386 54.438  36.394 1.00 72.63  ? 128 ASP F C   1 
ATOM   9815  O  O   . ASP F  1 137 ? -17.611 54.561  36.459 1.00 73.19  ? 128 ASP F O   1 
ATOM   9816  C  CB  . ASP F  1 137 ? -16.260 54.503  33.894 1.00 75.25  ? 128 ASP F CB  1 
ATOM   9817  C  CG  . ASP F  1 137 ? -16.021 56.005  33.869 1.00 78.71  ? 128 ASP F CG  1 
ATOM   9818  O  OD1 . ASP F  1 137 ? -15.124 56.481  34.598 1.00 82.05  ? 128 ASP F OD1 1 
ATOM   9819  O  OD2 . ASP F  1 137 ? -16.727 56.705  33.107 1.00 72.53  ? 128 ASP F OD2 1 
ATOM   9820  N  N   . PRO F  1 138 ? -15.558 54.799  37.379 1.00 74.45  ? 129 PRO F N   1 
ATOM   9821  C  CA  . PRO F  1 138 ? -15.952 55.207  38.730 1.00 69.56  ? 129 PRO F CA  1 
ATOM   9822  C  C   . PRO F  1 138 ? -16.652 56.569  38.818 1.00 78.83  ? 129 PRO F C   1 
ATOM   9823  O  O   . PRO F  1 138 ? -17.242 56.840  39.855 1.00 80.83  ? 129 PRO F O   1 
ATOM   9824  C  CB  . PRO F  1 138 ? -14.626 55.218  39.489 1.00 66.42  ? 129 PRO F CB  1 
ATOM   9825  C  CG  . PRO F  1 138 ? -13.625 55.568  38.457 1.00 71.74  ? 129 PRO F CG  1 
ATOM   9826  C  CD  . PRO F  1 138 ? -14.104 54.924  37.171 1.00 73.42  ? 129 PRO F CD  1 
ATOM   9827  N  N   . THR F  1 139 ? -16.595 57.407  37.784 1.00 79.32  ? 130 THR F N   1 
ATOM   9828  C  CA  . THR F  1 139 ? -17.066 58.788  37.934 1.00 80.77  ? 130 THR F CA  1 
ATOM   9829  C  C   . THR F  1 139 ? -18.464 58.863  38.547 1.00 76.65  ? 130 THR F C   1 
ATOM   9830  O  O   . THR F  1 139 ? -19.335 58.040  38.261 1.00 66.34  ? 130 THR F O   1 
ATOM   9831  C  CB  . THR F  1 139 ? -16.997 59.626  36.619 1.00 84.13  ? 130 THR F CB  1 
ATOM   9832  O  OG1 . THR F  1 139 ? -17.376 58.822  35.495 1.00 84.40  ? 130 THR F OG1 1 
ATOM   9833  C  CG2 . THR F  1 139 ? -15.587 60.188  36.399 1.00 79.67  ? 130 THR F CG2 1 
ATOM   9834  N  N   . GLY F  1 140 ? -18.634 59.835  39.440 1.00 77.48  ? 131 GLY F N   1 
ATOM   9835  C  CA  . GLY F  1 140 ? -19.869 60.001  40.178 1.00 78.64  ? 131 GLY F CA  1 
ATOM   9836  C  C   . GLY F  1 140 ? -19.746 59.308  41.512 1.00 76.15  ? 131 GLY F C   1 
ATOM   9837  O  O   . GLY F  1 140 ? -20.681 59.273  42.312 1.00 72.79  ? 131 GLY F O   1 
ATOM   9838  N  N   . VAL F  1 141 ? -18.568 58.750  41.746 1.00 78.83  ? 132 VAL F N   1 
ATOM   9839  C  CA  . VAL F  1 141 ? -18.321 57.973  42.948 1.00 78.34  ? 132 VAL F CA  1 
ATOM   9840  C  C   . VAL F  1 141 ? -18.231 58.928  44.129 1.00 78.63  ? 132 VAL F C   1 
ATOM   9841  O  O   . VAL F  1 141 ? -18.549 58.564  45.267 1.00 72.90  ? 132 VAL F O   1 
ATOM   9842  C  CB  . VAL F  1 141 ? -17.030 57.129  42.810 1.00 71.21  ? 132 VAL F CB  1 
ATOM   9843  C  CG1 . VAL F  1 141 ? -15.795 58.019  42.809 1.00 74.10  ? 132 VAL F CG1 1 
ATOM   9844  C  CG2 . VAL F  1 141 ? -16.949 56.086  43.899 1.00 66.22  ? 132 VAL F CG2 1 
ATOM   9845  N  N   . ASP F  1 142 ? -17.813 60.160  43.836 1.00 79.12  ? 133 ASP F N   1 
ATOM   9846  C  CA  . ASP F  1 142 ? -17.683 61.205  44.848 1.00 75.65  ? 133 ASP F CA  1 
ATOM   9847  C  C   . ASP F  1 142 ? -18.954 62.047  45.001 1.00 75.48  ? 133 ASP F C   1 
ATOM   9848  O  O   . ASP F  1 142 ? -18.965 63.033  45.728 1.00 80.18  ? 133 ASP F O   1 
ATOM   9849  C  CB  . ASP F  1 142 ? -16.451 62.086  44.600 1.00 71.40  ? 133 ASP F CB  1 
ATOM   9850  C  CG  . ASP F  1 142 ? -16.433 62.687  43.217 1.00 79.34  ? 133 ASP F CG  1 
ATOM   9851  O  OD1 . ASP F  1 142 ? -17.480 62.647  42.550 1.00 83.04  ? 133 ASP F OD1 1 
ATOM   9852  O  OD2 . ASP F  1 142 ? -15.376 63.204  42.796 1.00 78.76  ? 133 ASP F OD2 1 
ATOM   9853  N  N   . SER F  1 143 ? -20.015 61.670  44.299 1.00 79.07  ? 134 SER F N   1 
ATOM   9854  C  CA  . SER F  1 143 ? -21.293 62.348  44.462 1.00 81.08  ? 134 SER F CA  1 
ATOM   9855  C  C   . SER F  1 143 ? -22.223 61.497  45.309 1.00 80.42  ? 134 SER F C   1 
ATOM   9856  O  O   . SER F  1 143 ? -21.870 60.399  45.705 1.00 84.35  ? 134 SER F O   1 
ATOM   9857  C  CB  . SER F  1 143 ? -21.938 62.641  43.104 1.00 81.46  ? 134 SER F CB  1 
ATOM   9858  O  OG  . SER F  1 143 ? -22.847 61.617  42.734 1.00 85.19  ? 134 SER F OG  1 
ATOM   9859  N  N   . GLU F  1 144 ? -23.412 62.012  45.590 1.00 92.38  ? 135 GLU F N   1 
ATOM   9860  C  CA  . GLU F  1 144 ? -24.366 61.319  46.450 1.00 102.17 ? 135 GLU F CA  1 
ATOM   9861  C  C   . GLU F  1 144 ? -25.195 60.271  45.700 1.00 93.90  ? 135 GLU F C   1 
ATOM   9862  O  O   . GLU F  1 144 ? -25.754 59.351  46.311 1.00 86.66  ? 135 GLU F O   1 
ATOM   9863  C  CB  . GLU F  1 144 ? -25.273 62.351  47.139 1.00 102.89 ? 135 GLU F CB  1 
ATOM   9864  C  CG  . GLU F  1 144 ? -26.101 61.823  48.296 1.00 109.86 ? 135 GLU F CG  1 
ATOM   9865  C  CD  . GLU F  1 144 ? -26.824 62.943  49.028 1.00 124.26 ? 135 GLU F CD  1 
ATOM   9866  O  OE1 . GLU F  1 144 ? -26.244 64.049  49.154 1.00 118.09 ? 135 GLU F OE1 1 
ATOM   9867  O  OE2 . GLU F  1 144 ? -27.973 62.720  49.467 1.00 130.72 ? 135 GLU F OE2 1 
ATOM   9868  N  N   . GLU F  1 145 ? -25.272 60.436  44.379 1.00 88.41  ? 136 GLU F N   1 
ATOM   9869  C  CA  . GLU F  1 145 ? -26.055 59.565  43.500 1.00 89.79  ? 136 GLU F CA  1 
ATOM   9870  C  C   . GLU F  1 145 ? -25.292 58.288  43.202 1.00 86.33  ? 136 GLU F C   1 
ATOM   9871  O  O   . GLU F  1 145 ? -25.874 57.252  42.886 1.00 74.66  ? 136 GLU F O   1 
ATOM   9872  C  CB  . GLU F  1 145 ? -26.407 60.292  42.194 1.00 91.56  ? 136 GLU F CB  1 
ATOM   9873  C  CG  . GLU F  1 145 ? -27.504 61.351  42.338 1.00 96.99  ? 136 GLU F CG  1 
ATOM   9874  C  CD  . GLU F  1 145 ? -27.083 62.554  43.184 1.00 103.71 ? 136 GLU F CD  1 
ATOM   9875  O  OE1 . GLU F  1 145 ? -25.925 63.006  43.053 1.00 100.67 ? 136 GLU F OE1 1 
ATOM   9876  O  OE2 . GLU F  1 145 ? -27.913 63.049  43.983 1.00 99.67  ? 136 GLU F OE2 1 
ATOM   9877  N  N   . GLY F  1 146 ? -23.972 58.390  43.291 1.00 90.57  ? 137 GLY F N   1 
ATOM   9878  C  CA  . GLY F  1 146 ? -23.100 57.240  43.195 1.00 77.34  ? 137 GLY F CA  1 
ATOM   9879  C  C   . GLY F  1 146 ? -22.683 56.907  41.784 1.00 79.64  ? 137 GLY F C   1 
ATOM   9880  O  O   . GLY F  1 146 ? -23.265 57.390  40.817 1.00 85.82  ? 137 GLY F O   1 
ATOM   9881  N  N   . ALA F  1 147 ? -21.653 56.076  41.682 1.00 78.59  ? 138 ALA F N   1 
ATOM   9882  C  CA  . ALA F  1 147 ? -21.202 55.521  40.422 1.00 75.26  ? 138 ALA F CA  1 
ATOM   9883  C  C   . ALA F  1 147 ? -21.865 54.164  40.260 1.00 72.10  ? 138 ALA F C   1 
ATOM   9884  O  O   . ALA F  1 147 ? -22.134 53.487  41.241 1.00 63.39  ? 138 ALA F O   1 
ATOM   9885  C  CB  . ALA F  1 147 ? -19.700 55.382  40.421 1.00 71.38  ? 138 ALA F CB  1 
ATOM   9886  N  N   . THR F  1 148 ? -22.194 53.785  39.033 1.00 75.05  ? 139 THR F N   1 
ATOM   9887  C  CA  . THR F  1 148 ? -22.676 52.428  38.815 1.00 74.21  ? 139 THR F CA  1 
ATOM   9888  C  C   . THR F  1 148 ? -21.722 51.638  37.936 1.00 71.35  ? 139 THR F C   1 
ATOM   9889  O  O   . THR F  1 148 ? -21.087 52.192  37.039 1.00 69.69  ? 139 THR F O   1 
ATOM   9890  C  CB  . THR F  1 148 ? -24.082 52.389  38.216 1.00 70.94  ? 139 THR F CB  1 
ATOM   9891  O  OG1 . THR F  1 148 ? -24.942 53.267  38.952 1.00 76.00  ? 139 THR F OG1 1 
ATOM   9892  C  CG2 . THR F  1 148 ? -24.634 50.978  38.297 1.00 70.84  ? 139 THR F CG2 1 
ATOM   9893  N  N   . CYS F  1 149 ? -21.607 50.344  38.220 1.00 75.78  ? 140 CYS F N   1 
ATOM   9894  C  CA  . CYS F  1 149 ? -20.775 49.456  37.415 1.00 72.35  ? 140 CYS F CA  1 
ATOM   9895  C  C   . CYS F  1 149 ? -21.321 48.047  37.339 1.00 66.36  ? 140 CYS F C   1 
ATOM   9896  O  O   . CYS F  1 149 ? -22.003 47.579  38.249 1.00 60.68  ? 140 CYS F O   1 
ATOM   9897  C  CB  . CYS F  1 149 ? -19.330 49.455  37.902 1.00 72.85  ? 140 CYS F CB  1 
ATOM   9898  S  SG  . CYS F  1 149 ? -18.427 50.890  37.293 1.00 81.58  ? 140 CYS F SG  1 
ATOM   9899  N  N   . ALA F  1 150 ? -21.028 47.388  36.227 1.00 68.80  ? 141 ALA F N   1 
ATOM   9900  C  CA  . ALA F  1 150 ? -21.542 46.052  35.990 1.00 70.50  ? 141 ALA F CA  1 
ATOM   9901  C  C   . ALA F  1 150 ? -20.491 45.146  35.364 1.00 71.72  ? 141 ALA F C   1 
ATOM   9902  O  O   . ALA F  1 150 ? -19.613 45.595  34.619 1.00 65.14  ? 141 ALA F O   1 
ATOM   9903  C  CB  . ALA F  1 150 ? -22.790 46.103  35.131 1.00 58.87  ? 141 ALA F CB  1 
ATOM   9904  N  N   . VAL F  1 151 ? -20.581 43.867  35.711 1.00 67.18  ? 142 VAL F N   1 
ATOM   9905  C  CA  . VAL F  1 151 ? -19.736 42.839  35.134 1.00 63.18  ? 142 VAL F CA  1 
ATOM   9906  C  C   . VAL F  1 151 ? -20.576 41.597  34.976 1.00 60.61  ? 142 VAL F C   1 
ATOM   9907  O  O   . VAL F  1 151 ? -21.338 41.253  35.873 1.00 57.24  ? 142 VAL F O   1 
ATOM   9908  C  CB  . VAL F  1 151 ? -18.530 42.525  36.025 1.00 65.09  ? 142 VAL F CB  1 
ATOM   9909  C  CG1 . VAL F  1 151 ? -18.978 42.186  37.440 1.00 60.96  ? 142 VAL F CG1 1 
ATOM   9910  C  CG2 . VAL F  1 151 ? -17.724 41.393  35.425 1.00 61.97  ? 142 VAL F CG2 1 
ATOM   9911  N  N   . LYS F  1 152 ? -20.444 40.933  33.830 1.00 62.18  ? 143 LYS F N   1 
ATOM   9912  C  CA  . LYS F  1 152 ? -21.241 39.742  33.550 1.00 62.43  ? 143 LYS F CA  1 
ATOM   9913  C  C   . LYS F  1 152 ? -20.493 38.433  33.807 1.00 60.13  ? 143 LYS F C   1 
ATOM   9914  O  O   . LYS F  1 152 ? -19.307 38.311  33.513 1.00 58.77  ? 143 LYS F O   1 
ATOM   9915  C  CB  . LYS F  1 152 ? -21.776 39.778  32.119 1.00 68.50  ? 143 LYS F CB  1 
ATOM   9916  C  CG  . LYS F  1 152 ? -22.946 40.712  31.936 1.00 73.41  ? 143 LYS F CG  1 
ATOM   9917  C  CD  . LYS F  1 152 ? -23.505 40.653  30.531 1.00 74.72  ? 143 LYS F CD  1 
ATOM   9918  C  CE  . LYS F  1 152 ? -24.597 41.690  30.370 1.00 79.88  ? 143 LYS F CE  1 
ATOM   9919  N  NZ  . LYS F  1 152 ? -25.245 41.643  29.040 1.00 92.64  ? 143 LYS F NZ  1 
ATOM   9920  N  N   . PHE F  1 153 ? -21.213 37.457  34.353 1.00 60.23  ? 144 PHE F N   1 
ATOM   9921  C  CA  . PHE F  1 153 ? -20.654 36.152  34.690 1.00 57.58  ? 144 PHE F CA  1 
ATOM   9922  C  C   . PHE F  1 153 ? -21.334 35.070  33.876 1.00 57.31  ? 144 PHE F C   1 
ATOM   9923  O  O   . PHE F  1 153 ? -22.535 35.122  33.683 1.00 66.78  ? 144 PHE F O   1 
ATOM   9924  C  CB  . PHE F  1 153 ? -20.833 35.868  36.195 1.00 55.94  ? 144 PHE F CB  1 
ATOM   9925  C  CG  . PHE F  1 153 ? -19.847 36.600  37.068 1.00 54.34  ? 144 PHE F CG  1 
ATOM   9926  C  CD1 . PHE F  1 153 ? -18.655 36.009  37.430 1.00 52.33  ? 144 PHE F CD1 1 
ATOM   9927  C  CD2 . PHE F  1 153 ? -20.101 37.891  37.495 1.00 56.88  ? 144 PHE F CD2 1 
ATOM   9928  C  CE1 . PHE F  1 153 ? -17.745 36.682  38.199 1.00 54.75  ? 144 PHE F CE1 1 
ATOM   9929  C  CE2 . PHE F  1 153 ? -19.188 38.568  38.273 1.00 56.14  ? 144 PHE F CE2 1 
ATOM   9930  C  CZ  . PHE F  1 153 ? -18.010 37.963  38.623 1.00 55.43  ? 144 PHE F CZ  1 
ATOM   9931  N  N   . GLY F  1 154 ? -20.576 34.092  33.394 1.00 54.94  ? 145 GLY F N   1 
ATOM   9932  C  CA  . GLY F  1 154 ? -21.162 32.961  32.692 1.00 55.46  ? 145 GLY F CA  1 
ATOM   9933  C  C   . GLY F  1 154 ? -20.106 31.947  32.293 1.00 57.24  ? 145 GLY F C   1 
ATOM   9934  O  O   . GLY F  1 154 ? -18.914 32.179  32.478 1.00 57.67  ? 145 GLY F O   1 
ATOM   9935  N  N   . SER F  1 155 ? -20.528 30.816  31.749 1.00 52.69  ? 146 SER F N   1 
ATOM   9936  C  CA  . SER F  1 155 ? -19.559 29.870  31.224 1.00 54.62  ? 146 SER F CA  1 
ATOM   9937  C  C   . SER F  1 155 ? -18.756 30.516  30.113 1.00 57.67  ? 146 SER F C   1 
ATOM   9938  O  O   . SER F  1 155 ? -19.258 31.389  29.411 1.00 65.44  ? 146 SER F O   1 
ATOM   9939  C  CB  . SER F  1 155 ? -20.238 28.624  30.682 1.00 57.08  ? 146 SER F CB  1 
ATOM   9940  O  OG  . SER F  1 155 ? -19.259 27.752  30.160 1.00 54.22  ? 146 SER F OG  1 
ATOM   9941  N  N   . TRP F  1 156 ? -17.493 30.140  29.976 1.00 56.97  ? 147 TRP F N   1 
ATOM   9942  C  CA  . TRP F  1 156 ? -16.738 30.590  28.818 1.00 58.12  ? 147 TRP F CA  1 
ATOM   9943  C  C   . TRP F  1 156 ? -17.023 29.770  27.550 1.00 61.72  ? 147 TRP F C   1 
ATOM   9944  O  O   . TRP F  1 156 ? -17.305 30.318  26.501 1.00 64.11  ? 147 TRP F O   1 
ATOM   9945  C  CB  . TRP F  1 156 ? -15.252 30.591  29.150 1.00 56.54  ? 147 TRP F CB  1 
ATOM   9946  C  CG  . TRP F  1 156 ? -14.408 31.272  28.149 1.00 58.07  ? 147 TRP F CG  1 
ATOM   9947  C  CD1 . TRP F  1 156 ? -13.457 30.701  27.374 1.00 57.62  ? 147 TRP F CD1 1 
ATOM   9948  C  CD2 . TRP F  1 156 ? -14.425 32.665  27.803 1.00 59.10  ? 147 TRP F CD2 1 
ATOM   9949  N  NE1 . TRP F  1 156 ? -12.875 31.646  26.562 1.00 58.60  ? 147 TRP F NE1 1 
ATOM   9950  C  CE2 . TRP F  1 156 ? -13.455 32.861  26.810 1.00 57.01  ? 147 TRP F CE2 1 
ATOM   9951  C  CE3 . TRP F  1 156 ? -15.165 33.763  28.241 1.00 52.87  ? 147 TRP F CE3 1 
ATOM   9952  C  CZ2 . TRP F  1 156 ? -13.202 34.096  26.252 1.00 61.16  ? 147 TRP F CZ2 1 
ATOM   9953  C  CZ3 . TRP F  1 156 ? -14.914 34.986  27.688 1.00 54.77  ? 147 TRP F CZ3 1 
ATOM   9954  C  CH2 . TRP F  1 156 ? -13.942 35.148  26.705 1.00 60.53  ? 147 TRP F CH2 1 
ATOM   9955  N  N   . SER F  1 157 ? -16.950 28.451  27.673 1.00 66.02  ? 148 SER F N   1 
ATOM   9956  C  CA  . SER F  1 157 ? -17.085 27.535  26.541 1.00 62.14  ? 148 SER F CA  1 
ATOM   9957  C  C   . SER F  1 157 ? -18.429 26.822  26.297 1.00 64.36  ? 148 SER F C   1 
ATOM   9958  O  O   . SER F  1 157 ? -18.550 26.080  25.327 1.00 68.16  ? 148 SER F O   1 
ATOM   9959  C  CB  . SER F  1 157 ? -15.960 26.498  26.594 1.00 67.90  ? 148 SER F CB  1 
ATOM   9960  O  OG  . SER F  1 157 ? -14.692 27.128  26.554 1.00 70.93  ? 148 SER F OG  1 
ATOM   9961  N  N   . TYR F  1 158 ? -19.423 27.015  27.154 1.00 61.11  ? 149 TYR F N   1 
ATOM   9962  C  CA  . TYR F  1 158 ? -20.658 26.235  27.057 1.00 57.43  ? 149 TYR F CA  1 
ATOM   9963  C  C   . TYR F  1 158 ? -21.861 27.122  26.786 1.00 64.87  ? 149 TYR F C   1 
ATOM   9964  O  O   . TYR F  1 158 ? -21.947 28.224  27.313 1.00 71.11  ? 149 TYR F O   1 
ATOM   9965  C  CB  . TYR F  1 158 ? -20.911 25.469  28.358 1.00 58.86  ? 149 TYR F CB  1 
ATOM   9966  C  CG  . TYR F  1 158 ? -20.049 24.241  28.569 1.00 66.34  ? 149 TYR F CG  1 
ATOM   9967  C  CD1 . TYR F  1 158 ? -20.375 23.027  27.971 1.00 64.02  ? 149 TYR F CD1 1 
ATOM   9968  C  CD2 . TYR F  1 158 ? -18.919 24.287  29.386 1.00 64.62  ? 149 TYR F CD2 1 
ATOM   9969  C  CE1 . TYR F  1 158 ? -19.595 21.901  28.165 1.00 67.81  ? 149 TYR F CE1 1 
ATOM   9970  C  CE2 . TYR F  1 158 ? -18.130 23.162  29.587 1.00 66.76  ? 149 TYR F CE2 1 
ATOM   9971  C  CZ  . TYR F  1 158 ? -18.473 21.970  28.974 1.00 70.71  ? 149 TYR F CZ  1 
ATOM   9972  O  OH  . TYR F  1 158 ? -17.704 20.842  29.170 1.00 60.83  ? 149 TYR F OH  1 
ATOM   9973  N  N   . GLY F  1 159 ? -22.808 26.640  25.993 1.00 61.96  ? 150 GLY F N   1 
ATOM   9974  C  CA  . GLY F  1 159 ? -24.020 27.399  25.743 1.00 63.00  ? 150 GLY F CA  1 
ATOM   9975  C  C   . GLY F  1 159 ? -25.167 26.952  26.625 1.00 61.03  ? 150 GLY F C   1 
ATOM   9976  O  O   . GLY F  1 159 ? -25.025 25.990  27.361 1.00 63.10  ? 150 GLY F O   1 
ATOM   9977  N  N   . GLY F  1 160 ? -26.307 27.628  26.527 1.00 56.46  ? 151 GLY F N   1 
ATOM   9978  C  CA  . GLY F  1 160 ? -27.450 27.368  27.385 1.00 58.94  ? 151 GLY F CA  1 
ATOM   9979  C  C   . GLY F  1 160 ? -27.990 25.952  27.319 1.00 67.37  ? 151 GLY F C   1 
ATOM   9980  O  O   . GLY F  1 160 ? -28.783 25.533  28.177 1.00 61.87  ? 151 GLY F O   1 
ATOM   9981  N  N   . TRP F  1 161 ? -27.577 25.219  26.286 1.00 66.28  ? 152 TRP F N   1 
ATOM   9982  C  CA  . TRP F  1 161 ? -28.058 23.861  26.058 1.00 67.63  ? 152 TRP F CA  1 
ATOM   9983  C  C   . TRP F  1 161 ? -27.195 22.815  26.733 1.00 67.09  ? 152 TRP F C   1 
ATOM   9984  O  O   . TRP F  1 161 ? -27.572 21.652  26.827 1.00 77.15  ? 152 TRP F O   1 
ATOM   9985  C  CB  . TRP F  1 161 ? -28.104 23.571  24.561 1.00 77.75  ? 152 TRP F CB  1 
ATOM   9986  C  CG  . TRP F  1 161 ? -29.272 24.176  23.848 1.00 81.07  ? 152 TRP F CG  1 
ATOM   9987  C  CD1 . TRP F  1 161 ? -30.441 24.610  24.400 1.00 77.04  ? 152 TRP F CD1 1 
ATOM   9988  C  CD2 . TRP F  1 161 ? -29.380 24.410  22.441 1.00 87.50  ? 152 TRP F CD2 1 
ATOM   9989  N  NE1 . TRP F  1 161 ? -31.270 25.101  23.423 1.00 81.62  ? 152 TRP F NE1 1 
ATOM   9990  C  CE2 . TRP F  1 161 ? -30.643 24.986  22.210 1.00 84.89  ? 152 TRP F CE2 1 
ATOM   9991  C  CE3 . TRP F  1 161 ? -28.530 24.180  21.350 1.00 91.45  ? 152 TRP F CE3 1 
ATOM   9992  C  CZ2 . TRP F  1 161 ? -31.079 25.339  20.936 1.00 89.50  ? 152 TRP F CZ2 1 
ATOM   9993  C  CZ3 . TRP F  1 161 ? -28.959 24.537  20.085 1.00 89.58  ? 152 TRP F CZ3 1 
ATOM   9994  C  CH2 . TRP F  1 161 ? -30.224 25.109  19.888 1.00 92.50  ? 152 TRP F CH2 1 
ATOM   9995  N  N   . GLU F  1 162 ? -26.033 23.236  27.200 1.00 62.26  ? 153 GLU F N   1 
ATOM   9996  C  CA  . GLU F  1 162 ? -25.143 22.367  27.951 1.00 67.74  ? 153 GLU F CA  1 
ATOM   9997  C  C   . GLU F  1 162 ? -25.007 22.726  29.434 1.00 68.06  ? 153 GLU F C   1 
ATOM   9998  O  O   . GLU F  1 162 ? -25.084 21.858  30.307 1.00 64.06  ? 153 GLU F O   1 
ATOM   9999  C  CB  . GLU F  1 162 ? -23.729 22.402  27.374 1.00 66.33  ? 153 GLU F CB  1 
ATOM   10000 C  CG  . GLU F  1 162 ? -23.631 21.877  25.953 1.00 68.86  ? 153 GLU F CG  1 
ATOM   10001 C  CD  . GLU F  1 162 ? -23.795 22.957  24.897 1.00 74.74  ? 153 GLU F CD  1 
ATOM   10002 O  OE1 . GLU F  1 162 ? -23.374 24.111  25.132 1.00 74.01  ? 153 GLU F OE1 1 
ATOM   10003 O  OE2 . GLU F  1 162 ? -24.336 22.648  23.816 1.00 77.46  ? 153 GLU F OE2 1 
ATOM   10004 N  N   . ILE F  1 163 ? -24.747 24.009  29.686 1.00 63.56  ? 154 ILE F N   1 
ATOM   10005 C  CA  . ILE F  1 163 ? -24.835 24.633  30.997 1.00 59.69  ? 154 ILE F CA  1 
ATOM   10006 C  C   . ILE F  1 163 ? -25.890 25.744  31.039 1.00 62.96  ? 154 ILE F C   1 
ATOM   10007 O  O   . ILE F  1 163 ? -25.807 26.740  30.308 1.00 56.89  ? 154 ILE F O   1 
ATOM   10008 C  CB  . ILE F  1 163 ? -23.479 25.239  31.402 1.00 65.99  ? 154 ILE F CB  1 
ATOM   10009 C  CG1 . ILE F  1 163 ? -22.453 24.132  31.626 1.00 63.97  ? 154 ILE F CG1 1 
ATOM   10010 C  CG2 . ILE F  1 163 ? -23.615 26.121  32.644 1.00 60.06  ? 154 ILE F CG2 1 
ATOM   10011 C  CD1 . ILE F  1 163 ? -21.057 24.650  31.874 1.00 70.02  ? 154 ILE F CD1 1 
ATOM   10012 N  N   . ASP F  1 164 ? -26.867 25.572  31.923 1.00 67.50  ? 155 ASP F N   1 
ATOM   10013 C  CA  . ASP F  1 164 ? -27.897 26.577  32.183 1.00 72.15  ? 155 ASP F CA  1 
ATOM   10014 C  C   . ASP F  1 164 ? -27.657 27.268  33.536 1.00 68.68  ? 155 ASP F C   1 
ATOM   10015 O  O   . ASP F  1 164 ? -27.670 26.605  34.571 1.00 65.73  ? 155 ASP F O   1 
ATOM   10016 C  CB  . ASP F  1 164 ? -29.269 25.893  32.187 1.00 72.75  ? 155 ASP F CB  1 
ATOM   10017 C  CG  . ASP F  1 164 ? -30.422 26.875  32.246 1.00 74.53  ? 155 ASP F CG  1 
ATOM   10018 O  OD1 . ASP F  1 164 ? -30.244 28.045  31.812 1.00 66.13  ? 155 ASP F OD1 1 
ATOM   10019 O  OD2 . ASP F  1 164 ? -31.506 26.453  32.714 1.00 68.88  ? 155 ASP F OD2 1 
ATOM   10020 N  N   . LEU F  1 165 ? -27.440 28.586  33.516 1.00 63.13  ? 156 LEU F N   1 
ATOM   10021 C  CA  . LEU F  1 165 ? -27.307 29.396  34.730 1.00 61.29  ? 156 LEU F CA  1 
ATOM   10022 C  C   . LEU F  1 165 ? -28.646 29.811  35.323 1.00 67.14  ? 156 LEU F C   1 
ATOM   10023 O  O   . LEU F  1 165 ? -29.541 30.247  34.612 1.00 70.11  ? 156 LEU F O   1 
ATOM   10024 C  CB  . LEU F  1 165 ? -26.525 30.673  34.449 1.00 58.19  ? 156 LEU F CB  1 
ATOM   10025 C  CG  . LEU F  1 165 ? -25.023 30.545  34.260 1.00 63.25  ? 156 LEU F CG  1 
ATOM   10026 C  CD1 . LEU F  1 165 ? -24.384 31.916  34.256 1.00 57.63  ? 156 LEU F CD1 1 
ATOM   10027 C  CD2 . LEU F  1 165 ? -24.445 29.691  35.363 1.00 61.17  ? 156 LEU F CD2 1 
ATOM   10028 N  N   . LYS F  1 166 ? -28.780 29.684  36.636 1.00 70.06  ? 157 LYS F N   1 
ATOM   10029 C  CA  . LYS F  1 166 ? -29.916 30.263  37.331 1.00 74.60  ? 157 LYS F CA  1 
ATOM   10030 C  C   . LYS F  1 166 ? -29.369 31.062  38.493 1.00 77.37  ? 157 LYS F C   1 
ATOM   10031 O  O   . LYS F  1 166 ? -28.161 31.087  38.707 1.00 76.29  ? 157 LYS F O   1 
ATOM   10032 C  CB  . LYS F  1 166 ? -30.859 29.175  37.834 1.00 72.11  ? 157 LYS F CB  1 
ATOM   10033 C  CG  . LYS F  1 166 ? -31.279 28.184  36.763 1.00 75.23  ? 157 LYS F CG  1 
ATOM   10034 C  CD  . LYS F  1 166 ? -32.736 28.322  36.366 1.00 75.50  ? 157 LYS F CD  1 
ATOM   10035 C  CE  . LYS F  1 166 ? -33.303 26.975  35.899 1.00 87.10  ? 157 LYS F CE  1 
ATOM   10036 N  NZ  . LYS F  1 166 ? -33.536 26.001  37.024 1.00 85.43  ? 157 LYS F NZ  1 
ATOM   10037 N  N   . THR F  1 167 ? -30.251 31.718  39.236 1.00 80.20  ? 158 THR F N   1 
ATOM   10038 C  CA  . THR F  1 167 ? -29.871 32.353  40.490 1.00 77.90  ? 158 THR F CA  1 
ATOM   10039 C  C   . THR F  1 167 ? -30.973 32.040  41.485 1.00 82.51  ? 158 THR F C   1 
ATOM   10040 O  O   . THR F  1 167 ? -32.068 31.646  41.081 1.00 80.43  ? 158 THR F O   1 
ATOM   10041 C  CB  . THR F  1 167 ? -29.689 33.883  40.348 1.00 71.99  ? 158 THR F CB  1 
ATOM   10042 O  OG1 . THR F  1 167 ? -30.882 34.472  39.820 1.00 79.38  ? 158 THR F OG1 1 
ATOM   10043 C  CG2 . THR F  1 167 ? -28.527 34.208  39.428 1.00 63.34  ? 158 THR F CG2 1 
ATOM   10044 N  N   . ASP F  1 168 ? -30.682 32.184  42.776 1.00 86.51  ? 159 ASP F N   1 
ATOM   10045 C  CA  . ASP F  1 168 ? -31.706 32.031  43.820 1.00 95.18  ? 159 ASP F CA  1 
ATOM   10046 C  C   . ASP F  1 168 ? -32.580 33.292  43.948 1.00 90.59  ? 159 ASP F C   1 
ATOM   10047 O  O   . ASP F  1 168 ? -33.803 33.208  44.090 1.00 80.41  ? 159 ASP F O   1 
ATOM   10048 C  CB  . ASP F  1 168 ? -31.060 31.716  45.178 1.00 95.05  ? 159 ASP F CB  1 
ATOM   10049 C  CG  . ASP F  1 168 ? -29.991 30.635  45.088 1.00 102.25 ? 159 ASP F CG  1 
ATOM   10050 O  OD1 . ASP F  1 168 ? -28.923 30.789  45.726 1.00 95.94  ? 159 ASP F OD1 1 
ATOM   10051 O  OD2 . ASP F  1 168 ? -30.215 29.629  44.381 1.00 106.82 ? 159 ASP F OD2 1 
ATOM   10052 N  N   . THR F  1 169 ? -31.928 34.451  43.885 1.00 80.89  ? 160 THR F N   1 
ATOM   10053 C  CA  . THR F  1 169 ? -32.559 35.740  44.127 1.00 82.01  ? 160 THR F CA  1 
ATOM   10054 C  C   . THR F  1 169 ? -31.871 36.810  43.292 1.00 84.19  ? 160 THR F C   1 
ATOM   10055 O  O   . THR F  1 169 ? -30.764 36.599  42.800 1.00 87.06  ? 160 THR F O   1 
ATOM   10056 C  CB  . THR F  1 169 ? -32.441 36.119  45.613 1.00 83.57  ? 160 THR F CB  1 
ATOM   10057 O  OG1 . THR F  1 169 ? -33.212 35.198  46.392 1.00 85.89  ? 160 THR F OG1 1 
ATOM   10058 C  CG2 . THR F  1 169 ? -32.941 37.545  45.873 1.00 80.49  ? 160 THR F CG2 1 
ATOM   10059 N  N   . ASP F  1 170 ? -32.524 37.955  43.124 1.00 78.37  ? 161 ASP F N   1 
ATOM   10060 C  CA  . ASP F  1 170 ? -31.929 39.057  42.383 1.00 76.40  ? 161 ASP F CA  1 
ATOM   10061 C  C   . ASP F  1 170 ? -31.162 40.011  43.295 1.00 79.65  ? 161 ASP F C   1 
ATOM   10062 O  O   . ASP F  1 170 ? -30.614 41.025  42.850 1.00 79.72  ? 161 ASP F O   1 
ATOM   10063 C  CB  . ASP F  1 170 ? -32.998 39.799  41.583 1.00 81.00  ? 161 ASP F CB  1 
ATOM   10064 C  CG  . ASP F  1 170 ? -33.356 39.079  40.291 1.00 97.62  ? 161 ASP F CG  1 
ATOM   10065 O  OD1 . ASP F  1 170 ? -33.199 37.828  40.265 1.00 95.67  ? 161 ASP F OD1 1 
ATOM   10066 O  OD2 . ASP F  1 170 ? -33.776 39.757  39.310 1.00 92.61  ? 161 ASP F OD2 1 
ATOM   10067 N  N   . GLN F  1 171 ? -31.117 39.678  44.576 1.00 77.88  ? 162 GLN F N   1 
ATOM   10068 C  CA  . GLN F  1 171 ? -30.414 40.516  45.530 1.00 81.11  ? 162 GLN F CA  1 
ATOM   10069 C  C   . GLN F  1 171 ? -29.069 39.918  45.949 1.00 78.70  ? 162 GLN F C   1 
ATOM   10070 O  O   . GLN F  1 171 ? -29.001 38.848  46.567 1.00 73.14  ? 162 GLN F O   1 
ATOM   10071 C  CB  . GLN F  1 171 ? -31.302 40.823  46.742 1.00 86.66  ? 162 GLN F CB  1 
ATOM   10072 C  CG  . GLN F  1 171 ? -32.425 41.826  46.444 1.00 91.08  ? 162 GLN F CG  1 
ATOM   10073 C  CD  . GLN F  1 171 ? -31.978 43.291  46.537 1.00 90.89  ? 162 GLN F CD  1 
ATOM   10074 O  OE1 . GLN F  1 171 ? -31.654 43.925  45.530 1.00 89.58  ? 162 GLN F OE1 1 
ATOM   10075 N  NE2 . GLN F  1 171 ? -31.984 43.834  47.750 1.00 89.70  ? 162 GLN F NE2 1 
ATOM   10076 N  N   . VAL F  1 172 ? -28.000 40.616  45.582 1.00 72.85  ? 163 VAL F N   1 
ATOM   10077 C  CA  . VAL F  1 172 ? -26.676 40.284  46.068 1.00 64.77  ? 163 VAL F CA  1 
ATOM   10078 C  C   . VAL F  1 172 ? -26.706 40.376  47.583 1.00 72.26  ? 163 VAL F C   1 
ATOM   10079 O  O   . VAL F  1 172 ? -27.387 41.242  48.138 1.00 70.99  ? 163 VAL F O   1 
ATOM   10080 C  CB  . VAL F  1 172 ? -25.642 41.269  45.531 1.00 60.40  ? 163 VAL F CB  1 
ATOM   10081 C  CG1 . VAL F  1 172 ? -24.270 41.003  46.131 1.00 63.53  ? 163 VAL F CG1 1 
ATOM   10082 C  CG2 . VAL F  1 172 ? -25.593 41.184  44.027 1.00 64.32  ? 163 VAL F CG2 1 
ATOM   10083 N  N   . ASP F  1 173 ? -25.953 39.497  48.243 1.00 74.43  ? 164 ASP F N   1 
ATOM   10084 C  CA  . ASP F  1 173 ? -25.923 39.418  49.699 1.00 66.62  ? 164 ASP F CA  1 
ATOM   10085 C  C   . ASP F  1 173 ? -24.862 40.380  50.226 1.00 70.09  ? 164 ASP F C   1 
ATOM   10086 O  O   . ASP F  1 173 ? -23.674 40.243  49.920 1.00 67.87  ? 164 ASP F O   1 
ATOM   10087 C  CB  . ASP F  1 173 ? -25.611 37.978  50.127 1.00 61.97  ? 164 ASP F CB  1 
ATOM   10088 C  CG  . ASP F  1 173 ? -25.642 37.788  51.633 1.00 75.49  ? 164 ASP F CG  1 
ATOM   10089 O  OD1 . ASP F  1 173 ? -26.175 38.685  52.325 1.00 81.32  ? 164 ASP F OD1 1 
ATOM   10090 O  OD2 . ASP F  1 173 ? -25.145 36.743  52.121 1.00 63.17  ? 164 ASP F OD2 1 
ATOM   10091 N  N   . LEU F  1 174 ? -25.327 41.391  50.963 1.00 70.94  ? 165 LEU F N   1 
ATOM   10092 C  CA  . LEU F  1 174 ? -24.482 42.433  51.551 1.00 65.36  ? 165 LEU F CA  1 
ATOM   10093 C  C   . LEU F  1 174 ? -24.151 42.253  53.032 1.00 65.20  ? 165 LEU F C   1 
ATOM   10094 O  O   . LEU F  1 174 ? -23.459 43.083  53.624 1.00 61.31  ? 165 LEU F O   1 
ATOM   10095 C  CB  . LEU F  1 174 ? -25.116 43.802  51.317 1.00 58.27  ? 165 LEU F CB  1 
ATOM   10096 C  CG  . LEU F  1 174 ? -25.424 44.099  49.852 1.00 65.56  ? 165 LEU F CG  1 
ATOM   10097 C  CD1 . LEU F  1 174 ? -26.336 45.303  49.724 1.00 63.34  ? 165 LEU F CD1 1 
ATOM   10098 C  CD2 . LEU F  1 174 ? -24.132 44.297  49.074 1.00 63.95  ? 165 LEU F CD2 1 
ATOM   10099 N  N   . SER F  1 175 ? -24.671 41.194  53.640 1.00 65.81  ? 166 SER F N   1 
ATOM   10100 C  CA  . SER F  1 175 ? -24.556 41.045  55.089 1.00 68.93  ? 166 SER F CA  1 
ATOM   10101 C  C   . SER F  1 175 ? -23.131 40.774  55.595 1.00 61.39  ? 166 SER F C   1 
ATOM   10102 O  O   . SER F  1 175 ? -22.880 40.856  56.784 1.00 59.72  ? 166 SER F O   1 
ATOM   10103 C  CB  . SER F  1 175 ? -25.536 39.985  55.617 1.00 71.62  ? 166 SER F CB  1 
ATOM   10104 O  OG  . SER F  1 175 ? -25.059 38.671  55.394 1.00 62.78  ? 166 SER F OG  1 
ATOM   10105 N  N   . SER F  1 176 ? -22.218 40.388  54.713 1.00 70.12  ? 167 SER F N   1 
ATOM   10106 C  CA  . SER F  1 176 ? -20.798 40.320  55.067 1.00 62.53  ? 167 SER F CA  1 
ATOM   10107 C  C   . SER F  1 176 ? -19.950 41.523  54.622 1.00 63.76  ? 167 SER F C   1 
ATOM   10108 O  O   . SER F  1 176 ? -18.733 41.510  54.818 1.00 63.70  ? 167 SER F O   1 
ATOM   10109 C  CB  . SER F  1 176 ? -20.155 39.017  54.579 1.00 66.18  ? 167 SER F CB  1 
ATOM   10110 O  OG  . SER F  1 176 ? -20.707 37.891  55.229 1.00 63.28  ? 167 SER F OG  1 
ATOM   10111 N  N   . TYR F  1 177 ? -20.568 42.528  53.996 1.00 60.06  ? 168 TYR F N   1 
ATOM   10112 C  CA  . TYR F  1 177 ? -19.822 43.672  53.462 1.00 55.92  ? 168 TYR F CA  1 
ATOM   10113 C  C   . TYR F  1 177 ? -19.092 44.442  54.547 1.00 58.98  ? 168 TYR F C   1 
ATOM   10114 O  O   . TYR F  1 177 ? -19.604 44.620  55.653 1.00 63.03  ? 168 TYR F O   1 
ATOM   10115 C  CB  . TYR F  1 177 ? -20.712 44.643  52.667 1.00 56.77  ? 168 TYR F CB  1 
ATOM   10116 C  CG  . TYR F  1 177 ? -19.893 45.651  51.875 1.00 54.30  ? 168 TYR F CG  1 
ATOM   10117 C  CD1 . TYR F  1 177 ? -19.356 45.319  50.636 1.00 59.09  ? 168 TYR F CD1 1 
ATOM   10118 C  CD2 . TYR F  1 177 ? -19.628 46.916  52.378 1.00 57.05  ? 168 TYR F CD2 1 
ATOM   10119 C  CE1 . TYR F  1 177 ? -18.584 46.221  49.915 1.00 57.66  ? 168 TYR F CE1 1 
ATOM   10120 C  CE2 . TYR F  1 177 ? -18.857 47.831  51.661 1.00 61.59  ? 168 TYR F CE2 1 
ATOM   10121 C  CZ  . TYR F  1 177 ? -18.339 47.476  50.431 1.00 57.28  ? 168 TYR F CZ  1 
ATOM   10122 O  OH  . TYR F  1 177 ? -17.577 48.373  49.720 1.00 51.54  ? 168 TYR F OH  1 
ATOM   10123 N  N   . TYR F  1 178 ? -17.914 44.947  54.207 1.00 51.82  ? 169 TYR F N   1 
ATOM   10124 C  CA  . TYR F  1 178 ? -17.049 45.552  55.198 1.00 60.73  ? 169 TYR F CA  1 
ATOM   10125 C  C   . TYR F  1 178 ? -17.505 46.982  55.548 1.00 67.20  ? 169 TYR F C   1 
ATOM   10126 O  O   . TYR F  1 178 ? -17.461 47.901  54.715 1.00 66.06  ? 169 TYR F O   1 
ATOM   10127 C  CB  . TYR F  1 178 ? -15.632 45.545  54.641 1.00 56.36  ? 169 TYR F CB  1 
ATOM   10128 C  CG  . TYR F  1 178 ? -14.609 46.174  55.534 1.00 61.05  ? 169 TYR F CG  1 
ATOM   10129 C  CD1 . TYR F  1 178 ? -14.545 45.843  56.880 1.00 59.06  ? 169 TYR F CD1 1 
ATOM   10130 C  CD2 . TYR F  1 178 ? -13.689 47.082  55.027 1.00 58.02  ? 169 TYR F CD2 1 
ATOM   10131 C  CE1 . TYR F  1 178 ? -13.602 46.399  57.701 1.00 58.65  ? 169 TYR F CE1 1 
ATOM   10132 C  CE2 . TYR F  1 178 ? -12.741 47.649  55.839 1.00 59.63  ? 169 TYR F CE2 1 
ATOM   10133 C  CZ  . TYR F  1 178 ? -12.701 47.303  57.179 1.00 61.24  ? 169 TYR F CZ  1 
ATOM   10134 O  OH  . TYR F  1 178 ? -11.758 47.859  58.009 1.00 66.30  ? 169 TYR F OH  1 
ATOM   10135 N  N   . ALA F  1 179 ? -17.884 47.180  56.809 1.00 61.21  ? 170 ALA F N   1 
ATOM   10136 C  CA  . ALA F  1 179 ? -18.545 48.416  57.205 1.00 63.21  ? 170 ALA F CA  1 
ATOM   10137 C  C   . ALA F  1 179 ? -17.591 49.588  57.129 1.00 63.42  ? 170 ALA F C   1 
ATOM   10138 O  O   . ALA F  1 179 ? -18.017 50.739  57.072 1.00 62.40  ? 170 ALA F O   1 
ATOM   10139 C  CB  . ALA F  1 179 ? -19.132 48.294  58.598 1.00 53.18  ? 170 ALA F CB  1 
ATOM   10140 N  N   . SER F  1 180 ? -16.298 49.291  57.167 1.00 58.11  ? 171 SER F N   1 
ATOM   10141 C  CA  . SER F  1 180 ? -15.267 50.326  57.125 1.00 64.51  ? 171 SER F CA  1 
ATOM   10142 C  C   . SER F  1 180 ? -14.638 50.605  55.761 1.00 64.98  ? 171 SER F C   1 
ATOM   10143 O  O   . SER F  1 180 ? -13.668 51.355  55.672 1.00 62.45  ? 171 SER F O   1 
ATOM   10144 C  CB  . SER F  1 180 ? -14.213 50.143  58.222 1.00 70.68  ? 171 SER F CB  1 
ATOM   10145 O  OG  . SER F  1 180 ? -14.781 50.318  59.520 1.00 68.69  ? 171 SER F OG  1 
ATOM   10146 N  N   . SER F  1 181 ? -15.166 49.984  54.712 1.00 58.58  ? 172 SER F N   1 
ATOM   10147 C  CA  . SER F  1 181 ? -14.639 50.189  53.363 1.00 64.66  ? 172 SER F CA  1 
ATOM   10148 C  C   . SER F  1 181 ? -14.583 51.677  52.966 1.00 63.41  ? 172 SER F C   1 
ATOM   10149 O  O   . SER F  1 181 ? -15.352 52.487  53.471 1.00 63.69  ? 172 SER F O   1 
ATOM   10150 C  CB  . SER F  1 181 ? -15.487 49.419  52.344 1.00 60.95  ? 172 SER F CB  1 
ATOM   10151 O  OG  . SER F  1 181 ? -15.058 49.677  51.015 1.00 55.53  ? 172 SER F OG  1 
ATOM   10152 N  N   . LYS F  1 182 ? -13.628 52.052  52.119 1.00 58.13  ? 173 LYS F N   1 
ATOM   10153 C  CA  . LYS F  1 182 ? -13.651 53.391  51.542 1.00 59.55  ? 173 LYS F CA  1 
ATOM   10154 C  C   . LYS F  1 182 ? -14.968 53.573  50.824 1.00 62.09  ? 173 LYS F C   1 
ATOM   10155 O  O   . LYS F  1 182 ? -15.393 54.694  50.568 1.00 66.96  ? 173 LYS F O   1 
ATOM   10156 C  CB  . LYS F  1 182 ? -12.538 53.590  50.521 1.00 56.46  ? 173 LYS F CB  1 
ATOM   10157 C  CG  . LYS F  1 182 ? -11.171 53.279  51.034 1.00 61.99  ? 173 LYS F CG  1 
ATOM   10158 C  CD  . LYS F  1 182 ? -10.786 54.248  52.105 1.00 60.62  ? 173 LYS F CD  1 
ATOM   10159 C  CE  . LYS F  1 182 ? -10.684 55.635  51.550 1.00 57.46  ? 173 LYS F CE  1 
ATOM   10160 N  NZ  . LYS F  1 182 ? -9.800  56.437  52.426 1.00 69.71  ? 173 LYS F NZ  1 
ATOM   10161 N  N   . TYR F  1 183 ? -15.615 52.465  50.485 1.00 58.30  ? 174 TYR F N   1 
ATOM   10162 C  CA  . TYR F  1 183 ? -16.795 52.547  49.649 1.00 58.79  ? 174 TYR F CA  1 
ATOM   10163 C  C   . TYR F  1 183 ? -18.015 51.938  50.317 1.00 61.50  ? 174 TYR F C   1 
ATOM   10164 O  O   . TYR F  1 183 ? -17.918 50.991  51.081 1.00 58.73  ? 174 TYR F O   1 
ATOM   10165 C  CB  . TYR F  1 183 ? -16.525 51.958  48.248 1.00 59.24  ? 174 TYR F CB  1 
ATOM   10166 C  CG  . TYR F  1 183 ? -15.375 52.642  47.511 1.00 60.59  ? 174 TYR F CG  1 
ATOM   10167 C  CD1 . TYR F  1 183 ? -15.573 53.820  46.795 1.00 58.78  ? 174 TYR F CD1 1 
ATOM   10168 C  CD2 . TYR F  1 183 ? -14.090 52.115  47.551 1.00 57.32  ? 174 TYR F CD2 1 
ATOM   10169 C  CE1 . TYR F  1 183 ? -14.516 54.448  46.147 1.00 56.75  ? 174 TYR F CE1 1 
ATOM   10170 C  CE2 . TYR F  1 183 ? -13.034 52.733  46.906 1.00 55.51  ? 174 TYR F CE2 1 
ATOM   10171 C  CZ  . TYR F  1 183 ? -13.247 53.897  46.204 1.00 60.24  ? 174 TYR F CZ  1 
ATOM   10172 O  OH  . TYR F  1 183 ? -12.183 54.503  45.556 1.00 54.38  ? 174 TYR F OH  1 
ATOM   10173 N  N   . GLU F  1 184 ? -19.164 52.525  50.010 1.00 70.73  ? 175 GLU F N   1 
ATOM   10174 C  CA  . GLU F  1 184 ? -20.458 52.156  50.570 1.00 73.41  ? 175 GLU F CA  1 
ATOM   10175 C  C   . GLU F  1 184 ? -21.363 51.604  49.444 1.00 69.02  ? 175 GLU F C   1 
ATOM   10176 O  O   . GLU F  1 184 ? -21.339 52.089  48.313 1.00 65.76  ? 175 GLU F O   1 
ATOM   10177 C  CB  . GLU F  1 184 ? -21.054 53.413  51.218 1.00 78.02  ? 175 GLU F CB  1 
ATOM   10178 C  CG  . GLU F  1 184 ? -22.383 53.282  51.939 1.00 84.68  ? 175 GLU F CG  1 
ATOM   10179 C  CD  . GLU F  1 184 ? -22.989 54.657  52.278 1.00 104.65 ? 175 GLU F CD  1 
ATOM   10180 O  OE1 . GLU F  1 184 ? -22.236 55.669  52.317 1.00 93.04  ? 175 GLU F OE1 1 
ATOM   10181 O  OE2 . GLU F  1 184 ? -24.224 54.726  52.488 1.00 109.13 ? 175 GLU F OE2 1 
ATOM   10182 N  N   . ILE F  1 185 ? -22.143 50.569  49.735 1.00 67.23  ? 176 ILE F N   1 
ATOM   10183 C  CA  . ILE F  1 185 ? -22.994 49.978  48.698 1.00 71.35  ? 176 ILE F CA  1 
ATOM   10184 C  C   . ILE F  1 185 ? -24.403 50.576  48.747 1.00 65.55  ? 176 ILE F C   1 
ATOM   10185 O  O   . ILE F  1 185 ? -25.157 50.334  49.686 1.00 66.18  ? 176 ILE F O   1 
ATOM   10186 C  CB  . ILE F  1 185 ? -23.071 48.400  48.815 1.00 66.70  ? 176 ILE F CB  1 
ATOM   10187 C  CG1 . ILE F  1 185 ? -21.698 47.755  48.637 1.00 54.52  ? 176 ILE F CG1 1 
ATOM   10188 C  CG2 . ILE F  1 185 ? -24.040 47.808  47.810 1.00 56.52  ? 176 ILE F CG2 1 
ATOM   10189 C  CD1 . ILE F  1 185 ? -20.883 48.370  47.552 1.00 56.51  ? 176 ILE F CD1 1 
ATOM   10190 N  N   . LEU F  1 186 ? -24.763 51.347  47.730 1.00 60.91  ? 177 LEU F N   1 
ATOM   10191 C  CA  . LEU F  1 186 ? -26.141 51.811  47.585 1.00 66.45  ? 177 LEU F CA  1 
ATOM   10192 C  C   . LEU F  1 186 ? -27.080 50.651  47.199 1.00 73.29  ? 177 LEU F C   1 
ATOM   10193 O  O   . LEU F  1 186 ? -28.095 50.429  47.864 1.00 73.39  ? 177 LEU F O   1 
ATOM   10194 C  CB  . LEU F  1 186 ? -26.211 52.957  46.571 1.00 60.09  ? 177 LEU F CB  1 
ATOM   10195 C  CG  . LEU F  1 186 ? -25.177 54.046  46.870 1.00 65.11  ? 177 LEU F CG  1 
ATOM   10196 C  CD1 . LEU F  1 186 ? -24.897 54.927  45.669 1.00 61.65  ? 177 LEU F CD1 1 
ATOM   10197 C  CD2 . LEU F  1 186 ? -25.607 54.878  48.068 1.00 69.58  ? 177 LEU F CD2 1 
ATOM   10198 N  N   . SER F  1 187 ? -26.747 49.922  46.128 1.00 75.26  ? 178 SER F N   1 
ATOM   10199 C  CA  . SER F  1 187 ? -27.425 48.656  45.807 1.00 73.82  ? 178 SER F CA  1 
ATOM   10200 C  C   . SER F  1 187 ? -26.567 47.685  44.986 1.00 72.08  ? 178 SER F C   1 
ATOM   10201 O  O   . SER F  1 187 ? -25.681 48.095  44.229 1.00 67.86  ? 178 SER F O   1 
ATOM   10202 C  CB  . SER F  1 187 ? -28.745 48.907  45.081 1.00 75.46  ? 178 SER F CB  1 
ATOM   10203 O  OG  . SER F  1 187 ? -28.522 49.476  43.803 1.00 81.33  ? 178 SER F OG  1 
ATOM   10204 N  N   . ALA F  1 188 ? -26.850 46.394  45.137 1.00 68.37  ? 179 ALA F N   1 
ATOM   10205 C  CA  . ALA F  1 188 ? -26.182 45.364  44.356 1.00 59.22  ? 179 ALA F CA  1 
ATOM   10206 C  C   . ALA F  1 188 ? -27.208 44.333  43.945 1.00 58.44  ? 179 ALA F C   1 
ATOM   10207 O  O   . ALA F  1 188 ? -27.908 43.784  44.784 1.00 64.21  ? 179 ALA F O   1 
ATOM   10208 C  CB  . ALA F  1 188 ? -25.082 44.720  45.158 1.00 59.48  ? 179 ALA F CB  1 
ATOM   10209 N  N   . THR F  1 189 ? -27.282 44.067  42.646 1.00 66.52  ? 180 THR F N   1 
ATOM   10210 C  CA  . THR F  1 189 ? -28.259 43.129  42.087 1.00 75.11  ? 180 THR F CA  1 
ATOM   10211 C  C   . THR F  1 189 ? -27.587 42.071  41.213 1.00 66.62  ? 180 THR F C   1 
ATOM   10212 O  O   . THR F  1 189 ? -26.618 42.357  40.511 1.00 63.41  ? 180 THR F O   1 
ATOM   10213 C  CB  . THR F  1 189 ? -29.333 43.860  41.246 1.00 70.98  ? 180 THR F CB  1 
ATOM   10214 O  OG1 . THR F  1 189 ? -28.693 44.743  40.317 1.00 71.23  ? 180 THR F OG1 1 
ATOM   10215 C  CG2 . THR F  1 189 ? -30.235 44.680  42.136 1.00 70.54  ? 180 THR F CG2 1 
ATOM   10216 N  N   . GLN F  1 190 ? -28.101 40.848  41.270 1.00 64.32  ? 181 GLN F N   1 
ATOM   10217 C  CA  . GLN F  1 190 ? -27.656 39.794  40.365 1.00 63.09  ? 181 GLN F CA  1 
ATOM   10218 C  C   . GLN F  1 190 ? -28.810 39.271  39.484 1.00 66.11  ? 181 GLN F C   1 
ATOM   10219 O  O   . GLN F  1 190 ? -29.725 38.594  39.965 1.00 64.11  ? 181 GLN F O   1 
ATOM   10220 C  CB  . GLN F  1 190 ? -27.004 38.662  41.161 1.00 61.40  ? 181 GLN F CB  1 
ATOM   10221 C  CG  . GLN F  1 190 ? -27.766 38.274  42.412 1.00 67.56  ? 181 GLN F CG  1 
ATOM   10222 C  CD  . GLN F  1 190 ? -27.103 37.153  43.189 1.00 63.40  ? 181 GLN F CD  1 
ATOM   10223 O  OE1 . GLN F  1 190 ? -25.889 37.139  43.382 1.00 62.28  ? 181 GLN F OE1 1 
ATOM   10224 N  NE2 . GLN F  1 190 ? -27.903 36.208  43.636 1.00 61.80  ? 181 GLN F NE2 1 
ATOM   10225 N  N   . THR F  1 191 ? -28.736 39.568  38.185 1.00 63.40  ? 182 THR F N   1 
ATOM   10226 C  CA  . THR F  1 191 ? -29.835 39.288  37.260 1.00 70.27  ? 182 THR F CA  1 
ATOM   10227 C  C   . THR F  1 191 ? -29.458 38.416  36.060 1.00 64.70  ? 182 THR F C   1 
ATOM   10228 O  O   . THR F  1 191 ? -28.560 38.747  35.291 1.00 63.71  ? 182 THR F O   1 
ATOM   10229 C  CB  . THR F  1 191 ? -30.450 40.583  36.710 1.00 69.10  ? 182 THR F CB  1 
ATOM   10230 O  OG1 . THR F  1 191 ? -30.763 41.463  37.791 1.00 64.80  ? 182 THR F OG1 1 
ATOM   10231 C  CG2 . THR F  1 191 ? -31.715 40.262  35.940 1.00 72.21  ? 182 THR F CG2 1 
ATOM   10232 N  N   . ARG F  1 192 ? -30.178 37.317  35.893 1.00 61.46  ? 183 ARG F N   1 
ATOM   10233 C  CA  . ARG F  1 192 ? -29.962 36.442  34.760 1.00 61.53  ? 183 ARG F CA  1 
ATOM   10234 C  C   . ARG F  1 192 ? -30.475 37.052  33.464 1.00 64.63  ? 183 ARG F C   1 
ATOM   10235 O  O   . ARG F  1 192 ? -31.589 37.557  33.411 1.00 73.76  ? 183 ARG F O   1 
ATOM   10236 C  CB  . ARG F  1 192 ? -30.665 35.120  34.999 1.00 58.95  ? 183 ARG F CB  1 
ATOM   10237 C  CG  . ARG F  1 192 ? -30.558 34.163  33.850 1.00 69.59  ? 183 ARG F CG  1 
ATOM   10238 C  CD  . ARG F  1 192 ? -31.312 32.890  34.148 1.00 68.42  ? 183 ARG F CD  1 
ATOM   10239 N  NE  . ARG F  1 192 ? -31.170 31.921  33.070 1.00 72.53  ? 183 ARG F NE  1 
ATOM   10240 C  CZ  . ARG F  1 192 ? -31.958 31.868  32.004 1.00 69.95  ? 183 ARG F CZ  1 
ATOM   10241 N  NH1 . ARG F  1 192 ? -32.953 32.737  31.873 1.00 65.47  ? 183 ARG F NH1 1 
ATOM   10242 N  NH2 . ARG F  1 192 ? -31.750 30.940  31.077 1.00 62.23  ? 183 ARG F NH2 1 
ATOM   10243 N  N   . SER F  1 193 ? -29.665 36.999  32.415 1.00 65.95  ? 184 SER F N   1 
ATOM   10244 C  CA  . SER F  1 193 ? -30.116 37.422  31.091 1.00 73.70  ? 184 SER F CA  1 
ATOM   10245 C  C   . SER F  1 193 ? -29.794 36.358  30.037 1.00 69.81  ? 184 SER F C   1 
ATOM   10246 O  O   . SER F  1 193 ? -28.800 35.650  30.155 1.00 68.71  ? 184 SER F O   1 
ATOM   10247 C  CB  . SER F  1 193 ? -29.501 38.777  30.710 1.00 73.55  ? 184 SER F CB  1 
ATOM   10248 O  OG  . SER F  1 193 ? -28.332 38.631  29.922 1.00 78.02  ? 184 SER F OG  1 
ATOM   10249 N  N   . GLU F  1 194 ? -30.644 36.225  29.023 1.00 74.80  ? 185 GLU F N   1 
ATOM   10250 C  CA  . GLU F  1 194 ? -30.333 35.335  27.905 1.00 72.82  ? 185 GLU F CA  1 
ATOM   10251 C  C   . GLU F  1 194 ? -29.904 36.128  26.696 1.00 76.93  ? 185 GLU F C   1 
ATOM   10252 O  O   . GLU F  1 194 ? -30.448 37.190  26.393 1.00 75.67  ? 185 GLU F O   1 
ATOM   10253 C  CB  . GLU F  1 194 ? -31.497 34.412  27.539 1.00 67.23  ? 185 GLU F CB  1 
ATOM   10254 C  CG  . GLU F  1 194 ? -31.606 33.196  28.432 1.00 72.12  ? 185 GLU F CG  1 
ATOM   10255 C  CD  . GLU F  1 194 ? -32.326 32.054  27.770 1.00 77.52  ? 185 GLU F CD  1 
ATOM   10256 O  OE1 . GLU F  1 194 ? -32.562 31.014  28.418 1.00 81.49  ? 185 GLU F OE1 1 
ATOM   10257 O  OE2 . GLU F  1 194 ? -32.655 32.197  26.584 1.00 92.89  ? 185 GLU F OE2 1 
ATOM   10258 N  N   . ARG F  1 195 ? -28.900 35.607  26.015 1.00 78.68  ? 186 ARG F N   1 
ATOM   10259 C  CA  . ARG F  1 195 ? -28.407 36.233  24.810 1.00 79.12  ? 186 ARG F CA  1 
ATOM   10260 C  C   . ARG F  1 195 ? -28.589 35.283  23.637 1.00 79.93  ? 186 ARG F C   1 
ATOM   10261 O  O   . ARG F  1 195 ? -28.407 34.076  23.763 1.00 79.82  ? 186 ARG F O   1 
ATOM   10262 C  CB  . ARG F  1 195 ? -26.933 36.602  24.966 1.00 82.84  ? 186 ARG F CB  1 
ATOM   10263 C  CG  . ARG F  1 195 ? -26.692 38.045  25.313 1.00 86.09  ? 186 ARG F CG  1 
ATOM   10264 C  CD  . ARG F  1 195 ? -25.418 38.526  24.641 1.00 103.37 ? 186 ARG F CD  1 
ATOM   10265 N  NE  . ARG F  1 195 ? -25.448 38.303  23.194 1.00 113.91 ? 186 ARG F NE  1 
ATOM   10266 C  CZ  . ARG F  1 195 ? -24.492 38.695  22.352 1.00 125.28 ? 186 ARG F CZ  1 
ATOM   10267 N  NH1 . ARG F  1 195 ? -23.417 39.336  22.811 1.00 116.17 ? 186 ARG F NH1 1 
ATOM   10268 N  NH2 . ARG F  1 195 ? -24.613 38.448  21.048 1.00 118.20 ? 186 ARG F NH2 1 
ATOM   10269 N  N   . PHE F  1 196 ? -28.954 35.824  22.488 1.00 89.77  ? 187 PHE F N   1 
ATOM   10270 C  CA  . PHE F  1 196 ? -29.011 35.006  21.294 1.00 78.86  ? 187 PHE F CA  1 
ATOM   10271 C  C   . PHE F  1 196 ? -28.038 35.511  20.238 1.00 89.52  ? 187 PHE F C   1 
ATOM   10272 O  O   . PHE F  1 196 ? -27.904 36.715  20.011 1.00 97.28  ? 187 PHE F O   1 
ATOM   10273 C  CB  . PHE F  1 196 ? -30.431 34.944  20.762 1.00 69.45  ? 187 PHE F CB  1 
ATOM   10274 C  CG  . PHE F  1 196 ? -31.336 34.054  21.561 1.00 65.77  ? 187 PHE F CG  1 
ATOM   10275 C  CD1 . PHE F  1 196 ? -31.345 32.685  21.343 1.00 68.38  ? 187 PHE F CD1 1 
ATOM   10276 C  CD2 . PHE F  1 196 ? -32.188 34.585  22.510 1.00 62.95  ? 187 PHE F CD2 1 
ATOM   10277 C  CE1 . PHE F  1 196 ? -32.180 31.862  22.064 1.00 68.98  ? 187 PHE F CE1 1 
ATOM   10278 C  CE2 . PHE F  1 196 ? -33.029 33.765  23.239 1.00 69.85  ? 187 PHE F CE2 1 
ATOM   10279 C  CZ  . PHE F  1 196 ? -33.024 32.400  23.015 1.00 64.69  ? 187 PHE F CZ  1 
ATOM   10280 N  N   . TYR F  1 197 ? -27.400 34.563  19.563 1.00 96.80  ? 188 TYR F N   1 
ATOM   10281 C  CA  . TYR F  1 197 ? -26.458 34.859  18.502 1.00 107.61 ? 188 TYR F CA  1 
ATOM   10282 C  C   . TYR F  1 197 ? -27.217 34.391  17.246 1.00 117.92 ? 188 TYR F C   1 
ATOM   10283 O  O   . TYR F  1 197 ? -27.594 33.212  17.158 1.00 115.32 ? 188 TYR F O   1 
ATOM   10284 C  CB  . TYR F  1 197 ? -25.155 34.092  18.744 1.00 110.41 ? 188 TYR F CB  1 
ATOM   10285 C  CG  . TYR F  1 197 ? -24.409 34.641  19.954 1.00 110.98 ? 188 TYR F CG  1 
ATOM   10286 C  CD1 . TYR F  1 197 ? -24.536 34.064  21.216 1.00 104.59 ? 188 TYR F CD1 1 
ATOM   10287 C  CD2 . TYR F  1 197 ? -23.611 35.774  19.841 1.00 109.53 ? 188 TYR F CD2 1 
ATOM   10288 C  CE1 . TYR F  1 197 ? -23.866 34.594  22.323 1.00 102.60 ? 188 TYR F CE1 1 
ATOM   10289 C  CE2 . TYR F  1 197 ? -22.942 36.304  20.944 1.00 105.48 ? 188 TYR F CE2 1 
ATOM   10290 C  CZ  . TYR F  1 197 ? -23.073 35.711  22.180 1.00 108.01 ? 188 TYR F CZ  1 
ATOM   10291 O  OH  . TYR F  1 197 ? -22.414 36.231  23.276 1.00 113.13 ? 188 TYR F OH  1 
ATOM   10292 N  N   . GLU F  1 198 ? -27.474 35.270  16.308 1.00 119.28 ? 189 GLU F N   1 
ATOM   10293 C  CA  . GLU F  1 198 ? -28.229 34.813  15.143 1.00 126.61 ? 189 GLU F CA  1 
ATOM   10294 C  C   . GLU F  1 198 ? -27.499 33.723  14.355 1.00 119.69 ? 189 GLU F C   1 
ATOM   10295 O  O   . GLU F  1 198 ? -28.158 32.990  13.559 1.00 107.48 ? 189 GLU F O   1 
ATOM   10296 C  CB  . GLU F  1 198 ? -28.825 35.897  14.256 1.00 120.21 ? 189 GLU F CB  1 
ATOM   10297 C  CG  . GLU F  1 198 ? -29.741 35.252  13.193 1.00 117.04 ? 189 GLU F CG  1 
ATOM   10298 C  CD  . GLU F  1 198 ? -31.201 35.246  13.633 1.00 119.02 ? 189 GLU F CD  1 
ATOM   10299 O  OE1 . GLU F  1 198 ? -31.552 36.381  13.999 1.00 115.93 ? 189 GLU F OE1 1 
ATOM   10300 O  OE2 . GLU F  1 198 ? -31.988 34.282  13.580 1.00 107.63 ? 189 GLU F OE2 1 
ATOM   10301 N  N   . CYS F  1 199 ? -26.232 33.712  14.534 1.00 109.82 ? 190 CYS F N   1 
ATOM   10302 C  CA  . CYS F  1 199 ? -25.360 32.715  13.946 1.00 114.04 ? 190 CYS F CA  1 
ATOM   10303 C  C   . CYS F  1 199 ? -25.809 31.333  14.419 1.00 117.17 ? 190 CYS F C   1 
ATOM   10304 O  O   . CYS F  1 199 ? -25.489 30.317  13.799 1.00 116.15 ? 190 CYS F O   1 
ATOM   10305 C  CB  . CYS F  1 199 ? -23.922 32.933  14.410 1.00 115.12 ? 190 CYS F CB  1 
ATOM   10306 S  SG  . CYS F  1 199 ? -23.518 32.099  15.926 1.00 137.97 ? 190 CYS F SG  1 
ATOM   10307 N  N   . CYS F  1 200 ? -26.554 31.318  15.527 1.00 114.16 ? 191 CYS F N   1 
ATOM   10308 C  CA  . CYS F  1 200 ? -26.909 30.100  16.260 1.00 111.41 ? 191 CYS F CA  1 
ATOM   10309 C  C   . CYS F  1 200 ? -28.347 30.238  16.779 1.00 101.72 ? 191 CYS F C   1 
ATOM   10310 O  O   . CYS F  1 200 ? -28.870 31.340  16.867 1.00 96.50  ? 191 CYS F O   1 
ATOM   10311 C  CB  . CYS F  1 200 ? -25.824 29.773  17.299 1.00 111.72 ? 191 CYS F CB  1 
ATOM   10312 S  SG  . CYS F  1 200 ? -24.135 30.001  16.755 1.00 137.90 ? 191 CYS F SG  1 
ATOM   10313 N  N   . LYS F  1 201 ? -28.990 29.127  17.130 1.00 98.12  ? 192 LYS F N   1 
ATOM   10314 C  CA  A LYS F  1 201 ? -30.269 29.165  17.828 0.40 99.22  ? 192 LYS F CA  1 
ATOM   10315 C  CA  B LYS F  1 201 ? -30.272 29.187  17.833 0.60 99.27  ? 192 LYS F CA  1 
ATOM   10316 C  C   . LYS F  1 201 ? -30.090 28.824  19.307 1.00 94.71  ? 192 LYS F C   1 
ATOM   10317 O  O   . LYS F  1 201 ? -31.053 28.825  20.084 1.00 92.63  ? 192 LYS F O   1 
ATOM   10318 C  CB  A LYS F  1 201 ? -31.281 28.220  17.171 0.40 97.33  ? 192 LYS F CB  1 
ATOM   10319 C  CB  B LYS F  1 201 ? -31.328 28.293  17.166 0.60 97.33  ? 192 LYS F CB  1 
ATOM   10320 C  CG  A LYS F  1 201 ? -32.724 28.476  17.577 0.40 97.76  ? 192 LYS F CG  1 
ATOM   10321 C  CG  B LYS F  1 201 ? -32.781 28.592  17.566 0.60 97.81  ? 192 LYS F CG  1 
ATOM   10322 C  CD  A LYS F  1 201 ? -33.711 27.818  16.623 0.40 96.33  ? 192 LYS F CD  1 
ATOM   10323 C  CD  B LYS F  1 201 ? -33.200 30.032  17.254 0.60 92.76  ? 192 LYS F CD  1 
ATOM   10324 C  CE  A LYS F  1 201 ? -35.102 28.421  16.787 0.40 94.85  ? 192 LYS F CE  1 
ATOM   10325 C  CE  B LYS F  1 201 ? -33.715 30.748  18.500 0.60 90.92  ? 192 LYS F CE  1 
ATOM   10326 N  NZ  A LYS F  1 201 ? -36.048 28.011  15.712 0.40 90.29  ? 192 LYS F NZ  1 
ATOM   10327 N  NZ  B LYS F  1 201 ? -34.033 32.175  18.226 0.60 79.54  ? 192 LYS F NZ  1 
ATOM   10328 N  N   . GLU F  1 202 ? -28.849 28.530  19.693 1.00 92.86  ? 193 GLU F N   1 
ATOM   10329 C  CA  . GLU F  1 202 ? -28.541 28.248  21.093 1.00 88.59  ? 193 GLU F CA  1 
ATOM   10330 C  C   . GLU F  1 202 ? -28.567 29.543  21.873 1.00 79.54  ? 193 GLU F C   1 
ATOM   10331 O  O   . GLU F  1 202 ? -27.922 30.516  21.476 1.00 80.26  ? 193 GLU F O   1 
ATOM   10332 C  CB  . GLU F  1 202 ? -27.166 27.593  21.245 1.00 85.39  ? 193 GLU F CB  1 
ATOM   10333 C  CG  . GLU F  1 202 ? -27.059 26.681  22.466 1.00 78.85  ? 193 GLU F CG  1 
ATOM   10334 C  CD  . GLU F  1 202 ? -25.694 26.032  22.597 1.00 77.33  ? 193 GLU F CD  1 
ATOM   10335 O  OE1 . GLU F  1 202 ? -24.809 26.344  21.779 1.00 76.43  ? 193 GLU F OE1 1 
ATOM   10336 O  OE2 . GLU F  1 202 ? -25.500 25.215  23.519 1.00 74.55  ? 193 GLU F OE2 1 
ATOM   10337 N  N   . PRO F  1 203 ? -29.340 29.566  22.969 1.00 72.07  ? 194 PRO F N   1 
ATOM   10338 C  CA  . PRO F  1 203 ? -29.337 30.693  23.902 1.00 73.14  ? 194 PRO F CA  1 
ATOM   10339 C  C   . PRO F  1 203 ? -28.050 30.693  24.731 1.00 76.45  ? 194 PRO F C   1 
ATOM   10340 O  O   . PRO F  1 203 ? -27.549 29.627  25.066 1.00 78.10  ? 194 PRO F O   1 
ATOM   10341 C  CB  . PRO F  1 203 ? -30.555 30.409  24.790 1.00 76.50  ? 194 PRO F CB  1 
ATOM   10342 C  CG  . PRO F  1 203 ? -30.730 28.936  24.739 1.00 72.92  ? 194 PRO F CG  1 
ATOM   10343 C  CD  . PRO F  1 203 ? -30.291 28.512  23.366 1.00 71.12  ? 194 PRO F CD  1 
ATOM   10344 N  N   . TYR F  1 204 ? -27.497 31.862  25.022 1.00 73.40  ? 195 TYR F N   1 
ATOM   10345 C  CA  . TYR F  1 204 ? -26.345 31.951  25.909 1.00 67.93  ? 195 TYR F CA  1 
ATOM   10346 C  C   . TYR F  1 204 ? -26.627 32.753  27.195 1.00 72.71  ? 195 TYR F C   1 
ATOM   10347 O  O   . TYR F  1 204 ? -26.754 33.983  27.143 1.00 67.15  ? 195 TYR F O   1 
ATOM   10348 C  CB  . TYR F  1 204 ? -25.167 32.530  25.138 1.00 70.96  ? 195 TYR F CB  1 
ATOM   10349 C  CG  . TYR F  1 204 ? -24.628 31.588  24.092 1.00 77.59  ? 195 TYR F CG  1 
ATOM   10350 C  CD1 . TYR F  1 204 ? -25.372 31.250  22.972 1.00 88.20  ? 195 TYR F CD1 1 
ATOM   10351 C  CD2 . TYR F  1 204 ? -23.373 31.029  24.226 1.00 80.54  ? 195 TYR F CD2 1 
ATOM   10352 C  CE1 . TYR F  1 204 ? -24.868 30.376  22.008 1.00 85.91  ? 195 TYR F CE1 1 
ATOM   10353 C  CE2 . TYR F  1 204 ? -22.868 30.161  23.280 1.00 81.17  ? 195 TYR F CE2 1 
ATOM   10354 C  CZ  . TYR F  1 204 ? -23.611 29.841  22.174 1.00 77.80  ? 195 TYR F CZ  1 
ATOM   10355 O  OH  . TYR F  1 204 ? -23.081 28.982  21.247 1.00 72.90  ? 195 TYR F OH  1 
ATOM   10356 N  N   . PRO F  1 205 ? -26.722 32.058  28.352 1.00 69.72  ? 196 PRO F N   1 
ATOM   10357 C  CA  . PRO F  1 205 ? -27.020 32.713  29.630 1.00 62.42  ? 196 PRO F CA  1 
ATOM   10358 C  C   . PRO F  1 205 ? -25.821 33.409  30.250 1.00 64.26  ? 196 PRO F C   1 
ATOM   10359 O  O   . PRO F  1 205 ? -24.672 33.074  29.972 1.00 65.70  ? 196 PRO F O   1 
ATOM   10360 C  CB  . PRO F  1 205 ? -27.485 31.562  30.527 1.00 57.53  ? 196 PRO F CB  1 
ATOM   10361 C  CG  . PRO F  1 205 ? -27.728 30.414  29.616 1.00 63.57  ? 196 PRO F CG  1 
ATOM   10362 C  CD  . PRO F  1 205 ? -26.750 30.598  28.502 1.00 68.15  ? 196 PRO F CD  1 
ATOM   10363 N  N   . ASP F  1 206 ? -26.117 34.417  31.056 1.00 63.18  ? 197 ASP F N   1 
ATOM   10364 C  CA  . ASP F  1 206 ? -25.131 35.057  31.894 1.00 59.33  ? 197 ASP F CA  1 
ATOM   10365 C  C   . ASP F  1 206 ? -25.876 35.708  33.038 1.00 66.42  ? 197 ASP F C   1 
ATOM   10366 O  O   . ASP F  1 206 ? -27.067 35.987  32.923 1.00 62.04  ? 197 ASP F O   1 
ATOM   10367 C  CB  . ASP F  1 206 ? -24.350 36.112  31.126 1.00 60.85  ? 197 ASP F CB  1 
ATOM   10368 C  CG  . ASP F  1 206 ? -25.222 37.270  30.679 1.00 74.07  ? 197 ASP F CG  1 
ATOM   10369 O  OD1 . ASP F  1 206 ? -25.635 38.078  31.543 1.00 67.63  ? 197 ASP F OD1 1 
ATOM   10370 O  OD2 . ASP F  1 206 ? -25.480 37.375  29.453 1.00 79.34  ? 197 ASP F OD2 1 
ATOM   10371 N  N   . VAL F  1 207 ? -25.157 35.943  34.137 1.00 70.18  ? 198 VAL F N   1 
ATOM   10372 C  CA  . VAL F  1 207 ? -25.661 36.688  35.281 1.00 61.64  ? 198 VAL F CA  1 
ATOM   10373 C  C   . VAL F  1 207 ? -24.985 38.044  35.316 1.00 63.17  ? 198 VAL F C   1 
ATOM   10374 O  O   . VAL F  1 207 ? -23.763 38.127  35.353 1.00 61.78  ? 198 VAL F O   1 
ATOM   10375 C  CB  . VAL F  1 207 ? -25.379 35.962  36.587 1.00 57.84  ? 198 VAL F CB  1 
ATOM   10376 C  CG1 . VAL F  1 207 ? -25.960 36.727  37.730 1.00 54.17  ? 198 VAL F CG1 1 
ATOM   10377 C  CG2 . VAL F  1 207 ? -25.977 34.572  36.540 1.00 66.59  ? 198 VAL F CG2 1 
ATOM   10378 N  N   . ASN F  1 208 ? -25.790 39.102  35.281 1.00 67.34  ? 199 ASN F N   1 
ATOM   10379 C  CA  . ASN F  1 208 ? -25.282 40.462  35.365 1.00 63.48  ? 199 ASN F CA  1 
ATOM   10380 C  C   . ASN F  1 208 ? -25.240 40.916  36.830 1.00 64.34  ? 199 ASN F C   1 
ATOM   10381 O  O   . ASN F  1 208 ? -26.267 41.004  37.500 1.00 64.72  ? 199 ASN F O   1 
ATOM   10382 C  CB  . ASN F  1 208 ? -26.148 41.408  34.526 1.00 60.11  ? 199 ASN F CB  1 
ATOM   10383 C  CG  . ASN F  1 208 ? -25.390 42.656  34.059 1.00 74.22  ? 199 ASN F CG  1 
ATOM   10384 O  OD1 . ASN F  1 208 ? -24.175 42.754  34.221 1.00 76.18  ? 199 ASN F OD1 1 
ATOM   10385 N  ND2 . ASN F  1 208 ? -26.109 43.608  33.464 1.00 67.72  ? 199 ASN F ND2 1 
ATOM   10386 N  N   . LEU F  1 209 ? -24.038 41.172  37.327 1.00 64.72  ? 200 LEU F N   1 
ATOM   10387 C  CA  . LEU F  1 209 ? -23.857 41.738  38.652 1.00 63.68  ? 200 LEU F CA  1 
ATOM   10388 C  C   . LEU F  1 209 ? -23.715 43.245  38.519 1.00 68.13  ? 200 LEU F C   1 
ATOM   10389 O  O   . LEU F  1 209 ? -22.802 43.735  37.855 1.00 67.52  ? 200 LEU F O   1 
ATOM   10390 C  CB  . LEU F  1 209 ? -22.612 41.158  39.302 1.00 59.20  ? 200 LEU F CB  1 
ATOM   10391 C  CG  . LEU F  1 209 ? -22.223 41.682  40.676 1.00 62.21  ? 200 LEU F CG  1 
ATOM   10392 C  CD1 . LEU F  1 209 ? -23.423 41.749  41.597 1.00 61.90  ? 200 LEU F CD1 1 
ATOM   10393 C  CD2 . LEU F  1 209 ? -21.171 40.764  41.227 1.00 59.33  ? 200 LEU F CD2 1 
ATOM   10394 N  N   . VAL F  1 210 ? -24.633 43.978  39.137 1.00 66.27  ? 201 VAL F N   1 
ATOM   10395 C  CA  . VAL F  1 210 ? -24.671 45.426  38.989 1.00 67.45  ? 201 VAL F CA  1 
ATOM   10396 C  C   . VAL F  1 210 ? -24.578 46.080  40.354 1.00 63.79  ? 201 VAL F C   1 
ATOM   10397 O  O   . VAL F  1 210 ? -25.336 45.753  41.264 1.00 67.99  ? 201 VAL F O   1 
ATOM   10398 C  CB  . VAL F  1 210 ? -25.953 45.888  38.255 1.00 70.40  ? 201 VAL F CB  1 
ATOM   10399 C  CG1 . VAL F  1 210 ? -25.934 47.400  38.053 1.00 57.55  ? 201 VAL F CG1 1 
ATOM   10400 C  CG2 . VAL F  1 210 ? -26.107 45.143  36.917 1.00 57.26  ? 201 VAL F CG2 1 
ATOM   10401 N  N   . VAL F  1 211 ? -23.634 46.999  40.499 1.00 66.54  ? 202 VAL F N   1 
ATOM   10402 C  CA  . VAL F  1 211 ? -23.372 47.603  41.795 1.00 65.94  ? 202 VAL F CA  1 
ATOM   10403 C  C   . VAL F  1 211 ? -23.341 49.133  41.733 1.00 74.89  ? 202 VAL F C   1 
ATOM   10404 O  O   . VAL F  1 211 ? -22.637 49.725  40.903 1.00 67.94  ? 202 VAL F O   1 
ATOM   10405 C  CB  . VAL F  1 211 ? -22.057 47.088  42.373 1.00 62.19  ? 202 VAL F CB  1 
ATOM   10406 C  CG1 . VAL F  1 211 ? -21.866 47.606  43.785 1.00 59.28  ? 202 VAL F CG1 1 
ATOM   10407 C  CG2 . VAL F  1 211 ? -22.046 45.572  42.348 1.00 61.16  ? 202 VAL F CG2 1 
ATOM   10408 N  N   . LYS F  1 212 ? -24.128 49.755  42.611 1.00 72.29  ? 203 LYS F N   1 
ATOM   10409 C  CA  . LYS F  1 212 ? -24.132 51.199  42.777 1.00 66.55  ? 203 LYS F CA  1 
ATOM   10410 C  C   . LYS F  1 212 ? -23.406 51.510  44.061 1.00 64.45  ? 203 LYS F C   1 
ATOM   10411 O  O   . LYS F  1 212 ? -23.824 51.067  45.118 1.00 74.17  ? 203 LYS F O   1 
ATOM   10412 C  CB  . LYS F  1 212 ? -25.562 51.730  42.851 1.00 71.41  ? 203 LYS F CB  1 
ATOM   10413 C  CG  . LYS F  1 212 ? -26.306 51.649  41.534 1.00 87.20  ? 203 LYS F CG  1 
ATOM   10414 C  CD  . LYS F  1 212 ? -27.683 52.293  41.612 1.00 92.18  ? 203 LYS F CD  1 
ATOM   10415 C  CE  . LYS F  1 212 ? -28.403 52.193  40.267 1.00 98.42  ? 203 LYS F CE  1 
ATOM   10416 N  NZ  . LYS F  1 212 ? -28.514 50.782  39.790 1.00 82.91  ? 203 LYS F NZ  1 
ATOM   10417 N  N   . PHE F  1 213 ? -22.314 52.262  43.970 1.00 67.55  ? 204 PHE F N   1 
ATOM   10418 C  CA  . PHE F  1 213 ? -21.465 52.533  45.125 1.00 65.62  ? 204 PHE F CA  1 
ATOM   10419 C  C   . PHE F  1 213 ? -21.007 53.985  45.159 1.00 67.27  ? 204 PHE F C   1 
ATOM   10420 O  O   . PHE F  1 213 ? -21.010 54.670  44.143 1.00 66.09  ? 204 PHE F O   1 
ATOM   10421 C  CB  . PHE F  1 213 ? -20.254 51.574  45.153 1.00 65.99  ? 204 PHE F CB  1 
ATOM   10422 C  CG  . PHE F  1 213 ? -19.325 51.719  43.975 1.00 62.01  ? 204 PHE F CG  1 
ATOM   10423 C  CD1 . PHE F  1 213 ? -18.040 52.212  44.143 1.00 63.71  ? 204 PHE F CD1 1 
ATOM   10424 C  CD2 . PHE F  1 213 ? -19.737 51.367  42.699 1.00 62.20  ? 204 PHE F CD2 1 
ATOM   10425 C  CE1 . PHE F  1 213 ? -17.181 52.351  43.051 1.00 62.94  ? 204 PHE F CE1 1 
ATOM   10426 C  CE2 . PHE F  1 213 ? -18.888 51.508  41.608 1.00 63.02  ? 204 PHE F CE2 1 
ATOM   10427 C  CZ  . PHE F  1 213 ? -17.606 52.003  41.786 1.00 59.33  ? 204 PHE F CZ  1 
ATOM   10428 N  N   . ARG F  1 214 ? -20.616 54.454  46.336 1.00 73.74  ? 205 ARG F N   1 
ATOM   10429 C  CA  . ARG F  1 214 ? -20.103 55.812  46.478 1.00 76.46  ? 205 ARG F CA  1 
ATOM   10430 C  C   . ARG F  1 214 ? -19.167 55.896  47.669 1.00 72.79  ? 205 ARG F C   1 
ATOM   10431 O  O   . ARG F  1 214 ? -19.179 55.030  48.539 1.00 69.44  ? 205 ARG F O   1 
ATOM   10432 C  CB  . ARG F  1 214 ? -21.244 56.805  46.671 1.00 76.66  ? 205 ARG F CB  1 
ATOM   10433 C  CG  . ARG F  1 214 ? -21.883 56.682  48.026 1.00 82.54  ? 205 ARG F CG  1 
ATOM   10434 C  CD  . ARG F  1 214 ? -23.046 57.626  48.192 1.00 83.86  ? 205 ARG F CD  1 
ATOM   10435 N  NE  . ARG F  1 214 ? -23.690 57.403  49.480 1.00 92.88  ? 205 ARG F NE  1 
ATOM   10436 C  CZ  . ARG F  1 214 ? -24.844 57.948  49.834 1.00 92.95  ? 205 ARG F CZ  1 
ATOM   10437 N  NH1 . ARG F  1 214 ? -25.357 57.689  51.031 1.00 85.62  ? 205 ARG F NH1 1 
ATOM   10438 N  NH2 . ARG F  1 214 ? -25.480 58.751  48.987 1.00 95.76  ? 205 ARG F NH2 1 
ATOM   10439 N  N   . GLU F  1 215 ? -18.371 56.958  47.711 1.00 74.23  ? 206 GLU F N   1 
ATOM   10440 C  CA  . GLU F  1 215 ? -17.466 57.176  48.823 1.00 71.27  ? 206 GLU F CA  1 
ATOM   10441 C  C   . GLU F  1 215 ? -18.297 57.441  50.074 1.00 67.05  ? 206 GLU F C   1 
ATOM   10442 O  O   . GLU F  1 215 ? -19.491 57.714  49.989 1.00 62.31  ? 206 GLU F O   1 
ATOM   10443 C  CB  . GLU F  1 215 ? -16.521 58.329  48.511 1.00 68.13  ? 206 GLU F CB  1 
ATOM   10444 C  CG  . GLU F  1 215 ? -15.842 58.184  47.167 1.00 67.00  ? 206 GLU F CG  1 
ATOM   10445 C  CD  . GLU F  1 215 ? -15.099 59.430  46.759 1.00 78.06  ? 206 GLU F CD  1 
ATOM   10446 O  OE1 . GLU F  1 215 ? -15.231 60.443  47.476 1.00 78.84  ? 206 GLU F OE1 1 
ATOM   10447 O  OE2 . GLU F  1 215 ? -14.390 59.402  45.727 1.00 69.36  ? 206 GLU F OE2 1 
ATOM   10448 N  N   . ARG F  1 216 ? -17.688 57.279  51.238 1.00 76.37  ? 207 ARG F N   1 
ATOM   10449 C  CA  . ARG F  1 216 ? -18.419 57.446  52.485 1.00 80.61  ? 207 ARG F CA  1 
ATOM   10450 C  C   . ARG F  1 216 ? -18.465 58.898  52.946 1.00 76.00  ? 207 ARG F C   1 
ATOM   10451 O  O   . ARG F  1 216 ? -17.641 59.324  53.751 1.00 77.42  ? 207 ARG F O   1 
ATOM   10452 C  CB  . ARG F  1 216 ? -17.810 56.569  53.567 1.00 65.87  ? 207 ARG F CB  1 
ATOM   10453 C  CG  . ARG F  1 216 ? -18.220 55.137  53.462 1.00 69.08  ? 207 ARG F CG  1 
ATOM   10454 C  CD  . ARG F  1 216 ? -18.208 54.476  54.835 1.00 80.11  ? 207 ARG F CD  1 
ATOM   10455 N  NE  . ARG F  1 216 ? -19.088 53.310  54.862 1.00 91.11  ? 207 ARG F NE  1 
ATOM   10456 C  CZ  . ARG F  1 216 ? -18.690 52.067  54.594 1.00 89.32  ? 207 ARG F CZ  1 
ATOM   10457 N  NH1 . ARG F  1 216 ? -17.419 51.833  54.297 1.00 82.84  ? 207 ARG F NH1 1 
ATOM   10458 N  NH2 . ARG F  1 216 ? -19.555 51.054  54.623 1.00 86.56  ? 207 ARG F NH2 1 
ATOM   10459 N  N   . LYS G  1 3   ? 32.199  1.066   63.270 1.00 104.25 ? -6  LYS G N   1 
ATOM   10460 C  CA  . LYS G  1 3   ? 32.387  2.173   64.194 1.00 108.94 ? -6  LYS G CA  1 
ATOM   10461 C  C   . LYS G  1 3   ? 31.053  2.828   64.559 1.00 109.35 ? -6  LYS G C   1 
ATOM   10462 O  O   . LYS G  1 3   ? 30.068  2.143   64.848 1.00 93.59  ? -6  LYS G O   1 
ATOM   10463 C  CB  . LYS G  1 3   ? 33.355  3.213   63.603 1.00 111.87 ? -6  LYS G CB  1 
ATOM   10464 C  CG  . LYS G  1 3   ? 33.831  4.277   64.599 1.00 109.54 ? -6  LYS G CG  1 
ATOM   10465 C  CD  . LYS G  1 3   ? 34.380  3.627   65.863 1.00 101.23 ? -6  LYS G CD  1 
ATOM   10466 C  CE  . LYS G  1 3   ? 34.333  4.571   67.050 1.00 99.38  ? -6  LYS G CE  1 
ATOM   10467 N  NZ  . LYS G  1 3   ? 32.944  4.879   67.485 1.00 100.21 ? -6  LYS G NZ  1 
ATOM   10468 N  N   . ASP G  1 4   ? 31.043  4.160   64.531 1.00 114.06 ? -5  ASP G N   1 
ATOM   10469 C  CA  . ASP G  1 4   ? 29.905  4.965   64.951 1.00 104.35 ? -5  ASP G CA  1 
ATOM   10470 C  C   . ASP G  1 4   ? 29.026  5.334   63.760 1.00 99.60  ? -5  ASP G C   1 
ATOM   10471 O  O   . ASP G  1 4   ? 28.018  6.028   63.903 1.00 92.35  ? -5  ASP G O   1 
ATOM   10472 C  CB  . ASP G  1 4   ? 30.400  6.233   65.651 1.00 107.83 ? -5  ASP G CB  1 
ATOM   10473 C  CG  . ASP G  1 4   ? 29.289  6.982   66.355 1.00 111.42 ? -5  ASP G CG  1 
ATOM   10474 O  OD1 . ASP G  1 4   ? 28.856  6.520   67.434 1.00 102.56 ? -5  ASP G OD1 1 
ATOM   10475 O  OD2 . ASP G  1 4   ? 28.850  8.028   65.828 1.00 106.34 ? -5  ASP G OD2 1 
ATOM   10476 N  N   . ASP G  1 5   ? 29.420  4.874   62.580 1.00 97.00  ? -4  ASP G N   1 
ATOM   10477 C  CA  . ASP G  1 5   ? 28.629  5.108   61.384 1.00 96.72  ? -4  ASP G CA  1 
ATOM   10478 C  C   . ASP G  1 5   ? 27.457  4.136   61.299 1.00 91.17  ? -4  ASP G C   1 
ATOM   10479 O  O   . ASP G  1 5   ? 26.431  4.438   60.686 1.00 84.70  ? -4  ASP G O   1 
ATOM   10480 C  CB  . ASP G  1 5   ? 29.501  4.973   60.140 1.00 107.48 ? -4  ASP G CB  1 
ATOM   10481 C  CG  . ASP G  1 5   ? 30.730  5.843   60.198 1.00 109.42 ? -4  ASP G CG  1 
ATOM   10482 O  OD1 . ASP G  1 5   ? 31.801  5.331   60.597 1.00 109.21 ? -4  ASP G OD1 1 
ATOM   10483 O  OD2 . ASP G  1 5   ? 30.621  7.037   59.844 1.00 102.86 ? -4  ASP G OD2 1 
ATOM   10484 N  N   . ASP G  1 6   ? 27.612  2.961   61.898 1.00 86.19  ? -3  ASP G N   1 
ATOM   10485 C  CA  . ASP G  1 6   ? 26.544  1.981   61.847 1.00 85.18  ? -3  ASP G CA  1 
ATOM   10486 C  C   . ASP G  1 6   ? 25.347  2.516   62.634 1.00 79.78  ? -3  ASP G C   1 
ATOM   10487 O  O   . ASP G  1 6   ? 24.194  2.261   62.278 1.00 76.64  ? -3  ASP G O   1 
ATOM   10488 C  CB  . ASP G  1 6   ? 27.011  0.616   62.370 1.00 85.38  ? -3  ASP G CB  1 
ATOM   10489 C  CG  . ASP G  1 6   ? 25.949  -0.474  62.204 1.00 78.60  ? -3  ASP G CG  1 
ATOM   10490 O  OD1 . ASP G  1 6   ? 26.101  -1.359  61.346 1.00 72.91  ? -3  ASP G OD1 1 
ATOM   10491 O  OD2 . ASP G  1 6   ? 24.944  -0.455  62.941 1.00 77.87  ? -3  ASP G OD2 1 
ATOM   10492 N  N   . ASP G  1 7   ? 25.624  3.278   63.690 1.00 80.00  ? -2  ASP G N   1 
ATOM   10493 C  CA  . ASP G  1 7   ? 24.564  3.863   64.512 1.00 81.28  ? -2  ASP G CA  1 
ATOM   10494 C  C   . ASP G  1 7   ? 23.836  4.964   63.771 1.00 73.16  ? -2  ASP G C   1 
ATOM   10495 O  O   . ASP G  1 7   ? 22.656  5.190   64.006 1.00 70.97  ? -2  ASP G O   1 
ATOM   10496 C  CB  . ASP G  1 7   ? 25.111  4.396   65.839 1.00 89.77  ? -2  ASP G CB  1 
ATOM   10497 C  CG  . ASP G  1 7   ? 25.124  3.341   66.933 1.00 97.13  ? -2  ASP G CG  1 
ATOM   10498 O  OD1 . ASP G  1 7   ? 26.167  3.214   67.615 1.00 107.26 ? -2  ASP G OD1 1 
ATOM   10499 O  OD2 . ASP G  1 7   ? 24.095  2.644   67.113 1.00 79.63  ? -2  ASP G OD2 1 
ATOM   10500 N  N   . LYS G  1 8   ? 24.554  5.643   62.881 1.00 75.47  ? -1  LYS G N   1 
ATOM   10501 C  CA  . LYS G  1 8   ? 23.962  6.637   61.984 1.00 74.16  ? -1  LYS G CA  1 
ATOM   10502 C  C   . LYS G  1 8   ? 23.195  5.989   60.827 1.00 73.07  ? -1  LYS G C   1 
ATOM   10503 O  O   . LYS G  1 8   ? 22.190  6.531   60.356 1.00 70.12  ? -1  LYS G O   1 
ATOM   10504 C  CB  . LYS G  1 8   ? 25.044  7.546   61.404 1.00 70.43  ? -1  LYS G CB  1 
ATOM   10505 C  CG  . LYS G  1 8   ? 25.683  8.487   62.394 1.00 82.91  ? -1  LYS G CG  1 
ATOM   10506 C  CD  . LYS G  1 8   ? 26.803  9.269   61.727 1.00 88.66  ? -1  LYS G CD  1 
ATOM   10507 C  CE  . LYS G  1 8   ? 27.567  10.117  62.723 1.00 84.43  ? -1  LYS G CE  1 
ATOM   10508 N  NZ  . LYS G  1 8   ? 28.889  10.469  62.158 1.00 83.10  ? -1  LYS G NZ  1 
ATOM   10509 N  N   . LEU G  1 9   ? 23.691  4.846   60.359 1.00 68.69  ? 0   LEU G N   1 
ATOM   10510 C  CA  . LEU G  1 9   ? 23.058  4.120   59.276 1.00 62.45  ? 0   LEU G CA  1 
ATOM   10511 C  C   . LEU G  1 9   ? 21.688  3.633   59.678 1.00 66.25  ? 0   LEU G C   1 
ATOM   10512 O  O   . LEU G  1 9   ? 20.729  3.769   58.925 1.00 60.42  ? 0   LEU G O   1 
ATOM   10513 C  CB  . LEU G  1 9   ? 23.913  2.937   58.881 1.00 75.71  ? 0   LEU G CB  1 
ATOM   10514 C  CG  . LEU G  1 9   ? 25.108  3.327   58.031 1.00 84.05  ? 0   LEU G CG  1 
ATOM   10515 C  CD1 . LEU G  1 9   ? 26.167  2.231   58.049 1.00 89.54  ? 0   LEU G CD1 1 
ATOM   10516 C  CD2 . LEU G  1 9   ? 24.621  3.610   56.624 1.00 76.33  ? 0   LEU G CD2 1 
ATOM   10517 N  N   . HIS G  1 10  ? 21.596  3.063   60.871 1.00 66.11  ? 1   HIS G N   1 
ATOM   10518 C  CA  . HIS G  1 10  ? 20.329  2.540   61.346 1.00 67.07  ? 1   HIS G CA  1 
ATOM   10519 C  C   . HIS G  1 10  ? 19.332  3.664   61.539 1.00 60.38  ? 1   HIS G C   1 
ATOM   10520 O  O   . HIS G  1 10  ? 18.148  3.511   61.253 1.00 58.09  ? 1   HIS G O   1 
ATOM   10521 C  CB  . HIS G  1 10  ? 20.526  1.773   62.644 1.00 63.24  ? 1   HIS G CB  1 
ATOM   10522 C  CG  . HIS G  1 10  ? 21.183  0.444   62.461 1.00 65.99  ? 1   HIS G CG  1 
ATOM   10523 N  ND1 . HIS G  1 10  ? 20.541  -0.743  62.731 1.00 68.32  ? 1   HIS G ND1 1 
ATOM   10524 C  CD2 . HIS G  1 10  ? 22.423  0.114   62.036 1.00 67.31  ? 1   HIS G CD2 1 
ATOM   10525 C  CE1 . HIS G  1 10  ? 21.364  -1.749  62.494 1.00 69.83  ? 1   HIS G CE1 1 
ATOM   10526 N  NE2 . HIS G  1 10  ? 22.510  -1.254  62.068 1.00 66.18  ? 1   HIS G NE2 1 
ATOM   10527 N  N   . SER G  1 11  ? 19.824  4.799   62.020 1.00 56.41  ? 2   SER G N   1 
ATOM   10528 C  CA  . SER G  1 11  ? 18.971  5.953   62.240 1.00 61.48  ? 2   SER G CA  1 
ATOM   10529 C  C   . SER G  1 11  ? 18.341  6.461   60.943 1.00 64.04  ? 2   SER G C   1 
ATOM   10530 O  O   . SER G  1 11  ? 17.171  6.832   60.939 1.00 65.84  ? 2   SER G O   1 
ATOM   10531 C  CB  . SER G  1 11  ? 19.724  7.081   62.958 1.00 64.01  ? 2   SER G CB  1 
ATOM   10532 O  OG  . SER G  1 11  ? 20.475  7.865   62.057 1.00 71.26  ? 2   SER G OG  1 
ATOM   10533 N  N   . GLN G  1 12  ? 19.101  6.481   59.849 1.00 55.17  ? 3   GLN G N   1 
ATOM   10534 C  CA  . GLN G  1 12  ? 18.527  6.869   58.562 1.00 58.49  ? 3   GLN G CA  1 
ATOM   10535 C  C   . GLN G  1 12  ? 17.478  5.883   58.070 1.00 59.91  ? 3   GLN G C   1 
ATOM   10536 O  O   . GLN G  1 12  ? 16.410  6.288   57.618 1.00 57.82  ? 3   GLN G O   1 
ATOM   10537 C  CB  . GLN G  1 12  ? 19.601  7.049   57.502 1.00 64.46  ? 3   GLN G CB  1 
ATOM   10538 C  CG  . GLN G  1 12  ? 20.331  8.348   57.610 1.00 66.64  ? 3   GLN G CG  1 
ATOM   10539 C  CD  . GLN G  1 12  ? 21.633  8.323   56.865 1.00 72.92  ? 3   GLN G CD  1 
ATOM   10540 O  OE1 . GLN G  1 12  ? 21.761  7.648   55.848 1.00 68.79  ? 3   GLN G OE1 1 
ATOM   10541 N  NE2 . GLN G  1 12  ? 22.619  9.053   57.372 1.00 79.30  ? 3   GLN G NE2 1 
ATOM   10542 N  N   . ALA G  1 13  ? 17.788  4.593   58.165 1.00 61.58  ? 4   ALA G N   1 
ATOM   10543 C  CA  . ALA G  1 13  ? 16.874  3.540   57.731 1.00 61.12  ? 4   ALA G CA  1 
ATOM   10544 C  C   . ALA G  1 13  ? 15.605  3.559   58.560 1.00 58.11  ? 4   ALA G C   1 
ATOM   10545 O  O   . ALA G  1 13  ? 14.496  3.453   58.043 1.00 57.75  ? 4   ALA G O   1 
ATOM   10546 C  CB  . ALA G  1 13  ? 17.539  2.192   57.845 1.00 62.27  ? 4   ALA G CB  1 
ATOM   10547 N  N   . ASN G  1 14  ? 15.781  3.679   59.863 1.00 61.16  ? 5   ASN G N   1 
ATOM   10548 C  CA  . ASN G  1 14  ? 14.652  3.747   60.765 1.00 64.99  ? 5   ASN G CA  1 
ATOM   10549 C  C   . ASN G  1 14  ? 13.707  4.866   60.388 1.00 61.39  ? 5   ASN G C   1 
ATOM   10550 O  O   . ASN G  1 14  ? 12.490  4.686   60.355 1.00 63.20  ? 5   ASN G O   1 
ATOM   10551 C  CB  . ASN G  1 14  ? 15.148  3.938   62.189 1.00 64.53  ? 5   ASN G CB  1 
ATOM   10552 C  CG  . ASN G  1 14  ? 15.656  2.663   62.779 1.00 63.64  ? 5   ASN G CG  1 
ATOM   10553 O  OD1 . ASN G  1 14  ? 15.220  1.587   62.389 1.00 63.96  ? 5   ASN G OD1 1 
ATOM   10554 N  ND2 . ASN G  1 14  ? 16.582  2.766   63.714 1.00 66.34  ? 5   ASN G ND2 1 
ATOM   10555 N  N   . LEU G  1 15  ? 14.276  6.027   60.108 1.00 54.29  ? 6   LEU G N   1 
ATOM   10556 C  CA  . LEU G  1 15  ? 13.470  7.159   59.734 1.00 53.74  ? 6   LEU G CA  1 
ATOM   10557 C  C   . LEU G  1 15  ? 12.748  6.859   58.431 1.00 57.61  ? 6   LEU G C   1 
ATOM   10558 O  O   . LEU G  1 15  ? 11.533  7.007   58.364 1.00 62.33  ? 6   LEU G O   1 
ATOM   10559 C  CB  . LEU G  1 15  ? 14.321  8.419   59.621 1.00 53.66  ? 6   LEU G CB  1 
ATOM   10560 C  CG  . LEU G  1 15  ? 13.529  9.694   59.340 1.00 50.12  ? 6   LEU G CG  1 
ATOM   10561 C  CD1 . LEU G  1 15  ? 12.356  9.840   60.309 1.00 45.44  ? 6   LEU G CD1 1 
ATOM   10562 C  CD2 . LEU G  1 15  ? 14.451  10.890  59.370 1.00 43.35  ? 6   LEU G CD2 1 
ATOM   10563 N  N   . MET G  1 16  ? 13.484  6.427   57.406 1.00 58.33  ? 7   MET G N   1 
ATOM   10564 C  CA  . MET G  1 16  ? 12.877  6.088   56.111 1.00 60.20  ? 7   MET G CA  1 
ATOM   10565 C  C   . MET G  1 16  ? 11.772  5.053   56.245 1.00 56.27  ? 7   MET G C   1 
ATOM   10566 O  O   . MET G  1 16  ? 10.711  5.179   55.626 1.00 54.16  ? 7   MET G O   1 
ATOM   10567 C  CB  . MET G  1 16  ? 13.927  5.588   55.125 1.00 53.28  ? 7   MET G CB  1 
ATOM   10568 C  CG  . MET G  1 16  ? 14.734  6.692   54.480 1.00 58.10  ? 7   MET G CG  1 
ATOM   10569 S  SD  . MET G  1 16  ? 16.337  6.050   53.987 1.00 86.32  ? 7   MET G SD  1 
ATOM   10570 C  CE  . MET G  1 16  ? 17.097  7.472   53.222 1.00 81.20  ? 7   MET G CE  1 
ATOM   10571 N  N   . ARG G  1 17  ? 12.026  4.037   57.064 1.00 55.12  ? 8   ARG G N   1 
ATOM   10572 C  CA  . ARG G  1 17  ? 11.049  2.986   57.294 1.00 56.84  ? 8   ARG G CA  1 
ATOM   10573 C  C   . ARG G  1 17  ? 9.817   3.523   58.015 1.00 63.96  ? 8   ARG G C   1 
ATOM   10574 O  O   . ARG G  1 17  ? 8.694   3.171   57.670 1.00 72.75  ? 8   ARG G O   1 
ATOM   10575 C  CB  . ARG G  1 17  ? 11.669  1.813   58.046 1.00 51.82  ? 8   ARG G CB  1 
ATOM   10576 C  CG  . ARG G  1 17  ? 10.665  0.746   58.448 1.00 65.78  ? 8   ARG G CG  1 
ATOM   10577 C  CD  . ARG G  1 17  ? 11.354  -0.494  58.976 1.00 65.47  ? 8   ARG G CD  1 
ATOM   10578 N  NE  . ARG G  1 17  ? 12.328  -0.180  60.017 1.00 48.18  ? 8   ARG G NE  1 
ATOM   10579 C  CZ  . ARG G  1 17  ? 12.080  -0.301  61.314 1.00 57.97  ? 8   ARG G CZ  1 
ATOM   10580 N  NH1 . ARG G  1 17  ? 10.895  -0.727  61.725 1.00 59.34  ? 8   ARG G NH1 1 
ATOM   10581 N  NH2 . ARG G  1 17  ? 13.012  0.006   62.201 1.00 66.72  ? 8   ARG G NH2 1 
ATOM   10582 N  N   . LEU G  1 18  ? 10.021  4.390   58.999 1.00 60.61  ? 9   LEU G N   1 
ATOM   10583 C  CA  . LEU G  1 18  ? 8.904   5.028   59.677 1.00 56.32  ? 9   LEU G CA  1 
ATOM   10584 C  C   . LEU G  1 18  ? 8.018   5.797   58.696 1.00 58.98  ? 9   LEU G C   1 
ATOM   10585 O  O   . LEU G  1 18  ? 6.791   5.689   58.729 1.00 60.87  ? 9   LEU G O   1 
ATOM   10586 C  CB  . LEU G  1 18  ? 9.409   5.949   60.784 1.00 51.41  ? 9   LEU G CB  1 
ATOM   10587 C  CG  . LEU G  1 18  ? 8.345   6.833   61.429 1.00 53.46  ? 9   LEU G CG  1 
ATOM   10588 C  CD1 . LEU G  1 18  ? 7.251   5.996   62.041 1.00 51.44  ? 9   LEU G CD1 1 
ATOM   10589 C  CD2 . LEU G  1 18  ? 8.950   7.774   62.447 1.00 52.64  ? 9   LEU G CD2 1 
ATOM   10590 N  N   . LYS G  1 19  ? 8.644   6.568   57.813 1.00 62.97  ? 10  LYS G N   1 
ATOM   10591 C  CA  . LYS G  1 19  ? 7.910   7.365   56.827 1.00 65.22  ? 10  LYS G CA  1 
ATOM   10592 C  C   . LYS G  1 19  ? 7.171   6.482   55.832 1.00 66.28  ? 10  LYS G C   1 
ATOM   10593 O  O   . LYS G  1 19  ? 6.042   6.785   55.466 1.00 67.92  ? 10  LYS G O   1 
ATOM   10594 C  CB  . LYS G  1 19  ? 8.845   8.331   56.095 1.00 55.80  ? 10  LYS G CB  1 
ATOM   10595 C  CG  . LYS G  1 19  ? 9.820   9.045   57.011 1.00 57.98  ? 10  LYS G CG  1 
ATOM   10596 C  CD  . LYS G  1 19  ? 9.530   10.518  57.119 1.00 55.15  ? 10  LYS G CD  1 
ATOM   10597 C  CE  . LYS G  1 19  ? 9.939   11.238  55.851 1.00 57.14  ? 10  LYS G CE  1 
ATOM   10598 N  NZ  . LYS G  1 19  ? 10.435  12.614  56.131 1.00 65.90  ? 10  LYS G NZ  1 
ATOM   10599 N  N   . SER G  1 20  ? 7.800   5.385   55.409 1.00 65.36  ? 11  SER G N   1 
ATOM   10600 C  CA  . SER G  1 20  ? 7.156   4.448   54.495 1.00 69.77  ? 11  SER G CA  1 
ATOM   10601 C  C   . SER G  1 20  ? 5.958   3.772   55.151 1.00 69.98  ? 11  SER G C   1 
ATOM   10602 O  O   . SER G  1 20  ? 4.925   3.596   54.524 1.00 75.39  ? 11  SER G O   1 
ATOM   10603 C  CB  . SER G  1 20  ? 8.140   3.396   54.000 1.00 68.06  ? 11  SER G CB  1 
ATOM   10604 O  OG  . SER G  1 20  ? 8.307   2.379   54.971 1.00 73.38  ? 11  SER G OG  1 
ATOM   10605 N  N   . ASP G  1 21  ? 6.099   3.386   56.432 1.00 69.57  ? 12  ASP G N   1 
ATOM   10606 C  CA  . ASP G  1 21  ? 4.994   2.767   57.155 1.00 75.24  ? 12  ASP G CA  1 
ATOM   10607 C  C   . ASP G  1 21  ? 3.807   3.716   57.307 1.00 78.99  ? 12  ASP G C   1 
ATOM   10608 O  O   . ASP G  1 21  ? 2.654   3.306   57.207 1.00 86.19  ? 12  ASP G O   1 
ATOM   10609 C  CB  . ASP G  1 21  ? 5.454   2.227   58.517 1.00 71.98  ? 12  ASP G CB  1 
ATOM   10610 C  CG  . ASP G  1 21  ? 6.350   1.002   58.387 1.00 80.50  ? 12  ASP G CG  1 
ATOM   10611 O  OD1 . ASP G  1 21  ? 6.923   0.817   57.287 1.00 88.40  ? 12  ASP G OD1 1 
ATOM   10612 O  OD2 . ASP G  1 21  ? 6.479   0.224   59.365 1.00 75.54  ? 12  ASP G OD2 1 
ATOM   10613 N  N   . LEU G  1 22  ? 4.084   5.001   57.520 1.00 77.99  ? 13  LEU G N   1 
ATOM   10614 C  CA  . LEU G  1 22  ? 3.022   5.994   57.623 1.00 74.39  ? 13  LEU G CA  1 
ATOM   10615 C  C   . LEU G  1 22  ? 2.433   6.436   56.271 1.00 78.88  ? 13  LEU G C   1 
ATOM   10616 O  O   . LEU G  1 22  ? 1.214   6.522   56.141 1.00 85.07  ? 13  LEU G O   1 
ATOM   10617 C  CB  . LEU G  1 22  ? 3.514   7.203   58.413 1.00 66.23  ? 13  LEU G CB  1 
ATOM   10618 C  CG  . LEU G  1 22  ? 3.958   6.956   59.855 1.00 62.11  ? 13  LEU G CG  1 
ATOM   10619 C  CD1 . LEU G  1 22  ? 4.744   8.142   60.367 1.00 55.42  ? 13  LEU G CD1 1 
ATOM   10620 C  CD2 . LEU G  1 22  ? 2.776   6.688   60.759 1.00 60.78  ? 13  LEU G CD2 1 
ATOM   10621 N  N   . PHE G  1 23  ? 3.296   6.732   55.291 1.00 77.77  ? 14  PHE G N   1 
ATOM   10622 C  CA  . PHE G  1 23  ? 2.907   7.388   54.012 1.00 79.84  ? 14  PHE G CA  1 
ATOM   10623 C  C   . PHE G  1 23  ? 2.718   6.563   52.717 1.00 83.88  ? 14  PHE G C   1 
ATOM   10624 O  O   . PHE G  1 23  ? 2.346   7.119   51.681 1.00 77.75  ? 14  PHE G O   1 
ATOM   10625 C  CB  . PHE G  1 23  ? 3.898   8.515   53.693 1.00 79.28  ? 14  PHE G CB  1 
ATOM   10626 C  CG  . PHE G  1 23  ? 3.926   9.610   54.720 1.00 77.89  ? 14  PHE G CG  1 
ATOM   10627 C  CD1 . PHE G  1 23  ? 2.799   9.903   55.477 1.00 68.31  ? 14  PHE G CD1 1 
ATOM   10628 C  CD2 . PHE G  1 23  ? 5.075   10.343  54.924 1.00 69.32  ? 14  PHE G CD2 1 
ATOM   10629 C  CE1 . PHE G  1 23  ? 2.825   10.892  56.398 1.00 67.54  ? 14  PHE G CE1 1 
ATOM   10630 C  CE2 . PHE G  1 23  ? 5.104   11.333  55.853 1.00 67.39  ? 14  PHE G CE2 1 
ATOM   10631 C  CZ  . PHE G  1 23  ? 3.983   11.608  56.594 1.00 69.20  ? 14  PHE G CZ  1 
ATOM   10632 N  N   . ASN G  1 24  ? 3.007   5.265   52.781 1.00 97.60  ? 15  ASN G N   1 
ATOM   10633 C  CA  . ASN G  1 24  ? 3.056   4.348   51.624 1.00 97.00  ? 15  ASN G CA  1 
ATOM   10634 C  C   . ASN G  1 24  ? 2.227   3.099   51.922 1.00 100.05 ? 15  ASN G C   1 
ATOM   10635 O  O   . ASN G  1 24  ? 1.346   2.693   51.157 1.00 95.39  ? 15  ASN G O   1 
ATOM   10636 C  CB  . ASN G  1 24  ? 4.496   3.958   51.273 1.00 93.83  ? 15  ASN G CB  1 
ATOM   10637 C  CG  . ASN G  1 24  ? 5.276   5.097   50.637 1.00 93.47  ? 15  ASN G CG  1 
ATOM   10638 O  OD1 . ASN G  1 24  ? 4.843   6.252   50.648 1.00 88.05  ? 15  ASN G OD1 1 
ATOM   10639 N  ND2 . ASN G  1 24  ? 6.442   4.775   50.085 1.00 93.30  ? 15  ASN G ND2 1 
ATOM   10640 N  N   . ARG G  1 25  ? 2.583   2.483   53.043 1.00 94.22  ? 16  ARG G N   1 
ATOM   10641 C  CA  . ARG G  1 25  ? 1.920   1.323   53.612 1.00 93.33  ? 16  ARG G CA  1 
ATOM   10642 C  C   . ARG G  1 25  ? 0.632   1.739   54.334 1.00 97.17  ? 16  ARG G C   1 
ATOM   10643 O  O   . ARG G  1 25  ? 0.046   0.965   55.092 1.00 98.84  ? 16  ARG G O   1 
ATOM   10644 C  CB  . ARG G  1 25  ? 2.851   0.611   54.582 1.00 97.01  ? 16  ARG G CB  1 
ATOM   10645 C  CG  . ARG G  1 25  ? 3.892   -0.291  53.944 1.00 95.69  ? 16  ARG G CG  1 
ATOM   10646 C  CD  . ARG G  1 25  ? 4.205   -1.420  54.913 1.00 103.79 ? 16  ARG G CD  1 
ATOM   10647 N  NE  . ARG G  1 25  ? 2.986   -1.996  55.483 1.00 103.31 ? 16  ARG G NE  1 
ATOM   10648 C  CZ  . ARG G  1 25  ? 2.402   -1.578  56.607 1.00 104.80 ? 16  ARG G CZ  1 
ATOM   10649 N  NH1 . ARG G  1 25  ? 2.924   -0.577  57.312 1.00 91.73  ? 16  ARG G NH1 1 
ATOM   10650 N  NH2 . ARG G  1 25  ? 1.287   -2.165  57.031 1.00 101.71 ? 16  ARG G NH2 1 
ATOM   10651 N  N   . SER G  1 26  ? 0.219   2.980   54.098 1.00 96.87  ? 17  SER G N   1 
ATOM   10652 C  CA  . SER G  1 26  ? -1.042  3.512   54.599 1.00 97.04  ? 17  SER G CA  1 
ATOM   10653 C  C   . SER G  1 26  ? -1.298  4.818   53.860 1.00 99.84  ? 17  SER G C   1 
ATOM   10654 O  O   . SER G  1 26  ? -0.374  5.603   53.626 1.00 94.73  ? 17  SER G O   1 
ATOM   10655 C  CB  . SER G  1 26  ? -0.969  3.782   56.103 1.00 92.77  ? 17  SER G CB  1 
ATOM   10656 O  OG  . SER G  1 26  ? -1.381  2.663   56.859 1.00 71.53  ? 17  SER G OG  1 
ATOM   10657 N  N   . PRO G  1 27  ? -2.563  5.025   53.450 1.00 110.15 ? 18  PRO G N   1 
ATOM   10658 C  CA  . PRO G  1 27  ? -3.040  6.118   52.590 1.00 106.23 ? 18  PRO G CA  1 
ATOM   10659 C  C   . PRO G  1 27  ? -3.233  7.401   53.372 1.00 109.91 ? 18  PRO G C   1 
ATOM   10660 O  O   . PRO G  1 27  ? -3.436  7.345   54.591 1.00 101.99 ? 18  PRO G O   1 
ATOM   10661 C  CB  . PRO G  1 27  ? -4.398  5.611   52.117 1.00 98.48  ? 18  PRO G CB  1 
ATOM   10662 C  CG  . PRO G  1 27  ? -4.896  4.808   53.279 1.00 107.65 ? 18  PRO G CG  1 
ATOM   10663 C  CD  . PRO G  1 27  ? -3.675  4.174   53.916 1.00 105.86 ? 18  PRO G CD  1 
ATOM   10664 N  N   . MET G  1 28  ? -3.200  8.537   52.681 1.00 109.33 ? 19  MET G N   1 
ATOM   10665 C  CA  . MET G  1 28  ? -3.354  9.825   53.354 1.00 105.92 ? 19  MET G CA  1 
ATOM   10666 C  C   . MET G  1 28  ? -4.710  9.918   54.051 1.00 99.07  ? 19  MET G C   1 
ATOM   10667 O  O   . MET G  1 28  ? -5.682  9.275   53.652 1.00 98.00  ? 19  MET G O   1 
ATOM   10668 C  CB  . MET G  1 28  ? -3.166  11.008  52.393 1.00 97.99  ? 19  MET G CB  1 
ATOM   10669 C  CG  . MET G  1 28  ? -2.767  12.307  53.102 1.00 92.00  ? 19  MET G CG  1 
ATOM   10670 S  SD  . MET G  1 28  ? -2.989  13.810  52.120 1.00 96.39  ? 19  MET G SD  1 
ATOM   10671 C  CE  . MET G  1 28  ? -4.775  13.961  52.146 1.00 82.59  ? 19  MET G CE  1 
ATOM   10672 N  N   . TYR G  1 29  ? -4.745  10.708  55.114 1.00 82.33  ? 20  TYR G N   1 
ATOM   10673 C  CA  . TYR G  1 29  ? -5.951  10.969  55.870 1.00 72.98  ? 20  TYR G CA  1 
ATOM   10674 C  C   . TYR G  1 29  ? -7.017  11.542  54.929 1.00 77.20  ? 20  TYR G C   1 
ATOM   10675 O  O   . TYR G  1 29  ? -6.718  12.387  54.080 1.00 74.06  ? 20  TYR G O   1 
ATOM   10676 C  CB  . TYR G  1 29  ? -5.571  11.956  56.973 1.00 73.55  ? 20  TYR G CB  1 
ATOM   10677 C  CG  . TYR G  1 29  ? -6.603  12.273  58.027 1.00 69.09  ? 20  TYR G CG  1 
ATOM   10678 C  CD1 . TYR G  1 29  ? -7.128  11.290  58.850 1.00 64.93  ? 20  TYR G CD1 1 
ATOM   10679 C  CD2 . TYR G  1 29  ? -6.999  13.587  58.237 1.00 69.60  ? 20  TYR G CD2 1 
ATOM   10680 C  CE1 . TYR G  1 29  ? -8.053  11.614  59.821 1.00 69.92  ? 20  TYR G CE1 1 
ATOM   10681 C  CE2 . TYR G  1 29  ? -7.911  13.919  59.198 1.00 62.21  ? 20  TYR G CE2 1 
ATOM   10682 C  CZ  . TYR G  1 29  ? -8.438  12.942  59.989 1.00 68.43  ? 20  TYR G CZ  1 
ATOM   10683 O  OH  . TYR G  1 29  ? -9.351  13.324  60.953 1.00 76.00  ? 20  TYR G OH  1 
ATOM   10684 N  N   . PRO G  1 30  ? -8.258  11.043  55.037 1.00 69.56  ? 21  PRO G N   1 
ATOM   10685 C  CA  . PRO G  1 30  ? -9.395  11.570  54.270 1.00 65.88  ? 21  PRO G CA  1 
ATOM   10686 C  C   . PRO G  1 30  ? -9.873  12.953  54.732 1.00 68.48  ? 21  PRO G C   1 
ATOM   10687 O  O   . PRO G  1 30  ? -10.582 13.629  53.968 1.00 68.62  ? 21  PRO G O   1 
ATOM   10688 C  CB  . PRO G  1 30  ? -10.494 10.534  54.518 1.00 56.94  ? 21  PRO G CB  1 
ATOM   10689 C  CG  . PRO G  1 30  ? -10.136 9.914   55.801 1.00 61.35  ? 21  PRO G CG  1 
ATOM   10690 C  CD  . PRO G  1 30  ? -8.639  9.879   55.851 1.00 67.95  ? 21  PRO G CD  1 
ATOM   10691 N  N   . GLY G  1 31  ? -9.490  13.344  55.953 1.00 61.25  ? 22  GLY G N   1 
ATOM   10692 C  CA  . GLY G  1 31  ? -9.993  14.533  56.619 1.00 60.03  ? 22  GLY G CA  1 
ATOM   10693 C  C   . GLY G  1 31  ? -10.912 14.225  57.791 1.00 58.66  ? 22  GLY G C   1 
ATOM   10694 O  O   . GLY G  1 31  ? -11.369 13.103  57.936 1.00 62.22  ? 22  GLY G O   1 
ATOM   10695 N  N   . PRO G  1 32  ? -11.192 15.227  58.640 1.00 59.03  ? 23  PRO G N   1 
ATOM   10696 C  CA  . PRO G  1 32  ? -12.068 15.029  59.796 1.00 57.77  ? 23  PRO G CA  1 
ATOM   10697 C  C   . PRO G  1 32  ? -13.518 14.857  59.393 1.00 63.86  ? 23  PRO G C   1 
ATOM   10698 O  O   . PRO G  1 32  ? -13.960 15.420  58.390 1.00 58.12  ? 23  PRO G O   1 
ATOM   10699 C  CB  . PRO G  1 32  ? -11.929 16.341  60.563 1.00 60.31  ? 23  PRO G CB  1 
ATOM   10700 C  CG  . PRO G  1 32  ? -11.649 17.330  59.530 1.00 64.54  ? 23  PRO G CG  1 
ATOM   10701 C  CD  . PRO G  1 32  ? -10.772 16.632  58.521 1.00 62.59  ? 23  PRO G CD  1 
ATOM   10702 N  N   . THR G  1 33  ? -14.251 14.089  60.191 1.00 67.35  ? 24  THR G N   1 
ATOM   10703 C  CA  . THR G  1 33  ? -15.680 13.908  59.995 1.00 66.78  ? 24  THR G CA  1 
ATOM   10704 C  C   . THR G  1 33  ? -16.403 14.106  61.319 1.00 66.63  ? 24  THR G C   1 
ATOM   10705 O  O   . THR G  1 33  ? -15.769 14.181  62.371 1.00 63.58  ? 24  THR G O   1 
ATOM   10706 C  CB  . THR G  1 33  ? -16.004 12.519  59.419 1.00 66.24  ? 24  THR G CB  1 
ATOM   10707 O  OG1 . THR G  1 33  ? -15.424 11.502  60.244 1.00 70.84  ? 24  THR G OG1 1 
ATOM   10708 C  CG2 . THR G  1 33  ? -15.449 12.390  58.016 1.00 57.34  ? 24  THR G CG2 1 
ATOM   10709 N  N   . LYS G  1 34  ? -17.728 14.204  61.260 1.00 68.57  ? 25  LYS G N   1 
ATOM   10710 C  CA  . LYS G  1 34  ? -18.543 14.290  62.469 1.00 71.66  ? 25  LYS G CA  1 
ATOM   10711 C  C   . LYS G  1 34  ? -18.259 13.129  63.428 1.00 69.02  ? 25  LYS G C   1 
ATOM   10712 O  O   . LYS G  1 34  ? -18.276 13.314  64.645 1.00 74.06  ? 25  LYS G O   1 
ATOM   10713 C  CB  . LYS G  1 34  ? -20.039 14.372  62.124 1.00 72.60  ? 25  LYS G CB  1 
ATOM   10714 C  CG  . LYS G  1 34  ? -20.444 13.579  60.889 1.00 79.94  ? 25  LYS G CG  1 
ATOM   10715 C  CD  . LYS G  1 34  ? -21.954 13.431  60.775 1.00 80.34  ? 25  LYS G CD  1 
ATOM   10716 C  CE  . LYS G  1 34  ? -22.313 12.294  59.822 1.00 85.66  ? 25  LYS G CE  1 
ATOM   10717 N  NZ  . LYS G  1 34  ? -23.765 11.956  59.822 1.00 87.01  ? 25  LYS G NZ  1 
ATOM   10718 N  N   . ASP G  1 35  ? -17.979 11.952  62.867 1.00 66.48  ? 26  ASP G N   1 
ATOM   10719 C  CA  . ASP G  1 35  ? -17.689 10.739  63.637 1.00 69.21  ? 26  ASP G CA  1 
ATOM   10720 C  C   . ASP G  1 35  ? -16.225 10.642  64.054 1.00 71.42  ? 26  ASP G C   1 
ATOM   10721 O  O   . ASP G  1 35  ? -15.836 9.778   64.854 1.00 70.22  ? 26  ASP G O   1 
ATOM   10722 C  CB  . ASP G  1 35  ? -18.047 9.502   62.820 1.00 65.31  ? 26  ASP G CB  1 
ATOM   10723 C  CG  . ASP G  1 35  ? -19.483 9.493   62.400 1.00 77.38  ? 26  ASP G CG  1 
ATOM   10724 O  OD1 . ASP G  1 35  ? -20.341 9.754   63.265 1.00 79.60  ? 26  ASP G OD1 1 
ATOM   10725 O  OD2 . ASP G  1 35  ? -19.757 9.251   61.206 1.00 76.92  ? 26  ASP G OD2 1 
ATOM   10726 N  N   . ASP G  1 36  ? -15.416 11.515  63.474 1.00 69.87  ? 27  ASP G N   1 
ATOM   10727 C  CA  . ASP G  1 36  ? -13.990 11.552  63.736 1.00 72.26  ? 27  ASP G CA  1 
ATOM   10728 C  C   . ASP G  1 36  ? -13.615 13.018  63.705 1.00 68.92  ? 27  ASP G C   1 
ATOM   10729 O  O   . ASP G  1 36  ? -13.006 13.479  62.744 1.00 72.08  ? 27  ASP G O   1 
ATOM   10730 C  CB  . ASP G  1 36  ? -13.241 10.777  62.640 1.00 71.42  ? 27  ASP G CB  1 
ATOM   10731 C  CG  . ASP G  1 36  ? -11.741 10.650  62.905 1.00 74.17  ? 27  ASP G CG  1 
ATOM   10732 O  OD1 . ASP G  1 36  ? -11.327 10.524  64.083 1.00 81.01  ? 27  ASP G OD1 1 
ATOM   10733 O  OD2 . ASP G  1 36  ? -10.976 10.661  61.918 1.00 65.70  ? 27  ASP G OD2 1 
ATOM   10734 N  N   . PRO G  1 37  ? -14.006 13.768  64.742 1.00 67.28  ? 28  PRO G N   1 
ATOM   10735 C  CA  . PRO G  1 37  ? -13.778 15.214  64.791 1.00 60.07  ? 28  PRO G CA  1 
ATOM   10736 C  C   . PRO G  1 37  ? -12.330 15.519  65.112 1.00 57.03  ? 28  PRO G C   1 
ATOM   10737 O  O   . PRO G  1 37  ? -11.629 14.684  65.667 1.00 65.98  ? 28  PRO G O   1 
ATOM   10738 C  CB  . PRO G  1 37  ? -14.675 15.673  65.944 1.00 60.26  ? 28  PRO G CB  1 
ATOM   10739 C  CG  . PRO G  1 37  ? -15.561 14.500  66.264 1.00 73.07  ? 28  PRO G CG  1 
ATOM   10740 C  CD  . PRO G  1 37  ? -14.731 13.302  65.928 1.00 72.59  ? 28  PRO G CD  1 
ATOM   10741 N  N   . LEU G  1 38  ? -11.883 16.709  64.763 1.00 48.66  ? 29  LEU G N   1 
ATOM   10742 C  CA  . LEU G  1 38  ? -10.511 17.092  65.004 1.00 49.87  ? 29  LEU G CA  1 
ATOM   10743 C  C   . LEU G  1 38  ? -10.414 18.483  65.652 1.00 56.16  ? 29  LEU G C   1 
ATOM   10744 O  O   . LEU G  1 38  ? -11.188 19.382  65.340 1.00 51.79  ? 29  LEU G O   1 
ATOM   10745 C  CB  . LEU G  1 38  ? -9.784  17.093  63.680 1.00 56.35  ? 29  LEU G CB  1 
ATOM   10746 C  CG  . LEU G  1 38  ? -8.330  17.490  63.786 1.00 60.71  ? 29  LEU G CG  1 
ATOM   10747 C  CD1 . LEU G  1 38  ? -7.586  16.338  64.417 1.00 60.90  ? 29  LEU G CD1 1 
ATOM   10748 C  CD2 . LEU G  1 38  ? -7.803  17.816  62.405 1.00 55.84  ? 29  LEU G CD2 1 
ATOM   10749 N  N   . THR G  1 39  ? -9.465  18.656  66.562 1.00 52.87  ? 30  THR G N   1 
ATOM   10750 C  CA  . THR G  1 39  ? -9.239  19.956  67.176 1.00 55.89  ? 30  THR G CA  1 
ATOM   10751 C  C   . THR G  1 39  ? -7.942  20.546  66.655 1.00 59.20  ? 30  THR G C   1 
ATOM   10752 O  O   . THR G  1 39  ? -6.895  19.896  66.691 1.00 61.80  ? 30  THR G O   1 
ATOM   10753 C  CB  . THR G  1 39  ? -9.173  19.877  68.719 1.00 64.74  ? 30  THR G CB  1 
ATOM   10754 O  OG1 . THR G  1 39  ? -10.446 19.478  69.234 1.00 65.33  ? 30  THR G OG1 1 
ATOM   10755 C  CG2 . THR G  1 39  ? -8.811  21.231  69.317 1.00 63.06  ? 30  THR G CG2 1 
ATOM   10756 N  N   . VAL G  1 40  ? -8.020  21.777  66.162 1.00 54.24  ? 31  VAL G N   1 
ATOM   10757 C  CA  . VAL G  1 40  ? -6.850  22.450  65.631 1.00 58.49  ? 31  VAL G CA  1 
ATOM   10758 C  C   . VAL G  1 40  ? -6.535  23.660  66.488 1.00 56.78  ? 31  VAL G C   1 
ATOM   10759 O  O   . VAL G  1 40  ? -7.415  24.448  66.818 1.00 54.09  ? 31  VAL G O   1 
ATOM   10760 C  CB  . VAL G  1 40  ? -7.049  22.863  64.149 1.00 57.68  ? 31  VAL G CB  1 
ATOM   10761 C  CG1 . VAL G  1 40  ? -5.814  23.575  63.617 1.00 51.33  ? 31  VAL G CG1 1 
ATOM   10762 C  CG2 . VAL G  1 40  ? -7.365  21.642  63.306 1.00 59.92  ? 31  VAL G CG2 1 
ATOM   10763 N  N   . TYR G  1 41  ? -5.269  23.794  66.853 1.00 57.03  ? 32  TYR G N   1 
ATOM   10764 C  CA  . TYR G  1 41  ? -4.842  24.877  67.719 1.00 56.04  ? 32  TYR G CA  1 
ATOM   10765 C  C   . TYR G  1 41  ? -4.196  26.012  66.947 1.00 58.07  ? 32  TYR G C   1 
ATOM   10766 O  O   . TYR G  1 41  ? -3.222  25.815  66.228 1.00 61.71  ? 32  TYR G O   1 
ATOM   10767 C  CB  . TYR G  1 41  ? -3.863  24.369  68.770 1.00 58.85  ? 32  TYR G CB  1 
ATOM   10768 C  CG  . TYR G  1 41  ? -4.494  23.518  69.837 1.00 66.41  ? 32  TYR G CG  1 
ATOM   10769 C  CD1 . TYR G  1 41  ? -5.134  24.104  70.927 1.00 60.43  ? 32  TYR G CD1 1 
ATOM   10770 C  CD2 . TYR G  1 41  ? -4.436  22.122  69.765 1.00 68.55  ? 32  TYR G CD2 1 
ATOM   10771 C  CE1 . TYR G  1 41  ? -5.709  23.330  71.915 1.00 64.11  ? 32  TYR G CE1 1 
ATOM   10772 C  CE2 . TYR G  1 41  ? -5.008  21.332  70.753 1.00 73.69  ? 32  TYR G CE2 1 
ATOM   10773 C  CZ  . TYR G  1 41  ? -5.644  21.944  71.831 1.00 75.50  ? 32  TYR G CZ  1 
ATOM   10774 O  OH  . TYR G  1 41  ? -6.218  21.173  72.822 1.00 73.67  ? 32  TYR G OH  1 
ATOM   10775 N  N   . LEU G  1 42  ? -4.736  27.209  67.131 1.00 56.61  ? 33  LEU G N   1 
ATOM   10776 C  CA  . LEU G  1 42  ? -4.187  28.403  66.525 1.00 49.58  ? 33  LEU G CA  1 
ATOM   10777 C  C   . LEU G  1 42  ? -3.538  29.334  67.525 1.00 54.12  ? 33  LEU G C   1 
ATOM   10778 O  O   . LEU G  1 42  ? -4.116  29.671  68.550 1.00 60.28  ? 33  LEU G O   1 
ATOM   10779 C  CB  . LEU G  1 42  ? -5.289  29.146  65.815 1.00 58.04  ? 33  LEU G CB  1 
ATOM   10780 C  CG  . LEU G  1 42  ? -5.394  28.689  64.380 1.00 62.41  ? 33  LEU G CG  1 
ATOM   10781 C  CD1 . LEU G  1 42  ? -6.615  29.332  63.761 1.00 64.82  ? 33  LEU G CD1 1 
ATOM   10782 C  CD2 . LEU G  1 42  ? -4.116  29.103  63.684 1.00 59.42  ? 33  LEU G CD2 1 
ATOM   10783 N  N   . SER G  1 43  ? -2.323  29.751  67.221 1.00 55.15  ? 34  SER G N   1 
ATOM   10784 C  CA  . SER G  1 43  ? -1.673  30.766  68.014 1.00 57.14  ? 34  SER G CA  1 
ATOM   10785 C  C   . SER G  1 43  ? -0.855  31.649  67.078 1.00 55.79  ? 34  SER G C   1 
ATOM   10786 O  O   . SER G  1 43  ? -0.171  31.136  66.196 1.00 53.90  ? 34  SER G O   1 
ATOM   10787 C  CB  . SER G  1 43  ? -0.797  30.116  69.079 1.00 55.37  ? 34  SER G CB  1 
ATOM   10788 O  OG  . SER G  1 43  ? -0.103  31.102  69.818 1.00 63.32  ? 34  SER G OG  1 
ATOM   10789 N  N   . PHE G  1 44  ? -0.932  32.966  67.270 1.00 48.60  ? 35  PHE G N   1 
ATOM   10790 C  CA  . PHE G  1 44  ? -0.218  33.916  66.425 1.00 46.75  ? 35  PHE G CA  1 
ATOM   10791 C  C   . PHE G  1 44  ? 0.926   34.639  67.115 1.00 52.79  ? 35  PHE G C   1 
ATOM   10792 O  O   . PHE G  1 44  ? 0.893   34.890  68.306 1.00 53.79  ? 35  PHE G O   1 
ATOM   10793 C  CB  . PHE G  1 44  ? -1.175  34.963  65.871 1.00 50.94  ? 35  PHE G CB  1 
ATOM   10794 C  CG  . PHE G  1 44  ? -2.277  34.391  65.048 1.00 54.87  ? 35  PHE G CG  1 
ATOM   10795 C  CD1 . PHE G  1 44  ? -2.107  34.184  63.694 1.00 50.68  ? 35  PHE G CD1 1 
ATOM   10796 C  CD2 . PHE G  1 44  ? -3.487  34.056  65.632 1.00 56.47  ? 35  PHE G CD2 1 
ATOM   10797 C  CE1 . PHE G  1 44  ? -3.124  33.661  62.948 1.00 54.08  ? 35  PHE G CE1 1 
ATOM   10798 C  CE2 . PHE G  1 44  ? -4.509  33.535  64.889 1.00 52.45  ? 35  PHE G CE2 1 
ATOM   10799 C  CZ  . PHE G  1 44  ? -4.328  33.331  63.548 1.00 56.71  ? 35  PHE G CZ  1 
ATOM   10800 N  N   . SER G  1 45  ? 1.936   34.979  66.332 1.00 51.07  ? 36  SER G N   1 
ATOM   10801 C  CA  . SER G  1 45  ? 3.058   35.757  66.794 1.00 48.05  ? 36  SER G CA  1 
ATOM   10802 C  C   . SER G  1 45  ? 3.343   36.854  65.756 1.00 50.58  ? 36  SER G C   1 
ATOM   10803 O  O   . SER G  1 45  ? 3.710   36.542  64.636 1.00 55.50  ? 36  SER G O   1 
ATOM   10804 C  CB  . SER G  1 45  ? 4.242   34.815  66.945 1.00 46.28  ? 36  SER G CB  1 
ATOM   10805 O  OG  . SER G  1 45  ? 5.396   35.494  67.377 1.00 63.44  ? 36  SER G OG  1 
ATOM   10806 N  N   . LEU G  1 46  ? 3.176   38.134  66.112 1.00 52.73  ? 37  LEU G N   1 
ATOM   10807 C  CA  . LEU G  1 46  ? 3.346   39.239  65.141 1.00 46.27  ? 37  LEU G CA  1 
ATOM   10808 C  C   . LEU G  1 46  ? 4.775   39.676  64.913 1.00 46.13  ? 37  LEU G C   1 
ATOM   10809 O  O   . LEU G  1 46  ? 5.558   39.791  65.841 1.00 56.41  ? 37  LEU G O   1 
ATOM   10810 C  CB  . LEU G  1 46  ? 2.574   40.476  65.569 1.00 48.66  ? 37  LEU G CB  1 
ATOM   10811 C  CG  . LEU G  1 46  ? 1.174   40.760  65.051 1.00 58.46  ? 37  LEU G CG  1 
ATOM   10812 C  CD1 . LEU G  1 46  ? 0.298   39.523  65.111 1.00 63.64  ? 37  LEU G CD1 1 
ATOM   10813 C  CD2 . LEU G  1 46  ? 0.576   41.885  65.874 1.00 54.38  ? 37  LEU G CD2 1 
ATOM   10814 N  N   . LEU G  1 47  ? 5.095   39.975  63.669 1.00 47.66  ? 38  LEU G N   1 
ATOM   10815 C  CA  . LEU G  1 47  ? 6.440   40.397  63.298 1.00 55.35  ? 38  LEU G CA  1 
ATOM   10816 C  C   . LEU G  1 47  ? 6.516   41.841  62.822 1.00 53.72  ? 38  LEU G C   1 
ATOM   10817 O  O   . LEU G  1 47  ? 7.285   42.634  63.336 1.00 59.10  ? 38  LEU G O   1 
ATOM   10818 C  CB  . LEU G  1 47  ? 7.055   39.456  62.271 1.00 58.72  ? 38  LEU G CB  1 
ATOM   10819 C  CG  . LEU G  1 47  ? 7.958   38.392  62.885 1.00 58.86  ? 38  LEU G CG  1 
ATOM   10820 C  CD1 . LEU G  1 47  ? 7.121   37.412  63.686 1.00 56.90  ? 38  LEU G CD1 1 
ATOM   10821 C  CD2 . LEU G  1 47  ? 8.738   37.684  61.801 1.00 57.16  ? 38  LEU G CD2 1 
ATOM   10822 N  N   . ASP G  1 48  ? 5.778   42.166  61.775 1.00 56.42  ? 39  ASP G N   1 
ATOM   10823 C  CA  . ASP G  1 48  ? 5.780   43.533  61.282 1.00 58.46  ? 39  ASP G CA  1 
ATOM   10824 C  C   . ASP G  1 48  ? 4.394   43.932  60.816 1.00 55.83  ? 39  ASP G C   1 
ATOM   10825 O  O   . ASP G  1 48  ? 3.719   43.155  60.147 1.00 51.88  ? 39  ASP G O   1 
ATOM   10826 C  CB  . ASP G  1 48  ? 6.771   43.688  60.121 1.00 54.75  ? 39  ASP G CB  1 
ATOM   10827 C  CG  . ASP G  1 48  ? 7.319   45.095  60.015 1.00 61.94  ? 39  ASP G CG  1 
ATOM   10828 O  OD1 . ASP G  1 48  ? 6.869   45.960  60.798 1.00 59.49  ? 39  ASP G OD1 1 
ATOM   10829 O  OD2 . ASP G  1 48  ? 8.192   45.347  59.154 1.00 65.52  ? 39  ASP G OD2 1 
ATOM   10830 N  N   . ILE G  1 49  ? 3.964   45.136  61.179 1.00 52.07  ? 40  ILE G N   1 
ATOM   10831 C  CA  . ILE G  1 49  ? 2.918   45.764  60.411 1.00 51.16  ? 40  ILE G CA  1 
ATOM   10832 C  C   . ILE G  1 49  ? 3.700   46.598  59.407 1.00 55.41  ? 40  ILE G C   1 
ATOM   10833 O  O   . ILE G  1 49  ? 4.310   47.604  59.764 1.00 60.87  ? 40  ILE G O   1 
ATOM   10834 C  CB  . ILE G  1 49  ? 2.002   46.626  61.273 1.00 49.42  ? 40  ILE G CB  1 
ATOM   10835 C  CG1 . ILE G  1 49  ? 1.190   45.744  62.213 1.00 50.36  ? 40  ILE G CG1 1 
ATOM   10836 C  CG2 . ILE G  1 49  ? 1.058   47.433  60.402 1.00 45.03  ? 40  ILE G CG2 1 
ATOM   10837 C  CD1 . ILE G  1 49  ? 0.134   46.493  63.007 1.00 48.75  ? 40  ILE G CD1 1 
ATOM   10838 N  N   . VAL G  1 50  ? 3.695   46.146  58.153 1.00 53.14  ? 41  VAL G N   1 
ATOM   10839 C  CA  . VAL G  1 50  ? 4.548   46.700  57.104 1.00 52.61  ? 41  VAL G CA  1 
ATOM   10840 C  C   . VAL G  1 50  ? 3.994   47.979  56.507 1.00 53.53  ? 41  VAL G C   1 
ATOM   10841 O  O   . VAL G  1 50  ? 4.715   48.965  56.308 1.00 54.20  ? 41  VAL G O   1 
ATOM   10842 C  CB  . VAL G  1 50  ? 4.764   45.701  55.949 1.00 48.71  ? 41  VAL G CB  1 
ATOM   10843 C  CG1 . VAL G  1 50  ? 5.627   46.331  54.886 1.00 48.92  ? 41  VAL G CG1 1 
ATOM   10844 C  CG2 . VAL G  1 50  ? 5.411   44.442  56.453 1.00 51.98  ? 41  VAL G CG2 1 
ATOM   10845 N  N   . LYS G  1 51  ? 2.707   47.945  56.204 1.00 49.71  ? 42  LYS G N   1 
ATOM   10846 C  CA  . LYS G  1 51  ? 2.095   49.043  55.504 1.00 51.77  ? 42  LYS G CA  1 
ATOM   10847 C  C   . LYS G  1 51  ? 0.652   49.167  55.938 1.00 57.23  ? 42  LYS G C   1 
ATOM   10848 O  O   . LYS G  1 51  ? -0.013  48.155  56.211 1.00 53.04  ? 42  LYS G O   1 
ATOM   10849 C  CB  . LYS G  1 51  ? 2.196   48.805  53.997 1.00 50.97  ? 42  LYS G CB  1 
ATOM   10850 C  CG  . LYS G  1 51  ? 1.456   49.794  53.140 1.00 59.50  ? 42  LYS G CG  1 
ATOM   10851 C  CD  . LYS G  1 51  ? 0.783   49.113  51.947 1.00 66.93  ? 42  LYS G CD  1 
ATOM   10852 C  CE  . LYS G  1 51  ? 1.653   49.155  50.692 1.00 61.25  ? 42  LYS G CE  1 
ATOM   10853 N  NZ  . LYS G  1 51  ? 0.869   48.756  49.488 1.00 76.13  ? 42  LYS G NZ  1 
ATOM   10854 N  N   . ALA G  1 52  ? 0.189   50.416  56.037 1.00 55.30  ? 43  ALA G N   1 
ATOM   10855 C  CA  . ALA G  1 52  ? -1.227  50.710  56.239 1.00 57.12  ? 43  ALA G CA  1 
ATOM   10856 C  C   . ALA G  1 52  ? -1.690  51.700  55.181 1.00 59.93  ? 43  ALA G C   1 
ATOM   10857 O  O   . ALA G  1 52  ? -1.302  52.861  55.204 1.00 69.87  ? 43  ALA G O   1 
ATOM   10858 C  CB  . ALA G  1 52  ? -1.460  51.270  57.632 1.00 58.59  ? 43  ALA G CB  1 
ATOM   10859 N  N   . ASP G  1 53  ? -2.531  51.252  54.259 1.00 60.18  ? 44  ASP G N   1 
ATOM   10860 C  CA  . ASP G  1 53  ? -2.892  52.077  53.111 1.00 60.55  ? 44  ASP G CA  1 
ATOM   10861 C  C   . ASP G  1 53  ? -4.275  52.653  53.372 1.00 61.94  ? 44  ASP G C   1 
ATOM   10862 O  O   . ASP G  1 53  ? -5.272  51.924  53.427 1.00 57.09  ? 44  ASP G O   1 
ATOM   10863 C  CB  . ASP G  1 53  ? -2.830  51.251  51.817 1.00 53.36  ? 44  ASP G CB  1 
ATOM   10864 C  CG  . ASP G  1 53  ? -3.324  52.009  50.596 1.00 59.21  ? 44  ASP G CG  1 
ATOM   10865 O  OD1 . ASP G  1 53  ? -4.019  53.033  50.756 1.00 61.91  ? 44  ASP G OD1 1 
ATOM   10866 O  OD2 . ASP G  1 53  ? -3.033  51.562  49.463 1.00 59.10  ? 44  ASP G OD2 1 
ATOM   10867 N  N   . SER G  1 54  ? -4.325  53.967  53.565 1.00 64.53  ? 45  SER G N   1 
ATOM   10868 C  CA  . SER G  1 54  ? -5.557  54.606  54.010 1.00 66.24  ? 45  SER G CA  1 
ATOM   10869 C  C   . SER G  1 54  ? -6.427  54.902  52.815 1.00 59.69  ? 45  SER G C   1 
ATOM   10870 O  O   . SER G  1 54  ? -7.614  55.195  52.958 1.00 57.18  ? 45  SER G O   1 
ATOM   10871 C  CB  . SER G  1 54  ? -5.262  55.891  54.785 1.00 58.84  ? 45  SER G CB  1 
ATOM   10872 O  OG  . SER G  1 54  ? -4.910  56.916  53.888 1.00 67.20  ? 45  SER G OG  1 
ATOM   10873 N  N   . SER G  1 55  ? -5.817  54.816  51.636 1.00 60.30  ? 46  SER G N   1 
ATOM   10874 C  CA  . SER G  1 55  ? -6.511  55.070  50.378 1.00 65.27  ? 46  SER G CA  1 
ATOM   10875 C  C   . SER G  1 55  ? -7.335  53.869  49.927 1.00 60.48  ? 46  SER G C   1 
ATOM   10876 O  O   . SER G  1 55  ? -8.413  54.025  49.348 1.00 54.22  ? 46  SER G O   1 
ATOM   10877 C  CB  . SER G  1 55  ? -5.523  55.484  49.286 1.00 56.20  ? 46  SER G CB  1 
ATOM   10878 O  OG  . SER G  1 55  ? -5.158  54.379  48.494 1.00 60.99  ? 46  SER G OG  1 
ATOM   10879 N  N   . THR G  1 56  ? -6.798  52.673  50.138 1.00 57.85  ? 47  THR G N   1 
ATOM   10880 C  CA  . THR G  1 56  ? -7.560  51.462  49.862 1.00 59.69  ? 47  THR G CA  1 
ATOM   10881 C  C   . THR G  1 56  ? -8.163  50.757  51.078 1.00 56.87  ? 47  THR G C   1 
ATOM   10882 O  O   . THR G  1 56  ? -8.967  49.845  50.921 1.00 58.25  ? 47  THR G O   1 
ATOM   10883 C  CB  . THR G  1 56  ? -6.716  50.484  49.055 1.00 56.47  ? 47  THR G CB  1 
ATOM   10884 O  OG1 . THR G  1 56  ? -5.661  49.977  49.876 1.00 53.87  ? 47  THR G OG1 1 
ATOM   10885 C  CG2 . THR G  1 56  ? -6.118  51.208  47.843 1.00 55.63  ? 47  THR G CG2 1 
ATOM   10886 N  N   . ASN G  1 57  ? -7.812  51.220  52.279 1.00 61.85  ? 48  ASN G N   1 
ATOM   10887 C  CA  . ASN G  1 57  ? -8.205  50.573  53.539 1.00 57.44  ? 48  ASN G CA  1 
ATOM   10888 C  C   . ASN G  1 57  ? -7.733  49.116  53.719 1.00 54.22  ? 48  ASN G C   1 
ATOM   10889 O  O   . ASN G  1 57  ? -8.497  48.230  54.100 1.00 51.83  ? 48  ASN G O   1 
ATOM   10890 C  CB  . ASN G  1 57  ? -9.711  50.709  53.773 1.00 59.93  ? 48  ASN G CB  1 
ATOM   10891 C  CG  . ASN G  1 57  ? -10.072 51.996  54.508 1.00 67.75  ? 48  ASN G CG  1 
ATOM   10892 O  OD1 . ASN G  1 57  ? -9.197  52.797  54.857 1.00 69.31  ? 48  ASN G OD1 1 
ATOM   10893 N  ND2 . ASN G  1 57  ? -11.364 52.199  54.745 1.00 64.36  ? 48  ASN G ND2 1 
ATOM   10894 N  N   . GLU G  1 58  ? -6.455  48.892  53.447 1.00 53.18  ? 49  GLU G N   1 
ATOM   10895 C  CA  . GLU G  1 58  ? -5.842  47.582  53.562 1.00 53.13  ? 49  GLU G CA  1 
ATOM   10896 C  C   . GLU G  1 58  ? -4.617  47.695  54.454 1.00 54.31  ? 49  GLU G C   1 
ATOM   10897 O  O   . GLU G  1 58  ? -3.833  48.629  54.322 1.00 55.06  ? 49  GLU G O   1 
ATOM   10898 C  CB  . GLU G  1 58  ? -5.370  47.082  52.190 1.00 52.89  ? 49  GLU G CB  1 
ATOM   10899 C  CG  . GLU G  1 58  ? -6.443  46.608  51.231 1.00 50.94  ? 49  GLU G CG  1 
ATOM   10900 C  CD  . GLU G  1 58  ? -5.897  46.371  49.817 1.00 63.56  ? 49  GLU G CD  1 
ATOM   10901 O  OE1 . GLU G  1 58  ? -5.301  47.306  49.221 1.00 56.11  ? 49  GLU G OE1 1 
ATOM   10902 O  OE2 . GLU G  1 58  ? -6.062  45.240  49.304 1.00 60.94  ? 49  GLU G OE2 1 
ATOM   10903 N  N   . VAL G  1 59  ? -4.431  46.733  55.347 1.00 53.52  ? 50  VAL G N   1 
ATOM   10904 C  CA  . VAL G  1 59  ? -3.181  46.664  56.094 1.00 53.48  ? 50  VAL G CA  1 
ATOM   10905 C  C   . VAL G  1 59  ? -2.378  45.431  55.677 1.00 53.42  ? 50  VAL G C   1 
ATOM   10906 O  O   . VAL G  1 59  ? -2.945  44.421  55.251 1.00 46.71  ? 50  VAL G O   1 
ATOM   10907 C  CB  . VAL G  1 59  ? -3.425  46.713  57.614 1.00 51.11  ? 50  VAL G CB  1 
ATOM   10908 C  CG1 . VAL G  1 59  ? -2.216  46.262  58.376 1.00 55.44  ? 50  VAL G CG1 1 
ATOM   10909 C  CG2 . VAL G  1 59  ? -3.761  48.107  58.011 1.00 58.08  ? 50  VAL G CG2 1 
ATOM   10910 N  N   . ASP G  1 60  ? -1.056  45.548  55.765 1.00 48.36  ? 51  ASP G N   1 
ATOM   10911 C  CA  . ASP G  1 60  ? -0.165  44.448  55.446 1.00 47.21  ? 51  ASP G CA  1 
ATOM   10912 C  C   . ASP G  1 60  ? 0.587   44.042  56.688 1.00 52.02  ? 51  ASP G C   1 
ATOM   10913 O  O   . ASP G  1 60  ? 1.330   44.826  57.262 1.00 45.74  ? 51  ASP G O   1 
ATOM   10914 C  CB  . ASP G  1 60  ? 0.829   44.826  54.352 1.00 48.53  ? 51  ASP G CB  1 
ATOM   10915 C  CG  . ASP G  1 60  ? 0.186   44.907  52.973 1.00 62.59  ? 51  ASP G CG  1 
ATOM   10916 O  OD1 . ASP G  1 60  ? -1.061  45.045  52.869 1.00 60.71  ? 51  ASP G OD1 1 
ATOM   10917 O  OD2 . ASP G  1 60  ? 0.944   44.847  51.980 1.00 72.65  ? 51  ASP G OD2 1 
ATOM   10918 N  N   . LEU G  1 61  ? 0.392   42.789  57.073 1.00 55.42  ? 52  LEU G N   1 
ATOM   10919 C  CA  . LEU G  1 61  ? 0.915   42.238  58.307 1.00 49.07  ? 52  LEU G CA  1 
ATOM   10920 C  C   . LEU G  1 61  ? 1.827   41.042  58.020 1.00 50.02  ? 52  LEU G C   1 
ATOM   10921 O  O   . LEU G  1 61  ? 1.494   40.184  57.217 1.00 53.74  ? 52  LEU G O   1 
ATOM   10922 C  CB  . LEU G  1 61  ? -0.273  41.814  59.149 1.00 44.81  ? 52  LEU G CB  1 
ATOM   10923 C  CG  . LEU G  1 61  ? -0.107  41.073  60.462 1.00 57.62  ? 52  LEU G CG  1 
ATOM   10924 C  CD1 . LEU G  1 61  ? 0.677   41.886  61.503 1.00 52.83  ? 52  LEU G CD1 1 
ATOM   10925 C  CD2 . LEU G  1 61  ? -1.516  40.774  60.930 1.00 61.10  ? 52  LEU G CD2 1 
ATOM   10926 N  N   . VAL G  1 62  ? 2.992   41.010  58.650 1.00 44.59  ? 53  VAL G N   1 
ATOM   10927 C  CA  . VAL G  1 62  ? 3.871   39.851  58.595 1.00 48.74  ? 53  VAL G CA  1 
ATOM   10928 C  C   . VAL G  1 62  ? 3.770   39.073  59.914 1.00 50.93  ? 53  VAL G C   1 
ATOM   10929 O  O   . VAL G  1 62  ? 3.862   39.666  60.984 1.00 50.74  ? 53  VAL G O   1 
ATOM   10930 C  CB  . VAL G  1 62  ? 5.329   40.285  58.385 1.00 48.67  ? 53  VAL G CB  1 
ATOM   10931 C  CG1 . VAL G  1 62  ? 6.285   39.160  58.740 1.00 46.32  ? 53  VAL G CG1 1 
ATOM   10932 C  CG2 . VAL G  1 62  ? 5.541   40.745  56.960 1.00 50.97  ? 53  VAL G CG2 1 
ATOM   10933 N  N   . TYR G  1 63  ? 3.577   37.759  59.857 1.00 48.20  ? 54  TYR G N   1 
ATOM   10934 C  CA  . TYR G  1 63  ? 3.428   37.000  61.093 1.00 51.39  ? 54  TYR G CA  1 
ATOM   10935 C  C   . TYR G  1 63  ? 3.706   35.498  60.993 1.00 52.06  ? 54  TYR G C   1 
ATOM   10936 O  O   . TYR G  1 63  ? 3.951   34.972  59.908 1.00 49.80  ? 54  TYR G O   1 
ATOM   10937 C  CB  . TYR G  1 63  ? 2.024   37.214  61.643 1.00 50.65  ? 54  TYR G CB  1 
ATOM   10938 C  CG  . TYR G  1 63  ? 0.953   36.718  60.722 1.00 50.42  ? 54  TYR G CG  1 
ATOM   10939 C  CD1 . TYR G  1 63  ? 0.344   35.503  60.936 1.00 47.51  ? 54  TYR G CD1 1 
ATOM   10940 C  CD2 . TYR G  1 63  ? 0.557   37.465  59.631 1.00 53.19  ? 54  TYR G CD2 1 
ATOM   10941 C  CE1 . TYR G  1 63  ? -0.626  35.048  60.097 1.00 51.56  ? 54  TYR G CE1 1 
ATOM   10942 C  CE2 . TYR G  1 63  ? -0.424  37.016  58.783 1.00 52.45  ? 54  TYR G CE2 1 
ATOM   10943 C  CZ  . TYR G  1 63  ? -1.006  35.803  59.025 1.00 50.25  ? 54  TYR G CZ  1 
ATOM   10944 O  OH  . TYR G  1 63  ? -1.984  35.344  58.188 1.00 56.49  ? 54  TYR G OH  1 
ATOM   10945 N  N   . TRP G  1 64  ? 3.658   34.827  62.148 1.00 48.08  ? 55  TRP G N   1 
ATOM   10946 C  CA  . TRP G  1 64  ? 3.772   33.373  62.242 1.00 51.11  ? 55  TRP G CA  1 
ATOM   10947 C  C   . TRP G  1 64  ? 2.453   32.859  62.731 1.00 50.94  ? 55  TRP G C   1 
ATOM   10948 O  O   . TRP G  1 64  ? 1.900   33.386  63.678 1.00 50.01  ? 55  TRP G O   1 
ATOM   10949 C  CB  . TRP G  1 64  ? 4.865   32.948  63.225 1.00 48.19  ? 55  TRP G CB  1 
ATOM   10950 C  CG  . TRP G  1 64  ? 6.200   33.440  62.831 1.00 53.97  ? 55  TRP G CG  1 
ATOM   10951 C  CD1 . TRP G  1 64  ? 6.594   33.795  61.579 1.00 59.29  ? 55  TRP G CD1 1 
ATOM   10952 C  CD2 . TRP G  1 64  ? 7.321   33.677  63.683 1.00 60.58  ? 55  TRP G CD2 1 
ATOM   10953 N  NE1 . TRP G  1 64  ? 7.896   34.224  61.586 1.00 58.80  ? 55  TRP G NE1 1 
ATOM   10954 C  CE2 . TRP G  1 64  ? 8.369   34.161  62.871 1.00 66.68  ? 55  TRP G CE2 1 
ATOM   10955 C  CE3 . TRP G  1 64  ? 7.548   33.526  65.051 1.00 64.61  ? 55  TRP G CE3 1 
ATOM   10956 C  CZ2 . TRP G  1 64  ? 9.624   34.502  63.384 1.00 67.40  ? 55  TRP G CZ2 1 
ATOM   10957 C  CZ3 . TRP G  1 64  ? 8.792   33.863  65.554 1.00 69.85  ? 55  TRP G CZ3 1 
ATOM   10958 C  CH2 . TRP G  1 64  ? 9.814   34.347  64.721 1.00 65.66  ? 55  TRP G CH2 1 
ATOM   10959 N  N   . GLU G  1 65  ? 1.938   31.835  62.071 1.00 48.51  ? 56  GLU G N   1 
ATOM   10960 C  CA  . GLU G  1 65  ? 0.718   31.194  62.518 1.00 49.71  ? 56  GLU G CA  1 
ATOM   10961 C  C   . GLU G  1 65  ? 1.092   29.803  62.983 1.00 53.45  ? 56  GLU G C   1 
ATOM   10962 O  O   . GLU G  1 65  ? 1.565   29.000  62.189 1.00 54.50  ? 56  GLU G O   1 
ATOM   10963 C  CB  . GLU G  1 65  ? -0.258  31.111  61.361 1.00 46.92  ? 56  GLU G CB  1 
ATOM   10964 C  CG  . GLU G  1 65  ? -1.653  30.635  61.676 1.00 46.54  ? 56  GLU G CG  1 
ATOM   10965 C  CD  . GLU G  1 65  ? -2.530  30.756  60.439 1.00 57.62  ? 56  GLU G CD  1 
ATOM   10966 O  OE1 . GLU G  1 65  ? -2.106  31.492  59.528 1.00 60.36  ? 56  GLU G OE1 1 
ATOM   10967 O  OE2 . GLU G  1 65  ? -3.611  30.129  60.345 1.00 54.50  ? 56  GLU G OE2 1 
ATOM   10968 N  N   . GLN G  1 66  ? 0.922   29.516  64.268 1.00 49.85  ? 57  GLN G N   1 
ATOM   10969 C  CA  . GLN G  1 66  ? 1.114   28.156  64.706 1.00 49.41  ? 57  GLN G CA  1 
ATOM   10970 C  C   . GLN G  1 66  ? -0.179  27.365  64.676 1.00 50.13  ? 57  GLN G C   1 
ATOM   10971 O  O   . GLN G  1 66  ? -1.204  27.808  65.191 1.00 48.29  ? 57  GLN G O   1 
ATOM   10972 C  CB  . GLN G  1 66  ? 1.713   28.079  66.089 1.00 57.26  ? 57  GLN G CB  1 
ATOM   10973 C  CG  . GLN G  1 66  ? 1.425   26.720  66.689 1.00 65.41  ? 57  GLN G CG  1 
ATOM   10974 C  CD  . GLN G  1 66  ? 2.259   26.426  67.879 1.00 63.67  ? 57  GLN G CD  1 
ATOM   10975 O  OE1 . GLN G  1 66  ? 1.934   26.834  68.986 1.00 77.94  ? 57  GLN G OE1 1 
ATOM   10976 N  NE2 . GLN G  1 66  ? 3.351   25.711  67.671 1.00 73.90  ? 57  GLN G NE2 1 
ATOM   10977 N  N   . GLN G  1 67  ? -0.108  26.186  64.061 1.00 47.72  ? 58  GLN G N   1 
ATOM   10978 C  CA  . GLN G  1 67  ? -1.231  25.265  63.978 1.00 50.20  ? 58  GLN G CA  1 
ATOM   10979 C  C   . GLN G  1 67  ? -0.789  23.913  64.489 1.00 51.88  ? 58  GLN G C   1 
ATOM   10980 O  O   . GLN G  1 67  ? 0.260   23.404  64.097 1.00 52.59  ? 58  GLN G O   1 
ATOM   10981 C  CB  . GLN G  1 67  ? -1.711  25.115  62.539 1.00 43.85  ? 58  GLN G CB  1 
ATOM   10982 C  CG  . GLN G  1 67  ? -1.839  26.415  61.788 1.00 50.19  ? 58  GLN G CG  1 
ATOM   10983 C  CD  . GLN G  1 67  ? -2.375  26.224  60.389 1.00 48.92  ? 58  GLN G CD  1 
ATOM   10984 O  OE1 . GLN G  1 67  ? -2.545  25.101  59.933 1.00 51.22  ? 58  GLN G OE1 1 
ATOM   10985 N  NE2 . GLN G  1 67  ? -2.646  27.323  59.703 1.00 47.04  ? 58  GLN G NE2 1 
ATOM   10986 N  N   . SER G  1 68  ? -1.587  23.331  65.372 1.00 50.51  ? 59  SER G N   1 
ATOM   10987 C  CA  . SER G  1 68  ? -1.280  22.019  65.901 1.00 48.21  ? 59  SER G CA  1 
ATOM   10988 C  C   . SER G  1 68  ? -2.529  21.199  65.845 1.00 53.05  ? 59  SER G C   1 
ATOM   10989 O  O   . SER G  1 68  ? -3.626  21.724  66.042 1.00 54.25  ? 59  SER G O   1 
ATOM   10990 C  CB  . SER G  1 68  ? -0.825  22.101  67.352 1.00 51.00  ? 59  SER G CB  1 
ATOM   10991 O  OG  . SER G  1 68  ? 0.334   22.896  67.488 1.00 63.94  ? 59  SER G OG  1 
ATOM   10992 N  N   . TRP G  1 69  ? -2.361  19.909  65.576 1.00 51.14  ? 60  TRP G N   1 
ATOM   10993 C  CA  . TRP G  1 69  ? -3.466  18.966  65.663 1.00 54.62  ? 60  TRP G CA  1 
ATOM   10994 C  C   . TRP G  1 69  ? -2.958  17.579  65.991 1.00 55.28  ? 60  TRP G C   1 
ATOM   10995 O  O   . TRP G  1 69  ? -1.756  17.330  65.965 1.00 55.11  ? 60  TRP G O   1 
ATOM   10996 C  CB  . TRP G  1 69  ? -4.338  18.974  64.406 1.00 50.72  ? 60  TRP G CB  1 
ATOM   10997 C  CG  . TRP G  1 69  ? -3.638  18.597  63.155 1.00 53.24  ? 60  TRP G CG  1 
ATOM   10998 C  CD1 . TRP G  1 69  ? -3.633  17.371  62.565 1.00 52.36  ? 60  TRP G CD1 1 
ATOM   10999 C  CD2 . TRP G  1 69  ? -2.864  19.459  62.301 1.00 50.94  ? 60  TRP G CD2 1 
ATOM   11000 N  NE1 . TRP G  1 69  ? -2.897  17.413  61.403 1.00 54.06  ? 60  TRP G NE1 1 
ATOM   11001 C  CE2 . TRP G  1 69  ? -2.413  18.681  61.223 1.00 46.55  ? 60  TRP G CE2 1 
ATOM   11002 C  CE3 . TRP G  1 69  ? -2.511  20.812  62.346 1.00 50.35  ? 60  TRP G CE3 1 
ATOM   11003 C  CZ2 . TRP G  1 69  ? -1.618  19.203  60.211 1.00 48.88  ? 60  TRP G CZ2 1 
ATOM   11004 C  CZ3 . TRP G  1 69  ? -1.720  21.329  61.330 1.00 48.30  ? 60  TRP G CZ3 1 
ATOM   11005 C  CH2 . TRP G  1 69  ? -1.282  20.524  60.283 1.00 48.67  ? 60  TRP G CH2 1 
ATOM   11006 N  N   . LYS G  1 70  ? -3.871  16.692  66.363 1.00 60.31  ? 61  LYS G N   1 
ATOM   11007 C  CA  . LYS G  1 70  ? -3.487  15.326  66.703 1.00 62.55  ? 61  LYS G CA  1 
ATOM   11008 C  C   . LYS G  1 70  ? -4.200  14.269  65.836 1.00 63.11  ? 61  LYS G C   1 
ATOM   11009 O  O   . LYS G  1 70  ? -5.431  14.181  65.800 1.00 58.47  ? 61  LYS G O   1 
ATOM   11010 C  CB  . LYS G  1 70  ? -3.707  15.083  68.195 1.00 62.26  ? 61  LYS G CB  1 
ATOM   11011 C  CG  . LYS G  1 70  ? -2.964  13.905  68.746 1.00 65.75  ? 61  LYS G CG  1 
ATOM   11012 C  CD  . LYS G  1 70  ? -3.841  12.676  68.808 1.00 69.93  ? 61  LYS G CD  1 
ATOM   11013 C  CE  . LYS G  1 70  ? -3.212  11.639  69.735 1.00 82.24  ? 61  LYS G CE  1 
ATOM   11014 N  NZ  . LYS G  1 70  ? -3.953  10.344  69.766 1.00 83.18  ? 61  LYS G NZ  1 
ATOM   11015 N  N   . LEU G  1 71  ? -3.406  13.481  65.122 1.00 57.65  ? 62  LEU G N   1 
ATOM   11016 C  CA  . LEU G  1 71  ? -3.944  12.409  64.304 1.00 56.70  ? 62  LEU G CA  1 
ATOM   11017 C  C   . LEU G  1 71  ? -3.513  11.041  64.831 1.00 64.01  ? 62  LEU G C   1 
ATOM   11018 O  O   . LEU G  1 71  ? -2.326  10.805  65.074 1.00 59.83  ? 62  LEU G O   1 
ATOM   11019 C  CB  . LEU G  1 71  ? -3.522  12.571  62.839 1.00 55.14  ? 62  LEU G CB  1 
ATOM   11020 C  CG  . LEU G  1 71  ? -4.185  13.660  62.002 1.00 50.01  ? 62  LEU G CG  1 
ATOM   11021 C  CD1 . LEU G  1 71  ? -3.811  13.447  60.572 1.00 52.13  ? 62  LEU G CD1 1 
ATOM   11022 C  CD2 . LEU G  1 71  ? -5.677  13.624  62.142 1.00 56.54  ? 62  LEU G CD2 1 
ATOM   11023 N  N   . ASN G  1 72  ? -4.489  10.149  65.005 1.00 63.30  ? 63  ASN G N   1 
ATOM   11024 C  CA  . ASN G  1 72  ? -4.214  8.783   65.436 1.00 65.06  ? 63  ASN G CA  1 
ATOM   11025 C  C   . ASN G  1 72  ? -3.389  8.038   64.391 1.00 60.28  ? 63  ASN G C   1 
ATOM   11026 O  O   . ASN G  1 72  ? -2.572  7.194   64.741 1.00 60.66  ? 63  ASN G O   1 
ATOM   11027 C  CB  . ASN G  1 72  ? -5.515  8.022   65.752 1.00 75.69  ? 63  ASN G CB  1 
ATOM   11028 C  CG  . ASN G  1 72  ? -6.142  8.424   67.097 1.00 79.02  ? 63  ASN G CG  1 
ATOM   11029 O  OD1 . ASN G  1 72  ? -5.514  9.085   67.925 1.00 75.84  ? 63  ASN G OD1 1 
ATOM   11030 N  ND2 . ASN G  1 72  ? -7.380  7.999   67.318 1.00 81.08  ? 63  ASN G ND2 1 
ATOM   11031 N  N   . SER G  1 73  ? -3.607  8.376   63.116 1.00 64.13  ? 64  SER G N   1 
ATOM   11032 C  CA  . SER G  1 73  ? -2.915  7.772   61.966 1.00 56.21  ? 64  SER G CA  1 
ATOM   11033 C  C   . SER G  1 73  ? -1.408  7.966   61.978 1.00 65.42  ? 64  SER G C   1 
ATOM   11034 O  O   . SER G  1 73  ? -0.682  7.208   61.330 1.00 64.91  ? 64  SER G O   1 
ATOM   11035 C  CB  . SER G  1 73  ? -3.440  8.373   60.672 1.00 57.75  ? 64  SER G CB  1 
ATOM   11036 O  OG  . SER G  1 73  ? -4.723  8.920   60.877 1.00 66.85  ? 64  SER G OG  1 
ATOM   11037 N  N   . LEU G  1 74  ? -0.963  9.009   62.684 1.00 66.41  ? 65  LEU G N   1 
ATOM   11038 C  CA  . LEU G  1 74  ? 0.444   9.396   62.774 1.00 58.67  ? 65  LEU G CA  1 
ATOM   11039 C  C   . LEU G  1 74  ? 1.188   8.942   64.030 1.00 62.44  ? 65  LEU G C   1 
ATOM   11040 O  O   . LEU G  1 74  ? 2.362   9.281   64.204 1.00 64.20  ? 65  LEU G O   1 
ATOM   11041 C  CB  . LEU G  1 74  ? 0.568   10.903  62.609 1.00 60.33  ? 65  LEU G CB  1 
ATOM   11042 C  CG  . LEU G  1 74  ? 0.164   11.377  61.218 1.00 61.45  ? 65  LEU G CG  1 
ATOM   11043 C  CD1 . LEU G  1 74  ? -0.293  12.810  61.230 1.00 55.21  ? 65  LEU G CD1 1 
ATOM   11044 C  CD2 . LEU G  1 74  ? 1.309   11.179  60.248 1.00 64.84  ? 65  LEU G CD2 1 
ATOM   11045 N  N   . MET G  1 75  ? 0.514   8.196   64.906 1.00 65.35  ? 66  MET G N   1 
ATOM   11046 C  CA  . MET G  1 75  ? 1.154   7.658   66.107 1.00 60.97  ? 66  MET G CA  1 
ATOM   11047 C  C   . MET G  1 75  ? 2.089   6.496   65.757 1.00 62.00  ? 66  MET G C   1 
ATOM   11048 O  O   . MET G  1 75  ? 1.868   5.787   64.771 1.00 63.45  ? 66  MET G O   1 
ATOM   11049 C  CB  . MET G  1 75  ? 0.104   7.175   67.112 1.00 60.97  ? 66  MET G CB  1 
ATOM   11050 C  CG  . MET G  1 75  ? -1.036  8.136   67.397 1.00 64.78  ? 66  MET G CG  1 
ATOM   11051 S  SD  . MET G  1 75  ? -2.193  7.512   68.645 1.00 67.01  ? 66  MET G SD  1 
ATOM   11052 C  CE  . MET G  1 75  ? -1.144  7.441   70.094 1.00 62.60  ? 66  MET G CE  1 
ATOM   11053 N  N   . TRP G  1 76  ? 3.133   6.305   66.562 1.00 61.25  ? 67  TRP G N   1 
ATOM   11054 C  CA  . TRP G  1 76  ? 3.979   5.116   66.457 1.00 57.23  ? 67  TRP G CA  1 
ATOM   11055 C  C   . TRP G  1 76  ? 4.731   4.811   67.759 1.00 64.04  ? 67  TRP G C   1 
ATOM   11056 O  O   . TRP G  1 76  ? 4.852   5.672   68.626 1.00 61.79  ? 67  TRP G O   1 
ATOM   11057 C  CB  . TRP G  1 76  ? 4.963   5.258   65.304 1.00 53.41  ? 67  TRP G CB  1 
ATOM   11058 C  CG  . TRP G  1 76  ? 6.059   6.235   65.542 1.00 55.37  ? 67  TRP G CG  1 
ATOM   11059 C  CD1 . TRP G  1 76  ? 7.268   5.979   66.100 1.00 55.78  ? 67  TRP G CD1 1 
ATOM   11060 C  CD2 . TRP G  1 76  ? 6.063   7.624   65.200 1.00 60.86  ? 67  TRP G CD2 1 
ATOM   11061 N  NE1 . TRP G  1 76  ? 8.024   7.118   66.148 1.00 55.48  ? 67  TRP G NE1 1 
ATOM   11062 C  CE2 . TRP G  1 76  ? 7.307   8.149   65.591 1.00 59.79  ? 67  TRP G CE2 1 
ATOM   11063 C  CE3 . TRP G  1 76  ? 5.132   8.483   64.605 1.00 55.04  ? 67  TRP G CE3 1 
ATOM   11064 C  CZ2 . TRP G  1 76  ? 7.650   9.486   65.405 1.00 55.61  ? 67  TRP G CZ2 1 
ATOM   11065 C  CZ3 . TRP G  1 76  ? 5.471   9.805   64.427 1.00 50.22  ? 67  TRP G CZ3 1 
ATOM   11066 C  CH2 . TRP G  1 76  ? 6.716   10.295  64.824 1.00 50.48  ? 67  TRP G CH2 1 
ATOM   11067 N  N   . ASP G  1 77  ? 5.230   3.583   67.890 1.00 68.66  ? 68  ASP G N   1 
ATOM   11068 C  CA  . ASP G  1 77  ? 6.060   3.195   69.029 1.00 65.41  ? 68  ASP G CA  1 
ATOM   11069 C  C   . ASP G  1 77  ? 7.538   3.455   68.737 1.00 62.66  ? 68  ASP G C   1 
ATOM   11070 O  O   . ASP G  1 77  ? 8.133   2.769   67.913 1.00 67.61  ? 68  ASP G O   1 
ATOM   11071 C  CB  . ASP G  1 77  ? 5.848   1.708   69.322 1.00 71.45  ? 68  ASP G CB  1 
ATOM   11072 C  CG  . ASP G  1 77  ? 6.465   1.263   70.647 1.00 79.42  ? 68  ASP G CG  1 
ATOM   11073 O  OD1 . ASP G  1 77  ? 7.218   2.046   71.279 1.00 68.81  ? 68  ASP G OD1 1 
ATOM   11074 O  OD2 . ASP G  1 77  ? 6.201   0.103   71.038 1.00 83.54  ? 68  ASP G OD2 1 
ATOM   11075 N  N   . PRO G  1 78  ? 8.135   4.442   69.419 1.00 54.74  ? 69  PRO G N   1 
ATOM   11076 C  CA  . PRO G  1 78  ? 9.553   4.790   69.283 1.00 64.57  ? 69  PRO G CA  1 
ATOM   11077 C  C   . PRO G  1 78  ? 10.524  3.648   69.537 1.00 72.26  ? 69  PRO G C   1 
ATOM   11078 O  O   . PRO G  1 78  ? 11.657  3.780   69.101 1.00 74.49  ? 69  PRO G O   1 
ATOM   11079 C  CB  . PRO G  1 78  ? 9.760   5.871   70.342 1.00 54.43  ? 69  PRO G CB  1 
ATOM   11080 C  CG  . PRO G  1 78  ? 8.453   6.484   70.485 1.00 54.33  ? 69  PRO G CG  1 
ATOM   11081 C  CD  . PRO G  1 78  ? 7.422   5.413   70.254 1.00 55.95  ? 69  PRO G CD  1 
ATOM   11082 N  N   . ASN G  1 79  ? 10.127  2.583   70.232 1.00 67.54  ? 70  ASN G N   1 
ATOM   11083 C  CA  . ASN G  1 79  ? 11.018  1.427   70.386 1.00 73.52  ? 70  ASN G CA  1 
ATOM   11084 C  C   . ASN G  1 79  ? 11.185  0.652   69.074 1.00 75.15  ? 70  ASN G C   1 
ATOM   11085 O  O   . ASN G  1 79  ? 12.283  0.230   68.707 1.00 68.24  ? 70  ASN G O   1 
ATOM   11086 C  CB  . ASN G  1 79  ? 10.519  0.479   71.482 1.00 79.81  ? 70  ASN G CB  1 
ATOM   11087 C  CG  . ASN G  1 79  ? 10.646  1.068   72.874 1.00 95.54  ? 70  ASN G CG  1 
ATOM   11088 O  OD1 . ASN G  1 79  ? 9.664   1.141   73.617 1.00 98.13  ? 70  ASN G OD1 1 
ATOM   11089 N  ND2 . ASN G  1 79  ? 11.858  1.487   73.240 1.00 97.31  ? 70  ASN G ND2 1 
ATOM   11090 N  N   . GLU G  1 80  ? 10.074  0.472   68.368 1.00 69.72  ? 71  GLU G N   1 
ATOM   11091 C  CA  . GLU G  1 80  ? 10.082  -0.220  67.084 1.00 71.70  ? 71  GLU G CA  1 
ATOM   11092 C  C   . GLU G  1 80  ? 11.081  0.410   66.120 1.00 75.25  ? 71  GLU G C   1 
ATOM   11093 O  O   . GLU G  1 80  ? 11.640  -0.269  65.259 1.00 72.69  ? 71  GLU G O   1 
ATOM   11094 C  CB  . GLU G  1 80  ? 8.683   -0.215  66.466 1.00 82.99  ? 71  GLU G CB  1 
ATOM   11095 C  CG  . GLU G  1 80  ? 8.078   -1.598  66.288 1.00 103.48 ? 71  GLU G CG  1 
ATOM   11096 C  CD  . GLU G  1 80  ? 6.578   -1.555  66.076 1.00 107.10 ? 71  GLU G CD  1 
ATOM   11097 O  OE1 . GLU G  1 80  ? 5.853   -1.174  67.019 1.00 106.38 ? 71  GLU G OE1 1 
ATOM   11098 O  OE2 . GLU G  1 80  ? 6.123   -1.901  64.965 1.00 98.12  ? 71  GLU G OE2 1 
ATOM   11099 N  N   . TYR G  1 81  ? 11.301  1.712   66.270 1.00 77.39  ? 72  TYR G N   1 
ATOM   11100 C  CA  . TYR G  1 81  ? 11.758  2.544   65.162 1.00 72.75  ? 72  TYR G CA  1 
ATOM   11101 C  C   . TYR G  1 81  ? 13.056  3.263   65.509 1.00 74.12  ? 72  TYR G C   1 
ATOM   11102 O  O   . TYR G  1 81  ? 13.402  4.271   64.894 1.00 75.92  ? 72  TYR G O   1 
ATOM   11103 C  CB  . TYR G  1 81  ? 10.681  3.559   64.775 1.00 67.47  ? 72  TYR G CB  1 
ATOM   11104 C  CG  . TYR G  1 81  ? 9.610   2.999   63.867 1.00 65.93  ? 72  TYR G CG  1 
ATOM   11105 C  CD1 . TYR G  1 81  ? 9.916   2.573   62.581 1.00 64.39  ? 72  TYR G CD1 1 
ATOM   11106 C  CD2 . TYR G  1 81  ? 8.293   2.895   64.295 1.00 59.57  ? 72  TYR G CD2 1 
ATOM   11107 C  CE1 . TYR G  1 81  ? 8.942   2.059   61.748 1.00 63.02  ? 72  TYR G CE1 1 
ATOM   11108 C  CE2 . TYR G  1 81  ? 7.312   2.383   63.468 1.00 60.37  ? 72  TYR G CE2 1 
ATOM   11109 C  CZ  . TYR G  1 81  ? 7.641   1.967   62.196 1.00 64.80  ? 72  TYR G CZ  1 
ATOM   11110 O  OH  . TYR G  1 81  ? 6.668   1.456   61.369 1.00 69.51  ? 72  TYR G OH  1 
ATOM   11111 N  N   . GLY G  1 82  ? 13.772  2.739   66.499 1.00 70.93  ? 73  GLY G N   1 
ATOM   11112 C  CA  . GLY G  1 82  ? 15.089  3.243   66.837 1.00 69.52  ? 73  GLY G CA  1 
ATOM   11113 C  C   . GLY G  1 82  ? 15.031  4.437   67.769 1.00 67.71  ? 73  GLY G C   1 
ATOM   11114 O  O   . GLY G  1 82  ? 15.954  5.249   67.811 1.00 71.83  ? 73  GLY G O   1 
ATOM   11115 N  N   . ASN G  1 83  ? 13.939  4.542   68.520 1.00 70.12  ? 74  ASN G N   1 
ATOM   11116 C  CA  . ASN G  1 83  ? 13.770  5.631   69.482 1.00 72.65  ? 74  ASN G CA  1 
ATOM   11117 C  C   . ASN G  1 83  ? 13.549  7.001   68.849 1.00 75.96  ? 74  ASN G C   1 
ATOM   11118 O  O   . ASN G  1 83  ? 13.978  8.026   69.397 1.00 74.74  ? 74  ASN G O   1 
ATOM   11119 C  CB  . ASN G  1 83  ? 14.921  5.664   70.506 1.00 78.40  ? 74  ASN G CB  1 
ATOM   11120 C  CG  . ASN G  1 83  ? 14.563  4.947   71.820 1.00 100.92 ? 74  ASN G CG  1 
ATOM   11121 O  OD1 . ASN G  1 83  ? 13.441  5.068   72.314 1.00 98.44  ? 74  ASN G OD1 1 
ATOM   11122 N  ND2 . ASN G  1 83  ? 15.517  4.196   72.382 1.00 111.05 ? 74  ASN G ND2 1 
ATOM   11123 N  N   . ILE G  1 84  ? 12.830  7.014   67.724 1.00 72.28  ? 75  ILE G N   1 
ATOM   11124 C  CA  . ILE G  1 84  ? 12.544  8.247   67.007 1.00 64.79  ? 75  ILE G CA  1 
ATOM   11125 C  C   . ILE G  1 84  ? 11.276  8.791   67.628 1.00 65.24  ? 75  ILE G C   1 
ATOM   11126 O  O   . ILE G  1 84  ? 10.216  8.187   67.511 1.00 63.70  ? 75  ILE G O   1 
ATOM   11127 C  CB  . ILE G  1 84  ? 12.332  7.967   65.494 1.00 63.78  ? 75  ILE G CB  1 
ATOM   11128 C  CG1 . ILE G  1 84  ? 13.669  7.638   64.826 1.00 62.84  ? 75  ILE G CG1 1 
ATOM   11129 C  CG2 . ILE G  1 84  ? 11.635  9.130   64.786 1.00 57.60  ? 75  ILE G CG2 1 
ATOM   11130 C  CD1 . ILE G  1 84  ? 13.663  7.786   63.328 1.00 60.00  ? 75  ILE G CD1 1 
ATOM   11131 N  N   . THR G  1 85  ? 11.409  9.904   68.345 1.00 69.57  ? 76  THR G N   1 
ATOM   11132 C  CA  . THR G  1 85  ? 10.274  10.552  68.980 1.00 67.92  ? 76  THR G CA  1 
ATOM   11133 C  C   . THR G  1 85  ? 9.569   11.503  68.031 1.00 62.34  ? 76  THR G C   1 
ATOM   11134 O  O   . THR G  1 85  ? 8.393   11.802  68.214 1.00 67.06  ? 76  THR G O   1 
ATOM   11135 C  CB  . THR G  1 85  ? 10.694  11.273  70.272 1.00 69.16  ? 76  THR G CB  1 
ATOM   11136 O  OG1 . THR G  1 85  ? 11.786  12.160  69.997 1.00 79.84  ? 76  THR G OG1 1 
ATOM   11137 C  CG2 . THR G  1 85  ? 11.165  10.265  71.271 1.00 68.75  ? 76  THR G CG2 1 
ATOM   11138 N  N   . ASP G  1 86  ? 10.313  12.036  67.064 1.00 57.75  ? 77  ASP G N   1 
ATOM   11139 C  CA  . ASP G  1 86  ? 9.714   12.918  66.065 1.00 60.76  ? 77  ASP G CA  1 
ATOM   11140 C  C   . ASP G  1 86  ? 10.554  13.123  64.798 1.00 57.07  ? 77  ASP G C   1 
ATOM   11141 O  O   . ASP G  1 86  ? 11.765  12.943  64.818 1.00 57.10  ? 77  ASP G O   1 
ATOM   11142 C  CB  . ASP G  1 86  ? 9.351   14.252  66.708 1.00 57.38  ? 77  ASP G CB  1 
ATOM   11143 C  CG  . ASP G  1 86  ? 10.526  14.916  67.374 1.00 63.23  ? 77  ASP G CG  1 
ATOM   11144 O  OD1 . ASP G  1 86  ? 11.674  14.549  67.058 1.00 62.75  ? 77  ASP G OD1 1 
ATOM   11145 O  OD2 . ASP G  1 86  ? 10.288  15.829  68.196 1.00 71.62  ? 77  ASP G OD2 1 
ATOM   11146 N  N   . PHE G  1 87  ? 9.913   13.528  63.707 1.00 51.54  ? 78  PHE G N   1 
ATOM   11147 C  CA  . PHE G  1 87  ? 10.644  13.812  62.476 1.00 48.49  ? 78  PHE G CA  1 
ATOM   11148 C  C   . PHE G  1 87  ? 10.146  15.096  61.835 1.00 52.31  ? 78  PHE G C   1 
ATOM   11149 O  O   . PHE G  1 87  ? 9.083   15.604  62.198 1.00 49.87  ? 78  PHE G O   1 
ATOM   11150 C  CB  . PHE G  1 87  ? 10.566  12.641  61.486 1.00 44.85  ? 78  PHE G CB  1 
ATOM   11151 C  CG  . PHE G  1 87  ? 9.163   12.278  61.069 1.00 50.47  ? 78  PHE G CG  1 
ATOM   11152 C  CD1 . PHE G  1 87  ? 8.466   11.281  61.731 1.00 48.26  ? 78  PHE G CD1 1 
ATOM   11153 C  CD2 . PHE G  1 87  ? 8.547   12.921  60.010 1.00 51.17  ? 78  PHE G CD2 1 
ATOM   11154 C  CE1 . PHE G  1 87  ? 7.184   10.947  61.360 1.00 47.80  ? 78  PHE G CE1 1 
ATOM   11155 C  CE2 . PHE G  1 87  ? 7.261   12.590  59.634 1.00 49.78  ? 78  PHE G CE2 1 
ATOM   11156 C  CZ  . PHE G  1 87  ? 6.579   11.605  60.313 1.00 50.19  ? 78  PHE G CZ  1 
ATOM   11157 N  N   . ARG G  1 88  ? 10.935  15.627  60.900 1.00 56.17  ? 79  ARG G N   1 
ATOM   11158 C  CA  . ARG G  1 88  ? 10.480  16.727  60.045 1.00 59.79  ? 79  ARG G CA  1 
ATOM   11159 C  C   . ARG G  1 88  ? 9.970   16.211  58.689 1.00 54.57  ? 79  ARG G C   1 
ATOM   11160 O  O   . ARG G  1 88  ? 10.591  15.356  58.060 1.00 58.79  ? 79  ARG G O   1 
ATOM   11161 C  CB  . ARG G  1 88  ? 11.593  17.755  59.824 1.00 60.00  ? 79  ARG G CB  1 
ATOM   11162 C  CG  . ARG G  1 88  ? 12.494  18.005  61.032 1.00 58.31  ? 79  ARG G CG  1 
ATOM   11163 C  CD  . ARG G  1 88  ? 11.750  18.618  62.194 1.00 59.47  ? 79  ARG G CD  1 
ATOM   11164 N  NE  . ARG G  1 88  ? 12.667  19.243  63.142 1.00 60.27  ? 79  ARG G NE  1 
ATOM   11165 C  CZ  . ARG G  1 88  ? 13.292  18.599  64.125 1.00 67.55  ? 79  ARG G CZ  1 
ATOM   11166 N  NH1 . ARG G  1 88  ? 14.118  19.262  64.923 1.00 66.41  ? 79  ARG G NH1 1 
ATOM   11167 N  NH2 . ARG G  1 88  ? 13.105  17.294  64.314 1.00 69.17  ? 79  ARG G NH2 1 
ATOM   11168 N  N   . THR G  1 89  ? 8.825   16.717  58.254 1.00 51.74  ? 80  THR G N   1 
ATOM   11169 C  CA  . THR G  1 89  ? 8.319   16.391  56.928 1.00 59.83  ? 80  THR G CA  1 
ATOM   11170 C  C   . THR G  1 89  ? 7.860   17.659  56.203 1.00 62.17  ? 80  THR G C   1 
ATOM   11171 O  O   . THR G  1 89  ? 7.751   18.714  56.814 1.00 63.97  ? 80  THR G O   1 
ATOM   11172 C  CB  . THR G  1 89  ? 7.171   15.356  56.977 1.00 61.06  ? 80  THR G CB  1 
ATOM   11173 O  OG1 . THR G  1 89  ? 7.269   14.475  55.846 1.00 70.42  ? 80  THR G OG1 1 
ATOM   11174 C  CG2 . THR G  1 89  ? 5.812   16.048  56.968 1.00 55.27  ? 80  THR G CG2 1 
ATOM   11175 N  N   . SER G  1 90  ? 7.618   17.570  54.900 1.00 60.30  ? 81  SER G N   1 
ATOM   11176 C  CA  . SER G  1 90  ? 7.086   18.712  54.178 1.00 57.34  ? 81  SER G CA  1 
ATOM   11177 C  C   . SER G  1 90  ? 5.560   18.702  54.251 1.00 57.61  ? 81  SER G C   1 
ATOM   11178 O  O   . SER G  1 90  ? 4.941   17.647  54.274 1.00 58.43  ? 81  SER G O   1 
ATOM   11179 C  CB  . SER G  1 90  ? 7.576   18.720  52.739 1.00 58.79  ? 81  SER G CB  1 
ATOM   11180 O  OG  . SER G  1 90  ? 6.608   18.155  51.885 1.00 66.36  ? 81  SER G OG  1 
ATOM   11181 N  N   . ALA G  1 91  ? 4.959   19.882  54.319 1.00 57.76  ? 82  ALA G N   1 
ATOM   11182 C  CA  . ALA G  1 91  ? 3.520   19.993  54.537 1.00 57.76  ? 82  ALA G CA  1 
ATOM   11183 C  C   . ALA G  1 91  ? 2.679   19.313  53.447 1.00 54.26  ? 82  ALA G C   1 
ATOM   11184 O  O   . ALA G  1 91  ? 1.514   18.985  53.658 1.00 54.90  ? 82  ALA G O   1 
ATOM   11185 C  CB  . ALA G  1 91  ? 3.127   21.461  54.708 1.00 48.94  ? 82  ALA G CB  1 
ATOM   11186 N  N   . ALA G  1 92  ? 3.288   19.099  52.288 1.00 54.94  ? 83  ALA G N   1 
ATOM   11187 C  CA  . ALA G  1 92  ? 2.621   18.468  51.149 1.00 60.78  ? 83  ALA G CA  1 
ATOM   11188 C  C   . ALA G  1 92  ? 2.358   16.973  51.373 1.00 62.69  ? 83  ALA G C   1 
ATOM   11189 O  O   . ALA G  1 92  ? 1.491   16.389  50.724 1.00 60.64  ? 83  ALA G O   1 
ATOM   11190 C  CB  . ALA G  1 92  ? 3.447   18.661  49.904 1.00 44.02  ? 83  ALA G CB  1 
ATOM   11191 N  N   . ASP G  1 93  ? 3.110   16.369  52.295 1.00 61.68  ? 84  ASP G N   1 
ATOM   11192 C  CA  . ASP G  1 93  ? 3.027   14.936  52.561 1.00 60.35  ? 84  ASP G CA  1 
ATOM   11193 C  C   . ASP G  1 93  ? 2.004   14.567  53.620 1.00 57.20  ? 84  ASP G C   1 
ATOM   11194 O  O   . ASP G  1 93  ? 1.677   13.404  53.792 1.00 63.75  ? 84  ASP G O   1 
ATOM   11195 C  CB  . ASP G  1 93  ? 4.393   14.390  52.969 1.00 67.26  ? 84  ASP G CB  1 
ATOM   11196 C  CG  . ASP G  1 93  ? 5.422   14.490  51.851 1.00 77.85  ? 84  ASP G CG  1 
ATOM   11197 O  OD1 . ASP G  1 93  ? 5.058   14.789  50.680 1.00 65.63  ? 84  ASP G OD1 1 
ATOM   11198 O  OD2 . ASP G  1 93  ? 6.607   14.258  52.160 1.00 88.35  ? 84  ASP G OD2 1 
ATOM   11199 N  N   . ILE G  1 94  ? 1.493   15.556  54.329 1.00 57.86  ? 85  ILE G N   1 
ATOM   11200 C  CA  . ILE G  1 94  ? 0.480   15.292  55.327 1.00 54.28  ? 85  ILE G CA  1 
ATOM   11201 C  C   . ILE G  1 94  ? -0.776  16.088  55.036 1.00 51.92  ? 85  ILE G C   1 
ATOM   11202 O  O   . ILE G  1 94  ? -0.743  17.091  54.334 1.00 49.75  ? 85  ILE G O   1 
ATOM   11203 C  CB  . ILE G  1 94  ? 0.976   15.649  56.744 1.00 56.34  ? 85  ILE G CB  1 
ATOM   11204 C  CG1 . ILE G  1 94  ? 1.519   17.080  56.775 1.00 51.72  ? 85  ILE G CG1 1 
ATOM   11205 C  CG2 . ILE G  1 94  ? 2.038   14.664  57.210 1.00 56.95  ? 85  ILE G CG2 1 
ATOM   11206 C  CD1 . ILE G  1 94  ? 1.438   17.710  58.132 1.00 47.32  ? 85  ILE G CD1 1 
ATOM   11207 N  N   . TRP G  1 95  ? -1.886  15.630  55.586 1.00 46.70  ? 86  TRP G N   1 
ATOM   11208 C  CA  . TRP G  1 95  ? -3.110  16.386  55.535 1.00 45.15  ? 86  TRP G CA  1 
ATOM   11209 C  C   . TRP G  1 95  ? -2.947  17.619  56.382 1.00 48.96  ? 86  TRP G C   1 
ATOM   11210 O  O   . TRP G  1 95  ? -2.397  17.545  57.472 1.00 53.72  ? 86  TRP G O   1 
ATOM   11211 C  CB  . TRP G  1 95  ? -4.231  15.565  56.115 1.00 52.97  ? 86  TRP G CB  1 
ATOM   11212 C  CG  . TRP G  1 95  ? -5.467  16.328  56.211 1.00 52.69  ? 86  TRP G CG  1 
ATOM   11213 C  CD1 . TRP G  1 95  ? -6.449  16.396  55.279 1.00 55.36  ? 86  TRP G CD1 1 
ATOM   11214 C  CD2 . TRP G  1 95  ? -5.877  17.158  57.301 1.00 49.46  ? 86  TRP G CD2 1 
ATOM   11215 N  NE1 . TRP G  1 95  ? -7.458  17.208  55.721 1.00 60.37  ? 86  TRP G NE1 1 
ATOM   11216 C  CE2 . TRP G  1 95  ? -7.132  17.692  56.959 1.00 56.75  ? 86  TRP G CE2 1 
ATOM   11217 C  CE3 . TRP G  1 95  ? -5.311  17.493  58.532 1.00 52.52  ? 86  TRP G CE3 1 
ATOM   11218 C  CZ2 . TRP G  1 95  ? -7.830  18.560  57.802 1.00 49.15  ? 86  TRP G CZ2 1 
ATOM   11219 C  CZ3 . TRP G  1 95  ? -6.005  18.359  59.369 1.00 52.72  ? 86  TRP G CZ3 1 
ATOM   11220 C  CH2 . TRP G  1 95  ? -7.253  18.881  58.995 1.00 50.14  ? 86  TRP G CH2 1 
ATOM   11221 N  N   . THR G  1 96  ? -3.420  18.758  55.899 1.00 44.84  ? 87  THR G N   1 
ATOM   11222 C  CA  . THR G  1 96  ? -3.339  19.974  56.678 1.00 46.19  ? 87  THR G CA  1 
ATOM   11223 C  C   . THR G  1 96  ? -4.694  20.653  56.679 1.00 49.23  ? 87  THR G C   1 
ATOM   11224 O  O   . THR G  1 96  ? -5.482  20.413  55.774 1.00 47.23  ? 87  THR G O   1 
ATOM   11225 C  CB  . THR G  1 96  ? -2.288  20.918  56.121 1.00 49.64  ? 87  THR G CB  1 
ATOM   11226 O  OG1 . THR G  1 96  ? -2.584  21.181  54.747 1.00 44.15  ? 87  THR G OG1 1 
ATOM   11227 C  CG2 . THR G  1 96  ? -0.891  20.305  56.266 1.00 44.73  ? 87  THR G CG2 1 
ATOM   11228 N  N   . PRO G  1 97  ? -4.944  21.535  57.633 1.00 55.99  ? 88  PRO G N   1 
ATOM   11229 C  CA  . PRO G  1 97  ? -6.201  22.248  57.796 1.00 51.37  ? 88  PRO G CA  1 
ATOM   11230 C  C   . PRO G  1 97  ? -6.419  23.405  56.880 1.00 48.31  ? 88  PRO G C   1 
ATOM   11231 O  O   . PRO G  1 97  ? -5.506  24.128  56.597 1.00 50.06  ? 88  PRO G O   1 
ATOM   11232 C  CB  . PRO G  1 97  ? -6.062  22.791  59.191 1.00 49.52  ? 88  PRO G CB  1 
ATOM   11233 C  CG  . PRO G  1 97  ? -5.301  21.843  59.840 1.00 50.14  ? 88  PRO G CG  1 
ATOM   11234 C  CD  . PRO G  1 97  ? -4.258  21.442  58.912 1.00 54.83  ? 88  PRO G CD  1 
ATOM   11235 N  N   . ASP G  1 98  ? -7.642  23.601  56.442 1.00 49.11  ? 89  ASP G N   1 
ATOM   11236 C  CA  . ASP G  1 98  ? -7.901  24.703  55.574 1.00 59.53  ? 89  ASP G CA  1 
ATOM   11237 C  C   . ASP G  1 98  ? -8.350  25.798  56.471 1.00 59.94  ? 89  ASP G C   1 
ATOM   11238 O  O   . ASP G  1 98  ? -9.482  26.170  56.467 1.00 58.81  ? 89  ASP G O   1 
ATOM   11239 C  CB  . ASP G  1 98  ? -8.985  24.349  54.597 1.00 55.50  ? 89  ASP G CB  1 
ATOM   11240 C  CG  . ASP G  1 98  ? -10.309 24.273  55.214 1.00 54.63  ? 89  ASP G CG  1 
ATOM   11241 O  OD1 . ASP G  1 98  ? -10.410 23.997  56.390 1.00 52.01  ? 89  ASP G OD1 1 
ATOM   11242 O  OD2 . ASP G  1 98  ? -11.273 24.472  54.506 1.00 54.36  ? 89  ASP G OD2 1 
ATOM   11243 N  N   . ILE G  1 99  ? -7.416  26.344  57.205 1.00 55.27  ? 90  ILE G N   1 
ATOM   11244 C  CA  . ILE G  1 99  ? -7.578  27.557  57.948 1.00 59.79  ? 90  ILE G CA  1 
ATOM   11245 C  C   . ILE G  1 99  ? -7.328  28.697  57.018 1.00 58.22  ? 90  ILE G C   1 
ATOM   11246 O  O   . ILE G  1 99  ? -6.476  28.595  56.183 1.00 56.19  ? 90  ILE G O   1 
ATOM   11247 C  CB  . ILE G  1 99  ? -6.554  27.618  59.046 1.00 55.84  ? 90  ILE G CB  1 
ATOM   11248 C  CG1 . ILE G  1 99  ? -6.713  26.429  59.963 1.00 49.70  ? 90  ILE G CG1 1 
ATOM   11249 C  CG2 . ILE G  1 99  ? -6.714  28.868  59.796 1.00 49.66  ? 90  ILE G CG2 1 
ATOM   11250 C  CD1 . ILE G  1 99  ? -8.069  26.250  60.416 1.00 47.00  ? 90  ILE G CD1 1 
ATOM   11251 N  N   . THR G  1 100 ? -8.053  29.792  57.165 1.00 43.49  ? 91  THR G N   1 
ATOM   11252 C  CA  . THR G  1 100 ? -7.919  30.898  56.231 1.00 49.93  ? 91  THR G CA  1 
ATOM   11253 C  C   . THR G  1 100 ? -8.340  32.235  56.866 1.00 50.36  ? 91  THR G C   1 
ATOM   11254 O  O   . THR G  1 100 ? -9.235  32.266  57.706 1.00 51.00  ? 91  THR G O   1 
ATOM   11255 C  CB  . THR G  1 100 ? -8.730  30.635  54.917 1.00 47.03  ? 91  THR G CB  1 
ATOM   11256 O  OG1 . THR G  1 100 ? -8.555  31.728  54.009 1.00 48.39  ? 91  THR G OG1 1 
ATOM   11257 C  CG2 . THR G  1 100 ? -10.204 30.476  55.205 1.00 46.21  ? 91  THR G CG2 1 
ATOM   11258 N  N   . ALA G  1 101 ? -7.697  33.334  56.465 1.00 49.39  ? 92  ALA G N   1 
ATOM   11259 C  CA  . ALA G  1 101 ? -8.150  34.665  56.876 1.00 53.10  ? 92  ALA G CA  1 
ATOM   11260 C  C   . ALA G  1 101 ? -9.443  34.961  56.144 1.00 54.10  ? 92  ALA G C   1 
ATOM   11261 O  O   . ALA G  1 101 ? -9.527  34.780  54.943 1.00 57.09  ? 92  ALA G O   1 
ATOM   11262 C  CB  . ALA G  1 101 ? -7.102  35.734  56.573 1.00 47.25  ? 92  ALA G CB  1 
ATOM   11263 N  N   . TYR G  1 102 ? -10.461 35.388  56.870 1.00 52.08  ? 93  TYR G N   1 
ATOM   11264 C  CA  . TYR G  1 102 ? -11.764 35.589  56.269 1.00 51.99  ? 93  TYR G CA  1 
ATOM   11265 C  C   . TYR G  1 102 ? -11.882 36.913  55.531 1.00 49.79  ? 93  TYR G C   1 
ATOM   11266 O  O   . TYR G  1 102 ? -12.711 37.059  54.642 1.00 61.52  ? 93  TYR G O   1 
ATOM   11267 C  CB  . TYR G  1 102 ? -12.831 35.475  57.338 1.00 57.26  ? 93  TYR G CB  1 
ATOM   11268 C  CG  . TYR G  1 102 ? -13.037 34.065  57.795 1.00 63.90  ? 93  TYR G CG  1 
ATOM   11269 C  CD1 . TYR G  1 102 ? -12.781 33.000  56.947 1.00 60.92  ? 93  TYR G CD1 1 
ATOM   11270 C  CD2 . TYR G  1 102 ? -13.494 33.788  59.067 1.00 67.74  ? 93  TYR G CD2 1 
ATOM   11271 C  CE1 . TYR G  1 102 ? -12.984 31.700  57.353 1.00 57.90  ? 93  TYR G CE1 1 
ATOM   11272 C  CE2 . TYR G  1 102 ? -13.694 32.485  59.479 1.00 63.36  ? 93  TYR G CE2 1 
ATOM   11273 C  CZ  . TYR G  1 102 ? -13.442 31.455  58.616 1.00 56.95  ? 93  TYR G CZ  1 
ATOM   11274 O  OH  . TYR G  1 102 ? -13.649 30.173  59.037 1.00 67.17  ? 93  TYR G OH  1 
ATOM   11275 N  N   . SER G  1 103 ? -11.114 37.898  55.979 1.00 57.63  ? 94  SER G N   1 
ATOM   11276 C  CA  . SER G  1 103 ? -11.040 39.245  55.388 1.00 50.43  ? 94  SER G CA  1 
ATOM   11277 C  C   . SER G  1 103 ? -9.825  39.592  54.524 1.00 53.56  ? 94  SER G C   1 
ATOM   11278 O  O   . SER G  1 103 ? -9.565  40.771  54.298 1.00 54.05  ? 94  SER G O   1 
ATOM   11279 C  CB  . SER G  1 103 ? -11.321 40.342  56.410 1.00 49.24  ? 94  SER G CB  1 
ATOM   11280 O  OG  . SER G  1 103 ? -10.826 39.980  57.685 1.00 63.51  ? 94  SER G OG  1 
ATOM   11281 N  N   . SER G  1 104 ? -9.015  38.602  54.150 1.00 55.95  ? 95  SER G N   1 
ATOM   11282 C  CA  . SER G  1 104 ? -7.898  38.845  53.221 1.00 53.42  ? 95  SER G CA  1 
ATOM   11283 C  C   . SER G  1 104 ? -8.350  39.564  51.945 1.00 50.34  ? 95  SER G C   1 
ATOM   11284 O  O   . SER G  1 104 ? -9.364  39.196  51.356 1.00 56.48  ? 95  SER G O   1 
ATOM   11285 C  CB  . SER G  1 104 ? -7.236  37.533  52.818 1.00 48.98  ? 95  SER G CB  1 
ATOM   11286 O  OG  . SER G  1 104 ? -8.095  36.795  51.969 1.00 54.91  ? 95  SER G OG  1 
ATOM   11287 N  N   . THR G  1 105 ? -7.611  40.598  51.540 1.00 50.81  ? 96  THR G N   1 
ATOM   11288 C  CA  . THR G  1 105 ? -7.831  41.297  50.266 1.00 52.89  ? 96  THR G CA  1 
ATOM   11289 C  C   . THR G  1 105 ? -6.962  40.822  49.089 1.00 48.46  ? 96  THR G C   1 
ATOM   11290 O  O   . THR G  1 105 ? -7.201  41.202  47.957 1.00 48.82  ? 96  THR G O   1 
ATOM   11291 C  CB  . THR G  1 105 ? -7.657  42.822  50.426 1.00 56.73  ? 96  THR G CB  1 
ATOM   11292 O  OG1 . THR G  1 105 ? -6.302  43.128  50.806 1.00 57.81  ? 96  THR G OG1 1 
ATOM   11293 C  CG2 . THR G  1 105 ? -8.623  43.358  51.470 1.00 55.06  ? 96  THR G CG2 1 
ATOM   11294 N  N   . ARG G  1 106 ? -5.966  39.990  49.379 1.00 54.06  ? 97  ARG G N   1 
ATOM   11295 C  CA  . ARG G  1 106 ? -5.051  39.416  48.390 1.00 50.05  ? 97  ARG G CA  1 
ATOM   11296 C  C   . ARG G  1 106 ? -4.677  38.013  48.842 1.00 47.00  ? 97  ARG G C   1 
ATOM   11297 O  O   . ARG G  1 106 ? -4.744  37.720  50.030 1.00 55.38  ? 97  ARG G O   1 
ATOM   11298 C  CB  . ARG G  1 106 ? -3.787  40.260  48.263 1.00 51.20  ? 97  ARG G CB  1 
ATOM   11299 C  CG  . ARG G  1 106 ? -3.938  41.449  47.369 1.00 58.19  ? 97  ARG G CG  1 
ATOM   11300 C  CD  . ARG G  1 106 ? -2.763  42.375  47.498 1.00 63.95  ? 97  ARG G CD  1 
ATOM   11301 N  NE  . ARG G  1 106 ? -3.231  43.725  47.786 1.00 74.92  ? 97  ARG G NE  1 
ATOM   11302 C  CZ  . ARG G  1 106 ? -2.507  44.676  48.382 1.00 80.58  ? 97  ARG G CZ  1 
ATOM   11303 N  NH1 . ARG G  1 106 ? -1.254  44.438  48.763 1.00 83.38  ? 97  ARG G NH1 1 
ATOM   11304 N  NH2 . ARG G  1 106 ? -3.039  45.877  48.605 1.00 71.97  ? 97  ARG G NH2 1 
ATOM   11305 N  N   . PRO G  1 107 ? -4.286  37.135  47.901 1.00 51.77  ? 98  PRO G N   1 
ATOM   11306 C  CA  . PRO G  1 107 ? -3.889  35.779  48.304 1.00 49.17  ? 98  PRO G CA  1 
ATOM   11307 C  C   . PRO G  1 107 ? -2.673  35.844  49.208 1.00 45.56  ? 98  PRO G C   1 
ATOM   11308 O  O   . PRO G  1 107 ? -1.780  36.644  48.936 1.00 48.38  ? 98  PRO G O   1 
ATOM   11309 C  CB  . PRO G  1 107 ? -3.552  35.095  46.968 1.00 42.16  ? 98  PRO G CB  1 
ATOM   11310 C  CG  . PRO G  1 107 ? -3.403  36.174  45.989 1.00 46.92  ? 98  PRO G CG  1 
ATOM   11311 C  CD  . PRO G  1 107 ? -4.275  37.297  46.439 1.00 53.45  ? 98  PRO G CD  1 
ATOM   11312 N  N   . VAL G  1 108 ? -2.646  35.041  50.268 1.00 43.55  ? 99  VAL G N   1 
ATOM   11313 C  CA  . VAL G  1 108 ? -1.580  35.140  51.272 1.00 46.05  ? 99  VAL G CA  1 
ATOM   11314 C  C   . VAL G  1 108 ? -0.233  34.774  50.681 1.00 45.14  ? 99  VAL G C   1 
ATOM   11315 O  O   . VAL G  1 108 ? -0.162  33.920  49.823 1.00 56.76  ? 99  VAL G O   1 
ATOM   11316 C  CB  . VAL G  1 108 ? -1.859  34.248  52.506 1.00 44.08  ? 99  VAL G CB  1 
ATOM   11317 C  CG1 . VAL G  1 108 ? -0.728  34.356  53.497 1.00 51.75  ? 99  VAL G CG1 1 
ATOM   11318 C  CG2 . VAL G  1 108 ? -3.146  34.667  53.184 1.00 51.72  ? 99  VAL G CG2 1 
ATOM   11319 N  N   . GLN G  1 109 ? 0.837   35.418  51.116 1.00 42.33  ? 100 GLN G N   1 
ATOM   11320 C  CA  . GLN G  1 109 ? 2.152   35.003  50.665 1.00 46.02  ? 100 GLN G CA  1 
ATOM   11321 C  C   . GLN G  1 109 ? 2.946   34.279  51.753 1.00 51.62  ? 100 GLN G C   1 
ATOM   11322 O  O   . GLN G  1 109 ? 3.112   34.775  52.863 1.00 52.50  ? 100 GLN G O   1 
ATOM   11323 C  CB  . GLN G  1 109 ? 2.958   36.179  50.161 1.00 43.78  ? 100 GLN G CB  1 
ATOM   11324 C  CG  . GLN G  1 109 ? 2.176   37.186  49.390 1.00 50.85  ? 100 GLN G CG  1 
ATOM   11325 C  CD  . GLN G  1 109 ? 3.082   38.272  48.862 1.00 58.16  ? 100 GLN G CD  1 
ATOM   11326 O  OE1 . GLN G  1 109 ? 3.060   39.413  49.328 1.00 58.50  ? 100 GLN G OE1 1 
ATOM   11327 N  NE2 . GLN G  1 109 ? 3.914   37.911  47.902 1.00 50.27  ? 100 GLN G NE2 1 
ATOM   11328 N  N   . VAL G  1 110 ? 3.455   33.106  51.399 1.00 53.14  ? 101 VAL G N   1 
ATOM   11329 C  CA  . VAL G  1 110 ? 4.254   32.278  52.285 1.00 51.40  ? 101 VAL G CA  1 
ATOM   11330 C  C   . VAL G  1 110 ? 5.685   32.805  52.388 1.00 48.49  ? 101 VAL G C   1 
ATOM   11331 O  O   . VAL G  1 110 ? 6.375   32.952  51.392 1.00 54.22  ? 101 VAL G O   1 
ATOM   11332 C  CB  . VAL G  1 110 ? 4.264   30.833  51.759 1.00 52.65  ? 101 VAL G CB  1 
ATOM   11333 C  CG1 . VAL G  1 110 ? 4.806   29.884  52.803 1.00 51.58  ? 101 VAL G CG1 1 
ATOM   11334 C  CG2 . VAL G  1 110 ? 2.866   30.429  51.375 1.00 52.69  ? 101 VAL G CG2 1 
ATOM   11335 N  N   . LEU G  1 111 ? 6.143   33.071  53.588 1.00 47.99  ? 102 LEU G N   1 
ATOM   11336 C  CA  . LEU G  1 111 ? 7.469   33.591  53.781 1.00 52.06  ? 102 LEU G CA  1 
ATOM   11337 C  C   . LEU G  1 111 ? 8.447   32.615  54.344 1.00 51.72  ? 102 LEU G C   1 
ATOM   11338 O  O   . LEU G  1 111 ? 9.503   32.995  54.766 1.00 52.93  ? 102 LEU G O   1 
ATOM   11339 C  CB  . LEU G  1 111 ? 7.389   34.806  54.680 1.00 53.21  ? 102 LEU G CB  1 
ATOM   11340 C  CG  . LEU G  1 111 ? 6.569   35.932  54.093 1.00 53.41  ? 102 LEU G CG  1 
ATOM   11341 C  CD1 . LEU G  1 111 ? 5.876   36.694  55.131 1.00 49.30  ? 102 LEU G CD1 1 
ATOM   11342 C  CD2 . LEU G  1 111 ? 7.500   36.802  53.463 1.00 55.36  ? 102 LEU G CD2 1 
ATOM   11343 N  N   . SER G  1 112 ? 8.080   31.357  54.372 1.00 48.55  ? 103 SER G N   1 
ATOM   11344 C  CA  . SER G  1 112 ? 8.926   30.295  54.963 1.00 50.62  ? 103 SER G CA  1 
ATOM   11345 C  C   . SER G  1 112 ? 8.728   28.947  54.286 1.00 49.07  ? 103 SER G C   1 
ATOM   11346 O  O   . SER G  1 112 ? 7.706   28.725  53.640 1.00 45.97  ? 103 SER G O   1 
ATOM   11347 C  CB  . SER G  1 112 ? 8.690   30.142  56.479 1.00 48.87  ? 103 SER G CB  1 
ATOM   11348 O  OG  . SER G  1 112 ? 7.512   29.399  56.774 1.00 47.36  ? 103 SER G OG  1 
ATOM   11349 N  N   . PRO G  1 113 ? 9.717   28.050  54.424 1.00 45.84  ? 104 PRO G N   1 
ATOM   11350 C  CA  . PRO G  1 113 ? 9.620   26.697  53.891 1.00 44.33  ? 104 PRO G CA  1 
ATOM   11351 C  C   . PRO G  1 113 ? 8.394   26.061  54.462 1.00 46.52  ? 104 PRO G C   1 
ATOM   11352 O  O   . PRO G  1 113 ? 8.090   26.345  55.604 1.00 52.19  ? 104 PRO G O   1 
ATOM   11353 C  CB  . PRO G  1 113 ? 10.860  26.028  54.453 1.00 46.51  ? 104 PRO G CB  1 
ATOM   11354 C  CG  . PRO G  1 113 ? 11.827  27.114  54.534 1.00 45.98  ? 104 PRO G CG  1 
ATOM   11355 C  CD  . PRO G  1 113 ? 11.042  28.299  55.002 1.00 47.80  ? 104 PRO G CD  1 
ATOM   11356 N  N   . GLN G  1 114 ? 7.677   25.242  53.708 1.00 50.34  ? 105 GLN G N   1 
ATOM   11357 C  CA  . GLN G  1 114 ? 6.506   24.658  54.318 1.00 54.01  ? 105 GLN G CA  1 
ATOM   11358 C  C   . GLN G  1 114 ? 6.814   23.230  54.723 1.00 55.41  ? 105 GLN G C   1 
ATOM   11359 O  O   . GLN G  1 114 ? 6.665   22.279  53.954 1.00 50.38  ? 105 GLN G O   1 
ATOM   11360 C  CB  . GLN G  1 114 ? 5.336   24.763  53.350 1.00 51.45  ? 105 GLN G CB  1 
ATOM   11361 C  CG  . GLN G  1 114 ? 5.060   26.206  52.985 1.00 46.45  ? 105 GLN G CG  1 
ATOM   11362 C  CD  . GLN G  1 114 ? 3.984   26.368  51.937 1.00 63.47  ? 105 GLN G CD  1 
ATOM   11363 O  OE1 . GLN G  1 114 ? 2.945   26.974  52.208 1.00 65.67  ? 105 GLN G OE1 1 
ATOM   11364 N  NE2 . GLN G  1 114 ? 4.233   25.855  50.721 1.00 51.86  ? 105 GLN G NE2 1 
ATOM   11365 N  N   . ASN G  1 115 ? 7.139   23.115  56.006 1.00 55.45  ? 106 ASN G N   1 
ATOM   11366 C  CA  . ASN G  1 115 ? 7.642   21.906  56.627 1.00 55.57  ? 106 ASN G CA  1 
ATOM   11367 C  C   . ASN G  1 115 ? 6.883   21.796  57.938 1.00 54.88  ? 106 ASN G C   1 
ATOM   11368 O  O   . ASN G  1 115 ? 6.530   22.809  58.543 1.00 61.21  ? 106 ASN G O   1 
ATOM   11369 C  CB  . ASN G  1 115 ? 9.147   22.025  56.903 1.00 54.82  ? 106 ASN G CB  1 
ATOM   11370 C  CG  . ASN G  1 115 ? 10.008  21.781  55.664 1.00 59.47  ? 106 ASN G CG  1 
ATOM   11371 O  OD1 . ASN G  1 115 ? 9.783   20.841  54.913 1.00 63.59  ? 106 ASN G OD1 1 
ATOM   11372 N  ND2 . ASN G  1 115 ? 11.011  22.625  55.461 1.00 59.41  ? 106 ASN G ND2 1 
ATOM   11373 N  N   . ALA G  1 116 ? 6.608   20.578  58.373 1.00 50.06  ? 107 ALA G N   1 
ATOM   11374 C  CA  . ALA G  1 116 ? 5.849   20.371  59.587 1.00 49.11  ? 107 ALA G CA  1 
ATOM   11375 C  C   . ALA G  1 116 ? 6.589   19.398  60.479 1.00 49.97  ? 107 ALA G C   1 
ATOM   11376 O  O   . ALA G  1 116 ? 7.348   18.571  59.996 1.00 50.48  ? 107 ALA G O   1 
ATOM   11377 C  CB  . ALA G  1 116 ? 4.470   19.843  59.257 1.00 49.73  ? 107 ALA G CB  1 
ATOM   11378 N  N   . LEU G  1 117 ? 6.368   19.510  61.784 1.00 51.62  ? 108 LEU G N   1 
ATOM   11379 C  CA  . LEU G  1 117 ? 6.902   18.554  62.738 1.00 49.74  ? 108 LEU G CA  1 
ATOM   11380 C  C   . LEU G  1 117 ? 5.827   17.559  63.165 1.00 53.37  ? 108 LEU G C   1 
ATOM   11381 O  O   . LEU G  1 117 ? 4.714   17.946  63.520 1.00 50.38  ? 108 LEU G O   1 
ATOM   11382 C  CB  . LEU G  1 117 ? 7.444   19.266  63.962 1.00 48.76  ? 108 LEU G CB  1 
ATOM   11383 C  CG  . LEU G  1 117 ? 8.198   18.362  64.930 1.00 56.67  ? 108 LEU G CG  1 
ATOM   11384 C  CD1 . LEU G  1 117 ? 9.564   18.091  64.363 1.00 59.30  ? 108 LEU G CD1 1 
ATOM   11385 C  CD2 . LEU G  1 117 ? 8.316   18.981  66.321 1.00 58.96  ? 108 LEU G CD2 1 
ATOM   11386 N  N   . VAL G  1 118 ? 6.170   16.273  63.108 1.00 53.20  ? 109 VAL G N   1 
ATOM   11387 C  CA  . VAL G  1 118 ? 5.280   15.200  63.544 1.00 53.47  ? 109 VAL G CA  1 
ATOM   11388 C  C   . VAL G  1 118 ? 5.975   14.471  64.691 1.00 53.16  ? 109 VAL G C   1 
ATOM   11389 O  O   . VAL G  1 118 ? 7.182   14.246  64.623 1.00 55.95  ? 109 VAL G O   1 
ATOM   11390 C  CB  . VAL G  1 118 ? 4.964   14.191  62.379 1.00 48.51  ? 109 VAL G CB  1 
ATOM   11391 C  CG1 . VAL G  1 118 ? 3.933   13.167  62.800 1.00 51.82  ? 109 VAL G CG1 1 
ATOM   11392 C  CG2 . VAL G  1 118 ? 4.453   14.911  61.141 1.00 52.97  ? 109 VAL G CG2 1 
ATOM   11393 N  N   . ASN G  1 119 ? 5.244   14.131  65.754 1.00 52.99  ? 110 ASN G N   1 
ATOM   11394 C  CA  . ASN G  1 119 ? 5.801   13.229  66.781 1.00 60.99  ? 110 ASN G CA  1 
ATOM   11395 C  C   . ASN G  1 119 ? 4.987   11.989  67.157 1.00 61.49  ? 110 ASN G C   1 
ATOM   11396 O  O   . ASN G  1 119 ? 3.880   11.772  66.662 1.00 57.01  ? 110 ASN G O   1 
ATOM   11397 C  CB  . ASN G  1 119 ? 6.263   13.970  68.039 1.00 63.32  ? 110 ASN G CB  1 
ATOM   11398 C  CG  . ASN G  1 119 ? 5.134   14.634  68.794 1.00 69.82  ? 110 ASN G CG  1 
ATOM   11399 O  OD1 . ASN G  1 119 ? 4.006   14.164  68.839 1.00 58.56  ? 110 ASN G OD1 1 
ATOM   11400 N  ND2 . ASN G  1 119 ? 5.458   15.726  69.429 1.00 79.35  ? 110 ASN G ND2 1 
ATOM   11401 N  N   . SER G  1 120 ? 5.564   11.180  68.044 1.00 60.11  ? 111 SER G N   1 
ATOM   11402 C  CA  . SER G  1 120 ? 5.142   9.788   68.180 1.00 63.15  ? 111 SER G CA  1 
ATOM   11403 C  C   . SER G  1 120 ? 3.709   9.627   68.667 1.00 62.93  ? 111 SER G C   1 
ATOM   11404 O  O   . SER G  1 120 ? 3.056   8.626   68.368 1.00 62.20  ? 111 SER G O   1 
ATOM   11405 C  CB  . SER G  1 120 ? 6.136   8.960   69.005 1.00 56.59  ? 111 SER G CB  1 
ATOM   11406 O  OG  . SER G  1 120 ? 6.388   9.545   70.261 1.00 57.91  ? 111 SER G OG  1 
ATOM   11407 N  N   . SER G  1 121 ? 3.203   10.635  69.362 1.00 54.24  ? 112 SER G N   1 
ATOM   11408 C  CA  . SER G  1 121 ? 1.847   10.568  69.869 1.00 60.24  ? 112 SER G CA  1 
ATOM   11409 C  C   . SER G  1 121 ? 0.863   11.094  68.843 1.00 59.79  ? 112 SER G C   1 
ATOM   11410 O  O   . SER G  1 121 ? -0.305  11.289  69.152 1.00 63.38  ? 112 SER G O   1 
ATOM   11411 C  CB  . SER G  1 121 ? 1.710   11.299  71.198 1.00 56.14  ? 112 SER G CB  1 
ATOM   11412 O  OG  . SER G  1 121 ? 2.163   12.628  71.083 1.00 76.91  ? 112 SER G OG  1 
ATOM   11413 N  N   . GLY G  1 122 ? 1.360   11.363  67.637 1.00 60.78  ? 113 GLY G N   1 
ATOM   11414 C  CA  . GLY G  1 122 ? 0.524   11.761  66.508 1.00 63.68  ? 113 GLY G CA  1 
ATOM   11415 C  C   . GLY G  1 122 ? 0.306   13.257  66.290 1.00 60.64  ? 113 GLY G C   1 
ATOM   11416 O  O   . GLY G  1 122 ? -0.440  13.664  65.401 1.00 56.78  ? 113 GLY G O   1 
ATOM   11417 N  N   . HIS G  1 123 ? 0.962   14.071  67.110 1.00 62.27  ? 114 HIS G N   1 
ATOM   11418 C  CA  . HIS G  1 123 ? 0.807   15.515  67.068 1.00 56.33  ? 114 HIS G CA  1 
ATOM   11419 C  C   . HIS G  1 123 ? 1.591   16.126  65.910 1.00 52.36  ? 114 HIS G C   1 
ATOM   11420 O  O   . HIS G  1 123 ? 2.689   15.696  65.574 1.00 51.80  ? 114 HIS G O   1 
ATOM   11421 C  CB  . HIS G  1 123 ? 1.235   16.128  68.412 1.00 62.89  ? 114 HIS G CB  1 
ATOM   11422 C  CG  . HIS G  1 123 ? 0.283   15.845  69.539 1.00 77.79  ? 114 HIS G CG  1 
ATOM   11423 N  ND1 . HIS G  1 123 ? 0.270   14.649  70.229 1.00 77.61  ? 114 HIS G ND1 1 
ATOM   11424 C  CD2 . HIS G  1 123 ? -0.698  16.603  70.087 1.00 75.25  ? 114 HIS G CD2 1 
ATOM   11425 C  CE1 . HIS G  1 123 ? -0.677  14.682  71.149 1.00 68.24  ? 114 HIS G CE1 1 
ATOM   11426 N  NE2 . HIS G  1 123 ? -1.276  15.857  71.086 1.00 74.74  ? 114 HIS G NE2 1 
ATOM   11427 N  N   . VAL G  1 124 ? 1.005   17.131  65.291 1.00 48.15  ? 115 VAL G N   1 
ATOM   11428 C  CA  . VAL G  1 124 ? 1.645   17.809  64.177 1.00 52.97  ? 115 VAL G CA  1 
ATOM   11429 C  C   . VAL G  1 124 ? 1.820   19.270  64.556 1.00 51.85  ? 115 VAL G C   1 
ATOM   11430 O  O   . VAL G  1 124 ? 0.952   19.871  65.190 1.00 49.60  ? 115 VAL G O   1 
ATOM   11431 C  CB  . VAL G  1 124 ? 0.808   17.692  62.857 1.00 44.60  ? 115 VAL G CB  1 
ATOM   11432 C  CG1 . VAL G  1 124 ? 1.339   18.611  61.778 1.00 46.22  ? 115 VAL G CG1 1 
ATOM   11433 C  CG2 . VAL G  1 124 ? 0.793   16.280  62.366 1.00 42.95  ? 115 VAL G CG2 1 
ATOM   11434 N  N   . GLN G  1 125 ? 2.955   19.836  64.179 1.00 51.41  ? 116 GLN G N   1 
ATOM   11435 C  CA  . GLN G  1 125 ? 3.155   21.249  64.382 1.00 52.62  ? 116 GLN G CA  1 
ATOM   11436 C  C   . GLN G  1 125 ? 3.606   21.959  63.099 1.00 56.92  ? 116 GLN G C   1 
ATOM   11437 O  O   . GLN G  1 125 ? 4.723   21.766  62.613 1.00 52.16  ? 116 GLN G O   1 
ATOM   11438 C  CB  . GLN G  1 125 ? 4.141   21.453  65.513 1.00 56.94  ? 116 GLN G CB  1 
ATOM   11439 C  CG  . GLN G  1 125 ? 4.366   22.890  65.888 1.00 71.53  ? 116 GLN G CG  1 
ATOM   11440 C  CD  . GLN G  1 125 ? 5.121   23.008  67.193 1.00 88.09  ? 116 GLN G CD  1 
ATOM   11441 O  OE1 . GLN G  1 125 ? 4.745   22.399  68.204 1.00 90.46  ? 116 GLN G OE1 1 
ATOM   11442 N  NE2 . GLN G  1 125 ? 6.203   23.781  67.178 1.00 81.59  ? 116 GLN G NE2 1 
ATOM   11443 N  N   . TYR G  1 126 ? 2.721   22.806  62.585 1.00 52.73  ? 117 TYR G N   1 
ATOM   11444 C  CA  . TYR G  1 126 ? 2.952   23.548  61.353 1.00 51.52  ? 117 TYR G CA  1 
ATOM   11445 C  C   . TYR G  1 126 ? 3.072   25.060  61.618 1.00 51.75  ? 117 TYR G C   1 
ATOM   11446 O  O   . TYR G  1 126 ? 2.133   25.682  62.097 1.00 51.08  ? 117 TYR G O   1 
ATOM   11447 C  CB  . TYR G  1 126 ? 1.811   23.245  60.378 1.00 47.19  ? 117 TYR G CB  1 
ATOM   11448 C  CG  . TYR G  1 126 ? 1.952   23.875  59.018 1.00 46.75  ? 117 TYR G CG  1 
ATOM   11449 C  CD1 . TYR G  1 126 ? 3.142   23.773  58.303 1.00 52.41  ? 117 TYR G CD1 1 
ATOM   11450 C  CD2 . TYR G  1 126 ? 0.892   24.561  58.438 1.00 47.85  ? 117 TYR G CD2 1 
ATOM   11451 C  CE1 . TYR G  1 126 ? 3.275   24.351  57.050 1.00 51.67  ? 117 TYR G CE1 1 
ATOM   11452 C  CE2 . TYR G  1 126 ? 1.014   25.140  57.194 1.00 48.85  ? 117 TYR G CE2 1 
ATOM   11453 C  CZ  . TYR G  1 126 ? 2.206   25.031  56.505 1.00 53.56  ? 117 TYR G CZ  1 
ATOM   11454 O  OH  . TYR G  1 126 ? 2.329   25.610  55.263 1.00 58.79  ? 117 TYR G OH  1 
ATOM   11455 N  N   . LEU G  1 127 ? 4.225   25.642  61.299 1.00 52.20  ? 118 LEU G N   1 
ATOM   11456 C  CA  . LEU G  1 127 ? 4.488   27.050  61.602 1.00 51.90  ? 118 LEU G CA  1 
ATOM   11457 C  C   . LEU G  1 127 ? 4.838   27.888  60.379 1.00 52.44  ? 118 LEU G C   1 
ATOM   11458 O  O   . LEU G  1 127 ? 5.993   28.246  60.170 1.00 58.49  ? 118 LEU G O   1 
ATOM   11459 C  CB  . LEU G  1 127 ? 5.624   27.167  62.619 1.00 59.01  ? 118 LEU G CB  1 
ATOM   11460 C  CG  . LEU G  1 127 ? 5.180   27.443  64.045 1.00 67.85  ? 118 LEU G CG  1 
ATOM   11461 C  CD1 . LEU G  1 127 ? 6.245   27.021  65.024 1.00 73.49  ? 118 LEU G CD1 1 
ATOM   11462 C  CD2 . LEU G  1 127 ? 4.852   28.916  64.174 1.00 62.23  ? 118 LEU G CD2 1 
ATOM   11463 N  N   . PRO G  1 128 ? 3.846   28.189  59.552 1.00 45.43  ? 119 PRO G N   1 
ATOM   11464 C  CA  . PRO G  1 128 ? 4.091   29.035  58.384 1.00 49.86  ? 119 PRO G CA  1 
ATOM   11465 C  C   . PRO G  1 128 ? 4.284   30.527  58.689 1.00 47.26  ? 119 PRO G C   1 
ATOM   11466 O  O   . PRO G  1 128 ? 3.468   31.110  59.400 1.00 51.51  ? 119 PRO G O   1 
ATOM   11467 C  CB  . PRO G  1 128 ? 2.826   28.822  57.546 1.00 52.45  ? 119 PRO G CB  1 
ATOM   11468 C  CG  . PRO G  1 128 ? 1.763   28.477  58.541 1.00 50.25  ? 119 PRO G CG  1 
ATOM   11469 C  CD  . PRO G  1 128 ? 2.443   27.757  59.661 1.00 48.31  ? 119 PRO G CD  1 
ATOM   11470 N  N   . ALA G  1 129 ? 5.307   31.153  58.115 1.00 46.14  ? 120 ALA G N   1 
ATOM   11471 C  CA  . ALA G  1 129 ? 5.398   32.614  58.176 1.00 49.32  ? 120 ALA G CA  1 
ATOM   11472 C  C   . ALA G  1 129 ? 4.634   33.195  57.001 1.00 46.05  ? 120 ALA G C   1 
ATOM   11473 O  O   . ALA G  1 129 ? 4.745   32.709  55.895 1.00 53.70  ? 120 ALA G O   1 
ATOM   11474 C  CB  . ALA G  1 129 ? 6.834   33.077  58.147 1.00 45.83  ? 120 ALA G CB  1 
ATOM   11475 N  N   . GLN G  1 130 ? 3.857   34.236  57.229 1.00 45.28  ? 121 GLN G N   1 
ATOM   11476 C  CA  . GLN G  1 130 ? 2.976   34.731  56.184 1.00 49.73  ? 121 GLN G CA  1 
ATOM   11477 C  C   . GLN G  1 130 ? 2.993   36.266  56.082 1.00 50.71  ? 121 GLN G C   1 
ATOM   11478 O  O   . GLN G  1 130 ? 3.228   36.949  57.066 1.00 49.76  ? 121 GLN G O   1 
ATOM   11479 C  CB  . GLN G  1 130 ? 1.543   34.209  56.410 1.00 51.01  ? 121 GLN G CB  1 
ATOM   11480 C  CG  . GLN G  1 130 ? 1.384   32.686  56.260 1.00 50.21  ? 121 GLN G CG  1 
ATOM   11481 C  CD  . GLN G  1 130 ? -0.071  32.202  56.346 1.00 57.21  ? 121 GLN G CD  1 
ATOM   11482 O  OE1 . GLN G  1 130 ? -0.992  32.974  56.626 1.00 58.58  ? 121 GLN G OE1 1 
ATOM   11483 N  NE2 . GLN G  1 130 ? -0.277  30.908  56.102 1.00 56.50  ? 121 GLN G NE2 1 
ATOM   11484 N  N   . ARG G  1 131 ? 2.774   36.803  54.884 1.00 48.29  ? 122 ARG G N   1 
ATOM   11485 C  CA  . ARG G  1 131 ? 2.432   38.214  54.751 1.00 45.92  ? 122 ARG G CA  1 
ATOM   11486 C  C   . ARG G  1 131 ? 0.991   38.306  54.298 1.00 47.47  ? 122 ARG G C   1 
ATOM   11487 O  O   . ARG G  1 131 ? 0.610   37.674  53.325 1.00 50.42  ? 122 ARG G O   1 
ATOM   11488 C  CB  . ARG G  1 131 ? 3.334   38.936  53.770 1.00 41.05  ? 122 ARG G CB  1 
ATOM   11489 C  CG  . ARG G  1 131 ? 2.911   40.361  53.574 1.00 47.17  ? 122 ARG G CG  1 
ATOM   11490 C  CD  . ARG G  1 131 ? 3.843   41.111  52.645 1.00 52.82  ? 122 ARG G CD  1 
ATOM   11491 N  NE  . ARG G  1 131 ? 3.366   42.471  52.382 1.00 56.78  ? 122 ARG G NE  1 
ATOM   11492 C  CZ  . ARG G  1 131 ? 4.157   43.535  52.300 1.00 53.44  ? 122 ARG G CZ  1 
ATOM   11493 N  NH1 . ARG G  1 131 ? 5.469   43.404  52.462 1.00 47.66  ? 122 ARG G NH1 1 
ATOM   11494 N  NH2 . ARG G  1 131 ? 3.638   44.731  52.053 1.00 52.06  ? 122 ARG G NH2 1 
ATOM   11495 N  N   . LEU G  1 132 ? 0.178   39.074  55.014 1.00 48.71  ? 123 LEU G N   1 
ATOM   11496 C  CA  . LEU G  1 132 ? -1.251  39.124  54.713 1.00 51.35  ? 123 LEU G CA  1 
ATOM   11497 C  C   . LEU G  1 132 ? -1.754  40.552  54.565 1.00 52.16  ? 123 LEU G C   1 
ATOM   11498 O  O   . LEU G  1 132 ? -1.378  41.424  55.343 1.00 52.87  ? 123 LEU G O   1 
ATOM   11499 C  CB  . LEU G  1 132 ? -2.062  38.400  55.786 1.00 50.74  ? 123 LEU G CB  1 
ATOM   11500 C  CG  . LEU G  1 132 ? -3.581  38.520  55.652 1.00 51.19  ? 123 LEU G CG  1 
ATOM   11501 C  CD1 . LEU G  1 132 ? -4.154  37.425  54.777 1.00 53.94  ? 123 LEU G CD1 1 
ATOM   11502 C  CD2 . LEU G  1 132 ? -4.229  38.468  57.008 1.00 55.92  ? 123 LEU G CD2 1 
ATOM   11503 N  N   . SER G  1 133 ? -2.577  40.781  53.540 1.00 49.49  ? 124 SER G N   1 
ATOM   11504 C  CA  . SER G  1 133 ? -3.305  42.034  53.382 1.00 48.22  ? 124 SER G CA  1 
ATOM   11505 C  C   . SER G  1 133 ? -4.742  41.798  53.779 1.00 51.36  ? 124 SER G C   1 
ATOM   11506 O  O   . SER G  1 133 ? -5.395  40.943  53.209 1.00 54.08  ? 124 SER G O   1 
ATOM   11507 C  CB  . SER G  1 133 ? -3.270  42.517  51.934 1.00 50.62  ? 124 SER G CB  1 
ATOM   11508 O  OG  . SER G  1 133 ? -1.980  42.955  51.571 1.00 53.51  ? 124 SER G OG  1 
ATOM   11509 N  N   . PHE G  1 134 ? -5.243  42.542  54.754 1.00 50.09  ? 125 PHE G N   1 
ATOM   11510 C  CA  . PHE G  1 134 ? -6.634  42.379  55.140 1.00 49.53  ? 125 PHE G CA  1 
ATOM   11511 C  C   . PHE G  1 134 ? -7.336  43.722  55.238 1.00 59.66  ? 125 PHE G C   1 
ATOM   11512 O  O   . PHE G  1 134 ? -6.681  44.772  55.351 1.00 57.73  ? 125 PHE G O   1 
ATOM   11513 C  CB  . PHE G  1 134 ? -6.766  41.581  56.440 1.00 54.72  ? 125 PHE G CB  1 
ATOM   11514 C  CG  . PHE G  1 134 ? -6.001  42.165  57.613 1.00 68.27  ? 125 PHE G CG  1 
ATOM   11515 C  CD1 . PHE G  1 134 ? -6.656  42.924  58.586 1.00 66.36  ? 125 PHE G CD1 1 
ATOM   11516 C  CD2 . PHE G  1 134 ? -4.634  41.936  57.758 1.00 61.42  ? 125 PHE G CD2 1 
ATOM   11517 C  CE1 . PHE G  1 134 ? -5.961  43.455  59.659 1.00 58.71  ? 125 PHE G CE1 1 
ATOM   11518 C  CE2 . PHE G  1 134 ? -3.936  42.467  58.836 1.00 64.29  ? 125 PHE G CE2 1 
ATOM   11519 C  CZ  . PHE G  1 134 ? -4.602  43.225  59.782 1.00 62.36  ? 125 PHE G CZ  1 
ATOM   11520 N  N   . MET G  1 135 ? -8.671  43.684  55.217 1.00 63.24  ? 126 MET G N   1 
ATOM   11521 C  CA  . MET G  1 135 ? -9.462  44.904  55.142 1.00 57.23  ? 126 MET G CA  1 
ATOM   11522 C  C   . MET G  1 135 ? -9.369  45.565  56.499 1.00 60.42  ? 126 MET G C   1 
ATOM   11523 O  O   . MET G  1 135 ? -9.827  45.016  57.491 1.00 60.04  ? 126 MET G O   1 
ATOM   11524 C  CB  . MET G  1 135 ? -10.925 44.560  54.862 1.00 50.44  ? 126 MET G CB  1 
ATOM   11525 C  CG  . MET G  1 135 ? -11.132 43.688  53.655 1.00 51.45  ? 126 MET G CG  1 
ATOM   11526 S  SD  . MET G  1 135 ? -12.799 43.014  53.582 1.00 58.46  ? 126 MET G SD  1 
ATOM   11527 C  CE  . MET G  1 135 ? -12.610 41.807  52.267 1.00 53.55  ? 126 MET G CE  1 
ATOM   11528 N  N   . CYS G  1 136 ? -8.772  46.751  56.526 1.00 64.48  ? 127 CYS G N   1 
ATOM   11529 C  CA  . CYS G  1 136 ? -8.564  47.486  57.760 1.00 58.44  ? 127 CYS G CA  1 
ATOM   11530 C  C   . CYS G  1 136 ? -8.637  48.993  57.517 1.00 63.41  ? 127 CYS G C   1 
ATOM   11531 O  O   . CYS G  1 136 ? -7.930  49.520  56.662 1.00 61.15  ? 127 CYS G O   1 
ATOM   11532 C  CB  . CYS G  1 136 ? -7.205  47.089  58.325 1.00 60.56  ? 127 CYS G CB  1 
ATOM   11533 S  SG  . CYS G  1 136 ? -6.508  48.184  59.531 1.00 70.29  ? 127 CYS G SG  1 
ATOM   11534 N  N   . ASP G  1 137 ? -9.447  49.696  58.300 1.00 68.26  ? 128 ASP G N   1 
ATOM   11535 C  CA  . ASP G  1 137 ? -9.539  51.150  58.182 1.00 65.54  ? 128 ASP G CA  1 
ATOM   11536 C  C   . ASP G  1 137 ? -8.600  51.774  59.197 1.00 62.52  ? 128 ASP G C   1 
ATOM   11537 O  O   . ASP G  1 137 ? -8.877  51.728  60.387 1.00 71.79  ? 128 ASP G O   1 
ATOM   11538 C  CB  . ASP G  1 137 ? -10.972 51.596  58.469 1.00 68.56  ? 128 ASP G CB  1 
ATOM   11539 C  CG  . ASP G  1 137 ? -11.102 53.093  58.576 1.00 71.39  ? 128 ASP G CG  1 
ATOM   11540 O  OD1 . ASP G  1 137 ? -10.061 53.783  58.529 1.00 68.33  ? 128 ASP G OD1 1 
ATOM   11541 O  OD2 . ASP G  1 137 ? -12.244 53.578  58.722 1.00 73.28  ? 128 ASP G OD2 1 
ATOM   11542 N  N   . PRO G  1 138 ? -7.472  52.339  58.745 1.00 62.06  ? 129 PRO G N   1 
ATOM   11543 C  CA  . PRO G  1 138 ? -6.519  52.794  59.759 1.00 69.24  ? 129 PRO G CA  1 
ATOM   11544 C  C   . PRO G  1 138 ? -6.703  54.188  60.393 1.00 70.48  ? 129 PRO G C   1 
ATOM   11545 O  O   . PRO G  1 138 ? -5.783  54.682  61.053 1.00 67.58  ? 129 PRO G O   1 
ATOM   11546 C  CB  . PRO G  1 138 ? -5.173  52.614  59.042 1.00 57.69  ? 129 PRO G CB  1 
ATOM   11547 C  CG  . PRO G  1 138 ? -5.488  52.831  57.596 1.00 57.51  ? 129 PRO G CG  1 
ATOM   11548 C  CD  . PRO G  1 138 ? -6.983  52.601  57.385 1.00 65.23  ? 129 PRO G CD  1 
ATOM   11549 N  N   . THR G  1 139 ? -7.901  54.754  60.303 1.00 67.84  ? 130 THR G N   1 
ATOM   11550 C  CA  . THR G  1 139 ? -8.140  56.059  60.897 1.00 72.59  ? 130 THR G CA  1 
ATOM   11551 C  C   . THR G  1 139 ? -7.747  56.139  62.371 1.00 77.19  ? 130 THR G C   1 
ATOM   11552 O  O   . THR G  1 139 ? -8.238  55.360  63.193 1.00 76.77  ? 130 THR G O   1 
ATOM   11553 C  CB  . THR G  1 139 ? -9.605  56.492  60.701 1.00 70.38  ? 130 THR G CB  1 
ATOM   11554 O  OG1 . THR G  1 139 ? -9.917  56.488  59.305 1.00 70.34  ? 130 THR G OG1 1 
ATOM   11555 C  CG2 . THR G  1 139 ? -9.838  57.887  61.249 1.00 62.16  ? 130 THR G CG2 1 
ATOM   11556 N  N   . GLY G  1 140 ? -6.840  57.057  62.695 1.00 67.13  ? 131 GLY G N   1 
ATOM   11557 C  CA  . GLY G  1 140 ? -6.374  57.217  64.057 1.00 70.96  ? 131 GLY G CA  1 
ATOM   11558 C  C   . GLY G  1 140 ? -4.988  56.651  64.315 1.00 71.84  ? 131 GLY G C   1 
ATOM   11559 O  O   . GLY G  1 140 ? -4.490  56.687  65.434 1.00 73.17  ? 131 GLY G O   1 
ATOM   11560 N  N   . VAL G  1 141 ? -4.350  56.117  63.287 1.00 71.77  ? 132 VAL G N   1 
ATOM   11561 C  CA  . VAL G  1 141 ? -3.034  55.524  63.481 1.00 73.48  ? 132 VAL G CA  1 
ATOM   11562 C  C   . VAL G  1 141 ? -2.001  56.630  63.694 1.00 69.73  ? 132 VAL G C   1 
ATOM   11563 O  O   . VAL G  1 141 ? -0.896  56.389  64.170 1.00 67.13  ? 132 VAL G O   1 
ATOM   11564 C  CB  . VAL G  1 141 ? -2.655  54.576  62.304 1.00 74.34  ? 132 VAL G CB  1 
ATOM   11565 C  CG1 . VAL G  1 141 ? -2.480  55.352  60.979 1.00 58.61  ? 132 VAL G CG1 1 
ATOM   11566 C  CG2 . VAL G  1 141 ? -1.420  53.750  62.655 1.00 68.45  ? 132 VAL G CG2 1 
ATOM   11567 N  N   . ASP G  1 142 ? -2.388  57.845  63.327 1.00 72.08  ? 133 ASP G N   1 
ATOM   11568 C  CA  . ASP G  1 142 ? -1.576  59.035  63.546 1.00 73.93  ? 133 ASP G CA  1 
ATOM   11569 C  C   . ASP G  1 142 ? -1.960  59.794  64.819 1.00 76.71  ? 133 ASP G C   1 
ATOM   11570 O  O   . ASP G  1 142 ? -1.478  60.899  65.040 1.00 79.87  ? 133 ASP G O   1 
ATOM   11571 C  CB  . ASP G  1 142 ? -1.584  59.960  62.317 1.00 82.40  ? 133 ASP G CB  1 
ATOM   11572 C  CG  . ASP G  1 142 ? -2.971  60.516  61.991 1.00 87.16  ? 133 ASP G CG  1 
ATOM   11573 O  OD1 . ASP G  1 142 ? -3.976  59.980  62.511 1.00 82.16  ? 133 ASP G OD1 1 
ATOM   11574 O  OD2 . ASP G  1 142 ? -3.050  61.487  61.197 1.00 78.49  ? 133 ASP G OD2 1 
ATOM   11575 N  N   . SER G  1 143 ? -2.853  59.223  65.629 1.00 78.27  ? 134 SER G N   1 
ATOM   11576 C  CA  . SER G  1 143 ? -3.195  59.808  66.931 1.00 80.51  ? 134 SER G CA  1 
ATOM   11577 C  C   . SER G  1 143 ? -2.658  58.900  68.032 1.00 80.48  ? 134 SER G C   1 
ATOM   11578 O  O   . SER G  1 143 ? -2.088  57.857  67.739 1.00 81.59  ? 134 SER G O   1 
ATOM   11579 C  CB  . SER G  1 143 ? -4.709  59.999  67.076 1.00 77.43  ? 134 SER G CB  1 
ATOM   11580 O  OG  . SER G  1 143 ? -5.345  58.825  67.545 1.00 80.08  ? 134 SER G OG  1 
ATOM   11581 N  N   . GLU G  1 144 ? -2.815  59.284  69.294 1.00 88.87  ? 135 GLU G N   1 
ATOM   11582 C  CA  . GLU G  1 144 ? -2.187  58.503  70.362 1.00 87.51  ? 135 GLU G CA  1 
ATOM   11583 C  C   . GLU G  1 144 ? -3.014  57.308  70.806 1.00 83.35  ? 135 GLU G C   1 
ATOM   11584 O  O   . GLU G  1 144 ? -2.468  56.360  71.376 1.00 81.56  ? 135 GLU G O   1 
ATOM   11585 C  CB  . GLU G  1 144 ? -1.772  59.375  71.556 1.00 87.76  ? 135 GLU G CB  1 
ATOM   11586 C  CG  . GLU G  1 144 ? -0.723  60.457  71.215 1.00 108.00 ? 135 GLU G CG  1 
ATOM   11587 C  CD  . GLU G  1 144 ? 0.637   59.901  70.762 1.00 112.04 ? 135 GLU G CD  1 
ATOM   11588 O  OE1 . GLU G  1 144 ? 1.521   59.737  71.643 1.00 113.52 ? 135 GLU G OE1 1 
ATOM   11589 O  OE2 . GLU G  1 144 ? 0.828   59.657  69.538 1.00 89.78  ? 135 GLU G OE2 1 
ATOM   11590 N  N   . GLU G  1 145 ? -4.318  57.341  70.537 1.00 80.34  ? 136 GLU G N   1 
ATOM   11591 C  CA  . GLU G  1 145 ? -5.181  56.211  70.890 1.00 86.20  ? 136 GLU G CA  1 
ATOM   11592 C  C   . GLU G  1 145 ? -5.027  55.077  69.881 1.00 84.73  ? 136 GLU G C   1 
ATOM   11593 O  O   . GLU G  1 145 ? -5.437  53.939  70.131 1.00 73.34  ? 136 GLU G O   1 
ATOM   11594 C  CB  . GLU G  1 145 ? -6.650  56.632  71.004 1.00 94.42  ? 136 GLU G CB  1 
ATOM   11595 C  CG  . GLU G  1 145 ? -7.204  57.359  69.778 1.00 99.13  ? 136 GLU G CG  1 
ATOM   11596 C  CD  . GLU G  1 145 ? -7.553  58.815  70.074 1.00 103.03 ? 136 GLU G CD  1 
ATOM   11597 O  OE1 . GLU G  1 145 ? -6.662  59.559  70.556 1.00 94.80  ? 136 GLU G OE1 1 
ATOM   11598 O  OE2 . GLU G  1 145 ? -8.722  59.205  69.836 1.00 91.15  ? 136 GLU G OE2 1 
ATOM   11599 N  N   . GLY G  1 146 ? -4.429  55.408  68.739 1.00 79.86  ? 137 GLY G N   1 
ATOM   11600 C  CA  . GLY G  1 146 ? -4.127  54.432  67.711 1.00 74.32  ? 137 GLY G CA  1 
ATOM   11601 C  C   . GLY G  1 146 ? -5.322  54.036  66.863 1.00 72.19  ? 137 GLY G C   1 
ATOM   11602 O  O   . GLY G  1 146 ? -6.418  54.571  67.021 1.00 73.50  ? 137 GLY G O   1 
ATOM   11603 N  N   . ALA G  1 147 ? -5.103  53.087  65.961 1.00 61.98  ? 138 ALA G N   1 
ATOM   11604 C  CA  . ALA G  1 147 ? -6.156  52.589  65.107 1.00 61.75  ? 138 ALA G CA  1 
ATOM   11605 C  C   . ALA G  1 147 ? -6.371  51.150  65.512 1.00 62.22  ? 138 ALA G C   1 
ATOM   11606 O  O   . ALA G  1 147 ? -5.488  50.550  66.117 1.00 62.21  ? 138 ALA G O   1 
ATOM   11607 C  CB  . ALA G  1 147 ? -5.739  52.680  63.674 1.00 60.52  ? 138 ALA G CB  1 
ATOM   11608 N  N   . THR G  1 148 ? -7.548  50.602  65.226 1.00 55.83  ? 139 THR G N   1 
ATOM   11609 C  CA  . THR G  1 148 ? -7.843  49.236  65.642 1.00 58.56  ? 139 THR G CA  1 
ATOM   11610 C  C   . THR G  1 148 ? -8.431  48.390  64.529 1.00 62.02  ? 139 THR G C   1 
ATOM   11611 O  O   . THR G  1 148 ? -9.440  48.754  63.932 1.00 58.59  ? 139 THR G O   1 
ATOM   11612 C  CB  . THR G  1 148 ? -8.805  49.187  66.846 1.00 67.16  ? 139 THR G CB  1 
ATOM   11613 O  OG1 . THR G  1 148 ? -8.128  49.630  68.033 1.00 74.97  ? 139 THR G OG1 1 
ATOM   11614 C  CG2 . THR G  1 148 ? -9.308  47.764  67.061 1.00 65.52  ? 139 THR G CG2 1 
ATOM   11615 N  N   . CYS G  1 149 ? -7.805  47.241  64.282 1.00 58.34  ? 140 CYS G N   1 
ATOM   11616 C  CA  . CYS G  1 149 ? -8.274  46.321  63.255 1.00 61.87  ? 140 CYS G CA  1 
ATOM   11617 C  C   . CYS G  1 149 ? -8.431  44.852  63.681 1.00 61.70  ? 140 CYS G C   1 
ATOM   11618 O  O   . CYS G  1 149 ? -7.730  44.354  64.553 1.00 60.74  ? 140 CYS G O   1 
ATOM   11619 C  CB  . CYS G  1 149 ? -7.398  46.442  62.014 1.00 63.60  ? 140 CYS G CB  1 
ATOM   11620 S  SG  . CYS G  1 149 ? -7.692  48.007  61.162 1.00 76.82  ? 140 CYS G SG  1 
ATOM   11621 N  N   . ALA G  1 150 ? -9.373  44.167  63.052 1.00 64.26  ? 141 ALA G N   1 
ATOM   11622 C  CA  . ALA G  1 150 ? -9.660  42.787  63.385 1.00 56.42  ? 141 ALA G CA  1 
ATOM   11623 C  C   . ALA G  1 150 ? -9.649  41.926  62.116 1.00 52.26  ? 141 ALA G C   1 
ATOM   11624 O  O   . ALA G  1 150 ? -10.055 42.373  61.047 1.00 58.33  ? 141 ALA G O   1 
ATOM   11625 C  CB  . ALA G  1 150 ? -11.007 42.692  64.114 1.00 47.11  ? 141 ALA G CB  1 
ATOM   11626 N  N   . VAL G  1 151 ? -9.133  40.709  62.231 1.00 53.20  ? 142 VAL G N   1 
ATOM   11627 C  CA  . VAL G  1 151 ? -9.214  39.718  61.163 1.00 53.75  ? 142 VAL G CA  1 
ATOM   11628 C  C   . VAL G  1 151 ? -9.490  38.332  61.762 1.00 53.31  ? 142 VAL G C   1 
ATOM   11629 O  O   . VAL G  1 151 ? -8.776  37.903  62.662 1.00 55.88  ? 142 VAL G O   1 
ATOM   11630 C  CB  . VAL G  1 151 ? -7.935  39.719  60.276 1.00 48.18  ? 142 VAL G CB  1 
ATOM   11631 C  CG1 . VAL G  1 151 ? -6.679  39.680  61.115 1.00 55.93  ? 142 VAL G CG1 1 
ATOM   11632 C  CG2 . VAL G  1 151 ? -7.965  38.574  59.294 1.00 46.25  ? 142 VAL G CG2 1 
ATOM   11633 N  N   . LYS G  1 152 ? -10.530 37.649  61.280 1.00 51.91  ? 143 LYS G N   1 
ATOM   11634 C  CA  . LYS G  1 152 ? -10.883 36.316  61.786 1.00 51.18  ? 143 LYS G CA  1 
ATOM   11635 C  C   . LYS G  1 152 ? -10.249 35.177  60.964 1.00 55.69  ? 143 LYS G C   1 
ATOM   11636 O  O   . LYS G  1 152 ? -10.167 35.255  59.734 1.00 53.46  ? 143 LYS G O   1 
ATOM   11637 C  CB  . LYS G  1 152 ? -12.405 36.119  61.822 1.00 55.05  ? 143 LYS G CB  1 
ATOM   11638 C  CG  . LYS G  1 152 ? -13.200 37.293  62.332 1.00 64.38  ? 143 LYS G CG  1 
ATOM   11639 C  CD  . LYS G  1 152 ? -14.570 36.852  62.820 1.00 72.08  ? 143 LYS G CD  1 
ATOM   11640 C  CE  . LYS G  1 152 ? -15.452 38.044  63.179 1.00 77.75  ? 143 LYS G CE  1 
ATOM   11641 N  NZ  . LYS G  1 152 ? -15.855 38.832  61.966 1.00 88.23  ? 143 LYS G NZ  1 
ATOM   11642 N  N   . PHE G  1 153 ? -9.815  34.120  61.647 1.00 55.16  ? 144 PHE G N   1 
ATOM   11643 C  CA  . PHE G  1 153 ? -9.328  32.917  60.986 1.00 51.54  ? 144 PHE G CA  1 
ATOM   11644 C  C   . PHE G  1 153 ? -10.199 31.718  61.324 1.00 57.12  ? 144 PHE G C   1 
ATOM   11645 O  O   . PHE G  1 153 ? -10.623 31.561  62.472 1.00 55.59  ? 144 PHE G O   1 
ATOM   11646 C  CB  . PHE G  1 153 ? -7.901  32.603  61.418 1.00 46.04  ? 144 PHE G CB  1 
ATOM   11647 C  CG  . PHE G  1 153 ? -6.905  33.625  61.007 1.00 44.31  ? 144 PHE G CG  1 
ATOM   11648 C  CD1 . PHE G  1 153 ? -5.989  33.351  60.023 1.00 48.06  ? 144 PHE G CD1 1 
ATOM   11649 C  CD2 . PHE G  1 153 ? -6.869  34.853  61.617 1.00 42.74  ? 144 PHE G CD2 1 
ATOM   11650 C  CE1 . PHE G  1 153 ? -5.069  34.290  59.645 1.00 47.96  ? 144 PHE G CE1 1 
ATOM   11651 C  CE2 . PHE G  1 153 ? -5.942  35.793  61.246 1.00 46.78  ? 144 PHE G CE2 1 
ATOM   11652 C  CZ  . PHE G  1 153 ? -5.045  35.513  60.259 1.00 48.65  ? 144 PHE G CZ  1 
ATOM   11653 N  N   . GLY G  1 154 ? -10.444 30.866  60.326 1.00 59.64  ? 145 GLY G N   1 
ATOM   11654 C  CA  . GLY G  1 154 ? -11.079 29.571  60.543 1.00 55.59  ? 145 GLY G CA  1 
ATOM   11655 C  C   . GLY G  1 154 ? -11.083 28.623  59.352 1.00 49.87  ? 145 GLY G C   1 
ATOM   11656 O  O   . GLY G  1 154 ? -10.661 28.967  58.247 1.00 46.04  ? 145 GLY G O   1 
ATOM   11657 N  N   . SER G  1 155 ? -11.568 27.411  59.571 1.00 50.49  ? 146 SER G N   1 
ATOM   11658 C  CA  . SER G  1 155 ? -11.727 26.488  58.460 1.00 45.56  ? 146 SER G CA  1 
ATOM   11659 C  C   . SER G  1 155 ? -12.626 27.129  57.454 1.00 49.67  ? 146 SER G C   1 
ATOM   11660 O  O   . SER G  1 155 ? -13.647 27.707  57.816 1.00 51.93  ? 146 SER G O   1 
ATOM   11661 C  CB  . SER G  1 155 ? -12.381 25.194  58.913 1.00 47.46  ? 146 SER G CB  1 
ATOM   11662 O  OG  . SER G  1 155 ? -12.467 24.284  57.838 1.00 47.23  ? 146 SER G OG  1 
ATOM   11663 N  N   . TRP G  1 156 ? -12.255 27.024  56.184 1.00 55.98  ? 147 TRP G N   1 
ATOM   11664 C  CA  . TRP G  1 156 ? -13.122 27.527  55.122 1.00 56.80  ? 147 TRP G CA  1 
ATOM   11665 C  C   . TRP G  1 156 ? -14.260 26.574  54.824 1.00 56.37  ? 147 TRP G C   1 
ATOM   11666 O  O   . TRP G  1 156 ? -15.405 26.990  54.721 1.00 59.95  ? 147 TRP G O   1 
ATOM   11667 C  CB  . TRP G  1 156 ? -12.341 27.841  53.849 1.00 52.97  ? 147 TRP G CB  1 
ATOM   11668 C  CG  . TRP G  1 156 ? -13.186 28.515  52.814 1.00 59.49  ? 147 TRP G CG  1 
ATOM   11669 C  CD1 . TRP G  1 156 ? -13.649 27.972  51.648 1.00 59.12  ? 147 TRP G CD1 1 
ATOM   11670 C  CD2 . TRP G  1 156 ? -13.694 29.854  52.857 1.00 63.66  ? 147 TRP G CD2 1 
ATOM   11671 N  NE1 . TRP G  1 156 ? -14.398 28.894  50.962 1.00 62.49  ? 147 TRP G NE1 1 
ATOM   11672 C  CE2 . TRP G  1 156 ? -14.441 30.059  51.683 1.00 60.57  ? 147 TRP G CE2 1 
ATOM   11673 C  CE3 . TRP G  1 156 ? -13.586 30.900  53.772 1.00 56.67  ? 147 TRP G CE3 1 
ATOM   11674 C  CZ2 . TRP G  1 156 ? -15.072 31.257  51.406 1.00 51.84  ? 147 TRP G CZ2 1 
ATOM   11675 C  CZ3 . TRP G  1 156 ? -14.212 32.080  53.491 1.00 56.65  ? 147 TRP G CZ3 1 
ATOM   11676 C  CH2 . TRP G  1 156 ? -14.946 32.250  52.323 1.00 58.35  ? 147 TRP G CH2 1 
ATOM   11677 N  N   . SER G  1 157 ? -13.943 25.295  54.668 1.00 58.11  ? 148 SER G N   1 
ATOM   11678 C  CA  . SER G  1 157 ? -14.971 24.319  54.324 1.00 55.72  ? 148 SER G CA  1 
ATOM   11679 C  C   . SER G  1 157 ? -15.616 23.500  55.452 1.00 52.95  ? 148 SER G C   1 
ATOM   11680 O  O   . SER G  1 157 ? -16.678 22.931  55.253 1.00 57.41  ? 148 SER G O   1 
ATOM   11681 C  CB  . SER G  1 157 ? -14.453 23.413  53.209 1.00 50.62  ? 148 SER G CB  1 
ATOM   11682 O  OG  . SER G  1 157 ? -14.042 24.198  52.094 1.00 58.04  ? 148 SER G OG  1 
ATOM   11683 N  N   . TYR G  1 158 ? -15.035 23.498  56.647 1.00 55.14  ? 149 TYR G N   1 
ATOM   11684 C  CA  . TYR G  1 158 ? -15.515 22.619  57.713 1.00 49.18  ? 149 TYR G CA  1 
ATOM   11685 C  C   . TYR G  1 158 ? -16.217 23.358  58.843 1.00 57.63  ? 149 TYR G C   1 
ATOM   11686 O  O   . TYR G  1 158 ? -15.890 24.506  59.158 1.00 57.16  ? 149 TYR G O   1 
ATOM   11687 C  CB  . TYR G  1 158 ? -14.361 21.834  58.318 1.00 49.13  ? 149 TYR G CB  1 
ATOM   11688 C  CG  . TYR G  1 158 ? -13.745 20.761  57.450 1.00 56.18  ? 149 TYR G CG  1 
ATOM   11689 C  CD1 . TYR G  1 158 ? -14.315 19.498  57.360 1.00 56.29  ? 149 TYR G CD1 1 
ATOM   11690 C  CD2 . TYR G  1 158 ? -12.565 20.995  56.760 1.00 55.65  ? 149 TYR G CD2 1 
ATOM   11691 C  CE1 . TYR G  1 158 ? -13.737 18.510  56.597 1.00 57.86  ? 149 TYR G CE1 1 
ATOM   11692 C  CE2 . TYR G  1 158 ? -11.985 20.018  55.985 1.00 55.93  ? 149 TYR G CE2 1 
ATOM   11693 C  CZ  . TYR G  1 158 ? -12.569 18.775  55.908 1.00 63.30  ? 149 TYR G CZ  1 
ATOM   11694 O  OH  . TYR G  1 158 ? -11.979 17.791  55.138 1.00 59.82  ? 149 TYR G OH  1 
ATOM   11695 N  N   . GLY G  1 159 ? -17.169 22.680  59.473 1.00 58.14  ? 150 GLY G N   1 
ATOM   11696 C  CA  . GLY G  1 159 ? -17.835 23.213  60.649 1.00 59.64  ? 150 GLY G CA  1 
ATOM   11697 C  C   . GLY G  1 159 ? -17.211 22.757  61.964 1.00 62.88  ? 150 GLY G C   1 
ATOM   11698 O  O   . GLY G  1 159 ? -16.201 22.061  61.979 1.00 60.56  ? 150 GLY G O   1 
ATOM   11699 N  N   . GLY G  1 160 ? -17.825 23.138  63.078 1.00 62.27  ? 151 GLY G N   1 
ATOM   11700 C  CA  . GLY G  1 160 ? -17.251 22.883  64.385 1.00 60.63  ? 151 GLY G CA  1 
ATOM   11701 C  C   . GLY G  1 160 ? -17.324 21.430  64.787 1.00 61.99  ? 151 GLY G C   1 
ATOM   11702 O  O   . GLY G  1 160 ? -16.532 20.959  65.604 1.00 65.06  ? 151 GLY G O   1 
ATOM   11703 N  N   . TRP G  1 161 ? -18.287 20.725  64.211 1.00 60.90  ? 152 TRP G N   1 
ATOM   11704 C  CA  . TRP G  1 161 ? -18.489 19.313  64.486 1.00 59.57  ? 152 TRP G CA  1 
ATOM   11705 C  C   . TRP G  1 161 ? -17.435 18.416  63.854 1.00 59.64  ? 152 TRP G C   1 
ATOM   11706 O  O   . TRP G  1 161 ? -17.245 17.294  64.299 1.00 62.69  ? 152 TRP G O   1 
ATOM   11707 C  CB  . TRP G  1 161 ? -19.872 18.889  64.012 1.00 63.26  ? 152 TRP G CB  1 
ATOM   11708 C  CG  . TRP G  1 161 ? -20.935 19.297  64.942 1.00 63.96  ? 152 TRP G CG  1 
ATOM   11709 C  CD1 . TRP G  1 161 ? -20.781 19.654  66.250 1.00 62.46  ? 152 TRP G CD1 1 
ATOM   11710 C  CD2 . TRP G  1 161 ? -22.332 19.394  64.656 1.00 67.53  ? 152 TRP G CD2 1 
ATOM   11711 N  NE1 . TRP G  1 161 ? -22.000 19.966  66.799 1.00 66.99  ? 152 TRP G NE1 1 
ATOM   11712 C  CE2 . TRP G  1 161 ? -22.970 19.816  65.841 1.00 74.00  ? 152 TRP G CE2 1 
ATOM   11713 C  CE3 . TRP G  1 161 ? -23.108 19.168  63.513 1.00 73.10  ? 152 TRP G CE3 1 
ATOM   11714 C  CZ2 . TRP G  1 161 ? -24.353 20.017  65.915 1.00 75.41  ? 152 TRP G CZ2 1 
ATOM   11715 C  CZ3 . TRP G  1 161 ? -24.483 19.371  63.586 1.00 77.06  ? 152 TRP G CZ3 1 
ATOM   11716 C  CH2 . TRP G  1 161 ? -25.090 19.793  64.780 1.00 74.37  ? 152 TRP G CH2 1 
ATOM   11717 N  N   . GLU G  1 162 ? -16.775 18.908  62.809 1.00 63.71  ? 153 GLU G N   1 
ATOM   11718 C  CA  . GLU G  1 162 ? -15.652 18.220  62.169 1.00 61.83  ? 153 GLU G CA  1 
ATOM   11719 C  C   . GLU G  1 162 ? -14.347 18.825  62.651 1.00 62.18  ? 153 GLU G C   1 
ATOM   11720 O  O   . GLU G  1 162 ? -13.465 18.111  63.112 1.00 67.10  ? 153 GLU G O   1 
ATOM   11721 C  CB  . GLU G  1 162 ? -15.711 18.269  60.649 1.00 62.53  ? 153 GLU G CB  1 
ATOM   11722 C  CG  . GLU G  1 162 ? -16.966 17.693  60.036 1.00 71.31  ? 153 GLU G CG  1 
ATOM   11723 C  CD  . GLU G  1 162 ? -18.165 18.568  60.291 1.00 70.92  ? 153 GLU G CD  1 
ATOM   11724 O  OE1 . GLU G  1 162 ? -18.418 19.505  59.502 1.00 65.31  ? 153 GLU G OE1 1 
ATOM   11725 O  OE2 . GLU G  1 162 ? -18.848 18.322  61.302 1.00 75.95  ? 153 GLU G OE2 1 
ATOM   11726 N  N   . ILE G  1 163 ? -14.191 20.128  62.458 1.00 54.27  ? 154 ILE G N   1 
ATOM   11727 C  CA  . ILE G  1 163 ? -13.031 20.837  62.986 1.00 56.53  ? 154 ILE G CA  1 
ATOM   11728 C  C   . ILE G  1 163 ? -13.370 21.801  64.143 1.00 60.41  ? 154 ILE G C   1 
ATOM   11729 O  O   . ILE G  1 163 ? -14.181 22.713  64.002 1.00 60.83  ? 154 ILE G O   1 
ATOM   11730 C  CB  . ILE G  1 163 ? -12.283 21.584  61.854 1.00 57.94  ? 154 ILE G CB  1 
ATOM   11731 C  CG1 . ILE G  1 163 ? -11.855 20.591  60.768 1.00 51.82  ? 154 ILE G CG1 1 
ATOM   11732 C  CG2 . ILE G  1 163 ? -11.109 22.409  62.414 1.00 53.06  ? 154 ILE G CG2 1 
ATOM   11733 C  CD1 . ILE G  1 163 ? -10.894 21.147  59.761 1.00 46.23  ? 154 ILE G CD1 1 
ATOM   11734 N  N   . ASP G  1 164 ? -12.745 21.597  65.291 1.00 56.31  ? 155 ASP G N   1 
ATOM   11735 C  CA  . ASP G  1 164 ? -12.903 22.537  66.392 1.00 64.62  ? 155 ASP G CA  1 
ATOM   11736 C  C   . ASP G  1 164 ? -11.650 23.405  66.571 1.00 64.83  ? 155 ASP G C   1 
ATOM   11737 O  O   . ASP G  1 164 ? -10.529 22.895  66.626 1.00 64.36  ? 155 ASP G O   1 
ATOM   11738 C  CB  . ASP G  1 164 ? -13.237 21.794  67.691 1.00 71.28  ? 155 ASP G CB  1 
ATOM   11739 C  CG  . ASP G  1 164 ? -13.714 22.728  68.798 1.00 72.73  ? 155 ASP G CG  1 
ATOM   11740 O  OD1 . ASP G  1 164 ? -14.030 23.904  68.499 1.00 63.86  ? 155 ASP G OD1 1 
ATOM   11741 O  OD2 . ASP G  1 164 ? -13.788 22.272  69.961 1.00 70.73  ? 155 ASP G OD2 1 
ATOM   11742 N  N   . LEU G  1 165 ? -11.848 24.715  66.666 1.00 61.74  ? 156 LEU G N   1 
ATOM   11743 C  CA  . LEU G  1 165 ? -10.742 25.643  66.856 1.00 59.47  ? 156 LEU G CA  1 
ATOM   11744 C  C   . LEU G  1 165 ? -10.534 25.900  68.330 1.00 61.28  ? 156 LEU G C   1 
ATOM   11745 O  O   . LEU G  1 165 ? -11.490 25.935  69.091 1.00 70.15  ? 156 LEU G O   1 
ATOM   11746 C  CB  . LEU G  1 165 ? -11.024 26.968  66.156 1.00 61.31  ? 156 LEU G CB  1 
ATOM   11747 C  CG  . LEU G  1 165 ? -10.743 27.037  64.659 1.00 59.88  ? 156 LEU G CG  1 
ATOM   11748 C  CD1 . LEU G  1 165 ? -11.057 28.424  64.138 1.00 59.35  ? 156 LEU G CD1 1 
ATOM   11749 C  CD2 . LEU G  1 165 ? -9.294  26.669  64.399 1.00 61.14  ? 156 LEU G CD2 1 
ATOM   11750 N  N   . LYS G  1 166 ? -9.281  26.060  68.736 1.00 61.12  ? 157 LYS G N   1 
ATOM   11751 C  CA  . LYS G  1 166 ? -8.956  26.419  70.114 1.00 69.56  ? 157 LYS G CA  1 
ATOM   11752 C  C   . LYS G  1 166 ? -7.665  27.224  70.101 1.00 69.91  ? 157 LYS G C   1 
ATOM   11753 O  O   . LYS G  1 166 ? -6.915  27.179  69.130 1.00 65.35  ? 157 LYS G O   1 
ATOM   11754 C  CB  . LYS G  1 166 ? -8.842  25.173  71.026 1.00 65.65  ? 157 LYS G CB  1 
ATOM   11755 C  CG  . LYS G  1 166 ? -10.194 24.552  71.417 1.00 63.55  ? 157 LYS G CG  1 
ATOM   11756 C  CD  . LYS G  1 166 ? -10.064 23.310  72.278 1.00 74.46  ? 157 LYS G CD  1 
ATOM   11757 C  CE  . LYS G  1 166 ? -10.201 23.614  73.757 1.00 87.22  ? 157 LYS G CE  1 
ATOM   11758 N  NZ  . LYS G  1 166 ? -9.887  22.405  74.571 1.00 80.53  ? 157 LYS G NZ  1 
ATOM   11759 N  N   . THR G  1 167 ? -7.417  27.976  71.167 1.00 76.50  ? 158 THR G N   1 
ATOM   11760 C  CA  . THR G  1 167 ? -6.200  28.767  71.269 1.00 73.46  ? 158 THR G CA  1 
ATOM   11761 C  C   . THR G  1 167 ? -5.484  28.409  72.562 1.00 85.72  ? 158 THR G C   1 
ATOM   11762 O  O   . THR G  1 167 ? -6.129  28.010  73.538 1.00 85.06  ? 158 THR G O   1 
ATOM   11763 C  CB  . THR G  1 167 ? -6.526  30.261  71.261 1.00 68.04  ? 158 THR G CB  1 
ATOM   11764 O  OG1 . THR G  1 167 ? -7.554  30.517  72.222 1.00 70.83  ? 158 THR G OG1 1 
ATOM   11765 C  CG2 . THR G  1 167 ? -7.028  30.686  69.890 1.00 60.65  ? 158 THR G CG2 1 
ATOM   11766 N  N   . ASP G  1 168 ? -4.154  28.513  72.563 1.00 91.53  ? 159 ASP G N   1 
ATOM   11767 C  CA  . ASP G  1 168 ? -3.370  28.293  73.784 1.00 89.77  ? 159 ASP G CA  1 
ATOM   11768 C  C   . ASP G  1 168 ? -3.704  29.359  74.824 1.00 91.19  ? 159 ASP G C   1 
ATOM   11769 O  O   . ASP G  1 168 ? -4.180  29.061  75.918 1.00 82.89  ? 159 ASP G O   1 
ATOM   11770 C  CB  . ASP G  1 168 ? -1.868  28.349  73.480 1.00 86.68  ? 159 ASP G CB  1 
ATOM   11771 C  CG  . ASP G  1 168 ? -1.393  27.180  72.638 1.00 103.77 ? 159 ASP G CG  1 
ATOM   11772 O  OD1 . ASP G  1 168 ? -0.849  26.221  73.230 1.00 105.22 ? 159 ASP G OD1 1 
ATOM   11773 O  OD2 . ASP G  1 168 ? -1.562  27.216  71.391 1.00 93.14  ? 159 ASP G OD2 1 
ATOM   11774 N  N   . THR G  1 169 ? -3.476  30.610  74.444 1.00 89.29  ? 160 THR G N   1 
ATOM   11775 C  CA  . THR G  1 169 ? -3.608  31.739  75.345 1.00 85.03  ? 160 THR G CA  1 
ATOM   11776 C  C   . THR G  1 169 ? -4.620  32.668  74.727 1.00 77.92  ? 160 THR G C   1 
ATOM   11777 O  O   . THR G  1 169 ? -5.160  32.365  73.673 1.00 75.99  ? 160 THR G O   1 
ATOM   11778 C  CB  . THR G  1 169 ? -2.280  32.504  75.448 1.00 80.31  ? 160 THR G CB  1 
ATOM   11779 O  OG1 . THR G  1 169 ? -2.213  33.488  74.407 1.00 71.52  ? 160 THR G OG1 1 
ATOM   11780 C  CG2 . THR G  1 169 ? -1.100  31.544  75.308 1.00 74.95  ? 160 THR G CG2 1 
ATOM   11781 N  N   . ASP G  1 170 ? -4.908  33.774  75.401 1.00 76.09  ? 161 ASP G N   1 
ATOM   11782 C  CA  . ASP G  1 170 ? -5.668  34.869  74.798 1.00 80.70  ? 161 ASP G CA  1 
ATOM   11783 C  C   . ASP G  1 170 ? -4.763  36.015  74.328 1.00 71.85  ? 161 ASP G C   1 
ATOM   11784 O  O   . ASP G  1 170 ? -5.233  37.050  73.855 1.00 69.08  ? 161 ASP G O   1 
ATOM   11785 C  CB  . ASP G  1 170 ? -6.773  35.377  75.744 1.00 96.56  ? 161 ASP G CB  1 
ATOM   11786 C  CG  . ASP G  1 170 ? -8.147  34.742  75.448 1.00 104.04 ? 161 ASP G CG  1 
ATOM   11787 O  OD1 . ASP G  1 170 ? -9.179  35.301  75.911 1.00 93.86  ? 161 ASP G OD1 1 
ATOM   11788 O  OD2 . ASP G  1 170 ? -8.193  33.693  74.749 1.00 99.72  ? 161 ASP G OD2 1 
ATOM   11789 N  N   . GLN G  1 171 ? -3.460  35.842  74.475 1.00 68.04  ? 162 GLN G N   1 
ATOM   11790 C  CA  . GLN G  1 171 ? -2.552  36.922  74.132 1.00 69.86  ? 162 GLN G CA  1 
ATOM   11791 C  C   . GLN G  1 171 ? -1.634  36.538  72.988 1.00 73.40  ? 162 GLN G C   1 
ATOM   11792 O  O   . GLN G  1 171 ? -0.940  35.510  73.041 1.00 69.33  ? 162 GLN G O   1 
ATOM   11793 C  CB  . GLN G  1 171 ? -1.723  37.343  75.346 1.00 71.41  ? 162 GLN G CB  1 
ATOM   11794 C  CG  . GLN G  1 171 ? -2.567  37.722  76.559 1.00 85.86  ? 162 GLN G CG  1 
ATOM   11795 C  CD  . GLN G  1 171 ? -3.458  38.917  76.298 1.00 86.89  ? 162 GLN G CD  1 
ATOM   11796 O  OE1 . GLN G  1 171 ? -2.987  39.954  75.825 1.00 90.91  ? 162 GLN G OE1 1 
ATOM   11797 N  NE2 . GLN G  1 171 ? -4.755  38.777  76.591 1.00 72.79  ? 162 GLN G NE2 1 
ATOM   11798 N  N   . VAL G  1 172 ? -1.642  37.371  71.950 1.00 66.18  ? 163 VAL G N   1 
ATOM   11799 C  CA  . VAL G  1 172 ? -0.707  37.229  70.858 1.00 54.53  ? 163 VAL G CA  1 
ATOM   11800 C  C   . VAL G  1 172 ? 0.708   37.406  71.384 1.00 57.85  ? 163 VAL G C   1 
ATOM   11801 O  O   . VAL G  1 172 ? 0.962   38.263  72.225 1.00 63.26  ? 163 VAL G O   1 
ATOM   11802 C  CB  . VAL G  1 172 ? -0.958  38.281  69.779 1.00 57.51  ? 163 VAL G CB  1 
ATOM   11803 C  CG1 . VAL G  1 172 ? 0.093   38.170  68.674 1.00 60.95  ? 163 VAL G CG1 1 
ATOM   11804 C  CG2 . VAL G  1 172 ? -2.367  38.145  69.218 1.00 54.63  ? 163 VAL G CG2 1 
ATOM   11805 N  N   . ASP G  1 173 ? 1.630   36.598  70.876 1.00 57.85  ? 164 ASP G N   1 
ATOM   11806 C  CA  . ASP G  1 173 ? 3.039   36.736  71.214 1.00 55.71  ? 164 ASP G CA  1 
ATOM   11807 C  C   . ASP G  1 173 ? 3.668   37.922  70.446 1.00 62.12  ? 164 ASP G C   1 
ATOM   11808 O  O   . ASP G  1 173 ? 3.661   37.979  69.189 1.00 53.33  ? 164 ASP G O   1 
ATOM   11809 C  CB  . ASP G  1 173 ? 3.764   35.432  70.891 1.00 46.83  ? 164 ASP G CB  1 
ATOM   11810 C  CG  . ASP G  1 173 ? 5.258   35.576  70.930 1.00 59.25  ? 164 ASP G CG  1 
ATOM   11811 O  OD1 . ASP G  1 173 ? 5.732   36.387  71.750 1.00 59.61  ? 164 ASP G OD1 1 
ATOM   11812 O  OD2 . ASP G  1 173 ? 5.956   34.891  70.140 1.00 56.93  ? 164 ASP G OD2 1 
ATOM   11813 N  N   . LEU G  1 174 ? 4.145   38.913  71.201 1.00 55.73  ? 165 LEU G N   1 
ATOM   11814 C  CA  . LEU G  1 174 ? 4.826   40.046  70.573 1.00 58.74  ? 165 LEU G CA  1 
ATOM   11815 C  C   . LEU G  1 174 ? 6.353   40.023  70.682 1.00 58.43  ? 165 LEU G C   1 
ATOM   11816 O  O   . LEU G  1 174 ? 7.017   40.929  70.183 1.00 54.65  ? 165 LEU G O   1 
ATOM   11817 C  CB  . LEU G  1 174 ? 4.242   41.383  71.034 1.00 46.25  ? 165 LEU G CB  1 
ATOM   11818 C  CG  . LEU G  1 174 ? 2.722   41.514  70.934 1.00 45.17  ? 165 LEU G CG  1 
ATOM   11819 C  CD1 . LEU G  1 174 ? 2.277   42.797  71.569 1.00 54.37  ? 165 LEU G CD1 1 
ATOM   11820 C  CD2 . LEU G  1 174 ? 2.229   41.459  69.506 1.00 51.39  ? 165 LEU G CD2 1 
ATOM   11821 N  N   . SER G  1 175 ? 6.913   39.009  71.339 1.00 54.24  ? 166 SER G N   1 
ATOM   11822 C  CA  . SER G  1 175 ? 8.340   39.057  71.649 1.00 55.83  ? 166 SER G CA  1 
ATOM   11823 C  C   . SER G  1 175 ? 9.245   39.145  70.429 1.00 56.79  ? 166 SER G C   1 
ATOM   11824 O  O   . SER G  1 175 ? 10.367  39.629  70.529 1.00 61.62  ? 166 SER G O   1 
ATOM   11825 C  CB  . SER G  1 175 ? 8.776   37.926  72.587 1.00 56.00  ? 166 SER G CB  1 
ATOM   11826 O  OG  . SER G  1 175 ? 8.072   36.727  72.347 1.00 56.30  ? 166 SER G OG  1 
ATOM   11827 N  N   . SER G  1 176 ? 8.769   38.694  69.276 1.00 55.20  ? 167 SER G N   1 
ATOM   11828 C  CA  . SER G  1 176 ? 9.579   38.786  68.062 1.00 57.04  ? 167 SER G CA  1 
ATOM   11829 C  C   . SER G  1 176 ? 9.262   40.019  67.190 1.00 59.18  ? 167 SER G C   1 
ATOM   11830 O  O   . SER G  1 176 ? 9.929   40.271  66.192 1.00 64.09  ? 167 SER G O   1 
ATOM   11831 C  CB  . SER G  1 176 ? 9.489   37.482  67.257 1.00 69.00  ? 167 SER G CB  1 
ATOM   11832 O  OG  . SER G  1 176 ? 10.117  36.394  67.927 1.00 65.97  ? 167 SER G OG  1 
ATOM   11833 N  N   . TYR G  1 177 ? 8.268   40.807  67.587 1.00 60.51  ? 168 TYR G N   1 
ATOM   11834 C  CA  . TYR G  1 177 ? 7.916   42.025  66.854 1.00 55.72  ? 168 TYR G CA  1 
ATOM   11835 C  C   . TYR G  1 177 ? 9.093   42.981  66.605 1.00 55.15  ? 168 TYR G C   1 
ATOM   11836 O  O   . TYR G  1 177 ? 9.818   43.351  67.519 1.00 58.97  ? 168 TYR G O   1 
ATOM   11837 C  CB  . TYR G  1 177 ? 6.771   42.777  67.544 1.00 51.99  ? 168 TYR G CB  1 
ATOM   11838 C  CG  . TYR G  1 177 ? 6.124   43.779  66.629 1.00 52.60  ? 168 TYR G CG  1 
ATOM   11839 C  CD1 . TYR G  1 177 ? 5.093   43.398  65.758 1.00 57.15  ? 168 TYR G CD1 1 
ATOM   11840 C  CD2 . TYR G  1 177 ? 6.560   45.094  66.592 1.00 54.83  ? 168 TYR G CD2 1 
ATOM   11841 C  CE1 . TYR G  1 177 ? 4.506   44.300  64.890 1.00 48.70  ? 168 TYR G CE1 1 
ATOM   11842 C  CE2 . TYR G  1 177 ? 5.974   46.013  65.727 1.00 63.22  ? 168 TYR G CE2 1 
ATOM   11843 C  CZ  . TYR G  1 177 ? 4.948   45.605  64.878 1.00 56.03  ? 168 TYR G CZ  1 
ATOM   11844 O  OH  . TYR G  1 177 ? 4.366   46.511  64.028 1.00 54.77  ? 168 TYR G OH  1 
ATOM   11845 N  N   . TYR G  1 178 ? 9.252   43.382  65.348 1.00 59.94  ? 169 TYR G N   1 
ATOM   11846 C  CA  . TYR G  1 178 ? 10.315  44.290  64.900 1.00 64.00  ? 169 TYR G CA  1 
ATOM   11847 C  C   . TYR G  1 178 ? 10.239  45.634  65.630 1.00 62.32  ? 169 TYR G C   1 
ATOM   11848 O  O   . TYR G  1 178 ? 9.201   46.312  65.611 1.00 59.59  ? 169 TYR G O   1 
ATOM   11849 C  CB  . TYR G  1 178 ? 10.219  44.488  63.364 1.00 63.84  ? 169 TYR G CB  1 
ATOM   11850 C  CG  . TYR G  1 178 ? 11.310  45.349  62.735 1.00 62.92  ? 169 TYR G CG  1 
ATOM   11851 C  CD1 . TYR G  1 178 ? 12.648  45.187  63.097 1.00 58.40  ? 169 TYR G CD1 1 
ATOM   11852 C  CD2 . TYR G  1 178 ? 11.003  46.311  61.769 1.00 57.46  ? 169 TYR G CD2 1 
ATOM   11853 C  CE1 . TYR G  1 178 ? 13.643  45.960  62.533 1.00 54.53  ? 169 TYR G CE1 1 
ATOM   11854 C  CE2 . TYR G  1 178 ? 11.999  47.094  61.198 1.00 56.34  ? 169 TYR G CE2 1 
ATOM   11855 C  CZ  . TYR G  1 178 ? 13.319  46.910  61.588 1.00 58.94  ? 169 TYR G CZ  1 
ATOM   11856 O  OH  . TYR G  1 178 ? 14.332  47.671  61.049 1.00 59.28  ? 169 TYR G OH  1 
ATOM   11857 N  N   . ALA G  1 179 ? 11.346  46.020  66.262 1.00 68.38  ? 170 ALA G N   1 
ATOM   11858 C  CA  . ALA G  1 179 ? 11.376  47.229  67.091 1.00 64.27  ? 170 ALA G CA  1 
ATOM   11859 C  C   . ALA G  1 179 ? 11.265  48.480  66.241 1.00 66.97  ? 170 ALA G C   1 
ATOM   11860 O  O   . ALA G  1 179 ? 10.662  49.459  66.663 1.00 68.62  ? 170 ALA G O   1 
ATOM   11861 C  CB  . ALA G  1 179 ? 12.646  47.280  67.933 1.00 45.58  ? 170 ALA G CB  1 
ATOM   11862 N  N   . SER G  1 180 ? 11.850  48.437  65.048 1.00 59.20  ? 171 SER G N   1 
ATOM   11863 C  CA  . SER G  1 180 ? 11.951  49.603  64.178 1.00 55.90  ? 171 SER G CA  1 
ATOM   11864 C  C   . SER G  1 180 ? 10.817  49.728  63.159 1.00 56.36  ? 171 SER G C   1 
ATOM   11865 O  O   . SER G  1 180 ? 10.898  50.509  62.216 1.00 57.73  ? 171 SER G O   1 
ATOM   11866 C  CB  . SER G  1 180 ? 13.321  49.675  63.520 1.00 58.13  ? 171 SER G CB  1 
ATOM   11867 O  OG  . SER G  1 180 ? 14.324  49.835  64.506 1.00 54.68  ? 171 SER G OG  1 
ATOM   11868 N  N   . SER G  1 181 ? 9.787   48.910  63.316 1.00 59.45  ? 172 SER G N   1 
ATOM   11869 C  CA  . SER G  1 181 ? 8.628   48.981  62.439 1.00 57.40  ? 172 SER G CA  1 
ATOM   11870 C  C   . SER G  1 181 ? 8.010   50.361  62.432 1.00 54.82  ? 172 SER G C   1 
ATOM   11871 O  O   . SER G  1 181 ? 8.023   51.058  63.439 1.00 62.03  ? 172 SER G O   1 
ATOM   11872 C  CB  . SER G  1 181 ? 7.561   47.980  62.868 1.00 58.52  ? 172 SER G CB  1 
ATOM   11873 O  OG  . SER G  1 181 ? 6.347   48.224  62.173 1.00 56.76  ? 172 SER G OG  1 
ATOM   11874 N  N   . LYS G  1 182 ? 7.442   50.739  61.292 1.00 53.60  ? 173 LYS G N   1 
ATOM   11875 C  CA  . LYS G  1 182 ? 6.734   52.006  61.167 1.00 53.96  ? 173 LYS G CA  1 
ATOM   11876 C  C   . LYS G  1 182 ? 5.569   52.073  62.142 1.00 54.54  ? 173 LYS G C   1 
ATOM   11877 O  O   . LYS G  1 182 ? 4.989   53.132  62.339 1.00 59.39  ? 173 LYS G O   1 
ATOM   11878 C  CB  . LYS G  1 182 ? 6.216   52.215  59.738 1.00 54.54  ? 173 LYS G CB  1 
ATOM   11879 C  CG  . LYS G  1 182 ? 7.178   52.929  58.805 1.00 58.75  ? 173 LYS G CG  1 
ATOM   11880 C  CD  . LYS G  1 182 ? 7.677   54.225  59.426 1.00 65.65  ? 173 LYS G CD  1 
ATOM   11881 C  CE  . LYS G  1 182 ? 8.159   55.214  58.373 1.00 65.38  ? 173 LYS G CE  1 
ATOM   11882 N  NZ  . LYS G  1 182 ? 7.024   55.962  57.765 1.00 57.76  ? 173 LYS G NZ  1 
ATOM   11883 N  N   . TYR G  1 183 ? 5.212   50.942  62.737 1.00 50.12  ? 174 TYR G N   1 
ATOM   11884 C  CA  . TYR G  1 183 ? 4.080   50.914  63.648 1.00 53.82  ? 174 TYR G CA  1 
ATOM   11885 C  C   . TYR G  1 183 ? 4.387   50.237  64.983 1.00 62.29  ? 174 TYR G C   1 
ATOM   11886 O  O   . TYR G  1 183 ? 4.907   49.119  65.019 1.00 59.90  ? 174 TYR G O   1 
ATOM   11887 C  CB  . TYR G  1 183 ? 2.861   50.265  62.980 1.00 48.60  ? 174 TYR G CB  1 
ATOM   11888 C  CG  . TYR G  1 183 ? 2.426   51.020  61.770 1.00 53.09  ? 174 TYR G CG  1 
ATOM   11889 C  CD1 . TYR G  1 183 ? 1.566   52.100  61.881 1.00 54.27  ? 174 TYR G CD1 1 
ATOM   11890 C  CD2 . TYR G  1 183 ? 2.913   50.685  60.511 1.00 52.25  ? 174 TYR G CD2 1 
ATOM   11891 C  CE1 . TYR G  1 183 ? 1.193   52.817  60.778 1.00 52.60  ? 174 TYR G CE1 1 
ATOM   11892 C  CE2 . TYR G  1 183 ? 2.553   51.395  59.405 1.00 50.01  ? 174 TYR G CE2 1 
ATOM   11893 C  CZ  . TYR G  1 183 ? 1.686   52.462  59.537 1.00 56.40  ? 174 TYR G CZ  1 
ATOM   11894 O  OH  . TYR G  1 183 ? 1.306   53.182  58.417 1.00 60.64  ? 174 TYR G OH  1 
ATOM   11895 N  N   . GLU G  1 184 ? 4.086   50.933  66.077 1.00 60.61  ? 175 GLU G N   1 
ATOM   11896 C  CA  . GLU G  1 184 ? 4.072   50.292  67.386 1.00 66.96  ? 175 GLU G CA  1 
ATOM   11897 C  C   . GLU G  1 184 ? 2.731   49.605  67.687 1.00 64.05  ? 175 GLU G C   1 
ATOM   11898 O  O   . GLU G  1 184 ? 1.672   50.029  67.205 1.00 58.13  ? 175 GLU G O   1 
ATOM   11899 C  CB  . GLU G  1 184 ? 4.546   51.223  68.522 1.00 64.88  ? 175 GLU G CB  1 
ATOM   11900 C  CG  . GLU G  1 184 ? 4.081   52.663  68.473 1.00 70.94  ? 175 GLU G CG  1 
ATOM   11901 C  CD  . GLU G  1 184 ? 4.574   53.457  69.677 1.00 76.26  ? 175 GLU G CD  1 
ATOM   11902 O  OE1 . GLU G  1 184 ? 5.133   52.833  70.590 1.00 79.00  ? 175 GLU G OE1 1 
ATOM   11903 O  OE2 . GLU G  1 184 ? 4.412   54.695  69.721 1.00 78.36  ? 175 GLU G OE2 1 
ATOM   11904 N  N   . ILE G  1 185 ? 2.803   48.521  68.455 1.00 57.02  ? 176 ILE G N   1 
ATOM   11905 C  CA  . ILE G  1 185 ? 1.619   47.758  68.823 1.00 59.27  ? 176 ILE G CA  1 
ATOM   11906 C  C   . ILE G  1 185 ? 1.177   48.087  70.248 1.00 58.22  ? 176 ILE G C   1 
ATOM   11907 O  O   . ILE G  1 185 ? 1.947   47.920  71.186 1.00 61.57  ? 176 ILE G O   1 
ATOM   11908 C  CB  . ILE G  1 185 ? 1.897   46.246  68.725 1.00 57.58  ? 176 ILE G CB  1 
ATOM   11909 C  CG1 . ILE G  1 185 ? 2.471   45.908  67.356 1.00 53.88  ? 176 ILE G CG1 1 
ATOM   11910 C  CG2 . ILE G  1 185 ? 0.641   45.444  69.013 1.00 53.12  ? 176 ILE G CG2 1 
ATOM   11911 C  CD1 . ILE G  1 185 ? 1.459   45.979  66.246 1.00 57.34  ? 176 ILE G CD1 1 
ATOM   11912 N  N   . LEU G  1 186 ? -0.050  48.582  70.400 1.00 58.28  ? 177 LEU G N   1 
ATOM   11913 C  CA  . LEU G  1 186 ? -0.602  48.905  71.711 1.00 53.19  ? 177 LEU G CA  1 
ATOM   11914 C  C   . LEU G  1 186 ? -1.124  47.663  72.406 1.00 58.44  ? 177 LEU G C   1 
ATOM   11915 O  O   . LEU G  1 186 ? -0.801  47.412  73.560 1.00 64.76  ? 177 LEU G O   1 
ATOM   11916 C  CB  . LEU G  1 186 ? -1.704  49.952  71.579 1.00 56.04  ? 177 LEU G CB  1 
ATOM   11917 C  CG  . LEU G  1 186 ? -1.270  51.137  70.710 1.00 66.82  ? 177 LEU G CG  1 
ATOM   11918 C  CD1 . LEU G  1 186 ? -2.390  52.130  70.457 1.00 63.26  ? 177 LEU G CD1 1 
ATOM   11919 C  CD2 . LEU G  1 186 ? -0.069  51.820  71.329 1.00 67.60  ? 177 LEU G CD2 1 
ATOM   11920 N  N   . SER G  1 187 ? -1.924  46.879  71.698 1.00 60.28  ? 178 SER G N   1 
ATOM   11921 C  CA  . SER G  1 187 ? -2.373  45.581  72.201 1.00 62.93  ? 178 SER G CA  1 
ATOM   11922 C  C   . SER G  1 187 ? -2.623  44.631  71.042 1.00 62.62  ? 178 SER G C   1 
ATOM   11923 O  O   . SER G  1 187 ? -2.949  45.067  69.938 1.00 62.80  ? 178 SER G O   1 
ATOM   11924 C  CB  . SER G  1 187 ? -3.637  45.709  73.063 1.00 61.97  ? 178 SER G CB  1 
ATOM   11925 O  OG  . SER G  1 187 ? -4.736  46.236  72.340 1.00 58.76  ? 178 SER G OG  1 
ATOM   11926 N  N   . ALA G  1 188 ? -2.431  43.339  71.278 1.00 57.30  ? 179 ALA G N   1 
ATOM   11927 C  CA  . ALA G  1 188 ? -2.759  42.328  70.288 1.00 54.63  ? 179 ALA G CA  1 
ATOM   11928 C  C   . ALA G  1 188 ? -3.381  41.137  70.999 1.00 59.33  ? 179 ALA G C   1 
ATOM   11929 O  O   . ALA G  1 188 ? -2.745  40.542  71.874 1.00 63.23  ? 179 ALA G O   1 
ATOM   11930 C  CB  . ALA G  1 188 ? -1.505  41.911  69.533 1.00 50.63  ? 179 ALA G CB  1 
ATOM   11931 N  N   . THR G  1 189 ? -4.605  40.767  70.630 1.00 58.06  ? 180 THR G N   1 
ATOM   11932 C  CA  . THR G  1 189 ? -5.252  39.619  71.278 1.00 62.94  ? 180 THR G CA  1 
ATOM   11933 C  C   . THR G  1 189 ? -5.920  38.635  70.330 1.00 53.83  ? 180 THR G C   1 
ATOM   11934 O  O   . THR G  1 189 ? -6.552  39.043  69.373 1.00 57.72  ? 180 THR G O   1 
ATOM   11935 C  CB  . THR G  1 189 ? -6.310  40.058  72.300 1.00 59.08  ? 180 THR G CB  1 
ATOM   11936 O  OG1 . THR G  1 189 ? -7.270  40.898  71.658 1.00 58.50  ? 180 THR G OG1 1 
ATOM   11937 C  CG2 . THR G  1 189 ? -5.664  40.810  73.435 1.00 73.92  ? 180 THR G CG2 1 
ATOM   11938 N  N   . GLN G  1 190 ? -5.801  37.341  70.636 1.00 55.93  ? 181 GLN G N   1 
ATOM   11939 C  CA  . GLN G  1 190 ? -6.484  36.275  69.894 1.00 51.04  ? 181 GLN G CA  1 
ATOM   11940 C  C   . GLN G  1 190 ? -7.604  35.590  70.690 1.00 56.40  ? 181 GLN G C   1 
ATOM   11941 O  O   . GLN G  1 190 ? -7.367  34.955  71.705 1.00 64.66  ? 181 GLN G O   1 
ATOM   11942 C  CB  . GLN G  1 190 ? -5.479  35.244  69.406 1.00 49.82  ? 181 GLN G CB  1 
ATOM   11943 C  CG  . GLN G  1 190 ? -4.805  34.469  70.482 1.00 50.49  ? 181 GLN G CG  1 
ATOM   11944 C  CD  . GLN G  1 190 ? -3.421  34.046  70.077 1.00 55.75  ? 181 GLN G CD  1 
ATOM   11945 O  OE1 . GLN G  1 190 ? -2.934  34.426  69.024 1.00 53.57  ? 181 GLN G OE1 1 
ATOM   11946 N  NE2 . GLN G  1 190 ? -2.770  33.262  70.920 1.00 66.05  ? 181 GLN G NE2 1 
ATOM   11947 N  N   . THR G  1 191 ? -8.828  35.722  70.200 1.00 54.49  ? 182 THR G N   1 
ATOM   11948 C  CA  . THR G  1 191 ? -10.028 35.289  70.908 1.00 58.21  ? 182 THR G CA  1 
ATOM   11949 C  C   . THR G  1 191 ? -10.788 34.262  70.075 1.00 49.94  ? 182 THR G C   1 
ATOM   11950 O  O   . THR G  1 191 ? -10.977 34.441  68.887 1.00 49.12  ? 182 THR G O   1 
ATOM   11951 C  CB  . THR G  1 191 ? -10.992 36.488  71.132 1.00 65.48  ? 182 THR G CB  1 
ATOM   11952 O  OG1 . THR G  1 191 ? -10.288 37.580  71.731 1.00 65.77  ? 182 THR G OG1 1 
ATOM   11953 C  CG2 . THR G  1 191 ? -12.202 36.095  71.991 1.00 62.58  ? 182 THR G CG2 1 
ATOM   11954 N  N   . ARG G  1 192 ? -11.261 33.209  70.712 1.00 46.98  ? 183 ARG G N   1 
ATOM   11955 C  CA  . ARG G  1 192 ? -11.987 32.161  70.022 1.00 48.11  ? 183 ARG G CA  1 
ATOM   11956 C  C   . ARG G  1 192 ? -13.484 32.324  70.239 1.00 50.10  ? 183 ARG G C   1 
ATOM   11957 O  O   . ARG G  1 192 ? -13.919 32.659  71.333 1.00 60.55  ? 183 ARG G O   1 
ATOM   11958 C  CB  . ARG G  1 192 ? -11.495 30.807  70.533 1.00 53.52  ? 183 ARG G CB  1 
ATOM   11959 C  CG  . ARG G  1 192 ? -12.092 29.597  69.871 1.00 52.84  ? 183 ARG G CG  1 
ATOM   11960 C  CD  . ARG G  1 192 ? -13.228 29.034  70.675 1.00 54.40  ? 183 ARG G CD  1 
ATOM   11961 N  NE  . ARG G  1 192 ? -13.569 27.701  70.217 1.00 57.12  ? 183 ARG G NE  1 
ATOM   11962 C  CZ  . ARG G  1 192 ? -14.507 26.939  70.759 1.00 63.32  ? 183 ARG G CZ  1 
ATOM   11963 N  NH1 . ARG G  1 192 ? -15.207 27.368  71.792 1.00 74.21  ? 183 ARG G NH1 1 
ATOM   11964 N  NH2 . ARG G  1 192 ? -14.744 25.739  70.264 1.00 75.61  ? 183 ARG G NH2 1 
ATOM   11965 N  N   . SER G  1 193 ? -14.274 32.104  69.195 1.00 46.66  ? 184 SER G N   1 
ATOM   11966 C  CA  . SER G  1 193 ? -15.727 32.241  69.293 1.00 52.06  ? 184 SER G CA  1 
ATOM   11967 C  C   . SER G  1 193 ? -16.459 31.266  68.376 1.00 58.83  ? 184 SER G C   1 
ATOM   11968 O  O   . SER G  1 193 ? -15.915 30.819  67.365 1.00 53.75  ? 184 SER G O   1 
ATOM   11969 C  CB  . SER G  1 193 ? -16.165 33.671  68.973 1.00 50.70  ? 184 SER G CB  1 
ATOM   11970 O  OG  . SER G  1 193 ? -15.245 34.610  69.496 1.00 54.27  ? 184 SER G OG  1 
ATOM   11971 N  N   . GLU G  1 194 ? -17.699 30.945  68.730 1.00 58.98  ? 185 GLU G N   1 
ATOM   11972 C  CA  . GLU G  1 194 ? -18.488 30.021  67.939 1.00 62.88  ? 185 GLU G CA  1 
ATOM   11973 C  C   . GLU G  1 194 ? -19.679 30.728  67.337 1.00 61.10  ? 185 GLU G C   1 
ATOM   11974 O  O   . GLU G  1 194 ? -20.489 31.294  68.053 1.00 63.29  ? 185 GLU G O   1 
ATOM   11975 C  CB  . GLU G  1 194 ? -18.954 28.846  68.794 1.00 62.61  ? 185 GLU G CB  1 
ATOM   11976 C  CG  . GLU G  1 194 ? -17.821 27.949  69.244 1.00 71.27  ? 185 GLU G CG  1 
ATOM   11977 C  CD  . GLU G  1 194 ? -18.306 26.721  69.991 1.00 89.98  ? 185 GLU G CD  1 
ATOM   11978 O  OE1 . GLU G  1 194 ? -17.499 26.101  70.723 1.00 94.23  ? 185 GLU G OE1 1 
ATOM   11979 O  OE2 . GLU G  1 194 ? -19.495 26.370  69.847 1.00 90.20  ? 185 GLU G OE2 1 
ATOM   11980 N  N   . ARG G  1 195 ? -19.777 30.702  66.014 1.00 61.73  ? 186 ARG G N   1 
ATOM   11981 C  CA  . ARG G  1 195 ? -20.933 31.264  65.327 1.00 68.94  ? 186 ARG G CA  1 
ATOM   11982 C  C   . ARG G  1 195 ? -22.062 30.265  65.165 1.00 64.18  ? 186 ARG G C   1 
ATOM   11983 O  O   . ARG G  1 195 ? -21.830 29.108  64.866 1.00 66.90  ? 186 ARG G O   1 
ATOM   11984 C  CB  . ARG G  1 195 ? -20.543 31.762  63.945 1.00 73.71  ? 186 ARG G CB  1 
ATOM   11985 C  CG  . ARG G  1 195 ? -20.262 33.238  63.883 1.00 85.65  ? 186 ARG G CG  1 
ATOM   11986 C  CD  . ARG G  1 195 ? -20.747 33.780  62.565 1.00 89.58  ? 186 ARG G CD  1 
ATOM   11987 N  NE  . ARG G  1 195 ? -20.270 35.131  62.316 1.00 88.80  ? 186 ARG G NE  1 
ATOM   11988 C  CZ  . ARG G  1 195 ? -20.453 35.765  61.168 1.00 92.09  ? 186 ARG G CZ  1 
ATOM   11989 N  NH1 . ARG G  1 195 ? -21.100 35.154  60.181 1.00 100.82 ? 186 ARG G NH1 1 
ATOM   11990 N  NH2 . ARG G  1 195 ? -19.992 36.998  61.004 1.00 92.41  ? 186 ARG G NH2 1 
ATOM   11991 N  N   . PHE G  1 196 ? -23.288 30.725  65.361 1.00 66.75  ? 187 PHE G N   1 
ATOM   11992 C  CA  . PHE G  1 196 ? -24.447 29.934  65.014 1.00 69.26  ? 187 PHE G CA  1 
ATOM   11993 C  C   . PHE G  1 196 ? -25.326 30.722  64.087 1.00 76.31  ? 187 PHE G C   1 
ATOM   11994 O  O   . PHE G  1 196 ? -25.955 31.688  64.494 1.00 78.36  ? 187 PHE G O   1 
ATOM   11995 C  CB  . PHE G  1 196 ? -25.246 29.592  66.262 1.00 71.48  ? 187 PHE G CB  1 
ATOM   11996 C  CG  . PHE G  1 196 ? -24.554 28.633  67.151 1.00 68.12  ? 187 PHE G CG  1 
ATOM   11997 C  CD1 . PHE G  1 196 ? -24.833 27.287  67.077 1.00 60.80  ? 187 PHE G CD1 1 
ATOM   11998 C  CD2 . PHE G  1 196 ? -23.586 29.070  68.030 1.00 68.00  ? 187 PHE G CD2 1 
ATOM   11999 C  CE1 . PHE G  1 196 ? -24.176 26.402  67.871 1.00 64.25  ? 187 PHE G CE1 1 
ATOM   12000 C  CE2 . PHE G  1 196 ? -22.927 28.186  68.826 1.00 66.73  ? 187 PHE G CE2 1 
ATOM   12001 C  CZ  . PHE G  1 196 ? -23.223 26.850  68.749 1.00 67.56  ? 187 PHE G CZ  1 
ATOM   12002 N  N   . TYR G  1 197 ? -25.433 30.250  62.863 1.00 87.92  ? 188 TYR G N   1 
ATOM   12003 C  CA  . TYR G  1 197 ? -26.456 30.703  61.958 1.00 87.13  ? 188 TYR G CA  1 
ATOM   12004 C  C   . TYR G  1 197 ? -27.653 29.817  62.209 1.00 95.17  ? 188 TYR G C   1 
ATOM   12005 O  O   . TYR G  1 197 ? -27.493 28.652  62.460 1.00 99.41  ? 188 TYR G O   1 
ATOM   12006 C  CB  . TYR G  1 197 ? -25.995 30.569  60.522 1.00 87.83  ? 188 TYR G CB  1 
ATOM   12007 C  CG  . TYR G  1 197 ? -24.541 30.872  60.287 1.00 88.40  ? 188 TYR G CG  1 
ATOM   12008 C  CD1 . TYR G  1 197 ? -24.148 32.063  59.751 1.00 87.58  ? 188 TYR G CD1 1 
ATOM   12009 C  CD2 . TYR G  1 197 ? -23.578 29.949  60.566 1.00 87.34  ? 188 TYR G CD2 1 
ATOM   12010 C  CE1 . TYR G  1 197 ? -22.851 32.335  59.525 1.00 90.58  ? 188 TYR G CE1 1 
ATOM   12011 C  CE2 . TYR G  1 197 ? -22.281 30.209  60.338 1.00 86.02  ? 188 TYR G CE2 1 
ATOM   12012 C  CZ  . TYR G  1 197 ? -21.916 31.404  59.815 1.00 94.39  ? 188 TYR G CZ  1 
ATOM   12013 O  OH  . TYR G  1 197 ? -20.591 31.666  59.588 1.00 97.24  ? 188 TYR G OH  1 
ATOM   12014 N  N   . GLU G  1 198 ? -28.855 30.361  62.151 1.00 102.38 ? 189 GLU G N   1 
ATOM   12015 C  CA  . GLU G  1 198 ? -29.912 29.635  62.647 1.00 103.38 ? 189 GLU G CA  1 
ATOM   12016 C  C   . GLU G  1 198 ? -30.568 28.644  61.656 1.00 100.21 ? 189 GLU G C   1 
ATOM   12017 O  O   . GLU G  1 198 ? -31.494 27.920  61.949 1.00 101.74 ? 189 GLU G O   1 
ATOM   12018 C  CB  . GLU G  1 198 ? -30.990 30.549  63.281 1.00 106.25 ? 189 GLU G CB  1 
ATOM   12019 C  CG  . GLU G  1 198 ? -31.796 31.464  62.347 1.00 118.62 ? 189 GLU G CG  1 
ATOM   12020 C  CD  . GLU G  1 198 ? -33.206 31.778  62.873 1.00 111.40 ? 189 GLU G CD  1 
ATOM   12021 O  OE1 . GLU G  1 198 ? -33.346 31.997  64.082 1.00 92.70  ? 189 GLU G OE1 1 
ATOM   12022 O  OE2 . GLU G  1 198 ? -34.172 31.797  62.074 1.00 118.23 ? 189 GLU G OE2 1 
ATOM   12023 N  N   . CYS G  1 199 ? -29.995 28.609  60.474 1.00 94.46  ? 190 CYS G N   1 
ATOM   12024 C  CA  . CYS G  1 199 ? -30.308 27.545  59.554 1.00 100.34 ? 190 CYS G CA  1 
ATOM   12025 C  C   . CYS G  1 199 ? -29.863 26.231  60.137 1.00 96.67  ? 190 CYS G C   1 
ATOM   12026 O  O   . CYS G  1 199 ? -30.563 25.243  60.047 1.00 93.59  ? 190 CYS G O   1 
ATOM   12027 C  CB  . CYS G  1 199 ? -29.520 27.733  58.287 1.00 94.03  ? 190 CYS G CB  1 
ATOM   12028 S  SG  . CYS G  1 199 ? -27.864 27.194  58.513 1.00 99.05  ? 190 CYS G SG  1 
ATOM   12029 N  N   . CYS G  1 200 ? -28.685 26.220  60.741 1.00 96.23  ? 191 CYS G N   1 
ATOM   12030 C  CA  . CYS G  1 200 ? -28.108 24.986  61.237 1.00 93.75  ? 191 CYS G CA  1 
ATOM   12031 C  C   . CYS G  1 200 ? -27.862 24.992  62.722 1.00 89.46  ? 191 CYS G C   1 
ATOM   12032 O  O   . CYS G  1 200 ? -27.686 26.031  63.326 1.00 81.49  ? 191 CYS G O   1 
ATOM   12033 C  CB  . CYS G  1 200 ? -26.774 24.714  60.578 1.00 96.55  ? 191 CYS G CB  1 
ATOM   12034 S  SG  . CYS G  1 200 ? -26.587 25.360  58.972 1.00 105.55 ? 191 CYS G SG  1 
ATOM   12035 N  N   . LYS G  1 201 ? -27.852 23.803  63.301 1.00 84.86  ? 192 LYS G N   1 
ATOM   12036 C  CA  . LYS G  1 201 ? -27.557 23.651  64.707 1.00 76.44  ? 192 LYS G CA  1 
ATOM   12037 C  C   . LYS G  1 201 ? -26.058 23.513  64.912 1.00 73.69  ? 192 LYS G C   1 
ATOM   12038 O  O   . LYS G  1 201 ? -25.580 23.541  66.037 1.00 74.17  ? 192 LYS G O   1 
ATOM   12039 C  CB  . LYS G  1 201 ? -28.293 22.445  65.285 1.00 70.16  ? 192 LYS G CB  1 
ATOM   12040 C  CG  . LYS G  1 201 ? -29.773 22.684  65.524 0.00 87.85  ? 192 LYS G CG  1 
ATOM   12041 C  CD  . LYS G  1 201 ? -30.620 22.176  64.373 0.00 94.38  ? 192 LYS G CD  1 
ATOM   12042 C  CE  . LYS G  1 201 ? -32.096 22.411  64.645 0.00 100.65 ? 192 LYS G CE  1 
ATOM   12043 N  NZ  . LYS G  1 201 ? -32.950 21.454  63.893 0.00 104.42 ? 192 LYS G NZ  1 
ATOM   12044 N  N   . GLU G  1 202 ? -25.313 23.380  63.821 1.00 76.28  ? 193 GLU G N   1 
ATOM   12045 C  CA  . GLU G  1 202 ? -23.865 23.213  63.913 1.00 71.60  ? 193 GLU G CA  1 
ATOM   12046 C  C   . GLU G  1 202 ? -23.140 24.551  64.013 1.00 73.97  ? 193 GLU G C   1 
ATOM   12047 O  O   . GLU G  1 202 ? -23.405 25.473  63.229 1.00 71.83  ? 193 GLU G O   1 
ATOM   12048 C  CB  . GLU G  1 202 ? -23.312 22.408  62.733 1.00 75.13  ? 193 GLU G CB  1 
ATOM   12049 C  CG  . GLU G  1 202 ? -21.794 22.313  62.728 1.00 69.45  ? 193 GLU G CG  1 
ATOM   12050 C  CD  . GLU G  1 202 ? -21.241 21.505  61.567 1.00 76.34  ? 193 GLU G CD  1 
ATOM   12051 O  OE1 . GLU G  1 202 ? -21.915 21.388  60.520 1.00 74.32  ? 193 GLU G OE1 1 
ATOM   12052 O  OE2 . GLU G  1 202 ? -20.119 20.977  61.711 1.00 74.95  ? 193 GLU G OE2 1 
ATOM   12053 N  N   . PRO G  1 203 ? -22.224 24.651  64.995 1.00 69.55  ? 194 PRO G N   1 
ATOM   12054 C  CA  . PRO G  1 203 ? -21.368 25.796  65.314 1.00 65.32  ? 194 PRO G CA  1 
ATOM   12055 C  C   . PRO G  1 203 ? -20.191 26.003  64.355 1.00 62.03  ? 194 PRO G C   1 
ATOM   12056 O  O   . PRO G  1 203 ? -19.549 25.052  63.928 1.00 60.91  ? 194 PRO G O   1 
ATOM   12057 C  CB  . PRO G  1 203 ? -20.836 25.427  66.700 1.00 64.78  ? 194 PRO G CB  1 
ATOM   12058 C  CG  . PRO G  1 203 ? -20.776 23.969  66.675 1.00 51.62  ? 194 PRO G CG  1 
ATOM   12059 C  CD  . PRO G  1 203 ? -22.020 23.558  65.960 1.00 63.96  ? 194 PRO G CD  1 
ATOM   12060 N  N   . TYR G  1 204 ? -19.895 27.256  64.044 1.00 61.35  ? 195 TYR G N   1 
ATOM   12061 C  CA  . TYR G  1 204 ? -18.707 27.572  63.277 1.00 60.29  ? 195 TYR G CA  1 
ATOM   12062 C  C   . TYR G  1 204 ? -17.726 28.408  64.082 1.00 63.84  ? 195 TYR G C   1 
ATOM   12063 O  O   . TYR G  1 204 ? -17.935 29.600  64.270 1.00 67.31  ? 195 TYR G O   1 
ATOM   12064 C  CB  . TYR G  1 204 ? -19.118 28.285  61.999 1.00 65.54  ? 195 TYR G CB  1 
ATOM   12065 C  CG  . TYR G  1 204 ? -20.019 27.398  61.181 1.00 75.94  ? 195 TYR G CG  1 
ATOM   12066 C  CD1 . TYR G  1 204 ? -19.496 26.343  60.456 1.00 75.65  ? 195 TYR G CD1 1 
ATOM   12067 C  CD2 . TYR G  1 204 ? -21.390 27.580  61.175 1.00 74.61  ? 195 TYR G CD2 1 
ATOM   12068 C  CE1 . TYR G  1 204 ? -20.306 25.513  59.730 1.00 77.33  ? 195 TYR G CE1 1 
ATOM   12069 C  CE2 . TYR G  1 204 ? -22.206 26.759  60.449 1.00 78.69  ? 195 TYR G CE2 1 
ATOM   12070 C  CZ  . TYR G  1 204 ? -21.661 25.722  59.727 1.00 83.10  ? 195 TYR G CZ  1 
ATOM   12071 O  OH  . TYR G  1 204 ? -22.475 24.887  58.992 1.00 85.71  ? 195 TYR G OH  1 
ATOM   12072 N  N   . PRO G  1 205 ? -16.645 27.780  64.557 1.00 56.61  ? 196 PRO G N   1 
ATOM   12073 C  CA  . PRO G  1 205 ? -15.614 28.493  65.307 1.00 57.02  ? 196 PRO G CA  1 
ATOM   12074 C  C   . PRO G  1 205 ? -14.713 29.332  64.424 1.00 56.89  ? 196 PRO G C   1 
ATOM   12075 O  O   . PRO G  1 205 ? -14.324 28.894  63.354 1.00 59.21  ? 196 PRO G O   1 
ATOM   12076 C  CB  . PRO G  1 205 ? -14.811 27.367  65.948 1.00 53.25  ? 196 PRO G CB  1 
ATOM   12077 C  CG  . PRO G  1 205 ? -15.026 26.216  65.072 1.00 61.69  ? 196 PRO G CG  1 
ATOM   12078 C  CD  . PRO G  1 205 ? -16.411 26.333  64.538 1.00 53.79  ? 196 PRO G CD  1 
ATOM   12079 N  N   . ASP G  1 206 ? -14.389 30.530  64.894 1.00 57.10  ? 197 ASP G N   1 
ATOM   12080 C  CA  . ASP G  1 206 ? -13.339 31.355  64.317 1.00 56.70  ? 197 ASP G CA  1 
ATOM   12081 C  C   . ASP G  1 206 ? -12.441 31.869  65.439 1.00 56.24  ? 197 ASP G C   1 
ATOM   12082 O  O   . ASP G  1 206 ? -12.797 31.813  66.606 1.00 52.31  ? 197 ASP G O   1 
ATOM   12083 C  CB  . ASP G  1 206 ? -13.927 32.539  63.550 1.00 61.90  ? 197 ASP G CB  1 
ATOM   12084 C  CG  . ASP G  1 206 ? -15.025 33.247  64.318 1.00 68.03  ? 197 ASP G CG  1 
ATOM   12085 O  OD1 . ASP G  1 206 ? -14.718 34.144  65.141 1.00 62.38  ? 197 ASP G OD1 1 
ATOM   12086 O  OD2 . ASP G  1 206 ? -16.204 32.909  64.088 1.00 71.70  ? 197 ASP G OD2 1 
ATOM   12087 N  N   . VAL G  1 207 ? -11.266 32.355  65.077 1.00 55.86  ? 198 VAL G N   1 
ATOM   12088 C  CA  . VAL G  1 207 ? -10.386 33.008  66.025 1.00 50.43  ? 198 VAL G CA  1 
ATOM   12089 C  C   . VAL G  1 207 ? -10.209 34.447  65.561 1.00 55.14  ? 198 VAL G C   1 
ATOM   12090 O  O   . VAL G  1 207 ? -9.802  34.698  64.429 1.00 58.10  ? 198 VAL G O   1 
ATOM   12091 C  CB  . VAL G  1 207 ? -9.027  32.291  66.121 1.00 53.16  ? 198 VAL G CB  1 
ATOM   12092 C  CG1 . VAL G  1 207 ? -7.950  33.218  66.671 1.00 48.28  ? 198 VAL G CG1 1 
ATOM   12093 C  CG2 . VAL G  1 207 ? -9.155  31.027  66.964 1.00 53.02  ? 198 VAL G CG2 1 
ATOM   12094 N  N   . ASN G  1 208 ? -10.548 35.393  66.429 1.00 55.02  ? 199 ASN G N   1 
ATOM   12095 C  CA  . ASN G  1 208 ? -10.486 36.803  66.088 1.00 53.24  ? 199 ASN G CA  1 
ATOM   12096 C  C   . ASN G  1 208 ? -9.168  37.387  66.550 1.00 49.34  ? 199 ASN G C   1 
ATOM   12097 O  O   . ASN G  1 208 ? -8.862  37.365  67.723 1.00 51.24  ? 199 ASN G O   1 
ATOM   12098 C  CB  . ASN G  1 208 ? -11.654 37.541  66.732 1.00 55.85  ? 199 ASN G CB  1 
ATOM   12099 C  CG  . ASN G  1 208 ? -11.838 38.935  66.179 1.00 58.89  ? 199 ASN G CG  1 
ATOM   12100 O  OD1 . ASN G  1 208 ? -11.453 39.220  65.048 1.00 60.16  ? 199 ASN G OD1 1 
ATOM   12101 N  ND2 . ASN G  1 208 ? -12.437 39.816  66.978 1.00 53.33  ? 199 ASN G ND2 1 
ATOM   12102 N  N   . LEU G  1 209 ? -8.376  37.884  65.615 1.00 50.21  ? 200 LEU G N   1 
ATOM   12103 C  CA  . LEU G  1 209 ? -7.101  38.487  65.943 1.00 49.86  ? 200 LEU G CA  1 
ATOM   12104 C  C   . LEU G  1 209 ? -7.275  39.989  65.855 1.00 56.38  ? 200 LEU G C   1 
ATOM   12105 O  O   . LEU G  1 209 ? -7.410  40.529  64.767 1.00 57.83  ? 200 LEU G O   1 
ATOM   12106 C  CB  . LEU G  1 209 ? -6.043  38.042  64.942 1.00 52.20  ? 200 LEU G CB  1 
ATOM   12107 C  CG  . LEU G  1 209 ? -4.708  38.774  64.973 1.00 50.62  ? 200 LEU G CG  1 
ATOM   12108 C  CD1 . LEU G  1 209 ? -3.938  38.290  66.148 1.00 61.23  ? 200 LEU G CD1 1 
ATOM   12109 C  CD2 . LEU G  1 209 ? -3.921  38.502  63.728 1.00 50.17  ? 200 LEU G CD2 1 
ATOM   12110 N  N   . VAL G  1 210 ? -7.268  40.662  67.003 1.00 62.91  ? 201 VAL G N   1 
ATOM   12111 C  CA  . VAL G  1 210 ? -7.480  42.103  67.062 1.00 56.56  ? 201 VAL G CA  1 
ATOM   12112 C  C   . VAL G  1 210 ? -6.192  42.828  67.410 1.00 54.71  ? 201 VAL G C   1 
ATOM   12113 O  O   . VAL G  1 210 ? -5.538  42.507  68.401 1.00 54.90  ? 201 VAL G O   1 
ATOM   12114 C  CB  . VAL G  1 210 ? -8.541  42.465  68.102 1.00 54.70  ? 201 VAL G CB  1 
ATOM   12115 C  CG1 . VAL G  1 210 ? -8.783  43.976  68.097 1.00 50.90  ? 201 VAL G CG1 1 
ATOM   12116 C  CG2 . VAL G  1 210 ? -9.827  41.698  67.829 1.00 52.48  ? 201 VAL G CG2 1 
ATOM   12117 N  N   . VAL G  1 211 ? -5.834  43.810  66.594 1.00 51.49  ? 202 VAL G N   1 
ATOM   12118 C  CA  . VAL G  1 211 ? -4.602  44.561  66.800 1.00 52.32  ? 202 VAL G CA  1 
ATOM   12119 C  C   . VAL G  1 211 ? -4.859  46.063  66.956 1.00 59.05  ? 202 VAL G C   1 
ATOM   12120 O  O   . VAL G  1 211 ? -5.521  46.685  66.125 1.00 64.61  ? 202 VAL G O   1 
ATOM   12121 C  CB  . VAL G  1 211 ? -3.613  44.318  65.653 1.00 48.38  ? 202 VAL G CB  1 
ATOM   12122 C  CG1 . VAL G  1 211 ? -2.384  45.170  65.818 1.00 47.54  ? 202 VAL G CG1 1 
ATOM   12123 C  CG2 . VAL G  1 211 ? -3.249  42.846  65.579 1.00 50.00  ? 202 VAL G CG2 1 
ATOM   12124 N  N   . LYS G  1 212 ? -4.343  46.632  68.040 1.00 60.04  ? 203 LYS G N   1 
ATOM   12125 C  CA  . LYS G  1 212 ? -4.386  48.072  68.263 1.00 63.87  ? 203 LYS G CA  1 
ATOM   12126 C  C   . LYS G  1 212 ? -2.971  48.595  68.010 1.00 61.72  ? 203 LYS G C   1 
ATOM   12127 O  O   . LYS G  1 212 ? -2.015  48.095  68.599 1.00 62.48  ? 203 LYS G O   1 
ATOM   12128 C  CB  . LYS G  1 212 ? -4.827  48.377  69.707 1.00 65.35  ? 203 LYS G CB  1 
ATOM   12129 C  CG  . LYS G  1 212 ? -5.411  49.769  69.917 1.00 71.17  ? 203 LYS G CG  1 
ATOM   12130 C  CD  . LYS G  1 212 ? -5.278  50.239  71.366 1.00 79.04  ? 203 LYS G CD  1 
ATOM   12131 C  CE  . LYS G  1 212 ? -6.404  49.725  72.263 1.00 82.38  ? 203 LYS G CE  1 
ATOM   12132 N  NZ  . LYS G  1 212 ? -7.654  50.530  72.178 1.00 71.77  ? 203 LYS G NZ  1 
ATOM   12133 N  N   . PHE G  1 213 ? -2.823  49.580  67.130 1.00 58.14  ? 204 PHE G N   1 
ATOM   12134 C  CA  . PHE G  1 213 ? -1.489  50.017  66.726 1.00 58.33  ? 204 PHE G CA  1 
ATOM   12135 C  C   . PHE G  1 213 ? -1.468  51.492  66.313 1.00 62.38  ? 204 PHE G C   1 
ATOM   12136 O  O   . PHE G  1 213 ? -2.507  52.065  65.957 1.00 58.38  ? 204 PHE G O   1 
ATOM   12137 C  CB  . PHE G  1 213 ? -0.983  49.139  65.570 1.00 57.91  ? 204 PHE G CB  1 
ATOM   12138 C  CG  . PHE G  1 213 ? -1.780  49.293  64.300 1.00 54.42  ? 204 PHE G CG  1 
ATOM   12139 C  CD1 . PHE G  1 213 ? -1.253  49.971  63.207 1.00 50.51  ? 204 PHE G CD1 1 
ATOM   12140 C  CD2 . PHE G  1 213 ? -3.071  48.796  64.212 1.00 55.52  ? 204 PHE G CD2 1 
ATOM   12141 C  CE1 . PHE G  1 213 ? -1.992  50.129  62.054 1.00 50.72  ? 204 PHE G CE1 1 
ATOM   12142 C  CE2 . PHE G  1 213 ? -3.817  48.955  63.050 1.00 56.39  ? 204 PHE G CE2 1 
ATOM   12143 C  CZ  . PHE G  1 213 ? -3.274  49.617  61.973 1.00 50.08  ? 204 PHE G CZ  1 
ATOM   12144 N  N   . ARG G  1 214 ? -0.283  52.098  66.339 1.00 61.46  ? 205 ARG G N   1 
ATOM   12145 C  CA  . ARG G  1 214 ? -0.133  53.500  65.946 1.00 66.79  ? 205 ARG G CA  1 
ATOM   12146 C  C   . ARG G  1 214 ? 1.256   53.754  65.359 1.00 65.42  ? 205 ARG G C   1 
ATOM   12147 O  O   . ARG G  1 214 ? 2.158   52.932  65.508 1.00 58.54  ? 205 ARG G O   1 
ATOM   12148 C  CB  . ARG G  1 214 ? -0.379  54.430  67.142 1.00 67.16  ? 205 ARG G CB  1 
ATOM   12149 C  CG  . ARG G  1 214 ? 0.763   54.430  68.126 1.00 62.70  ? 205 ARG G CG  1 
ATOM   12150 C  CD  . ARG G  1 214 ? 0.552   55.361  69.291 1.00 72.81  ? 205 ARG G CD  1 
ATOM   12151 N  NE  . ARG G  1 214 ? 1.657   55.202  70.225 1.00 73.03  ? 205 ARG G NE  1 
ATOM   12152 C  CZ  . ARG G  1 214 ? 1.536   55.231  71.545 1.00 75.74  ? 205 ARG G CZ  1 
ATOM   12153 N  NH1 . ARG G  1 214 ? 0.345   55.434  72.095 1.00 82.68  ? 205 ARG G NH1 1 
ATOM   12154 N  NH2 . ARG G  1 214 ? 2.606   55.053  72.310 1.00 66.04  ? 205 ARG G NH2 1 
ATOM   12155 N  N   . GLU G  1 215 ? 1.425   54.889  64.688 1.00 65.37  ? 206 GLU G N   1 
ATOM   12156 C  CA  . GLU G  1 215 ? 2.708   55.211  64.080 1.00 62.85  ? 206 GLU G CA  1 
ATOM   12157 C  C   . GLU G  1 215 ? 3.771   55.426  65.136 1.00 62.78  ? 206 GLU G C   1 
ATOM   12158 O  O   . GLU G  1 215 ? 3.481   55.846  66.246 1.00 65.04  ? 206 GLU G O   1 
ATOM   12159 C  CB  . GLU G  1 215 ? 2.616   56.467  63.225 1.00 66.38  ? 206 GLU G CB  1 
ATOM   12160 C  CG  . GLU G  1 215 ? 1.613   56.432  62.098 1.00 64.20  ? 206 GLU G CG  1 
ATOM   12161 C  CD  . GLU G  1 215 ? 1.436   57.805  61.466 1.00 74.54  ? 206 GLU G CD  1 
ATOM   12162 O  OE1 . GLU G  1 215 ? 1.968   58.796  62.019 1.00 73.57  ? 206 GLU G OE1 1 
ATOM   12163 O  OE2 . GLU G  1 215 ? 0.768   57.902  60.418 1.00 80.32  ? 206 GLU G OE2 1 
ATOM   12164 N  N   . ARG G  1 216 ? 5.014   55.166  64.765 1.00 64.13  ? 207 ARG G N   1 
ATOM   12165 C  CA  . ARG G  1 216 ? 6.129   55.317  65.675 1.00 67.77  ? 207 ARG G CA  1 
ATOM   12166 C  C   . ARG G  1 216 ? 6.922   56.563  65.311 1.00 72.18  ? 207 ARG G C   1 
ATOM   12167 O  O   . ARG G  1 216 ? 6.671   57.644  65.841 1.00 78.86  ? 207 ARG G O   1 
ATOM   12168 C  CB  . ARG G  1 216 ? 7.026   54.085  65.589 1.00 75.10  ? 207 ARG G CB  1 
ATOM   12169 C  CG  . ARG G  1 216 ? 8.121   54.036  66.635 1.00 81.09  ? 207 ARG G CG  1 
ATOM   12170 C  CD  . ARG G  1 216 ? 9.161   52.990  66.287 1.00 76.52  ? 207 ARG G CD  1 
ATOM   12171 N  NE  . ARG G  1 216 ? 8.631   51.633  66.386 1.00 82.00  ? 207 ARG G NE  1 
ATOM   12172 C  CZ  . ARG G  1 216 ? 8.518   50.958  67.532 1.00 91.47  ? 207 ARG G CZ  1 
ATOM   12173 N  NH1 . ARG G  1 216 ? 8.889   51.535  68.673 1.00 87.46  ? 207 ARG G NH1 1 
ATOM   12174 N  NH2 . ARG G  1 216 ? 8.040   49.708  67.543 1.00 79.85  ? 207 ARG G NH2 1 
ATOM   12175 N  N   . LYS H  1 3   ? 37.676  7.178   18.131 1.00 98.95  ? -6  LYS H N   1 
ATOM   12176 C  CA  . LYS H  1 3   ? 39.044  6.952   18.593 1.00 113.31 ? -6  LYS H CA  1 
ATOM   12177 C  C   . LYS H  1 3   ? 39.275  7.522   20.003 1.00 110.81 ? -6  LYS H C   1 
ATOM   12178 O  O   . LYS H  1 3   ? 39.439  6.777   20.973 1.00 95.70  ? -6  LYS H O   1 
ATOM   12179 C  CB  . LYS H  1 3   ? 40.045  7.554   17.596 1.00 120.29 ? -6  LYS H CB  1 
ATOM   12180 C  CG  . LYS H  1 3   ? 39.703  8.970   17.119 1.00 106.13 ? -6  LYS H CG  1 
ATOM   12181 C  CD  . LYS H  1 3   ? 40.957  9.736   16.688 1.00 111.29 ? -6  LYS H CD  1 
ATOM   12182 C  CE  . LYS H  1 3   ? 41.944  9.944   17.849 1.00 113.50 ? -6  LYS H CE  1 
ATOM   12183 N  NZ  . LYS H  1 3   ? 42.901  11.068  17.576 1.00 112.66 ? -6  LYS H NZ  1 
ATOM   12184 N  N   . ASP H  1 4   ? 39.317  8.851   20.089 1.00 115.15 ? -5  ASP H N   1 
ATOM   12185 C  CA  . ASP H  1 4   ? 39.281  9.567   21.360 1.00 108.82 ? -5  ASP H CA  1 
ATOM   12186 C  C   . ASP H  1 4   ? 37.820  9.919   21.681 1.00 103.26 ? -5  ASP H C   1 
ATOM   12187 O  O   . ASP H  1 4   ? 37.515  10.543  22.702 1.00 93.83  ? -5  ASP H O   1 
ATOM   12188 C  CB  . ASP H  1 4   ? 40.172  10.822  21.309 1.00 110.81 ? -5  ASP H CB  1 
ATOM   12189 C  CG  . ASP H  1 4   ? 39.850  11.746  20.124 1.00 112.76 ? -5  ASP H CG  1 
ATOM   12190 O  OD1 . ASP H  1 4   ? 39.272  11.282  19.116 1.00 108.80 ? -5  ASP H OD1 1 
ATOM   12191 O  OD2 . ASP H  1 4   ? 40.193  12.948  20.199 1.00 107.36 ? -5  ASP H OD2 1 
ATOM   12192 N  N   . ASP H  1 5   ? 36.930  9.526   20.767 1.00 101.75 ? -4  ASP H N   1 
ATOM   12193 C  CA  . ASP H  1 5   ? 35.488  9.649   20.952 1.00 95.63  ? -4  ASP H CA  1 
ATOM   12194 C  C   . ASP H  1 5   ? 34.888  8.530   21.805 1.00 96.62  ? -4  ASP H C   1 
ATOM   12195 O  O   . ASP H  1 5   ? 33.977  8.768   22.589 1.00 101.63 ? -4  ASP H O   1 
ATOM   12196 C  CB  . ASP H  1 5   ? 34.766  9.726   19.604 1.00 100.17 ? -4  ASP H CB  1 
ATOM   12197 C  CG  . ASP H  1 5   ? 33.320  9.239   19.684 1.00 108.55 ? -4  ASP H CG  1 
ATOM   12198 O  OD1 . ASP H  1 5   ? 32.605  9.582   20.655 1.00 90.80  ? -4  ASP H OD1 1 
ATOM   12199 O  OD2 . ASP H  1 5   ? 32.896  8.497   18.768 1.00 112.59 ? -4  ASP H OD2 1 
ATOM   12200 N  N   . ASP H  1 6   ? 35.362  7.302   21.639 1.00 96.67  ? -3  ASP H N   1 
ATOM   12201 C  CA  . ASP H  1 6   ? 34.920  6.243   22.534 1.00 98.07  ? -3  ASP H CA  1 
ATOM   12202 C  C   . ASP H  1 6   ? 35.173  6.744   23.957 1.00 94.81  ? -3  ASP H C   1 
ATOM   12203 O  O   . ASP H  1 6   ? 34.339  6.583   24.854 1.00 85.93  ? -3  ASP H O   1 
ATOM   12204 C  CB  . ASP H  1 6   ? 35.682  4.946   22.262 1.00 96.08  ? -3  ASP H CB  1 
ATOM   12205 C  CG  . ASP H  1 6   ? 34.863  3.712   22.591 1.00 91.12  ? -3  ASP H CG  1 
ATOM   12206 O  OD1 . ASP H  1 6   ? 33.685  3.881   22.965 1.00 88.43  ? -3  ASP H OD1 1 
ATOM   12207 O  OD2 . ASP H  1 6   ? 35.385  2.577   22.468 1.00 91.29  ? -3  ASP H OD2 1 
ATOM   12208 N  N   . ASP H  1 7   ? 36.323  7.394   24.121 1.00 94.67  ? -2  ASP H N   1 
ATOM   12209 C  CA  . ASP H  1 7   ? 36.749  8.017   25.371 1.00 95.11  ? -2  ASP H CA  1 
ATOM   12210 C  C   . ASP H  1 7   ? 35.667  8.912   25.988 1.00 92.11  ? -2  ASP H C   1 
ATOM   12211 O  O   . ASP H  1 7   ? 35.493  8.941   27.211 1.00 84.69  ? -2  ASP H O   1 
ATOM   12212 C  CB  . ASP H  1 7   ? 38.016  8.835   25.110 1.00 98.32  ? -2  ASP H CB  1 
ATOM   12213 C  CG  . ASP H  1 7   ? 39.106  8.573   26.128 1.00 98.36  ? -2  ASP H CG  1 
ATOM   12214 O  OD1 . ASP H  1 7   ? 39.925  9.488   26.371 1.00 98.63  ? -2  ASP H OD1 1 
ATOM   12215 O  OD2 . ASP H  1 7   ? 39.149  7.454   26.680 1.00 96.73  ? -2  ASP H OD2 1 
ATOM   12216 N  N   . LYS H  1 8   ? 34.940  9.626   25.129 1.00 91.53  ? -1  LYS H N   1 
ATOM   12217 C  CA  . LYS H  1 8   ? 33.899  10.572  25.545 1.00 87.23  ? -1  LYS H CA  1 
ATOM   12218 C  C   . LYS H  1 8   ? 32.649  9.861   26.042 1.00 87.67  ? -1  LYS H C   1 
ATOM   12219 O  O   . LYS H  1 8   ? 32.238  10.047  27.186 1.00 87.92  ? -1  LYS H O   1 
ATOM   12220 C  CB  . LYS H  1 8   ? 33.502  11.508  24.404 1.00 81.34  ? -1  LYS H CB  1 
ATOM   12221 C  CG  . LYS H  1 8   ? 34.548  12.514  23.991 1.00 86.28  ? -1  LYS H CG  1 
ATOM   12222 C  CD  . LYS H  1 8   ? 33.902  13.593  23.135 1.00 91.38  ? -1  LYS H CD  1 
ATOM   12223 C  CE  . LYS H  1 8   ? 34.882  14.690  22.750 1.00 90.65  ? -1  LYS H CE  1 
ATOM   12224 N  NZ  . LYS H  1 8   ? 34.185  15.834  22.108 1.00 81.30  ? -1  LYS H NZ  1 
ATOM   12225 N  N   . LEU H  1 9   ? 32.018  9.087   25.165 1.00 83.50  ? 0   LEU H N   1 
ATOM   12226 C  CA  . LEU H  1 9   ? 30.765  8.417   25.502 1.00 85.12  ? 0   LEU H CA  1 
ATOM   12227 C  C   . LEU H  1 9   ? 30.896  7.454   26.688 1.00 82.26  ? 0   LEU H C   1 
ATOM   12228 O  O   . LEU H  1 9   ? 29.893  7.019   27.252 1.00 80.17  ? 0   LEU H O   1 
ATOM   12229 C  CB  . LEU H  1 9   ? 30.163  7.721   24.278 1.00 81.55  ? 0   LEU H CB  1 
ATOM   12230 C  CG  . LEU H  1 9   ? 30.774  6.401   23.837 1.00 91.78  ? 0   LEU H CG  1 
ATOM   12231 C  CD1 . LEU H  1 9   ? 29.976  5.243   24.439 1.00 85.46  ? 0   LEU H CD1 1 
ATOM   12232 C  CD2 . LEU H  1 9   ? 30.792  6.336   22.317 1.00 89.46  ? 0   LEU H CD2 1 
ATOM   12233 N  N   . HIS H  1 10  ? 32.129  7.135   27.068 1.00 81.39  ? 1   HIS H N   1 
ATOM   12234 C  CA  . HIS H  1 10  ? 32.380  6.449   28.331 1.00 77.61  ? 1   HIS H CA  1 
ATOM   12235 C  C   . HIS H  1 10  ? 32.166  7.362   29.529 1.00 80.56  ? 1   HIS H C   1 
ATOM   12236 O  O   . HIS H  1 10  ? 31.560  6.971   30.527 1.00 76.17  ? 1   HIS H O   1 
ATOM   12237 C  CB  . HIS H  1 10  ? 33.802  5.919   28.371 1.00 78.90  ? 1   HIS H CB  1 
ATOM   12238 C  CG  . HIS H  1 10  ? 33.939  4.549   27.800 1.00 79.18  ? 1   HIS H CG  1 
ATOM   12239 N  ND1 . HIS H  1 10  ? 33.209  3.477   28.263 1.00 73.71  ? 1   HIS H ND1 1 
ATOM   12240 C  CD2 . HIS H  1 10  ? 34.714  4.076   26.801 1.00 84.12  ? 1   HIS H CD2 1 
ATOM   12241 C  CE1 . HIS H  1 10  ? 33.526  2.402   27.571 1.00 79.30  ? 1   HIS H CE1 1 
ATOM   12242 N  NE2 . HIS H  1 10  ? 34.438  2.738   26.680 1.00 81.98  ? 1   HIS H NE2 1 
ATOM   12243 N  N   . SER H  1 11  ? 32.687  8.578   29.430 1.00 82.60  ? 2   SER H N   1 
ATOM   12244 C  CA  . SER H  1 11  ? 32.503  9.561   30.479 1.00 79.68  ? 2   SER H CA  1 
ATOM   12245 C  C   . SER H  1 11  ? 31.049  10.017  30.560 1.00 79.33  ? 2   SER H C   1 
ATOM   12246 O  O   . SER H  1 11  ? 30.611  10.474  31.613 1.00 86.11  ? 2   SER H O   1 
ATOM   12247 C  CB  . SER H  1 11  ? 33.416  10.762  30.254 1.00 86.73  ? 2   SER H CB  1 
ATOM   12248 O  OG  . SER H  1 11  ? 33.022  11.475  29.099 1.00 91.84  ? 2   SER H OG  1 
ATOM   12249 N  N   . GLN H  1 12  ? 30.310  9.933   29.454 1.00 73.68  ? 3   GLN H N   1 
ATOM   12250 C  CA  . GLN H  1 12  ? 28.869  10.173  29.507 1.00 72.36  ? 3   GLN H CA  1 
ATOM   12251 C  C   . GLN H  1 12  ? 28.175  9.007   30.215 1.00 73.12  ? 3   GLN H C   1 
ATOM   12252 O  O   . GLN H  1 12  ? 27.426  9.201   31.171 1.00 73.70  ? 3   GLN H O   1 
ATOM   12253 C  CB  . GLN H  1 12  ? 28.272  10.368  28.112 1.00 72.68  ? 3   GLN H CB  1 
ATOM   12254 C  CG  . GLN H  1 12  ? 28.738  11.612  27.359 1.00 83.36  ? 3   GLN H CG  1 
ATOM   12255 C  CD  . GLN H  1 12  ? 27.914  11.864  26.085 1.00 95.64  ? 3   GLN H CD  1 
ATOM   12256 O  OE1 . GLN H  1 12  ? 26.936  11.158  25.823 1.00 89.26  ? 3   GLN H OE1 1 
ATOM   12257 N  NE2 . GLN H  1 12  ? 28.302  12.876  25.299 1.00 87.89  ? 3   GLN H NE2 1 
ATOM   12258 N  N   . ALA H  1 13  ? 28.439  7.792   29.747 1.00 75.71  ? 4   ALA H N   1 
ATOM   12259 C  CA  . ALA H  1 13  ? 27.877  6.596   30.368 1.00 75.63  ? 4   ALA H CA  1 
ATOM   12260 C  C   . ALA H  1 13  ? 28.195  6.559   31.860 1.00 71.65  ? 4   ALA H C   1 
ATOM   12261 O  O   . ALA H  1 13  ? 27.308  6.348   32.689 1.00 70.93  ? 4   ALA H O   1 
ATOM   12262 C  CB  . ALA H  1 13  ? 28.399  5.338   29.677 1.00 64.53  ? 4   ALA H CB  1 
ATOM   12263 N  N   . ASN H  1 14  ? 29.466  6.764   32.187 1.00 68.15  ? 5   ASN H N   1 
ATOM   12264 C  CA  . ASN H  1 14  ? 29.918  6.778   33.571 1.00 72.22  ? 5   ASN H CA  1 
ATOM   12265 C  C   . ASN H  1 14  ? 29.114  7.714   34.463 1.00 69.24  ? 5   ASN H C   1 
ATOM   12266 O  O   . ASN H  1 14  ? 28.773  7.365   35.592 1.00 66.70  ? 5   ASN H O   1 
ATOM   12267 C  CB  . ASN H  1 14  ? 31.395  7.145   33.643 1.00 75.83  ? 5   ASN H CB  1 
ATOM   12268 C  CG  . ASN H  1 14  ? 32.291  5.999   33.273 1.00 71.46  ? 5   ASN H CG  1 
ATOM   12269 O  OD1 . ASN H  1 14  ? 31.969  4.842   33.531 1.00 68.08  ? 5   ASN H OD1 1 
ATOM   12270 N  ND2 . ASN H  1 14  ? 33.426  6.307   32.665 1.00 75.98  ? 5   ASN H ND2 1 
ATOM   12271 N  N   . LEU H  1 15  ? 28.815  8.902   33.955 1.00 68.68  ? 6   LEU H N   1 
ATOM   12272 C  CA  . LEU H  1 15  ? 28.074  9.881   34.732 1.00 67.18  ? 6   LEU H CA  1 
ATOM   12273 C  C   . LEU H  1 15  ? 26.643  9.436   34.951 1.00 64.83  ? 6   LEU H C   1 
ATOM   12274 O  O   . LEU H  1 15  ? 26.139  9.495   36.064 1.00 61.73  ? 6   LEU H O   1 
ATOM   12275 C  CB  . LEU H  1 15  ? 28.093  11.247  34.061 1.00 66.70  ? 6   LEU H CB  1 
ATOM   12276 C  CG  . LEU H  1 15  ? 27.617  12.359  34.996 1.00 67.26  ? 6   LEU H CG  1 
ATOM   12277 C  CD1 . LEU H  1 15  ? 28.362  12.305  36.336 1.00 55.14  ? 6   LEU H CD1 1 
ATOM   12278 C  CD2 . LEU H  1 15  ? 27.765  13.722  34.318 1.00 73.32  ? 6   LEU H CD2 1 
ATOM   12279 N  N   . MET H  1 16  ? 25.982  8.997   33.888 1.00 64.65  ? 7   MET H N   1 
ATOM   12280 C  CA  . MET H  1 16  ? 24.616  8.524   34.023 1.00 62.39  ? 7   MET H CA  1 
ATOM   12281 C  C   . MET H  1 16  ? 24.599  7.368   35.004 1.00 62.53  ? 7   MET H C   1 
ATOM   12282 O  O   . MET H  1 16  ? 23.664  7.222   35.787 1.00 67.84  ? 7   MET H O   1 
ATOM   12283 C  CB  . MET H  1 16  ? 24.047  8.109   32.671 1.00 65.29  ? 7   MET H CB  1 
ATOM   12284 C  CG  . MET H  1 16  ? 23.662  9.276   31.757 1.00 74.63  ? 7   MET H CG  1 
ATOM   12285 S  SD  . MET H  1 16  ? 23.603  8.767   30.017 1.00 97.95  ? 7   MET H SD  1 
ATOM   12286 C  CE  . MET H  1 16  ? 22.941  10.212  29.188 1.00 98.95  ? 7   MET H CE  1 
ATOM   12287 N  N   . ARG H  1 17  ? 25.660  6.568   34.978 1.00 62.90  ? 8   ARG H N   1 
ATOM   12288 C  CA  . ARG H  1 17  ? 25.771  5.395   35.836 1.00 67.20  ? 8   ARG H CA  1 
ATOM   12289 C  C   . ARG H  1 17  ? 25.946  5.786   37.296 1.00 65.11  ? 8   ARG H C   1 
ATOM   12290 O  O   . ARG H  1 17  ? 25.440  5.112   38.189 1.00 70.41  ? 8   ARG H O   1 
ATOM   12291 C  CB  . ARG H  1 17  ? 26.928  4.504   35.371 1.00 72.82  ? 8   ARG H CB  1 
ATOM   12292 C  CG  . ARG H  1 17  ? 27.001  3.132   36.038 1.00 61.27  ? 8   ARG H CG  1 
ATOM   12293 C  CD  . ARG H  1 17  ? 27.990  2.225   35.309 1.00 60.96  ? 8   ARG H CD  1 
ATOM   12294 N  NE  . ARG H  1 17  ? 29.346  2.764   35.273 1.00 63.51  ? 8   ARG H NE  1 
ATOM   12295 C  CZ  . ARG H  1 17  ? 30.234  2.659   36.263 1.00 70.87  ? 8   ARG H CZ  1 
ATOM   12296 N  NH1 . ARG H  1 17  ? 29.933  2.027   37.400 1.00 62.40  ? 8   ARG H NH1 1 
ATOM   12297 N  NH2 . ARG H  1 17  ? 31.438  3.197   36.115 1.00 71.03  ? 8   ARG H NH2 1 
ATOM   12298 N  N   . LEU H  1 18  ? 26.652  6.884   37.528 1.00 68.70  ? 9   LEU H N   1 
ATOM   12299 C  CA  . LEU H  1 18  ? 26.846  7.440   38.865 1.00 66.59  ? 9   LEU H CA  1 
ATOM   12300 C  C   . LEU H  1 18  ? 25.630  8.083   39.490 1.00 64.77  ? 9   LEU H C   1 
ATOM   12301 O  O   . LEU H  1 18  ? 25.253  7.777   40.590 1.00 62.53  ? 9   LEU H O   1 
ATOM   12302 C  CB  . LEU H  1 18  ? 27.892  8.518   38.775 1.00 61.49  ? 9   LEU H CB  1 
ATOM   12303 C  CG  . LEU H  1 18  ? 28.155  9.238   40.058 1.00 57.44  ? 9   LEU H CG  1 
ATOM   12304 C  CD1 . LEU H  1 18  ? 28.672  8.252   40.984 1.00 57.41  ? 9   LEU H CD1 1 
ATOM   12305 C  CD2 . LEU H  1 18  ? 29.133  10.279  39.792 1.00 58.21  ? 9   LEU H CD2 1 
ATOM   12306 N  N   . LYS H  1 19  ? 24.986  8.965   38.755 1.00 64.09  ? 10  LYS H N   1 
ATOM   12307 C  CA  . LYS H  1 19  ? 23.765  9.592   39.243 1.00 66.80  ? 10  LYS H CA  1 
ATOM   12308 C  C   . LYS H  1 19  ? 22.670  8.568   39.529 1.00 73.39  ? 10  LYS H C   1 
ATOM   12309 O  O   . LYS H  1 19  ? 21.949  8.685   40.516 1.00 69.93  ? 10  LYS H O   1 
ATOM   12310 C  CB  . LYS H  1 19  ? 23.293  10.675  38.269 1.00 57.79  ? 10  LYS H CB  1 
ATOM   12311 C  CG  . LYS H  1 19  ? 24.328  11.763  38.094 1.00 58.06  ? 10  LYS H CG  1 
ATOM   12312 C  CD  . LYS H  1 19  ? 23.993  12.707  36.985 1.00 56.67  ? 10  LYS H CD  1 
ATOM   12313 C  CE  . LYS H  1 19  ? 23.092  13.817  37.462 1.00 63.92  ? 10  LYS H CE  1 
ATOM   12314 N  NZ  . LYS H  1 19  ? 22.977  14.905  36.437 1.00 76.92  ? 10  LYS H NZ  1 
ATOM   12315 N  N   . SER H  1 20  ? 22.564  7.553   38.676 1.00 77.09  ? 11  SER H N   1 
ATOM   12316 C  CA  . SER H  1 20  ? 21.616  6.464   38.900 1.00 80.00  ? 11  SER H CA  1 
ATOM   12317 C  C   . SER H  1 20  ? 21.933  5.702   40.185 1.00 75.02  ? 11  SER H C   1 
ATOM   12318 O  O   . SER H  1 20  ? 21.034  5.386   40.955 1.00 81.04  ? 11  SER H O   1 
ATOM   12319 C  CB  . SER H  1 20  ? 21.623  5.490   37.735 1.00 73.91  ? 11  SER H CB  1 
ATOM   12320 O  OG  . SER H  1 20  ? 22.444  4.384   38.061 1.00 88.58  ? 11  SER H OG  1 
ATOM   12321 N  N   . ASP H  1 21  ? 23.206  5.402   40.414 1.00 69.67  ? 12  ASP H N   1 
ATOM   12322 C  CA  . ASP H  1 21  ? 23.613  4.718   41.640 1.00 74.18  ? 12  ASP H CA  1 
ATOM   12323 C  C   . ASP H  1 21  ? 23.246  5.486   42.900 1.00 71.41  ? 12  ASP H C   1 
ATOM   12324 O  O   . ASP H  1 21  ? 22.878  4.897   43.909 1.00 78.28  ? 12  ASP H O   1 
ATOM   12325 C  CB  . ASP H  1 21  ? 25.111  4.438   41.639 1.00 68.97  ? 12  ASP H CB  1 
ATOM   12326 C  CG  . ASP H  1 21  ? 25.459  3.143   40.951 1.00 74.21  ? 12  ASP H CG  1 
ATOM   12327 O  OD1 . ASP H  1 21  ? 26.444  3.096   40.185 1.00 71.96  ? 12  ASP H OD1 1 
ATOM   12328 O  OD2 . ASP H  1 21  ? 24.728  2.166   41.169 1.00 91.11  ? 12  ASP H OD2 1 
ATOM   12329 N  N   . LEU H  1 22  ? 23.352  6.789   42.833 1.00 72.74  ? 13  LEU H N   1 
ATOM   12330 C  CA  . LEU H  1 22  ? 23.009  7.584   43.971 1.00 70.35  ? 13  LEU H CA  1 
ATOM   12331 C  C   . LEU H  1 22  ? 21.549  7.940   44.087 1.00 80.87  ? 13  LEU H C   1 
ATOM   12332 O  O   . LEU H  1 22  ? 21.016  7.908   45.165 1.00 80.54  ? 13  LEU H O   1 
ATOM   12333 C  CB  . LEU H  1 22  ? 23.801  8.867   43.943 1.00 71.00  ? 13  LEU H CB  1 
ATOM   12334 C  CG  . LEU H  1 22  ? 25.273  8.790   43.605 1.00 71.62  ? 13  LEU H CG  1 
ATOM   12335 C  CD1 . LEU H  1 22  ? 25.656  10.113  43.074 1.00 63.76  ? 13  LEU H CD1 1 
ATOM   12336 C  CD2 . LEU H  1 22  ? 26.093  8.482   44.809 1.00 60.00  ? 13  LEU H CD2 1 
ATOM   12337 N  N   . PHE H  1 23  ? 20.897  8.292   42.986 1.00 82.30  ? 14  PHE H N   1 
ATOM   12338 C  CA  . PHE H  1 23  ? 19.496  8.701   43.066 1.00 81.73  ? 14  PHE H CA  1 
ATOM   12339 C  C   . PHE H  1 23  ? 18.376  7.752   42.771 1.00 84.73  ? 14  PHE H C   1 
ATOM   12340 O  O   . PHE H  1 23  ? 17.510  7.541   43.592 1.00 93.49  ? 14  PHE H O   1 
ATOM   12341 C  CB  . PHE H  1 23  ? 19.243  9.841   42.090 1.00 81.70  ? 14  PHE H CB  1 
ATOM   12342 C  CG  . PHE H  1 23  ? 20.173  10.986  42.222 1.00 81.00  ? 14  PHE H CG  1 
ATOM   12343 C  CD1 . PHE H  1 23  ? 20.775  11.273  43.410 1.00 76.43  ? 14  PHE H CD1 1 
ATOM   12344 C  CD2 . PHE H  1 23  ? 20.404  11.805  41.157 1.00 72.66  ? 14  PHE H CD2 1 
ATOM   12345 C  CE1 . PHE H  1 23  ? 21.602  12.319  43.511 1.00 70.05  ? 14  PHE H CE1 1 
ATOM   12346 C  CE2 . PHE H  1 23  ? 21.236  12.852  41.269 1.00 76.24  ? 14  PHE H CE2 1 
ATOM   12347 C  CZ  . PHE H  1 23  ? 21.836  13.108  42.440 1.00 70.66  ? 14  PHE H CZ  1 
ATOM   12348 N  N   . ASN H  1 24  ? 18.357  7.217   41.570 1.00 92.49  ? 15  ASN H N   1 
ATOM   12349 C  CA  . ASN H  1 24  ? 17.309  6.295   41.185 1.00 102.41 ? 15  ASN H CA  1 
ATOM   12350 C  C   . ASN H  1 24  ? 17.371  4.941   41.896 1.00 104.15 ? 15  ASN H C   1 
ATOM   12351 O  O   . ASN H  1 24  ? 16.362  4.422   42.351 1.00 105.67 ? 15  ASN H O   1 
ATOM   12352 C  CB  . ASN H  1 24  ? 17.297  6.156   39.671 1.00 98.87  ? 15  ASN H CB  1 
ATOM   12353 C  CG  . ASN H  1 24  ? 17.397  7.493   38.974 1.00 100.36 ? 15  ASN H CG  1 
ATOM   12354 O  OD1 . ASN H  1 24  ? 18.428  7.838   38.421 1.00 95.01  ? 15  ASN H OD1 1 
ATOM   12355 N  ND2 . ASN H  1 24  ? 16.326  8.253   39.002 1.00 102.16 ? 15  ASN H ND2 1 
ATOM   12356 N  N   . ARG H  1 25  ? 18.573  4.392   41.993 1.00 96.09  ? 16  ARG H N   1 
ATOM   12357 C  CA  . ARG H  1 25  ? 18.836  3.110   42.652 1.00 95.75  ? 16  ARG H CA  1 
ATOM   12358 C  C   . ARG H  1 25  ? 18.801  3.172   44.183 1.00 95.58  ? 16  ARG H C   1 
ATOM   12359 O  O   . ARG H  1 25  ? 18.503  2.175   44.834 1.00 90.51  ? 16  ARG H O   1 
ATOM   12360 C  CB  . ARG H  1 25  ? 20.194  2.548   42.230 1.00 98.06  ? 16  ARG H CB  1 
ATOM   12361 C  CG  . ARG H  1 25  ? 20.404  2.347   40.731 1.00 95.23  ? 16  ARG H CG  1 
ATOM   12362 C  CD  . ARG H  1 25  ? 21.886  2.142   40.462 1.00 89.58  ? 16  ARG H CD  1 
ATOM   12363 N  NE  . ARG H  1 25  ? 22.379  1.055   41.289 1.00 96.18  ? 16  ARG H NE  1 
ATOM   12364 C  CZ  . ARG H  1 25  ? 21.715  -0.078  41.438 1.00 102.43 ? 16  ARG H CZ  1 
ATOM   12365 N  NH1 . ARG H  1 25  ? 20.570  -0.229  40.792 1.00 107.18 ? 16  ARG H NH1 1 
ATOM   12366 N  NH2 . ARG H  1 25  ? 22.181  -1.043  42.215 1.00 95.62  ? 16  ARG H NH2 1 
ATOM   12367 N  N   . SER H  1 26  ? 19.088  4.347   44.737 1.00 93.88  ? 17  SER H N   1 
ATOM   12368 C  CA  . SER H  1 26  ? 19.153  4.533   46.185 1.00 105.55 ? 17  SER H CA  1 
ATOM   12369 C  C   . SER H  1 26  ? 18.086  5.490   46.715 1.00 104.48 ? 17  SER H C   1 
ATOM   12370 O  O   . SER H  1 26  ? 17.793  6.515   46.100 1.00 101.64 ? 17  SER H O   1 
ATOM   12371 C  CB  . SER H  1 26  ? 20.544  5.020   46.598 1.00 104.01 ? 17  SER H CB  1 
ATOM   12372 O  OG  . SER H  1 26  ? 21.541  4.081   46.235 1.00 91.74  ? 17  SER H OG  1 
ATOM   12373 N  N   . PRO H  1 27  ? 17.509  5.140   47.862 1.00 109.34 ? 18  PRO H N   1 
ATOM   12374 C  CA  . PRO H  1 27  ? 16.452  5.943   48.488 1.00 100.80 ? 18  PRO H CA  1 
ATOM   12375 C  C   . PRO H  1 27  ? 16.935  7.330   48.909 1.00 94.57  ? 18  PRO H C   1 
ATOM   12376 O  O   . PRO H  1 27  ? 18.076  7.490   49.342 1.00 92.08  ? 18  PRO H O   1 
ATOM   12377 C  CB  . PRO H  1 27  ? 16.081  5.120   49.723 1.00 96.76  ? 18  PRO H CB  1 
ATOM   12378 C  CG  . PRO H  1 27  ? 17.324  4.377   50.059 1.00 106.05 ? 18  PRO H CG  1 
ATOM   12379 C  CD  . PRO H  1 27  ? 17.985  4.063   48.747 1.00 103.40 ? 18  PRO H CD  1 
ATOM   12380 N  N   . MET H  1 28  ? 16.061  8.313   48.790 1.00 96.24  ? 19  MET H N   1 
ATOM   12381 C  CA  . MET H  1 28  ? 16.414  9.686   49.107 1.00 101.01 ? 19  MET H CA  1 
ATOM   12382 C  C   . MET H  1 28  ? 16.670  10.010  50.568 1.00 94.98  ? 19  MET H C   1 
ATOM   12383 O  O   . MET H  1 28  ? 16.005  9.518   51.457 1.00 87.32  ? 19  MET H O   1 
ATOM   12384 C  CB  . MET H  1 28  ? 15.343  10.619  48.597 1.00 104.83 ? 19  MET H CB  1 
ATOM   12385 C  CG  . MET H  1 28  ? 14.786  10.228  47.279 1.00 109.79 ? 19  MET H CG  1 
ATOM   12386 S  SD  . MET H  1 28  ? 13.686  11.559  46.876 1.00 149.52 ? 19  MET H SD  1 
ATOM   12387 C  CE  . MET H  1 28  ? 13.023  11.883  48.511 1.00 95.82  ? 19  MET H CE  1 
ATOM   12388 N  N   . TYR H  1 29  ? 17.628  10.890  50.781 1.00 85.86  ? 20  TYR H N   1 
ATOM   12389 C  CA  . TYR H  1 29  ? 18.027  11.326  52.110 1.00 68.70  ? 20  TYR H CA  1 
ATOM   12390 C  C   . TYR H  1 29  ? 16.855  11.970  52.839 1.00 71.04  ? 20  TYR H C   1 
ATOM   12391 O  O   . TYR H  1 29  ? 16.278  12.953  52.367 1.00 69.17  ? 20  TYR H O   1 
ATOM   12392 C  CB  . TYR H  1 29  ? 19.173  12.322  51.980 1.00 63.70  ? 20  TYR H CB  1 
ATOM   12393 C  CG  . TYR H  1 29  ? 19.800  12.765  53.277 1.00 65.09  ? 20  TYR H CG  1 
ATOM   12394 C  CD1 . TYR H  1 29  ? 19.752  14.097  53.676 1.00 65.15  ? 20  TYR H CD1 1 
ATOM   12395 C  CD2 . TYR H  1 29  ? 20.460  11.861  54.096 1.00 68.57  ? 20  TYR H CD2 1 
ATOM   12396 C  CE1 . TYR H  1 29  ? 20.338  14.518  54.864 1.00 64.80  ? 20  TYR H CE1 1 
ATOM   12397 C  CE2 . TYR H  1 29  ? 21.048  12.272  55.285 1.00 67.43  ? 20  TYR H CE2 1 
ATOM   12398 C  CZ  . TYR H  1 29  ? 20.982  13.610  55.659 1.00 63.31  ? 20  TYR H CZ  1 
ATOM   12399 O  OH  . TYR H  1 29  ? 21.552  14.064  56.825 1.00 67.50  ? 20  TYR H OH  1 
ATOM   12400 N  N   . PRO H  1 30  ? 16.545  11.386  53.973 1.00 72.21  ? 21  PRO H N   1 
ATOM   12401 C  CA  . PRO H  1 30  ? 15.450  11.787  54.833 1.00 64.45  ? 21  PRO H CA  1 
ATOM   12402 C  C   . PRO H  1 30  ? 15.667  13.071  55.585 1.00 62.91  ? 21  PRO H C   1 
ATOM   12403 O  O   . PRO H  1 30  ? 14.714  13.566  56.127 1.00 66.66  ? 21  PRO H O   1 
ATOM   12404 C  CB  . PRO H  1 30  ? 15.358  10.626  55.799 1.00 61.58  ? 21  PRO H CB  1 
ATOM   12405 C  CG  . PRO H  1 30  ? 16.712  10.116  55.886 1.00 63.20  ? 21  PRO H CG  1 
ATOM   12406 C  CD  . PRO H  1 30  ? 17.441  10.448  54.649 1.00 73.50  ? 21  PRO H CD  1 
ATOM   12407 N  N   . GLY H  1 31  ? 16.876  13.590  55.637 1.00 55.95  ? 22  GLY H N   1 
ATOM   12408 C  CA  . GLY H  1 31  ? 17.129  14.803  56.363 1.00 58.74  ? 22  GLY H CA  1 
ATOM   12409 C  C   . GLY H  1 31  ? 17.771  14.386  57.637 1.00 60.88  ? 22  GLY H C   1 
ATOM   12410 O  O   . GLY H  1 31  ? 17.610  13.277  58.047 1.00 71.71  ? 22  GLY H O   1 
ATOM   12411 N  N   . PRO H  1 32  ? 18.498  15.286  58.263 1.00 65.39  ? 23  PRO H N   1 
ATOM   12412 C  CA  . PRO H  1 32  ? 19.242  15.011  59.479 1.00 62.02  ? 23  PRO H CA  1 
ATOM   12413 C  C   . PRO H  1 32  ? 18.428  14.778  60.697 1.00 54.92  ? 23  PRO H C   1 
ATOM   12414 O  O   . PRO H  1 32  ? 17.316  15.190  60.793 1.00 54.76  ? 23  PRO H O   1 
ATOM   12415 C  CB  . PRO H  1 32  ? 20.030  16.283  59.662 1.00 58.38  ? 23  PRO H CB  1 
ATOM   12416 C  CG  . PRO H  1 32  ? 19.222  17.282  59.077 1.00 62.34  ? 23  PRO H CG  1 
ATOM   12417 C  CD  . PRO H  1 32  ? 18.608  16.691  57.890 1.00 65.65  ? 23  PRO H CD  1 
ATOM   12418 N  N   . THR H  1 33  ? 19.013  14.083  61.640 1.00 58.06  ? 24  THR H N   1 
ATOM   12419 C  CA  . THR H  1 33  ? 18.344  13.795  62.891 1.00 64.39  ? 24  THR H CA  1 
ATOM   12420 C  C   . THR H  1 33  ? 19.304  14.023  64.049 1.00 63.76  ? 24  THR H C   1 
ATOM   12421 O  O   . THR H  1 33  ? 20.496  14.240  63.839 1.00 64.39  ? 24  THR H O   1 
ATOM   12422 C  CB  . THR H  1 33  ? 17.827  12.364  62.917 1.00 71.09  ? 24  THR H CB  1 
ATOM   12423 O  OG1 . THR H  1 33  ? 18.915  11.462  62.663 1.00 73.41  ? 24  THR H OG1 1 
ATOM   12424 C  CG2 . THR H  1 33  ? 16.749  12.184  61.850 1.00 56.95  ? 24  THR H CG2 1 
ATOM   12425 N  N   . LYS H  1 34  ? 18.772  14.024  65.265 1.00 67.17  ? 25  LYS H N   1 
ATOM   12426 C  CA  . LYS H  1 34  ? 19.606  14.113  66.458 1.00 67.90  ? 25  LYS H CA  1 
ATOM   12427 C  C   . LYS H  1 34  ? 20.716  13.045  66.433 1.00 71.59  ? 25  LYS H C   1 
ATOM   12428 O  O   . LYS H  1 34  ? 21.812  13.280  66.937 1.00 71.24  ? 25  LYS H O   1 
ATOM   12429 C  CB  . LYS H  1 34  ? 18.747  14.011  67.731 1.00 65.26  ? 25  LYS H CB  1 
ATOM   12430 C  CG  . LYS H  1 34  ? 17.873  12.745  67.825 1.00 79.68  ? 25  LYS H CG  1 
ATOM   12431 C  CD  . LYS H  1 34  ? 16.638  12.952  68.718 1.00 82.61  ? 25  LYS H CD  1 
ATOM   12432 C  CE  . LYS H  1 34  ? 15.666  11.765  68.651 1.00 82.03  ? 25  LYS H CE  1 
ATOM   12433 N  NZ  . LYS H  1 34  ? 16.207  10.540  69.310 1.00 74.05  ? 25  LYS H NZ  1 
ATOM   12434 N  N   . ASP H  1 35  ? 20.427  11.883  65.843 1.00 67.09  ? 26  ASP H N   1 
ATOM   12435 C  CA  . ASP H  1 35  ? 21.388  10.777  65.766 1.00 70.77  ? 26  ASP H CA  1 
ATOM   12436 C  C   . ASP H  1 35  ? 22.292  10.843  64.547 1.00 67.26  ? 26  ASP H C   1 
ATOM   12437 O  O   . ASP H  1 35  ? 23.268  10.092  64.432 1.00 61.99  ? 26  ASP H O   1 
ATOM   12438 C  CB  . ASP H  1 35  ? 20.658  9.432   65.765 1.00 75.02  ? 26  ASP H CB  1 
ATOM   12439 C  CG  . ASP H  1 35  ? 20.009  9.126   67.091 1.00 82.64  ? 26  ASP H CG  1 
ATOM   12440 O  OD1 . ASP H  1 35  ? 18.764  9.026   67.133 1.00 81.19  ? 26  ASP H OD1 1 
ATOM   12441 O  OD2 . ASP H  1 35  ? 20.746  8.988   68.092 1.00 80.11  ? 26  ASP H OD2 1 
ATOM   12442 N  N   . ASP H  1 36  ? 21.931  11.717  63.618 1.00 66.30  ? 27  ASP H N   1 
ATOM   12443 C  CA  . ASP H  1 36  ? 22.680  11.889  62.380 1.00 67.80  ? 27  ASP H CA  1 
ATOM   12444 C  C   . ASP H  1 36  ? 22.659  13.379  62.043 1.00 63.49  ? 27  ASP H C   1 
ATOM   12445 O  O   . ASP H  1 36  ? 22.059  13.788  61.057 1.00 65.65  ? 27  ASP H O   1 
ATOM   12446 C  CB  . ASP H  1 36  ? 22.030  11.030  61.275 1.00 67.58  ? 27  ASP H CB  1 
ATOM   12447 C  CG  . ASP H  1 36  ? 22.815  11.022  59.968 1.00 70.65  ? 27  ASP H CG  1 
ATOM   12448 O  OD1 . ASP H  1 36  ? 24.056  10.898  59.993 1.00 71.68  ? 27  ASP H OD1 1 
ATOM   12449 O  OD2 . ASP H  1 36  ? 22.168  11.126  58.905 1.00 70.69  ? 27  ASP H OD2 1 
ATOM   12450 N  N   . PRO H  1 37  ? 23.305  14.200  62.877 1.00 59.90  ? 28  PRO H N   1 
ATOM   12451 C  CA  . PRO H  1 37  ? 23.253  15.655  62.744 1.00 58.41  ? 28  PRO H CA  1 
ATOM   12452 C  C   . PRO H  1 37  ? 24.141  16.125  61.615 1.00 56.45  ? 28  PRO H C   1 
ATOM   12453 O  O   . PRO H  1 37  ? 25.128  15.468  61.281 1.00 50.88  ? 28  PRO H O   1 
ATOM   12454 C  CB  . PRO H  1 37  ? 23.814  16.159  64.074 1.00 57.75  ? 28  PRO H CB  1 
ATOM   12455 C  CG  . PRO H  1 37  ? 24.281  14.941  64.817 1.00 60.70  ? 28  PRO H CG  1 
ATOM   12456 C  CD  . PRO H  1 37  ? 24.300  13.792  63.870 1.00 64.23  ? 28  PRO H CD  1 
ATOM   12457 N  N   . LEU H  1 38  ? 23.783  17.270  61.049 1.00 54.24  ? 29  LEU H N   1 
ATOM   12458 C  CA  . LEU H  1 38  ? 24.448  17.802  59.879 1.00 59.14  ? 29  LEU H CA  1 
ATOM   12459 C  C   . LEU H  1 38  ? 25.080  19.154  60.174 1.00 63.18  ? 29  LEU H C   1 
ATOM   12460 O  O   . LEU H  1 38  ? 24.567  19.942  60.969 1.00 60.38  ? 29  LEU H O   1 
ATOM   12461 C  CB  . LEU H  1 38  ? 23.438  17.955  58.733 1.00 60.60  ? 29  LEU H CB  1 
ATOM   12462 C  CG  . LEU H  1 38  ? 24.005  18.408  57.385 1.00 64.09  ? 29  LEU H CG  1 
ATOM   12463 C  CD1 . LEU H  1 38  ? 24.885  17.315  56.792 1.00 65.85  ? 29  LEU H CD1 1 
ATOM   12464 C  CD2 . LEU H  1 38  ? 22.909  18.801  56.417 1.00 54.93  ? 29  LEU H CD2 1 
ATOM   12465 N  N   . THR H  1 39  ? 26.192  19.428  59.514 1.00 64.58  ? 30  THR H N   1 
ATOM   12466 C  CA  . THR H  1 39  ? 26.745  20.767  59.544 1.00 59.57  ? 30  THR H CA  1 
ATOM   12467 C  C   . THR H  1 39  ? 26.622  21.447  58.182 1.00 57.06  ? 30  THR H C   1 
ATOM   12468 O  O   . THR H  1 39  ? 27.021  20.909  57.149 1.00 59.46  ? 30  THR H O   1 
ATOM   12469 C  CB  . THR H  1 39  ? 28.185  20.744  59.977 1.00 54.07  ? 30  THR H CB  1 
ATOM   12470 O  OG1 . THR H  1 39  ? 28.300  19.859  61.091 1.00 52.36  ? 30  THR H OG1 1 
ATOM   12471 C  CG2 . THR H  1 39  ? 28.624  22.129  60.362 1.00 56.48  ? 30  THR H CG2 1 
ATOM   12472 N  N   . VAL H  1 40  ? 26.057  22.640  58.201 1.00 50.64  ? 31  VAL H N   1 
ATOM   12473 C  CA  . VAL H  1 40  ? 25.890  23.416  57.006 1.00 52.22  ? 31  VAL H CA  1 
ATOM   12474 C  C   . VAL H  1 40  ? 26.631  24.724  57.174 1.00 55.10  ? 31  VAL H C   1 
ATOM   12475 O  O   . VAL H  1 40  ? 26.456  25.411  58.171 1.00 53.34  ? 31  VAL H O   1 
ATOM   12476 C  CB  . VAL H  1 40  ? 24.406  23.683  56.771 1.00 55.57  ? 31  VAL H CB  1 
ATOM   12477 C  CG1 . VAL H  1 40  ? 24.196  24.511  55.525 1.00 48.58  ? 31  VAL H CG1 1 
ATOM   12478 C  CG2 . VAL H  1 40  ? 23.671  22.363  56.658 1.00 60.20  ? 31  VAL H CG2 1 
ATOM   12479 N  N   . TYR H  1 41  ? 27.470  25.059  56.200 1.00 54.20  ? 32  TYR H N   1 
ATOM   12480 C  CA  . TYR H  1 41  ? 28.194  26.318  56.222 1.00 52.95  ? 32  TYR H CA  1 
ATOM   12481 C  C   . TYR H  1 41  ? 27.490  27.386  55.410 1.00 55.05  ? 32  TYR H C   1 
ATOM   12482 O  O   . TYR H  1 41  ? 27.202  27.182  54.237 1.00 61.66  ? 32  TYR H O   1 
ATOM   12483 C  CB  . TYR H  1 41  ? 29.604  26.129  55.683 1.00 51.91  ? 32  TYR H CB  1 
ATOM   12484 C  CG  . TYR H  1 41  ? 30.472  25.341  56.615 1.00 64.37  ? 32  TYR H CG  1 
ATOM   12485 C  CD1 . TYR H  1 41  ? 31.226  25.975  57.592 1.00 72.95  ? 32  TYR H CD1 1 
ATOM   12486 C  CD2 . TYR H  1 41  ? 30.521  23.958  56.541 1.00 63.50  ? 32  TYR H CD2 1 
ATOM   12487 C  CE1 . TYR H  1 41  ? 32.014  25.250  58.455 1.00 75.62  ? 32  TYR H CE1 1 
ATOM   12488 C  CE2 . TYR H  1 41  ? 31.297  23.228  57.391 1.00 60.77  ? 32  TYR H CE2 1 
ATOM   12489 C  CZ  . TYR H  1 41  ? 32.047  23.871  58.346 1.00 75.14  ? 32  TYR H CZ  1 
ATOM   12490 O  OH  . TYR H  1 41  ? 32.833  23.126  59.201 1.00 86.55  ? 32  TYR H OH  1 
ATOM   12491 N  N   . LEU H  1 42  ? 27.233  28.533  56.033 1.00 51.26  ? 33  LEU H N   1 
ATOM   12492 C  CA  . LEU H  1 42  ? 26.720  29.694  55.322 1.00 51.40  ? 33  LEU H CA  1 
ATOM   12493 C  C   . LEU H  1 42  ? 27.834  30.692  55.062 1.00 55.91  ? 33  LEU H C   1 
ATOM   12494 O  O   . LEU H  1 42  ? 28.761  30.834  55.866 1.00 60.69  ? 33  LEU H O   1 
ATOM   12495 C  CB  . LEU H  1 42  ? 25.607  30.383  56.100 1.00 52.91  ? 33  LEU H CB  1 
ATOM   12496 C  CG  . LEU H  1 42  ? 24.242  29.731  56.212 1.00 50.96  ? 33  LEU H CG  1 
ATOM   12497 C  CD1 . LEU H  1 42  ? 23.225  30.810  56.474 1.00 49.85  ? 33  LEU H CD1 1 
ATOM   12498 C  CD2 . LEU H  1 42  ? 23.901  28.976  54.957 1.00 50.86  ? 33  LEU H CD2 1 
ATOM   12499 N  N   . SER H  1 43  ? 27.748  31.354  53.915 1.00 53.75  ? 34  SER H N   1 
ATOM   12500 C  CA  . SER H  1 43  ? 28.620  32.469  53.589 1.00 57.99  ? 34  SER H CA  1 
ATOM   12501 C  C   . SER H  1 43  ? 27.900  33.436  52.627 1.00 58.66  ? 34  SER H C   1 
ATOM   12502 O  O   . SER H  1 43  ? 27.112  32.992  51.800 1.00 60.70  ? 34  SER H O   1 
ATOM   12503 C  CB  . SER H  1 43  ? 29.907  31.931  52.977 1.00 60.01  ? 34  SER H CB  1 
ATOM   12504 O  OG  . SER H  1 43  ? 30.918  32.919  53.029 1.00 77.03  ? 34  SER H OG  1 
ATOM   12505 N  N   . PHE H  1 44  ? 28.151  34.742  52.708 1.00 54.70  ? 35  PHE H N   1 
ATOM   12506 C  CA  . PHE H  1 44  ? 27.423  35.666  51.823 1.00 55.87  ? 35  PHE H CA  1 
ATOM   12507 C  C   . PHE H  1 44  ? 28.297  36.562  50.968 1.00 55.72  ? 35  PHE H C   1 
ATOM   12508 O  O   . PHE H  1 44  ? 29.277  37.124  51.439 1.00 67.16  ? 35  PHE H O   1 
ATOM   12509 C  CB  . PHE H  1 44  ? 26.468  36.557  52.603 1.00 50.84  ? 35  PHE H CB  1 
ATOM   12510 C  CG  . PHE H  1 44  ? 25.433  35.814  53.373 1.00 54.40  ? 35  PHE H CG  1 
ATOM   12511 C  CD1 . PHE H  1 44  ? 24.165  35.634  52.858 1.00 51.43  ? 35  PHE H CD1 1 
ATOM   12512 C  CD2 . PHE H  1 44  ? 25.721  35.319  54.636 1.00 63.15  ? 35  PHE H CD2 1 
ATOM   12513 C  CE1 . PHE H  1 44  ? 23.200  34.962  53.583 1.00 57.25  ? 35  PHE H CE1 1 
ATOM   12514 C  CE2 . PHE H  1 44  ? 24.771  34.637  55.373 1.00 58.39  ? 35  PHE H CE2 1 
ATOM   12515 C  CZ  . PHE H  1 44  ? 23.507  34.456  54.849 1.00 60.06  ? 35  PHE H CZ  1 
ATOM   12516 N  N   . SER H  1 45  ? 27.932  36.686  49.702 1.00 51.21  ? 36  SER H N   1 
ATOM   12517 C  CA  . SER H  1 45  ? 28.480  37.733  48.858 1.00 59.24  ? 36  SER H CA  1 
ATOM   12518 C  C   . SER H  1 45  ? 27.396  38.770  48.613 1.00 56.05  ? 36  SER H C   1 
ATOM   12519 O  O   . SER H  1 45  ? 26.328  38.488  48.078 1.00 48.84  ? 36  SER H O   1 
ATOM   12520 C  CB  . SER H  1 45  ? 29.035  37.188  47.542 1.00 61.88  ? 36  SER H CB  1 
ATOM   12521 O  OG  . SER H  1 45  ? 30.451  37.150  47.565 1.00 61.92  ? 36  SER H OG  1 
ATOM   12522 N  N   . LEU H  1 46  ? 27.660  39.982  49.053 1.00 59.04  ? 37  LEU H N   1 
ATOM   12523 C  CA  . LEU H  1 46  ? 26.665  41.003  48.892 1.00 54.27  ? 37  LEU H CA  1 
ATOM   12524 C  C   . LEU H  1 46  ? 26.922  41.714  47.571 1.00 53.71  ? 37  LEU H C   1 
ATOM   12525 O  O   . LEU H  1 46  ? 28.070  42.023  47.243 1.00 52.90  ? 37  LEU H O   1 
ATOM   12526 C  CB  . LEU H  1 46  ? 26.672  41.945  50.078 1.00 56.93  ? 37  LEU H CB  1 
ATOM   12527 C  CG  . LEU H  1 46  ? 25.483  42.887  49.941 1.00 69.07  ? 37  LEU H CG  1 
ATOM   12528 C  CD1 . LEU H  1 46  ? 24.184  42.099  50.013 1.00 69.40  ? 37  LEU H CD1 1 
ATOM   12529 C  CD2 . LEU H  1 46  ? 25.515  43.981  50.991 1.00 69.95  ? 37  LEU H CD2 1 
ATOM   12530 N  N   . LEU H  1 47  ? 25.841  41.930  46.815 1.00 60.13  ? 38  LEU H N   1 
ATOM   12531 C  CA  . LEU H  1 47  ? 25.864  42.380  45.410 1.00 56.96  ? 38  LEU H CA  1 
ATOM   12532 C  C   . LEU H  1 47  ? 25.265  43.706  44.947 1.00 55.43  ? 38  LEU H C   1 
ATOM   12533 O  O   . LEU H  1 47  ? 25.744  44.303  43.975 1.00 60.58  ? 38  LEU H O   1 
ATOM   12534 C  CB  . LEU H  1 47  ? 25.076  41.427  44.498 1.00 54.02  ? 38  LEU H CB  1 
ATOM   12535 C  CG  . LEU H  1 47  ? 25.891  40.381  43.729 1.00 51.28  ? 38  LEU H CG  1 
ATOM   12536 C  CD1 . LEU H  1 47  ? 26.550  39.504  44.721 1.00 62.44  ? 38  LEU H CD1 1 
ATOM   12537 C  CD2 . LEU H  1 47  ? 25.017  39.564  42.819 1.00 57.97  ? 38  LEU H CD2 1 
ATOM   12538 N  N   . ASP H  1 48  ? 24.143  44.077  45.563 1.00 51.09  ? 39  ASP H N   1 
ATOM   12539 C  CA  . ASP H  1 48  ? 23.536  45.399  45.450 1.00 52.36  ? 39  ASP H CA  1 
ATOM   12540 C  C   . ASP H  1 48  ? 22.538  45.583  46.591 1.00 49.96  ? 39  ASP H C   1 
ATOM   12541 O  O   . ASP H  1 48  ? 21.792  44.667  46.915 1.00 55.23  ? 39  ASP H O   1 
ATOM   12542 C  CB  . ASP H  1 48  ? 22.784  45.505  44.100 1.00 54.77  ? 39  ASP H CB  1 
ATOM   12543 C  CG  . ASP H  1 48  ? 22.516  46.950  43.674 1.00 57.70  ? 39  ASP H CG  1 
ATOM   12544 O  OD1 . ASP H  1 48  ? 22.726  47.847  44.517 1.00 58.58  ? 39  ASP H OD1 1 
ATOM   12545 O  OD2 . ASP H  1 48  ? 22.089  47.194  42.514 1.00 52.72  ? 39  ASP H OD2 1 
ATOM   12546 N  N   . ILE H  1 49  ? 22.500  46.763  47.190 1.00 46.12  ? 40  ILE H N   1 
ATOM   12547 C  CA  . ILE H  1 49  ? 21.323  47.154  47.938 1.00 44.33  ? 40  ILE H CA  1 
ATOM   12548 C  C   . ILE H  1 49  ? 20.502  47.924  46.897 1.00 56.55  ? 40  ILE H C   1 
ATOM   12549 O  O   . ILE H  1 49  ? 20.882  49.001  46.432 1.00 53.01  ? 40  ILE H O   1 
ATOM   12550 C  CB  . ILE H  1 49  ? 21.677  48.030  49.166 1.00 44.98  ? 40  ILE H CB  1 
ATOM   12551 C  CG1 . ILE H  1 49  ? 22.547  47.232  50.153 1.00 49.99  ? 40  ILE H CG1 1 
ATOM   12552 C  CG2 . ILE H  1 49  ? 20.417  48.570  49.834 1.00 43.74  ? 40  ILE H CG2 1 
ATOM   12553 C  CD1 . ILE H  1 49  ? 22.862  47.926  51.462 1.00 41.35  ? 40  ILE H CD1 1 
ATOM   12554 N  N   . VAL H  1 50  ? 19.392  47.336  46.489 1.00 58.59  ? 41  VAL H N   1 
ATOM   12555 C  CA  . VAL H  1 50  ? 18.663  47.879  45.373 1.00 53.16  ? 41  VAL H CA  1 
ATOM   12556 C  C   . VAL H  1 50  ? 17.877  49.113  45.761 1.00 58.85  ? 41  VAL H C   1 
ATOM   12557 O  O   . VAL H  1 50  ? 17.955  50.144  45.088 1.00 68.88  ? 41  VAL H O   1 
ATOM   12558 C  CB  . VAL H  1 50  ? 17.687  46.852  44.801 1.00 60.20  ? 41  VAL H CB  1 
ATOM   12559 C  CG1 . VAL H  1 50  ? 16.932  47.472  43.626 1.00 57.23  ? 41  VAL H CG1 1 
ATOM   12560 C  CG2 . VAL H  1 50  ? 18.425  45.557  44.412 1.00 55.60  ? 41  VAL H CG2 1 
ATOM   12561 N  N   . LYS H  1 51  ? 17.111  49.004  46.839 1.00 56.05  ? 42  LYS H N   1 
ATOM   12562 C  CA  . LYS H  1 51  ? 16.182  50.062  47.218 1.00 61.37  ? 42  LYS H CA  1 
ATOM   12563 C  C   . LYS H  1 51  ? 15.951  50.108  48.729 1.00 57.65  ? 42  LYS H C   1 
ATOM   12564 O  O   . LYS H  1 51  ? 15.843  49.060  49.353 1.00 57.63  ? 42  LYS H O   1 
ATOM   12565 C  CB  . LYS H  1 51  ? 14.843  49.832  46.504 1.00 59.04  ? 42  LYS H CB  1 
ATOM   12566 C  CG  . LYS H  1 51  ? 13.655  50.336  47.275 1.00 60.98  ? 42  LYS H CG  1 
ATOM   12567 C  CD  . LYS H  1 51  ? 12.401  49.565  46.933 1.00 60.40  ? 42  LYS H CD  1 
ATOM   12568 C  CE  . LYS H  1 51  ? 11.725  50.143  45.723 1.00 60.85  ? 42  LYS H CE  1 
ATOM   12569 N  NZ  . LYS H  1 51  ? 10.273  49.880  45.787 1.00 64.55  ? 42  LYS H NZ  1 
ATOM   12570 N  N   . ALA H  1 52  ? 15.817  51.304  49.310 1.00 59.92  ? 43  ALA H N   1 
ATOM   12571 C  CA  . ALA H  1 52  ? 15.511  51.420  50.743 1.00 56.40  ? 43  ALA H CA  1 
ATOM   12572 C  C   . ALA H  1 52  ? 14.239  52.230  50.946 1.00 55.56  ? 43  ALA H C   1 
ATOM   12573 O  O   . ALA H  1 52  ? 14.228  53.424  50.690 1.00 60.92  ? 43  ALA H O   1 
ATOM   12574 C  CB  . ALA H  1 52  ? 16.668  52.059  51.483 1.00 54.91  ? 43  ALA H CB  1 
ATOM   12575 N  N   . ASP H  1 53  ? 13.173  51.610  51.433 1.00 53.61  ? 44  ASP H N   1 
ATOM   12576 C  CA  . ASP H  1 53  ? 11.882  52.287  51.457 1.00 51.17  ? 44  ASP H CA  1 
ATOM   12577 C  C   . ASP H  1 53  ? 11.613  52.761  52.863 1.00 55.12  ? 44  ASP H C   1 
ATOM   12578 O  O   . ASP H  1 53  ? 11.268  51.979  53.745 1.00 57.40  ? 44  ASP H O   1 
ATOM   12579 C  CB  . ASP H  1 53  ? 10.764  51.329  51.023 1.00 52.65  ? 44  ASP H CB  1 
ATOM   12580 C  CG  . ASP H  1 53  ? 9.482   52.047  50.634 1.00 54.21  ? 44  ASP H CG  1 
ATOM   12581 O  OD1 . ASP H  1 53  ? 9.318   53.219  50.989 1.00 62.99  ? 44  ASP H OD1 1 
ATOM   12582 O  OD2 . ASP H  1 53  ? 8.624   51.445  49.966 1.00 56.37  ? 44  ASP H OD2 1 
ATOM   12583 N  N   . SER H  1 54  ? 11.710  54.063  53.064 1.00 52.70  ? 45  SER H N   1 
ATOM   12584 C  CA  . SER H  1 54  ? 11.522  54.609  54.386 1.00 56.32  ? 45  SER H CA  1 
ATOM   12585 C  C   . SER H  1 54  ? 10.040  54.812  54.695 1.00 60.75  ? 45  SER H C   1 
ATOM   12586 O  O   . SER H  1 54  ? 9.689   55.226  55.797 1.00 71.99  ? 45  SER H O   1 
ATOM   12587 C  CB  . SER H  1 54  ? 12.312  55.899  54.552 1.00 52.79  ? 45  SER H CB  1 
ATOM   12588 O  OG  . SER H  1 54  ? 12.050  56.787  53.486 1.00 68.20  ? 45  SER H OG  1 
ATOM   12589 N  N   . SER H  1 55  ? 9.170   54.525  53.731 1.00 53.47  ? 46  SER H N   1 
ATOM   12590 C  CA  . SER H  1 55  ? 7.731   54.577  53.982 1.00 53.61  ? 46  SER H CA  1 
ATOM   12591 C  C   . SER H  1 55  ? 7.169   53.326  54.666 1.00 57.48  ? 46  SER H C   1 
ATOM   12592 O  O   . SER H  1 55  ? 6.280   53.432  55.504 1.00 57.72  ? 46  SER H O   1 
ATOM   12593 C  CB  . SER H  1 55  ? 6.947   54.913  52.702 1.00 60.61  ? 46  SER H CB  1 
ATOM   12594 O  OG  . SER H  1 55  ? 6.996   53.877  51.729 1.00 66.84  ? 46  SER H OG  1 
ATOM   12595 N  N   . THR H  1 56  ? 7.608   52.148  54.220 1.00 58.60  ? 47  THR H N   1 
ATOM   12596 C  CA  . THR H  1 56  ? 7.285   50.867  54.870 1.00 59.73  ? 47  THR H CA  1 
ATOM   12597 C  C   . THR H  1 56  ? 8.375   50.266  55.767 1.00 56.41  ? 47  THR H C   1 
ATOM   12598 O  O   . THR H  1 56  ? 8.155   49.231  56.398 1.00 49.56  ? 47  THR H O   1 
ATOM   12599 C  CB  . THR H  1 56  ? 6.886   49.795  53.832 1.00 57.26  ? 47  THR H CB  1 
ATOM   12600 O  OG1 . THR H  1 56  ? 7.948   49.631  52.881 1.00 52.49  ? 47  THR H OG1 1 
ATOM   12601 C  CG2 . THR H  1 56  ? 5.588   50.182  53.121 1.00 47.98  ? 47  THR H CG2 1 
ATOM   12602 N  N   . ASN H  1 57  ? 9.536   50.916  55.814 1.00 56.38  ? 48  ASN H N   1 
ATOM   12603 C  CA  . ASN H  1 57  ? 10.742  50.362  56.458 1.00 58.14  ? 48  ASN H CA  1 
ATOM   12604 C  C   . ASN H  1 57  ? 11.185  48.984  55.940 1.00 56.50  ? 48  ASN H C   1 
ATOM   12605 O  O   . ASN H  1 57  ? 11.403  48.051  56.720 1.00 54.96  ? 48  ASN H O   1 
ATOM   12606 C  CB  . ASN H  1 57  ? 10.628  50.356  57.990 1.00 57.82  ? 48  ASN H CB  1 
ATOM   12607 C  CG  . ASN H  1 57  ? 10.969  51.704  58.611 1.00 59.18  ? 48  ASN H CG  1 
ATOM   12608 O  OD1 . ASN H  1 57  ? 11.544  52.582  57.964 1.00 61.36  ? 48  ASN H OD1 1 
ATOM   12609 N  ND2 . ASN H  1 57  ? 10.627  51.865  59.880 1.00 58.43  ? 48  ASN H ND2 1 
ATOM   12610 N  N   . GLU H  1 58  ? 11.320  48.887  54.617 1.00 62.34  ? 49  GLU H N   1 
ATOM   12611 C  CA  . GLU H  1 58  ? 11.753  47.675  53.927 1.00 55.17  ? 49  GLU H CA  1 
ATOM   12612 C  C   . GLU H  1 58  ? 12.976  47.959  53.065 1.00 55.09  ? 49  GLU H C   1 
ATOM   12613 O  O   . GLU H  1 58  ? 13.038  48.973  52.382 1.00 52.42  ? 49  GLU H O   1 
ATOM   12614 C  CB  . GLU H  1 58  ? 10.641  47.174  53.015 1.00 51.59  ? 49  GLU H CB  1 
ATOM   12615 C  CG  . GLU H  1 58  ? 9.375   46.751  53.713 1.00 49.78  ? 49  GLU H CG  1 
ATOM   12616 C  CD  . GLU H  1 58  ? 8.350   46.211  52.744 1.00 58.48  ? 49  GLU H CD  1 
ATOM   12617 O  OE1 . GLU H  1 58  ? 7.638   47.013  52.100 1.00 53.67  ? 49  GLU H OE1 1 
ATOM   12618 O  OE2 . GLU H  1 58  ? 8.265   44.973  52.614 1.00 58.88  ? 49  GLU H OE2 1 
ATOM   12619 N  N   . VAL H  1 59  ? 13.941  47.052  53.078 1.00 52.35  ? 50  VAL H N   1 
ATOM   12620 C  CA  . VAL H  1 59  ? 15.118  47.181  52.223 1.00 55.07  ? 50  VAL H CA  1 
ATOM   12621 C  C   . VAL H  1 59  ? 15.204  45.969  51.290 1.00 47.36  ? 50  VAL H C   1 
ATOM   12622 O  O   . VAL H  1 59  ? 14.808  44.875  51.640 1.00 49.92  ? 50  VAL H O   1 
ATOM   12623 C  CB  . VAL H  1 59  ? 16.421  47.400  53.060 1.00 55.97  ? 50  VAL H CB  1 
ATOM   12624 C  CG1 . VAL H  1 59  ? 17.673  47.186  52.243 1.00 48.34  ? 50  VAL H CG1 1 
ATOM   12625 C  CG2 . VAL H  1 59  ? 16.431  48.784  53.634 1.00 61.71  ? 50  VAL H CG2 1 
ATOM   12626 N  N   . ASP H  1 60  ? 15.682  46.190  50.081 1.00 47.13  ? 51  ASP H N   1 
ATOM   12627 C  CA  . ASP H  1 60  ? 15.751  45.137  49.096 1.00 47.54  ? 51  ASP H CA  1 
ATOM   12628 C  C   . ASP H  1 60  ? 17.220  44.813  48.876 1.00 54.29  ? 51  ASP H C   1 
ATOM   12629 O  O   . ASP H  1 60  ? 18.022  45.703  48.607 1.00 53.39  ? 51  ASP H O   1 
ATOM   12630 C  CB  . ASP H  1 60  ? 15.075  45.568  47.787 1.00 52.91  ? 51  ASP H CB  1 
ATOM   12631 C  CG  . ASP H  1 60  ? 13.539  45.629  47.895 1.00 58.26  ? 51  ASP H CG  1 
ATOM   12632 O  OD1 . ASP H  1 60  ? 13.002  45.812  49.008 1.00 52.21  ? 51  ASP H OD1 1 
ATOM   12633 O  OD2 . ASP H  1 60  ? 12.857  45.512  46.850 1.00 64.02  ? 51  ASP H OD2 1 
ATOM   12634 N  N   . LEU H  1 61  ? 17.566  43.535  49.008 1.00 49.23  ? 52  LEU H N   1 
ATOM   12635 C  CA  . LEU H  1 61  ? 18.942  43.091  48.916 1.00 41.13  ? 52  LEU H CA  1 
ATOM   12636 C  C   . LEU H  1 61  ? 19.101  42.124  47.789 1.00 44.67  ? 52  LEU H C   1 
ATOM   12637 O  O   . LEU H  1 61  ? 18.207  41.344  47.530 1.00 51.97  ? 52  LEU H O   1 
ATOM   12638 C  CB  . LEU H  1 61  ? 19.325  42.366  50.189 1.00 54.61  ? 52  LEU H CB  1 
ATOM   12639 C  CG  . LEU H  1 61  ? 20.331  43.107  51.050 1.00 65.94  ? 52  LEU H CG  1 
ATOM   12640 C  CD1 . LEU H  1 61  ? 20.849  42.199  52.156 1.00 63.80  ? 52  LEU H CD1 1 
ATOM   12641 C  CD2 . LEU H  1 61  ? 21.452  43.574  50.150 1.00 63.11  ? 52  LEU H CD2 1 
ATOM   12642 N  N   . VAL H  1 62  ? 20.245  42.167  47.122 1.00 48.25  ? 53  VAL H N   1 
ATOM   12643 C  CA  . VAL H  1 62  ? 20.618  41.118  46.183 1.00 47.42  ? 53  VAL H CA  1 
ATOM   12644 C  C   . VAL H  1 62  ? 21.980  40.620  46.586 1.00 52.21  ? 53  VAL H C   1 
ATOM   12645 O  O   . VAL H  1 62  ? 22.943  41.376  46.617 1.00 55.72  ? 53  VAL H O   1 
ATOM   12646 C  CB  . VAL H  1 62  ? 20.686  41.604  44.723 1.00 45.97  ? 53  VAL H CB  1 
ATOM   12647 C  CG1 . VAL H  1 62  ? 21.361  40.563  43.856 1.00 44.08  ? 53  VAL H CG1 1 
ATOM   12648 C  CG2 . VAL H  1 62  ? 19.296  41.910  44.198 1.00 49.71  ? 53  VAL H CG2 1 
ATOM   12649 N  N   . TYR H  1 63  ? 22.054  39.337  46.898 1.00 47.41  ? 54  TYR H N   1 
ATOM   12650 C  CA  . TYR H  1 63  ? 23.274  38.747  47.402 1.00 50.28  ? 54  TYR H CA  1 
ATOM   12651 C  C   . TYR H  1 63  ? 23.353  37.311  46.898 1.00 52.78  ? 54  TYR H C   1 
ATOM   12652 O  O   . TYR H  1 63  ? 22.356  36.726  46.496 1.00 48.11  ? 54  TYR H O   1 
ATOM   12653 C  CB  . TYR H  1 63  ? 23.235  38.755  48.931 1.00 46.90  ? 54  TYR H CB  1 
ATOM   12654 C  CG  . TYR H  1 63  ? 22.003  38.068  49.457 1.00 46.26  ? 54  TYR H CG  1 
ATOM   12655 C  CD1 . TYR H  1 63  ? 22.033  36.718  49.777 1.00 46.98  ? 54  TYR H CD1 1 
ATOM   12656 C  CD2 . TYR H  1 63  ? 20.796  38.751  49.579 1.00 49.72  ? 54  TYR H CD2 1 
ATOM   12657 C  CE1 . TYR H  1 63  ? 20.914  36.067  50.229 1.00 51.09  ? 54  TYR H CE1 1 
ATOM   12658 C  CE2 . TYR H  1 63  ? 19.660  38.109  50.026 1.00 50.06  ? 54  TYR H CE2 1 
ATOM   12659 C  CZ  . TYR H  1 63  ? 19.733  36.762  50.357 1.00 53.83  ? 54  TYR H CZ  1 
ATOM   12660 O  OH  . TYR H  1 63  ? 18.628  36.091  50.814 1.00 51.25  ? 54  TYR H OH  1 
ATOM   12661 N  N   . TRP H  1 64  ? 24.551  36.752  46.911 1.00 57.66  ? 55  TRP H N   1 
ATOM   12662 C  CA  . TRP H  1 64  ? 24.736  35.317  46.762 1.00 55.85  ? 55  TRP H CA  1 
ATOM   12663 C  C   . TRP H  1 64  ? 24.800  34.656  48.139 1.00 57.93  ? 55  TRP H C   1 
ATOM   12664 O  O   . TRP H  1 64  ? 25.553  35.075  49.014 1.00 58.08  ? 55  TRP H O   1 
ATOM   12665 C  CB  . TRP H  1 64  ? 26.043  35.034  46.034 1.00 59.28  ? 55  TRP H CB  1 
ATOM   12666 C  CG  . TRP H  1 64  ? 26.082  35.575  44.670 1.00 61.86  ? 55  TRP H CG  1 
ATOM   12667 C  CD1 . TRP H  1 64  ? 25.018  35.816  43.849 1.00 64.29  ? 55  TRP H CD1 1 
ATOM   12668 C  CD2 . TRP H  1 64  ? 27.247  35.948  43.941 1.00 66.44  ? 55  TRP H CD2 1 
ATOM   12669 N  NE1 . TRP H  1 64  ? 25.453  36.310  42.641 1.00 66.49  ? 55  TRP H NE1 1 
ATOM   12670 C  CE2 . TRP H  1 64  ? 26.819  36.400  42.674 1.00 72.19  ? 55  TRP H CE2 1 
ATOM   12671 C  CE3 . TRP H  1 64  ? 28.612  35.936  44.230 1.00 71.05  ? 55  TRP H CE3 1 
ATOM   12672 C  CZ2 . TRP H  1 64  ? 27.708  36.842  41.707 1.00 76.81  ? 55  TRP H CZ2 1 
ATOM   12673 C  CZ3 . TRP H  1 64  ? 29.488  36.376  43.275 1.00 75.93  ? 55  TRP H CZ3 1 
ATOM   12674 C  CH2 . TRP H  1 64  ? 29.036  36.820  42.024 1.00 83.71  ? 55  TRP H CH2 1 
ATOM   12675 N  N   . GLU H  1 65  ? 24.025  33.604  48.326 1.00 58.10  ? 56  GLU H N   1 
ATOM   12676 C  CA  . GLU H  1 65  ? 24.088  32.846  49.557 1.00 55.20  ? 56  GLU H CA  1 
ATOM   12677 C  C   . GLU H  1 65  ? 24.787  31.519  49.317 1.00 56.85  ? 56  GLU H C   1 
ATOM   12678 O  O   . GLU H  1 65  ? 24.256  30.658  48.636 1.00 57.64  ? 56  GLU H O   1 
ATOM   12679 C  CB  . GLU H  1 65  ? 22.671  32.608  50.044 1.00 57.11  ? 56  GLU H CB  1 
ATOM   12680 C  CG  . GLU H  1 65  ? 22.534  31.686  51.201 1.00 52.28  ? 56  GLU H CG  1 
ATOM   12681 C  CD  . GLU H  1 65  ? 21.166  31.822  51.796 1.00 60.83  ? 56  GLU H CD  1 
ATOM   12682 O  OE1 . GLU H  1 65  ? 20.367  32.604  51.239 1.00 61.15  ? 56  GLU H OE1 1 
ATOM   12683 O  OE2 . GLU H  1 65  ? 20.883  31.173  52.817 1.00 68.33  ? 56  GLU H OE2 1 
ATOM   12684 N  N   . GLN H  1 66  ? 25.979  31.353  49.876 1.00 56.91  ? 57  GLN H N   1 
ATOM   12685 C  CA  . GLN H  1 66  ? 26.698  30.089  49.762 1.00 56.65  ? 57  GLN H CA  1 
ATOM   12686 C  C   . GLN H  1 66  ? 26.351  29.106  50.870 1.00 52.47  ? 57  GLN H C   1 
ATOM   12687 O  O   . GLN H  1 66  ? 26.455  29.423  52.042 1.00 53.29  ? 57  GLN H O   1 
ATOM   12688 C  CB  . GLN H  1 66  ? 28.200  30.322  49.768 1.00 65.02  ? 57  GLN H CB  1 
ATOM   12689 C  CG  . GLN H  1 66  ? 28.985  29.075  50.115 1.00 58.86  ? 57  GLN H CG  1 
ATOM   12690 C  CD  . GLN H  1 66  ? 30.340  29.079  49.472 1.00 67.06  ? 57  GLN H CD  1 
ATOM   12691 O  OE1 . GLN H  1 66  ? 30.749  30.083  48.883 1.00 84.38  ? 57  GLN H OE1 1 
ATOM   12692 N  NE2 . GLN H  1 66  ? 31.046  27.959  49.560 1.00 67.06  ? 57  GLN H NE2 1 
ATOM   12693 N  N   . GLN H  1 67  ? 25.945  27.905  50.483 1.00 52.17  ? 58  GLN H N   1 
ATOM   12694 C  CA  . GLN H  1 67  ? 25.630  26.845  51.426 1.00 48.88  ? 58  GLN H CA  1 
ATOM   12695 C  C   . GLN H  1 67  ? 26.413  25.593  51.055 1.00 50.04  ? 58  GLN H C   1 
ATOM   12696 O  O   . GLN H  1 67  ? 26.478  25.221  49.899 1.00 52.47  ? 58  GLN H O   1 
ATOM   12697 C  CB  . GLN H  1 67  ? 24.133  26.531  51.386 1.00 46.30  ? 58  GLN H CB  1 
ATOM   12698 C  CG  . GLN H  1 67  ? 23.231  27.725  51.588 1.00 50.41  ? 58  GLN H CG  1 
ATOM   12699 C  CD  . GLN H  1 67  ? 21.765  27.377  51.438 1.00 54.81  ? 58  GLN H CD  1 
ATOM   12700 O  OE1 . GLN H  1 67  ? 21.401  26.212  51.397 1.00 56.05  ? 58  GLN H OE1 1 
ATOM   12701 N  NE2 . GLN H  1 67  ? 20.916  28.392  51.357 1.00 56.05  ? 58  GLN H NE2 1 
ATOM   12702 N  N   . SER H  1 68  ? 27.024  24.932  52.018 1.00 50.44  ? 59  SER H N   1 
ATOM   12703 C  CA  . SER H  1 68  ? 27.581  23.624  51.715 1.00 52.28  ? 59  SER H CA  1 
ATOM   12704 C  C   . SER H  1 68  ? 27.534  22.710  52.923 1.00 56.40  ? 59  SER H C   1 
ATOM   12705 O  O   . SER H  1 68  ? 27.644  23.147  54.069 1.00 54.05  ? 59  SER H O   1 
ATOM   12706 C  CB  . SER H  1 68  ? 29.003  23.737  51.184 1.00 52.89  ? 59  SER H CB  1 
ATOM   12707 O  OG  . SER H  1 68  ? 29.852  24.263  52.179 1.00 55.57  ? 59  SER H OG  1 
ATOM   12708 N  N   . TRP H  1 69  ? 27.351  21.431  52.651 1.00 52.36  ? 60  TRP H N   1 
ATOM   12709 C  CA  . TRP H  1 69  ? 27.267  20.446  53.695 1.00 53.44  ? 60  TRP H CA  1 
ATOM   12710 C  C   . TRP H  1 69  ? 27.801  19.187  53.062 1.00 60.02  ? 60  TRP H C   1 
ATOM   12711 O  O   . TRP H  1 69  ? 28.210  19.217  51.905 1.00 58.12  ? 60  TRP H O   1 
ATOM   12712 C  CB  . TRP H  1 69  ? 25.825  20.273  54.138 1.00 53.52  ? 60  TRP H CB  1 
ATOM   12713 C  CG  . TRP H  1 69  ? 24.917  19.880  53.021 1.00 55.18  ? 60  TRP H CG  1 
ATOM   12714 C  CD1 . TRP H  1 69  ? 24.500  18.620  52.719 1.00 54.50  ? 60  TRP H CD1 1 
ATOM   12715 C  CD2 . TRP H  1 69  ? 24.307  20.751  52.054 1.00 54.90  ? 60  TRP H CD2 1 
ATOM   12716 N  NE1 . TRP H  1 69  ? 23.670  18.648  51.633 1.00 60.80  ? 60  TRP H NE1 1 
ATOM   12717 C  CE2 . TRP H  1 69  ? 23.534  19.941  51.199 1.00 58.97  ? 60  TRP H CE2 1 
ATOM   12718 C  CE3 . TRP H  1 69  ? 24.337  22.134  51.832 1.00 52.67  ? 60  TRP H CE3 1 
ATOM   12719 C  CZ2 . TRP H  1 69  ? 22.802  20.465  50.127 1.00 53.31  ? 60  TRP H CZ2 1 
ATOM   12720 C  CZ3 . TRP H  1 69  ? 23.613  22.650  50.785 1.00 53.47  ? 60  TRP H CZ3 1 
ATOM   12721 C  CH2 . TRP H  1 69  ? 22.853  21.815  49.938 1.00 53.43  ? 60  TRP H CH2 1 
ATOM   12722 N  N   . LYS H  1 70  ? 27.819  18.094  53.816 1.00 63.76  ? 61  LYS H N   1 
ATOM   12723 C  CA  . LYS H  1 70  ? 28.434  16.860  53.348 1.00 64.04  ? 61  LYS H CA  1 
ATOM   12724 C  C   . LYS H  1 70  ? 27.589  15.680  53.765 1.00 65.76  ? 61  LYS H C   1 
ATOM   12725 O  O   . LYS H  1 70  ? 27.166  15.595  54.911 1.00 59.64  ? 61  LYS H O   1 
ATOM   12726 C  CB  . LYS H  1 70  ? 29.851  16.723  53.907 1.00 59.37  ? 61  LYS H CB  1 
ATOM   12727 C  CG  . LYS H  1 70  ? 30.365  15.314  53.961 1.00 62.22  ? 61  LYS H CG  1 
ATOM   12728 C  CD  . LYS H  1 70  ? 31.867  15.319  53.890 1.00 69.31  ? 61  LYS H CD  1 
ATOM   12729 C  CE  . LYS H  1 70  ? 32.445  13.934  54.097 1.00 74.86  ? 61  LYS H CE  1 
ATOM   12730 N  NZ  . LYS H  1 70  ? 33.933  13.967  53.973 1.00 73.95  ? 61  LYS H NZ  1 
ATOM   12731 N  N   . LEU H  1 71  ? 27.321  14.788  52.820 1.00 65.50  ? 62  LEU H N   1 
ATOM   12732 C  CA  . LEU H  1 71  ? 26.569  13.579  53.104 1.00 63.43  ? 62  LEU H CA  1 
ATOM   12733 C  C   . LEU H  1 71  ? 27.384  12.360  52.720 1.00 69.91  ? 62  LEU H C   1 
ATOM   12734 O  O   . LEU H  1 71  ? 27.979  12.317  51.638 1.00 67.27  ? 62  LEU H O   1 
ATOM   12735 C  CB  . LEU H  1 71  ? 25.260  13.555  52.319 1.00 57.72  ? 62  LEU H CB  1 
ATOM   12736 C  CG  . LEU H  1 71  ? 24.179  14.587  52.604 1.00 53.58  ? 62  LEU H CG  1 
ATOM   12737 C  CD1 . LEU H  1 71  ? 22.933  14.147  51.893 1.00 51.49  ? 62  LEU H CD1 1 
ATOM   12738 C  CD2 . LEU H  1 71  ? 23.911  14.734  54.090 1.00 53.10  ? 62  LEU H CD2 1 
ATOM   12739 N  N   . ASN H  1 72  ? 27.399  11.366  53.603 1.00 67.90  ? 63  ASN H N   1 
ATOM   12740 C  CA  . ASN H  1 72  ? 28.063  10.105  53.317 1.00 58.28  ? 63  ASN H CA  1 
ATOM   12741 C  C   . ASN H  1 72  ? 27.391  9.420   52.163 1.00 57.20  ? 63  ASN H C   1 
ATOM   12742 O  O   . ASN H  1 72  ? 28.049  8.813   51.335 1.00 63.78  ? 63  ASN H O   1 
ATOM   12743 C  CB  . ASN H  1 72  ? 28.052  9.216   54.551 1.00 61.32  ? 63  ASN H CB  1 
ATOM   12744 C  CG  . ASN H  1 72  ? 28.751  9.865   55.718 1.00 67.11  ? 63  ASN H CG  1 
ATOM   12745 O  OD1 . ASN H  1 72  ? 29.978  9.897   55.767 1.00 66.06  ? 63  ASN H OD1 1 
ATOM   12746 N  ND2 . ASN H  1 72  ? 27.976  10.430  56.646 1.00 71.78  ? 63  ASN H ND2 1 
ATOM   12747 N  N   . SER H  1 73  ? 26.071  9.551   52.105 1.00 61.65  ? 64  SER H N   1 
ATOM   12748 C  CA  . SER H  1 73  ? 25.259  8.968   51.036 1.00 59.35  ? 64  SER H CA  1 
ATOM   12749 C  C   . SER H  1 73  ? 25.516  9.575   49.658 1.00 65.89  ? 64  SER H C   1 
ATOM   12750 O  O   . SER H  1 73  ? 25.058  9.048   48.642 1.00 65.50  ? 64  SER H O   1 
ATOM   12751 C  CB  . SER H  1 73  ? 23.787  9.115   51.378 1.00 51.25  ? 64  SER H CB  1 
ATOM   12752 O  OG  . SER H  1 73  ? 23.598  10.304  52.121 1.00 64.43  ? 64  SER H OG  1 
ATOM   12753 N  N   . LEU H  1 74  ? 26.194  10.715  49.617 1.00 68.29  ? 65  LEU H N   1 
ATOM   12754 C  CA  . LEU H  1 74  ? 26.628  11.269  48.338 1.00 68.99  ? 65  LEU H CA  1 
ATOM   12755 C  C   . LEU H  1 74  ? 28.082  10.966  47.977 1.00 67.09  ? 65  LEU H C   1 
ATOM   12756 O  O   . LEU H  1 74  ? 28.560  11.431  46.952 1.00 68.90  ? 65  LEU H O   1 
ATOM   12757 C  CB  . LEU H  1 74  ? 26.326  12.765  48.245 1.00 69.14  ? 65  LEU H CB  1 
ATOM   12758 C  CG  . LEU H  1 74  ? 24.831  13.090  48.229 1.00 57.40  ? 65  LEU H CG  1 
ATOM   12759 C  CD1 . LEU H  1 74  ? 24.620  14.585  48.273 1.00 57.49  ? 65  LEU H CD1 1 
ATOM   12760 C  CD2 . LEU H  1 74  ? 24.181  12.489  47.008 1.00 58.73  ? 65  LEU H CD2 1 
ATOM   12761 N  N   . MET H  1 75  ? 28.785  10.211  48.821 1.00 63.58  ? 66  MET H N   1 
ATOM   12762 C  CA  . MET H  1 75  ? 30.167  9.832   48.528 1.00 62.36  ? 66  MET H CA  1 
ATOM   12763 C  C   . MET H  1 75  ? 30.263  8.768   47.435 1.00 65.35  ? 66  MET H C   1 
ATOM   12764 O  O   . MET H  1 75  ? 29.366  7.946   47.267 1.00 66.88  ? 66  MET H O   1 
ATOM   12765 C  CB  . MET H  1 75  ? 30.871  9.304   49.773 1.00 58.48  ? 66  MET H CB  1 
ATOM   12766 C  CG  . MET H  1 75  ? 30.764  10.171  50.997 1.00 64.03  ? 66  MET H CG  1 
ATOM   12767 S  SD  . MET H  1 75  ? 31.574  9.394   52.409 1.00 68.86  ? 66  MET H SD  1 
ATOM   12768 C  CE  . MET H  1 75  ? 33.302  9.661   52.000 1.00 70.11  ? 66  MET H CE  1 
ATOM   12769 N  N   . TRP H  1 76  ? 31.363  8.789   46.695 1.00 61.50  ? 67  TRP H N   1 
ATOM   12770 C  CA  . TRP H  1 76  ? 31.685  7.695   45.800 1.00 64.17  ? 67  TRP H CA  1 
ATOM   12771 C  C   . TRP H  1 76  ? 33.182  7.634   45.582 1.00 67.71  ? 67  TRP H C   1 
ATOM   12772 O  O   . TRP H  1 76  ? 33.926  8.468   46.089 1.00 67.22  ? 67  TRP H O   1 
ATOM   12773 C  CB  . TRP H  1 76  ? 30.958  7.838   44.460 1.00 70.60  ? 67  TRP H CB  1 
ATOM   12774 C  CG  . TRP H  1 76  ? 31.511  8.904   43.530 1.00 73.82  ? 67  TRP H CG  1 
ATOM   12775 C  CD1 . TRP H  1 76  ? 32.465  8.739   42.566 1.00 70.46  ? 67  TRP H CD1 1 
ATOM   12776 C  CD2 . TRP H  1 76  ? 31.114  10.282  43.465 1.00 72.31  ? 67  TRP H CD2 1 
ATOM   12777 N  NE1 . TRP H  1 76  ? 32.691  9.927   41.913 1.00 67.66  ? 67  TRP H NE1 1 
ATOM   12778 C  CE2 . TRP H  1 76  ? 31.873  10.888  42.445 1.00 67.93  ? 67  TRP H CE2 1 
ATOM   12779 C  CE3 . TRP H  1 76  ? 30.189  11.059  44.169 1.00 61.00  ? 67  TRP H CE3 1 
ATOM   12780 C  CZ2 . TRP H  1 76  ? 31.738  12.231  42.117 1.00 64.25  ? 67  TRP H CZ2 1 
ATOM   12781 C  CZ3 . TRP H  1 76  ? 30.058  12.387  43.840 1.00 63.78  ? 67  TRP H CZ3 1 
ATOM   12782 C  CH2 . TRP H  1 76  ? 30.826  12.961  42.824 1.00 64.74  ? 67  TRP H CH2 1 
ATOM   12783 N  N   . ASP H  1 77  ? 33.618  6.644   44.817 1.00 68.84  ? 68  ASP H N   1 
ATOM   12784 C  CA  . ASP H  1 77  ? 35.030  6.482   44.526 1.00 74.52  ? 68  ASP H CA  1 
ATOM   12785 C  C   . ASP H  1 77  ? 35.284  6.793   43.064 1.00 77.30  ? 68  ASP H C   1 
ATOM   12786 O  O   . ASP H  1 77  ? 34.766  6.108   42.188 1.00 77.82  ? 68  ASP H O   1 
ATOM   12787 C  CB  . ASP H  1 77  ? 35.471  5.053   44.842 1.00 85.15  ? 68  ASP H CB  1 
ATOM   12788 C  CG  . ASP H  1 77  ? 36.923  4.796   44.484 1.00 90.61  ? 68  ASP H CG  1 
ATOM   12789 O  OD1 . ASP H  1 77  ? 37.655  5.775   44.214 1.00 90.08  ? 68  ASP H OD1 1 
ATOM   12790 O  OD2 . ASP H  1 77  ? 37.334  3.613   44.486 1.00 89.25  ? 68  ASP H OD2 1 
ATOM   12791 N  N   . PRO H  1 78  ? 36.081  7.836   42.796 1.00 74.32  ? 69  PRO H N   1 
ATOM   12792 C  CA  . PRO H  1 78  ? 36.425  8.230   41.433 1.00 74.67  ? 69  PRO H CA  1 
ATOM   12793 C  C   . PRO H  1 78  ? 36.926  7.067   40.568 1.00 80.45  ? 69  PRO H C   1 
ATOM   12794 O  O   . PRO H  1 78  ? 36.625  7.038   39.378 1.00 75.11  ? 69  PRO H O   1 
ATOM   12795 C  CB  . PRO H  1 78  ? 37.533  9.259   41.656 1.00 73.83  ? 69  PRO H CB  1 
ATOM   12796 C  CG  . PRO H  1 78  ? 37.167  9.892   42.927 1.00 66.69  ? 69  PRO H CG  1 
ATOM   12797 C  CD  . PRO H  1 78  ? 36.631  8.778   43.783 1.00 70.78  ? 69  PRO H CD  1 
ATOM   12798 N  N   . ASN H  1 79  ? 37.658  6.124   41.156 1.00 83.23  ? 70  ASN H N   1 
ATOM   12799 C  CA  . ASN H  1 79  ? 38.220  4.997   40.404 1.00 80.23  ? 70  ASN H CA  1 
ATOM   12800 C  C   . ASN H  1 79  ? 37.184  4.079   39.751 1.00 82.53  ? 70  ASN H C   1 
ATOM   12801 O  O   . ASN H  1 79  ? 37.442  3.491   38.697 1.00 80.81  ? 70  ASN H O   1 
ATOM   12802 C  CB  . ASN H  1 79  ? 39.156  4.173   41.288 1.00 82.30  ? 70  ASN H CB  1 
ATOM   12803 C  CG  . ASN H  1 79  ? 40.292  4.998   41.855 1.00 101.50 ? 70  ASN H CG  1 
ATOM   12804 O  OD1 . ASN H  1 79  ? 40.575  6.099   41.367 1.00 100.34 ? 70  ASN H OD1 1 
ATOM   12805 N  ND2 . ASN H  1 79  ? 40.957  4.471   42.887 1.00 98.95  ? 70  ASN H ND2 1 
ATOM   12806 N  N   . GLU H  1 80  ? 36.035  3.955   40.393 1.00 79.70  ? 71  GLU H N   1 
ATOM   12807 C  CA  . GLU H  1 80  ? 34.986  3.103   39.899 1.00 77.75  ? 71  GLU H CA  1 
ATOM   12808 C  C   . GLU H  1 80  ? 34.116  3.819   38.943 1.00 72.98  ? 71  GLU H C   1 
ATOM   12809 O  O   . GLU H  1 80  ? 33.280  3.228   38.320 1.00 66.40  ? 71  GLU H O   1 
ATOM   12810 C  CB  . GLU H  1 80  ? 34.124  2.614   41.034 1.00 80.67  ? 71  GLU H CB  1 
ATOM   12811 C  CG  . GLU H  1 80  ? 34.757  1.537   41.841 1.00 89.49  ? 71  GLU H CG  1 
ATOM   12812 C  CD  . GLU H  1 80  ? 34.026  1.311   43.110 1.00 96.13  ? 71  GLU H CD  1 
ATOM   12813 O  OE1 . GLU H  1 80  ? 34.637  0.823   44.079 1.00 97.68  ? 71  GLU H OE1 1 
ATOM   12814 O  OE2 . GLU H  1 80  ? 32.833  1.643   43.141 1.00 96.03  ? 71  GLU H OE2 1 
ATOM   12815 N  N   . TYR H  1 81  ? 34.294  5.114   38.841 1.00 79.05  ? 72  TYR H N   1 
ATOM   12816 C  CA  . TYR H  1 81  ? 33.429  5.906   38.000 1.00 79.58  ? 72  TYR H CA  1 
ATOM   12817 C  C   . TYR H  1 81  ? 34.189  6.732   36.988 1.00 76.06  ? 72  TYR H C   1 
ATOM   12818 O  O   . TYR H  1 81  ? 33.802  7.825   36.664 1.00 75.80  ? 72  TYR H O   1 
ATOM   12819 C  CB  . TYR H  1 81  ? 32.481  6.739   38.849 1.00 72.92  ? 72  TYR H CB  1 
ATOM   12820 C  CG  . TYR H  1 81  ? 31.413  5.913   39.520 1.00 63.75  ? 72  TYR H CG  1 
ATOM   12821 C  CD1 . TYR H  1 81  ? 30.245  5.619   38.873 1.00 62.22  ? 72  TYR H CD1 1 
ATOM   12822 C  CD2 . TYR H  1 81  ? 31.575  5.419   40.784 1.00 66.17  ? 72  TYR H CD2 1 
ATOM   12823 C  CE1 . TYR H  1 81  ? 29.277  4.880   39.459 1.00 59.10  ? 72  TYR H CE1 1 
ATOM   12824 C  CE2 . TYR H  1 81  ? 30.596  4.664   41.378 1.00 68.12  ? 72  TYR H CE2 1 
ATOM   12825 C  CZ  . TYR H  1 81  ? 29.447  4.397   40.703 1.00 63.17  ? 72  TYR H CZ  1 
ATOM   12826 O  OH  . TYR H  1 81  ? 28.444  3.651   41.262 1.00 55.30  ? 72  TYR H OH  1 
ATOM   12827 N  N   . GLY H  1 82  ? 35.266  6.175   36.470 1.00 73.36  ? 73  GLY H N   1 
ATOM   12828 C  CA  . GLY H  1 82  ? 36.073  6.851   35.479 1.00 67.03  ? 73  GLY H CA  1 
ATOM   12829 C  C   . GLY H  1 82  ? 36.726  8.147   35.866 1.00 74.37  ? 73  GLY H C   1 
ATOM   12830 O  O   . GLY H  1 82  ? 36.751  9.077   35.101 1.00 73.79  ? 73  GLY H O   1 
ATOM   12831 N  N   . ASN H  1 83  ? 37.265  8.194   37.067 1.00 73.22  ? 74  ASN H N   1 
ATOM   12832 C  CA  . ASN H  1 83  ? 37.803  9.420   37.647 1.00 72.75  ? 74  ASN H CA  1 
ATOM   12833 C  C   . ASN H  1 83  ? 36.925  10.674  37.567 1.00 79.69  ? 74  ASN H C   1 
ATOM   12834 O  O   . ASN H  1 83  ? 37.428  11.780  37.347 1.00 87.82  ? 74  ASN H O   1 
ATOM   12835 C  CB  . ASN H  1 83  ? 39.214  9.698   37.133 1.00 79.15  ? 74  ASN H CB  1 
ATOM   12836 C  CG  . ASN H  1 83  ? 40.278  8.969   37.936 1.00 96.85  ? 74  ASN H CG  1 
ATOM   12837 O  OD1 . ASN H  1 83  ? 40.176  7.764   38.194 1.00 91.74  ? 74  ASN H OD1 1 
ATOM   12838 N  ND2 . ASN H  1 83  ? 41.306  9.704   38.348 1.00 108.11 ? 74  ASN H ND2 1 
ATOM   12839 N  N   . ILE H  1 84  ? 35.622  10.506  37.782 1.00 71.88  ? 75  ILE H N   1 
ATOM   12840 C  CA  . ILE H  1 84  ? 34.743  11.651  37.934 1.00 67.34  ? 75  ILE H CA  1 
ATOM   12841 C  C   . ILE H  1 84  ? 34.875  12.060  39.394 1.00 67.69  ? 75  ILE H C   1 
ATOM   12842 O  O   . ILE H  1 84  ? 34.573  11.282  40.293 1.00 61.79  ? 75  ILE H O   1 
ATOM   12843 C  CB  . ILE H  1 84  ? 33.275  11.274  37.644 1.00 63.33  ? 75  ILE H CB  1 
ATOM   12844 C  CG1 . ILE H  1 84  ? 33.134  10.681  36.250 1.00 61.68  ? 75  ILE H CG1 1 
ATOM   12845 C  CG2 . ILE H  1 84  ? 32.346  12.476  37.794 1.00 64.48  ? 75  ILE H CG2 1 
ATOM   12846 C  CD1 . ILE H  1 84  ? 31.711  10.614  35.782 1.00 66.67  ? 75  ILE H CD1 1 
ATOM   12847 N  N   . THR H  1 85  ? 35.387  13.262  39.628 1.00 64.04  ? 76  THR H N   1 
ATOM   12848 C  CA  . THR H  1 85  ? 35.526  13.767  40.977 1.00 66.76  ? 76  THR H CA  1 
ATOM   12849 C  C   . THR H  1 85  ? 34.368  14.646  41.434 1.00 66.92  ? 76  THR H C   1 
ATOM   12850 O  O   . THR H  1 85  ? 34.256  14.992  42.614 1.00 66.97  ? 76  THR H O   1 
ATOM   12851 C  CB  . THR H  1 85  ? 36.792  14.576  41.074 1.00 78.15  ? 76  THR H CB  1 
ATOM   12852 O  OG1 . THR H  1 85  ? 36.833  15.468  39.957 1.00 82.35  ? 76  THR H OG1 1 
ATOM   12853 C  CG2 . THR H  1 85  ? 38.000  13.658  41.022 1.00 76.14  ? 76  THR H CG2 1 
ATOM   12854 N  N   . ASP H  1 86  ? 33.510  15.027  40.503 1.00 61.37  ? 77  ASP H N   1 
ATOM   12855 C  CA  . ASP H  1 86  ? 32.388  15.883  40.860 1.00 64.97  ? 77  ASP H CA  1 
ATOM   12856 C  C   . ASP H  1 86  ? 31.409  16.019  39.709 1.00 61.52  ? 77  ASP H C   1 
ATOM   12857 O  O   . ASP H  1 86  ? 31.655  15.507  38.622 1.00 60.99  ? 77  ASP H O   1 
ATOM   12858 C  CB  . ASP H  1 86  ? 32.876  17.264  41.346 1.00 69.29  ? 77  ASP H CB  1 
ATOM   12859 C  CG  . ASP H  1 86  ? 33.734  18.001  40.311 1.00 72.59  ? 77  ASP H CG  1 
ATOM   12860 O  OD1 . ASP H  1 86  ? 33.297  18.159  39.151 1.00 72.01  ? 77  ASP H OD1 1 
ATOM   12861 O  OD2 . ASP H  1 86  ? 34.854  18.429  40.665 1.00 72.32  ? 77  ASP H OD2 1 
ATOM   12862 N  N   . PHE H  1 87  ? 30.337  16.768  39.936 1.00 56.83  ? 78  PHE H N   1 
ATOM   12863 C  CA  . PHE H  1 87  ? 29.339  16.994  38.903 1.00 58.66  ? 78  PHE H CA  1 
ATOM   12864 C  C   . PHE H  1 87  ? 28.251  17.956  39.350 1.00 54.80  ? 78  PHE H C   1 
ATOM   12865 O  O   . PHE H  1 87  ? 28.040  18.168  40.535 1.00 49.92  ? 78  PHE H O   1 
ATOM   12866 C  CB  . PHE H  1 87  ? 28.701  15.659  38.483 1.00 59.93  ? 78  PHE H CB  1 
ATOM   12867 C  CG  . PHE H  1 87  ? 27.828  15.028  39.539 1.00 54.17  ? 78  PHE H CG  1 
ATOM   12868 C  CD1 . PHE H  1 87  ? 26.490  15.379  39.656 1.00 54.06  ? 78  PHE H CD1 1 
ATOM   12869 C  CD2 . PHE H  1 87  ? 28.337  14.065  40.395 1.00 56.71  ? 78  PHE H CD2 1 
ATOM   12870 C  CE1 . PHE H  1 87  ? 25.683  14.799  40.622 1.00 58.00  ? 78  PHE H CE1 1 
ATOM   12871 C  CE2 . PHE H  1 87  ? 27.533  13.480  41.371 1.00 54.53  ? 78  PHE H CE2 1 
ATOM   12872 C  CZ  . PHE H  1 87  ? 26.205  13.850  41.484 1.00 50.70  ? 78  PHE H CZ  1 
ATOM   12873 N  N   . ARG H  1 88  ? 27.550  18.520  38.375 1.00 57.05  ? 79  ARG H N   1 
ATOM   12874 C  CA  . ARG H  1 88  ? 26.479  19.470  38.634 1.00 57.39  ? 79  ARG H CA  1 
ATOM   12875 C  C   . ARG H  1 88  ? 25.147  18.744  38.542 1.00 61.11  ? 79  ARG H C   1 
ATOM   12876 O  O   . ARG H  1 88  ? 24.995  17.837  37.735 1.00 67.85  ? 79  ARG H O   1 
ATOM   12877 C  CB  . ARG H  1 88  ? 26.502  20.601  37.612 1.00 55.73  ? 79  ARG H CB  1 
ATOM   12878 C  CG  . ARG H  1 88  ? 27.636  21.579  37.755 1.00 60.91  ? 79  ARG H CG  1 
ATOM   12879 C  CD  . ARG H  1 88  ? 28.975  20.998  37.341 1.00 67.13  ? 79  ARG H CD  1 
ATOM   12880 N  NE  . ARG H  1 88  ? 30.018  22.022  37.385 1.00 71.30  ? 79  ARG H NE  1 
ATOM   12881 C  CZ  . ARG H  1 88  ? 31.306  21.810  37.121 1.00 79.87  ? 79  ARG H CZ  1 
ATOM   12882 N  NH1 . ARG H  1 88  ? 31.732  20.591  36.789 1.00 78.15  ? 79  ARG H NH1 1 
ATOM   12883 N  NH2 . ARG H  1 88  ? 32.168  22.824  37.189 1.00 78.93  ? 79  ARG H NH2 1 
ATOM   12884 N  N   . THR H  1 89  ? 24.184  19.119  39.370 1.00 54.82  ? 80  THR H N   1 
ATOM   12885 C  CA  . THR H  1 89  ? 22.861  18.534  39.259 1.00 56.64  ? 80  THR H CA  1 
ATOM   12886 C  C   . THR H  1 89  ? 21.807  19.553  39.666 1.00 56.31  ? 80  THR H C   1 
ATOM   12887 O  O   . THR H  1 89  ? 22.122  20.564  40.269 1.00 55.65  ? 80  THR H O   1 
ATOM   12888 C  CB  . THR H  1 89  ? 22.734  17.235  40.091 1.00 60.43  ? 80  THR H CB  1 
ATOM   12889 O  OG1 . THR H  1 89  ? 21.662  16.435  39.582 1.00 72.62  ? 80  THR H OG1 1 
ATOM   12890 C  CG2 . THR H  1 89  ? 22.475  17.542  41.555 1.00 61.75  ? 80  THR H CG2 1 
ATOM   12891 N  N   . SER H  1 90  ? 20.564  19.299  39.290 1.00 58.07  ? 81  SER H N   1 
ATOM   12892 C  CA  . SER H  1 90  ? 19.447  20.116  39.718 1.00 53.13  ? 81  SER H CA  1 
ATOM   12893 C  C   . SER H  1 90  ? 19.391  20.042  41.223 1.00 60.82  ? 81  SER H C   1 
ATOM   12894 O  O   . SER H  1 90  ? 19.515  18.962  41.782 1.00 63.69  ? 81  SER H O   1 
ATOM   12895 C  CB  . SER H  1 90  ? 18.160  19.545  39.133 1.00 61.02  ? 81  SER H CB  1 
ATOM   12896 O  OG  . SER H  1 90  ? 17.027  20.296  39.511 1.00 61.10  ? 81  SER H OG  1 
ATOM   12897 N  N   . ALA H  1 91  ? 19.217  21.173  41.900 1.00 66.56  ? 82  ALA H N   1 
ATOM   12898 C  CA  . ALA H  1 91  ? 19.123  21.137  43.358 1.00 56.98  ? 82  ALA H CA  1 
ATOM   12899 C  C   . ALA H  1 91  ? 17.903  20.341  43.818 1.00 53.57  ? 82  ALA H C   1 
ATOM   12900 O  O   . ALA H  1 91  ? 17.869  19.850  44.927 1.00 61.60  ? 82  ALA H O   1 
ATOM   12901 C  CB  . ALA H  1 91  ? 19.094  22.533  43.928 1.00 50.14  ? 82  ALA H CB  1 
ATOM   12902 N  N   . ALA H  1 92  ? 16.903  20.210  42.958 1.00 58.93  ? 83  ALA H N   1 
ATOM   12903 C  CA  . ALA H  1 92  ? 15.683  19.496  43.309 1.00 59.23  ? 83  ALA H CA  1 
ATOM   12904 C  C   . ALA H  1 92  ? 15.934  18.003  43.411 1.00 55.65  ? 83  ALA H C   1 
ATOM   12905 O  O   . ALA H  1 92  ? 15.111  17.265  43.936 1.00 55.97  ? 83  ALA H O   1 
ATOM   12906 C  CB  . ALA H  1 92  ? 14.587  19.780  42.290 1.00 52.05  ? 83  ALA H CB  1 
ATOM   12907 N  N   . ASP H  1 93  ? 17.078  17.573  42.894 1.00 59.39  ? 84  ASP H N   1 
ATOM   12908 C  CA  . ASP H  1 93  ? 17.461  16.162  42.879 1.00 61.43  ? 84  ASP H CA  1 
ATOM   12909 C  C   . ASP H  1 93  ? 18.046  15.726  44.200 1.00 58.09  ? 84  ASP H C   1 
ATOM   12910 O  O   . ASP H  1 93  ? 18.138  14.530  44.476 1.00 66.77  ? 84  ASP H O   1 
ATOM   12911 C  CB  . ASP H  1 93  ? 18.491  15.885  41.782 1.00 63.21  ? 84  ASP H CB  1 
ATOM   12912 C  CG  . ASP H  1 93  ? 17.878  15.878  40.410 1.00 68.27  ? 84  ASP H CG  1 
ATOM   12913 O  OD1 . ASP H  1 93  ? 16.676  16.208  40.322 1.00 63.41  ? 84  ASP H OD1 1 
ATOM   12914 O  OD2 . ASP H  1 93  ? 18.588  15.544  39.432 1.00 70.90  ? 84  ASP H OD2 1 
ATOM   12915 N  N   . ILE H  1 94  ? 18.465  16.699  45.000 1.00 54.15  ? 85  ILE H N   1 
ATOM   12916 C  CA  . ILE H  1 94  ? 19.093  16.417  46.281 1.00 53.62  ? 85  ILE H CA  1 
ATOM   12917 C  C   . ILE H  1 94  ? 18.373  17.093  47.422 1.00 53.40  ? 85  ILE H C   1 
ATOM   12918 O  O   . ILE H  1 94  ? 17.554  17.998  47.237 1.00 52.30  ? 85  ILE H O   1 
ATOM   12919 C  CB  . ILE H  1 94  ? 20.569  16.848  46.332 1.00 51.10  ? 85  ILE H CB  1 
ATOM   12920 C  CG1 . ILE H  1 94  ? 20.730  18.292  45.860 1.00 52.56  ? 85  ILE H CG1 1 
ATOM   12921 C  CG2 . ILE H  1 94  ? 21.429  15.906  45.525 1.00 52.07  ? 85  ILE H CG2 1 
ATOM   12922 C  CD1 . ILE H  1 94  ? 22.126  18.809  46.002 1.00 49.72  ? 85  ILE H CD1 1 
ATOM   12923 N  N   . TRP H  1 95  ? 18.673  16.619  48.617 1.00 53.97  ? 86  TRP H N   1 
ATOM   12924 C  CA  . TRP H  1 95  ? 18.155  17.250  49.803 1.00 55.58  ? 86  TRP H CA  1 
ATOM   12925 C  C   . TRP H  1 95  ? 18.818  18.625  49.924 1.00 55.45  ? 86  TRP H C   1 
ATOM   12926 O  O   . TRP H  1 95  ? 20.024  18.764  49.731 1.00 59.32  ? 86  TRP H O   1 
ATOM   12927 C  CB  . TRP H  1 95  ? 18.436  16.374  51.034 1.00 52.06  ? 86  TRP H CB  1 
ATOM   12928 C  CG  . TRP H  1 95  ? 17.948  16.994  52.277 1.00 49.34  ? 86  TRP H CG  1 
ATOM   12929 C  CD1 . TRP H  1 95  ? 16.696  16.908  52.794 1.00 56.63  ? 86  TRP H CD1 1 
ATOM   12930 C  CD2 . TRP H  1 95  ? 18.686  17.849  53.140 1.00 47.95  ? 86  TRP H CD2 1 
ATOM   12931 N  NE1 . TRP H  1 95  ? 16.605  17.654  53.941 1.00 57.67  ? 86  TRP H NE1 1 
ATOM   12932 C  CE2 . TRP H  1 95  ? 17.819  18.246  54.176 1.00 53.21  ? 86  TRP H CE2 1 
ATOM   12933 C  CE3 . TRP H  1 95  ? 19.995  18.325  53.138 1.00 47.71  ? 86  TRP H CE3 1 
ATOM   12934 C  CZ2 . TRP H  1 95  ? 18.220  19.084  55.210 1.00 56.01  ? 86  TRP H CZ2 1 
ATOM   12935 C  CZ3 . TRP H  1 95  ? 20.397  19.156  54.160 1.00 55.97  ? 86  TRP H CZ3 1 
ATOM   12936 C  CH2 . TRP H  1 95  ? 19.513  19.528  55.190 1.00 54.94  ? 86  TRP H CH2 1 
ATOM   12937 N  N   . THR H  1 96  ? 18.033  19.649  50.215 1.00 49.71  ? 87  THR H N   1 
ATOM   12938 C  CA  . THR H  1 96  ? 18.623  20.929  50.526 1.00 46.39  ? 87  THR H CA  1 
ATOM   12939 C  C   . THR H  1 96  ? 18.114  21.352  51.888 1.00 49.88  ? 87  THR H C   1 
ATOM   12940 O  O   . THR H  1 96  ? 16.982  21.028  52.246 1.00 48.73  ? 87  THR H O   1 
ATOM   12941 C  CB  . THR H  1 96  ? 18.288  21.995  49.461 1.00 53.21  ? 87  THR H CB  1 
ATOM   12942 O  OG1 . THR H  1 96  ? 16.871  22.103  49.322 1.00 55.15  ? 87  THR H OG1 1 
ATOM   12943 C  CG2 . THR H  1 96  ? 18.887  21.630  48.122 1.00 46.95  ? 87  THR H CG2 1 
ATOM   12944 N  N   . PRO H  1 97  ? 18.961  22.059  52.663 1.00 56.83  ? 88  PRO H N   1 
ATOM   12945 C  CA  . PRO H  1 97  ? 18.644  22.592  54.003 1.00 54.51  ? 88  PRO H CA  1 
ATOM   12946 C  C   . PRO H  1 97  ? 17.618  23.713  53.932 1.00 54.27  ? 88  PRO H C   1 
ATOM   12947 O  O   . PRO H  1 97  ? 17.691  24.489  52.980 1.00 58.16  ? 88  PRO H O   1 
ATOM   12948 C  CB  . PRO H  1 97  ? 19.989  23.167  54.477 1.00 50.12  ? 88  PRO H CB  1 
ATOM   12949 C  CG  . PRO H  1 97  ? 20.759  23.440  53.207 1.00 47.79  ? 88  PRO H CG  1 
ATOM   12950 C  CD  . PRO H  1 97  ? 20.364  22.321  52.288 1.00 50.76  ? 88  PRO H CD  1 
ATOM   12951 N  N   . ASP H  1 98  ? 16.723  23.864  54.908 1.00 49.70  ? 89  ASP H N   1 
ATOM   12952 C  CA  . ASP H  1 98  ? 15.729  24.902  54.715 1.00 47.53  ? 89  ASP H CA  1 
ATOM   12953 C  C   . ASP H  1 98  ? 16.152  26.140  55.490 1.00 52.36  ? 89  ASP H C   1 
ATOM   12954 O  O   . ASP H  1 98  ? 15.712  26.385  56.605 1.00 50.74  ? 89  ASP H O   1 
ATOM   12955 C  CB  . ASP H  1 98  ? 14.388  24.394  55.278 1.00 43.95  ? 89  ASP H CB  1 
ATOM   12956 C  CG  . ASP H  1 98  ? 14.476  23.954  56.770 1.00 52.94  ? 89  ASP H CG  1 
ATOM   12957 O  OD1 . ASP H  1 98  ? 15.572  23.593  57.258 1.00 42.15  ? 89  ASP H OD1 1 
ATOM   12958 O  OD2 . ASP H  1 98  ? 13.433  23.959  57.464 1.00 55.28  ? 89  ASP H OD2 1 
ATOM   12959 N  N   . ILE H  1 99  ? 16.768  27.057  54.767 1.00 50.14  ? 90  ILE H N   1 
ATOM   12960 C  CA  . ILE H  1 99  ? 17.464  28.152  55.395 1.00 52.17  ? 90  ILE H CA  1 
ATOM   12961 C  C   . ILE H  1 99  ? 16.759  29.380  54.894 1.00 54.59  ? 90  ILE H C   1 
ATOM   12962 O  O   . ILE H  1 99  ? 16.713  29.619  53.690 1.00 53.11  ? 90  ILE H O   1 
ATOM   12963 C  CB  . ILE H  1 99  ? 18.956  28.213  54.974 1.00 56.76  ? 90  ILE H CB  1 
ATOM   12964 C  CG1 . ILE H  1 99  ? 19.657  26.877  55.212 1.00 54.43  ? 90  ILE H CG1 1 
ATOM   12965 C  CG2 . ILE H  1 99  ? 19.690  29.333  55.711 1.00 52.35  ? 90  ILE H CG2 1 
ATOM   12966 C  CD1 . ILE H  1 99  ? 20.034  26.633  56.622 1.00 49.52  ? 90  ILE H CD1 1 
ATOM   12967 N  N   . THR H  1 100 ? 16.203  30.143  55.824 1.00 53.99  ? 91  THR H N   1 
ATOM   12968 C  CA  . THR H  1 100 ? 15.372  31.280  55.504 1.00 49.69  ? 91  THR H CA  1 
ATOM   12969 C  C   . THR H  1 100 ? 15.896  32.555  56.131 1.00 52.79  ? 91  THR H C   1 
ATOM   12970 O  O   . THR H  1 100 ? 16.508  32.550  57.204 1.00 52.29  ? 91  THR H O   1 
ATOM   12971 C  CB  . THR H  1 100 ? 13.958  31.082  56.069 1.00 52.84  ? 91  THR H CB  1 
ATOM   12972 O  OG1 . THR H  1 100 ? 13.594  29.706  55.967 1.00 60.31  ? 91  THR H OG1 1 
ATOM   12973 C  CG2 . THR H  1 100 ? 12.933  31.952  55.334 1.00 51.92  ? 91  THR H CG2 1 
ATOM   12974 N  N   . ALA H  1 101 ? 15.612  33.658  55.461 1.00 52.23  ? 92  ALA H N   1 
ATOM   12975 C  CA  . ALA H  1 101 ? 15.666  34.942  56.108 1.00 58.60  ? 92  ALA H CA  1 
ATOM   12976 C  C   . ALA H  1 101 ? 14.498  34.941  57.111 1.00 57.27  ? 92  ALA H C   1 
ATOM   12977 O  O   . ALA H  1 101 ? 13.346  34.672  56.723 1.00 55.32  ? 92  ALA H O   1 
ATOM   12978 C  CB  . ALA H  1 101 ? 15.512  36.052  55.067 1.00 48.30  ? 92  ALA H CB  1 
ATOM   12979 N  N   . TYR H  1 102 ? 14.799  35.213  58.387 1.00 46.09  ? 93  TYR H N   1 
ATOM   12980 C  CA  . TYR H  1 102 ? 13.781  35.225  59.438 1.00 48.38  ? 93  TYR H CA  1 
ATOM   12981 C  C   . TYR H  1 102 ? 12.918  36.481  59.430 1.00 57.70  ? 93  TYR H C   1 
ATOM   12982 O  O   . TYR H  1 102 ? 11.783  36.451  59.907 1.00 58.93  ? 93  TYR H O   1 
ATOM   12983 C  CB  . TYR H  1 102 ? 14.416  35.112  60.810 1.00 50.70  ? 93  TYR H CB  1 
ATOM   12984 C  CG  . TYR H  1 102 ? 14.955  33.755  61.150 1.00 59.47  ? 93  TYR H CG  1 
ATOM   12985 C  CD1 . TYR H  1 102 ? 14.362  32.605  60.657 1.00 62.90  ? 93  TYR H CD1 1 
ATOM   12986 C  CD2 . TYR H  1 102 ? 16.064  33.622  61.968 1.00 58.81  ? 93  TYR H CD2 1 
ATOM   12987 C  CE1 . TYR H  1 102 ? 14.860  31.368  60.974 1.00 56.97  ? 93  TYR H CE1 1 
ATOM   12988 C  CE2 . TYR H  1 102 ? 16.565  32.395  62.278 1.00 57.34  ? 93  TYR H CE2 1 
ATOM   12989 C  CZ  . TYR H  1 102 ? 15.961  31.275  61.785 1.00 53.19  ? 93  TYR H CZ  1 
ATOM   12990 O  OH  . TYR H  1 102 ? 16.463  30.048  62.101 1.00 53.27  ? 93  TYR H OH  1 
ATOM   12991 N  N   . SER H  1 103 ? 13.498  37.590  58.966 1.00 55.29  ? 94  SER H N   1 
ATOM   12992 C  CA  . SER H  1 103 ? 12.829  38.894  58.824 1.00 52.28  ? 94  SER H CA  1 
ATOM   12993 C  C   . SER H  1 103 ? 12.267  39.295  57.425 1.00 55.97  ? 94  SER H C   1 
ATOM   12994 O  O   . SER H  1 103 ? 11.908  40.452  57.206 1.00 49.38  ? 94  SER H O   1 
ATOM   12995 C  CB  . SER H  1 103 ? 13.655  40.010  59.460 1.00 47.95  ? 94  SER H CB  1 
ATOM   12996 O  OG  . SER H  1 103 ? 14.994  39.979  59.003 1.00 53.30  ? 94  SER H OG  1 
ATOM   12997 N  N   . SER H  1 104 ? 12.280  38.386  56.456 1.00 57.08  ? 95  SER H N   1 
ATOM   12998 C  CA  . SER H  1 104 ? 11.711  38.687  55.132 1.00 54.60  ? 95  SER H CA  1 
ATOM   12999 C  C   . SER H  1 104 ? 10.256  39.215  55.168 1.00 55.83  ? 95  SER H C   1 
ATOM   13000 O  O   . SER H  1 104 ? 9.404   38.709  55.904 1.00 55.18  ? 95  SER H O   1 
ATOM   13001 C  CB  . SER H  1 104 ? 11.814  37.466  54.220 1.00 51.59  ? 95  SER H CB  1 
ATOM   13002 O  OG  . SER H  1 104 ? 10.984  36.402  54.667 1.00 60.88  ? 95  SER H OG  1 
ATOM   13003 N  N   . THR H  1 105 ? 10.005  40.296  54.434 1.00 51.90  ? 96  THR H N   1 
ATOM   13004 C  CA  . THR H  1 105 ? 8.645   40.817  54.245 1.00 51.99  ? 96  THR H CA  1 
ATOM   13005 C  C   . THR H  1 105 ? 7.911   40.369  52.958 1.00 47.09  ? 96  THR H C   1 
ATOM   13006 O  O   . THR H  1 105 ? 6.699   40.528  52.816 1.00 43.14  ? 96  THR H O   1 
ATOM   13007 C  CB  . THR H  1 105 ? 8.681   42.349  54.301 1.00 57.81  ? 96  THR H CB  1 
ATOM   13008 O  OG1 . THR H  1 105 ? 9.563   42.830  53.272 1.00 55.09  ? 96  THR H OG1 1 
ATOM   13009 C  CG2 . THR H  1 105 ? 9.163   42.827  55.698 1.00 49.55  ? 96  THR H CG2 1 
ATOM   13010 N  N   . ARG H  1 106 ? 8.652   39.772  52.039 1.00 50.49  ? 97  ARG H N   1 
ATOM   13011 C  CA  A ARG H  1 106 ? 8.084   39.294  50.790 0.50 49.14  ? 97  ARG H CA  1 
ATOM   13012 C  CA  B ARG H  1 106 ? 8.115   39.335  50.754 0.50 49.13  ? 97  ARG H CA  1 
ATOM   13013 C  C   . ARG H  1 106 ? 8.795   38.021  50.394 1.00 46.74  ? 97  ARG H C   1 
ATOM   13014 O  O   . ARG H  1 106 ? 9.964   37.828  50.726 1.00 52.82  ? 97  ARG H O   1 
ATOM   13015 C  CB  A ARG H  1 106 ? 8.210   40.346  49.685 0.50 47.70  ? 97  ARG H CB  1 
ATOM   13016 C  CB  B ARG H  1 106 ? 8.409   40.377  49.661 0.50 47.68  ? 97  ARG H CB  1 
ATOM   13017 C  CG  A ARG H  1 106 ? 7.297   41.541  49.877 0.50 50.30  ? 97  ARG H CG  1 
ATOM   13018 C  CG  B ARG H  1 106 ? 7.885   41.790  49.931 0.50 50.06  ? 97  ARG H CG  1 
ATOM   13019 C  CD  A ARG H  1 106 ? 7.231   42.411  48.644 0.50 49.52  ? 97  ARG H CD  1 
ATOM   13020 C  CD  B ARG H  1 106 ? 8.352   42.778  48.861 0.50 51.80  ? 97  ARG H CD  1 
ATOM   13021 N  NE  A ARG H  1 106 ? 6.223   43.459  48.776 0.50 48.98  ? 97  ARG H NE  1 
ATOM   13022 N  NE  B ARG H  1 106 ? 7.904   44.153  49.107 0.50 56.89  ? 97  ARG H NE  1 
ATOM   13023 C  CZ  A ARG H  1 106 ? 4.916   43.238  48.723 0.50 49.70  ? 97  ARG H CZ  1 
ATOM   13024 C  CZ  B ARG H  1 106 ? 8.212   45.201  48.338 0.50 56.98  ? 97  ARG H CZ  1 
ATOM   13025 N  NH1 A ARG H  1 106 ? 4.462   42.003  48.559 0.50 50.66  ? 97  ARG H NH1 1 
ATOM   13026 N  NH1 B ARG H  1 106 ? 8.976   45.055  47.259 0.50 49.50  ? 97  ARG H NH1 1 
ATOM   13027 N  NH2 A ARG H  1 106 ? 4.065   44.246  48.844 0.50 49.67  ? 97  ARG H NH2 1 
ATOM   13028 N  NH2 B ARG H  1 106 ? 7.750   46.404  48.645 0.50 56.19  ? 97  ARG H NH2 1 
ATOM   13029 N  N   . PRO H  1 107 ? 8.086   37.126  49.700 1.00 45.08  ? 98  PRO H N   1 
ATOM   13030 C  CA  . PRO H  1 107 ? 8.746   35.860  49.356 1.00 44.08  ? 98  PRO H CA  1 
ATOM   13031 C  C   . PRO H  1 107 ? 10.073  36.087  48.622 1.00 43.96  ? 98  PRO H C   1 
ATOM   13032 O  O   . PRO H  1 107 ? 10.155  36.971  47.781 1.00 45.92  ? 98  PRO H O   1 
ATOM   13033 C  CB  . PRO H  1 107 ? 7.726   35.173  48.466 1.00 31.14  ? 98  PRO H CB  1 
ATOM   13034 C  CG  . PRO H  1 107 ? 6.411   35.759  48.886 1.00 41.56  ? 98  PRO H CG  1 
ATOM   13035 C  CD  . PRO H  1 107 ? 6.674   37.167  49.287 1.00 39.27  ? 98  PRO H CD  1 
ATOM   13036 N  N   . VAL H  1 108 ? 11.104  35.323  48.967 1.00 51.13  ? 99  VAL H N   1 
ATOM   13037 C  CA  . VAL H  1 108 ? 12.425  35.443  48.346 1.00 49.45  ? 99  VAL H CA  1 
ATOM   13038 C  C   . VAL H  1 108 ? 12.347  35.120  46.869 1.00 47.27  ? 99  VAL H C   1 
ATOM   13039 O  O   . VAL H  1 108 ? 11.702  34.152  46.490 1.00 52.34  ? 99  VAL H O   1 
ATOM   13040 C  CB  . VAL H  1 108 ? 13.390  34.400  48.936 1.00 48.06  ? 99  VAL H CB  1 
ATOM   13041 C  CG1 . VAL H  1 108 ? 14.837  34.732  48.582 1.00 47.39  ? 99  VAL H CG1 1 
ATOM   13042 C  CG2 . VAL H  1 108 ? 13.187  34.287  50.428 1.00 66.39  ? 99  VAL H CG2 1 
ATOM   13043 N  N   . GLN H  1 109 ? 13.020  35.892  46.030 1.00 50.36  ? 100 GLN H N   1 
ATOM   13044 C  CA  . GLN H  1 109 ? 13.071  35.560  44.604 1.00 55.62  ? 100 GLN H CA  1 
ATOM   13045 C  C   . GLN H  1 109 ? 14.438  35.004  44.220 1.00 56.99  ? 100 GLN H C   1 
ATOM   13046 O  O   . GLN H  1 109 ? 15.466  35.505  44.665 1.00 57.65  ? 100 GLN H O   1 
ATOM   13047 C  CB  . GLN H  1 109 ? 12.706  36.765  43.743 1.00 45.75  ? 100 GLN H CB  1 
ATOM   13048 C  CG  . GLN H  1 109 ? 11.269  37.206  43.940 1.00 54.49  ? 100 GLN H CG  1 
ATOM   13049 C  CD  . GLN H  1 109 ? 11.001  38.604  43.417 1.00 60.40  ? 100 GLN H CD  1 
ATOM   13050 O  OE1 . GLN H  1 109 ? 11.590  39.579  43.874 1.00 55.66  ? 100 GLN H OE1 1 
ATOM   13051 N  NE2 . GLN H  1 109 ? 10.109  38.703  42.446 1.00 62.21  ? 100 GLN H NE2 1 
ATOM   13052 N  N   . VAL H  1 110 ? 14.449  33.948  43.413 1.00 55.58  ? 101 VAL H N   1 
ATOM   13053 C  CA  . VAL H  1 110 ? 15.706  33.334  43.030 1.00 49.27  ? 101 VAL H CA  1 
ATOM   13054 C  C   . VAL H  1 110 ? 16.176  33.883  41.702 1.00 44.09  ? 101 VAL H C   1 
ATOM   13055 O  O   . VAL H  1 110 ? 15.421  33.921  40.761 1.00 49.80  ? 101 VAL H O   1 
ATOM   13056 C  CB  . VAL H  1 110 ? 15.598  31.829  42.987 1.00 46.90  ? 101 VAL H CB  1 
ATOM   13057 C  CG1 . VAL H  1 110 ? 16.901  31.253  42.499 1.00 51.07  ? 101 VAL H CG1 1 
ATOM   13058 C  CG2 . VAL H  1 110 ? 15.265  31.301  44.378 1.00 50.02  ? 101 VAL H CG2 1 
ATOM   13059 N  N   . LEU H  1 111 ? 17.401  34.386  41.662 1.00 45.93  ? 102 LEU H N   1 
ATOM   13060 C  CA  . LEU H  1 111 ? 17.930  35.019  40.460 1.00 48.24  ? 102 LEU H CA  1 
ATOM   13061 C  C   . LEU H  1 111 ? 18.832  34.155  39.572 1.00 50.33  ? 102 LEU H C   1 
ATOM   13062 O  O   . LEU H  1 111 ? 19.233  34.591  38.486 1.00 59.43  ? 102 LEU H O   1 
ATOM   13063 C  CB  . LEU H  1 111 ? 18.633  36.339  40.810 1.00 44.80  ? 102 LEU H CB  1 
ATOM   13064 C  CG  . LEU H  1 111 ? 17.802  37.261  41.702 1.00 48.67  ? 102 LEU H CG  1 
ATOM   13065 C  CD1 . LEU H  1 111 ? 18.594  38.468  42.133 1.00 48.32  ? 102 LEU H CD1 1 
ATOM   13066 C  CD2 . LEU H  1 111 ? 16.519  37.664  41.032 1.00 45.89  ? 102 LEU H CD2 1 
ATOM   13067 N  N   . SER H  1 112 ? 19.141  32.937  39.998 1.00 50.45  ? 103 SER H N   1 
ATOM   13068 C  CA  . SER H  1 112 ? 20.008  32.089  39.187 1.00 52.57  ? 103 SER H CA  1 
ATOM   13069 C  C   . SER H  1 112 ? 19.397  30.714  39.048 1.00 52.57  ? 103 SER H C   1 
ATOM   13070 O  O   . SER H  1 112 ? 18.372  30.429  39.661 1.00 52.33  ? 103 SER H O   1 
ATOM   13071 C  CB  . SER H  1 112 ? 21.418  32.008  39.794 1.00 55.24  ? 103 SER H CB  1 
ATOM   13072 O  OG  . SER H  1 112 ? 21.395  31.662  41.171 1.00 49.69  ? 103 SER H OG  1 
ATOM   13073 N  N   . PRO H  1 113 ? 20.033  29.848  38.252 1.00 53.53  ? 104 PRO H N   1 
ATOM   13074 C  CA  . PRO H  1 113 ? 19.526  28.483  38.067 1.00 57.10  ? 104 PRO H CA  1 
ATOM   13075 C  C   . PRO H  1 113 ? 19.667  27.675  39.358 1.00 60.58  ? 104 PRO H C   1 
ATOM   13076 O  O   . PRO H  1 113 ? 20.657  27.872  40.072 1.00 57.09  ? 104 PRO H O   1 
ATOM   13077 C  CB  . PRO H  1 113 ? 20.444  27.923  36.978 1.00 52.23  ? 104 PRO H CB  1 
ATOM   13078 C  CG  . PRO H  1 113 ? 20.901  29.124  36.227 1.00 54.25  ? 104 PRO H CG  1 
ATOM   13079 C  CD  . PRO H  1 113 ? 21.078  30.186  37.271 1.00 54.14  ? 104 PRO H CD  1 
ATOM   13080 N  N   . GLN H  1 114 ? 18.728  26.787  39.683 1.00 59.32  ? 105 GLN H N   1 
ATOM   13081 C  CA  . GLN H  1 114 ? 18.940  26.060  40.922 1.00 57.20  ? 105 GLN H CA  1 
ATOM   13082 C  C   . GLN H  1 114 ? 19.647  24.762  40.574 1.00 57.39  ? 105 GLN H C   1 
ATOM   13083 O  O   . GLN H  1 114 ? 19.033  23.775  40.171 1.00 55.35  ? 105 GLN H O   1 
ATOM   13084 C  CB  . GLN H  1 114 ? 17.610  25.755  41.611 1.00 58.04  ? 105 GLN H CB  1 
ATOM   13085 C  CG  . GLN H  1 114 ? 16.461  26.672  41.240 1.00 54.10  ? 105 GLN H CG  1 
ATOM   13086 C  CD  . GLN H  1 114 ? 16.027  27.517  42.403 1.00 55.99  ? 105 GLN H CD  1 
ATOM   13087 O  OE1 . GLN H  1 114 ? 16.857  27.977  43.179 1.00 64.34  ? 105 GLN H OE1 1 
ATOM   13088 N  NE2 . GLN H  1 114 ? 14.726  27.718  42.545 1.00 52.28  ? 105 GLN H NE2 1 
ATOM   13089 N  N   . ASN H  1 115 ? 20.929  24.745  40.898 1.00 54.17  ? 106 ASN H N   1 
ATOM   13090 C  CA  . ASN H  1 115 ? 21.845  23.710  40.484 1.00 55.85  ? 106 ASN H CA  1 
ATOM   13091 C  C   . ASN H  1 115 ? 22.851  23.665  41.599 1.00 56.87  ? 106 ASN H C   1 
ATOM   13092 O  O   . ASN H  1 115 ? 23.079  24.676  42.245 1.00 59.93  ? 106 ASN H O   1 
ATOM   13093 C  CB  . ASN H  1 115 ? 22.550  24.085  39.172 1.00 58.98  ? 106 ASN H CB  1 
ATOM   13094 C  CG  . ASN H  1 115 ? 21.611  24.061  37.949 1.00 64.27  ? 106 ASN H CG  1 
ATOM   13095 O  OD1 . ASN H  1 115 ? 20.663  23.281  37.885 1.00 58.47  ? 106 ASN H OD1 1 
ATOM   13096 N  ND2 . ASN H  1 115 ? 21.893  24.920  36.972 1.00 63.98  ? 106 ASN H ND2 1 
ATOM   13097 N  N   . ALA H  1 116 ? 23.453  22.505  41.826 1.00 61.83  ? 107 ALA H N   1 
ATOM   13098 C  CA  . ALA H  1 116 ? 24.413  22.331  42.906 1.00 50.60  ? 107 ALA H CA  1 
ATOM   13099 C  C   . ALA H  1 116 ? 25.584  21.488  42.439 1.00 55.00  ? 107 ALA H C   1 
ATOM   13100 O  O   . ALA H  1 116 ? 25.416  20.571  41.648 1.00 64.09  ? 107 ALA H O   1 
ATOM   13101 C  CB  . ALA H  1 116 ? 23.745  21.669  44.068 1.00 51.21  ? 107 ALA H CB  1 
ATOM   13102 N  N   . LEU H  1 117 ? 26.777  21.804  42.917 1.00 51.71  ? 108 LEU H N   1 
ATOM   13103 C  CA  . LEU H  1 117 ? 27.936  20.971  42.643 1.00 55.97  ? 108 LEU H CA  1 
ATOM   13104 C  C   . LEU H  1 117 ? 28.129  19.943  43.760 1.00 55.81  ? 108 LEU H C   1 
ATOM   13105 O  O   . LEU H  1 117 ? 28.347  20.312  44.910 1.00 56.46  ? 108 LEU H O   1 
ATOM   13106 C  CB  . LEU H  1 117 ? 29.194  21.831  42.477 1.00 57.07  ? 108 LEU H CB  1 
ATOM   13107 C  CG  . LEU H  1 117 ? 30.528  21.082  42.367 1.00 64.37  ? 108 LEU H CG  1 
ATOM   13108 C  CD1 . LEU H  1 117 ? 30.736  20.509  40.970 1.00 60.78  ? 108 LEU H CD1 1 
ATOM   13109 C  CD2 . LEU H  1 117 ? 31.680  21.991  42.748 1.00 69.28  ? 108 LEU H CD2 1 
ATOM   13110 N  N   . VAL H  1 118 ? 28.032  18.656  43.420 1.00 65.16  ? 109 VAL H N   1 
ATOM   13111 C  CA  . VAL H  1 118 ? 28.317  17.575  44.368 1.00 61.11  ? 109 VAL H CA  1 
ATOM   13112 C  C   . VAL H  1 118 ? 29.720  16.997  44.114 1.00 58.42  ? 109 VAL H C   1 
ATOM   13113 O  O   . VAL H  1 118 ? 30.125  16.837  42.970 1.00 54.19  ? 109 VAL H O   1 
ATOM   13114 C  CB  . VAL H  1 118 ? 27.221  16.453  44.323 1.00 56.28  ? 109 VAL H CB  1 
ATOM   13115 C  CG1 . VAL H  1 118 ? 27.466  15.414  45.402 1.00 55.26  ? 109 VAL H CG1 1 
ATOM   13116 C  CG2 . VAL H  1 118 ? 25.830  17.048  44.476 1.00 56.34  ? 109 VAL H CG2 1 
ATOM   13117 N  N   . ASN H  1 119 ? 30.469  16.668  45.160 1.00 59.95  ? 110 ASN H N   1 
ATOM   13118 C  CA  . ASN H  1 119 ? 31.788  16.074  44.919 1.00 64.38  ? 110 ASN H CA  1 
ATOM   13119 C  C   . ASN H  1 119 ? 32.012  14.695  45.561 1.00 64.12  ? 110 ASN H C   1 
ATOM   13120 O  O   . ASN H  1 119 ? 31.208  14.256  46.379 1.00 63.66  ? 110 ASN H O   1 
ATOM   13121 C  CB  . ASN H  1 119 ? 32.931  17.094  45.121 1.00 68.95  ? 110 ASN H CB  1 
ATOM   13122 C  CG  . ASN H  1 119 ? 33.529  17.074  46.526 1.00 73.61  ? 110 ASN H CG  1 
ATOM   13123 O  OD1 . ASN H  1 119 ? 32.871  16.717  47.490 1.00 71.00  ? 110 ASN H OD1 1 
ATOM   13124 N  ND2 . ASN H  1 119 ? 34.773  17.500  46.639 1.00 77.47  ? 110 ASN H ND2 1 
ATOM   13125 N  N   . SER H  1 120 ? 33.047  13.990  45.108 1.00 63.56  ? 111 SER H N   1 
ATOM   13126 C  CA  . SER H  1 120 ? 33.269  12.580  45.457 1.00 68.23  ? 111 SER H CA  1 
ATOM   13127 C  C   . SER H  1 120 ? 33.204  12.269  46.948 1.00 66.12  ? 111 SER H C   1 
ATOM   13128 O  O   . SER H  1 120 ? 32.793  11.178  47.341 1.00 71.34  ? 111 SER H O   1 
ATOM   13129 C  CB  . SER H  1 120 ? 34.600  12.074  44.894 1.00 67.31  ? 111 SER H CB  1 
ATOM   13130 O  OG  . SER H  1 120 ? 35.687  12.711  45.524 1.00 72.24  ? 111 SER H OG  1 
ATOM   13131 N  N   . SER H  1 121 ? 33.616  13.208  47.784 1.00 69.04  ? 112 SER H N   1 
ATOM   13132 C  CA  . SER H  1 121 ? 33.595  12.954  49.215 1.00 70.75  ? 112 SER H CA  1 
ATOM   13133 C  C   . SER H  1 121 ? 32.215  13.214  49.811 1.00 69.72  ? 112 SER H C   1 
ATOM   13134 O  O   . SER H  1 121 ? 31.999  13.025  51.003 1.00 71.50  ? 112 SER H O   1 
ATOM   13135 C  CB  . SER H  1 121 ? 34.674  13.769  49.931 1.00 67.53  ? 112 SER H CB  1 
ATOM   13136 O  OG  . SER H  1 121 ? 34.639  15.122  49.532 1.00 80.22  ? 112 SER H OG  1 
ATOM   13137 N  N   . GLY H  1 122 ? 31.278  13.638  48.977 1.00 64.84  ? 113 GLY H N   1 
ATOM   13138 C  CA  . GLY H  1 122 ? 29.939  13.914  49.451 1.00 68.37  ? 113 GLY H CA  1 
ATOM   13139 C  C   . GLY H  1 122 ? 29.702  15.366  49.834 1.00 70.86  ? 113 GLY H C   1 
ATOM   13140 O  O   . GLY H  1 122 ? 28.671  15.694  50.425 1.00 68.68  ? 113 GLY H O   1 
ATOM   13141 N  N   . HIS H  1 123 ? 30.647  16.245  49.513 1.00 69.85  ? 114 HIS H N   1 
ATOM   13142 C  CA  . HIS H  1 123 ? 30.433  17.664  49.782 1.00 69.69  ? 114 HIS H CA  1 
ATOM   13143 C  C   . HIS H  1 123 ? 29.531  18.262  48.711 1.00 61.89  ? 114 HIS H C   1 
ATOM   13144 O  O   . HIS H  1 123 ? 29.817  18.175  47.522 1.00 66.13  ? 114 HIS H O   1 
ATOM   13145 C  CB  . HIS H  1 123 ? 31.757  18.435  49.902 1.00 72.99  ? 114 HIS H CB  1 
ATOM   13146 C  CG  . HIS H  1 123 ? 32.547  18.093  51.130 1.00 78.73  ? 114 HIS H CG  1 
ATOM   13147 N  ND1 . HIS H  1 123 ? 33.519  17.114  51.143 1.00 81.10  ? 114 HIS H ND1 1 
ATOM   13148 C  CD2 . HIS H  1 123 ? 32.509  18.599  52.385 1.00 71.35  ? 114 HIS H CD2 1 
ATOM   13149 C  CE1 . HIS H  1 123 ? 34.043  17.031  52.351 1.00 77.61  ? 114 HIS H CE1 1 
ATOM   13150 N  NE2 . HIS H  1 123 ? 33.446  17.919  53.124 1.00 76.68  ? 114 HIS H NE2 1 
ATOM   13151 N  N   . VAL H  1 124 ? 28.423  18.839  49.150 1.00 54.48  ? 115 VAL H N   1 
ATOM   13152 C  CA  . VAL H  1 124 ? 27.505  19.507  48.256 1.00 55.67  ? 115 VAL H CA  1 
ATOM   13153 C  C   . VAL H  1 124 ? 27.756  20.983  48.400 1.00 58.11  ? 115 VAL H C   1 
ATOM   13154 O  O   . VAL H  1 124 ? 28.087  21.453  49.492 1.00 56.75  ? 115 VAL H O   1 
ATOM   13155 C  CB  . VAL H  1 124 ? 26.049  19.229  48.624 1.00 53.73  ? 115 VAL H CB  1 
ATOM   13156 C  CG1 . VAL H  1 124 ? 25.103  20.123  47.793 1.00 44.10  ? 115 VAL H CG1 1 
ATOM   13157 C  CG2 . VAL H  1 124 ? 25.740  17.736  48.465 1.00 49.89  ? 115 VAL H CG2 1 
ATOM   13158 N  N   . GLN H  1 125 ? 27.643  21.712  47.298 1.00 56.44  ? 116 GLN H N   1 
ATOM   13159 C  CA  . GLN H  1 125 ? 27.810  23.151  47.342 1.00 53.46  ? 116 GLN H CA  1 
ATOM   13160 C  C   . GLN H  1 125 ? 26.748  23.842  46.507 1.00 47.26  ? 116 GLN H C   1 
ATOM   13161 O  O   . GLN H  1 125 ? 26.706  23.671  45.319 1.00 52.59  ? 116 GLN H O   1 
ATOM   13162 C  CB  . GLN H  1 125 ? 29.201  23.500  46.854 1.00 58.34  ? 116 GLN H CB  1 
ATOM   13163 C  CG  . GLN H  1 125 ? 29.407  24.959  46.593 1.00 76.78  ? 116 GLN H CG  1 
ATOM   13164 C  CD  . GLN H  1 125 ? 30.820  25.235  46.146 1.00 94.10  ? 116 GLN H CD  1 
ATOM   13165 O  OE1 . GLN H  1 125 ? 31.728  24.453  46.445 1.00 106.31 ? 116 GLN H OE1 1 
ATOM   13166 N  NE2 . GLN H  1 125 ? 31.022  26.337  45.420 1.00 80.16  ? 116 GLN H NE2 1 
ATOM   13167 N  N   . TYR H  1 126 ? 25.915  24.654  47.133 1.00 47.07  ? 117 TYR H N   1 
ATOM   13168 C  CA  . TYR H  1 126 ? 24.778  25.264  46.469 1.00 44.05  ? 117 TYR H CA  1 
ATOM   13169 C  C   . TYR H  1 126 ? 24.856  26.803  46.585 1.00 53.21  ? 117 TYR H C   1 
ATOM   13170 O  O   . TYR H  1 126 ? 25.111  27.338  47.657 1.00 53.88  ? 117 TYR H O   1 
ATOM   13171 C  CB  . TYR H  1 126 ? 23.511  24.689  47.089 1.00 38.43  ? 117 TYR H CB  1 
ATOM   13172 C  CG  . TYR H  1 126 ? 22.228  25.285  46.615 1.00 45.57  ? 117 TYR H CG  1 
ATOM   13173 C  CD1 . TYR H  1 126 ? 22.017  25.564  45.280 1.00 51.34  ? 117 TYR H CD1 1 
ATOM   13174 C  CD2 . TYR H  1 126 ? 21.205  25.538  47.500 1.00 56.89  ? 117 TYR H CD2 1 
ATOM   13175 C  CE1 . TYR H  1 126 ? 20.832  26.106  44.841 1.00 55.14  ? 117 TYR H CE1 1 
ATOM   13176 C  CE2 . TYR H  1 126 ? 20.006  26.079  47.068 1.00 63.40  ? 117 TYR H CE2 1 
ATOM   13177 C  CZ  . TYR H  1 126 ? 19.826  26.361  45.737 1.00 57.98  ? 117 TYR H CZ  1 
ATOM   13178 O  OH  . TYR H  1 126 ? 18.639  26.912  45.303 1.00 63.74  ? 117 TYR H OH  1 
ATOM   13179 N  N   . LEU H  1 127 ? 24.723  27.516  45.488 1.00 53.47  ? 118 LEU H N   1 
ATOM   13180 C  CA  . LEU H  1 127 ? 24.880  28.942  45.565 1.00 56.18  ? 118 LEU H CA  1 
ATOM   13181 C  C   . LEU H  1 127 ? 23.853  29.790  44.896 1.00 55.20  ? 118 LEU H C   1 
ATOM   13182 O  O   . LEU H  1 127 ? 24.129  30.376  43.894 1.00 59.88  ? 118 LEU H O   1 
ATOM   13183 C  CB  . LEU H  1 127 ? 26.216  29.283  44.967 1.00 58.09  ? 118 LEU H CB  1 
ATOM   13184 C  CG  . LEU H  1 127 ? 26.698  30.639  45.398 1.00 71.62  ? 118 LEU H CG  1 
ATOM   13185 C  CD1 . LEU H  1 127 ? 28.169  30.557  45.478 1.00 80.00  ? 118 LEU H CD1 1 
ATOM   13186 C  CD2 . LEU H  1 127 ? 26.261  31.632  44.391 1.00 77.58  ? 118 LEU H CD2 1 
ATOM   13187 N  N   . PRO H  1 128 ? 22.678  29.880  45.464 1.00 52.75  ? 119 PRO H N   1 
ATOM   13188 C  CA  . PRO H  1 128 ? 21.588  30.681  44.887 1.00 53.52  ? 119 PRO H CA  1 
ATOM   13189 C  C   . PRO H  1 128 ? 21.754  32.203  44.941 1.00 49.62  ? 119 PRO H C   1 
ATOM   13190 O  O   . PRO H  1 128 ? 22.105  32.738  45.981 1.00 50.84  ? 119 PRO H O   1 
ATOM   13191 C  CB  . PRO H  1 128 ? 20.367  30.259  45.715 1.00 60.21  ? 119 PRO H CB  1 
ATOM   13192 C  CG  . PRO H  1 128 ? 20.915  29.625  46.939 1.00 52.94  ? 119 PRO H CG  1 
ATOM   13193 C  CD  . PRO H  1 128 ? 22.204  29.004  46.547 1.00 51.89  ? 119 PRO H CD  1 
ATOM   13194 N  N   . ALA H  1 129 ? 21.476  32.890  43.834 1.00 52.38  ? 120 ALA H N   1 
ATOM   13195 C  CA  . ALA H  1 129 ? 21.427  34.354  43.848 1.00 55.55  ? 120 ALA H CA  1 
ATOM   13196 C  C   . ALA H  1 129 ? 20.014  34.756  44.210 1.00 53.47  ? 120 ALA H C   1 
ATOM   13197 O  O   . ALA H  1 129 ? 19.068  34.149  43.732 1.00 55.32  ? 120 ALA H O   1 
ATOM   13198 C  CB  . ALA H  1 129 ? 21.813  34.933  42.514 1.00 44.20  ? 120 ALA H CB  1 
ATOM   13199 N  N   . GLN H  1 130 ? 19.862  35.758  45.067 1.00 48.13  ? 121 GLN H N   1 
ATOM   13200 C  CA  . GLN H  1 130 ? 18.545  36.070  45.605 1.00 46.84  ? 121 GLN H CA  1 
ATOM   13201 C  C   . GLN H  1 130 ? 18.253  37.557  45.768 1.00 50.43  ? 121 GLN H C   1 
ATOM   13202 O  O   . GLN H  1 130 ? 19.140  38.359  46.073 1.00 50.66  ? 121 GLN H O   1 
ATOM   13203 C  CB  . GLN H  1 130 ? 18.355  35.375  46.949 1.00 48.59  ? 121 GLN H CB  1 
ATOM   13204 C  CG  . GLN H  1 130 ? 18.622  33.893  46.938 1.00 48.08  ? 121 GLN H CG  1 
ATOM   13205 C  CD  . GLN H  1 130 ? 18.081  33.239  48.175 1.00 53.82  ? 121 GLN H CD  1 
ATOM   13206 O  OE1 . GLN H  1 130 ? 18.099  33.833  49.252 1.00 56.18  ? 121 GLN H OE1 1 
ATOM   13207 N  NE2 . GLN H  1 130 ? 17.574  32.021  48.037 1.00 53.76  ? 121 GLN H NE2 1 
ATOM   13208 N  N   . ARG H  1 131 ? 16.990  37.907  45.562 1.00 46.20  ? 122 ARG H N   1 
ATOM   13209 C  CA  . ARG H  1 131 ? 16.512  39.222  45.912 1.00 47.07  ? 122 ARG H CA  1 
ATOM   13210 C  C   . ARG H  1 131 ? 15.560  39.103  47.092 1.00 47.63  ? 122 ARG H C   1 
ATOM   13211 O  O   . ARG H  1 131 ? 14.505  38.478  46.995 1.00 48.00  ? 122 ARG H O   1 
ATOM   13212 C  CB  . ARG H  1 131 ? 15.831  39.924  44.746 1.00 41.04  ? 122 ARG H CB  1 
ATOM   13213 C  CG  . ARG H  1 131 ? 15.476  41.360  45.099 1.00 52.10  ? 122 ARG H CG  1 
ATOM   13214 C  CD  . ARG H  1 131 ? 14.467  41.919  44.139 1.00 59.25  ? 122 ARG H CD  1 
ATOM   13215 N  NE  . ARG H  1 131 ? 13.924  43.207  44.559 1.00 53.44  ? 122 ARG H NE  1 
ATOM   13216 C  CZ  . ARG H  1 131 ? 14.133  44.340  43.907 1.00 59.96  ? 122 ARG H CZ  1 
ATOM   13217 N  NH1 . ARG H  1 131 ? 14.895  44.348  42.822 1.00 59.80  ? 122 ARG H NH1 1 
ATOM   13218 N  NH2 . ARG H  1 131 ? 13.577  45.459  44.335 1.00 60.89  ? 122 ARG H NH2 1 
ATOM   13219 N  N   . LEU H  1 132 ? 15.961  39.734  48.196 1.00 48.13  ? 123 LEU H N   1 
ATOM   13220 C  CA  . LEU H  1 132 ? 15.286  39.645  49.483 1.00 46.96  ? 123 LEU H CA  1 
ATOM   13221 C  C   . LEU H  1 132 ? 14.761  40.994  49.999 1.00 44.33  ? 123 LEU H C   1 
ATOM   13222 O  O   . LEU H  1 132 ? 15.467  41.987  49.976 1.00 44.39  ? 123 LEU H O   1 
ATOM   13223 C  CB  . LEU H  1 132 ? 16.254  39.048  50.508 1.00 48.01  ? 123 LEU H CB  1 
ATOM   13224 C  CG  . LEU H  1 132 ? 15.701  39.028  51.928 1.00 46.08  ? 123 LEU H CG  1 
ATOM   13225 C  CD1 . LEU H  1 132 ? 14.636  37.968  52.016 1.00 46.00  ? 123 LEU H CD1 1 
ATOM   13226 C  CD2 . LEU H  1 132 ? 16.807  38.793  52.924 1.00 46.86  ? 123 LEU H CD2 1 
ATOM   13227 N  N   . SER H  1 133 ? 13.512  41.020  50.449 1.00 50.07  ? 124 SER H N   1 
ATOM   13228 C  CA  . SER H  1 133 ? 12.966  42.178  51.150 1.00 47.93  ? 124 SER H CA  1 
ATOM   13229 C  C   . SER H  1 133 ? 12.867  41.846  52.639 1.00 53.21  ? 124 SER H C   1 
ATOM   13230 O  O   . SER H  1 133 ? 12.158  40.921  53.038 1.00 54.70  ? 124 SER H O   1 
ATOM   13231 C  CB  . SER H  1 133 ? 11.579  42.542  50.615 1.00 43.19  ? 124 SER H CB  1 
ATOM   13232 O  OG  . SER H  1 133 ? 11.682  43.453  49.550 1.00 46.57  ? 124 SER H OG  1 
ATOM   13233 N  N   . PHE H  1 134 ? 13.566  42.593  53.476 1.00 51.46  ? 125 PHE H N   1 
ATOM   13234 C  CA  . PHE H  1 134 ? 13.501  42.298  54.901 1.00 61.16  ? 125 PHE H CA  1 
ATOM   13235 C  C   . PHE H  1 134 ? 13.211  43.551  55.704 1.00 59.45  ? 125 PHE H C   1 
ATOM   13236 O  O   . PHE H  1 134 ? 13.268  44.658  55.173 1.00 59.84  ? 125 PHE H O   1 
ATOM   13237 C  CB  . PHE H  1 134 ? 14.769  41.586  55.386 1.00 57.18  ? 125 PHE H CB  1 
ATOM   13238 C  CG  . PHE H  1 134 ? 16.024  42.393  55.234 1.00 59.35  ? 125 PHE H CG  1 
ATOM   13239 C  CD1 . PHE H  1 134 ? 16.650  42.931  56.353 1.00 62.26  ? 125 PHE H CD1 1 
ATOM   13240 C  CD2 . PHE H  1 134 ? 16.589  42.607  53.979 1.00 58.85  ? 125 PHE H CD2 1 
ATOM   13241 C  CE1 . PHE H  1 134 ? 17.816  43.675  56.234 1.00 63.29  ? 125 PHE H CE1 1 
ATOM   13242 C  CE2 . PHE H  1 134 ? 17.757  43.348  53.842 1.00 61.10  ? 125 PHE H CE2 1 
ATOM   13243 C  CZ  . PHE H  1 134 ? 18.372  43.885  54.980 1.00 69.45  ? 125 PHE H CZ  1 
ATOM   13244 N  N   . MET H  1 135 ? 12.870  43.371  56.975 1.00 58.90  ? 126 MET H N   1 
ATOM   13245 C  CA  . MET H  1 135 ? 12.513  44.500  57.823 1.00 57.90  ? 126 MET H CA  1 
ATOM   13246 C  C   . MET H  1 135 ? 13.741  45.331  58.101 1.00 56.75  ? 126 MET H C   1 
ATOM   13247 O  O   . MET H  1 135 ? 14.734  44.833  58.629 1.00 61.94  ? 126 MET H O   1 
ATOM   13248 C  CB  . MET H  1 135 ? 11.949  43.986  59.139 1.00 52.21  ? 126 MET H CB  1 
ATOM   13249 C  CG  . MET H  1 135 ? 10.627  43.281  58.978 1.00 51.97  ? 126 MET H CG  1 
ATOM   13250 S  SD  . MET H  1 135 ? 10.355  42.138  60.316 1.00 53.77  ? 126 MET H SD  1 
ATOM   13251 C  CE  . MET H  1 135 ? 8.871   41.308  59.782 1.00 59.38  ? 126 MET H CE  1 
ATOM   13252 N  N   . CYS H  1 136 ? 13.676  46.595  57.704 1.00 60.02  ? 127 CYS H N   1 
ATOM   13253 C  CA  . CYS H  1 136 ? 14.738  47.538  58.007 1.00 63.44  ? 127 CYS H CA  1 
ATOM   13254 C  C   . CYS H  1 136 ? 14.325  49.026  58.059 1.00 66.55  ? 127 CYS H C   1 
ATOM   13255 O  O   . CYS H  1 136 ? 13.578  49.502  57.195 1.00 59.30  ? 127 CYS H O   1 
ATOM   13256 C  CB  . CYS H  1 136 ? 15.865  47.334  57.012 1.00 65.46  ? 127 CYS H CB  1 
ATOM   13257 S  SG  . CYS H  1 136 ? 17.055  48.580  57.149 1.00 62.94  ? 127 CYS H SG  1 
ATOM   13258 N  N   . ASP H  1 137 ? 14.879  49.747  59.013 1.00 69.07  ? 128 ASP H N   1 
ATOM   13259 C  CA  . ASP H  1 137 ? 14.684  51.173  59.093 1.00 65.69  ? 128 ASP H CA  1 
ATOM   13260 C  C   . ASP H  1 137 ? 15.978  51.829  58.657 1.00 64.08  ? 128 ASP H C   1 
ATOM   13261 O  O   . ASP H  1 137 ? 17.014  51.669  59.258 1.00 65.36  ? 128 ASP H O   1 
ATOM   13262 C  CB  . ASP H  1 137 ? 14.346  51.580  60.493 1.00 64.86  ? 128 ASP H CB  1 
ATOM   13263 C  CG  . ASP H  1 137 ? 14.078  53.006  60.584 1.00 69.36  ? 128 ASP H CG  1 
ATOM   13264 O  OD1 . ASP H  1 137 ? 14.038  53.621  59.523 1.00 68.85  ? 128 ASP H OD1 1 
ATOM   13265 O  OD2 . ASP H  1 137 ? 13.905  53.516  61.684 1.00 70.16  ? 128 ASP H OD2 1 
ATOM   13266 N  N   . PRO H  1 138 ? 15.894  52.566  57.579 1.00 65.07  ? 129 PRO H N   1 
ATOM   13267 C  CA  . PRO H  1 138 ? 17.035  53.134  56.885 1.00 70.46  ? 129 PRO H CA  1 
ATOM   13268 C  C   . PRO H  1 138 ? 17.405  54.539  57.303 1.00 73.91  ? 129 PRO H C   1 
ATOM   13269 O  O   . PRO H  1 138 ? 18.305  55.175  56.772 1.00 60.75  ? 129 PRO H O   1 
ATOM   13270 C  CB  . PRO H  1 138 ? 16.551  53.137  55.459 1.00 66.99  ? 129 PRO H CB  1 
ATOM   13271 C  CG  . PRO H  1 138 ? 15.108  53.288  55.564 1.00 63.58  ? 129 PRO H CG  1 
ATOM   13272 C  CD  . PRO H  1 138 ? 14.645  52.856  56.887 1.00 60.76  ? 129 PRO H CD  1 
ATOM   13273 N  N   . THR H  1 139 ? 16.684  55.020  58.280 1.00 75.67  ? 130 THR H N   1 
ATOM   13274 C  CA  . THR H  1 139 ? 16.899  56.326  58.767 1.00 68.86  ? 130 THR H CA  1 
ATOM   13275 C  C   . THR H  1 139 ? 18.371  56.430  59.048 1.00 73.18  ? 130 THR H C   1 
ATOM   13276 O  O   . THR H  1 139 ? 18.972  55.507  59.537 1.00 64.85  ? 130 THR H O   1 
ATOM   13277 C  CB  . THR H  1 139 ? 16.175  56.442  60.042 1.00 65.46  ? 130 THR H CB  1 
ATOM   13278 O  OG1 . THR H  1 139 ? 14.948  57.112  59.811 1.00 64.64  ? 130 THR H OG1 1 
ATOM   13279 C  CG2 . THR H  1 139 ? 16.962  57.197  60.977 1.00 63.81  ? 130 THR H CG2 1 
ATOM   13280 N  N   . GLY H  1 140 ? 18.952  57.566  58.700 1.00 67.16  ? 131 GLY H N   1 
ATOM   13281 C  CA  . GLY H  1 140 ? 20.379  57.799  58.846 1.00 64.84  ? 131 GLY H CA  1 
ATOM   13282 C  C   . GLY H  1 140 ? 21.143  57.590  57.552 1.00 65.99  ? 131 GLY H C   1 
ATOM   13283 O  O   . GLY H  1 140 ? 22.336  57.875  57.463 1.00 67.33  ? 131 GLY H O   1 
ATOM   13284 N  N   . VAL H  1 141 ? 20.449  57.082  56.540 1.00 70.46  ? 132 VAL H N   1 
ATOM   13285 C  CA  . VAL H  1 141 ? 21.097  56.676  55.295 1.00 72.00  ? 132 VAL H CA  1 
ATOM   13286 C  C   . VAL H  1 141 ? 21.626  57.869  54.499 1.00 71.55  ? 132 VAL H C   1 
ATOM   13287 O  O   . VAL H  1 141 ? 22.706  57.797  53.918 1.00 72.36  ? 132 VAL H O   1 
ATOM   13288 C  CB  . VAL H  1 141 ? 20.176  55.761  54.431 1.00 65.89  ? 132 VAL H CB  1 
ATOM   13289 C  CG1 . VAL H  1 141 ? 18.950  56.505  53.965 1.00 61.53  ? 132 VAL H CG1 1 
ATOM   13290 C  CG2 . VAL H  1 141 ? 20.941  55.182  53.266 1.00 63.67  ? 132 VAL H CG2 1 
ATOM   13291 N  N   . ASP H  1 142 ? 20.875  58.968  54.496 1.00 73.59  ? 133 ASP H N   1 
ATOM   13292 C  CA  . ASP H  1 142 ? 21.296  60.191  53.809 1.00 75.31  ? 133 ASP H CA  1 
ATOM   13293 C  C   . ASP H  1 142 ? 22.424  60.888  54.559 1.00 76.53  ? 133 ASP H C   1 
ATOM   13294 O  O   . ASP H  1 142 ? 23.114  61.741  54.008 1.00 79.12  ? 133 ASP H O   1 
ATOM   13295 C  CB  . ASP H  1 142 ? 20.120  61.142  53.641 1.00 75.08  ? 133 ASP H CB  1 
ATOM   13296 C  CG  . ASP H  1 142 ? 19.280  61.240  54.891 1.00 84.50  ? 133 ASP H CG  1 
ATOM   13297 O  OD1 . ASP H  1 142 ? 19.794  60.917  55.991 1.00 77.16  ? 133 ASP H OD1 1 
ATOM   13298 O  OD2 . ASP H  1 142 ? 18.102  61.642  54.767 1.00 91.88  ? 133 ASP H OD2 1 
ATOM   13299 N  N   . SER H  1 143 ? 22.602  60.514  55.819 1.00 76.61  ? 134 SER H N   1 
ATOM   13300 C  CA  . SER H  1 143 ? 23.715  61.000  56.608 1.00 72.91  ? 134 SER H CA  1 
ATOM   13301 C  C   . SER H  1 143 ? 25.000  60.329  56.137 1.00 77.41  ? 134 SER H C   1 
ATOM   13302 O  O   . SER H  1 143 ? 24.971  59.452  55.277 1.00 76.99  ? 134 SER H O   1 
ATOM   13303 C  CB  . SER H  1 143 ? 23.447  60.676  58.080 1.00 80.91  ? 134 SER H CB  1 
ATOM   13304 O  OG  . SER H  1 143 ? 24.625  60.605  58.869 1.00 92.22  ? 134 SER H OG  1 
ATOM   13305 N  N   . GLU H  1 144 ? 26.123  60.728  56.723 1.00 85.57  ? 135 GLU H N   1 
ATOM   13306 C  CA  . GLU H  1 144 ? 27.435  60.168  56.394 1.00 88.68  ? 135 GLU H CA  1 
ATOM   13307 C  C   . GLU H  1 144 ? 27.740  58.993  57.317 1.00 92.63  ? 135 GLU H C   1 
ATOM   13308 O  O   . GLU H  1 144 ? 28.734  58.281  57.134 1.00 89.99  ? 135 GLU H O   1 
ATOM   13309 C  CB  . GLU H  1 144 ? 28.530  61.233  56.522 1.00 85.94  ? 135 GLU H CB  1 
ATOM   13310 C  CG  . GLU H  1 144 ? 28.218  62.574  55.829 1.00 103.18 ? 135 GLU H CG  1 
ATOM   13311 C  CD  . GLU H  1 144 ? 27.433  63.561  56.716 1.00 110.87 ? 135 GLU H CD  1 
ATOM   13312 O  OE1 . GLU H  1 144 ? 27.949  64.669  57.000 1.00 96.27  ? 135 GLU H OE1 1 
ATOM   13313 O  OE2 . GLU H  1 144 ? 26.293  63.240  57.121 1.00 107.50 ? 135 GLU H OE2 1 
ATOM   13314 N  N   . GLU H  1 145 ? 26.879  58.815  58.320 1.00 92.09  ? 136 GLU H N   1 
ATOM   13315 C  CA  A GLU H  1 145 ? 27.023  57.731  59.282 0.60 86.15  ? 136 GLU H CA  1 
ATOM   13316 C  CA  B GLU H  1 145 ? 27.008  57.731  59.288 0.40 86.18  ? 136 GLU H CA  1 
ATOM   13317 C  C   . GLU H  1 145 ? 26.233  56.487  58.861 1.00 81.51  ? 136 GLU H C   1 
ATOM   13318 O  O   . GLU H  1 145 ? 26.397  55.416  59.427 1.00 76.36  ? 136 GLU H O   1 
ATOM   13319 C  CB  A GLU H  1 145 ? 26.589  58.226  60.665 0.60 88.80  ? 136 GLU H CB  1 
ATOM   13320 C  CB  B GLU H  1 145 ? 26.520  58.202  60.658 0.40 88.80  ? 136 GLU H CB  1 
ATOM   13321 C  CG  A GLU H  1 145 ? 27.424  59.412  61.161 0.60 96.29  ? 136 GLU H CG  1 
ATOM   13322 C  CG  B GLU H  1 145 ? 27.274  59.398  61.189 0.40 96.18  ? 136 GLU H CG  1 
ATOM   13323 C  CD  A GLU H  1 145 ? 26.589  60.473  61.864 0.60 96.84  ? 136 GLU H CD  1 
ATOM   13324 C  CD  B GLU H  1 145 ? 28.765  59.150  61.261 0.40 95.91  ? 136 GLU H CD  1 
ATOM   13325 O  OE1 A GLU H  1 145 ? 27.008  61.649  61.900 0.60 90.22  ? 136 GLU H OE1 1 
ATOM   13326 O  OE1 B GLU H  1 145 ? 29.168  58.084  61.778 0.40 91.32  ? 136 GLU H OE1 1 
ATOM   13327 O  OE2 A GLU H  1 145 ? 25.511  60.129  62.384 0.60 99.10  ? 136 GLU H OE2 1 
ATOM   13328 O  OE2 B GLU H  1 145 ? 29.532  60.023  60.799 0.40 94.12  ? 136 GLU H OE2 1 
ATOM   13329 N  N   . GLY H  1 146 ? 25.393  56.635  57.843 1.00 81.22  ? 137 GLY H N   1 
ATOM   13330 C  CA  . GLY H  1 146 ? 24.622  55.530  57.312 1.00 69.21  ? 137 GLY H CA  1 
ATOM   13331 C  C   . GLY H  1 146 ? 23.559  54.986  58.241 1.00 67.62  ? 137 GLY H C   1 
ATOM   13332 O  O   . GLY H  1 146 ? 23.373  55.478  59.353 1.00 64.84  ? 137 GLY H O   1 
ATOM   13333 N  N   . ALA H  1 147 ? 22.880  53.939  57.783 1.00 64.01  ? 138 ALA H N   1 
ATOM   13334 C  CA  . ALA H  1 147 ? 21.921  53.220  58.608 1.00 67.14  ? 138 ALA H CA  1 
ATOM   13335 C  C   . ALA H  1 147 ? 22.472  51.827  58.881 1.00 58.78  ? 138 ALA H C   1 
ATOM   13336 O  O   . ALA H  1 147 ? 23.354  51.353  58.174 1.00 55.54  ? 138 ALA H O   1 
ATOM   13337 C  CB  . ALA H  1 147 ? 20.569  53.134  57.924 1.00 61.31  ? 138 ALA H CB  1 
ATOM   13338 N  N   . THR H  1 148 ? 22.017  51.212  59.963 1.00 59.94  ? 139 THR H N   1 
ATOM   13339 C  CA  . THR H  1 148 ? 22.277  49.795  60.162 1.00 66.63  ? 139 THR H CA  1 
ATOM   13340 C  C   . THR H  1 148 ? 20.992  48.998  60.174 1.00 66.65  ? 139 THR H C   1 
ATOM   13341 O  O   . THR H  1 148 ? 20.046  49.337  60.898 1.00 62.21  ? 139 THR H O   1 
ATOM   13342 C  CB  . THR H  1 148 ? 23.037  49.475  61.459 1.00 51.64  ? 139 THR H CB  1 
ATOM   13343 O  OG1 . THR H  1 148 ? 24.347  50.025  61.386 1.00 59.54  ? 139 THR H OG1 1 
ATOM   13344 C  CG2 . THR H  1 148 ? 23.186  47.984  61.601 1.00 47.24  ? 139 THR H CG2 1 
ATOM   13345 N  N   . CYS H  1 149 ? 20.973  47.949  59.349 1.00 61.68  ? 140 CYS H N   1 
ATOM   13346 C  CA  . CYS H  1 149 ? 19.979  46.887  59.459 1.00 63.93  ? 140 CYS H CA  1 
ATOM   13347 C  C   . CYS H  1 149 ? 20.678  45.569  59.682 1.00 63.62  ? 140 CYS H C   1 
ATOM   13348 O  O   . CYS H  1 149 ? 21.858  45.399  59.357 1.00 59.50  ? 140 CYS H O   1 
ATOM   13349 C  CB  . CYS H  1 149 ? 19.136  46.773  58.204 1.00 62.78  ? 140 CYS H CB  1 
ATOM   13350 S  SG  . CYS H  1 149 ? 19.026  48.290  57.338 1.00 82.15  ? 140 CYS H SG  1 
ATOM   13351 N  N   . ALA H  1 150 ? 19.935  44.632  60.248 1.00 62.67  ? 141 ALA H N   1 
ATOM   13352 C  CA  . ALA H  1 150 ? 20.421  43.277  60.390 1.00 56.54  ? 141 ALA H CA  1 
ATOM   13353 C  C   . ALA H  1 150 ? 19.337  42.305  59.949 1.00 59.46  ? 141 ALA H C   1 
ATOM   13354 O  O   . ALA H  1 150 ? 18.135  42.589  60.074 1.00 57.12  ? 141 ALA H O   1 
ATOM   13355 C  CB  . ALA H  1 150 ? 20.830  43.016  61.810 1.00 59.87  ? 141 ALA H CB  1 
ATOM   13356 N  N   . VAL H  1 151 ? 19.770  41.171  59.406 1.00 55.44  ? 142 VAL H N   1 
ATOM   13357 C  CA  . VAL H  1 151 ? 18.852  40.101  59.020 1.00 54.04  ? 142 VAL H CA  1 
ATOM   13358 C  C   . VAL H  1 151 ? 19.400  38.723  59.419 1.00 54.04  ? 142 VAL H C   1 
ATOM   13359 O  O   . VAL H  1 151 ? 20.558  38.398  59.157 1.00 53.45  ? 142 VAL H O   1 
ATOM   13360 C  CB  . VAL H  1 151 ? 18.464  40.166  57.512 1.00 55.89  ? 142 VAL H CB  1 
ATOM   13361 C  CG1 . VAL H  1 151 ? 19.702  40.199  56.623 1.00 56.44  ? 142 VAL H CG1 1 
ATOM   13362 C  CG2 . VAL H  1 151 ? 17.531  39.012  57.152 1.00 47.81  ? 142 VAL H CG2 1 
ATOM   13363 N  N   . LYS H  1 152 ? 18.562  37.929  60.075 1.00 53.82  ? 143 LYS H N   1 
ATOM   13364 C  CA  . LYS H  1 152 ? 18.975  36.628  60.583 1.00 48.73  ? 143 LYS H CA  1 
ATOM   13365 C  C   . LYS H  1 152 ? 18.543  35.455  59.695 1.00 48.83  ? 143 LYS H C   1 
ATOM   13366 O  O   . LYS H  1 152 ? 17.406  35.375  59.242 1.00 54.40  ? 143 LYS H O   1 
ATOM   13367 C  CB  . LYS H  1 152 ? 18.469  36.444  62.014 1.00 51.47  ? 143 LYS H CB  1 
ATOM   13368 C  CG  . LYS H  1 152 ? 19.416  36.986  63.098 1.00 56.86  ? 143 LYS H CG  1 
ATOM   13369 C  CD  . LYS H  1 152 ? 18.834  36.830  64.515 1.00 65.89  ? 143 LYS H CD  1 
ATOM   13370 C  CE  . LYS H  1 152 ? 19.181  38.009  65.422 1.00 59.57  ? 143 LYS H CE  1 
ATOM   13371 N  NZ  . LYS H  1 152 ? 18.947  39.320  64.734 1.00 64.84  ? 143 LYS H NZ  1 
ATOM   13372 N  N   . PHE H  1 153 ? 19.481  34.554  59.446 1.00 50.09  ? 144 PHE H N   1 
ATOM   13373 C  CA  . PHE H  1 153 ? 19.241  33.331  58.688 1.00 50.93  ? 144 PHE H CA  1 
ATOM   13374 C  C   . PHE H  1 153 ? 19.450  32.089  59.563 1.00 49.75  ? 144 PHE H C   1 
ATOM   13375 O  O   . PHE H  1 153 ? 20.302  32.078  60.442 1.00 52.18  ? 144 PHE H O   1 
ATOM   13376 C  CB  . PHE H  1 153 ? 20.221  33.244  57.523 1.00 51.63  ? 144 PHE H CB  1 
ATOM   13377 C  CG  . PHE H  1 153 ? 20.046  34.312  56.486 1.00 49.35  ? 144 PHE H CG  1 
ATOM   13378 C  CD1 . PHE H  1 153 ? 19.353  34.049  55.319 1.00 49.33  ? 144 PHE H CD1 1 
ATOM   13379 C  CD2 . PHE H  1 153 ? 20.609  35.562  56.654 1.00 51.11  ? 144 PHE H CD2 1 
ATOM   13380 C  CE1 . PHE H  1 153 ? 19.207  35.017  54.369 1.00 51.84  ? 144 PHE H CE1 1 
ATOM   13381 C  CE2 . PHE H  1 153 ? 20.456  36.535  55.696 1.00 48.66  ? 144 PHE H CE2 1 
ATOM   13382 C  CZ  . PHE H  1 153 ? 19.758  36.259  54.556 1.00 48.07  ? 144 PHE H CZ  1 
ATOM   13383 N  N   . GLY H  1 154 ? 18.682  31.039  59.306 1.00 47.50  ? 145 GLY H N   1 
ATOM   13384 C  CA  . GLY H  1 154 ? 18.929  29.751  59.924 1.00 48.27  ? 145 GLY H CA  1 
ATOM   13385 C  C   . GLY H  1 154 ? 17.903  28.748  59.474 1.00 46.41  ? 145 GLY H C   1 
ATOM   13386 O  O   . GLY H  1 154 ? 17.024  29.072  58.703 1.00 51.18  ? 145 GLY H O   1 
ATOM   13387 N  N   . SER H  1 155 ? 17.989  27.524  59.948 1.00 42.89  ? 146 SER H N   1 
ATOM   13388 C  CA  . SER H  1 155 ? 16.982  26.565  59.546 1.00 45.66  ? 146 SER H CA  1 
ATOM   13389 C  C   . SER H  1 155 ? 15.646  27.010  60.093 1.00 45.43  ? 146 SER H C   1 
ATOM   13390 O  O   . SER H  1 155 ? 15.585  27.624  61.135 1.00 50.49  ? 146 SER H O   1 
ATOM   13391 C  CB  . SER H  1 155 ? 17.314  25.160  60.026 1.00 49.94  ? 146 SER H CB  1 
ATOM   13392 O  OG  . SER H  1 155 ? 16.253  24.292  59.716 1.00 49.82  ? 146 SER H OG  1 
ATOM   13393 N  N   . TRP H  1 156 ? 14.581  26.776  59.343 1.00 50.74  ? 147 TRP H N   1 
ATOM   13394 C  CA  . TRP H  1 156 ? 13.240  27.025  59.840 1.00 53.10  ? 147 TRP H CA  1 
ATOM   13395 C  C   . TRP H  1 156 ? 12.695  25.899  60.746 1.00 55.87  ? 147 TRP H C   1 
ATOM   13396 O  O   . TRP H  1 156 ? 12.126  26.152  61.796 1.00 56.02  ? 147 TRP H O   1 
ATOM   13397 C  CB  . TRP H  1 156 ? 12.301  27.314  58.672 1.00 47.13  ? 147 TRP H CB  1 
ATOM   13398 C  CG  . TRP H  1 156 ? 10.946  27.740  59.096 1.00 51.25  ? 147 TRP H CG  1 
ATOM   13399 C  CD1 . TRP H  1 156 ? 9.790   27.027  58.975 1.00 55.03  ? 147 TRP H CD1 1 
ATOM   13400 C  CD2 . TRP H  1 156 ? 10.590  28.974  59.721 1.00 54.90  ? 147 TRP H CD2 1 
ATOM   13401 N  NE1 . TRP H  1 156 ? 8.736   27.738  59.487 1.00 53.69  ? 147 TRP H NE1 1 
ATOM   13402 C  CE2 . TRP H  1 156 ? 9.203   28.943  59.953 1.00 58.02  ? 147 TRP H CE2 1 
ATOM   13403 C  CE3 . TRP H  1 156 ? 11.307  30.109  60.103 1.00 54.43  ? 147 TRP H CE3 1 
ATOM   13404 C  CZ2 . TRP H  1 156 ? 8.520   30.000  60.547 1.00 52.76  ? 147 TRP H CZ2 1 
ATOM   13405 C  CZ3 . TRP H  1 156 ? 10.628  31.150  60.686 1.00 53.44  ? 147 TRP H CZ3 1 
ATOM   13406 C  CH2 . TRP H  1 156 ? 9.252   31.090  60.904 1.00 52.74  ? 147 TRP H CH2 1 
ATOM   13407 N  N   . SER H  1 157 ? 12.834  24.657  60.308 1.00 58.30  ? 148 SER H N   1 
ATOM   13408 C  CA  . SER H  1 157 ? 12.294  23.524  61.058 1.00 57.03  ? 148 SER H CA  1 
ATOM   13409 C  C   . SER H  1 157 ? 13.262  22.716  61.945 1.00 57.61  ? 148 SER H C   1 
ATOM   13410 O  O   . SER H  1 157 ? 12.831  21.795  62.626 1.00 59.73  ? 148 SER H O   1 
ATOM   13411 C  CB  . SER H  1 157 ? 11.524  22.596  60.110 1.00 56.35  ? 148 SER H CB  1 
ATOM   13412 O  OG  . SER H  1 157 ? 10.249  23.135  59.819 1.00 53.91  ? 148 SER H OG  1 
ATOM   13413 N  N   . TYR H  1 158 ? 14.551  23.049  61.943 1.00 59.46  ? 149 TYR H N   1 
ATOM   13414 C  CA  . TYR H  1 158 ? 15.548  22.228  62.638 1.00 53.54  ? 149 TYR H CA  1 
ATOM   13415 C  C   . TYR H  1 158 ? 16.320  22.983  63.727 1.00 59.93  ? 149 TYR H C   1 
ATOM   13416 O  O   . TYR H  1 158 ? 16.884  24.061  63.485 1.00 62.57  ? 149 TYR H O   1 
ATOM   13417 C  CB  . TYR H  1 158 ? 16.562  21.646  61.651 1.00 48.39  ? 149 TYR H CB  1 
ATOM   13418 C  CG  . TYR H  1 158 ? 16.052  20.585  60.696 1.00 56.64  ? 149 TYR H CG  1 
ATOM   13419 C  CD1 . TYR H  1 158 ? 16.034  19.246  61.053 1.00 54.46  ? 149 TYR H CD1 1 
ATOM   13420 C  CD2 . TYR H  1 158 ? 15.637  20.920  59.410 1.00 58.48  ? 149 TYR H CD2 1 
ATOM   13421 C  CE1 . TYR H  1 158 ? 15.593  18.271  60.167 1.00 53.24  ? 149 TYR H CE1 1 
ATOM   13422 C  CE2 . TYR H  1 158 ? 15.193  19.954  58.519 1.00 53.13  ? 149 TYR H CE2 1 
ATOM   13423 C  CZ  . TYR H  1 158 ? 15.168  18.628  58.899 1.00 58.80  ? 149 TYR H CZ  1 
ATOM   13424 O  OH  . TYR H  1 158 ? 14.729  17.670  58.004 1.00 57.80  ? 149 TYR H OH  1 
ATOM   13425 N  N   . GLY H  1 159 ? 16.367  22.396  64.920 1.00 54.52  ? 150 GLY H N   1 
ATOM   13426 C  CA  . GLY H  1 159 ? 17.239  22.877  65.975 1.00 59.58  ? 150 GLY H CA  1 
ATOM   13427 C  C   . GLY H  1 159 ? 18.681  22.446  65.768 1.00 60.98  ? 150 GLY H C   1 
ATOM   13428 O  O   . GLY H  1 159 ? 18.957  21.554  64.974 1.00 56.10  ? 150 GLY H O   1 
ATOM   13429 N  N   . GLY H  1 160 ? 19.603  23.062  66.500 1.00 62.25  ? 151 GLY H N   1 
ATOM   13430 C  CA  . GLY H  1 160 ? 21.023  22.863  66.268 1.00 58.87  ? 151 GLY H CA  1 
ATOM   13431 C  C   . GLY H  1 160 ? 21.527  21.454  66.502 1.00 54.96  ? 151 GLY H C   1 
ATOM   13432 O  O   . GLY H  1 160 ? 22.658  21.125  66.148 1.00 52.04  ? 151 GLY H O   1 
ATOM   13433 N  N   . TRP H  1 161 ? 20.687  20.628  67.110 1.00 58.63  ? 152 TRP H N   1 
ATOM   13434 C  CA  . TRP H  1 161 ? 21.019  19.228  67.354 1.00 60.84  ? 152 TRP H CA  1 
ATOM   13435 C  C   . TRP H  1 161 ? 20.858  18.391  66.091 1.00 61.37  ? 152 TRP H C   1 
ATOM   13436 O  O   . TRP H  1 161 ? 21.387  17.282  65.999 1.00 64.35  ? 152 TRP H O   1 
ATOM   13437 C  CB  . TRP H  1 161 ? 20.130  18.654  68.455 1.00 62.40  ? 152 TRP H CB  1 
ATOM   13438 C  CG  . TRP H  1 161 ? 20.538  19.016  69.850 1.00 67.22  ? 152 TRP H CG  1 
ATOM   13439 C  CD1 . TRP H  1 161 ? 21.708  19.603  70.246 1.00 66.17  ? 152 TRP H CD1 1 
ATOM   13440 C  CD2 . TRP H  1 161 ? 19.767  18.814  71.041 1.00 74.68  ? 152 TRP H CD2 1 
ATOM   13441 N  NE1 . TRP H  1 161 ? 21.710  19.776  71.609 1.00 65.21  ? 152 TRP H NE1 1 
ATOM   13442 C  CE2 . TRP H  1 161 ? 20.532  19.297  72.122 1.00 70.17  ? 152 TRP H CE2 1 
ATOM   13443 C  CE3 . TRP H  1 161 ? 18.501  18.271  71.299 1.00 71.62  ? 152 TRP H CE3 1 
ATOM   13444 C  CZ2 . TRP H  1 161 ? 20.075  19.251  73.441 1.00 68.75  ? 152 TRP H CZ2 1 
ATOM   13445 C  CZ3 . TRP H  1 161 ? 18.048  18.226  72.613 1.00 72.79  ? 152 TRP H CZ3 1 
ATOM   13446 C  CH2 . TRP H  1 161 ? 18.834  18.714  73.665 1.00 70.27  ? 152 TRP H CH2 1 
ATOM   13447 N  N   . GLU H  1 162 ? 20.102  18.937  65.137 1.00 64.49  ? 153 GLU H N   1 
ATOM   13448 C  CA  . GLU H  1 162 ? 19.874  18.338  63.816 1.00 60.98  ? 153 GLU H CA  1 
ATOM   13449 C  C   . GLU H  1 162 ? 20.596  19.021  62.648 1.00 59.75  ? 153 GLU H C   1 
ATOM   13450 O  O   . GLU H  1 162 ? 21.173  18.355  61.789 1.00 61.34  ? 153 GLU H O   1 
ATOM   13451 C  CB  . GLU H  1 162 ? 18.395  18.406  63.412 1.00 55.33  ? 153 GLU H CB  1 
ATOM   13452 C  CG  . GLU H  1 162 ? 17.461  17.513  64.204 1.00 53.61  ? 153 GLU H CG  1 
ATOM   13453 C  CD  . GLU H  1 162 ? 17.174  18.039  65.602 1.00 67.32  ? 153 GLU H CD  1 
ATOM   13454 O  OE1 . GLU H  1 162 ? 16.922  19.249  65.748 1.00 67.11  ? 153 GLU H OE1 1 
ATOM   13455 O  OE2 . GLU H  1 162 ? 17.194  17.245  66.567 1.00 72.96  ? 153 GLU H OE2 1 
ATOM   13456 N  N   . ILE H  1 163 ? 20.516  20.351  62.606 1.00 55.10  ? 154 ILE H N   1 
ATOM   13457 C  CA  . ILE H  1 163 ? 21.343  21.198  61.741 1.00 60.59  ? 154 ILE H CA  1 
ATOM   13458 C  C   . ILE H  1 163 ? 22.223  22.158  62.548 1.00 61.03  ? 154 ILE H C   1 
ATOM   13459 O  O   . ILE H  1 163 ? 21.725  23.001  63.300 1.00 57.79  ? 154 ILE H O   1 
ATOM   13460 C  CB  . ILE H  1 163 ? 20.480  22.040  60.739 1.00 52.90  ? 154 ILE H CB  1 
ATOM   13461 C  CG1 . ILE H  1 163 ? 19.574  21.129  59.919 1.00 54.75  ? 154 ILE H CG1 1 
ATOM   13462 C  CG2 . ILE H  1 163 ? 21.361  22.879  59.815 1.00 44.62  ? 154 ILE H CG2 1 
ATOM   13463 C  CD1 . ILE H  1 163 ? 18.879  21.832  58.800 1.00 59.16  ? 154 ILE H CD1 1 
ATOM   13464 N  N   . ASP H  1 164 ? 23.531  22.045  62.387 1.00 53.60  ? 155 ASP H N   1 
ATOM   13465 C  CA  . ASP H  1 164 ? 24.402  23.013  63.017 1.00 59.27  ? 155 ASP H CA  1 
ATOM   13466 C  C   . ASP H  1 164 ? 24.942  24.030  62.010 1.00 59.45  ? 155 ASP H C   1 
ATOM   13467 O  O   . ASP H  1 164 ? 25.687  23.675  61.105 1.00 61.99  ? 155 ASP H O   1 
ATOM   13468 C  CB  . ASP H  1 164 ? 25.547  22.316  63.751 1.00 65.75  ? 155 ASP H CB  1 
ATOM   13469 C  CG  . ASP H  1 164 ? 26.319  23.263  64.654 1.00 76.65  ? 155 ASP H CG  1 
ATOM   13470 O  OD1 . ASP H  1 164 ? 25.705  24.198  65.240 1.00 66.78  ? 155 ASP H OD1 1 
ATOM   13471 O  OD2 . ASP H  1 164 ? 27.547  23.071  64.765 1.00 78.94  ? 155 ASP H OD2 1 
ATOM   13472 N  N   . LEU H  1 165 ? 24.562  25.294  62.185 1.00 57.72  ? 156 LEU H N   1 
ATOM   13473 C  CA  . LEU H  1 165 ? 25.072  26.394  61.372 1.00 60.27  ? 156 LEU H CA  1 
ATOM   13474 C  C   . LEU H  1 165 ? 26.504  26.808  61.706 1.00 63.32  ? 156 LEU H C   1 
ATOM   13475 O  O   . LEU H  1 165 ? 26.911  26.812  62.854 1.00 63.67  ? 156 LEU H O   1 
ATOM   13476 C  CB  . LEU H  1 165 ? 24.142  27.601  61.474 1.00 60.00  ? 156 LEU H CB  1 
ATOM   13477 C  CG  . LEU H  1 165 ? 22.857  27.413  60.666 1.00 60.89  ? 156 LEU H CG  1 
ATOM   13478 C  CD1 . LEU H  1 165 ? 21.792  28.378  61.094 1.00 63.45  ? 156 LEU H CD1 1 
ATOM   13479 C  CD2 . LEU H  1 165 ? 23.116  27.529  59.164 1.00 54.16  ? 156 LEU H CD2 1 
ATOM   13480 N  N   . LYS H  1 166 ? 27.261  27.150  60.674 1.00 63.68  ? 157 LYS H N   1 
ATOM   13481 C  CA  . LYS H  1 166 ? 28.654  27.542  60.810 1.00 63.50  ? 157 LYS H CA  1 
ATOM   13482 C  C   . LYS H  1 166 ? 28.954  28.522  59.702 1.00 60.43  ? 157 LYS H C   1 
ATOM   13483 O  O   . LYS H  1 166 ? 28.391  28.416  58.632 1.00 66.96  ? 157 LYS H O   1 
ATOM   13484 C  CB  . LYS H  1 166 ? 29.582  26.335  60.650 1.00 63.42  ? 157 LYS H CB  1 
ATOM   13485 C  CG  . LYS H  1 166 ? 29.511  25.311  61.764 1.00 62.12  ? 157 LYS H CG  1 
ATOM   13486 C  CD  . LYS H  1 166 ? 29.924  25.912  63.087 1.00 77.82  ? 157 LYS H CD  1 
ATOM   13487 C  CE  . LYS H  1 166 ? 30.223  24.819  64.103 1.00 85.32  ? 157 LYS H CE  1 
ATOM   13488 N  NZ  . LYS H  1 166 ? 30.239  25.325  65.514 1.00 85.14  ? 157 LYS H NZ  1 
ATOM   13489 N  N   . THR H  1 167 ? 29.837  29.475  59.959 1.00 63.73  ? 158 THR H N   1 
ATOM   13490 C  CA  . THR H  1 167 ? 30.317  30.382  58.928 1.00 69.13  ? 158 THR H CA  1 
ATOM   13491 C  C   . THR H  1 167 ? 31.822  30.346  59.021 1.00 78.56  ? 158 THR H C   1 
ATOM   13492 O  O   . THR H  1 167 ? 32.357  30.278  60.126 1.00 80.34  ? 158 THR H O   1 
ATOM   13493 C  CB  . THR H  1 167 ? 29.866  31.814  59.191 1.00 65.84  ? 158 THR H CB  1 
ATOM   13494 O  OG1 . THR H  1 167 ? 30.324  32.225  60.485 1.00 63.41  ? 158 THR H OG1 1 
ATOM   13495 C  CG2 . THR H  1 167 ? 28.357  31.913  59.142 1.00 62.19  ? 158 THR H CG2 1 
ATOM   13496 N  N   . ASP H  1 168 ? 32.518  30.394  57.888 1.00 81.15  ? 159 ASP H N   1 
ATOM   13497 C  CA  . ASP H  1 168 ? 33.975  30.269  57.939 1.00 87.82  ? 159 ASP H CA  1 
ATOM   13498 C  C   . ASP H  1 168 ? 34.705  31.602  58.101 1.00 77.18  ? 159 ASP H C   1 
ATOM   13499 O  O   . ASP H  1 168 ? 35.926  31.634  58.228 1.00 80.02  ? 159 ASP H O   1 
ATOM   13500 C  CB  . ASP H  1 168 ? 34.529  29.444  56.768 1.00 92.48  ? 159 ASP H CB  1 
ATOM   13501 C  CG  . ASP H  1 168 ? 35.622  28.460  57.213 1.00 110.95 ? 159 ASP H CG  1 
ATOM   13502 O  OD1 . ASP H  1 168 ? 35.726  28.181  58.433 1.00 114.36 ? 159 ASP H OD1 1 
ATOM   13503 O  OD2 . ASP H  1 168 ? 36.383  27.964  56.353 1.00 112.22 ? 159 ASP H OD2 1 
ATOM   13504 N  N   . THR H  1 169 ? 33.945  32.691  58.113 1.00 71.43  ? 160 THR H N   1 
ATOM   13505 C  CA  . THR H  1 169 ? 34.470  34.010  58.456 1.00 67.18  ? 160 THR H CA  1 
ATOM   13506 C  C   . THR H  1 169 ? 33.363  34.874  59.044 1.00 64.38  ? 160 THR H C   1 
ATOM   13507 O  O   . THR H  1 169 ? 32.191  34.587  58.851 1.00 62.29  ? 160 THR H O   1 
ATOM   13508 C  CB  . THR H  1 169 ? 35.072  34.727  57.240 1.00 68.33  ? 160 THR H CB  1 
ATOM   13509 O  OG1 . THR H  1 169 ? 35.330  36.098  57.575 1.00 65.44  ? 160 THR H OG1 1 
ATOM   13510 C  CG2 . THR H  1 169 ? 34.110  34.674  56.061 1.00 72.92  ? 160 THR H CG2 1 
ATOM   13511 N  N   . ASP H  1 170 ? 33.735  35.918  59.781 1.00 66.69  ? 161 ASP H N   1 
ATOM   13512 C  CA  . ASP H  1 170 ? 32.758  36.900  60.246 1.00 63.82  ? 161 ASP H CA  1 
ATOM   13513 C  C   . ASP H  1 170 ? 32.592  38.003  59.206 1.00 66.72  ? 161 ASP H C   1 
ATOM   13514 O  O   . ASP H  1 170 ? 31.781  38.915  59.382 1.00 67.44  ? 161 ASP H O   1 
ATOM   13515 C  CB  . ASP H  1 170 ? 33.162  37.503  61.590 1.00 63.79  ? 161 ASP H CB  1 
ATOM   13516 C  CG  . ASP H  1 170 ? 32.384  36.905  62.753 1.00 90.19  ? 161 ASP H CG  1 
ATOM   13517 O  OD1 . ASP H  1 170 ? 32.111  35.679  62.725 1.00 89.97  ? 161 ASP H OD1 1 
ATOM   13518 O  OD2 . ASP H  1 170 ? 32.035  37.661  63.695 1.00 93.03  ? 161 ASP H OD2 1 
ATOM   13519 N  N   . GLN H  1 171 ? 33.346  37.898  58.111 1.00 63.62  ? 162 GLN H N   1 
ATOM   13520 C  CA  . GLN H  1 171 ? 33.375  38.939  57.089 1.00 71.59  ? 162 GLN H CA  1 
ATOM   13521 C  C   . GLN H  1 171 ? 32.552  38.594  55.851 1.00 67.02  ? 162 GLN H C   1 
ATOM   13522 O  O   . GLN H  1 171 ? 32.926  37.709  55.082 1.00 66.89  ? 162 GLN H O   1 
ATOM   13523 C  CB  . GLN H  1 171 ? 34.823  39.213  56.661 1.00 73.92  ? 162 GLN H CB  1 
ATOM   13524 C  CG  . GLN H  1 171 ? 34.986  40.452  55.790 1.00 71.85  ? 162 GLN H CG  1 
ATOM   13525 C  CD  . GLN H  1 171 ? 34.640  41.734  56.538 1.00 85.75  ? 162 GLN H CD  1 
ATOM   13526 O  OE1 . GLN H  1 171 ? 35.185  42.006  57.615 1.00 90.70  ? 162 GLN H OE1 1 
ATOM   13527 N  NE2 . GLN H  1 171 ? 33.721  42.523  55.976 1.00 77.22  ? 162 GLN H NE2 1 
ATOM   13528 N  N   . VAL H  1 172 ? 31.447  39.308  55.654 1.00 60.62  ? 163 VAL H N   1 
ATOM   13529 C  CA  . VAL H  1 172 ? 30.682  39.229  54.405 1.00 68.06  ? 163 VAL H CA  1 
ATOM   13530 C  C   . VAL H  1 172 ? 31.559  39.641  53.213 1.00 64.37  ? 163 VAL H C   1 
ATOM   13531 O  O   . VAL H  1 172 ? 32.351  40.573  53.332 1.00 70.62  ? 163 VAL H O   1 
ATOM   13532 C  CB  . VAL H  1 172 ? 29.436  40.146  54.457 1.00 58.41  ? 163 VAL H CB  1 
ATOM   13533 C  CG1 . VAL H  1 172 ? 28.772  40.211  53.110 1.00 58.12  ? 163 VAL H CG1 1 
ATOM   13534 C  CG2 . VAL H  1 172 ? 28.464  39.666  55.502 1.00 55.19  ? 163 VAL H CG2 1 
ATOM   13535 N  N   . ASP H  1 173 ? 31.427  38.966  52.071 1.00 58.01  ? 164 ASP H N   1 
ATOM   13536 C  CA  . ASP H  1 173 ? 32.270  39.289  50.914 1.00 59.43  ? 164 ASP H CA  1 
ATOM   13537 C  C   . ASP H  1 173 ? 31.698  40.423  50.039 1.00 60.56  ? 164 ASP H C   1 
ATOM   13538 O  O   . ASP H  1 173 ? 30.620  40.307  49.461 1.00 61.23  ? 164 ASP H O   1 
ATOM   13539 C  CB  . ASP H  1 173 ? 32.520  38.029  50.086 1.00 56.66  ? 164 ASP H CB  1 
ATOM   13540 C  CG  . ASP H  1 173 ? 33.249  38.310  48.789 1.00 67.55  ? 164 ASP H CG  1 
ATOM   13541 O  OD1 . ASP H  1 173 ? 33.713  39.454  48.605 1.00 72.87  ? 164 ASP H OD1 1 
ATOM   13542 O  OD2 . ASP H  1 173 ? 33.361  37.381  47.953 1.00 65.32  ? 164 ASP H OD2 1 
ATOM   13543 N  N   . LEU H  1 174 ? 32.427  41.531  49.973 1.00 55.62  ? 165 LEU H N   1 
ATOM   13544 C  CA  . LEU H  1 174 ? 32.004  42.696  49.202 1.00 58.56  ? 165 LEU H CA  1 
ATOM   13545 C  C   . LEU H  1 174 ? 32.652  42.845  47.825 1.00 60.94  ? 165 LEU H C   1 
ATOM   13546 O  O   . LEU H  1 174 ? 32.348  43.791  47.090 1.00 54.34  ? 165 LEU H O   1 
ATOM   13547 C  CB  . LEU H  1 174 ? 32.233  43.960  50.022 1.00 56.12  ? 165 LEU H CB  1 
ATOM   13548 C  CG  . LEU H  1 174 ? 31.584  43.907  51.397 1.00 61.28  ? 165 LEU H CG  1 
ATOM   13549 C  CD1 . LEU H  1 174 ? 32.224  44.908  52.331 1.00 49.02  ? 165 LEU H CD1 1 
ATOM   13550 C  CD2 . LEU H  1 174 ? 30.083  44.130  51.255 1.00 64.29  ? 165 LEU H CD2 1 
ATOM   13551 N  N   . SER H  1 175 ? 33.557  41.937  47.485 1.00 54.99  ? 166 SER H N   1 
ATOM   13552 C  CA  . SER H  1 175 ? 34.371  42.127  46.295 1.00 58.06  ? 166 SER H CA  1 
ATOM   13553 C  C   . SER H  1 175 ? 33.536  42.239  45.005 1.00 61.34  ? 166 SER H C   1 
ATOM   13554 O  O   . SER H  1 175 ? 33.960  42.855  44.026 1.00 60.86  ? 166 SER H O   1 
ATOM   13555 C  CB  . SER H  1 175 ? 35.454  41.043  46.196 1.00 61.46  ? 166 SER H CB  1 
ATOM   13556 O  OG  . SER H  1 175 ? 34.913  39.732  46.235 1.00 58.26  ? 166 SER H OG  1 
ATOM   13557 N  N   . SER H  1 176 ? 32.351  41.638  45.012 1.00 64.65  ? 167 SER H N   1 
ATOM   13558 C  CA  . SER H  1 176 ? 31.452  41.658  43.856 1.00 61.42  ? 167 SER H CA  1 
ATOM   13559 C  C   . SER H  1 176 ? 30.398  42.755  43.926 1.00 59.89  ? 167 SER H C   1 
ATOM   13560 O  O   . SER H  1 176 ? 29.488  42.785  43.105 1.00 61.63  ? 167 SER H O   1 
ATOM   13561 C  CB  . SER H  1 176 ? 30.774  40.297  43.645 1.00 70.82  ? 167 SER H CB  1 
ATOM   13562 O  OG  . SER H  1 176 ? 31.705  39.296  43.265 1.00 67.43  ? 167 SER H OG  1 
ATOM   13563 N  N   . TYR H  1 177 ? 30.477  43.616  44.935 1.00 61.85  ? 168 TYR H N   1 
ATOM   13564 C  CA  . TYR H  1 177 ? 29.451  44.647  45.121 1.00 59.01  ? 168 TYR H CA  1 
ATOM   13565 C  C   . TYR H  1 177 ? 29.433  45.695  44.002 1.00 59.06  ? 168 TYR H C   1 
ATOM   13566 O  O   . TYR H  1 177 ? 30.481  46.093  43.487 1.00 58.96  ? 168 TYR H O   1 
ATOM   13567 C  CB  . TYR H  1 177 ? 29.561  45.317  46.499 1.00 58.29  ? 168 TYR H CB  1 
ATOM   13568 C  CG  . TYR H  1 177 ? 28.344  46.154  46.818 1.00 58.28  ? 168 TYR H CG  1 
ATOM   13569 C  CD1 . TYR H  1 177 ? 27.160  45.564  47.226 1.00 61.45  ? 168 TYR H CD1 1 
ATOM   13570 C  CD2 . TYR H  1 177 ? 28.368  47.525  46.689 1.00 54.11  ? 168 TYR H CD2 1 
ATOM   13571 C  CE1 . TYR H  1 177 ? 26.041  46.317  47.494 1.00 56.45  ? 168 TYR H CE1 1 
ATOM   13572 C  CE2 . TYR H  1 177 ? 27.253  48.282  46.957 1.00 54.58  ? 168 TYR H CE2 1 
ATOM   13573 C  CZ  . TYR H  1 177 ? 26.095  47.673  47.357 1.00 51.76  ? 168 TYR H CZ  1 
ATOM   13574 O  OH  . TYR H  1 177 ? 24.989  48.431  47.626 1.00 50.55  ? 168 TYR H OH  1 
ATOM   13575 N  N   . TYR H  1 178 ? 28.235  46.152  43.648 1.00 54.07  ? 169 TYR H N   1 
ATOM   13576 C  CA  . TYR H  1 178 ? 28.066  47.014  42.484 1.00 60.39  ? 169 TYR H CA  1 
ATOM   13577 C  C   . TYR H  1 178 ? 28.543  48.427  42.784 1.00 64.45  ? 169 TYR H C   1 
ATOM   13578 O  O   . TYR H  1 178 ? 27.964  49.124  43.621 1.00 61.11  ? 169 TYR H O   1 
ATOM   13579 C  CB  . TYR H  1 178 ? 26.583  47.043  42.092 1.00 62.82  ? 169 TYR H CB  1 
ATOM   13580 C  CG  . TYR H  1 178 ? 26.214  47.922  40.903 1.00 60.24  ? 169 TYR H CG  1 
ATOM   13581 C  CD1 . TYR H  1 178 ? 26.992  47.930  39.755 1.00 55.32  ? 169 TYR H CD1 1 
ATOM   13582 C  CD2 . TYR H  1 178 ? 25.053  48.698  40.923 1.00 53.16  ? 169 TYR H CD2 1 
ATOM   13583 C  CE1 . TYR H  1 178 ? 26.651  48.697  38.681 1.00 63.90  ? 169 TYR H CE1 1 
ATOM   13584 C  CE2 . TYR H  1 178 ? 24.699  49.473  39.854 1.00 52.60  ? 169 TYR H CE2 1 
ATOM   13585 C  CZ  . TYR H  1 178 ? 25.506  49.478  38.728 1.00 66.24  ? 169 TYR H CZ  1 
ATOM   13586 O  OH  . TYR H  1 178 ? 25.180  50.255  37.624 1.00 67.58  ? 169 TYR H OH  1 
ATOM   13587 N  N   . ALA H  1 179 ? 29.546  48.866  42.025 1.00 65.39  ? 170 ALA H N   1 
ATOM   13588 C  CA  . ALA H  1 179 ? 30.250  50.111  42.300 1.00 61.13  ? 170 ALA H CA  1 
ATOM   13589 C  C   . ALA H  1 179 ? 29.338  51.313  42.099 1.00 62.37  ? 170 ALA H C   1 
ATOM   13590 O  O   . ALA H  1 179 ? 29.552  52.385  42.678 1.00 61.24  ? 170 ALA H O   1 
ATOM   13591 C  CB  . ALA H  1 179 ? 31.474  50.215  41.411 1.00 55.61  ? 170 ALA H CB  1 
ATOM   13592 N  N   . SER H  1 180 ? 28.334  51.127  41.252 1.00 57.58  ? 171 SER H N   1 
ATOM   13593 C  CA  . SER H  1 180 ? 27.410  52.193  40.899 1.00 59.83  ? 171 SER H CA  1 
ATOM   13594 C  C   . SER H  1 180 ? 26.093  52.228  41.678 1.00 59.78  ? 171 SER H C   1 
ATOM   13595 O  O   . SER H  1 180 ? 25.202  52.987  41.319 1.00 62.00  ? 171 SER H O   1 
ATOM   13596 C  CB  . SER H  1 180 ? 27.184  52.240  39.391 1.00 63.83  ? 171 SER H CB  1 
ATOM   13597 O  OG  . SER H  1 180 ? 28.415  52.455  38.721 1.00 55.48  ? 171 SER H OG  1 
ATOM   13598 N  N   . SER H  1 181 ? 25.953  51.376  42.695 1.00 57.61  ? 172 SER H N   1 
ATOM   13599 C  CA  . SER H  1 181 ? 24.712  51.273  43.476 1.00 50.77  ? 172 SER H CA  1 
ATOM   13600 C  C   . SER H  1 181 ? 24.312  52.580  44.162 1.00 58.50  ? 172 SER H C   1 
ATOM   13601 O  O   . SER H  1 181 ? 25.171  53.391  44.504 1.00 65.76  ? 172 SER H O   1 
ATOM   13602 C  CB  . SER H  1 181 ? 24.826  50.160  44.525 1.00 55.14  ? 172 SER H CB  1 
ATOM   13603 O  OG  . SER H  1 181 ? 23.713  50.166  45.410 1.00 52.09  ? 172 SER H OG  1 
ATOM   13604 N  N   . LYS H  1 182 ? 23.008  52.779  44.365 1.00 56.62  ? 173 LYS H N   1 
ATOM   13605 C  CA  . LYS H  1 182 ? 22.506  54.011  44.972 1.00 53.02  ? 173 LYS H CA  1 
ATOM   13606 C  C   . LYS H  1 182 ? 22.972  54.117  46.406 1.00 59.37  ? 173 LYS H C   1 
ATOM   13607 O  O   . LYS H  1 182 ? 22.898  55.186  47.028 1.00 66.19  ? 173 LYS H O   1 
ATOM   13608 C  CB  . LYS H  1 182 ? 20.976  54.103  44.915 1.00 52.78  ? 173 LYS H CB  1 
ATOM   13609 C  CG  . LYS H  1 182 ? 20.401  54.495  43.554 1.00 64.56  ? 173 LYS H CG  1 
ATOM   13610 C  CD  . LYS H  1 182 ? 21.063  55.742  42.963 1.00 73.71  ? 173 LYS H CD  1 
ATOM   13611 C  CE  . LYS H  1 182 ? 20.498  57.031  43.562 1.00 73.30  ? 173 LYS H CE  1 
ATOM   13612 N  NZ  . LYS H  1 182 ? 19.064  57.240  43.206 1.00 69.32  ? 173 LYS H NZ  1 
ATOM   13613 N  N   . TYR H  1 183 ? 23.458  52.998  46.925 1.00 56.26  ? 174 TYR H N   1 
ATOM   13614 C  CA  . TYR H  1 183 ? 23.957  52.930  48.281 1.00 56.21  ? 174 TYR H CA  1 
ATOM   13615 C  C   . TYR H  1 183 ? 25.359  52.360  48.283 1.00 55.32  ? 174 TYR H C   1 
ATOM   13616 O  O   . TYR H  1 183 ? 25.733  51.661  47.359 1.00 58.32  ? 174 TYR H O   1 
ATOM   13617 C  CB  . TYR H  1 183 ? 23.014  52.076  49.106 1.00 56.59  ? 174 TYR H CB  1 
ATOM   13618 C  CG  . TYR H  1 183 ? 21.624  52.638  49.098 1.00 52.39  ? 174 TYR H CG  1 
ATOM   13619 C  CD1 . TYR H  1 183 ? 21.241  53.589  50.025 1.00 53.71  ? 174 TYR H CD1 1 
ATOM   13620 C  CD2 . TYR H  1 183 ? 20.705  52.244  48.147 1.00 53.82  ? 174 TYR H CD2 1 
ATOM   13621 C  CE1 . TYR H  1 183 ? 19.973  54.122  50.015 1.00 60.00  ? 174 TYR H CE1 1 
ATOM   13622 C  CE2 . TYR H  1 183 ? 19.431  52.770  48.128 1.00 57.94  ? 174 TYR H CE2 1 
ATOM   13623 C  CZ  . TYR H  1 183 ? 19.070  53.712  49.064 1.00 59.56  ? 174 TYR H CZ  1 
ATOM   13624 O  OH  . TYR H  1 183 ? 17.799  54.236  49.058 1.00 59.06  ? 174 TYR H OH  1 
ATOM   13625 N  N   . GLU H  1 184 ? 26.147  52.682  49.304 1.00 62.90  ? 175 GLU H N   1 
ATOM   13626 C  CA  . GLU H  1 184 ? 27.492  52.121  49.427 1.00 66.68  ? 175 GLU H CA  1 
ATOM   13627 C  C   . GLU H  1 184 ? 27.669  51.426  50.769 1.00 65.93  ? 175 GLU H C   1 
ATOM   13628 O  O   . GLU H  1 184 ? 27.086  51.836  51.779 1.00 65.96  ? 175 GLU H O   1 
ATOM   13629 C  CB  . GLU H  1 184 ? 28.570  53.189  49.224 1.00 71.25  ? 175 GLU H CB  1 
ATOM   13630 C  CG  . GLU H  1 184 ? 28.510  54.338  50.212 1.00 79.49  ? 175 GLU H CG  1 
ATOM   13631 C  CD  . GLU H  1 184 ? 29.641  55.336  50.006 1.00 93.42  ? 175 GLU H CD  1 
ATOM   13632 O  OE1 . GLU H  1 184 ? 30.509  55.069  49.138 1.00 95.98  ? 175 GLU H OE1 1 
ATOM   13633 O  OE2 . GLU H  1 184 ? 29.657  56.379  50.710 1.00 83.19  ? 175 GLU H OE2 1 
ATOM   13634 N  N   . ILE H  1 185 ? 28.471  50.370  50.779 1.00 56.07  ? 176 ILE H N   1 
ATOM   13635 C  CA  . ILE H  1 185 ? 28.587  49.550  51.974 1.00 63.06  ? 176 ILE H CA  1 
ATOM   13636 C  C   . ILE H  1 185 ? 29.719  50.044  52.875 1.00 61.38  ? 176 ILE H C   1 
ATOM   13637 O  O   . ILE H  1 185 ? 30.885  50.036  52.490 1.00 55.54  ? 176 ILE H O   1 
ATOM   13638 C  CB  . ILE H  1 185 ? 28.785  48.044  51.627 1.00 59.42  ? 176 ILE H CB  1 
ATOM   13639 C  CG1 . ILE H  1 185 ? 27.741  47.575  50.609 1.00 61.81  ? 176 ILE H CG1 1 
ATOM   13640 C  CG2 . ILE H  1 185 ? 28.741  47.182  52.880 1.00 57.53  ? 176 ILE H CG2 1 
ATOM   13641 C  CD1 . ILE H  1 185 ? 26.296  47.758  51.038 1.00 61.91  ? 176 ILE H CD1 1 
ATOM   13642 N  N   . LEU H  1 186 ? 29.368  50.498  54.073 1.00 61.85  ? 177 LEU H N   1 
ATOM   13643 C  CA  . LEU H  1 186 ? 30.384  50.878  55.043 1.00 62.56  ? 177 LEU H CA  1 
ATOM   13644 C  C   . LEU H  1 186 ? 30.989  49.636  55.706 1.00 67.27  ? 177 LEU H C   1 
ATOM   13645 O  O   . LEU H  1 186 ? 32.213  49.472  55.749 1.00 67.34  ? 177 LEU H O   1 
ATOM   13646 C  CB  . LEU H  1 186 ? 29.804  51.861  56.063 1.00 59.13  ? 177 LEU H CB  1 
ATOM   13647 C  CG  . LEU H  1 186 ? 29.200  53.112  55.407 1.00 59.48  ? 177 LEU H CG  1 
ATOM   13648 C  CD1 . LEU H  1 186 ? 28.399  53.947  56.393 1.00 60.91  ? 177 LEU H CD1 1 
ATOM   13649 C  CD2 . LEU H  1 186 ? 30.268  53.944  54.714 1.00 51.71  ? 177 LEU H CD2 1 
ATOM   13650 N  N   . SER H  1 187 ? 30.130  48.737  56.178 1.00 67.34  ? 178 SER H N   1 
ATOM   13651 C  CA  . SER H  1 187 ? 30.595  47.461  56.724 1.00 70.53  ? 178 SER H CA  1 
ATOM   13652 C  C   . SER H  1 187 ? 29.565  46.352  56.567 1.00 59.58  ? 178 SER H C   1 
ATOM   13653 O  O   . SER H  1 187 ? 28.358  46.582  56.616 1.00 56.56  ? 178 SER H O   1 
ATOM   13654 C  CB  . SER H  1 187 ? 30.959  47.602  58.204 1.00 62.34  ? 178 SER H CB  1 
ATOM   13655 O  OG  . SER H  1 187 ? 29.791  47.817  58.971 1.00 62.66  ? 178 SER H OG  1 
ATOM   13656 N  N   . ALA H  1 188 ? 30.055  45.139  56.380 1.00 62.77  ? 179 ALA H N   1 
ATOM   13657 C  CA  . ALA H  1 188 ? 29.177  43.982  56.321 1.00 62.73  ? 179 ALA H CA  1 
ATOM   13658 C  C   . ALA H  1 188 ? 29.749  42.805  57.113 1.00 61.80  ? 179 ALA H C   1 
ATOM   13659 O  O   . ALA H  1 188 ? 30.835  42.301  56.805 1.00 61.02  ? 179 ALA H O   1 
ATOM   13660 C  CB  . ALA H  1 188 ? 28.926  43.592  54.874 1.00 63.84  ? 179 ALA H CB  1 
ATOM   13661 N  N   . THR H  1 189 ? 29.011  42.363  58.129 1.00 62.42  ? 180 THR H N   1 
ATOM   13662 C  CA  . THR H  1 189 ? 29.426  41.204  58.925 1.00 64.24  ? 180 THR H CA  1 
ATOM   13663 C  C   . THR H  1 189 ? 28.404  40.075  58.849 1.00 60.86  ? 180 THR H C   1 
ATOM   13664 O  O   . THR H  1 189 ? 27.205  40.318  58.695 1.00 58.94  ? 180 THR H O   1 
ATOM   13665 C  CB  . THR H  1 189 ? 29.624  41.557  60.413 1.00 64.07  ? 180 THR H CB  1 
ATOM   13666 O  OG1 . THR H  1 189 ? 28.349  41.609  61.074 1.00 65.27  ? 180 THR H OG1 1 
ATOM   13667 C  CG2 . THR H  1 189 ? 30.369  42.891  60.574 1.00 60.81  ? 180 THR H CG2 1 
ATOM   13668 N  N   . GLN H  1 190 ? 28.887  38.840  58.932 1.00 63.22  ? 181 GLN H N   1 
ATOM   13669 C  CA  . GLN H  1 190 ? 28.008  37.686  59.130 1.00 66.29  ? 181 GLN H CA  1 
ATOM   13670 C  C   . GLN H  1 190 ? 28.366  37.011  60.464 1.00 66.04  ? 181 GLN H C   1 
ATOM   13671 O  O   . GLN H  1 190 ? 29.421  36.392  60.606 1.00 68.96  ? 181 GLN H O   1 
ATOM   13672 C  CB  . GLN H  1 190 ? 28.092  36.710  57.939 1.00 56.92  ? 181 GLN H CB  1 
ATOM   13673 C  CG  . GLN H  1 190 ? 29.457  36.086  57.734 1.00 57.48  ? 181 GLN H CG  1 
ATOM   13674 C  CD  . GLN H  1 190 ? 29.735  35.710  56.300 1.00 61.30  ? 181 GLN H CD  1 
ATOM   13675 O  OE1 . GLN H  1 190 ? 28.896  35.899  55.434 1.00 63.15  ? 181 GLN H OE1 1 
ATOM   13676 N  NE2 . GLN H  1 190 ? 30.922  35.177  56.039 1.00 63.64  ? 181 GLN H NE2 1 
ATOM   13677 N  N   . THR H  1 191 ? 27.472  37.119  61.440 1.00 62.27  ? 182 THR H N   1 
ATOM   13678 C  CA  . THR H  1 191 ? 27.793  36.689  62.796 1.00 65.44  ? 182 THR H CA  1 
ATOM   13679 C  C   . THR H  1 191 ? 26.970  35.500  63.265 1.00 58.46  ? 182 THR H C   1 
ATOM   13680 O  O   . THR H  1 191 ? 25.749  35.588  63.374 1.00 59.15  ? 182 THR H O   1 
ATOM   13681 C  CB  . THR H  1 191 ? 27.625  37.853  63.797 1.00 71.83  ? 182 THR H CB  1 
ATOM   13682 O  OG1 . THR H  1 191 ? 28.796  38.682  63.766 1.00 73.88  ? 182 THR H OG1 1 
ATOM   13683 C  CG2 . THR H  1 191 ? 27.390  37.323  65.232 1.00 68.76  ? 182 THR H CG2 1 
ATOM   13684 N  N   . ARG H  1 192 ? 27.641  34.394  63.556 1.00 56.94  ? 183 ARG H N   1 
ATOM   13685 C  CA  . ARG H  1 192 ? 26.946  33.223  64.068 1.00 55.13  ? 183 ARG H CA  1 
ATOM   13686 C  C   . ARG H  1 192 ? 26.641  33.292  65.575 1.00 59.24  ? 183 ARG H C   1 
ATOM   13687 O  O   . ARG H  1 192 ? 27.482  33.673  66.387 1.00 67.94  ? 183 ARG H O   1 
ATOM   13688 C  CB  . ARG H  1 192 ? 27.742  31.964  63.761 1.00 55.34  ? 183 ARG H CB  1 
ATOM   13689 C  CG  . ARG H  1 192 ? 27.344  30.837  64.664 1.00 58.13  ? 183 ARG H CG  1 
ATOM   13690 C  CD  . ARG H  1 192 ? 28.000  29.568  64.292 1.00 61.83  ? 183 ARG H CD  1 
ATOM   13691 N  NE  . ARG H  1 192 ? 27.151  28.503  64.774 1.00 70.68  ? 183 ARG H NE  1 
ATOM   13692 C  CZ  . ARG H  1 192 ? 27.380  27.813  65.875 1.00 74.39  ? 183 ARG H CZ  1 
ATOM   13693 N  NH1 . ARG H  1 192 ? 28.465  28.062  66.594 1.00 78.45  ? 183 ARG H NH1 1 
ATOM   13694 N  NH2 . ARG H  1 192 ? 26.534  26.857  66.235 1.00 75.47  ? 183 ARG H NH2 1 
ATOM   13695 N  N   . SER H  1 193 ? 25.430  32.912  65.947 1.00 59.93  ? 184 SER H N   1 
ATOM   13696 C  CA  . SER H  1 193 ? 25.028  32.913  67.350 1.00 57.99  ? 184 SER H CA  1 
ATOM   13697 C  C   . SER H  1 193 ? 24.007  31.813  67.581 1.00 64.76  ? 184 SER H C   1 
ATOM   13698 O  O   . SER H  1 193 ? 23.412  31.300  66.634 1.00 68.51  ? 184 SER H O   1 
ATOM   13699 C  CB  . SER H  1 193 ? 24.457  34.270  67.765 1.00 61.75  ? 184 SER H CB  1 
ATOM   13700 O  OG  . SER H  1 193 ? 23.731  34.891  66.702 1.00 68.06  ? 184 SER H OG  1 
ATOM   13701 N  N   . GLU H  1 194 ? 23.820  31.447  68.843 1.00 71.19  ? 185 GLU H N   1 
ATOM   13702 C  CA  . GLU H  1 194 ? 22.951  30.338  69.227 1.00 66.30  ? 185 GLU H CA  1 
ATOM   13703 C  C   . GLU H  1 194 ? 21.990  30.893  70.242 1.00 66.39  ? 185 GLU H C   1 
ATOM   13704 O  O   . GLU H  1 194 ? 22.401  31.600  71.147 1.00 71.28  ? 185 GLU H O   1 
ATOM   13705 C  CB  . GLU H  1 194 ? 23.776  29.258  69.898 1.00 58.15  ? 185 GLU H CB  1 
ATOM   13706 C  CG  . GLU H  1 194 ? 23.260  27.880  69.704 1.00 63.91  ? 185 GLU H CG  1 
ATOM   13707 C  CD  . GLU H  1 194 ? 24.396  26.877  69.714 1.00 86.91  ? 185 GLU H CD  1 
ATOM   13708 O  OE1 . GLU H  1 194 ? 25.563  27.314  69.733 1.00 88.82  ? 185 GLU H OE1 1 
ATOM   13709 O  OE2 . GLU H  1 194 ? 24.142  25.657  69.699 1.00 95.06  ? 185 GLU H OE2 1 
ATOM   13710 N  N   . ARG H  1 195 ? 20.711  30.600  70.118 1.00 61.06  ? 186 ARG H N   1 
ATOM   13711 C  CA  . ARG H  1 195 ? 19.801  31.129  71.106 1.00 62.49  ? 186 ARG H CA  1 
ATOM   13712 C  C   . ARG H  1 195 ? 18.985  30.042  71.770 1.00 64.90  ? 186 ARG H C   1 
ATOM   13713 O  O   . ARG H  1 195 ? 18.635  29.052  71.148 1.00 64.58  ? 186 ARG H O   1 
ATOM   13714 C  CB  . ARG H  1 195 ? 18.930  32.245  70.532 1.00 66.44  ? 186 ARG H CB  1 
ATOM   13715 C  CG  . ARG H  1 195 ? 18.028  31.857  69.421 1.00 76.32  ? 186 ARG H CG  1 
ATOM   13716 C  CD  . ARG H  1 195 ? 16.882  32.812  69.397 1.00 81.56  ? 186 ARG H CD  1 
ATOM   13717 N  NE  . ARG H  1 195 ? 17.337  34.201  69.414 1.00 84.23  ? 186 ARG H NE  1 
ATOM   13718 C  CZ  . ARG H  1 195 ? 16.514  35.246  69.323 1.00 90.08  ? 186 ARG H CZ  1 
ATOM   13719 N  NH1 . ARG H  1 195 ? 15.203  35.049  69.217 1.00 87.56  ? 186 ARG H NH1 1 
ATOM   13720 N  NH2 . ARG H  1 195 ? 16.993  36.486  69.336 1.00 80.68  ? 186 ARG H NH2 1 
ATOM   13721 N  N   . PHE H  1 196 ? 18.698  30.227  73.053 1.00 71.26  ? 187 PHE H N   1 
ATOM   13722 C  CA  . PHE H  1 196 ? 17.958  29.226  73.802 1.00 71.22  ? 187 PHE H CA  1 
ATOM   13723 C  C   . PHE H  1 196 ? 16.619  29.772  74.182 1.00 70.14  ? 187 PHE H C   1 
ATOM   13724 O  O   . PHE H  1 196 ? 16.421  30.975  74.257 1.00 75.47  ? 187 PHE H O   1 
ATOM   13725 C  CB  . PHE H  1 196 ? 18.702  28.812  75.062 1.00 63.76  ? 187 PHE H CB  1 
ATOM   13726 C  CG  . PHE H  1 196 ? 19.885  27.950  74.803 1.00 57.31  ? 187 PHE H CG  1 
ATOM   13727 C  CD1 . PHE H  1 196 ? 21.097  28.515  74.431 1.00 57.15  ? 187 PHE H CD1 1 
ATOM   13728 C  CD2 . PHE H  1 196 ? 19.788  26.576  74.919 1.00 54.80  ? 187 PHE H CD2 1 
ATOM   13729 C  CE1 . PHE H  1 196 ? 22.193  27.725  74.191 1.00 51.96  ? 187 PHE H CE1 1 
ATOM   13730 C  CE2 . PHE H  1 196 ? 20.880  25.774  74.680 1.00 58.05  ? 187 PHE H CE2 1 
ATOM   13731 C  CZ  . PHE H  1 196 ? 22.086  26.350  74.312 1.00 57.26  ? 187 PHE H CZ  1 
ATOM   13732 N  N   . TYR H  1 197 ? 15.688  28.868  74.397 1.00 74.89  ? 188 TYR H N   1 
ATOM   13733 C  CA  . TYR H  1 197 ? 14.387  29.265  74.862 1.00 86.21  ? 188 TYR H CA  1 
ATOM   13734 C  C   . TYR H  1 197 ? 14.084  28.520  76.158 1.00 88.21  ? 188 TYR H C   1 
ATOM   13735 O  O   . TYR H  1 197 ? 14.729  27.519  76.476 1.00 84.66  ? 188 TYR H O   1 
ATOM   13736 C  CB  . TYR H  1 197 ? 13.349  28.990  73.775 1.00 100.45 ? 188 TYR H CB  1 
ATOM   13737 C  CG  . TYR H  1 197 ? 13.529  29.836  72.525 1.00 93.55  ? 188 TYR H CG  1 
ATOM   13738 C  CD1 . TYR H  1 197 ? 13.881  29.259  71.305 1.00 94.91  ? 188 TYR H CD1 1 
ATOM   13739 C  CD2 . TYR H  1 197 ? 13.342  31.214  72.571 1.00 97.88  ? 188 TYR H CD2 1 
ATOM   13740 C  CE1 . TYR H  1 197 ? 14.041  30.042  70.162 1.00 97.46  ? 188 TYR H CE1 1 
ATOM   13741 C  CE2 . TYR H  1 197 ? 13.498  32.001  71.444 1.00 97.50  ? 188 TYR H CE2 1 
ATOM   13742 C  CZ  . TYR H  1 197 ? 13.847  31.416  70.243 1.00 101.67 ? 188 TYR H CZ  1 
ATOM   13743 O  OH  . TYR H  1 197 ? 13.997  32.216  69.130 1.00 90.48  ? 188 TYR H OH  1 
ATOM   13744 N  N   . GLU H  1 198 ? 13.129  29.027  76.927 1.00 92.90  ? 189 GLU H N   1 
ATOM   13745 C  CA  . GLU H  1 198 ? 12.787  28.398  78.189 1.00 95.44  ? 189 GLU H CA  1 
ATOM   13746 C  C   . GLU H  1 198 ? 12.247  26.997  77.933 1.00 93.42  ? 189 GLU H C   1 
ATOM   13747 O  O   . GLU H  1 198 ? 12.430  26.090  78.746 1.00 93.31  ? 189 GLU H O   1 
ATOM   13748 C  CB  . GLU H  1 198 ? 11.779  29.243  78.965 1.00 107.02 ? 189 GLU H CB  1 
ATOM   13749 C  CG  . GLU H  1 198 ? 10.553  29.658  78.178 1.00 114.44 ? 189 GLU H CG  1 
ATOM   13750 C  CD  . GLU H  1 198 ? 9.530   30.362  79.047 1.00 123.40 ? 189 GLU H CD  1 
ATOM   13751 O  OE1 . GLU H  1 198 ? 8.897   29.685  79.884 1.00 122.38 ? 189 GLU H OE1 1 
ATOM   13752 O  OE2 . GLU H  1 198 ? 9.367   31.592  78.903 1.00 113.90 ? 189 GLU H OE2 1 
ATOM   13753 N  N   . CYS H  1 199 ? 11.610  26.828  76.780 1.00 91.46  ? 190 CYS H N   1 
ATOM   13754 C  CA  . CYS H  1 199 ? 11.000  25.557  76.396 1.00 98.46  ? 190 CYS H CA  1 
ATOM   13755 C  C   . CYS H  1 199 ? 11.982  24.391  76.195 1.00 92.02  ? 190 CYS H C   1 
ATOM   13756 O  O   . CYS H  1 199 ? 11.662  23.238  76.499 1.00 80.80  ? 190 CYS H O   1 
ATOM   13757 C  CB  . CYS H  1 199 ? 10.201  25.741  75.103 1.00 99.65  ? 190 CYS H CB  1 
ATOM   13758 S  SG  . CYS H  1 199 ? 11.133  25.323  73.589 1.00 105.09 ? 190 CYS H SG  1 
ATOM   13759 N  N   . CYS H  1 200 ? 13.166  24.685  75.666 1.00 94.93  ? 191 CYS H N   1 
ATOM   13760 C  CA  . CYS H  1 200 ? 14.062  23.625  75.212 1.00 91.68  ? 191 CYS H CA  1 
ATOM   13761 C  C   . CYS H  1 200 ? 15.508  23.834  75.624 1.00 75.92  ? 191 CYS H C   1 
ATOM   13762 O  O   . CYS H  1 200 ? 15.981  24.958  75.744 1.00 70.17  ? 191 CYS H O   1 
ATOM   13763 C  CB  . CYS H  1 200 ? 13.998  23.494  73.687 1.00 85.77  ? 191 CYS H CB  1 
ATOM   13764 S  SG  . CYS H  1 200 ? 12.372  23.815  72.994 1.00 104.19 ? 191 CYS H SG  1 
ATOM   13765 N  N   . LYS H  1 201 ? 16.208  22.727  75.821 1.00 73.17  ? 192 LYS H N   1 
ATOM   13766 C  CA  . LYS H  1 201 ? 17.629  22.765  76.096 1.00 73.81  ? 192 LYS H CA  1 
ATOM   13767 C  C   . LYS H  1 201 ? 18.465  22.665  74.824 1.00 75.55  ? 192 LYS H C   1 
ATOM   13768 O  O   . LYS H  1 201 ? 19.687  22.851  74.873 1.00 75.01  ? 192 LYS H O   1 
ATOM   13769 C  CB  . LYS H  1 201 ? 18.007  21.649  77.067 1.00 85.70  ? 192 LYS H CB  1 
ATOM   13770 C  CG  . LYS H  1 201 ? 19.468  21.679  77.485 1.00 101.60 ? 192 LYS H CG  1 
ATOM   13771 C  CD  . LYS H  1 201 ? 19.816  22.954  78.244 1.00 95.53  ? 192 LYS H CD  1 
ATOM   13772 C  CE  . LYS H  1 201 ? 19.141  22.972  79.599 1.00 100.54 ? 192 LYS H CE  1 
ATOM   13773 N  NZ  . LYS H  1 201 ? 19.701  24.048  80.457 1.00 98.18  ? 192 LYS H NZ  1 
ATOM   13774 N  N   . GLU H  1 202 ? 17.802  22.378  73.696 1.00 74.50  ? 193 GLU H N   1 
ATOM   13775 C  CA  . GLU H  1 202 ? 18.439  22.337  72.365 1.00 66.12  ? 193 GLU H CA  1 
ATOM   13776 C  C   . GLU H  1 202 ? 18.656  23.728  71.781 1.00 64.73  ? 193 GLU H C   1 
ATOM   13777 O  O   . GLU H  1 202 ? 17.738  24.542  71.759 1.00 67.18  ? 193 GLU H O   1 
ATOM   13778 C  CB  . GLU H  1 202 ? 17.576  21.551  71.387 1.00 69.55  ? 193 GLU H CB  1 
ATOM   13779 C  CG  . GLU H  1 202 ? 18.112  21.512  69.954 1.00 69.64  ? 193 GLU H CG  1 
ATOM   13780 C  CD  . GLU H  1 202 ? 17.047  21.110  68.939 1.00 73.87  ? 193 GLU H CD  1 
ATOM   13781 O  OE1 . GLU H  1 202 ? 15.896  21.568  69.109 1.00 77.27  ? 193 GLU H OE1 1 
ATOM   13782 O  OE2 . GLU H  1 202 ? 17.352  20.346  67.986 1.00 63.18  ? 193 GLU H OE2 1 
ATOM   13783 N  N   . PRO H  1 203 ? 19.866  23.994  71.274 1.00 64.40  ? 194 PRO H N   1 
ATOM   13784 C  CA  . PRO H  1 203 ? 20.244  25.313  70.747 1.00 57.68  ? 194 PRO H CA  1 
ATOM   13785 C  C   . PRO H  1 203 ? 19.581  25.617  69.408 1.00 56.82  ? 194 PRO H C   1 
ATOM   13786 O  O   . PRO H  1 203 ? 19.311  24.684  68.661 1.00 57.55  ? 194 PRO H O   1 
ATOM   13787 C  CB  . PRO H  1 203 ? 21.744  25.180  70.523 1.00 56.07  ? 194 PRO H CB  1 
ATOM   13788 C  CG  . PRO H  1 203 ? 22.136  23.786  70.941 1.00 56.59  ? 194 PRO H CG  1 
ATOM   13789 C  CD  . PRO H  1 203 ? 20.911  22.979  71.069 1.00 60.41  ? 194 PRO H CD  1 
ATOM   13790 N  N   . TYR H  1 204 ? 19.334  26.889  69.103 1.00 57.81  ? 195 TYR H N   1 
ATOM   13791 C  CA  . TYR H  1 204 ? 18.798  27.280  67.791 1.00 54.79  ? 195 TYR H CA  1 
ATOM   13792 C  C   . TYR H  1 204 ? 19.677  28.305  67.095 1.00 54.25  ? 195 TYR H C   1 
ATOM   13793 O  O   . TYR H  1 204 ? 19.428  29.504  67.185 1.00 56.96  ? 195 TYR H O   1 
ATOM   13794 C  CB  . TYR H  1 204 ? 17.341  27.756  67.879 1.00 59.09  ? 195 TYR H CB  1 
ATOM   13795 C  CG  . TYR H  1 204 ? 16.447  26.651  68.361 1.00 69.19  ? 195 TYR H CG  1 
ATOM   13796 C  CD1 . TYR H  1 204 ? 15.829  25.784  67.473 1.00 71.16  ? 195 TYR H CD1 1 
ATOM   13797 C  CD2 . TYR H  1 204 ? 16.269  26.434  69.717 1.00 76.23  ? 195 TYR H CD2 1 
ATOM   13798 C  CE1 . TYR H  1 204 ? 15.026  24.735  67.936 1.00 77.46  ? 195 TYR H CE1 1 
ATOM   13799 C  CE2 . TYR H  1 204 ? 15.478  25.397  70.191 1.00 83.70  ? 195 TYR H CE2 1 
ATOM   13800 C  CZ  . TYR H  1 204 ? 14.860  24.544  69.306 1.00 83.00  ? 195 TYR H CZ  1 
ATOM   13801 O  OH  . TYR H  1 204 ? 14.078  23.519  69.816 1.00 66.73  ? 195 TYR H OH  1 
ATOM   13802 N  N   . PRO H  1 205 ? 20.682  27.820  66.349 1.00 53.84  ? 196 PRO H N   1 
ATOM   13803 C  CA  . PRO H  1 205 ? 21.717  28.641  65.728 1.00 53.83  ? 196 PRO H CA  1 
ATOM   13804 C  C   . PRO H  1 205 ? 21.164  29.558  64.665 1.00 55.55  ? 196 PRO H C   1 
ATOM   13805 O  O   . PRO H  1 205 ? 20.031  29.392  64.227 1.00 59.97  ? 196 PRO H O   1 
ATOM   13806 C  CB  . PRO H  1 205 ? 22.665  27.617  65.108 1.00 47.35  ? 196 PRO H CB  1 
ATOM   13807 C  CG  . PRO H  1 205 ? 21.911  26.420  64.996 1.00 49.32  ? 196 PRO H CG  1 
ATOM   13808 C  CD  . PRO H  1 205 ? 20.838  26.402  66.001 1.00 46.17  ? 196 PRO H CD  1 
ATOM   13809 N  N   . ASP H  1 206 ? 21.974  30.518  64.249 1.00 55.90  ? 197 ASP H N   1 
ATOM   13810 C  CA  . ASP H  1 206 ? 21.600  31.384  63.156 1.00 52.18  ? 197 ASP H CA  1 
ATOM   13811 C  C   . ASP H  1 206 ? 22.758  32.266  62.795 1.00 57.70  ? 197 ASP H C   1 
ATOM   13812 O  O   . ASP H  1 206 ? 23.673  32.475  63.594 1.00 55.45  ? 197 ASP H O   1 
ATOM   13813 C  CB  . ASP H  1 206 ? 20.422  32.278  63.563 1.00 57.90  ? 197 ASP H CB  1 
ATOM   13814 C  CG  . ASP H  1 206 ? 20.801  33.350  64.591 1.00 61.56  ? 197 ASP H CG  1 
ATOM   13815 O  OD1 . ASP H  1 206 ? 21.795  34.080  64.404 1.00 59.29  ? 197 ASP H OD1 1 
ATOM   13816 O  OD2 . ASP H  1 206 ? 20.083  33.474  65.598 1.00 64.64  ? 197 ASP H OD2 1 
ATOM   13817 N  N   . VAL H  1 207 ? 22.696  32.799  61.581 1.00 52.38  ? 198 VAL H N   1 
ATOM   13818 C  CA  . VAL H  1 207 ? 23.701  33.719  61.108 1.00 49.62  ? 198 VAL H CA  1 
ATOM   13819 C  C   . VAL H  1 207 ? 23.021  35.058  61.051 1.00 49.83  ? 198 VAL H C   1 
ATOM   13820 O  O   . VAL H  1 207 ? 21.889  35.167  60.614 1.00 52.45  ? 198 VAL H O   1 
ATOM   13821 C  CB  . VAL H  1 207 ? 24.281  33.301  59.755 1.00 46.78  ? 198 VAL H CB  1 
ATOM   13822 C  CG1 . VAL H  1 207 ? 25.275  34.320  59.274 1.00 44.85  ? 198 VAL H CG1 1 
ATOM   13823 C  CG2 . VAL H  1 207 ? 24.957  31.951  59.894 1.00 48.67  ? 198 VAL H CG2 1 
ATOM   13824 N  N   . ASN H  1 208 ? 23.696  36.067  61.577 1.00 59.16  ? 199 ASN H N   1 
ATOM   13825 C  CA  . ASN H  1 208 ? 23.171  37.419  61.602 1.00 57.79  ? 199 ASN H CA  1 
ATOM   13826 C  C   . ASN H  1 208 ? 23.962  38.207  60.579 1.00 56.50  ? 199 ASN H C   1 
ATOM   13827 O  O   . ASN H  1 208 ? 25.176  38.349  60.704 1.00 62.37  ? 199 ASN H O   1 
ATOM   13828 C  CB  . ASN H  1 208 ? 23.303  38.017  63.012 1.00 52.59  ? 199 ASN H CB  1 
ATOM   13829 C  CG  . ASN H  1 208 ? 22.490  39.286  63.201 1.00 54.21  ? 199 ASN H CG  1 
ATOM   13830 O  OD1 . ASN H  1 208 ? 21.477  39.520  62.549 1.00 57.82  ? 199 ASN H OD1 1 
ATOM   13831 N  ND2 . ASN H  1 208 ? 22.942  40.115  64.106 1.00 58.21  ? 199 ASN H ND2 1 
ATOM   13832 N  N   . LEU H  1 209 ? 23.280  38.669  59.538 1.00 57.92  ? 200 LEU H N   1 
ATOM   13833 C  CA  . LEU H  1 209 ? 23.898  39.514  58.526 1.00 55.28  ? 200 LEU H CA  1 
ATOM   13834 C  C   . LEU H  1 209 ? 23.629  40.932  58.979 1.00 58.98  ? 200 LEU H C   1 
ATOM   13835 O  O   . LEU H  1 209 ? 22.478  41.370  59.024 1.00 61.81  ? 200 LEU H O   1 
ATOM   13836 C  CB  . LEU H  1 209 ? 23.260  39.262  57.156 1.00 52.68  ? 200 LEU H CB  1 
ATOM   13837 C  CG  . LEU H  1 209 ? 23.795  39.998  55.931 1.00 53.31  ? 200 LEU H CG  1 
ATOM   13838 C  CD1 . LEU H  1 209 ? 25.228  39.626  55.707 1.00 55.97  ? 200 LEU H CD1 1 
ATOM   13839 C  CD2 . LEU H  1 209 ? 22.976  39.642  54.720 1.00 38.92  ? 200 LEU H CD2 1 
ATOM   13840 N  N   . VAL H  1 210 ? 24.689  41.636  59.356 1.00 58.79  ? 201 VAL H N   1 
ATOM   13841 C  CA  . VAL H  1 210 ? 24.568  43.014  59.824 1.00 60.73  ? 201 VAL H CA  1 
ATOM   13842 C  C   . VAL H  1 210 ? 25.181  43.957  58.783 1.00 58.06  ? 201 VAL H C   1 
ATOM   13843 O  O   . VAL H  1 210 ? 26.362  43.842  58.428 1.00 55.87  ? 201 VAL H O   1 
ATOM   13844 C  CB  . VAL H  1 210 ? 25.221  43.204  61.217 1.00 56.42  ? 201 VAL H CB  1 
ATOM   13845 C  CG1 . VAL H  1 210 ? 25.192  44.671  61.630 1.00 51.99  ? 201 VAL H CG1 1 
ATOM   13846 C  CG2 . VAL H  1 210 ? 24.525  42.338  62.246 1.00 52.28  ? 201 VAL H CG2 1 
ATOM   13847 N  N   . VAL H  1 211 ? 24.364  44.873  58.277 1.00 48.92  ? 202 VAL H N   1 
ATOM   13848 C  CA  . VAL H  1 211 ? 24.794  45.738  57.186 1.00 52.84  ? 202 VAL H CA  1 
ATOM   13849 C  C   . VAL H  1 211 ? 24.652  47.228  57.514 1.00 56.52  ? 202 VAL H C   1 
ATOM   13850 O  O   . VAL H  1 211 ? 23.587  47.704  57.937 1.00 48.52  ? 202 VAL H O   1 
ATOM   13851 C  CB  . VAL H  1 211 ? 24.069  45.379  55.851 1.00 55.36  ? 202 VAL H CB  1 
ATOM   13852 C  CG1 . VAL H  1 211 ? 24.403  46.376  54.770 1.00 50.90  ? 202 VAL H CG1 1 
ATOM   13853 C  CG2 . VAL H  1 211 ? 24.456  43.983  55.405 1.00 51.84  ? 202 VAL H CG2 1 
ATOM   13854 N  N   . LYS H  1 212 ? 25.762  47.937  57.319 1.00 58.18  ? 203 LYS H N   1 
ATOM   13855 C  CA  . LYS H  1 212 ? 25.855  49.384  57.488 1.00 63.02  ? 203 LYS H CA  1 
ATOM   13856 C  C   . LYS H  1 212 ? 25.987  50.042  56.110 1.00 61.79  ? 203 LYS H C   1 
ATOM   13857 O  O   . LYS H  1 212 ? 26.907  49.731  55.356 1.00 63.11  ? 203 LYS H O   1 
ATOM   13858 C  CB  . LYS H  1 212 ? 27.086  49.715  58.345 1.00 67.65  ? 203 LYS H CB  1 
ATOM   13859 C  CG  . LYS H  1 212 ? 27.158  51.152  58.853 1.00 71.34  ? 203 LYS H CG  1 
ATOM   13860 C  CD  . LYS H  1 212 ? 26.411  51.325  60.172 1.00 75.30  ? 203 LYS H CD  1 
ATOM   13861 C  CE  . LYS H  1 212 ? 25.878  52.761  60.317 1.00 85.93  ? 203 LYS H CE  1 
ATOM   13862 N  NZ  . LYS H  1 212 ? 24.907  53.001  61.449 1.00 74.70  ? 203 LYS H NZ  1 
ATOM   13863 N  N   . PHE H  1 213 ? 25.076  50.949  55.772 1.00 62.10  ? 204 PHE H N   1 
ATOM   13864 C  CA  . PHE H  1 213 ? 25.116  51.573  54.450 1.00 61.65  ? 204 PHE H CA  1 
ATOM   13865 C  C   . PHE H  1 213 ? 24.641  53.031  54.422 1.00 63.59  ? 204 PHE H C   1 
ATOM   13866 O  O   . PHE H  1 213 ? 23.766  53.435  55.189 1.00 61.88  ? 204 PHE H O   1 
ATOM   13867 C  CB  . PHE H  1 213 ? 24.302  50.735  53.456 1.00 62.89  ? 204 PHE H CB  1 
ATOM   13868 C  CG  . PHE H  1 213 ? 22.836  50.658  53.787 1.00 61.31  ? 204 PHE H CG  1 
ATOM   13869 C  CD1 . PHE H  1 213 ? 21.892  51.226  52.943 1.00 53.20  ? 204 PHE H CD1 1 
ATOM   13870 C  CD2 . PHE H  1 213 ? 22.402  50.028  54.947 1.00 54.12  ? 204 PHE H CD2 1 
ATOM   13871 C  CE1 . PHE H  1 213 ? 20.545  51.162  53.248 1.00 54.20  ? 204 PHE H CE1 1 
ATOM   13872 C  CE2 . PHE H  1 213 ? 21.060  49.958  55.252 1.00 47.36  ? 204 PHE H CE2 1 
ATOM   13873 C  CZ  . PHE H  1 213 ? 20.131  50.528  54.410 1.00 53.42  ? 204 PHE H CZ  1 
ATOM   13874 N  N   . ARG H  1 214 ? 25.219  53.814  53.517 1.00 66.92  ? 205 ARG H N   1 
ATOM   13875 C  CA  . ARG H  1 214 ? 24.788  55.193  53.307 1.00 69.33  ? 205 ARG H CA  1 
ATOM   13876 C  C   . ARG H  1 214 ? 24.522  55.445  51.821 1.00 63.85  ? 205 ARG H C   1 
ATOM   13877 O  O   . ARG H  1 214 ? 25.000  54.693  50.982 1.00 64.92  ? 205 ARG H O   1 
ATOM   13878 C  CB  . ARG H  1 214 ? 25.848  56.171  53.830 1.00 72.95  ? 205 ARG H CB  1 
ATOM   13879 C  CG  . ARG H  1 214 ? 27.144  56.188  53.033 1.00 68.46  ? 205 ARG H CG  1 
ATOM   13880 C  CD  . ARG H  1 214 ? 28.042  57.317  53.495 1.00 67.61  ? 205 ARG H CD  1 
ATOM   13881 N  NE  . ARG H  1 214 ? 29.372  57.231  52.899 1.00 73.29  ? 205 ARG H NE  1 
ATOM   13882 C  CZ  . ARG H  1 214 ? 30.505  57.460  53.561 1.00 72.12  ? 205 ARG H CZ  1 
ATOM   13883 N  NH1 . ARG H  1 214 ? 30.467  57.796  54.844 1.00 60.29  ? 205 ARG H NH1 1 
ATOM   13884 N  NH2 . ARG H  1 214 ? 31.677  57.355  52.940 1.00 63.49  ? 205 ARG H NH2 1 
ATOM   13885 N  N   . GLU H  1 215 ? 23.764  56.496  51.501 1.00 64.20  ? 206 GLU H N   1 
ATOM   13886 C  CA  . GLU H  1 215 ? 23.572  56.902  50.111 1.00 68.20  ? 206 GLU H CA  1 
ATOM   13887 C  C   . GLU H  1 215 ? 24.930  57.215  49.501 1.00 71.35  ? 206 GLU H C   1 
ATOM   13888 O  O   . GLU H  1 215 ? 25.770  57.826  50.152 1.00 75.38  ? 206 GLU H O   1 
ATOM   13889 C  CB  . GLU H  1 215 ? 22.662  58.128  50.017 1.00 64.12  ? 206 GLU H CB  1 
ATOM   13890 C  CG  . GLU H  1 215 ? 21.472  58.101  50.966 1.00 70.76  ? 206 GLU H CG  1 
ATOM   13891 C  CD  . GLU H  1 215 ? 20.200  58.653  50.341 1.00 75.29  ? 206 GLU H CD  1 
ATOM   13892 O  OE1 . GLU H  1 215 ? 19.669  59.690  50.817 1.00 60.41  ? 206 GLU H OE1 1 
ATOM   13893 O  OE2 . GLU H  1 215 ? 19.726  58.023  49.372 1.00 83.69  ? 206 GLU H OE2 1 
ATOM   13894 N  N   . ARG H  1 216 ? 25.154  56.803  48.258 1.00 67.23  ? 207 ARG H N   1 
ATOM   13895 C  CA  . ARG H  1 216 ? 26.477  56.949  47.658 1.00 78.43  ? 207 ARG H CA  1 
ATOM   13896 C  C   . ARG H  1 216 ? 26.959  58.397  47.660 1.00 88.93  ? 207 ARG H C   1 
ATOM   13897 O  O   . ARG H  1 216 ? 26.287  59.280  47.122 1.00 86.51  ? 207 ARG H O   1 
ATOM   13898 C  CB  . ARG H  1 216 ? 26.485  56.407  46.228 1.00 78.10  ? 207 ARG H CB  1 
ATOM   13899 C  CG  . ARG H  1 216 ? 27.868  56.370  45.586 1.00 87.47  ? 207 ARG H CG  1 
ATOM   13900 C  CD  . ARG H  1 216 ? 27.911  55.341  44.475 1.00 81.78  ? 207 ARG H CD  1 
ATOM   13901 N  NE  . ARG H  1 216 ? 26.808  55.557  43.542 1.00 83.86  ? 207 ARG H NE  1 
ATOM   13902 C  CZ  . ARG H  1 216 ? 26.943  56.057  42.316 1.00 86.76  ? 207 ARG H CZ  1 
ATOM   13903 N  NH1 . ARG H  1 216 ? 28.149  56.382  41.855 1.00 89.19  ? 207 ARG H NH1 1 
ATOM   13904 N  NH2 . ARG H  1 216 ? 25.870  56.221  41.549 1.00 75.98  ? 207 ARG H NH2 1 
ATOM   13905 N  N   . ARG H  1 217 ? 28.146  58.612  48.230 1.00 86.32  ? 208 ARG H N   1 
ATOM   13906 C  CA  . ARG H  1 217 ? 28.731  59.945  48.401 1.00 91.91  ? 208 ARG H CA  1 
ATOM   13907 C  C   . ARG H  1 217 ? 27.680  61.061  48.418 1.00 96.00  ? 208 ARG H C   1 
ATOM   13908 O  O   . ARG H  1 217 ? 27.399  61.691  47.391 1.00 94.19  ? 208 ARG H O   1 
ATOM   13909 C  CB  . ARG H  1 217 ? 29.780  60.224  47.319 1.00 94.91  ? 208 ARG H CB  1 
ATOM   13910 C  CG  . ARG H  1 217 ? 30.574  59.005  46.880 1.00 95.97  ? 208 ARG H CG  1 
ATOM   13911 C  CD  . ARG H  1 217 ? 31.199  59.249  45.509 1.00 104.44 ? 208 ARG H CD  1 
ATOM   13912 N  NE  . ARG H  1 217 ? 31.465  58.002  44.791 1.00 109.26 ? 208 ARG H NE  1 
ATOM   13913 C  CZ  . ARG H  1 217 ? 31.508  57.891  43.465 1.00 115.07 ? 208 ARG H CZ  1 
ATOM   13914 N  NH1 . ARG H  1 217 ? 31.298  58.957  42.698 1.00 104.61 ? 208 ARG H NH1 1 
ATOM   13915 N  NH2 . ARG H  1 217 ? 31.754  56.709  42.903 1.00 108.63 ? 208 ARG H NH2 1 
ATOM   13916 N  N   . ASP I  1 4   ? 0.644   12.166  -1.142 1.00 87.74  ? -5  ASP I N   1 
ATOM   13917 C  CA  . ASP I  1 4   ? -0.769  11.914  -0.879 1.00 93.51  ? -5  ASP I CA  1 
ATOM   13918 C  C   . ASP I  1 4   ? -1.125  12.323  0.560  1.00 95.56  ? -5  ASP I C   1 
ATOM   13919 O  O   . ASP I  1 4   ? -0.522  13.241  1.111  1.00 97.67  ? -5  ASP I O   1 
ATOM   13920 C  CB  . ASP I  1 4   ? -1.097  10.438  -1.149 1.00 84.72  ? -5  ASP I CB  1 
ATOM   13921 C  CG  . ASP I  1 4   ? -2.585  10.179  -1.221 1.00 89.17  ? -5  ASP I CG  1 
ATOM   13922 O  OD1 . ASP I  1 4   ? -3.337  11.117  -1.564 1.00 88.16  ? -5  ASP I OD1 1 
ATOM   13923 O  OD2 . ASP I  1 4   ? -3.006  9.045   -0.921 1.00 81.59  ? -5  ASP I OD2 1 
ATOM   13924 N  N   . ASP I  1 5   ? -2.126  11.679  1.153  1.00 96.90  ? -4  ASP I N   1 
ATOM   13925 C  CA  . ASP I  1 5   ? -2.327  11.771  2.593  1.00 90.84  ? -4  ASP I CA  1 
ATOM   13926 C  C   . ASP I  1 5   ? -1.343  10.829  3.245  1.00 92.22  ? -4  ASP I C   1 
ATOM   13927 O  O   . ASP I  1 5   ? -0.714  11.154  4.250  1.00 94.63  ? -4  ASP I O   1 
ATOM   13928 C  CB  . ASP I  1 5   ? -3.728  11.320  2.982  1.00 100.97 ? -4  ASP I CB  1 
ATOM   13929 C  CG  . ASP I  1 5   ? -4.798  12.268  2.510  1.00 114.05 ? -4  ASP I CG  1 
ATOM   13930 O  OD1 . ASP I  1 5   ? -4.519  13.486  2.433  1.00 111.12 ? -4  ASP I OD1 1 
ATOM   13931 O  OD2 . ASP I  1 5   ? -5.919  11.788  2.222  1.00 117.59 ? -4  ASP I OD2 1 
ATOM   13932 N  N   . ASP I  1 6   ? -1.220  9.644   2.660  1.00 89.38  ? -3  ASP I N   1 
ATOM   13933 C  CA  . ASP I  1 6   ? -0.342  8.627   3.203  1.00 86.01  ? -3  ASP I CA  1 
ATOM   13934 C  C   . ASP I  1 6   ? 1.065   9.180   3.412  1.00 82.55  ? -3  ASP I C   1 
ATOM   13935 O  O   . ASP I  1 6   ? 1.728   8.833   4.380  1.00 77.57  ? -3  ASP I O   1 
ATOM   13936 C  CB  . ASP I  1 6   ? -0.321  7.388   2.304  1.00 78.45  ? -3  ASP I CB  1 
ATOM   13937 C  CG  . ASP I  1 6   ? 0.579   6.289   2.847  1.00 75.93  ? -3  ASP I CG  1 
ATOM   13938 O  OD1 . ASP I  1 6   ? 0.320   5.790   3.962  1.00 66.49  ? -3  ASP I OD1 1 
ATOM   13939 O  OD2 . ASP I  1 6   ? 1.555   5.925   2.154  1.00 74.14  ? -3  ASP I OD2 1 
ATOM   13940 N  N   . ASP I  1 7   ? 1.516   10.054  2.522  1.00 84.51  ? -2  ASP I N   1 
ATOM   13941 C  CA  . ASP I  1 7   ? 2.849   10.626  2.661  1.00 86.66  ? -2  ASP I CA  1 
ATOM   13942 C  C   . ASP I  1 7   ? 2.986   11.487  3.931  1.00 87.40  ? -2  ASP I C   1 
ATOM   13943 O  O   . ASP I  1 7   ? 4.056   11.516  4.554  1.00 81.91  ? -2  ASP I O   1 
ATOM   13944 C  CB  . ASP I  1 7   ? 3.253   11.409  1.404  1.00 95.76  ? -2  ASP I CB  1 
ATOM   13945 C  CG  . ASP I  1 7   ? 3.560   10.502  0.220  1.00 104.53 ? -2  ASP I CG  1 
ATOM   13946 O  OD1 . ASP I  1 7   ? 4.567   9.765   0.292  1.00 104.49 ? -2  ASP I OD1 1 
ATOM   13947 O  OD2 . ASP I  1 7   ? 2.807   10.537  -0.785 1.00 105.77 ? -2  ASP I OD2 1 
ATOM   13948 N  N   . LYS I  1 8   ? 1.909   12.178  4.313  1.00 84.75  ? -1  LYS I N   1 
ATOM   13949 C  CA  . LYS I  1 8   ? 1.899   12.937  5.566  1.00 82.56  ? -1  LYS I CA  1 
ATOM   13950 C  C   . LYS I  1 8   ? 1.819   11.991  6.764  1.00 78.53  ? -1  LYS I C   1 
ATOM   13951 O  O   . LYS I  1 8   ? 2.464   12.212  7.787  1.00 74.86  ? -1  LYS I O   1 
ATOM   13952 C  CB  . LYS I  1 8   ? 0.718   13.910  5.636  1.00 79.92  ? -1  LYS I CB  1 
ATOM   13953 C  CG  . LYS I  1 8   ? 0.271   14.501  4.320  1.00 92.81  ? -1  LYS I CG  1 
ATOM   13954 C  CD  . LYS I  1 8   ? -0.915  15.443  4.535  1.00 94.50  ? -1  LYS I CD  1 
ATOM   13955 C  CE  . LYS I  1 8   ? -1.592  15.821  3.225  1.00 87.54  ? -1  LYS I CE  1 
ATOM   13956 N  NZ  . LYS I  1 8   ? -2.798  16.645  3.476  1.00 77.80  ? -1  LYS I NZ  1 
ATOM   13957 N  N   . LEU I  1 9   ? 1.004   10.950  6.642  1.00 76.17  ? 0   LEU I N   1 
ATOM   13958 C  CA  . LEU I  1 9   ? 0.867   9.988   7.714  1.00 71.46  ? 0   LEU I CA  1 
ATOM   13959 C  C   . LEU I  1 9   ? 2.229   9.375   7.985  1.00 68.30  ? 0   LEU I C   1 
ATOM   13960 O  O   . LEU I  1 9   ? 2.667   9.286   9.123  1.00 65.73  ? 0   LEU I O   1 
ATOM   13961 C  CB  . LEU I  1 9   ? -0.149  8.911   7.353  1.00 78.30  ? 0   LEU I CB  1 
ATOM   13962 C  CG  . LEU I  1 9   ? -0.827  8.292   8.568  1.00 81.06  ? 0   LEU I CG  1 
ATOM   13963 C  CD1 . LEU I  1 9   ? -1.540  9.373   9.361  1.00 84.34  ? 0   LEU I CD1 1 
ATOM   13964 C  CD2 . LEU I  1 9   ? -1.795  7.223   8.129  1.00 84.31  ? 0   LEU I CD2 1 
ATOM   13965 N  N   . HIS I  1 10  ? 2.912   8.971   6.930  1.00 68.73  ? 1   HIS I N   1 
ATOM   13966 C  CA  . HIS I  1 10  ? 4.252   8.444   7.072  1.00 67.69  ? 1   HIS I CA  1 
ATOM   13967 C  C   . HIS I  1 10  ? 5.199   9.479   7.675  1.00 69.15  ? 1   HIS I C   1 
ATOM   13968 O  O   . HIS I  1 10  ? 6.199   9.122   8.290  1.00 66.17  ? 1   HIS I O   1 
ATOM   13969 C  CB  . HIS I  1 10  ? 4.783   7.961   5.719  1.00 68.56  ? 1   HIS I CB  1 
ATOM   13970 C  CG  . HIS I  1 10  ? 4.081   6.749   5.197  1.00 74.42  ? 1   HIS I CG  1 
ATOM   13971 N  ND1 . HIS I  1 10  ? 4.750   5.715   4.570  1.00 74.61  ? 1   HIS I ND1 1 
ATOM   13972 C  CD2 . HIS I  1 10  ? 2.776   6.401   5.197  1.00 77.22  ? 1   HIS I CD2 1 
ATOM   13973 C  CE1 . HIS I  1 10  ? 3.885   4.786   4.219  1.00 61.04  ? 1   HIS I CE1 1 
ATOM   13974 N  NE2 . HIS I  1 10  ? 2.677   5.178   4.585  1.00 59.96  ? 1   HIS I NE2 1 
ATOM   13975 N  N   . SER I  1 11  ? 4.898   10.760  7.478  1.00 73.11  ? 2   SER I N   1 
ATOM   13976 C  CA  . SER I  1 11  ? 5.766   11.824  7.981  1.00 74.17  ? 2   SER I CA  1 
ATOM   13977 C  C   . SER I  1 11  ? 5.550   12.106  9.468  1.00 72.91  ? 2   SER I C   1 
ATOM   13978 O  O   . SER I  1 11  ? 6.507   12.381  10.189 1.00 71.68  ? 2   SER I O   1 
ATOM   13979 C  CB  . SER I  1 11  ? 5.640   13.098  7.142  1.00 82.41  ? 2   SER I CB  1 
ATOM   13980 O  OG  . SER I  1 11  ? 4.488   13.827  7.506  1.00 90.13  ? 2   SER I OG  1 
ATOM   13981 N  N   . GLN I  1 12  ? 4.297   12.052  9.914  1.00 71.11  ? 3   GLN I N   1 
ATOM   13982 C  CA  . GLN I  1 12  ? 3.993   12.114  11.343 1.00 68.88  ? 3   GLN I CA  1 
ATOM   13983 C  C   . GLN I  1 12  ? 4.568   10.916  12.074 1.00 69.20  ? 3   GLN I C   1 
ATOM   13984 O  O   . GLN I  1 12  ? 5.190   11.055  13.129 1.00 69.77  ? 3   GLN I O   1 
ATOM   13985 C  CB  . GLN I  1 12  ? 2.495   12.142  11.594 1.00 63.50  ? 3   GLN I CB  1 
ATOM   13986 C  CG  . GLN I  1 12  ? 1.825   13.420  11.219 1.00 76.61  ? 3   GLN I CG  1 
ATOM   13987 C  CD  . GLN I  1 12  ? 0.337   13.297  11.344 1.00 83.55  ? 3   GLN I CD  1 
ATOM   13988 O  OE1 . GLN I  1 12  ? -0.159  12.599  12.226 1.00 81.34  ? 3   GLN I OE1 1 
ATOM   13989 N  NE2 . GLN I  1 12  ? -0.392  13.946  10.446 1.00 81.72  ? 3   GLN I NE2 1 
ATOM   13990 N  N   . ALA I  1 13  ? 4.341   9.730   11.524 1.00 68.96  ? 4   ALA I N   1 
ATOM   13991 C  CA  . ALA I  1 13  ? 4.835   8.527   12.166 1.00 70.74  ? 4   ALA I CA  1 
ATOM   13992 C  C   . ALA I  1 13  ? 6.352   8.534   12.163 1.00 66.33  ? 4   ALA I C   1 
ATOM   13993 O  O   . ALA I  1 13  ? 6.977   8.071   13.110 1.00 69.62  ? 4   ALA I O   1 
ATOM   13994 C  CB  . ALA I  1 13  ? 4.294   7.288   11.496 1.00 52.03  ? 4   ALA I CB  1 
ATOM   13995 N  N   . ASN I  1 14  ? 6.947   9.074   11.110 1.00 61.90  ? 5   ASN I N   1 
ATOM   13996 C  CA  . ASN I  1 14  ? 8.397   9.109   11.025 1.00 66.46  ? 5   ASN I CA  1 
ATOM   13997 C  C   . ASN I  1 14  ? 9.011   9.995   12.082 1.00 71.12  ? 5   ASN I C   1 
ATOM   13998 O  O   . ASN I  1 14  ? 10.070  9.690   12.632 1.00 68.44  ? 5   ASN I O   1 
ATOM   13999 C  CB  . ASN I  1 14  ? 8.839   9.597   9.662  1.00 65.62  ? 5   ASN I CB  1 
ATOM   14000 C  CG  . ASN I  1 14  ? 9.118   8.474   8.720  1.00 66.49  ? 5   ASN I CG  1 
ATOM   14001 O  OD1 . ASN I  1 14  ? 9.403   7.355   9.133  1.00 59.38  ? 5   ASN I OD1 1 
ATOM   14002 N  ND2 . ASN I  1 14  ? 9.044   8.763   7.438  1.00 78.01  ? 5   ASN I ND2 1 
ATOM   14003 N  N   . LEU I  1 15  ? 8.336   11.109  12.337 1.00 71.55  ? 6   LEU I N   1 
ATOM   14004 C  CA  . LEU I  1 15  ? 8.784   12.112  13.288 1.00 64.75  ? 6   LEU I CA  1 
ATOM   14005 C  C   . LEU I  1 15  ? 8.620   11.599  14.714 1.00 66.45  ? 6   LEU I C   1 
ATOM   14006 O  O   . LEU I  1 15  ? 9.566   11.633  15.498 1.00 68.63  ? 6   LEU I O   1 
ATOM   14007 C  CB  . LEU I  1 15  ? 7.989   13.399  13.072 1.00 63.18  ? 6   LEU I CB  1 
ATOM   14008 C  CG  . LEU I  1 15  ? 8.185   14.589  13.996 1.00 61.94  ? 6   LEU I CG  1 
ATOM   14009 C  CD1 . LEU I  1 15  ? 9.599   15.090  13.875 1.00 62.95  ? 6   LEU I CD1 1 
ATOM   14010 C  CD2 . LEU I  1 15  ? 7.179   15.663  13.648 1.00 47.19  ? 6   LEU I CD2 1 
ATOM   14011 N  N   . MET I  1 16  ? 7.427   11.107  15.041 1.00 62.83  ? 7   MET I N   1 
ATOM   14012 C  CA  . MET I  1 16  ? 7.186   10.505  16.345 1.00 64.83  ? 7   MET I CA  1 
ATOM   14013 C  C   . MET I  1 16  ? 8.221   9.423   16.643 1.00 63.17  ? 7   MET I C   1 
ATOM   14014 O  O   . MET I  1 16  ? 8.718   9.312   17.765 1.00 64.46  ? 7   MET I O   1 
ATOM   14015 C  CB  . MET I  1 16  ? 5.782   9.923   16.424 1.00 61.01  ? 7   MET I CB  1 
ATOM   14016 C  CG  . MET I  1 16  ? 4.678   10.911  16.104 1.00 70.39  ? 7   MET I CG  1 
ATOM   14017 S  SD  . MET I  1 16  ? 3.065   10.250  16.583 1.00 104.86 ? 7   MET I SD  1 
ATOM   14018 C  CE  . MET I  1 16  ? 1.921   11.335  15.723 1.00 85.73  ? 7   MET I CE  1 
ATOM   14019 N  N   . ARG I  1 17  ? 8.549   8.638   15.626 1.00 64.87  ? 8   ARG I N   1 
ATOM   14020 C  CA  . ARG I  1 17  ? 9.575   7.617   15.749 1.00 64.26  ? 8   ARG I CA  1 
ATOM   14021 C  C   . ARG I  1 17  ? 10.959  8.226   15.995 1.00 69.98  ? 8   ARG I C   1 
ATOM   14022 O  O   . ARG I  1 17  ? 11.658  7.803   16.904 1.00 75.60  ? 8   ARG I O   1 
ATOM   14023 C  CB  . ARG I  1 17  ? 9.575   6.707   14.526 1.00 64.33  ? 8   ARG I CB  1 
ATOM   14024 C  CG  . ARG I  1 17  ? 10.344  5.418   14.714 1.00 70.96  ? 8   ARG I CG  1 
ATOM   14025 C  CD  . ARG I  1 17  ? 10.003  4.423   13.628 1.00 75.54  ? 8   ARG I CD  1 
ATOM   14026 N  NE  . ARG I  1 17  ? 10.096  5.025   12.299 1.00 69.28  ? 8   ARG I NE  1 
ATOM   14027 C  CZ  . ARG I  1 17  ? 11.231  5.155   11.617 1.00 69.17  ? 8   ARG I CZ  1 
ATOM   14028 N  NH1 . ARG I  1 17  ? 12.378  4.729   12.139 1.00 73.13  ? 8   ARG I NH1 1 
ATOM   14029 N  NH2 . ARG I  1 17  ? 11.223  5.710   10.414 1.00 70.18  ? 8   ARG I NH2 1 
ATOM   14030 N  N   . LEU I  1 18  ? 11.349  9.234   15.220 1.00 68.08  ? 9   LEU I N   1 
ATOM   14031 C  CA  . LEU I  1 18  ? 12.614  9.939   15.473 1.00 69.29  ? 9   LEU I CA  1 
ATOM   14032 C  C   . LEU I  1 18  ? 12.746  10.462  16.918 1.00 75.49  ? 9   LEU I C   1 
ATOM   14033 O  O   . LEU I  1 18  ? 13.792  10.327  17.569 1.00 69.94  ? 9   LEU I O   1 
ATOM   14034 C  CB  . LEU I  1 18  ? 12.774  11.096  14.493 1.00 61.19  ? 9   LEU I CB  1 
ATOM   14035 C  CG  . LEU I  1 18  ? 13.967  12.016  14.723 1.00 60.92  ? 9   LEU I CG  1 
ATOM   14036 C  CD1 . LEU I  1 18  ? 15.244  11.223  14.722 1.00 56.72  ? 9   LEU I CD1 1 
ATOM   14037 C  CD2 . LEU I  1 18  ? 13.998  13.068  13.643 1.00 69.39  ? 9   LEU I CD2 1 
ATOM   14038 N  N   . LYS I  1 19  ? 11.675  11.069  17.409 1.00 69.84  ? 10  LYS I N   1 
ATOM   14039 C  CA  . LYS I  1 19  ? 11.656  11.607  18.753 1.00 68.78  ? 10  LYS I CA  1 
ATOM   14040 C  C   . LYS I  1 19  ? 11.692  10.513  19.809 1.00 76.87  ? 10  LYS I C   1 
ATOM   14041 O  O   . LYS I  1 19  ? 12.378  10.649  20.829 1.00 77.06  ? 10  LYS I O   1 
ATOM   14042 C  CB  . LYS I  1 19  ? 10.424  12.478  18.936 1.00 66.67  ? 10  LYS I CB  1 
ATOM   14043 C  CG  . LYS I  1 19  ? 10.598  13.860  18.384 1.00 57.85  ? 10  LYS I CG  1 
ATOM   14044 C  CD  . LYS I  1 19  ? 9.307   14.595  18.447 1.00 57.39  ? 10  LYS I CD  1 
ATOM   14045 C  CE  . LYS I  1 19  ? 9.579   16.067  18.506 1.00 63.88  ? 10  LYS I CE  1 
ATOM   14046 N  NZ  . LYS I  1 19  ? 8.317   16.805  18.739 1.00 72.95  ? 10  LYS I NZ  1 
ATOM   14047 N  N   . SER I  1 20  ? 10.944  9.438   19.570 1.00 76.83  ? 11  SER I N   1 
ATOM   14048 C  CA  . SER I  1 20  ? 11.005  8.276   20.440 1.00 76.87  ? 11  SER I CA  1 
ATOM   14049 C  C   . SER I  1 20  ? 12.412  7.712   20.416 1.00 77.36  ? 11  SER I C   1 
ATOM   14050 O  O   . SER I  1 20  ? 13.000  7.463   21.454 1.00 77.52  ? 11  SER I O   1 
ATOM   14051 C  CB  . SER I  1 20  ? 10.005  7.214   20.008 1.00 75.17  ? 11  SER I CB  1 
ATOM   14052 O  OG  . SER I  1 20  ? 9.879   6.212   21.004 1.00 90.55  ? 11  SER I OG  1 
ATOM   14053 N  N   . ASP I  1 21  ? 12.962  7.531   19.225 1.00 75.52  ? 12  ASP I N   1 
ATOM   14054 C  CA  . ASP I  1 21  ? 14.319  7.007   19.094 1.00 82.56  ? 12  ASP I CA  1 
ATOM   14055 C  C   . ASP I  1 21  ? 15.333  7.845   19.835 1.00 82.55  ? 12  ASP I C   1 
ATOM   14056 O  O   . ASP I  1 21  ? 16.411  7.372   20.169 1.00 86.25  ? 12  ASP I O   1 
ATOM   14057 C  CB  . ASP I  1 21  ? 14.745  6.921   17.632 1.00 80.12  ? 12  ASP I CB  1 
ATOM   14058 C  CG  . ASP I  1 21  ? 14.036  5.824   16.891 1.00 84.23  ? 12  ASP I CG  1 
ATOM   14059 O  OD1 . ASP I  1 21  ? 12.806  5.695   17.069 1.00 91.22  ? 12  ASP I OD1 1 
ATOM   14060 O  OD2 . ASP I  1 21  ? 14.699  5.082   16.142 1.00 84.36  ? 12  ASP I OD2 1 
ATOM   14061 N  N   . LEU I  1 22  ? 14.996  9.107   20.056 1.00 83.92  ? 13  LEU I N   1 
ATOM   14062 C  CA  . LEU I  1 22  ? 15.901  10.031  20.719 1.00 80.16  ? 13  LEU I CA  1 
ATOM   14063 C  C   . LEU I  1 22  ? 15.643  10.272  22.211 1.00 83.30  ? 13  LEU I C   1 
ATOM   14064 O  O   . LEU I  1 22  ? 16.541  10.082  23.034 1.00 82.42  ? 13  LEU I O   1 
ATOM   14065 C  CB  . LEU I  1 22  ? 15.892  11.393  20.017 1.00 71.30  ? 13  LEU I CB  1 
ATOM   14066 C  CG  . LEU I  1 22  ? 16.626  11.506  18.678 1.00 69.25  ? 13  LEU I CG  1 
ATOM   14067 C  CD1 . LEU I  1 22  ? 16.411  12.880  18.084 1.00 68.03  ? 13  LEU I CD1 1 
ATOM   14068 C  CD2 . LEU I  1 22  ? 18.107  11.240  18.831 1.00 65.28  ? 13  LEU I CD2 1 
ATOM   14069 N  N   . PHE I  1 23  ? 14.421  10.687  22.551 1.00 85.54  ? 14  PHE I N   1 
ATOM   14070 C  CA  . PHE I  1 23  ? 14.077  11.039  23.941 1.00 87.38  ? 14  PHE I CA  1 
ATOM   14071 C  C   . PHE I  1 23  ? 13.640  9.913   24.876 1.00 94.50  ? 14  PHE I C   1 
ATOM   14072 O  O   . PHE I  1 23  ? 13.762  10.042  26.092 1.00 101.31 ? 14  PHE I O   1 
ATOM   14073 C  CB  . PHE I  1 23  ? 13.020  12.148  23.976 1.00 84.58  ? 14  PHE I CB  1 
ATOM   14074 C  CG  . PHE I  1 23  ? 13.438  13.396  23.259 1.00 83.74  ? 14  PHE I CG  1 
ATOM   14075 C  CD1 . PHE I  1 23  ? 14.753  13.833  23.316 1.00 77.47  ? 14  PHE I CD1 1 
ATOM   14076 C  CD2 . PHE I  1 23  ? 12.526  14.119  22.510 1.00 76.27  ? 14  PHE I CD2 1 
ATOM   14077 C  CE1 . PHE I  1 23  ? 15.143  14.961  22.645 1.00 72.92  ? 14  PHE I CE1 1 
ATOM   14078 C  CE2 . PHE I  1 23  ? 12.917  15.252  21.834 1.00 66.68  ? 14  PHE I CE2 1 
ATOM   14079 C  CZ  . PHE I  1 23  ? 14.224  15.672  21.899 1.00 69.07  ? 14  PHE I CZ  1 
ATOM   14080 N  N   . ASN I  1 24  ? 13.107  8.834   24.316 1.00 104.15 ? 15  ASN I N   1 
ATOM   14081 C  CA  . ASN I  1 24  ? 12.607  7.705   25.102 1.00 106.75 ? 15  ASN I CA  1 
ATOM   14082 C  C   . ASN I  1 24  ? 13.591  6.560   25.226 1.00 105.99 ? 15  ASN I C   1 
ATOM   14083 O  O   . ASN I  1 24  ? 13.910  6.109   26.320 1.00 111.93 ? 15  ASN I O   1 
ATOM   14084 C  CB  . ASN I  1 24  ? 11.371  7.078   24.454 1.00 107.33 ? 15  ASN I CB  1 
ATOM   14085 C  CG  . ASN I  1 24  ? 10.165  7.996   24.473 1.00 109.44 ? 15  ASN I CG  1 
ATOM   14086 O  OD1 . ASN I  1 24  ? 10.209  9.098   25.028 1.00 107.77 ? 15  ASN I OD1 1 
ATOM   14087 N  ND2 . ASN I  1 24  ? 9.076   7.546   23.851 1.00 99.54  ? 15  ASN I ND2 1 
ATOM   14088 N  N   . ARG I  1 25  ? 14.055  6.077   24.084 1.00 97.98  ? 16  ARG I N   1 
ATOM   14089 C  CA  . ARG I  1 25  ? 15.077  5.052   24.060 1.00 99.88  ? 16  ARG I CA  1 
ATOM   14090 C  C   . ARG I  1 25  ? 16.337  5.461   24.801 1.00 111.89 ? 16  ARG I C   1 
ATOM   14091 O  O   . ARG I  1 25  ? 16.987  4.614   25.431 1.00 122.33 ? 16  ARG I O   1 
ATOM   14092 C  CB  . ARG I  1 25  ? 15.426  4.714   22.623 1.00 103.23 ? 16  ARG I CB  1 
ATOM   14093 C  CG  . ARG I  1 25  ? 14.196  4.357   21.831 1.00 110.39 ? 16  ARG I CG  1 
ATOM   14094 C  CD  . ARG I  1 25  ? 13.498  3.138   22.401 1.00 114.18 ? 16  ARG I CD  1 
ATOM   14095 N  NE  . ARG I  1 25  ? 14.293  1.935   22.195 1.00 109.19 ? 16  ARG I NE  1 
ATOM   14096 C  CZ  . ARG I  1 25  ? 14.976  1.295   23.140 1.00 117.29 ? 16  ARG I CZ  1 
ATOM   14097 N  NH1 . ARG I  1 25  ? 14.976  1.728   24.405 1.00 111.75 ? 16  ARG I NH1 1 
ATOM   14098 N  NH2 . ARG I  1 25  ? 15.659  0.209   22.807 1.00 105.98 ? 16  ARG I NH2 1 
ATOM   14099 N  N   . SER I  1 26  ? 16.691  6.742   24.752 1.00 107.28 ? 17  SER I N   1 
ATOM   14100 C  CA  . SER I  1 26  ? 17.895  7.141   25.451 1.00 115.53 ? 17  SER I CA  1 
ATOM   14101 C  C   . SER I  1 26  ? 17.601  7.811   26.814 1.00 112.33 ? 17  SER I C   1 
ATOM   14102 O  O   . SER I  1 26  ? 16.451  8.085   27.149 1.00 110.55 ? 17  SER I O   1 
ATOM   14103 C  CB  . SER I  1 26  ? 18.662  8.086   24.523 1.00 106.99 ? 17  SER I CB  1 
ATOM   14104 O  OG  . SER I  1 26  ? 19.901  8.446   25.086 1.00 108.93 ? 17  SER I OG  1 
ATOM   14105 N  N   . PRO I  1 27  ? 18.651  8.052   27.618 1.00 116.22 ? 18  PRO I N   1 
ATOM   14106 C  CA  . PRO I  1 27  ? 18.692  8.959   28.774 1.00 110.94 ? 18  PRO I CA  1 
ATOM   14107 C  C   . PRO I  1 27  ? 18.899  10.392  28.325 1.00 111.66 ? 18  PRO I C   1 
ATOM   14108 O  O   . PRO I  1 27  ? 19.599  10.594  27.334 1.00 109.87 ? 18  PRO I O   1 
ATOM   14109 C  CB  . PRO I  1 27  ? 19.896  8.457   29.568 1.00 104.69 ? 18  PRO I CB  1 
ATOM   14110 C  CG  . PRO I  1 27  ? 20.784  7.910   28.531 1.00 114.55 ? 18  PRO I CG  1 
ATOM   14111 C  CD  . PRO I  1 27  ? 19.896  7.277   27.505 1.00 114.31 ? 18  PRO I CD  1 
ATOM   14112 N  N   . MET I  1 28  ? 18.347  11.370  29.032 1.00 106.05 ? 19  MET I N   1 
ATOM   14113 C  CA  . MET I  1 28  ? 18.613  12.750  28.662 1.00 98.65  ? 19  MET I CA  1 
ATOM   14114 C  C   . MET I  1 28  ? 20.088  13.036  28.923 1.00 97.12  ? 19  MET I C   1 
ATOM   14115 O  O   . MET I  1 28  ? 20.709  12.401  29.774 1.00 95.63  ? 19  MET I O   1 
ATOM   14116 C  CB  . MET I  1 28  ? 17.723  13.714  29.445 1.00 95.60  ? 19  MET I CB  1 
ATOM   14117 C  CG  . MET I  1 28  ? 17.564  15.076  28.790 1.00 85.48  ? 19  MET I CG  1 
ATOM   14118 S  SD  . MET I  1 28  ? 17.426  16.404  29.994 1.00 102.70 ? 19  MET I SD  1 
ATOM   14119 C  CE  . MET I  1 28  ? 19.104  16.501  30.634 1.00 79.76  ? 19  MET I CE  1 
ATOM   14120 N  N   . TYR I  1 29  ? 20.643  13.979  28.175 1.00 87.81  ? 20  TYR I N   1 
ATOM   14121 C  CA  . TYR I  1 29  ? 22.050  14.341  28.285 1.00 79.55  ? 20  TYR I CA  1 
ATOM   14122 C  C   . TYR I  1 29  ? 22.414  14.830  29.718 1.00 83.34  ? 20  TYR I C   1 
ATOM   14123 O  O   . TYR I  1 29  ? 21.770  15.739  30.257 1.00 79.58  ? 20  TYR I O   1 
ATOM   14124 C  CB  . TYR I  1 29  ? 22.347  15.376  27.195 1.00 77.38  ? 20  TYR I CB  1 
ATOM   14125 C  CG  . TYR I  1 29  ? 23.771  15.842  27.103 1.00 77.13  ? 20  TYR I CG  1 
ATOM   14126 C  CD1 . TYR I  1 29  ? 24.116  17.127  27.507 1.00 72.85  ? 20  TYR I CD1 1 
ATOM   14127 C  CD2 . TYR I  1 29  ? 24.770  15.012  26.607 1.00 73.76  ? 20  TYR I CD2 1 
ATOM   14128 C  CE1 . TYR I  1 29  ? 25.413  17.579  27.439 1.00 72.18  ? 20  TYR I CE1 1 
ATOM   14129 C  CE2 . TYR I  1 29  ? 26.081  15.456  26.533 1.00 82.73  ? 20  TYR I CE2 1 
ATOM   14130 C  CZ  . TYR I  1 29  ? 26.394  16.748  26.955 1.00 82.17  ? 20  TYR I CZ  1 
ATOM   14131 O  OH  . TYR I  1 29  ? 27.684  17.228  26.897 1.00 82.33  ? 20  TYR I OH  1 
ATOM   14132 N  N   . PRO I  1 30  ? 23.436  14.204  30.346 1.00 78.82  ? 21  PRO I N   1 
ATOM   14133 C  CA  . PRO I  1 30  ? 23.867  14.508  31.720 1.00 69.88  ? 21  PRO I CA  1 
ATOM   14134 C  C   . PRO I  1 30  ? 24.477  15.898  31.891 1.00 72.27  ? 21  PRO I C   1 
ATOM   14135 O  O   . PRO I  1 30  ? 24.631  16.347  33.021 1.00 76.87  ? 21  PRO I O   1 
ATOM   14136 C  CB  . PRO I  1 30  ? 24.935  13.444  31.993 1.00 67.97  ? 21  PRO I CB  1 
ATOM   14137 C  CG  . PRO I  1 30  ? 25.446  13.071  30.656 1.00 69.68  ? 21  PRO I CG  1 
ATOM   14138 C  CD  . PRO I  1 30  ? 24.269  13.150  29.738 1.00 73.94  ? 21  PRO I CD  1 
ATOM   14139 N  N   . GLY I  1 31  ? 24.843  16.547  30.791 1.00 69.76  ? 22  GLY I N   1 
ATOM   14140 C  CA  . GLY I  1 31  ? 25.524  17.826  30.828 1.00 68.12  ? 22  GLY I CA  1 
ATOM   14141 C  C   . GLY I  1 31  ? 26.990  17.609  30.532 1.00 70.76  ? 22  GLY I C   1 
ATOM   14142 O  O   . GLY I  1 31  ? 27.453  16.484  30.580 1.00 74.81  ? 22  GLY I O   1 
ATOM   14143 N  N   . PRO I  1 32  ? 27.729  18.682  30.226 1.00 69.67  ? 23  PRO I N   1 
ATOM   14144 C  CA  . PRO I  1 32  ? 29.154  18.609  29.891 1.00 68.69  ? 23  PRO I CA  1 
ATOM   14145 C  C   . PRO I  1 32  ? 30.000  18.147  31.053 1.00 73.82  ? 23  PRO I C   1 
ATOM   14146 O  O   . PRO I  1 32  ? 29.622  18.309  32.210 1.00 75.43  ? 23  PRO I O   1 
ATOM   14147 C  CB  . PRO I  1 32  ? 29.520  20.059  29.598 1.00 68.65  ? 23  PRO I CB  1 
ATOM   14148 C  CG  . PRO I  1 32  ? 28.261  20.721  29.313 1.00 70.49  ? 23  PRO I CG  1 
ATOM   14149 C  CD  . PRO I  1 32  ? 27.226  20.055  30.141 1.00 65.21  ? 23  PRO I CD  1 
ATOM   14150 N  N   . THR I  1 33  ? 31.157  17.588  30.736 1.00 78.97  ? 24  THR I N   1 
ATOM   14151 C  CA  . THR I  1 33  ? 32.137  17.215  31.740 1.00 82.85  ? 24  THR I CA  1 
ATOM   14152 C  C   . THR I  1 33  ? 33.481  17.668  31.202 1.00 84.53  ? 24  THR I C   1 
ATOM   14153 O  O   . THR I  1 33  ? 33.593  18.028  30.032 1.00 79.12  ? 24  THR I O   1 
ATOM   14154 C  CB  . THR I  1 33  ? 32.159  15.691  31.989 1.00 80.50  ? 24  THR I CB  1 
ATOM   14155 O  OG1 . THR I  1 33  ? 32.574  15.006  30.800 1.00 78.50  ? 24  THR I OG1 1 
ATOM   14156 C  CG2 . THR I  1 33  ? 30.781  15.192  32.399 1.00 72.65  ? 24  THR I CG2 1 
ATOM   14157 N  N   . LYS I  1 34  ? 34.496  17.676  32.055 1.00 86.10  ? 25  LYS I N   1 
ATOM   14158 C  CA  . LYS I  1 34  ? 35.843  17.984  31.601 1.00 81.24  ? 25  LYS I CA  1 
ATOM   14159 C  C   . LYS I  1 34  ? 36.237  17.077  30.427 1.00 89.55  ? 25  LYS I C   1 
ATOM   14160 O  O   . LYS I  1 34  ? 36.975  17.500  29.540 1.00 89.56  ? 25  LYS I O   1 
ATOM   14161 C  CB  . LYS I  1 34  ? 36.844  17.850  32.756 1.00 82.22  ? 25  LYS I CB  1 
ATOM   14162 C  CG  . LYS I  1 34  ? 36.745  16.540  33.549 1.00 85.97  ? 25  LYS I CG  1 
ATOM   14163 C  CD  . LYS I  1 34  ? 37.769  16.491  34.678 1.00 82.15  ? 25  LYS I CD  1 
ATOM   14164 C  CE  . LYS I  1 34  ? 37.784  15.139  35.375 1.00 92.09  ? 25  LYS I CE  1 
ATOM   14165 N  NZ  . LYS I  1 34  ? 38.638  15.127  36.612 1.00 99.66  ? 25  LYS I NZ  1 
ATOM   14166 N  N   . ASP I  1 35  ? 35.735  15.839  30.428 1.00 82.61  ? 26  ASP I N   1 
ATOM   14167 C  CA  . ASP I  1 35  ? 36.064  14.859  29.396 1.00 77.44  ? 26  ASP I CA  1 
ATOM   14168 C  C   . ASP I  1 35  ? 35.144  15.022  28.196 1.00 87.07  ? 26  ASP I C   1 
ATOM   14169 O  O   . ASP I  1 35  ? 35.347  14.411  27.148 1.00 89.90  ? 26  ASP I O   1 
ATOM   14170 C  CB  . ASP I  1 35  ? 35.911  13.432  29.925 1.00 81.78  ? 26  ASP I CB  1 
ATOM   14171 C  CG  . ASP I  1 35  ? 36.496  13.246  31.311 1.00 95.43  ? 26  ASP I CG  1 
ATOM   14172 O  OD1 . ASP I  1 35  ? 37.718  13.002  31.414 1.00 95.27  ? 26  ASP I OD1 1 
ATOM   14173 O  OD2 . ASP I  1 35  ? 35.725  13.321  32.296 1.00 94.20  ? 26  ASP I OD2 1 
ATOM   14174 N  N   . ASP I  1 36  ? 34.110  15.830  28.362 1.00 89.39  ? 27  ASP I N   1 
ATOM   14175 C  CA  . ASP I  1 36  ? 33.103  15.998  27.329 1.00 85.09  ? 27  ASP I CA  1 
ATOM   14176 C  C   . ASP I  1 36  ? 32.704  17.480  27.319 1.00 82.21  ? 27  ASP I C   1 
ATOM   14177 O  O   . ASP I  1 36  ? 31.586  17.838  27.688 1.00 82.46  ? 27  ASP I O   1 
ATOM   14178 C  CB  . ASP I  1 36  ? 31.915  15.075  27.643 1.00 76.10  ? 27  ASP I CB  1 
ATOM   14179 C  CG  . ASP I  1 36  ? 30.928  14.959  26.501 1.00 84.01  ? 27  ASP I CG  1 
ATOM   14180 O  OD1 . ASP I  1 36  ? 31.348  15.001  25.328 1.00 86.50  ? 27  ASP I OD1 1 
ATOM   14181 O  OD2 . ASP I  1 36  ? 29.720  14.811  26.786 1.00 84.60  ? 27  ASP I OD2 1 
ATOM   14182 N  N   . PRO I  1 37  ? 33.641  18.359  26.933 1.00 77.04  ? 28  PRO I N   1 
ATOM   14183 C  CA  . PRO I  1 37  ? 33.339  19.795  26.873 1.00 78.03  ? 28  PRO I CA  1 
ATOM   14184 C  C   . PRO I  1 37  ? 32.322  20.129  25.792 1.00 70.73  ? 28  PRO I C   1 
ATOM   14185 O  O   . PRO I  1 37  ? 32.067  19.330  24.896 1.00 67.09  ? 28  PRO I O   1 
ATOM   14186 C  CB  . PRO I  1 37  ? 34.694  20.439  26.565 1.00 73.58  ? 28  PRO I CB  1 
ATOM   14187 C  CG  . PRO I  1 37  ? 35.533  19.340  26.016 1.00 82.18  ? 28  PRO I CG  1 
ATOM   14188 C  CD  . PRO I  1 37  ? 35.055  18.074  26.649 1.00 81.52  ? 28  PRO I CD  1 
ATOM   14189 N  N   . LEU I  1 38  ? 31.729  21.306  25.896 1.00 67.66  ? 29  LEU I N   1 
ATOM   14190 C  CA  . LEU I  1 38  ? 30.671  21.704  24.984 1.00 71.65  ? 29  LEU I CA  1 
ATOM   14191 C  C   . LEU I  1 38  ? 30.724  23.209  24.739 1.00 72.01  ? 29  LEU I C   1 
ATOM   14192 O  O   . LEU I  1 38  ? 31.065  23.981  25.632 1.00 73.77  ? 29  LEU I O   1 
ATOM   14193 C  CB  . LEU I  1 38  ? 29.316  21.318  25.562 1.00 67.33  ? 29  LEU I CB  1 
ATOM   14194 C  CG  . LEU I  1 38  ? 28.163  22.197  25.097 1.00 69.32  ? 29  LEU I CG  1 
ATOM   14195 C  CD1 . LEU I  1 38  ? 27.865  21.928  23.622 1.00 66.15  ? 29  LEU I CD1 1 
ATOM   14196 C  CD2 . LEU I  1 38  ? 26.947  21.953  25.977 1.00 68.23  ? 29  LEU I CD2 1 
ATOM   14197 N  N   . THR I  1 39  ? 30.394  23.632  23.529 1.00 62.62  ? 30  THR I N   1 
ATOM   14198 C  CA  . THR I  1 39  ? 30.468  25.043  23.227 1.00 69.15  ? 30  THR I CA  1 
ATOM   14199 C  C   . THR I  1 39  ? 29.093  25.646  22.979 1.00 68.99  ? 30  THR I C   1 
ATOM   14200 O  O   . THR I  1 39  ? 28.346  25.185  22.124 1.00 69.60  ? 30  THR I O   1 
ATOM   14201 C  CB  . THR I  1 39  ? 31.371  25.301  22.022 1.00 80.04  ? 30  THR I CB  1 
ATOM   14202 O  OG1 . THR I  1 39  ? 32.712  24.901  22.331 1.00 72.80  ? 30  THR I OG1 1 
ATOM   14203 C  CG2 . THR I  1 39  ? 31.356  26.774  21.672 1.00 83.00  ? 30  THR I CG2 1 
ATOM   14204 N  N   . VAL I  1 40  ? 28.760  26.675  23.745 1.00 67.02  ? 31  VAL I N   1 
ATOM   14205 C  CA  . VAL I  1 40  ? 27.499  27.377  23.566 1.00 67.51  ? 31  VAL I CA  1 
ATOM   14206 C  C   . VAL I  1 40  ? 27.755  28.675  22.817 1.00 70.91  ? 31  VAL I C   1 
ATOM   14207 O  O   . VAL I  1 40  ? 28.592  29.474  23.230 1.00 71.83  ? 31  VAL I O   1 
ATOM   14208 C  CB  . VAL I  1 40  ? 26.841  27.710  24.920 1.00 61.49  ? 31  VAL I CB  1 
ATOM   14209 C  CG1 . VAL I  1 40  ? 25.495  28.393  24.699 1.00 60.15  ? 31  VAL I CG1 1 
ATOM   14210 C  CG2 . VAL I  1 40  ? 26.692  26.445  25.775 1.00 58.74  ? 31  VAL I CG2 1 
ATOM   14211 N  N   . TYR I  1 41  ? 27.058  28.890  21.710 1.00 64.49  ? 32  TYR I N   1 
ATOM   14212 C  CA  . TYR I  1 41  ? 27.177  30.171  21.031 1.00 66.18  ? 32  TYR I CA  1 
ATOM   14213 C  C   . TYR I  1 41  ? 26.096  31.117  21.501 1.00 63.74  ? 32  TYR I C   1 
ATOM   14214 O  O   . TYR I  1 41  ? 24.959  30.721  21.715 1.00 66.34  ? 32  TYR I O   1 
ATOM   14215 C  CB  . TYR I  1 41  ? 27.163  30.017  19.514 1.00 69.76  ? 32  TYR I CB  1 
ATOM   14216 C  CG  . TYR I  1 41  ? 28.500  29.596  18.961 1.00 77.59  ? 32  TYR I CG  1 
ATOM   14217 C  CD1 . TYR I  1 41  ? 29.454  30.540  18.599 1.00 75.75  ? 32  TYR I CD1 1 
ATOM   14218 C  CD2 . TYR I  1 41  ? 28.818  28.250  18.818 1.00 86.53  ? 32  TYR I CD2 1 
ATOM   14219 C  CE1 . TYR I  1 41  ? 30.688  30.152  18.093 1.00 83.13  ? 32  TYR I CE1 1 
ATOM   14220 C  CE2 . TYR I  1 41  ? 30.047  27.849  18.317 1.00 92.33  ? 32  TYR I CE2 1 
ATOM   14221 C  CZ  . TYR I  1 41  ? 30.979  28.800  17.956 1.00 94.10  ? 32  TYR I CZ  1 
ATOM   14222 O  OH  . TYR I  1 41  ? 32.198  28.382  17.466 1.00 84.62  ? 32  TYR I OH  1 
ATOM   14223 N  N   . LEU I  1 42  ? 26.470  32.372  21.679 1.00 65.20  ? 33  LEU I N   1 
ATOM   14224 C  CA  . LEU I  1 42  ? 25.589  33.342  22.293 1.00 63.17  ? 33  LEU I CA  1 
ATOM   14225 C  C   . LEU I  1 42  ? 25.544  34.577  21.431 1.00 65.16  ? 33  LEU I C   1 
ATOM   14226 O  O   . LEU I  1 42  ? 26.576  35.117  21.049 1.00 69.36  ? 33  LEU I O   1 
ATOM   14227 C  CB  . LEU I  1 42  ? 26.100  33.705  23.687 1.00 62.38  ? 33  LEU I CB  1 
ATOM   14228 C  CG  . LEU I  1 42  ? 25.065  33.852  24.797 1.00 59.23  ? 33  LEU I CG  1 
ATOM   14229 C  CD1 . LEU I  1 42  ? 24.528  32.497  25.228 1.00 64.94  ? 33  LEU I CD1 1 
ATOM   14230 C  CD2 . LEU I  1 42  ? 25.705  34.538  25.956 1.00 55.60  ? 33  LEU I CD2 1 
ATOM   14231 N  N   . SER I  1 43  ? 24.335  35.007  21.107 1.00 70.62  ? 34  SER I N   1 
ATOM   14232 C  CA  . SER I  1 43  ? 24.132  36.248  20.380 1.00 71.52  ? 34  SER I CA  1 
ATOM   14233 C  C   . SER I  1 43  ? 22.900  36.980  20.919 1.00 71.61  ? 34  SER I C   1 
ATOM   14234 O  O   . SER I  1 43  ? 21.921  36.358  21.334 1.00 67.35  ? 34  SER I O   1 
ATOM   14235 C  CB  . SER I  1 43  ? 23.988  35.983  18.880 1.00 62.07  ? 34  SER I CB  1 
ATOM   14236 O  OG  . SER I  1 43  ? 24.129  37.187  18.136 1.00 67.93  ? 34  SER I OG  1 
ATOM   14237 N  N   . PHE I  1 44  ? 22.951  38.306  20.914 1.00 70.22  ? 35  PHE I N   1 
ATOM   14238 C  CA  . PHE I  1 44  ? 21.810  39.093  21.344 1.00 62.79  ? 35  PHE I CA  1 
ATOM   14239 C  C   . PHE I  1 44  ? 21.253  39.949  20.216 1.00 61.34  ? 35  PHE I C   1 
ATOM   14240 O  O   . PHE I  1 44  ? 21.988  40.365  19.328 1.00 62.51  ? 35  PHE I O   1 
ATOM   14241 C  CB  . PHE I  1 44  ? 22.211  39.984  22.515 1.00 62.69  ? 35  PHE I CB  1 
ATOM   14242 C  CG  . PHE I  1 44  ? 22.747  39.228  23.686 1.00 65.01  ? 35  PHE I CG  1 
ATOM   14243 C  CD1 . PHE I  1 44  ? 21.895  38.749  24.663 1.00 62.73  ? 35  PHE I CD1 1 
ATOM   14244 C  CD2 . PHE I  1 44  ? 24.100  38.982  23.805 1.00 65.46  ? 35  PHE I CD2 1 
ATOM   14245 C  CE1 . PHE I  1 44  ? 22.386  38.046  25.731 1.00 58.77  ? 35  PHE I CE1 1 
ATOM   14246 C  CE2 . PHE I  1 44  ? 24.592  38.288  24.881 1.00 61.92  ? 35  PHE I CE2 1 
ATOM   14247 C  CZ  . PHE I  1 44  ? 23.736  37.817  25.838 1.00 61.18  ? 35  PHE I CZ  1 
ATOM   14248 N  N   . SER I  1 45  ? 19.944  40.171  20.247 1.00 57.79  ? 36  SER I N   1 
ATOM   14249 C  CA  . SER I  1 45  ? 19.334  41.285  19.533 1.00 63.82  ? 36  SER I CA  1 
ATOM   14250 C  C   . SER I  1 45  ? 18.409  42.060  20.473 1.00 60.59  ? 36  SER I C   1 
ATOM   14251 O  O   . SER I  1 45  ? 17.521  41.500  21.101 1.00 59.11  ? 36  SER I O   1 
ATOM   14252 C  CB  . SER I  1 45  ? 18.606  40.841  18.258 1.00 55.79  ? 36  SER I CB  1 
ATOM   14253 O  OG  . SER I  1 45  ? 17.737  39.753  18.495 1.00 64.14  ? 36  SER I OG  1 
ATOM   14254 N  N   . LEU I  1 46  ? 18.646  43.359  20.571 1.00 67.37  ? 37  LEU I N   1 
ATOM   14255 C  CA  . LEU I  1 46  ? 17.870  44.231  21.435 1.00 57.72  ? 37  LEU I CA  1 
ATOM   14256 C  C   . LEU I  1 46  ? 16.557  44.645  20.800 1.00 61.29  ? 37  LEU I C   1 
ATOM   14257 O  O   . LEU I  1 46  ? 16.499  45.013  19.621 1.00 61.46  ? 37  LEU I O   1 
ATOM   14258 C  CB  . LEU I  1 46  ? 18.667  45.485  21.734 1.00 60.19  ? 37  LEU I CB  1 
ATOM   14259 C  CG  . LEU I  1 46  ? 18.857  45.817  23.197 1.00 67.46  ? 37  LEU I CG  1 
ATOM   14260 C  CD1 . LEU I  1 46  ? 19.372  44.581  23.887 1.00 75.01  ? 37  LEU I CD1 1 
ATOM   14261 C  CD2 . LEU I  1 46  ? 19.827  46.982  23.355 1.00 68.75  ? 37  LEU I CD2 1 
ATOM   14262 N  N   . LEU I  1 47  ? 15.517  44.616  21.619 1.00 56.28  ? 38  LEU I N   1 
ATOM   14263 C  CA  . LEU I  1 47  ? 14.160  44.986  21.229 1.00 60.87  ? 38  LEU I CA  1 
ATOM   14264 C  C   . LEU I  1 47  ? 13.768  46.342  21.819 1.00 62.73  ? 38  LEU I C   1 
ATOM   14265 O  O   . LEU I  1 47  ? 13.313  47.227  21.092 1.00 62.60  ? 38  LEU I O   1 
ATOM   14266 C  CB  . LEU I  1 47  ? 13.135  43.902  21.560 1.00 58.00  ? 38  LEU I CB  1 
ATOM   14267 C  CG  . LEU I  1 47  ? 12.800  42.998  20.382 1.00 56.17  ? 38  LEU I CG  1 
ATOM   14268 C  CD1 . LEU I  1 47  ? 14.065  42.358  19.877 1.00 61.66  ? 38  LEU I CD1 1 
ATOM   14269 C  CD2 . LEU I  1 47  ? 11.785  41.960  20.799 1.00 64.93  ? 38  LEU I CD2 1 
ATOM   14270 N  N   . ASP I  1 48  ? 13.815  46.460  23.141 1.00 48.07  ? 39  ASP I N   1 
ATOM   14271 C  CA  . ASP I  1 48  ? 13.437  47.706  23.779 1.00 52.50  ? 39  ASP I CA  1 
ATOM   14272 C  C   . ASP I  1 48  ? 14.200  47.942  25.077 1.00 55.11  ? 39  ASP I C   1 
ATOM   14273 O  O   . ASP I  1 48  ? 14.550  47.009  25.779 1.00 58.01  ? 39  ASP I O   1 
ATOM   14274 C  CB  . ASP I  1 48  ? 11.930  47.692  24.061 1.00 55.39  ? 39  ASP I CB  1 
ATOM   14275 C  CG  . ASP I  1 48  ? 11.335  49.079  24.147 1.00 61.24  ? 39  ASP I CG  1 
ATOM   14276 O  OD1 . ASP I  1 48  ? 12.104  50.062  24.123 1.00 59.92  ? 39  ASP I OD1 1 
ATOM   14277 O  OD2 . ASP I  1 48  ? 10.096  49.188  24.247 1.00 62.26  ? 39  ASP I OD2 1 
ATOM   14278 N  N   . ILE I  1 49  ? 14.466  49.197  25.402 1.00 60.59  ? 40  ILE I N   1 
ATOM   14279 C  CA  . ILE I  1 49  ? 14.778  49.527  26.781 1.00 55.34  ? 40  ILE I CA  1 
ATOM   14280 C  C   . ILE I  1 49  ? 13.497  50.159  27.307 1.00 58.86  ? 40  ILE I C   1 
ATOM   14281 O  O   . ILE I  1 49  ? 13.154  51.279  26.942 1.00 63.09  ? 40  ILE I O   1 
ATOM   14282 C  CB  . ILE I  1 49  ? 15.970  50.488  26.868 1.00 50.58  ? 40  ILE I CB  1 
ATOM   14283 C  CG1 . ILE I  1 49  ? 17.241  49.776  26.423 1.00 50.72  ? 40  ILE I CG1 1 
ATOM   14284 C  CG2 . ILE I  1 49  ? 16.152  51.005  28.261 1.00 50.86  ? 40  ILE I CG2 1 
ATOM   14285 C  CD1 . ILE I  1 49  ? 18.481  50.505  26.796 1.00 48.87  ? 40  ILE I CD1 1 
ATOM   14286 N  N   . VAL I  1 50  ? 12.782  49.437  28.161 1.00 54.15  ? 41  VAL I N   1 
ATOM   14287 C  CA  . VAL I  1 50  ? 11.454  49.880  28.554 1.00 60.13  ? 41  VAL I CA  1 
ATOM   14288 C  C   . VAL I  1 50  ? 11.512  50.987  29.586 1.00 61.21  ? 41  VAL I C   1 
ATOM   14289 O  O   . VAL I  1 50  ? 10.720  51.938  29.537 1.00 62.91  ? 41  VAL I O   1 
ATOM   14290 C  CB  . VAL I  1 50  ? 10.627  48.747  29.134 1.00 54.80  ? 41  VAL I CB  1 
ATOM   14291 C  CG1 . VAL I  1 50  ? 9.247   49.245  29.486 1.00 52.70  ? 41  VAL I CG1 1 
ATOM   14292 C  CG2 . VAL I  1 50  ? 10.536  47.637  28.143 1.00 57.58  ? 41  VAL I CG2 1 
ATOM   14293 N  N   . LYS I  1 51  ? 12.432  50.833  30.538 1.00 60.97  ? 42  LYS I N   1 
ATOM   14294 C  CA  . LYS I  1 51  ? 12.512  51.720  31.690 1.00 63.12  ? 42  LYS I CA  1 
ATOM   14295 C  C   . LYS I  1 51  ? 13.947  51.906  32.170 1.00 61.15  ? 42  LYS I C   1 
ATOM   14296 O  O   . LYS I  1 51  ? 14.683  50.929  32.295 1.00 56.53  ? 42  LYS I O   1 
ATOM   14297 C  CB  . LYS I  1 51  ? 11.710  51.079  32.814 1.00 57.36  ? 42  LYS I CB  1 
ATOM   14298 C  CG  . LYS I  1 51  ? 11.151  52.025  33.808 1.00 60.47  ? 42  LYS I CG  1 
ATOM   14299 C  CD  . LYS I  1 51  ? 10.852  51.272  35.082 1.00 72.33  ? 42  LYS I CD  1 
ATOM   14300 C  CE  . LYS I  1 51  ? 9.434   50.754  35.135 1.00 77.76  ? 42  LYS I CE  1 
ATOM   14301 N  NZ  . LYS I  1 51  ? 9.220   50.073  36.445 1.00 68.34  ? 42  LYS I NZ  1 
ATOM   14302 N  N   . ALA I  1 52  ? 14.334  53.138  32.498 1.00 64.22  ? 43  ALA I N   1 
ATOM   14303 C  CA  . ALA I  1 52  ? 15.584  53.376  33.233 1.00 61.76  ? 43  ALA I CA  1 
ATOM   14304 C  C   . ALA I  1 52  ? 15.165  53.990  34.541 1.00 65.84  ? 43  ALA I C   1 
ATOM   14305 O  O   . ALA I  1 52  ? 14.403  54.953  34.538 1.00 69.80  ? 43  ALA I O   1 
ATOM   14306 C  CB  . ALA I  1 52  ? 16.514  54.317  32.484 1.00 60.35  ? 43  ALA I CB  1 
ATOM   14307 N  N   . ASP I  1 53  ? 15.620  53.428  35.661 1.00 67.46  ? 44  ASP I N   1 
ATOM   14308 C  CA  . ASP I  1 53  ? 15.185  53.921  36.976 1.00 62.98  ? 44  ASP I CA  1 
ATOM   14309 C  C   . ASP I  1 53  ? 16.322  54.539  37.822 1.00 63.84  ? 44  ASP I C   1 
ATOM   14310 O  O   . ASP I  1 53  ? 17.219  53.832  38.276 1.00 66.52  ? 44  ASP I O   1 
ATOM   14311 C  CB  . ASP I  1 53  ? 14.421  52.827  37.736 1.00 59.38  ? 44  ASP I CB  1 
ATOM   14312 C  CG  . ASP I  1 53  ? 13.615  53.377  38.894 1.00 64.30  ? 44  ASP I CG  1 
ATOM   14313 O  OD1 . ASP I  1 53  ? 14.025  54.410  39.444 1.00 70.66  ? 44  ASP I OD1 1 
ATOM   14314 O  OD2 . ASP I  1 53  ? 12.584  52.785  39.268 1.00 59.24  ? 44  ASP I OD2 1 
ATOM   14315 N  N   . SER I  1 54  ? 16.273  55.860  38.015 1.00 65.58  ? 45  SER I N   1 
ATOM   14316 C  CA  . SER I  1 54  ? 17.294  56.580  38.789 1.00 65.94  ? 45  SER I CA  1 
ATOM   14317 C  C   . SER I  1 54  ? 17.203  56.285  40.301 1.00 69.25  ? 45  SER I C   1 
ATOM   14318 O  O   . SER I  1 54  ? 18.224  56.252  40.998 1.00 69.81  ? 45  SER I O   1 
ATOM   14319 C  CB  . SER I  1 54  ? 17.224  58.100  38.547 1.00 56.52  ? 45  SER I CB  1 
ATOM   14320 O  OG  . SER I  1 54  ? 16.792  58.432  37.239 1.00 65.24  ? 45  SER I OG  1 
ATOM   14321 N  N   . SER I  1 55  ? 15.985  56.068  40.817 1.00 60.71  ? 46  SER I N   1 
ATOM   14322 C  CA  . SER I  1 55  ? 15.801  55.819  42.242 1.00 66.52  ? 46  SER I CA  1 
ATOM   14323 C  C   . SER I  1 55  ? 16.413  54.499  42.703 1.00 64.11  ? 46  SER I C   1 
ATOM   14324 O  O   . SER I  1 55  ? 17.057  54.447  43.757 1.00 63.97  ? 46  SER I O   1 
ATOM   14325 C  CB  . SER I  1 55  ? 14.325  55.918  42.641 1.00 63.74  ? 46  SER I CB  1 
ATOM   14326 O  OG  . SER I  1 55  ? 13.551  54.922  42.024 1.00 69.09  ? 46  SER I OG  1 
ATOM   14327 N  N   . THR I  1 56  ? 16.176  53.433  41.941 1.00 64.45  ? 47  THR I N   1 
ATOM   14328 C  CA  . THR I  1 56  ? 16.761  52.132  42.254 1.00 62.24  ? 47  THR I CA  1 
ATOM   14329 C  C   . THR I  1 56  ? 18.031  51.766  41.462 1.00 55.57  ? 47  THR I C   1 
ATOM   14330 O  O   . THR I  1 56  ? 18.661  50.752  41.744 1.00 50.48  ? 47  THR I O   1 
ATOM   14331 C  CB  . THR I  1 56  ? 15.735  51.017  42.074 1.00 53.45  ? 47  THR I CB  1 
ATOM   14332 O  OG1 . THR I  1 56  ? 15.393  50.933  40.696 1.00 60.63  ? 47  THR I OG1 1 
ATOM   14333 C  CG2 . THR I  1 56  ? 14.470  51.304  42.845 1.00 53.82  ? 47  THR I CG2 1 
ATOM   14334 N  N   . ASN I  1 57  ? 18.435  52.604  40.515 1.00 57.82  ? 48  ASN I N   1 
ATOM   14335 C  CA  . ASN I  1 57  ? 19.490  52.233  39.557 1.00 61.64  ? 48  ASN I CA  1 
ATOM   14336 C  C   . ASN I  1 57  ? 19.280  50.888  38.844 1.00 62.02  ? 48  ASN I C   1 
ATOM   14337 O  O   . ASN I  1 57  ? 20.148  50.020  38.870 1.00 62.73  ? 48  ASN I O   1 
ATOM   14338 C  CB  . ASN I  1 57  ? 20.876  52.288  40.190 1.00 62.57  ? 48  ASN I CB  1 
ATOM   14339 C  CG  . ASN I  1 57  ? 21.506  53.647  40.060 1.00 64.68  ? 48  ASN I CG  1 
ATOM   14340 O  OD1 . ASN I  1 57  ? 20.864  54.588  39.606 1.00 65.68  ? 48  ASN I OD1 1 
ATOM   14341 N  ND2 . ASN I  1 57  ? 22.763  53.763  40.457 1.00 64.65  ? 48  ASN I ND2 1 
ATOM   14342 N  N   . GLU I  1 58  ? 18.129  50.745  38.204 1.00 57.28  ? 49  GLU I N   1 
ATOM   14343 C  CA  . GLU I  1 58  ? 17.752  49.488  37.591 1.00 56.13  ? 49  GLU I CA  1 
ATOM   14344 C  C   . GLU I  1 58  ? 17.198  49.781  36.221 1.00 59.03  ? 49  GLU I C   1 
ATOM   14345 O  O   . GLU I  1 58  ? 16.343  50.649  36.067 1.00 64.22  ? 49  GLU I O   1 
ATOM   14346 C  CB  . GLU I  1 58  ? 16.636  48.838  38.398 1.00 56.66  ? 49  GLU I CB  1 
ATOM   14347 C  CG  . GLU I  1 58  ? 17.038  48.124  39.669 1.00 52.96  ? 49  GLU I CG  1 
ATOM   14348 C  CD  . GLU I  1 58  ? 15.825  47.530  40.362 1.00 61.35  ? 49  GLU I CD  1 
ATOM   14349 O  OE1 . GLU I  1 58  ? 15.068  48.304  40.975 1.00 71.14  ? 49  GLU I OE1 1 
ATOM   14350 O  OE2 . GLU I  1 58  ? 15.607  46.301  40.284 1.00 62.37  ? 49  GLU I OE2 1 
ATOM   14351 N  N   . VAL I  1 59  ? 17.643  49.017  35.230 1.00 54.61  ? 50  VAL I N   1 
ATOM   14352 C  CA  . VAL I  1 59  ? 17.127  49.217  33.887 1.00 58.25  ? 50  VAL I CA  1 
ATOM   14353 C  C   . VAL I  1 59  ? 16.414  47.990  33.365 1.00 55.32  ? 50  VAL I C   1 
ATOM   14354 O  O   . VAL I  1 59  ? 16.886  46.878  33.529 1.00 54.61  ? 50  VAL I O   1 
ATOM   14355 C  CB  . VAL I  1 59  ? 18.238  49.633  32.927 1.00 62.63  ? 50  VAL I CB  1 
ATOM   14356 C  CG1 . VAL I  1 59  ? 17.703  49.753  31.530 1.00 57.13  ? 50  VAL I CG1 1 
ATOM   14357 C  CG2 . VAL I  1 59  ? 18.805  50.963  33.375 1.00 71.86  ? 50  VAL I CG2 1 
ATOM   14358 N  N   . ASP I  1 60  ? 15.265  48.211  32.740 1.00 53.16  ? 51  ASP I N   1 
ATOM   14359 C  CA  . ASP I  1 60  ? 14.480  47.133  32.162 1.00 51.48  ? 51  ASP I CA  1 
ATOM   14360 C  C   . ASP I  1 60  ? 14.766  46.956  30.682 1.00 51.80  ? 51  ASP I C   1 
ATOM   14361 O  O   . ASP I  1 60  ? 14.844  47.908  29.926 1.00 52.82  ? 51  ASP I O   1 
ATOM   14362 C  CB  . ASP I  1 60  ? 12.993  47.360  32.392 1.00 53.61  ? 51  ASP I CB  1 
ATOM   14363 C  CG  . ASP I  1 60  ? 12.606  47.176  33.832 1.00 59.69  ? 51  ASP I CG  1 
ATOM   14364 O  OD1 . ASP I  1 60  ? 13.447  46.701  34.627 1.00 60.44  ? 51  ASP I OD1 1 
ATOM   14365 O  OD2 . ASP I  1 60  ? 11.457  47.500  34.174 1.00 72.12  ? 51  ASP I OD2 1 
ATOM   14366 N  N   . LEU I  1 61  ? 14.908  45.711  30.274 1.00 53.79  ? 52  LEU I N   1 
ATOM   14367 C  CA  . LEU I  1 61  ? 15.380  45.412  28.943 1.00 51.74  ? 52  LEU I CA  1 
ATOM   14368 C  C   . LEU I  1 61  ? 14.600  44.241  28.339 1.00 54.69  ? 52  LEU I C   1 
ATOM   14369 O  O   . LEU I  1 61  ? 14.379  43.213  28.988 1.00 56.53  ? 52  LEU I O   1 
ATOM   14370 C  CB  . LEU I  1 61  ? 16.877  45.115  29.022 1.00 49.85  ? 52  LEU I CB  1 
ATOM   14371 C  CG  . LEU I  1 61  ? 17.609  44.635  27.776 1.00 63.90  ? 52  LEU I CG  1 
ATOM   14372 C  CD1 . LEU I  1 61  ? 17.199  45.454  26.559 1.00 57.53  ? 52  LEU I CD1 1 
ATOM   14373 C  CD2 . LEU I  1 61  ? 19.121  44.685  28.010 1.00 57.42  ? 52  LEU I CD2 1 
ATOM   14374 N  N   . VAL I  1 62  ? 14.153  44.408  27.102 1.00 48.22  ? 53  VAL I N   1 
ATOM   14375 C  CA  . VAL I  1 62  ? 13.538  43.302  26.369 1.00 53.94  ? 53  VAL I CA  1 
ATOM   14376 C  C   . VAL I  1 62  ? 14.446  42.891  25.231 1.00 47.80  ? 53  VAL I C   1 
ATOM   14377 O  O   . VAL I  1 62  ? 14.804  43.704  24.406 1.00 50.36  ? 53  VAL I O   1 
ATOM   14378 C  CB  . VAL I  1 62  ? 12.168  43.657  25.788 1.00 46.30  ? 53  VAL I CB  1 
ATOM   14379 C  CG1 . VAL I  1 62  ? 11.780  42.622  24.798 1.00 45.04  ? 53  VAL I CG1 1 
ATOM   14380 C  CG2 . VAL I  1 62  ? 11.116  43.753  26.886 1.00 42.18  ? 53  VAL I CG2 1 
ATOM   14381 N  N   . TYR I  1 63  ? 14.827  41.626  25.190 1.00 49.90  ? 54  TYR I N   1 
ATOM   14382 C  CA  . TYR I  1 63  ? 15.706  41.172  24.129 1.00 54.68  ? 54  TYR I CA  1 
ATOM   14383 C  C   . TYR I  1 63  ? 15.508  39.710  23.754 1.00 56.72  ? 54  TYR I C   1 
ATOM   14384 O  O   . TYR I  1 63  ? 14.745  38.982  24.386 1.00 53.96  ? 54  TYR I O   1 
ATOM   14385 C  CB  . TYR I  1 63  ? 17.157  41.383  24.550 1.00 52.80  ? 54  TYR I CB  1 
ATOM   14386 C  CG  . TYR I  1 63  ? 17.529  40.619  25.790 1.00 53.96  ? 54  TYR I CG  1 
ATOM   14387 C  CD1 . TYR I  1 63  ? 18.207  39.416  25.711 1.00 52.11  ? 54  TYR I CD1 1 
ATOM   14388 C  CD2 . TYR I  1 63  ? 17.186  41.098  27.047 1.00 58.71  ? 54  TYR I CD2 1 
ATOM   14389 C  CE1 . TYR I  1 63  ? 18.548  38.711  26.857 1.00 58.98  ? 54  TYR I CE1 1 
ATOM   14390 C  CE2 . TYR I  1 63  ? 17.514  40.402  28.199 1.00 57.15  ? 54  TYR I CE2 1 
ATOM   14391 C  CZ  . TYR I  1 63  ? 18.202  39.208  28.105 1.00 59.49  ? 54  TYR I CZ  1 
ATOM   14392 O  OH  . TYR I  1 63  ? 18.535  38.515  29.259 1.00 58.95  ? 54  TYR I OH  1 
ATOM   14393 N  N   . TRP I  1 64  ? 16.238  39.292  22.728 1.00 54.76  ? 55  TRP I N   1 
ATOM   14394 C  CA  . TRP I  1 64  ? 16.265  37.908  22.317 1.00 58.24  ? 55  TRP I CA  1 
ATOM   14395 C  C   . TRP I  1 64  ? 17.660  37.386  22.541 1.00 60.33  ? 55  TRP I C   1 
ATOM   14396 O  O   . TRP I  1 64  ? 18.642  38.021  22.157 1.00 58.14  ? 55  TRP I O   1 
ATOM   14397 C  CB  . TRP I  1 64  ? 15.946  37.774  20.840 1.00 62.59  ? 55  TRP I CB  1 
ATOM   14398 C  CG  . TRP I  1 64  ? 14.588  38.227  20.448 1.00 68.63  ? 55  TRP I CG  1 
ATOM   14399 C  CD1 . TRP I  1 64  ? 13.478  38.333  21.245 1.00 66.67  ? 55  TRP I CD1 1 
ATOM   14400 C  CD2 . TRP I  1 64  ? 14.191  38.652  19.150 1.00 71.07  ? 55  TRP I CD2 1 
ATOM   14401 N  NE1 . TRP I  1 64  ? 12.407  38.792  20.510 1.00 60.12  ? 55  TRP I NE1 1 
ATOM   14402 C  CE2 . TRP I  1 64  ? 12.823  38.999  19.218 1.00 70.07  ? 55  TRP I CE2 1 
ATOM   14403 C  CE3 . TRP I  1 64  ? 14.861  38.776  17.927 1.00 67.88  ? 55  TRP I CE3 1 
ATOM   14404 C  CZ2 . TRP I  1 64  ? 12.116  39.458  18.114 1.00 74.10  ? 55  TRP I CZ2 1 
ATOM   14405 C  CZ3 . TRP I  1 64  ? 14.160  39.228  16.836 1.00 81.56  ? 55  TRP I CZ3 1 
ATOM   14406 C  CH2 . TRP I  1 64  ? 12.799  39.564  16.933 1.00 81.31  ? 55  TRP I CH2 1 
ATOM   14407 N  N   . GLU I  1 65  ? 17.745  36.213  23.149 1.00 53.61  ? 56  GLU I N   1 
ATOM   14408 C  CA  . GLU I  1 65  ? 19.031  35.624  23.427 1.00 58.22  ? 56  GLU I CA  1 
ATOM   14409 C  C   . GLU I  1 65  ? 19.163  34.362  22.614 1.00 60.57  ? 56  GLU I C   1 
ATOM   14410 O  O   . GLU I  1 65  ? 18.436  33.408  22.830 1.00 61.20  ? 56  GLU I O   1 
ATOM   14411 C  CB  . GLU I  1 65  ? 19.130  35.305  24.910 1.00 66.70  ? 56  GLU I CB  1 
ATOM   14412 C  CG  . GLU I  1 65  ? 20.491  34.881  25.390 1.00 58.26  ? 56  GLU I CG  1 
ATOM   14413 C  CD  . GLU I  1 65  ? 20.463  34.614  26.860 1.00 59.23  ? 56  GLU I CD  1 
ATOM   14414 O  OE1 . GLU I  1 65  ? 19.605  35.200  27.549 1.00 58.44  ? 56  GLU I OE1 1 
ATOM   14415 O  OE2 . GLU I  1 65  ? 21.276  33.803  27.329 1.00 72.87  ? 56  GLU I OE2 1 
ATOM   14416 N  N   . GLN I  1 66  ? 20.094  34.363  21.673 1.00 65.76  ? 57  GLN I N   1 
ATOM   14417 C  CA  . GLN I  1 66  ? 20.268  33.232  20.790 1.00 64.24  ? 57  GLN I CA  1 
ATOM   14418 C  C   . GLN I  1 66  ? 21.358  32.302  21.311 1.00 64.86  ? 57  GLN I C   1 
ATOM   14419 O  O   . GLN I  1 66  ? 22.536  32.653  21.365 1.00 66.13  ? 57  GLN I O   1 
ATOM   14420 C  CB  . GLN I  1 66  ? 20.587  33.711  19.380 1.00 72.30  ? 57  GLN I CB  1 
ATOM   14421 C  CG  . GLN I  1 66  ? 20.264  32.689  18.314 1.00 82.66  ? 57  GLN I CG  1 
ATOM   14422 C  CD  . GLN I  1 66  ? 21.383  32.517  17.316 1.00 86.50  ? 57  GLN I CD  1 
ATOM   14423 O  OE1 . GLN I  1 66  ? 22.567  32.637  17.656 1.00 89.20  ? 57  GLN I OE1 1 
ATOM   14424 N  NE2 . GLN I  1 66  ? 21.019  32.228  16.072 1.00 79.25  ? 57  GLN I NE2 1 
ATOM   14425 N  N   . GLN I  1 67  ? 20.942  31.106  21.702 1.00 68.28  ? 58  GLN I N   1 
ATOM   14426 C  CA  . GLN I  1 67  ? 21.848  30.101  22.230 1.00 62.75  ? 58  GLN I CA  1 
ATOM   14427 C  C   . GLN I  1 67  ? 21.922  28.923  21.270 1.00 58.06  ? 58  GLN I C   1 
ATOM   14428 O  O   . GLN I  1 67  ? 20.904  28.434  20.804 1.00 60.42  ? 58  GLN I O   1 
ATOM   14429 C  CB  . GLN I  1 67  ? 21.359  29.637  23.598 1.00 53.25  ? 58  GLN I CB  1 
ATOM   14430 C  CG  . GLN I  1 67  ? 21.209  30.763  24.571 1.00 65.20  ? 58  GLN I CG  1 
ATOM   14431 C  CD  . GLN I  1 67  ? 20.484  30.358  25.826 1.00 66.75  ? 58  GLN I CD  1 
ATOM   14432 O  OE1 . GLN I  1 67  ? 20.454  29.183  26.187 1.00 70.90  ? 58  GLN I OE1 1 
ATOM   14433 N  NE2 . GLN I  1 67  ? 19.886  31.331  26.501 1.00 62.96  ? 58  GLN I NE2 1 
ATOM   14434 N  N   . SER I  1 68  ? 23.131  28.490  20.950 1.00 56.91  ? 59  SER I N   1 
ATOM   14435 C  CA  . SER I  1 68  ? 23.298  27.258  20.198 1.00 61.80  ? 59  SER I CA  1 
ATOM   14436 C  C   . SER I  1 68  ? 24.511  26.465  20.650 1.00 62.84  ? 59  SER I C   1 
ATOM   14437 O  O   . SER I  1 68  ? 25.509  27.018  21.116 1.00 64.36  ? 59  SER I O   1 
ATOM   14438 C  CB  . SER I  1 68  ? 23.307  27.484  18.674 1.00 64.20  ? 59  SER I CB  1 
ATOM   14439 O  OG  . SER I  1 68  ? 24.006  28.658  18.312 1.00 66.82  ? 59  SER I OG  1 
ATOM   14440 N  N   . TRP I  1 69  ? 24.374  25.151  20.535 1.00 57.96  ? 60  TRP I N   1 
ATOM   14441 C  CA  . TRP I  1 69  ? 25.417  24.204  20.860 1.00 60.43  ? 60  TRP I CA  1 
ATOM   14442 C  C   . TRP I  1 69  ? 25.069  22.978  20.034 1.00 64.20  ? 60  TRP I C   1 
ATOM   14443 O  O   . TRP I  1 69  ? 24.045  22.961  19.347 1.00 56.86  ? 60  TRP I O   1 
ATOM   14444 C  CB  . TRP I  1 69  ? 25.406  23.874  22.362 1.00 57.76  ? 60  TRP I CB  1 
ATOM   14445 C  CG  . TRP I  1 69  ? 24.105  23.291  22.829 1.00 52.64  ? 60  TRP I CG  1 
ATOM   14446 C  CD1 . TRP I  1 69  ? 23.811  21.972  23.008 1.00 51.51  ? 60  TRP I CD1 1 
ATOM   14447 C  CD2 . TRP I  1 69  ? 22.911  24.013  23.140 1.00 52.62  ? 60  TRP I CD2 1 
ATOM   14448 N  NE1 . TRP I  1 69  ? 22.513  21.830  23.427 1.00 52.20  ? 60  TRP I NE1 1 
ATOM   14449 C  CE2 . TRP I  1 69  ? 21.937  23.068  23.510 1.00 50.53  ? 60  TRP I CE2 1 
ATOM   14450 C  CE3 . TRP I  1 69  ? 22.577  25.375  23.155 1.00 53.84  ? 60  TRP I CE3 1 
ATOM   14451 C  CZ2 . TRP I  1 69  ? 20.650  23.437  23.891 1.00 53.94  ? 60  TRP I CZ2 1 
ATOM   14452 C  CZ3 . TRP I  1 69  ? 21.299  25.741  23.537 1.00 52.34  ? 60  TRP I CZ3 1 
ATOM   14453 C  CH2 . TRP I  1 69  ? 20.352  24.776  23.903 1.00 54.03  ? 60  TRP I CH2 1 
ATOM   14454 N  N   . LYS I  1 70  ? 25.902  21.950  20.125 1.00 62.97  ? 61  LYS I N   1 
ATOM   14455 C  CA  . LYS I  1 70  ? 25.718  20.749  19.339 1.00 59.85  ? 61  LYS I CA  1 
ATOM   14456 C  C   . LYS I  1 70  ? 25.989  19.521  20.192 1.00 64.80  ? 61  LYS I C   1 
ATOM   14457 O  O   . LYS I  1 70  ? 26.977  19.482  20.918 1.00 65.82  ? 61  LYS I O   1 
ATOM   14458 C  CB  . LYS I  1 70  ? 26.649  20.790  18.126 1.00 63.63  ? 61  LYS I CB  1 
ATOM   14459 C  CG  . LYS I  1 70  ? 27.218  19.449  17.722 1.00 77.57  ? 61  LYS I CG  1 
ATOM   14460 C  CD  . LYS I  1 70  ? 27.307  19.315  16.202 1.00 82.69  ? 61  LYS I CD  1 
ATOM   14461 C  CE  . LYS I  1 70  ? 27.728  17.904  15.799 1.00 84.36  ? 61  LYS I CE  1 
ATOM   14462 N  NZ  . LYS I  1 70  ? 27.732  17.709  14.319 1.00 94.33  ? 61  LYS I NZ  1 
ATOM   14463 N  N   . LEU I  1 71  ? 25.104  18.528  20.110 1.00 68.34  ? 62  LEU I N   1 
ATOM   14464 C  CA  . LEU I  1 71  ? 25.283  17.257  20.824 1.00 68.55  ? 62  LEU I CA  1 
ATOM   14465 C  C   . LEU I  1 71  ? 25.219  16.044  19.896 1.00 67.76  ? 62  LEU I C   1 
ATOM   14466 O  O   . LEU I  1 71  ? 24.225  15.852  19.209 1.00 70.44  ? 62  LEU I O   1 
ATOM   14467 C  CB  . LEU I  1 71  ? 24.218  17.093  21.920 1.00 64.24  ? 62  LEU I CB  1 
ATOM   14468 C  CG  . LEU I  1 71  ? 24.242  18.082  23.089 1.00 62.86  ? 62  LEU I CG  1 
ATOM   14469 C  CD1 . LEU I  1 71  ? 23.057  17.888  24.023 1.00 63.24  ? 62  LEU I CD1 1 
ATOM   14470 C  CD2 . LEU I  1 71  ? 25.539  17.959  23.845 1.00 63.72  ? 62  LEU I CD2 1 
ATOM   14471 N  N   . ASN I  1 72  ? 26.258  15.209  19.907 1.00 71.41  ? 63  ASN I N   1 
ATOM   14472 C  CA  . ASN I  1 72  ? 26.236  13.938  19.175 1.00 68.33  ? 63  ASN I CA  1 
ATOM   14473 C  C   . ASN I  1 72  ? 25.004  13.103  19.532 1.00 65.29  ? 63  ASN I C   1 
ATOM   14474 O  O   . ASN I  1 72  ? 24.442  12.448  18.672 1.00 71.43  ? 63  ASN I O   1 
ATOM   14475 C  CB  . ASN I  1 72  ? 27.521  13.130  19.408 1.00 68.63  ? 63  ASN I CB  1 
ATOM   14476 C  CG  . ASN I  1 72  ? 28.774  13.847  18.903 1.00 82.00  ? 63  ASN I CG  1 
ATOM   14477 O  OD1 . ASN I  1 72  ? 28.817  14.330  17.767 1.00 77.77  ? 63  ASN I OD1 1 
ATOM   14478 N  ND2 . ASN I  1 72  ? 29.799  13.925  19.758 1.00 70.59  ? 63  ASN I ND2 1 
ATOM   14479 N  N   . SER I  1 73  ? 24.585  13.158  20.796 1.00 67.70  ? 64  SER I N   1 
ATOM   14480 C  CA  . SER I  1 73  ? 23.367  12.473  21.227 1.00 60.75  ? 64  SER I CA  1 
ATOM   14481 C  C   . SER I  1 73  ? 22.129  12.925  20.434 1.00 62.21  ? 64  SER I C   1 
ATOM   14482 O  O   . SER I  1 73  ? 21.099  12.255  20.448 1.00 64.25  ? 64  SER I O   1 
ATOM   14483 C  CB  . SER I  1 73  ? 23.127  12.695  22.727 1.00 68.74  ? 64  SER I CB  1 
ATOM   14484 O  OG  . SER I  1 73  ? 24.329  13.018  23.419 1.00 80.66  ? 64  SER I OG  1 
ATOM   14485 N  N   . LEU I  1 74  ? 22.204  14.068  19.765 1.00 65.60  ? 65  LEU I N   1 
ATOM   14486 C  CA  . LEU I  1 74  ? 21.095  14.587  18.952 1.00 64.87  ? 65  LEU I CA  1 
ATOM   14487 C  C   . LEU I  1 74  ? 21.169  14.326  17.435 1.00 68.75  ? 65  LEU I C   1 
ATOM   14488 O  O   . LEU I  1 74  ? 20.285  14.752  16.696 1.00 68.85  ? 65  LEU I O   1 
ATOM   14489 C  CB  . LEU I  1 74  ? 20.885  16.079  19.224 1.00 63.68  ? 65  LEU I CB  1 
ATOM   14490 C  CG  . LEU I  1 74  ? 20.430  16.395  20.647 1.00 60.40  ? 65  LEU I CG  1 
ATOM   14491 C  CD1 . LEU I  1 74  ? 20.193  17.866  20.828 1.00 62.28  ? 65  LEU I CD1 1 
ATOM   14492 C  CD2 . LEU I  1 74  ? 19.175  15.620  20.965 1.00 50.71  ? 65  LEU I CD2 1 
ATOM   14493 N  N   . MET I  1 75  ? 22.213  13.643  16.973 1.00 73.06  ? 66  MET I N   1 
ATOM   14494 C  CA  . MET I  1 75  ? 22.391  13.387  15.546 1.00 66.92  ? 66  MET I CA  1 
ATOM   14495 C  C   . MET I  1 75  ? 21.575  12.195  15.057 1.00 71.31  ? 66  MET I C   1 
ATOM   14496 O  O   . MET I  1 75  ? 21.420  11.199  15.763 1.00 67.08  ? 66  MET I O   1 
ATOM   14497 C  CB  . MET I  1 75  ? 23.858  13.120  15.231 1.00 70.21  ? 66  MET I CB  1 
ATOM   14498 C  CG  . MET I  1 75  ? 24.819  14.061  15.886 1.00 72.48  ? 66  MET I CG  1 
ATOM   14499 S  SD  . MET I  1 75  ? 26.500  13.659  15.407 1.00 79.51  ? 66  MET I SD  1 
ATOM   14500 C  CE  . MET I  1 75  ? 26.571  14.389  13.764 1.00 74.72  ? 66  MET I CE  1 
ATOM   14501 N  N   . TRP I  1 76  ? 21.070  12.312  13.832 1.00 73.38  ? 67  TRP I N   1 
ATOM   14502 C  CA  . TRP I  1 76  ? 20.395  11.220  13.141 1.00 67.86  ? 67  TRP I CA  1 
ATOM   14503 C  C   . TRP I  1 76  ? 20.632  11.366  11.642 1.00 77.58  ? 67  TRP I C   1 
ATOM   14504 O  O   . TRP I  1 76  ? 20.742  12.489  11.132 1.00 69.51  ? 67  TRP I O   1 
ATOM   14505 C  CB  . TRP I  1 76  ? 18.891  11.225  13.440 1.00 64.98  ? 67  TRP I CB  1 
ATOM   14506 C  CG  . TRP I  1 76  ? 18.125  12.387  12.845 1.00 65.39  ? 67  TRP I CG  1 
ATOM   14507 C  CD1 . TRP I  1 76  ? 17.488  12.409  11.648 1.00 64.74  ? 67  TRP I CD1 1 
ATOM   14508 C  CD2 . TRP I  1 76  ? 17.902  13.679  13.439 1.00 67.59  ? 67  TRP I CD2 1 
ATOM   14509 N  NE1 . TRP I  1 76  ? 16.892  13.626  11.448 1.00 64.85  ? 67  TRP I NE1 1 
ATOM   14510 C  CE2 . TRP I  1 76  ? 17.132  14.425  12.532 1.00 64.24  ? 67  TRP I CE2 1 
ATOM   14511 C  CE3 . TRP I  1 76  ? 18.278  14.271  14.651 1.00 63.46  ? 67  TRP I CE3 1 
ATOM   14512 C  CZ2 . TRP I  1 76  ? 16.728  15.730  12.792 1.00 67.80  ? 67  TRP I CZ2 1 
ATOM   14513 C  CZ3 . TRP I  1 76  ? 17.883  15.565  14.904 1.00 64.63  ? 67  TRP I CZ3 1 
ATOM   14514 C  CH2 . TRP I  1 76  ? 17.116  16.283  13.980 1.00 68.61  ? 67  TRP I CH2 1 
ATOM   14515 N  N   . ASP I  1 77  ? 20.734  10.234  10.944 1.00 80.09  ? 68  ASP I N   1 
ATOM   14516 C  CA  . ASP I  1 77  ? 20.757  10.243  9.488  1.00 77.65  ? 68  ASP I CA  1 
ATOM   14517 C  C   . ASP I  1 77  ? 19.326  10.399  8.991  1.00 77.92  ? 68  ASP I C   1 
ATOM   14518 O  O   . ASP I  1 77  ? 18.463  9.571   9.298  1.00 75.81  ? 68  ASP I O   1 
ATOM   14519 C  CB  . ASP I  1 77  ? 21.378  8.958   8.931  1.00 86.70  ? 68  ASP I CB  1 
ATOM   14520 C  CG  . ASP I  1 77  ? 21.251  8.850   7.409  1.00 94.54  ? 68  ASP I CG  1 
ATOM   14521 O  OD1 . ASP I  1 77  ? 21.450  9.873   6.709  1.00 95.52  ? 68  ASP I OD1 1 
ATOM   14522 O  OD2 . ASP I  1 77  ? 20.947  7.739   6.913  1.00 92.68  ? 68  ASP I OD2 1 
ATOM   14523 N  N   . PRO I  1 78  ? 19.067  11.477  8.235  1.00 74.41  ? 69  PRO I N   1 
ATOM   14524 C  CA  . PRO I  1 78  ? 17.724  11.776  7.724  1.00 80.45  ? 69  PRO I CA  1 
ATOM   14525 C  C   . PRO I  1 78  ? 17.104  10.668  6.851  1.00 86.87  ? 69  PRO I C   1 
ATOM   14526 O  O   . PRO I  1 78  ? 15.878  10.528  6.861  1.00 83.68  ? 69  PRO I O   1 
ATOM   14527 C  CB  . PRO I  1 78  ? 17.940  13.061  6.916  1.00 78.63  ? 69  PRO I CB  1 
ATOM   14528 C  CG  . PRO I  1 78  ? 19.118  13.706  7.561  1.00 71.06  ? 69  PRO I CG  1 
ATOM   14529 C  CD  . PRO I  1 78  ? 20.018  12.568  7.957  1.00 73.01  ? 69  PRO I CD  1 
ATOM   14530 N  N   . ASN I  1 79  ? 17.923  9.904   6.124  1.00 89.24  ? 70  ASN I N   1 
ATOM   14531 C  CA  . ASN I  1 79  ? 17.427  8.824   5.263  1.00 90.12  ? 70  ASN I CA  1 
ATOM   14532 C  C   . ASN I  1 79  ? 16.522  7.854   6.004  1.00 86.87  ? 70  ASN I C   1 
ATOM   14533 O  O   . ASN I  1 79  ? 15.456  7.484   5.511  1.00 82.91  ? 70  ASN I O   1 
ATOM   14534 C  CB  . ASN I  1 79  ? 18.583  8.040   4.641  1.00 90.31  ? 70  ASN I CB  1 
ATOM   14535 C  CG  . ASN I  1 79  ? 19.259  8.786   3.514  1.00 97.62  ? 70  ASN I CG  1 
ATOM   14536 O  OD1 . ASN I  1 79  ? 18.621  9.541   2.774  1.00 95.88  ? 70  ASN I OD1 1 
ATOM   14537 N  ND2 . ASN I  1 79  ? 20.565  8.576   3.373  1.00 93.28  ? 70  ASN I ND2 1 
ATOM   14538 N  N   . GLU I  1 80  ? 16.964  7.442   7.191  1.00 86.15  ? 71  GLU I N   1 
ATOM   14539 C  CA  . GLU I  1 80  ? 16.256  6.448   7.992  1.00 81.82  ? 71  GLU I CA  1 
ATOM   14540 C  C   . GLU I  1 80  ? 14.974  7.036   8.570  1.00 79.13  ? 71  GLU I C   1 
ATOM   14541 O  O   . GLU I  1 80  ? 14.098  6.308   9.023  1.00 76.83  ? 71  GLU I O   1 
ATOM   14542 C  CB  . GLU I  1 80  ? 17.172  5.921   9.102  1.00 79.04  ? 71  GLU I CB  1 
ATOM   14543 C  CG  . GLU I  1 80  ? 18.659  6.032   8.741  1.00 95.55  ? 71  GLU I CG  1 
ATOM   14544 C  CD  . GLU I  1 80  ? 19.566  5.052   9.488  1.00 108.77 ? 71  GLU I CD  1 
ATOM   14545 O  OE1 . GLU I  1 80  ? 19.326  4.796   10.694 1.00 99.87  ? 71  GLU I OE1 1 
ATOM   14546 O  OE2 . GLU I  1 80  ? 20.529  4.546   8.859  1.00 106.74 ? 71  GLU I OE2 1 
ATOM   14547 N  N   . TYR I  1 81  ? 14.853  8.344   8.528  1.00 82.81  ? 72  TYR I N   1 
ATOM   14548 C  CA  . TYR I  1 81  ? 13.689  8.955   9.122  1.00 82.33  ? 72  TYR I CA  1 
ATOM   14549 C  C   . TYR I  1 81  ? 12.671  9.618   8.202  1.00 79.61  ? 72  TYR I C   1 
ATOM   14550 O  O   . TYR I  1 81  ? 11.783  10.277  8.674  1.00 82.68  ? 72  TYR I O   1 
ATOM   14551 C  CB  . TYR I  1 81  ? 14.110  9.851   10.274 1.00 76.36  ? 72  TYR I CB  1 
ATOM   14552 C  CG  . TYR I  1 81  ? 14.599  9.056   11.454 1.00 68.63  ? 72  TYR I CG  1 
ATOM   14553 C  CD1 . TYR I  1 81  ? 15.934  8.793   11.631 1.00 72.22  ? 72  TYR I CD1 1 
ATOM   14554 C  CD2 . TYR I  1 81  ? 13.719  8.561   12.377 1.00 66.01  ? 72  TYR I CD2 1 
ATOM   14555 C  CE1 . TYR I  1 81  ? 16.366  8.067   12.691 1.00 68.36  ? 72  TYR I CE1 1 
ATOM   14556 C  CE2 . TYR I  1 81  ? 14.146  7.838   13.426 1.00 68.41  ? 72  TYR I CE2 1 
ATOM   14557 C  CZ  . TYR I  1 81  ? 15.467  7.593   13.584 1.00 64.51  ? 72  TYR I CZ  1 
ATOM   14558 O  OH  . TYR I  1 81  ? 15.891  6.860   14.657 1.00 72.34  ? 72  TYR I OH  1 
ATOM   14559 N  N   . GLY I  1 82  ? 12.776  9.435   6.900  1.00 75.99  ? 73  GLY I N   1 
ATOM   14560 C  CA  . GLY I  1 82  ? 11.812  10.022  5.991  1.00 68.50  ? 73  GLY I CA  1 
ATOM   14561 C  C   . GLY I  1 82  ? 12.351  11.364  5.571  1.00 78.72  ? 73  GLY I C   1 
ATOM   14562 O  O   . GLY I  1 82  ? 11.615  12.270  5.192  1.00 72.28  ? 73  GLY I O   1 
ATOM   14563 N  N   . ASN I  1 83  ? 13.667  11.481  5.654  1.00 82.01  ? 74  ASN I N   1 
ATOM   14564 C  CA  A ASN I  1 83  ? 14.375  12.662  5.177  0.50 83.06  ? 74  ASN I CA  1 
ATOM   14565 C  CA  B ASN I  1 83  ? 14.347  12.661  5.156  0.50 83.06  ? 74  ASN I CA  1 
ATOM   14566 C  C   . ASN I  1 83  ? 13.948  13.926  5.920  1.00 87.36  ? 74  ASN I C   1 
ATOM   14567 O  O   . ASN I  1 83  ? 13.731  14.983  5.311  1.00 92.31  ? 74  ASN I O   1 
ATOM   14568 C  CB  A ASN I  1 83  ? 14.172  12.840  3.675  0.50 89.61  ? 74  ASN I CB  1 
ATOM   14569 C  CB  B ASN I  1 83  ? 14.053  12.826  3.658  0.50 89.63  ? 74  ASN I CB  1 
ATOM   14570 C  CG  A ASN I  1 83  ? 14.746  14.142  3.165  0.50 94.72  ? 74  ASN I CG  1 
ATOM   14571 C  CG  B ASN I  1 83  ? 15.018  12.046  2.781  0.50 94.86  ? 74  ASN I CG  1 
ATOM   14572 O  OD1 A ASN I  1 83  ? 14.023  15.003  2.691  0.50 92.15  ? 74  ASN I OD1 1 
ATOM   14573 O  OD1 B ASN I  1 83  ? 16.147  12.499  2.539  0.50 93.49  ? 74  ASN I OD1 1 
ATOM   14574 N  ND2 A ASN I  1 83  ? 16.048  14.280  3.260  0.50 96.81  ? 74  ASN I ND2 1 
ATOM   14575 N  ND2 B ASN I  1 83  ? 14.589  10.855  2.310  0.50 97.17  ? 74  ASN I ND2 1 
ATOM   14576 N  N   . ILE I  1 84  ? 13.846  13.797  7.250  1.00 84.54  ? 75  ILE I N   1 
ATOM   14577 C  CA  . ILE I  1 84  ? 13.553  14.882  8.189  1.00 74.43  ? 75  ILE I CA  1 
ATOM   14578 C  C   . ILE I  1 84  ? 14.892  15.456  8.619  1.00 68.72  ? 75  ILE I C   1 
ATOM   14579 O  O   . ILE I  1 84  ? 15.706  14.761  9.211  1.00 64.69  ? 75  ILE I O   1 
ATOM   14580 C  CB  . ILE I  1 84  ? 12.855  14.325  9.455  1.00 69.99  ? 75  ILE I CB  1 
ATOM   14581 C  CG1 . ILE I  1 84  ? 11.402  13.945  9.167  1.00 58.68  ? 75  ILE I CG1 1 
ATOM   14582 C  CG2 . ILE I  1 84  ? 12.946  15.308  10.621 1.00 68.04  ? 75  ILE I CG2 1 
ATOM   14583 C  CD1 . ILE I  1 84  ? 10.637  13.488  10.386 1.00 69.45  ? 75  ILE I CD1 1 
ATOM   14584 N  N   . THR I  1 85  ? 15.156  16.703  8.262  1.00 70.07  ? 76  THR I N   1 
ATOM   14585 C  CA  . THR I  1 85  ? 16.390  17.331  8.684  1.00 70.21  ? 76  THR I CA  1 
ATOM   14586 C  C   . THR I  1 85  ? 16.265  18.146  9.981  1.00 73.28  ? 76  THR I C   1 
ATOM   14587 O  O   . THR I  1 85  ? 17.273  18.534  10.577 1.00 72.42  ? 76  THR I O   1 
ATOM   14588 C  CB  . THR I  1 85  ? 16.914  18.226  7.564  1.00 73.88  ? 76  THR I CB  1 
ATOM   14589 O  OG1 . THR I  1 85  ? 15.892  19.160  7.199  1.00 78.76  ? 76  THR I OG1 1 
ATOM   14590 C  CG2 . THR I  1 85  ? 17.263  17.383  6.348  1.00 79.74  ? 76  THR I CG2 1 
ATOM   14591 N  N   . ASP I  1 86  ? 15.042  18.413  10.424 1.00 66.52  ? 77  ASP I N   1 
ATOM   14592 C  CA  . ASP I  1 86  ? 14.874  19.102  11.696 1.00 66.73  ? 77  ASP I CA  1 
ATOM   14593 C  C   . ASP I  1 86  ? 13.485  18.994  12.328 1.00 66.79  ? 77  ASP I C   1 
ATOM   14594 O  O   . ASP I  1 86  ? 12.505  18.665  11.654 1.00 56.57  ? 77  ASP I O   1 
ATOM   14595 C  CB  . ASP I  1 86  ? 15.351  20.554  11.612 1.00 63.11  ? 77  ASP I CB  1 
ATOM   14596 C  CG  . ASP I  1 86  ? 14.586  21.359  10.600 1.00 72.14  ? 77  ASP I CG  1 
ATOM   14597 O  OD1 . ASP I  1 86  ? 13.441  20.982  10.270 1.00 72.18  ? 77  ASP I OD1 1 
ATOM   14598 O  OD2 . ASP I  1 86  ? 15.132  22.383  10.143 1.00 78.38  ? 77  ASP I OD2 1 
ATOM   14599 N  N   . PHE I  1 87  ? 13.417  19.282  13.628 1.00 61.82  ? 78  PHE I N   1 
ATOM   14600 C  CA  . PHE I  1 87  ? 12.143  19.356  14.336 1.00 61.47  ? 78  PHE I CA  1 
ATOM   14601 C  C   . PHE I  1 87  ? 12.164  20.397  15.468 1.00 59.00  ? 78  PHE I C   1 
ATOM   14602 O  O   . PHE I  1 87  ? 13.221  20.793  15.958 1.00 54.29  ? 78  PHE I O   1 
ATOM   14603 C  CB  . PHE I  1 87  ? 11.731  17.972  14.863 1.00 56.41  ? 78  PHE I CB  1 
ATOM   14604 C  CG  . PHE I  1 87  ? 12.713  17.382  15.827 1.00 63.27  ? 78  PHE I CG  1 
ATOM   14605 C  CD1 . PHE I  1 87  ? 12.472  17.420  17.195 1.00 63.83  ? 78  PHE I CD1 1 
ATOM   14606 C  CD2 . PHE I  1 87  ? 13.885  16.811  15.377 1.00 60.28  ? 78  PHE I CD2 1 
ATOM   14607 C  CE1 . PHE I  1 87  ? 13.379  16.893  18.093 1.00 63.08  ? 78  PHE I CE1 1 
ATOM   14608 C  CE2 . PHE I  1 87  ? 14.792  16.278  16.272 1.00 65.76  ? 78  PHE I CE2 1 
ATOM   14609 C  CZ  . PHE I  1 87  ? 14.538  16.323  17.634 1.00 63.98  ? 78  PHE I CZ  1 
ATOM   14610 N  N   . ARG I  1 88  ? 10.977  20.843  15.861 1.00 63.02  ? 79  ARG I N   1 
ATOM   14611 C  CA  . ARG I  1 88  ? 10.811  21.733  16.998 1.00 56.63  ? 79  ARG I CA  1 
ATOM   14612 C  C   . ARG I  1 88  ? 10.424  20.921  18.252 1.00 65.37  ? 79  ARG I C   1 
ATOM   14613 O  O   . ARG I  1 88  ? 9.605   20.006  18.183 1.00 65.87  ? 79  ARG I O   1 
ATOM   14614 C  CB  . ARG I  1 88  ? 9.745   22.786  16.685 1.00 52.40  ? 79  ARG I CB  1 
ATOM   14615 C  CG  . ARG I  1 88  ? 10.188  23.896  15.734 1.00 56.68  ? 79  ARG I CG  1 
ATOM   14616 C  CD  . ARG I  1 88  ? 10.038  23.517  14.264 1.00 66.98  ? 79  ARG I CD  1 
ATOM   14617 N  NE  . ARG I  1 88  ? 10.477  24.588  13.364 1.00 69.18  ? 79  ARG I NE  1 
ATOM   14618 C  CZ  . ARG I  1 88  ? 10.889  24.408  12.110 1.00 63.93  ? 79  ARG I CZ  1 
ATOM   14619 N  NH1 . ARG I  1 88  ? 11.281  25.450  11.389 1.00 54.91  ? 79  ARG I NH1 1 
ATOM   14620 N  NH2 . ARG I  1 88  ? 10.931  23.189  11.582 1.00 68.77  ? 79  ARG I NH2 1 
ATOM   14621 N  N   . THR I  1 89  ? 11.028  21.241  19.395 1.00 59.39  ? 80  THR I N   1 
ATOM   14622 C  CA  . THR I  1 89  ? 10.722  20.537  20.640 1.00 63.24  ? 80  THR I CA  1 
ATOM   14623 C  C   . THR I  1 89  ? 10.505  21.510  21.803 1.00 63.51  ? 80  THR I C   1 
ATOM   14624 O  O   . THR I  1 89  ? 11.111  22.580  21.857 1.00 62.36  ? 80  THR I O   1 
ATOM   14625 C  CB  . THR I  1 89  ? 11.830  19.485  21.017 1.00 71.03  ? 80  THR I CB  1 
ATOM   14626 O  OG1 . THR I  1 89  ? 11.349  18.593  22.038 1.00 69.20  ? 80  THR I OG1 1 
ATOM   14627 C  CG2 . THR I  1 89  ? 13.102  20.168  21.510 1.00 63.83  ? 80  THR I CG2 1 
ATOM   14628 N  N   . SER I  1 90  ? 9.620   21.142  22.722 1.00 61.63  ? 81  SER I N   1 
ATOM   14629 C  CA  . SER I  1 90  ? 9.513   21.854  23.980 1.00 64.54  ? 81  SER I CA  1 
ATOM   14630 C  C   . SER I  1 90  ? 10.916  21.883  24.608 1.00 67.04  ? 81  SER I C   1 
ATOM   14631 O  O   . SER I  1 90  ? 11.609  20.869  24.624 1.00 64.82  ? 81  SER I O   1 
ATOM   14632 C  CB  . SER I  1 90  ? 8.511   21.133  24.882 1.00 68.49  ? 81  SER I CB  1 
ATOM   14633 O  OG  . SER I  1 90  ? 8.428   21.716  26.169 1.00 63.72  ? 81  SER I OG  1 
ATOM   14634 N  N   . ALA I  1 91  ? 11.352  23.044  25.095 1.00 67.09  ? 82  ALA I N   1 
ATOM   14635 C  CA  . ALA I  1 91  ? 12.697  23.168  25.662 1.00 60.81  ? 82  ALA I CA  1 
ATOM   14636 C  C   . ALA I  1 91  ? 12.853  22.299  26.910 1.00 67.70  ? 82  ALA I C   1 
ATOM   14637 O  O   . ALA I  1 91  ? 13.965  21.981  27.325 1.00 70.63  ? 82  ALA I O   1 
ATOM   14638 C  CB  . ALA I  1 91  ? 13.016  24.613  25.972 1.00 48.62  ? 82  ALA I CB  1 
ATOM   14639 N  N   . ALA I  1 92  ? 11.725  21.917  27.497 1.00 63.59  ? 83  ALA I N   1 
ATOM   14640 C  CA  . ALA I  1 92  ? 11.697  21.011  28.630 1.00 59.13  ? 83  ALA I CA  1 
ATOM   14641 C  C   . ALA I  1 92  ? 12.128  19.565  28.283 1.00 63.48  ? 83  ALA I C   1 
ATOM   14642 O  O   . ALA I  1 92  ? 12.522  18.798  29.163 1.00 62.53  ? 83  ALA I O   1 
ATOM   14643 C  CB  . ALA I  1 92  ? 10.314  21.021  29.232 1.00 60.10  ? 83  ALA I CB  1 
ATOM   14644 N  N   . ASP I  1 93  ? 12.070  19.191  27.011 1.00 62.38  ? 84  ASP I N   1 
ATOM   14645 C  CA  . ASP I  1 93  ? 12.425  17.825  26.621 1.00 66.35  ? 84  ASP I CA  1 
ATOM   14646 C  C   . ASP I  1 93  ? 13.897  17.648  26.275 1.00 64.86  ? 84  ASP I C   1 
ATOM   14647 O  O   . ASP I  1 93  ? 14.318  16.562  25.895 1.00 65.88  ? 84  ASP I O   1 
ATOM   14648 C  CB  . ASP I  1 93  ? 11.602  17.362  25.419 1.00 68.42  ? 84  ASP I CB  1 
ATOM   14649 C  CG  . ASP I  1 93  ? 10.119  17.534  25.625 1.00 72.01  ? 84  ASP I CG  1 
ATOM   14650 O  OD1 . ASP I  1 93  ? 9.668   17.535  26.794 1.00 72.03  ? 84  ASP I OD1 1 
ATOM   14651 O  OD2 . ASP I  1 93  ? 9.407   17.672  24.604 1.00 75.36  ? 84  ASP I OD2 1 
ATOM   14652 N  N   . ILE I  1 94  ? 14.681  18.710  26.380 1.00 62.73  ? 85  ILE I N   1 
ATOM   14653 C  CA  . ILE I  1 94  ? 16.098  18.605  26.066 1.00 60.69  ? 85  ILE I CA  1 
ATOM   14654 C  C   . ILE I  1 94  ? 16.927  19.349  27.092 1.00 58.55  ? 85  ILE I C   1 
ATOM   14655 O  O   . ILE I  1 94  ? 16.422  20.183  27.829 1.00 68.90  ? 85  ILE I O   1 
ATOM   14656 C  CB  . ILE I  1 94  ? 16.427  19.170  24.669 1.00 65.36  ? 85  ILE I CB  1 
ATOM   14657 C  CG1 . ILE I  1 94  ? 16.121  20.667  24.626 1.00 67.20  ? 85  ILE I CG1 1 
ATOM   14658 C  CG2 . ILE I  1 94  ? 15.664  18.427  23.581 1.00 58.57  ? 85  ILE I CG2 1 
ATOM   14659 C  CD1 . ILE I  1 94  ? 16.394  21.304  23.304 1.00 59.19  ? 85  ILE I CD1 1 
ATOM   14660 N  N   . TRP I  1 95  ? 18.210  19.035  27.132 1.00 61.32  ? 86  TRP I N   1 
ATOM   14661 C  CA  . TRP I  1 95  ? 19.136  19.702  28.023 1.00 58.29  ? 86  TRP I CA  1 
ATOM   14662 C  C   . TRP I  1 95  ? 19.439  21.083  27.483 1.00 61.27  ? 86  TRP I C   1 
ATOM   14663 O  O   . TRP I  1 95  ? 19.765  21.239  26.307 1.00 62.79  ? 86  TRP I O   1 
ATOM   14664 C  CB  . TRP I  1 95  ? 20.429  18.904  28.141 1.00 57.17  ? 86  TRP I CB  1 
ATOM   14665 C  CG  . TRP I  1 95  ? 21.459  19.572  28.978 1.00 63.28  ? 86  TRP I CG  1 
ATOM   14666 C  CD1 . TRP I  1 95  ? 21.712  19.341  30.288 1.00 59.25  ? 86  TRP I CD1 1 
ATOM   14667 C  CD2 . TRP I  1 95  ? 22.377  20.593  28.563 1.00 61.25  ? 86  TRP I CD2 1 
ATOM   14668 N  NE1 . TRP I  1 95  ? 22.731  20.139  30.716 1.00 57.54  ? 86  TRP I NE1 1 
ATOM   14669 C  CE2 . TRP I  1 95  ? 23.158  20.923  29.679 1.00 58.43  ? 86  TRP I CE2 1 
ATOM   14670 C  CE3 . TRP I  1 95  ? 22.615  21.259  27.352 1.00 56.27  ? 86  TRP I CE3 1 
ATOM   14671 C  CZ2 . TRP I  1 95  ? 24.159  21.887  29.633 1.00 61.05  ? 86  TRP I CZ2 1 
ATOM   14672 C  CZ3 . TRP I  1 95  ? 23.608  22.206  27.302 1.00 51.61  ? 86  TRP I CZ3 1 
ATOM   14673 C  CH2 . TRP I  1 95  ? 24.370  22.515  28.437 1.00 56.47  ? 86  TRP I CH2 1 
ATOM   14674 N  N   . THR I  1 96  ? 19.321  22.081  28.353 1.00 61.17  ? 87  THR I N   1 
ATOM   14675 C  CA  . THR I  1 96  ? 19.606  23.459  28.000 1.00 57.00  ? 87  THR I CA  1 
ATOM   14676 C  C   . THR I  1 96  ? 20.731  23.951  28.873 1.00 57.72  ? 87  THR I C   1 
ATOM   14677 O  O   . THR I  1 96  ? 20.899  23.480  29.995 1.00 61.69  ? 87  THR I O   1 
ATOM   14678 C  CB  . THR I  1 96  ? 18.388  24.326  28.231 1.00 56.65  ? 87  THR I CB  1 
ATOM   14679 O  OG1 . THR I  1 96  ? 17.746  23.886  29.429 1.00 62.11  ? 87  THR I OG1 1 
ATOM   14680 C  CG2 . THR I  1 96  ? 17.409  24.182  27.057 1.00 55.45  ? 87  THR I CG2 1 
ATOM   14681 N  N   . PRO I  1 97  ? 21.540  24.879  28.354 1.00 64.00  ? 88  PRO I N   1 
ATOM   14682 C  CA  . PRO I  1 97  ? 22.608  25.429  29.200 1.00 64.56  ? 88  PRO I CA  1 
ATOM   14683 C  C   . PRO I  1 97  ? 22.076  26.423  30.252 1.00 65.11  ? 88  PRO I C   1 
ATOM   14684 O  O   . PRO I  1 97  ? 21.019  27.037  30.076 1.00 71.97  ? 88  PRO I O   1 
ATOM   14685 C  CB  . PRO I  1 97  ? 23.554  26.100  28.186 1.00 60.11  ? 88  PRO I CB  1 
ATOM   14686 C  CG  . PRO I  1 97  ? 22.705  26.392  27.000 1.00 52.81  ? 88  PRO I CG  1 
ATOM   14687 C  CD  . PRO I  1 97  ? 21.638  25.331  26.956 1.00 55.28  ? 88  PRO I CD  1 
ATOM   14688 N  N   . ASP I  1 98  ? 22.842  26.593  31.322 1.00 60.29  ? 89  ASP I N   1 
ATOM   14689 C  CA  . ASP I  1 98  ? 22.438  27.345  32.511 1.00 51.63  ? 89  ASP I CA  1 
ATOM   14690 C  C   . ASP I  1 98  ? 22.758  28.829  32.463 1.00 59.41  ? 89  ASP I C   1 
ATOM   14691 O  O   . ASP I  1 98  ? 22.849  29.467  33.507 1.00 55.66  ? 89  ASP I O   1 
ATOM   14692 C  CB  . ASP I  1 98  ? 22.882  26.703  33.816 1.00 56.36  ? 89  ASP I CB  1 
ATOM   14693 C  CG  . ASP I  1 98  ? 24.362  26.610  33.944 1.00 62.81  ? 89  ASP I CG  1 
ATOM   14694 O  OD1 . ASP I  1 98  ? 25.064  26.686  32.910 1.00 55.66  ? 89  ASP I OD1 1 
ATOM   14695 O  OD2 . ASP I  1 98  ? 24.808  26.444  35.103 1.00 65.01  ? 89  ASP I OD2 1 
ATOM   14696 N  N   . ILE I  1 99  ? 23.094  29.326  31.274 1.00 56.36  ? 90  ILE I N   1 
ATOM   14697 C  CA  . ILE I  1 99  ? 23.443  30.725  31.093 1.00 56.24  ? 90  ILE I CA  1 
ATOM   14698 C  C   . ILE I  1 99  ? 22.430  31.639  31.730 1.00 54.70  ? 90  ILE I C   1 
ATOM   14699 O  O   . ILE I  1 99  ? 21.225  31.416  31.604 1.00 58.04  ? 90  ILE I O   1 
ATOM   14700 C  CB  . ILE I  1 99  ? 23.416  31.115  29.629 1.00 59.36  ? 90  ILE I CB  1 
ATOM   14701 C  CG1 . ILE I  1 99  ? 24.195  30.108  28.788 1.00 57.24  ? 90  ILE I CG1 1 
ATOM   14702 C  CG2 . ILE I  1 99  ? 23.927  32.547  29.477 1.00 54.73  ? 90  ILE I CG2 1 
ATOM   14703 C  CD1 . ILE I  1 99  ? 25.616  29.898  29.248 1.00 56.04  ? 90  ILE I CD1 1 
ATOM   14704 N  N   . THR I  1 100 ? 22.939  32.676  32.397 1.00 48.19  ? 91  THR I N   1 
ATOM   14705 C  CA  . THR I  1 100 ? 22.131  33.576  33.210 1.00 50.75  ? 91  THR I CA  1 
ATOM   14706 C  C   . THR I  1 100 ? 22.783  34.953  33.301 1.00 55.22  ? 91  THR I C   1 
ATOM   14707 O  O   . THR I  1 100 ? 23.997  35.077  33.134 1.00 55.15  ? 91  THR I O   1 
ATOM   14708 C  CB  . THR I  1 100 ? 21.971  33.023  34.642 1.00 57.82  ? 91  THR I CB  1 
ATOM   14709 O  OG1 . THR I  1 100 ? 21.315  34.001  35.456 1.00 69.54  ? 91  THR I OG1 1 
ATOM   14710 C  CG2 . THR I  1 100 ? 23.336  32.671  35.264 1.00 48.58  ? 91  THR I CG2 1 
ATOM   14711 N  N   . ALA I  1 101 ? 21.993  35.987  33.588 1.00 52.50  ? 92  ALA I N   1 
ATOM   14712 C  CA  . ALA I  1 101 ? 22.547  37.348  33.712 1.00 60.95  ? 92  ALA I CA  1 
ATOM   14713 C  C   . ALA I  1 101 ? 23.088  37.628  35.115 1.00 51.84  ? 92  ALA I C   1 
ATOM   14714 O  O   . ALA I  1 101 ? 22.338  37.608  36.079 1.00 52.11  ? 92  ALA I O   1 
ATOM   14715 C  CB  . ALA I  1 101 ? 21.497  38.394  33.333 1.00 58.71  ? 92  ALA I CB  1 
ATOM   14716 N  N   . TYR I  1 102 ? 24.379  37.816  35.230 1.00 49.85  ? 93  TYR I N   1 
ATOM   14717 C  CA  . TYR I  1 102 ? 25.002  37.890  36.517 1.00 53.80  ? 93  TYR I CA  1 
ATOM   14718 C  C   . TYR I  1 102 ? 24.522  39.025  37.357 1.00 57.62  ? 93  TYR I C   1 
ATOM   14719 O  O   . TYR I  1 102 ? 24.512  38.930  38.558 1.00 55.99  ? 93  TYR I O   1 
ATOM   14720 C  CB  . TYR I  1 102 ? 26.502  37.926  36.401 1.00 60.80  ? 93  TYR I CB  1 
ATOM   14721 C  CG  . TYR I  1 102 ? 27.109  36.675  35.841 1.00 67.79  ? 93  TYR I CG  1 
ATOM   14722 C  CD1 . TYR I  1 102 ? 26.474  35.476  35.927 1.00 65.78  ? 93  TYR I CD1 1 
ATOM   14723 C  CD2 . TYR I  1 102 ? 28.332  36.700  35.252 1.00 70.32  ? 93  TYR I CD2 1 
ATOM   14724 C  CE1 . TYR I  1 102 ? 27.034  34.367  35.430 1.00 62.89  ? 93  TYR I CE1 1 
ATOM   14725 C  CE2 . TYR I  1 102 ? 28.880  35.596  34.750 1.00 63.47  ? 93  TYR I CE2 1 
ATOM   14726 C  CZ  . TYR I  1 102 ? 28.234  34.438  34.839 1.00 63.48  ? 93  TYR I CZ  1 
ATOM   14727 O  OH  . TYR I  1 102 ? 28.820  33.332  34.331 1.00 56.25  ? 93  TYR I OH  1 
ATOM   14728 N  N   . SER I  1 103 ? 24.171  40.127  36.740 1.00 56.86  ? 94  SER I N   1 
ATOM   14729 C  CA  . SER I  1 103 ? 23.765  41.300  37.486 1.00 55.51  ? 94  SER I CA  1 
ATOM   14730 C  C   . SER I  1 103 ? 22.293  41.568  37.552 1.00 54.92  ? 94  SER I C   1 
ATOM   14731 O  O   . SER I  1 103 ? 21.900  42.656  37.801 1.00 57.89  ? 94  SER I O   1 
ATOM   14732 C  CB  . SER I  1 103 ? 24.487  42.533  36.985 1.00 55.88  ? 94  SER I CB  1 
ATOM   14733 O  OG  . SER I  1 103 ? 24.682  42.466  35.606 1.00 69.87  ? 94  SER I OG  1 
ATOM   14734 N  N   . SER I  1 104 ? 21.468  40.594  37.274 1.00 49.63  ? 95  SER I N   1 
ATOM   14735 C  CA  . SER I  1 104 ? 20.043  40.816  37.335 1.00 51.68  ? 95  SER I CA  1 
ATOM   14736 C  C   . SER I  1 104 ? 19.549  41.091  38.719 1.00 53.81  ? 95  SER I C   1 
ATOM   14737 O  O   . SER I  1 104 ? 19.968  40.451  39.628 1.00 53.37  ? 95  SER I O   1 
ATOM   14738 C  CB  . SER I  1 104 ? 19.331  39.588  36.831 1.00 50.36  ? 95  SER I CB  1 
ATOM   14739 O  OG  . SER I  1 104 ? 19.414  38.554  37.753 1.00 53.17  ? 95  SER I OG  1 
ATOM   14740 N  N   . THR I  1 105 ? 18.633  42.034  38.868 1.00 55.18  ? 96  THR I N   1 
ATOM   14741 C  CA  . THR I  1 105 ? 18.021  42.313  40.152 1.00 57.89  ? 96  THR I CA  1 
ATOM   14742 C  C   . THR I  1 105 ? 16.613  41.817  40.337 1.00 51.47  ? 96  THR I C   1 
ATOM   14743 O  O   . THR I  1 105 ? 16.019  42.077  41.338 1.00 48.55  ? 96  THR I O   1 
ATOM   14744 C  CB  . THR I  1 105 ? 17.978  43.778  40.444 1.00 61.13  ? 96  THR I CB  1 
ATOM   14745 O  OG1 . THR I  1 105 ? 16.867  44.357  39.777 1.00 59.13  ? 96  THR I OG1 1 
ATOM   14746 C  CG2 . THR I  1 105 ? 19.215  44.423  39.995 1.00 53.93  ? 96  THR I CG2 1 
ATOM   14747 N  N   . ARG I  1 106 ? 16.077  41.120  39.360 1.00 53.70  ? 97  ARG I N   1 
ATOM   14748 C  CA  . ARG I  1 106 ? 14.756  40.500  39.459 1.00 55.52  ? 97  ARG I CA  1 
ATOM   14749 C  C   . ARG I  1 106 ? 14.769  39.181  38.704 1.00 51.72  ? 97  ARG I C   1 
ATOM   14750 O  O   . ARG I  1 106 ? 15.650  38.960  37.881 1.00 52.14  ? 97  ARG I O   1 
ATOM   14751 C  CB  . ARG I  1 106 ? 13.669  41.429  38.930 1.00 52.38  ? 97  ARG I CB  1 
ATOM   14752 C  CG  . ARG I  1 106 ? 13.073  42.320  39.988 1.00 57.68  ? 97  ARG I CG  1 
ATOM   14753 C  CD  . ARG I  1 106 ? 12.059  43.253  39.381 1.00 68.35  ? 97  ARG I CD  1 
ATOM   14754 N  NE  . ARG I  1 106 ? 12.590  44.602  39.205 1.00 79.28  ? 97  ARG I NE  1 
ATOM   14755 C  CZ  . ARG I  1 106 ? 11.871  45.640  38.778 1.00 83.92  ? 97  ARG I CZ  1 
ATOM   14756 N  NH1 . ARG I  1 106 ? 10.588  45.478  38.471 1.00 90.08  ? 97  ARG I NH1 1 
ATOM   14757 N  NH2 . ARG I  1 106 ? 12.431  46.842  38.657 1.00 71.82  ? 97  ARG I NH2 1 
ATOM   14758 N  N   . PRO I  1 107 ? 13.834  38.272  39.017 1.00 54.26  ? 98  PRO I N   1 
ATOM   14759 C  CA  . PRO I  1 107 ? 13.848  37.039  38.231 1.00 53.39  ? 98  PRO I CA  1 
ATOM   14760 C  C   . PRO I  1 107 ? 13.415  37.380  36.803 1.00 58.32  ? 98  PRO I C   1 
ATOM   14761 O  O   . PRO I  1 107 ? 12.547  38.251  36.631 1.00 62.43  ? 98  PRO I O   1 
ATOM   14762 C  CB  . PRO I  1 107 ? 12.803  36.159  38.925 1.00 37.10  ? 98  PRO I CB  1 
ATOM   14763 C  CG  . PRO I  1 107 ? 12.503  36.813  40.199 1.00 45.88  ? 98  PRO I CG  1 
ATOM   14764 C  CD  . PRO I  1 107 ? 12.760  38.266  40.019 1.00 56.34  ? 98  PRO I CD  1 
ATOM   14765 N  N   . VAL I  1 108 ? 14.025  36.727  35.813 1.00 48.28  ? 99  VAL I N   1 
ATOM   14766 C  CA  . VAL I  1 108 ? 13.770  37.001  34.403 1.00 52.78  ? 99  VAL I CA  1 
ATOM   14767 C  C   . VAL I  1 108 ? 12.359  36.649  33.973 1.00 47.73  ? 99  VAL I C   1 
ATOM   14768 O  O   . VAL I  1 108 ? 11.796  35.658  34.419 1.00 44.02  ? 99  VAL I O   1 
ATOM   14769 C  CB  . VAL I  1 108 ? 14.734  36.210  33.513 1.00 52.71  ? 99  VAL I CB  1 
ATOM   14770 C  CG1 . VAL I  1 108 ? 14.473  36.523  32.073 1.00 49.34  ? 99  VAL I CG1 1 
ATOM   14771 C  CG2 . VAL I  1 108 ? 16.159  36.549  33.868 1.00 58.16  ? 99  VAL I CG2 1 
ATOM   14772 N  N   . GLN I  1 109 ? 11.792  37.459  33.091 1.00 50.83  ? 100 GLN I N   1 
ATOM   14773 C  CA  . GLN I  1 109 ? 10.487  37.138  32.520 1.00 50.05  ? 100 GLN I CA  1 
ATOM   14774 C  C   . GLN I  1 109 ? 10.538  36.623  31.054 1.00 56.24  ? 100 GLN I C   1 
ATOM   14775 O  O   . GLN I  1 109 ? 11.078  37.266  30.158 1.00 55.28  ? 100 GLN I O   1 
ATOM   14776 C  CB  . GLN I  1 109 ? 9.567   38.334  32.630 1.00 44.59  ? 100 GLN I CB  1 
ATOM   14777 C  CG  . GLN I  1 109 ? 9.727   39.110  33.900 1.00 49.34  ? 100 GLN I CG  1 
ATOM   14778 C  CD  . GLN I  1 109 ? 8.427   39.745  34.278 1.00 55.28  ? 100 GLN I CD  1 
ATOM   14779 O  OE1 . GLN I  1 109 ? 8.186   40.933  34.025 1.00 50.20  ? 100 GLN I OE1 1 
ATOM   14780 N  NE2 . GLN I  1 109 ? 7.542   38.938  34.844 1.00 54.54  ? 100 GLN I NE2 1 
ATOM   14781 N  N   . VAL I  1 110 ? 9.952   35.454  30.832 1.00 51.72  ? 101 VAL I N   1 
ATOM   14782 C  CA  . VAL I  1 110 ? 9.961   34.817  29.538 1.00 48.57  ? 101 VAL I CA  1 
ATOM   14783 C  C   . VAL I  1 110 ? 8.788   35.292  28.657 1.00 56.97  ? 101 VAL I C   1 
ATOM   14784 O  O   . VAL I  1 110 ? 7.614   35.117  29.011 1.00 50.69  ? 101 VAL I O   1 
ATOM   14785 C  CB  . VAL I  1 110 ? 9.951   33.308  29.730 1.00 56.78  ? 101 VAL I CB  1 
ATOM   14786 C  CG1 . VAL I  1 110 ? 9.838   32.584  28.388 1.00 59.48  ? 101 VAL I CG1 1 
ATOM   14787 C  CG2 . VAL I  1 110 ? 11.208  32.906  30.472 1.00 51.41  ? 101 VAL I CG2 1 
ATOM   14788 N  N   . LEU I  1 111 ? 9.136   35.908  27.520 1.00 61.24  ? 102 LEU I N   1 
ATOM   14789 C  CA  . LEU I  1 111 ? 8.182   36.619  26.666 1.00 53.76  ? 102 LEU I CA  1 
ATOM   14790 C  C   . LEU I  1 111 ? 7.638   35.836  25.479 1.00 48.49  ? 102 LEU I C   1 
ATOM   14791 O  O   . LEU I  1 111 ? 6.721   36.292  24.795 1.00 54.52  ? 102 LEU I O   1 
ATOM   14792 C  CB  . LEU I  1 111 ? 8.812   37.931  26.189 1.00 52.53  ? 102 LEU I CB  1 
ATOM   14793 C  CG  . LEU I  1 111 ? 9.025   38.938  27.328 1.00 54.69  ? 102 LEU I CG  1 
ATOM   14794 C  CD1 . LEU I  1 111 ? 9.664   40.226  26.841 1.00 49.53  ? 102 LEU I CD1 1 
ATOM   14795 C  CD2 . LEU I  1 111 ? 7.711   39.234  28.012 1.00 50.56  ? 102 LEU I CD2 1 
ATOM   14796 N  N   . SER I  1 112 ? 8.172   34.635  25.294 1.00 51.07  ? 103 SER I N   1 
ATOM   14797 C  CA  . SER I  1 112 ? 7.980   33.827  24.091 1.00 50.85  ? 103 SER I CA  1 
ATOM   14798 C  C   . SER I  1 112 ? 7.827   32.364  24.500 1.00 55.08  ? 103 SER I C   1 
ATOM   14799 O  O   . SER I  1 112 ? 8.233   31.990  25.604 1.00 56.73  ? 103 SER I O   1 
ATOM   14800 C  CB  . SER I  1 112 ? 9.214   33.961  23.197 1.00 50.98  ? 103 SER I CB  1 
ATOM   14801 O  OG  . SER I  1 112 ? 10.302  33.175  23.674 1.00 45.48  ? 103 SER I OG  1 
ATOM   14802 N  N   . PRO I  1 113 ? 7.226   31.529  23.634 1.00 47.20  ? 104 PRO I N   1 
ATOM   14803 C  CA  . PRO I  1 113 ? 7.167   30.101  23.946 1.00 51.61  ? 104 PRO I CA  1 
ATOM   14804 C  C   . PRO I  1 113 ? 8.542   29.472  24.035 1.00 53.38  ? 104 PRO I C   1 
ATOM   14805 O  O   . PRO I  1 113 ? 9.480   29.943  23.385 1.00 52.14  ? 104 PRO I O   1 
ATOM   14806 C  CB  . PRO I  1 113 ? 6.364   29.533  22.782 1.00 49.56  ? 104 PRO I CB  1 
ATOM   14807 C  CG  . PRO I  1 113 ? 5.425   30.588  22.480 1.00 50.40  ? 104 PRO I CG  1 
ATOM   14808 C  CD  . PRO I  1 113 ? 6.238   31.873  22.607 1.00 58.09  ? 104 PRO I CD  1 
ATOM   14809 N  N   . GLN I  1 114 ? 8.691   28.452  24.876 1.00 56.99  ? 105 GLN I N   1 
ATOM   14810 C  CA  . GLN I  1 114 ? 10.018  27.891  24.996 1.00 64.27  ? 105 GLN I CA  1 
ATOM   14811 C  C   . GLN I  1 114 ? 10.059  26.602  24.220 1.00 64.11  ? 105 GLN I C   1 
ATOM   14812 O  O   . GLN I  1 114 ? 9.635   25.538  24.694 1.00 60.12  ? 105 GLN I O   1 
ATOM   14813 C  CB  . GLN I  1 114 ? 10.381  27.683  26.466 1.00 56.50  ? 105 GLN I CB  1 
ATOM   14814 C  CG  . GLN I  1 114 ? 10.302  28.975  27.260 1.00 58.05  ? 105 GLN I CG  1 
ATOM   14815 C  CD  . GLN I  1 114 ? 10.498  28.800  28.763 1.00 70.50  ? 105 GLN I CD  1 
ATOM   14816 O  OE1 . GLN I  1 114 ? 9.610   28.316  29.467 1.00 63.54  ? 105 GLN I OE1 1 
ATOM   14817 N  NE2 . GLN I  1 114 ? 11.655  29.228  29.262 1.00 64.71  ? 105 GLN I NE2 1 
ATOM   14818 N  N   . ASN I  1 115 ? 10.696  26.718  23.058 1.00 62.83  ? 106 ASN I N   1 
ATOM   14819 C  CA  . ASN I  1 115 ? 10.824  25.650  22.097 1.00 59.11  ? 106 ASN I CA  1 
ATOM   14820 C  C   . ASN I  1 115 ? 12.148  25.878  21.446 1.00 62.65  ? 106 ASN I C   1 
ATOM   14821 O  O   . ASN I  1 115 ? 12.567  27.017  21.263 1.00 63.16  ? 106 ASN I O   1 
ATOM   14822 C  CB  . ASN I  1 115 ? 9.746   25.737  21.033 1.00 57.94  ? 106 ASN I CB  1 
ATOM   14823 C  CG  . ASN I  1 115 ? 8.362   25.620  21.603 1.00 60.59  ? 106 ASN I CG  1 
ATOM   14824 O  OD1 . ASN I  1 115 ? 8.080   24.705  22.381 1.00 62.81  ? 106 ASN I OD1 1 
ATOM   14825 N  ND2 . ASN I  1 115 ? 7.481   26.555  21.230 1.00 55.89  ? 106 ASN I ND2 1 
ATOM   14826 N  N   . ALA I  1 116 ? 12.804  24.783  21.101 1.00 67.51  ? 107 ALA I N   1 
ATOM   14827 C  CA  . ALA I  1 116 ? 14.101  24.826  20.467 1.00 60.76  ? 107 ALA I CA  1 
ATOM   14828 C  C   . ALA I  1 116 ? 13.951  24.092  19.163 1.00 58.08  ? 107 ALA I C   1 
ATOM   14829 O  O   . ALA I  1 116 ? 12.988  23.367  18.961 1.00 60.23  ? 107 ALA I O   1 
ATOM   14830 C  CB  . ALA I  1 116 ? 15.134  24.145  21.338 1.00 60.63  ? 107 ALA I CB  1 
ATOM   14831 N  N   . LEU I  1 117 ? 14.898  24.306  18.267 1.00 69.68  ? 108 LEU I N   1 
ATOM   14832 C  CA  . LEU I  1 117 ? 14.934  23.587  17.008 1.00 63.05  ? 108 LEU I CA  1 
ATOM   14833 C  C   . LEU I  1 117 ? 16.163  22.700  17.035 1.00 62.38  ? 108 LEU I C   1 
ATOM   14834 O  O   . LEU I  1 117 ? 17.257  23.151  17.373 1.00 64.59  ? 108 LEU I O   1 
ATOM   14835 C  CB  . LEU I  1 117 ? 15.030  24.570  15.848 1.00 58.89  ? 108 LEU I CB  1 
ATOM   14836 C  CG  . LEU I  1 117 ? 14.864  23.997  14.458 1.00 56.41  ? 108 LEU I CG  1 
ATOM   14837 C  CD1 . LEU I  1 117 ? 13.407  23.791  14.217 1.00 58.43  ? 108 LEU I CD1 1 
ATOM   14838 C  CD2 . LEU I  1 117 ? 15.418  25.006  13.522 1.00 57.20  ? 108 LEU I CD2 1 
ATOM   14839 N  N   . VAL I  1 118 ? 15.986  21.431  16.708 1.00 58.63  ? 109 VAL I N   1 
ATOM   14840 C  CA  . VAL I  1 118 ? 17.116  20.520  16.631 1.00 60.15  ? 109 VAL I CA  1 
ATOM   14841 C  C   . VAL I  1 118 ? 17.205  20.004  15.196 1.00 62.69  ? 109 VAL I C   1 
ATOM   14842 O  O   . VAL I  1 118 ? 16.169  19.768  14.574 1.00 63.93  ? 109 VAL I O   1 
ATOM   14843 C  CB  . VAL I  1 118 ? 16.936  19.336  17.614 1.00 63.38  ? 109 VAL I CB  1 
ATOM   14844 C  CG1 . VAL I  1 118 ? 18.256  18.608  17.852 1.00 58.55  ? 109 VAL I CG1 1 
ATOM   14845 C  CG2 . VAL I  1 118 ? 16.334  19.813  18.928 1.00 58.91  ? 109 VAL I CG2 1 
ATOM   14846 N  N   . ASN I  1 119 ? 18.462  19.888  14.671 1.00 65.32  ? 110 ASN I N   1 
ATOM   14847 C  CA  . ASN I  1 119 ? 18.672  19.474  13.287 1.00 67.42  ? 110 ASN I CA  1 
ATOM   14848 C  C   . ASN I  1 119 ? 19.502  18.195  13.179 1.00 64.24  ? 110 ASN I C   1 
ATOM   14849 O  O   . ASN I  1 119 ? 20.108  17.776  14.149 1.00 64.82  ? 110 ASN I O   1 
ATOM   14850 C  CB  . ASN I  1 119 ? 19.214  20.634  12.429 1.00 71.20  ? 110 ASN I CB  1 
ATOM   14851 C  CG  . ASN I  1 119 ? 20.712  20.842  12.561 1.00 71.71  ? 110 ASN I CG  1 
ATOM   14852 O  OD1 . ASN I  1 119 ? 21.338  20.382  13.500 1.00 73.34  ? 110 ASN I OD1 1 
ATOM   14853 N  ND2 . ASN I  1 119 ? 21.294  21.525  11.572 1.00 86.13  ? 110 ASN I ND2 1 
ATOM   14854 N  N   . SER I  1 120 ? 19.454  17.438  12.058 1.00 67.53  ? 111 SER I N   1 
ATOM   14855 C  CA  . SER I  1 120 ? 20.097  16.149  11.820 1.00 65.22  ? 111 SER I CA  1 
ATOM   14856 C  C   . SER I  1 120 ? 21.554  16.100  12.253 1.00 65.07  ? 111 SER I C   1 
ATOM   14857 O  O   . SER I  1 120 ? 22.051  15.026  12.576 1.00 69.65  ? 111 SER I O   1 
ATOM   14858 C  CB  . SER I  1 120 ? 19.995  15.767  10.336 1.00 70.76  ? 111 SER I CB  1 
ATOM   14859 O  OG  . SER I  1 120 ? 20.800  16.599  9.506  1.00 67.74  ? 111 SER I OG  1 
ATOM   14860 N  N   . SER I  1 121 ? 22.235  17.246  12.257 1.00 64.88  ? 112 SER I N   1 
ATOM   14861 C  CA  . SER I  1 121 ? 23.646  17.331  12.669 1.00 72.42  ? 112 SER I CA  1 
ATOM   14862 C  C   . SER I  1 121 ? 23.866  17.379  14.200 1.00 76.04  ? 112 SER I C   1 
ATOM   14863 O  O   . SER I  1 121 ? 24.996  17.348  14.686 1.00 71.70  ? 112 SER I O   1 
ATOM   14864 C  CB  . SER I  1 121 ? 24.305  18.541  12.011 1.00 72.94  ? 112 SER I CB  1 
ATOM   14865 O  OG  . SER I  1 121 ? 24.308  18.399  10.602 1.00 81.98  ? 112 SER I OG  1 
ATOM   14866 N  N   . GLY I  1 122 ? 22.778  17.452  14.953 1.00 73.30  ? 113 GLY I N   1 
ATOM   14867 C  CA  . GLY I  1 122 ? 22.863  17.534  16.393 1.00 67.28  ? 113 GLY I CA  1 
ATOM   14868 C  C   . GLY I  1 122 ? 23.011  18.964  16.857 1.00 67.73  ? 113 GLY I C   1 
ATOM   14869 O  O   . GLY I  1 122 ? 23.412  19.201  17.998 1.00 65.27  ? 113 GLY I O   1 
ATOM   14870 N  N   . HIS I  1 123 ? 22.691  19.911  15.975 1.00 68.62  ? 114 HIS I N   1 
ATOM   14871 C  CA  . HIS I  1 123 ? 22.700  21.340  16.311 1.00 70.13  ? 114 HIS I CA  1 
ATOM   14872 C  C   . HIS I  1 123 ? 21.390  21.823  16.957 1.00 63.32  ? 114 HIS I C   1 
ATOM   14873 O  O   . HIS I  1 123 ? 20.309  21.609  16.421 1.00 67.41  ? 114 HIS I O   1 
ATOM   14874 C  CB  . HIS I  1 123 ? 23.030  22.200  15.078 1.00 78.61  ? 114 HIS I CB  1 
ATOM   14875 C  CG  . HIS I  1 123 ? 24.489  22.243  14.739 1.00 82.43  ? 114 HIS I CG  1 
ATOM   14876 N  ND1 . HIS I  1 123 ? 25.078  21.361  13.859 1.00 85.41  ? 114 HIS I ND1 1 
ATOM   14877 C  CD2 . HIS I  1 123 ? 25.480  23.061  15.170 1.00 82.70  ? 114 HIS I CD2 1 
ATOM   14878 C  CE1 . HIS I  1 123 ? 26.368  21.632  13.762 1.00 86.97  ? 114 HIS I CE1 1 
ATOM   14879 N  NE2 . HIS I  1 123 ? 26.638  22.658  14.549 1.00 85.62  ? 114 HIS I NE2 1 
ATOM   14880 N  N   . VAL I  1 124 ? 21.502  22.479  18.111 1.00 64.66  ? 115 VAL I N   1 
ATOM   14881 C  CA  . VAL I  1 124 ? 20.345  23.072  18.782 1.00 64.60  ? 115 VAL I CA  1 
ATOM   14882 C  C   . VAL I  1 124 ? 20.396  24.606  18.752 1.00 63.48  ? 115 VAL I C   1 
ATOM   14883 O  O   . VAL I  1 124 ? 21.434  25.211  19.026 1.00 56.31  ? 115 VAL I O   1 
ATOM   14884 C  CB  . VAL I  1 124 ? 20.215  22.587  20.247 1.00 60.08  ? 115 VAL I CB  1 
ATOM   14885 C  CG1 . VAL I  1 124 ? 18.906  23.078  20.868 1.00 58.32  ? 115 VAL I CG1 1 
ATOM   14886 C  CG2 . VAL I  1 124 ? 20.282  21.084  20.302 1.00 53.90  ? 115 VAL I CG2 1 
ATOM   14887 N  N   . GLN I  1 125 ? 19.268  25.210  18.392 1.00 58.20  ? 116 GLN I N   1 
ATOM   14888 C  CA  . GLN I  1 125 ? 19.108  26.648  18.410 1.00 57.73  ? 116 GLN I CA  1 
ATOM   14889 C  C   . GLN I  1 125 ? 17.922  26.992  19.301 1.00 62.09  ? 116 GLN I C   1 
ATOM   14890 O  O   . GLN I  1 125 ? 16.814  26.521  19.079 1.00 64.91  ? 116 GLN I O   1 
ATOM   14891 C  CB  . GLN I  1 125 ? 18.878  27.167  16.996 1.00 65.97  ? 116 GLN I CB  1 
ATOM   14892 C  CG  . GLN I  1 125 ? 20.145  27.257  16.132 1.00 80.06  ? 116 GLN I CG  1 
ATOM   14893 C  CD  . GLN I  1 125 ? 20.707  28.682  16.019 1.00 95.29  ? 116 GLN I CD  1 
ATOM   14894 O  OE1 . GLN I  1 125 ? 21.904  28.869  15.762 1.00 100.23 ? 116 GLN I OE1 1 
ATOM   14895 N  NE2 . GLN I  1 125 ? 19.842  29.689  16.197 1.00 87.59  ? 116 GLN I NE2 1 
ATOM   14896 N  N   . TYR I  1 126 ? 18.170  27.810  20.317 1.00 60.49  ? 117 TYR I N   1 
ATOM   14897 C  CA  . TYR I  1 126 ? 17.164  28.196  21.302 1.00 54.34  ? 117 TYR I CA  1 
ATOM   14898 C  C   . TYR I  1 126 ? 17.107  29.716  21.345 1.00 55.37  ? 117 TYR I C   1 
ATOM   14899 O  O   . TYR I  1 126 ? 18.115  30.356  21.603 1.00 60.49  ? 117 TYR I O   1 
ATOM   14900 C  CB  . TYR I  1 126 ? 17.567  27.638  22.671 1.00 57.20  ? 117 TYR I CB  1 
ATOM   14901 C  CG  . TYR I  1 126 ? 16.588  27.891  23.798 1.00 60.47  ? 117 TYR I CG  1 
ATOM   14902 C  CD1 . TYR I  1 126 ? 15.211  27.858  23.580 1.00 62.41  ? 117 TYR I CD1 1 
ATOM   14903 C  CD2 . TYR I  1 126 ? 17.043  28.149  25.094 1.00 60.67  ? 117 TYR I CD2 1 
ATOM   14904 C  CE1 . TYR I  1 126 ? 14.306  28.097  24.625 1.00 60.33  ? 117 TYR I CE1 1 
ATOM   14905 C  CE2 . TYR I  1 126 ? 16.156  28.388  26.141 1.00 62.15  ? 117 TYR I CE2 1 
ATOM   14906 C  CZ  . TYR I  1 126 ? 14.789  28.356  25.903 1.00 68.07  ? 117 TYR I CZ  1 
ATOM   14907 O  OH  . TYR I  1 126 ? 13.916  28.589  26.948 1.00 64.25  ? 117 TYR I OH  1 
ATOM   14908 N  N   . LEU I  1 127 ? 15.947  30.303  21.075 1.00 60.04  ? 118 LEU I N   1 
ATOM   14909 C  CA  . LEU I  1 127 ? 15.829  31.765  21.038 1.00 58.18  ? 118 LEU I CA  1 
ATOM   14910 C  C   . LEU I  1 127 ? 14.761  32.324  21.963 1.00 57.18  ? 118 LEU I C   1 
ATOM   14911 O  O   . LEU I  1 127 ? 13.722  32.780  21.488 1.00 59.88  ? 118 LEU I O   1 
ATOM   14912 C  CB  . LEU I  1 127 ? 15.523  32.237  19.621 1.00 61.87  ? 118 LEU I CB  1 
ATOM   14913 C  CG  . LEU I  1 127 ? 16.736  32.391  18.715 1.00 75.98  ? 118 LEU I CG  1 
ATOM   14914 C  CD1 . LEU I  1 127 ? 16.513  31.694  17.374 1.00 77.69  ? 118 LEU I CD1 1 
ATOM   14915 C  CD2 . LEU I  1 127 ? 17.067  33.870  18.537 1.00 75.75  ? 118 LEU I CD2 1 
ATOM   14916 N  N   . PRO I  1 128 ? 15.002  32.269  23.287 1.00 55.29  ? 119 PRO I N   1 
ATOM   14917 C  CA  . PRO I  1 128 ? 14.094  32.832  24.286 1.00 52.64  ? 119 PRO I CA  1 
ATOM   14918 C  C   . PRO I  1 128 ? 14.078  34.343  24.269 1.00 58.62  ? 119 PRO I C   1 
ATOM   14919 O  O   . PRO I  1 128 ? 15.133  34.986  24.354 1.00 55.53  ? 119 PRO I O   1 
ATOM   14920 C  CB  . PRO I  1 128 ? 14.712  32.373  25.598 1.00 49.69  ? 119 PRO I CB  1 
ATOM   14921 C  CG  . PRO I  1 128 ? 16.155  32.336  25.316 1.00 54.26  ? 119 PRO I CG  1 
ATOM   14922 C  CD  . PRO I  1 128 ? 16.281  31.864  23.897 1.00 59.19  ? 119 PRO I CD  1 
ATOM   14923 N  N   . ALA I  1 129 ? 12.871  34.894  24.238 1.00 64.22  ? 120 ALA I N   1 
ATOM   14924 C  CA  . ALA I  1 129 ? 12.655  36.327  24.394 1.00 60.52  ? 120 ALA I CA  1 
ATOM   14925 C  C   . ALA I  1 129 ? 12.364  36.598  25.861 1.00 52.84  ? 120 ALA I C   1 
ATOM   14926 O  O   . ALA I  1 129 ? 11.570  35.896  26.481 1.00 46.25  ? 120 ALA I O   1 
ATOM   14927 C  CB  . ALA I  1 129 ? 11.492  36.784  23.527 1.00 57.21  ? 120 ALA I CB  1 
ATOM   14928 N  N   . GLN I  1 130 ? 13.015  37.615  26.407 1.00 54.27  ? 121 GLN I N   1 
ATOM   14929 C  CA  . GLN I  1 130 ? 12.908  37.900  27.830 1.00 51.89  ? 121 GLN I CA  1 
ATOM   14930 C  C   . GLN I  1 130 ? 13.034  39.369  28.182 1.00 49.70  ? 121 GLN I C   1 
ATOM   14931 O  O   . GLN I  1 130 ? 13.684  40.134  27.485 1.00 54.52  ? 121 GLN I O   1 
ATOM   14932 C  CB  . GLN I  1 130 ? 13.935  37.085  28.624 1.00 52.07  ? 121 GLN I CB  1 
ATOM   14933 C  CG  . GLN I  1 130 ? 15.242  36.824  27.910 1.00 53.93  ? 121 GLN I CG  1 
ATOM   14934 C  CD  . GLN I  1 130 ? 16.147  35.868  28.676 1.00 62.87  ? 121 GLN I CD  1 
ATOM   14935 O  OE1 . GLN I  1 130 ? 15.818  34.695  28.864 1.00 61.44  ? 121 GLN I OE1 1 
ATOM   14936 N  NE2 . GLN I  1 130 ? 17.290  36.371  29.136 1.00 67.35  ? 121 GLN I NE2 1 
ATOM   14937 N  N   . ARG I  1 131 ? 12.385  39.748  29.277 1.00 56.15  ? 122 ARG I N   1 
ATOM   14938 C  CA  . ARG I  1 131 ? 12.606  41.038  29.926 1.00 50.63  ? 122 ARG I CA  1 
ATOM   14939 C  C   . ARG I  1 131 ? 13.513  40.860  31.122 1.00 50.38  ? 122 ARG I C   1 
ATOM   14940 O  O   . ARG I  1 131 ? 13.232  40.052  32.013 1.00 54.09  ? 122 ARG I O   1 
ATOM   14941 C  CB  . ARG I  1 131 ? 11.298  41.613  30.418 1.00 44.67  ? 122 ARG I CB  1 
ATOM   14942 C  CG  . ARG I  1 131 ? 11.463  42.855  31.248 1.00 47.00  ? 122 ARG I CG  1 
ATOM   14943 C  CD  . ARG I  1 131 ? 10.170  43.626  31.212 1.00 55.66  ? 122 ARG I CD  1 
ATOM   14944 N  NE  . ARG I  1 131 ? 10.193  44.903  31.908 1.00 53.38  ? 122 ARG I NE  1 
ATOM   14945 C  CZ  . ARG I  1 131 ? 9.201   45.778  31.825 1.00 54.16  ? 122 ARG I CZ  1 
ATOM   14946 N  NH1 . ARG I  1 131 ? 8.147   45.508  31.066 1.00 52.15  ? 122 ARG I NH1 1 
ATOM   14947 N  NH2 . ARG I  1 131 ? 9.257   46.920  32.488 1.00 56.19  ? 122 ARG I NH2 1 
ATOM   14948 N  N   . LEU I  1 132 ? 14.599  41.622  31.147 1.00 50.67  ? 123 LEU I N   1 
ATOM   14949 C  CA  . LEU I  1 132 ? 15.547  41.576  32.253 1.00 51.83  ? 123 LEU I CA  1 
ATOM   14950 C  C   . LEU I  1 132 ? 15.639  42.921  32.981 1.00 50.51  ? 123 LEU I C   1 
ATOM   14951 O  O   . LEU I  1 132 ? 15.738  43.957  32.335 1.00 50.98  ? 123 LEU I O   1 
ATOM   14952 C  CB  . LEU I  1 132 ? 16.918  41.160  31.725 1.00 49.49  ? 123 LEU I CB  1 
ATOM   14953 C  CG  . LEU I  1 132 ? 18.101  41.191  32.682 1.00 55.25  ? 123 LEU I CG  1 
ATOM   14954 C  CD1 . LEU I  1 132 ? 17.880  40.239  33.851 1.00 58.13  ? 123 LEU I CD1 1 
ATOM   14955 C  CD2 . LEU I  1 132 ? 19.353  40.834  31.920 1.00 57.01  ? 123 LEU I CD2 1 
ATOM   14956 N  N   . SER I  1 133 ? 15.575  42.892  34.318 1.00 48.78  ? 124 SER I N   1 
ATOM   14957 C  CA  . SER I  1 133 ? 15.942  44.030  35.170 1.00 49.72  ? 124 SER I CA  1 
ATOM   14958 C  C   . SER I  1 133 ? 17.362  43.789  35.625 1.00 50.91  ? 124 SER I C   1 
ATOM   14959 O  O   . SER I  1 133 ? 17.638  42.762  36.204 1.00 58.31  ? 124 SER I O   1 
ATOM   14960 C  CB  . SER I  1 133 ? 15.068  44.095  36.428 1.00 55.89  ? 124 SER I CB  1 
ATOM   14961 O  OG  . SER I  1 133 ? 13.754  44.532  36.162 1.00 59.10  ? 124 SER I OG  1 
ATOM   14962 N  N   . PHE I  1 134 ? 18.275  44.715  35.380 1.00 56.04  ? 125 PHE I N   1 
ATOM   14963 C  CA  . PHE I  1 134 ? 19.646  44.540  35.879 1.00 61.95  ? 125 PHE I CA  1 
ATOM   14964 C  C   . PHE I  1 134 ? 20.224  45.798  36.555 1.00 62.62  ? 125 PHE I C   1 
ATOM   14965 O  O   . PHE I  1 134 ? 19.542  46.824  36.702 1.00 59.70  ? 125 PHE I O   1 
ATOM   14966 C  CB  . PHE I  1 134 ? 20.584  44.009  34.780 1.00 58.80  ? 125 PHE I CB  1 
ATOM   14967 C  CG  . PHE I  1 134 ? 20.756  44.949  33.630 1.00 61.18  ? 125 PHE I CG  1 
ATOM   14968 C  CD1 . PHE I  1 134 ? 21.824  45.827  33.590 1.00 63.93  ? 125 PHE I CD1 1 
ATOM   14969 C  CD2 . PHE I  1 134 ? 19.839  44.970  32.598 1.00 58.37  ? 125 PHE I CD2 1 
ATOM   14970 C  CE1 . PHE I  1 134 ? 21.979  46.700  32.539 1.00 65.62  ? 125 PHE I CE1 1 
ATOM   14971 C  CE2 . PHE I  1 134 ? 19.991  45.838  31.551 1.00 61.90  ? 125 PHE I CE2 1 
ATOM   14972 C  CZ  . PHE I  1 134 ? 21.064  46.707  31.523 1.00 62.03  ? 125 PHE I CZ  1 
ATOM   14973 N  N   . MET I  1 135 ? 21.488  45.718  36.953 1.00 60.90  ? 126 MET I N   1 
ATOM   14974 C  CA  . MET I  1 135 ? 22.077  46.806  37.700 1.00 57.36  ? 126 MET I CA  1 
ATOM   14975 C  C   . MET I  1 135 ? 22.722  47.769  36.731 1.00 61.91  ? 126 MET I C   1 
ATOM   14976 O  O   . MET I  1 135 ? 23.720  47.442  36.089 1.00 63.05  ? 126 MET I O   1 
ATOM   14977 C  CB  . MET I  1 135 ? 23.116  46.264  38.669 1.00 52.94  ? 126 MET I CB  1 
ATOM   14978 C  CG  . MET I  1 135 ? 22.505  45.629  39.882 1.00 51.49  ? 126 MET I CG  1 
ATOM   14979 S  SD  . MET I  1 135 ? 23.419  44.218  40.504 1.00 63.92  ? 126 MET I SD  1 
ATOM   14980 C  CE  . MET I  1 135 ? 25.103  44.783  40.382 1.00 60.00  ? 126 MET I CE  1 
ATOM   14981 N  N   . CYS I  1 136 ? 22.117  48.952  36.632 1.00 58.81  ? 127 CYS I N   1 
ATOM   14982 C  CA  . CYS I  1 136 ? 22.574  50.029  35.765 1.00 61.33  ? 127 CYS I CA  1 
ATOM   14983 C  C   . CYS I  1 136 ? 22.370  51.407  36.404 1.00 64.32  ? 127 CYS I C   1 
ATOM   14984 O  O   . CYS I  1 136 ? 21.273  51.732  36.865 1.00 62.74  ? 127 CYS I O   1 
ATOM   14985 C  CB  . CYS I  1 136 ? 21.824  49.962  34.428 1.00 69.65  ? 127 CYS I CB  1 
ATOM   14986 S  SG  . CYS I  1 136 ? 21.786  51.499  33.455 1.00 78.53  ? 127 CYS I SG  1 
ATOM   14987 N  N   . ASP I  1 137 ? 23.417  52.227  36.388 1.00 69.21  ? 128 ASP I N   1 
ATOM   14988 C  CA  . ASP I  1 137 ? 23.290  53.642  36.731 1.00 67.43  ? 128 ASP I CA  1 
ATOM   14989 C  C   . ASP I  1 137 ? 23.051  54.409  35.432 1.00 68.28  ? 128 ASP I C   1 
ATOM   14990 O  O   . ASP I  1 137 ? 23.949  54.538  34.604 1.00 71.22  ? 128 ASP I O   1 
ATOM   14991 C  CB  . ASP I  1 137 ? 24.566  54.147  37.424 1.00 71.34  ? 128 ASP I CB  1 
ATOM   14992 C  CG  . ASP I  1 137 ? 24.487  55.622  37.823 1.00 81.38  ? 128 ASP I CG  1 
ATOM   14993 O  OD1 . ASP I  1 137 ? 23.536  56.323  37.413 1.00 78.39  ? 128 ASP I OD1 1 
ATOM   14994 O  OD2 . ASP I  1 137 ? 25.401  56.088  38.535 1.00 77.15  ? 128 ASP I OD2 1 
ATOM   14995 N  N   . PRO I  1 138 ? 21.826  54.912  35.245 1.00 66.39  ? 129 PRO I N   1 
ATOM   14996 C  CA  . PRO I  1 138 ? 21.481  55.595  34.005 1.00 69.80  ? 129 PRO I CA  1 
ATOM   14997 C  C   . PRO I  1 138 ? 21.757  57.068  34.328 1.00 79.10  ? 129 PRO I C   1 
ATOM   14998 O  O   . PRO I  1 138 ? 20.833  57.853  34.517 1.00 79.12  ? 129 PRO I O   1 
ATOM   14999 C  CB  . PRO I  1 138 ? 19.982  55.342  33.913 1.00 63.32  ? 129 PRO I CB  1 
ATOM   15000 C  CG  . PRO I  1 138 ? 19.541  55.431  35.344 1.00 64.29  ? 129 PRO I CG  1 
ATOM   15001 C  CD  . PRO I  1 138 ? 20.676  54.855  36.164 1.00 70.09  ? 129 PRO I CD  1 
ATOM   15002 N  N   . THR I  1 139 ? 23.029  57.436  34.403 1.00 79.67  ? 130 THR I N   1 
ATOM   15003 C  CA  . THR I  1 139 ? 23.395  58.836  34.573 1.00 83.48  ? 130 THR I CA  1 
ATOM   15004 C  C   . THR I  1 139 ? 23.981  59.422  33.288 1.00 88.36  ? 130 THR I C   1 
ATOM   15005 O  O   . THR I  1 139 ? 24.871  58.835  32.673 1.00 90.73  ? 130 THR I O   1 
ATOM   15006 C  CB  . THR I  1 139 ? 24.336  59.033  35.778 1.00 79.79  ? 130 THR I CB  1 
ATOM   15007 O  OG1 . THR I  1 139 ? 23.551  59.099  36.972 1.00 76.64  ? 130 THR I OG1 1 
ATOM   15008 C  CG2 . THR I  1 139 ? 25.119  60.320  35.645 1.00 72.91  ? 130 THR I CG2 1 
ATOM   15009 N  N   . GLY I  1 140 ? 23.467  60.577  32.882 1.00 83.79  ? 131 GLY I N   1 
ATOM   15010 C  CA  . GLY I  1 140 ? 23.824  61.140  31.597 1.00 79.55  ? 131 GLY I CA  1 
ATOM   15011 C  C   . GLY I  1 140 ? 22.914  60.565  30.535 1.00 77.35  ? 131 GLY I C   1 
ATOM   15012 O  O   . GLY I  1 140 ? 23.231  60.581  29.350 1.00 83.95  ? 131 GLY I O   1 
ATOM   15013 N  N   . VAL I  1 141 ? 21.769  60.081  30.962 1.00 78.79  ? 132 VAL I N   1 
ATOM   15014 C  CA  . VAL I  1 141 ? 20.771  59.565  30.061 1.00 78.73  ? 132 VAL I CA  1 
ATOM   15015 C  C   . VAL I  1 141 ? 20.229  60.686  29.216 1.00 80.48  ? 132 VAL I C   1 
ATOM   15016 O  O   . VAL I  1 141 ? 19.990  60.534  28.045 1.00 72.44  ? 132 VAL I O   1 
ATOM   15017 C  CB  . VAL I  1 141 ? 19.619  59.016  30.852 1.00 67.13  ? 132 VAL I CB  1 
ATOM   15018 C  CG1 . VAL I  1 141 ? 18.967  57.908  30.117 1.00 69.57  ? 132 VAL I CG1 1 
ATOM   15019 C  CG2 . VAL I  1 141 ? 20.122  58.538  32.161 1.00 75.10  ? 132 VAL I CG2 1 
ATOM   15020 N  N   . ASP I  1 142 ? 20.019  61.822  29.853 1.00 82.08  ? 133 ASP I N   1 
ATOM   15021 C  CA  . ASP I  1 142 ? 19.472  63.024  29.216 1.00 82.28  ? 133 ASP I CA  1 
ATOM   15022 C  C   . ASP I  1 142 ? 20.537  63.837  28.468 1.00 82.66  ? 133 ASP I C   1 
ATOM   15023 O  O   . ASP I  1 142 ? 20.229  64.775  27.745 1.00 81.27  ? 133 ASP I O   1 
ATOM   15024 C  CB  . ASP I  1 142 ? 18.810  63.901  30.275 1.00 85.21  ? 133 ASP I CB  1 
ATOM   15025 C  CG  . ASP I  1 142 ? 19.593  63.927  31.585 1.00 91.06  ? 133 ASP I CG  1 
ATOM   15026 O  OD1 . ASP I  1 142 ? 20.795  63.576  31.580 1.00 87.50  ? 133 ASP I OD1 1 
ATOM   15027 O  OD2 . ASP I  1 142 ? 19.007  64.301  32.624 1.00 94.91  ? 133 ASP I OD2 1 
ATOM   15028 N  N   . SER I  1 143 ? 21.789  63.459  28.683 1.00 84.61  ? 134 SER I N   1 
ATOM   15029 C  CA  . SER I  1 143 ? 22.967  63.952  27.980 1.00 82.41  ? 134 SER I CA  1 
ATOM   15030 C  C   . SER I  1 143 ? 22.979  63.481  26.515 1.00 88.85  ? 134 SER I C   1 
ATOM   15031 O  O   . SER I  1 143 ? 22.213  62.597  26.139 1.00 89.89  ? 134 SER I O   1 
ATOM   15032 C  CB  . SER I  1 143 ? 24.210  63.448  28.729 1.00 89.23  ? 134 SER I CB  1 
ATOM   15033 O  OG  . SER I  1 143 ? 25.419  63.787  28.085 1.00 99.94  ? 134 SER I OG  1 
ATOM   15034 N  N   . GLU I  1 144 ? 23.783  64.119  25.670 1.00 93.69  ? 135 GLU I N   1 
ATOM   15035 C  CA  . GLU I  1 144 ? 24.009  63.614  24.311 1.00 98.26  ? 135 GLU I CA  1 
ATOM   15036 C  C   . GLU I  1 144 ? 24.986  62.436  24.289 1.00 94.24  ? 135 GLU I C   1 
ATOM   15037 O  O   . GLU I  1 144 ? 25.082  61.717  23.291 1.00 87.49  ? 135 GLU I O   1 
ATOM   15038 C  CB  . GLU I  1 144 ? 24.545  64.716  23.388 1.00 108.95 ? 135 GLU I CB  1 
ATOM   15039 C  CG  . GLU I  1 144 ? 23.627  65.918  23.209 1.00 114.63 ? 135 GLU I CG  1 
ATOM   15040 C  CD  . GLU I  1 144 ? 22.309  65.566  22.542 1.00 115.23 ? 135 GLU I CD  1 
ATOM   15041 O  OE1 . GLU I  1 144 ? 22.145  64.407  22.101 1.00 112.15 ? 135 GLU I OE1 1 
ATOM   15042 O  OE2 . GLU I  1 144 ? 21.431  66.453  22.462 1.00 125.43 ? 135 GLU I OE2 1 
ATOM   15043 N  N   . GLU I  1 145 ? 25.728  62.260  25.382 1.00 95.84  ? 136 GLU I N   1 
ATOM   15044 C  CA  . GLU I  1 145 ? 26.716  61.190  25.477 1.00 90.17  ? 136 GLU I CA  1 
ATOM   15045 C  C   . GLU I  1 145 ? 26.063  59.937  26.028 1.00 84.13  ? 136 GLU I C   1 
ATOM   15046 O  O   . GLU I  1 145 ? 26.674  58.872  26.063 1.00 79.76  ? 136 GLU I O   1 
ATOM   15047 C  CB  . GLU I  1 145 ? 27.898  61.597  26.361 1.00 95.65  ? 136 GLU I CB  1 
ATOM   15048 C  CG  . GLU I  1 145 ? 28.799  62.669  25.768 1.00 104.68 ? 136 GLU I CG  1 
ATOM   15049 C  CD  . GLU I  1 145 ? 28.258  64.080  25.969 1.00 113.31 ? 136 GLU I CD  1 
ATOM   15050 O  OE1 . GLU I  1 145 ? 27.027  64.241  26.114 1.00 111.59 ? 136 GLU I OE1 1 
ATOM   15051 O  OE2 . GLU I  1 145 ? 29.066  65.036  25.985 1.00 112.63 ? 136 GLU I OE2 1 
ATOM   15052 N  N   . GLY I  1 146 ? 24.815  60.079  26.460 1.00 82.68  ? 137 GLY I N   1 
ATOM   15053 C  CA  . GLY I  1 146 ? 24.026  58.955  26.922 1.00 78.93  ? 137 GLY I CA  1 
ATOM   15054 C  C   . GLY I  1 146 ? 24.497  58.389  28.247 1.00 84.02  ? 137 GLY I C   1 
ATOM   15055 O  O   . GLY I  1 146 ? 25.306  58.992  28.947 1.00 89.32  ? 137 GLY I O   1 
ATOM   15056 N  N   . ALA I  1 147 ? 23.996  57.214  28.589 1.00 74.25  ? 138 ALA I N   1 
ATOM   15057 C  CA  . ALA I  1 147 ? 24.400  56.551  29.811 1.00 72.72  ? 138 ALA I CA  1 
ATOM   15058 C  C   . ALA I  1 147 ? 24.957  55.218  29.362 1.00 71.90  ? 138 ALA I C   1 
ATOM   15059 O  O   . ALA I  1 147 ? 24.756  54.833  28.216 1.00 73.20  ? 138 ALA I O   1 
ATOM   15060 C  CB  . ALA I  1 147 ? 23.213  56.361  30.715 1.00 71.29  ? 138 ALA I CB  1 
ATOM   15061 N  N   . THR I  1 148 ? 25.702  54.529  30.213 1.00 65.41  ? 139 THR I N   1 
ATOM   15062 C  CA  . THR I  1 148 ? 26.193  53.222  29.808 1.00 65.00  ? 139 THR I CA  1 
ATOM   15063 C  C   . THR I  1 148 ? 25.983  52.161  30.871 1.00 71.90  ? 139 THR I C   1 
ATOM   15064 O  O   . THR I  1 148 ? 26.113  52.425  32.072 1.00 70.80  ? 139 THR I O   1 
ATOM   15065 C  CB  . THR I  1 148 ? 27.668  53.255  29.405 1.00 69.17  ? 139 THR I CB  1 
ATOM   15066 O  OG1 . THR I  1 148 ? 27.845  54.189  28.339 1.00 72.00  ? 139 THR I OG1 1 
ATOM   15067 C  CG2 . THR I  1 148 ? 28.106  51.887  28.924 1.00 70.95  ? 139 THR I CG2 1 
ATOM   15068 N  N   . CYS I  1 149 ? 25.654  50.957  30.414 1.00 65.91  ? 140 CYS I N   1 
ATOM   15069 C  CA  . CYS I  1 149 ? 25.458  49.827  31.305 1.00 64.52  ? 140 CYS I CA  1 
ATOM   15070 C  C   . CYS I  1 149 ? 25.980  48.538  30.741 1.00 60.41  ? 140 CYS I C   1 
ATOM   15071 O  O   . CYS I  1 149 ? 25.866  48.275  29.558 1.00 58.11  ? 140 CYS I O   1 
ATOM   15072 C  CB  . CYS I  1 149 ? 23.992  49.670  31.666 1.00 63.60  ? 140 CYS I CB  1 
ATOM   15073 S  SG  . CYS I  1 149 ? 23.592  50.664  33.091 1.00 84.64  ? 140 CYS I SG  1 
ATOM   15074 N  N   . ALA I  1 150 ? 26.550  47.722  31.611 1.00 64.62  ? 141 ALA I N   1 
ATOM   15075 C  CA  . ALA I  1 150 ? 27.008  46.407  31.204 1.00 64.15  ? 141 ALA I CA  1 
ATOM   15076 C  C   . ALA I  1 150 ? 26.311  45.304  32.003 1.00 57.71  ? 141 ALA I C   1 
ATOM   15077 O  O   . ALA I  1 150 ? 26.027  45.450  33.190 1.00 54.50  ? 141 ALA I O   1 
ATOM   15078 C  CB  . ALA I  1 150 ? 28.521  46.307  31.340 1.00 63.74  ? 141 ALA I CB  1 
ATOM   15079 N  N   . VAL I  1 151 ? 26.018  44.205  31.322 1.00 63.38  ? 142 VAL I N   1 
ATOM   15080 C  CA  . VAL I  1 151 ? 25.563  42.993  31.976 1.00 55.30  ? 142 VAL I CA  1 
ATOM   15081 C  C   . VAL I  1 151 ? 26.385  41.835  31.471 1.00 57.02  ? 142 VAL I C   1 
ATOM   15082 O  O   . VAL I  1 151 ? 26.547  41.661  30.265 1.00 57.35  ? 142 VAL I O   1 
ATOM   15083 C  CB  . VAL I  1 151 ? 24.116  42.699  31.653 1.00 56.47  ? 142 VAL I CB  1 
ATOM   15084 C  CG1 . VAL I  1 151 ? 23.583  41.691  32.628 1.00 57.42  ? 142 VAL I CG1 1 
ATOM   15085 C  CG2 . VAL I  1 151 ? 23.318  43.958  31.745 1.00 61.45  ? 142 VAL I CG2 1 
ATOM   15086 N  N   . LYS I  1 152 ? 26.912  41.045  32.397 1.00 61.21  ? 143 LYS I N   1 
ATOM   15087 C  CA  . LYS I  1 152 ? 27.616  39.818  32.039 1.00 64.04  ? 143 LYS I CA  1 
ATOM   15088 C  C   . LYS I  1 152 ? 26.684  38.608  32.040 1.00 60.25  ? 143 LYS I C   1 
ATOM   15089 O  O   . LYS I  1 152 ? 25.844  38.451  32.931 1.00 55.03  ? 143 LYS I O   1 
ATOM   15090 C  CB  . LYS I  1 152 ? 28.811  39.589  32.956 1.00 62.87  ? 143 LYS I CB  1 
ATOM   15091 C  CG  . LYS I  1 152 ? 29.980  40.468  32.611 1.00 71.06  ? 143 LYS I CG  1 
ATOM   15092 C  CD  . LYS I  1 152 ? 31.086  40.371  33.638 1.00 77.60  ? 143 LYS I CD  1 
ATOM   15093 C  CE  . LYS I  1 152 ? 32.145  41.410  33.347 1.00 81.70  ? 143 LYS I CE  1 
ATOM   15094 N  NZ  . LYS I  1 152 ? 31.509  42.747  33.074 1.00 82.92  ? 143 LYS I NZ  1 
ATOM   15095 N  N   . PHE I  1 153 ? 26.831  37.782  31.006 1.00 59.15  ? 144 PHE I N   1 
ATOM   15096 C  CA  . PHE I  1 153 ? 26.054  36.567  30.830 1.00 51.82  ? 144 PHE I CA  1 
ATOM   15097 C  C   . PHE I  1 153 ? 26.999  35.394  30.764 1.00 56.95  ? 144 PHE I C   1 
ATOM   15098 O  O   . PHE I  1 153 ? 27.987  35.435  30.036 1.00 58.39  ? 144 PHE I O   1 
ATOM   15099 C  CB  . PHE I  1 153 ? 25.280  36.621  29.525 1.00 50.58  ? 144 PHE I CB  1 
ATOM   15100 C  CG  . PHE I  1 153 ? 24.048  37.446  29.586 1.00 51.60  ? 144 PHE I CG  1 
ATOM   15101 C  CD1 . PHE I  1 153 ? 22.843  36.872  29.916 1.00 50.90  ? 144 PHE I CD1 1 
ATOM   15102 C  CD2 . PHE I  1 153 ? 24.087  38.792  29.300 1.00 53.10  ? 144 PHE I CD2 1 
ATOM   15103 C  CE1 . PHE I  1 153 ? 21.698  37.621  29.971 1.00 51.45  ? 144 PHE I CE1 1 
ATOM   15104 C  CE2 . PHE I  1 153 ? 22.941  39.552  29.355 1.00 57.24  ? 144 PHE I CE2 1 
ATOM   15105 C  CZ  . PHE I  1 153 ? 21.742  38.964  29.692 1.00 55.04  ? 144 PHE I CZ  1 
ATOM   15106 N  N   . GLY I  1 154 ? 26.683  34.342  31.514 1.00 60.90  ? 145 GLY I N   1 
ATOM   15107 C  CA  . GLY I  1 154 ? 27.500  33.140  31.537 1.00 61.00  ? 145 GLY I CA  1 
ATOM   15108 C  C   . GLY I  1 154 ? 26.838  31.979  32.250 1.00 60.62  ? 145 GLY I C   1 
ATOM   15109 O  O   . GLY I  1 154 ? 25.704  32.095  32.722 1.00 59.02  ? 145 GLY I O   1 
ATOM   15110 N  N   . SER I  1 155 ? 27.545  30.854  32.316 1.00 58.71  ? 146 SER I N   1 
ATOM   15111 C  CA  . SER I  1 155 ? 27.040  29.673  33.011 1.00 60.33  ? 146 SER I CA  1 
ATOM   15112 C  C   . SER I  1 155 ? 27.130  29.875  34.516 1.00 66.28  ? 146 SER I C   1 
ATOM   15113 O  O   . SER I  1 155 ? 28.146  30.340  35.013 1.00 70.55  ? 146 SER I O   1 
ATOM   15114 C  CB  . SER I  1 155 ? 27.848  28.440  32.608 1.00 61.70  ? 146 SER I CB  1 
ATOM   15115 O  OG  . SER I  1 155 ? 27.761  27.421  33.585 1.00 61.06  ? 146 SER I OG  1 
ATOM   15116 N  N   . TRP I  1 156 ? 26.073  29.544  35.249 1.00 65.14  ? 147 TRP I N   1 
ATOM   15117 C  CA  . TRP I  1 156 ? 26.132  29.687  36.695 1.00 65.13  ? 147 TRP I CA  1 
ATOM   15118 C  C   . TRP I  1 156 ? 27.041  28.642  37.317 1.00 70.91  ? 147 TRP I C   1 
ATOM   15119 O  O   . TRP I  1 156 ? 27.950  28.980  38.079 1.00 69.82  ? 147 TRP I O   1 
ATOM   15120 C  CB  . TRP I  1 156 ? 24.742  29.641  37.345 1.00 60.24  ? 147 TRP I CB  1 
ATOM   15121 C  CG  . TRP I  1 156 ? 24.761  30.167  38.751 1.00 59.63  ? 147 TRP I CG  1 
ATOM   15122 C  CD1 . TRP I  1 156 ? 24.597  29.452  39.905 1.00 65.41  ? 147 TRP I CD1 1 
ATOM   15123 C  CD2 . TRP I  1 156 ? 24.998  31.518  39.151 1.00 62.93  ? 147 TRP I CD2 1 
ATOM   15124 N  NE1 . TRP I  1 156 ? 24.700  30.279  40.999 1.00 59.34  ? 147 TRP I NE1 1 
ATOM   15125 C  CE2 . TRP I  1 156 ? 24.946  31.552  40.562 1.00 61.66  ? 147 TRP I CE2 1 
ATOM   15126 C  CE3 . TRP I  1 156 ? 25.238  32.703  38.454 1.00 62.62  ? 147 TRP I CE3 1 
ATOM   15127 C  CZ2 . TRP I  1 156 ? 25.132  32.723  41.282 1.00 58.15  ? 147 TRP I CZ2 1 
ATOM   15128 C  CZ3 . TRP I  1 156 ? 25.414  33.857  39.163 1.00 68.40  ? 147 TRP I CZ3 1 
ATOM   15129 C  CH2 . TRP I  1 156 ? 25.366  33.862  40.569 1.00 73.80  ? 147 TRP I CH2 1 
ATOM   15130 N  N   . SER I  1 157 ? 26.779  27.373  37.001 1.00 70.99  ? 148 SER I N   1 
ATOM   15131 C  CA  . SER I  1 157 ? 27.463  26.250  37.658 1.00 71.36  ? 148 SER I CA  1 
ATOM   15132 C  C   . SER I  1 157 ? 28.664  25.626  36.914 1.00 68.30  ? 148 SER I C   1 
ATOM   15133 O  O   . SER I  1 157 ? 29.342  24.763  37.463 1.00 61.78  ? 148 SER I O   1 
ATOM   15134 C  CB  . SER I  1 157 ? 26.438  25.155  38.006 1.00 69.65  ? 148 SER I CB  1 
ATOM   15135 O  OG  . SER I  1 157 ? 25.325  25.673  38.731 1.00 67.25  ? 148 SER I OG  1 
ATOM   15136 N  N   . TYR I  1 158 ? 28.945  26.075  35.692 1.00 68.08  ? 149 TYR I N   1 
ATOM   15137 C  CA  . TYR I  1 158 ? 29.934  25.412  34.835 1.00 64.06  ? 149 TYR I CA  1 
ATOM   15138 C  C   . TYR I  1 158 ? 31.044  26.361  34.417 1.00 72.41  ? 149 TYR I C   1 
ATOM   15139 O  O   . TYR I  1 158 ? 30.792  27.501  34.037 1.00 71.07  ? 149 TYR I O   1 
ATOM   15140 C  CB  . TYR I  1 158 ? 29.299  24.894  33.540 1.00 63.08  ? 149 TYR I CB  1 
ATOM   15141 C  CG  . TYR I  1 158 ? 28.407  23.670  33.605 1.00 61.03  ? 149 TYR I CG  1 
ATOM   15142 C  CD1 . TYR I  1 158 ? 28.938  22.394  33.674 1.00 56.98  ? 149 TYR I CD1 1 
ATOM   15143 C  CD2 . TYR I  1 158 ? 27.027  23.797  33.507 1.00 63.26  ? 149 TYR I CD2 1 
ATOM   15144 C  CE1 . TYR I  1 158 ? 28.119  21.288  33.693 1.00 61.77  ? 149 TYR I CE1 1 
ATOM   15145 C  CE2 . TYR I  1 158 ? 26.200  22.694  33.525 1.00 64.38  ? 149 TYR I CE2 1 
ATOM   15146 C  CZ  . TYR I  1 158 ? 26.752  21.443  33.617 1.00 62.41  ? 149 TYR I CZ  1 
ATOM   15147 O  OH  . TYR I  1 158 ? 25.939  20.340  33.639 1.00 60.30  ? 149 TYR I OH  1 
ATOM   15148 N  N   . GLY I  1 159 ? 32.273  25.866  34.440 1.00 77.47  ? 150 GLY I N   1 
ATOM   15149 C  CA  . GLY I  1 159 ? 33.415  26.650  34.014 1.00 78.68  ? 150 GLY I CA  1 
ATOM   15150 C  C   . GLY I  1 159 ? 33.822  26.342  32.594 1.00 72.24  ? 150 GLY I C   1 
ATOM   15151 O  O   . GLY I  1 159 ? 33.209  25.513  31.929 1.00 71.62  ? 150 GLY I O   1 
ATOM   15152 N  N   . GLY I  1 160 ? 34.881  26.999  32.142 1.00 73.83  ? 151 GLY I N   1 
ATOM   15153 C  CA  . GLY I  1 160 ? 35.278  26.959  30.747 1.00 78.05  ? 151 GLY I CA  1 
ATOM   15154 C  C   . GLY I  1 160 ? 35.690  25.600  30.216 1.00 82.86  ? 151 GLY I C   1 
ATOM   15155 O  O   . GLY I  1 160 ? 35.675  25.377  29.001 1.00 71.52  ? 151 GLY I O   1 
ATOM   15156 N  N   . TRP I  1 161 ? 36.066  24.691  31.115 1.00 86.64  ? 152 TRP I N   1 
ATOM   15157 C  CA  . TRP I  1 161 ? 36.512  23.360  30.702 1.00 84.95  ? 152 TRP I CA  1 
ATOM   15158 C  C   . TRP I  1 161 ? 35.360  22.388  30.496 1.00 81.35  ? 152 TRP I C   1 
ATOM   15159 O  O   . TRP I  1 161 ? 35.547  21.297  29.952 1.00 76.95  ? 152 TRP I O   1 
ATOM   15160 C  CB  . TRP I  1 161 ? 37.517  22.794  31.697 1.00 86.88  ? 152 TRP I CB  1 
ATOM   15161 C  CG  . TRP I  1 161 ? 38.834  23.449  31.569 1.00 93.66  ? 152 TRP I CG  1 
ATOM   15162 C  CD1 . TRP I  1 161 ? 39.241  24.270  30.559 1.00 95.38  ? 152 TRP I CD1 1 
ATOM   15163 C  CD2 . TRP I  1 161 ? 39.930  23.357  32.479 1.00 95.27  ? 152 TRP I CD2 1 
ATOM   15164 N  NE1 . TRP I  1 161 ? 40.528  24.695  30.783 1.00 99.04  ? 152 TRP I NE1 1 
ATOM   15165 C  CE2 . TRP I  1 161 ? 40.974  24.149  31.960 1.00 94.72  ? 152 TRP I CE2 1 
ATOM   15166 C  CE3 . TRP I  1 161 ? 40.131  22.687  33.686 1.00 91.08  ? 152 TRP I CE3 1 
ATOM   15167 C  CZ2 . TRP I  1 161 ? 42.199  24.283  32.599 1.00 94.60  ? 152 TRP I CZ2 1 
ATOM   15168 C  CZ3 . TRP I  1 161 ? 41.346  22.822  34.323 1.00 96.36  ? 152 TRP I CZ3 1 
ATOM   15169 C  CH2 . TRP I  1 161 ? 42.366  23.613  33.777 1.00 104.99 ? 152 TRP I CH2 1 
ATOM   15170 N  N   . GLU I  1 162 ? 34.179  22.794  30.949 1.00 77.10  ? 153 GLU I N   1 
ATOM   15171 C  CA  . GLU I  1 162 ? 32.950  22.064  30.691 1.00 75.09  ? 153 GLU I CA  1 
ATOM   15172 C  C   . GLU I  1 162 ? 32.055  22.756  29.676 1.00 71.30  ? 153 GLU I C   1 
ATOM   15173 O  O   . GLU I  1 162 ? 31.566  22.136  28.739 1.00 69.97  ? 153 GLU I O   1 
ATOM   15174 C  CB  . GLU I  1 162 ? 32.111  21.906  31.960 1.00 76.51  ? 153 GLU I CB  1 
ATOM   15175 C  CG  . GLU I  1 162 ? 32.804  21.127  33.076 1.00 79.16  ? 153 GLU I CG  1 
ATOM   15176 C  CD  . GLU I  1 162 ? 33.789  21.980  33.862 1.00 80.78  ? 153 GLU I CD  1 
ATOM   15177 O  OE1 . GLU I  1 162 ? 33.535  23.193  33.997 1.00 81.56  ? 153 GLU I OE1 1 
ATOM   15178 O  OE2 . GLU I  1 162 ? 34.815  21.445  34.342 1.00 79.80  ? 153 GLU I OE2 1 
ATOM   15179 N  N   . ILE I  1 163 ? 31.819  24.042  29.896 1.00 68.43  ? 154 ILE I N   1 
ATOM   15180 C  CA  . ILE I  1 163 ? 31.162  24.904  28.923 1.00 69.36  ? 154 ILE I CA  1 
ATOM   15181 C  C   . ILE I  1 163 ? 32.087  26.017  28.419 1.00 74.17  ? 154 ILE I C   1 
ATOM   15182 O  O   . ILE I  1 163 ? 32.685  26.742  29.216 1.00 76.00  ? 154 ILE I O   1 
ATOM   15183 C  CB  . ILE I  1 163 ? 29.931  25.575  29.537 1.00 64.43  ? 154 ILE I CB  1 
ATOM   15184 C  CG1 . ILE I  1 163 ? 28.834  24.556  29.797 1.00 58.40  ? 154 ILE I CG1 1 
ATOM   15185 C  CG2 . ILE I  1 163 ? 29.421  26.679  28.635 1.00 57.31  ? 154 ILE I CG2 1 
ATOM   15186 C  CD1 . ILE I  1 163 ? 27.518  25.203  30.137 1.00 61.71  ? 154 ILE I CD1 1 
ATOM   15187 N  N   . ASP I  1 164 ? 32.201  26.166  27.103 1.00 66.95  ? 155 ASP I N   1 
ATOM   15188 C  CA  . ASP I  1 164 ? 32.965  27.276  26.557 1.00 67.75  ? 155 ASP I CA  1 
ATOM   15189 C  C   . ASP I  1 164 ? 32.020  28.216  25.852 1.00 74.46  ? 155 ASP I C   1 
ATOM   15190 O  O   . ASP I  1 164 ? 31.221  27.792  25.021 1.00 77.60  ? 155 ASP I O   1 
ATOM   15191 C  CB  . ASP I  1 164 ? 34.047  26.799  25.589 1.00 72.24  ? 155 ASP I CB  1 
ATOM   15192 C  CG  . ASP I  1 164 ? 34.948  27.932  25.125 1.00 79.27  ? 155 ASP I CG  1 
ATOM   15193 O  OD1 . ASP I  1 164 ? 35.089  28.921  25.875 1.00 73.37  ? 155 ASP I OD1 1 
ATOM   15194 O  OD2 . ASP I  1 164 ? 35.511  27.836  24.011 1.00 77.57  ? 155 ASP I OD2 1 
ATOM   15195 N  N   . LEU I  1 165 ? 32.108  29.494  26.184 1.00 68.72  ? 156 LEU I N   1 
ATOM   15196 C  CA  . LEU I  1 165 ? 31.231  30.489  25.593 1.00 67.09  ? 156 LEU I CA  1 
ATOM   15197 C  C   . LEU I  1 165 ? 31.902  31.152  24.406 1.00 73.82  ? 156 LEU I C   1 
ATOM   15198 O  O   . LEU I  1 165 ? 33.121  31.322  24.395 1.00 77.50  ? 156 LEU I O   1 
ATOM   15199 C  CB  . LEU I  1 165 ? 30.848  31.535  26.629 1.00 71.20  ? 156 LEU I CB  1 
ATOM   15200 C  CG  . LEU I  1 165 ? 29.364  31.811  26.824 1.00 61.06  ? 156 LEU I CG  1 
ATOM   15201 C  CD1 . LEU I  1 165 ? 28.611  30.518  26.937 1.00 63.46  ? 156 LEU I CD1 1 
ATOM   15202 C  CD2 . LEU I  1 165 ? 29.178  32.636  28.072 1.00 63.15  ? 156 LEU I CD2 1 
ATOM   15203 N  N   . LYS I  1 166 ? 31.101  31.485  23.395 1.00 78.11  ? 157 LYS I N   1 
ATOM   15204 C  CA  . LYS I  1 166 ? 31.563  32.179  22.193 1.00 73.27  ? 157 LYS I CA  1 
ATOM   15205 C  C   . LYS I  1 166 ? 30.469  33.093  21.658 1.00 74.92  ? 157 LYS I C   1 
ATOM   15206 O  O   . LYS I  1 166 ? 29.285  32.827  21.824 1.00 74.19  ? 157 LYS I O   1 
ATOM   15207 C  CB  . LYS I  1 166 ? 31.915  31.181  21.085 1.00 78.05  ? 157 LYS I CB  1 
ATOM   15208 C  CG  . LYS I  1 166 ? 33.129  30.300  21.328 1.00 79.80  ? 157 LYS I CG  1 
ATOM   15209 C  CD  . LYS I  1 166 ? 34.426  31.005  20.981 1.00 83.21  ? 157 LYS I CD  1 
ATOM   15210 C  CE  . LYS I  1 166 ? 35.435  30.010  20.433 1.00 83.66  ? 157 LYS I CE  1 
ATOM   15211 N  NZ  . LYS I  1 166 ? 35.506  28.780  21.267 1.00 84.54  ? 157 LYS I NZ  1 
ATOM   15212 N  N   . THR I  1 167 ? 30.880  34.174  21.013 1.00 81.70  ? 158 THR I N   1 
ATOM   15213 C  CA  . THR I  1 167 ? 29.991  34.971  20.183 1.00 76.20  ? 158 THR I CA  1 
ATOM   15214 C  C   . THR I  1 167 ? 30.506  34.804  18.770 1.00 76.99  ? 158 THR I C   1 
ATOM   15215 O  O   . THR I  1 167 ? 31.708  34.652  18.575 1.00 81.64  ? 158 THR I O   1 
ATOM   15216 C  CB  . THR I  1 167 ? 30.083  36.454  20.554 1.00 79.72  ? 158 THR I CB  1 
ATOM   15217 O  OG1 . THR I  1 167 ? 31.378  36.723  21.109 1.00 79.61  ? 158 THR I OG1 1 
ATOM   15218 C  CG2 . THR I  1 167 ? 29.023  36.820  21.575 1.00 80.06  ? 158 THR I CG2 1 
ATOM   15219 N  N   . ASP I  1 168 ? 29.625  34.796  17.777 1.00 79.05  ? 159 ASP I N   1 
ATOM   15220 C  CA  . ASP I  1 168 ? 30.111  34.869  16.393 1.00 86.65  ? 159 ASP I CA  1 
ATOM   15221 C  C   . ASP I  1 168 ? 30.462  36.310  15.956 1.00 86.31  ? 159 ASP I C   1 
ATOM   15222 O  O   . ASP I  1 168 ? 31.326  36.518  15.099 1.00 82.38  ? 159 ASP I O   1 
ATOM   15223 C  CB  . ASP I  1 168 ? 29.178  34.153  15.398 1.00 82.52  ? 159 ASP I CB  1 
ATOM   15224 C  CG  . ASP I  1 168 ? 27.721  34.575  15.531 1.00 90.60  ? 159 ASP I CG  1 
ATOM   15225 O  OD1 . ASP I  1 168 ? 27.438  35.601  16.191 1.00 91.88  ? 159 ASP I OD1 1 
ATOM   15226 O  OD2 . ASP I  1 168 ? 26.855  33.879  14.957 1.00 81.25  ? 159 ASP I OD2 1 
ATOM   15227 N  N   . THR I  1 169 ? 29.806  37.290  16.579 1.00 81.27  ? 160 THR I N   1 
ATOM   15228 C  CA  . THR I  1 169 ? 30.071  38.706  16.335 1.00 77.80  ? 160 THR I CA  1 
ATOM   15229 C  C   . THR I  1 169 ? 30.332  39.453  17.632 1.00 84.71  ? 160 THR I C   1 
ATOM   15230 O  O   . THR I  1 169 ? 29.958  38.969  18.703 1.00 85.79  ? 160 THR I O   1 
ATOM   15231 C  CB  . THR I  1 169 ? 28.849  39.376  15.756 1.00 76.63  ? 160 THR I CB  1 
ATOM   15232 O  OG1 . THR I  1 169 ? 28.230  38.491  14.822 1.00 92.47  ? 160 THR I OG1 1 
ATOM   15233 C  CG2 . THR I  1 169 ? 29.234  40.689  15.082 1.00 73.81  ? 160 THR I CG2 1 
ATOM   15234 N  N   . ASP I  1 170 ? 30.973  40.624  17.536 1.00 79.94  ? 161 ASP I N   1 
ATOM   15235 C  CA  A ASP I  1 170 ? 31.117  41.529  18.684 0.50 82.53  ? 161 ASP I CA  1 
ATOM   15236 C  CA  B ASP I  1 170 ? 31.217  41.529  18.684 0.50 82.54  ? 161 ASP I CA  1 
ATOM   15237 C  C   . ASP I  1 170 ? 30.026  42.596  18.661 1.00 80.25  ? 161 ASP I C   1 
ATOM   15238 O  O   . ASP I  1 170 ? 29.973  43.465  19.535 1.00 74.06  ? 161 ASP I O   1 
ATOM   15239 C  CB  A ASP I  1 170 ? 32.542  42.145  18.795 0.50 83.41  ? 161 ASP I CB  1 
ATOM   15240 C  CB  B ASP I  1 170 ? 32.642  42.145  18.795 0.50 83.41  ? 161 ASP I CB  1 
ATOM   15241 C  CG  A ASP I  1 170 ? 32.753  43.396  17.921 0.50 78.28  ? 161 ASP I CG  1 
ATOM   15242 C  CG  B ASP I  1 170 ? 33.732  41.133  19.194 0.50 84.70  ? 161 ASP I CG  1 
ATOM   15243 O  OD1 A ASP I  1 170 ? 31.768  44.021  17.479 0.50 76.05  ? 161 ASP I OD1 1 
ATOM   15244 O  OD1 B ASP I  1 170 ? 33.591  40.436  20.220 0.50 79.15  ? 161 ASP I OD1 1 
ATOM   15245 O  OD2 A ASP I  1 170 ? 33.927  43.774  17.708 0.50 72.72  ? 161 ASP I OD2 1 
ATOM   15246 O  OD2 B ASP I  1 170 ? 34.727  41.012  18.444 0.50 86.79  ? 161 ASP I OD2 1 
ATOM   15247 N  N   . GLN I  1 171 ? 29.154  42.523  17.659 1.00 76.69  ? 162 GLN I N   1 
ATOM   15248 C  CA  . GLN I  1 171 ? 28.112  43.530  17.518 1.00 79.47  ? 162 GLN I CA  1 
ATOM   15249 C  C   . GLN I  1 171 ? 26.706  43.002  17.801 1.00 75.23  ? 162 GLN I C   1 
ATOM   15250 O  O   . GLN I  1 171 ? 26.289  41.953  17.297 1.00 73.54  ? 162 GLN I O   1 
ATOM   15251 C  CB  . GLN I  1 171 ? 28.174  44.200  16.140 1.00 74.69  ? 162 GLN I CB  1 
ATOM   15252 C  CG  . GLN I  1 171 ? 27.123  45.300  15.941 1.00 76.77  ? 162 GLN I CG  1 
ATOM   15253 C  CD  . GLN I  1 171 ? 27.486  46.623  16.612 1.00 77.66  ? 162 GLN I CD  1 
ATOM   15254 O  OE1 . GLN I  1 171 ? 28.665  46.983  16.704 1.00 79.26  ? 162 GLN I OE1 1 
ATOM   15255 N  NE2 . GLN I  1 171 ? 26.467  47.358  17.080 1.00 67.03  ? 162 GLN I NE2 1 
ATOM   15256 N  N   . VAL I  1 172 ? 25.981  43.760  18.614 1.00 70.71  ? 163 VAL I N   1 
ATOM   15257 C  CA  . VAL I  1 172 ? 24.623  43.401  18.991 1.00 71.50  ? 163 VAL I CA  1 
ATOM   15258 C  C   . VAL I  1 172 ? 23.648  43.751  17.871 1.00 65.86  ? 163 VAL I C   1 
ATOM   15259 O  O   . VAL I  1 172 ? 23.696  44.841  17.315 1.00 66.79  ? 163 VAL I O   1 
ATOM   15260 C  CB  . VAL I  1 172 ? 24.200  44.104  20.302 1.00 61.88  ? 163 VAL I CB  1 
ATOM   15261 C  CG1 . VAL I  1 172 ? 22.758  43.774  20.648 1.00 61.74  ? 163 VAL I CG1 1 
ATOM   15262 C  CG2 . VAL I  1 172 ? 25.123  43.710  21.429 1.00 57.53  ? 163 VAL I CG2 1 
ATOM   15263 N  N   . ASP I  1 173 ? 22.750  42.830  17.555 1.00 63.84  ? 164 ASP I N   1 
ATOM   15264 C  CA  . ASP I  1 173 ? 21.793  43.067  16.498 1.00 63.22  ? 164 ASP I CA  1 
ATOM   15265 C  C   . ASP I  1 173 ? 20.809  44.127  16.995 1.00 65.76  ? 164 ASP I C   1 
ATOM   15266 O  O   . ASP I  1 173 ? 20.110  43.940  17.999 1.00 60.50  ? 164 ASP I O   1 
ATOM   15267 C  CB  . ASP I  1 173 ? 21.085  41.736  16.215 1.00 60.08  ? 164 ASP I CB  1 
ATOM   15268 C  CG  . ASP I  1 173 ? 20.084  41.812  15.085 1.00 70.12  ? 164 ASP I CG  1 
ATOM   15269 O  OD1 . ASP I  1 173 ? 19.987  42.869  14.421 1.00 73.42  ? 164 ASP I OD1 1 
ATOM   15270 O  OD2 . ASP I  1 173 ? 19.393  40.791  14.862 1.00 72.70  ? 164 ASP I OD2 1 
ATOM   15271 N  N   . LEU I  1 174 ? 20.784  45.256  16.287 1.00 64.10  ? 165 LEU I N   1 
ATOM   15272 C  CA  . LEU I  1 174 ? 19.834  46.329  16.562 1.00 64.60  ? 165 LEU I CA  1 
ATOM   15273 C  C   . LEU I  1 174 ? 18.662  46.360  15.604 1.00 61.35  ? 165 LEU I C   1 
ATOM   15274 O  O   . LEU I  1 174 ? 17.764  47.187  15.753 1.00 54.44  ? 165 LEU I O   1 
ATOM   15275 C  CB  . LEU I  1 174 ? 20.540  47.685  16.614 1.00 56.29  ? 165 LEU I CB  1 
ATOM   15276 C  CG  . LEU I  1 174 ? 21.612  47.726  17.701 1.00 59.97  ? 165 LEU I CG  1 
ATOM   15277 C  CD1 . LEU I  1 174 ? 22.298  49.071  17.746 1.00 57.86  ? 165 LEU I CD1 1 
ATOM   15278 C  CD2 . LEU I  1 174 ? 20.975  47.410  19.033 1.00 64.11  ? 165 LEU I CD2 1 
ATOM   15279 N  N   . SER I  1 175 ? 18.679  45.461  14.625 1.00 60.50  ? 166 SER I N   1 
ATOM   15280 C  CA  . SER I  1 175 ? 17.765  45.567  13.490 1.00 62.24  ? 166 SER I CA  1 
ATOM   15281 C  C   . SER I  1 175 ? 16.291  45.586  13.899 1.00 65.85  ? 166 SER I C   1 
ATOM   15282 O  O   . SER I  1 175 ? 15.465  46.220  13.239 1.00 61.33  ? 166 SER I O   1 
ATOM   15283 C  CB  . SER I  1 175 ? 18.037  44.471  12.459 1.00 58.21  ? 166 SER I CB  1 
ATOM   15284 O  OG  . SER I  1 175 ? 18.034  43.187  13.055 1.00 64.41  ? 166 SER I OG  1 
ATOM   15285 N  N   . SER I  1 176 ? 15.966  44.888  14.984 1.00 67.45  ? 167 SER I N   1 
ATOM   15286 C  CA  . SER I  1 176 ? 14.591  44.853  15.480 1.00 64.94  ? 167 SER I CA  1 
ATOM   15287 C  C   . SER I  1 176 ? 14.284  45.846  16.604 1.00 64.80  ? 167 SER I C   1 
ATOM   15288 O  O   . SER I  1 176 ? 13.165  45.875  17.116 1.00 69.45  ? 167 SER I O   1 
ATOM   15289 C  CB  . SER I  1 176 ? 14.215  43.440  15.911 1.00 64.75  ? 167 SER I CB  1 
ATOM   15290 O  OG  . SER I  1 176 ? 14.154  42.580  14.794 1.00 67.73  ? 167 SER I OG  1 
ATOM   15291 N  N   . TYR I  1 177 ? 15.261  46.654  16.994 1.00 59.21  ? 168 TYR I N   1 
ATOM   15292 C  CA  . TYR I  1 177 ? 15.019  47.614  18.061 1.00 56.69  ? 168 TYR I CA  1 
ATOM   15293 C  C   . TYR I  1 177 ? 13.825  48.532  17.777 1.00 60.01  ? 168 TYR I C   1 
ATOM   15294 O  O   . TYR I  1 177 ? 13.643  49.008  16.662 1.00 61.87  ? 168 TYR I O   1 
ATOM   15295 C  CB  . TYR I  1 177 ? 16.260  48.437  18.362 1.00 52.94  ? 168 TYR I CB  1 
ATOM   15296 C  CG  . TYR I  1 177 ? 16.125  49.170  19.662 1.00 55.49  ? 168 TYR I CG  1 
ATOM   15297 C  CD1 . TYR I  1 177 ? 16.688  48.665  20.826 1.00 58.63  ? 168 TYR I CD1 1 
ATOM   15298 C  CD2 . TYR I  1 177 ? 15.405  50.350  19.739 1.00 58.97  ? 168 TYR I CD2 1 
ATOM   15299 C  CE1 . TYR I  1 177 ? 16.551  49.325  22.036 1.00 55.30  ? 168 TYR I CE1 1 
ATOM   15300 C  CE2 . TYR I  1 177 ? 15.265  51.022  20.941 1.00 63.82  ? 168 TYR I CE2 1 
ATOM   15301 C  CZ  . TYR I  1 177 ? 15.841  50.503  22.088 1.00 61.99  ? 168 TYR I CZ  1 
ATOM   15302 O  OH  . TYR I  1 177 ? 15.703  51.163  23.282 1.00 55.44  ? 168 TYR I OH  1 
ATOM   15303 N  N   . TYR I  1 178 ? 13.011  48.777  18.800 1.00 64.14  ? 169 TYR I N   1 
ATOM   15304 C  CA  . TYR I  1 178 ? 11.769  49.537  18.644 1.00 61.53  ? 169 TYR I CA  1 
ATOM   15305 C  C   . TYR I  1 178 ? 12.028  51.024  18.396 1.00 63.97  ? 169 TYR I C   1 
ATOM   15306 O  O   . TYR I  1 178 ? 12.651  51.723  19.200 1.00 60.66  ? 169 TYR I O   1 
ATOM   15307 C  CB  . TYR I  1 178 ? 10.878  49.318  19.872 1.00 60.48  ? 169 TYR I CB  1 
ATOM   15308 C  CG  . TYR I  1 178 ? 9.592   50.102  19.910 1.00 53.67  ? 169 TYR I CG  1 
ATOM   15309 C  CD1 . TYR I  1 178 ? 8.654   49.993  18.904 1.00 58.15  ? 169 TYR I CD1 1 
ATOM   15310 C  CD2 . TYR I  1 178 ? 9.303   50.921  20.978 1.00 56.37  ? 169 TYR I CD2 1 
ATOM   15311 C  CE1 . TYR I  1 178 ? 7.469   50.698  18.953 1.00 58.16  ? 169 TYR I CE1 1 
ATOM   15312 C  CE2 . TYR I  1 178 ? 8.133   51.628  21.038 1.00 58.51  ? 169 TYR I CE2 1 
ATOM   15313 C  CZ  . TYR I  1 178 ? 7.215   51.514  20.029 1.00 61.59  ? 169 TYR I CZ  1 
ATOM   15314 O  OH  . TYR I  1 178 ? 6.044   52.229  20.099 1.00 62.73  ? 169 TYR I OH  1 
ATOM   15315 N  N   . ALA I  1 179 ? 11.508  51.499  17.274 1.00 68.85  ? 170 ALA I N   1 
ATOM   15316 C  CA  . ALA I  1 179 ? 11.788  52.840  16.789 1.00 66.77  ? 170 ALA I CA  1 
ATOM   15317 C  C   . ALA I  1 179 ? 11.281  53.934  17.736 1.00 70.33  ? 170 ALA I C   1 
ATOM   15318 O  O   . ALA I  1 179 ? 11.912  54.978  17.901 1.00 75.54  ? 170 ALA I O   1 
ATOM   15319 C  CB  . ALA I  1 179 ? 11.174  53.003  15.414 1.00 66.36  ? 170 ALA I CB  1 
ATOM   15320 N  N   . SER I  1 180 ? 10.131  53.682  18.345 1.00 72.04  ? 171 SER I N   1 
ATOM   15321 C  CA  . SER I  1 180 ? 9.448   54.640  19.205 1.00 65.59  ? 171 SER I CA  1 
ATOM   15322 C  C   . SER I  1 180 ? 9.800   54.478  20.673 1.00 65.69  ? 171 SER I C   1 
ATOM   15323 O  O   . SER I  1 180 ? 9.127   55.036  21.537 1.00 69.78  ? 171 SER I O   1 
ATOM   15324 C  CB  . SER I  1 180 ? 7.937   54.638  18.981 1.00 71.00  ? 171 SER I CB  1 
ATOM   15325 O  OG  . SER I  1 180 ? 7.627   55.128  17.681 1.00 68.96  ? 171 SER I OG  1 
ATOM   15326 N  N   . SER I  1 181 ? 10.789  53.638  20.960 1.00 65.77  ? 172 SER I N   1 
ATOM   15327 C  CA  . SER I  1 181 ? 11.287  53.502  22.329 1.00 68.84  ? 172 SER I CA  1 
ATOM   15328 C  C   . SER I  1 181 ? 11.688  54.838  22.948 1.00 64.78  ? 172 SER I C   1 
ATOM   15329 O  O   . SER I  1 181 ? 12.275  55.688  22.286 1.00 68.49  ? 172 SER I O   1 
ATOM   15330 C  CB  . SER I  1 181 ? 12.493  52.563  22.376 1.00 68.20  ? 172 SER I CB  1 
ATOM   15331 O  OG  . SER I  1 181 ? 13.043  52.518  23.687 1.00 71.30  ? 172 SER I OG  1 
ATOM   15332 N  N   . LYS I  1 182 ? 11.384  54.997  24.229 1.00 58.10  ? 173 LYS I N   1 
ATOM   15333 C  CA  . LYS I  1 182 ? 11.736  56.197  24.968 1.00 65.89  ? 173 LYS I CA  1 
ATOM   15334 C  C   . LYS I  1 182 ? 13.232  56.480  24.945 1.00 67.10  ? 173 LYS I C   1 
ATOM   15335 O  O   . LYS I  1 182 ? 13.673  57.605  25.221 1.00 63.56  ? 173 LYS I O   1 
ATOM   15336 C  CB  . LYS I  1 182 ? 11.279  56.053  26.410 1.00 69.47  ? 173 LYS I CB  1 
ATOM   15337 C  CG  . LYS I  1 182 ? 9.813   56.276  26.590 1.00 67.97  ? 173 LYS I CG  1 
ATOM   15338 C  CD  . LYS I  1 182 ? 9.578   57.645  27.186 1.00 72.23  ? 173 LYS I CD  1 
ATOM   15339 C  CE  . LYS I  1 182 ? 8.608   58.451  26.354 1.00 69.50  ? 173 LYS I CE  1 
ATOM   15340 N  NZ  . LYS I  1 182 ? 8.111   59.583  27.178 1.00 78.73  ? 173 LYS I NZ  1 
ATOM   15341 N  N   . TYR I  1 183 ? 14.007  55.447  24.639 1.00 60.68  ? 174 TYR I N   1 
ATOM   15342 C  CA  . TYR I  1 183 ? 15.457  55.558  24.617 1.00 65.46  ? 174 TYR I CA  1 
ATOM   15343 C  C   . TYR I  1 183 ? 15.974  54.999  23.304 1.00 62.50  ? 174 TYR I C   1 
ATOM   15344 O  O   . TYR I  1 183 ? 15.456  54.009  22.791 1.00 56.64  ? 174 TYR I O   1 
ATOM   15345 C  CB  . TYR I  1 183 ? 16.098  54.801  25.799 1.00 63.85  ? 174 TYR I CB  1 
ATOM   15346 C  CG  . TYR I  1 183 ? 15.519  55.145  27.153 1.00 63.90  ? 174 TYR I CG  1 
ATOM   15347 C  CD1 . TYR I  1 183 ? 14.331  54.568  27.585 1.00 66.04  ? 174 TYR I CD1 1 
ATOM   15348 C  CD2 . TYR I  1 183 ? 16.154  56.039  28.000 1.00 62.34  ? 174 TYR I CD2 1 
ATOM   15349 C  CE1 . TYR I  1 183 ? 13.787  54.878  28.820 1.00 64.33  ? 174 TYR I CE1 1 
ATOM   15350 C  CE2 . TYR I  1 183 ? 15.619  56.349  29.240 1.00 58.50  ? 174 TYR I CE2 1 
ATOM   15351 C  CZ  . TYR I  1 183 ? 14.435  55.766  29.641 1.00 59.52  ? 174 TYR I CZ  1 
ATOM   15352 O  OH  . TYR I  1 183 ? 13.886  56.067  30.864 1.00 57.56  ? 174 TYR I OH  1 
ATOM   15353 N  N   . GLU I  1 184 ? 17.006  55.630  22.767 1.00 68.74  ? 175 GLU I N   1 
ATOM   15354 C  CA  . GLU I  1 184 ? 17.604  55.165  21.527 1.00 69.66  ? 175 GLU I CA  1 
ATOM   15355 C  C   . GLU I  1 184 ? 18.980  54.642  21.839 1.00 66.38  ? 175 GLU I C   1 
ATOM   15356 O  O   . GLU I  1 184 ? 19.602  55.053  22.825 1.00 63.86  ? 175 GLU I O   1 
ATOM   15357 C  CB  . GLU I  1 184 ? 17.669  56.282  20.486 1.00 73.32  ? 175 GLU I CB  1 
ATOM   15358 C  CG  . GLU I  1 184 ? 18.712  57.343  20.753 1.00 77.76  ? 175 GLU I CG  1 
ATOM   15359 C  CD  . GLU I  1 184 ? 18.420  58.615  19.997 1.00 85.19  ? 175 GLU I CD  1 
ATOM   15360 O  OE1 . GLU I  1 184 ? 17.325  58.693  19.396 1.00 84.18  ? 175 GLU I OE1 1 
ATOM   15361 O  OE2 . GLU I  1 184 ? 19.273  59.529  20.012 1.00 85.01  ? 175 GLU I OE2 1 
ATOM   15362 N  N   . ILE I  1 185 ? 19.438  53.696  21.032 1.00 65.53  ? 176 ILE I N   1 
ATOM   15363 C  CA  . ILE I  1 185 ? 20.713  53.061  21.304 1.00 62.06  ? 176 ILE I CA  1 
ATOM   15364 C  C   . ILE I  1 185 ? 21.784  53.756  20.503 1.00 58.48  ? 176 ILE I C   1 
ATOM   15365 O  O   . ILE I  1 185 ? 21.645  53.921  19.299 1.00 62.20  ? 176 ILE I O   1 
ATOM   15366 C  CB  . ILE I  1 185 ? 20.696  51.571  20.947 1.00 57.86  ? 176 ILE I CB  1 
ATOM   15367 C  CG1 . ILE I  1 185 ? 19.468  50.893  21.552 1.00 50.24  ? 176 ILE I CG1 1 
ATOM   15368 C  CG2 . ILE I  1 185 ? 21.995  50.914  21.381 1.00 59.53  ? 176 ILE I CG2 1 
ATOM   15369 C  CD1 . ILE I  1 185 ? 19.385  51.033  23.035 1.00 56.95  ? 176 ILE I CD1 1 
ATOM   15370 N  N   . LEU I  1 186 ? 22.813  54.234  21.186 1.00 63.92  ? 177 LEU I N   1 
ATOM   15371 C  CA  . LEU I  1 186 ? 23.995  54.763  20.517 1.00 63.95  ? 177 LEU I CA  1 
ATOM   15372 C  C   . LEU I  1 186 ? 24.921  53.629  20.074 1.00 61.16  ? 177 LEU I C   1 
ATOM   15373 O  O   . LEU I  1 186 ? 25.390  53.603  18.940 1.00 57.50  ? 177 LEU I O   1 
ATOM   15374 C  CB  . LEU I  1 186 ? 24.705  55.783  21.411 1.00 62.24  ? 177 LEU I CB  1 
ATOM   15375 C  CG  . LEU I  1 186 ? 23.722  56.850  21.910 1.00 63.68  ? 177 LEU I CG  1 
ATOM   15376 C  CD1 . LEU I  1 186 ? 24.339  57.792  22.943 1.00 70.11  ? 177 LEU I CD1 1 
ATOM   15377 C  CD2 . LEU I  1 186 ? 23.145  57.619  20.738 1.00 59.90  ? 177 LEU I CD2 1 
ATOM   15378 N  N   . SER I  1 187 ? 25.174  52.686  20.971 1.00 63.23  ? 178 SER I N   1 
ATOM   15379 C  CA  . SER I  1 187 ? 25.920  51.490  20.612 1.00 63.67  ? 178 SER I CA  1 
ATOM   15380 C  C   . SER I  1 187 ? 25.553  50.331  21.518 1.00 68.16  ? 178 SER I C   1 
ATOM   15381 O  O   . SER I  1 187 ? 25.196  50.530  22.677 1.00 70.73  ? 178 SER I O   1 
ATOM   15382 C  CB  . SER I  1 187 ? 27.424  51.743  20.702 1.00 63.66  ? 178 SER I CB  1 
ATOM   15383 O  OG  . SER I  1 187 ? 27.961  51.226  21.907 1.00 69.79  ? 178 SER I OG  1 
ATOM   15384 N  N   . ALA I  1 188 ? 25.666  49.119  20.987 1.00 65.02  ? 179 ALA I N   1 
ATOM   15385 C  CA  . ALA I  1 188 ? 25.482  47.905  21.766 1.00 60.44  ? 179 ALA I CA  1 
ATOM   15386 C  C   . ALA I  1 188 ? 26.490  46.882  21.273 1.00 63.40  ? 179 ALA I C   1 
ATOM   15387 O  O   . ALA I  1 188 ? 26.624  46.678  20.073 1.00 70.05  ? 179 ALA I O   1 
ATOM   15388 C  CB  . ALA I  1 188 ? 24.065  47.391  21.612 1.00 59.51  ? 179 ALA I CB  1 
ATOM   15389 N  N   . THR I  1 189 ? 27.205  46.240  22.187 1.00 60.19  ? 180 THR I N   1 
ATOM   15390 C  CA  . THR I  1 189 ? 28.272  45.330  21.796 1.00 65.95  ? 180 THR I CA  1 
ATOM   15391 C  C   . THR I  1 189 ? 28.312  44.062  22.655 1.00 67.46  ? 180 THR I C   1 
ATOM   15392 O  O   . THR I  1 189 ? 28.223  44.150  23.884 1.00 67.92  ? 180 THR I O   1 
ATOM   15393 C  CB  . THR I  1 189 ? 29.626  46.034  21.933 1.00 63.72  ? 180 THR I CB  1 
ATOM   15394 O  OG1 . THR I  1 189 ? 30.083  45.929  23.287 1.00 77.00  ? 180 THR I OG1 1 
ATOM   15395 C  CG2 . THR I  1 189 ? 29.491  47.482  21.603 1.00 63.80  ? 180 THR I CG2 1 
ATOM   15396 N  N   . GLN I  1 190 ? 28.474  42.893  22.028 1.00 60.38  ? 181 GLN I N   1 
ATOM   15397 C  CA  . GLN I  1 190 ? 28.651  41.664  22.800 1.00 62.50  ? 181 GLN I CA  1 
ATOM   15398 C  C   . GLN I  1 190 ? 30.076  41.100  22.738 1.00 68.67  ? 181 GLN I C   1 
ATOM   15399 O  O   . GLN I  1 190 ? 30.488  40.500  21.754 1.00 72.10  ? 181 GLN I O   1 
ATOM   15400 C  CB  . GLN I  1 190 ? 27.629  40.611  22.376 1.00 62.14  ? 181 GLN I CB  1 
ATOM   15401 C  CG  . GLN I  1 190 ? 27.553  40.391  20.887 1.00 74.67  ? 181 GLN I CG  1 
ATOM   15402 C  CD  . GLN I  1 190 ? 26.430  39.460  20.475 1.00 71.62  ? 181 GLN I CD  1 
ATOM   15403 O  OE1 . GLN I  1 190 ? 25.333  39.502  21.029 1.00 69.80  ? 181 GLN I OE1 1 
ATOM   15404 N  NE2 . GLN I  1 190 ? 26.701  38.619  19.489 1.00 75.69  ? 181 GLN I NE2 1 
ATOM   15405 N  N   . THR I  1 191 ? 30.790  41.234  23.850 1.00 72.35  ? 182 THR I N   1 
ATOM   15406 C  CA  . THR I  1 191 ? 32.220  40.956  23.914 1.00 72.32  ? 182 THR I CA  1 
ATOM   15407 C  C   . THR I  1 191 ? 32.459  39.757  24.806 1.00 66.90  ? 182 THR I C   1 
ATOM   15408 O  O   . THR I  1 191 ? 31.799  39.620  25.824 1.00 66.11  ? 182 THR I O   1 
ATOM   15409 C  CB  . THR I  1 191 ? 32.966  42.146  24.551 1.00 70.27  ? 182 THR I CB  1 
ATOM   15410 O  OG1 . THR I  1 191 ? 32.503  43.380  23.976 1.00 62.07  ? 182 THR I OG1 1 
ATOM   15411 C  CG2 . THR I  1 191 ? 34.483  41.995  24.395 1.00 54.72  ? 182 THR I CG2 1 
ATOM   15412 N  N   . ARG I  1 192 ? 33.403  38.896  24.443 1.00 67.98  ? 183 ARG I N   1 
ATOM   15413 C  CA  . ARG I  1 192 ? 33.747  37.766  25.301 1.00 63.34  ? 183 ARG I CA  1 
ATOM   15414 C  C   . ARG I  1 192 ? 35.081  37.942  26.004 1.00 71.17  ? 183 ARG I C   1 
ATOM   15415 O  O   . ARG I  1 192 ? 36.065  38.351  25.396 1.00 79.25  ? 183 ARG I O   1 
ATOM   15416 C  CB  . ARG I  1 192 ? 33.792  36.478  24.497 1.00 69.31  ? 183 ARG I CB  1 
ATOM   15417 C  CG  . ARG I  1 192 ? 34.516  35.354  25.199 1.00 69.20  ? 183 ARG I CG  1 
ATOM   15418 C  CD  . ARG I  1 192 ? 34.409  34.102  24.390 1.00 71.47  ? 183 ARG I CD  1 
ATOM   15419 N  NE  . ARG I  1 192 ? 34.988  32.950  25.061 1.00 78.24  ? 183 ARG I NE  1 
ATOM   15420 C  CZ  . ARG I  1 192 ? 36.287  32.784  25.257 1.00 77.16  ? 183 ARG I CZ  1 
ATOM   15421 N  NH1 . ARG I  1 192 ? 37.141  33.715  24.859 1.00 68.66  ? 183 ARG I NH1 1 
ATOM   15422 N  NH2 . ARG I  1 192 ? 36.724  31.694  25.867 1.00 83.31  ? 183 ARG I NH2 1 
ATOM   15423 N  N   . SER I  1 193 ? 35.116  37.615  27.287 1.00 71.43  ? 184 SER I N   1 
ATOM   15424 C  CA  . SER I  1 193 ? 36.364  37.657  28.030 1.00 78.23  ? 184 SER I CA  1 
ATOM   15425 C  C   . SER I  1 193 ? 36.539  36.406  28.892 1.00 74.51  ? 184 SER I C   1 
ATOM   15426 O  O   . SER I  1 193 ? 35.567  35.770  29.281 1.00 71.92  ? 184 SER I O   1 
ATOM   15427 C  CB  . SER I  1 193 ? 36.430  38.926  28.876 1.00 72.42  ? 184 SER I CB  1 
ATOM   15428 O  OG  . SER I  1 193 ? 35.245  39.080  29.630 1.00 87.84  ? 184 SER I OG  1 
ATOM   15429 N  N   . GLU I  1 194 ? 37.789  36.041  29.152 1.00 78.74  ? 185 GLU I N   1 
ATOM   15430 C  CA  . GLU I  1 194 ? 38.098  34.919  30.028 1.00 83.50  ? 185 GLU I CA  1 
ATOM   15431 C  C   . GLU I  1 194 ? 38.676  35.466  31.321 1.00 94.32  ? 185 GLU I C   1 
ATOM   15432 O  O   . GLU I  1 194 ? 39.544  36.346  31.309 1.00 90.63  ? 185 GLU I O   1 
ATOM   15433 C  CB  . GLU I  1 194 ? 39.071  33.928  29.369 1.00 79.05  ? 185 GLU I CB  1 
ATOM   15434 C  CG  . GLU I  1 194 ? 38.391  32.916  28.444 1.00 85.25  ? 185 GLU I CG  1 
ATOM   15435 C  CD  . GLU I  1 194 ? 39.367  32.136  27.565 1.00 93.26  ? 185 GLU I CD  1 
ATOM   15436 O  OE1 . GLU I  1 194 ? 39.653  32.595  26.433 1.00 95.90  ? 185 GLU I OE1 1 
ATOM   15437 O  OE2 . GLU I  1 194 ? 39.833  31.056  27.994 1.00 88.96  ? 185 GLU I OE2 1 
ATOM   15438 N  N   . ARG I  1 195 ? 38.172  34.951  32.437 1.00 93.50  ? 186 ARG I N   1 
ATOM   15439 C  CA  . ARG I  1 195 ? 38.559  35.437  33.750 1.00 95.82  ? 186 ARG I CA  1 
ATOM   15440 C  C   . ARG I  1 195 ? 39.089  34.264  34.569 1.00 96.21  ? 186 ARG I C   1 
ATOM   15441 O  O   . ARG I  1 195 ? 38.526  33.174  34.524 1.00 97.90  ? 186 ARG I O   1 
ATOM   15442 C  CB  . ARG I  1 195 ? 37.356  36.083  34.440 1.00 94.46  ? 186 ARG I CB  1 
ATOM   15443 C  CG  . ARG I  1 195 ? 37.720  36.907  35.652 1.00 110.10 ? 186 ARG I CG  1 
ATOM   15444 C  CD  . ARG I  1 195 ? 36.808  36.607  36.827 1.00 113.24 ? 186 ARG I CD  1 
ATOM   15445 N  NE  . ARG I  1 195 ? 37.185  37.398  37.993 1.00 112.53 ? 186 ARG I NE  1 
ATOM   15446 C  CZ  . ARG I  1 195 ? 36.971  38.704  38.088 1.00 117.17 ? 186 ARG I CZ  1 
ATOM   15447 N  NH1 . ARG I  1 195 ? 36.385  39.345  37.084 1.00 107.29 ? 186 ARG I NH1 1 
ATOM   15448 N  NH2 . ARG I  1 195 ? 37.341  39.367  39.176 1.00 112.55 ? 186 ARG I NH2 1 
ATOM   15449 N  N   . PHE I  1 196 ? 40.179  34.470  35.301 1.00 98.85  ? 187 PHE I N   1 
ATOM   15450 C  CA  . PHE I  1 196 ? 40.762  33.382  36.082 1.00 101.58 ? 187 PHE I CA  1 
ATOM   15451 C  C   . PHE I  1 196 ? 40.703  33.694  37.580 1.00 106.05 ? 187 PHE I C   1 
ATOM   15452 O  O   . PHE I  1 196 ? 41.293  34.671  38.036 1.00 111.73 ? 187 PHE I O   1 
ATOM   15453 C  CB  . PHE I  1 196 ? 42.206  33.095  35.634 1.00 96.98  ? 187 PHE I CB  1 
ATOM   15454 C  CG  . PHE I  1 196 ? 42.346  32.767  34.160 1.00 97.82  ? 187 PHE I CG  1 
ATOM   15455 C  CD1 . PHE I  1 196 ? 42.486  31.455  33.735 1.00 95.83  ? 187 PHE I CD1 1 
ATOM   15456 C  CD2 . PHE I  1 196 ? 42.348  33.775  33.198 1.00 99.63  ? 187 PHE I CD2 1 
ATOM   15457 C  CE1 . PHE I  1 196 ? 42.617  31.155  32.379 1.00 90.83  ? 187 PHE I CE1 1 
ATOM   15458 C  CE2 . PHE I  1 196 ? 42.481  33.478  31.840 1.00 85.62  ? 187 PHE I CE2 1 
ATOM   15459 C  CZ  . PHE I  1 196 ? 42.616  32.171  31.436 1.00 86.46  ? 187 PHE I CZ  1 
ATOM   15460 N  N   . TYR I  1 197 ? 39.965  32.882  38.335 1.00 102.03 ? 188 TYR I N   1 
ATOM   15461 C  CA  . TYR I  1 197 ? 39.936  33.000  39.789 1.00 104.07 ? 188 TYR I CA  1 
ATOM   15462 C  C   . TYR I  1 197 ? 41.139  32.222  40.315 1.00 118.31 ? 188 TYR I C   1 
ATOM   15463 O  O   . TYR I  1 197 ? 41.423  31.131  39.821 1.00 124.76 ? 188 TYR I O   1 
ATOM   15464 C  CB  . TYR I  1 197 ? 38.641  32.414  40.366 1.00 99.25  ? 188 TYR I CB  1 
ATOM   15465 C  CG  . TYR I  1 197 ? 37.362  33.072  39.888 1.00 97.11  ? 188 TYR I CG  1 
ATOM   15466 C  CD1 . TYR I  1 197 ? 37.015  34.351  40.297 1.00 101.02 ? 188 TYR I CD1 1 
ATOM   15467 C  CD2 . TYR I  1 197 ? 36.491  32.405  39.045 1.00 105.81 ? 188 TYR I CD2 1 
ATOM   15468 C  CE1 . TYR I  1 197 ? 35.845  34.950  39.867 1.00 99.85  ? 188 TYR I CE1 1 
ATOM   15469 C  CE2 . TYR I  1 197 ? 35.319  33.000  38.607 1.00 103.87 ? 188 TYR I CE2 1 
ATOM   15470 C  CZ  . TYR I  1 197 ? 35.003  34.267  39.025 1.00 101.97 ? 188 TYR I CZ  1 
ATOM   15471 O  OH  . TYR I  1 197 ? 33.841  34.854  38.594 1.00 103.51 ? 188 TYR I OH  1 
ATOM   15472 N  N   . GLU I  1 198 ? 41.852  32.765  41.302 1.00 117.61 ? 189 GLU I N   1 
ATOM   15473 C  CA  . GLU I  1 198 ? 43.114  32.155  41.735 1.00 115.34 ? 189 GLU I CA  1 
ATOM   15474 C  C   . GLU I  1 198 ? 42.949  30.790  42.421 1.00 114.49 ? 189 GLU I C   1 
ATOM   15475 O  O   . GLU I  1 198 ? 43.888  29.993  42.467 1.00 111.59 ? 189 GLU I O   1 
ATOM   15476 C  CB  . GLU I  1 198 ? 43.926  33.123  42.602 1.00 110.26 ? 189 GLU I CB  1 
ATOM   15477 C  CG  . GLU I  1 198 ? 45.390  33.258  42.171 1.00 118.04 ? 189 GLU I CG  1 
ATOM   15478 C  CD  . GLU I  1 198 ? 45.551  33.730  40.725 1.00 122.44 ? 189 GLU I CD  1 
ATOM   15479 O  OE1 . GLU I  1 198 ? 46.656  33.567  40.159 1.00 118.83 ? 189 GLU I OE1 1 
ATOM   15480 O  OE2 . GLU I  1 198 ? 44.577  34.270  40.155 1.00 112.74 ? 189 GLU I OE2 1 
ATOM   15481 N  N   . CYS I  1 199 ? 41.753  30.518  42.931 1.00 109.89 ? 190 CYS I N   1 
ATOM   15482 C  CA  . CYS I  1 199 ? 41.477  29.243  43.584 1.00 110.09 ? 190 CYS I CA  1 
ATOM   15483 C  C   . CYS I  1 199 ? 41.711  28.043  42.655 1.00 113.20 ? 190 CYS I C   1 
ATOM   15484 O  O   . CYS I  1 199 ? 42.227  27.009  43.079 1.00 104.86 ? 190 CYS I O   1 
ATOM   15485 C  CB  . CYS I  1 199 ? 40.039  29.221  44.112 1.00 109.45 ? 190 CYS I CB  1 
ATOM   15486 S  SG  . CYS I  1 199 ? 38.846  28.441  42.991 1.00 136.06 ? 190 CYS I SG  1 
ATOM   15487 N  N   . CYS I  1 200 ? 41.337  28.195  41.384 1.00 126.07 ? 191 CYS I N   1 
ATOM   15488 C  CA  . CYS I  1 200 ? 41.327  27.090  40.420 1.00 114.63 ? 191 CYS I CA  1 
ATOM   15489 C  C   . CYS I  1 200 ? 41.973  27.493  39.090 1.00 107.29 ? 191 CYS I C   1 
ATOM   15490 O  O   . CYS I  1 200 ? 41.884  28.650  38.678 1.00 100.98 ? 191 CYS I O   1 
ATOM   15491 C  CB  . CYS I  1 200 ? 39.886  26.625  40.181 1.00 105.20 ? 191 CYS I CB  1 
ATOM   15492 S  SG  . CYS I  1 200 ? 38.762  26.956  41.583 1.00 138.92 ? 191 CYS I SG  1 
ATOM   15493 N  N   . LYS I  1 201 ? 42.618  26.533  38.427 1.00 112.39 ? 192 LYS I N   1 
ATOM   15494 C  CA  . LYS I  1 201 ? 43.302  26.777  37.149 1.00 107.73 ? 192 LYS I CA  1 
ATOM   15495 C  C   . LYS I  1 201 ? 42.335  27.113  36.019 1.00 102.41 ? 192 LYS I C   1 
ATOM   15496 O  O   . LYS I  1 201 ? 42.637  27.944  35.162 1.00 96.78  ? 192 LYS I O   1 
ATOM   15497 C  CB  . LYS I  1 201 ? 44.140  25.565  36.740 1.00 97.83  ? 192 LYS I CB  1 
ATOM   15498 C  CG  . LYS I  1 201 ? 45.344  25.306  37.629 1.00 113.01 ? 192 LYS I CG  1 
ATOM   15499 C  CD  . LYS I  1 201 ? 46.284  26.500  37.653 1.00 106.88 ? 192 LYS I CD  1 
ATOM   15500 C  CE  . LYS I  1 201 ? 47.504  26.230  38.521 1.00 107.00 ? 192 LYS I CE  1 
ATOM   15501 N  NZ  . LYS I  1 201 ? 48.493  27.342  38.418 1.00 102.08 ? 192 LYS I NZ  1 
ATOM   15502 N  N   . GLU I  1 202 ? 41.179  26.450  36.040 1.00 107.26 ? 193 GLU I N   1 
ATOM   15503 C  CA  . GLU I  1 202 ? 40.144  26.547  35.003 1.00 102.45 ? 193 GLU I CA  1 
ATOM   15504 C  C   . GLU I  1 202 ? 39.635  27.959  34.734 1.00 96.87  ? 193 GLU I C   1 
ATOM   15505 O  O   . GLU I  1 202 ? 39.279  28.674  35.669 1.00 97.87  ? 193 GLU I O   1 
ATOM   15506 C  CB  . GLU I  1 202 ? 38.953  25.667  35.389 1.00 93.37  ? 193 GLU I CB  1 
ATOM   15507 C  CG  . GLU I  1 202 ? 37.812  25.709  34.398 1.00 94.78  ? 193 GLU I CG  1 
ATOM   15508 C  CD  . GLU I  1 202 ? 36.747  24.681  34.706 1.00 97.92  ? 193 GLU I CD  1 
ATOM   15509 O  OE1 . GLU I  1 202 ? 36.536  24.397  35.914 1.00 91.45  ? 193 GLU I OE1 1 
ATOM   15510 O  OE2 . GLU I  1 202 ? 36.132  24.162  33.739 1.00 89.28  ? 193 GLU I OE2 1 
ATOM   15511 N  N   . PRO I  1 203 ? 39.581  28.347  33.446 1.00 88.75  ? 194 PRO I N   1 
ATOM   15512 C  CA  . PRO I  1 203 ? 39.033  29.622  32.964 1.00 90.33  ? 194 PRO I CA  1 
ATOM   15513 C  C   . PRO I  1 203 ? 37.522  29.690  33.155 1.00 87.77  ? 194 PRO I C   1 
ATOM   15514 O  O   . PRO I  1 203 ? 36.847  28.670  33.011 1.00 83.76  ? 194 PRO I O   1 
ATOM   15515 C  CB  . PRO I  1 203 ? 39.346  29.601  31.461 1.00 86.08  ? 194 PRO I CB  1 
ATOM   15516 C  CG  . PRO I  1 203 ? 40.369  28.540  31.278 1.00 97.91  ? 194 PRO I CG  1 
ATOM   15517 C  CD  . PRO I  1 203 ? 40.109  27.528  32.346 1.00 93.53  ? 194 PRO I CD  1 
ATOM   15518 N  N   . TYR I  1 204 ? 37.007  30.864  33.513 1.00 86.54  ? 195 TYR I N   1 
ATOM   15519 C  CA  . TYR I  1 204 ? 35.566  31.096  33.532 1.00 80.69  ? 195 TYR I CA  1 
ATOM   15520 C  C   . TYR I  1 204 ? 35.162  32.169  32.509 1.00 74.64  ? 195 TYR I C   1 
ATOM   15521 O  O   . TYR I  1 204 ? 35.408  33.354  32.722 1.00 69.00  ? 195 TYR I O   1 
ATOM   15522 C  CB  . TYR I  1 204 ? 35.125  31.460  34.958 1.00 81.68  ? 195 TYR I CB  1 
ATOM   15523 C  CG  . TYR I  1 204 ? 35.267  30.296  35.911 1.00 79.19  ? 195 TYR I CG  1 
ATOM   15524 C  CD1 . TYR I  1 204 ? 34.167  29.537  36.278 1.00 81.15  ? 195 TYR I CD1 1 
ATOM   15525 C  CD2 . TYR I  1 204 ? 36.507  29.925  36.400 1.00 84.70  ? 195 TYR I CD2 1 
ATOM   15526 C  CE1 . TYR I  1 204 ? 34.293  28.451  37.125 1.00 85.53  ? 195 TYR I CE1 1 
ATOM   15527 C  CE2 . TYR I  1 204 ? 36.645  28.833  37.251 1.00 92.92  ? 195 TYR I CE2 1 
ATOM   15528 C  CZ  . TYR I  1 204 ? 35.533  28.102  37.609 1.00 86.77  ? 195 TYR I CZ  1 
ATOM   15529 O  OH  . TYR I  1 204 ? 35.660  27.021  38.452 1.00 78.88  ? 195 TYR I OH  1 
ATOM   15530 N  N   . PRO I  1 205 ? 34.540  31.760  31.386 1.00 72.32  ? 196 PRO I N   1 
ATOM   15531 C  CA  . PRO I  1 205 ? 34.266  32.853  30.458 1.00 71.71  ? 196 PRO I CA  1 
ATOM   15532 C  C   . PRO I  1 205 ? 32.904  33.474  30.666 1.00 65.99  ? 196 PRO I C   1 
ATOM   15533 O  O   . PRO I  1 205 ? 32.071  32.919  31.383 1.00 68.05  ? 196 PRO I O   1 
ATOM   15534 C  CB  . PRO I  1 205 ? 34.269  32.142  29.110 1.00 71.87  ? 196 PRO I CB  1 
ATOM   15535 C  CG  . PRO I  1 205 ? 33.723  30.802  29.432 1.00 66.98  ? 196 PRO I CG  1 
ATOM   15536 C  CD  . PRO I  1 205 ? 34.293  30.446  30.772 1.00 67.95  ? 196 PRO I CD  1 
ATOM   15537 N  N   . ASP I  1 206 ? 32.667  34.563  29.943 1.00 64.33  ? 197 ASP I N   1 
ATOM   15538 C  CA  . ASP I  1 206 ? 31.417  35.305  29.991 1.00 63.43  ? 197 ASP I CA  1 
ATOM   15539 C  C   . ASP I  1 206 ? 31.274  36.148  28.743 1.00 65.10  ? 197 ASP I C   1 
ATOM   15540 O  O   . ASP I  1 206 ? 32.246  36.417  28.043 1.00 67.35  ? 197 ASP I O   1 
ATOM   15541 C  CB  . ASP I  1 206 ? 31.337  36.212  31.223 1.00 64.77  ? 197 ASP I CB  1 
ATOM   15542 C  CG  . ASP I  1 206 ? 32.348  37.359  31.189 1.00 76.19  ? 197 ASP I CG  1 
ATOM   15543 O  OD1 . ASP I  1 206 ? 33.369  37.257  31.905 1.00 79.16  ? 197 ASP I OD1 1 
ATOM   15544 O  OD2 . ASP I  1 206 ? 32.118  38.367  30.470 1.00 69.35  ? 197 ASP I OD2 1 
ATOM   15545 N  N   . VAL I  1 207 ? 30.053  36.576  28.477 1.00 59.90  ? 198 VAL I N   1 
ATOM   15546 C  CA  . VAL I  1 207 ? 29.813  37.513  27.412 1.00 56.37  ? 198 VAL I CA  1 
ATOM   15547 C  C   . VAL I  1 207 ? 29.305  38.826  28.002 1.00 64.04  ? 198 VAL I C   1 
ATOM   15548 O  O   . VAL I  1 207 ? 28.275  38.857  28.674 1.00 64.44  ? 198 VAL I O   1 
ATOM   15549 C  CB  . VAL I  1 207 ? 28.812  36.945  26.445 1.00 51.72  ? 198 VAL I CB  1 
ATOM   15550 C  CG1 . VAL I  1 207 ? 28.429  37.989  25.429 1.00 59.38  ? 198 VAL I CG1 1 
ATOM   15551 C  CG2 . VAL I  1 207 ? 29.406  35.740  25.776 1.00 59.10  ? 198 VAL I CG2 1 
ATOM   15552 N  N   . ASN I  1 208 ? 30.039  39.909  27.772 1.00 64.12  ? 199 ASN I N   1 
ATOM   15553 C  CA  . ASN I  1 208 ? 29.665  41.193  28.329 1.00 62.29  ? 199 ASN I CA  1 
ATOM   15554 C  C   . ASN I  1 208 ? 28.838  41.950  27.298 1.00 60.83  ? 199 ASN I C   1 
ATOM   15555 O  O   . ASN I  1 208 ? 29.284  42.187  26.182 1.00 65.82  ? 199 ASN I O   1 
ATOM   15556 C  CB  . ASN I  1 208 ? 30.913  41.968  28.791 1.00 67.72  ? 199 ASN I CB  1 
ATOM   15557 C  CG  . ASN I  1 208 ? 30.573  43.246  29.561 1.00 68.36  ? 199 ASN I CG  1 
ATOM   15558 O  OD1 . ASN I  1 208 ? 29.417  43.503  29.880 1.00 65.92  ? 199 ASN I OD1 1 
ATOM   15559 N  ND2 . ASN I  1 208 ? 31.590  44.046  29.865 1.00 70.50  ? 199 ASN I ND2 1 
ATOM   15560 N  N   . LEU I  1 209 ? 27.610  42.286  27.670 1.00 56.71  ? 200 LEU I N   1 
ATOM   15561 C  CA  . LEU I  1 209 ? 26.730  43.036  26.801 1.00 54.03  ? 200 LEU I CA  1 
ATOM   15562 C  C   . LEU I  1 209 ? 26.778  44.451  27.295 1.00 63.36  ? 200 LEU I C   1 
ATOM   15563 O  O   . LEU I  1 209 ? 26.300  44.740  28.392 1.00 60.83  ? 200 LEU I O   1 
ATOM   15564 C  CB  . LEU I  1 209 ? 25.303  42.520  26.920 1.00 56.22  ? 200 LEU I CB  1 
ATOM   15565 C  CG  . LEU I  1 209 ? 24.205  43.344  26.243 1.00 60.82  ? 200 LEU I CG  1 
ATOM   15566 C  CD1 . LEU I  1 209 ? 24.353  43.255  24.746 1.00 66.72  ? 200 LEU I CD1 1 
ATOM   15567 C  CD2 . LEU I  1 209 ? 22.818  42.874  26.638 1.00 55.28  ? 200 LEU I CD2 1 
ATOM   15568 N  N   . VAL I  1 210 ? 27.377  45.333  26.497 1.00 69.78  ? 201 VAL I N   1 
ATOM   15569 C  CA  . VAL I  1 210 ? 27.526  46.741  26.874 1.00 65.69  ? 201 VAL I CA  1 
ATOM   15570 C  C   . VAL I  1 210 ? 26.648  47.599  25.978 1.00 54.83  ? 201 VAL I C   1 
ATOM   15571 O  O   . VAL I  1 210 ? 26.607  47.404  24.774 1.00 61.54  ? 201 VAL I O   1 
ATOM   15572 C  CB  . VAL I  1 210 ? 28.997  47.213  26.820 1.00 58.89  ? 201 VAL I CB  1 
ATOM   15573 C  CG1 . VAL I  1 210 ? 29.099  48.625  27.323 1.00 53.34  ? 201 VAL I CG1 1 
ATOM   15574 C  CG2 . VAL I  1 210 ? 29.886  46.295  27.653 1.00 58.14  ? 201 VAL I CG2 1 
ATOM   15575 N  N   . VAL I  1 211 ? 25.917  48.523  26.579 1.00 51.61  ? 202 VAL I N   1 
ATOM   15576 C  CA  . VAL I  1 211 ? 24.913  49.284  25.860 1.00 55.45  ? 202 VAL I CA  1 
ATOM   15577 C  C   . VAL I  1 211 ? 24.940  50.772  26.202 1.00 64.21  ? 202 VAL I C   1 
ATOM   15578 O  O   . VAL I  1 211 ? 24.739  51.143  27.349 1.00 68.10  ? 202 VAL I O   1 
ATOM   15579 C  CB  . VAL I  1 211 ? 23.529  48.743  26.187 1.00 49.62  ? 202 VAL I CB  1 
ATOM   15580 C  CG1 . VAL I  1 211 ? 22.470  49.554  25.490 1.00 55.29  ? 202 VAL I CG1 1 
ATOM   15581 C  CG2 . VAL I  1 211 ? 23.446  47.282  25.784 1.00 55.72  ? 202 VAL I CG2 1 
ATOM   15582 N  N   . LYS I  1 212 ? 25.170  51.632  25.214 1.00 68.00  ? 203 LYS I N   1 
ATOM   15583 C  CA  . LYS I  1 212 ? 25.063  53.071  25.451 1.00 64.51  ? 203 LYS I CA  1 
ATOM   15584 C  C   . LYS I  1 212 ? 23.738  53.581  24.894 1.00 62.02  ? 203 LYS I C   1 
ATOM   15585 O  O   . LYS I  1 212 ? 23.326  53.183  23.814 1.00 70.28  ? 203 LYS I O   1 
ATOM   15586 C  CB  . LYS I  1 212 ? 26.250  53.812  24.835 1.00 69.71  ? 203 LYS I CB  1 
ATOM   15587 C  CG  . LYS I  1 212 ? 27.597  53.153  25.115 1.00 78.47  ? 203 LYS I CG  1 
ATOM   15588 C  CD  . LYS I  1 212 ? 28.705  54.184  25.309 1.00 85.51  ? 203 LYS I CD  1 
ATOM   15589 C  CE  . LYS I  1 212 ? 30.052  53.507  25.525 1.00 90.22  ? 203 LYS I CE  1 
ATOM   15590 N  NZ  . LYS I  1 212 ? 31.172  54.490  25.511 1.00 97.27  ? 203 LYS I NZ  1 
ATOM   15591 N  N   . PHE I  1 213 ? 23.058  54.447  25.627 1.00 62.91  ? 204 PHE I N   1 
ATOM   15592 C  CA  . PHE I  1 213 ? 21.724  54.881  25.222 1.00 63.70  ? 204 PHE I CA  1 
ATOM   15593 C  C   . PHE I  1 213 ? 21.363  56.252  25.800 1.00 70.67  ? 204 PHE I C   1 
ATOM   15594 O  O   . PHE I  1 213 ? 22.029  56.758  26.711 1.00 69.32  ? 204 PHE I O   1 
ATOM   15595 C  CB  . PHE I  1 213 ? 20.684  53.840  25.638 1.00 58.59  ? 204 PHE I CB  1 
ATOM   15596 C  CG  . PHE I  1 213 ? 20.697  53.527  27.106 1.00 56.57  ? 204 PHE I CG  1 
ATOM   15597 C  CD1 . PHE I  1 213 ? 19.636  53.903  27.921 1.00 63.19  ? 204 PHE I CD1 1 
ATOM   15598 C  CD2 . PHE I  1 213 ? 21.778  52.873  27.680 1.00 53.49  ? 204 PHE I CD2 1 
ATOM   15599 C  CE1 . PHE I  1 213 ? 19.648  53.616  29.285 1.00 62.93  ? 204 PHE I CE1 1 
ATOM   15600 C  CE2 . PHE I  1 213 ? 21.800  52.591  29.041 1.00 59.56  ? 204 PHE I CE2 1 
ATOM   15601 C  CZ  . PHE I  1 213 ? 20.732  52.959  29.842 1.00 56.59  ? 204 PHE I CZ  1 
ATOM   15602 N  N   . ARG I  1 214 ? 20.320  56.866  25.257 1.00 68.45  ? 205 ARG I N   1 
ATOM   15603 C  CA  . ARG I  1 214 ? 19.855  58.128  25.800 1.00 68.53  ? 205 ARG I CA  1 
ATOM   15604 C  C   . ARG I  1 214 ? 18.396  58.348  25.462 1.00 70.54  ? 205 ARG I C   1 
ATOM   15605 O  O   . ARG I  1 214 ? 17.852  57.682  24.586 1.00 66.75  ? 205 ARG I O   1 
ATOM   15606 C  CB  . ARG I  1 214 ? 20.697  59.277  25.260 1.00 78.00  ? 205 ARG I CB  1 
ATOM   15607 C  CG  . ARG I  1 214 ? 20.429  59.601  23.813 1.00 77.05  ? 205 ARG I CG  1 
ATOM   15608 C  CD  . ARG I  1 214 ? 21.357  60.684  23.343 1.00 86.72  ? 205 ARG I CD  1 
ATOM   15609 N  NE  . ARG I  1 214 ? 21.060  61.101  21.979 1.00 93.15  ? 205 ARG I NE  1 
ATOM   15610 C  CZ  . ARG I  1 214 ? 21.989  61.472  21.106 1.00 90.99  ? 205 ARG I CZ  1 
ATOM   15611 N  NH1 . ARG I  1 214 ? 23.265  61.469  21.458 1.00 92.29  ? 205 ARG I NH1 1 
ATOM   15612 N  NH2 . ARG I  1 214 ? 21.648  61.843  19.884 1.00 86.03  ? 205 ARG I NH2 1 
ATOM   15613 N  N   . GLU I  1 215 ? 17.767  59.278  26.174 1.00 74.74  ? 206 GLU I N   1 
ATOM   15614 C  CA  . GLU I  1 215 ? 16.382  59.647  25.909 1.00 76.13  ? 206 GLU I CA  1 
ATOM   15615 C  C   . GLU I  1 215 ? 16.228  60.070  24.464 1.00 78.94  ? 206 GLU I C   1 
ATOM   15616 O  O   . GLU I  1 215 ? 17.104  60.741  23.915 1.00 87.65  ? 206 GLU I O   1 
ATOM   15617 C  CB  . GLU I  1 215 ? 15.955  60.797  26.816 1.00 78.37  ? 206 GLU I CB  1 
ATOM   15618 C  CG  . GLU I  1 215 ? 15.983  60.474  28.290 1.00 70.13  ? 206 GLU I CG  1 
ATOM   15619 C  CD  . GLU I  1 215 ? 15.790  61.704  29.138 1.00 85.18  ? 206 GLU I CD  1 
ATOM   15620 O  OE1 . GLU I  1 215 ? 15.560  62.791  28.565 1.00 88.44  ? 206 GLU I OE1 1 
ATOM   15621 O  OE2 . GLU I  1 215 ? 15.879  61.589  30.379 1.00 94.35  ? 206 GLU I OE2 1 
ATOM   15622 N  N   . ARG I  1 216 ? 15.114  59.682  23.849 1.00 79.38  ? 207 ARG I N   1 
ATOM   15623 C  CA  . ARG I  1 216 ? 14.857  60.038  22.456 1.00 85.11  ? 207 ARG I CA  1 
ATOM   15624 C  C   . ARG I  1 216 ? 14.164  61.398  22.359 1.00 89.97  ? 207 ARG I C   1 
ATOM   15625 O  O   . ARG I  1 216 ? 13.146  61.634  23.023 1.00 82.81  ? 207 ARG I O   1 
ATOM   15626 C  CB  . ARG I  1 216 ? 14.010  58.958  21.777 1.00 81.84  ? 207 ARG I CB  1 
ATOM   15627 C  CG  . ARG I  1 216 ? 14.104  58.937  20.251 1.00 88.68  ? 207 ARG I CG  1 
ATOM   15628 C  CD  . ARG I  1 216 ? 13.234  57.827  19.666 1.00 85.51  ? 207 ARG I CD  1 
ATOM   15629 N  NE  . ARG I  1 216 ? 11.885  57.841  20.240 1.00 90.53  ? 207 ARG I NE  1 
ATOM   15630 C  CZ  . ARG I  1 216 ? 10.787  58.279  19.617 1.00 88.96  ? 207 ARG I CZ  1 
ATOM   15631 N  NH1 . ARG I  1 216 ? 9.615   58.244  20.242 1.00 81.86  ? 207 ARG I NH1 1 
ATOM   15632 N  NH2 . ARG I  1 216 ? 10.851  58.752  18.375 1.00 78.62  ? 207 ARG I NH2 1 
ATOM   15633 N  N   . ARG I  1 217 ? 14.720  62.288  21.534 1.00 98.57  ? 208 ARG I N   1 
ATOM   15634 C  CA  . ARG I  1 217 ? 14.116  63.606  21.294 1.00 103.95 ? 208 ARG I CA  1 
ATOM   15635 C  C   . ARG I  1 217 ? 13.794  63.815  19.813 1.00 103.97 ? 208 ARG I C   1 
ATOM   15636 O  O   . ARG I  1 217 ? 13.204  62.943  19.163 1.00 100.35 ? 208 ARG I O   1 
ATOM   15637 C  CB  . ARG I  1 217 ? 15.020  64.735  21.808 1.00 101.81 ? 208 ARG I CB  1 
ATOM   15638 C  CG  . ARG I  1 217 ? 15.228  64.741  23.329 1.00 111.76 ? 208 ARG I CG  1 
ATOM   15639 C  CD  . ARG I  1 217 ? 16.291  65.765  23.755 1.00 121.69 ? 208 ARG I CD  1 
ATOM   15640 N  NE  . ARG I  1 217 ? 17.571  65.521  23.086 1.00 124.13 ? 208 ARG I NE  1 
ATOM   15641 C  CZ  . ARG I  1 217 ? 18.555  64.774  23.584 1.00 118.06 ? 208 ARG I CZ  1 
ATOM   15642 N  NH1 . ARG I  1 217 ? 18.430  64.195  24.776 1.00 109.77 ? 208 ARG I NH1 1 
ATOM   15643 N  NH2 . ARG I  1 217 ? 19.672  64.608  22.889 1.00 107.49 ? 208 ARG I NH2 1 
ATOM   15644 N  N   . LYS J  1 3   ? -35.392 4.334   30.789 1.00 105.27 ? -6  LYS J N   1 
ATOM   15645 C  CA  . LYS J  1 3   ? -36.069 5.322   29.960 1.00 106.15 ? -6  LYS J CA  1 
ATOM   15646 C  C   . LYS J  1 3   ? -35.077 6.297   29.309 1.00 112.76 ? -6  LYS J C   1 
ATOM   15647 O  O   . LYS J  1 3   ? -34.095 5.873   28.705 1.00 113.17 ? -6  LYS J O   1 
ATOM   15648 C  CB  . LYS J  1 3   ? -37.148 6.055   30.769 1.00 115.78 ? -6  LYS J CB  1 
ATOM   15649 C  CG  . LYS J  1 3   ? -36.638 6.894   31.941 1.00 118.90 ? -6  LYS J CG  1 
ATOM   15650 C  CD  . LYS J  1 3   ? -37.789 7.604   32.668 1.00 113.95 ? -6  LYS J CD  1 
ATOM   15651 C  CE  . LYS J  1 3   ? -39.018 7.809   31.765 1.00 118.10 ? -6  LYS J CE  1 
ATOM   15652 N  NZ  . LYS J  1 3   ? -38.732 8.502   30.465 1.00 102.31 ? -6  LYS J NZ  1 
ATOM   15653 N  N   . ASP J  1 4   ? -35.339 7.597   29.419 1.00 123.98 ? -5  ASP J N   1 
ATOM   15654 C  CA  . ASP J  1 4   ? -34.432 8.625   28.893 1.00 117.82 ? -5  ASP J CA  1 
ATOM   15655 C  C   . ASP J  1 4   ? -33.126 8.683   29.676 1.00 110.05 ? -5  ASP J C   1 
ATOM   15656 O  O   . ASP J  1 4   ? -32.093 9.079   29.146 1.00 103.55 ? -5  ASP J O   1 
ATOM   15657 C  CB  . ASP J  1 4   ? -35.103 10.003  28.924 1.00 122.20 ? -5  ASP J CB  1 
ATOM   15658 C  CG  . ASP J  1 4   ? -35.522 10.420  30.327 1.00 126.37 ? -5  ASP J CG  1 
ATOM   15659 O  OD1 . ASP J  1 4   ? -35.317 9.629   31.276 1.00 124.16 ? -5  ASP J OD1 1 
ATOM   15660 O  OD2 . ASP J  1 4   ? -36.066 11.537  30.478 1.00 124.98 ? -5  ASP J OD2 1 
ATOM   15661 N  N   . ASP J  1 5   ? -33.189 8.304   30.949 1.00 108.58 ? -4  ASP J N   1 
ATOM   15662 C  CA  . ASP J  1 5   ? -32.025 8.339   31.821 1.00 107.40 ? -4  ASP J CA  1 
ATOM   15663 C  C   . ASP J  1 5   ? -30.955 7.456   31.220 1.00 97.16  ? -4  ASP J C   1 
ATOM   15664 O  O   . ASP J  1 5   ? -29.759 7.666   31.416 1.00 95.49  ? -4  ASP J O   1 
ATOM   15665 C  CB  . ASP J  1 5   ? -32.380 7.838   33.223 1.00 109.56 ? -4  ASP J CB  1 
ATOM   15666 C  CG  . ASP J  1 5   ? -33.392 8.726   33.928 1.00 117.87 ? -4  ASP J CG  1 
ATOM   15667 O  OD1 . ASP J  1 5   ? -33.799 9.753   33.346 1.00 122.76 ? -4  ASP J OD1 1 
ATOM   15668 O  OD2 . ASP J  1 5   ? -33.779 8.402   35.071 1.00 111.02 ? -4  ASP J OD2 1 
ATOM   15669 N  N   . ASP J  1 6   ? -31.411 6.454   30.486 1.00 92.20  ? -3  ASP J N   1 
ATOM   15670 C  CA  . ASP J  1 6   ? -30.530 5.525   29.812 1.00 92.68  ? -3  ASP J CA  1 
ATOM   15671 C  C   . ASP J  1 6   ? -29.793 6.290   28.725 1.00 87.53  ? -3  ASP J C   1 
ATOM   15672 O  O   . ASP J  1 6   ? -28.609 6.060   28.484 1.00 82.07  ? -3  ASP J O   1 
ATOM   15673 C  CB  . ASP J  1 6   ? -31.374 4.406   29.208 1.00 100.15 ? -3  ASP J CB  1 
ATOM   15674 C  CG  . ASP J  1 6   ? -30.561 3.205   28.808 1.00 92.85  ? -3  ASP J CG  1 
ATOM   15675 O  OD1 . ASP J  1 6   ? -29.607 2.843   29.529 1.00 84.11  ? -3  ASP J OD1 1 
ATOM   15676 O  OD2 . ASP J  1 6   ? -30.898 2.618   27.759 1.00 91.45  ? -3  ASP J OD2 1 
ATOM   15677 N  N   . ASP J  1 7   ? -30.506 7.210   28.080 1.00 91.99  ? -2  ASP J N   1 
ATOM   15678 C  CA  . ASP J  1 7   ? -29.928 8.051   27.034 1.00 93.03  ? -2  ASP J CA  1 
ATOM   15679 C  C   . ASP J  1 7   ? -28.810 8.939   27.587 1.00 84.09  ? -2  ASP J C   1 
ATOM   15680 O  O   . ASP J  1 7   ? -27.748 9.064   26.977 1.00 80.07  ? -2  ASP J O   1 
ATOM   15681 C  CB  . ASP J  1 7   ? -31.013 8.907   26.368 1.00 100.96 ? -2  ASP J CB  1 
ATOM   15682 C  CG  . ASP J  1 7   ? -31.552 8.291   25.080 1.00 115.49 ? -2  ASP J CG  1 
ATOM   15683 O  OD1 . ASP J  1 7   ? -31.217 7.123   24.770 1.00 115.05 ? -2  ASP J OD1 1 
ATOM   15684 O  OD2 . ASP J  1 7   ? -32.325 8.982   24.378 1.00 117.26 ? -2  ASP J OD2 1 
ATOM   15685 N  N   . LYS J  1 8   ? -29.055 9.556   28.738 1.00 81.36  ? -1  LYS J N   1 
ATOM   15686 C  CA  . LYS J  1 8   ? -28.047 10.384  29.393 1.00 80.03  ? -1  LYS J CA  1 
ATOM   15687 C  C   . LYS J  1 8   ? -26.771 9.584   29.598 1.00 76.64  ? -1  LYS J C   1 
ATOM   15688 O  O   . LYS J  1 8   ? -25.678 10.047  29.281 1.00 75.43  ? -1  LYS J O   1 
ATOM   15689 C  CB  . LYS J  1 8   ? -28.560 10.887  30.743 1.00 78.85  ? -1  LYS J CB  1 
ATOM   15690 C  CG  . LYS J  1 8   ? -29.495 12.075  30.667 1.00 76.58  ? -1  LYS J CG  1 
ATOM   15691 C  CD  . LYS J  1 8   ? -29.912 12.503  32.058 1.00 84.38  ? -1  LYS J CD  1 
ATOM   15692 C  CE  . LYS J  1 8   ? -30.639 13.840  32.036 1.00 83.62  ? -1  LYS J CE  1 
ATOM   15693 N  NZ  . LYS J  1 8   ? -31.998 13.734  31.460 1.00 76.93  ? -1  LYS J NZ  1 
ATOM   15694 N  N   . LEU J  1 9   ? -26.931 8.369   30.116 1.00 73.13  ? 0   LEU J N   1 
ATOM   15695 C  CA  . LEU J  1 9   ? -25.812 7.491   30.440 1.00 71.23  ? 0   LEU J CA  1 
ATOM   15696 C  C   . LEU J  1 9   ? -25.023 7.057   29.210 1.00 70.21  ? 0   LEU J C   1 
ATOM   15697 O  O   . LEU J  1 9   ? -23.797 7.023   29.231 1.00 70.87  ? 0   LEU J O   1 
ATOM   15698 C  CB  . LEU J  1 9   ? -26.297 6.260   31.217 1.00 77.13  ? 0   LEU J CB  1 
ATOM   15699 C  CG  . LEU J  1 9   ? -26.213 6.306   32.753 1.00 82.16  ? 0   LEU J CG  1 
ATOM   15700 C  CD1 . LEU J  1 9   ? -27.328 7.139   33.381 1.00 75.03  ? 0   LEU J CD1 1 
ATOM   15701 C  CD2 . LEU J  1 9   ? -26.234 4.912   33.337 1.00 72.47  ? 0   LEU J CD2 1 
ATOM   15702 N  N   . HIS J  1 10  ? -25.724 6.712   28.141 1.00 71.35  ? 1   HIS J N   1 
ATOM   15703 C  CA  . HIS J  1 10  ? -25.055 6.306   26.920 1.00 66.33  ? 1   HIS J CA  1 
ATOM   15704 C  C   . HIS J  1 10  ? -24.285 7.488   26.359 1.00 67.45  ? 1   HIS J C   1 
ATOM   15705 O  O   . HIS J  1 10  ? -23.234 7.332   25.747 1.00 67.52  ? 1   HIS J O   1 
ATOM   15706 C  CB  . HIS J  1 10  ? -26.071 5.757   25.917 1.00 70.26  ? 1   HIS J CB  1 
ATOM   15707 C  CG  . HIS J  1 10  ? -26.418 4.322   26.149 1.00 69.92  ? 1   HIS J CG  1 
ATOM   15708 N  ND1 . HIS J  1 10  ? -25.826 3.293   25.451 1.00 68.68  ? 1   HIS J ND1 1 
ATOM   15709 C  CD2 . HIS J  1 10  ? -27.270 3.739   27.022 1.00 79.19  ? 1   HIS J CD2 1 
ATOM   15710 C  CE1 . HIS J  1 10  ? -26.308 2.138   25.875 1.00 78.87  ? 1   HIS J CE1 1 
ATOM   15711 N  NE2 . HIS J  1 10  ? -27.177 2.383   26.837 1.00 77.30  ? 1   HIS J NE2 1 
ATOM   15712 N  N   . SER J  1 11  ? -24.810 8.683   26.585 1.00 71.60  ? 2   SER J N   1 
ATOM   15713 C  CA  . SER J  1 11  ? -24.152 9.894   26.124 1.00 75.01  ? 2   SER J CA  1 
ATOM   15714 C  C   . SER J  1 11  ? -22.782 10.077  26.788 1.00 73.94  ? 2   SER J C   1 
ATOM   15715 O  O   . SER J  1 11  ? -21.770 10.276  26.113 1.00 72.56  ? 2   SER J O   1 
ATOM   15716 C  CB  . SER J  1 11  ? -25.046 11.106  26.383 1.00 79.93  ? 2   SER J CB  1 
ATOM   15717 O  OG  . SER J  1 11  ? -24.332 12.314  26.198 1.00 87.75  ? 2   SER J OG  1 
ATOM   15718 N  N   . GLN J  1 12  ? -22.759 10.014  28.114 1.00 67.43  ? 3   GLN J N   1 
ATOM   15719 C  CA  . GLN J  1 12  ? -21.513 10.114  28.857 1.00 68.70  ? 3   GLN J CA  1 
ATOM   15720 C  C   . GLN J  1 12  ? -20.537 9.011   28.466 1.00 69.23  ? 3   GLN J C   1 
ATOM   15721 O  O   . GLN J  1 12  ? -19.336 9.247   28.310 1.00 69.03  ? 3   GLN J O   1 
ATOM   15722 C  CB  . GLN J  1 12  ? -21.788 10.041  30.359 1.00 74.31  ? 3   GLN J CB  1 
ATOM   15723 C  CG  . GLN J  1 12  ? -22.825 11.035  30.837 1.00 83.96  ? 3   GLN J CG  1 
ATOM   15724 C  CD  . GLN J  1 12  ? -22.993 11.026  32.342 1.00 82.96  ? 3   GLN J CD  1 
ATOM   15725 O  OE1 . GLN J  1 12  ? -22.330 10.268  33.045 1.00 76.17  ? 3   GLN J OE1 1 
ATOM   15726 N  NE2 . GLN J  1 12  ? -23.883 11.876  32.844 1.00 85.43  ? 3   GLN J NE2 1 
ATOM   15727 N  N   . ALA J  1 13  ? -21.059 7.800   28.325 1.00 68.86  ? 4   ALA J N   1 
ATOM   15728 C  CA  . ALA J  1 13  ? -20.232 6.663   27.969 1.00 59.16  ? 4   ALA J CA  1 
ATOM   15729 C  C   . ALA J  1 13  ? -19.568 6.944   26.641 1.00 58.82  ? 4   ALA J C   1 
ATOM   15730 O  O   . ALA J  1 13  ? -18.372 6.745   26.475 1.00 62.61  ? 4   ALA J O   1 
ATOM   15731 C  CB  . ALA J  1 13  ? -21.064 5.431   27.888 1.00 48.75  ? 4   ALA J CB  1 
ATOM   15732 N  N   . ASN J  1 14  ? -20.355 7.437   25.699 1.00 59.84  ? 5   ASN J N   1 
ATOM   15733 C  CA  . ASN J  1 14  ? -19.856 7.720   24.367 1.00 62.49  ? 5   ASN J CA  1 
ATOM   15734 C  C   . ASN J  1 14  ? -18.738 8.757   24.350 1.00 66.08  ? 5   ASN J C   1 
ATOM   15735 O  O   . ASN J  1 14  ? -17.671 8.517   23.782 1.00 63.46  ? 5   ASN J O   1 
ATOM   15736 C  CB  . ASN J  1 14  ? -21.007 8.129   23.452 1.00 64.67  ? 5   ASN J CB  1 
ATOM   15737 C  CG  . ASN J  1 14  ? -21.902 6.963   23.106 1.00 62.65  ? 5   ASN J CG  1 
ATOM   15738 O  OD1 . ASN J  1 14  ? -21.440 5.828   23.011 1.00 61.20  ? 5   ASN J OD1 1 
ATOM   15739 N  ND2 . ASN J  1 14  ? -23.185 7.231   22.920 1.00 59.82  ? 5   ASN J ND2 1 
ATOM   15740 N  N   . LEU J  1 15  ? -18.981 9.906   24.978 1.00 70.02  ? 6   LEU J N   1 
ATOM   15741 C  CA  . LEU J  1 15  ? -17.974 10.959  25.049 1.00 67.44  ? 6   LEU J CA  1 
ATOM   15742 C  C   . LEU J  1 15  ? -16.683 10.450  25.691 1.00 65.15  ? 6   LEU J C   1 
ATOM   15743 O  O   . LEU J  1 15  ? -15.588 10.730  25.203 1.00 65.93  ? 6   LEU J O   1 
ATOM   15744 C  CB  . LEU J  1 15  ? -18.507 12.183  25.792 1.00 63.89  ? 6   LEU J CB  1 
ATOM   15745 C  CG  . LEU J  1 15  ? -17.631 13.445  25.818 1.00 57.35  ? 6   LEU J CG  1 
ATOM   15746 C  CD1 . LEU J  1 15  ? -17.176 13.856  24.414 1.00 51.69  ? 6   LEU J CD1 1 
ATOM   15747 C  CD2 . LEU J  1 15  ? -18.372 14.580  26.511 1.00 48.52  ? 6   LEU J CD2 1 
ATOM   15748 N  N   . MET J  1 16  ? -16.801 9.691   26.773 1.00 63.05  ? 7   MET J N   1 
ATOM   15749 C  CA  . MET J  1 16  ? -15.603 9.134   27.390 1.00 66.01  ? 7   MET J CA  1 
ATOM   15750 C  C   . MET J  1 16  ? -14.837 8.265   26.399 1.00 67.48  ? 7   MET J C   1 
ATOM   15751 O  O   . MET J  1 16  ? -13.602 8.291   26.361 1.00 63.64  ? 7   MET J O   1 
ATOM   15752 C  CB  . MET J  1 16  ? -15.938 8.381   28.675 1.00 64.90  ? 7   MET J CB  1 
ATOM   15753 C  CG  . MET J  1 16  ? -15.834 9.263   29.919 1.00 77.09  ? 7   MET J CG  1 
ATOM   15754 S  SD  . MET J  1 16  ? -17.063 8.816   31.156 1.00 109.00 ? 7   MET J SD  1 
ATOM   15755 C  CE  . MET J  1 16  ? -16.522 9.764   32.578 1.00 93.48  ? 7   MET J CE  1 
ATOM   15756 N  N   . ARG J  1 17  ? -15.582 7.532   25.574 1.00 67.28  ? 8   ARG J N   1 
ATOM   15757 C  CA  . ARG J  1 17  ? -14.998 6.657   24.559 1.00 65.72  ? 8   ARG J CA  1 
ATOM   15758 C  C   . ARG J  1 17  ? -14.288 7.440   23.457 1.00 67.43  ? 8   ARG J C   1 
ATOM   15759 O  O   . ARG J  1 17  ? -13.131 7.171   23.140 1.00 73.69  ? 8   ARG J O   1 
ATOM   15760 C  CB  . ARG J  1 17  ? -16.071 5.746   23.959 1.00 61.85  ? 8   ARG J CB  1 
ATOM   15761 C  CG  . ARG J  1 17  ? -15.523 4.620   23.095 1.00 73.01  ? 8   ARG J CG  1 
ATOM   15762 C  CD  . ARG J  1 17  ? -16.581 3.555   22.848 1.00 67.31  ? 8   ARG J CD  1 
ATOM   15763 N  NE  . ARG J  1 17  ? -17.874 4.140   22.501 1.00 62.84  ? 8   ARG J NE  1 
ATOM   15764 C  CZ  . ARG J  1 17  ? -18.331 4.279   21.255 1.00 69.70  ? 8   ARG J CZ  1 
ATOM   15765 N  NH1 . ARG J  1 17  ? -17.602 3.876   20.218 1.00 65.04  ? 8   ARG J NH1 1 
ATOM   15766 N  NH2 . ARG J  1 17  ? -19.522 4.829   21.042 1.00 69.02  ? 8   ARG J NH2 1 
ATOM   15767 N  N   . LEU J  1 18  ? -14.990 8.415   22.888 1.00 66.20  ? 9   LEU J N   1 
ATOM   15768 C  CA  . LEU J  1 18  ? -14.456 9.240   21.807 1.00 65.62  ? 9   LEU J CA  1 
ATOM   15769 C  C   . LEU J  1 18  ? -13.172 9.940   22.211 1.00 62.43  ? 9   LEU J C   1 
ATOM   15770 O  O   . LEU J  1 18  ? -12.193 9.940   21.469 1.00 56.46  ? 9   LEU J O   1 
ATOM   15771 C  CB  . LEU J  1 18  ? -15.496 10.276  21.377 1.00 59.96  ? 9   LEU J CB  1 
ATOM   15772 C  CG  . LEU J  1 18  ? -15.041 11.370  20.411 1.00 58.97  ? 9   LEU J CG  1 
ATOM   15773 C  CD1 . LEU J  1 18  ? -14.755 10.787  19.055 1.00 56.74  ? 9   LEU J CD1 1 
ATOM   15774 C  CD2 . LEU J  1 18  ? -16.075 12.479  20.311 1.00 56.42  ? 9   LEU J CD2 1 
ATOM   15775 N  N   . LYS J  1 19  ? -13.189 10.545  23.392 1.00 65.89  ? 10  LYS J N   1 
ATOM   15776 C  CA  . LYS J  1 19  ? -12.007 11.208  23.916 1.00 67.59  ? 10  LYS J CA  1 
ATOM   15777 C  C   . LYS J  1 19  ? -10.908 10.193  24.177 1.00 77.27  ? 10  LYS J C   1 
ATOM   15778 O  O   . LYS J  1 19  ? -9.732  10.494  23.989 1.00 81.79  ? 10  LYS J O   1 
ATOM   15779 C  CB  . LYS J  1 19  ? -12.336 11.988  25.186 1.00 65.83  ? 10  LYS J CB  1 
ATOM   15780 C  CG  . LYS J  1 19  ? -13.084 13.281  24.932 1.00 64.55  ? 10  LYS J CG  1 
ATOM   15781 C  CD  . LYS J  1 19  ? -13.518 13.938  26.227 1.00 60.67  ? 10  LYS J CD  1 
ATOM   15782 C  CE  . LYS J  1 19  ? -12.649 15.126  26.595 1.00 59.50  ? 10  LYS J CE  1 
ATOM   15783 N  NZ  . LYS J  1 19  ? -13.342 15.936  27.631 1.00 63.12  ? 10  LYS J NZ  1 
ATOM   15784 N  N   . SER J  1 20  ? -11.288 8.987   24.594 1.00 74.00  ? 11  SER J N   1 
ATOM   15785 C  CA  . SER J  1 20  ? -10.308 7.927   24.787 1.00 78.42  ? 11  SER J CA  1 
ATOM   15786 C  C   . SER J  1 20  ? -9.685  7.487   23.469 1.00 78.46  ? 11  SER J C   1 
ATOM   15787 O  O   . SER J  1 20  ? -8.481  7.309   23.389 1.00 91.24  ? 11  SER J O   1 
ATOM   15788 C  CB  . SER J  1 20  ? -10.909 6.725   25.506 1.00 84.54  ? 11  SER J CB  1 
ATOM   15789 O  OG  . SER J  1 20  ? -9.883  5.919   26.070 1.00 89.00  ? 11  SER J OG  1 
ATOM   15790 N  N   . ASP J  1 21  ? -10.484 7.316   22.423 1.00 75.58  ? 12  ASP J N   1 
ATOM   15791 C  CA  . ASP J  1 21  ? -9.948  6.926   21.116 1.00 86.34  ? 12  ASP J CA  1 
ATOM   15792 C  C   . ASP J  1 21  ? -8.928  7.924   20.568 1.00 89.62  ? 12  ASP J C   1 
ATOM   15793 O  O   . ASP J  1 21  ? -8.067  7.565   19.761 1.00 96.32  ? 12  ASP J O   1 
ATOM   15794 C  CB  . ASP J  1 21  ? -11.070 6.725   20.089 1.00 77.14  ? 12  ASP J CB  1 
ATOM   15795 C  CG  . ASP J  1 21  ? -11.775 5.386   20.244 1.00 81.12  ? 12  ASP J CG  1 
ATOM   15796 O  OD1 . ASP J  1 21  ? -11.559 4.695   21.266 1.00 83.40  ? 12  ASP J OD1 1 
ATOM   15797 O  OD2 . ASP J  1 21  ? -12.545 5.025   19.334 1.00 81.98  ? 12  ASP J OD2 1 
ATOM   15798 N  N   . LEU J  1 22  ? -9.043  9.181   21.019 1.00 86.51  ? 13  LEU J N   1 
ATOM   15799 C  CA  . LEU J  1 22  ? -8.239  10.278  20.490 1.00 75.95  ? 13  LEU J CA  1 
ATOM   15800 C  C   . LEU J  1 22  ? -6.915  10.451  21.222 1.00 87.81  ? 13  LEU J C   1 
ATOM   15801 O  O   . LEU J  1 22  ? -5.847  10.303  20.630 1.00 93.33  ? 13  LEU J O   1 
ATOM   15802 C  CB  . LEU J  1 22  ? -9.045  11.566  20.558 1.00 75.58  ? 13  LEU J CB  1 
ATOM   15803 C  CG  . LEU J  1 22  ? -10.218 11.586  19.584 1.00 71.04  ? 13  LEU J CG  1 
ATOM   15804 C  CD1 . LEU J  1 22  ? -11.196 12.690  19.903 1.00 63.75  ? 13  LEU J CD1 1 
ATOM   15805 C  CD2 . LEU J  1 22  ? -9.698  11.733  18.178 1.00 71.77  ? 13  LEU J CD2 1 
ATOM   15806 N  N   . PHE J  1 23  ? -7.009  10.810  22.513 1.00 86.69  ? 14  PHE J N   1 
ATOM   15807 C  CA  . PHE J  1 23  ? -5.898  11.126  23.458 1.00 92.67  ? 14  PHE J CA  1 
ATOM   15808 C  C   . PHE J  1 23  ? -5.243  10.170  24.387 1.00 92.79  ? 14  PHE J C   1 
ATOM   15809 O  O   . PHE J  1 23  ? -4.049  10.189  24.612 1.00 94.85  ? 14  PHE J O   1 
ATOM   15810 C  CB  . PHE J  1 23  ? -6.410  12.287  24.383 1.00 90.25  ? 14  PHE J CB  1 
ATOM   15811 C  CG  . PHE J  1 23  ? -7.232  13.408  23.706 1.00 79.16  ? 14  PHE J CG  1 
ATOM   15812 C  CD1 . PHE J  1 23  ? -6.847  14.000  22.511 1.00 70.51  ? 14  PHE J CD1 1 
ATOM   15813 C  CD2 . PHE J  1 23  ? -8.360  13.914  24.349 1.00 64.60  ? 14  PHE J CD2 1 
ATOM   15814 C  CE1 . PHE J  1 23  ? -7.601  15.020  21.959 1.00 69.67  ? 14  PHE J CE1 1 
ATOM   15815 C  CE2 . PHE J  1 23  ? -9.096  14.925  23.808 1.00 71.55  ? 14  PHE J CE2 1 
ATOM   15816 C  CZ  . PHE J  1 23  ? -8.724  15.478  22.618 1.00 74.46  ? 14  PHE J CZ  1 
ATOM   15817 N  N   . ASN J  1 24  ? -6.079  9.317   24.993 1.00 97.88  ? 15  ASN J N   1 
ATOM   15818 C  CA  . ASN J  1 24  ? -5.600  8.210   25.827 1.00 104.33 ? 15  ASN J CA  1 
ATOM   15819 C  C   . ASN J  1 24  ? -4.937  7.043   25.065 1.00 106.21 ? 15  ASN J C   1 
ATOM   15820 O  O   . ASN J  1 24  ? -3.857  6.602   25.451 1.00 111.91 ? 15  ASN J O   1 
ATOM   15821 C  CB  . ASN J  1 24  ? -6.699  7.714   26.791 1.00 101.54 ? 15  ASN J CB  1 
ATOM   15822 C  CG  . ASN J  1 24  ? -6.992  8.714   27.931 1.00 108.68 ? 15  ASN J CG  1 
ATOM   15823 O  OD1 . ASN J  1 24  ? -6.204  8.852   28.864 1.00 97.39  ? 15  ASN J OD1 1 
ATOM   15824 N  ND2 . ASN J  1 24  ? -8.132  9.398   27.854 1.00 105.11 ? 15  ASN J ND2 1 
ATOM   15825 N  N   . ARG J  1 25  ? -5.634  6.581   24.019 1.00 109.20 ? 16  ARG J N   1 
ATOM   15826 C  CA  . ARG J  1 25  ? -5.242  5.496   23.106 1.00 112.17 ? 16  ARG J CA  1 
ATOM   15827 C  C   . ARG J  1 25  ? -4.252  5.789   21.937 1.00 117.82 ? 16  ARG J C   1 
ATOM   15828 O  O   . ARG J  1 25  ? -3.544  4.883   21.496 1.00 112.05 ? 16  ARG J O   1 
ATOM   15829 C  CB  . ARG J  1 25  ? -6.508  4.782   22.544 1.00 114.05 ? 16  ARG J CB  1 
ATOM   15830 C  CG  . ARG J  1 25  ? -6.874  3.404   23.173 1.00 108.96 ? 16  ARG J CG  1 
ATOM   15831 C  CD  . ARG J  1 25  ? -8.268  2.836   22.728 1.00 105.36 ? 16  ARG J CD  1 
ATOM   15832 N  NE  . ARG J  1 25  ? -9.334  3.264   23.638 1.00 113.22 ? 16  ARG J NE  1 
ATOM   15833 C  CZ  . ARG J  1 25  ? -10.636 3.205   23.439 1.00 114.09 ? 16  ARG J CZ  1 
ATOM   15834 N  NH1 . ARG J  1 25  ? -11.173 2.749   22.296 1.00 113.33 ? 16  ARG J NH1 1 
ATOM   15835 N  NH2 . ARG J  1 25  ? -11.443 3.664   24.381 1.00 99.51  ? 16  ARG J NH2 1 
ATOM   15836 N  N   . SER J  1 26  ? -4.210  7.028   21.434 1.00 115.49 ? 17  SER J N   1 
ATOM   15837 C  CA  . SER J  1 26  ? -3.338  7.391   20.303 1.00 121.82 ? 17  SER J CA  1 
ATOM   15838 C  C   . SER J  1 26  ? -2.396  8.552   20.667 1.00 116.20 ? 17  SER J C   1 
ATOM   15839 O  O   . SER J  1 26  ? -2.789  9.446   21.416 1.00 111.33 ? 17  SER J O   1 
ATOM   15840 C  CB  . SER J  1 26  ? -4.147  7.704   19.031 1.00 113.16 ? 17  SER J CB  1 
ATOM   15841 O  OG  . SER J  1 26  ? -4.553  6.516   18.373 1.00 97.46  ? 17  SER J OG  1 
ATOM   15842 N  N   . PRO J  1 27  ? -1.149  8.534   20.143 1.00 115.70 ? 18  PRO J N   1 
ATOM   15843 C  CA  . PRO J  1 27  ? -0.142  9.574   20.421 1.00 107.05 ? 18  PRO J CA  1 
ATOM   15844 C  C   . PRO J  1 27  ? -0.568  10.968  19.964 1.00 110.78 ? 18  PRO J C   1 
ATOM   15845 O  O   . PRO J  1 27  ? -1.175  11.094  18.894 1.00 110.41 ? 18  PRO J O   1 
ATOM   15846 C  CB  . PRO J  1 27  ? 1.069   9.122   19.599 1.00 97.23  ? 18  PRO J CB  1 
ATOM   15847 C  CG  . PRO J  1 27  ? 0.883   7.661   19.413 1.00 100.77 ? 18  PRO J CG  1 
ATOM   15848 C  CD  . PRO J  1 27  ? -0.602  7.464   19.289 1.00 110.55 ? 18  PRO J CD  1 
ATOM   15849 N  N   . MET J  1 28  ? -0.243  11.993  20.758 1.00 107.06 ? 19  MET J N   1 
ATOM   15850 C  CA  . MET J  1 28  ? -0.584  13.379  20.421 1.00 98.80  ? 19  MET J CA  1 
ATOM   15851 C  C   . MET J  1 28  ? 0.225   13.900  19.232 1.00 94.05  ? 19  MET J C   1 
ATOM   15852 O  O   . MET J  1 28  ? 1.402   13.569  19.057 1.00 90.07  ? 19  MET J O   1 
ATOM   15853 C  CB  . MET J  1 28  ? -0.420  14.321  21.624 1.00 92.08  ? 19  MET J CB  1 
ATOM   15854 C  CG  . MET J  1 28  ? -0.887  15.762  21.355 1.00 87.62  ? 19  MET J CG  1 
ATOM   15855 S  SD  . MET J  1 28  ? -0.591  16.937  22.712 1.00 103.93 ? 19  MET J SD  1 
ATOM   15856 C  CE  . MET J  1 28  ? -1.552  16.193  24.037 1.00 80.93  ? 19  MET J CE  1 
ATOM   15857 N  N   . TYR J  1 29  ? -0.431  14.731  18.431 1.00 88.76  ? 20  TYR J N   1 
ATOM   15858 C  CA  . TYR J  1 29  ? 0.134   15.298  17.218 1.00 80.45  ? 20  TYR J CA  1 
ATOM   15859 C  C   . TYR J  1 29  ? 1.462   16.029  17.528 1.00 76.43  ? 20  TYR J C   1 
ATOM   15860 O  O   . TYR J  1 29  ? 1.501   16.942  18.352 1.00 72.49  ? 20  TYR J O   1 
ATOM   15861 C  CB  . TYR J  1 29  ? -0.951  16.194  16.589 1.00 71.41  ? 20  TYR J CB  1 
ATOM   15862 C  CG  . TYR J  1 29  ? -0.528  17.139  15.494 1.00 68.88  ? 20  TYR J CG  1 
ATOM   15863 C  CD1 . TYR J  1 29  ? -0.339  16.702  14.187 1.00 70.67  ? 20  TYR J CD1 1 
ATOM   15864 C  CD2 . TYR J  1 29  ? -0.367  18.483  15.762 1.00 62.43  ? 20  TYR J CD2 1 
ATOM   15865 C  CE1 . TYR J  1 29  ? 0.034   17.590  13.193 1.00 66.81  ? 20  TYR J CE1 1 
ATOM   15866 C  CE2 . TYR J  1 29  ? 0.000   19.364  14.785 1.00 63.79  ? 20  TYR J CE2 1 
ATOM   15867 C  CZ  . TYR J  1 29  ? 0.200   18.926  13.509 1.00 63.43  ? 20  TYR J CZ  1 
ATOM   15868 O  OH  . TYR J  1 29  ? 0.569   19.857  12.569 1.00 67.66  ? 20  TYR J OH  1 
ATOM   15869 N  N   . PRO J  1 30  ? 2.561   15.585  16.889 1.00 69.43  ? 21  PRO J N   1 
ATOM   15870 C  CA  . PRO J  1 30  ? 3.952   16.023  17.067 1.00 61.00  ? 21  PRO J CA  1 
ATOM   15871 C  C   . PRO J  1 30  ? 4.169   17.433  16.579 1.00 63.51  ? 21  PRO J C   1 
ATOM   15872 O  O   . PRO J  1 30  ? 5.234   18.012  16.797 1.00 56.48  ? 21  PRO J O   1 
ATOM   15873 C  CB  . PRO J  1 30  ? 4.738   15.056  16.188 1.00 63.56  ? 21  PRO J CB  1 
ATOM   15874 C  CG  . PRO J  1 30  ? 3.797   14.689  15.126 1.00 66.75  ? 21  PRO J CG  1 
ATOM   15875 C  CD  . PRO J  1 30  ? 2.446   14.616  15.788 1.00 72.98  ? 21  PRO J CD  1 
ATOM   15876 N  N   . GLY J  1 31  ? 3.194   17.938  15.836 1.00 62.62  ? 22  GLY J N   1 
ATOM   15877 C  CA  . GLY J  1 31  ? 3.299   19.251  15.243 1.00 60.17  ? 22  GLY J CA  1 
ATOM   15878 C  C   . GLY J  1 31  ? 3.513   19.224  13.744 1.00 63.63  ? 22  GLY J C   1 
ATOM   15879 O  O   . GLY J  1 31  ? 3.855   18.197  13.162 1.00 68.17  ? 22  GLY J O   1 
ATOM   15880 N  N   . PRO J  1 32  ? 3.304   20.377  13.110 1.00 60.46  ? 23  PRO J N   1 
ATOM   15881 C  CA  . PRO J  1 32  ? 3.441   20.656  11.688 1.00 55.87  ? 23  PRO J CA  1 
ATOM   15882 C  C   . PRO J  1 32  ? 4.816   20.336  11.116 1.00 56.75  ? 23  PRO J C   1 
ATOM   15883 O  O   . PRO J  1 32  ? 5.835   20.558  11.743 1.00 60.66  ? 23  PRO J O   1 
ATOM   15884 C  CB  . PRO J  1 32  ? 3.218   22.163  11.636 1.00 61.63  ? 23  PRO J CB  1 
ATOM   15885 C  CG  . PRO J  1 32  ? 2.338   22.447  12.768 1.00 52.25  ? 23  PRO J CG  1 
ATOM   15886 C  CD  . PRO J  1 32  ? 2.813   21.552  13.844 1.00 64.19  ? 23  PRO J CD  1 
ATOM   15887 N  N   . THR J  1 33  ? 4.824   19.828  9.895  1.00 64.79  ? 24  THR J N   1 
ATOM   15888 C  CA  . THR J  1 33  ? 6.033   19.761  9.092  1.00 68.17  ? 24  THR J CA  1 
ATOM   15889 C  C   . THR J  1 33  ? 5.721   20.311  7.708  1.00 70.15  ? 24  THR J C   1 
ATOM   15890 O  O   . THR J  1 33  ? 4.562   20.554  7.372  1.00 66.15  ? 24  THR J O   1 
ATOM   15891 C  CB  . THR J  1 33  ? 6.619   18.332  8.976  1.00 75.53  ? 24  THR J CB  1 
ATOM   15892 O  OG1 . THR J  1 33  ? 5.568   17.352  8.968  1.00 80.70  ? 24  THR J OG1 1 
ATOM   15893 C  CG2 . THR J  1 33  ? 7.535   18.059  10.138 1.00 72.31  ? 24  THR J CG2 1 
ATOM   15894 N  N   . LYS J  1 34  ? 6.775   20.554  6.938  1.00 74.24  ? 25  LYS J N   1 
ATOM   15895 C  CA  . LYS J  1 34  ? 6.674   20.980  5.552  1.00 72.95  ? 25  LYS J CA  1 
ATOM   15896 C  C   . LYS J  1 34  ? 5.955   19.883  4.781  1.00 71.98  ? 25  LYS J C   1 
ATOM   15897 O  O   . LYS J  1 34  ? 5.251   20.143  3.808  1.00 66.09  ? 25  LYS J O   1 
ATOM   15898 C  CB  . LYS J  1 34  ? 8.081   21.175  5.009  1.00 68.53  ? 25  LYS J CB  1 
ATOM   15899 C  CG  . LYS J  1 34  ? 9.035   20.192  5.653  1.00 68.15  ? 25  LYS J CG  1 
ATOM   15900 C  CD  . LYS J  1 34  ? 10.433  20.203  5.074  1.00 74.54  ? 25  LYS J CD  1 
ATOM   15901 C  CE  . LYS J  1 34  ? 11.159  18.914  5.486  1.00 87.16  ? 25  LYS J CE  1 
ATOM   15902 N  NZ  . LYS J  1 34  ? 12.530  18.783  4.921  1.00 96.60  ? 25  LYS J NZ  1 
ATOM   15903 N  N   . ASP J  1 35  ? 6.133   18.652  5.247  1.00 72.27  ? 26  ASP J N   1 
ATOM   15904 C  CA  . ASP J  1 35  ? 5.450   17.498  4.681  1.00 73.99  ? 26  ASP J CA  1 
ATOM   15905 C  C   . ASP J  1 35  ? 4.026   17.409  5.198  1.00 75.79  ? 26  ASP J C   1 
ATOM   15906 O  O   . ASP J  1 35  ? 3.203   16.690  4.642  1.00 70.15  ? 26  ASP J O   1 
ATOM   15907 C  CB  . ASP J  1 35  ? 6.184   16.207  5.050  1.00 83.74  ? 26  ASP J CB  1 
ATOM   15908 C  CG  . ASP J  1 35  ? 7.377   15.939  4.166  1.00 85.14  ? 26  ASP J CG  1 
ATOM   15909 O  OD1 . ASP J  1 35  ? 7.156   15.507  3.019  1.00 87.43  ? 26  ASP J OD1 1 
ATOM   15910 O  OD2 . ASP J  1 35  ? 8.529   16.141  4.615  1.00 82.73  ? 26  ASP J OD2 1 
ATOM   15911 N  N   . ASP J  1 36  ? 3.759   18.081  6.311  1.00 77.04  ? 27  ASP J N   1 
ATOM   15912 C  CA  . ASP J  1 36  ? 2.408   18.136  6.857  1.00 76.42  ? 27  ASP J CA  1 
ATOM   15913 C  C   . ASP J  1 36  ? 2.090   19.504  7.480  1.00 70.80  ? 27  ASP J C   1 
ATOM   15914 O  O   . ASP J  1 36  ? 1.933   19.628  8.696  1.00 61.59  ? 27  ASP J O   1 
ATOM   15915 C  CB  . ASP J  1 36  ? 2.191   16.999  7.856  1.00 67.21  ? 27  ASP J CB  1 
ATOM   15916 C  CG  . ASP J  1 36  ? 0.735   16.824  8.224  1.00 75.29  ? 27  ASP J CG  1 
ATOM   15917 O  OD1 . ASP J  1 36  ? -0.129  17.175  7.396  1.00 80.36  ? 27  ASP J OD1 1 
ATOM   15918 O  OD2 . ASP J  1 36  ? 0.452   16.340  9.340  1.00 79.13  ? 27  ASP J OD2 1 
ATOM   15919 N  N   . PRO J  1 37  ? 1.988   20.543  6.645  1.00 68.01  ? 28  PRO J N   1 
ATOM   15920 C  CA  . PRO J  1 37  ? 1.799   21.868  7.234  1.00 66.46  ? 28  PRO J CA  1 
ATOM   15921 C  C   . PRO J  1 37  ? 0.359   22.078  7.650  1.00 62.39  ? 28  PRO J C   1 
ATOM   15922 O  O   . PRO J  1 37  ? -0.497  21.240  7.377  1.00 59.44  ? 28  PRO J O   1 
ATOM   15923 C  CB  . PRO J  1 37  ? 2.156   22.813  6.085  1.00 61.95  ? 28  PRO J CB  1 
ATOM   15924 C  CG  . PRO J  1 37  ? 1.849   22.053  4.866  1.00 63.13  ? 28  PRO J CG  1 
ATOM   15925 C  CD  . PRO J  1 37  ? 2.053   20.586  5.177  1.00 63.02  ? 28  PRO J CD  1 
ATOM   15926 N  N   . LEU J  1 38  ? 0.096   23.224  8.258  1.00 55.23  ? 29  LEU J N   1 
ATOM   15927 C  CA  . LEU J  1 38  ? -1.188  23.489  8.858  1.00 51.67  ? 29  LEU J CA  1 
ATOM   15928 C  C   . LEU J  1 38  ? -1.532  24.965  8.705  1.00 59.50  ? 29  LEU J C   1 
ATOM   15929 O  O   . LEU J  1 38  ? -0.649  25.828  8.627  1.00 52.09  ? 29  LEU J O   1 
ATOM   15930 C  CB  . LEU J  1 38  ? -1.101  23.137  10.329 1.00 59.43  ? 29  LEU J CB  1 
ATOM   15931 C  CG  . LEU J  1 38  ? -2.372  23.108  11.155 1.00 64.66  ? 29  LEU J CG  1 
ATOM   15932 C  CD1 . LEU J  1 38  ? -3.252  21.963  10.669 1.00 66.75  ? 29  LEU J CD1 1 
ATOM   15933 C  CD2 . LEU J  1 38  ? -1.991  22.941  12.616 1.00 63.82  ? 29  LEU J CD2 1 
ATOM   15934 N  N   . THR J  1 39  ? -2.822  25.264  8.651  1.00 61.41  ? 30  THR J N   1 
ATOM   15935 C  CA  . THR J  1 39  ? -3.236  26.658  8.607  1.00 62.83  ? 30  THR J CA  1 
ATOM   15936 C  C   . THR J  1 39  ? -3.926  27.020  9.900  1.00 54.22  ? 30  THR J C   1 
ATOM   15937 O  O   . THR J  1 39  ? -4.880  26.367  10.321 1.00 56.18  ? 30  THR J O   1 
ATOM   15938 C  CB  . THR J  1 39  ? -4.178  26.988  7.400  1.00 68.99  ? 30  THR J CB  1 
ATOM   15939 O  OG1 . THR J  1 39  ? -3.452  26.900  6.163  1.00 58.09  ? 30  THR J OG1 1 
ATOM   15940 C  CG2 . THR J  1 39  ? -4.758  28.402  7.545  1.00 60.90  ? 30  THR J CG2 1 
ATOM   15941 N  N   . VAL J  1 40  ? -3.424  28.068  10.529 1.00 55.39  ? 31  VAL J N   1 
ATOM   15942 C  CA  . VAL J  1 40  ? -4.054  28.619  11.714 1.00 56.46  ? 31  VAL J CA  1 
ATOM   15943 C  C   . VAL J  1 40  ? -4.729  29.930  11.325 1.00 56.07  ? 31  VAL J C   1 
ATOM   15944 O  O   . VAL J  1 40  ? -4.078  30.858  10.841 1.00 49.73  ? 31  VAL J O   1 
ATOM   15945 C  CB  . VAL J  1 40  ? -3.015  28.857  12.857 1.00 55.27  ? 31  VAL J CB  1 
ATOM   15946 C  CG1 . VAL J  1 40  ? -3.696  29.346  14.121 1.00 48.35  ? 31  VAL J CG1 1 
ATOM   15947 C  CG2 . VAL J  1 40  ? -2.221  27.600  13.143 1.00 45.41  ? 31  VAL J CG2 1 
ATOM   15948 N  N   . TYR J  1 41  ? -6.040  29.991  11.515 1.00 58.31  ? 32  TYR J N   1 
ATOM   15949 C  CA  . TYR J  1 41  ? -6.752  31.250  11.372 1.00 64.52  ? 32  TYR J CA  1 
ATOM   15950 C  C   . TYR J  1 41  ? -6.685  32.039  12.671 1.00 66.18  ? 32  TYR J C   1 
ATOM   15951 O  O   . TYR J  1 41  ? -6.931  31.500  13.754 1.00 62.85  ? 32  TYR J O   1 
ATOM   15952 C  CB  . TYR J  1 41  ? -8.216  31.039  10.975 1.00 71.94  ? 32  TYR J CB  1 
ATOM   15953 C  CG  . TYR J  1 41  ? -8.384  30.418  9.619  1.00 70.98  ? 32  TYR J CG  1 
ATOM   15954 C  CD1 . TYR J  1 41  ? -8.285  31.184  8.463  1.00 75.79  ? 32  TYR J CD1 1 
ATOM   15955 C  CD2 . TYR J  1 41  ? -8.631  29.060  9.491  1.00 72.35  ? 32  TYR J CD2 1 
ATOM   15956 C  CE1 . TYR J  1 41  ? -8.430  30.604  7.214  1.00 81.70  ? 32  TYR J CE1 1 
ATOM   15957 C  CE2 . TYR J  1 41  ? -8.782  28.476  8.256  1.00 79.38  ? 32  TYR J CE2 1 
ATOM   15958 C  CZ  . TYR J  1 41  ? -8.680  29.248  7.121  1.00 82.50  ? 32  TYR J CZ  1 
ATOM   15959 O  OH  . TYR J  1 41  ? -8.825  28.650  5.897  1.00 75.33  ? 32  TYR J OH  1 
ATOM   15960 N  N   . LEU J  1 42  ? -6.353  33.320  12.534 1.00 68.90  ? 33  LEU J N   1 
ATOM   15961 C  CA  . LEU J  1 42  ? -6.285  34.257  13.640 1.00 62.89  ? 33  LEU J CA  1 
ATOM   15962 C  C   . LEU J  1 42  ? -7.305  35.365  13.411 1.00 62.94  ? 33  LEU J C   1 
ATOM   15963 O  O   . LEU J  1 42  ? -7.472  35.834  12.296 1.00 75.07  ? 33  LEU J O   1 
ATOM   15964 C  CB  . LEU J  1 42  ? -4.872  34.839  13.739 1.00 64.13  ? 33  LEU J CB  1 
ATOM   15965 C  CG  . LEU J  1 42  ? -4.221  34.754  15.127 1.00 69.95  ? 33  LEU J CG  1 
ATOM   15966 C  CD1 . LEU J  1 42  ? -4.184  33.313  15.587 1.00 73.52  ? 33  LEU J CD1 1 
ATOM   15967 C  CD2 . LEU J  1 42  ? -2.827  35.354  15.166 1.00 64.51  ? 33  LEU J CD2 1 
ATOM   15968 N  N   . SER J  1 43  ? -8.009  35.752  14.464 1.00 62.30  ? 34  SER J N   1 
ATOM   15969 C  CA  . SER J  1 43  ? -8.993  36.823  14.399 1.00 62.54  ? 34  SER J CA  1 
ATOM   15970 C  C   . SER J  1 43  ? -9.002  37.476  15.777 1.00 61.27  ? 34  SER J C   1 
ATOM   15971 O  O   . SER J  1 43  ? -8.857  36.778  16.777 1.00 63.28  ? 34  SER J O   1 
ATOM   15972 C  CB  . SER J  1 43  ? -10.369 36.231  14.055 1.00 71.87  ? 34  SER J CB  1 
ATOM   15973 O  OG  . SER J  1 43  ? -11.410 37.189  14.149 1.00 72.60  ? 34  SER J OG  1 
ATOM   15974 N  N   . PHE J  1 44  ? -9.168  38.796  15.847 1.00 59.60  ? 35  PHE J N   1 
ATOM   15975 C  CA  . PHE J  1 44  ? -9.168  39.503  17.140 1.00 54.83  ? 35  PHE J CA  1 
ATOM   15976 C  C   . PHE J  1 44  ? -10.453 40.245  17.461 1.00 58.36  ? 35  PHE J C   1 
ATOM   15977 O  O   . PHE J  1 44  ? -11.219 40.617  16.581 1.00 67.15  ? 35  PHE J O   1 
ATOM   15978 C  CB  . PHE J  1 44  ? -8.027  40.507  17.238 1.00 54.19  ? 35  PHE J CB  1 
ATOM   15979 C  CG  . PHE J  1 44  ? -6.674  39.886  17.285 1.00 57.09  ? 35  PHE J CG  1 
ATOM   15980 C  CD1 . PHE J  1 44  ? -6.109  39.528  18.485 1.00 56.52  ? 35  PHE J CD1 1 
ATOM   15981 C  CD2 . PHE J  1 44  ? -5.957  39.673  16.125 1.00 57.49  ? 35  PHE J CD2 1 
ATOM   15982 C  CE1 . PHE J  1 44  ? -4.849  38.968  18.523 1.00 59.65  ? 35  PHE J CE1 1 
ATOM   15983 C  CE2 . PHE J  1 44  ? -4.701  39.111  16.159 1.00 57.98  ? 35  PHE J CE2 1 
ATOM   15984 C  CZ  . PHE J  1 44  ? -4.148  38.757  17.354 1.00 56.92  ? 35  PHE J CZ  1 
ATOM   15985 N  N   . SER J  1 45  ? -10.673 40.465  18.745 1.00 60.55  ? 36  SER J N   1 
ATOM   15986 C  CA  . SER J  1 45  ? -11.817 41.220  19.202 1.00 57.81  ? 36  SER J CA  1 
ATOM   15987 C  C   . SER J  1 45  ? -11.313 42.103  20.332 1.00 60.99  ? 36  SER J C   1 
ATOM   15988 O  O   . SER J  1 45  ? -10.710 41.614  21.282 1.00 62.64  ? 36  SER J O   1 
ATOM   15989 C  CB  . SER J  1 45  ? -12.910 40.265  19.680 1.00 56.82  ? 36  SER J CB  1 
ATOM   15990 O  OG  . SER J  1 45  ? -14.110 40.946  19.975 1.00 63.66  ? 36  SER J OG  1 
ATOM   15991 N  N   . LEU J  1 46  ? -11.543 43.408  20.225 1.00 66.36  ? 37  LEU J N   1 
ATOM   15992 C  CA  . LEU J  1 46  ? -11.051 44.345  21.222 1.00 53.86  ? 37  LEU J CA  1 
ATOM   15993 C  C   . LEU J  1 46  ? -12.057 44.562  22.324 1.00 58.90  ? 37  LEU J C   1 
ATOM   15994 O  O   . LEU J  1 46  ? -13.252 44.784  22.085 1.00 59.37  ? 37  LEU J O   1 
ATOM   15995 C  CB  . LEU J  1 46  ? -10.660 45.681  20.598 1.00 57.82  ? 37  LEU J CB  1 
ATOM   15996 C  CG  . LEU J  1 46  ? -9.297  45.589  19.932 1.00 66.95  ? 37  LEU J CG  1 
ATOM   15997 C  CD1 . LEU J  1 46  ? -8.818  46.956  19.507 1.00 63.85  ? 37  LEU J CD1 1 
ATOM   15998 C  CD2 . LEU J  1 46  ? -8.346  44.972  20.934 1.00 71.48  ? 37  LEU J CD2 1 
ATOM   15999 N  N   . LEU J  1 47  ? -11.541 44.494  23.543 1.00 61.48  ? 38  LEU J N   1 
ATOM   16000 C  CA  . LEU J  1 47  ? -12.330 44.677  24.745 1.00 58.52  ? 38  LEU J CA  1 
ATOM   16001 C  C   . LEU J  1 47  ? -12.056 45.939  25.568 1.00 56.06  ? 38  LEU J C   1 
ATOM   16002 O  O   . LEU J  1 47  ? -12.979 46.638  25.956 1.00 54.39  ? 38  LEU J O   1 
ATOM   16003 C  CB  . LEU J  1 47  ? -12.180 43.482  25.675 1.00 49.76  ? 38  LEU J CB  1 
ATOM   16004 C  CG  . LEU J  1 47  ? -13.383 42.563  25.519 1.00 53.16  ? 38  LEU J CG  1 
ATOM   16005 C  CD1 . LEU J  1 47  ? -13.314 41.916  24.178 1.00 58.07  ? 38  LEU J CD1 1 
ATOM   16006 C  CD2 . LEU J  1 47  ? -13.406 41.527  26.603 1.00 64.06  ? 38  LEU J CD2 1 
ATOM   16007 N  N   . ASP J  1 48  ? -10.796 46.190  25.889 1.00 57.15  ? 39  ASP J N   1 
ATOM   16008 C  CA  . ASP J  1 48  ? -10.440 47.414  26.583 1.00 58.31  ? 39  ASP J CA  1 
ATOM   16009 C  C   . ASP J  1 48  ? -8.997  47.855  26.341 1.00 54.71  ? 39  ASP J C   1 
ATOM   16010 O  O   . ASP J  1 48  ? -8.085  47.039  26.345 1.00 54.25  ? 39  ASP J O   1 
ATOM   16011 C  CB  . ASP J  1 48  ? -10.656 47.202  28.085 1.00 55.27  ? 39  ASP J CB  1 
ATOM   16012 C  CG  . ASP J  1 48  ? -11.032 48.470  28.802 1.00 55.96  ? 39  ASP J CG  1 
ATOM   16013 O  OD1 . ASP J  1 48  ? -10.995 49.547  28.177 1.00 54.67  ? 39  ASP J OD1 1 
ATOM   16014 O  OD2 . ASP J  1 48  ? -11.362 48.393  29.996 1.00 60.04  ? 39  ASP J OD2 1 
ATOM   16015 N  N   . ILE J  1 49  ? -8.785  49.156  26.187 1.00 56.12  ? 40  ILE J N   1 
ATOM   16016 C  CA  . ILE J  1 49  ? -7.441  49.681  26.315 1.00 57.34  ? 40  ILE J CA  1 
ATOM   16017 C  C   . ILE J  1 49  ? -7.410  50.274  27.718 1.00 62.53  ? 40  ILE J C   1 
ATOM   16018 O  O   . ILE J  1 49  ? -7.990  51.335  27.990 1.00 64.45  ? 40  ILE J O   1 
ATOM   16019 C  CB  . ILE J  1 49  ? -7.138  50.761  25.262 1.00 55.86  ? 40  ILE J CB  1 
ATOM   16020 C  CG1 . ILE J  1 49  ? -7.266  50.179  23.872 1.00 53.19  ? 40  ILE J CG1 1 
ATOM   16021 C  CG2 . ILE J  1 49  ? -5.734  51.298  25.420 1.00 58.28  ? 40  ILE J CG2 1 
ATOM   16022 C  CD1 . ILE J  1 49  ? -6.736  51.072  22.794 1.00 58.65  ? 40  ILE J CD1 1 
ATOM   16023 N  N   . VAL J  1 50  ? -6.709  49.571  28.600 1.00 65.67  ? 41  VAL J N   1 
ATOM   16024 C  CA  . VAL J  1 50  ? -6.762  49.837  30.030 1.00 60.18  ? 41  VAL J CA  1 
ATOM   16025 C  C   . VAL J  1 50  ? -5.870  51.000  30.399 1.00 58.08  ? 41  VAL J C   1 
ATOM   16026 O  O   . VAL J  1 50  ? -6.239  51.849  31.210 1.00 66.57  ? 41  VAL J O   1 
ATOM   16027 C  CB  . VAL J  1 50  ? -6.353  48.598  30.842 1.00 54.28  ? 41  VAL J CB  1 
ATOM   16028 C  CG1 . VAL J  1 50  ? -6.466  48.890  32.320 1.00 54.30  ? 41  VAL J CG1 1 
ATOM   16029 C  CG2 . VAL J  1 50  ? -7.217  47.409  30.455 1.00 46.67  ? 41  VAL J CG2 1 
ATOM   16030 N  N   . LYS J  1 51  ? -4.681  51.027  29.819 1.00 51.51  ? 42  LYS J N   1 
ATOM   16031 C  CA  . LYS J  1 51  ? -3.815  52.159  30.026 1.00 56.27  ? 42  LYS J CA  1 
ATOM   16032 C  C   . LYS J  1 51  ? -2.763  52.279  28.941 1.00 58.07  ? 42  LYS J C   1 
ATOM   16033 O  O   . LYS J  1 51  ? -2.473  51.321  28.231 1.00 59.35  ? 42  LYS J O   1 
ATOM   16034 C  CB  . LYS J  1 51  ? -3.191  52.107  31.416 1.00 55.71  ? 42  LYS J CB  1 
ATOM   16035 C  CG  . LYS J  1 51  ? -1.805  51.562  31.463 1.00 61.16  ? 42  LYS J CG  1 
ATOM   16036 C  CD  . LYS J  1 51  ? -1.309  51.623  32.878 1.00 65.97  ? 42  LYS J CD  1 
ATOM   16037 C  CE  . LYS J  1 51  ? 0.063   51.010  32.994 1.00 74.76  ? 42  LYS J CE  1 
ATOM   16038 N  NZ  . LYS J  1 51  ? 0.107   50.166  34.207 1.00 77.17  ? 42  LYS J NZ  1 
ATOM   16039 N  N   . ALA J  1 52  ? -2.208  53.474  28.810 1.00 53.87  ? 43  ALA J N   1 
ATOM   16040 C  CA  . ALA J  1 52  ? -1.150  53.723  27.862 1.00 52.45  ? 43  ALA J CA  1 
ATOM   16041 C  C   . ALA J  1 52  ? -0.148  54.446  28.709 1.00 60.21  ? 43  ALA J C   1 
ATOM   16042 O  O   . ALA J  1 52  ? -0.537  55.237  29.550 1.00 62.14  ? 43  ALA J O   1 
ATOM   16043 C  CB  . ALA J  1 52  ? -1.650  54.607  26.739 1.00 57.50  ? 43  ALA J CB  1 
ATOM   16044 N  N   . ASP J  1 53  ? 1.134   54.168  28.535 1.00 66.53  ? 44  ASP J N   1 
ATOM   16045 C  CA  . ASP J  1 53  ? 2.120   54.692  29.474 1.00 64.72  ? 44  ASP J CA  1 
ATOM   16046 C  C   . ASP J  1 53  ? 3.157   55.570  28.785 1.00 64.72  ? 44  ASP J C   1 
ATOM   16047 O  O   . ASP J  1 53  ? 3.987   55.064  28.028 1.00 65.30  ? 44  ASP J O   1 
ATOM   16048 C  CB  . ASP J  1 53  ? 2.801   53.523  30.189 1.00 67.34  ? 44  ASP J CB  1 
ATOM   16049 C  CG  . ASP J  1 53  ? 3.461   53.928  31.485 1.00 68.83  ? 44  ASP J CG  1 
ATOM   16050 O  OD1 . ASP J  1 53  ? 3.978   55.063  31.574 1.00 65.29  ? 44  ASP J OD1 1 
ATOM   16051 O  OD2 . ASP J  1 53  ? 3.464   53.092  32.412 1.00 69.34  ? 44  ASP J OD2 1 
ATOM   16052 N  N   . SER J  1 54  ? 3.124   56.872  29.080 1.00 68.70  ? 45  SER J N   1 
ATOM   16053 C  CA  . SER J  1 54  ? 4.001   57.855  28.433 1.00 71.42  ? 45  SER J CA  1 
ATOM   16054 C  C   . SER J  1 54  ? 5.423   57.769  28.938 1.00 67.91  ? 45  SER J C   1 
ATOM   16055 O  O   . SER J  1 54  ? 6.354   58.137  28.237 1.00 64.34  ? 45  SER J O   1 
ATOM   16056 C  CB  . SER J  1 54  ? 3.501   59.275  28.671 1.00 67.29  ? 45  SER J CB  1 
ATOM   16057 O  OG  . SER J  1 54  ? 2.164   59.414  28.249 1.00 81.18  ? 45  SER J OG  1 
ATOM   16058 N  N   . SER J  1 55  ? 5.585   57.308  30.171 1.00 65.91  ? 46  SER J N   1 
ATOM   16059 C  CA  . SER J  1 55  ? 6.916   57.195  30.733 1.00 66.42  ? 46  SER J CA  1 
ATOM   16060 C  C   . SER J  1 55  ? 7.657   56.066  30.060 1.00 65.15  ? 46  SER J C   1 
ATOM   16061 O  O   . SER J  1 55  ? 8.808   56.233  29.648 1.00 64.41  ? 46  SER J O   1 
ATOM   16062 C  CB  . SER J  1 55  ? 6.883   57.025  32.255 1.00 65.10  ? 46  SER J CB  1 
ATOM   16063 O  OG  . SER J  1 55  ? 5.699   56.373  32.675 1.00 72.29  ? 46  SER J OG  1 
ATOM   16064 N  N   . THR J  1 56  ? 7.021   54.902  29.982 1.00 66.65  ? 47  THR J N   1 
ATOM   16065 C  CA  . THR J  1 56  ? 7.662   53.748  29.355 1.00 64.72  ? 47  THR J CA  1 
ATOM   16066 C  C   . THR J  1 56  ? 7.392   53.452  27.858 1.00 61.19  ? 47  THR J C   1 
ATOM   16067 O  O   . THR J  1 56  ? 8.126   52.671  27.245 1.00 62.66  ? 47  THR J O   1 
ATOM   16068 C  CB  . THR J  1 56  ? 7.350   52.487  30.164 1.00 61.35  ? 47  THR J CB  1 
ATOM   16069 O  OG1 . THR J  1 56  ? 5.946   52.457  30.465 1.00 58.12  ? 47  THR J OG1 1 
ATOM   16070 C  CG2 . THR J  1 56  ? 8.150   52.481  31.463 1.00 63.29  ? 47  THR J CG2 1 
ATOM   16071 N  N   . ASN J  1 57  ? 6.406   54.107  27.253 1.00 61.21  ? 48  ASN J N   1 
ATOM   16072 C  CA  . ASN J  1 57  ? 5.917   53.681  25.930 1.00 62.74  ? 48  ASN J CA  1 
ATOM   16073 C  C   . ASN J  1 57  ? 5.437   52.211  25.861 1.00 58.58  ? 48  ASN J C   1 
ATOM   16074 O  O   . ASN J  1 57  ? 5.977   51.408  25.110 1.00 53.37  ? 48  ASN J O   1 
ATOM   16075 C  CB  . ASN J  1 57  ? 6.916   53.996  24.804 1.00 64.15  ? 48  ASN J CB  1 
ATOM   16076 C  CG  . ASN J  1 57  ? 7.117   55.494  24.587 1.00 68.06  ? 48  ASN J CG  1 
ATOM   16077 O  OD1 . ASN J  1 57  ? 6.323   56.324  25.038 1.00 65.88  ? 48  ASN J OD1 1 
ATOM   16078 N  ND2 . ASN J  1 57  ? 8.193   55.839  23.894 1.00 68.73  ? 48  ASN J ND2 1 
ATOM   16079 N  N   . GLU J  1 58  ? 4.478   51.865  26.718 1.00 59.70  ? 49  GLU J N   1 
ATOM   16080 C  CA  . GLU J  1 58  ? 3.819   50.568  26.701 1.00 56.35  ? 49  GLU J CA  1 
ATOM   16081 C  C   . GLU J  1 58  ? 2.330   50.787  26.856 1.00 60.32  ? 49  GLU J C   1 
ATOM   16082 O  O   . GLU J  1 58  ? 1.904   51.591  27.687 1.00 59.23  ? 49  GLU J O   1 
ATOM   16083 C  CB  . GLU J  1 58  ? 4.236   49.705  27.890 1.00 55.04  ? 49  GLU J CB  1 
ATOM   16084 C  CG  . GLU J  1 58  ? 5.697   49.702  28.267 1.00 58.52  ? 49  GLU J CG  1 
ATOM   16085 C  CD  . GLU J  1 58  ? 5.890   49.166  29.672 1.00 62.62  ? 49  GLU J CD  1 
ATOM   16086 O  OE1 . GLU J  1 58  ? 5.704   49.938  30.642 1.00 54.09  ? 49  GLU J OE1 1 
ATOM   16087 O  OE2 . GLU J  1 58  ? 6.194   47.960  29.803 1.00 62.46  ? 49  GLU J OE2 1 
ATOM   16088 N  N   . VAL J  1 59  ? 1.539   50.033  26.102 1.00 55.54  ? 50  VAL J N   1 
ATOM   16089 C  CA  . VAL J  1 59  ? 0.089   50.070  26.243 1.00 52.69  ? 50  VAL J CA  1 
ATOM   16090 C  C   . VAL J  1 59  ? -0.437  48.709  26.735 1.00 51.32  ? 50  VAL J C   1 
ATOM   16091 O  O   . VAL J  1 59  ? 0.207   47.667  26.579 1.00 50.92  ? 50  VAL J O   1 
ATOM   16092 C  CB  . VAL J  1 59  ? -0.581  50.551  24.927 1.00 59.62  ? 50  VAL J CB  1 
ATOM   16093 C  CG1 . VAL J  1 59  ? -2.093  50.609  25.053 1.00 59.10  ? 50  VAL J CG1 1 
ATOM   16094 C  CG2 . VAL J  1 59  ? -0.051  51.924  24.566 1.00 57.38  ? 50  VAL J CG2 1 
ATOM   16095 N  N   . ASP J  1 60  ? -1.591  48.739  27.379 1.00 51.32  ? 51  ASP J N   1 
ATOM   16096 C  CA  . ASP J  1 60  ? -2.158  47.553  27.999 1.00 54.58  ? 51  ASP J CA  1 
ATOM   16097 C  C   . ASP J  1 60  ? -3.482  47.246  27.358 1.00 50.76  ? 51  ASP J C   1 
ATOM   16098 O  O   . ASP J  1 60  ? -4.441  47.998  27.495 1.00 51.86  ? 51  ASP J O   1 
ATOM   16099 C  CB  . ASP J  1 60  ? -2.363  47.742  29.511 1.00 50.98  ? 51  ASP J CB  1 
ATOM   16100 C  CG  . ASP J  1 60  ? -1.073  47.621  30.304 1.00 56.44  ? 51  ASP J CG  1 
ATOM   16101 O  OD1 . ASP J  1 60  ? -0.024  47.294  29.714 1.00 54.55  ? 51  ASP J OD1 1 
ATOM   16102 O  OD2 . ASP J  1 60  ? -1.110  47.839  31.534 1.00 69.10  ? 51  ASP J OD2 1 
ATOM   16103 N  N   . LEU J  1 61  ? -3.537  46.114  26.677 1.00 52.18  ? 52  LEU J N   1 
ATOM   16104 C  CA  . LEU J  1 61  ? -4.719  45.755  25.933 1.00 49.68  ? 52  LEU J CA  1 
ATOM   16105 C  C   . LEU J  1 61  ? -5.381  44.520  26.500 1.00 47.98  ? 52  LEU J C   1 
ATOM   16106 O  O   . LEU J  1 61  ? -4.710  43.577  26.910 1.00 48.61  ? 52  LEU J O   1 
ATOM   16107 C  CB  . LEU J  1 61  ? -4.345  45.512  24.478 1.00 55.92  ? 52  LEU J CB  1 
ATOM   16108 C  CG  . LEU J  1 61  ? -5.511  45.603  23.505 1.00 62.85  ? 52  LEU J CG  1 
ATOM   16109 C  CD1 . LEU J  1 61  ? -5.437  46.923  22.787 1.00 62.52  ? 52  LEU J CD1 1 
ATOM   16110 C  CD2 . LEU J  1 61  ? -5.451  44.472  22.524 1.00 62.59  ? 52  LEU J CD2 1 
ATOM   16111 N  N   . VAL J  1 62  ? -6.704  44.556  26.533 1.00 48.04  ? 53  VAL J N   1 
ATOM   16112 C  CA  . VAL J  1 62  ? -7.513  43.393  26.839 1.00 54.29  ? 53  VAL J CA  1 
ATOM   16113 C  C   . VAL J  1 62  ? -8.299  43.033  25.580 1.00 58.64  ? 53  VAL J C   1 
ATOM   16114 O  O   . VAL J  1 62  ? -8.981  43.885  25.001 1.00 54.91  ? 53  VAL J O   1 
ATOM   16115 C  CB  . VAL J  1 62  ? -8.481  43.648  28.028 1.00 50.66  ? 53  VAL J CB  1 
ATOM   16116 C  CG1 . VAL J  1 62  ? -9.538  42.560  28.098 1.00 56.70  ? 53  VAL J CG1 1 
ATOM   16117 C  CG2 . VAL J  1 62  ? -7.715  43.701  29.346 1.00 51.05  ? 53  VAL J CG2 1 
ATOM   16118 N  N   . TYR J  1 63  ? -8.187  41.774  25.151 1.00 62.56  ? 54  TYR J N   1 
ATOM   16119 C  CA  . TYR J  1 63  ? -8.858  41.297  23.938 1.00 55.84  ? 54  TYR J CA  1 
ATOM   16120 C  C   . TYR J  1 63  ? -9.143  39.809  23.956 1.00 57.46  ? 54  TYR J C   1 
ATOM   16121 O  O   . TYR J  1 63  ? -8.575  39.056  24.735 1.00 55.18  ? 54  TYR J O   1 
ATOM   16122 C  CB  . TYR J  1 63  ? -8.004  41.579  22.716 1.00 53.17  ? 54  TYR J CB  1 
ATOM   16123 C  CG  . TYR J  1 63  ? -6.644  40.934  22.774 1.00 54.09  ? 54  TYR J CG  1 
ATOM   16124 C  CD1 . TYR J  1 63  ? -6.425  39.659  22.271 1.00 50.66  ? 54  TYR J CD1 1 
ATOM   16125 C  CD2 . TYR J  1 63  ? -5.579  41.607  23.323 1.00 56.14  ? 54  TYR J CD2 1 
ATOM   16126 C  CE1 . TYR J  1 63  ? -5.177  39.084  22.317 1.00 52.15  ? 54  TYR J CE1 1 
ATOM   16127 C  CE2 . TYR J  1 63  ? -4.335  41.048  23.373 1.00 61.68  ? 54  TYR J CE2 1 
ATOM   16128 C  CZ  . TYR J  1 63  ? -4.131  39.788  22.874 1.00 61.27  ? 54  TYR J CZ  1 
ATOM   16129 O  OH  . TYR J  1 63  ? -2.860  39.259  22.963 1.00 62.80  ? 54  TYR J OH  1 
ATOM   16130 N  N   . TRP J  1 64  ? -10.029 39.389  23.069 1.00 60.32  ? 55  TRP J N   1 
ATOM   16131 C  CA  . TRP J  1 64  ? -10.180 37.978  22.756 1.00 59.23  ? 55  TRP J CA  1 
ATOM   16132 C  C   . TRP J  1 64  ? -9.378  37.653  21.509 1.00 58.02  ? 55  TRP J C   1 
ATOM   16133 O  O   . TRP J  1 64  ? -9.259  38.465  20.595 1.00 51.31  ? 55  TRP J O   1 
ATOM   16134 C  CB  . TRP J  1 64  ? -11.634 37.650  22.525 1.00 61.34  ? 55  TRP J CB  1 
ATOM   16135 C  CG  . TRP J  1 64  ? -12.470 38.016  23.663 1.00 64.09  ? 55  TRP J CG  1 
ATOM   16136 C  CD1 . TRP J  1 64  ? -12.069 38.177  24.965 1.00 64.07  ? 55  TRP J CD1 1 
ATOM   16137 C  CD2 . TRP J  1 64  ? -13.874 38.286  23.633 1.00 65.42  ? 55  TRP J CD2 1 
ATOM   16138 N  NE1 . TRP J  1 64  ? -13.151 38.512  25.747 1.00 69.44  ? 55  TRP J NE1 1 
ATOM   16139 C  CE2 . TRP J  1 64  ? -14.267 38.587  24.951 1.00 72.78  ? 55  TRP J CE2 1 
ATOM   16140 C  CE3 . TRP J  1 64  ? -14.836 38.291  22.624 1.00 66.80  ? 55  TRP J CE3 1 
ATOM   16141 C  CZ2 . TRP J  1 64  ? -15.589 38.895  25.274 1.00 69.89  ? 55  TRP J CZ2 1 
ATOM   16142 C  CZ3 . TRP J  1 64  ? -16.139 38.597  22.953 1.00 67.17  ? 55  TRP J CZ3 1 
ATOM   16143 C  CH2 . TRP J  1 64  ? -16.502 38.891  24.262 1.00 67.98  ? 55  TRP J CH2 1 
ATOM   16144 N  N   . GLU J  1 65  ? -8.795  36.469  21.498 1.00 57.52  ? 56  GLU J N   1 
ATOM   16145 C  CA  . GLU J  1 65  ? -8.031  36.029  20.359 1.00 52.79  ? 56  GLU J CA  1 
ATOM   16146 C  C   . GLU J  1 65  ? -8.562  34.680  19.961 1.00 57.61  ? 56  GLU J C   1 
ATOM   16147 O  O   . GLU J  1 65  ? -8.444  33.718  20.715 1.00 57.29  ? 56  GLU J O   1 
ATOM   16148 C  CB  . GLU J  1 65  ? -6.567  35.916  20.728 1.00 49.78  ? 56  GLU J CB  1 
ATOM   16149 C  CG  . GLU J  1 65  ? -5.774  35.134  19.745 1.00 57.15  ? 56  GLU J CG  1 
ATOM   16150 C  CD  . GLU J  1 65  ? -4.305  35.290  19.976 1.00 63.69  ? 56  GLU J CD  1 
ATOM   16151 O  OE1 . GLU J  1 65  ? -3.948  35.979  20.949 1.00 65.53  ? 56  GLU J OE1 1 
ATOM   16152 O  OE2 . GLU J  1 65  ? -3.509  34.740  19.187 1.00 67.79  ? 56  GLU J OE2 1 
ATOM   16153 N  N   . GLN J  1 66  ? -9.166  34.612  18.780 1.00 60.61  ? 57  GLN J N   1 
ATOM   16154 C  CA  . GLN J  1 66  ? -9.695  33.355  18.289 1.00 57.05  ? 57  GLN J CA  1 
ATOM   16155 C  C   . GLN J  1 66  ? -8.618  32.700  17.466 1.00 53.31  ? 57  GLN J C   1 
ATOM   16156 O  O   . GLN J  1 66  ? -7.993  33.333  16.625 1.00 55.24  ? 57  GLN J O   1 
ATOM   16157 C  CB  . GLN J  1 66  ? -10.969 33.561  17.470 1.00 60.26  ? 57  GLN J CB  1 
ATOM   16158 C  CG  . GLN J  1 66  ? -11.904 32.350  17.470 1.00 65.70  ? 57  GLN J CG  1 
ATOM   16159 C  CD  . GLN J  1 66  ? -12.676 32.182  16.159 1.00 72.38  ? 57  GLN J CD  1 
ATOM   16160 O  OE1 . GLN J  1 66  ? -12.126 32.378  15.069 1.00 80.37  ? 57  GLN J OE1 1 
ATOM   16161 N  NE2 . GLN J  1 66  ? -13.953 31.819  16.264 1.00 60.56  ? 57  GLN J NE2 1 
ATOM   16162 N  N   . GLN J  1 67  ? -8.383  31.431  17.759 1.00 56.38  ? 58  GLN J N   1 
ATOM   16163 C  CA  . GLN J  1 67  ? -7.466  30.598  16.993 1.00 64.78  ? 58  GLN J CA  1 
ATOM   16164 C  C   . GLN J  1 67  ? -8.227  29.394  16.456 1.00 61.71  ? 58  GLN J C   1 
ATOM   16165 O  O   . GLN J  1 67  ? -8.910  28.705  17.218 1.00 62.61  ? 58  GLN J O   1 
ATOM   16166 C  CB  . GLN J  1 67  ? -6.308  30.132  17.874 1.00 62.74  ? 58  GLN J CB  1 
ATOM   16167 C  CG  . GLN J  1 67  ? -5.549  31.280  18.505 1.00 64.41  ? 58  GLN J CG  1 
ATOM   16168 C  CD  . GLN J  1 67  ? -4.409  30.805  19.362 1.00 64.37  ? 58  GLN J CD  1 
ATOM   16169 O  OE1 . GLN J  1 67  ? -4.156  29.609  19.454 1.00 72.44  ? 58  GLN J OE1 1 
ATOM   16170 N  NE2 . GLN J  1 67  ? -3.713  31.736  20.001 1.00 61.18  ? 58  GLN J NE2 1 
ATOM   16171 N  N   . SER J  1 68  ? -8.129  29.158  15.149 1.00 56.87  ? 59  SER J N   1 
ATOM   16172 C  CA  . SER J  1 68  ? -8.776  28.003  14.548 1.00 57.16  ? 59  SER J CA  1 
ATOM   16173 C  C   . SER J  1 68  ? -7.777  27.217  13.747 1.00 58.32  ? 59  SER J C   1 
ATOM   16174 O  O   . SER J  1 68  ? -6.903  27.782  13.091 1.00 58.84  ? 59  SER J O   1 
ATOM   16175 C  CB  . SER J  1 68  ? -9.923  28.425  13.639 1.00 63.23  ? 59  SER J CB  1 
ATOM   16176 O  OG  . SER J  1 68  ? -10.673 29.463  14.238 1.00 75.54  ? 59  SER J OG  1 
ATOM   16177 N  N   . TRP J  1 69  ? -7.903  25.902  13.821 1.00 53.79  ? 60  TRP J N   1 
ATOM   16178 C  CA  . TRP J  1 69  ? -7.180  25.040  12.910 1.00 56.29  ? 60  TRP J CA  1 
ATOM   16179 C  C   . TRP J  1 69  ? -7.905  23.699  12.739 1.00 54.33  ? 60  TRP J C   1 
ATOM   16180 O  O   . TRP J  1 69  ? -8.906  23.431  13.392 1.00 51.32  ? 60  TRP J O   1 
ATOM   16181 C  CB  . TRP J  1 69  ? -5.729  24.859  13.387 1.00 59.83  ? 60  TRP J CB  1 
ATOM   16182 C  CG  . TRP J  1 69  ? -5.586  24.150  14.715 1.00 57.55  ? 60  TRP J CG  1 
ATOM   16183 C  CD1 . TRP J  1 69  ? -5.382  22.819  14.910 1.00 48.74  ? 60  TRP J CD1 1 
ATOM   16184 C  CD2 . TRP J  1 69  ? -5.633  24.742  16.020 1.00 55.02  ? 60  TRP J CD2 1 
ATOM   16185 N  NE1 . TRP J  1 69  ? -5.306  22.546  16.246 1.00 50.54  ? 60  TRP J NE1 1 
ATOM   16186 C  CE2 . TRP J  1 69  ? -5.458  23.709  16.950 1.00 54.55  ? 60  TRP J CE2 1 
ATOM   16187 C  CE3 . TRP J  1 69  ? -5.805  26.046  16.488 1.00 58.35  ? 60  TRP J CE3 1 
ATOM   16188 C  CZ2 . TRP J  1 69  ? -5.451  23.938  18.318 1.00 50.17  ? 60  TRP J CZ2 1 
ATOM   16189 C  CZ3 . TRP J  1 69  ? -5.791  26.271  17.845 1.00 51.39  ? 60  TRP J CZ3 1 
ATOM   16190 C  CH2 . TRP J  1 69  ? -5.622  25.224  18.742 1.00 48.30  ? 60  TRP J CH2 1 
ATOM   16191 N  N   . LYS J  1 70  ? -7.395  22.853  11.859 1.00 58.53  ? 61  LYS J N   1 
ATOM   16192 C  CA  . LYS J  1 70  ? -8.043  21.582  11.610 1.00 59.23  ? 61  LYS J CA  1 
ATOM   16193 C  C   . LYS J  1 70  ? -7.026  20.452  11.569 1.00 61.36  ? 61  LYS J C   1 
ATOM   16194 O  O   . LYS J  1 70  ? -5.998  20.528  10.895 1.00 61.04  ? 61  LYS J O   1 
ATOM   16195 C  CB  . LYS J  1 70  ? -8.861  21.616  10.326 1.00 57.79  ? 61  LYS J CB  1 
ATOM   16196 C  CG  . LYS J  1 70  ? -9.322  20.237  9.892  1.00 68.00  ? 61  LYS J CG  1 
ATOM   16197 C  CD  . LYS J  1 70  ? -10.353 20.289  8.770  1.00 82.10  ? 61  LYS J CD  1 
ATOM   16198 C  CE  . LYS J  1 70  ? -10.641 18.896  8.213  1.00 84.74  ? 61  LYS J CE  1 
ATOM   16199 N  NZ  . LYS J  1 70  ? -9.401  18.232  7.711  1.00 82.77  ? 61  LYS J NZ  1 
ATOM   16200 N  N   . LEU J  1 71  ? -7.341  19.389  12.283 1.00 60.77  ? 62  LEU J N   1 
ATOM   16201 C  CA  . LEU J  1 71  ? -6.476  18.244  12.334 1.00 63.08  ? 62  LEU J CA  1 
ATOM   16202 C  C   . LEU J  1 71  ? -7.167  16.994  11.869 1.00 69.23  ? 62  LEU J C   1 
ATOM   16203 O  O   . LEU J  1 71  ? -8.305  16.773  12.181 1.00 76.50  ? 62  LEU J O   1 
ATOM   16204 C  CB  . LEU J  1 71  ? -5.976  18.032  13.747 1.00 63.98  ? 62  LEU J CB  1 
ATOM   16205 C  CG  . LEU J  1 71  ? -4.546  18.473  13.871 1.00 52.70  ? 62  LEU J CG  1 
ATOM   16206 C  CD1 . LEU J  1 71  ? -4.449  19.914  13.683 1.00 63.33  ? 62  LEU J CD1 1 
ATOM   16207 C  CD2 . LEU J  1 71  ? -4.090  18.115  15.217 1.00 63.67  ? 62  LEU J CD2 1 
ATOM   16208 N  N   . ASN J  1 72  ? -6.475  16.167  11.111 1.00 67.90  ? 63  ASN J N   1 
ATOM   16209 C  CA  . ASN J  1 72  ? -7.077  14.907  10.682 1.00 68.93  ? 63  ASN J CA  1 
ATOM   16210 C  C   . ASN J  1 72  ? -7.170  13.974  11.872 1.00 66.26  ? 63  ASN J C   1 
ATOM   16211 O  O   . ASN J  1 72  ? -8.156  13.270  12.048 1.00 71.52  ? 63  ASN J O   1 
ATOM   16212 C  CB  . ASN J  1 72  ? -6.299  14.274  9.526  1.00 70.48  ? 63  ASN J CB  1 
ATOM   16213 C  CG  . ASN J  1 72  ? -6.556  14.973  8.209  1.00 68.69  ? 63  ASN J CG  1 
ATOM   16214 O  OD1 . ASN J  1 72  ? -7.701  15.238  7.859  1.00 69.49  ? 63  ASN J OD1 1 
ATOM   16215 N  ND2 . ASN J  1 72  ? -5.490  15.298  7.485  1.00 61.05  ? 63  ASN J ND2 1 
ATOM   16216 N  N   . SER J  1 73  ? -6.149  14.015  12.715 1.00 63.76  ? 64  SER J N   1 
ATOM   16217 C  CA  . SER J  1 73  ? -6.125  13.209  13.918 1.00 63.94  ? 64  SER J CA  1 
ATOM   16218 C  C   . SER J  1 73  ? -7.398  13.372  14.747 1.00 67.82  ? 64  SER J C   1 
ATOM   16219 O  O   . SER J  1 73  ? -7.841  12.416  15.380 1.00 68.67  ? 64  SER J O   1 
ATOM   16220 C  CB  . SER J  1 73  ? -4.897  13.560  14.753 1.00 65.34  ? 64  SER J CB  1 
ATOM   16221 O  OG  . SER J  1 73  ? -3.924  14.211  13.952 1.00 60.27  ? 64  SER J OG  1 
ATOM   16222 N  N   . LEU J  1 74  ? -7.985  14.572  14.733 1.00 63.90  ? 65  LEU J N   1 
ATOM   16223 C  CA  . LEU J  1 74  ? -9.121  14.906  15.603 1.00 65.43  ? 65  LEU J CA  1 
ATOM   16224 C  C   . LEU J  1 74  ? -10.504 14.659  15.006 1.00 67.01  ? 65  LEU J C   1 
ATOM   16225 O  O   . LEU J  1 74  ? -11.525 14.951  15.648 1.00 64.30  ? 65  LEU J O   1 
ATOM   16226 C  CB  . LEU J  1 74  ? -9.023  16.361  16.051 1.00 69.46  ? 65  LEU J CB  1 
ATOM   16227 C  CG  . LEU J  1 74  ? -7.789  16.680  16.883 1.00 63.58  ? 65  LEU J CG  1 
ATOM   16228 C  CD1 . LEU J  1 74  ? -7.730  18.154  17.220 1.00 63.78  ? 65  LEU J CD1 1 
ATOM   16229 C  CD2 . LEU J  1 74  ? -7.809  15.842  18.131 1.00 51.16  ? 65  LEU J CD2 1 
ATOM   16230 N  N   . MET J  1 75  ? -10.527 14.131  13.782 1.00 68.68  ? 66  MET J N   1 
ATOM   16231 C  CA  . MET J  1 75  ? -11.765 13.796  13.089 1.00 62.92  ? 66  MET J CA  1 
ATOM   16232 C  C   . MET J  1 75  ? -12.362 12.507  13.626 1.00 65.17  ? 66  MET J C   1 
ATOM   16233 O  O   . MET J  1 75  ? -11.651 11.640  14.147 1.00 63.77  ? 66  MET J O   1 
ATOM   16234 C  CB  . MET J  1 75  ? -11.495 13.612  11.608 1.00 61.25  ? 66  MET J CB  1 
ATOM   16235 C  CG  . MET J  1 75  ? -10.838 14.793  10.950 1.00 71.96  ? 66  MET J CG  1 
ATOM   16236 S  SD  . MET J  1 75  ? -10.672 14.500  9.188  1.00 81.35  ? 66  MET J SD  1 
ATOM   16237 C  CE  . MET J  1 75  ? -12.275 13.752  8.879  1.00 70.96  ? 66  MET J CE  1 
ATOM   16238 N  N   . TRP J  1 76  ? -13.678 12.390  13.511 1.00 60.19  ? 67  TRP J N   1 
ATOM   16239 C  CA  . TRP J  1 76  ? -14.360 11.146  13.840 1.00 69.30  ? 67  TRP J CA  1 
ATOM   16240 C  C   . TRP J  1 76  ? -15.699 11.064  13.095 1.00 71.94  ? 67  TRP J C   1 
ATOM   16241 O  O   . TRP J  1 76  ? -16.242 12.076  12.634 1.00 64.33  ? 67  TRP J O   1 
ATOM   16242 C  CB  . TRP J  1 76  ? -14.541 10.956  15.368 1.00 61.54  ? 67  TRP J CB  1 
ATOM   16243 C  CG  . TRP J  1 76  ? -15.557 11.870  15.970 1.00 62.95  ? 67  TRP J CG  1 
ATOM   16244 C  CD1 . TRP J  1 76  ? -16.888 11.626  16.147 1.00 62.90  ? 67  TRP J CD1 1 
ATOM   16245 C  CD2 . TRP J  1 76  ? -15.324 13.192  16.453 1.00 63.46  ? 67  TRP J CD2 1 
ATOM   16246 N  NE1 . TRP J  1 76  ? -17.498 12.720  16.707 1.00 61.05  ? 67  TRP J NE1 1 
ATOM   16247 C  CE2 . TRP J  1 76  ? -16.558 13.693  16.905 1.00 59.21  ? 67  TRP J CE2 1 
ATOM   16248 C  CE3 . TRP J  1 76  ? -14.188 14.003  16.545 1.00 59.89  ? 67  TRP J CE3 1 
ATOM   16249 C  CZ2 . TRP J  1 76  ? -16.683 14.962  17.445 1.00 56.68  ? 67  TRP J CZ2 1 
ATOM   16250 C  CZ3 . TRP J  1 76  ? -14.318 15.256  17.069 1.00 54.74  ? 67  TRP J CZ3 1 
ATOM   16251 C  CH2 . TRP J  1 76  ? -15.554 15.724  17.521 1.00 55.95  ? 67  TRP J CH2 1 
ATOM   16252 N  N   . ASP J  1 77  ? -16.203 9.839   12.968 1.00 76.29  ? 68  ASP J N   1 
ATOM   16253 C  CA  . ASP J  1 77  ? -17.530 9.587   12.438 1.00 77.46  ? 68  ASP J CA  1 
ATOM   16254 C  C   . ASP J  1 77  ? -18.505 9.625   13.614 1.00 71.71  ? 68  ASP J C   1 
ATOM   16255 O  O   . ASP J  1 77  ? -18.465 8.754   14.488 1.00 70.38  ? 68  ASP J O   1 
ATOM   16256 C  CB  . ASP J  1 77  ? -17.540 8.221   11.731 1.00 86.25  ? 68  ASP J CB  1 
ATOM   16257 C  CG  . ASP J  1 77  ? -18.913 7.824   11.204 1.00 82.07  ? 68  ASP J CG  1 
ATOM   16258 O  OD1 . ASP J  1 77  ? -19.762 8.714   10.957 1.00 78.04  ? 68  ASP J OD1 1 
ATOM   16259 O  OD2 . ASP J  1 77  ? -19.127 6.602   11.029 1.00 79.76  ? 68  ASP J OD2 1 
ATOM   16260 N  N   . PRO J  1 78  ? -19.365 10.655  13.647 1.00 61.30  ? 69  PRO J N   1 
ATOM   16261 C  CA  . PRO J  1 78  ? -20.384 10.844  14.676 1.00 63.25  ? 69  PRO J CA  1 
ATOM   16262 C  C   . PRO J  1 78  ? -21.248 9.608   14.879 1.00 70.65  ? 69  PRO J C   1 
ATOM   16263 O  O   . PRO J  1 78  ? -21.734 9.380   15.980 1.00 72.23  ? 69  PRO J O   1 
ATOM   16264 C  CB  . PRO J  1 78  ? -21.230 11.973  14.103 1.00 61.26  ? 69  PRO J CB  1 
ATOM   16265 C  CG  . PRO J  1 78  ? -20.278 12.767  13.335 1.00 60.08  ? 69  PRO J CG  1 
ATOM   16266 C  CD  . PRO J  1 78  ? -19.330 11.789  12.715 1.00 60.48  ? 69  PRO J CD  1 
ATOM   16267 N  N   . ASN J  1 79  ? -21.448 8.820   13.832 1.00 75.70  ? 70  ASN J N   1 
ATOM   16268 C  CA  . ASN J  1 79  ? -22.245 7.609   13.954 1.00 73.43  ? 70  ASN J CA  1 
ATOM   16269 C  C   . ASN J  1 79  ? -21.617 6.588   14.882 1.00 72.25  ? 70  ASN J C   1 
ATOM   16270 O  O   . ASN J  1 79  ? -22.310 5.974   15.688 1.00 69.89  ? 70  ASN J O   1 
ATOM   16271 C  CB  . ASN J  1 79  ? -22.488 6.984   12.586 1.00 81.02  ? 70  ASN J CB  1 
ATOM   16272 C  CG  . ASN J  1 79  ? -23.680 7.569   11.898 1.00 81.13  ? 70  ASN J CG  1 
ATOM   16273 O  OD1 . ASN J  1 79  ? -23.730 7.644   10.666 1.00 94.51  ? 70  ASN J OD1 1 
ATOM   16274 N  ND2 . ASN J  1 79  ? -24.660 7.988   12.684 1.00 73.39  ? 70  ASN J ND2 1 
ATOM   16275 N  N   . GLU J  1 80  ? -20.308 6.398   14.758 1.00 73.67  ? 71  GLU J N   1 
ATOM   16276 C  CA  . GLU J  1 80  ? -19.588 5.513   15.664 1.00 73.96  ? 71  GLU J CA  1 
ATOM   16277 C  C   . GLU J  1 80  ? -19.804 5.949   17.119 1.00 71.81  ? 71  GLU J C   1 
ATOM   16278 O  O   . GLU J  1 80  ? -19.753 5.144   18.049 1.00 72.53  ? 71  GLU J O   1 
ATOM   16279 C  CB  . GLU J  1 80  ? -18.087 5.534   15.351 1.00 78.01  ? 71  GLU J CB  1 
ATOM   16280 C  CG  . GLU J  1 80  ? -17.624 4.559   14.276 1.00 89.84  ? 71  GLU J CG  1 
ATOM   16281 C  CD  . GLU J  1 80  ? -16.201 4.033   14.519 1.00 97.18  ? 71  GLU J CD  1 
ATOM   16282 O  OE1 . GLU J  1 80  ? -15.677 4.156   15.652 1.00 87.63  ? 71  GLU J OE1 1 
ATOM   16283 O  OE2 . GLU J  1 80  ? -15.607 3.483   13.568 1.00 103.83 ? 71  GLU J OE2 1 
ATOM   16284 N  N   . TYR J  1 81  ? -20.033 7.230   17.300 1.00 71.85  ? 72  TYR J N   1 
ATOM   16285 C  CA  . TYR J  1 81  ? -20.065 7.799   18.628 1.00 75.40  ? 72  TYR J CA  1 
ATOM   16286 C  C   . TYR J  1 81  ? -21.377 8.305   19.191 1.00 76.49  ? 72  TYR J C   1 
ATOM   16287 O  O   . TYR J  1 81  ? -21.380 9.074   20.109 1.00 77.36  ? 72  TYR J O   1 
ATOM   16288 C  CB  . TYR J  1 81  ? -18.964 8.823   18.753 1.00 71.09  ? 72  TYR J CB  1 
ATOM   16289 C  CG  . TYR J  1 81  ? -17.626 8.217   18.502 1.00 69.32  ? 72  TYR J CG  1 
ATOM   16290 C  CD1 . TYR J  1 81  ? -16.964 7.571   19.489 1.00 58.38  ? 72  TYR J CD1 1 
ATOM   16291 C  CD2 . TYR J  1 81  ? -17.035 8.274   17.279 1.00 75.07  ? 72  TYR J CD2 1 
ATOM   16292 C  CE1 . TYR J  1 81  ? -15.760 7.013   19.282 1.00 61.94  ? 72  TYR J CE1 1 
ATOM   16293 C  CE2 . TYR J  1 81  ? -15.809 7.717   17.074 1.00 76.39  ? 72  TYR J CE2 1 
ATOM   16294 C  CZ  . TYR J  1 81  ? -15.184 7.088   18.086 1.00 66.76  ? 72  TYR J CZ  1 
ATOM   16295 O  OH  . TYR J  1 81  ? -13.963 6.519   17.923 1.00 67.13  ? 72  TYR J OH  1 
ATOM   16296 N  N   . GLY J  1 82  ? -22.492 7.882   18.642 1.00 73.00  ? 73  GLY J N   1 
ATOM   16297 C  CA  . GLY J  1 82  ? -23.776 8.249   19.204 1.00 73.16  ? 73  GLY J CA  1 
ATOM   16298 C  C   . GLY J  1 82  ? -24.100 9.681   18.852 1.00 75.14  ? 73  GLY J C   1 
ATOM   16299 O  O   . GLY J  1 82  ? -24.531 10.470  19.692 1.00 74.23  ? 73  GLY J O   1 
ATOM   16300 N  N   . ASN J  1 83  ? -23.846 10.009  17.591 1.00 74.98  ? 74  ASN J N   1 
ATOM   16301 C  CA  A ASN J  1 83  ? -24.161 11.309  17.028 0.60 77.27  ? 74  ASN J CA  1 
ATOM   16302 C  CA  B ASN J  1 83  ? -24.182 11.330  17.046 0.40 77.22  ? 74  ASN J CA  1 
ATOM   16303 C  C   . ASN J  1 83  ? -23.637 12.472  17.888 1.00 75.32  ? 74  ASN J C   1 
ATOM   16304 O  O   . ASN J  1 83  ? -24.371 13.386  18.260 1.00 76.04  ? 74  ASN J O   1 
ATOM   16305 C  CB  A ASN J  1 83  ? -25.663 11.386  16.713 0.60 81.18  ? 74  ASN J CB  1 
ATOM   16306 C  CB  B ASN J  1 83  ? -25.700 11.492  16.848 0.40 81.03  ? 74  ASN J CB  1 
ATOM   16307 C  CG  A ASN J  1 83  ? -26.148 10.193  15.865 0.60 76.12  ? 74  ASN J CG  1 
ATOM   16308 C  CG  B ASN J  1 83  ? -26.090 12.890  16.341 0.40 79.05  ? 74  ASN J CG  1 
ATOM   16309 O  OD1 A ASN J  1 83  ? -25.483 9.776   14.912 0.60 70.56  ? 74  ASN J OD1 1 
ATOM   16310 O  OD1 B ASN J  1 83  ? -25.240 13.671  15.907 0.40 73.03  ? 74  ASN J OD1 1 
ATOM   16311 N  ND2 A ASN J  1 83  ? -27.303 9.639   16.225 0.60 71.00  ? 74  ASN J ND2 1 
ATOM   16312 N  ND2 B ASN J  1 83  ? -27.383 13.202  16.401 0.40 75.60  ? 74  ASN J ND2 1 
ATOM   16313 N  N   . ILE J  1 84  ? -22.344 12.404  18.189 1.00 73.41  ? 75  ILE J N   1 
ATOM   16314 C  CA  . ILE J  1 84  ? -21.651 13.452  18.915 1.00 70.92  ? 75  ILE J CA  1 
ATOM   16315 C  C   . ILE J  1 84  ? -20.835 14.251  17.899 1.00 69.68  ? 75  ILE J C   1 
ATOM   16316 O  O   . ILE J  1 84  ? -19.904 13.724  17.277 1.00 64.45  ? 75  ILE J O   1 
ATOM   16317 C  CB  . ILE J  1 84  ? -20.734 12.860  20.006 1.00 69.37  ? 75  ILE J CB  1 
ATOM   16318 C  CG1 . ILE J  1 84  ? -21.571 12.267  21.137 1.00 62.88  ? 75  ILE J CG1 1 
ATOM   16319 C  CG2 . ILE J  1 84  ? -19.783 13.919  20.558 1.00 68.70  ? 75  ILE J CG2 1 
ATOM   16320 C  CD1 . ILE J  1 84  ? -20.743 11.831  22.320 1.00 71.33  ? 75  ILE J CD1 1 
ATOM   16321 N  N   . THR J  1 85  ? -21.255 15.489  17.658 1.00 70.79  ? 76  THR J N   1 
ATOM   16322 C  CA  . THR J  1 85  ? -20.584 16.318  16.665 1.00 69.50  ? 76  THR J CA  1 
ATOM   16323 C  C   . THR J  1 85  ? -19.482 17.248  17.172 1.00 67.20  ? 76  THR J C   1 
ATOM   16324 O  O   . THR J  1 85  ? -18.684 17.752  16.384 1.00 65.89  ? 76  THR J O   1 
ATOM   16325 C  CB  . THR J  1 85  ? -21.624 17.109  15.866 1.00 69.29  ? 76  THR J CB  1 
ATOM   16326 O  OG1 . THR J  1 85  ? -22.399 17.916  16.763 1.00 63.44  ? 76  THR J OG1 1 
ATOM   16327 C  CG2 . THR J  1 85  ? -22.552 16.137  15.144 1.00 58.80  ? 76  THR J CG2 1 
ATOM   16328 N  N   . ASP J  1 86  ? -19.428 17.471  18.481 1.00 66.97  ? 77  ASP J N   1 
ATOM   16329 C  CA  . ASP J  1 86  ? -18.359 18.284  19.066 1.00 63.99  ? 77  ASP J CA  1 
ATOM   16330 C  C   . ASP J  1 86  ? -18.210 18.064  20.567 1.00 62.72  ? 77  ASP J C   1 
ATOM   16331 O  O   . ASP J  1 86  ? -19.110 17.532  21.200 1.00 64.98  ? 77  ASP J O   1 
ATOM   16332 C  CB  . ASP J  1 86  ? -18.538 19.764  18.738 1.00 66.62  ? 77  ASP J CB  1 
ATOM   16333 C  CG  . ASP J  1 86  ? -19.890 20.282  19.138 1.00 79.46  ? 77  ASP J CG  1 
ATOM   16334 O  OD1 . ASP J  1 86  ? -20.358 19.928  20.245 1.00 79.36  ? 77  ASP J OD1 1 
ATOM   16335 O  OD2 . ASP J  1 86  ? -20.488 21.033  18.334 1.00 87.66  ? 77  ASP J OD2 1 
ATOM   16336 N  N   . PHE J  1 87  ? -17.077 18.470  21.133 1.00 59.45  ? 78  PHE J N   1 
ATOM   16337 C  CA  . PHE J  1 87  ? -16.903 18.445  22.582 1.00 55.95  ? 78  PHE J CA  1 
ATOM   16338 C  C   . PHE J  1 87  ? -15.931 19.517  23.051 1.00 55.88  ? 78  PHE J C   1 
ATOM   16339 O  O   . PHE J  1 87  ? -15.036 19.921  22.315 1.00 54.14  ? 78  PHE J O   1 
ATOM   16340 C  CB  . PHE J  1 87  ? -16.397 17.074  23.034 1.00 55.32  ? 78  PHE J CB  1 
ATOM   16341 C  CG  . PHE J  1 87  ? -15.030 16.739  22.517 1.00 57.41  ? 78  PHE J CG  1 
ATOM   16342 C  CD1 . PHE J  1 87  ? -13.901 16.976  23.296 1.00 53.85  ? 78  PHE J CD1 1 
ATOM   16343 C  CD2 . PHE J  1 87  ? -14.871 16.199  21.236 1.00 56.93  ? 78  PHE J CD2 1 
ATOM   16344 C  CE1 . PHE J  1 87  ? -12.638 16.676  22.819 1.00 54.67  ? 78  PHE J CE1 1 
ATOM   16345 C  CE2 . PHE J  1 87  ? -13.617 15.897  20.742 1.00 47.23  ? 78  PHE J CE2 1 
ATOM   16346 C  CZ  . PHE J  1 87  ? -12.493 16.135  21.536 1.00 57.57  ? 78  PHE J CZ  1 
ATOM   16347 N  N   . ARG J  1 88  ? -16.103 19.956  24.294 1.00 60.95  ? 79  ARG J N   1 
ATOM   16348 C  CA  . ARG J  1 88  ? -15.160 20.870  24.934 1.00 58.02  ? 79  ARG J CA  1 
ATOM   16349 C  C   . ARG J  1 88  ? -14.029 20.089  25.600 1.00 54.16  ? 79  ARG J C   1 
ATOM   16350 O  O   . ARG J  1 88  ? -14.253 19.016  26.143 1.00 59.54  ? 79  ARG J O   1 
ATOM   16351 C  CB  . ARG J  1 88  ? -15.877 21.727  25.966 1.00 58.75  ? 79  ARG J CB  1 
ATOM   16352 C  CG  . ARG J  1 88  ? -16.652 22.867  25.371 1.00 62.27  ? 79  ARG J CG  1 
ATOM   16353 C  CD  . ARG J  1 88  ? -17.997 22.442  24.851 1.00 68.14  ? 79  ARG J CD  1 
ATOM   16354 N  NE  . ARG J  1 88  ? -18.736 23.595  24.338 1.00 76.45  ? 79  ARG J NE  1 
ATOM   16355 C  CZ  . ARG J  1 88  ? -19.888 23.524  23.669 1.00 81.58  ? 79  ARG J CZ  1 
ATOM   16356 N  NH1 . ARG J  1 88  ? -20.447 22.344  23.418 1.00 86.35  ? 79  ARG J NH1 1 
ATOM   16357 N  NH2 . ARG J  1 88  ? -20.482 24.635  23.246 1.00 71.52  ? 79  ARG J NH2 1 
ATOM   16358 N  N   . THR J  1 89  ? -12.812 20.614  25.541 1.00 51.74  ? 80  THR J N   1 
ATOM   16359 C  CA  . THR J  1 89  ? -11.679 19.950  26.172 1.00 58.32  ? 80  THR J CA  1 
ATOM   16360 C  C   . THR J  1 89  ? -10.704 20.969  26.721 1.00 62.54  ? 80  THR J C   1 
ATOM   16361 O  O   . THR J  1 89  ? -10.652 22.103  26.244 1.00 63.83  ? 80  THR J O   1 
ATOM   16362 C  CB  . THR J  1 89  ? -10.885 19.127  25.191 1.00 62.77  ? 80  THR J CB  1 
ATOM   16363 O  OG1 . THR J  1 89  ? -9.792  18.511  25.887 1.00 68.49  ? 80  THR J OG1 1 
ATOM   16364 C  CG2 . THR J  1 89  ? -10.328 20.035  24.096 1.00 55.18  ? 80  THR J CG2 1 
ATOM   16365 N  N   . SER J  1 90  ? -9.928  20.576  27.724 1.00 58.50  ? 81  SER J N   1 
ATOM   16366 C  CA  A SER J  1 90  ? -8.904  21.460  28.257 0.30 59.63  ? 81  SER J CA  1 
ATOM   16367 C  CA  B SER J  1 90  ? -8.898  21.453  28.244 0.70 59.56  ? 81  SER J CA  1 
ATOM   16368 C  C   . SER J  1 90  ? -7.837  21.670  27.192 1.00 60.35  ? 81  SER J C   1 
ATOM   16369 O  O   . SER J  1 90  ? -7.453  20.734  26.506 1.00 61.54  ? 81  SER J O   1 
ATOM   16370 C  CB  A SER J  1 90  ? -8.272  20.856  29.508 0.30 60.30  ? 81  SER J CB  1 
ATOM   16371 C  CB  B SER J  1 90  ? -8.242  20.851  29.466 0.70 60.24  ? 81  SER J CB  1 
ATOM   16372 O  OG  A SER J  1 90  ? -9.207  20.786  30.576 0.30 63.87  ? 81  SER J OG  1 
ATOM   16373 O  OG  B SER J  1 90  ? -6.985  21.465  29.665 0.70 53.65  ? 81  SER J OG  1 
ATOM   16374 N  N   . ALA J  1 91  ? -7.356  22.900  27.065 1.00 57.91  ? 82  ALA J N   1 
ATOM   16375 C  CA  . ALA J  1 91  ? -6.351  23.210  26.058 1.00 58.55  ? 82  ALA J CA  1 
ATOM   16376 C  C   . ALA J  1 91  ? -5.013  22.508  26.294 1.00 58.58  ? 82  ALA J C   1 
ATOM   16377 O  O   . ALA J  1 91  ? -4.123  22.558  25.450 1.00 59.04  ? 82  ALA J O   1 
ATOM   16378 C  CB  . ALA J  1 91  ? -6.165  24.717  25.933 1.00 56.78  ? 82  ALA J CB  1 
ATOM   16379 N  N   . ALA J  1 92  ? -4.856  21.869  27.445 1.00 61.06  ? 83  ALA J N   1 
ATOM   16380 C  CA  . ALA J  1 92  ? -3.648  21.086  27.677 1.00 68.33  ? 83  ALA J CA  1 
ATOM   16381 C  C   . ALA J  1 92  ? -3.707  19.690  27.031 1.00 68.16  ? 83  ALA J C   1 
ATOM   16382 O  O   . ALA J  1 92  ? -2.673  19.043  26.813 1.00 67.68  ? 83  ALA J O   1 
ATOM   16383 C  CB  . ALA J  1 92  ? -3.374  20.977  29.144 1.00 65.78  ? 83  ALA J CB  1 
ATOM   16384 N  N   . ASP J  1 93  ? -4.919  19.239  26.722 1.00 64.78  ? 84  ASP J N   1 
ATOM   16385 C  CA  . ASP J  1 93  ? -5.133  17.903  26.156 1.00 69.13  ? 84  ASP J CA  1 
ATOM   16386 C  C   . ASP J  1 93  ? -4.803  17.808  24.672 1.00 63.43  ? 84  ASP J C   1 
ATOM   16387 O  O   . ASP J  1 93  ? -4.636  16.713  24.142 1.00 73.30  ? 84  ASP J O   1 
ATOM   16388 C  CB  . ASP J  1 93  ? -6.583  17.428  26.373 1.00 71.00  ? 84  ASP J CB  1 
ATOM   16389 C  CG  . ASP J  1 93  ? -6.985  17.402  27.853 1.00 76.37  ? 84  ASP J CG  1 
ATOM   16390 O  OD1 . ASP J  1 93  ? -6.083  17.425  28.729 1.00 68.25  ? 84  ASP J OD1 1 
ATOM   16391 O  OD2 . ASP J  1 93  ? -8.211  17.359  28.131 1.00 77.00  ? 84  ASP J OD2 1 
ATOM   16392 N  N   . ILE J  1 94  ? -4.711  18.953  24.006 1.00 64.70  ? 85  ILE J N   1 
ATOM   16393 C  CA  . ILE J  1 94  ? -4.508  18.987  22.560 1.00 63.05  ? 85  ILE J CA  1 
ATOM   16394 C  C   . ILE J  1 94  ? -3.256  19.755  22.233 1.00 62.90  ? 85  ILE J C   1 
ATOM   16395 O  O   . ILE J  1 94  ? -2.728  20.490  23.071 1.00 70.32  ? 85  ILE J O   1 
ATOM   16396 C  CB  . ILE J  1 94  ? -5.658  19.707  21.815 1.00 59.04  ? 85  ILE J CB  1 
ATOM   16397 C  CG1 . ILE J  1 94  ? -5.969  21.044  22.506 1.00 56.13  ? 85  ILE J CG1 1 
ATOM   16398 C  CG2 . ILE J  1 94  ? -6.870  18.789  21.668 1.00 55.62  ? 85  ILE J CG2 1 
ATOM   16399 C  CD1 . ILE J  1 94  ? -7.076  21.816  21.920 1.00 44.29  ? 85  ILE J CD1 1 
ATOM   16400 N  N   . TRP J  1 95  ? -2.772  19.571  21.013 1.00 59.76  ? 86  TRP J N   1 
ATOM   16401 C  CA  . TRP J  1 95  ? -1.704  20.402  20.505 1.00 58.58  ? 86  TRP J CA  1 
ATOM   16402 C  C   . TRP J  1 95  ? -2.280  21.781  20.297 1.00 59.09  ? 86  TRP J C   1 
ATOM   16403 O  O   . TRP J  1 95  ? -3.398  21.921  19.801 1.00 54.46  ? 86  TRP J O   1 
ATOM   16404 C  CB  . TRP J  1 95  ? -1.195  19.869  19.176 1.00 57.86  ? 86  TRP J CB  1 
ATOM   16405 C  CG  . TRP J  1 95  ? -0.062  20.652  18.616 1.00 49.75  ? 86  TRP J CG  1 
ATOM   16406 C  CD1 . TRP J  1 95  ? 1.262   20.453  18.853 1.00 56.68  ? 86  TRP J CD1 1 
ATOM   16407 C  CD2 . TRP J  1 95  ? -0.147  21.752  17.720 1.00 46.75  ? 86  TRP J CD2 1 
ATOM   16408 N  NE1 . TRP J  1 95  ? 2.009   21.360  18.155 1.00 59.82  ? 86  TRP J NE1 1 
ATOM   16409 C  CE2 . TRP J  1 95  ? 1.163   22.173  17.451 1.00 47.31  ? 86  TRP J CE2 1 
ATOM   16410 C  CE3 . TRP J  1 95  ? -1.207  22.426  17.117 1.00 54.99  ? 86  TRP J CE3 1 
ATOM   16411 C  CZ2 . TRP J  1 95  ? 1.444   23.237  16.626 1.00 48.36  ? 86  TRP J CZ2 1 
ATOM   16412 C  CZ3 . TRP J  1 95  ? -0.928  23.479  16.282 1.00 52.73  ? 86  TRP J CZ3 1 
ATOM   16413 C  CH2 . TRP J  1 95  ? 0.386   23.879  16.047 1.00 53.06  ? 86  TRP J CH2 1 
ATOM   16414 N  N   . THR J  1 96  ? -1.526  22.797  20.698 1.00 56.64  ? 87  THR J N   1 
ATOM   16415 C  CA  . THR J  1 96  ? -1.906  24.162  20.410 1.00 51.92  ? 87  THR J CA  1 
ATOM   16416 C  C   . THR J  1 96  ? -0.751  24.845  19.706 1.00 50.05  ? 87  THR J C   1 
ATOM   16417 O  O   . THR J  1 96  ? 0.398   24.467  19.910 1.00 51.48  ? 87  THR J O   1 
ATOM   16418 C  CB  . THR J  1 96  ? -2.285  24.925  21.680 1.00 50.24  ? 87  THR J CB  1 
ATOM   16419 O  OG1 . THR J  1 96  ? -1.274  24.715  22.662 1.00 56.38  ? 87  THR J OG1 1 
ATOM   16420 C  CG2 . THR J  1 96  ? -3.621  24.430  22.211 1.00 50.48  ? 87  THR J CG2 1 
ATOM   16421 N  N   . PRO J  1 97  ? -1.060  25.838  18.849 1.00 54.52  ? 88  PRO J N   1 
ATOM   16422 C  CA  . PRO J  1 97  ? -0.039  26.582  18.102 1.00 55.72  ? 88  PRO J CA  1 
ATOM   16423 C  C   . PRO J  1 97  ? 0.714   27.539  19.000 1.00 54.14  ? 88  PRO J C   1 
ATOM   16424 O  O   . PRO J  1 97  ? 0.104   28.085  19.921 1.00 47.93  ? 88  PRO J O   1 
ATOM   16425 C  CB  . PRO J  1 97  ? -0.867  27.380  17.089 1.00 47.85  ? 88  PRO J CB  1 
ATOM   16426 C  CG  . PRO J  1 97  ? -2.221  27.504  17.708 1.00 46.08  ? 88  PRO J CG  1 
ATOM   16427 C  CD  . PRO J  1 97  ? -2.429  26.243  18.469 1.00 51.06  ? 88  PRO J CD  1 
ATOM   16428 N  N   . ASP J  1 98  ? 1.981   27.818  18.713 1.00 51.80  ? 89  ASP J N   1 
ATOM   16429 C  CA  . ASP J  1 98  ? 2.643   28.738  19.601 1.00 55.37  ? 89  ASP J CA  1 
ATOM   16430 C  C   . ASP J  1 98  ? 2.577   30.099  18.936 1.00 55.99  ? 89  ASP J C   1 
ATOM   16431 O  O   . ASP J  1 98  ? 3.458   30.481  18.190 1.00 60.73  ? 89  ASP J O   1 
ATOM   16432 C  CB  . ASP J  1 98  ? 4.118   28.327  19.735 1.00 58.20  ? 89  ASP J CB  1 
ATOM   16433 C  CG  . ASP J  1 98  ? 4.848   28.266  18.381 1.00 58.89  ? 89  ASP J CG  1 
ATOM   16434 O  OD1 . ASP J  1 98  ? 4.182   28.073  17.352 1.00 56.22  ? 89  ASP J OD1 1 
ATOM   16435 O  OD2 . ASP J  1 98  ? 6.088   28.409  18.339 1.00 59.83  ? 89  ASP J OD2 1 
ATOM   16436 N  N   . ILE J  1 99  ? 1.637   30.910  19.391 1.00 52.71  ? 90  ILE J N   1 
ATOM   16437 C  CA  . ILE J  1 99  ? 1.378   32.183  18.761 1.00 53.57  ? 90  ILE J CA  1 
ATOM   16438 C  C   . ILE J  1 99  ? 1.676   33.201  19.804 1.00 59.40  ? 90  ILE J C   1 
ATOM   16439 O  O   . ILE J  1 99  ? 1.047   33.219  20.859 1.00 59.12  ? 90  ILE J O   1 
ATOM   16440 C  CB  . ILE J  1 99  ? -0.087  32.371  18.357 1.00 54.00  ? 90  ILE J CB  1 
ATOM   16441 C  CG1 . ILE J  1 99  ? -0.494  31.321  17.333 1.00 56.29  ? 90  ILE J CG1 1 
ATOM   16442 C  CG2 . ILE J  1 99  ? -0.289  33.774  17.782 1.00 49.88  ? 90  ILE J CG2 1 
ATOM   16443 C  CD1 . ILE J  1 99  ? 0.339   31.380  16.064 1.00 56.63  ? 90  ILE J CD1 1 
ATOM   16444 N  N   . THR J  1 100 ? 2.641   34.050  19.507 1.00 56.24  ? 91  THR J N   1 
ATOM   16445 C  CA  . THR J  1 100 ? 3.055   35.042  20.451 1.00 51.61  ? 91  THR J CA  1 
ATOM   16446 C  C   . THR J  1 100 ? 3.052   36.426  19.807 1.00 53.33  ? 91  THR J C   1 
ATOM   16447 O  O   . THR J  1 100 ? 3.305   36.575  18.611 1.00 53.60  ? 91  THR J O   1 
ATOM   16448 C  CB  . THR J  1 100 ? 4.441   34.678  21.049 1.00 48.50  ? 91  THR J CB  1 
ATOM   16449 O  OG1 . THR J  1 100 ? 4.908   35.749  21.883 1.00 65.86  ? 91  THR J OG1 1 
ATOM   16450 C  CG2 . THR J  1 100 ? 5.459   34.404  19.962 1.00 46.27  ? 91  THR J CG2 1 
ATOM   16451 N  N   . ALA J  1 101 ? 2.729   37.431  20.616 1.00 56.37  ? 92  ALA J N   1 
ATOM   16452 C  CA  . ALA J  1 101 ? 2.946   38.824  20.262 1.00 51.32  ? 92  ALA J CA  1 
ATOM   16453 C  C   . ALA J  1 101 ? 4.445   39.095  20.260 1.00 51.65  ? 92  ALA J C   1 
ATOM   16454 O  O   . ALA J  1 101 ? 5.151   38.758  21.196 1.00 51.32  ? 92  ALA J O   1 
ATOM   16455 C  CB  . ALA J  1 101 ? 2.239   39.731  21.243 1.00 47.81  ? 92  ALA J CB  1 
ATOM   16456 N  N   . TYR J  1 102 ? 4.927   39.680  19.177 1.00 55.12  ? 93  TYR J N   1 
ATOM   16457 C  CA  . TYR J  1 102 ? 6.352   39.885  18.986 1.00 59.50  ? 93  TYR J CA  1 
ATOM   16458 C  C   . TYR J  1 102 ? 6.871   41.080  19.785 1.00 52.00  ? 93  TYR J C   1 
ATOM   16459 O  O   . TYR J  1 102 ? 8.045   41.147  20.120 1.00 53.81  ? 93  TYR J O   1 
ATOM   16460 C  CB  . TYR J  1 102 ? 6.636   40.055  17.483 1.00 59.36  ? 93  TYR J CB  1 
ATOM   16461 C  CG  . TYR J  1 102 ? 6.445   38.785  16.680 1.00 59.34  ? 93  TYR J CG  1 
ATOM   16462 C  CD1 . TYR J  1 102 ? 6.713   37.549  17.235 1.00 61.06  ? 93  TYR J CD1 1 
ATOM   16463 C  CD2 . TYR J  1 102 ? 6.000   38.820  15.371 1.00 70.31  ? 93  TYR J CD2 1 
ATOM   16464 C  CE1 . TYR J  1 102 ? 6.549   36.394  16.523 1.00 57.87  ? 93  TYR J CE1 1 
ATOM   16465 C  CE2 . TYR J  1 102 ? 5.830   37.650  14.650 1.00 63.86  ? 93  TYR J CE2 1 
ATOM   16466 C  CZ  . TYR J  1 102 ? 6.111   36.445  15.239 1.00 57.42  ? 93  TYR J CZ  1 
ATOM   16467 O  OH  . TYR J  1 102 ? 5.958   35.277  14.545 1.00 56.74  ? 93  TYR J OH  1 
ATOM   16468 N  N   . SER J  1 103 ? 5.986   42.046  20.007 1.00 56.37  ? 94  SER J N   1 
ATOM   16469 C  CA  . SER J  1 103 ? 6.271   43.302  20.703 1.00 51.70  ? 94  SER J CA  1 
ATOM   16470 C  C   . SER J  1 103 ? 5.872   43.390  22.198 1.00 56.57  ? 94  SER J C   1 
ATOM   16471 O  O   . SER J  1 103 ? 5.936   44.469  22.797 1.00 51.98  ? 94  SER J O   1 
ATOM   16472 C  CB  . SER J  1 103 ? 5.761   44.511  19.896 1.00 61.81  ? 94  SER J CB  1 
ATOM   16473 O  OG  . SER J  1 103 ? 4.424   44.342  19.450 1.00 60.78  ? 94  SER J OG  1 
ATOM   16474 N  N   . SER J  1 104 ? 5.400   42.284  22.775 1.00 60.60  ? 95  SER J N   1 
ATOM   16475 C  CA  . SER J  1 104 ? 5.105   42.242  24.221 1.00 62.14  ? 95  SER J CA  1 
ATOM   16476 C  C   . SER J  1 104 ? 6.298   42.722  25.070 1.00 54.52  ? 95  SER J C   1 
ATOM   16477 O  O   . SER J  1 104 ? 7.454   42.431  24.747 1.00 50.66  ? 95  SER J O   1 
ATOM   16478 C  CB  . SER J  1 104 ? 4.672   40.830  24.665 1.00 55.29  ? 95  SER J CB  1 
ATOM   16479 O  OG  . SER J  1 104 ? 5.773   39.933  24.694 1.00 60.51  ? 95  SER J OG  1 
ATOM   16480 N  N   . THR J  1 105 ? 6.008   43.564  26.064 1.00 54.62  ? 96  THR J N   1 
ATOM   16481 C  CA  . THR J  1 105 ? 6.953   43.936  27.131 1.00 53.83  ? 96  THR J CA  1 
ATOM   16482 C  C   . THR J  1 105 ? 6.841   43.146  28.463 1.00 57.63  ? 96  THR J C   1 
ATOM   16483 O  O   . THR J  1 105 ? 7.702   43.249  29.338 1.00 51.76  ? 96  THR J O   1 
ATOM   16484 C  CB  . THR J  1 105 ? 6.809   45.412  27.436 1.00 54.94  ? 96  THR J CB  1 
ATOM   16485 O  OG1 . THR J  1 105 ? 5.465   45.660  27.868 1.00 54.05  ? 96  THR J OG1 1 
ATOM   16486 C  CG2 . THR J  1 105 ? 7.102   46.230  26.177 1.00 52.95  ? 96  THR J CG2 1 
ATOM   16487 N  N   A ARG J  1 106 ? 5.769   42.370  28.598 0.50 56.22  ? 97  ARG J N   1 
ATOM   16488 N  N   B ARG J  1 106 ? 5.767   42.374  28.595 0.50 56.16  ? 97  ARG J N   1 
ATOM   16489 C  CA  A ARG J  1 106 ? 5.516   41.567  29.790 0.50 54.21  ? 97  ARG J CA  1 
ATOM   16490 C  CA  B ARG J  1 106 ? 5.519   41.562  29.780 0.50 54.22  ? 97  ARG J CA  1 
ATOM   16491 C  C   A ARG J  1 106 ? 4.821   40.289  29.333 0.50 52.66  ? 97  ARG J C   1 
ATOM   16492 C  C   B ARG J  1 106 ? 4.789   40.295  29.353 0.50 52.51  ? 97  ARG J C   1 
ATOM   16493 O  O   A ARG J  1 106 ? 4.110   40.307  28.333 0.50 52.53  ? 97  ARG J O   1 
ATOM   16494 O  O   B ARG J  1 106 ? 4.013   40.328  28.404 0.50 52.52  ? 97  ARG J O   1 
ATOM   16495 C  CB  A ARG J  1 106 ? 4.611   42.320  30.785 0.50 55.74  ? 97  ARG J CB  1 
ATOM   16496 C  CB  B ARG J  1 106 ? 4.664   42.328  30.800 0.50 54.38  ? 97  ARG J CB  1 
ATOM   16497 C  CG  A ARG J  1 106 ? 5.066   43.734  31.169 0.50 55.23  ? 97  ARG J CG  1 
ATOM   16498 C  CG  B ARG J  1 106 ? 5.313   43.573  31.396 0.50 55.24  ? 97  ARG J CG  1 
ATOM   16499 C  CD  A ARG J  1 106 ? 3.989   44.498  31.971 0.50 56.71  ? 97  ARG J CD  1 
ATOM   16500 C  CD  B ARG J  1 106 ? 4.435   44.190  32.485 0.50 57.39  ? 97  ARG J CD  1 
ATOM   16501 N  NE  A ARG J  1 106 ? 4.261   45.940  32.038 0.50 57.27  ? 97  ARG J NE  1 
ATOM   16502 N  NE  B ARG J  1 106 ? 5.060   45.350  33.124 0.50 60.32  ? 97  ARG J NE  1 
ATOM   16503 C  CZ  A ARG J  1 106 ? 3.493   46.837  32.655 0.50 52.97  ? 97  ARG J CZ  1 
ATOM   16504 C  CZ  B ARG J  1 106 ? 6.061   45.272  33.996 0.50 55.10  ? 97  ARG J CZ  1 
ATOM   16505 N  NH1 A ARG J  1 106 ? 3.839   48.115  32.645 0.50 48.32  ? 97  ARG J NH1 1 
ATOM   16506 N  NH1 B ARG J  1 106 ? 6.566   46.377  34.528 0.50 54.09  ? 97  ARG J NH1 1 
ATOM   16507 N  NH2 A ARG J  1 106 ? 2.382   46.467  33.279 0.50 50.85  ? 97  ARG J NH2 1 
ATOM   16508 N  NH2 B ARG J  1 106 ? 6.565   44.088  34.322 0.50 51.34  ? 97  ARG J NH2 1 
ATOM   16509 N  N   . PRO J  1 107 ? 5.020   39.176  30.063 1.00 55.73  ? 98  PRO J N   1 
ATOM   16510 C  CA  . PRO J  1 107 ? 4.322   37.927  29.727 1.00 51.97  ? 98  PRO J CA  1 
ATOM   16511 C  C   . PRO J  1 107 ? 2.815   38.086  29.823 1.00 48.51  ? 98  PRO J C   1 
ATOM   16512 O  O   . PRO J  1 107 ? 2.319   38.713  30.738 1.00 54.70  ? 98  PRO J O   1 
ATOM   16513 C  CB  . PRO J  1 107 ? 4.826   36.937  30.772 1.00 37.33  ? 98  PRO J CB  1 
ATOM   16514 C  CG  . PRO J  1 107 ? 5.436   37.770  31.836 1.00 45.53  ? 98  PRO J CG  1 
ATOM   16515 C  CD  . PRO J  1 107 ? 5.947   38.999  31.193 1.00 51.90  ? 98  PRO J CD  1 
ATOM   16516 N  N   . VAL J  1 108 ? 2.106   37.518  28.863 1.00 51.78  ? 99  VAL J N   1 
ATOM   16517 C  CA  . VAL J  1 108 ? 0.672   37.682  28.739 1.00 49.73  ? 99  VAL J CA  1 
ATOM   16518 C  C   . VAL J  1 108 ? -0.100  37.071  29.883 1.00 49.61  ? 99  VAL J C   1 
ATOM   16519 O  O   . VAL J  1 108 ? 0.272   36.037  30.428 1.00 50.37  ? 99  VAL J O   1 
ATOM   16520 C  CB  . VAL J  1 108 ? 0.207   36.976  27.495 1.00 45.96  ? 99  VAL J CB  1 
ATOM   16521 C  CG1 . VAL J  1 108 ? -1.112  37.552  27.032 1.00 48.60  ? 99  VAL J CG1 1 
ATOM   16522 C  CG2 . VAL J  1 108 ? 1.267   37.113  26.464 1.00 54.77  ? 99  VAL J CG2 1 
ATOM   16523 N  N   . GLN J  1 109 ? -1.217  37.687  30.210 1.00 43.44  ? 100 GLN J N   1 
ATOM   16524 C  CA  . GLN J  1 109 ? -2.070  37.138  31.231 1.00 48.19  ? 100 GLN J CA  1 
ATOM   16525 C  C   . GLN J  1 109 ? -3.368  36.598  30.659 1.00 47.67  ? 100 GLN J C   1 
ATOM   16526 O  O   . GLN J  1 109 ? -4.106  37.308  30.022 1.00 51.07  ? 100 GLN J O   1 
ATOM   16527 C  CB  . GLN J  1 109 ? -2.346  38.193  32.293 1.00 50.65  ? 100 GLN J CB  1 
ATOM   16528 C  CG  . GLN J  1 109 ? -1.104  38.582  33.067 1.00 55.87  ? 100 GLN J CG  1 
ATOM   16529 C  CD  . GLN J  1 109 ? -1.238  39.926  33.723 1.00 65.32  ? 100 GLN J CD  1 
ATOM   16530 O  OE1 . GLN J  1 109 ? -2.298  40.548  33.667 1.00 71.89  ? 100 GLN J OE1 1 
ATOM   16531 N  NE2 . GLN J  1 109 ? -0.159  40.397  34.338 1.00 58.39  ? 100 GLN J NE2 1 
ATOM   16532 N  N   . VAL J  1 110 ? -3.634  35.325  30.892 1.00 51.31  ? 101 VAL J N   1 
ATOM   16533 C  CA  . VAL J  1 110 ? -4.897  34.733  30.510 1.00 47.29  ? 101 VAL J CA  1 
ATOM   16534 C  C   . VAL J  1 110 ? -5.983  35.135  31.508 1.00 45.98  ? 101 VAL J C   1 
ATOM   16535 O  O   . VAL J  1 110 ? -5.848  34.933  32.710 1.00 54.58  ? 101 VAL J O   1 
ATOM   16536 C  CB  . VAL J  1 110 ? -4.757  33.222  30.450 1.00 43.44  ? 101 VAL J CB  1 
ATOM   16537 C  CG1 . VAL J  1 110 ? -6.045  32.586  30.004 1.00 49.22  ? 101 VAL J CG1 1 
ATOM   16538 C  CG2 . VAL J  1 110 ? -3.639  32.872  29.518 1.00 45.11  ? 101 VAL J CG2 1 
ATOM   16539 N  N   . LEU J  1 111 ? -7.039  35.751  31.002 1.00 49.52  ? 102 LEU J N   1 
ATOM   16540 C  CA  . LEU J  1 111 ? -8.168  36.172  31.818 1.00 53.05  ? 102 LEU J CA  1 
ATOM   16541 C  C   . LEU J  1 111 ? -9.315  35.182  31.771 1.00 50.91  ? 102 LEU J C   1 
ATOM   16542 O  O   . LEU J  1 111 ? -10.381 35.435  32.331 1.00 57.19  ? 102 LEU J O   1 
ATOM   16543 C  CB  . LEU J  1 111 ? -8.647  37.559  31.395 1.00 51.91  ? 102 LEU J CB  1 
ATOM   16544 C  CG  . LEU J  1 111 ? -7.485  38.503  31.123 1.00 49.88  ? 102 LEU J CG  1 
ATOM   16545 C  CD1 . LEU J  1 111 ? -7.985  39.890  30.842 1.00 51.50  ? 102 LEU J CD1 1 
ATOM   16546 C  CD2 . LEU J  1 111 ? -6.523  38.493  32.284 1.00 46.83  ? 102 LEU J CD2 1 
ATOM   16547 N  N   . SER J  1 112 ? -9.104  34.074  31.068 1.00 52.38  ? 103 SER J N   1 
ATOM   16548 C  CA  . SER J  1 112 ? -10.173 33.101  30.814 1.00 57.23  ? 103 SER J CA  1 
ATOM   16549 C  C   . SER J  1 112 ? -9.739  31.663  31.067 1.00 48.79  ? 103 SER J C   1 
ATOM   16550 O  O   . SER J  1 112 ? -8.552  31.365  31.093 1.00 48.47  ? 103 SER J O   1 
ATOM   16551 C  CB  . SER J  1 112 ? -10.675 33.233  29.370 1.00 57.35  ? 103 SER J CB  1 
ATOM   16552 O  OG  . SER J  1 112 ? -9.654  32.920  28.433 1.00 55.16  ? 103 SER J OG  1 
ATOM   16553 N  N   . PRO J  1 113 ? -10.707 30.763  31.251 1.00 49.53  ? 104 PRO J N   1 
ATOM   16554 C  CA  . PRO J  1 113 ? -10.295 29.363  31.331 1.00 51.61  ? 104 PRO J CA  1 
ATOM   16555 C  C   . PRO J  1 113 ? -9.634  28.967  30.017 1.00 56.84  ? 104 PRO J C   1 
ATOM   16556 O  O   . PRO J  1 113 ? -9.960  29.539  28.966 1.00 54.49  ? 104 PRO J O   1 
ATOM   16557 C  CB  . PRO J  1 113 ? -11.620 28.618  31.513 1.00 46.19  ? 104 PRO J CB  1 
ATOM   16558 C  CG  . PRO J  1 113 ? -12.565 29.640  32.051 1.00 48.22  ? 104 PRO J CG  1 
ATOM   16559 C  CD  . PRO J  1 113 ? -12.158 30.933  31.421 1.00 49.14  ? 104 PRO J CD  1 
ATOM   16560 N  N   . GLN J  1 114 ? -8.709  28.019  30.044 1.00 56.61  ? 105 GLN J N   1 
ATOM   16561 C  CA  . GLN J  1 114 ? -8.177  27.582  28.768 1.00 57.46  ? 105 GLN J CA  1 
ATOM   16562 C  C   . GLN J  1 114 ? -8.788  26.266  28.383 1.00 56.02  ? 105 GLN J C   1 
ATOM   16563 O  O   . GLN J  1 114 ? -8.404  25.208  28.860 1.00 61.03  ? 105 GLN J O   1 
ATOM   16564 C  CB  . GLN J  1 114 ? -6.676  27.472  28.844 1.00 56.12  ? 105 GLN J CB  1 
ATOM   16565 C  CG  . GLN J  1 114 ? -6.074  28.790  29.230 1.00 61.71  ? 105 GLN J CG  1 
ATOM   16566 C  CD  . GLN J  1 114 ? -4.594  28.680  29.442 1.00 74.78  ? 105 GLN J CD  1 
ATOM   16567 O  OE1 . GLN J  1 114 ? -3.837  29.577  29.073 1.00 77.07  ? 105 GLN J OE1 1 
ATOM   16568 N  NE2 . GLN J  1 114 ? -4.161  27.566  30.028 1.00 67.77  ? 105 GLN J NE2 1 
ATOM   16569 N  N   . ASN J  1 115 ? -9.693  26.359  27.426 1.00 59.80  ? 106 ASN J N   1 
ATOM   16570 C  CA  . ASN J  1 115 ? -10.526 25.259  27.013 1.00 56.96  ? 106 ASN J CA  1 
ATOM   16571 C  C   . ASN J  1 115 ? -10.694 25.448  25.537 1.00 56.66  ? 106 ASN J C   1 
ATOM   16572 O  O   . ASN J  1 115 ? -10.788 26.574  25.068 1.00 57.06  ? 106 ASN J O   1 
ATOM   16573 C  CB  . ASN J  1 115 ? -11.902 25.360  27.664 1.00 59.18  ? 106 ASN J CB  1 
ATOM   16574 C  CG  . ASN J  1 115 ? -11.916 24.880  29.102 1.00 65.91  ? 106 ASN J CG  1 
ATOM   16575 O  OD1 . ASN J  1 115 ? -11.160 23.984  29.494 1.00 64.34  ? 106 ASN J OD1 1 
ATOM   16576 N  ND2 . ASN J  1 115 ? -12.797 25.473  29.898 1.00 67.68  ? 106 ASN J ND2 1 
ATOM   16577 N  N   . ALA J  1 116 ? -10.736 24.351  24.804 1.00 58.07  ? 107 ALA J N   1 
ATOM   16578 C  CA  . ALA J  1 116 ? -10.923 24.410  23.373 1.00 49.34  ? 107 ALA J CA  1 
ATOM   16579 C  C   . ALA J  1 116 ? -12.185 23.656  22.999 1.00 52.51  ? 107 ALA J C   1 
ATOM   16580 O  O   . ALA J  1 116 ? -12.574 22.715  23.678 1.00 59.45  ? 107 ALA J O   1 
ATOM   16581 C  CB  . ALA J  1 116 ? -9.734  23.805  22.691 1.00 53.23  ? 107 ALA J CB  1 
ATOM   16582 N  N   . LEU J  1 117 ? -12.836 24.087  21.927 1.00 60.95  ? 108 LEU J N   1 
ATOM   16583 C  CA  . LEU J  1 117 ? -13.931 23.331  21.334 1.00 57.33  ? 108 LEU J CA  1 
ATOM   16584 C  C   . LEU J  1 117 ? -13.379 22.543  20.152 1.00 57.60  ? 108 LEU J C   1 
ATOM   16585 O  O   . LEU J  1 117 ? -12.599 23.076  19.369 1.00 55.12  ? 108 LEU J O   1 
ATOM   16586 C  CB  . LEU J  1 117 ? -15.018 24.280  20.856 1.00 48.09  ? 108 LEU J CB  1 
ATOM   16587 C  CG  . LEU J  1 117 ? -16.173 23.646  20.100 1.00 60.97  ? 108 LEU J CG  1 
ATOM   16588 C  CD1 . LEU J  1 117 ? -17.068 22.904  21.068 1.00 68.23  ? 108 LEU J CD1 1 
ATOM   16589 C  CD2 . LEU J  1 117 ? -16.954 24.715  19.348 1.00 68.68  ? 108 LEU J CD2 1 
ATOM   16590 N  N   . VAL J  1 118 ? -13.754 21.268  20.045 1.00 64.79  ? 109 VAL J N   1 
ATOM   16591 C  CA  . VAL J  1 118 ? -13.352 20.413  18.917 1.00 64.04  ? 109 VAL J CA  1 
ATOM   16592 C  C   . VAL J  1 118 ? -14.576 19.758  18.285 1.00 58.42  ? 109 VAL J C   1 
ATOM   16593 O  O   . VAL J  1 118 ? -15.473 19.331  19.002 1.00 60.28  ? 109 VAL J O   1 
ATOM   16594 C  CB  . VAL J  1 118 ? -12.408 19.285  19.375 1.00 56.51  ? 109 VAL J CB  1 
ATOM   16595 C  CG1 . VAL J  1 118 ? -11.794 18.596  18.171 1.00 55.30  ? 109 VAL J CG1 1 
ATOM   16596 C  CG2 . VAL J  1 118 ? -11.322 19.826  20.310 1.00 53.27  ? 109 VAL J CG2 1 
ATOM   16597 N  N   . ASN J  1 119 ? -14.641 19.673  16.958 1.00 59.84  ? 110 ASN J N   1 
ATOM   16598 C  CA  . ASN J  1 119 ? -15.744 18.908  16.355 1.00 66.42  ? 110 ASN J CA  1 
ATOM   16599 C  C   . ASN J  1 119 ? -15.383 17.814  15.340 1.00 65.25  ? 110 ASN J C   1 
ATOM   16600 O  O   . ASN J  1 119 ? -14.216 17.635  14.992 1.00 67.06  ? 110 ASN J O   1 
ATOM   16601 C  CB  . ASN J  1 119 ? -16.850 19.820  15.824 1.00 69.57  ? 110 ASN J CB  1 
ATOM   16602 C  CG  . ASN J  1 119 ? -16.456 20.570  14.562 1.00 78.24  ? 110 ASN J CG  1 
ATOM   16603 O  OD1 . ASN J  1 119 ? -15.467 20.255  13.888 1.00 67.15  ? 110 ASN J OD1 1 
ATOM   16604 N  ND2 . ASN J  1 119 ? -17.255 21.581  14.234 1.00 88.85  ? 110 ASN J ND2 1 
ATOM   16605 N  N   . SER J  1 120 ? -16.406 17.104  14.863 1.00 68.06  ? 111 SER J N   1 
ATOM   16606 C  CA  . SER J  1 120 ? -16.220 15.858  14.112 1.00 67.53  ? 111 SER J CA  1 
ATOM   16607 C  C   . SER J  1 120 ? -15.251 15.979  12.937 1.00 64.70  ? 111 SER J C   1 
ATOM   16608 O  O   . SER J  1 120 ? -14.467 15.067  12.677 1.00 65.28  ? 111 SER J O   1 
ATOM   16609 C  CB  . SER J  1 120 ? -17.565 15.267  13.675 1.00 63.03  ? 111 SER J CB  1 
ATOM   16610 O  OG  . SER J  1 120 ? -18.234 16.125  12.780 1.00 70.55  ? 111 SER J OG  1 
ATOM   16611 N  N   . SER J  1 121 ? -15.259 17.119  12.262 1.00 62.16  ? 112 SER J N   1 
ATOM   16612 C  CA  . SER J  1 121 ? -14.391 17.285  11.101 1.00 68.51  ? 112 SER J CA  1 
ATOM   16613 C  C   . SER J  1 121 ? -12.955 17.657  11.478 1.00 68.37  ? 112 SER J C   1 
ATOM   16614 O  O   . SER J  1 121 ? -12.098 17.819  10.612 1.00 67.00  ? 112 SER J O   1 
ATOM   16615 C  CB  . SER J  1 121 ? -14.982 18.281  10.092 1.00 63.08  ? 112 SER J CB  1 
ATOM   16616 O  OG  . SER J  1 121 ? -14.864 19.616  10.532 1.00 70.95  ? 112 SER J OG  1 
ATOM   16617 N  N   . GLY J  1 122 ? -12.701 17.798  12.773 1.00 65.23  ? 113 GLY J N   1 
ATOM   16618 C  CA  . GLY J  1 122 ? -11.354 18.014  13.260 1.00 61.28  ? 113 GLY J CA  1 
ATOM   16619 C  C   . GLY J  1 122 ? -10.942 19.465  13.365 1.00 65.20  ? 113 GLY J C   1 
ATOM   16620 O  O   . GLY J  1 122 ? -9.761  19.762  13.538 1.00 63.46  ? 113 GLY J O   1 
ATOM   16621 N  N   . HIS J  1 123 ? -11.906 20.374  13.259 1.00 63.87  ? 114 HIS J N   1 
ATOM   16622 C  CA  . HIS J  1 123 ? -11.622 21.791  13.424 1.00 60.95  ? 114 HIS J CA  1 
ATOM   16623 C  C   . HIS J  1 123 ? -11.471 22.125  14.908 1.00 63.44  ? 114 HIS J C   1 
ATOM   16624 O  O   . HIS J  1 123 ? -12.268 21.690  15.749 1.00 62.97  ? 114 HIS J O   1 
ATOM   16625 C  CB  . HIS J  1 123 ? -12.724 22.642  12.796 1.00 66.37  ? 114 HIS J CB  1 
ATOM   16626 C  CG  . HIS J  1 123 ? -12.712 22.639  11.298 1.00 81.24  ? 114 HIS J CG  1 
ATOM   16627 N  ND1 . HIS J  1 123 ? -13.608 21.905  10.547 1.00 85.74  ? 114 HIS J ND1 1 
ATOM   16628 C  CD2 . HIS J  1 123 ? -11.916 23.280  10.408 1.00 79.46  ? 114 HIS J CD2 1 
ATOM   16629 C  CE1 . HIS J  1 123 ? -13.360 22.090  9.263  1.00 75.27  ? 114 HIS J CE1 1 
ATOM   16630 N  NE2 . HIS J  1 123 ? -12.338 22.921  9.151  1.00 78.22  ? 114 HIS J NE2 1 
ATOM   16631 N  N   . VAL J  1 124 ? -10.425 22.873  15.233 1.00 61.41  ? 115 VAL J N   1 
ATOM   16632 C  CA  . VAL J  1 124 ? -10.242 23.348  16.600 1.00 61.70  ? 115 VAL J CA  1 
ATOM   16633 C  C   . VAL J  1 124 ? -10.525 24.838  16.687 1.00 58.40  ? 115 VAL J C   1 
ATOM   16634 O  O   . VAL J  1 124 ? -10.216 25.617  15.786 1.00 51.86  ? 115 VAL J O   1 
ATOM   16635 C  CB  . VAL J  1 124 ? -8.831  23.041  17.199 1.00 57.14  ? 115 VAL J CB  1 
ATOM   16636 C  CG1 . VAL J  1 124 ? -8.812  23.340  18.683 1.00 47.33  ? 115 VAL J CG1 1 
ATOM   16637 C  CG2 . VAL J  1 124 ? -8.456  21.594  16.980 1.00 56.18  ? 115 VAL J CG2 1 
ATOM   16638 N  N   . GLN J  1 125 ? -11.131 25.205  17.802 1.00 61.83  ? 116 GLN J N   1 
ATOM   16639 C  CA  . GLN J  1 125 ? -11.466 26.571  18.090 1.00 57.46  ? 116 GLN J CA  1 
ATOM   16640 C  C   . GLN J  1 125 ? -11.019 26.890  19.512 1.00 60.67  ? 116 GLN J C   1 
ATOM   16641 O  O   . GLN J  1 125 ? -11.489 26.296  20.489 1.00 51.39  ? 116 GLN J O   1 
ATOM   16642 C  CB  . GLN J  1 125 ? -12.958 26.737  17.953 1.00 55.39  ? 116 GLN J CB  1 
ATOM   16643 C  CG  . GLN J  1 125 ? -13.358 28.050  17.405 1.00 69.26  ? 116 GLN J CG  1 
ATOM   16644 C  CD  . GLN J  1 125 ? -14.814 28.056  17.069 1.00 86.18  ? 116 GLN J CD  1 
ATOM   16645 O  OE1 . GLN J  1 125 ? -15.232 27.524  16.032 1.00 89.82  ? 116 GLN J OE1 1 
ATOM   16646 N  NE2 . GLN J  1 125 ? -15.615 28.631  17.956 1.00 78.48  ? 116 GLN J NE2 1 
ATOM   16647 N  N   . TYR J  1 126 ? -10.091 27.826  19.620 1.00 57.02  ? 117 TYR J N   1 
ATOM   16648 C  CA  . TYR J  1 126 ? -9.511  28.173  20.900 1.00 56.23  ? 117 TYR J CA  1 
ATOM   16649 C  C   . TYR J  1 126 ? -9.592  29.677  21.048 1.00 62.29  ? 117 TYR J C   1 
ATOM   16650 O  O   . TYR J  1 126 ? -8.955  30.393  20.283 1.00 66.41  ? 117 TYR J O   1 
ATOM   16651 C  CB  . TYR J  1 126 ? -8.055  27.753  20.892 1.00 55.76  ? 117 TYR J CB  1 
ATOM   16652 C  CG  . TYR J  1 126 ? -7.330  28.071  22.152 1.00 56.42  ? 117 TYR J CG  1 
ATOM   16653 C  CD1 . TYR J  1 126 ? -7.998  28.102  23.369 1.00 59.20  ? 117 TYR J CD1 1 
ATOM   16654 C  CD2 . TYR J  1 126 ? -5.975  28.341  22.136 1.00 55.74  ? 117 TYR J CD2 1 
ATOM   16655 C  CE1 . TYR J  1 126 ? -7.328  28.385  24.544 1.00 58.29  ? 117 TYR J CE1 1 
ATOM   16656 C  CE2 . TYR J  1 126 ? -5.296  28.633  23.297 1.00 57.17  ? 117 TYR J CE2 1 
ATOM   16657 C  CZ  . TYR J  1 126 ? -5.974  28.653  24.503 1.00 61.27  ? 117 TYR J CZ  1 
ATOM   16658 O  OH  . TYR J  1 126 ? -5.294  28.944  25.667 1.00 62.63  ? 117 TYR J OH  1 
ATOM   16659 N  N   . LEU J  1 127 ? -10.353 30.170  22.021 1.00 62.94  ? 118 LEU J N   1 
ATOM   16660 C  CA  . LEU J  1 127 ? -10.582 31.612  22.111 1.00 57.34  ? 118 LEU J CA  1 
ATOM   16661 C  C   . LEU J  1 127 ? -10.204 32.215  23.471 1.00 62.24  ? 118 LEU J C   1 
ATOM   16662 O  O   . LEU J  1 127 ? -11.075 32.631  24.240 1.00 61.44  ? 118 LEU J O   1 
ATOM   16663 C  CB  . LEU J  1 127 ? -12.036 31.924  21.761 1.00 62.70  ? 118 LEU J CB  1 
ATOM   16664 C  CG  . LEU J  1 127 ? -12.481 33.360  22.029 1.00 77.46  ? 118 LEU J CG  1 
ATOM   16665 C  CD1 . LEU J  1 127 ? -11.595 34.362  21.306 1.00 75.67  ? 118 LEU J CD1 1 
ATOM   16666 C  CD2 . LEU J  1 127 ? -13.915 33.542  21.641 1.00 82.60  ? 118 LEU J CD2 1 
ATOM   16667 N  N   . PRO J  1 128 ? -8.896  32.262  23.775 1.00 58.93  ? 119 PRO J N   1 
ATOM   16668 C  CA  . PRO J  1 128 ? -8.429  32.788  25.062 1.00 54.83  ? 119 PRO J CA  1 
ATOM   16669 C  C   . PRO J  1 128 ? -8.604  34.290  25.193 1.00 57.62  ? 119 PRO J C   1 
ATOM   16670 O  O   . PRO J  1 128 ? -8.237  35.031  24.290 1.00 58.19  ? 119 PRO J O   1 
ATOM   16671 C  CB  . PRO J  1 128 ? -6.938  32.461  25.050 1.00 51.41  ? 119 PRO J CB  1 
ATOM   16672 C  CG  . PRO J  1 128 ? -6.582  32.427  23.620 1.00 60.60  ? 119 PRO J CG  1 
ATOM   16673 C  CD  . PRO J  1 128 ? -7.780  31.907  22.887 1.00 57.20  ? 119 PRO J CD  1 
ATOM   16674 N  N   . ALA J  1 129 ? -9.126  34.730  26.333 1.00 58.48  ? 120 ALA J N   1 
ATOM   16675 C  CA  . ALA J  1 129 ? -9.169  36.144  26.665 1.00 51.77  ? 120 ALA J CA  1 
ATOM   16676 C  C   . ALA J  1 129 ? -7.854  36.471  27.344 1.00 46.78  ? 120 ALA J C   1 
ATOM   16677 O  O   . ALA J  1 129 ? -7.394  35.715  28.172 1.00 49.89  ? 120 ALA J O   1 
ATOM   16678 C  CB  . ALA J  1 129 ? -10.332 36.426  27.573 1.00 50.57  ? 120 ALA J CB  1 
ATOM   16679 N  N   . GLN J  1 130 ? -7.237  37.583  26.972 1.00 49.71  ? 121 GLN J N   1 
ATOM   16680 C  CA  . GLN J  1 130 ? -5.906  37.928  27.460 1.00 51.54  ? 121 GLN J CA  1 
ATOM   16681 C  C   . GLN J  1 130 ? -5.713  39.408  27.771 1.00 52.40  ? 121 GLN J C   1 
ATOM   16682 O  O   . GLN J  1 130 ? -6.463  40.261  27.301 1.00 55.88  ? 121 GLN J O   1 
ATOM   16683 C  CB  . GLN J  1 130 ? -4.869  37.523  26.428 1.00 50.47  ? 121 GLN J CB  1 
ATOM   16684 C  CG  . GLN J  1 130 ? -5.168  36.198  25.818 1.00 55.60  ? 121 GLN J CG  1 
ATOM   16685 C  CD  . GLN J  1 130 ? -4.005  35.663  25.058 1.00 63.56  ? 121 GLN J CD  1 
ATOM   16686 O  OE1 . GLN J  1 130 ? -3.239  36.419  24.459 1.00 61.11  ? 121 GLN J OE1 1 
ATOM   16687 N  NE2 . GLN J  1 130 ? -3.844  34.346  25.084 1.00 69.55  ? 121 GLN J NE2 1 
ATOM   16688 N  N   . ARG J  1 131 ? -4.695  39.705  28.567 1.00 43.06  ? 122 ARG J N   1 
ATOM   16689 C  CA  . ARG J  1 131 ? -4.250  41.070  28.728 1.00 45.25  ? 122 ARG J CA  1 
ATOM   16690 C  C   . ARG J  1 131 ? -2.782  41.165  28.367 1.00 50.49  ? 122 ARG J C   1 
ATOM   16691 O  O   . ARG J  1 131 ? -1.969  40.358  28.823 1.00 45.88  ? 122 ARG J O   1 
ATOM   16692 C  CB  . ARG J  1 131 ? -4.484  41.579  30.137 1.00 47.62  ? 122 ARG J CB  1 
ATOM   16693 C  CG  . ARG J  1 131 ? -3.907  42.966  30.352 1.00 49.42  ? 122 ARG J CG  1 
ATOM   16694 C  CD  . ARG J  1 131 ? -4.088  43.402  31.759 1.00 47.70  ? 122 ARG J CD  1 
ATOM   16695 N  NE  . ARG J  1 131 ? -3.385  44.632  32.046 1.00 47.18  ? 122 ARG J NE  1 
ATOM   16696 C  CZ  . ARG J  1 131 ? -3.897  45.586  32.805 1.00 50.64  ? 122 ARG J CZ  1 
ATOM   16697 N  NH1 . ARG J  1 131 ? -5.107  45.435  33.315 1.00 52.11  ? 122 ARG J NH1 1 
ATOM   16698 N  NH2 . ARG J  1 131 ? -3.212  46.688  33.044 1.00 47.08  ? 122 ARG J NH2 1 
ATOM   16699 N  N   . LEU J  1 132 ? -2.451  42.159  27.541 1.00 50.90  ? 123 LEU J N   1 
ATOM   16700 C  CA  . LEU J  1 132 ? -1.117  42.252  26.956 1.00 50.49  ? 123 LEU J CA  1 
ATOM   16701 C  C   . LEU J  1 132 ? -0.527  43.653  27.079 1.00 52.64  ? 123 LEU J C   1 
ATOM   16702 O  O   . LEU J  1 132 ? -1.220  44.647  26.858 1.00 48.87  ? 123 LEU J O   1 
ATOM   16703 C  CB  . LEU J  1 132 ? -1.162  41.807  25.486 1.00 55.79  ? 123 LEU J CB  1 
ATOM   16704 C  CG  . LEU J  1 132 ? 0.114   41.917  24.650 1.00 55.30  ? 123 LEU J CG  1 
ATOM   16705 C  CD1 . LEU J  1 132 ? 1.104   40.809  25.000 1.00 59.20  ? 123 LEU J CD1 1 
ATOM   16706 C  CD2 . LEU J  1 132 ? -0.228  41.898  23.180 1.00 45.92  ? 123 LEU J CD2 1 
ATOM   16707 N  N   . SER J  1 133 ? 0.751   43.718  27.458 1.00 51.97  ? 124 SER J N   1 
ATOM   16708 C  CA  . SER J  1 133 ? 1.498   44.975  27.502 1.00 49.61  ? 124 SER J CA  1 
ATOM   16709 C  C   . SER J  1 133 ? 2.502   44.915  26.384 1.00 53.29  ? 124 SER J C   1 
ATOM   16710 O  O   . SER J  1 133 ? 3.363   44.040  26.385 1.00 54.36  ? 124 SER J O   1 
ATOM   16711 C  CB  . SER J  1 133 ? 2.278   45.116  28.813 1.00 51.87  ? 124 SER J CB  1 
ATOM   16712 O  OG  . SER J  1 133 ? 1.435   45.236  29.949 1.00 56.82  ? 124 SER J OG  1 
ATOM   16713 N  N   . PHE J  1 134 ? 2.408   45.836  25.431 1.00 55.02  ? 125 PHE J N   1 
ATOM   16714 C  CA  . PHE J  1 134 ? 3.307   45.827  24.271 1.00 56.19  ? 125 PHE J CA  1 
ATOM   16715 C  C   . PHE J  1 134 ? 3.866   47.209  23.997 1.00 55.74  ? 125 PHE J C   1 
ATOM   16716 O  O   . PHE J  1 134 ? 3.368   48.195  24.546 1.00 58.10  ? 125 PHE J O   1 
ATOM   16717 C  CB  . PHE J  1 134 ? 2.601   45.286  23.026 1.00 57.53  ? 125 PHE J CB  1 
ATOM   16718 C  CG  . PHE J  1 134 ? 1.432   46.121  22.567 1.00 57.68  ? 125 PHE J CG  1 
ATOM   16719 C  CD1 . PHE J  1 134 ? 1.535   46.929  21.446 1.00 56.60  ? 125 PHE J CD1 1 
ATOM   16720 C  CD2 . PHE J  1 134 ? 0.224   46.075  23.242 1.00 60.19  ? 125 PHE J CD2 1 
ATOM   16721 C  CE1 . PHE J  1 134 ? 0.464   47.680  21.018 1.00 58.49  ? 125 PHE J CE1 1 
ATOM   16722 C  CE2 . PHE J  1 134 ? -0.856  46.831  22.811 1.00 62.94  ? 125 PHE J CE2 1 
ATOM   16723 C  CZ  . PHE J  1 134 ? -0.732  47.631  21.698 1.00 56.60  ? 125 PHE J CZ  1 
ATOM   16724 N  N   . MET J  1 135 ? 4.895   47.287  23.155 1.00 52.95  ? 126 MET J N   1 
ATOM   16725 C  CA  . MET J  1 135 ? 5.498   48.584  22.850 1.00 57.16  ? 126 MET J CA  1 
ATOM   16726 C  C   . MET J  1 135 ? 4.573   49.430  21.997 1.00 52.82  ? 126 MET J C   1 
ATOM   16727 O  O   . MET J  1 135 ? 4.194   49.044  20.907 1.00 56.96  ? 126 MET J O   1 
ATOM   16728 C  CB  . MET J  1 135 ? 6.814   48.374  22.123 1.00 49.74  ? 126 MET J CB  1 
ATOM   16729 C  CG  . MET J  1 135 ? 7.496   47.128  22.588 1.00 51.98  ? 126 MET J CG  1 
ATOM   16730 S  SD  . MET J  1 135 ? 9.104   46.890  21.871 1.00 55.66  ? 126 MET J SD  1 
ATOM   16731 C  CE  . MET J  1 135 ? 9.363   45.176  22.319 1.00 53.24  ? 126 MET J CE  1 
ATOM   16732 N  N   . CYS J  1 136 ? 4.209   50.593  22.510 1.00 61.47  ? 127 CYS J N   1 
ATOM   16733 C  CA  . CYS J  1 136 ? 3.431   51.558  21.748 1.00 66.71  ? 127 CYS J CA  1 
ATOM   16734 C  C   . CYS J  1 136 ? 3.810   52.955  22.237 1.00 66.87  ? 127 CYS J C   1 
ATOM   16735 O  O   . CYS J  1 136 ? 3.933   53.170  23.444 1.00 64.12  ? 127 CYS J O   1 
ATOM   16736 C  CB  . CYS J  1 136 ? 1.936   51.262  21.945 1.00 65.04  ? 127 CYS J CB  1 
ATOM   16737 S  SG  . CYS J  1 136 ? 0.743   52.510  21.405 1.00 60.51  ? 127 CYS J SG  1 
ATOM   16738 N  N   . ASP J  1 137 ? 3.970   53.905  21.318 1.00 64.82  ? 128 ASP J N   1 
ATOM   16739 C  CA  . ASP J  1 137 ? 4.193   55.292  21.710 1.00 64.03  ? 128 ASP J CA  1 
ATOM   16740 C  C   . ASP J  1 137 ? 2.841   55.990  21.658 1.00 64.65  ? 128 ASP J C   1 
ATOM   16741 O  O   . ASP J  1 137 ? 2.276   56.181  20.594 1.00 67.37  ? 128 ASP J O   1 
ATOM   16742 C  CB  . ASP J  1 137 ? 5.224   55.971  20.808 1.00 62.80  ? 128 ASP J CB  1 
ATOM   16743 C  CG  . ASP J  1 137 ? 5.399   57.451  21.126 1.00 73.01  ? 128 ASP J CG  1 
ATOM   16744 O  OD1 . ASP J  1 137 ? 4.474   58.044  21.723 1.00 71.11  ? 128 ASP J OD1 1 
ATOM   16745 O  OD2 . ASP J  1 137 ? 6.450   58.034  20.764 1.00 71.79  ? 128 ASP J OD2 1 
ATOM   16746 N  N   . PRO J  1 138 ? 2.301   56.324  22.830 1.00 61.99  ? 129 PRO J N   1 
ATOM   16747 C  CA  . PRO J  1 138 ? 0.979   56.903  23.085 1.00 66.28  ? 129 PRO J CA  1 
ATOM   16748 C  C   . PRO J  1 138 ? 0.815   58.345  22.569 1.00 70.12  ? 129 PRO J C   1 
ATOM   16749 O  O   . PRO J  1 138 ? -0.299  58.877  22.601 1.00 62.69  ? 129 PRO J O   1 
ATOM   16750 C  CB  . PRO J  1 138 ? 0.834   56.788  24.606 1.00 64.67  ? 129 PRO J CB  1 
ATOM   16751 C  CG  . PRO J  1 138 ? 2.222   56.838  25.107 1.00 66.75  ? 129 PRO J CG  1 
ATOM   16752 C  CD  . PRO J  1 138 ? 3.074   56.162  24.074 1.00 62.21  ? 129 PRO J CD  1 
ATOM   16753 N  N   . THR J  1 139 ? 1.918   58.982  22.169 1.00 72.94  ? 130 THR J N   1 
ATOM   16754 C  CA  . THR J  1 139 ? 1.921   60.400  21.805 1.00 76.50  ? 130 THR J CA  1 
ATOM   16755 C  C   . THR J  1 139 ? 0.824   60.787  20.816 1.00 78.52  ? 130 THR J C   1 
ATOM   16756 O  O   . THR J  1 139 ? 0.676   60.186  19.752 1.00 69.40  ? 130 THR J O   1 
ATOM   16757 C  CB  . THR J  1 139 ? 3.255   60.787  21.141 1.00 76.13  ? 130 THR J CB  1 
ATOM   16758 O  OG1 . THR J  1 139 ? 4.249   60.993  22.150 1.00 83.64  ? 130 THR J OG1 1 
ATOM   16759 C  CG2 . THR J  1 139 ? 3.093   62.065  20.326 1.00 69.48  ? 130 THR J CG2 1 
ATOM   16760 N  N   . GLY J  1 140 ? 0.072   61.823  21.167 1.00 72.81  ? 131 GLY J N   1 
ATOM   16761 C  CA  . GLY J  1 140 ? -1.024  62.254  20.333 1.00 75.70  ? 131 GLY J CA  1 
ATOM   16762 C  C   . GLY J  1 140 ? -2.317  61.528  20.624 1.00 73.77  ? 131 GLY J C   1 
ATOM   16763 O  O   . GLY J  1 140 ? -3.272  61.618  19.868 1.00 79.08  ? 131 GLY J O   1 
ATOM   16764 N  N   . VAL J  1 141 ? -2.363  60.792  21.717 1.00 75.34  ? 132 VAL J N   1 
ATOM   16765 C  CA  . VAL J  1 141 ? -3.612  60.157  22.099 1.00 77.15  ? 132 VAL J CA  1 
ATOM   16766 C  C   . VAL J  1 141 ? -4.561  61.249  22.601 1.00 81.85  ? 132 VAL J C   1 
ATOM   16767 O  O   . VAL J  1 141 ? -5.778  61.057  22.663 1.00 76.49  ? 132 VAL J O   1 
ATOM   16768 C  CB  . VAL J  1 141 ? -3.387  59.079  23.188 1.00 68.59  ? 132 VAL J CB  1 
ATOM   16769 C  CG1 . VAL J  1 141 ? -2.736  59.687  24.417 1.00 62.90  ? 132 VAL J CG1 1 
ATOM   16770 C  CG2 . VAL J  1 141 ? -4.691  58.411  23.551 1.00 66.50  ? 132 VAL J CG2 1 
ATOM   16771 N  N   . ASP J  1 142 ? -3.976  62.399  22.947 1.00 85.29  ? 133 ASP J N   1 
ATOM   16772 C  CA  . ASP J  1 142 ? -4.692  63.509  23.590 1.00 85.81  ? 133 ASP J CA  1 
ATOM   16773 C  C   . ASP J  1 142 ? -5.179  64.579  22.619 1.00 82.13  ? 133 ASP J C   1 
ATOM   16774 O  O   . ASP J  1 142 ? -5.728  65.596  23.038 1.00 81.37  ? 133 ASP J O   1 
ATOM   16775 C  CB  . ASP J  1 142 ? -3.845  64.143  24.702 1.00 79.01  ? 133 ASP J CB  1 
ATOM   16776 C  CG  . ASP J  1 142 ? -2.462  64.556  24.226 1.00 83.62  ? 133 ASP J CG  1 
ATOM   16777 O  OD1 . ASP J  1 142 ? -2.033  64.098  23.138 1.00 77.78  ? 133 ASP J OD1 1 
ATOM   16778 O  OD2 . ASP J  1 142 ? -1.801  65.331  24.956 1.00 76.46  ? 133 ASP J OD2 1 
ATOM   16779 N  N   . SER J  1 143 ? -4.965  64.345  21.328 1.00 82.42  ? 134 SER J N   1 
ATOM   16780 C  CA  . SER J  1 143 ? -5.416  65.264  20.289 1.00 84.37  ? 134 SER J CA  1 
ATOM   16781 C  C   . SER J  1 143 ? -6.526  64.599  19.476 1.00 85.59  ? 134 SER J C   1 
ATOM   16782 O  O   . SER J  1 143 ? -6.945  63.490  19.791 1.00 85.49  ? 134 SER J O   1 
ATOM   16783 C  CB  . SER J  1 143 ? -4.248  65.692  19.394 1.00 74.83  ? 134 SER J CB  1 
ATOM   16784 O  OG  . SER J  1 143 ? -3.731  64.601  18.657 1.00 73.99  ? 134 SER J OG  1 
ATOM   16785 N  N   . GLU J  1 144 ? -7.030  65.277  18.454 1.00 85.62  ? 135 GLU J N   1 
ATOM   16786 C  CA  . GLU J  1 144 ? -8.126  64.710  17.683 1.00 91.30  ? 135 GLU J CA  1 
ATOM   16787 C  C   . GLU J  1 144 ? -7.626  63.526  16.869 1.00 88.00  ? 135 GLU J C   1 
ATOM   16788 O  O   . GLU J  1 144 ? -8.359  62.562  16.661 1.00 84.12  ? 135 GLU J O   1 
ATOM   16789 C  CB  . GLU J  1 144 ? -8.779  65.766  16.775 1.00 108.14 ? 135 GLU J CB  1 
ATOM   16790 C  CG  . GLU J  1 144 ? -10.155 65.367  16.201 1.00 107.40 ? 135 GLU J CG  1 
ATOM   16791 C  CD  . GLU J  1 144 ? -11.087 66.562  15.985 1.00 113.88 ? 135 GLU J CD  1 
ATOM   16792 O  OE1 . GLU J  1 144 ? -10.617 67.718  16.073 1.00 111.98 ? 135 GLU J OE1 1 
ATOM   16793 O  OE2 . GLU J  1 144 ? -12.294 66.345  15.734 1.00 115.02 ? 135 GLU J OE2 1 
ATOM   16794 N  N   . GLU J  1 145 ? -6.368  63.594  16.437 1.00 83.57  ? 136 GLU J N   1 
ATOM   16795 C  CA  . GLU J  1 145 ? -5.803  62.587  15.542 1.00 81.35  ? 136 GLU J CA  1 
ATOM   16796 C  C   . GLU J  1 145 ? -5.660  61.202  16.164 1.00 83.89  ? 136 GLU J C   1 
ATOM   16797 O  O   . GLU J  1 145 ? -5.616  60.195  15.460 1.00 85.49  ? 136 GLU J O   1 
ATOM   16798 C  CB  . GLU J  1 145 ? -4.454  63.046  14.980 1.00 89.13  ? 136 GLU J CB  1 
ATOM   16799 C  CG  . GLU J  1 145 ? -4.564  63.892  13.706 1.00 104.44 ? 136 GLU J CG  1 
ATOM   16800 C  CD  . GLU J  1 145 ? -5.449  63.251  12.632 1.00 102.42 ? 136 GLU J CD  1 
ATOM   16801 O  OE1 . GLU J  1 145 ? -5.109  62.147  12.136 1.00 91.99  ? 136 GLU J OE1 1 
ATOM   16802 O  OE2 . GLU J  1 145 ? -6.491  63.856  12.286 1.00 95.00  ? 136 GLU J OE2 1 
ATOM   16803 N  N   . GLY J  1 146 ? -5.590  61.147  17.484 1.00 85.80  ? 137 GLY J N   1 
ATOM   16804 C  CA  . GLY J  1 146 ? -5.380  59.885  18.160 1.00 75.93  ? 137 GLY J CA  1 
ATOM   16805 C  C   . GLY J  1 146 ? -3.949  59.402  18.000 1.00 79.60  ? 137 GLY J C   1 
ATOM   16806 O  O   . GLY J  1 146 ? -3.132  60.052  17.341 1.00 76.14  ? 137 GLY J O   1 
ATOM   16807 N  N   . ALA J  1 147 ? -3.648  58.263  18.619 1.00 76.74  ? 138 ALA J N   1 
ATOM   16808 C  CA  . ALA J  1 147 ? -2.351  57.618  18.476 1.00 71.67  ? 138 ALA J CA  1 
ATOM   16809 C  C   . ALA J  1 147 ? -2.490  56.327  17.665 1.00 71.60  ? 138 ALA J C   1 
ATOM   16810 O  O   . ALA J  1 147 ? -3.525  55.653  17.710 1.00 66.38  ? 138 ALA J O   1 
ATOM   16811 C  CB  . ALA J  1 147 ? -1.756  57.333  19.837 1.00 69.28  ? 138 ALA J CB  1 
ATOM   16812 N  N   . THR J  1 148 ? -1.461  55.993  16.899 1.00 64.98  ? 139 THR J N   1 
ATOM   16813 C  CA  . THR J  1 148 ? -1.476  54.721  16.196 1.00 69.33  ? 139 THR J CA  1 
ATOM   16814 C  C   . THR J  1 148 ? -0.372  53.801  16.719 1.00 66.80  ? 139 THR J C   1 
ATOM   16815 O  O   . THR J  1 148 ? 0.780   54.209  16.897 1.00 61.57  ? 139 THR J O   1 
ATOM   16816 C  CB  . THR J  1 148 ? -1.411  54.874  14.638 1.00 66.06  ? 139 THR J CB  1 
ATOM   16817 O  OG1 . THR J  1 148 ? -2.619  55.476  14.152 1.00 67.55  ? 139 THR J OG1 1 
ATOM   16818 C  CG2 . THR J  1 148 ? -1.259  53.518  13.971 1.00 60.44  ? 139 THR J CG2 1 
ATOM   16819 N  N   . CYS J  1 149 ? -0.751  52.559  16.984 1.00 62.61  ? 140 CYS J N   1 
ATOM   16820 C  CA  . CYS J  1 149 ? 0.204   51.531  17.359 1.00 68.51  ? 140 CYS J CA  1 
ATOM   16821 C  C   . CYS J  1 149 ? -0.134  50.186  16.717 1.00 66.80  ? 140 CYS J C   1 
ATOM   16822 O  O   . CYS J  1 149 ? -1.286  49.922  16.337 1.00 59.08  ? 140 CYS J O   1 
ATOM   16823 C  CB  . CYS J  1 149 ? 0.322   51.425  18.885 1.00 71.25  ? 140 CYS J CB  1 
ATOM   16824 S  SG  . CYS J  1 149 ? 1.576   52.564  19.576 1.00 93.50  ? 140 CYS J SG  1 
ATOM   16825 N  N   . ALA J  1 150 ? 0.882   49.345  16.573 1.00 61.69  ? 141 ALA J N   1 
ATOM   16826 C  CA  . ALA J  1 150 ? 0.680   48.059  15.928 1.00 57.20  ? 141 ALA J CA  1 
ATOM   16827 C  C   . ALA J  1 150 ? 1.510   46.990  16.617 1.00 61.90  ? 141 ALA J C   1 
ATOM   16828 O  O   . ALA J  1 150 ? 2.629   47.256  17.072 1.00 64.36  ? 141 ALA J O   1 
ATOM   16829 C  CB  . ALA J  1 150 ? 1.031   48.144  14.468 1.00 51.36  ? 141 ALA J CB  1 
ATOM   16830 N  N   . VAL J  1 151 ? 0.944   45.791  16.705 1.00 52.59  ? 142 VAL J N   1 
ATOM   16831 C  CA  . VAL J  1 151 ? 1.641   44.650  17.285 1.00 56.26  ? 142 VAL J CA  1 
ATOM   16832 C  C   . VAL J  1 151 ? 1.514   43.396  16.406 1.00 54.85  ? 142 VAL J C   1 
ATOM   16833 O  O   . VAL J  1 151 ? 0.415   43.032  15.969 1.00 53.69  ? 142 VAL J O   1 
ATOM   16834 C  CB  . VAL J  1 151 ? 1.217   44.388  18.792 1.00 55.75  ? 142 VAL J CB  1 
ATOM   16835 C  CG1 . VAL J  1 151 ? -0.277  44.511  18.992 1.00 49.15  ? 142 VAL J CG1 1 
ATOM   16836 C  CG2 . VAL J  1 151 ? 1.711   43.043  19.281 1.00 46.26  ? 142 VAL J CG2 1 
ATOM   16837 N  N   . LYS J  1 152 ? 2.649   42.749  16.143 1.00 56.93  ? 143 LYS J N   1 
ATOM   16838 C  CA  . LYS J  1 152 ? 2.667   41.535  15.324 1.00 52.42  ? 143 LYS J CA  1 
ATOM   16839 C  C   . LYS J  1 152 ? 2.558   40.243  16.134 1.00 54.23  ? 143 LYS J C   1 
ATOM   16840 O  O   . LYS J  1 152 ? 3.315   40.007  17.082 1.00 51.10  ? 143 LYS J O   1 
ATOM   16841 C  CB  . LYS J  1 152 ? 3.912   41.486  14.431 1.00 52.78  ? 143 LYS J CB  1 
ATOM   16842 C  CG  . LYS J  1 152 ? 3.972   42.583  13.393 1.00 57.15  ? 143 LYS J CG  1 
ATOM   16843 C  CD  . LYS J  1 152 ? 5.232   42.465  12.571 1.00 74.26  ? 143 LYS J CD  1 
ATOM   16844 C  CE  . LYS J  1 152 ? 5.319   43.573  11.537 1.00 80.10  ? 143 LYS J CE  1 
ATOM   16845 N  NZ  . LYS J  1 152 ? 5.380   44.921  12.187 1.00 79.37  ? 143 LYS J NZ  1 
ATOM   16846 N  N   . PHE J  1 153 ? 1.606   39.408  15.729 1.00 54.97  ? 144 PHE J N   1 
ATOM   16847 C  CA  . PHE J  1 153 ? 1.440   38.067  16.269 1.00 51.91  ? 144 PHE J CA  1 
ATOM   16848 C  C   . PHE J  1 153 ? 1.843   37.012  15.252 1.00 50.72  ? 144 PHE J C   1 
ATOM   16849 O  O   . PHE J  1 153 ? 1.605   37.156  14.063 1.00 54.26  ? 144 PHE J O   1 
ATOM   16850 C  CB  . PHE J  1 153 ? -0.017  37.816  16.626 1.00 50.92  ? 144 PHE J CB  1 
ATOM   16851 C  CG  . PHE J  1 153 ? -0.544  38.691  17.717 1.00 51.33  ? 144 PHE J CG  1 
ATOM   16852 C  CD1 . PHE J  1 153 ? -0.567  38.246  19.024 1.00 49.05  ? 144 PHE J CD1 1 
ATOM   16853 C  CD2 . PHE J  1 153 ? -1.056  39.945  17.430 1.00 56.01  ? 144 PHE J CD2 1 
ATOM   16854 C  CE1 . PHE J  1 153 ? -1.073  39.031  20.015 1.00 48.88  ? 144 PHE J CE1 1 
ATOM   16855 C  CE2 . PHE J  1 153 ? -1.564  40.745  18.434 1.00 57.25  ? 144 PHE J CE2 1 
ATOM   16856 C  CZ  . PHE J  1 153 ? -1.570  40.285  19.723 1.00 55.86  ? 144 PHE J CZ  1 
ATOM   16857 N  N   . GLY J  1 154 ? 2.423   35.928  15.741 1.00 59.03  ? 145 GLY J N   1 
ATOM   16858 C  CA  . GLY J  1 154 ? 2.750   34.794  14.899 1.00 54.88  ? 145 GLY J CA  1 
ATOM   16859 C  C   . GLY J  1 154 ? 3.469   33.671  15.624 1.00 47.16  ? 145 GLY J C   1 
ATOM   16860 O  O   . GLY J  1 154 ? 3.835   33.775  16.788 1.00 45.14  ? 145 GLY J O   1 
ATOM   16861 N  N   . SER J  1 155 ? 3.659   32.579  14.912 1.00 39.07  ? 146 SER J N   1 
ATOM   16862 C  CA  . SER J  1 155 ? 4.369   31.463  15.449 1.00 44.09  ? 146 SER J CA  1 
ATOM   16863 C  C   . SER J  1 155 ? 5.787   31.888  15.686 1.00 55.54  ? 146 SER J C   1 
ATOM   16864 O  O   . SER J  1 155 ? 6.411   32.509  14.829 1.00 48.11  ? 146 SER J O   1 
ATOM   16865 C  CB  . SER J  1 155 ? 4.343   30.288  14.504 1.00 48.74  ? 146 SER J CB  1 
ATOM   16866 O  OG  . SER J  1 155 ? 5.392   29.416  14.823 1.00 55.49  ? 146 SER J OG  1 
ATOM   16867 N  N   . TRP J  1 156 ? 6.267   31.552  16.886 1.00 65.68  ? 147 TRP J N   1 
ATOM   16868 C  CA  . TRP J  1 156 ? 7.621   31.837  17.335 1.00 58.03  ? 147 TRP J CA  1 
ATOM   16869 C  C   . TRP J  1 156 ? 8.648   30.845  16.794 1.00 55.89  ? 147 TRP J C   1 
ATOM   16870 O  O   . TRP J  1 156 ? 9.763   31.225  16.481 1.00 64.07  ? 147 TRP J O   1 
ATOM   16871 C  CB  . TRP J  1 156 ? 7.673   31.877  18.870 1.00 56.97  ? 147 TRP J CB  1 
ATOM   16872 C  CG  . TRP J  1 156 ? 9.011   32.296  19.368 1.00 58.72  ? 147 TRP J CG  1 
ATOM   16873 C  CD1 . TRP J  1 156 ? 10.023  31.484  19.795 1.00 58.45  ? 147 TRP J CD1 1 
ATOM   16874 C  CD2 . TRP J  1 156 ? 9.510   33.628  19.444 1.00 55.44  ? 147 TRP J CD2 1 
ATOM   16875 N  NE1 . TRP J  1 156 ? 11.121  32.233  20.143 1.00 56.58  ? 147 TRP J NE1 1 
ATOM   16876 C  CE2 . TRP J  1 156 ? 10.827  33.559  19.935 1.00 56.26  ? 147 TRP J CE2 1 
ATOM   16877 C  CE3 . TRP J  1 156 ? 8.970   34.878  19.151 1.00 53.22  ? 147 TRP J CE3 1 
ATOM   16878 C  CZ2 . TRP J  1 156 ? 11.603  34.681  20.139 1.00 49.13  ? 147 TRP J CZ2 1 
ATOM   16879 C  CZ3 . TRP J  1 156 ? 9.740   35.985  19.348 1.00 56.39  ? 147 TRP J CZ3 1 
ATOM   16880 C  CH2 . TRP J  1 156 ? 11.042  35.884  19.837 1.00 57.14  ? 147 TRP J CH2 1 
ATOM   16881 N  N   . SER J  1 157 ? 8.306   29.562  16.784 1.00 58.77  ? 148 SER J N   1 
ATOM   16882 C  CA  . SER J  1 157 ? 9.219   28.534  16.276 1.00 60.42  ? 148 SER J CA  1 
ATOM   16883 C  C   . SER J  1 157 ? 9.078   28.044  14.819 1.00 63.80  ? 148 SER J C   1 
ATOM   16884 O  O   . SER J  1 157 ? 10.011  27.446  14.283 1.00 67.21  ? 148 SER J O   1 
ATOM   16885 C  CB  . SER J  1 157 ? 9.164   27.340  17.232 1.00 55.91  ? 148 SER J CB  1 
ATOM   16886 O  OG  . SER J  1 157 ? 9.232   27.800  18.584 1.00 63.92  ? 148 SER J OG  1 
ATOM   16887 N  N   . TYR J  1 158 ? 7.966   28.367  14.159 1.00 63.22  ? 149 TYR J N   1 
ATOM   16888 C  CA  . TYR J  1 158 ? 7.606   27.749  12.875 1.00 58.68  ? 149 TYR J CA  1 
ATOM   16889 C  C   . TYR J  1 158 ? 7.504   28.786  11.757 1.00 69.81  ? 149 TYR J C   1 
ATOM   16890 O  O   . TYR J  1 158 ? 7.064   29.922  11.975 1.00 63.76  ? 149 TYR J O   1 
ATOM   16891 C  CB  . TYR J  1 158 ? 6.258   27.014  12.960 1.00 56.88  ? 149 TYR J CB  1 
ATOM   16892 C  CG  . TYR J  1 158 ? 6.242   25.713  13.741 1.00 67.61  ? 149 TYR J CG  1 
ATOM   16893 C  CD1 . TYR J  1 158 ? 6.869   24.575  13.252 1.00 68.73  ? 149 TYR J CD1 1 
ATOM   16894 C  CD2 . TYR J  1 158 ? 5.570   25.613  14.962 1.00 63.62  ? 149 TYR J CD2 1 
ATOM   16895 C  CE1 . TYR J  1 158 ? 6.845   23.378  13.969 1.00 68.59  ? 149 TYR J CE1 1 
ATOM   16896 C  CE2 . TYR J  1 158 ? 5.543   24.429  15.679 1.00 56.61  ? 149 TYR J CE2 1 
ATOM   16897 C  CZ  . TYR J  1 158 ? 6.183   23.313  15.182 1.00 63.60  ? 149 TYR J CZ  1 
ATOM   16898 O  OH  . TYR J  1 158 ? 6.153   22.127  15.882 1.00 58.15  ? 149 TYR J OH  1 
ATOM   16899 N  N   . GLY J  1 159 ? 7.883   28.371  10.552 1.00 64.75  ? 150 GLY J N   1 
ATOM   16900 C  CA  . GLY J  1 159 ? 7.831   29.230  9.390  1.00 65.01  ? 150 GLY J CA  1 
ATOM   16901 C  C   . GLY J  1 159 ? 6.638   28.924  8.509  1.00 68.16  ? 150 GLY J C   1 
ATOM   16902 O  O   . GLY J  1 159 ? 5.766   28.131  8.882  1.00 59.73  ? 150 GLY J O   1 
ATOM   16903 N  N   . GLY J  1 160 ? 6.610   29.550  7.332  1.00 58.34  ? 151 GLY J N   1 
ATOM   16904 C  CA  . GLY J  1 160 ? 5.444   29.522  6.473  1.00 55.12  ? 151 GLY J CA  1 
ATOM   16905 C  C   . GLY J  1 160 ? 5.158   28.160  5.894  1.00 64.22  ? 151 GLY J C   1 
ATOM   16906 O  O   . GLY J  1 160 ? 4.018   27.852  5.547  1.00 63.12  ? 151 GLY J O   1 
ATOM   16907 N  N   . TRP J  1 161 ? 6.203   27.347  5.790  1.00 64.40  ? 152 TRP J N   1 
ATOM   16908 C  CA  . TRP J  1 161 ? 6.085   26.010  5.230  1.00 69.18  ? 152 TRP J CA  1 
ATOM   16909 C  C   . TRP J  1 161 ? 5.526   25.002  6.223  1.00 72.28  ? 152 TRP J C   1 
ATOM   16910 O  O   . TRP J  1 161 ? 4.875   24.034  5.835  1.00 79.31  ? 152 TRP J O   1 
ATOM   16911 C  CB  . TRP J  1 161 ? 7.433   25.546  4.663  1.00 78.15  ? 152 TRP J CB  1 
ATOM   16912 C  CG  . TRP J  1 161 ? 7.773   26.266  3.379  1.00 82.39  ? 152 TRP J CG  1 
ATOM   16913 C  CD1 . TRP J  1 161 ? 6.898   26.910  2.552  1.00 72.15  ? 152 TRP J CD1 1 
ATOM   16914 C  CD2 . TRP J  1 161 ? 9.073   26.429  2.792  1.00 81.34  ? 152 TRP J CD2 1 
ATOM   16915 N  NE1 . TRP J  1 161 ? 7.569   27.455  1.492  1.00 76.89  ? 152 TRP J NE1 1 
ATOM   16916 C  CE2 . TRP J  1 161 ? 8.902   27.176  1.614  1.00 79.61  ? 152 TRP J CE2 1 
ATOM   16917 C  CE3 . TRP J  1 161 ? 10.361  26.016  3.151  1.00 83.61  ? 152 TRP J CE3 1 
ATOM   16918 C  CZ2 . TRP J  1 161 ? 9.972   27.520  0.791  1.00 83.14  ? 152 TRP J CZ2 1 
ATOM   16919 C  CZ3 . TRP J  1 161 ? 11.421  26.359  2.331  1.00 83.65  ? 152 TRP J CZ3 1 
ATOM   16920 C  CH2 . TRP J  1 161 ? 11.220  27.104  1.166  1.00 86.45  ? 152 TRP J CH2 1 
ATOM   16921 N  N   . GLU J  1 162 ? 5.785   25.230  7.505  1.00 70.46  ? 153 GLU J N   1 
ATOM   16922 C  CA  . GLU J  1 162 ? 5.222   24.403  8.566  1.00 62.91  ? 153 GLU J CA  1 
ATOM   16923 C  C   . GLU J  1 162 ? 3.864   24.944  9.036  1.00 60.88  ? 153 GLU J C   1 
ATOM   16924 O  O   . GLU J  1 162 ? 2.859   24.243  8.950  1.00 58.67  ? 153 GLU J O   1 
ATOM   16925 C  CB  . GLU J  1 162 ? 6.211   24.249  9.714  1.00 62.86  ? 153 GLU J CB  1 
ATOM   16926 C  CG  . GLU J  1 162 ? 7.540   23.658  9.293  1.00 62.50  ? 153 GLU J CG  1 
ATOM   16927 C  CD  . GLU J  1 162 ? 8.592   24.720  9.064  1.00 68.75  ? 153 GLU J CD  1 
ATOM   16928 O  OE1 . GLU J  1 162 ? 8.362   25.868  9.492  1.00 66.10  ? 153 GLU J OE1 1 
ATOM   16929 O  OE2 . GLU J  1 162 ? 9.647   24.416  8.465  1.00 67.87  ? 153 GLU J OE2 1 
ATOM   16930 N  N   . ILE J  1 163 ? 3.847   26.170  9.562  1.00 58.00  ? 154 ILE J N   1 
ATOM   16931 C  CA  . ILE J  1 163 ? 2.601   26.830  9.984  1.00 59.95  ? 154 ILE J CA  1 
ATOM   16932 C  C   . ILE J  1 163 ? 2.217   28.015  9.081  1.00 60.46  ? 154 ILE J C   1 
ATOM   16933 O  O   . ILE J  1 163 ? 2.912   29.023  9.024  1.00 54.39  ? 154 ILE J O   1 
ATOM   16934 C  CB  . ILE J  1 163 ? 2.670   27.312  11.464 1.00 52.34  ? 154 ILE J CB  1 
ATOM   16935 C  CG1 . ILE J  1 163 ? 3.061   26.162  12.377 1.00 61.26  ? 154 ILE J CG1 1 
ATOM   16936 C  CG2 . ILE J  1 163 ? 1.346   27.892  11.929 1.00 46.42  ? 154 ILE J CG2 1 
ATOM   16937 C  CD1 . ILE J  1 163 ? 2.653   26.367  13.800 1.00 64.85  ? 154 ILE J CD1 1 
ATOM   16938 N  N   . ASP J  1 164 ? 1.101   27.897  8.378  1.00 54.69  ? 155 ASP J N   1 
ATOM   16939 C  CA  . ASP J  1 164 ? 0.635   29.017  7.592  1.00 62.20  ? 155 ASP J CA  1 
ATOM   16940 C  C   . ASP J  1 164 ? -0.420  29.801  8.354  1.00 64.18  ? 155 ASP J C   1 
ATOM   16941 O  O   . ASP J  1 164 ? -1.307  29.206  8.966  1.00 64.94  ? 155 ASP J O   1 
ATOM   16942 C  CB  . ASP J  1 164 ? 0.066   28.534  6.266  1.00 70.88  ? 155 ASP J CB  1 
ATOM   16943 C  CG  . ASP J  1 164 ? -0.425  29.674  5.400  1.00 71.97  ? 155 ASP J CG  1 
ATOM   16944 O  OD1 . ASP J  1 164 ? 0.201   30.765  5.452  1.00 60.73  ? 155 ASP J OD1 1 
ATOM   16945 O  OD2 . ASP J  1 164 ? -1.437  29.468  4.684  1.00 69.44  ? 155 ASP J OD2 1 
ATOM   16946 N  N   . LEU J  1 165 ? -0.341  31.131  8.271  1.00 62.55  ? 156 LEU J N   1 
ATOM   16947 C  CA  . LEU J  1 165 ? -1.126  32.029  9.122  1.00 63.17  ? 156 LEU J CA  1 
ATOM   16948 C  C   . LEU J  1 165 ? -2.081  32.912  8.315  1.00 59.39  ? 156 LEU J C   1 
ATOM   16949 O  O   . LEU J  1 165 ? -1.656  33.579  7.397  1.00 59.74  ? 156 LEU J O   1 
ATOM   16950 C  CB  . LEU J  1 165 ? -0.159  32.917  9.916  1.00 66.25  ? 156 LEU J CB  1 
ATOM   16951 C  CG  . LEU J  1 165 ? -0.426  33.386  11.350 1.00 60.51  ? 156 LEU J CG  1 
ATOM   16952 C  CD1 . LEU J  1 165 ? -1.077  32.292  12.147 1.00 64.55  ? 156 LEU J CD1 1 
ATOM   16953 C  CD2 . LEU J  1 165 ? 0.881   33.807  11.986 1.00 53.19  ? 156 LEU J CD2 1 
ATOM   16954 N  N   . LYS J  1 166 ? -3.361  32.925  8.686  1.00 64.02  ? 157 LYS J N   1 
ATOM   16955 C  CA  . LYS J  1 166 ? -4.409  33.665  7.973  1.00 64.60  ? 157 LYS J CA  1 
ATOM   16956 C  C   . LYS J  1 166 ? -5.321  34.419  8.945  1.00 69.13  ? 157 LYS J C   1 
ATOM   16957 O  O   . LYS J  1 166 ? -5.268  34.181  10.140 1.00 69.09  ? 157 LYS J O   1 
ATOM   16958 C  CB  . LYS J  1 166 ? -5.262  32.707  7.135  1.00 63.93  ? 157 LYS J CB  1 
ATOM   16959 C  CG  . LYS J  1 166 ? -4.553  32.117  5.928  1.00 68.16  ? 157 LYS J CG  1 
ATOM   16960 C  CD  . LYS J  1 166 ? -5.458  31.157  5.161  1.00 73.50  ? 157 LYS J CD  1 
ATOM   16961 C  CE  . LYS J  1 166 ? -5.303  31.323  3.648  1.00 86.77  ? 157 LYS J CE  1 
ATOM   16962 N  NZ  . LYS J  1 166 ? -3.870  31.376  3.214  1.00 90.81  ? 157 LYS J NZ  1 
ATOM   16963 N  N   . THR J  1 167 ? -6.153  35.328  8.437  1.00 79.24  ? 158 THR J N   1 
ATOM   16964 C  CA  . THR J  1 167 ? -7.170  35.992  9.263  1.00 75.42  ? 158 THR J CA  1 
ATOM   16965 C  C   . THR J  1 167 ? -8.572  35.785  8.698  1.00 81.48  ? 158 THR J C   1 
ATOM   16966 O  O   . THR J  1 167 ? -8.739  35.543  7.502  1.00 77.66  ? 158 THR J O   1 
ATOM   16967 C  CB  . THR J  1 167 ? -6.910  37.495  9.405  1.00 69.36  ? 158 THR J CB  1 
ATOM   16968 O  OG1 . THR J  1 167 ? -6.607  38.047  8.118  1.00 81.51  ? 158 THR J OG1 1 
ATOM   16969 C  CG2 . THR J  1 167 ? -5.743  37.732  10.310 1.00 60.17  ? 158 THR J CG2 1 
ATOM   16970 N  N   . ASP J  1 168 ? -9.579  35.873  9.564  1.00 84.79  ? 159 ASP J N   1 
ATOM   16971 C  CA  . ASP J  1 168 ? -10.969 35.654  9.153  1.00 91.04  ? 159 ASP J CA  1 
ATOM   16972 C  C   . ASP J  1 168 ? -11.424 36.771  8.206  1.00 99.31  ? 159 ASP J C   1 
ATOM   16973 O  O   . ASP J  1 168 ? -11.911 36.503  7.105  1.00 93.54  ? 159 ASP J O   1 
ATOM   16974 C  CB  . ASP J  1 168 ? -11.897 35.574  10.379 1.00 93.61  ? 159 ASP J CB  1 
ATOM   16975 C  CG  . ASP J  1 168 ? -11.850 34.197  11.095 1.00 106.26 ? 159 ASP J CG  1 
ATOM   16976 O  OD1 . ASP J  1 168 ? -10.867 33.431  10.926 1.00 93.41  ? 159 ASP J OD1 1 
ATOM   16977 O  OD2 . ASP J  1 168 ? -12.809 33.881  11.846 1.00 107.28 ? 159 ASP J OD2 1 
ATOM   16978 N  N   . THR J  1 169 ? -11.237 38.017  8.652  1.00 101.64 ? 160 THR J N   1 
ATOM   16979 C  CA  . THR J  1 169 ? -11.544 39.237  7.896  1.00 91.38  ? 160 THR J CA  1 
ATOM   16980 C  C   . THR J  1 169 ? -10.358 40.190  8.132  1.00 88.16  ? 160 THR J C   1 
ATOM   16981 O  O   . THR J  1 169 ? -9.446  39.832  8.869  1.00 92.66  ? 160 THR J O   1 
ATOM   16982 C  CB  . THR J  1 169 ? -12.893 39.846  8.396  1.00 90.35  ? 160 THR J CB  1 
ATOM   16983 O  OG1 . THR J  1 169 ? -13.955 39.493  7.499  1.00 97.04  ? 160 THR J OG1 1 
ATOM   16984 C  CG2 . THR J  1 169 ? -12.834 41.348  8.498  1.00 87.85  ? 160 THR J CG2 1 
ATOM   16985 N  N   . ASP J  1 170 ? -10.324 41.372  7.517  1.00 82.30  ? 161 ASP J N   1 
ATOM   16986 C  CA  . ASP J  1 170 ? -9.272  42.335  7.865  1.00 77.29  ? 161 ASP J CA  1 
ATOM   16987 C  C   . ASP J  1 170 ? -9.740  43.375  8.872  1.00 77.51  ? 161 ASP J C   1 
ATOM   16988 O  O   . ASP J  1 170 ? -8.966  44.212  9.335  1.00 74.57  ? 161 ASP J O   1 
ATOM   16989 C  CB  . ASP J  1 170 ? -8.651  42.988  6.632  1.00 80.51  ? 161 ASP J CB  1 
ATOM   16990 C  CG  . ASP J  1 170 ? -7.753  42.025  5.855  1.00 92.12  ? 161 ASP J CG  1 
ATOM   16991 O  OD1 . ASP J  1 170 ? -7.331  42.391  4.736  1.00 100.44 ? 161 ASP J OD1 1 
ATOM   16992 O  OD2 . ASP J  1 170 ? -7.477  40.902  6.351  1.00 85.26  ? 161 ASP J OD2 1 
ATOM   16993 N  N   . GLN J  1 171 ? -11.011 43.280  9.235  1.00 80.56  ? 162 GLN J N   1 
ATOM   16994 C  CA  . GLN J  1 171 ? -11.637 44.202  10.171 1.00 74.26  ? 162 GLN J CA  1 
ATOM   16995 C  C   . GLN J  1 171 ? -11.789 43.606  11.561 1.00 75.67  ? 162 GLN J C   1 
ATOM   16996 O  O   . GLN J  1 171 ? -12.504 42.606  11.735 1.00 72.79  ? 162 GLN J O   1 
ATOM   16997 C  CB  . GLN J  1 171 ? -13.004 44.607  9.641  1.00 78.28  ? 162 GLN J CB  1 
ATOM   16998 C  CG  . GLN J  1 171 ? -12.918 45.767  8.693  1.00 91.80  ? 162 GLN J CG  1 
ATOM   16999 C  CD  . GLN J  1 171 ? -12.494 47.006  9.423  1.00 84.41  ? 162 GLN J CD  1 
ATOM   17000 O  OE1 . GLN J  1 171 ? -12.769 47.141  10.618 1.00 84.68  ? 162 GLN J OE1 1 
ATOM   17001 N  NE2 . GLN J  1 171 ? -11.809 47.913  8.726  1.00 68.40  ? 162 GLN J NE2 1 
ATOM   17002 N  N   . VAL J  1 172 ? -11.133 44.242  12.542 1.00 72.45  ? 163 VAL J N   1 
ATOM   17003 C  CA  . VAL J  1 172 ? -11.133 43.796  13.940 1.00 60.26  ? 163 VAL J CA  1 
ATOM   17004 C  C   . VAL J  1 172 ? -12.469 44.015  14.612 1.00 62.07  ? 163 VAL J C   1 
ATOM   17005 O  O   . VAL J  1 172 ? -13.018 45.108  14.549 1.00 65.98  ? 163 VAL J O   1 
ATOM   17006 C  CB  . VAL J  1 172 ? -10.128 44.560  14.768 1.00 52.26  ? 163 VAL J CB  1 
ATOM   17007 C  CG1 . VAL J  1 172 ? -10.476 44.404  16.230 1.00 64.28  ? 163 VAL J CG1 1 
ATOM   17008 C  CG2 . VAL J  1 172 ? -8.733  44.070  14.497 1.00 53.65  ? 163 VAL J CG2 1 
ATOM   17009 N  N   . ASP J  1 173 ? -12.983 42.994  15.288 1.00 59.95  ? 164 ASP J N   1 
ATOM   17010 C  CA  . ASP J  1 173 ? -14.305 43.108  15.864 1.00 55.40  ? 164 ASP J CA  1 
ATOM   17011 C  C   . ASP J  1 173 ? -14.261 44.078  17.049 1.00 59.45  ? 164 ASP J C   1 
ATOM   17012 O  O   . ASP J  1 173 ? -13.518 43.882  17.999 1.00 57.16  ? 164 ASP J O   1 
ATOM   17013 C  CB  . ASP J  1 173 ? -14.746 41.721  16.304 1.00 53.44  ? 164 ASP J CB  1 
ATOM   17014 C  CG  . ASP J  1 173 ? -16.035 41.740  17.058 1.00 64.19  ? 164 ASP J CG  1 
ATOM   17015 O  OD1 . ASP J  1 173 ? -16.859 42.627  16.766 1.00 60.92  ? 164 ASP J OD1 1 
ATOM   17016 O  OD2 . ASP J  1 173 ? -16.213 40.881  17.954 1.00 67.54  ? 164 ASP J OD2 1 
ATOM   17017 N  N   . LEU J  1 174 ? -15.019 45.162  16.948 1.00 59.04  ? 165 LEU J N   1 
ATOM   17018 C  CA  . LEU J  1 174 ? -15.197 46.121  18.034 1.00 54.98  ? 165 LEU J CA  1 
ATOM   17019 C  C   . LEU J  1 174 ? -16.514 46.006  18.793 1.00 58.65  ? 165 LEU J C   1 
ATOM   17020 O  O   . LEU J  1 174 ? -16.798 46.819  19.684 1.00 51.36  ? 165 LEU J O   1 
ATOM   17021 C  CB  . LEU J  1 174 ? -14.962 47.538  17.535 1.00 52.76  ? 165 LEU J CB  1 
ATOM   17022 C  CG  . LEU J  1 174 ? -13.536 47.679  17.031 1.00 55.16  ? 165 LEU J CG  1 
ATOM   17023 C  CD1 . LEU J  1 174 ? -13.254 49.079  16.607 1.00 61.10  ? 165 LEU J CD1 1 
ATOM   17024 C  CD2 . LEU J  1 174 ? -12.623 47.303  18.144 1.00 62.53  ? 165 LEU J CD2 1 
ATOM   17025 N  N   . SER J  1 175 ? -17.335 45.038  18.400 1.00 53.58  ? 166 SER J N   1 
ATOM   17026 C  CA  . SER J  1 175 ? -18.695 44.933  18.913 1.00 56.94  ? 166 SER J CA  1 
ATOM   17027 C  C   . SER J  1 175 ? -18.755 44.790  20.438 1.00 60.13  ? 166 SER J C   1 
ATOM   17028 O  O   . SER J  1 175 ? -19.721 45.214  21.073 1.00 55.64  ? 166 SER J O   1 
ATOM   17029 C  CB  . SER J  1 175 ? -19.413 43.756  18.251 1.00 59.54  ? 166 SER J CB  1 
ATOM   17030 O  OG  . SER J  1 175 ? -19.005 42.526  18.830 1.00 68.23  ? 166 SER J OG  1 
ATOM   17031 N  N   . SER J  1 176 ? -17.736 44.157  21.012 1.00 61.01  ? 167 SER J N   1 
ATOM   17032 C  CA  . SER J  1 176 ? -17.672 43.963  22.458 1.00 64.64  ? 167 SER J CA  1 
ATOM   17033 C  C   . SER J  1 176 ? -16.827 44.978  23.251 1.00 62.44  ? 167 SER J C   1 
ATOM   17034 O  O   . SER J  1 176 ? -16.756 44.901  24.475 1.00 65.49  ? 167 SER J O   1 
ATOM   17035 C  CB  . SER J  1 176 ? -17.244 42.533  22.783 1.00 65.37  ? 167 SER J CB  1 
ATOM   17036 O  OG  . SER J  1 176 ? -18.365 41.672  22.775 1.00 65.28  ? 167 SER J OG  1 
ATOM   17037 N  N   . TYR J  1 177 ? -16.204 45.931  22.572 1.00 60.88  ? 168 TYR J N   1 
ATOM   17038 C  CA  . TYR J  1 177 ? -15.360 46.901  23.261 1.00 59.15  ? 168 TYR J CA  1 
ATOM   17039 C  C   . TYR J  1 177 ? -16.120 47.732  24.283 1.00 59.89  ? 168 TYR J C   1 
ATOM   17040 O  O   . TYR J  1 177 ? -17.301 48.018  24.134 1.00 59.50  ? 168 TYR J O   1 
ATOM   17041 C  CB  . TYR J  1 177 ? -14.706 47.834  22.276 1.00 49.17  ? 168 TYR J CB  1 
ATOM   17042 C  CG  . TYR J  1 177 ? -13.602 48.685  22.847 1.00 55.68  ? 168 TYR J CG  1 
ATOM   17043 C  CD1 . TYR J  1 177 ? -12.290 48.240  22.840 1.00 59.26  ? 168 TYR J CD1 1 
ATOM   17044 C  CD2 . TYR J  1 177 ? -13.860 49.945  23.355 1.00 49.78  ? 168 TYR J CD2 1 
ATOM   17045 C  CE1 . TYR J  1 177 ? -11.275 49.015  23.323 1.00 52.69  ? 168 TYR J CE1 1 
ATOM   17046 C  CE2 . TYR J  1 177 ? -12.842 50.740  23.839 1.00 46.82  ? 168 TYR J CE2 1 
ATOM   17047 C  CZ  . TYR J  1 177 ? -11.551 50.268  23.812 1.00 52.62  ? 168 TYR J CZ  1 
ATOM   17048 O  OH  . TYR J  1 177 ? -10.518 51.038  24.282 1.00 55.82  ? 168 TYR J OH  1 
ATOM   17049 N  N   . TYR J  1 178 ? -15.407 48.135  25.320 1.00 57.59  ? 169 TYR J N   1 
ATOM   17050 C  CA  . TYR J  1 178 ? -16.029 48.710  26.497 1.00 60.06  ? 169 TYR J CA  1 
ATOM   17051 C  C   . TYR J  1 178 ? -16.372 50.203  26.310 1.00 63.88  ? 169 TYR J C   1 
ATOM   17052 O  O   . TYR J  1 178 ? -15.486 51.050  26.116 1.00 62.50  ? 169 TYR J O   1 
ATOM   17053 C  CB  . TYR J  1 178 ? -15.124 48.446  27.720 1.00 57.25  ? 169 TYR J CB  1 
ATOM   17054 C  CG  . TYR J  1 178 ? -15.606 49.091  28.978 1.00 58.54  ? 169 TYR J CG  1 
ATOM   17055 C  CD1 . TYR J  1 178 ? -16.920 48.922  29.396 1.00 55.95  ? 169 TYR J CD1 1 
ATOM   17056 C  CD2 . TYR J  1 178 ? -14.753 49.880  29.748 1.00 57.27  ? 169 TYR J CD2 1 
ATOM   17057 C  CE1 . TYR J  1 178 ? -17.382 49.524  30.527 1.00 57.74  ? 169 TYR J CE1 1 
ATOM   17058 C  CE2 . TYR J  1 178 ? -15.202 50.489  30.890 1.00 56.47  ? 169 TYR J CE2 1 
ATOM   17059 C  CZ  . TYR J  1 178 ? -16.522 50.308  31.274 1.00 64.95  ? 169 TYR J CZ  1 
ATOM   17060 O  OH  . TYR J  1 178 ? -16.995 50.909  32.416 1.00 70.58  ? 169 TYR J OH  1 
ATOM   17061 N  N   . ALA J  1 179 ? -17.669 50.508  26.409 1.00 63.28  ? 170 ALA J N   1 
ATOM   17062 C  CA  . ALA J  1 179 ? -18.217 51.837  26.108 1.00 59.85  ? 170 ALA J CA  1 
ATOM   17063 C  C   . ALA J  1 179 ? -17.659 52.968  26.967 1.00 66.05  ? 170 ALA J C   1 
ATOM   17064 O  O   . ALA J  1 179 ? -17.531 54.099  26.505 1.00 68.93  ? 170 ALA J O   1 
ATOM   17065 C  CB  . ALA J  1 179 ? -19.730 51.810  26.213 1.00 49.40  ? 170 ALA J CB  1 
ATOM   17066 N  N   . SER J  1 180 ? -17.372 52.657  28.228 1.00 62.57  ? 171 SER J N   1 
ATOM   17067 C  CA  . SER J  1 180 ? -16.838 53.613  29.203 1.00 65.11  ? 171 SER J CA  1 
ATOM   17068 C  C   . SER J  1 180 ? -15.302 53.640  29.341 1.00 67.34  ? 171 SER J C   1 
ATOM   17069 O  O   . SER J  1 180 ? -14.771 54.236  30.274 1.00 60.32  ? 171 SER J O   1 
ATOM   17070 C  CB  . SER J  1 180 ? -17.543 53.496  30.558 1.00 63.72  ? 171 SER J CB  1 
ATOM   17071 O  OG  . SER J  1 180 ? -18.815 54.122  30.521 1.00 51.84  ? 171 SER J OG  1 
ATOM   17072 N  N   . SER J  1 181 ? -14.599 52.937  28.460 1.00 63.17  ? 172 SER J N   1 
ATOM   17073 C  CA  . SER J  1 181 ? -13.141 52.914  28.510 1.00 59.03  ? 172 SER J CA  1 
ATOM   17074 C  C   . SER J  1 181 ? -12.521 54.298  28.467 1.00 59.28  ? 172 SER J C   1 
ATOM   17075 O  O   . SER J  1 181 ? -13.039 55.207  27.832 1.00 65.71  ? 172 SER J O   1 
ATOM   17076 C  CB  . SER J  1 181 ? -12.571 52.098  27.354 1.00 58.54  ? 172 SER J CB  1 
ATOM   17077 O  OG  . SER J  1 181 ? -11.152 52.199  27.319 1.00 50.90  ? 172 SER J OG  1 
ATOM   17078 N  N   . LYS J  1 182 ? -11.396 54.442  29.151 1.00 59.53  ? 173 LYS J N   1 
ATOM   17079 C  CA  . LYS J  1 182 ? -10.615 55.669  29.117 1.00 58.44  ? 173 LYS J CA  1 
ATOM   17080 C  C   . LYS J  1 182 ? -10.261 56.053  27.684 1.00 59.05  ? 173 LYS J C   1 
ATOM   17081 O  O   . LYS J  1 182 ? -10.011 57.210  27.392 1.00 61.51  ? 173 LYS J O   1 
ATOM   17082 C  CB  . LYS J  1 182 ? -9.335  55.505  29.947 1.00 55.93  ? 173 LYS J CB  1 
ATOM   17083 C  CG  . LYS J  1 182 ? -9.076  56.628  30.926 1.00 60.87  ? 173 LYS J CG  1 
ATOM   17084 C  CD  . LYS J  1 182 ? -10.213 56.785  31.926 1.00 67.41  ? 173 LYS J CD  1 
ATOM   17085 C  CE  . LYS J  1 182 ? -10.295 58.243  32.386 1.00 71.43  ? 173 LYS J CE  1 
ATOM   17086 N  NZ  . LYS J  1 182 ? -11.477 58.514  33.254 1.00 83.05  ? 173 LYS J NZ  1 
ATOM   17087 N  N   . TYR J  1 183 ? -10.242 55.084  26.783 1.00 59.31  ? 174 TYR J N   1 
ATOM   17088 C  CA  . TYR J  1 183 ? -9.913  55.388  25.399 1.00 62.85  ? 174 TYR J CA  1 
ATOM   17089 C  C   . TYR J  1 183 ? -10.977 54.920  24.425 1.00 64.93  ? 174 TYR J C   1 
ATOM   17090 O  O   . TYR J  1 183 ? -11.660 53.934  24.670 1.00 66.71  ? 174 TYR J O   1 
ATOM   17091 C  CB  . TYR J  1 183 ? -8.572  54.783  25.034 1.00 56.72  ? 174 TYR J CB  1 
ATOM   17092 C  CG  . TYR J  1 183 ? -7.465  55.268  25.920 1.00 62.21  ? 174 TYR J CG  1 
ATOM   17093 C  CD1 . TYR J  1 183 ? -6.560  56.211  25.464 1.00 60.41  ? 174 TYR J CD1 1 
ATOM   17094 C  CD2 . TYR J  1 183 ? -7.324  54.790  27.229 1.00 65.00  ? 174 TYR J CD2 1 
ATOM   17095 C  CE1 . TYR J  1 183 ? -5.534  56.663  26.275 1.00 65.48  ? 174 TYR J CE1 1 
ATOM   17096 C  CE2 . TYR J  1 183 ? -6.299  55.243  28.051 1.00 55.93  ? 174 TYR J CE2 1 
ATOM   17097 C  CZ  . TYR J  1 183 ? -5.413  56.175  27.557 1.00 56.61  ? 174 TYR J CZ  1 
ATOM   17098 O  OH  . TYR J  1 183 ? -4.399  56.638  28.320 1.00 55.02  ? 174 TYR J OH  1 
ATOM   17099 N  N   . GLU J  1 184 ? -11.128 55.637  23.320 1.00 67.91  ? 175 GLU J N   1 
ATOM   17100 C  CA  . GLU J  1 184 ? -12.017 55.168  22.271 1.00 72.68  ? 175 GLU J CA  1 
ATOM   17101 C  C   . GLU J  1 184 ? -11.233 54.783  21.008 1.00 72.41  ? 175 GLU J C   1 
ATOM   17102 O  O   . GLU J  1 184 ? -10.153 55.324  20.747 1.00 67.25  ? 175 GLU J O   1 
ATOM   17103 C  CB  . GLU J  1 184 ? -13.139 56.172  21.993 1.00 78.04  ? 175 GLU J CB  1 
ATOM   17104 C  CG  . GLU J  1 184 ? -12.697 57.527  21.491 1.00 82.65  ? 175 GLU J CG  1 
ATOM   17105 C  CD  . GLU J  1 184 ? -13.878 58.367  21.028 1.00 92.16  ? 175 GLU J CD  1 
ATOM   17106 O  OE1 . GLU J  1 184 ? -14.617 58.894  21.896 1.00 88.43  ? 175 GLU J OE1 1 
ATOM   17107 O  OE2 . GLU J  1 184 ? -14.073 58.482  19.795 1.00 90.90  ? 175 GLU J OE2 1 
ATOM   17108 N  N   . ILE J  1 185 ? -11.766 53.816  20.259 1.00 68.93  ? 176 ILE J N   1 
ATOM   17109 C  CA  . ILE J  1 185 ? -11.096 53.270  19.073 1.00 67.92  ? 176 ILE J CA  1 
ATOM   17110 C  C   . ILE J  1 185 ? -11.544 53.990  17.796 1.00 68.59  ? 176 ILE J C   1 
ATOM   17111 O  O   . ILE J  1 185 ? -12.738 54.013  17.491 1.00 66.31  ? 176 ILE J O   1 
ATOM   17112 C  CB  . ILE J  1 185 ? -11.382 51.752  18.926 1.00 64.66  ? 176 ILE J CB  1 
ATOM   17113 C  CG1 . ILE J  1 185 ? -11.159 51.039  20.251 1.00 58.82  ? 176 ILE J CG1 1 
ATOM   17114 C  CG2 . ILE J  1 185 ? -10.480 51.122  17.876 1.00 65.70  ? 176 ILE J CG2 1 
ATOM   17115 C  CD1 . ILE J  1 185 ? -9.710  51.024  20.673 1.00 57.86  ? 176 ILE J CD1 1 
ATOM   17116 N  N   . LEU J  1 186 ? -10.593 54.605  17.084 1.00 66.71  ? 177 LEU J N   1 
ATOM   17117 C  CA  . LEU J  1 186 ? -10.849 55.220  15.775 1.00 62.93  ? 177 LEU J CA  1 
ATOM   17118 C  C   . LEU J  1 186 ? -10.910 54.187  14.666 1.00 67.79  ? 177 LEU J C   1 
ATOM   17119 O  O   . LEU J  1 186 ? -11.844 54.191  13.874 1.00 74.97  ? 177 LEU J O   1 
ATOM   17120 C  CB  . LEU J  1 186 ? -9.767  56.239  15.433 1.00 61.52  ? 177 LEU J CB  1 
ATOM   17121 C  CG  . LEU J  1 186 ? -9.524  57.304  16.498 1.00 60.91  ? 177 LEU J CG  1 
ATOM   17122 C  CD1 . LEU J  1 186 ? -8.371  58.202  16.100 1.00 63.85  ? 177 LEU J CD1 1 
ATOM   17123 C  CD2 . LEU J  1 186 ? -10.789 58.093  16.745 1.00 57.78  ? 177 LEU J CD2 1 
ATOM   17124 N  N   . SER J  1 187 ? -9.909  53.304  14.623 1.00 68.44  ? 178 SER J N   1 
ATOM   17125 C  CA  . SER J  1 187 ? -9.901  52.141  13.725 1.00 71.67  ? 178 SER J CA  1 
ATOM   17126 C  C   . SER J  1 187 ? -9.078  50.994  14.312 1.00 70.84  ? 178 SER J C   1 
ATOM   17127 O  O   . SER J  1 187 ? -8.152  51.219  15.105 1.00 64.49  ? 178 SER J O   1 
ATOM   17128 C  CB  . SER J  1 187 ? -9.341  52.505  12.348 1.00 65.86  ? 178 SER J CB  1 
ATOM   17129 O  OG  . SER J  1 187 ? -7.935  52.674  12.394 1.00 63.72  ? 178 SER J OG  1 
ATOM   17130 N  N   . ALA J  1 188 ? -9.438  49.764  13.956 1.00 66.77  ? 179 ALA J N   1 
ATOM   17131 C  CA  . ALA J  1 188 ? -8.619  48.598  14.291 1.00 62.43  ? 179 ALA J CA  1 
ATOM   17132 C  C   . ALA J  1 188 ? -8.585  47.622  13.130 1.00 58.19  ? 179 ALA J C   1 
ATOM   17133 O  O   . ALA J  1 188 ? -9.635  47.179  12.675 1.00 63.40  ? 179 ALA J O   1 
ATOM   17134 C  CB  . ALA J  1 188 ? -9.151  47.917  15.539 1.00 61.56  ? 179 ALA J CB  1 
ATOM   17135 N  N   . THR J  1 189 ? -7.398  47.267  12.654 1.00 55.14  ? 180 THR J N   1 
ATOM   17136 C  CA  . THR J  1 189 ? -7.321  46.311  11.546 1.00 65.76  ? 180 THR J CA  1 
ATOM   17137 C  C   . THR J  1 189 ? -6.385  45.138  11.822 1.00 62.46  ? 180 THR J C   1 
ATOM   17138 O  O   . THR J  1 189 ? -5.442  45.252  12.598 1.00 61.86  ? 180 THR J O   1 
ATOM   17139 C  CB  . THR J  1 189 ? -6.935  46.980  10.182 1.00 60.91  ? 180 THR J CB  1 
ATOM   17140 O  OG1 . THR J  1 189 ? -5.575  47.430  10.214 1.00 57.01  ? 180 THR J OG1 1 
ATOM   17141 C  CG2 . THR J  1 189 ? -7.853  48.147  9.859  1.00 54.64  ? 180 THR J CG2 1 
ATOM   17142 N  N   . GLN J  1 190 ? -6.666  44.010  11.174 1.00 64.03  ? 181 GLN J N   1 
ATOM   17143 C  CA  . GLN J  1 190 ? -5.816  42.824  11.247 1.00 61.40  ? 181 GLN J CA  1 
ATOM   17144 C  C   . GLN J  1 190 ? -5.429  42.393  9.826  1.00 64.36  ? 181 GLN J C   1 
ATOM   17145 O  O   . GLN J  1 190 ? -6.288  42.162  8.974  1.00 64.59  ? 181 GLN J O   1 
ATOM   17146 C  CB  . GLN J  1 190 ? -6.511  41.689  12.029 1.00 50.85  ? 181 GLN J CB  1 
ATOM   17147 C  CG  . GLN J  1 190 ? -7.823  41.221  11.423 1.00 59.16  ? 181 GLN J CG  1 
ATOM   17148 C  CD  . GLN J  1 190 ? -8.746  40.582  12.428 1.00 55.65  ? 181 GLN J CD  1 
ATOM   17149 O  OE1 . GLN J  1 190 ? -8.483  40.605  13.608 1.00 51.53  ? 181 GLN J OE1 1 
ATOM   17150 N  NE2 . GLN J  1 190 ? -9.847  40.022  11.959 1.00 65.64  ? 181 GLN J NE2 1 
ATOM   17151 N  N   . THR J  1 191 ? -4.129  42.291  9.576  1.00 62.60  ? 182 THR J N   1 
ATOM   17152 C  CA  . THR J  1 191 ? -3.617  42.085  8.228  1.00 64.93  ? 182 THR J CA  1 
ATOM   17153 C  C   . THR J  1 191 ? -2.518  41.040  8.194  1.00 57.19  ? 182 THR J C   1 
ATOM   17154 O  O   . THR J  1 191 ? -1.519  41.182  8.895  1.00 53.26  ? 182 THR J O   1 
ATOM   17155 C  CB  . THR J  1 191 ? -2.983  43.385  7.684  1.00 68.75  ? 182 THR J CB  1 
ATOM   17156 O  OG1 . THR J  1 191 ? -3.777  44.520  8.063  1.00 67.11  ? 182 THR J OG1 1 
ATOM   17157 C  CG2 . THR J  1 191 ? -2.832  43.312  6.173  1.00 62.90  ? 182 THR J CG2 1 
ATOM   17158 N  N   . ARG J  1 192 ? -2.681  40.021  7.351  1.00 55.95  ? 183 ARG J N   1 
ATOM   17159 C  CA  . ARG J  1 192 ? -1.633  39.022  7.147  1.00 51.91  ? 183 ARG J CA  1 
ATOM   17160 C  C   . ARG J  1 192 ? -0.396  39.620  6.479  1.00 49.37  ? 183 ARG J C   1 
ATOM   17161 O  O   . ARG J  1 192 ? -0.482  40.630  5.815  1.00 56.94  ? 183 ARG J O   1 
ATOM   17162 C  CB  . ARG J  1 192 ? -2.159  37.851  6.333  1.00 54.47  ? 183 ARG J CB  1 
ATOM   17163 C  CG  . ARG J  1 192 ? -1.187  36.700  6.212  1.00 51.19  ? 183 ARG J CG  1 
ATOM   17164 C  CD  . ARG J  1 192 ? -1.618  35.717  5.117  1.00 61.95  ? 183 ARG J CD  1 
ATOM   17165 N  NE  . ARG J  1 192 ? -0.793  34.514  5.156  1.00 65.70  ? 183 ARG J NE  1 
ATOM   17166 C  CZ  . ARG J  1 192 ? 0.321   34.328  4.452  1.00 64.33  ? 183 ARG J CZ  1 
ATOM   17167 N  NH1 . ARG J  1 192 ? 0.746   35.261  3.623  1.00 68.25  ? 183 ARG J NH1 1 
ATOM   17168 N  NH2 . ARG J  1 192 ? 1.013   33.203  4.574  1.00 60.09  ? 183 ARG J NH2 1 
ATOM   17169 N  N   . SER J  1 193 ? 0.764   39.022  6.704  1.00 52.00  ? 184 SER J N   1 
ATOM   17170 C  CA  . SER J  1 193 ? 1.991   39.469  6.066  1.00 55.69  ? 184 SER J CA  1 
ATOM   17171 C  C   . SER J  1 193 ? 2.956   38.328  5.898  1.00 60.43  ? 184 SER J C   1 
ATOM   17172 O  O   . SER J  1 193 ? 3.036   37.469  6.763  1.00 63.59  ? 184 SER J O   1 
ATOM   17173 C  CB  . SER J  1 193 ? 2.668   40.543  6.895  1.00 57.29  ? 184 SER J CB  1 
ATOM   17174 O  OG  . SER J  1 193 ? 1.746   41.570  7.149  1.00 73.42  ? 184 SER J OG  1 
ATOM   17175 N  N   . GLU J  1 194 ? 3.709   38.336  4.804  1.00 57.16  ? 185 GLU J N   1 
ATOM   17176 C  CA  . GLU J  1 194 ? 4.804   37.399  4.638  1.00 59.43  ? 185 GLU J CA  1 
ATOM   17177 C  C   . GLU J  1 194 ? 6.103   38.159  4.618  1.00 59.61  ? 185 GLU J C   1 
ATOM   17178 O  O   . GLU J  1 194 ? 6.164   39.288  4.173  1.00 61.79  ? 185 GLU J O   1 
ATOM   17179 C  CB  . GLU J  1 194 ? 4.657   36.625  3.348  1.00 59.43  ? 185 GLU J CB  1 
ATOM   17180 C  CG  . GLU J  1 194 ? 3.281   36.168  3.097  1.00 51.91  ? 185 GLU J CG  1 
ATOM   17181 C  CD  . GLU J  1 194 ? 3.220   35.326  1.881  1.00 62.32  ? 185 GLU J CD  1 
ATOM   17182 O  OE1 . GLU J  1 194 ? 2.921   35.861  0.792  1.00 80.05  ? 185 GLU J OE1 1 
ATOM   17183 O  OE2 . GLU J  1 194 ? 3.491   34.125  2.009  1.00 59.94  ? 185 GLU J OE2 1 
ATOM   17184 N  N   . ARG J  1 195 ? 7.153   37.529  5.095  1.00 64.28  ? 186 ARG J N   1 
ATOM   17185 C  CA  A ARG J  1 195 ? 8.431   38.195  5.197  0.60 69.18  ? 186 ARG J CA  1 
ATOM   17186 C  CA  B ARG J  1 195 ? 8.434   38.195  5.246  0.40 69.29  ? 186 ARG J CA  1 
ATOM   17187 C  C   . ARG J  1 195 ? 9.503   37.202  4.826  1.00 70.58  ? 186 ARG J C   1 
ATOM   17188 O  O   . ARG J  1 195 ? 9.450   36.042  5.208  1.00 72.65  ? 186 ARG J O   1 
ATOM   17189 C  CB  A ARG J  1 195 ? 8.641   38.720  6.618  0.60 70.09  ? 186 ARG J CB  1 
ATOM   17190 C  CB  B ARG J  1 195 ? 8.620   38.613  6.713  0.40 70.10  ? 186 ARG J CB  1 
ATOM   17191 C  CG  A ARG J  1 195 ? 7.571   39.697  7.057  0.60 66.95  ? 186 ARG J CG  1 
ATOM   17192 C  CG  B ARG J  1 195 ? 9.932   39.312  7.042  0.40 74.22  ? 186 ARG J CG  1 
ATOM   17193 C  CD  A ARG J  1 195 ? 8.061   40.554  8.187  0.60 70.78  ? 186 ARG J CD  1 
ATOM   17194 C  CD  B ARG J  1 195 ? 9.787   40.832  7.064  0.40 75.82  ? 186 ARG J CD  1 
ATOM   17195 N  NE  A ARG J  1 195 ? 7.564   41.925  8.113  0.60 70.67  ? 186 ARG J NE  1 
ATOM   17196 N  NE  B ARG J  1 195 ? 11.065  41.486  7.342  0.40 76.39  ? 186 ARG J NE  1 
ATOM   17197 C  CZ  A ARG J  1 195 ? 6.292   42.272  8.279  0.60 73.77  ? 186 ARG J CZ  1 
ATOM   17198 C  CZ  B ARG J  1 195 ? 11.338  42.759  7.073  0.40 73.49  ? 186 ARG J CZ  1 
ATOM   17199 N  NH1 A ARG J  1 195 ? 5.369   41.341  8.499  0.60 72.91  ? 186 ARG J NH1 1 
ATOM   17200 N  NH1 B ARG J  1 195 ? 10.426  43.539  6.512  0.40 70.38  ? 186 ARG J NH1 1 
ATOM   17201 N  NH2 A ARG J  1 195 ? 5.938   43.550  8.210  0.60 68.15  ? 186 ARG J NH2 1 
ATOM   17202 N  NH2 B ARG J  1 195 ? 12.534  43.251  7.364  0.40 77.33  ? 186 ARG J NH2 1 
ATOM   17203 N  N   . PHE J  1 196 ? 10.469  37.640  4.043  1.00 70.48  ? 187 PHE J N   1 
ATOM   17204 C  CA  . PHE J  1 196 ? 11.493  36.704  3.624  1.00 78.03  ? 187 PHE J CA  1 
ATOM   17205 C  C   . PHE J  1 196 ? 12.802  37.236  4.107  1.00 85.55  ? 187 PHE J C   1 
ATOM   17206 O  O   . PHE J  1 196 ? 13.211  38.321  3.719  1.00 99.82  ? 187 PHE J O   1 
ATOM   17207 C  CB  . PHE J  1 196 ? 11.491  36.531  2.100  1.00 76.12  ? 187 PHE J CB  1 
ATOM   17208 C  CG  . PHE J  1 196 ? 10.140  36.185  1.541  1.00 67.49  ? 187 PHE J CG  1 
ATOM   17209 C  CD1 . PHE J  1 196 ? 9.190   37.174  1.328  1.00 70.93  ? 187 PHE J CD1 1 
ATOM   17210 C  CD2 . PHE J  1 196 ? 9.807   34.876  1.253  1.00 62.78  ? 187 PHE J CD2 1 
ATOM   17211 C  CE1 . PHE J  1 196 ? 7.938   36.856  0.834  1.00 70.71  ? 187 PHE J CE1 1 
ATOM   17212 C  CE2 . PHE J  1 196 ? 8.560   34.557  0.760  1.00 67.61  ? 187 PHE J CE2 1 
ATOM   17213 C  CZ  . PHE J  1 196 ? 7.625   35.545  0.551  1.00 66.82  ? 187 PHE J CZ  1 
ATOM   17214 N  N   . TYR J  1 197 ? 13.450  36.500  4.991  1.00 87.21  ? 188 TYR J N   1 
ATOM   17215 C  CA  . TYR J  1 197 ? 14.724  36.965  5.501  1.00 102.20 ? 188 TYR J CA  1 
ATOM   17216 C  C   . TYR J  1 197 ? 15.807  36.666  4.477  1.00 108.28 ? 188 TYR J C   1 
ATOM   17217 O  O   . TYR J  1 197 ? 15.693  35.708  3.712  1.00 105.69 ? 188 TYR J O   1 
ATOM   17218 C  CB  . TYR J  1 197 ? 15.022  36.351  6.866  1.00 107.27 ? 188 TYR J CB  1 
ATOM   17219 C  CG  . TYR J  1 197 ? 13.990  36.724  7.902  1.00 98.04  ? 188 TYR J CG  1 
ATOM   17220 C  CD1 . TYR J  1 197 ? 14.020  37.968  8.516  1.00 99.08  ? 188 TYR J CD1 1 
ATOM   17221 C  CD2 . TYR J  1 197 ? 12.976  35.842  8.252  1.00 87.60  ? 188 TYR J CD2 1 
ATOM   17222 C  CE1 . TYR J  1 197 ? 13.080  38.322  9.458  1.00 99.83  ? 188 TYR J CE1 1 
ATOM   17223 C  CE2 . TYR J  1 197 ? 12.030  36.184  9.193  1.00 95.24  ? 188 TYR J CE2 1 
ATOM   17224 C  CZ  . TYR J  1 197 ? 12.086  37.429  9.799  1.00 102.20 ? 188 TYR J CZ  1 
ATOM   17225 O  OH  . TYR J  1 197 ? 11.147  37.790  10.747 1.00 94.09  ? 188 TYR J OH  1 
ATOM   17226 N  N   . GLU J  1 198 ? 16.840  37.503  4.450  1.00 113.41 ? 189 GLU J N   1 
ATOM   17227 C  CA  . GLU J  1 198 ? 17.909  37.373  3.468  1.00 116.35 ? 189 GLU J CA  1 
ATOM   17228 C  C   . GLU J  1 198 ? 18.422  35.930  3.358  1.00 116.38 ? 189 GLU J C   1 
ATOM   17229 O  O   . GLU J  1 198 ? 18.527  35.368  2.264  1.00 114.43 ? 189 GLU J O   1 
ATOM   17230 C  CB  . GLU J  1 198 ? 19.065  38.299  3.847  1.00 113.09 ? 189 GLU J CB  1 
ATOM   17231 C  CG  . GLU J  1 198 ? 20.387  37.917  3.196  0.00 120.38 ? 189 GLU J CG  1 
ATOM   17232 C  CD  . GLU J  1 198 ? 21.590  38.343  4.014  0.00 122.71 ? 189 GLU J CD  1 
ATOM   17233 O  OE1 . GLU J  1 198 ? 22.435  37.477  4.313  0.00 123.34 ? 189 GLU J OE1 1 
ATOM   17234 O  OE2 . GLU J  1 198 ? 21.697  39.539  4.353  0.00 124.10 ? 189 GLU J OE2 1 
ATOM   17235 N  N   . CYS J  1 199 ? 18.721  35.339  4.509  1.00 112.52 ? 190 CYS J N   1 
ATOM   17236 C  CA  . CYS J  1 199 ? 19.303  34.004  4.591  1.00 110.95 ? 190 CYS J CA  1 
ATOM   17237 C  C   . CYS J  1 199 ? 18.436  32.898  3.991  1.00 113.65 ? 190 CYS J C   1 
ATOM   17238 O  O   . CYS J  1 199 ? 18.896  32.116  3.152  1.00 121.96 ? 190 CYS J O   1 
ATOM   17239 C  CB  . CYS J  1 199 ? 19.594  33.658  6.058  1.00 113.45 ? 190 CYS J CB  1 
ATOM   17240 S  SG  . CYS J  1 199 ? 18.126  33.387  7.111  1.00 117.56 ? 190 CYS J SG  1 
ATOM   17241 N  N   . CYS J  1 200 ? 17.179  32.860  4.420  1.00 112.22 ? 191 CYS J N   1 
ATOM   17242 C  CA  . CYS J  1 200 ? 16.316  31.705  4.235  1.00 108.26 ? 191 CYS J CA  1 
ATOM   17243 C  C   . CYS J  1 200 ? 15.243  31.933  3.170  1.00 105.45 ? 191 CYS J C   1 
ATOM   17244 O  O   . CYS J  1 200 ? 14.715  33.029  3.034  1.00 106.50 ? 191 CYS J O   1 
ATOM   17245 C  CB  . CYS J  1 200 ? 15.708  31.336  5.586  1.00 109.37 ? 191 CYS J CB  1 
ATOM   17246 S  SG  . CYS J  1 200 ? 16.794  31.825  6.974  1.00 129.37 ? 191 CYS J SG  1 
ATOM   17247 N  N   . LYS J  1 201 ? 14.944  30.880  2.417  1.00 102.05 ? 192 LYS J N   1 
ATOM   17248 C  CA  . LYS J  1 201 ? 14.056  30.930  1.267  1.00 93.70  ? 192 LYS J CA  1 
ATOM   17249 C  C   . LYS J  1 201 ? 12.609  30.789  1.694  1.00 88.76  ? 192 LYS J C   1 
ATOM   17250 O  O   . LYS J  1 201 ? 11.691  30.930  0.888  1.00 80.92  ? 192 LYS J O   1 
ATOM   17251 C  CB  . LYS J  1 201 ? 14.422  29.794  0.315  1.00 99.49  ? 192 LYS J CB  1 
ATOM   17252 C  CG  . LYS J  1 201 ? 15.912  29.504  0.294  0.00 104.03 ? 192 LYS J CG  1 
ATOM   17253 C  CD  . LYS J  1 201 ? 16.342  28.844  -0.998 0.00 106.72 ? 192 LYS J CD  1 
ATOM   17254 C  CE  . LYS J  1 201 ? 17.699  29.367  -1.435 0.00 108.63 ? 192 LYS J CE  1 
ATOM   17255 N  NZ  . LYS J  1 201 ? 17.672  30.844  -1.639 0.00 109.09 ? 192 LYS J NZ  1 
ATOM   17256 N  N   . GLU J  1 202 ? 12.416  30.506  2.975  1.00 94.21  ? 193 GLU J N   1 
ATOM   17257 C  CA  . GLU J  1 202 ? 11.088  30.326  3.546  1.00 81.00  ? 193 GLU J CA  1 
ATOM   17258 C  C   . GLU J  1 202 ? 10.424  31.662  3.918  1.00 77.90  ? 193 GLU J C   1 
ATOM   17259 O  O   . GLU J  1 202 ? 11.075  32.551  4.488  1.00 75.26  ? 193 GLU J O   1 
ATOM   17260 C  CB  . GLU J  1 202 ? 11.178  29.424  4.789  1.00 81.22  ? 193 GLU J CB  1 
ATOM   17261 C  CG  . GLU J  1 202 ? 9.948   28.562  4.998  1.00 76.80  ? 193 GLU J CG  1 
ATOM   17262 C  CD  . GLU J  1 202 ? 9.916   27.851  6.331  1.00 70.05  ? 193 GLU J CD  1 
ATOM   17263 O  OE1 . GLU J  1 202 ? 10.968  27.720  6.978  1.00 69.02  ? 193 GLU J OE1 1 
ATOM   17264 O  OE2 . GLU J  1 202 ? 8.820   27.419  6.730  1.00 69.37  ? 193 GLU J OE2 1 
ATOM   17265 N  N   . PRO J  1 203 ? 9.127   31.804  3.585  1.00 70.07  ? 194 PRO J N   1 
ATOM   17266 C  CA  . PRO J  1 203 ? 8.200   32.874  3.980  1.00 68.49  ? 194 PRO J CA  1 
ATOM   17267 C  C   . PRO J  1 203 ? 7.805   32.819  5.468  1.00 64.23  ? 194 PRO J C   1 
ATOM   17268 O  O   . PRO J  1 203 ? 7.424   31.771  5.982  1.00 67.03  ? 194 PRO J O   1 
ATOM   17269 C  CB  . PRO J  1 203 ? 6.971   32.592  3.120  1.00 61.06  ? 194 PRO J CB  1 
ATOM   17270 C  CG  . PRO J  1 203 ? 6.988   31.137  2.943  1.00 64.64  ? 194 PRO J CG  1 
ATOM   17271 C  CD  . PRO J  1 203 ? 8.440   30.774  2.789  1.00 69.90  ? 194 PRO J CD  1 
ATOM   17272 N  N   . TYR J  1 204 ? 7.843   33.940  6.164  1.00 65.89  ? 195 TYR J N   1 
ATOM   17273 C  CA  . TYR J  1 204 ? 7.409   33.925  7.548  1.00 55.85  ? 195 TYR J CA  1 
ATOM   17274 C  C   . TYR J  1 204 ? 6.204   34.802  7.730  1.00 57.61  ? 195 TYR J C   1 
ATOM   17275 O  O   . TYR J  1 204 ? 6.317   36.022  7.730  1.00 62.75  ? 195 TYR J O   1 
ATOM   17276 C  CB  . TYR J  1 204 ? 8.553   34.354  8.441  1.00 58.50  ? 195 TYR J CB  1 
ATOM   17277 C  CG  . TYR J  1 204 ? 9.626   33.316  8.458  1.00 67.71  ? 195 TYR J CG  1 
ATOM   17278 C  CD1 . TYR J  1 204 ? 9.636   32.326  9.423  1.00 71.31  ? 195 TYR J CD1 1 
ATOM   17279 C  CD2 . TYR J  1 204 ? 10.608  33.294  7.483  1.00 68.30  ? 195 TYR J CD2 1 
ATOM   17280 C  CE1 . TYR J  1 204 ? 10.610  31.351  9.431  1.00 74.44  ? 195 TYR J CE1 1 
ATOM   17281 C  CE2 . TYR J  1 204 ? 11.590  32.329  7.485  1.00 75.47  ? 195 TYR J CE2 1 
ATOM   17282 C  CZ  . TYR J  1 204 ? 11.589  31.353  8.460  1.00 78.34  ? 195 TYR J CZ  1 
ATOM   17283 O  OH  . TYR J  1 204 ? 12.567  30.380  8.463  1.00 73.70  ? 195 TYR J OH  1 
ATOM   17284 N  N   . PRO J  1 205 ? 5.038   34.183  7.908  1.00 53.95  ? 196 PRO J N   1 
ATOM   17285 C  CA  . PRO J  1 205 ? 3.800   34.945  8.048  1.00 55.31  ? 196 PRO J CA  1 
ATOM   17286 C  C   . PRO J  1 205 ? 3.625   35.545  9.433  1.00 57.41  ? 196 PRO J C   1 
ATOM   17287 O  O   . PRO J  1 205 ? 4.230   35.105  10.410 1.00 57.84  ? 196 PRO J O   1 
ATOM   17288 C  CB  . PRO J  1 205 ? 2.697   33.905  7.786  1.00 53.74  ? 196 PRO J CB  1 
ATOM   17289 C  CG  . PRO J  1 205 ? 3.378   32.670  7.406  1.00 58.15  ? 196 PRO J CG  1 
ATOM   17290 C  CD  . PRO J  1 205 ? 4.783   32.743  7.915  1.00 59.76  ? 196 PRO J CD  1 
ATOM   17291 N  N   . ASP J  1 206 ? 2.808   36.583  9.494  1.00 58.37  ? 197 ASP J N   1 
ATOM   17292 C  CA  . ASP J  1 206 ? 2.300   37.092  10.754 1.00 60.92  ? 197 ASP J CA  1 
ATOM   17293 C  C   . ASP J  1 206 ? 1.045   37.896  10.465 1.00 60.96  ? 197 ASP J C   1 
ATOM   17294 O  O   . ASP J  1 206 ? 0.846   38.338  9.347  1.00 54.99  ? 197 ASP J O   1 
ATOM   17295 C  CB  . ASP J  1 206 ? 3.343   37.958  11.465 1.00 55.76  ? 197 ASP J CB  1 
ATOM   17296 C  CG  . ASP J  1 206 ? 3.799   39.134  10.627 1.00 61.84  ? 197 ASP J CG  1 
ATOM   17297 O  OD1 . ASP J  1 206 ? 3.004   40.080  10.443 1.00 60.67  ? 197 ASP J OD1 1 
ATOM   17298 O  OD2 . ASP J  1 206 ? 4.958   39.115  10.163 1.00 65.44  ? 197 ASP J OD2 1 
ATOM   17299 N  N   . VAL J  1 207 ? 0.210   38.088  11.478 1.00 63.03  ? 198 VAL J N   1 
ATOM   17300 C  CA  . VAL J  1 207 ? -0.933  38.978  11.381 1.00 57.64  ? 198 VAL J CA  1 
ATOM   17301 C  C   . VAL J  1 207 ? -0.586  40.276  12.093 1.00 56.99  ? 198 VAL J C   1 
ATOM   17302 O  O   . VAL J  1 207 ? -0.190  40.255  13.246 1.00 57.68  ? 198 VAL J O   1 
ATOM   17303 C  CB  . VAL J  1 207 ? -2.153  38.361  12.044 1.00 52.77  ? 198 VAL J CB  1 
ATOM   17304 C  CG1 . VAL J  1 207 ? -3.259  39.377  12.159 1.00 55.11  ? 198 VAL J CG1 1 
ATOM   17305 C  CG2 . VAL J  1 207 ? -2.602  37.176  11.251 1.00 57.90  ? 198 VAL J CG2 1 
ATOM   17306 N  N   . ASN J  1 208 ? -0.705  41.404  11.405 1.00 56.02  ? 199 ASN J N   1 
ATOM   17307 C  CA  . ASN J  1 208 ? -0.371  42.671  12.019 1.00 52.41  ? 199 ASN J CA  1 
ATOM   17308 C  C   . ASN J  1 208 ? -1.625  43.341  12.557 1.00 54.77  ? 199 ASN J C   1 
ATOM   17309 O  O   . ASN J  1 208 ? -2.608  43.484  11.849 1.00 61.83  ? 199 ASN J O   1 
ATOM   17310 C  CB  . ASN J  1 208 ? 0.360   43.567  11.032 1.00 51.54  ? 199 ASN J CB  1 
ATOM   17311 C  CG  . ASN J  1 208 ? 0.859   44.842  11.671 1.00 65.32  ? 199 ASN J CG  1 
ATOM   17312 O  OD1 . ASN J  1 208 ? 1.360   44.837  12.800 1.00 58.23  ? 199 ASN J OD1 1 
ATOM   17313 N  ND2 . ASN J  1 208 ? 0.719   45.953  10.954 1.00 63.00  ? 199 ASN J ND2 1 
ATOM   17314 N  N   . LEU J  1 209 ? -1.600  43.721  13.829 1.00 56.62  ? 200 LEU J N   1 
ATOM   17315 C  CA  . LEU J  1 209 ? -2.758  44.337  14.464 1.00 55.78  ? 200 LEU J CA  1 
ATOM   17316 C  C   . LEU J  1 209 ? -2.472  45.811  14.697 1.00 58.96  ? 200 LEU J C   1 
ATOM   17317 O  O   . LEU J  1 209 ? -1.666  46.160  15.573 1.00 56.93  ? 200 LEU J O   1 
ATOM   17318 C  CB  . LEU J  1 209 ? -3.044  43.651  15.799 1.00 57.90  ? 200 LEU J CB  1 
ATOM   17319 C  CG  . LEU J  1 209 ? -4.139  44.250  16.686 1.00 61.60  ? 200 LEU J CG  1 
ATOM   17320 C  CD1 . LEU J  1 209 ? -5.476  44.208  15.970 1.00 58.52  ? 200 LEU J CD1 1 
ATOM   17321 C  CD2 . LEU J  1 209 ? -4.227  43.514  18.028 1.00 55.00  ? 200 LEU J CD2 1 
ATOM   17322 N  N   . VAL J  1 210 ? -3.143  46.672  13.926 1.00 55.88  ? 201 VAL J N   1 
ATOM   17323 C  CA  . VAL J  1 210 ? -2.931  48.120  14.015 1.00 55.08  ? 201 VAL J CA  1 
ATOM   17324 C  C   . VAL J  1 210 ? -4.136  48.761  14.672 1.00 53.12  ? 201 VAL J C   1 
ATOM   17325 O  O   . VAL J  1 210 ? -5.275  48.492  14.292 1.00 52.50  ? 201 VAL J O   1 
ATOM   17326 C  CB  . VAL J  1 210 ? -2.662  48.789  12.639 1.00 48.91  ? 201 VAL J CB  1 
ATOM   17327 C  CG1 . VAL J  1 210 ? -2.330  50.251  12.829 1.00 48.32  ? 201 VAL J CG1 1 
ATOM   17328 C  CG2 . VAL J  1 210 ? -1.518  48.118  11.926 1.00 45.62  ? 201 VAL J CG2 1 
ATOM   17329 N  N   . VAL J  1 211 ? -3.880  49.582  15.684 1.00 53.39  ? 202 VAL J N   1 
ATOM   17330 C  CA  . VAL J  1 211 ? -4.961  50.209  16.428 1.00 58.05  ? 202 VAL J CA  1 
ATOM   17331 C  C   . VAL J  1 211 ? -4.763  51.717  16.530 1.00 62.03  ? 202 VAL J C   1 
ATOM   17332 O  O   . VAL J  1 211 ? -3.680  52.189  16.859 1.00 57.74  ? 202 VAL J O   1 
ATOM   17333 C  CB  . VAL J  1 211 ? -5.125  49.592  17.830 1.00 57.57  ? 202 VAL J CB  1 
ATOM   17334 C  CG1 . VAL J  1 211 ? -6.239  50.278  18.576 1.00 61.34  ? 202 VAL J CG1 1 
ATOM   17335 C  CG2 . VAL J  1 211 ? -5.431  48.113  17.721 1.00 57.55  ? 202 VAL J CG2 1 
ATOM   17336 N  N   . LYS J  1 212 ? -5.820  52.462  16.214 1.00 68.28  ? 203 LYS J N   1 
ATOM   17337 C  CA  . LYS J  1 212 ? -5.810  53.919  16.277 1.00 63.05  ? 203 LYS J CA  1 
ATOM   17338 C  C   . LYS J  1 212 ? -6.786  54.385  17.367 1.00 63.60  ? 203 LYS J C   1 
ATOM   17339 O  O   . LYS J  1 212 ? -7.981  54.082  17.330 1.00 62.15  ? 203 LYS J O   1 
ATOM   17340 C  CB  . LYS J  1 212 ? -6.178  54.502  14.905 1.00 71.18  ? 203 LYS J CB  1 
ATOM   17341 C  CG  . LYS J  1 212 ? -5.801  55.967  14.706 1.00 76.63  ? 203 LYS J CG  1 
ATOM   17342 C  CD  . LYS J  1 212 ? -5.902  56.353  13.239 1.00 82.44  ? 203 LYS J CD  1 
ATOM   17343 C  CE  . LYS J  1 212 ? -5.749  57.857  13.040 1.00 93.73  ? 203 LYS J CE  1 
ATOM   17344 N  NZ  . LYS J  1 212 ? -6.069  58.261  11.640 1.00 77.03  ? 203 LYS J NZ  1 
ATOM   17345 N  N   . PHE J  1 213 ? -6.272  55.107  18.354 1.00 64.36  ? 204 PHE J N   1 
ATOM   17346 C  CA  . PHE J  1 213 ? -7.072  55.423  19.527 1.00 61.97  ? 204 PHE J CA  1 
ATOM   17347 C  C   . PHE J  1 213 ? -6.698  56.778  20.107 1.00 63.30  ? 204 PHE J C   1 
ATOM   17348 O  O   . PHE J  1 213 ? -5.586  57.256  19.902 1.00 62.00  ? 204 PHE J O   1 
ATOM   17349 C  CB  . PHE J  1 213 ? -6.916  54.314  20.586 1.00 61.74  ? 204 PHE J CB  1 
ATOM   17350 C  CG  . PHE J  1 213 ? -5.512  54.187  21.152 1.00 61.72  ? 204 PHE J CG  1 
ATOM   17351 C  CD1 . PHE J  1 213 ? -5.242  54.556  22.460 1.00 57.72  ? 204 PHE J CD1 1 
ATOM   17352 C  CD2 . PHE J  1 213 ? -4.468  53.703  20.378 1.00 62.20  ? 204 PHE J CD2 1 
ATOM   17353 C  CE1 . PHE J  1 213 ? -3.966  54.455  22.968 1.00 59.36  ? 204 PHE J CE1 1 
ATOM   17354 C  CE2 . PHE J  1 213 ? -3.182  53.595  20.892 1.00 54.58  ? 204 PHE J CE2 1 
ATOM   17355 C  CZ  . PHE J  1 213 ? -2.935  53.971  22.182 1.00 58.25  ? 204 PHE J CZ  1 
ATOM   17356 N  N   . ARG J  1 214 ? -7.639  57.383  20.832 1.00 67.66  ? 205 ARG J N   1 
ATOM   17357 C  CA  . ARG J  1 214 ? -7.406  58.621  21.583 1.00 68.70  ? 205 ARG J CA  1 
ATOM   17358 C  C   . ARG J  1 214 ? -8.245  58.615  22.858 1.00 70.73  ? 205 ARG J C   1 
ATOM   17359 O  O   . ARG J  1 214 ? -9.233  57.877  22.952 1.00 64.61  ? 205 ARG J O   1 
ATOM   17360 C  CB  . ARG J  1 214 ? -7.805  59.840  20.753 1.00 76.21  ? 205 ARG J CB  1 
ATOM   17361 C  CG  . ARG J  1 214 ? -9.296  60.094  20.775 1.00 73.64  ? 205 ARG J CG  1 
ATOM   17362 C  CD  . ARG J  1 214 ? -9.742  60.903  19.594 1.00 75.95  ? 205 ARG J CD  1 
ATOM   17363 N  NE  . ARG J  1 214 ? -11.192 60.852  19.450 1.00 79.06  ? 205 ARG J NE  1 
ATOM   17364 C  CZ  . ARG J  1 214 ? -11.866 61.470  18.488 1.00 71.83  ? 205 ARG J CZ  1 
ATOM   17365 N  NH1 . ARG J  1 214 ? -11.214 62.184  17.581 1.00 76.22  ? 205 ARG J NH1 1 
ATOM   17366 N  NH2 . ARG J  1 214 ? -13.188 61.372  18.436 1.00 61.98  ? 205 ARG J NH2 1 
ATOM   17367 N  N   . GLU J  1 215 ? -7.870  59.451  23.827 1.00 75.50  ? 206 GLU J N   1 
ATOM   17368 C  CA  . GLU J  1 215 ? -8.654  59.582  25.051 1.00 69.51  ? 206 GLU J CA  1 
ATOM   17369 C  C   . GLU J  1 215 ? -10.111 59.910  24.720 1.00 76.57  ? 206 GLU J C   1 
ATOM   17370 O  O   . GLU J  1 215 ? -10.392 60.758  23.873 1.00 78.55  ? 206 GLU J O   1 
ATOM   17371 C  CB  . GLU J  1 215 ? -8.089  60.670  25.956 1.00 68.11  ? 206 GLU J CB  1 
ATOM   17372 C  CG  . GLU J  1 215 ? -6.588  60.704  26.064 1.00 72.99  ? 206 GLU J CG  1 
ATOM   17373 C  CD  . GLU J  1 215 ? -6.110  61.763  27.052 1.00 86.29  ? 206 GLU J CD  1 
ATOM   17374 O  OE1 . GLU J  1 215 ? -6.948  62.314  27.801 1.00 83.32  ? 206 GLU J OE1 1 
ATOM   17375 O  OE2 . GLU J  1 215 ? -4.895  62.050  27.076 1.00 92.92  ? 206 GLU J OE2 1 
ATOM   17376 N  N   . ARG J  1 216 ? -11.034 59.225  25.385 1.00 78.27  ? 207 ARG J N   1 
ATOM   17377 C  CA  . ARG J  1 216 ? -12.456 59.516  25.254 1.00 79.69  ? 207 ARG J CA  1 
ATOM   17378 C  C   . ARG J  1 216 ? -12.771 60.860  25.913 1.00 93.57  ? 207 ARG J C   1 
ATOM   17379 O  O   . ARG J  1 216 ? -12.286 61.149  27.009 1.00 93.32  ? 207 ARG J O   1 
ATOM   17380 C  CB  . ARG J  1 216 ? -13.283 58.411  25.909 1.00 74.45  ? 207 ARG J CB  1 
ATOM   17381 C  CG  . ARG J  1 216 ? -14.782 58.639  25.853 1.00 83.89  ? 207 ARG J CG  1 
ATOM   17382 C  CD  . ARG J  1 216 ? -15.545 57.522  26.560 1.00 90.84  ? 207 ARG J CD  1 
ATOM   17383 N  NE  . ARG J  1 216 ? -15.175 56.192  26.066 1.00 93.93  ? 207 ARG J NE  1 
ATOM   17384 C  CZ  . ARG J  1 216 ? -15.623 55.654  24.930 1.00 93.92  ? 207 ARG J CZ  1 
ATOM   17385 N  NH1 . ARG J  1 216 ? -16.465 56.332  24.149 1.00 94.37  ? 207 ARG J NH1 1 
ATOM   17386 N  NH2 . ARG J  1 216 ? -15.227 54.435  24.570 1.00 79.98  ? 207 ARG J NH2 1 
ATOM   17387 N  N   . ARG J  1 217 ? -13.589 61.674  25.247 1.00 103.57 ? 208 ARG J N   1 
ATOM   17388 C  CA  . ARG J  1 217 ? -13.936 63.012  25.739 1.00 101.13 ? 208 ARG J CA  1 
ATOM   17389 C  C   . ARG J  1 217 ? -12.735 63.716  26.369 1.00 101.19 ? 208 ARG J C   1 
ATOM   17390 O  O   . ARG J  1 217 ? -11.720 63.948  25.700 1.00 95.46  ? 208 ARG J O   1 
ATOM   17391 C  CB  . ARG J  1 217 ? -15.136 62.963  26.703 1.00 98.86  ? 208 ARG J CB  1 
ATOM   17392 C  CG  . ARG J  1 217 ? -16.494 63.080  25.980 1.00 108.03 ? 208 ARG J CG  1 
ATOM   17393 C  CD  . ARG J  1 217 ? -17.665 62.468  26.768 1.00 112.00 ? 208 ARG J CD  1 
ATOM   17394 N  NE  . ARG J  1 217 ? -18.108 61.175  26.227 1.00 113.27 ? 208 ARG J NE  1 
ATOM   17395 C  CZ  . ARG J  1 217 ? -19.383 60.787  26.148 1.00 114.81 ? 208 ARG J CZ  1 
ATOM   17396 N  NH1 . ARG J  1 217 ? -20.352 61.592  26.574 1.00 114.01 ? 208 ARG J NH1 1 
ATOM   17397 N  NH2 . ARG J  1 217 ? -19.693 59.594  25.640 1.00 98.40  ? 208 ARG J NH2 1 
HETATM 17398 MG MG  . MG  K  2 .   ? 24.235  -2.226  62.214 1.00 37.86  ? 222 MG  A MG  1 
HETATM 17399 C  C1  . NAG L  3 .   ? 35.072  -19.411 42.374 1.00 97.67  ? 250 NAG A C1  1 
HETATM 17400 C  C2  . NAG L  3 .   ? 36.384  -18.956 43.000 1.00 107.59 ? 250 NAG A C2  1 
HETATM 17401 C  C3  . NAG L  3 .   ? 37.560  -19.250 42.077 1.00 109.88 ? 250 NAG A C3  1 
HETATM 17402 C  C4  . NAG L  3 .   ? 37.511  -20.687 41.573 1.00 120.07 ? 250 NAG A C4  1 
HETATM 17403 C  C5  . NAG L  3 .   ? 36.126  -21.033 41.041 1.00 112.94 ? 250 NAG A C5  1 
HETATM 17404 C  C6  . NAG L  3 .   ? 36.055  -22.493 40.611 1.00 118.82 ? 250 NAG A C6  1 
HETATM 17405 C  C7  . NAG L  3 .   ? 37.024  -17.008 44.375 1.00 103.24 ? 250 NAG A C7  1 
HETATM 17406 C  C8  . NAG L  3 .   ? 37.930  -15.822 44.135 1.00 93.80  ? 250 NAG A C8  1 
HETATM 17407 N  N2  . NAG L  3 .   ? 36.327  -17.538 43.295 1.00 107.15 ? 250 NAG A N2  1 
HETATM 17408 O  O3  . NAG L  3 .   ? 38.778  -19.034 42.777 1.00 117.35 ? 250 NAG A O3  1 
HETATM 17409 O  O4  . NAG L  3 .   ? 38.472  -20.860 40.540 1.00 132.00 ? 250 NAG A O4  1 
HETATM 17410 O  O5  . NAG L  3 .   ? 35.158  -20.789 42.048 1.00 104.63 ? 250 NAG A O5  1 
HETATM 17411 O  O6  . NAG L  3 .   ? 34.780  -22.757 40.040 1.00 113.78 ? 250 NAG A O6  1 
HETATM 17412 O  O7  . NAG L  3 .   ? 36.907  -17.524 45.596 1.00 99.27  ? 250 NAG A O7  1 
HETATM 17413 C  C1  . NAG M  3 .   ? 39.500  -21.747 41.021 1.00 135.55 ? 251 NAG A C1  1 
HETATM 17414 C  C2  . NAG M  3 .   ? 39.667  -22.901 40.040 1.00 141.03 ? 251 NAG A C2  1 
HETATM 17415 C  C3  . NAG M  3 .   ? 40.773  -23.847 40.492 1.00 143.08 ? 251 NAG A C3  1 
HETATM 17416 C  C4  . NAG M  3 .   ? 42.035  -23.077 40.860 1.00 143.87 ? 251 NAG A C4  1 
HETATM 17417 C  C5  . NAG M  3 .   ? 41.715  -21.912 41.787 1.00 140.09 ? 251 NAG A C5  1 
HETATM 17418 C  C6  . NAG M  3 .   ? 42.965  -21.094 42.087 1.00 134.27 ? 251 NAG A C6  1 
HETATM 17419 C  C7  . NAG M  3 .   ? 38.278  -24.634 38.963 1.00 137.63 ? 251 NAG A C7  1 
HETATM 17420 C  C8  . NAG M  3 .   ? 37.889  -26.016 39.438 1.00 122.52 ? 251 NAG A C8  1 
HETATM 17421 N  N2  . NAG M  3 .   ? 38.418  -23.624 39.908 1.00 142.84 ? 251 NAG A N2  1 
HETATM 17422 O  O3  . NAG M  3 .   ? 41.065  -24.766 39.449 1.00 138.95 ? 251 NAG A O3  1 
HETATM 17423 O  O4  . NAG M  3 .   ? 42.954  -23.953 41.499 1.00 138.10 ? 251 NAG A O4  1 
HETATM 17424 O  O5  . NAG M  3 .   ? 40.741  -21.079 41.181 1.00 142.02 ? 251 NAG A O5  1 
HETATM 17425 O  O6  . NAG M  3 .   ? 43.493  -20.575 40.875 1.00 126.20 ? 251 NAG A O6  1 
HETATM 17426 O  O7  . NAG M  3 .   ? 38.478  -24.404 37.668 1.00 129.40 ? 251 NAG A O7  1 
HETATM 17427 O  O8  . MLK N  4 .   ? 24.588  -35.395 14.389 1.00 90.32  ? 301 MLK A O8  1 
HETATM 17428 C  C8  . MLK N  4 .   ? 24.521  -36.053 15.420 1.00 95.44  ? 301 MLK A C8  1 
HETATM 17429 C  C9  . MLK N  4 .   ? 23.414  -37.018 15.806 1.00 84.41  ? 301 MLK A C9  1 
HETATM 17430 C  C10 . MLK N  4 .   ? 24.221  -38.037 16.628 1.00 82.83  ? 301 MLK A C10 1 
HETATM 17431 C  C12 . MLK N  4 .   ? 23.331  -38.850 17.573 1.00 80.80  ? 301 MLK A C12 1 
HETATM 17432 C  C11 . MLK N  4 .   ? 25.173  -37.066 17.300 1.00 86.59  ? 301 MLK A C11 1 
HETATM 17433 O  O11 . MLK N  4 .   ? 25.625  -37.147 18.421 1.00 93.78  ? 301 MLK A O11 1 
HETATM 17434 N  N7  . MLK N  4 .   ? 25.433  -36.085 16.415 1.00 93.66  ? 301 MLK A N7  1 
HETATM 17435 C  C6  . MLK N  4 .   ? 26.544  -35.210 16.492 1.00 94.11  ? 301 MLK A C6  1 
HETATM 17436 C  C5  . MLK N  4 .   ? 27.833  -35.747 16.461 1.00 90.91  ? 301 MLK A C5  1 
HETATM 17437 C  C4  . MLK N  4 .   ? 28.957  -34.946 16.521 1.00 88.92  ? 301 MLK A C4  1 
HETATM 17438 C  C3  . MLK N  4 .   ? 28.809  -33.572 16.609 1.00 90.22  ? 301 MLK A C3  1 
HETATM 17439 C  C2  . MLK N  4 .   ? 27.551  -33.004 16.632 1.00 87.14  ? 301 MLK A C2  1 
HETATM 17440 C  C1  . MLK N  4 .   ? 26.397  -33.800 16.571 1.00 89.75  ? 301 MLK A C1  1 
HETATM 17441 C  C13 . MLK N  4 .   ? 25.064  -33.142 16.596 1.00 86.59  ? 301 MLK A C13 1 
HETATM 17442 O  O13 . MLK N  4 .   ? 24.046  -33.790 16.760 1.00 85.79  ? 301 MLK A O13 1 
HETATM 17443 O  O14 . MLK N  4 .   ? 24.963  -31.807 16.425 1.00 84.96  ? 301 MLK A O14 1 
HETATM 17444 C  C15 . MLK N  4 .   ? 23.666  -31.154 16.378 1.00 78.22  ? 301 MLK A C15 1 
HETATM 17445 C  C16 . MLK N  4 .   ? 23.949  -29.669 16.169 1.00 83.29  ? 301 MLK A C16 1 
HETATM 17446 C  C21 . MLK N  4 .   ? 24.912  -29.245 17.272 1.00 82.77  ? 301 MLK A C21 1 
HETATM 17447 C  C20 . MLK N  4 .   ? 26.008  -28.294 16.769 1.00 87.39  ? 301 MLK A C20 1 
HETATM 17448 C  C19 . MLK N  4 .   ? 25.542  -27.333 15.683 1.00 89.66  ? 301 MLK A C19 1 
HETATM 17449 O  O19 . MLK N  4 .   ? 24.798  -26.260 16.261 1.00 91.70  ? 301 MLK A O19 1 
HETATM 17450 C  C22 . MLK N  4 .   ? 25.729  -25.515 17.058 1.00 82.30  ? 301 MLK A C22 1 
HETATM 17451 C  C18 . MLK N  4 .   ? 24.776  -27.968 14.552 1.00 93.81  ? 301 MLK A C18 1 
HETATM 17452 C  C17 . MLK N  4 .   ? 24.585  -29.479 14.768 1.00 92.90  ? 301 MLK A C17 1 
HETATM 17453 C  C26 . MLK N  4 .   ? 23.289  -27.515 14.375 1.00 92.73  ? 301 MLK A C26 1 
HETATM 17454 N  N23 . MLK N  4 .   ? 22.610  -27.584 15.656 1.00 85.28  ? 301 MLK A N23 1 
HETATM 17455 C  C24 . MLK N  4 .   ? 21.233  -27.131 15.483 1.00 79.83  ? 301 MLK A C24 1 
HETATM 17456 C  C25 . MLK N  4 .   ? 21.058  -25.680 15.932 1.00 81.02  ? 301 MLK A C25 1 
HETATM 17457 C  C23 . MLK N  4 .   ? 22.641  -28.873 16.320 1.00 83.35  ? 301 MLK A C23 1 
HETATM 17458 C  C30 . MLK N  4 .   ? 25.542  -27.635 13.284 1.00 98.57  ? 301 MLK A C30 1 
HETATM 17459 C  C33 . MLK N  4 .   ? 25.635  -26.116 13.077 1.00 98.61  ? 301 MLK A C33 1 
HETATM 17460 C  C34 . MLK N  4 .   ? 25.255  -25.866 11.590 1.00 99.81  ? 301 MLK A C34 1 
HETATM 17461 C  C35 . MLK N  4 .   ? 23.741  -25.549 11.578 1.00 99.59  ? 301 MLK A C35 1 
HETATM 17462 O  O35 . MLK N  4 .   ? 23.415  -24.646 10.519 1.00 100.38 ? 301 MLK A O35 1 
HETATM 17463 C  C37 . MLK N  4 .   ? 23.084  -23.394 11.130 1.00 92.99  ? 301 MLK A C37 1 
HETATM 17464 C  C36 . MLK N  4 .   ? 22.827  -26.771 11.615 1.00 95.43  ? 301 MLK A C36 1 
HETATM 17465 C  C31 . MLK N  4 .   ? 24.932  -28.212 11.979 1.00 103.63 ? 301 MLK A C31 1 
HETATM 17466 C  C38 . MLK N  4 .   ? 25.464  -27.231 10.893 1.00 100.12 ? 301 MLK A C38 1 
HETATM 17467 O  O38 . MLK N  4 .   ? 24.753  -27.346 9.670  1.00 96.42  ? 301 MLK A O38 1 
HETATM 17468 C  C39 . MLK N  4 .   ? 25.655  -26.920 8.650  1.00 102.77 ? 301 MLK A C39 1 
HETATM 17469 C  C32 . MLK N  4 .   ? 23.410  -28.145 11.937 1.00 100.27 ? 301 MLK A C32 1 
HETATM 17470 O  O32 . MLK N  4 .   ? 22.926  -29.099 10.955 1.00 91.64  ? 301 MLK A O32 1 
HETATM 17471 C  C27 . MLK N  4 .   ? 22.810  -28.556 13.311 1.00 96.78  ? 301 MLK A C27 1 
HETATM 17472 O  O27 . MLK N  4 .   ? 21.389  -28.705 13.172 1.00 90.33  ? 301 MLK A O27 1 
HETATM 17473 C  C28 . MLK N  4 .   ? 23.443  -29.890 13.799 1.00 94.37  ? 301 MLK A C28 1 
HETATM 17474 O  O28 . MLK N  4 .   ? 23.923  -30.758 12.776 1.00 94.80  ? 301 MLK A O28 1 
HETATM 17475 C  C29 . MLK N  4 .   ? 24.860  -31.657 13.388 1.00 88.65  ? 301 MLK A C29 1 
HETATM 17476 C  C1  . MRD O  5 .   ? 20.356  -18.482 26.068 1.00 83.21  ? 305 MRD A C1  1 
HETATM 17477 C  C2  . MRD O  5 .   ? 20.952  -17.733 24.881 1.00 76.36  ? 305 MRD A C2  1 
HETATM 17478 O  O2  . MRD O  5 .   ? 22.386  -17.613 25.059 1.00 76.55  ? 305 MRD A O2  1 
HETATM 17479 C  CM  . MRD O  5 .   ? 20.674  -18.562 23.637 1.00 76.63  ? 305 MRD A CM  1 
HETATM 17480 C  C3  . MRD O  5 .   ? 20.391  -16.321 24.711 1.00 74.81  ? 305 MRD A C3  1 
HETATM 17481 C  C4  . MRD O  5 .   ? 19.146  -16.050 25.555 1.00 86.41  ? 305 MRD A C4  1 
HETATM 17482 O  O4  . MRD O  5 .   ? 18.238  -17.132 25.363 1.00 83.37  ? 305 MRD A O4  1 
HETATM 17483 C  C5  . MRD O  5 .   ? 18.493  -14.715 25.166 1.00 70.70  ? 305 MRD A C5  1 
HETATM 17484 C  C1  . MPD P  6 .   ? 16.769  -22.058 47.805 1.00 75.52  ? 223 MPD A C1  1 
HETATM 17485 C  C2  . MPD P  6 .   ? 17.644  -20.962 47.192 1.00 83.38  ? 223 MPD A C2  1 
HETATM 17486 O  O2  . MPD P  6 .   ? 18.392  -20.308 48.259 1.00 91.05  ? 223 MPD A O2  1 
HETATM 17487 C  CM  . MPD P  6 .   ? 18.652  -21.514 46.184 1.00 62.75  ? 223 MPD A CM  1 
HETATM 17488 C  C3  . MPD P  6 .   ? 16.788  -19.891 46.538 1.00 74.14  ? 223 MPD A C3  1 
HETATM 17489 C  C4  . MPD P  6 .   ? 17.683  -18.664 46.468 1.00 83.37  ? 223 MPD A C4  1 
HETATM 17490 O  O4  . MPD P  6 .   ? 18.500  -18.799 45.318 1.00 87.53  ? 223 MPD A O4  1 
HETATM 17491 C  C5  . MPD P  6 .   ? 16.894  -17.358 46.415 1.00 86.93  ? 223 MPD A C5  1 
HETATM 17492 C  C1  . MPD Q  6 .   ? 13.990  -17.856 30.910 1.00 102.66 ? 306 MPD A C1  1 
HETATM 17493 C  C2  . MPD Q  6 .   ? 14.782  -18.512 32.043 1.00 105.10 ? 306 MPD A C2  1 
HETATM 17494 O  O2  . MPD Q  6 .   ? 15.361  -17.453 32.864 1.00 97.99  ? 306 MPD A O2  1 
HETATM 17495 C  CM  . MPD Q  6 .   ? 13.848  -19.367 32.910 1.00 84.73  ? 306 MPD A CM  1 
HETATM 17496 C  C3  . MPD Q  6 .   ? 15.902  -19.384 31.456 1.00 105.71 ? 306 MPD A C3  1 
HETATM 17497 C  C4  . MPD Q  6 .   ? 17.282  -18.720 31.489 1.00 105.21 ? 306 MPD A C4  1 
HETATM 17498 O  O4  . MPD Q  6 .   ? 18.125  -19.369 32.441 1.00 88.46  ? 306 MPD A O4  1 
HETATM 17499 C  C5  . MPD Q  6 .   ? 17.913  -18.692 30.094 1.00 90.79  ? 306 MPD A C5  1 
HETATM 17500 MG MG  . MG  R  2 .   ? -14.389 -2.758  64.471 1.00 47.57  ? 222 MG  B MG  1 
HETATM 17501 C  C1  . NAG S  3 .   ? 5.395   -21.482 66.655 1.00 87.13  ? 250 NAG B C1  1 
HETATM 17502 C  C2  . NAG S  3 .   ? 4.993   -21.498 68.133 1.00 95.73  ? 250 NAG B C2  1 
HETATM 17503 C  C3  . NAG S  3 .   ? 6.117   -22.003 69.034 1.00 102.73 ? 250 NAG B C3  1 
HETATM 17504 C  C4  . NAG S  3 .   ? 6.886   -23.190 68.450 1.00 104.11 ? 250 NAG B C4  1 
HETATM 17505 C  C5  . NAG S  3 .   ? 7.099   -23.088 66.941 1.00 93.12  ? 250 NAG B C5  1 
HETATM 17506 C  C6  . NAG S  3 .   ? 7.507   -24.453 66.411 1.00 97.04  ? 250 NAG B C6  1 
HETATM 17507 C  C7  . NAG S  3 .   ? 3.305   -19.748 68.426 1.00 101.60 ? 250 NAG B C7  1 
HETATM 17508 C  C8  . NAG S  3 .   ? 3.118   -18.255 68.539 1.00 89.64  ? 250 NAG B C8  1 
HETATM 17509 N  N2  . NAG S  3 .   ? 4.559   -20.188 68.595 1.00 95.30  ? 250 NAG B N2  1 
HETATM 17510 O  O3  . NAG S  3 .   ? 5.514   -22.440 70.229 1.00 105.63 ? 250 NAG B O3  1 
HETATM 17511 O  O4  . NAG S  3 .   ? 8.128   -23.355 69.115 1.00 106.73 ? 250 NAG B O4  1 
HETATM 17512 O  O5  . NAG S  3 .   ? 5.893   -22.749 66.302 1.00 89.59  ? 250 NAG B O5  1 
HETATM 17513 O  O6  . NAG S  3 .   ? 6.611   -25.404 66.946 1.00 100.19 ? 250 NAG B O6  1 
HETATM 17514 O  O7  . NAG S  3 .   ? 2.341   -20.490 68.182 1.00 94.59  ? 250 NAG B O7  1 
HETATM 17515 C  C1  A NAG T  3 .   ? -5.251  -9.145  71.050 0.60 94.71  ? 275 NAG B C1  1 
HETATM 17516 C  C1  B NAG T  3 .   ? -4.340  -14.294 71.823 0.40 96.91  ? 275 NAG B C1  1 
HETATM 17517 C  C2  A NAG T  3 .   ? -5.747  -8.707  72.422 0.60 99.61  ? 275 NAG B C2  1 
HETATM 17518 C  C2  B NAG T  3 .   ? -4.844  -14.259 73.274 0.40 99.51  ? 275 NAG B C2  1 
HETATM 17519 C  C3  A NAG T  3 .   ? -7.240  -8.421  72.394 0.60 102.74 ? 275 NAG B C3  1 
HETATM 17520 C  C3  B NAG T  3 .   ? -5.635  -15.483 73.705 0.40 97.36  ? 275 NAG B C3  1 
HETATM 17521 C  C4  A NAG T  3 .   ? -7.521  -7.432  71.281 0.60 103.62 ? 275 NAG B C4  1 
HETATM 17522 C  C4  B NAG T  3 .   ? -6.604  -15.873 72.612 0.40 98.67  ? 275 NAG B C4  1 
HETATM 17523 C  C5  A NAG T  3 .   ? -7.001  -8.007  69.972 0.60 95.87  ? 275 NAG B C5  1 
HETATM 17524 C  C5  B NAG T  3 .   ? -5.800  -16.220 71.372 0.40 99.99  ? 275 NAG B C5  1 
HETATM 17525 C  C6  A NAG T  3 .   ? -7.326  -7.103  68.787 0.60 89.04  ? 275 NAG B C6  1 
HETATM 17526 C  C6  B NAG T  3 .   ? -6.712  -16.760 70.271 0.40 98.27  ? 275 NAG B C6  1 
HETATM 17527 C  C7  A NAG T  3 .   ? -5.079  -9.296  74.682 0.60 102.93 ? 275 NAG B C7  1 
HETATM 17528 C  C7  B NAG T  3 .   ? -3.835  -13.496 75.352 0.40 103.82 ? 275 NAG B C7  1 
HETATM 17529 C  C8  A NAG T  3 .   ? -4.852  -10.397 75.690 0.60 105.76 ? 275 NAG B C8  1 
HETATM 17530 C  C8  B NAG T  3 .   ? -2.997  -12.268 75.562 0.40 102.63 ? 275 NAG B C8  1 
HETATM 17531 N  N2  A NAG T  3 .   ? -5.425  -9.689  73.445 0.60 98.16  ? 275 NAG B N2  1 
HETATM 17532 N  N2  B NAG T  3 .   ? -3.716  -14.098 74.171 0.40 101.44 ? 275 NAG B N2  1 
HETATM 17533 O  O3  A NAG T  3 .   ? -7.671  -7.864  73.614 0.60 106.33 ? 275 NAG B O3  1 
HETATM 17534 O  O3  B NAG T  3 .   ? -6.359  -15.177 74.872 0.40 100.21 ? 275 NAG B O3  1 
HETATM 17535 O  O4  A NAG T  3 .   ? -8.903  -7.172  71.210 0.60 105.23 ? 275 NAG B O4  1 
HETATM 17536 O  O4  B NAG T  3 .   ? -7.391  -16.963 73.036 0.40 93.77  ? 275 NAG B O4  1 
HETATM 17537 O  O5  A NAG T  3 .   ? -5.607  -8.183  70.084 0.60 92.38  ? 275 NAG B O5  1 
HETATM 17538 O  O5  B NAG T  3 .   ? -5.098  -15.076 70.910 0.40 94.50  ? 275 NAG B O5  1 
HETATM 17539 O  O6  A NAG T  3 .   ? -6.703  -5.854  68.968 0.60 78.64  ? 275 NAG B O6  1 
HETATM 17540 O  O6  B NAG T  3 .   ? -7.548  -17.787 70.766 0.40 93.78  ? 275 NAG B O6  1 
HETATM 17541 O  O7  A NAG T  3 .   ? -4.950  -8.107  75.017 0.60 98.95  ? 275 NAG B O7  1 
HETATM 17542 O  O7  B NAG T  3 .   ? -4.580  -13.914 76.240 0.40 103.49 ? 275 NAG B O7  1 
HETATM 17543 O  O8  . MLK U  4 .   ? 27.094  -39.446 46.216 1.00 88.51  ? 301 MLK B O8  1 
HETATM 17544 C  C8  . MLK U  4 .   ? 26.331  -40.277 46.663 1.00 92.24  ? 301 MLK B C8  1 
HETATM 17545 C  C9  . MLK U  4 .   ? 26.210  -41.714 46.193 1.00 95.28  ? 301 MLK B C9  1 
HETATM 17546 C  C10 . MLK U  4 .   ? 24.744  -42.038 46.547 1.00 99.02  ? 301 MLK B C10 1 
HETATM 17547 C  C12 . MLK U  4 .   ? 23.918  -42.169 45.264 1.00 93.09  ? 301 MLK B C12 1 
HETATM 17548 C  C11 . MLK U  4 .   ? 24.317  -40.836 47.378 1.00 97.50  ? 301 MLK B C11 1 
HETATM 17549 O  O11 . MLK U  4 .   ? 23.165  -40.606 47.708 1.00 83.77  ? 301 MLK B O11 1 
HETATM 17550 N  N7  . MLK U  4 .   ? 25.435  -40.111 47.653 1.00 100.61 ? 301 MLK B N7  1 
HETATM 17551 C  C6  . MLK U  4 .   ? 25.712  -39.337 48.823 1.00 91.92  ? 301 MLK B C6  1 
HETATM 17552 C  C5  . MLK U  4 .   ? 26.174  -39.988 49.971 1.00 88.48  ? 301 MLK B C5  1 
HETATM 17553 C  C4  . MLK U  4 .   ? 26.476  -39.282 51.132 1.00 87.28  ? 301 MLK B C4  1 
HETATM 17554 C  C3  . MLK U  4 .   ? 26.332  -37.904 51.187 1.00 87.54  ? 301 MLK B C3  1 
HETATM 17555 C  C2  . MLK U  4 .   ? 25.888  -37.227 50.071 1.00 81.81  ? 301 MLK B C2  1 
HETATM 17556 C  C1  . MLK U  4 .   ? 25.580  -37.921 48.889 1.00 83.70  ? 301 MLK B C1  1 
HETATM 17557 C  C13 . MLK U  4 .   ? 25.112  -37.120 47.748 1.00 80.34  ? 301 MLK B C13 1 
HETATM 17558 O  O13 . MLK U  4 .   ? 24.647  -37.661 46.766 1.00 82.36  ? 301 MLK B O13 1 
HETATM 17559 O  O14 . MLK U  4 .   ? 25.236  -35.781 47.785 1.00 76.53  ? 301 MLK B O14 1 
HETATM 17560 C  C15 . MLK U  4 .   ? 25.691  -35.104 46.583 1.00 80.57  ? 301 MLK B C15 1 
HETATM 17561 C  C16 . MLK U  4 .   ? 25.993  -33.641 46.892 1.00 79.91  ? 301 MLK B C16 1 
HETATM 17562 C  C21 . MLK U  4 .   ? 25.352  -33.380 48.245 1.00 71.55  ? 301 MLK B C21 1 
HETATM 17563 C  C20 . MLK U  4 .   ? 25.510  -31.916 48.636 1.00 74.09  ? 301 MLK B C20 1 
HETATM 17564 C  C19 . MLK U  4 .   ? 26.951  -31.454 48.506 1.00 80.29  ? 301 MLK B C19 1 
HETATM 17565 O  O19 . MLK U  4 .   ? 26.920  -30.020 48.441 1.00 78.72  ? 301 MLK B O19 1 
HETATM 17566 C  C22 . MLK U  4 .   ? 25.711  -29.576 49.067 1.00 69.32  ? 301 MLK B C22 1 
HETATM 17567 C  C18 . MLK U  4 .   ? 27.763  -31.967 47.333 1.00 85.45  ? 301 MLK B C18 1 
HETATM 17568 C  C17 . MLK U  4 .   ? 27.527  -33.443 46.970 1.00 82.35  ? 301 MLK B C17 1 
HETATM 17569 C  C26 . MLK U  4 .   ? 27.375  -31.291 45.975 1.00 91.57  ? 301 MLK B C26 1 
HETATM 17570 N  N23 . MLK U  4 .   ? 25.939  -31.375 45.796 1.00 83.64  ? 301 MLK B N23 1 
HETATM 17571 C  C24 . MLK U  4 .   ? 25.557  -30.593 44.623 1.00 76.63  ? 301 MLK B C24 1 
HETATM 17572 C  C25 . MLK U  4 .   ? 26.121  -29.172 44.771 1.00 73.16  ? 301 MLK B C25 1 
HETATM 17573 C  C23 . MLK U  4 .   ? 25.392  -32.723 45.802 1.00 81.69  ? 301 MLK B C23 1 
HETATM 17574 C  C30 . MLK U  4 .   ? 29.237  -31.708 47.599 1.00 89.30  ? 301 MLK B C30 1 
HETATM 17575 C  C33 . MLK U  4 .   ? 29.589  -30.228 47.837 1.00 85.62  ? 301 MLK B C33 1 
HETATM 17576 C  C34 . MLK U  4 .   ? 30.899  -29.962 47.037 1.00 98.58  ? 301 MLK B C34 1 
HETATM 17577 C  C35 . MLK U  4 .   ? 30.494  -29.341 45.666 1.00 104.53 ? 301 MLK B C35 1 
HETATM 17578 O  O35 . MLK U  4 .   ? 31.617  -28.774 44.978 1.00 111.25 ? 301 MLK B O35 1 
HETATM 17579 C  C37 . MLK U  4 .   ? 32.468  -28.165 45.962 1.00 107.16 ? 301 MLK B C37 1 
HETATM 17580 C  C36 . MLK U  4 .   ? 29.698  -30.258 44.743 1.00 85.99  ? 301 MLK B C36 1 
HETATM 17581 C  C31 . MLK U  4 .   ? 30.166  -32.156 46.438 1.00 99.78  ? 301 MLK B C31 1 
HETATM 17582 C  C38 . MLK U  4 .   ? 31.477  -31.381 46.788 1.00 103.39 ? 301 MLK B C38 1 
HETATM 17583 O  O38 . MLK U  4 .   ? 32.462  -31.458 45.763 1.00 102.00 ? 301 MLK B O38 1 
HETATM 17584 C  C39 . MLK U  4 .   ? 33.009  -32.780 45.797 1.00 105.02 ? 301 MLK B C39 1 
HETATM 17585 C  C32 . MLK U  4 .   ? 29.651  -31.755 45.050 1.00 93.38  ? 301 MLK B C32 1 
HETATM 17586 O  O32 . MLK U  4 .   ? 30.367  -32.499 44.024 1.00 83.96  ? 301 MLK B O32 1 
HETATM 17587 C  C27 . MLK U  4 .   ? 28.157  -32.154 44.951 1.00 92.02  ? 301 MLK B C27 1 
HETATM 17588 O  O27 . MLK U  4 .   ? 27.681  -32.066 43.599 1.00 94.14  ? 301 MLK B O27 1 
HETATM 17589 C  C28 . MLK U  4 .   ? 27.976  -33.590 45.482 1.00 88.45  ? 301 MLK B C28 1 
HETATM 17590 O  O28 . MLK U  4 .   ? 29.148  -34.369 45.291 1.00 93.22  ? 301 MLK B O28 1 
HETATM 17591 C  C29 . MLK U  4 .   ? 28.762  -35.736 45.360 1.00 91.15  ? 301 MLK B C29 1 
HETATM 17592 C  C1  . MRD V  5 .   ? -1.891  -20.057 50.179 1.00 86.47  ? 305 MRD B C1  1 
HETATM 17593 C  C2  . MRD V  5 .   ? -3.328  -19.695 49.804 1.00 95.66  ? 305 MRD B C2  1 
HETATM 17594 O  O2  . MRD V  5 .   ? -3.787  -18.613 50.684 1.00 85.61  ? 305 MRD B O2  1 
HETATM 17595 C  CM  . MRD V  5 .   ? -3.332  -19.190 48.353 1.00 75.61  ? 305 MRD B CM  1 
HETATM 17596 C  C3  . MRD V  5 .   ? -4.204  -20.953 49.954 1.00 75.43  ? 305 MRD B C3  1 
HETATM 17597 C  C4  . MRD V  5 .   ? -4.837  -21.120 51.341 1.00 73.19  ? 305 MRD B C4  1 
HETATM 17598 O  O4  . MRD V  5 .   ? -6.011  -20.341 51.399 1.00 70.65  ? 305 MRD B O4  1 
HETATM 17599 C  C5  . MRD V  5 .   ? -3.918  -20.738 52.503 1.00 66.83  ? 305 MRD B C5  1 
HETATM 17600 MG MG  . MG  W  2 .   ? -29.054 1.789   27.219 1.00 57.00  ? 222 MG  C MG  1 
HETATM 17601 C  C1  . NAG X  3 .   ? -27.665 -19.130 46.351 1.00 96.61  ? 250 NAG C C1  1 
HETATM 17602 C  C2  . NAG X  3 .   ? -29.209 -18.945 46.112 1.00 106.46 ? 250 NAG C C2  1 
HETATM 17603 C  C3  . NAG X  3 .   ? -30.029 -19.379 47.311 1.00 110.88 ? 250 NAG C C3  1 
HETATM 17604 C  C4  . NAG X  3 .   ? -29.597 -20.778 47.709 1.00 109.10 ? 250 NAG C C4  1 
HETATM 17605 C  C5  . NAG X  3 .   ? -28.146 -20.718 48.179 1.00 100.18 ? 250 NAG C C5  1 
HETATM 17606 C  C6  . NAG X  3 .   ? -27.660 -22.105 48.543 1.00 102.51 ? 250 NAG C C6  1 
HETATM 17607 C  C7  . NAG X  3 .   ? -30.416 -17.333 44.690 1.00 107.49 ? 250 NAG C C7  1 
HETATM 17608 C  C8  . NAG X  3 .   ? -31.789 -17.978 44.673 1.00 100.55 ? 250 NAG C C8  1 
HETATM 17609 N  N2  . NAG X  3 .   ? -29.613 -17.576 45.757 1.00 109.58 ? 250 NAG C N2  1 
HETATM 17610 O  O3  . NAG X  3 .   ? -31.362 -19.399 46.888 1.00 116.87 ? 250 NAG C O3  1 
HETATM 17611 O  O4  . NAG X  3 .   ? -30.456 -21.318 48.702 1.00 109.08 ? 250 NAG C O4  1 
HETATM 17612 O  O5  . NAG X  3 .   ? -27.272 -20.248 47.170 1.00 91.81  ? 250 NAG C O5  1 
HETATM 17613 O  O6  . NAG X  3 .   ? -27.937 -22.949 47.451 1.00 95.13  ? 250 NAG C O6  1 
HETATM 17614 O  O7  . NAG X  3 .   ? -30.100 -16.606 43.732 1.00 100.78 ? 250 NAG C O7  1 
HETATM 17615 O  O8  . MLK Y  4 .   ? -2.667  -40.249 58.527 1.00 102.16 ? 301 MLK C O8  1 
HETATM 17616 C  C8  . MLK Y  4 .   ? -3.421  -40.901 57.828 1.00 93.98  ? 301 MLK C C8  1 
HETATM 17617 C  C9  . MLK Y  4 .   ? -3.159  -42.302 57.308 1.00 92.38  ? 301 MLK C C9  1 
HETATM 17618 C  C10 . MLK Y  4 .   ? -4.406  -42.594 56.442 1.00 97.26  ? 301 MLK C C10 1 
HETATM 17619 C  C12 . MLK Y  4 .   ? -4.038  -43.173 55.072 1.00 73.28  ? 301 MLK C C12 1 
HETATM 17620 C  C11 . MLK Y  4 .   ? -5.038  -41.221 56.333 1.00 91.11  ? 301 MLK C C11 1 
HETATM 17621 O  O11 . MLK Y  4 .   ? -5.777  -40.849 55.444 1.00 86.40  ? 301 MLK C O11 1 
HETATM 17622 N  N7  . MLK Y  4 .   ? -4.631  -40.511 57.401 1.00 92.66  ? 301 MLK C N7  1 
HETATM 17623 C  C6  . MLK Y  4 .   ? -5.411  -39.538 58.063 1.00 92.91  ? 301 MLK C C6  1 
HETATM 17624 C  C5  . MLK Y  4 .   ? -6.482  -40.030 58.798 1.00 90.36  ? 301 MLK C C5  1 
HETATM 17625 C  C4  . MLK Y  4 .   ? -7.328  -39.193 59.500 1.00 92.33  ? 301 MLK C C4  1 
HETATM 17626 C  C3  . MLK Y  4 .   ? -7.123  -37.826 59.504 1.00 89.04  ? 301 MLK C C3  1 
HETATM 17627 C  C2  . MLK Y  4 .   ? -6.065  -37.306 58.791 1.00 91.39  ? 301 MLK C C2  1 
HETATM 17628 C  C1  . MLK Y  4 .   ? -5.189  -38.127 58.062 1.00 89.65  ? 301 MLK C C1  1 
HETATM 17629 C  C13 . MLK Y  4 .   ? -4.099  -37.425 57.342 1.00 85.01  ? 301 MLK C C13 1 
HETATM 17630 O  O13 . MLK Y  4 .   ? -3.192  -38.021 56.798 1.00 89.17  ? 301 MLK C O13 1 
HETATM 17631 O  O14 . MLK Y  4 .   ? -4.115  -36.074 57.313 1.00 82.18  ? 301 MLK C O14 1 
HETATM 17632 C  C15 . MLK Y  4 .   ? -2.863  -35.343 57.225 1.00 81.93  ? 301 MLK C C15 1 
HETATM 17633 C  C16 . MLK Y  4 .   ? -2.966  -33.997 57.958 1.00 86.22  ? 301 MLK C C16 1 
HETATM 17634 C  C21 . MLK Y  4 .   ? -4.386  -33.462 57.753 1.00 81.86  ? 301 MLK C C21 1 
HETATM 17635 C  C20 . MLK Y  4 .   ? -4.952  -32.814 59.019 1.00 81.73  ? 301 MLK C C20 1 
HETATM 17636 C  C19 . MLK Y  4 .   ? -3.898  -32.032 59.788 1.00 87.91  ? 301 MLK C C19 1 
HETATM 17637 O  O19 . MLK Y  4 .   ? -3.697  -30.768 59.124 1.00 79.89  ? 301 MLK C O19 1 
HETATM 17638 C  C22 . MLK Y  4 .   ? -4.991  -30.175 58.977 1.00 64.63  ? 301 MLK C C22 1 
HETATM 17639 C  C18 . MLK Y  4 .   ? -2.618  -32.800 60.098 1.00 84.98  ? 301 MLK C C18 1 
HETATM 17640 C  C17 . MLK Y  4 .   ? -2.624  -34.197 59.459 1.00 86.54  ? 301 MLK C C17 1 
HETATM 17641 C  C26 . MLK Y  4 .   ? -1.302  -32.215 59.499 1.00 85.90  ? 301 MLK C C26 1 
HETATM 17642 N  N23 . MLK Y  4 .   ? -1.523  -31.919 58.104 1.00 87.20  ? 301 MLK C N23 1 
HETATM 17643 C  C24 . MLK Y  4 .   ? -0.323  -31.298 57.545 1.00 84.57  ? 301 MLK C C24 1 
HETATM 17644 C  C25 . MLK Y  4 .   ? -0.495  -29.788 57.333 1.00 85.01  ? 301 MLK C C25 1 
HETATM 17645 C  C23 . MLK Y  4 .   ? -1.952  -33.041 57.299 1.00 83.93  ? 301 MLK C C23 1 
HETATM 17646 C  C30 . MLK Y  4 .   ? -2.448  -32.900 61.612 1.00 92.04  ? 301 MLK C C30 1 
HETATM 17647 C  C33 . MLK Y  4 .   ? -2.428  -31.533 62.322 1.00 92.15  ? 301 MLK C C33 1 
HETATM 17648 C  C34 . MLK Y  4 .   ? -1.183  -31.534 63.252 1.00 92.47  ? 301 MLK C C34 1 
HETATM 17649 C  C35 . MLK Y  4 .   ? -0.052  -30.954 62.367 1.00 100.31 ? 301 MLK C C35 1 
HETATM 17650 O  O35 . MLK Y  4 .   ? 0.851   -30.111 63.091 1.00 95.25  ? 301 MLK C O35 1 
HETATM 17651 C  C37 . MLK Y  4 .   ? 0.973   -28.878 62.368 1.00 84.02  ? 301 MLK C C37 1 
HETATM 17652 C  C36 . MLK Y  4 .   ? 0.682   -31.983 61.506 1.00 100.65 ? 301 MLK C C36 1 
HETATM 17653 C  C31 . MLK Y  4 .   ? -1.169  -33.645 62.095 1.00 94.98  ? 301 MLK C C31 1 
HETATM 17654 C  C38 . MLK Y  4 .   ? -0.906  -33.034 63.509 1.00 95.45  ? 301 MLK C C38 1 
HETATM 17655 O  O38 . MLK Y  4 .   ? 0.411   -33.303 63.968 1.00 91.74  ? 301 MLK C O38 1 
HETATM 17656 C  C39 . MLK Y  4 .   ? 0.298   -33.711 65.330 1.00 93.17  ? 301 MLK C C39 1 
HETATM 17657 C  C32 . MLK Y  4 .   ? 0.062   -33.354 61.250 1.00 98.16  ? 301 MLK C C32 1 
HETATM 17658 O  O32 . MLK Y  4 .   ? 1.072   -34.379 61.474 1.00 97.01  ? 301 MLK C O32 1 
HETATM 17659 C  C27 . MLK Y  4 .   ? -0.310  -33.387 59.744 1.00 93.07  ? 301 MLK C C27 1 
HETATM 17660 O  O27 . MLK Y  4 .   ? 0.882   -33.393 58.946 1.00 91.14  ? 301 MLK C O27 1 
HETATM 17661 C  C28 . MLK Y  4 .   ? -1.134  -34.654 59.421 1.00 91.84  ? 301 MLK C C28 1 
HETATM 17662 O  O28 . MLK Y  4 .   ? -0.819  -35.765 60.267 1.00 95.68  ? 301 MLK C O28 1 
HETATM 17663 C  C29 . MLK Y  4 .   ? -1.682  -36.862 59.939 1.00 88.01  ? 301 MLK C C29 1 
HETATM 17664 C  C1  . MPD Z  6 .   ? -21.230 -5.642  45.905 1.00 83.00  ? 306 MPD C C1  1 
HETATM 17665 C  C2  . MPD Z  6 .   ? -19.887 -5.420  46.607 1.00 97.49  ? 306 MPD C C2  1 
HETATM 17666 O  O2  . MPD Z  6 .   ? -18.952 -4.902  45.610 1.00 88.45  ? 306 MPD C O2  1 
HETATM 17667 C  CM  . MPD Z  6 .   ? -20.028 -4.411  47.754 1.00 87.89  ? 306 MPD C CM  1 
HETATM 17668 C  C3  . MPD Z  6 .   ? -19.373 -6.773  47.121 1.00 97.31  ? 306 MPD C C3  1 
HETATM 17669 C  C4  . MPD Z  6 .   ? -18.640 -6.752  48.473 1.00 100.15 ? 306 MPD C C4  1 
HETATM 17670 O  O4  . MPD Z  6 .   ? -19.108 -7.830  49.270 1.00 82.96  ? 306 MPD C O4  1 
HETATM 17671 C  C5  . MPD Z  6 .   ? -17.113 -6.831  48.345 1.00 86.51  ? 306 MPD C C5  1 
HETATM 17672 C  C1  . MRD AA 5 .   ? -12.964 -17.793 32.261 1.00 72.81  ? 305 MRD D C1  1 
HETATM 17673 C  C2  . MRD AA 5 .   ? -14.298 -17.194 31.795 1.00 90.59  ? 305 MRD D C2  1 
HETATM 17674 O  O2  . MRD AA 5 .   ? -15.168 -16.977 32.935 1.00 86.01  ? 305 MRD D O2  1 
HETATM 17675 C  CM  . MRD AA 5 .   ? -14.100 -15.823 31.131 1.00 81.76  ? 305 MRD D CM  1 
HETATM 17676 C  C3  . MRD AA 5 .   ? -14.957 -18.174 30.817 1.00 84.28  ? 305 MRD D C3  1 
HETATM 17677 C  C4  . MRD AA 5 .   ? -16.043 -19.079 31.398 1.00 74.44  ? 305 MRD D C4  1 
HETATM 17678 O  O4  . MRD AA 5 .   ? -17.260 -18.366 31.450 1.00 74.17  ? 305 MRD D O4  1 
HETATM 17679 C  C5  . MRD AA 5 .   ? -15.694 -19.629 32.779 1.00 72.71  ? 305 MRD D C5  1 
HETATM 17680 C  C1  . NAG BA 3 .   ? -16.887 -15.021 8.712  1.00 95.37  ? 250 NAG D C1  1 
HETATM 17681 C  C2  . NAG BA 3 .   ? -17.626 -14.699 7.407  1.00 103.61 ? 250 NAG D C2  1 
HETATM 17682 C  C3  . NAG BA 3 .   ? -19.112 -14.953 7.526  1.00 104.96 ? 250 NAG D C3  1 
HETATM 17683 C  C4  . NAG BA 3 .   ? -19.338 -16.339 8.110  1.00 113.44 ? 250 NAG D C4  1 
HETATM 17684 C  C5  . NAG BA 3 .   ? -18.637 -16.551 9.445  1.00 98.09  ? 250 NAG D C5  1 
HETATM 17685 C  C6  . NAG BA 3 .   ? -18.793 -18.021 9.844  1.00 105.36 ? 250 NAG D C6  1 
HETATM 17686 C  C7  . NAG BA 3 .   ? -16.363 -12.837 6.372  1.00 104.64 ? 250 NAG D C7  1 
HETATM 17687 C  C8  . NAG BA 3 .   ? -16.239 -11.337 6.232  1.00 94.59  ? 250 NAG D C8  1 
HETATM 17688 N  N2  . NAG BA 3 .   ? -17.456 -13.305 7.010  1.00 100.30 ? 250 NAG D N2  1 
HETATM 17689 O  O3  . NAG BA 3 .   ? -19.695 -14.829 6.246  1.00 108.82 ? 250 NAG D O3  1 
HETATM 17690 O  O4  . NAG BA 3 .   ? -20.716 -16.598 8.267  1.00 123.17 ? 250 NAG D O4  1 
HETATM 17691 O  O5  . NAG BA 3 .   ? -17.267 -16.198 9.403  1.00 87.93  ? 250 NAG D O5  1 
HETATM 17692 O  O6  . NAG BA 3 .   ? -18.267 -18.857 8.831  1.00 96.44  ? 250 NAG D O6  1 
HETATM 17693 O  O7  . NAG BA 3 .   ? -15.469 -13.564 5.908  1.00 104.35 ? 250 NAG D O7  1 
HETATM 17694 C  C1  . NAG CA 3 .   ? -21.030 -17.692 7.394  1.00 130.17 ? 251 NAG D C1  1 
HETATM 17695 C  C2  . NAG CA 3 .   ? -22.514 -17.991 7.485  1.00 133.07 ? 251 NAG D C2  1 
HETATM 17696 C  C3  . NAG CA 3 .   ? -22.842 -19.097 6.532  1.00 132.91 ? 251 NAG D C3  1 
HETATM 17697 C  C4  . NAG CA 3 .   ? -22.542 -18.609 5.160  1.00 134.66 ? 251 NAG D C4  1 
HETATM 17698 C  C5  . NAG CA 3 .   ? -21.057 -18.349 5.119  1.00 135.86 ? 251 NAG D C5  1 
HETATM 17699 C  C6  . NAG CA 3 .   ? -20.735 -17.820 3.739  1.00 135.74 ? 251 NAG D C6  1 
HETATM 17700 C  C7  . NAG CA 3 .   ? -22.882 -19.792 9.023  1.00 124.54 ? 251 NAG D C7  1 
HETATM 17701 C  C8  . NAG CA 3 .   ? -22.550 -20.202 10.411 1.00 118.22 ? 251 NAG D C8  1 
HETATM 17702 N  N2  . NAG CA 3 .   ? -22.863 -18.494 8.782  1.00 130.62 ? 251 NAG D N2  1 
HETATM 17703 O  O3  . NAG CA 3 .   ? -24.212 -19.332 6.640  1.00 131.98 ? 251 NAG D O3  1 
HETATM 17704 O  O4  . NAG CA 3 .   ? -22.871 -19.658 4.301  1.00 128.12 ? 251 NAG D O4  1 
HETATM 17705 O  O5  . NAG CA 3 .   ? -20.718 -17.359 6.062  1.00 127.78 ? 251 NAG D O5  1 
HETATM 17706 O  O6  . NAG CA 3 .   ? -21.641 -18.390 2.829  1.00 136.57 ? 251 NAG D O6  1 
HETATM 17707 O  O7  . NAG CA 3 .   ? -23.147 -20.643 8.198  1.00 120.23 ? 251 NAG D O7  1 
HETATM 17708 O  O8  . MLK DA 4 .   ? -24.350 -38.037 34.008 1.00 104.60 ? 301 MLK D O8  1 
HETATM 17709 C  C8  . MLK DA 4 .   ? -23.669 -38.544 33.137 1.00 99.67  ? 301 MLK D C8  1 
HETATM 17710 C  C9  . MLK DA 4 .   ? -22.864 -39.822 33.273 1.00 92.97  ? 301 MLK D C9  1 
HETATM 17711 C  C10 . MLK DA 4 .   ? -21.752 -39.571 32.243 1.00 89.31  ? 301 MLK D C10 1 
HETATM 17712 C  C12 . MLK DA 4 .   ? -20.596 -38.810 32.898 1.00 81.45  ? 301 MLK D C12 1 
HETATM 17713 C  C11 . MLK DA 4 .   ? -22.476 -38.681 31.253 1.00 100.46 ? 301 MLK D C11 1 
HETATM 17714 O  O11 . MLK DA 4 .   ? -22.204 -38.559 30.072 1.00 97.70  ? 301 MLK D O11 1 
HETATM 17715 N  N7  . MLK DA 4 .   ? -23.491 -38.074 31.892 1.00 98.66  ? 301 MLK D N7  1 
HETATM 17716 C  C6  . MLK DA 4 .   ? -24.312 -37.104 31.286 1.00 96.35  ? 301 MLK D C6  1 
HETATM 17717 C  C5  . MLK DA 4 .   ? -25.328 -37.585 30.465 1.00 98.00  ? 301 MLK D C5  1 
HETATM 17718 C  C4  . MLK DA 4 .   ? -26.188 -36.714 29.824 1.00 102.45 ? 301 MLK D C4  1 
HETATM 17719 C  C3  . MLK DA 4 .   ? -26.052 -35.340 29.993 1.00 99.89  ? 301 MLK D C3  1 
HETATM 17720 C  C2  . MLK DA 4 .   ? -25.055 -34.835 30.801 1.00 92.32  ? 301 MLK D C2  1 
HETATM 17721 C  C1  . MLK DA 4 .   ? -24.172 -35.699 31.462 1.00 91.80  ? 301 MLK D C1  1 
HETATM 17722 C  C13 . MLK DA 4 .   ? -23.130 -35.081 32.308 1.00 90.66  ? 301 MLK D C13 1 
HETATM 17723 O  O13 . MLK DA 4 .   ? -22.163 -35.736 32.654 1.00 87.92  ? 301 MLK D O13 1 
HETATM 17724 O  O14 . MLK DA 4 .   ? -23.268 -33.784 32.687 1.00 84.47  ? 301 MLK D O14 1 
HETATM 17725 C  C15 . MLK DA 4 .   ? -22.429 -33.217 33.732 1.00 86.17  ? 301 MLK D C15 1 
HETATM 17726 C  C16 . MLK DA 4 .   ? -22.860 -31.783 34.067 1.00 90.93  ? 301 MLK D C16 1 
HETATM 17727 C  C21 . MLK DA 4 .   ? -22.966 -31.053 32.730 1.00 84.05  ? 301 MLK D C21 1 
HETATM 17728 C  C20 . MLK DA 4 .   ? -24.193 -30.137 32.677 1.00 88.74  ? 301 MLK D C20 1 
HETATM 17729 C  C19 . MLK DA 4 .   ? -24.464 -29.397 33.984 1.00 93.43  ? 301 MLK D C19 1 
HETATM 17730 O  O19 . MLK DA 4 .   ? -23.532 -28.310 34.160 1.00 91.93  ? 301 MLK D O19 1 
HETATM 17731 C  C22 . MLK DA 4 .   ? -24.011 -27.174 33.430 1.00 76.78  ? 301 MLK D C22 1 
HETATM 17732 C  C18 . MLK DA 4 .   ? -24.528 -30.305 35.194 1.00 92.06  ? 301 MLK D C18 1 
HETATM 17733 C  C17 . MLK DA 4 .   ? -24.211 -31.775 34.839 1.00 93.21  ? 301 MLK D C17 1 
HETATM 17734 C  C26 . MLK DA 4 .   ? -23.456 -30.041 36.294 1.00 95.10  ? 301 MLK D C26 1 
HETATM 17735 N  N23 . MLK DA 4 .   ? -22.171 -29.940 35.641 1.00 86.97  ? 301 MLK D N23 1 
HETATM 17736 C  C24 . MLK DA 4 .   ? -21.175 -29.426 36.584 1.00 82.22  ? 301 MLK D C24 1 
HETATM 17737 C  C25 . MLK DA 4 .   ? -21.694 -28.155 37.271 1.00 75.89  ? 301 MLK D C25 1 
HETATM 17738 C  C23 . MLK DA 4 .   ? -21.756 -31.137 34.933 1.00 85.16  ? 301 MLK D C23 1 
HETATM 17739 C  C30 . MLK DA 4 .   ? -25.885 -30.101 35.849 1.00 94.46  ? 301 MLK D C30 1 
HETATM 17740 C  C33 . MLK DA 4 .   ? -26.071 -28.660 36.341 1.00 93.07  ? 301 MLK D C33 1 
HETATM 17741 C  C34 . MLK DA 4 .   ? -26.742 -28.756 37.740 1.00 99.31  ? 301 MLK D C34 1 
HETATM 17742 C  C35 . MLK DA 4 .   ? -25.592 -28.585 38.763 1.00 99.95  ? 301 MLK D C35 1 
HETATM 17743 O  O35 . MLK DA 4 .   ? -26.070 -28.102 40.021 1.00 92.42  ? 301 MLK D O35 1 
HETATM 17744 C  C37 . MLK DA 4 .   ? -25.866 -26.688 39.989 1.00 83.80  ? 301 MLK D C37 1 
HETATM 17745 C  C36 . MLK DA 4 .   ? -24.682 -29.804 38.894 1.00 98.83  ? 301 MLK D C36 1 
HETATM 17746 C  C31 . MLK DA 4 .   ? -26.139 -30.982 37.097 1.00 102.07 ? 301 MLK D C31 1 
HETATM 17747 C  C38 . MLK DA 4 .   ? -27.275 -30.209 37.832 1.00 105.38 ? 301 MLK D C38 1 
HETATM 17748 O  O38 . MLK DA 4 .   ? -27.451 -30.675 39.168 1.00 110.04 ? 301 MLK D O38 1 
HETATM 17749 C  C39 . MLK DA 4 .   ? -28.777 -31.200 39.266 1.00 108.73 ? 301 MLK D C39 1 
HETATM 17750 C  C32 . MLK DA 4 .   ? -24.939 -31.055 38.040 1.00 106.94 ? 301 MLK D C32 1 
HETATM 17751 O  O32 . MLK DA 4 .   ? -25.116 -32.191 38.933 1.00 104.10 ? 301 MLK D O32 1 
HETATM 17752 C  C27 . MLK DA 4 .   ? -23.643 -31.297 37.200 1.00 104.28 ? 301 MLK D C27 1 
HETATM 17753 O  O27 . MLK DA 4 .   ? -22.534 -31.618 38.057 1.00 103.59 ? 301 MLK D O27 1 
HETATM 17754 C  C28 . MLK DA 4 .   ? -23.832 -32.460 36.185 1.00 94.06  ? 301 MLK D C28 1 
HETATM 17755 O  O28 . MLK DA 4 .   ? -24.738 -33.489 36.610 1.00 98.40  ? 301 MLK D O28 1 
HETATM 17756 C  C29 . MLK DA 4 .   ? -24.953 -34.400 35.523 1.00 89.93  ? 301 MLK D C29 1 
HETATM 17757 MG MG  . MG  EA 2 .   ? 35.218  2.263   24.734 1.00 57.70  ? 222 MG  E MG  1 
HETATM 17758 C  C1  . NAG FA 3 .   ? 21.539  -14.494 7.028  1.00 100.07 ? 250 NAG E C1  1 
HETATM 17759 C  C2  . NAG FA 3 .   ? 22.809  -14.726 6.193  1.00 115.14 ? 250 NAG E C2  1 
HETATM 17760 C  C3  . NAG FA 3 .   ? 22.459  -14.926 4.722  1.00 115.65 ? 250 NAG E C3  1 
HETATM 17761 C  C4  . NAG FA 3 .   ? 21.365  -15.979 4.591  1.00 113.49 ? 250 NAG E C4  1 
HETATM 17762 C  C5  . NAG FA 3 .   ? 20.144  -15.702 5.458  1.00 104.84 ? 250 NAG E C5  1 
HETATM 17763 C  C6  . NAG FA 3 .   ? 19.222  -16.921 5.436  1.00 105.65 ? 250 NAG E C6  1 
HETATM 17764 C  C7  . NAG FA 3 .   ? 25.081  -13.856 6.677  1.00 120.10 ? 250 NAG E C7  1 
HETATM 17765 C  C8  . NAG FA 3 .   ? 25.461  -13.625 8.115  1.00 101.44 ? 250 NAG E C8  1 
HETATM 17766 N  N2  . NAG FA 3 .   ? 23.793  -13.647 6.347  1.00 111.94 ? 250 NAG E N2  1 
HETATM 17767 O  O3  . NAG FA 3 .   ? 23.613  -15.331 4.013  1.00 121.65 ? 250 NAG E O3  1 
HETATM 17768 O  O4  . NAG FA 3 .   ? 20.955  -16.097 3.247  1.00 123.88 ? 250 NAG E O4  1 
HETATM 17769 O  O5  . NAG FA 3 .   ? 20.478  -15.406 6.794  1.00 95.32  ? 250 NAG E O5  1 
HETATM 17770 O  O6  . NAG FA 3 .   ? 19.967  -18.117 5.366  1.00 105.01 ? 250 NAG E O6  1 
HETATM 17771 O  O7  . NAG FA 3 .   ? 25.945  -14.213 5.866  1.00 124.55 ? 250 NAG E O7  1 
HETATM 17772 C  C1  . NAG GA 3 .   ? 21.452  -17.370 2.784  1.00 134.23 ? 251 NAG E C1  1 
HETATM 17773 C  C2  . NAG GA 3 .   ? 20.644  -17.892 1.583  1.00 134.31 ? 251 NAG E C2  1 
HETATM 17774 C  C3  . NAG GA 3 .   ? 21.298  -19.116 0.931  1.00 139.13 ? 251 NAG E C3  1 
HETATM 17775 C  C4  . NAG GA 3 .   ? 22.825  -19.078 0.934  1.00 142.14 ? 251 NAG E C4  1 
HETATM 17776 C  C5  . NAG GA 3 .   ? 23.376  -18.597 2.270  1.00 135.60 ? 251 NAG E C5  1 
HETATM 17777 C  C6  . NAG GA 3 .   ? 24.900  -18.540 2.261  1.00 126.42 ? 251 NAG E C6  1 
HETATM 17778 C  C7  . NAG GA 3 .   ? 18.622  -19.348 1.988  1.00 137.30 ? 251 NAG E C7  1 
HETATM 17779 C  C8  . NAG GA 3 .   ? 17.120  -19.295 1.928  1.00 123.20 ? 251 NAG E C8  1 
HETATM 17780 N  N2  . NAG GA 3 .   ? 19.249  -18.154 1.956  1.00 133.29 ? 251 NAG E N2  1 
HETATM 17781 O  O3  . NAG GA 3 .   ? 20.859  -19.215 -0.404 1.00 130.71 ? 251 NAG E O3  1 
HETATM 17782 O  O4  . NAG GA 3 .   ? 23.322  -20.370 0.656  1.00 144.05 ? 251 NAG E O4  1 
HETATM 17783 O  O5  . NAG GA 3 .   ? 22.841  -17.317 2.516  1.00 139.14 ? 251 NAG E O5  1 
HETATM 17784 O  O6  . NAG GA 3 .   ? 25.337  -17.893 1.084  1.00 127.99 ? 251 NAG E O6  1 
HETATM 17785 O  O7  . NAG GA 3 .   ? 19.175  -20.453 2.077  1.00 129.00 ? 251 NAG E O7  1 
HETATM 17786 C  C1  . MRD HA 5 .   ? 0.180   -17.034 17.316 1.00 75.39  ? 305 MRD E C1  1 
HETATM 17787 C  C2  . MRD HA 5 .   ? -0.152  -16.445 15.945 1.00 85.90  ? 305 MRD E C2  1 
HETATM 17788 O  O2  . MRD HA 5 .   ? 0.619   -17.126 14.920 1.00 79.34  ? 305 MRD E O2  1 
HETATM 17789 C  CM  . MRD HA 5 .   ? -1.632  -16.640 15.642 1.00 69.20  ? 305 MRD E CM  1 
HETATM 17790 C  C3  . MRD HA 5 .   ? 0.163   -14.953 15.941 1.00 85.24  ? 305 MRD E C3  1 
HETATM 17791 C  C4  . MRD HA 5 .   ? 0.370   -14.448 17.378 1.00 99.82  ? 305 MRD E C4  1 
HETATM 17792 O  O4  . MRD HA 5 .   ? -0.890  -14.075 17.939 1.00 104.25 ? 305 MRD E O4  1 
HETATM 17793 C  C5  . MRD HA 5 .   ? 1.345   -13.257 17.453 1.00 90.98  ? 305 MRD E C5  1 
HETATM 17794 C  C1  A NAG IA 3 .   ? 32.364  -2.313  12.091 0.50 106.06 ? 275 NAG E C1  1 
HETATM 17795 C  C1  B NAG IA 3 .   ? 32.186  -8.245  9.759  0.50 108.23 ? 275 NAG E C1  1 
HETATM 17796 C  C2  A NAG IA 3 .   ? 32.804  -1.375  13.213 0.50 106.05 ? 275 NAG E C2  1 
HETATM 17797 C  C2  B NAG IA 3 .   ? 33.480  -8.818  9.168  0.50 114.03 ? 275 NAG E C2  1 
HETATM 17798 C  C3  A NAG IA 3 .   ? 33.961  -0.492  12.775 0.50 111.20 ? 275 NAG E C3  1 
HETATM 17799 C  C3  B NAG IA 3 .   ? 33.247  -10.015 8.253  0.50 112.21 ? 275 NAG E C3  1 
HETATM 17800 C  C4  A NAG IA 3 .   ? 35.067  -1.395  12.267 0.50 115.82 ? 275 NAG E C4  1 
HETATM 17801 C  C4  B NAG IA 3 .   ? 32.372  -11.060 8.909  0.50 114.04 ? 275 NAG E C4  1 
HETATM 17802 C  C5  A NAG IA 3 .   ? 34.537  -2.194  11.084 0.50 115.58 ? 275 NAG E C5  1 
HETATM 17803 C  C5  B NAG IA 3 .   ? 31.126  -10.420 9.500  0.50 107.76 ? 275 NAG E C5  1 
HETATM 17804 C  C6  A NAG IA 3 .   ? 35.632  -3.065  10.482 0.50 112.29 ? 275 NAG E C6  1 
HETATM 17805 C  C6  B NAG IA 3 .   ? 30.343  -11.478 10.286 0.50 100.00 ? 275 NAG E C6  1 
HETATM 17806 C  C7  A NAG IA 3 .   ? 31.533  -0.214  14.983 0.50 111.26 ? 275 NAG E C7  1 
HETATM 17807 C  C7  B NAG IA 3 .   ? 35.048  -8.193  7.408  0.50 121.58 ? 275 NAG E C7  1 
HETATM 17808 C  C8  A NAG IA 3 .   ? 30.421  0.741   15.357 0.50 105.93 ? 275 NAG E C8  1 
HETATM 17809 C  C8  B NAG IA 3 .   ? 36.523  -7.918  7.515  0.50 119.84 ? 275 NAG E C8  1 
HETATM 17810 N  N2  A NAG IA 3 .   ? 31.688  -0.556  13.644 0.50 105.63 ? 275 NAG E N2  1 
HETATM 17811 N  N2  B NAG IA 3 .   ? 34.295  -7.839  8.462  0.50 116.49 ? 275 NAG E N2  1 
HETATM 17812 O  O3  A NAG IA 3 .   ? 34.430  0.270   13.878 0.50 112.58 ? 275 NAG E O3  1 
HETATM 17813 O  O3  B NAG IA 3 .   ? 34.495  -10.626 7.993  0.50 112.08 ? 275 NAG E O3  1 
HETATM 17814 O  O4  A NAG IA 3 .   ? 36.191  -0.624  11.866 0.50 113.14 ? 275 NAG E O4  1 
HETATM 17815 O  O4  B NAG IA 3 .   ? 32.009  -12.037 7.958  0.50 109.47 ? 275 NAG E O4  1 
HETATM 17816 O  O5  A NAG IA 3 .   ? 33.454  -3.016  11.499 0.50 114.10 ? 275 NAG E O5  1 
HETATM 17817 O  O5  B NAG IA 3 .   ? 31.457  -9.319  10.332 0.50 106.07 ? 275 NAG E O5  1 
HETATM 17818 O  O6  A NAG IA 3 .   ? 35.088  -3.849  9.428  0.50 110.01 ? 275 NAG E O6  1 
HETATM 17819 O  O6  B NAG IA 3 .   ? 30.597  -11.419 11.675 0.50 91.08  ? 275 NAG E O6  1 
HETATM 17820 O  O7  A NAG IA 3 .   ? 32.336  -0.707  15.922 0.50 117.57 ? 275 NAG E O7  1 
HETATM 17821 O  O7  B NAG IA 3 .   ? 34.581  -8.737  6.398  0.50 123.52 ? 275 NAG E O7  1 
HETATM 17822 O  O8  . MLK JA 4 .   ? -6.752  -34.536 6.149  1.00 108.35 ? 301 MLK E O8  1 
HETATM 17823 C  C8  . MLK JA 4 .   ? -5.869  -35.271 6.548  1.00 104.15 ? 301 MLK E C8  1 
HETATM 17824 C  C9  . MLK JA 4 .   ? -6.082  -36.622 7.209  1.00 97.38  ? 301 MLK E C9  1 
HETATM 17825 C  C10 . MLK JA 4 .   ? -4.735  -37.301 6.897  1.00 105.16 ? 301 MLK E C10 1 
HETATM 17826 C  C12 . MLK JA 4 .   ? -4.370  -38.394 7.910  1.00 95.79  ? 301 MLK E C12 1 
HETATM 17827 C  C11 . MLK JA 4 .   ? -3.834  -36.081 6.970  1.00 102.38 ? 301 MLK E C11 1 
HETATM 17828 O  O11 . MLK JA 4 .   ? -2.710  -36.083 7.447  1.00 94.96  ? 301 MLK E O11 1 
HETATM 17829 N  N7  . MLK JA 4 .   ? -4.542  -35.044 6.437  1.00 101.92 ? 301 MLK E N7  1 
HETATM 17830 C  C6  . MLK JA 4 .   ? -4.018  -33.896 5.766  1.00 95.35  ? 301 MLK E C6  1 
HETATM 17831 C  C5  . MLK JA 4 .   ? -3.379  -34.156 4.552  1.00 91.01  ? 301 MLK E C5  1 
HETATM 17832 C  C4  . MLK JA 4 .   ? -2.834  -33.142 3.779  1.00 88.66  ? 301 MLK E C4  1 
HETATM 17833 C  C3  . MLK JA 4 .   ? -2.920  -31.818 4.182  1.00 80.57  ? 301 MLK E C3  1 
HETATM 17834 C  C2  . MLK JA 4 .   ? -3.556  -31.520 5.368  1.00 87.58  ? 301 MLK E C2  1 
HETATM 17835 C  C1  . MLK JA 4 .   ? -4.118  -32.517 6.186  1.00 88.67  ? 301 MLK E C1  1 
HETATM 17836 C  C13 . MLK JA 4 .   ? -4.760  -32.004 7.431  1.00 82.13  ? 301 MLK E C13 1 
HETATM 17837 O  O13 . MLK JA 4 .   ? -5.317  -32.762 8.204  1.00 84.01  ? 301 MLK E O13 1 
HETATM 17838 O  O14 . MLK JA 4 .   ? -4.759  -30.671 7.714  1.00 71.62  ? 301 MLK E O14 1 
HETATM 17839 C  C15 . MLK JA 4 .   ? -5.840  -30.137 8.529  1.00 71.07  ? 301 MLK E C15 1 
HETATM 17840 C  C16 . MLK JA 4 .   ? -6.026  -28.637 8.317  1.00 77.61  ? 301 MLK E C16 1 
HETATM 17841 C  C21 . MLK JA 4 .   ? -4.740  -28.139 7.667  1.00 75.47  ? 301 MLK E C21 1 
HETATM 17842 C  C20 . MLK JA 4 .   ? -4.757  -26.618 7.466  1.00 69.57  ? 301 MLK E C20 1 
HETATM 17843 C  C19 . MLK JA 4 .   ? -6.094  -26.039 7.006  1.00 76.02  ? 301 MLK E C19 1 
HETATM 17844 O  O19 . MLK JA 4 .   ? -6.272  -24.791 7.697  1.00 76.88  ? 301 MLK E O19 1 
HETATM 17845 C  C22 . MLK JA 4 .   ? -5.101  -24.004 7.471  1.00 72.22  ? 301 MLK E C22 1 
HETATM 17846 C  C18 . MLK JA 4 .   ? -7.370  -26.829 7.219  1.00 83.26  ? 301 MLK E C18 1 
HETATM 17847 C  C17 . MLK JA 4 .   ? -7.196  -28.362 7.344  1.00 83.99  ? 301 MLK E C17 1 
HETATM 17848 C  C26 . MLK JA 4 .   ? -8.040  -26.508 8.590  1.00 87.47  ? 301 MLK E C26 1 
HETATM 17849 N  N23 . MLK JA 4 .   ? -7.023  -26.672 9.617  1.00 87.09  ? 301 MLK E N23 1 
HETATM 17850 C  C24 . MLK JA 4 .   ? -7.565  -26.226 10.907 1.00 81.28  ? 301 MLK E C24 1 
HETATM 17851 C  C25 . MLK JA 4 .   ? -7.856  -24.715 10.902 1.00 71.36  ? 301 MLK E C25 1 
HETATM 17852 C  C23 . MLK JA 4 .   ? -6.340  -27.970 9.680  1.00 76.30  ? 301 MLK E C23 1 
HETATM 17853 C  C30 . MLK JA 4 .   ? -8.370  -26.460 6.130  1.00 86.77  ? 301 MLK E C30 1 
HETATM 17854 C  C33 . MLK JA 4 .   ? -8.786  -24.981 6.139  1.00 89.45  ? 301 MLK E C33 1 
HETATM 17855 C  C34 . MLK JA 4 .   ? -10.281 -24.953 5.698  1.00 94.87  ? 301 MLK E C34 1 
HETATM 17856 C  C35 . MLK JA 4 .   ? -11.105 -24.731 6.987  1.00 100.86 ? 301 MLK E C35 1 
HETATM 17857 O  O35 . MLK JA 4 .   ? -12.505 -24.649 6.683  1.00 102.37 ? 301 MLK E O35 1 
HETATM 17858 C  C37 . MLK JA 4 .   ? -12.780 -23.289 6.338  1.00 97.08  ? 301 MLK E C37 1 
HETATM 17859 C  C36 . MLK JA 4 .   ? -10.784 -25.752 8.080  1.00 95.56  ? 301 MLK E C36 1 
HETATM 17860 C  C31 . MLK JA 4 .   ? -9.722  -27.209 6.232  1.00 93.33  ? 301 MLK E C31 1 
HETATM 17861 C  C38 . MLK JA 4 .   ? -10.583 -26.395 5.212  1.00 90.59  ? 301 MLK E C38 1 
HETATM 17862 O  O38 . MLK JA 4 .   ? -11.959 -26.753 5.254  1.00 86.82  ? 301 MLK E O38 1 
HETATM 17863 C  C39 . MLK JA 4 .   ? -12.091 -27.945 4.478  1.00 91.80  ? 301 MLK E C39 1 
HETATM 17864 C  C32 . MLK JA 4 .   ? -10.296 -27.140 7.653  1.00 93.06  ? 301 MLK E C32 1 
HETATM 17865 O  O32 . MLK JA 4 .   ? -11.393 -28.084 7.818  1.00 83.49  ? 301 MLK E O32 1 
HETATM 17866 C  C27 . MLK JA 4 .   ? -9.172  -27.570 8.644  1.00 92.16  ? 301 MLK E C27 1 
HETATM 17867 O  O27 . MLK JA 4 .   ? -9.714  -27.785 9.959  1.00 91.21  ? 301 MLK E O27 1 
HETATM 17868 C  C28 . MLK JA 4 .   ? -8.447  -28.854 8.132  1.00 87.32  ? 301 MLK E C28 1 
HETATM 17869 O  O28 . MLK JA 4 .   ? -9.252  -29.737 7.350  1.00 93.12  ? 301 MLK E O28 1 
HETATM 17870 C  C29 . MLK JA 4 .   ? -8.509  -30.936 7.103  1.00 84.84  ? 301 MLK E C29 1 
HETATM 17871 C  C1  . MRD KA 5 .   ? -13.903 22.093  31.856 1.00 77.07  ? 305 MRD F C1  1 
HETATM 17872 C  C2  . MRD KA 5 .   ? -14.405 21.288  30.654 1.00 81.26  ? 305 MRD F C2  1 
HETATM 17873 O  O2  . MRD KA 5 .   ? -15.422 20.360  31.119 1.00 75.97  ? 305 MRD F O2  1 
HETATM 17874 C  CM  . MRD KA 5 .   ? -14.996 22.197  29.582 1.00 75.54  ? 305 MRD F CM  1 
HETATM 17875 C  C3  . MRD KA 5 .   ? -13.283 20.519  29.978 1.00 79.00  ? 305 MRD F C3  1 
HETATM 17876 C  C4  . MRD KA 5 .   ? -12.591 19.567  30.943 1.00 85.60  ? 305 MRD F C4  1 
HETATM 17877 O  O4  . MRD KA 5 .   ? -11.419 19.092  30.307 1.00 90.52  ? 305 MRD F O4  1 
HETATM 17878 C  C5  . MRD KA 5 .   ? -13.505 18.406  31.322 1.00 77.94  ? 305 MRD F C5  1 
HETATM 17879 C  C1  . NAG LA 3 .   ? -27.396 18.141  49.515 1.00 91.89  ? 250 NAG F C1  1 
HETATM 17880 C  C2  . NAG LA 3 .   ? -28.112 17.670  50.791 1.00 100.12 ? 250 NAG F C2  1 
HETATM 17881 C  C3  . NAG LA 3 .   ? -29.626 17.818  50.694 1.00 103.23 ? 250 NAG F C3  1 
HETATM 17882 C  C4  . NAG LA 3 .   ? -29.965 19.237  50.248 1.00 108.13 ? 250 NAG F C4  1 
HETATM 17883 C  C5  . NAG LA 3 .   ? -29.252 19.550  48.931 1.00 99.43  ? 250 NAG F C5  1 
HETATM 17884 C  C6  . NAG LA 3 .   ? -29.541 20.965  48.447 1.00 96.87  ? 250 NAG F C6  1 
HETATM 17885 C  C7  . NAG LA 3 .   ? -27.695 15.822  52.370 1.00 108.60 ? 250 NAG F C7  1 
HETATM 17886 C  C8  . NAG LA 3 .   ? -27.134 16.730  53.441 1.00 92.92  ? 250 NAG F C8  1 
HETATM 17887 N  N2  . NAG LA 3 .   ? -27.790 16.289  51.115 1.00 103.67 ? 250 NAG F N2  1 
HETATM 17888 O  O3  . NAG LA 3 .   ? -30.191 17.549  51.961 1.00 108.57 ? 250 NAG F O3  1 
HETATM 17889 O  O4  . NAG LA 3 .   ? -31.367 19.422  50.150 1.00 97.77  ? 250 NAG F O4  1 
HETATM 17890 O  O5  . NAG LA 3 .   ? -27.853 19.420  49.097 1.00 92.43  ? 250 NAG F O5  1 
HETATM 17891 O  O6  . NAG LA 3 .   ? -28.565 21.841  48.967 1.00 98.28  ? 250 NAG F O6  1 
HETATM 17892 O  O7  . NAG LA 3 .   ? -28.051 14.673  52.658 1.00 104.36 ? 250 NAG F O7  1 
HETATM 17893 O  O8  . MLK MA 4 .   ? -18.852 39.983  24.979 1.00 102.90 ? 301 MLK F O8  1 
HETATM 17894 C  C8  . MLK MA 4 .   ? -19.041 40.822  25.840 1.00 96.70  ? 301 MLK F C8  1 
HETATM 17895 C  C9  . MLK MA 4 .   ? -18.423 42.205  25.854 1.00 89.24  ? 301 MLK F C9  1 
HETATM 17896 C  C10 . MLK MA 4 .   ? -18.607 42.658  27.312 1.00 93.48  ? 301 MLK F C10 1 
HETATM 17897 C  C12 . MLK MA 4 .   ? -17.233 42.740  27.991 1.00 72.87  ? 301 MLK F C12 1 
HETATM 17898 C  C11 . MLK MA 4 .   ? -19.520 41.581  27.884 1.00 97.35  ? 301 MLK F C11 1 
HETATM 17899 O  O11 . MLK MA 4 .   ? -19.927 41.532  29.025 1.00 102.32 ? 301 MLK F O11 1 
HETATM 17900 N  N7  . MLK MA 4 .   ? -19.826 40.692  26.923 1.00 91.49  ? 301 MLK F N7  1 
HETATM 17901 C  C6  . MLK MA 4 .   ? -20.886 39.761  27.028 1.00 96.09  ? 301 MLK F C6  1 
HETATM 17902 C  C5  . MLK MA 4 .   ? -22.156 40.285  27.249 1.00 97.04  ? 301 MLK F C5  1 
HETATM 17903 C  C4  . MLK MA 4 .   ? -23.264 39.461  27.355 1.00 99.19  ? 301 MLK F C4  1 
HETATM 17904 C  C3  . MLK MA 4 .   ? -23.136 38.086  27.235 1.00 93.20  ? 301 MLK F C3  1 
HETATM 17905 C  C2  . MLK MA 4 .   ? -21.896 37.535  27.007 1.00 88.90  ? 301 MLK F C2  1 
HETATM 17906 C  C1  . MLK MA 4 .   ? -20.755 38.344  26.895 1.00 92.65  ? 301 MLK F C1  1 
HETATM 17907 C  C13 . MLK MA 4 .   ? -19.475 37.635  26.660 1.00 86.51  ? 301 MLK F C13 1 
HETATM 17908 O  O13 . MLK MA 4 .   ? -18.404 38.139  26.935 1.00 81.74  ? 301 MLK F O13 1 
HETATM 17909 O  O14 . MLK MA 4 .   ? -19.502 36.391  26.132 1.00 91.74  ? 301 MLK F O14 1 
HETATM 17910 C  C15 . MLK MA 4 .   ? -18.270 35.703  25.772 1.00 86.86  ? 301 MLK F C15 1 
HETATM 17911 C  C16 . MLK MA 4 .   ? -18.611 34.312  25.230 1.00 89.13  ? 301 MLK F C16 1 
HETATM 17912 C  C21 . MLK MA 4 .   ? -19.441 33.588  26.293 1.00 85.06  ? 301 MLK F C21 1 
HETATM 17913 C  C20 . MLK MA 4 .   ? -20.667 32.912  25.673 1.00 91.81  ? 301 MLK F C20 1 
HETATM 17914 C  C19 . MLK MA 4 .   ? -20.278 32.160  24.413 1.00 91.00  ? 301 MLK F C19 1 
HETATM 17915 O  O19 . MLK MA 4 .   ? -19.372 31.102  24.754 1.00 87.93  ? 301 MLK F O19 1 
HETATM 17916 C  C22 . MLK MA 4 .   ? -20.130 29.964  25.175 1.00 81.97  ? 301 MLK F C22 1 
HETATM 17917 C  C18 . MLK MA 4 .   ? -19.656 33.045  23.368 1.00 92.19  ? 301 MLK F C18 1 
HETATM 17918 C  C17 . MLK MA 4 .   ? -19.388 34.467  23.898 1.00 92.61  ? 301 MLK F C17 1 
HETATM 17919 C  C26 . MLK MA 4 .   ? -18.215 32.625  22.939 1.00 92.82  ? 301 MLK F C26 1 
HETATM 17920 N  N23 . MLK MA 4 .   ? -17.387 32.413  24.107 1.00 91.70  ? 301 MLK F N23 1 
HETATM 17921 C  C24 . MLK MA 4 .   ? -16.073 31.935  23.668 1.00 86.85  ? 301 MLK F C24 1 
HETATM 17922 C  C25 . MLK MA 4 .   ? -15.690 30.570  24.252 1.00 80.05  ? 301 MLK F C25 1 
HETATM 17923 C  C23 . MLK MA 4 .   ? -17.287 33.561  24.993 1.00 87.25  ? 301 MLK F C23 1 
HETATM 17924 C  C30 . MLK MA 4 .   ? -20.560 33.036  22.137 1.00 101.37 ? 301 MLK F C30 1 
HETATM 17925 C  C33 . MLK MA 4 .   ? -20.796 31.632  21.549 1.00 101.17 ? 301 MLK F C33 1 
HETATM 17926 C  C34 . MLK MA 4 .   ? -20.466 31.730  20.037 1.00 99.38  ? 301 MLK F C34 1 
HETATM 17927 C  C35 . MLK MA 4 .   ? -18.946 31.417  20.007 1.00 99.73  ? 301 MLK F C35 1 
HETATM 17928 O  O35 . MLK MA 4 .   ? -18.519 30.528  18.976 1.00 105.11 ? 301 MLK F O35 1 
HETATM 17929 C  C37 . MLK MA 4 .   ? -17.288 30.016  19.484 1.00 87.52  ? 301 MLK F C37 1 
HETATM 17930 C  C36 . MLK MA 4 .   ? -18.035 32.624  20.041 1.00 95.66  ? 301 MLK F C36 1 
HETATM 17931 C  C31 . MLK MA 4 .   ? -20.059 33.908  20.955 1.00 101.56 ? 301 MLK F C31 1 
HETATM 17932 C  C38 . MLK MA 4 .   ? -20.745 33.225  19.731 1.00 102.68 ? 301 MLK F C38 1 
HETATM 17933 O  O38 . MLK MA 4 .   ? -20.222 33.662  18.482 1.00 115.05 ? 301 MLK F O38 1 
HETATM 17934 C  C39 . MLK MA 4 .   ? -21.164 34.559  17.886 1.00 109.15 ? 301 MLK F C39 1 
HETATM 17935 C  C32 . MLK MA 4 .   ? -18.544 33.853  20.761 1.00 104.22 ? 301 MLK F C32 1 
HETATM 17936 O  O32 . MLK MA 4 .   ? -18.099 35.010  20.002 1.00 108.61 ? 301 MLK F O32 1 
HETATM 17937 C  C27 . MLK MA 4 .   ? -17.791 33.876  22.121 1.00 101.21 ? 301 MLK F C27 1 
HETATM 17938 O  O27 . MLK MA 4 .   ? -16.380 33.997  21.894 1.00 95.66  ? 301 MLK F O27 1 
HETATM 17939 C  C28 . MLK MA 4 .   ? -18.300 35.072  22.963 1.00 96.28  ? 301 MLK F C28 1 
HETATM 17940 O  O28 . MLK MA 4 .   ? -18.745 36.169  22.161 1.00 93.71  ? 301 MLK F O28 1 
HETATM 17941 C  C29 . MLK MA 4 .   ? -19.500 37.066  22.975 1.00 90.12  ? 301 MLK F C29 1 
HETATM 17942 C  C   . ACT NA 7 .   ? 21.109  -1.306  57.325 1.00 90.57  ? 308 ACT G C   1 
HETATM 17943 O  O   . ACT NA 7 .   ? 21.548  -1.904  56.208 1.00 89.88  ? 308 ACT G O   1 
HETATM 17944 O  OXT . ACT NA 7 .   ? 21.802  -0.256  57.840 1.00 85.23  ? 308 ACT G OXT 1 
HETATM 17945 C  CH3 . ACT NA 7 .   ? 19.817  -1.796  57.993 1.00 74.19  ? 308 ACT G CH3 1 
HETATM 17946 C  C1  . NAG OA 3 .   ? 4.828   15.697  70.743 1.00 93.28  ? 250 NAG G C1  1 
HETATM 17947 C  C2  . NAG OA 3 .   ? 5.545   15.477  72.092 1.00 109.56 ? 250 NAG G C2  1 
HETATM 17948 C  C3  . NAG OA 3 .   ? 4.531   15.385  73.227 1.00 107.43 ? 250 NAG G C3  1 
HETATM 17949 C  C4  . NAG OA 3 .   ? 3.558   16.558  73.157 1.00 106.21 ? 250 NAG G C4  1 
HETATM 17950 C  C5  . NAG OA 3 .   ? 2.929   16.701  71.778 1.00 97.13  ? 250 NAG G C5  1 
HETATM 17951 C  C6  . NAG OA 3 .   ? 2.109   17.979  71.671 1.00 99.95  ? 250 NAG G C6  1 
HETATM 17952 C  C7  . NAG OA 3 .   ? 7.744   14.361  72.002 1.00 105.54 ? 250 NAG G C7  1 
HETATM 17953 C  C8  . NAG OA 3 .   ? 8.501   13.053  71.930 1.00 81.18  ? 250 NAG G C8  1 
HETATM 17954 N  N2  . NAG OA 3 .   ? 6.406   14.295  72.113 1.00 110.16 ? 250 NAG G N2  1 
HETATM 17955 O  O3  . NAG OA 3 .   ? 5.200   15.384  74.467 1.00 105.03 ? 250 NAG G O3  1 
HETATM 17956 O  O4  . NAG OA 3 .   ? 2.549   16.388  74.121 1.00 112.84 ? 250 NAG G O4  1 
HETATM 17957 O  O5  . NAG OA 3 .   ? 3.944   16.797  70.811 1.00 93.28  ? 250 NAG G O5  1 
HETATM 17958 O  O6  . NAG OA 3 .   ? 2.983   19.086  71.607 1.00 95.77  ? 250 NAG G O6  1 
HETATM 17959 O  O7  . NAG OA 3 .   ? 8.352   15.442  71.969 1.00 97.20  ? 250 NAG G O7  1 
HETATM 17960 C  C1  . NAG PA 3 .   ? 2.497   17.585  74.918 1.00 122.32 ? 251 NAG G C1  1 
HETATM 17961 C  C2  . NAG PA 3 .   ? 1.147   17.657  75.633 1.00 127.30 ? 251 NAG G C2  1 
HETATM 17962 C  C3  . NAG PA 3 .   ? 1.045   18.867  76.559 1.00 130.27 ? 251 NAG G C3  1 
HETATM 17963 C  C4  . NAG PA 3 .   ? 2.342   19.133  77.323 1.00 135.88 ? 251 NAG G C4  1 
HETATM 17964 C  C5  . NAG PA 3 .   ? 3.572   18.968  76.438 1.00 130.46 ? 251 NAG G C5  1 
HETATM 17965 C  C6  . NAG PA 3 .   ? 4.864   19.170  77.225 1.00 120.61 ? 251 NAG G C6  1 
HETATM 17966 C  C7  . NAG PA 3 .   ? -0.646  18.650  74.211 1.00 125.09 ? 251 NAG G C7  1 
HETATM 17967 C  C8  . NAG PA 3 .   ? -1.972  18.330  73.577 1.00 103.91 ? 251 NAG G C8  1 
HETATM 17968 N  N2  . NAG PA 3 .   ? 0.051   17.599  74.668 1.00 123.82 ? 251 NAG G N2  1 
HETATM 17969 O  O3  . NAG PA 3 .   ? -0.001  18.623  77.474 1.00 128.48 ? 251 NAG G O3  1 
HETATM 17970 O  O4  . NAG PA 3 .   ? 2.322   20.451  77.825 1.00 140.72 ? 251 NAG G O4  1 
HETATM 17971 O  O5  . NAG PA 3 .   ? 3.555   17.687  75.848 1.00 128.73 ? 251 NAG G O5  1 
HETATM 17972 O  O6  . NAG PA 3 .   ? 5.455   20.390  76.836 1.00 106.93 ? 251 NAG G O6  1 
HETATM 17973 O  O7  . NAG PA 3 .   ? -0.261  19.824  74.269 1.00 126.61 ? 251 NAG G O7  1 
HETATM 17974 O  O8  . MLK QA 4 .   ? -19.167 36.523  58.101 1.00 103.72 ? 301 MLK G O8  1 
HETATM 17975 C  C8  . MLK QA 4 .   ? -18.092 37.091  58.055 1.00 99.47  ? 301 MLK G C8  1 
HETATM 17976 C  C9  . MLK QA 4 .   ? -17.773 38.230  57.110 1.00 93.65  ? 301 MLK G C9  1 
HETATM 17977 C  C10 . MLK QA 4 .   ? -16.461 38.793  57.676 1.00 96.26  ? 301 MLK G C10 1 
HETATM 17978 C  C12 . MLK QA 4 .   ? -15.399 38.884  56.577 1.00 83.79  ? 301 MLK G C12 1 
HETATM 17979 C  C11 . MLK QA 4 .   ? -16.086 37.804  58.766 1.00 95.52  ? 301 MLK G C11 1 
HETATM 17980 O  O11 . MLK QA 4 .   ? -15.099 37.932  59.464 1.00 96.71  ? 301 MLK G O11 1 
HETATM 17981 N  N7  . MLK QA 4 .   ? -17.026 36.826  58.839 1.00 97.54  ? 301 MLK G N7  1 
HETATM 17982 C  C6  . MLK QA 4 .   ? -16.990 35.671  59.674 1.00 89.95  ? 301 MLK G C6  1 
HETATM 17983 C  C5  . MLK QA 4 .   ? -17.168 35.839  61.048 1.00 90.71  ? 301 MLK G C5  1 
HETATM 17984 C  C4  . MLK QA 4 .   ? -17.169 34.773  61.938 1.00 86.93  ? 301 MLK G C4  1 
HETATM 17985 C  C3  . MLK QA 4 .   ? -17.009 33.474  61.490 1.00 82.45  ? 301 MLK G C3  1 
HETATM 17986 C  C2  . MLK QA 4 .   ? -16.848 33.269  60.139 1.00 94.24  ? 301 MLK G C2  1 
HETATM 17987 C  C1  . MLK QA 4 .   ? -16.841 34.335  59.212 1.00 90.57  ? 301 MLK G C1  1 
HETATM 17988 C  C13 . MLK QA 4 .   ? -16.650 33.950  57.794 1.00 86.88  ? 301 MLK G C13 1 
HETATM 17989 O  O13 . MLK QA 4 .   ? -16.213 34.726  56.965 1.00 86.98  ? 301 MLK G O13 1 
HETATM 17990 O  O14 . MLK QA 4 .   ? -16.961 32.683  57.451 1.00 77.59  ? 301 MLK G O14 1 
HETATM 17991 C  C15 . MLK QA 4 .   ? -16.752 32.171  56.119 1.00 79.26  ? 301 MLK G C15 1 
HETATM 17992 C  C16 . MLK QA 4 .   ? -17.194 30.707  56.137 1.00 82.48  ? 301 MLK G C16 1 
HETATM 17993 C  C21 . MLK QA 4 .   ? -16.288 29.986  57.138 1.00 78.13  ? 301 MLK G C21 1 
HETATM 17994 C  C20 . MLK QA 4 .   ? -17.048 28.986  58.019 1.00 83.25  ? 301 MLK G C20 1 
HETATM 17995 C  C19 . MLK QA 4 .   ? -18.158 28.238  57.294 1.00 83.53  ? 301 MLK G C19 1 
HETATM 17996 O  O19 . MLK QA 4 .   ? -17.570 27.216  56.476 1.00 78.86  ? 301 MLK G O19 1 
HETATM 17997 C  C22 . MLK QA 4 .   ? -17.931 25.954  57.037 1.00 72.17  ? 301 MLK G C22 1 
HETATM 17998 C  C18 . MLK QA 4 .   ? -19.087 29.119  56.490 1.00 88.92  ? 301 MLK G C18 1 
HETATM 17999 C  C17 . MLK QA 4 .   ? -18.691 30.605  56.538 1.00 85.41  ? 301 MLK G C17 1 
HETATM 18000 C  C26 . MLK QA 4 .   ? -19.064 28.873  54.944 1.00 92.23  ? 301 MLK G C26 1 
HETATM 18001 N  N23 . MLK QA 4 .   ? -17.698 28.908  54.464 1.00 87.91  ? 301 MLK G N23 1 
HETATM 18002 C  C24 . MLK QA 4 .   ? -17.662 28.539  53.050 1.00 82.52  ? 301 MLK G C24 1 
HETATM 18003 C  C25 . MLK QA 4 .   ? -18.274 27.147  52.846 1.00 81.58  ? 301 MLK G C25 1 
HETATM 18004 C  C23 . MLK QA 4 .   ? -16.982 30.142  54.718 1.00 79.21  ? 301 MLK G C23 1 
HETATM 18005 C  C30 . MLK QA 4 .   ? -20.515 28.904  56.982 1.00 94.63  ? 301 MLK G C30 1 
HETATM 18006 C  C33 . MLK QA 4 .   ? -20.990 27.451  56.860 1.00 92.36  ? 301 MLK G C33 1 
HETATM 18007 C  C34 . MLK QA 4 .   ? -22.451 27.513  56.320 1.00 97.91  ? 301 MLK G C34 1 
HETATM 18008 C  C35 . MLK QA 4 .   ? -22.349 27.256  54.795 1.00 108.20 ? 301 MLK G C35 1 
HETATM 18009 O  O35 . MLK QA 4 .   ? -23.616 26.969  54.190 1.00 107.95 ? 301 MLK G O35 1 
HETATM 18010 C  C37 . MLK QA 4 .   ? -23.376 25.867  53.308 1.00 100.35 ? 301 MLK G C37 1 
HETATM 18011 C  C36 . MLK QA 4 .   ? -21.597 28.341  54.039 1.00 95.19  ? 301 MLK G C36 1 
HETATM 18012 C  C31 . MLK QA 4 .   ? -21.584 29.728  56.215 1.00 96.71  ? 301 MLK G C31 1 
HETATM 18013 C  C38 . MLK QA 4 .   ? -22.905 28.979  56.517 1.00 97.42  ? 301 MLK G C38 1 
HETATM 18014 O  O38 . MLK QA 4 .   ? -23.917 29.396  55.613 1.00 102.39 ? 301 MLK G O38 1 
HETATM 18015 C  C39 . MLK QA 4 .   ? -25.157 29.005  56.202 1.00 105.00 ? 301 MLK G C39 1 
HETATM 18016 C  C32 . MLK QA 4 .   ? -21.383 29.685  54.709 1.00 91.78  ? 301 MLK G C32 1 
HETATM 18017 O  O32 . MLK QA 4 .   ? -22.262 30.622  54.052 1.00 85.08  ? 301 MLK G O32 1 
HETATM 18018 C  C27 . MLK QA 4 .   ? -19.916 30.061  54.426 1.00 94.55  ? 301 MLK G C27 1 
HETATM 18019 O  O27 . MLK QA 4 .   ? -19.759 30.338  53.026 1.00 83.79  ? 301 MLK G O27 1 
HETATM 18020 C  C28 . MLK QA 4 .   ? -19.460 31.247  55.342 1.00 91.07  ? 301 MLK G C28 1 
HETATM 18021 O  O28 . MLK QA 4 .   ? -20.495 32.125  55.801 1.00 87.12  ? 301 MLK G O28 1 
HETATM 18022 C  C29 . MLK QA 4 .   ? -19.903 33.370  56.182 1.00 83.58  ? 301 MLK G C29 1 
HETATM 18023 C  C1  . MPD RA 6 .   ? -8.770  20.185  53.949 1.00 65.63  ? 305 MPD G C1  1 
HETATM 18024 C  C2  . MPD RA 6 .   ? -9.340  19.087  53.032 1.00 85.17  ? 305 MPD G C2  1 
HETATM 18025 O  O2  . MPD RA 6 .   ? -9.411  17.828  53.778 1.00 75.48  ? 305 MPD G O2  1 
HETATM 18026 C  CM  . MPD RA 6 .   ? -10.732 19.466  52.532 1.00 74.39  ? 305 MPD G CM  1 
HETATM 18027 C  C3  . MPD RA 6 .   ? -8.462  18.903  51.797 1.00 73.86  ? 305 MPD G C3  1 
HETATM 18028 C  C4  . MPD RA 6 .   ? -8.287  17.441  51.383 1.00 94.65  ? 305 MPD G C4  1 
HETATM 18029 O  O4  . MPD RA 6 .   ? -9.534  16.754  51.314 1.00 88.20  ? 305 MPD G O4  1 
HETATM 18030 C  C5  . MPD RA 6 .   ? -7.573  17.396  50.025 1.00 93.88  ? 305 MPD G C5  1 
HETATM 18031 C  C1  . MPD SA 6 .   ? 12.677  18.628  53.565 1.00 69.31  ? 222 MPD G C1  1 
HETATM 18032 C  C2  . MPD SA 6 .   ? 12.495  17.998  54.941 1.00 76.68  ? 222 MPD G C2  1 
HETATM 18033 O  O2  . MPD SA 6 .   ? 13.756  18.067  55.654 1.00 70.00  ? 222 MPD G O2  1 
HETATM 18034 C  CM  . MPD SA 6 .   ? 11.442  18.761  55.734 1.00 68.16  ? 222 MPD G CM  1 
HETATM 18035 C  C3  . MPD SA 6 .   ? 12.092  16.535  54.801 1.00 79.74  ? 222 MPD G C3  1 
HETATM 18036 C  C4  . MPD SA 6 .   ? 11.787  16.191  53.348 1.00 92.94  ? 222 MPD G C4  1 
HETATM 18037 O  O4  . MPD SA 6 .   ? 12.877  15.488  52.793 1.00 91.06  ? 222 MPD G O4  1 
HETATM 18038 C  C5  . MPD SA 6 .   ? 10.527  15.341  53.241 1.00 84.41  ? 222 MPD G C5  1 
HETATM 18039 C  C1  . NAG TA 3 .   ? 34.955  17.654  48.209 1.00 89.76  ? 250 NAG H C1  1 
HETATM 18040 C  C2  . NAG TA 3 .   ? 36.457  17.428  48.075 1.00 101.69 ? 250 NAG H C2  1 
HETATM 18041 C  C3  . NAG TA 3 .   ? 37.158  18.031  49.286 1.00 105.70 ? 250 NAG H C3  1 
HETATM 18042 C  C4  . NAG TA 3 .   ? 36.604  19.409  49.651 1.00 110.45 ? 250 NAG H C4  1 
HETATM 18043 C  C5  . NAG TA 3 .   ? 35.084  19.520  49.510 1.00 99.20  ? 250 NAG H C5  1 
HETATM 18044 C  C6  . NAG TA 3 .   ? 34.568  20.940  49.748 1.00 95.01  ? 250 NAG H C6  1 
HETATM 18045 C  C7  . NAG TA 3 .   ? 37.427  15.212  48.781 1.00 105.44 ? 250 NAG H C7  1 
HETATM 18046 C  C8  . NAG TA 3 .   ? 37.934  13.910  48.227 1.00 93.12  ? 250 NAG H C8  1 
HETATM 18047 N  N2  . NAG TA 3 .   ? 36.761  16.004  47.911 1.00 106.45 ? 250 NAG H N2  1 
HETATM 18048 O  O3  . NAG TA 3 .   ? 38.542  18.090  49.014 1.00 111.77 ? 250 NAG H O3  1 
HETATM 18049 O  O4  . NAG TA 3 .   ? 36.927  19.667  51.000 1.00 128.22 ? 250 NAG H O4  1 
HETATM 18050 O  O5  . NAG TA 3 .   ? 34.684  19.031  48.253 1.00 86.30  ? 250 NAG H O5  1 
HETATM 18051 O  O6  . NAG TA 3 .   ? 35.569  21.872  49.413 1.00 106.83 ? 250 NAG H O6  1 
HETATM 18052 O  O7  . NAG TA 3 .   ? 37.638  15.464  49.975 1.00 109.57 ? 250 NAG H O7  1 
HETATM 18053 C  C1  . NAG UA 3 .   ? 38.119  20.234  51.268 1.00 133.41 ? 251 NAG H C1  1 
HETATM 18054 C  C2  . NAG UA 3 .   ? 38.173  20.515  52.767 1.00 132.64 ? 251 NAG H C2  1 
HETATM 18055 C  C3  . NAG UA 3 .   ? 39.471  21.207  53.190 1.00 147.47 ? 251 NAG H C3  1 
HETATM 18056 C  C4  . NAG UA 3 .   ? 40.721  20.685  52.454 1.00 147.23 ? 251 NAG H C4  1 
HETATM 18057 C  C5  . NAG UA 3 .   ? 40.442  20.357  50.989 1.00 142.79 ? 251 NAG H C5  1 
HETATM 18058 C  C6  . NAG UA 3 .   ? 41.627  19.685  50.280 1.00 142.78 ? 251 NAG H C6  1 
HETATM 18059 C  C7  . NAG UA 3 .   ? 36.745  22.533  52.965 1.00 126.36 ? 251 NAG H C7  1 
HETATM 18060 C  C8  . NAG UA 3 .   ? 35.510  23.113  53.614 1.00 106.08 ? 251 NAG H C8  1 
HETATM 18061 N  N2  . NAG UA 3 .   ? 36.977  21.230  53.230 1.00 123.71 ? 251 NAG H N2  1 
HETATM 18062 O  O3  . NAG UA 3 .   ? 39.582  20.973  54.580 1.00 146.73 ? 251 NAG H O3  1 
HETATM 18063 O  O4  . NAG UA 3 .   ? 41.771  21.639  52.455 1.00 152.58 ? 251 NAG H O4  1 
HETATM 18064 O  O5  . NAG UA 3 .   ? 39.294  19.541  50.896 1.00 140.47 ? 251 NAG H O5  1 
HETATM 18065 O  O6  . NAG UA 3 .   ? 42.709  19.410  51.146 1.00 136.18 ? 251 NAG H O6  1 
HETATM 18066 O  O7  . NAG UA 3 .   ? 37.464  23.249  52.243 1.00 127.45 ? 251 NAG H O7  1 
HETATM 18067 C  C1  . BMA VA 8 .   ? 41.613  22.600  53.526 1.00 148.65 ? 252 BMA H C1  1 
HETATM 18068 C  C2  . BMA VA 8 .   ? 42.181  22.076  54.861 1.00 146.35 ? 252 BMA H C2  1 
HETATM 18069 C  C3  . BMA VA 8 .   ? 43.157  23.072  55.485 1.00 144.52 ? 252 BMA H C3  1 
HETATM 18070 C  C4  . BMA VA 8 .   ? 42.500  24.446  55.560 1.00 142.55 ? 252 BMA H C4  1 
HETATM 18071 C  C5  . BMA VA 8 .   ? 41.831  24.840  54.242 1.00 141.47 ? 252 BMA H C5  1 
HETATM 18072 C  C6  . BMA VA 8 .   ? 42.227  26.250  53.811 1.00 135.46 ? 252 BMA H C6  1 
HETATM 18073 O  O2  . BMA VA 8 .   ? 42.815  20.793  54.733 1.00 136.94 ? 252 BMA H O2  1 
HETATM 18074 O  O3  . BMA VA 8 .   ? 44.416  23.124  54.794 1.00 140.77 ? 252 BMA H O3  1 
HETATM 18075 O  O4  . BMA VA 8 .   ? 41.518  24.398  56.602 1.00 126.82 ? 252 BMA H O4  1 
HETATM 18076 O  O5  . BMA VA 8 .   ? 42.153  23.892  53.222 1.00 142.15 ? 252 BMA H O5  1 
HETATM 18077 O  O6  . BMA VA 8 .   ? 43.650  26.397  53.860 1.00 132.37 ? 252 BMA H O6  1 
HETATM 18078 O  O8  . MLK WA 4 .   ? 12.787  35.404  66.830 1.00 94.67  ? 301 MLK H O8  1 
HETATM 18079 C  C8  . MLK WA 4 .   ? 13.499  36.219  66.277 1.00 96.40  ? 301 MLK H C8  1 
HETATM 18080 C  C9  . MLK WA 4 .   ? 13.370  37.718  66.443 1.00 94.71  ? 301 MLK H C9  1 
HETATM 18081 C  C10 . MLK WA 4 .   ? 13.843  38.200  65.053 1.00 98.03  ? 301 MLK H C10 1 
HETATM 18082 C  C12 . MLK WA 4 .   ? 12.664  38.455  64.107 1.00 70.22  ? 301 MLK H C12 1 
HETATM 18083 C  C11 . MLK WA 4 .   ? 14.665  37.026  64.555 1.00 90.82  ? 301 MLK H C11 1 
HETATM 18084 O  O11 . MLK WA 4 .   ? 15.341  37.068  63.546 1.00 89.86  ? 301 MLK H O11 1 
HETATM 18085 N  N7  . MLK WA 4 .   ? 14.519  35.991  65.418 1.00 90.60  ? 301 MLK H N7  1 
HETATM 18086 C  C6  . MLK WA 4 .   ? 15.374  34.861  65.506 1.00 83.53  ? 301 MLK H C6  1 
HETATM 18087 C  C5  . MLK WA 4 .   ? 16.623  35.095  66.074 1.00 81.67  ? 301 MLK H C5  1 
HETATM 18088 C  C4  . MLK WA 4 .   ? 17.556  34.083  66.247 1.00 80.19  ? 301 MLK H C4  1 
HETATM 18089 C  C3  . MLK WA 4 .   ? 17.283  32.780  65.875 1.00 72.43  ? 301 MLK H C3  1 
HETATM 18090 C  C2  . MLK WA 4 .   ? 16.056  32.515  65.311 1.00 78.95  ? 301 MLK H C2  1 
HETATM 18091 C  C1  . MLK WA 4 .   ? 15.080  33.514  65.114 1.00 82.39  ? 301 MLK H C1  1 
HETATM 18092 C  C13 . MLK WA 4 .   ? 13.820  33.020  64.499 1.00 75.94  ? 301 MLK H C13 1 
HETATM 18093 O  O13 . MLK WA 4 .   ? 12.963  33.773  64.072 1.00 75.09  ? 301 MLK H O13 1 
HETATM 18094 O  O14 . MLK WA 4 .   ? 13.650  31.677  64.432 1.00 69.67  ? 301 MLK H O14 1 
HETATM 18095 C  C15 . MLK WA 4 .   ? 12.484  31.061  63.819 1.00 74.98  ? 301 MLK H C15 1 
HETATM 18096 C  C16 . MLK WA 4 .   ? 12.451  29.574  64.194 1.00 74.91  ? 301 MLK H C16 1 
HETATM 18097 C  C21 . MLK WA 4 .   ? 13.804  28.976  63.808 1.00 70.34  ? 301 MLK H C21 1 
HETATM 18098 C  C20 . MLK WA 4 .   ? 14.407  28.099  64.908 1.00 78.10  ? 301 MLK H C20 1 
HETATM 18099 C  C19 . MLK WA 4 .   ? 13.352  27.250  65.599 1.00 83.53  ? 301 MLK H C19 1 
HETATM 18100 O  O19 . MLK WA 4 .   ? 13.050  26.152  64.727 1.00 78.22  ? 301 MLK H O19 1 
HETATM 18101 C  C22 . MLK WA 4 .   ? 14.295  25.486  64.509 1.00 67.34  ? 301 MLK H C22 1 
HETATM 18102 C  C18 . MLK WA 4 .   ? 12.115  27.997  66.086 1.00 85.86  ? 301 MLK H C18 1 
HETATM 18103 C  C17 . MLK WA 4 .   ? 12.141  29.490  65.706 1.00 82.36  ? 301 MLK H C17 1 
HETATM 18104 C  C26 . MLK WA 4 .   ? 10.770  27.573  65.425 1.00 80.25  ? 301 MLK H C26 1 
HETATM 18105 N  N23 . MLK WA 4 .   ? 10.966  27.565  64.004 1.00 75.58  ? 301 MLK H N23 1 
HETATM 18106 C  C24 . MLK WA 4 .   ? 9.771   26.968  63.425 1.00 74.85  ? 301 MLK H C24 1 
HETATM 18107 C  C25 . MLK WA 4 .   ? 9.520   25.636  64.146 1.00 73.19  ? 301 MLK H C25 1 
HETATM 18108 C  C23 . MLK WA 4 .   ? 11.340  28.838  63.420 1.00 73.77  ? 301 MLK H C23 1 
HETATM 18109 C  C30 . MLK WA 4 .   ? 11.948  27.814  67.597 1.00 92.27  ? 301 MLK H C30 1 
HETATM 18110 C  C33 . MLK WA 4 .   ? 11.776  26.352  68.042 1.00 85.06  ? 301 MLK H C33 1 
HETATM 18111 C  C34 . MLK WA 4 .   ? 10.614  26.358  69.080 1.00 96.12  ? 301 MLK H C34 1 
HETATM 18112 C  C35 . MLK WA 4 .   ? 9.349   25.966  68.276 1.00 91.40  ? 301 MLK H C35 1 
HETATM 18113 O  O35 . MLK WA 4 .   ? 8.359   25.337  69.095 1.00 99.25  ? 301 MLK H O35 1 
HETATM 18114 C  C37 . MLK WA 4 .   ? 8.407   23.938  68.799 1.00 94.53  ? 301 MLK H C37 1 
HETATM 18115 C  C36 . MLK WA 4 .   ? 8.756   27.090  67.445 1.00 87.21  ? 301 MLK H C36 1 
HETATM 18116 C  C31 . MLK WA 4 .   ? 10.733  28.573  68.205 1.00 92.44  ? 301 MLK H C31 1 
HETATM 18117 C  C38 . MLK WA 4 .   ? 10.513  27.835  69.554 1.00 97.98  ? 301 MLK H C38 1 
HETATM 18118 O  O38 . MLK WA 4 .   ? 9.279   28.207  70.161 1.00 101.17 ? 301 MLK H O38 1 
HETATM 18119 C  C39 . MLK WA 4 .   ? 9.572   28.551  71.516 1.00 90.47  ? 301 MLK H C39 1 
HETATM 18120 C  C32 . MLK WA 4 .   ? 9.450   28.445  67.390 1.00 92.78  ? 301 MLK H C32 1 
HETATM 18121 O  O32 . MLK WA 4 .   ? 8.506   29.454  67.854 1.00 90.49  ? 301 MLK H O32 1 
HETATM 18122 C  C27 . MLK WA 4 .   ? 9.791   28.689  65.885 1.00 89.61  ? 301 MLK H C27 1 
HETATM 18123 O  O27 . MLK WA 4 .   ? 8.603   28.784  65.071 1.00 83.43  ? 301 MLK H O27 1 
HETATM 18124 C  C28 . MLK WA 4 .   ? 10.655  29.975  65.759 1.00 87.72  ? 301 MLK H C28 1 
HETATM 18125 O  O28 . MLK WA 4 .   ? 10.397  30.950  66.775 1.00 83.86  ? 301 MLK H O28 1 
HETATM 18126 C  C29 . MLK WA 4 .   ? 11.197  32.093  66.488 1.00 76.91  ? 301 MLK H C29 1 
HETATM 18127 MG MG  . MG  XA 2 .   ? 2.015   4.146   3.114  1.00 34.10  ? 222 MG  I MG  1 
HETATM 18128 C  C1  . NAG YA 3 .   ? 22.509  22.210  11.946 1.00 91.96  ? 250 NAG I C1  1 
HETATM 18129 C  C2  . NAG YA 3 .   ? 23.076  22.434  10.537 1.00 98.03  ? 250 NAG I C2  1 
HETATM 18130 C  C3  . NAG YA 3 .   ? 24.246  23.419  10.521 1.00 103.17 ? 250 NAG I C3  1 
HETATM 18131 C  C4  . NAG YA 3 .   ? 23.882  24.688  11.286 1.00 103.49 ? 250 NAG I C4  1 
HETATM 18132 C  C5  . NAG YA 3 .   ? 23.297  24.370  12.658 1.00 102.63 ? 250 NAG I C5  1 
HETATM 18133 C  C6  . NAG YA 3 .   ? 22.850  25.638  13.400 1.00 104.08 ? 250 NAG I C6  1 
HETATM 18134 C  C7  . NAG YA 3 .   ? 22.613  20.559  9.074  1.00 97.63  ? 250 NAG I C7  1 
HETATM 18135 C  C8  . NAG YA 3 .   ? 23.159  19.356  8.334  1.00 88.70  ? 250 NAG I C8  1 
HETATM 18136 N  N2  . NAG YA 3 .   ? 23.456  21.165  9.932  1.00 99.34  ? 250 NAG I N2  1 
HETATM 18137 O  O3  . NAG YA 3 .   ? 24.606  23.761  9.193  1.00 91.98  ? 250 NAG I O3  1 
HETATM 18138 O  O4  . NAG YA 3 .   ? 25.037  25.475  11.472 1.00 100.12 ? 250 NAG I O4  1 
HETATM 18139 O  O5  . NAG YA 3 .   ? 22.224  23.450  12.562 1.00 100.29 ? 250 NAG I O5  1 
HETATM 18140 O  O6  . NAG YA 3 .   ? 21.929  26.396  12.639 1.00 91.83  ? 250 NAG I O6  1 
HETATM 18141 O  O7  . NAG YA 3 .   ? 21.446  20.946  8.880  1.00 82.65  ? 250 NAG I O7  1 
HETATM 18142 C  C1  A NAG ZA 3 .   ? 16.365  15.556  2.525  0.50 96.64  ? 275 NAG I C1  1 
HETATM 18143 C  C1  B NAG ZA 3 .   ? 13.773  10.967  1.110  0.50 94.13  ? 275 NAG I C1  1 
HETATM 18144 C  C2  A NAG ZA 3 .   ? 17.760  15.392  1.928  0.50 97.77  ? 275 NAG I C2  1 
HETATM 18145 C  C2  B NAG ZA 3 .   ? 12.479  10.300  0.611  0.50 95.25  ? 275 NAG I C2  1 
HETATM 18146 C  C3  A NAG ZA 3 .   ? 18.495  16.724  1.904  0.50 97.67  ? 275 NAG I C3  1 
HETATM 18147 C  C3  B NAG ZA 3 .   ? 12.662  8.983   -0.166 0.50 102.01 ? 275 NAG I C3  1 
HETATM 18148 C  C4  A NAG ZA 3 .   ? 17.629  17.719  1.159  0.50 102.16 ? 275 NAG I C4  1 
HETATM 18149 C  C4  B NAG ZA 3 .   ? 13.893  8.981   -1.059 0.50 103.46 ? 275 NAG I C4  1 
HETATM 18150 C  C5  A NAG ZA 3 .   ? 16.309  17.868  1.901  0.50 103.49 ? 275 NAG I C5  1 
HETATM 18151 C  C5  B NAG ZA 3 .   ? 15.005  9.664   -0.266 0.50 102.40 ? 275 NAG I C5  1 
HETATM 18152 C  C6  A NAG ZA 3 .   ? 15.423  18.913  1.232  0.50 105.91 ? 275 NAG I C6  1 
HETATM 18153 C  C6  B NAG ZA 3 .   ? 16.381  9.675   -0.906 0.50 96.71  ? 275 NAG I C6  1 
HETATM 18154 C  C7  A NAG ZA 3 .   ? 19.864  14.205  2.468  0.50 103.71 ? 275 NAG I C7  1 
HETATM 18155 C  C7  B NAG ZA 3 .   ? 11.120  9.020   2.207  0.50 92.37  ? 275 NAG I C7  1 
HETATM 18156 C  C8  A NAG ZA 3 .   ? 20.727  13.744  3.621  0.50 99.94  ? 275 NAG I C8  1 
HETATM 18157 C  C8  B NAG ZA 3 .   ? 12.169  8.072   2.701  0.50 81.71  ? 275 NAG I C8  1 
HETATM 18158 N  N2  A NAG ZA 3 .   ? 18.511  14.422  2.701  0.50 99.51  ? 275 NAG I N2  1 
HETATM 18159 N  N2  B NAG ZA 3 .   ? 11.533  10.182  1.706  0.50 89.75  ? 275 NAG I N2  1 
HETATM 18160 O  O3  A NAG ZA 3 .   ? 19.741  16.581  1.238  0.50 99.41  ? 275 NAG I O3  1 
HETATM 18161 O  O3  B NAG ZA 3 .   ? 11.523  8.781   -0.971 0.50 95.57  ? 275 NAG I O3  1 
HETATM 18162 O  O4  A NAG ZA 3 .   ? 18.283  18.978  1.076  0.50 99.38  ? 275 NAG I O4  1 
HETATM 18163 O  O4  B NAG ZA 3 .   ? 14.222  7.638   -1.336 0.50 98.37  ? 275 NAG I O4  1 
HETATM 18164 O  O5  A NAG ZA 3 .   ? 15.628  16.622  1.931  0.50 98.86  ? 275 NAG I O5  1 
HETATM 18165 O  O5  B NAG ZA 3 .   ? 14.645  11.002  0.005  0.50 97.77  ? 275 NAG I O5  1 
HETATM 18166 O  O6  A NAG ZA 3 .   ? 15.211  18.555  -0.127 0.50 96.14  ? 275 NAG I O6  1 
HETATM 18167 O  O6  B NAG ZA 3 .   ? 16.486  10.935  -1.517 0.50 86.33  ? 275 NAG I O6  1 
HETATM 18168 O  O7  A NAG ZA 3 .   ? 20.399  14.378  1.262  0.50 102.00 ? 275 NAG I O7  1 
HETATM 18169 O  O7  B NAG ZA 3 .   ? 9.937   8.702   2.290  0.50 89.88  ? 275 NAG I O7  1 
HETATM 18170 O  O8  . MLK AB 4 .   ? 31.100  38.746  40.138 1.00 101.22 ? 301 MLK I O8  1 
HETATM 18171 C  C8  . MLK AB 4 .   ? 30.363  39.461  39.492 1.00 96.25  ? 301 MLK I C8  1 
HETATM 18172 C  C9  . MLK AB 4 .   ? 29.356  40.436  40.062 1.00 94.21  ? 301 MLK I C9  1 
HETATM 18173 C  C10 . MLK AB 4 .   ? 29.046  41.347  38.861 1.00 92.44  ? 301 MLK I C10 1 
HETATM 18174 C  C12 . MLK AB 4 .   ? 27.552  41.662  38.761 1.00 83.51  ? 301 MLK I C12 1 
HETATM 18175 C  C11 . MLK AB 4 .   ? 29.505  40.496  37.699 1.00 97.34  ? 301 MLK I C11 1 
HETATM 18176 O  O11 . MLK AB 4 .   ? 29.168  40.679  36.547 1.00 102.27 ? 301 MLK I O11 1 
HETATM 18177 N  N7  . MLK AB 4 .   ? 30.326  39.525  38.156 1.00 97.54  ? 301 MLK I N7  1 
HETATM 18178 C  C6  . MLK AB 4 .   ? 31.093  38.666  37.336 1.00 97.99  ? 301 MLK I C6  1 
HETATM 18179 C  C5  . MLK AB 4 .   ? 32.139  39.208  36.590 1.00 99.01  ? 301 MLK I C5  1 
HETATM 18180 C  C4  . MLK AB 4 .   ? 32.925  38.407  35.778 1.00 108.75 ? 301 MLK I C4  1 
HETATM 18181 C  C3  . MLK AB 4 .   ? 32.697  37.039  35.692 1.00 101.47 ? 301 MLK I C3  1 
HETATM 18182 C  C2  . MLK AB 4 .   ? 31.677  36.475  36.426 1.00 94.34  ? 301 MLK I C2  1 
HETATM 18183 C  C1  . MLK AB 4 .   ? 30.864  37.266  37.257 1.00 96.53  ? 301 MLK I C1  1 
HETATM 18184 C  C13 . MLK AB 4 .   ? 29.797  36.575  38.020 1.00 92.02  ? 301 MLK I C13 1 
HETATM 18185 O  O13 . MLK AB 4 .   ? 28.948  37.192  38.637 1.00 88.08  ? 301 MLK I O13 1 
HETATM 18186 O  O14 . MLK AB 4 .   ? 29.806  35.223  38.037 1.00 87.52  ? 301 MLK I O14 1 
HETATM 18187 C  C15 . MLK AB 4 .   ? 29.168  34.454  39.089 1.00 86.29  ? 301 MLK I C15 1 
HETATM 18188 C  C16 . MLK AB 4 .   ? 29.607  32.991  38.955 1.00 88.51  ? 301 MLK I C16 1 
HETATM 18189 C  C21 . MLK AB 4 .   ? 29.633  32.662  37.463 1.00 82.46  ? 301 MLK I C21 1 
HETATM 18190 C  C20 . MLK AB 4 .   ? 30.896  31.915  37.023 1.00 85.32  ? 301 MLK I C20 1 
HETATM 18191 C  C19 . MLK AB 4 .   ? 31.316  30.849  38.020 1.00 92.54  ? 301 MLK I C19 1 
HETATM 18192 O  O19 . MLK AB 4 .   ? 30.451  29.707  37.887 1.00 86.47  ? 301 MLK I O19 1 
HETATM 18193 C  C22 . MLK AB 4 .   ? 31.137  28.721  37.107 1.00 78.17  ? 301 MLK I C22 1 
HETATM 18194 C  C18 . MLK AB 4 .   ? 31.393  31.341  39.453 1.00 93.93  ? 301 MLK I C18 1 
HETATM 18195 C  C17 . MLK AB 4 .   ? 30.998  32.818  39.624 1.00 93.51  ? 301 MLK I C17 1 
HETATM 18196 C  C26 . MLK AB 4 .   ? 30.384  30.665  40.444 1.00 98.94  ? 301 MLK I C26 1 
HETATM 18197 N  N23 . MLK AB 4 .   ? 29.025  30.743  39.937 1.00 95.39  ? 301 MLK I N23 1 
HETATM 18198 C  C24 . MLK AB 4 .   ? 28.118  30.052  40.861 1.00 85.13  ? 301 MLK I C24 1 
HETATM 18199 C  C25 . MLK AB 4 .   ? 28.595  28.625  41.164 1.00 76.52  ? 301 MLK I C25 1 
HETATM 18200 C  C23 . MLK AB 4 .   ? 28.558  32.084  39.630 1.00 88.28  ? 301 MLK I C23 1 
HETATM 18201 C  C30 . MLK AB 4 .   ? 32.806  31.092  39.956 1.00 98.72  ? 301 MLK I C30 1 
HETATM 18202 C  C33 . MLK AB 4 .   ? 33.190  29.604  39.925 1.00 98.29  ? 301 MLK I C33 1 
HETATM 18203 C  C34 . MLK AB 4 .   ? 34.014  29.345  41.224 1.00 104.56 ? 301 MLK I C34 1 
HETATM 18204 C  C35 . MLK AB 4 .   ? 33.044  28.677  42.220 1.00 102.33 ? 301 MLK I C35 1 
HETATM 18205 O  O35 . MLK AB 4 .   ? 33.764  28.171  43.350 1.00 95.30  ? 301 MLK I O35 1 
HETATM 18206 C  C37 . MLK AB 4 .   ? 33.372  26.810  43.532 1.00 92.14  ? 301 MLK I C37 1 
HETATM 18207 C  C36 . MLK AB 4 .   ? 31.867  29.579  42.597 1.00 98.52  ? 301 MLK I C36 1 
HETATM 18208 C  C31 . MLK AB 4 .   ? 33.064  31.536  41.419 1.00 105.31 ? 301 MLK I C31 1 
HETATM 18209 C  C38 . MLK AB 4 .   ? 34.358  30.747  41.801 1.00 106.51 ? 301 MLK I C38 1 
HETATM 18210 O  O38 . MLK AB 4 .   ? 34.615  30.758  43.208 1.00 105.33 ? 301 MLK I O38 1 
HETATM 18211 C  C39 . MLK AB 4 .   ? 36.030  30.798  43.419 1.00 100.34 ? 301 MLK I C39 1 
HETATM 18212 C  C32 . MLK AB 4 .   ? 31.940  31.090  42.344 1.00 100.41 ? 301 MLK I C32 1 
HETATM 18213 O  O32 . MLK AB 4 .   ? 32.053  31.761  43.624 1.00 97.86  ? 301 MLK I O32 1 
HETATM 18214 C  C27 . MLK AB 4 .   ? 30.591  31.528  41.712 1.00 98.16  ? 301 MLK I C27 1 
HETATM 18215 O  O27 . MLK AB 4 .   ? 29.526  31.417  42.671 1.00 96.95  ? 301 MLK I O27 1 
HETATM 18216 C  C28 . MLK AB 4 .   ? 30.692  32.979  41.145 1.00 93.98  ? 301 MLK I C28 1 
HETATM 18217 O  O28 . MLK AB 4 .   ? 31.615  33.836  41.829 1.00 95.70  ? 301 MLK I O28 1 
HETATM 18218 C  C29 . MLK AB 4 .   ? 31.730  35.072  41.116 1.00 90.96  ? 301 MLK I C29 1 
HETATM 18219 C  C1  . MPD BB 6 .   ? 21.253  21.019  33.292 1.00 82.89  ? 305 MPD I C1  1 
HETATM 18220 C  C2  . MPD BB 6 .   ? 22.345  20.919  34.351 1.00 79.83  ? 305 MPD I C2  1 
HETATM 18221 O  O2  . MPD BB 6 .   ? 23.503  20.181  33.896 1.00 79.39  ? 305 MPD I O2  1 
HETATM 18222 C  CM  . MPD BB 6 .   ? 22.815  22.335  34.658 1.00 80.93  ? 305 MPD I CM  1 
HETATM 18223 C  C3  . MPD BB 6 .   ? 21.784  20.134  35.533 1.00 79.26  ? 305 MPD I C3  1 
HETATM 18224 C  C4  . MPD BB 6 .   ? 20.747  19.094  35.019 1.00 92.47  ? 305 MPD I C4  1 
HETATM 18225 O  O4  . MPD BB 6 .   ? 21.289  17.777  34.857 1.00 90.68  ? 305 MPD I O4  1 
HETATM 18226 C  C5  . MPD BB 6 .   ? 19.503  19.015  35.929 1.00 81.74  ? 305 MPD I C5  1 
HETATM 18227 C  C1  . MPD CB 6 .   ? 7.028   22.026  19.834 1.00 64.35  ? 305 MPD J C1  1 
HETATM 18228 C  C2  . MPD CB 6 .   ? 5.581   21.537  19.909 1.00 82.67  ? 305 MPD J C2  1 
HETATM 18229 O  O2  . MPD CB 6 .   ? 4.747   22.723  19.724 1.00 68.71  ? 305 MPD J O2  1 
HETATM 18230 C  CM  . MPD CB 6 .   ? 5.301   20.482  18.848 1.00 75.06  ? 305 MPD J CM  1 
HETATM 18231 C  C3  . MPD CB 6 .   ? 5.251   20.832  21.224 1.00 82.02  ? 305 MPD J C3  1 
HETATM 18232 C  C4  . MPD CB 6 .   ? 4.201   21.575  22.051 1.00 97.39  ? 305 MPD J C4  1 
HETATM 18233 O  O4  . MPD CB 6 .   ? 2.898   21.058  21.796 1.00 83.99  ? 305 MPD J O4  1 
HETATM 18234 C  C5  . MPD CB 6 .   ? 4.567   21.513  23.540 1.00 89.76  ? 305 MPD J C5  1 
HETATM 18235 C  C1  . NAG DB 3 .   ? -16.737 21.915  12.524 1.00 94.80  ? 250 NAG J C1  1 
HETATM 18236 C  C2  . NAG DB 3 .   ? -18.206 21.880  12.149 1.00 108.78 ? 250 NAG J C2  1 
HETATM 18237 C  C3  . NAG DB 3 .   ? -18.462 22.509  10.777 1.00 112.23 ? 250 NAG J C3  1 
HETATM 18238 C  C4  . NAG DB 3 .   ? -17.722 23.842  10.601 1.00 119.87 ? 250 NAG J C4  1 
HETATM 18239 C  C5  . NAG DB 3 .   ? -16.266 23.661  11.056 1.00 102.70 ? 250 NAG J C5  1 
HETATM 18240 C  C6  . NAG DB 3 .   ? -15.441 24.947  11.081 1.00 99.06  ? 250 NAG J C6  1 
HETATM 18241 C  C7  . NAG DB 3 .   ? -19.817 20.265  13.036 1.00 110.82 ? 250 NAG J C7  1 
HETATM 18242 C  C8  . NAG DB 3 .   ? -20.393 18.880  12.908 1.00 96.41  ? 250 NAG J C8  1 
HETATM 18243 N  N2  . NAG DB 3 .   ? -18.782 20.532  12.202 1.00 105.05 ? 250 NAG J N2  1 
HETATM 18244 O  O3  . NAG DB 3 .   ? -19.858 22.677  10.564 1.00 119.38 ? 250 NAG J O3  1 
HETATM 18245 O  O4  . NAG DB 3 .   ? -17.811 24.265  9.242  1.00 132.62 ? 250 NAG J O4  1 
HETATM 18246 O  O5  . NAG DB 3 .   ? -16.267 23.221  12.375 1.00 94.33  ? 250 NAG J O5  1 
HETATM 18247 O  O6  . NAG DB 3 .   ? -15.654 25.559  12.340 1.00 91.15  ? 250 NAG J O6  1 
HETATM 18248 O  O7  . NAG DB 3 .   ? -20.299 21.068  13.862 1.00 111.06 ? 250 NAG J O7  1 
HETATM 18249 C  C1  . NAG EB 3 .   ? -18.374 25.533  9.156  1.00 137.36 ? 251 NAG J C1  1 
HETATM 18250 C  C2  . NAG EB 3 .   ? -17.511 26.420  8.253  1.00 135.27 ? 251 NAG J C2  1 
HETATM 18251 C  C3  . NAG EB 3 .   ? -18.133 27.800  8.036  1.00 144.99 ? 251 NAG J C3  1 
HETATM 18252 C  C4  . NAG EB 3 .   ? -19.643 27.768  7.775  1.00 148.41 ? 251 NAG J C4  1 
HETATM 18253 C  C5  . NAG EB 3 .   ? -20.341 26.736  8.663  1.00 143.98 ? 251 NAG J C5  1 
HETATM 18254 C  C6  . NAG EB 3 .   ? -21.813 26.625  8.261  1.00 133.08 ? 251 NAG J C6  1 
HETATM 18255 C  C7  . NAG EB 3 .   ? -15.285 27.490  8.297  1.00 136.47 ? 251 NAG J C7  1 
HETATM 18256 C  C8  . NAG EB 3 .   ? -14.692 28.431  9.317  1.00 123.54 ? 251 NAG J C8  1 
HETATM 18257 N  N2  . NAG EB 3 .   ? -16.147 26.569  8.751  1.00 136.79 ? 251 NAG J N2  1 
HETATM 18258 O  O3  . NAG EB 3 .   ? -17.478 28.382  6.929  1.00 144.98 ? 251 NAG J O3  1 
HETATM 18259 O  O4  . NAG EB 3 .   ? -20.239 29.052  7.975  1.00 149.43 ? 251 NAG J O4  1 
HETATM 18260 O  O5  . NAG EB 3 .   ? -19.681 25.478  8.605  1.00 138.75 ? 251 NAG J O5  1 
HETATM 18261 O  O6  . NAG EB 3 .   ? -22.566 26.020  9.287  1.00 136.36 ? 251 NAG J O6  1 
HETATM 18262 O  O7  . NAG EB 3 .   ? -14.968 27.580  7.107  1.00 125.12 ? 251 NAG J O7  1 
HETATM 18263 C  C1  . BMA FB 8 .   ? -19.810 30.034  6.994  1.00 152.20 ? 252 BMA J C1  1 
HETATM 18264 C  C2  . BMA FB 8 .   ? -20.886 31.096  6.735  1.00 152.98 ? 252 BMA J C2  1 
HETATM 18265 C  C3  . BMA FB 8 .   ? -20.435 32.076  5.645  1.00 151.42 ? 252 BMA J C3  1 
HETATM 18266 C  C4  . BMA FB 8 .   ? -19.028 32.611  5.907  1.00 148.88 ? 252 BMA J C4  1 
HETATM 18267 C  C5  . BMA FB 8 .   ? -18.055 31.481  6.267  1.00 152.63 ? 252 BMA J C5  1 
HETATM 18268 C  C6  . BMA FB 8 .   ? -16.642 31.988  6.603  1.00 143.94 ? 252 BMA J C6  1 
HETATM 18269 O  O2  . BMA FB 8 .   ? -21.187 31.810  7.945  1.00 149.49 ? 252 BMA J O2  1 
HETATM 18270 O  O3  . BMA FB 8 .   ? -21.342 33.186  5.544  1.00 145.27 ? 252 BMA J O3  1 
HETATM 18271 O  O4  . BMA FB 8 .   ? -18.583 33.301  4.729  1.00 140.28 ? 252 BMA J O4  1 
HETATM 18272 O  O5  . BMA FB 8 .   ? -18.592 30.701  7.345  1.00 158.14 ? 252 BMA J O5  1 
HETATM 18273 O  O6  . BMA FB 8 .   ? -16.454 32.230  8.007  1.00 139.15 ? 252 BMA J O6  1 
HETATM 18274 O  O8  . MLK GB 4 .   ? 11.588  41.902  14.231 1.00 87.70  ? 301 MLK J O8  1 
HETATM 18275 C  C8  . MLK GB 4 .   ? 10.681  42.493  14.783 1.00 93.26  ? 301 MLK J C8  1 
HETATM 18276 C  C9  . MLK GB 4 .   ? 10.843  43.675  15.725 1.00 98.50  ? 301 MLK J C9  1 
HETATM 18277 C  C10 . MLK GB 4 .   ? 9.393   44.184  15.874 1.00 101.69 ? 301 MLK J C10 1 
HETATM 18278 C  C12 . MLK GB 4 .   ? 9.081   44.613  17.308 1.00 91.63  ? 301 MLK J C12 1 
HETATM 18279 C  C11 . MLK GB 4 .   ? 8.601   42.956  15.478 1.00 94.92  ? 301 MLK J C11 1 
HETATM 18280 O  O11 . MLK GB 4 .   ? 7.481   42.701  15.873 1.00 88.56  ? 301 MLK J O11 1 
HETATM 18281 N  N7  . MLK GB 4 .   ? 9.369   42.233  14.634 1.00 90.95  ? 301 MLK J N7  1 
HETATM 18282 C  C6  . MLK GB 4 .   ? 8.894   41.364  13.631 1.00 92.34  ? 301 MLK J C6  1 
HETATM 18283 C  C5  . MLK GB 4 .   ? 8.461   41.965  12.448 1.00 96.38  ? 301 MLK J C5  1 
HETATM 18284 C  C4  . MLK GB 4 .   ? 7.987   41.211  11.385 1.00 92.05  ? 301 MLK J C4  1 
HETATM 18285 C  C3  . MLK GB 4 .   ? 7.941   39.825  11.481 1.00 92.94  ? 301 MLK J C3  1 
HETATM 18286 C  C2  . MLK GB 4 .   ? 8.371   39.201  12.635 1.00 89.60  ? 301 MLK J C2  1 
HETATM 18287 C  C1  . MLK GB 4 .   ? 8.858   39.943  13.723 1.00 89.57  ? 301 MLK J C1  1 
HETATM 18288 C  C13 . MLK GB 4 .   ? 9.282   39.174  14.914 1.00 87.23  ? 301 MLK J C13 1 
HETATM 18289 O  O13 . MLK GB 4 .   ? 9.502   39.736  15.966 1.00 87.43  ? 301 MLK J O13 1 
HETATM 18290 O  O14 . MLK GB 4 .   ? 9.429   37.832  14.827 1.00 80.74  ? 301 MLK J O14 1 
HETATM 18291 C  C15 . MLK GB 4 .   ? 10.525  37.159  15.508 1.00 82.54  ? 301 MLK J C15 1 
HETATM 18292 C  C16 . MLK GB 4 .   ? 10.672  35.745  14.935 1.00 86.94  ? 301 MLK J C16 1 
HETATM 18293 C  C21 . MLK GB 4 .   ? 9.314   35.407  14.327 1.00 81.99  ? 301 MLK J C21 1 
HETATM 18294 C  C20 . MLK GB 4 .   ? 9.283   33.970  13.806 1.00 81.47  ? 301 MLK J C20 1 
HETATM 18295 C  C19 . MLK GB 4 .   ? 10.526  33.578  13.015 1.00 88.12  ? 301 MLK J C19 1 
HETATM 18296 O  O19 . MLK GB 4 .   ? 10.710  32.157  13.192 1.00 85.20  ? 301 MLK J O19 1 
HETATM 18297 C  C22 . MLK GB 4 .   ? 9.443   31.501  13.045 1.00 72.00  ? 301 MLK J C22 1 
HETATM 18298 C  C18 . MLK GB 4 .   ? 11.846  34.277  13.305 1.00 88.55  ? 301 MLK J C18 1 
HETATM 18299 C  C17 . MLK GB 4 .   ? 11.732  35.728  13.808 1.00 92.21  ? 301 MLK J C17 1 
HETATM 18300 C  C26 . MLK GB 4 .   ? 12.634  33.637  14.492 1.00 88.37  ? 301 MLK J C26 1 
HETATM 18301 N  N23 . MLK GB 4 .   ? 11.692  33.518  15.588 1.00 86.48  ? 301 MLK J N23 1 
HETATM 18302 C  C24 . MLK GB 4 .   ? 12.277  32.698  16.648 1.00 75.53  ? 301 MLK J C24 1 
HETATM 18303 C  C25 . MLK GB 4 .   ? 12.659  31.329  16.063 1.00 78.37  ? 301 MLK J C25 1 
HETATM 18304 C  C23 . MLK GB 4 .   ? 11.080  34.754  16.053 1.00 82.83  ? 301 MLK J C23 1 
HETATM 18305 C  C30 . MLK GB 4 .   ? 12.706  34.232  12.050 1.00 96.33  ? 301 MLK J C30 1 
HETATM 18306 C  C33 . MLK GB 4 .   ? 12.925  32.814  11.504 1.00 94.70  ? 301 MLK J C33 1 
HETATM 18307 C  C34 . MLK GB 4 .   ? 14.430  32.730  11.127 1.00 100.94 ? 301 MLK J C34 1 
HETATM 18308 C  C35 . MLK GB 4 .   ? 15.131  32.069  12.332 1.00 103.57 ? 301 MLK J C35 1 
HETATM 18309 O  O35 . MLK GB 4 .   ? 16.414  31.583  11.936 1.00 102.83 ? 301 MLK J O35 1 
HETATM 18310 C  C37 . MLK GB 4 .   ? 16.286  30.160  11.980 1.00 97.16  ? 301 MLK J C37 1 
HETATM 18311 C  C36 . MLK GB 4 .   ? 15.162  32.917  13.606 1.00 95.60  ? 301 MLK J C36 1 
HETATM 18312 C  C31 . MLK GB 4 .   ? 14.127  34.828  12.239 1.00 103.62 ? 301 MLK J C31 1 
HETATM 18313 C  C38 . MLK GB 4 .   ? 14.928  34.196  11.064 1.00 108.00 ? 301 MLK J C38 1 
HETATM 18314 O  O38 . MLK GB 4 .   ? 16.330  34.343  11.272 1.00 113.14 ? 301 MLK J O38 1 
HETATM 18315 C  C39 . MLK GB 4 .   ? 16.663  35.664  10.817 1.00 106.89 ? 301 MLK J C39 1 
HETATM 18316 C  C32 . MLK GB 4 .   ? 14.785  34.395  13.546 1.00 95.49  ? 301 MLK J C32 1 
HETATM 18317 O  O32 . MLK GB 4 .   ? 15.981  35.170  13.820 1.00 92.89  ? 301 MLK J O32 1 
HETATM 18318 C  C27 . MLK GB 4 .   ? 13.785  34.660  14.699 1.00 93.28  ? 301 MLK J C27 1 
HETATM 18319 O  O27 . MLK GB 4 .   ? 14.476  34.646  15.957 1.00 96.28  ? 301 MLK J O27 1 
HETATM 18320 C  C28 . MLK GB 4 .   ? 13.080  36.026  14.536 1.00 94.49  ? 301 MLK J C28 1 
HETATM 18321 O  O28 . MLK GB 4 .   ? 13.879  36.994  13.861 1.00 103.55 ? 301 MLK J O28 1 
HETATM 18322 C  C29 . MLK GB 4 .   ? 13.106  38.191  13.738 1.00 95.92  ? 301 MLK J C29 1 
HETATM 18323 O  O   . HOH HB 9 .   ? 29.019  -12.560 69.133 1.00 62.44  ? 310 HOH A O   1 
HETATM 18324 O  O   . HOH HB 9 .   ? 26.387  -7.586  67.037 1.00 74.06  ? 311 HOH A O   1 
HETATM 18325 O  O   . HOH HB 9 .   ? 10.009  -50.417 34.084 1.00 65.99  ? 313 HOH A O   1 
HETATM 18326 O  O   . HOH HB 9 .   ? 19.181  -49.430 39.481 1.00 55.76  ? 314 HOH A O   1 
HETATM 18327 O  O   . HOH HB 9 .   ? 32.744  -12.430 29.384 1.00 74.90  ? 316 HOH A O   1 
HETATM 18328 O  O   . HOH HB 9 .   ? 30.509  -11.100 30.896 1.00 68.18  ? 317 HOH A O   1 
HETATM 18329 O  O   . HOH HB 9 .   ? 19.288  -33.064 26.419 1.00 67.46  ? 325 HOH A O   1 
HETATM 18330 O  O   . HOH HB 9 .   ? 42.198  -30.448 30.145 1.00 75.22  ? 327 HOH A O   1 
HETATM 18331 O  O   . HOH HB 9 .   ? 36.940  -25.125 7.546  1.00 73.89  ? 329 HOH A O   1 
HETATM 18332 O  O   . HOH HB 9 .   ? 38.423  -26.141 5.379  1.00 59.45  ? 330 HOH A O   1 
HETATM 18333 O  O   . HOH HB 9 .   ? 41.341  -25.501 4.046  1.00 46.09  ? 331 HOH A O   1 
HETATM 18334 O  O   . HOH HB 9 .   ? 41.777  -27.951 21.186 1.00 64.79  ? 332 HOH A O   1 
HETATM 18335 O  O   . HOH IB 9 .   ? -18.266 -0.740  64.640 1.00 69.20  ? 312 HOH B O   1 
HETATM 18336 O  O   . HOH IB 9 .   ? 12.366  -20.643 47.975 1.00 55.98  ? 320 HOH B O   1 
HETATM 18337 O  O   . HOH IB 9 .   ? 10.512  -15.685 53.444 1.00 62.08  ? 323 HOH B O   1 
HETATM 18338 O  O   . HOH IB 9 .   ? 10.654  -44.159 34.354 1.00 54.01  ? 324 HOH B O   1 
HETATM 18339 O  O   . HOH IB 9 .   ? 38.239  -32.052 54.186 1.00 87.92  ? 325 HOH B O   1 
HETATM 18340 O  O   . HOH IB 9 .   ? 22.400  -17.844 49.469 1.00 64.21  ? 327 HOH B O   1 
HETATM 18341 O  O   . HOH IB 9 .   ? 14.660  -47.786 69.064 1.00 73.10  ? 328 HOH B O   1 
HETATM 18342 O  O   . HOH IB 9 .   ? 5.564   -45.325 64.807 1.00 59.21  ? 329 HOH B O   1 
HETATM 18343 O  O   . HOH IB 9 .   ? -7.630  -50.884 52.061 1.00 73.83  ? 330 HOH B O   1 
HETATM 18344 O  O   . HOH IB 9 .   ? 4.347   -52.229 58.284 1.00 70.26  ? 331 HOH B O   1 
HETATM 18345 O  O   . HOH IB 9 .   ? 18.536  -44.504 59.551 1.00 62.43  ? 332 HOH B O   1 
HETATM 18346 O  O   . HOH IB 9 .   ? 38.995  -34.469 53.516 1.00 72.77  ? 333 HOH B O   1 
HETATM 18347 O  O   . HOH JB 9 .   ? -3.971  -56.226 38.302 1.00 58.03  ? 316 HOH C O   1 
HETATM 18348 O  O   . HOH JB 9 .   ? -6.730  -20.839 44.373 1.00 60.89  ? 320 HOH C O   1 
HETATM 18349 O  O   . HOH JB 9 .   ? -12.410 -15.119 47.159 1.00 57.77  ? 323 HOH C O   1 
HETATM 18350 O  O   . HOH JB 9 .   ? -14.034 -18.248 47.325 1.00 54.58  ? 324 HOH C O   1 
HETATM 18351 O  O   . HOH JB 9 .   ? -8.289  -45.095 54.821 1.00 63.09  ? 327 HOH C O   1 
HETATM 18352 O  O   . HOH JB 9 .   ? -7.317  -35.510 60.826 1.00 73.09  ? 333 HOH C O   1 
HETATM 18353 O  O   . HOH JB 9 .   ? -4.742  -34.679 76.251 1.00 58.44  ? 334 HOH C O   1 
HETATM 18354 O  O   . HOH KB 9 .   ? -0.735  -14.148 23.871 1.00 61.66  ? 318 HOH D O   1 
HETATM 18355 O  O   . HOH KB 9 .   ? -13.524 -12.455 23.194 1.00 55.53  ? 323 HOH D O   1 
HETATM 18356 O  O   . HOH KB 9 .   ? -21.303 -43.602 28.464 1.00 58.70  ? 327 HOH D O   1 
HETATM 18357 O  O   . HOH LB 9 .   ? 17.341  -30.200 8.022  1.00 52.88  ? 313 HOH E O   1 
HETATM 18358 O  O   . HOH LB 9 .   ? 26.314  1.143   5.631  1.00 64.19  ? 316 HOH E O   1 
HETATM 18359 O  O   . HOH LB 9 .   ? 9.482   -14.100 25.989 1.00 64.47  ? 318 HOH E O   1 
HETATM 18360 O  O   . HOH LB 9 .   ? 6.241   -17.854 19.611 1.00 60.05  ? 320 HOH E O   1 
HETATM 18361 O  O   . HOH LB 9 .   ? 8.966   -11.819 15.674 1.00 52.90  ? 323 HOH E O   1 
HETATM 18362 O  O   . HOH LB 9 .   ? -1.597  -31.966 14.633 1.00 59.96  ? 325 HOH E O   1 
HETATM 18363 O  O   . HOH LB 9 .   ? 16.535  -33.702 26.306 1.00 53.89  ? 326 HOH E O   1 
HETATM 18364 O  O   . HOH LB 9 .   ? 27.221  -15.888 2.437  1.00 89.24  ? 327 HOH E O   1 
HETATM 18365 O  O   . HOH LB 9 .   ? -12.276 -19.330 -1.468 1.00 83.73  ? 328 HOH E O   1 
HETATM 18366 O  O   . HOH MB 9 .   ? -10.609 19.799  38.045 1.00 69.25  ? 320 HOH F O   1 
HETATM 18367 O  O   . HOH MB 9 .   ? -17.333 14.933  39.078 1.00 56.82  ? 323 HOH F O   1 
HETATM 18368 O  O   . HOH MB 9 .   ? -9.871  33.767  52.573 1.00 49.00  ? 325 HOH F O   1 
HETATM 18369 O  O   . HOH MB 9 .   ? -6.274  25.934  46.855 1.00 60.08  ? 326 HOH F O   1 
HETATM 18370 O  O   . HOH MB 9 .   ? -4.917  29.035  42.850 1.00 57.42  ? 327 HOH F O   1 
HETATM 18371 O  O   . HOH NB 9 .   ? -11.724 50.003  51.021 1.00 66.43  ? 314 HOH G O   1 
HETATM 18372 O  O   . HOH NB 9 .   ? -1.105  19.496  52.816 1.00 59.78  ? 320 HOH G O   1 
HETATM 18373 O  O   . HOH NB 9 .   ? -1.056  18.151  50.366 1.00 57.54  ? 321 HOH G O   1 
HETATM 18374 O  O   . HOH NB 9 .   ? -1.513  12.584  57.241 1.00 57.38  ? 323 HOH G O   1 
HETATM 18375 O  O   . HOH NB 9 .   ? -4.360  23.075  53.498 1.00 48.52  ? 326 HOH G O   1 
HETATM 18376 O  O   . HOH OB 9 .   ? 20.374  13.823  48.720 1.00 48.66  ? 323 HOH H O   1 
HETATM 18377 O  O   . HOH OB 9 .   ? 28.618  24.637  67.965 1.00 72.59  ? 328 HOH H O   1 
HETATM 18378 O  O   . HOH OB 9 .   ? 27.895  60.883  44.600 1.00 60.52  ? 336 HOH H O   1 
HETATM 18379 O  O   . HOH OB 9 .   ? 42.801  27.419  50.889 1.00 62.26  ? 337 HOH H O   1 
HETATM 18380 O  O   . HOH OB 9 .   ? 43.679  21.145  57.490 1.00 82.55  ? 338 HOH H O   1 
HETATM 18381 O  O   . HOH PB 9 .   ? 3.635   8.168   -3.110 1.00 58.39  ? 310 HOH I O   1 
HETATM 18382 O  O   . HOH PB 9 .   ? 10.887  52.355  26.089 1.00 61.37  ? 315 HOH I O   1 
HETATM 18383 O  O   . HOH PB 9 .   ? 26.947  14.687  22.587 1.00 68.02  ? 317 HOH I O   1 
HETATM 18384 O  O   . HOH PB 9 .   ? 38.249  27.861  23.252 1.00 73.64  ? 326 HOH I O   1 
HETATM 18385 O  O   . HOH PB 9 .   ? 33.731  33.525  18.075 1.00 73.79  ? 327 HOH I O   1 
HETATM 18386 O  O   . HOH PB 9 .   ? 33.704  25.064  38.980 1.00 79.35  ? 333 HOH I O   1 
HETATM 18387 O  O   . HOH PB 9 .   ? 27.030  21.662  9.153  1.00 71.80  ? 334 HOH I O   1 
HETATM 18388 O  O   . HOH PB 9 .   ? 27.752  26.707  10.905 1.00 52.76  ? 335 HOH I O   1 
HETATM 18389 O  O   . HOH QB 9 .   ? -31.143 4.686   24.448 1.00 84.72  ? 310 HOH J O   1 
HETATM 18390 O  O   . HOH QB 9 .   ? -11.361 7.683   16.053 1.00 57.16  ? 316 HOH J O   1 
HETATM 18391 O  O   . HOH QB 9 .   ? -3.985  14.348  25.926 1.00 67.56  ? 318 HOH J O   1 
HETATM 18392 O  O   . HOH QB 9 .   ? -3.917  17.103  19.514 1.00 64.24  ? 323 HOH J O   1 
HETATM 18393 O  O   . HOH QB 9 .   ? -23.843 34.414  7.003  1.00 77.60  ? 330 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   -8  ?   ?   ?   A . n 
A 1 2   TYR 2   -7  ?   ?   ?   A . n 
A 1 3   LYS 3   -6  ?   ?   ?   A . n 
A 1 4   ASP 4   -5  -5  ASP ASP A . n 
A 1 5   ASP 5   -4  -4  ASP ASP A . n 
A 1 6   ASP 6   -3  -3  ASP ASP A . n 
A 1 7   ASP 7   -2  -2  ASP ASP A . n 
A 1 8   LYS 8   -1  -1  LYS LYS A . n 
A 1 9   LEU 9   0   0   LEU LEU A . n 
A 1 10  HIS 10  1   1   HIS HIS A . n 
A 1 11  SER 11  2   2   SER SER A . n 
A 1 12  GLN 12  3   3   GLN GLN A . n 
A 1 13  ALA 13  4   4   ALA ALA A . n 
A 1 14  ASN 14  5   5   ASN ASN A . n 
A 1 15  LEU 15  6   6   LEU LEU A . n 
A 1 16  MET 16  7   7   MET MET A . n 
A 1 17  ARG 17  8   8   ARG ARG A . n 
A 1 18  LEU 18  9   9   LEU LEU A . n 
A 1 19  LYS 19  10  10  LYS LYS A . n 
A 1 20  SER 20  11  11  SER SER A . n 
A 1 21  ASP 21  12  12  ASP ASP A . n 
A 1 22  LEU 22  13  13  LEU LEU A . n 
A 1 23  PHE 23  14  14  PHE PHE A . n 
A 1 24  ASN 24  15  15  ASN ASN A . n 
A 1 25  ARG 25  16  16  ARG ARG A . n 
A 1 26  SER 26  17  17  SER SER A . n 
A 1 27  PRO 27  18  18  PRO PRO A . n 
A 1 28  MET 28  19  19  MET MET A . n 
A 1 29  TYR 29  20  20  TYR TYR A . n 
A 1 30  PRO 30  21  21  PRO PRO A . n 
A 1 31  GLY 31  22  22  GLY GLY A . n 
A 1 32  PRO 32  23  23  PRO PRO A . n 
A 1 33  THR 33  24  24  THR THR A . n 
A 1 34  LYS 34  25  25  LYS LYS A . n 
A 1 35  ASP 35  26  26  ASP ASP A . n 
A 1 36  ASP 36  27  27  ASP ASP A . n 
A 1 37  PRO 37  28  28  PRO PRO A . n 
A 1 38  LEU 38  29  29  LEU LEU A . n 
A 1 39  THR 39  30  30  THR THR A . n 
A 1 40  VAL 40  31  31  VAL VAL A . n 
A 1 41  TYR 41  32  32  TYR TYR A . n 
A 1 42  LEU 42  33  33  LEU LEU A . n 
A 1 43  SER 43  34  34  SER SER A . n 
A 1 44  PHE 44  35  35  PHE PHE A . n 
A 1 45  SER 45  36  36  SER SER A . n 
A 1 46  LEU 46  37  37  LEU LEU A . n 
A 1 47  LEU 47  38  38  LEU LEU A . n 
A 1 48  ASP 48  39  39  ASP ASP A . n 
A 1 49  ILE 49  40  40  ILE ILE A . n 
A 1 50  VAL 50  41  41  VAL VAL A . n 
A 1 51  LYS 51  42  42  LYS LYS A . n 
A 1 52  ALA 52  43  43  ALA ALA A . n 
A 1 53  ASP 53  44  44  ASP ASP A . n 
A 1 54  SER 54  45  45  SER SER A . n 
A 1 55  SER 55  46  46  SER SER A . n 
A 1 56  THR 56  47  47  THR THR A . n 
A 1 57  ASN 57  48  48  ASN ASN A . n 
A 1 58  GLU 58  49  49  GLU GLU A . n 
A 1 59  VAL 59  50  50  VAL VAL A . n 
A 1 60  ASP 60  51  51  ASP ASP A . n 
A 1 61  LEU 61  52  52  LEU LEU A . n 
A 1 62  VAL 62  53  53  VAL VAL A . n 
A 1 63  TYR 63  54  54  TYR TYR A . n 
A 1 64  TRP 64  55  55  TRP TRP A . n 
A 1 65  GLU 65  56  56  GLU GLU A . n 
A 1 66  GLN 66  57  57  GLN GLN A . n 
A 1 67  GLN 67  58  58  GLN GLN A . n 
A 1 68  SER 68  59  59  SER SER A . n 
A 1 69  TRP 69  60  60  TRP TRP A . n 
A 1 70  LYS 70  61  61  LYS LYS A . n 
A 1 71  LEU 71  62  62  LEU LEU A . n 
A 1 72  ASN 72  63  63  ASN ASN A . n 
A 1 73  SER 73  64  64  SER SER A . n 
A 1 74  LEU 74  65  65  LEU LEU A . n 
A 1 75  MET 75  66  66  MET MET A . n 
A 1 76  TRP 76  67  67  TRP TRP A . n 
A 1 77  ASP 77  68  68  ASP ASP A . n 
A 1 78  PRO 78  69  69  PRO PRO A . n 
A 1 79  ASN 79  70  70  ASN ASN A . n 
A 1 80  GLU 80  71  71  GLU GLU A . n 
A 1 81  TYR 81  72  72  TYR TYR A . n 
A 1 82  GLY 82  73  73  GLY GLY A . n 
A 1 83  ASN 83  74  74  ASN ASN A . n 
A 1 84  ILE 84  75  75  ILE ILE A . n 
A 1 85  THR 85  76  76  THR THR A . n 
A 1 86  ASP 86  77  77  ASP ASP A . n 
A 1 87  PHE 87  78  78  PHE PHE A . n 
A 1 88  ARG 88  79  79  ARG ARG A . n 
A 1 89  THR 89  80  80  THR THR A . n 
A 1 90  SER 90  81  81  SER SER A . n 
A 1 91  ALA 91  82  82  ALA ALA A . n 
A 1 92  ALA 92  83  83  ALA ALA A . n 
A 1 93  ASP 93  84  84  ASP ASP A . n 
A 1 94  ILE 94  85  85  ILE ILE A . n 
A 1 95  TRP 95  86  86  TRP TRP A . n 
A 1 96  THR 96  87  87  THR THR A . n 
A 1 97  PRO 97  88  88  PRO PRO A . n 
A 1 98  ASP 98  89  89  ASP ASP A . n 
A 1 99  ILE 99  90  90  ILE ILE A . n 
A 1 100 THR 100 91  91  THR THR A . n 
A 1 101 ALA 101 92  92  ALA ALA A . n 
A 1 102 TYR 102 93  93  TYR TYR A . n 
A 1 103 SER 103 94  94  SER SER A . n 
A 1 104 SER 104 95  95  SER SER A . n 
A 1 105 THR 105 96  96  THR THR A . n 
A 1 106 ARG 106 97  97  ARG ARG A . n 
A 1 107 PRO 107 98  98  PRO PRO A . n 
A 1 108 VAL 108 99  99  VAL VAL A . n 
A 1 109 GLN 109 100 100 GLN GLN A . n 
A 1 110 VAL 110 101 101 VAL VAL A . n 
A 1 111 LEU 111 102 102 LEU LEU A . n 
A 1 112 SER 112 103 103 SER SER A . n 
A 1 113 PRO 113 104 104 PRO PRO A . n 
A 1 114 GLN 114 105 105 GLN GLN A . n 
A 1 115 ASN 115 106 106 ASN ASN A . n 
A 1 116 ALA 116 107 107 ALA ALA A . n 
A 1 117 LEU 117 108 108 LEU LEU A . n 
A 1 118 VAL 118 109 109 VAL VAL A . n 
A 1 119 ASN 119 110 110 ASN ASN A . n 
A 1 120 SER 120 111 111 SER SER A . n 
A 1 121 SER 121 112 112 SER SER A . n 
A 1 122 GLY 122 113 113 GLY GLY A . n 
A 1 123 HIS 123 114 114 HIS HIS A . n 
A 1 124 VAL 124 115 115 VAL VAL A . n 
A 1 125 GLN 125 116 116 GLN GLN A . n 
A 1 126 TYR 126 117 117 TYR TYR A . n 
A 1 127 LEU 127 118 118 LEU LEU A . n 
A 1 128 PRO 128 119 119 PRO PRO A . n 
A 1 129 ALA 129 120 120 ALA ALA A . n 
A 1 130 GLN 130 121 121 GLN GLN A . n 
A 1 131 ARG 131 122 122 ARG ARG A . n 
A 1 132 LEU 132 123 123 LEU LEU A . n 
A 1 133 SER 133 124 124 SER SER A . n 
A 1 134 PHE 134 125 125 PHE PHE A . n 
A 1 135 MET 135 126 126 MET MET A . n 
A 1 136 CYS 136 127 127 CYS CYS A . n 
A 1 137 ASP 137 128 128 ASP ASP A . n 
A 1 138 PRO 138 129 129 PRO PRO A . n 
A 1 139 THR 139 130 130 THR THR A . n 
A 1 140 GLY 140 131 131 GLY GLY A . n 
A 1 141 VAL 141 132 132 VAL VAL A . n 
A 1 142 ASP 142 133 133 ASP ASP A . n 
A 1 143 SER 143 134 134 SER SER A . n 
A 1 144 GLU 144 135 135 GLU GLU A . n 
A 1 145 GLU 145 136 136 GLU GLU A . n 
A 1 146 GLY 146 137 137 GLY GLY A . n 
A 1 147 ALA 147 138 138 ALA ALA A . n 
A 1 148 THR 148 139 139 THR THR A . n 
A 1 149 CYS 149 140 140 CYS CYS A . n 
A 1 150 ALA 150 141 141 ALA ALA A . n 
A 1 151 VAL 151 142 142 VAL VAL A . n 
A 1 152 LYS 152 143 143 LYS LYS A . n 
A 1 153 PHE 153 144 144 PHE PHE A . n 
A 1 154 GLY 154 145 145 GLY GLY A . n 
A 1 155 SER 155 146 146 SER SER A . n 
A 1 156 TRP 156 147 147 TRP TRP A . n 
A 1 157 SER 157 148 148 SER SER A . n 
A 1 158 TYR 158 149 149 TYR TYR A . n 
A 1 159 GLY 159 150 150 GLY GLY A . n 
A 1 160 GLY 160 151 151 GLY GLY A . n 
A 1 161 TRP 161 152 152 TRP TRP A . n 
A 1 162 GLU 162 153 153 GLU GLU A . n 
A 1 163 ILE 163 154 154 ILE ILE A . n 
A 1 164 ASP 164 155 155 ASP ASP A . n 
A 1 165 LEU 165 156 156 LEU LEU A . n 
A 1 166 LYS 166 157 157 LYS LYS A . n 
A 1 167 THR 167 158 158 THR THR A . n 
A 1 168 ASP 168 159 159 ASP ASP A . n 
A 1 169 THR 169 160 160 THR THR A . n 
A 1 170 ASP 170 161 161 ASP ASP A . n 
A 1 171 GLN 171 162 162 GLN GLN A . n 
A 1 172 VAL 172 163 163 VAL VAL A . n 
A 1 173 ASP 173 164 164 ASP ASP A . n 
A 1 174 LEU 174 165 165 LEU LEU A . n 
A 1 175 SER 175 166 166 SER SER A . n 
A 1 176 SER 176 167 167 SER SER A . n 
A 1 177 TYR 177 168 168 TYR TYR A . n 
A 1 178 TYR 178 169 169 TYR TYR A . n 
A 1 179 ALA 179 170 170 ALA ALA A . n 
A 1 180 SER 180 171 171 SER SER A . n 
A 1 181 SER 181 172 172 SER SER A . n 
A 1 182 LYS 182 173 173 LYS LYS A . n 
A 1 183 TYR 183 174 174 TYR TYR A . n 
A 1 184 GLU 184 175 175 GLU GLU A . n 
A 1 185 ILE 185 176 176 ILE ILE A . n 
A 1 186 LEU 186 177 177 LEU LEU A . n 
A 1 187 SER 187 178 178 SER SER A . n 
A 1 188 ALA 188 179 179 ALA ALA A . n 
A 1 189 THR 189 180 180 THR THR A . n 
A 1 190 GLN 190 181 181 GLN GLN A . n 
A 1 191 THR 191 182 182 THR THR A . n 
A 1 192 ARG 192 183 183 ARG ARG A . n 
A 1 193 SER 193 184 184 SER SER A . n 
A 1 194 GLU 194 185 185 GLU GLU A . n 
A 1 195 ARG 195 186 186 ARG ARG A . n 
A 1 196 PHE 196 187 187 PHE PHE A . n 
A 1 197 TYR 197 188 188 TYR TYR A . n 
A 1 198 GLU 198 189 189 GLU GLU A . n 
A 1 199 CYS 199 190 190 CYS CYS A . n 
A 1 200 CYS 200 191 191 CYS CYS A . n 
A 1 201 LYS 201 192 192 LYS LYS A . n 
A 1 202 GLU 202 193 193 GLU GLU A . n 
A 1 203 PRO 203 194 194 PRO PRO A . n 
A 1 204 TYR 204 195 195 TYR TYR A . n 
A 1 205 PRO 205 196 196 PRO PRO A . n 
A 1 206 ASP 206 197 197 ASP ASP A . n 
A 1 207 VAL 207 198 198 VAL VAL A . n 
A 1 208 ASN 208 199 199 ASN ASN A . n 
A 1 209 LEU 209 200 200 LEU LEU A . n 
A 1 210 VAL 210 201 201 VAL VAL A . n 
A 1 211 VAL 211 202 202 VAL VAL A . n 
A 1 212 LYS 212 203 203 LYS LYS A . n 
A 1 213 PHE 213 204 204 PHE PHE A . n 
A 1 214 ARG 214 205 205 ARG ARG A . n 
A 1 215 GLU 215 206 206 GLU GLU A . n 
A 1 216 ARG 216 207 207 ARG ARG A . n 
A 1 217 ARG 217 208 208 ARG ARG A . n 
A 1 218 ALA 218 209 ?   ?   ?   A . n 
A 1 219 GLY 219 210 ?   ?   ?   A . n 
A 1 220 ASN 220 211 ?   ?   ?   A . n 
A 1 221 GLY 221 212 ?   ?   ?   A . n 
A 1 222 PHE 222 213 ?   ?   ?   A . n 
A 1 223 PHE 223 214 ?   ?   ?   A . n 
A 1 224 ARG 224 215 ?   ?   ?   A . n 
A 1 225 ASN 225 216 ?   ?   ?   A . n 
A 1 226 LEU 226 217 ?   ?   ?   A . n 
A 1 227 PHE 227 218 ?   ?   ?   A . n 
A 1 228 ASP 228 219 ?   ?   ?   A . n 
A 1 229 SER 229 220 ?   ?   ?   A . n 
A 1 230 ARG 230 221 ?   ?   ?   A . n 
B 1 1   ASP 1   -8  ?   ?   ?   B . n 
B 1 2   TYR 2   -7  ?   ?   ?   B . n 
B 1 3   LYS 3   -6  -6  LYS LYS B . n 
B 1 4   ASP 4   -5  -5  ASP ASP B . n 
B 1 5   ASP 5   -4  -4  ASP ASP B . n 
B 1 6   ASP 6   -3  -3  ASP ASP B . n 
B 1 7   ASP 7   -2  -2  ASP ASP B . n 
B 1 8   LYS 8   -1  -1  LYS LYS B . n 
B 1 9   LEU 9   0   0   LEU LEU B . n 
B 1 10  HIS 10  1   1   HIS HIS B . n 
B 1 11  SER 11  2   2   SER SER B . n 
B 1 12  GLN 12  3   3   GLN GLN B . n 
B 1 13  ALA 13  4   4   ALA ALA B . n 
B 1 14  ASN 14  5   5   ASN ASN B . n 
B 1 15  LEU 15  6   6   LEU LEU B . n 
B 1 16  MET 16  7   7   MET MET B . n 
B 1 17  ARG 17  8   8   ARG ARG B . n 
B 1 18  LEU 18  9   9   LEU LEU B . n 
B 1 19  LYS 19  10  10  LYS LYS B . n 
B 1 20  SER 20  11  11  SER SER B . n 
B 1 21  ASP 21  12  12  ASP ASP B . n 
B 1 22  LEU 22  13  13  LEU LEU B . n 
B 1 23  PHE 23  14  14  PHE PHE B . n 
B 1 24  ASN 24  15  15  ASN ASN B . n 
B 1 25  ARG 25  16  16  ARG ARG B . n 
B 1 26  SER 26  17  17  SER SER B . n 
B 1 27  PRO 27  18  18  PRO PRO B . n 
B 1 28  MET 28  19  19  MET MET B . n 
B 1 29  TYR 29  20  20  TYR TYR B . n 
B 1 30  PRO 30  21  21  PRO PRO B . n 
B 1 31  GLY 31  22  22  GLY GLY B . n 
B 1 32  PRO 32  23  23  PRO PRO B . n 
B 1 33  THR 33  24  24  THR THR B . n 
B 1 34  LYS 34  25  25  LYS LYS B . n 
B 1 35  ASP 35  26  26  ASP ASP B . n 
B 1 36  ASP 36  27  27  ASP ASP B . n 
B 1 37  PRO 37  28  28  PRO PRO B . n 
B 1 38  LEU 38  29  29  LEU LEU B . n 
B 1 39  THR 39  30  30  THR THR B . n 
B 1 40  VAL 40  31  31  VAL VAL B . n 
B 1 41  TYR 41  32  32  TYR TYR B . n 
B 1 42  LEU 42  33  33  LEU LEU B . n 
B 1 43  SER 43  34  34  SER SER B . n 
B 1 44  PHE 44  35  35  PHE PHE B . n 
B 1 45  SER 45  36  36  SER SER B . n 
B 1 46  LEU 46  37  37  LEU LEU B . n 
B 1 47  LEU 47  38  38  LEU LEU B . n 
B 1 48  ASP 48  39  39  ASP ASP B . n 
B 1 49  ILE 49  40  40  ILE ILE B . n 
B 1 50  VAL 50  41  41  VAL VAL B . n 
B 1 51  LYS 51  42  42  LYS LYS B . n 
B 1 52  ALA 52  43  43  ALA ALA B . n 
B 1 53  ASP 53  44  44  ASP ASP B . n 
B 1 54  SER 54  45  45  SER SER B . n 
B 1 55  SER 55  46  46  SER SER B . n 
B 1 56  THR 56  47  47  THR THR B . n 
B 1 57  ASN 57  48  48  ASN ASN B . n 
B 1 58  GLU 58  49  49  GLU GLU B . n 
B 1 59  VAL 59  50  50  VAL VAL B . n 
B 1 60  ASP 60  51  51  ASP ASP B . n 
B 1 61  LEU 61  52  52  LEU LEU B . n 
B 1 62  VAL 62  53  53  VAL VAL B . n 
B 1 63  TYR 63  54  54  TYR TYR B . n 
B 1 64  TRP 64  55  55  TRP TRP B . n 
B 1 65  GLU 65  56  56  GLU GLU B . n 
B 1 66  GLN 66  57  57  GLN GLN B . n 
B 1 67  GLN 67  58  58  GLN GLN B . n 
B 1 68  SER 68  59  59  SER SER B . n 
B 1 69  TRP 69  60  60  TRP TRP B . n 
B 1 70  LYS 70  61  61  LYS LYS B . n 
B 1 71  LEU 71  62  62  LEU LEU B . n 
B 1 72  ASN 72  63  63  ASN ASN B . n 
B 1 73  SER 73  64  64  SER SER B . n 
B 1 74  LEU 74  65  65  LEU LEU B . n 
B 1 75  MET 75  66  66  MET MET B . n 
B 1 76  TRP 76  67  67  TRP TRP B . n 
B 1 77  ASP 77  68  68  ASP ASP B . n 
B 1 78  PRO 78  69  69  PRO PRO B . n 
B 1 79  ASN 79  70  70  ASN ASN B . n 
B 1 80  GLU 80  71  71  GLU GLU B . n 
B 1 81  TYR 81  72  72  TYR TYR B . n 
B 1 82  GLY 82  73  73  GLY GLY B . n 
B 1 83  ASN 83  74  74  ASN ASN B . n 
B 1 84  ILE 84  75  75  ILE ILE B . n 
B 1 85  THR 85  76  76  THR THR B . n 
B 1 86  ASP 86  77  77  ASP ASP B . n 
B 1 87  PHE 87  78  78  PHE PHE B . n 
B 1 88  ARG 88  79  79  ARG ARG B . n 
B 1 89  THR 89  80  80  THR THR B . n 
B 1 90  SER 90  81  81  SER SER B . n 
B 1 91  ALA 91  82  82  ALA ALA B . n 
B 1 92  ALA 92  83  83  ALA ALA B . n 
B 1 93  ASP 93  84  84  ASP ASP B . n 
B 1 94  ILE 94  85  85  ILE ILE B . n 
B 1 95  TRP 95  86  86  TRP TRP B . n 
B 1 96  THR 96  87  87  THR THR B . n 
B 1 97  PRO 97  88  88  PRO PRO B . n 
B 1 98  ASP 98  89  89  ASP ASP B . n 
B 1 99  ILE 99  90  90  ILE ILE B . n 
B 1 100 THR 100 91  91  THR THR B . n 
B 1 101 ALA 101 92  92  ALA ALA B . n 
B 1 102 TYR 102 93  93  TYR TYR B . n 
B 1 103 SER 103 94  94  SER SER B . n 
B 1 104 SER 104 95  95  SER SER B . n 
B 1 105 THR 105 96  96  THR THR B . n 
B 1 106 ARG 106 97  97  ARG ARG B . n 
B 1 107 PRO 107 98  98  PRO PRO B . n 
B 1 108 VAL 108 99  99  VAL VAL B . n 
B 1 109 GLN 109 100 100 GLN GLN B . n 
B 1 110 VAL 110 101 101 VAL VAL B . n 
B 1 111 LEU 111 102 102 LEU LEU B . n 
B 1 112 SER 112 103 103 SER SER B . n 
B 1 113 PRO 113 104 104 PRO PRO B . n 
B 1 114 GLN 114 105 105 GLN GLN B . n 
B 1 115 ASN 115 106 106 ASN ASN B . n 
B 1 116 ALA 116 107 107 ALA ALA B . n 
B 1 117 LEU 117 108 108 LEU LEU B . n 
B 1 118 VAL 118 109 109 VAL VAL B . n 
B 1 119 ASN 119 110 110 ASN ASN B . n 
B 1 120 SER 120 111 111 SER SER B . n 
B 1 121 SER 121 112 112 SER SER B . n 
B 1 122 GLY 122 113 113 GLY GLY B . n 
B 1 123 HIS 123 114 114 HIS HIS B . n 
B 1 124 VAL 124 115 115 VAL VAL B . n 
B 1 125 GLN 125 116 116 GLN GLN B . n 
B 1 126 TYR 126 117 117 TYR TYR B . n 
B 1 127 LEU 127 118 118 LEU LEU B . n 
B 1 128 PRO 128 119 119 PRO PRO B . n 
B 1 129 ALA 129 120 120 ALA ALA B . n 
B 1 130 GLN 130 121 121 GLN GLN B . n 
B 1 131 ARG 131 122 122 ARG ARG B . n 
B 1 132 LEU 132 123 123 LEU LEU B . n 
B 1 133 SER 133 124 124 SER SER B . n 
B 1 134 PHE 134 125 125 PHE PHE B . n 
B 1 135 MET 135 126 126 MET MET B . n 
B 1 136 CYS 136 127 127 CYS CYS B . n 
B 1 137 ASP 137 128 128 ASP ASP B . n 
B 1 138 PRO 138 129 129 PRO PRO B . n 
B 1 139 THR 139 130 130 THR THR B . n 
B 1 140 GLY 140 131 131 GLY GLY B . n 
B 1 141 VAL 141 132 132 VAL VAL B . n 
B 1 142 ASP 142 133 133 ASP ASP B . n 
B 1 143 SER 143 134 134 SER SER B . n 
B 1 144 GLU 144 135 135 GLU GLU B . n 
B 1 145 GLU 145 136 136 GLU GLU B . n 
B 1 146 GLY 146 137 137 GLY GLY B . n 
B 1 147 ALA 147 138 138 ALA ALA B . n 
B 1 148 THR 148 139 139 THR THR B . n 
B 1 149 CYS 149 140 140 CYS CYS B . n 
B 1 150 ALA 150 141 141 ALA ALA B . n 
B 1 151 VAL 151 142 142 VAL VAL B . n 
B 1 152 LYS 152 143 143 LYS LYS B . n 
B 1 153 PHE 153 144 144 PHE PHE B . n 
B 1 154 GLY 154 145 145 GLY GLY B . n 
B 1 155 SER 155 146 146 SER SER B . n 
B 1 156 TRP 156 147 147 TRP TRP B . n 
B 1 157 SER 157 148 148 SER SER B . n 
B 1 158 TYR 158 149 149 TYR TYR B . n 
B 1 159 GLY 159 150 150 GLY GLY B . n 
B 1 160 GLY 160 151 151 GLY GLY B . n 
B 1 161 TRP 161 152 152 TRP TRP B . n 
B 1 162 GLU 162 153 153 GLU GLU B . n 
B 1 163 ILE 163 154 154 ILE ILE B . n 
B 1 164 ASP 164 155 155 ASP ASP B . n 
B 1 165 LEU 165 156 156 LEU LEU B . n 
B 1 166 LYS 166 157 157 LYS LYS B . n 
B 1 167 THR 167 158 158 THR THR B . n 
B 1 168 ASP 168 159 159 ASP ASP B . n 
B 1 169 THR 169 160 160 THR THR B . n 
B 1 170 ASP 170 161 161 ASP ASP B . n 
B 1 171 GLN 171 162 162 GLN GLN B . n 
B 1 172 VAL 172 163 163 VAL VAL B . n 
B 1 173 ASP 173 164 164 ASP ASP B . n 
B 1 174 LEU 174 165 165 LEU LEU B . n 
B 1 175 SER 175 166 166 SER SER B . n 
B 1 176 SER 176 167 167 SER SER B . n 
B 1 177 TYR 177 168 168 TYR TYR B . n 
B 1 178 TYR 178 169 169 TYR TYR B . n 
B 1 179 ALA 179 170 170 ALA ALA B . n 
B 1 180 SER 180 171 171 SER SER B . n 
B 1 181 SER 181 172 172 SER SER B . n 
B 1 182 LYS 182 173 173 LYS LYS B . n 
B 1 183 TYR 183 174 174 TYR TYR B . n 
B 1 184 GLU 184 175 175 GLU GLU B . n 
B 1 185 ILE 185 176 176 ILE ILE B . n 
B 1 186 LEU 186 177 177 LEU LEU B . n 
B 1 187 SER 187 178 178 SER SER B . n 
B 1 188 ALA 188 179 179 ALA ALA B . n 
B 1 189 THR 189 180 180 THR THR B . n 
B 1 190 GLN 190 181 181 GLN GLN B . n 
B 1 191 THR 191 182 182 THR THR B . n 
B 1 192 ARG 192 183 183 ARG ARG B . n 
B 1 193 SER 193 184 184 SER SER B . n 
B 1 194 GLU 194 185 185 GLU GLU B . n 
B 1 195 ARG 195 186 186 ARG ARG B . n 
B 1 196 PHE 196 187 187 PHE PHE B . n 
B 1 197 TYR 197 188 188 TYR TYR B . n 
B 1 198 GLU 198 189 189 GLU GLU B . n 
B 1 199 CYS 199 190 190 CYS CYS B . n 
B 1 200 CYS 200 191 191 CYS CYS B . n 
B 1 201 LYS 201 192 192 LYS LYS B . n 
B 1 202 GLU 202 193 193 GLU GLU B . n 
B 1 203 PRO 203 194 194 PRO PRO B . n 
B 1 204 TYR 204 195 195 TYR TYR B . n 
B 1 205 PRO 205 196 196 PRO PRO B . n 
B 1 206 ASP 206 197 197 ASP ASP B . n 
B 1 207 VAL 207 198 198 VAL VAL B . n 
B 1 208 ASN 208 199 199 ASN ASN B . n 
B 1 209 LEU 209 200 200 LEU LEU B . n 
B 1 210 VAL 210 201 201 VAL VAL B . n 
B 1 211 VAL 211 202 202 VAL VAL B . n 
B 1 212 LYS 212 203 203 LYS LYS B . n 
B 1 213 PHE 213 204 204 PHE PHE B . n 
B 1 214 ARG 214 205 205 ARG ARG B . n 
B 1 215 GLU 215 206 206 GLU GLU B . n 
B 1 216 ARG 216 207 207 ARG ARG B . n 
B 1 217 ARG 217 208 208 ARG ARG B . n 
B 1 218 ALA 218 209 ?   ?   ?   B . n 
B 1 219 GLY 219 210 ?   ?   ?   B . n 
B 1 220 ASN 220 211 ?   ?   ?   B . n 
B 1 221 GLY 221 212 ?   ?   ?   B . n 
B 1 222 PHE 222 213 ?   ?   ?   B . n 
B 1 223 PHE 223 214 ?   ?   ?   B . n 
B 1 224 ARG 224 215 ?   ?   ?   B . n 
B 1 225 ASN 225 216 ?   ?   ?   B . n 
B 1 226 LEU 226 217 ?   ?   ?   B . n 
B 1 227 PHE 227 218 ?   ?   ?   B . n 
B 1 228 ASP 228 219 ?   ?   ?   B . n 
B 1 229 SER 229 220 ?   ?   ?   B . n 
B 1 230 ARG 230 221 ?   ?   ?   B . n 
C 1 1   ASP 1   -8  ?   ?   ?   C . n 
C 1 2   TYR 2   -7  ?   ?   ?   C . n 
C 1 3   LYS 3   -6  -6  LYS LYS C . n 
C 1 4   ASP 4   -5  -5  ASP ASP C . n 
C 1 5   ASP 5   -4  -4  ASP ASP C . n 
C 1 6   ASP 6   -3  -3  ASP ASP C . n 
C 1 7   ASP 7   -2  -2  ASP ASP C . n 
C 1 8   LYS 8   -1  -1  LYS LYS C . n 
C 1 9   LEU 9   0   0   LEU LEU C . n 
C 1 10  HIS 10  1   1   HIS HIS C . n 
C 1 11  SER 11  2   2   SER SER C . n 
C 1 12  GLN 12  3   3   GLN GLN C . n 
C 1 13  ALA 13  4   4   ALA ALA C . n 
C 1 14  ASN 14  5   5   ASN ASN C . n 
C 1 15  LEU 15  6   6   LEU LEU C . n 
C 1 16  MET 16  7   7   MET MET C . n 
C 1 17  ARG 17  8   8   ARG ARG C . n 
C 1 18  LEU 18  9   9   LEU LEU C . n 
C 1 19  LYS 19  10  10  LYS LYS C . n 
C 1 20  SER 20  11  11  SER SER C . n 
C 1 21  ASP 21  12  12  ASP ASP C . n 
C 1 22  LEU 22  13  13  LEU LEU C . n 
C 1 23  PHE 23  14  14  PHE PHE C . n 
C 1 24  ASN 24  15  15  ASN ASN C . n 
C 1 25  ARG 25  16  16  ARG ARG C . n 
C 1 26  SER 26  17  17  SER SER C . n 
C 1 27  PRO 27  18  18  PRO PRO C . n 
C 1 28  MET 28  19  19  MET MET C . n 
C 1 29  TYR 29  20  20  TYR TYR C . n 
C 1 30  PRO 30  21  21  PRO PRO C . n 
C 1 31  GLY 31  22  22  GLY GLY C . n 
C 1 32  PRO 32  23  23  PRO PRO C . n 
C 1 33  THR 33  24  24  THR THR C . n 
C 1 34  LYS 34  25  25  LYS LYS C . n 
C 1 35  ASP 35  26  26  ASP ASP C . n 
C 1 36  ASP 36  27  27  ASP ASP C . n 
C 1 37  PRO 37  28  28  PRO PRO C . n 
C 1 38  LEU 38  29  29  LEU LEU C . n 
C 1 39  THR 39  30  30  THR THR C . n 
C 1 40  VAL 40  31  31  VAL VAL C . n 
C 1 41  TYR 41  32  32  TYR TYR C . n 
C 1 42  LEU 42  33  33  LEU LEU C . n 
C 1 43  SER 43  34  34  SER SER C . n 
C 1 44  PHE 44  35  35  PHE PHE C . n 
C 1 45  SER 45  36  36  SER SER C . n 
C 1 46  LEU 46  37  37  LEU LEU C . n 
C 1 47  LEU 47  38  38  LEU LEU C . n 
C 1 48  ASP 48  39  39  ASP ASP C . n 
C 1 49  ILE 49  40  40  ILE ILE C . n 
C 1 50  VAL 50  41  41  VAL VAL C . n 
C 1 51  LYS 51  42  42  LYS LYS C . n 
C 1 52  ALA 52  43  43  ALA ALA C . n 
C 1 53  ASP 53  44  44  ASP ASP C . n 
C 1 54  SER 54  45  45  SER SER C . n 
C 1 55  SER 55  46  46  SER SER C . n 
C 1 56  THR 56  47  47  THR THR C . n 
C 1 57  ASN 57  48  48  ASN ASN C . n 
C 1 58  GLU 58  49  49  GLU GLU C . n 
C 1 59  VAL 59  50  50  VAL VAL C . n 
C 1 60  ASP 60  51  51  ASP ASP C . n 
C 1 61  LEU 61  52  52  LEU LEU C . n 
C 1 62  VAL 62  53  53  VAL VAL C . n 
C 1 63  TYR 63  54  54  TYR TYR C . n 
C 1 64  TRP 64  55  55  TRP TRP C . n 
C 1 65  GLU 65  56  56  GLU GLU C . n 
C 1 66  GLN 66  57  57  GLN GLN C . n 
C 1 67  GLN 67  58  58  GLN GLN C . n 
C 1 68  SER 68  59  59  SER SER C . n 
C 1 69  TRP 69  60  60  TRP TRP C . n 
C 1 70  LYS 70  61  61  LYS LYS C . n 
C 1 71  LEU 71  62  62  LEU LEU C . n 
C 1 72  ASN 72  63  63  ASN ASN C . n 
C 1 73  SER 73  64  64  SER SER C . n 
C 1 74  LEU 74  65  65  LEU LEU C . n 
C 1 75  MET 75  66  66  MET MET C . n 
C 1 76  TRP 76  67  67  TRP TRP C . n 
C 1 77  ASP 77  68  68  ASP ASP C . n 
C 1 78  PRO 78  69  69  PRO PRO C . n 
C 1 79  ASN 79  70  70  ASN ASN C . n 
C 1 80  GLU 80  71  71  GLU GLU C . n 
C 1 81  TYR 81  72  72  TYR TYR C . n 
C 1 82  GLY 82  73  73  GLY GLY C . n 
C 1 83  ASN 83  74  74  ASN ASN C . n 
C 1 84  ILE 84  75  75  ILE ILE C . n 
C 1 85  THR 85  76  76  THR THR C . n 
C 1 86  ASP 86  77  77  ASP ASP C . n 
C 1 87  PHE 87  78  78  PHE PHE C . n 
C 1 88  ARG 88  79  79  ARG ARG C . n 
C 1 89  THR 89  80  80  THR THR C . n 
C 1 90  SER 90  81  81  SER SER C . n 
C 1 91  ALA 91  82  82  ALA ALA C . n 
C 1 92  ALA 92  83  83  ALA ALA C . n 
C 1 93  ASP 93  84  84  ASP ASP C . n 
C 1 94  ILE 94  85  85  ILE ILE C . n 
C 1 95  TRP 95  86  86  TRP TRP C . n 
C 1 96  THR 96  87  87  THR THR C . n 
C 1 97  PRO 97  88  88  PRO PRO C . n 
C 1 98  ASP 98  89  89  ASP ASP C . n 
C 1 99  ILE 99  90  90  ILE ILE C . n 
C 1 100 THR 100 91  91  THR THR C . n 
C 1 101 ALA 101 92  92  ALA ALA C . n 
C 1 102 TYR 102 93  93  TYR TYR C . n 
C 1 103 SER 103 94  94  SER SER C . n 
C 1 104 SER 104 95  95  SER SER C . n 
C 1 105 THR 105 96  96  THR THR C . n 
C 1 106 ARG 106 97  97  ARG ARG C . n 
C 1 107 PRO 107 98  98  PRO PRO C . n 
C 1 108 VAL 108 99  99  VAL VAL C . n 
C 1 109 GLN 109 100 100 GLN GLN C . n 
C 1 110 VAL 110 101 101 VAL VAL C . n 
C 1 111 LEU 111 102 102 LEU LEU C . n 
C 1 112 SER 112 103 103 SER SER C . n 
C 1 113 PRO 113 104 104 PRO PRO C . n 
C 1 114 GLN 114 105 105 GLN GLN C . n 
C 1 115 ASN 115 106 106 ASN ASN C . n 
C 1 116 ALA 116 107 107 ALA ALA C . n 
C 1 117 LEU 117 108 108 LEU LEU C . n 
C 1 118 VAL 118 109 109 VAL VAL C . n 
C 1 119 ASN 119 110 110 ASN ASN C . n 
C 1 120 SER 120 111 111 SER SER C . n 
C 1 121 SER 121 112 112 SER SER C . n 
C 1 122 GLY 122 113 113 GLY GLY C . n 
C 1 123 HIS 123 114 114 HIS HIS C . n 
C 1 124 VAL 124 115 115 VAL VAL C . n 
C 1 125 GLN 125 116 116 GLN GLN C . n 
C 1 126 TYR 126 117 117 TYR TYR C . n 
C 1 127 LEU 127 118 118 LEU LEU C . n 
C 1 128 PRO 128 119 119 PRO PRO C . n 
C 1 129 ALA 129 120 120 ALA ALA C . n 
C 1 130 GLN 130 121 121 GLN GLN C . n 
C 1 131 ARG 131 122 122 ARG ARG C . n 
C 1 132 LEU 132 123 123 LEU LEU C . n 
C 1 133 SER 133 124 124 SER SER C . n 
C 1 134 PHE 134 125 125 PHE PHE C . n 
C 1 135 MET 135 126 126 MET MET C . n 
C 1 136 CYS 136 127 127 CYS CYS C . n 
C 1 137 ASP 137 128 128 ASP ASP C . n 
C 1 138 PRO 138 129 129 PRO PRO C . n 
C 1 139 THR 139 130 130 THR THR C . n 
C 1 140 GLY 140 131 131 GLY GLY C . n 
C 1 141 VAL 141 132 132 VAL VAL C . n 
C 1 142 ASP 142 133 133 ASP ASP C . n 
C 1 143 SER 143 134 134 SER SER C . n 
C 1 144 GLU 144 135 135 GLU GLU C . n 
C 1 145 GLU 145 136 136 GLU GLU C . n 
C 1 146 GLY 146 137 137 GLY GLY C . n 
C 1 147 ALA 147 138 138 ALA ALA C . n 
C 1 148 THR 148 139 139 THR THR C . n 
C 1 149 CYS 149 140 140 CYS CYS C . n 
C 1 150 ALA 150 141 141 ALA ALA C . n 
C 1 151 VAL 151 142 142 VAL VAL C . n 
C 1 152 LYS 152 143 143 LYS LYS C . n 
C 1 153 PHE 153 144 144 PHE PHE C . n 
C 1 154 GLY 154 145 145 GLY GLY C . n 
C 1 155 SER 155 146 146 SER SER C . n 
C 1 156 TRP 156 147 147 TRP TRP C . n 
C 1 157 SER 157 148 148 SER SER C . n 
C 1 158 TYR 158 149 149 TYR TYR C . n 
C 1 159 GLY 159 150 150 GLY GLY C . n 
C 1 160 GLY 160 151 151 GLY GLY C . n 
C 1 161 TRP 161 152 152 TRP TRP C . n 
C 1 162 GLU 162 153 153 GLU GLU C . n 
C 1 163 ILE 163 154 154 ILE ILE C . n 
C 1 164 ASP 164 155 155 ASP ASP C . n 
C 1 165 LEU 165 156 156 LEU LEU C . n 
C 1 166 LYS 166 157 157 LYS LYS C . n 
C 1 167 THR 167 158 158 THR THR C . n 
C 1 168 ASP 168 159 159 ASP ASP C . n 
C 1 169 THR 169 160 160 THR THR C . n 
C 1 170 ASP 170 161 161 ASP ASP C . n 
C 1 171 GLN 171 162 162 GLN GLN C . n 
C 1 172 VAL 172 163 163 VAL VAL C . n 
C 1 173 ASP 173 164 164 ASP ASP C . n 
C 1 174 LEU 174 165 165 LEU LEU C . n 
C 1 175 SER 175 166 166 SER SER C . n 
C 1 176 SER 176 167 167 SER SER C . n 
C 1 177 TYR 177 168 168 TYR TYR C . n 
C 1 178 TYR 178 169 169 TYR TYR C . n 
C 1 179 ALA 179 170 170 ALA ALA C . n 
C 1 180 SER 180 171 171 SER SER C . n 
C 1 181 SER 181 172 172 SER SER C . n 
C 1 182 LYS 182 173 173 LYS LYS C . n 
C 1 183 TYR 183 174 174 TYR TYR C . n 
C 1 184 GLU 184 175 175 GLU GLU C . n 
C 1 185 ILE 185 176 176 ILE ILE C . n 
C 1 186 LEU 186 177 177 LEU LEU C . n 
C 1 187 SER 187 178 178 SER SER C . n 
C 1 188 ALA 188 179 179 ALA ALA C . n 
C 1 189 THR 189 180 180 THR THR C . n 
C 1 190 GLN 190 181 181 GLN GLN C . n 
C 1 191 THR 191 182 182 THR THR C . n 
C 1 192 ARG 192 183 183 ARG ARG C . n 
C 1 193 SER 193 184 184 SER SER C . n 
C 1 194 GLU 194 185 185 GLU GLU C . n 
C 1 195 ARG 195 186 186 ARG ARG C . n 
C 1 196 PHE 196 187 187 PHE PHE C . n 
C 1 197 TYR 197 188 188 TYR TYR C . n 
C 1 198 GLU 198 189 189 GLU GLU C . n 
C 1 199 CYS 199 190 190 CYS CYS C . n 
C 1 200 CYS 200 191 191 CYS CYS C . n 
C 1 201 LYS 201 192 192 LYS LYS C . n 
C 1 202 GLU 202 193 193 GLU GLU C . n 
C 1 203 PRO 203 194 194 PRO PRO C . n 
C 1 204 TYR 204 195 195 TYR TYR C . n 
C 1 205 PRO 205 196 196 PRO PRO C . n 
C 1 206 ASP 206 197 197 ASP ASP C . n 
C 1 207 VAL 207 198 198 VAL VAL C . n 
C 1 208 ASN 208 199 199 ASN ASN C . n 
C 1 209 LEU 209 200 200 LEU LEU C . n 
C 1 210 VAL 210 201 201 VAL VAL C . n 
C 1 211 VAL 211 202 202 VAL VAL C . n 
C 1 212 LYS 212 203 203 LYS LYS C . n 
C 1 213 PHE 213 204 204 PHE PHE C . n 
C 1 214 ARG 214 205 205 ARG ARG C . n 
C 1 215 GLU 215 206 206 GLU GLU C . n 
C 1 216 ARG 216 207 207 ARG ARG C . n 
C 1 217 ARG 217 208 208 ARG ARG C . n 
C 1 218 ALA 218 209 209 ALA ALA C . n 
C 1 219 GLY 219 210 ?   ?   ?   C . n 
C 1 220 ASN 220 211 ?   ?   ?   C . n 
C 1 221 GLY 221 212 ?   ?   ?   C . n 
C 1 222 PHE 222 213 ?   ?   ?   C . n 
C 1 223 PHE 223 214 ?   ?   ?   C . n 
C 1 224 ARG 224 215 ?   ?   ?   C . n 
C 1 225 ASN 225 216 ?   ?   ?   C . n 
C 1 226 LEU 226 217 ?   ?   ?   C . n 
C 1 227 PHE 227 218 ?   ?   ?   C . n 
C 1 228 ASP 228 219 ?   ?   ?   C . n 
C 1 229 SER 229 220 ?   ?   ?   C . n 
C 1 230 ARG 230 221 ?   ?   ?   C . n 
D 1 1   ASP 1   -8  ?   ?   ?   D . n 
D 1 2   TYR 2   -7  ?   ?   ?   D . n 
D 1 3   LYS 3   -6  -6  LYS LYS D . n 
D 1 4   ASP 4   -5  -5  ASP ASP D . n 
D 1 5   ASP 5   -4  -4  ASP ASP D . n 
D 1 6   ASP 6   -3  -3  ASP ASP D . n 
D 1 7   ASP 7   -2  -2  ASP ASP D . n 
D 1 8   LYS 8   -1  -1  LYS LYS D . n 
D 1 9   LEU 9   0   0   LEU LEU D . n 
D 1 10  HIS 10  1   1   HIS HIS D . n 
D 1 11  SER 11  2   2   SER SER D . n 
D 1 12  GLN 12  3   3   GLN GLN D . n 
D 1 13  ALA 13  4   4   ALA ALA D . n 
D 1 14  ASN 14  5   5   ASN ASN D . n 
D 1 15  LEU 15  6   6   LEU LEU D . n 
D 1 16  MET 16  7   7   MET MET D . n 
D 1 17  ARG 17  8   8   ARG ARG D . n 
D 1 18  LEU 18  9   9   LEU LEU D . n 
D 1 19  LYS 19  10  10  LYS LYS D . n 
D 1 20  SER 20  11  11  SER SER D . n 
D 1 21  ASP 21  12  12  ASP ASP D . n 
D 1 22  LEU 22  13  13  LEU LEU D . n 
D 1 23  PHE 23  14  14  PHE PHE D . n 
D 1 24  ASN 24  15  15  ASN ASN D . n 
D 1 25  ARG 25  16  16  ARG ARG D . n 
D 1 26  SER 26  17  17  SER SER D . n 
D 1 27  PRO 27  18  18  PRO PRO D . n 
D 1 28  MET 28  19  19  MET MET D . n 
D 1 29  TYR 29  20  20  TYR TYR D . n 
D 1 30  PRO 30  21  21  PRO PRO D . n 
D 1 31  GLY 31  22  22  GLY GLY D . n 
D 1 32  PRO 32  23  23  PRO PRO D . n 
D 1 33  THR 33  24  24  THR THR D . n 
D 1 34  LYS 34  25  25  LYS LYS D . n 
D 1 35  ASP 35  26  26  ASP ASP D . n 
D 1 36  ASP 36  27  27  ASP ASP D . n 
D 1 37  PRO 37  28  28  PRO PRO D . n 
D 1 38  LEU 38  29  29  LEU LEU D . n 
D 1 39  THR 39  30  30  THR THR D . n 
D 1 40  VAL 40  31  31  VAL VAL D . n 
D 1 41  TYR 41  32  32  TYR TYR D . n 
D 1 42  LEU 42  33  33  LEU LEU D . n 
D 1 43  SER 43  34  34  SER SER D . n 
D 1 44  PHE 44  35  35  PHE PHE D . n 
D 1 45  SER 45  36  36  SER SER D . n 
D 1 46  LEU 46  37  37  LEU LEU D . n 
D 1 47  LEU 47  38  38  LEU LEU D . n 
D 1 48  ASP 48  39  39  ASP ASP D . n 
D 1 49  ILE 49  40  40  ILE ILE D . n 
D 1 50  VAL 50  41  41  VAL VAL D . n 
D 1 51  LYS 51  42  42  LYS LYS D . n 
D 1 52  ALA 52  43  43  ALA ALA D . n 
D 1 53  ASP 53  44  44  ASP ASP D . n 
D 1 54  SER 54  45  45  SER SER D . n 
D 1 55  SER 55  46  46  SER SER D . n 
D 1 56  THR 56  47  47  THR THR D . n 
D 1 57  ASN 57  48  48  ASN ASN D . n 
D 1 58  GLU 58  49  49  GLU GLU D . n 
D 1 59  VAL 59  50  50  VAL VAL D . n 
D 1 60  ASP 60  51  51  ASP ASP D . n 
D 1 61  LEU 61  52  52  LEU LEU D . n 
D 1 62  VAL 62  53  53  VAL VAL D . n 
D 1 63  TYR 63  54  54  TYR TYR D . n 
D 1 64  TRP 64  55  55  TRP TRP D . n 
D 1 65  GLU 65  56  56  GLU GLU D . n 
D 1 66  GLN 66  57  57  GLN GLN D . n 
D 1 67  GLN 67  58  58  GLN GLN D . n 
D 1 68  SER 68  59  59  SER SER D . n 
D 1 69  TRP 69  60  60  TRP TRP D . n 
D 1 70  LYS 70  61  61  LYS LYS D . n 
D 1 71  LEU 71  62  62  LEU LEU D . n 
D 1 72  ASN 72  63  63  ASN ASN D . n 
D 1 73  SER 73  64  64  SER SER D . n 
D 1 74  LEU 74  65  65  LEU LEU D . n 
D 1 75  MET 75  66  66  MET MET D . n 
D 1 76  TRP 76  67  67  TRP TRP D . n 
D 1 77  ASP 77  68  68  ASP ASP D . n 
D 1 78  PRO 78  69  69  PRO PRO D . n 
D 1 79  ASN 79  70  70  ASN ASN D . n 
D 1 80  GLU 80  71  71  GLU GLU D . n 
D 1 81  TYR 81  72  72  TYR TYR D . n 
D 1 82  GLY 82  73  73  GLY GLY D . n 
D 1 83  ASN 83  74  74  ASN ASN D . n 
D 1 84  ILE 84  75  75  ILE ILE D . n 
D 1 85  THR 85  76  76  THR THR D . n 
D 1 86  ASP 86  77  77  ASP ASP D . n 
D 1 87  PHE 87  78  78  PHE PHE D . n 
D 1 88  ARG 88  79  79  ARG ARG D . n 
D 1 89  THR 89  80  80  THR THR D . n 
D 1 90  SER 90  81  81  SER SER D . n 
D 1 91  ALA 91  82  82  ALA ALA D . n 
D 1 92  ALA 92  83  83  ALA ALA D . n 
D 1 93  ASP 93  84  84  ASP ASP D . n 
D 1 94  ILE 94  85  85  ILE ILE D . n 
D 1 95  TRP 95  86  86  TRP TRP D . n 
D 1 96  THR 96  87  87  THR THR D . n 
D 1 97  PRO 97  88  88  PRO PRO D . n 
D 1 98  ASP 98  89  89  ASP ASP D . n 
D 1 99  ILE 99  90  90  ILE ILE D . n 
D 1 100 THR 100 91  91  THR THR D . n 
D 1 101 ALA 101 92  92  ALA ALA D . n 
D 1 102 TYR 102 93  93  TYR TYR D . n 
D 1 103 SER 103 94  94  SER SER D . n 
D 1 104 SER 104 95  95  SER SER D . n 
D 1 105 THR 105 96  96  THR THR D . n 
D 1 106 ARG 106 97  97  ARG ARG D . n 
D 1 107 PRO 107 98  98  PRO PRO D . n 
D 1 108 VAL 108 99  99  VAL VAL D . n 
D 1 109 GLN 109 100 100 GLN GLN D . n 
D 1 110 VAL 110 101 101 VAL VAL D . n 
D 1 111 LEU 111 102 102 LEU LEU D . n 
D 1 112 SER 112 103 103 SER SER D . n 
D 1 113 PRO 113 104 104 PRO PRO D . n 
D 1 114 GLN 114 105 105 GLN GLN D . n 
D 1 115 ASN 115 106 106 ASN ASN D . n 
D 1 116 ALA 116 107 107 ALA ALA D . n 
D 1 117 LEU 117 108 108 LEU LEU D . n 
D 1 118 VAL 118 109 109 VAL VAL D . n 
D 1 119 ASN 119 110 110 ASN ASN D . n 
D 1 120 SER 120 111 111 SER SER D . n 
D 1 121 SER 121 112 112 SER SER D . n 
D 1 122 GLY 122 113 113 GLY GLY D . n 
D 1 123 HIS 123 114 114 HIS HIS D . n 
D 1 124 VAL 124 115 115 VAL VAL D . n 
D 1 125 GLN 125 116 116 GLN GLN D . n 
D 1 126 TYR 126 117 117 TYR TYR D . n 
D 1 127 LEU 127 118 118 LEU LEU D . n 
D 1 128 PRO 128 119 119 PRO PRO D . n 
D 1 129 ALA 129 120 120 ALA ALA D . n 
D 1 130 GLN 130 121 121 GLN GLN D . n 
D 1 131 ARG 131 122 122 ARG ARG D . n 
D 1 132 LEU 132 123 123 LEU LEU D . n 
D 1 133 SER 133 124 124 SER SER D . n 
D 1 134 PHE 134 125 125 PHE PHE D . n 
D 1 135 MET 135 126 126 MET MET D . n 
D 1 136 CYS 136 127 127 CYS CYS D . n 
D 1 137 ASP 137 128 128 ASP ASP D . n 
D 1 138 PRO 138 129 129 PRO PRO D . n 
D 1 139 THR 139 130 130 THR THR D . n 
D 1 140 GLY 140 131 131 GLY GLY D . n 
D 1 141 VAL 141 132 132 VAL VAL D . n 
D 1 142 ASP 142 133 133 ASP ASP D . n 
D 1 143 SER 143 134 134 SER SER D . n 
D 1 144 GLU 144 135 135 GLU GLU D . n 
D 1 145 GLU 145 136 136 GLU GLU D . n 
D 1 146 GLY 146 137 137 GLY GLY D . n 
D 1 147 ALA 147 138 138 ALA ALA D . n 
D 1 148 THR 148 139 139 THR THR D . n 
D 1 149 CYS 149 140 140 CYS CYS D . n 
D 1 150 ALA 150 141 141 ALA ALA D . n 
D 1 151 VAL 151 142 142 VAL VAL D . n 
D 1 152 LYS 152 143 143 LYS LYS D . n 
D 1 153 PHE 153 144 144 PHE PHE D . n 
D 1 154 GLY 154 145 145 GLY GLY D . n 
D 1 155 SER 155 146 146 SER SER D . n 
D 1 156 TRP 156 147 147 TRP TRP D . n 
D 1 157 SER 157 148 148 SER SER D . n 
D 1 158 TYR 158 149 149 TYR TYR D . n 
D 1 159 GLY 159 150 150 GLY GLY D . n 
D 1 160 GLY 160 151 151 GLY GLY D . n 
D 1 161 TRP 161 152 152 TRP TRP D . n 
D 1 162 GLU 162 153 153 GLU GLU D . n 
D 1 163 ILE 163 154 154 ILE ILE D . n 
D 1 164 ASP 164 155 155 ASP ASP D . n 
D 1 165 LEU 165 156 156 LEU LEU D . n 
D 1 166 LYS 166 157 157 LYS LYS D . n 
D 1 167 THR 167 158 158 THR THR D . n 
D 1 168 ASP 168 159 159 ASP ASP D . n 
D 1 169 THR 169 160 160 THR THR D . n 
D 1 170 ASP 170 161 161 ASP ASP D . n 
D 1 171 GLN 171 162 162 GLN GLN D . n 
D 1 172 VAL 172 163 163 VAL VAL D . n 
D 1 173 ASP 173 164 164 ASP ASP D . n 
D 1 174 LEU 174 165 165 LEU LEU D . n 
D 1 175 SER 175 166 166 SER SER D . n 
D 1 176 SER 176 167 167 SER SER D . n 
D 1 177 TYR 177 168 168 TYR TYR D . n 
D 1 178 TYR 178 169 169 TYR TYR D . n 
D 1 179 ALA 179 170 170 ALA ALA D . n 
D 1 180 SER 180 171 171 SER SER D . n 
D 1 181 SER 181 172 172 SER SER D . n 
D 1 182 LYS 182 173 173 LYS LYS D . n 
D 1 183 TYR 183 174 174 TYR TYR D . n 
D 1 184 GLU 184 175 175 GLU GLU D . n 
D 1 185 ILE 185 176 176 ILE ILE D . n 
D 1 186 LEU 186 177 177 LEU LEU D . n 
D 1 187 SER 187 178 178 SER SER D . n 
D 1 188 ALA 188 179 179 ALA ALA D . n 
D 1 189 THR 189 180 180 THR THR D . n 
D 1 190 GLN 190 181 181 GLN GLN D . n 
D 1 191 THR 191 182 182 THR THR D . n 
D 1 192 ARG 192 183 183 ARG ARG D . n 
D 1 193 SER 193 184 184 SER SER D . n 
D 1 194 GLU 194 185 185 GLU GLU D . n 
D 1 195 ARG 195 186 186 ARG ARG D . n 
D 1 196 PHE 196 187 187 PHE PHE D . n 
D 1 197 TYR 197 188 188 TYR TYR D . n 
D 1 198 GLU 198 189 189 GLU GLU D . n 
D 1 199 CYS 199 190 190 CYS CYS D . n 
D 1 200 CYS 200 191 191 CYS CYS D . n 
D 1 201 LYS 201 192 192 LYS LYS D . n 
D 1 202 GLU 202 193 193 GLU GLU D . n 
D 1 203 PRO 203 194 194 PRO PRO D . n 
D 1 204 TYR 204 195 195 TYR TYR D . n 
D 1 205 PRO 205 196 196 PRO PRO D . n 
D 1 206 ASP 206 197 197 ASP ASP D . n 
D 1 207 VAL 207 198 198 VAL VAL D . n 
D 1 208 ASN 208 199 199 ASN ASN D . n 
D 1 209 LEU 209 200 200 LEU LEU D . n 
D 1 210 VAL 210 201 201 VAL VAL D . n 
D 1 211 VAL 211 202 202 VAL VAL D . n 
D 1 212 LYS 212 203 203 LYS LYS D . n 
D 1 213 PHE 213 204 204 PHE PHE D . n 
D 1 214 ARG 214 205 205 ARG ARG D . n 
D 1 215 GLU 215 206 206 GLU GLU D . n 
D 1 216 ARG 216 207 207 ARG ARG D . n 
D 1 217 ARG 217 208 ?   ?   ?   D . n 
D 1 218 ALA 218 209 ?   ?   ?   D . n 
D 1 219 GLY 219 210 ?   ?   ?   D . n 
D 1 220 ASN 220 211 ?   ?   ?   D . n 
D 1 221 GLY 221 212 ?   ?   ?   D . n 
D 1 222 PHE 222 213 ?   ?   ?   D . n 
D 1 223 PHE 223 214 ?   ?   ?   D . n 
D 1 224 ARG 224 215 ?   ?   ?   D . n 
D 1 225 ASN 225 216 ?   ?   ?   D . n 
D 1 226 LEU 226 217 ?   ?   ?   D . n 
D 1 227 PHE 227 218 ?   ?   ?   D . n 
D 1 228 ASP 228 219 ?   ?   ?   D . n 
D 1 229 SER 229 220 ?   ?   ?   D . n 
D 1 230 ARG 230 221 ?   ?   ?   D . n 
E 1 1   ASP 1   -8  ?   ?   ?   E . n 
E 1 2   TYR 2   -7  ?   ?   ?   E . n 
E 1 3   LYS 3   -6  -6  LYS LYS E . n 
E 1 4   ASP 4   -5  -5  ASP ASP E . n 
E 1 5   ASP 5   -4  -4  ASP ASP E . n 
E 1 6   ASP 6   -3  -3  ASP ASP E . n 
E 1 7   ASP 7   -2  -2  ASP ASP E . n 
E 1 8   LYS 8   -1  -1  LYS LYS E . n 
E 1 9   LEU 9   0   0   LEU LEU E . n 
E 1 10  HIS 10  1   1   HIS HIS E . n 
E 1 11  SER 11  2   2   SER SER E . n 
E 1 12  GLN 12  3   3   GLN GLN E . n 
E 1 13  ALA 13  4   4   ALA ALA E . n 
E 1 14  ASN 14  5   5   ASN ASN E . n 
E 1 15  LEU 15  6   6   LEU LEU E . n 
E 1 16  MET 16  7   7   MET MET E . n 
E 1 17  ARG 17  8   8   ARG ARG E . n 
E 1 18  LEU 18  9   9   LEU LEU E . n 
E 1 19  LYS 19  10  10  LYS LYS E . n 
E 1 20  SER 20  11  11  SER SER E . n 
E 1 21  ASP 21  12  12  ASP ASP E . n 
E 1 22  LEU 22  13  13  LEU LEU E . n 
E 1 23  PHE 23  14  14  PHE PHE E . n 
E 1 24  ASN 24  15  15  ASN ASN E . n 
E 1 25  ARG 25  16  16  ARG ARG E . n 
E 1 26  SER 26  17  17  SER SER E . n 
E 1 27  PRO 27  18  18  PRO PRO E . n 
E 1 28  MET 28  19  19  MET MET E . n 
E 1 29  TYR 29  20  20  TYR TYR E . n 
E 1 30  PRO 30  21  21  PRO PRO E . n 
E 1 31  GLY 31  22  22  GLY GLY E . n 
E 1 32  PRO 32  23  23  PRO PRO E . n 
E 1 33  THR 33  24  24  THR THR E . n 
E 1 34  LYS 34  25  25  LYS LYS E . n 
E 1 35  ASP 35  26  26  ASP ASP E . n 
E 1 36  ASP 36  27  27  ASP ASP E . n 
E 1 37  PRO 37  28  28  PRO PRO E . n 
E 1 38  LEU 38  29  29  LEU LEU E . n 
E 1 39  THR 39  30  30  THR THR E . n 
E 1 40  VAL 40  31  31  VAL VAL E . n 
E 1 41  TYR 41  32  32  TYR TYR E . n 
E 1 42  LEU 42  33  33  LEU LEU E . n 
E 1 43  SER 43  34  34  SER SER E . n 
E 1 44  PHE 44  35  35  PHE PHE E . n 
E 1 45  SER 45  36  36  SER SER E . n 
E 1 46  LEU 46  37  37  LEU LEU E . n 
E 1 47  LEU 47  38  38  LEU LEU E . n 
E 1 48  ASP 48  39  39  ASP ASP E . n 
E 1 49  ILE 49  40  40  ILE ILE E . n 
E 1 50  VAL 50  41  41  VAL VAL E . n 
E 1 51  LYS 51  42  42  LYS LYS E . n 
E 1 52  ALA 52  43  43  ALA ALA E . n 
E 1 53  ASP 53  44  44  ASP ASP E . n 
E 1 54  SER 54  45  45  SER SER E . n 
E 1 55  SER 55  46  46  SER SER E . n 
E 1 56  THR 56  47  47  THR THR E . n 
E 1 57  ASN 57  48  48  ASN ASN E . n 
E 1 58  GLU 58  49  49  GLU GLU E . n 
E 1 59  VAL 59  50  50  VAL VAL E . n 
E 1 60  ASP 60  51  51  ASP ASP E . n 
E 1 61  LEU 61  52  52  LEU LEU E . n 
E 1 62  VAL 62  53  53  VAL VAL E . n 
E 1 63  TYR 63  54  54  TYR TYR E . n 
E 1 64  TRP 64  55  55  TRP TRP E . n 
E 1 65  GLU 65  56  56  GLU GLU E . n 
E 1 66  GLN 66  57  57  GLN GLN E . n 
E 1 67  GLN 67  58  58  GLN GLN E . n 
E 1 68  SER 68  59  59  SER SER E . n 
E 1 69  TRP 69  60  60  TRP TRP E . n 
E 1 70  LYS 70  61  61  LYS LYS E . n 
E 1 71  LEU 71  62  62  LEU LEU E . n 
E 1 72  ASN 72  63  63  ASN ASN E . n 
E 1 73  SER 73  64  64  SER SER E . n 
E 1 74  LEU 74  65  65  LEU LEU E . n 
E 1 75  MET 75  66  66  MET MET E . n 
E 1 76  TRP 76  67  67  TRP TRP E . n 
E 1 77  ASP 77  68  68  ASP ASP E . n 
E 1 78  PRO 78  69  69  PRO PRO E . n 
E 1 79  ASN 79  70  70  ASN ASN E . n 
E 1 80  GLU 80  71  71  GLU GLU E . n 
E 1 81  TYR 81  72  72  TYR TYR E . n 
E 1 82  GLY 82  73  73  GLY GLY E . n 
E 1 83  ASN 83  74  74  ASN ASN E . n 
E 1 84  ILE 84  75  75  ILE ILE E . n 
E 1 85  THR 85  76  76  THR THR E . n 
E 1 86  ASP 86  77  77  ASP ASP E . n 
E 1 87  PHE 87  78  78  PHE PHE E . n 
E 1 88  ARG 88  79  79  ARG ARG E . n 
E 1 89  THR 89  80  80  THR THR E . n 
E 1 90  SER 90  81  81  SER SER E . n 
E 1 91  ALA 91  82  82  ALA ALA E . n 
E 1 92  ALA 92  83  83  ALA ALA E . n 
E 1 93  ASP 93  84  84  ASP ASP E . n 
E 1 94  ILE 94  85  85  ILE ILE E . n 
E 1 95  TRP 95  86  86  TRP TRP E . n 
E 1 96  THR 96  87  87  THR THR E . n 
E 1 97  PRO 97  88  88  PRO PRO E . n 
E 1 98  ASP 98  89  89  ASP ASP E . n 
E 1 99  ILE 99  90  90  ILE ILE E . n 
E 1 100 THR 100 91  91  THR THR E . n 
E 1 101 ALA 101 92  92  ALA ALA E . n 
E 1 102 TYR 102 93  93  TYR TYR E . n 
E 1 103 SER 103 94  94  SER SER E . n 
E 1 104 SER 104 95  95  SER SER E . n 
E 1 105 THR 105 96  96  THR THR E . n 
E 1 106 ARG 106 97  97  ARG ARG E . n 
E 1 107 PRO 107 98  98  PRO PRO E . n 
E 1 108 VAL 108 99  99  VAL VAL E . n 
E 1 109 GLN 109 100 100 GLN GLN E . n 
E 1 110 VAL 110 101 101 VAL VAL E . n 
E 1 111 LEU 111 102 102 LEU LEU E . n 
E 1 112 SER 112 103 103 SER SER E . n 
E 1 113 PRO 113 104 104 PRO PRO E . n 
E 1 114 GLN 114 105 105 GLN GLN E . n 
E 1 115 ASN 115 106 106 ASN ASN E . n 
E 1 116 ALA 116 107 107 ALA ALA E . n 
E 1 117 LEU 117 108 108 LEU LEU E . n 
E 1 118 VAL 118 109 109 VAL VAL E . n 
E 1 119 ASN 119 110 110 ASN ASN E . n 
E 1 120 SER 120 111 111 SER SER E . n 
E 1 121 SER 121 112 112 SER SER E . n 
E 1 122 GLY 122 113 113 GLY GLY E . n 
E 1 123 HIS 123 114 114 HIS HIS E . n 
E 1 124 VAL 124 115 115 VAL VAL E . n 
E 1 125 GLN 125 116 116 GLN GLN E . n 
E 1 126 TYR 126 117 117 TYR TYR E . n 
E 1 127 LEU 127 118 118 LEU LEU E . n 
E 1 128 PRO 128 119 119 PRO PRO E . n 
E 1 129 ALA 129 120 120 ALA ALA E . n 
E 1 130 GLN 130 121 121 GLN GLN E . n 
E 1 131 ARG 131 122 122 ARG ARG E . n 
E 1 132 LEU 132 123 123 LEU LEU E . n 
E 1 133 SER 133 124 124 SER SER E . n 
E 1 134 PHE 134 125 125 PHE PHE E . n 
E 1 135 MET 135 126 126 MET MET E . n 
E 1 136 CYS 136 127 127 CYS CYS E . n 
E 1 137 ASP 137 128 128 ASP ASP E . n 
E 1 138 PRO 138 129 129 PRO PRO E . n 
E 1 139 THR 139 130 130 THR THR E . n 
E 1 140 GLY 140 131 131 GLY GLY E . n 
E 1 141 VAL 141 132 132 VAL VAL E . n 
E 1 142 ASP 142 133 133 ASP ASP E . n 
E 1 143 SER 143 134 134 SER SER E . n 
E 1 144 GLU 144 135 135 GLU GLU E . n 
E 1 145 GLU 145 136 136 GLU GLU E . n 
E 1 146 GLY 146 137 137 GLY GLY E . n 
E 1 147 ALA 147 138 138 ALA ALA E . n 
E 1 148 THR 148 139 139 THR THR E . n 
E 1 149 CYS 149 140 140 CYS CYS E . n 
E 1 150 ALA 150 141 141 ALA ALA E . n 
E 1 151 VAL 151 142 142 VAL VAL E . n 
E 1 152 LYS 152 143 143 LYS LYS E . n 
E 1 153 PHE 153 144 144 PHE PHE E . n 
E 1 154 GLY 154 145 145 GLY GLY E . n 
E 1 155 SER 155 146 146 SER SER E . n 
E 1 156 TRP 156 147 147 TRP TRP E . n 
E 1 157 SER 157 148 148 SER SER E . n 
E 1 158 TYR 158 149 149 TYR TYR E . n 
E 1 159 GLY 159 150 150 GLY GLY E . n 
E 1 160 GLY 160 151 151 GLY GLY E . n 
E 1 161 TRP 161 152 152 TRP TRP E . n 
E 1 162 GLU 162 153 153 GLU GLU E . n 
E 1 163 ILE 163 154 154 ILE ILE E . n 
E 1 164 ASP 164 155 155 ASP ASP E . n 
E 1 165 LEU 165 156 156 LEU LEU E . n 
E 1 166 LYS 166 157 157 LYS LYS E . n 
E 1 167 THR 167 158 158 THR THR E . n 
E 1 168 ASP 168 159 159 ASP ASP E . n 
E 1 169 THR 169 160 160 THR THR E . n 
E 1 170 ASP 170 161 161 ASP ASP E . n 
E 1 171 GLN 171 162 162 GLN GLN E . n 
E 1 172 VAL 172 163 163 VAL VAL E . n 
E 1 173 ASP 173 164 164 ASP ASP E . n 
E 1 174 LEU 174 165 165 LEU LEU E . n 
E 1 175 SER 175 166 166 SER SER E . n 
E 1 176 SER 176 167 167 SER SER E . n 
E 1 177 TYR 177 168 168 TYR TYR E . n 
E 1 178 TYR 178 169 169 TYR TYR E . n 
E 1 179 ALA 179 170 170 ALA ALA E . n 
E 1 180 SER 180 171 171 SER SER E . n 
E 1 181 SER 181 172 172 SER SER E . n 
E 1 182 LYS 182 173 173 LYS LYS E . n 
E 1 183 TYR 183 174 174 TYR TYR E . n 
E 1 184 GLU 184 175 175 GLU GLU E . n 
E 1 185 ILE 185 176 176 ILE ILE E . n 
E 1 186 LEU 186 177 177 LEU LEU E . n 
E 1 187 SER 187 178 178 SER SER E . n 
E 1 188 ALA 188 179 179 ALA ALA E . n 
E 1 189 THR 189 180 180 THR THR E . n 
E 1 190 GLN 190 181 181 GLN GLN E . n 
E 1 191 THR 191 182 182 THR THR E . n 
E 1 192 ARG 192 183 183 ARG ARG E . n 
E 1 193 SER 193 184 184 SER SER E . n 
E 1 194 GLU 194 185 185 GLU GLU E . n 
E 1 195 ARG 195 186 186 ARG ARG E . n 
E 1 196 PHE 196 187 187 PHE PHE E . n 
E 1 197 TYR 197 188 188 TYR TYR E . n 
E 1 198 GLU 198 189 189 GLU GLU E . n 
E 1 199 CYS 199 190 190 CYS CYS E . n 
E 1 200 CYS 200 191 191 CYS CYS E . n 
E 1 201 LYS 201 192 192 LYS LYS E . n 
E 1 202 GLU 202 193 193 GLU GLU E . n 
E 1 203 PRO 203 194 194 PRO PRO E . n 
E 1 204 TYR 204 195 195 TYR TYR E . n 
E 1 205 PRO 205 196 196 PRO PRO E . n 
E 1 206 ASP 206 197 197 ASP ASP E . n 
E 1 207 VAL 207 198 198 VAL VAL E . n 
E 1 208 ASN 208 199 199 ASN ASN E . n 
E 1 209 LEU 209 200 200 LEU LEU E . n 
E 1 210 VAL 210 201 201 VAL VAL E . n 
E 1 211 VAL 211 202 202 VAL VAL E . n 
E 1 212 LYS 212 203 203 LYS LYS E . n 
E 1 213 PHE 213 204 204 PHE PHE E . n 
E 1 214 ARG 214 205 205 ARG ARG E . n 
E 1 215 GLU 215 206 206 GLU GLU E . n 
E 1 216 ARG 216 207 207 ARG ARG E . n 
E 1 217 ARG 217 208 208 ARG ARG E . n 
E 1 218 ALA 218 209 ?   ?   ?   E . n 
E 1 219 GLY 219 210 ?   ?   ?   E . n 
E 1 220 ASN 220 211 ?   ?   ?   E . n 
E 1 221 GLY 221 212 ?   ?   ?   E . n 
E 1 222 PHE 222 213 ?   ?   ?   E . n 
E 1 223 PHE 223 214 ?   ?   ?   E . n 
E 1 224 ARG 224 215 ?   ?   ?   E . n 
E 1 225 ASN 225 216 ?   ?   ?   E . n 
E 1 226 LEU 226 217 ?   ?   ?   E . n 
E 1 227 PHE 227 218 ?   ?   ?   E . n 
E 1 228 ASP 228 219 ?   ?   ?   E . n 
E 1 229 SER 229 220 ?   ?   ?   E . n 
E 1 230 ARG 230 221 ?   ?   ?   E . n 
F 1 1   ASP 1   -8  ?   ?   ?   F . n 
F 1 2   TYR 2   -7  ?   ?   ?   F . n 
F 1 3   LYS 3   -6  -6  LYS LYS F . n 
F 1 4   ASP 4   -5  -5  ASP ASP F . n 
F 1 5   ASP 5   -4  -4  ASP ASP F . n 
F 1 6   ASP 6   -3  -3  ASP ASP F . n 
F 1 7   ASP 7   -2  -2  ASP ASP F . n 
F 1 8   LYS 8   -1  -1  LYS LYS F . n 
F 1 9   LEU 9   0   0   LEU LEU F . n 
F 1 10  HIS 10  1   1   HIS HIS F . n 
F 1 11  SER 11  2   2   SER SER F . n 
F 1 12  GLN 12  3   3   GLN GLN F . n 
F 1 13  ALA 13  4   4   ALA ALA F . n 
F 1 14  ASN 14  5   5   ASN ASN F . n 
F 1 15  LEU 15  6   6   LEU LEU F . n 
F 1 16  MET 16  7   7   MET MET F . n 
F 1 17  ARG 17  8   8   ARG ARG F . n 
F 1 18  LEU 18  9   9   LEU LEU F . n 
F 1 19  LYS 19  10  10  LYS LYS F . n 
F 1 20  SER 20  11  11  SER SER F . n 
F 1 21  ASP 21  12  12  ASP ASP F . n 
F 1 22  LEU 22  13  13  LEU LEU F . n 
F 1 23  PHE 23  14  14  PHE PHE F . n 
F 1 24  ASN 24  15  15  ASN ASN F . n 
F 1 25  ARG 25  16  16  ARG ARG F . n 
F 1 26  SER 26  17  17  SER SER F . n 
F 1 27  PRO 27  18  18  PRO PRO F . n 
F 1 28  MET 28  19  19  MET MET F . n 
F 1 29  TYR 29  20  20  TYR TYR F . n 
F 1 30  PRO 30  21  21  PRO PRO F . n 
F 1 31  GLY 31  22  22  GLY GLY F . n 
F 1 32  PRO 32  23  23  PRO PRO F . n 
F 1 33  THR 33  24  24  THR THR F . n 
F 1 34  LYS 34  25  25  LYS LYS F . n 
F 1 35  ASP 35  26  26  ASP ASP F . n 
F 1 36  ASP 36  27  27  ASP ASP F . n 
F 1 37  PRO 37  28  28  PRO PRO F . n 
F 1 38  LEU 38  29  29  LEU LEU F . n 
F 1 39  THR 39  30  30  THR THR F . n 
F 1 40  VAL 40  31  31  VAL VAL F . n 
F 1 41  TYR 41  32  32  TYR TYR F . n 
F 1 42  LEU 42  33  33  LEU LEU F . n 
F 1 43  SER 43  34  34  SER SER F . n 
F 1 44  PHE 44  35  35  PHE PHE F . n 
F 1 45  SER 45  36  36  SER SER F . n 
F 1 46  LEU 46  37  37  LEU LEU F . n 
F 1 47  LEU 47  38  38  LEU LEU F . n 
F 1 48  ASP 48  39  39  ASP ASP F . n 
F 1 49  ILE 49  40  40  ILE ILE F . n 
F 1 50  VAL 50  41  41  VAL VAL F . n 
F 1 51  LYS 51  42  42  LYS LYS F . n 
F 1 52  ALA 52  43  43  ALA ALA F . n 
F 1 53  ASP 53  44  44  ASP ASP F . n 
F 1 54  SER 54  45  45  SER SER F . n 
F 1 55  SER 55  46  46  SER SER F . n 
F 1 56  THR 56  47  47  THR THR F . n 
F 1 57  ASN 57  48  48  ASN ASN F . n 
F 1 58  GLU 58  49  49  GLU GLU F . n 
F 1 59  VAL 59  50  50  VAL VAL F . n 
F 1 60  ASP 60  51  51  ASP ASP F . n 
F 1 61  LEU 61  52  52  LEU LEU F . n 
F 1 62  VAL 62  53  53  VAL VAL F . n 
F 1 63  TYR 63  54  54  TYR TYR F . n 
F 1 64  TRP 64  55  55  TRP TRP F . n 
F 1 65  GLU 65  56  56  GLU GLU F . n 
F 1 66  GLN 66  57  57  GLN GLN F . n 
F 1 67  GLN 67  58  58  GLN GLN F . n 
F 1 68  SER 68  59  59  SER SER F . n 
F 1 69  TRP 69  60  60  TRP TRP F . n 
F 1 70  LYS 70  61  61  LYS LYS F . n 
F 1 71  LEU 71  62  62  LEU LEU F . n 
F 1 72  ASN 72  63  63  ASN ASN F . n 
F 1 73  SER 73  64  64  SER SER F . n 
F 1 74  LEU 74  65  65  LEU LEU F . n 
F 1 75  MET 75  66  66  MET MET F . n 
F 1 76  TRP 76  67  67  TRP TRP F . n 
F 1 77  ASP 77  68  68  ASP ASP F . n 
F 1 78  PRO 78  69  69  PRO PRO F . n 
F 1 79  ASN 79  70  70  ASN ASN F . n 
F 1 80  GLU 80  71  71  GLU GLU F . n 
F 1 81  TYR 81  72  72  TYR TYR F . n 
F 1 82  GLY 82  73  73  GLY GLY F . n 
F 1 83  ASN 83  74  74  ASN ASN F . n 
F 1 84  ILE 84  75  75  ILE ILE F . n 
F 1 85  THR 85  76  76  THR THR F . n 
F 1 86  ASP 86  77  77  ASP ASP F . n 
F 1 87  PHE 87  78  78  PHE PHE F . n 
F 1 88  ARG 88  79  79  ARG ARG F . n 
F 1 89  THR 89  80  80  THR THR F . n 
F 1 90  SER 90  81  81  SER SER F . n 
F 1 91  ALA 91  82  82  ALA ALA F . n 
F 1 92  ALA 92  83  83  ALA ALA F . n 
F 1 93  ASP 93  84  84  ASP ASP F . n 
F 1 94  ILE 94  85  85  ILE ILE F . n 
F 1 95  TRP 95  86  86  TRP TRP F . n 
F 1 96  THR 96  87  87  THR THR F . n 
F 1 97  PRO 97  88  88  PRO PRO F . n 
F 1 98  ASP 98  89  89  ASP ASP F . n 
F 1 99  ILE 99  90  90  ILE ILE F . n 
F 1 100 THR 100 91  91  THR THR F . n 
F 1 101 ALA 101 92  92  ALA ALA F . n 
F 1 102 TYR 102 93  93  TYR TYR F . n 
F 1 103 SER 103 94  94  SER SER F . n 
F 1 104 SER 104 95  95  SER SER F . n 
F 1 105 THR 105 96  96  THR THR F . n 
F 1 106 ARG 106 97  97  ARG ARG F . n 
F 1 107 PRO 107 98  98  PRO PRO F . n 
F 1 108 VAL 108 99  99  VAL VAL F . n 
F 1 109 GLN 109 100 100 GLN GLN F . n 
F 1 110 VAL 110 101 101 VAL VAL F . n 
F 1 111 LEU 111 102 102 LEU LEU F . n 
F 1 112 SER 112 103 103 SER SER F . n 
F 1 113 PRO 113 104 104 PRO PRO F . n 
F 1 114 GLN 114 105 105 GLN GLN F . n 
F 1 115 ASN 115 106 106 ASN ASN F . n 
F 1 116 ALA 116 107 107 ALA ALA F . n 
F 1 117 LEU 117 108 108 LEU LEU F . n 
F 1 118 VAL 118 109 109 VAL VAL F . n 
F 1 119 ASN 119 110 110 ASN ASN F . n 
F 1 120 SER 120 111 111 SER SER F . n 
F 1 121 SER 121 112 112 SER SER F . n 
F 1 122 GLY 122 113 113 GLY GLY F . n 
F 1 123 HIS 123 114 114 HIS HIS F . n 
F 1 124 VAL 124 115 115 VAL VAL F . n 
F 1 125 GLN 125 116 116 GLN GLN F . n 
F 1 126 TYR 126 117 117 TYR TYR F . n 
F 1 127 LEU 127 118 118 LEU LEU F . n 
F 1 128 PRO 128 119 119 PRO PRO F . n 
F 1 129 ALA 129 120 120 ALA ALA F . n 
F 1 130 GLN 130 121 121 GLN GLN F . n 
F 1 131 ARG 131 122 122 ARG ARG F . n 
F 1 132 LEU 132 123 123 LEU LEU F . n 
F 1 133 SER 133 124 124 SER SER F . n 
F 1 134 PHE 134 125 125 PHE PHE F . n 
F 1 135 MET 135 126 126 MET MET F . n 
F 1 136 CYS 136 127 127 CYS CYS F . n 
F 1 137 ASP 137 128 128 ASP ASP F . n 
F 1 138 PRO 138 129 129 PRO PRO F . n 
F 1 139 THR 139 130 130 THR THR F . n 
F 1 140 GLY 140 131 131 GLY GLY F . n 
F 1 141 VAL 141 132 132 VAL VAL F . n 
F 1 142 ASP 142 133 133 ASP ASP F . n 
F 1 143 SER 143 134 134 SER SER F . n 
F 1 144 GLU 144 135 135 GLU GLU F . n 
F 1 145 GLU 145 136 136 GLU GLU F . n 
F 1 146 GLY 146 137 137 GLY GLY F . n 
F 1 147 ALA 147 138 138 ALA ALA F . n 
F 1 148 THR 148 139 139 THR THR F . n 
F 1 149 CYS 149 140 140 CYS CYS F . n 
F 1 150 ALA 150 141 141 ALA ALA F . n 
F 1 151 VAL 151 142 142 VAL VAL F . n 
F 1 152 LYS 152 143 143 LYS LYS F . n 
F 1 153 PHE 153 144 144 PHE PHE F . n 
F 1 154 GLY 154 145 145 GLY GLY F . n 
F 1 155 SER 155 146 146 SER SER F . n 
F 1 156 TRP 156 147 147 TRP TRP F . n 
F 1 157 SER 157 148 148 SER SER F . n 
F 1 158 TYR 158 149 149 TYR TYR F . n 
F 1 159 GLY 159 150 150 GLY GLY F . n 
F 1 160 GLY 160 151 151 GLY GLY F . n 
F 1 161 TRP 161 152 152 TRP TRP F . n 
F 1 162 GLU 162 153 153 GLU GLU F . n 
F 1 163 ILE 163 154 154 ILE ILE F . n 
F 1 164 ASP 164 155 155 ASP ASP F . n 
F 1 165 LEU 165 156 156 LEU LEU F . n 
F 1 166 LYS 166 157 157 LYS LYS F . n 
F 1 167 THR 167 158 158 THR THR F . n 
F 1 168 ASP 168 159 159 ASP ASP F . n 
F 1 169 THR 169 160 160 THR THR F . n 
F 1 170 ASP 170 161 161 ASP ASP F . n 
F 1 171 GLN 171 162 162 GLN GLN F . n 
F 1 172 VAL 172 163 163 VAL VAL F . n 
F 1 173 ASP 173 164 164 ASP ASP F . n 
F 1 174 LEU 174 165 165 LEU LEU F . n 
F 1 175 SER 175 166 166 SER SER F . n 
F 1 176 SER 176 167 167 SER SER F . n 
F 1 177 TYR 177 168 168 TYR TYR F . n 
F 1 178 TYR 178 169 169 TYR TYR F . n 
F 1 179 ALA 179 170 170 ALA ALA F . n 
F 1 180 SER 180 171 171 SER SER F . n 
F 1 181 SER 181 172 172 SER SER F . n 
F 1 182 LYS 182 173 173 LYS LYS F . n 
F 1 183 TYR 183 174 174 TYR TYR F . n 
F 1 184 GLU 184 175 175 GLU GLU F . n 
F 1 185 ILE 185 176 176 ILE ILE F . n 
F 1 186 LEU 186 177 177 LEU LEU F . n 
F 1 187 SER 187 178 178 SER SER F . n 
F 1 188 ALA 188 179 179 ALA ALA F . n 
F 1 189 THR 189 180 180 THR THR F . n 
F 1 190 GLN 190 181 181 GLN GLN F . n 
F 1 191 THR 191 182 182 THR THR F . n 
F 1 192 ARG 192 183 183 ARG ARG F . n 
F 1 193 SER 193 184 184 SER SER F . n 
F 1 194 GLU 194 185 185 GLU GLU F . n 
F 1 195 ARG 195 186 186 ARG ARG F . n 
F 1 196 PHE 196 187 187 PHE PHE F . n 
F 1 197 TYR 197 188 188 TYR TYR F . n 
F 1 198 GLU 198 189 189 GLU GLU F . n 
F 1 199 CYS 199 190 190 CYS CYS F . n 
F 1 200 CYS 200 191 191 CYS CYS F . n 
F 1 201 LYS 201 192 192 LYS LYS F . n 
F 1 202 GLU 202 193 193 GLU GLU F . n 
F 1 203 PRO 203 194 194 PRO PRO F . n 
F 1 204 TYR 204 195 195 TYR TYR F . n 
F 1 205 PRO 205 196 196 PRO PRO F . n 
F 1 206 ASP 206 197 197 ASP ASP F . n 
F 1 207 VAL 207 198 198 VAL VAL F . n 
F 1 208 ASN 208 199 199 ASN ASN F . n 
F 1 209 LEU 209 200 200 LEU LEU F . n 
F 1 210 VAL 210 201 201 VAL VAL F . n 
F 1 211 VAL 211 202 202 VAL VAL F . n 
F 1 212 LYS 212 203 203 LYS LYS F . n 
F 1 213 PHE 213 204 204 PHE PHE F . n 
F 1 214 ARG 214 205 205 ARG ARG F . n 
F 1 215 GLU 215 206 206 GLU GLU F . n 
F 1 216 ARG 216 207 207 ARG ARG F . n 
F 1 217 ARG 217 208 ?   ?   ?   F . n 
F 1 218 ALA 218 209 ?   ?   ?   F . n 
F 1 219 GLY 219 210 ?   ?   ?   F . n 
F 1 220 ASN 220 211 ?   ?   ?   F . n 
F 1 221 GLY 221 212 ?   ?   ?   F . n 
F 1 222 PHE 222 213 ?   ?   ?   F . n 
F 1 223 PHE 223 214 ?   ?   ?   F . n 
F 1 224 ARG 224 215 ?   ?   ?   F . n 
F 1 225 ASN 225 216 ?   ?   ?   F . n 
F 1 226 LEU 226 217 ?   ?   ?   F . n 
F 1 227 PHE 227 218 ?   ?   ?   F . n 
F 1 228 ASP 228 219 ?   ?   ?   F . n 
F 1 229 SER 229 220 ?   ?   ?   F . n 
F 1 230 ARG 230 221 ?   ?   ?   F . n 
G 1 1   ASP 1   -8  ?   ?   ?   G . n 
G 1 2   TYR 2   -7  ?   ?   ?   G . n 
G 1 3   LYS 3   -6  -6  LYS LYS G . n 
G 1 4   ASP 4   -5  -5  ASP ASP G . n 
G 1 5   ASP 5   -4  -4  ASP ASP G . n 
G 1 6   ASP 6   -3  -3  ASP ASP G . n 
G 1 7   ASP 7   -2  -2  ASP ASP G . n 
G 1 8   LYS 8   -1  -1  LYS LYS G . n 
G 1 9   LEU 9   0   0   LEU LEU G . n 
G 1 10  HIS 10  1   1   HIS HIS G . n 
G 1 11  SER 11  2   2   SER SER G . n 
G 1 12  GLN 12  3   3   GLN GLN G . n 
G 1 13  ALA 13  4   4   ALA ALA G . n 
G 1 14  ASN 14  5   5   ASN ASN G . n 
G 1 15  LEU 15  6   6   LEU LEU G . n 
G 1 16  MET 16  7   7   MET MET G . n 
G 1 17  ARG 17  8   8   ARG ARG G . n 
G 1 18  LEU 18  9   9   LEU LEU G . n 
G 1 19  LYS 19  10  10  LYS LYS G . n 
G 1 20  SER 20  11  11  SER SER G . n 
G 1 21  ASP 21  12  12  ASP ASP G . n 
G 1 22  LEU 22  13  13  LEU LEU G . n 
G 1 23  PHE 23  14  14  PHE PHE G . n 
G 1 24  ASN 24  15  15  ASN ASN G . n 
G 1 25  ARG 25  16  16  ARG ARG G . n 
G 1 26  SER 26  17  17  SER SER G . n 
G 1 27  PRO 27  18  18  PRO PRO G . n 
G 1 28  MET 28  19  19  MET MET G . n 
G 1 29  TYR 29  20  20  TYR TYR G . n 
G 1 30  PRO 30  21  21  PRO PRO G . n 
G 1 31  GLY 31  22  22  GLY GLY G . n 
G 1 32  PRO 32  23  23  PRO PRO G . n 
G 1 33  THR 33  24  24  THR THR G . n 
G 1 34  LYS 34  25  25  LYS LYS G . n 
G 1 35  ASP 35  26  26  ASP ASP G . n 
G 1 36  ASP 36  27  27  ASP ASP G . n 
G 1 37  PRO 37  28  28  PRO PRO G . n 
G 1 38  LEU 38  29  29  LEU LEU G . n 
G 1 39  THR 39  30  30  THR THR G . n 
G 1 40  VAL 40  31  31  VAL VAL G . n 
G 1 41  TYR 41  32  32  TYR TYR G . n 
G 1 42  LEU 42  33  33  LEU LEU G . n 
G 1 43  SER 43  34  34  SER SER G . n 
G 1 44  PHE 44  35  35  PHE PHE G . n 
G 1 45  SER 45  36  36  SER SER G . n 
G 1 46  LEU 46  37  37  LEU LEU G . n 
G 1 47  LEU 47  38  38  LEU LEU G . n 
G 1 48  ASP 48  39  39  ASP ASP G . n 
G 1 49  ILE 49  40  40  ILE ILE G . n 
G 1 50  VAL 50  41  41  VAL VAL G . n 
G 1 51  LYS 51  42  42  LYS LYS G . n 
G 1 52  ALA 52  43  43  ALA ALA G . n 
G 1 53  ASP 53  44  44  ASP ASP G . n 
G 1 54  SER 54  45  45  SER SER G . n 
G 1 55  SER 55  46  46  SER SER G . n 
G 1 56  THR 56  47  47  THR THR G . n 
G 1 57  ASN 57  48  48  ASN ASN G . n 
G 1 58  GLU 58  49  49  GLU GLU G . n 
G 1 59  VAL 59  50  50  VAL VAL G . n 
G 1 60  ASP 60  51  51  ASP ASP G . n 
G 1 61  LEU 61  52  52  LEU LEU G . n 
G 1 62  VAL 62  53  53  VAL VAL G . n 
G 1 63  TYR 63  54  54  TYR TYR G . n 
G 1 64  TRP 64  55  55  TRP TRP G . n 
G 1 65  GLU 65  56  56  GLU GLU G . n 
G 1 66  GLN 66  57  57  GLN GLN G . n 
G 1 67  GLN 67  58  58  GLN GLN G . n 
G 1 68  SER 68  59  59  SER SER G . n 
G 1 69  TRP 69  60  60  TRP TRP G . n 
G 1 70  LYS 70  61  61  LYS LYS G . n 
G 1 71  LEU 71  62  62  LEU LEU G . n 
G 1 72  ASN 72  63  63  ASN ASN G . n 
G 1 73  SER 73  64  64  SER SER G . n 
G 1 74  LEU 74  65  65  LEU LEU G . n 
G 1 75  MET 75  66  66  MET MET G . n 
G 1 76  TRP 76  67  67  TRP TRP G . n 
G 1 77  ASP 77  68  68  ASP ASP G . n 
G 1 78  PRO 78  69  69  PRO PRO G . n 
G 1 79  ASN 79  70  70  ASN ASN G . n 
G 1 80  GLU 80  71  71  GLU GLU G . n 
G 1 81  TYR 81  72  72  TYR TYR G . n 
G 1 82  GLY 82  73  73  GLY GLY G . n 
G 1 83  ASN 83  74  74  ASN ASN G . n 
G 1 84  ILE 84  75  75  ILE ILE G . n 
G 1 85  THR 85  76  76  THR THR G . n 
G 1 86  ASP 86  77  77  ASP ASP G . n 
G 1 87  PHE 87  78  78  PHE PHE G . n 
G 1 88  ARG 88  79  79  ARG ARG G . n 
G 1 89  THR 89  80  80  THR THR G . n 
G 1 90  SER 90  81  81  SER SER G . n 
G 1 91  ALA 91  82  82  ALA ALA G . n 
G 1 92  ALA 92  83  83  ALA ALA G . n 
G 1 93  ASP 93  84  84  ASP ASP G . n 
G 1 94  ILE 94  85  85  ILE ILE G . n 
G 1 95  TRP 95  86  86  TRP TRP G . n 
G 1 96  THR 96  87  87  THR THR G . n 
G 1 97  PRO 97  88  88  PRO PRO G . n 
G 1 98  ASP 98  89  89  ASP ASP G . n 
G 1 99  ILE 99  90  90  ILE ILE G . n 
G 1 100 THR 100 91  91  THR THR G . n 
G 1 101 ALA 101 92  92  ALA ALA G . n 
G 1 102 TYR 102 93  93  TYR TYR G . n 
G 1 103 SER 103 94  94  SER SER G . n 
G 1 104 SER 104 95  95  SER SER G . n 
G 1 105 THR 105 96  96  THR THR G . n 
G 1 106 ARG 106 97  97  ARG ARG G . n 
G 1 107 PRO 107 98  98  PRO PRO G . n 
G 1 108 VAL 108 99  99  VAL VAL G . n 
G 1 109 GLN 109 100 100 GLN GLN G . n 
G 1 110 VAL 110 101 101 VAL VAL G . n 
G 1 111 LEU 111 102 102 LEU LEU G . n 
G 1 112 SER 112 103 103 SER SER G . n 
G 1 113 PRO 113 104 104 PRO PRO G . n 
G 1 114 GLN 114 105 105 GLN GLN G . n 
G 1 115 ASN 115 106 106 ASN ASN G . n 
G 1 116 ALA 116 107 107 ALA ALA G . n 
G 1 117 LEU 117 108 108 LEU LEU G . n 
G 1 118 VAL 118 109 109 VAL VAL G . n 
G 1 119 ASN 119 110 110 ASN ASN G . n 
G 1 120 SER 120 111 111 SER SER G . n 
G 1 121 SER 121 112 112 SER SER G . n 
G 1 122 GLY 122 113 113 GLY GLY G . n 
G 1 123 HIS 123 114 114 HIS HIS G . n 
G 1 124 VAL 124 115 115 VAL VAL G . n 
G 1 125 GLN 125 116 116 GLN GLN G . n 
G 1 126 TYR 126 117 117 TYR TYR G . n 
G 1 127 LEU 127 118 118 LEU LEU G . n 
G 1 128 PRO 128 119 119 PRO PRO G . n 
G 1 129 ALA 129 120 120 ALA ALA G . n 
G 1 130 GLN 130 121 121 GLN GLN G . n 
G 1 131 ARG 131 122 122 ARG ARG G . n 
G 1 132 LEU 132 123 123 LEU LEU G . n 
G 1 133 SER 133 124 124 SER SER G . n 
G 1 134 PHE 134 125 125 PHE PHE G . n 
G 1 135 MET 135 126 126 MET MET G . n 
G 1 136 CYS 136 127 127 CYS CYS G . n 
G 1 137 ASP 137 128 128 ASP ASP G . n 
G 1 138 PRO 138 129 129 PRO PRO G . n 
G 1 139 THR 139 130 130 THR THR G . n 
G 1 140 GLY 140 131 131 GLY GLY G . n 
G 1 141 VAL 141 132 132 VAL VAL G . n 
G 1 142 ASP 142 133 133 ASP ASP G . n 
G 1 143 SER 143 134 134 SER SER G . n 
G 1 144 GLU 144 135 135 GLU GLU G . n 
G 1 145 GLU 145 136 136 GLU GLU G . n 
G 1 146 GLY 146 137 137 GLY GLY G . n 
G 1 147 ALA 147 138 138 ALA ALA G . n 
G 1 148 THR 148 139 139 THR THR G . n 
G 1 149 CYS 149 140 140 CYS CYS G . n 
G 1 150 ALA 150 141 141 ALA ALA G . n 
G 1 151 VAL 151 142 142 VAL VAL G . n 
G 1 152 LYS 152 143 143 LYS LYS G . n 
G 1 153 PHE 153 144 144 PHE PHE G . n 
G 1 154 GLY 154 145 145 GLY GLY G . n 
G 1 155 SER 155 146 146 SER SER G . n 
G 1 156 TRP 156 147 147 TRP TRP G . n 
G 1 157 SER 157 148 148 SER SER G . n 
G 1 158 TYR 158 149 149 TYR TYR G . n 
G 1 159 GLY 159 150 150 GLY GLY G . n 
G 1 160 GLY 160 151 151 GLY GLY G . n 
G 1 161 TRP 161 152 152 TRP TRP G . n 
G 1 162 GLU 162 153 153 GLU GLU G . n 
G 1 163 ILE 163 154 154 ILE ILE G . n 
G 1 164 ASP 164 155 155 ASP ASP G . n 
G 1 165 LEU 165 156 156 LEU LEU G . n 
G 1 166 LYS 166 157 157 LYS LYS G . n 
G 1 167 THR 167 158 158 THR THR G . n 
G 1 168 ASP 168 159 159 ASP ASP G . n 
G 1 169 THR 169 160 160 THR THR G . n 
G 1 170 ASP 170 161 161 ASP ASP G . n 
G 1 171 GLN 171 162 162 GLN GLN G . n 
G 1 172 VAL 172 163 163 VAL VAL G . n 
G 1 173 ASP 173 164 164 ASP ASP G . n 
G 1 174 LEU 174 165 165 LEU LEU G . n 
G 1 175 SER 175 166 166 SER SER G . n 
G 1 176 SER 176 167 167 SER SER G . n 
G 1 177 TYR 177 168 168 TYR TYR G . n 
G 1 178 TYR 178 169 169 TYR TYR G . n 
G 1 179 ALA 179 170 170 ALA ALA G . n 
G 1 180 SER 180 171 171 SER SER G . n 
G 1 181 SER 181 172 172 SER SER G . n 
G 1 182 LYS 182 173 173 LYS LYS G . n 
G 1 183 TYR 183 174 174 TYR TYR G . n 
G 1 184 GLU 184 175 175 GLU GLU G . n 
G 1 185 ILE 185 176 176 ILE ILE G . n 
G 1 186 LEU 186 177 177 LEU LEU G . n 
G 1 187 SER 187 178 178 SER SER G . n 
G 1 188 ALA 188 179 179 ALA ALA G . n 
G 1 189 THR 189 180 180 THR THR G . n 
G 1 190 GLN 190 181 181 GLN GLN G . n 
G 1 191 THR 191 182 182 THR THR G . n 
G 1 192 ARG 192 183 183 ARG ARG G . n 
G 1 193 SER 193 184 184 SER SER G . n 
G 1 194 GLU 194 185 185 GLU GLU G . n 
G 1 195 ARG 195 186 186 ARG ARG G . n 
G 1 196 PHE 196 187 187 PHE PHE G . n 
G 1 197 TYR 197 188 188 TYR TYR G . n 
G 1 198 GLU 198 189 189 GLU GLU G . n 
G 1 199 CYS 199 190 190 CYS CYS G . n 
G 1 200 CYS 200 191 191 CYS CYS G . n 
G 1 201 LYS 201 192 192 LYS LYS G . n 
G 1 202 GLU 202 193 193 GLU GLU G . n 
G 1 203 PRO 203 194 194 PRO PRO G . n 
G 1 204 TYR 204 195 195 TYR TYR G . n 
G 1 205 PRO 205 196 196 PRO PRO G . n 
G 1 206 ASP 206 197 197 ASP ASP G . n 
G 1 207 VAL 207 198 198 VAL VAL G . n 
G 1 208 ASN 208 199 199 ASN ASN G . n 
G 1 209 LEU 209 200 200 LEU LEU G . n 
G 1 210 VAL 210 201 201 VAL VAL G . n 
G 1 211 VAL 211 202 202 VAL VAL G . n 
G 1 212 LYS 212 203 203 LYS LYS G . n 
G 1 213 PHE 213 204 204 PHE PHE G . n 
G 1 214 ARG 214 205 205 ARG ARG G . n 
G 1 215 GLU 215 206 206 GLU GLU G . n 
G 1 216 ARG 216 207 207 ARG ARG G . n 
G 1 217 ARG 217 208 ?   ?   ?   G . n 
G 1 218 ALA 218 209 ?   ?   ?   G . n 
G 1 219 GLY 219 210 ?   ?   ?   G . n 
G 1 220 ASN 220 211 ?   ?   ?   G . n 
G 1 221 GLY 221 212 ?   ?   ?   G . n 
G 1 222 PHE 222 213 ?   ?   ?   G . n 
G 1 223 PHE 223 214 ?   ?   ?   G . n 
G 1 224 ARG 224 215 ?   ?   ?   G . n 
G 1 225 ASN 225 216 ?   ?   ?   G . n 
G 1 226 LEU 226 217 ?   ?   ?   G . n 
G 1 227 PHE 227 218 ?   ?   ?   G . n 
G 1 228 ASP 228 219 ?   ?   ?   G . n 
G 1 229 SER 229 220 ?   ?   ?   G . n 
G 1 230 ARG 230 221 ?   ?   ?   G . n 
H 1 1   ASP 1   -8  ?   ?   ?   H . n 
H 1 2   TYR 2   -7  ?   ?   ?   H . n 
H 1 3   LYS 3   -6  -6  LYS LYS H . n 
H 1 4   ASP 4   -5  -5  ASP ASP H . n 
H 1 5   ASP 5   -4  -4  ASP ASP H . n 
H 1 6   ASP 6   -3  -3  ASP ASP H . n 
H 1 7   ASP 7   -2  -2  ASP ASP H . n 
H 1 8   LYS 8   -1  -1  LYS LYS H . n 
H 1 9   LEU 9   0   0   LEU LEU H . n 
H 1 10  HIS 10  1   1   HIS HIS H . n 
H 1 11  SER 11  2   2   SER SER H . n 
H 1 12  GLN 12  3   3   GLN GLN H . n 
H 1 13  ALA 13  4   4   ALA ALA H . n 
H 1 14  ASN 14  5   5   ASN ASN H . n 
H 1 15  LEU 15  6   6   LEU LEU H . n 
H 1 16  MET 16  7   7   MET MET H . n 
H 1 17  ARG 17  8   8   ARG ARG H . n 
H 1 18  LEU 18  9   9   LEU LEU H . n 
H 1 19  LYS 19  10  10  LYS LYS H . n 
H 1 20  SER 20  11  11  SER SER H . n 
H 1 21  ASP 21  12  12  ASP ASP H . n 
H 1 22  LEU 22  13  13  LEU LEU H . n 
H 1 23  PHE 23  14  14  PHE PHE H . n 
H 1 24  ASN 24  15  15  ASN ASN H . n 
H 1 25  ARG 25  16  16  ARG ARG H . n 
H 1 26  SER 26  17  17  SER SER H . n 
H 1 27  PRO 27  18  18  PRO PRO H . n 
H 1 28  MET 28  19  19  MET MET H . n 
H 1 29  TYR 29  20  20  TYR TYR H . n 
H 1 30  PRO 30  21  21  PRO PRO H . n 
H 1 31  GLY 31  22  22  GLY GLY H . n 
H 1 32  PRO 32  23  23  PRO PRO H . n 
H 1 33  THR 33  24  24  THR THR H . n 
H 1 34  LYS 34  25  25  LYS LYS H . n 
H 1 35  ASP 35  26  26  ASP ASP H . n 
H 1 36  ASP 36  27  27  ASP ASP H . n 
H 1 37  PRO 37  28  28  PRO PRO H . n 
H 1 38  LEU 38  29  29  LEU LEU H . n 
H 1 39  THR 39  30  30  THR THR H . n 
H 1 40  VAL 40  31  31  VAL VAL H . n 
H 1 41  TYR 41  32  32  TYR TYR H . n 
H 1 42  LEU 42  33  33  LEU LEU H . n 
H 1 43  SER 43  34  34  SER SER H . n 
H 1 44  PHE 44  35  35  PHE PHE H . n 
H 1 45  SER 45  36  36  SER SER H . n 
H 1 46  LEU 46  37  37  LEU LEU H . n 
H 1 47  LEU 47  38  38  LEU LEU H . n 
H 1 48  ASP 48  39  39  ASP ASP H . n 
H 1 49  ILE 49  40  40  ILE ILE H . n 
H 1 50  VAL 50  41  41  VAL VAL H . n 
H 1 51  LYS 51  42  42  LYS LYS H . n 
H 1 52  ALA 52  43  43  ALA ALA H . n 
H 1 53  ASP 53  44  44  ASP ASP H . n 
H 1 54  SER 54  45  45  SER SER H . n 
H 1 55  SER 55  46  46  SER SER H . n 
H 1 56  THR 56  47  47  THR THR H . n 
H 1 57  ASN 57  48  48  ASN ASN H . n 
H 1 58  GLU 58  49  49  GLU GLU H . n 
H 1 59  VAL 59  50  50  VAL VAL H . n 
H 1 60  ASP 60  51  51  ASP ASP H . n 
H 1 61  LEU 61  52  52  LEU LEU H . n 
H 1 62  VAL 62  53  53  VAL VAL H . n 
H 1 63  TYR 63  54  54  TYR TYR H . n 
H 1 64  TRP 64  55  55  TRP TRP H . n 
H 1 65  GLU 65  56  56  GLU GLU H . n 
H 1 66  GLN 66  57  57  GLN GLN H . n 
H 1 67  GLN 67  58  58  GLN GLN H . n 
H 1 68  SER 68  59  59  SER SER H . n 
H 1 69  TRP 69  60  60  TRP TRP H . n 
H 1 70  LYS 70  61  61  LYS LYS H . n 
H 1 71  LEU 71  62  62  LEU LEU H . n 
H 1 72  ASN 72  63  63  ASN ASN H . n 
H 1 73  SER 73  64  64  SER SER H . n 
H 1 74  LEU 74  65  65  LEU LEU H . n 
H 1 75  MET 75  66  66  MET MET H . n 
H 1 76  TRP 76  67  67  TRP TRP H . n 
H 1 77  ASP 77  68  68  ASP ASP H . n 
H 1 78  PRO 78  69  69  PRO PRO H . n 
H 1 79  ASN 79  70  70  ASN ASN H . n 
H 1 80  GLU 80  71  71  GLU GLU H . n 
H 1 81  TYR 81  72  72  TYR TYR H . n 
H 1 82  GLY 82  73  73  GLY GLY H . n 
H 1 83  ASN 83  74  74  ASN ASN H . n 
H 1 84  ILE 84  75  75  ILE ILE H . n 
H 1 85  THR 85  76  76  THR THR H . n 
H 1 86  ASP 86  77  77  ASP ASP H . n 
H 1 87  PHE 87  78  78  PHE PHE H . n 
H 1 88  ARG 88  79  79  ARG ARG H . n 
H 1 89  THR 89  80  80  THR THR H . n 
H 1 90  SER 90  81  81  SER SER H . n 
H 1 91  ALA 91  82  82  ALA ALA H . n 
H 1 92  ALA 92  83  83  ALA ALA H . n 
H 1 93  ASP 93  84  84  ASP ASP H . n 
H 1 94  ILE 94  85  85  ILE ILE H . n 
H 1 95  TRP 95  86  86  TRP TRP H . n 
H 1 96  THR 96  87  87  THR THR H . n 
H 1 97  PRO 97  88  88  PRO PRO H . n 
H 1 98  ASP 98  89  89  ASP ASP H . n 
H 1 99  ILE 99  90  90  ILE ILE H . n 
H 1 100 THR 100 91  91  THR THR H . n 
H 1 101 ALA 101 92  92  ALA ALA H . n 
H 1 102 TYR 102 93  93  TYR TYR H . n 
H 1 103 SER 103 94  94  SER SER H . n 
H 1 104 SER 104 95  95  SER SER H . n 
H 1 105 THR 105 96  96  THR THR H . n 
H 1 106 ARG 106 97  97  ARG ARG H . n 
H 1 107 PRO 107 98  98  PRO PRO H . n 
H 1 108 VAL 108 99  99  VAL VAL H . n 
H 1 109 GLN 109 100 100 GLN GLN H . n 
H 1 110 VAL 110 101 101 VAL VAL H . n 
H 1 111 LEU 111 102 102 LEU LEU H . n 
H 1 112 SER 112 103 103 SER SER H . n 
H 1 113 PRO 113 104 104 PRO PRO H . n 
H 1 114 GLN 114 105 105 GLN GLN H . n 
H 1 115 ASN 115 106 106 ASN ASN H . n 
H 1 116 ALA 116 107 107 ALA ALA H . n 
H 1 117 LEU 117 108 108 LEU LEU H . n 
H 1 118 VAL 118 109 109 VAL VAL H . n 
H 1 119 ASN 119 110 110 ASN ASN H . n 
H 1 120 SER 120 111 111 SER SER H . n 
H 1 121 SER 121 112 112 SER SER H . n 
H 1 122 GLY 122 113 113 GLY GLY H . n 
H 1 123 HIS 123 114 114 HIS HIS H . n 
H 1 124 VAL 124 115 115 VAL VAL H . n 
H 1 125 GLN 125 116 116 GLN GLN H . n 
H 1 126 TYR 126 117 117 TYR TYR H . n 
H 1 127 LEU 127 118 118 LEU LEU H . n 
H 1 128 PRO 128 119 119 PRO PRO H . n 
H 1 129 ALA 129 120 120 ALA ALA H . n 
H 1 130 GLN 130 121 121 GLN GLN H . n 
H 1 131 ARG 131 122 122 ARG ARG H . n 
H 1 132 LEU 132 123 123 LEU LEU H . n 
H 1 133 SER 133 124 124 SER SER H . n 
H 1 134 PHE 134 125 125 PHE PHE H . n 
H 1 135 MET 135 126 126 MET MET H . n 
H 1 136 CYS 136 127 127 CYS CYS H . n 
H 1 137 ASP 137 128 128 ASP ASP H . n 
H 1 138 PRO 138 129 129 PRO PRO H . n 
H 1 139 THR 139 130 130 THR THR H . n 
H 1 140 GLY 140 131 131 GLY GLY H . n 
H 1 141 VAL 141 132 132 VAL VAL H . n 
H 1 142 ASP 142 133 133 ASP ASP H . n 
H 1 143 SER 143 134 134 SER SER H . n 
H 1 144 GLU 144 135 135 GLU GLU H . n 
H 1 145 GLU 145 136 136 GLU GLU H . n 
H 1 146 GLY 146 137 137 GLY GLY H . n 
H 1 147 ALA 147 138 138 ALA ALA H . n 
H 1 148 THR 148 139 139 THR THR H . n 
H 1 149 CYS 149 140 140 CYS CYS H . n 
H 1 150 ALA 150 141 141 ALA ALA H . n 
H 1 151 VAL 151 142 142 VAL VAL H . n 
H 1 152 LYS 152 143 143 LYS LYS H . n 
H 1 153 PHE 153 144 144 PHE PHE H . n 
H 1 154 GLY 154 145 145 GLY GLY H . n 
H 1 155 SER 155 146 146 SER SER H . n 
H 1 156 TRP 156 147 147 TRP TRP H . n 
H 1 157 SER 157 148 148 SER SER H . n 
H 1 158 TYR 158 149 149 TYR TYR H . n 
H 1 159 GLY 159 150 150 GLY GLY H . n 
H 1 160 GLY 160 151 151 GLY GLY H . n 
H 1 161 TRP 161 152 152 TRP TRP H . n 
H 1 162 GLU 162 153 153 GLU GLU H . n 
H 1 163 ILE 163 154 154 ILE ILE H . n 
H 1 164 ASP 164 155 155 ASP ASP H . n 
H 1 165 LEU 165 156 156 LEU LEU H . n 
H 1 166 LYS 166 157 157 LYS LYS H . n 
H 1 167 THR 167 158 158 THR THR H . n 
H 1 168 ASP 168 159 159 ASP ASP H . n 
H 1 169 THR 169 160 160 THR THR H . n 
H 1 170 ASP 170 161 161 ASP ASP H . n 
H 1 171 GLN 171 162 162 GLN GLN H . n 
H 1 172 VAL 172 163 163 VAL VAL H . n 
H 1 173 ASP 173 164 164 ASP ASP H . n 
H 1 174 LEU 174 165 165 LEU LEU H . n 
H 1 175 SER 175 166 166 SER SER H . n 
H 1 176 SER 176 167 167 SER SER H . n 
H 1 177 TYR 177 168 168 TYR TYR H . n 
H 1 178 TYR 178 169 169 TYR TYR H . n 
H 1 179 ALA 179 170 170 ALA ALA H . n 
H 1 180 SER 180 171 171 SER SER H . n 
H 1 181 SER 181 172 172 SER SER H . n 
H 1 182 LYS 182 173 173 LYS LYS H . n 
H 1 183 TYR 183 174 174 TYR TYR H . n 
H 1 184 GLU 184 175 175 GLU GLU H . n 
H 1 185 ILE 185 176 176 ILE ILE H . n 
H 1 186 LEU 186 177 177 LEU LEU H . n 
H 1 187 SER 187 178 178 SER SER H . n 
H 1 188 ALA 188 179 179 ALA ALA H . n 
H 1 189 THR 189 180 180 THR THR H . n 
H 1 190 GLN 190 181 181 GLN GLN H . n 
H 1 191 THR 191 182 182 THR THR H . n 
H 1 192 ARG 192 183 183 ARG ARG H . n 
H 1 193 SER 193 184 184 SER SER H . n 
H 1 194 GLU 194 185 185 GLU GLU H . n 
H 1 195 ARG 195 186 186 ARG ARG H . n 
H 1 196 PHE 196 187 187 PHE PHE H . n 
H 1 197 TYR 197 188 188 TYR TYR H . n 
H 1 198 GLU 198 189 189 GLU GLU H . n 
H 1 199 CYS 199 190 190 CYS CYS H . n 
H 1 200 CYS 200 191 191 CYS CYS H . n 
H 1 201 LYS 201 192 192 LYS LYS H . n 
H 1 202 GLU 202 193 193 GLU GLU H . n 
H 1 203 PRO 203 194 194 PRO PRO H . n 
H 1 204 TYR 204 195 195 TYR TYR H . n 
H 1 205 PRO 205 196 196 PRO PRO H . n 
H 1 206 ASP 206 197 197 ASP ASP H . n 
H 1 207 VAL 207 198 198 VAL VAL H . n 
H 1 208 ASN 208 199 199 ASN ASN H . n 
H 1 209 LEU 209 200 200 LEU LEU H . n 
H 1 210 VAL 210 201 201 VAL VAL H . n 
H 1 211 VAL 211 202 202 VAL VAL H . n 
H 1 212 LYS 212 203 203 LYS LYS H . n 
H 1 213 PHE 213 204 204 PHE PHE H . n 
H 1 214 ARG 214 205 205 ARG ARG H . n 
H 1 215 GLU 215 206 206 GLU GLU H . n 
H 1 216 ARG 216 207 207 ARG ARG H . n 
H 1 217 ARG 217 208 208 ARG ARG H . n 
H 1 218 ALA 218 209 ?   ?   ?   H . n 
H 1 219 GLY 219 210 ?   ?   ?   H . n 
H 1 220 ASN 220 211 ?   ?   ?   H . n 
H 1 221 GLY 221 212 ?   ?   ?   H . n 
H 1 222 PHE 222 213 ?   ?   ?   H . n 
H 1 223 PHE 223 214 ?   ?   ?   H . n 
H 1 224 ARG 224 215 ?   ?   ?   H . n 
H 1 225 ASN 225 216 ?   ?   ?   H . n 
H 1 226 LEU 226 217 ?   ?   ?   H . n 
H 1 227 PHE 227 218 ?   ?   ?   H . n 
H 1 228 ASP 228 219 ?   ?   ?   H . n 
H 1 229 SER 229 220 ?   ?   ?   H . n 
H 1 230 ARG 230 221 ?   ?   ?   H . n 
I 1 1   ASP 1   -8  ?   ?   ?   I . n 
I 1 2   TYR 2   -7  ?   ?   ?   I . n 
I 1 3   LYS 3   -6  ?   ?   ?   I . n 
I 1 4   ASP 4   -5  -5  ASP ASP I . n 
I 1 5   ASP 5   -4  -4  ASP ASP I . n 
I 1 6   ASP 6   -3  -3  ASP ASP I . n 
I 1 7   ASP 7   -2  -2  ASP ASP I . n 
I 1 8   LYS 8   -1  -1  LYS LYS I . n 
I 1 9   LEU 9   0   0   LEU LEU I . n 
I 1 10  HIS 10  1   1   HIS HIS I . n 
I 1 11  SER 11  2   2   SER SER I . n 
I 1 12  GLN 12  3   3   GLN GLN I . n 
I 1 13  ALA 13  4   4   ALA ALA I . n 
I 1 14  ASN 14  5   5   ASN ASN I . n 
I 1 15  LEU 15  6   6   LEU LEU I . n 
I 1 16  MET 16  7   7   MET MET I . n 
I 1 17  ARG 17  8   8   ARG ARG I . n 
I 1 18  LEU 18  9   9   LEU LEU I . n 
I 1 19  LYS 19  10  10  LYS LYS I . n 
I 1 20  SER 20  11  11  SER SER I . n 
I 1 21  ASP 21  12  12  ASP ASP I . n 
I 1 22  LEU 22  13  13  LEU LEU I . n 
I 1 23  PHE 23  14  14  PHE PHE I . n 
I 1 24  ASN 24  15  15  ASN ASN I . n 
I 1 25  ARG 25  16  16  ARG ARG I . n 
I 1 26  SER 26  17  17  SER SER I . n 
I 1 27  PRO 27  18  18  PRO PRO I . n 
I 1 28  MET 28  19  19  MET MET I . n 
I 1 29  TYR 29  20  20  TYR TYR I . n 
I 1 30  PRO 30  21  21  PRO PRO I . n 
I 1 31  GLY 31  22  22  GLY GLY I . n 
I 1 32  PRO 32  23  23  PRO PRO I . n 
I 1 33  THR 33  24  24  THR THR I . n 
I 1 34  LYS 34  25  25  LYS LYS I . n 
I 1 35  ASP 35  26  26  ASP ASP I . n 
I 1 36  ASP 36  27  27  ASP ASP I . n 
I 1 37  PRO 37  28  28  PRO PRO I . n 
I 1 38  LEU 38  29  29  LEU LEU I . n 
I 1 39  THR 39  30  30  THR THR I . n 
I 1 40  VAL 40  31  31  VAL VAL I . n 
I 1 41  TYR 41  32  32  TYR TYR I . n 
I 1 42  LEU 42  33  33  LEU LEU I . n 
I 1 43  SER 43  34  34  SER SER I . n 
I 1 44  PHE 44  35  35  PHE PHE I . n 
I 1 45  SER 45  36  36  SER SER I . n 
I 1 46  LEU 46  37  37  LEU LEU I . n 
I 1 47  LEU 47  38  38  LEU LEU I . n 
I 1 48  ASP 48  39  39  ASP ASP I . n 
I 1 49  ILE 49  40  40  ILE ILE I . n 
I 1 50  VAL 50  41  41  VAL VAL I . n 
I 1 51  LYS 51  42  42  LYS LYS I . n 
I 1 52  ALA 52  43  43  ALA ALA I . n 
I 1 53  ASP 53  44  44  ASP ASP I . n 
I 1 54  SER 54  45  45  SER SER I . n 
I 1 55  SER 55  46  46  SER SER I . n 
I 1 56  THR 56  47  47  THR THR I . n 
I 1 57  ASN 57  48  48  ASN ASN I . n 
I 1 58  GLU 58  49  49  GLU GLU I . n 
I 1 59  VAL 59  50  50  VAL VAL I . n 
I 1 60  ASP 60  51  51  ASP ASP I . n 
I 1 61  LEU 61  52  52  LEU LEU I . n 
I 1 62  VAL 62  53  53  VAL VAL I . n 
I 1 63  TYR 63  54  54  TYR TYR I . n 
I 1 64  TRP 64  55  55  TRP TRP I . n 
I 1 65  GLU 65  56  56  GLU GLU I . n 
I 1 66  GLN 66  57  57  GLN GLN I . n 
I 1 67  GLN 67  58  58  GLN GLN I . n 
I 1 68  SER 68  59  59  SER SER I . n 
I 1 69  TRP 69  60  60  TRP TRP I . n 
I 1 70  LYS 70  61  61  LYS LYS I . n 
I 1 71  LEU 71  62  62  LEU LEU I . n 
I 1 72  ASN 72  63  63  ASN ASN I . n 
I 1 73  SER 73  64  64  SER SER I . n 
I 1 74  LEU 74  65  65  LEU LEU I . n 
I 1 75  MET 75  66  66  MET MET I . n 
I 1 76  TRP 76  67  67  TRP TRP I . n 
I 1 77  ASP 77  68  68  ASP ASP I . n 
I 1 78  PRO 78  69  69  PRO PRO I . n 
I 1 79  ASN 79  70  70  ASN ASN I . n 
I 1 80  GLU 80  71  71  GLU GLU I . n 
I 1 81  TYR 81  72  72  TYR TYR I . n 
I 1 82  GLY 82  73  73  GLY GLY I . n 
I 1 83  ASN 83  74  74  ASN ASN I . n 
I 1 84  ILE 84  75  75  ILE ILE I . n 
I 1 85  THR 85  76  76  THR THR I . n 
I 1 86  ASP 86  77  77  ASP ASP I . n 
I 1 87  PHE 87  78  78  PHE PHE I . n 
I 1 88  ARG 88  79  79  ARG ARG I . n 
I 1 89  THR 89  80  80  THR THR I . n 
I 1 90  SER 90  81  81  SER SER I . n 
I 1 91  ALA 91  82  82  ALA ALA I . n 
I 1 92  ALA 92  83  83  ALA ALA I . n 
I 1 93  ASP 93  84  84  ASP ASP I . n 
I 1 94  ILE 94  85  85  ILE ILE I . n 
I 1 95  TRP 95  86  86  TRP TRP I . n 
I 1 96  THR 96  87  87  THR THR I . n 
I 1 97  PRO 97  88  88  PRO PRO I . n 
I 1 98  ASP 98  89  89  ASP ASP I . n 
I 1 99  ILE 99  90  90  ILE ILE I . n 
I 1 100 THR 100 91  91  THR THR I . n 
I 1 101 ALA 101 92  92  ALA ALA I . n 
I 1 102 TYR 102 93  93  TYR TYR I . n 
I 1 103 SER 103 94  94  SER SER I . n 
I 1 104 SER 104 95  95  SER SER I . n 
I 1 105 THR 105 96  96  THR THR I . n 
I 1 106 ARG 106 97  97  ARG ARG I . n 
I 1 107 PRO 107 98  98  PRO PRO I . n 
I 1 108 VAL 108 99  99  VAL VAL I . n 
I 1 109 GLN 109 100 100 GLN GLN I . n 
I 1 110 VAL 110 101 101 VAL VAL I . n 
I 1 111 LEU 111 102 102 LEU LEU I . n 
I 1 112 SER 112 103 103 SER SER I . n 
I 1 113 PRO 113 104 104 PRO PRO I . n 
I 1 114 GLN 114 105 105 GLN GLN I . n 
I 1 115 ASN 115 106 106 ASN ASN I . n 
I 1 116 ALA 116 107 107 ALA ALA I . n 
I 1 117 LEU 117 108 108 LEU LEU I . n 
I 1 118 VAL 118 109 109 VAL VAL I . n 
I 1 119 ASN 119 110 110 ASN ASN I . n 
I 1 120 SER 120 111 111 SER SER I . n 
I 1 121 SER 121 112 112 SER SER I . n 
I 1 122 GLY 122 113 113 GLY GLY I . n 
I 1 123 HIS 123 114 114 HIS HIS I . n 
I 1 124 VAL 124 115 115 VAL VAL I . n 
I 1 125 GLN 125 116 116 GLN GLN I . n 
I 1 126 TYR 126 117 117 TYR TYR I . n 
I 1 127 LEU 127 118 118 LEU LEU I . n 
I 1 128 PRO 128 119 119 PRO PRO I . n 
I 1 129 ALA 129 120 120 ALA ALA I . n 
I 1 130 GLN 130 121 121 GLN GLN I . n 
I 1 131 ARG 131 122 122 ARG ARG I . n 
I 1 132 LEU 132 123 123 LEU LEU I . n 
I 1 133 SER 133 124 124 SER SER I . n 
I 1 134 PHE 134 125 125 PHE PHE I . n 
I 1 135 MET 135 126 126 MET MET I . n 
I 1 136 CYS 136 127 127 CYS CYS I . n 
I 1 137 ASP 137 128 128 ASP ASP I . n 
I 1 138 PRO 138 129 129 PRO PRO I . n 
I 1 139 THR 139 130 130 THR THR I . n 
I 1 140 GLY 140 131 131 GLY GLY I . n 
I 1 141 VAL 141 132 132 VAL VAL I . n 
I 1 142 ASP 142 133 133 ASP ASP I . n 
I 1 143 SER 143 134 134 SER SER I . n 
I 1 144 GLU 144 135 135 GLU GLU I . n 
I 1 145 GLU 145 136 136 GLU GLU I . n 
I 1 146 GLY 146 137 137 GLY GLY I . n 
I 1 147 ALA 147 138 138 ALA ALA I . n 
I 1 148 THR 148 139 139 THR THR I . n 
I 1 149 CYS 149 140 140 CYS CYS I . n 
I 1 150 ALA 150 141 141 ALA ALA I . n 
I 1 151 VAL 151 142 142 VAL VAL I . n 
I 1 152 LYS 152 143 143 LYS LYS I . n 
I 1 153 PHE 153 144 144 PHE PHE I . n 
I 1 154 GLY 154 145 145 GLY GLY I . n 
I 1 155 SER 155 146 146 SER SER I . n 
I 1 156 TRP 156 147 147 TRP TRP I . n 
I 1 157 SER 157 148 148 SER SER I . n 
I 1 158 TYR 158 149 149 TYR TYR I . n 
I 1 159 GLY 159 150 150 GLY GLY I . n 
I 1 160 GLY 160 151 151 GLY GLY I . n 
I 1 161 TRP 161 152 152 TRP TRP I . n 
I 1 162 GLU 162 153 153 GLU GLU I . n 
I 1 163 ILE 163 154 154 ILE ILE I . n 
I 1 164 ASP 164 155 155 ASP ASP I . n 
I 1 165 LEU 165 156 156 LEU LEU I . n 
I 1 166 LYS 166 157 157 LYS LYS I . n 
I 1 167 THR 167 158 158 THR THR I . n 
I 1 168 ASP 168 159 159 ASP ASP I . n 
I 1 169 THR 169 160 160 THR THR I . n 
I 1 170 ASP 170 161 161 ASP ASP I . n 
I 1 171 GLN 171 162 162 GLN GLN I . n 
I 1 172 VAL 172 163 163 VAL VAL I . n 
I 1 173 ASP 173 164 164 ASP ASP I . n 
I 1 174 LEU 174 165 165 LEU LEU I . n 
I 1 175 SER 175 166 166 SER SER I . n 
I 1 176 SER 176 167 167 SER SER I . n 
I 1 177 TYR 177 168 168 TYR TYR I . n 
I 1 178 TYR 178 169 169 TYR TYR I . n 
I 1 179 ALA 179 170 170 ALA ALA I . n 
I 1 180 SER 180 171 171 SER SER I . n 
I 1 181 SER 181 172 172 SER SER I . n 
I 1 182 LYS 182 173 173 LYS LYS I . n 
I 1 183 TYR 183 174 174 TYR TYR I . n 
I 1 184 GLU 184 175 175 GLU GLU I . n 
I 1 185 ILE 185 176 176 ILE ILE I . n 
I 1 186 LEU 186 177 177 LEU LEU I . n 
I 1 187 SER 187 178 178 SER SER I . n 
I 1 188 ALA 188 179 179 ALA ALA I . n 
I 1 189 THR 189 180 180 THR THR I . n 
I 1 190 GLN 190 181 181 GLN GLN I . n 
I 1 191 THR 191 182 182 THR THR I . n 
I 1 192 ARG 192 183 183 ARG ARG I . n 
I 1 193 SER 193 184 184 SER SER I . n 
I 1 194 GLU 194 185 185 GLU GLU I . n 
I 1 195 ARG 195 186 186 ARG ARG I . n 
I 1 196 PHE 196 187 187 PHE PHE I . n 
I 1 197 TYR 197 188 188 TYR TYR I . n 
I 1 198 GLU 198 189 189 GLU GLU I . n 
I 1 199 CYS 199 190 190 CYS CYS I . n 
I 1 200 CYS 200 191 191 CYS CYS I . n 
I 1 201 LYS 201 192 192 LYS LYS I . n 
I 1 202 GLU 202 193 193 GLU GLU I . n 
I 1 203 PRO 203 194 194 PRO PRO I . n 
I 1 204 TYR 204 195 195 TYR TYR I . n 
I 1 205 PRO 205 196 196 PRO PRO I . n 
I 1 206 ASP 206 197 197 ASP ASP I . n 
I 1 207 VAL 207 198 198 VAL VAL I . n 
I 1 208 ASN 208 199 199 ASN ASN I . n 
I 1 209 LEU 209 200 200 LEU LEU I . n 
I 1 210 VAL 210 201 201 VAL VAL I . n 
I 1 211 VAL 211 202 202 VAL VAL I . n 
I 1 212 LYS 212 203 203 LYS LYS I . n 
I 1 213 PHE 213 204 204 PHE PHE I . n 
I 1 214 ARG 214 205 205 ARG ARG I . n 
I 1 215 GLU 215 206 206 GLU GLU I . n 
I 1 216 ARG 216 207 207 ARG ARG I . n 
I 1 217 ARG 217 208 208 ARG ARG I . n 
I 1 218 ALA 218 209 ?   ?   ?   I . n 
I 1 219 GLY 219 210 ?   ?   ?   I . n 
I 1 220 ASN 220 211 ?   ?   ?   I . n 
I 1 221 GLY 221 212 ?   ?   ?   I . n 
I 1 222 PHE 222 213 ?   ?   ?   I . n 
I 1 223 PHE 223 214 ?   ?   ?   I . n 
I 1 224 ARG 224 215 ?   ?   ?   I . n 
I 1 225 ASN 225 216 ?   ?   ?   I . n 
I 1 226 LEU 226 217 ?   ?   ?   I . n 
I 1 227 PHE 227 218 ?   ?   ?   I . n 
I 1 228 ASP 228 219 ?   ?   ?   I . n 
I 1 229 SER 229 220 ?   ?   ?   I . n 
I 1 230 ARG 230 221 ?   ?   ?   I . n 
J 1 1   ASP 1   -8  ?   ?   ?   J . n 
J 1 2   TYR 2   -7  ?   ?   ?   J . n 
J 1 3   LYS 3   -6  -6  LYS LYS J . n 
J 1 4   ASP 4   -5  -5  ASP ASP J . n 
J 1 5   ASP 5   -4  -4  ASP ASP J . n 
J 1 6   ASP 6   -3  -3  ASP ASP J . n 
J 1 7   ASP 7   -2  -2  ASP ASP J . n 
J 1 8   LYS 8   -1  -1  LYS LYS J . n 
J 1 9   LEU 9   0   0   LEU LEU J . n 
J 1 10  HIS 10  1   1   HIS HIS J . n 
J 1 11  SER 11  2   2   SER SER J . n 
J 1 12  GLN 12  3   3   GLN GLN J . n 
J 1 13  ALA 13  4   4   ALA ALA J . n 
J 1 14  ASN 14  5   5   ASN ASN J . n 
J 1 15  LEU 15  6   6   LEU LEU J . n 
J 1 16  MET 16  7   7   MET MET J . n 
J 1 17  ARG 17  8   8   ARG ARG J . n 
J 1 18  LEU 18  9   9   LEU LEU J . n 
J 1 19  LYS 19  10  10  LYS LYS J . n 
J 1 20  SER 20  11  11  SER SER J . n 
J 1 21  ASP 21  12  12  ASP ASP J . n 
J 1 22  LEU 22  13  13  LEU LEU J . n 
J 1 23  PHE 23  14  14  PHE PHE J . n 
J 1 24  ASN 24  15  15  ASN ASN J . n 
J 1 25  ARG 25  16  16  ARG ARG J . n 
J 1 26  SER 26  17  17  SER SER J . n 
J 1 27  PRO 27  18  18  PRO PRO J . n 
J 1 28  MET 28  19  19  MET MET J . n 
J 1 29  TYR 29  20  20  TYR TYR J . n 
J 1 30  PRO 30  21  21  PRO PRO J . n 
J 1 31  GLY 31  22  22  GLY GLY J . n 
J 1 32  PRO 32  23  23  PRO PRO J . n 
J 1 33  THR 33  24  24  THR THR J . n 
J 1 34  LYS 34  25  25  LYS LYS J . n 
J 1 35  ASP 35  26  26  ASP ASP J . n 
J 1 36  ASP 36  27  27  ASP ASP J . n 
J 1 37  PRO 37  28  28  PRO PRO J . n 
J 1 38  LEU 38  29  29  LEU LEU J . n 
J 1 39  THR 39  30  30  THR THR J . n 
J 1 40  VAL 40  31  31  VAL VAL J . n 
J 1 41  TYR 41  32  32  TYR TYR J . n 
J 1 42  LEU 42  33  33  LEU LEU J . n 
J 1 43  SER 43  34  34  SER SER J . n 
J 1 44  PHE 44  35  35  PHE PHE J . n 
J 1 45  SER 45  36  36  SER SER J . n 
J 1 46  LEU 46  37  37  LEU LEU J . n 
J 1 47  LEU 47  38  38  LEU LEU J . n 
J 1 48  ASP 48  39  39  ASP ASP J . n 
J 1 49  ILE 49  40  40  ILE ILE J . n 
J 1 50  VAL 50  41  41  VAL VAL J . n 
J 1 51  LYS 51  42  42  LYS LYS J . n 
J 1 52  ALA 52  43  43  ALA ALA J . n 
J 1 53  ASP 53  44  44  ASP ASP J . n 
J 1 54  SER 54  45  45  SER SER J . n 
J 1 55  SER 55  46  46  SER SER J . n 
J 1 56  THR 56  47  47  THR THR J . n 
J 1 57  ASN 57  48  48  ASN ASN J . n 
J 1 58  GLU 58  49  49  GLU GLU J . n 
J 1 59  VAL 59  50  50  VAL VAL J . n 
J 1 60  ASP 60  51  51  ASP ASP J . n 
J 1 61  LEU 61  52  52  LEU LEU J . n 
J 1 62  VAL 62  53  53  VAL VAL J . n 
J 1 63  TYR 63  54  54  TYR TYR J . n 
J 1 64  TRP 64  55  55  TRP TRP J . n 
J 1 65  GLU 65  56  56  GLU GLU J . n 
J 1 66  GLN 66  57  57  GLN GLN J . n 
J 1 67  GLN 67  58  58  GLN GLN J . n 
J 1 68  SER 68  59  59  SER SER J . n 
J 1 69  TRP 69  60  60  TRP TRP J . n 
J 1 70  LYS 70  61  61  LYS LYS J . n 
J 1 71  LEU 71  62  62  LEU LEU J . n 
J 1 72  ASN 72  63  63  ASN ASN J . n 
J 1 73  SER 73  64  64  SER SER J . n 
J 1 74  LEU 74  65  65  LEU LEU J . n 
J 1 75  MET 75  66  66  MET MET J . n 
J 1 76  TRP 76  67  67  TRP TRP J . n 
J 1 77  ASP 77  68  68  ASP ASP J . n 
J 1 78  PRO 78  69  69  PRO PRO J . n 
J 1 79  ASN 79  70  70  ASN ASN J . n 
J 1 80  GLU 80  71  71  GLU GLU J . n 
J 1 81  TYR 81  72  72  TYR TYR J . n 
J 1 82  GLY 82  73  73  GLY GLY J . n 
J 1 83  ASN 83  74  74  ASN ASN J . n 
J 1 84  ILE 84  75  75  ILE ILE J . n 
J 1 85  THR 85  76  76  THR THR J . n 
J 1 86  ASP 86  77  77  ASP ASP J . n 
J 1 87  PHE 87  78  78  PHE PHE J . n 
J 1 88  ARG 88  79  79  ARG ARG J . n 
J 1 89  THR 89  80  80  THR THR J . n 
J 1 90  SER 90  81  81  SER SER J . n 
J 1 91  ALA 91  82  82  ALA ALA J . n 
J 1 92  ALA 92  83  83  ALA ALA J . n 
J 1 93  ASP 93  84  84  ASP ASP J . n 
J 1 94  ILE 94  85  85  ILE ILE J . n 
J 1 95  TRP 95  86  86  TRP TRP J . n 
J 1 96  THR 96  87  87  THR THR J . n 
J 1 97  PRO 97  88  88  PRO PRO J . n 
J 1 98  ASP 98  89  89  ASP ASP J . n 
J 1 99  ILE 99  90  90  ILE ILE J . n 
J 1 100 THR 100 91  91  THR THR J . n 
J 1 101 ALA 101 92  92  ALA ALA J . n 
J 1 102 TYR 102 93  93  TYR TYR J . n 
J 1 103 SER 103 94  94  SER SER J . n 
J 1 104 SER 104 95  95  SER SER J . n 
J 1 105 THR 105 96  96  THR THR J . n 
J 1 106 ARG 106 97  97  ARG ARG J . n 
J 1 107 PRO 107 98  98  PRO PRO J . n 
J 1 108 VAL 108 99  99  VAL VAL J . n 
J 1 109 GLN 109 100 100 GLN GLN J . n 
J 1 110 VAL 110 101 101 VAL VAL J . n 
J 1 111 LEU 111 102 102 LEU LEU J . n 
J 1 112 SER 112 103 103 SER SER J . n 
J 1 113 PRO 113 104 104 PRO PRO J . n 
J 1 114 GLN 114 105 105 GLN GLN J . n 
J 1 115 ASN 115 106 106 ASN ASN J . n 
J 1 116 ALA 116 107 107 ALA ALA J . n 
J 1 117 LEU 117 108 108 LEU LEU J . n 
J 1 118 VAL 118 109 109 VAL VAL J . n 
J 1 119 ASN 119 110 110 ASN ASN J . n 
J 1 120 SER 120 111 111 SER SER J . n 
J 1 121 SER 121 112 112 SER SER J . n 
J 1 122 GLY 122 113 113 GLY GLY J . n 
J 1 123 HIS 123 114 114 HIS HIS J . n 
J 1 124 VAL 124 115 115 VAL VAL J . n 
J 1 125 GLN 125 116 116 GLN GLN J . n 
J 1 126 TYR 126 117 117 TYR TYR J . n 
J 1 127 LEU 127 118 118 LEU LEU J . n 
J 1 128 PRO 128 119 119 PRO PRO J . n 
J 1 129 ALA 129 120 120 ALA ALA J . n 
J 1 130 GLN 130 121 121 GLN GLN J . n 
J 1 131 ARG 131 122 122 ARG ARG J . n 
J 1 132 LEU 132 123 123 LEU LEU J . n 
J 1 133 SER 133 124 124 SER SER J . n 
J 1 134 PHE 134 125 125 PHE PHE J . n 
J 1 135 MET 135 126 126 MET MET J . n 
J 1 136 CYS 136 127 127 CYS CYS J . n 
J 1 137 ASP 137 128 128 ASP ASP J . n 
J 1 138 PRO 138 129 129 PRO PRO J . n 
J 1 139 THR 139 130 130 THR THR J . n 
J 1 140 GLY 140 131 131 GLY GLY J . n 
J 1 141 VAL 141 132 132 VAL VAL J . n 
J 1 142 ASP 142 133 133 ASP ASP J . n 
J 1 143 SER 143 134 134 SER SER J . n 
J 1 144 GLU 144 135 135 GLU GLU J . n 
J 1 145 GLU 145 136 136 GLU GLU J . n 
J 1 146 GLY 146 137 137 GLY GLY J . n 
J 1 147 ALA 147 138 138 ALA ALA J . n 
J 1 148 THR 148 139 139 THR THR J . n 
J 1 149 CYS 149 140 140 CYS CYS J . n 
J 1 150 ALA 150 141 141 ALA ALA J . n 
J 1 151 VAL 151 142 142 VAL VAL J . n 
J 1 152 LYS 152 143 143 LYS LYS J . n 
J 1 153 PHE 153 144 144 PHE PHE J . n 
J 1 154 GLY 154 145 145 GLY GLY J . n 
J 1 155 SER 155 146 146 SER SER J . n 
J 1 156 TRP 156 147 147 TRP TRP J . n 
J 1 157 SER 157 148 148 SER SER J . n 
J 1 158 TYR 158 149 149 TYR TYR J . n 
J 1 159 GLY 159 150 150 GLY GLY J . n 
J 1 160 GLY 160 151 151 GLY GLY J . n 
J 1 161 TRP 161 152 152 TRP TRP J . n 
J 1 162 GLU 162 153 153 GLU GLU J . n 
J 1 163 ILE 163 154 154 ILE ILE J . n 
J 1 164 ASP 164 155 155 ASP ASP J . n 
J 1 165 LEU 165 156 156 LEU LEU J . n 
J 1 166 LYS 166 157 157 LYS LYS J . n 
J 1 167 THR 167 158 158 THR THR J . n 
J 1 168 ASP 168 159 159 ASP ASP J . n 
J 1 169 THR 169 160 160 THR THR J . n 
J 1 170 ASP 170 161 161 ASP ASP J . n 
J 1 171 GLN 171 162 162 GLN GLN J . n 
J 1 172 VAL 172 163 163 VAL VAL J . n 
J 1 173 ASP 173 164 164 ASP ASP J . n 
J 1 174 LEU 174 165 165 LEU LEU J . n 
J 1 175 SER 175 166 166 SER SER J . n 
J 1 176 SER 176 167 167 SER SER J . n 
J 1 177 TYR 177 168 168 TYR TYR J . n 
J 1 178 TYR 178 169 169 TYR TYR J . n 
J 1 179 ALA 179 170 170 ALA ALA J . n 
J 1 180 SER 180 171 171 SER SER J . n 
J 1 181 SER 181 172 172 SER SER J . n 
J 1 182 LYS 182 173 173 LYS LYS J . n 
J 1 183 TYR 183 174 174 TYR TYR J . n 
J 1 184 GLU 184 175 175 GLU GLU J . n 
J 1 185 ILE 185 176 176 ILE ILE J . n 
J 1 186 LEU 186 177 177 LEU LEU J . n 
J 1 187 SER 187 178 178 SER SER J . n 
J 1 188 ALA 188 179 179 ALA ALA J . n 
J 1 189 THR 189 180 180 THR THR J . n 
J 1 190 GLN 190 181 181 GLN GLN J . n 
J 1 191 THR 191 182 182 THR THR J . n 
J 1 192 ARG 192 183 183 ARG ARG J . n 
J 1 193 SER 193 184 184 SER SER J . n 
J 1 194 GLU 194 185 185 GLU GLU J . n 
J 1 195 ARG 195 186 186 ARG ARG J . n 
J 1 196 PHE 196 187 187 PHE PHE J . n 
J 1 197 TYR 197 188 188 TYR TYR J . n 
J 1 198 GLU 198 189 189 GLU GLU J . n 
J 1 199 CYS 199 190 190 CYS CYS J . n 
J 1 200 CYS 200 191 191 CYS CYS J . n 
J 1 201 LYS 201 192 192 LYS LYS J . n 
J 1 202 GLU 202 193 193 GLU GLU J . n 
J 1 203 PRO 203 194 194 PRO PRO J . n 
J 1 204 TYR 204 195 195 TYR TYR J . n 
J 1 205 PRO 205 196 196 PRO PRO J . n 
J 1 206 ASP 206 197 197 ASP ASP J . n 
J 1 207 VAL 207 198 198 VAL VAL J . n 
J 1 208 ASN 208 199 199 ASN ASN J . n 
J 1 209 LEU 209 200 200 LEU LEU J . n 
J 1 210 VAL 210 201 201 VAL VAL J . n 
J 1 211 VAL 211 202 202 VAL VAL J . n 
J 1 212 LYS 212 203 203 LYS LYS J . n 
J 1 213 PHE 213 204 204 PHE PHE J . n 
J 1 214 ARG 214 205 205 ARG ARG J . n 
J 1 215 GLU 215 206 206 GLU GLU J . n 
J 1 216 ARG 216 207 207 ARG ARG J . n 
J 1 217 ARG 217 208 208 ARG ARG J . n 
J 1 218 ALA 218 209 ?   ?   ?   J . n 
J 1 219 GLY 219 210 ?   ?   ?   J . n 
J 1 220 ASN 220 211 ?   ?   ?   J . n 
J 1 221 GLY 221 212 ?   ?   ?   J . n 
J 1 222 PHE 222 213 ?   ?   ?   J . n 
J 1 223 PHE 223 214 ?   ?   ?   J . n 
J 1 224 ARG 224 215 ?   ?   ?   J . n 
J 1 225 ASN 225 216 ?   ?   ?   J . n 
J 1 226 LEU 226 217 ?   ?   ?   J . n 
J 1 227 PHE 227 218 ?   ?   ?   J . n 
J 1 228 ASP 228 219 ?   ?   ?   J . n 
J 1 229 SER 229 220 ?   ?   ?   J . n 
J 1 230 ARG 230 221 ?   ?   ?   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 MG  1  222 222 MG  MG  A . 
L  3 NAG 1  250 250 NAG NAG A . 
M  3 NAG 2  251 251 NAG NAG A . 
N  4 MLK 1  301 301 MLK MLK A . 
O  5 MRD 1  305 305 MRD MRD A . 
P  6 MPD 1  223 223 MPD MPD A . 
Q  6 MPD 1  306 306 MPD MPD A . 
R  2 MG  1  222 222 MG  MG  B . 
S  3 NAG 1  250 250 NAG NAG B . 
T  3 NAG 1  275 275 NAG NAG B . 
U  4 MLK 1  301 301 MLK MLK B . 
V  5 MRD 1  305 305 MRD MRD B . 
W  2 MG  1  222 222 MG  MG  C . 
X  3 NAG 1  250 250 NAG NAG C . 
Y  4 MLK 1  301 301 MLK MLK C . 
Z  6 MPD 1  306 306 MPD MPD C . 
AA 5 MRD 1  305 305 MRD MRD D . 
BA 3 NAG 1  250 250 NAG NAG D . 
CA 3 NAG 2  251 251 NAG NAG D . 
DA 4 MLK 1  301 301 MLK MLK D . 
EA 2 MG  1  222 222 MG  MG  E . 
FA 3 NAG 1  250 250 NAG NAG E . 
GA 3 NAG 2  251 251 NAG NAG E . 
HA 5 MRD 1  305 305 MRD MRD E . 
IA 3 NAG 1  275 275 NAG NAG E . 
JA 4 MLK 1  301 301 MLK MLK E . 
KA 5 MRD 1  305 305 MRD MRD F . 
LA 3 NAG 1  250 250 NAG NAG F . 
MA 4 MLK 1  301 301 MLK MLK F . 
NA 7 ACT 1  308 308 ACT ACT G . 
OA 3 NAG 1  250 250 NAG NAG G . 
PA 3 NAG 2  251 251 NAG NAG G . 
QA 4 MLK 1  301 301 MLK MLK G . 
RA 6 MPD 1  305 305 MPD MPD G . 
SA 6 MPD 1  222 222 MPD MPD G . 
TA 3 NAG 1  250 250 NAG NAG H . 
UA 3 NAG 2  251 251 NAG NAG H . 
VA 8 BMA 3  252 252 BMA BMA H . 
WA 4 MLK 1  301 301 MLK MLK H . 
XA 2 MG  1  222 222 MG  MG  I . 
YA 3 NAG 1  250 250 NAG NAG I . 
ZA 3 NAG 1  275 275 NAG NAG I . 
AB 4 MLK 1  301 301 MLK MLK I . 
BB 6 MPD 1  305 305 MPD MPD I . 
CB 6 MPD 1  305 305 MPD MPD J . 
DB 3 NAG 1  250 250 NAG NAG J . 
EB 3 NAG 2  251 251 NAG NAG J . 
FB 8 BMA 3  252 252 BMA BMA J . 
GB 4 MLK 1  301 301 MLK MLK J . 
HB 9 HOH 1  310 310 HOH HOH A . 
HB 9 HOH 2  311 311 HOH HOH A . 
HB 9 HOH 3  313 313 HOH HOH A . 
HB 9 HOH 4  314 314 HOH HOH A . 
HB 9 HOH 5  316 316 HOH HOH A . 
HB 9 HOH 6  317 317 HOH HOH A . 
HB 9 HOH 7  325 325 HOH HOH A . 
HB 9 HOH 8  327 327 HOH HOH A . 
HB 9 HOH 9  329 329 HOH HOH A . 
HB 9 HOH 10 330 330 HOH HOH A . 
HB 9 HOH 11 331 331 HOH HOH A . 
HB 9 HOH 12 332 332 HOH HOH A . 
IB 9 HOH 1  312 312 HOH HOH B . 
IB 9 HOH 2  320 320 HOH HOH B . 
IB 9 HOH 3  323 323 HOH HOH B . 
IB 9 HOH 4  324 324 HOH HOH B . 
IB 9 HOH 5  325 325 HOH HOH B . 
IB 9 HOH 6  327 327 HOH HOH B . 
IB 9 HOH 7  328 328 HOH HOH B . 
IB 9 HOH 8  329 329 HOH HOH B . 
IB 9 HOH 9  330 330 HOH HOH B . 
IB 9 HOH 10 331 331 HOH HOH B . 
IB 9 HOH 11 332 332 HOH HOH B . 
IB 9 HOH 12 333 333 HOH HOH B . 
JB 9 HOH 1  316 316 HOH HOH C . 
JB 9 HOH 2  320 320 HOH HOH C . 
JB 9 HOH 3  323 323 HOH HOH C . 
JB 9 HOH 4  324 324 HOH HOH C . 
JB 9 HOH 5  327 327 HOH HOH C . 
JB 9 HOH 6  333 333 HOH HOH C . 
JB 9 HOH 7  334 334 HOH HOH C . 
KB 9 HOH 1  318 318 HOH HOH D . 
KB 9 HOH 2  323 323 HOH HOH D . 
KB 9 HOH 3  327 327 HOH HOH D . 
LB 9 HOH 1  313 313 HOH HOH E . 
LB 9 HOH 2  316 316 HOH HOH E . 
LB 9 HOH 3  318 318 HOH HOH E . 
LB 9 HOH 4  320 320 HOH HOH E . 
LB 9 HOH 5  323 323 HOH HOH E . 
LB 9 HOH 6  325 325 HOH HOH E . 
LB 9 HOH 7  326 326 HOH HOH E . 
LB 9 HOH 8  327 327 HOH HOH E . 
LB 9 HOH 9  328 328 HOH HOH E . 
MB 9 HOH 1  320 320 HOH HOH F . 
MB 9 HOH 2  323 323 HOH HOH F . 
MB 9 HOH 3  325 325 HOH HOH F . 
MB 9 HOH 4  326 326 HOH HOH F . 
MB 9 HOH 5  327 327 HOH HOH F . 
NB 9 HOH 1  314 314 HOH HOH G . 
NB 9 HOH 2  320 320 HOH HOH G . 
NB 9 HOH 3  321 321 HOH HOH G . 
NB 9 HOH 4  323 323 HOH HOH G . 
NB 9 HOH 5  326 326 HOH HOH G . 
OB 9 HOH 1  323 323 HOH HOH H . 
OB 9 HOH 2  328 328 HOH HOH H . 
OB 9 HOH 3  336 336 HOH HOH H . 
OB 9 HOH 4  337 337 HOH HOH H . 
OB 9 HOH 5  338 338 HOH HOH H . 
PB 9 HOH 1  310 310 HOH HOH I . 
PB 9 HOH 2  315 315 HOH HOH I . 
PB 9 HOH 3  317 317 HOH HOH I . 
PB 9 HOH 4  326 326 HOH HOH I . 
PB 9 HOH 5  327 327 HOH HOH I . 
PB 9 HOH 6  333 333 HOH HOH I . 
PB 9 HOH 7  334 334 HOH HOH I . 
PB 9 HOH 8  335 335 HOH HOH I . 
QB 9 HOH 1  310 310 HOH HOH J . 
QB 9 HOH 2  316 316 HOH HOH J . 
QB 9 HOH 3  318 318 HOH HOH J . 
QB 9 HOH 4  323 323 HOH HOH J . 
QB 9 HOH 5  330 330 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  A ASN 119 A ASN 110 ? ASN 'GLYCOSYLATION SITE' 
2  B ASN 119 B ASN 110 ? ASN 'GLYCOSYLATION SITE' 
3  C ASN 119 C ASN 110 ? ASN 'GLYCOSYLATION SITE' 
4  D ASN 119 D ASN 110 ? ASN 'GLYCOSYLATION SITE' 
5  E ASN 119 E ASN 110 ? ASN 'GLYCOSYLATION SITE' 
6  F ASN 119 F ASN 110 ? ASN 'GLYCOSYLATION SITE' 
7  G ASN 119 G ASN 110 ? ASN 'GLYCOSYLATION SITE' 
8  H ASN 119 H ASN 110 ? ASN 'GLYCOSYLATION SITE' 
9  I ASN 119 I ASN 110 ? ASN 'GLYCOSYLATION SITE' 
10 J ASN 119 J ASN 110 ? ASN 'GLYCOSYLATION SITE' 
11 B ASN 83  B ASN 74  ? ASN 'GLYCOSYLATION SITE' 
12 E ASN 83  E ASN 74  ? ASN 'GLYCOSYLATION SITE' 
13 I ASN 83  I ASN 74  ? 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,GA,HA,IA,JA,HB,IB,JB,KB,LB        
2 1 F,G,H,I,J,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,AB,BB,CB,DB,EB,FB,GB,MB,NB,OB,PB,QB 
# 
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)' 24050 ? 
1 MORE         -54   ? 
1 'SSA (A^2)'  46090 ? 
2 'ABSA (A^2)' 23650 ? 
2 MORE         -78   ? 
2 'SSA (A^2)'  45760 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD2 ? G ASP 6 ? G ASP -3 ? 1_555 MG ? K  MG . ? A MG 222 ? 1_555 OD2 ? A ASP 6 ? A ASP -3 ? 1_555 113.7 ? 
2  OD2 ? G ASP 6 ? G ASP -3 ? 1_555 MG ? K  MG . ? A MG 222 ? 1_555 OD1 ? G ASP 6 ? G ASP -3 ? 1_555 60.8  ? 
3  OD2 ? A ASP 6 ? A ASP -3 ? 1_555 MG ? K  MG . ? A MG 222 ? 1_555 OD1 ? G ASP 6 ? G ASP -3 ? 1_555 102.8 ? 
4  OD2 ? G ASP 6 ? G ASP -3 ? 1_555 MG ? K  MG . ? A MG 222 ? 1_555 OD1 ? A ASP 6 ? A ASP -3 ? 1_555 130.6 ? 
5  OD2 ? A ASP 6 ? A ASP -3 ? 1_555 MG ? K  MG . ? A MG 222 ? 1_555 OD1 ? A ASP 6 ? A ASP -3 ? 1_555 58.1  ? 
6  OD1 ? G ASP 6 ? G ASP -3 ? 1_555 MG ? K  MG . ? A MG 222 ? 1_555 OD1 ? A ASP 6 ? A ASP -3 ? 1_555 159.6 ? 
7  OD2 ? I ASP 6 ? I ASP -3 ? 1_555 MG ? XA MG . ? I MG 222 ? 1_555 OD1 ? D ASP 6 ? D ASP -3 ? 1_555 126.1 ? 
8  OD2 ? I ASP 6 ? I ASP -3 ? 1_555 MG ? XA MG . ? I MG 222 ? 1_555 OD1 ? I ASP 6 ? I ASP -3 ? 1_555 56.2  ? 
9  OD1 ? D ASP 6 ? D ASP -3 ? 1_555 MG ? XA MG . ? I MG 222 ? 1_555 OD1 ? I ASP 6 ? I ASP -3 ? 1_555 151.0 ? 
10 OD2 ? I ASP 6 ? I ASP -3 ? 1_555 MG ? XA MG . ? I MG 222 ? 1_555 OD2 ? D ASP 6 ? D ASP -3 ? 1_555 119.7 ? 
11 OD1 ? D ASP 6 ? D ASP -3 ? 1_555 MG ? XA MG . ? I MG 222 ? 1_555 OD2 ? D ASP 6 ? D ASP -3 ? 1_555 52.5  ? 
12 OD1 ? I ASP 6 ? I ASP -3 ? 1_555 MG ? XA MG . ? I MG 222 ? 1_555 OD2 ? D ASP 6 ? D ASP -3 ? 1_555 156.2 ? 
13 OD2 ? J ASP 6 ? J ASP -3 ? 1_555 MG ? W  MG . ? C MG 222 ? 1_555 OD2 ? C ASP 6 ? C ASP -3 ? 1_555 77.7  ? 
14 OD2 ? J ASP 6 ? J ASP -3 ? 1_555 MG ? W  MG . ? C MG 222 ? 1_555 OD1 ? C ASP 6 ? C ASP -3 ? 1_555 126.8 ? 
15 OD2 ? C ASP 6 ? C ASP -3 ? 1_555 MG ? W  MG . ? C MG 222 ? 1_555 OD1 ? C ASP 6 ? C ASP -3 ? 1_555 56.9  ? 
16 OD2 ? J ASP 6 ? J ASP -3 ? 1_555 MG ? W  MG . ? C MG 222 ? 1_555 OD1 ? J ASP 6 ? J ASP -3 ? 1_555 54.7  ? 
17 OD2 ? C ASP 6 ? C ASP -3 ? 1_555 MG ? W  MG . ? C MG 222 ? 1_555 OD1 ? J ASP 6 ? J ASP -3 ? 1_555 114.5 ? 
18 OD1 ? C ASP 6 ? C ASP -3 ? 1_555 MG ? W  MG . ? C MG 222 ? 1_555 OD1 ? J ASP 6 ? J ASP -3 ? 1_555 166.2 ? 
19 OD2 ? F ASP 6 ? F ASP -3 ? 1_555 MG ? R  MG . ? B MG 222 ? 1_555 OD1 ? B ASP 6 ? B ASP -3 ? 1_555 136.8 ? 
20 OD2 ? F ASP 6 ? F ASP -3 ? 1_555 MG ? R  MG . ? B MG 222 ? 1_555 OD2 ? B ASP 6 ? B ASP -3 ? 1_555 81.1  ? 
21 OD1 ? B ASP 6 ? B ASP -3 ? 1_555 MG ? R  MG . ? B MG 222 ? 1_555 OD2 ? B ASP 6 ? B ASP -3 ? 1_555 57.8  ? 
22 OD2 ? F ASP 6 ? F ASP -3 ? 1_555 MG ? R  MG . ? B MG 222 ? 1_555 OD1 ? F ASP 6 ? F ASP -3 ? 1_555 56.2  ? 
23 OD1 ? B ASP 6 ? B ASP -3 ? 1_555 MG ? R  MG . ? B MG 222 ? 1_555 OD1 ? F ASP 6 ? F ASP -3 ? 1_555 162.4 ? 
24 OD2 ? B ASP 6 ? B ASP -3 ? 1_555 MG ? R  MG . ? B MG 222 ? 1_555 OD1 ? F ASP 6 ? F ASP -3 ? 1_555 137.3 ? 
25 OD2 ? H ASP 6 ? H ASP -3 ? 1_555 MG ? EA MG . ? E MG 222 ? 1_555 OD1 ? E ASP 6 ? E ASP -3 ? 1_555 89.5  ? 
26 OD2 ? H ASP 6 ? H ASP -3 ? 1_555 MG ? EA MG . ? E MG 222 ? 1_555 OD2 ? E ASP 6 ? E ASP -3 ? 1_555 121.1 ? 
27 OD1 ? E ASP 6 ? E ASP -3 ? 1_555 MG ? EA MG . ? E MG 222 ? 1_555 OD2 ? E ASP 6 ? E ASP -3 ? 1_555 52.9  ? 
28 OD2 ? H ASP 6 ? H ASP -3 ? 1_555 MG ? EA MG . ? E MG 222 ? 1_555 OD1 ? H ASP 6 ? H ASP -3 ? 1_555 49.2  ? 
29 OD1 ? E ASP 6 ? E ASP -3 ? 1_555 MG ? EA MG . ? E MG 222 ? 1_555 OD1 ? H ASP 6 ? H ASP -3 ? 1_555 138.6 ? 
30 OD2 ? E ASP 6 ? E ASP -3 ? 1_555 MG ? EA MG . ? E MG 222 ? 1_555 OD1 ? H ASP 6 ? H ASP -3 ? 1_555 145.1 ? 
# 
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 2011-10-26 
2 'Structure model' 1 1 2013-07-17 
3 'Structure model' 1 2 2017-11-08 
# 
_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' Advisory                 
3 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' pdbx_unobs_or_zero_occ_atoms 
2 3 'Structure model' software                     
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CCP4     'model building' 'Program Suite 6.1.3'      ? 1 
PHENIX   refinement       '(phenix.refine: 1.7_650)' ? 2 
HKL-2000 'data reduction' .                          ? 3 
HKL-2000 'data scaling'   .                          ? 4 
CCP4     phasing          'Program Suite 6.1.3'      ? 5 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             E 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              208 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             B 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             E 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              208 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             B 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             E 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              208 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                93.92 
_pdbx_validate_rmsd_angle.angle_target_value         110.40 
_pdbx_validate_rmsd_angle.angle_deviation            -16.48 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.00 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
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 ASN A 15 ? ? -132.70 -47.26 
2 1 TYR A 72 ? ? -144.44 19.52  
3 1 TYR C 72 ? ? -147.81 23.36  
4 1 ASN D 15 ? ? -126.38 -61.29 
5 1 LEU E 38 ? ? -121.11 -61.26 
6 1 LEU F 38 ? ? -123.36 -61.46 
7 1 ASN G 15 ? ? -129.96 -54.75 
8 1 ASN G 74 ? ? 70.32   35.81  
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C1 
_pdbx_validate_chiral.label_alt_id    B 
_pdbx_validate_chiral.auth_asym_id    I 
_pdbx_validate_chiral.auth_comp_id    NAG 
_pdbx_validate_chiral.auth_seq_id     275 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         'WRONG HAND' 
_pdbx_validate_chiral.omega           . 
# 
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 ASP -8  ? A ASP 1   
2   1 Y 1 A TYR -7  ? A TYR 2   
3   1 Y 1 A LYS -6  ? A LYS 3   
4   1 Y 1 A ALA 209 ? A ALA 218 
5   1 Y 1 A GLY 210 ? A GLY 219 
6   1 Y 1 A ASN 211 ? A ASN 220 
7   1 Y 1 A GLY 212 ? A GLY 221 
8   1 Y 1 A PHE 213 ? A PHE 222 
9   1 Y 1 A PHE 214 ? A PHE 223 
10  1 Y 1 A ARG 215 ? A ARG 224 
11  1 Y 1 A ASN 216 ? A ASN 225 
12  1 Y 1 A LEU 217 ? A LEU 226 
13  1 Y 1 A PHE 218 ? A PHE 227 
14  1 Y 1 A ASP 219 ? A ASP 228 
15  1 Y 1 A SER 220 ? A SER 229 
16  1 Y 1 A ARG 221 ? A ARG 230 
17  1 Y 1 B ASP -8  ? B ASP 1   
18  1 Y 1 B TYR -7  ? B TYR 2   
19  1 Y 1 B ALA 209 ? B ALA 218 
20  1 Y 1 B GLY 210 ? B GLY 219 
21  1 Y 1 B ASN 211 ? B ASN 220 
22  1 Y 1 B GLY 212 ? B GLY 221 
23  1 Y 1 B PHE 213 ? B PHE 222 
24  1 Y 1 B PHE 214 ? B PHE 223 
25  1 Y 1 B ARG 215 ? B ARG 224 
26  1 Y 1 B ASN 216 ? B ASN 225 
27  1 Y 1 B LEU 217 ? B LEU 226 
28  1 Y 1 B PHE 218 ? B PHE 227 
29  1 Y 1 B ASP 219 ? B ASP 228 
30  1 Y 1 B SER 220 ? B SER 229 
31  1 Y 1 B ARG 221 ? B ARG 230 
32  1 Y 1 C ASP -8  ? C ASP 1   
33  1 Y 1 C TYR -7  ? C TYR 2   
34  1 Y 1 C GLY 210 ? C GLY 219 
35  1 Y 1 C ASN 211 ? C ASN 220 
36  1 Y 1 C GLY 212 ? C GLY 221 
37  1 Y 1 C PHE 213 ? C PHE 222 
38  1 Y 1 C PHE 214 ? C PHE 223 
39  1 Y 1 C ARG 215 ? C ARG 224 
40  1 Y 1 C ASN 216 ? C ASN 225 
41  1 Y 1 C LEU 217 ? C LEU 226 
42  1 Y 1 C PHE 218 ? C PHE 227 
43  1 Y 1 C ASP 219 ? C ASP 228 
44  1 Y 1 C SER 220 ? C SER 229 
45  1 Y 1 C ARG 221 ? C ARG 230 
46  1 Y 1 D ASP -8  ? D ASP 1   
47  1 Y 1 D TYR -7  ? D TYR 2   
48  1 Y 1 D ARG 208 ? D ARG 217 
49  1 Y 1 D ALA 209 ? D ALA 218 
50  1 Y 1 D GLY 210 ? D GLY 219 
51  1 Y 1 D ASN 211 ? D ASN 220 
52  1 Y 1 D GLY 212 ? D GLY 221 
53  1 Y 1 D PHE 213 ? D PHE 222 
54  1 Y 1 D PHE 214 ? D PHE 223 
55  1 Y 1 D ARG 215 ? D ARG 224 
56  1 Y 1 D ASN 216 ? D ASN 225 
57  1 Y 1 D LEU 217 ? D LEU 226 
58  1 Y 1 D PHE 218 ? D PHE 227 
59  1 Y 1 D ASP 219 ? D ASP 228 
60  1 Y 1 D SER 220 ? D SER 229 
61  1 Y 1 D ARG 221 ? D ARG 230 
62  1 Y 1 E ASP -8  ? E ASP 1   
63  1 Y 1 E TYR -7  ? E TYR 2   
64  1 Y 1 E ALA 209 ? E ALA 218 
65  1 Y 1 E GLY 210 ? E GLY 219 
66  1 Y 1 E ASN 211 ? E ASN 220 
67  1 Y 1 E GLY 212 ? E GLY 221 
68  1 Y 1 E PHE 213 ? E PHE 222 
69  1 Y 1 E PHE 214 ? E PHE 223 
70  1 Y 1 E ARG 215 ? E ARG 224 
71  1 Y 1 E ASN 216 ? E ASN 225 
72  1 Y 1 E LEU 217 ? E LEU 226 
73  1 Y 1 E PHE 218 ? E PHE 227 
74  1 Y 1 E ASP 219 ? E ASP 228 
75  1 Y 1 E SER 220 ? E SER 229 
76  1 Y 1 E ARG 221 ? E ARG 230 
77  1 Y 1 F ASP -8  ? F ASP 1   
78  1 Y 1 F TYR -7  ? F TYR 2   
79  1 Y 1 F ARG 208 ? F ARG 217 
80  1 Y 1 F ALA 209 ? F ALA 218 
81  1 Y 1 F GLY 210 ? F GLY 219 
82  1 Y 1 F ASN 211 ? F ASN 220 
83  1 Y 1 F GLY 212 ? F GLY 221 
84  1 Y 1 F PHE 213 ? F PHE 222 
85  1 Y 1 F PHE 214 ? F PHE 223 
86  1 Y 1 F ARG 215 ? F ARG 224 
87  1 Y 1 F ASN 216 ? F ASN 225 
88  1 Y 1 F LEU 217 ? F LEU 226 
89  1 Y 1 F PHE 218 ? F PHE 227 
90  1 Y 1 F ASP 219 ? F ASP 228 
91  1 Y 1 F SER 220 ? F SER 229 
92  1 Y 1 F ARG 221 ? F ARG 230 
93  1 Y 1 G ASP -8  ? G ASP 1   
94  1 Y 1 G TYR -7  ? G TYR 2   
95  1 Y 1 G ARG 208 ? G ARG 217 
96  1 Y 1 G ALA 209 ? G ALA 218 
97  1 Y 1 G GLY 210 ? G GLY 219 
98  1 Y 1 G ASN 211 ? G ASN 220 
99  1 Y 1 G GLY 212 ? G GLY 221 
100 1 Y 1 G PHE 213 ? G PHE 222 
101 1 Y 1 G PHE 214 ? G PHE 223 
102 1 Y 1 G ARG 215 ? G ARG 224 
103 1 Y 1 G ASN 216 ? G ASN 225 
104 1 Y 1 G LEU 217 ? G LEU 226 
105 1 Y 1 G PHE 218 ? G PHE 227 
106 1 Y 1 G ASP 219 ? G ASP 228 
107 1 Y 1 G SER 220 ? G SER 229 
108 1 Y 1 G ARG 221 ? G ARG 230 
109 1 Y 1 H ASP -8  ? H ASP 1   
110 1 Y 1 H TYR -7  ? H TYR 2   
111 1 Y 1 H ALA 209 ? H ALA 218 
112 1 Y 1 H GLY 210 ? H GLY 219 
113 1 Y 1 H ASN 211 ? H ASN 220 
114 1 Y 1 H GLY 212 ? H GLY 221 
115 1 Y 1 H PHE 213 ? H PHE 222 
116 1 Y 1 H PHE 214 ? H PHE 223 
117 1 Y 1 H ARG 215 ? H ARG 224 
118 1 Y 1 H ASN 216 ? H ASN 225 
119 1 Y 1 H LEU 217 ? H LEU 226 
120 1 Y 1 H PHE 218 ? H PHE 227 
121 1 Y 1 H ASP 219 ? H ASP 228 
122 1 Y 1 H SER 220 ? H SER 229 
123 1 Y 1 H ARG 221 ? H ARG 230 
124 1 Y 1 I ASP -8  ? I ASP 1   
125 1 Y 1 I TYR -7  ? I TYR 2   
126 1 Y 1 I LYS -6  ? I LYS 3   
127 1 Y 1 I ALA 209 ? I ALA 218 
128 1 Y 1 I GLY 210 ? I GLY 219 
129 1 Y 1 I ASN 211 ? I ASN 220 
130 1 Y 1 I GLY 212 ? I GLY 221 
131 1 Y 1 I PHE 213 ? I PHE 222 
132 1 Y 1 I PHE 214 ? I PHE 223 
133 1 Y 1 I ARG 215 ? I ARG 224 
134 1 Y 1 I ASN 216 ? I ASN 225 
135 1 Y 1 I LEU 217 ? I LEU 226 
136 1 Y 1 I PHE 218 ? I PHE 227 
137 1 Y 1 I ASP 219 ? I ASP 228 
138 1 Y 1 I SER 220 ? I SER 229 
139 1 Y 1 I ARG 221 ? I ARG 230 
140 1 Y 1 J ASP -8  ? J ASP 1   
141 1 Y 1 J TYR -7  ? J TYR 2   
142 1 Y 1 J ALA 209 ? J ALA 218 
143 1 Y 1 J GLY 210 ? J GLY 219 
144 1 Y 1 J ASN 211 ? J ASN 220 
145 1 Y 1 J GLY 212 ? J GLY 221 
146 1 Y 1 J PHE 213 ? J PHE 222 
147 1 Y 1 J PHE 214 ? J PHE 223 
148 1 Y 1 J ARG 215 ? J ARG 224 
149 1 Y 1 J ASN 216 ? J ASN 225 
150 1 Y 1 J LEU 217 ? J LEU 226 
151 1 Y 1 J PHE 218 ? J PHE 227 
152 1 Y 1 J ASP 219 ? J ASP 228 
153 1 Y 1 J SER 220 ? J SER 229 
154 1 Y 1 J ARG 221 ? J ARG 230 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MAGNESIUM ION'                 MG  
3 N-ACETYL-D-GLUCOSAMINE          NAG 
4 METHYLLYCACONITINE              MLK 
5 '(4R)-2-METHYLPENTANE-2,4-DIOL' MRD 
6 '(4S)-2-METHYL-2,4-PENTANEDIOL' MPD 
7 'ACETATE ION'                   ACT 
8 BETA-D-MANNOSE                  BMA 
9 water                           HOH 
# 
