data_5EUK
# 
_entry.id   5EUK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.288 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5EUK         
WWPDB D_1000215532 
# 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.db_id          5ESQ 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        . 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5EUK 
_pdbx_database_status.recvd_initial_deposition_date   2015-11-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Bzymek, K.P.'   1 
'Williams, J.C.' 2 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acta Crystallogr F Struct Biol Commun' 
_citation.journal_id_ASTM           ACSFEN 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2053-230X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            72 
_citation.language                  ? 
_citation.page_first                820 
_citation.page_last                 830 
_citation.title                     
'Natural and non-natural amino-acid side-chain substitutions: affinity and diffraction studies of meditope-Fab complexes.' 
_citation.year                      2016 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1107/S2053230X16016149 
_citation.pdbx_database_id_PubMed   27834791 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Bzymek, K.P.'   1 
primary 'Avery, K.A.'    2 
primary 'Ma, Y.'         3 
primary 'Horne, D.A.'    4 
primary 'Williams, J.C.' 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5EUK 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.930 
_cell.length_a_esd                 ? 
_cell.length_b                     82.060 
_cell.length_b_esd                 ? 
_cell.length_c                     212.090 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         5EUK 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Cetuximab Fab light chain' 23287.705 2   ? ? ? ? 
2 polymer     man 'Cetuximab Fab heavy chain' 23638.426 2   ? ? ? ? 
3 polymer     syn 'F3H meditope'              1463.729  2   ? ? ? ? 
4 non-polymer syn 'PHOSPHATE ION'             94.971    4   ? ? ? ? 
5 non-polymer man N-ACETYL-D-GLUCOSAMINE      221.208   2   ? ? ? ? 
6 non-polymer syn MESO-ERYTHRITOL             122.120   1   ? ? ? ? 
7 water       nat water                       18.015    410 ? ? ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;DILLTQSPVILSVSPGERVSFSCRASQSIGTNIHWYQQRTNGSPRLLIKYASESISGIPSRFSGSGSGTDFTLSINSVES
EDIADYYCQQNNNWPTTFGAGTKLELKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGA
;
;DILLTQSPVILSVSPGERVSFSCRASQSIGTNIHWYQQRTNGSPRLLIKYASESISGIPSRFSGSGSGTDFTLSINSVES
EDIADYYCQQNNNWPTTFGAGTKLELKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGA
;
A,C ? 
2 'polypeptide(L)' no no 
;QVQLKQSGPGLVQPSQSLSITCTVSGFSLTNYGVHWVRQSPGKGLEWLGVIWSGGNTDYNTPFTSRLSINKDNSKSQVFF
KMNSLQSNDTAIYYCARALTYYDYEFAYWGQGTLVTVSAASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSW
NSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPK
;
;QVQLKQSGPGLVQPSQSLSITCTVSGFSLTNYGVHWVRQSPGKGLEWLGVIWSGGNTDYNTPFTSRLSINKDNSKSQVFF
KMNSLQSNDTAIYYCARALTYYDYEFAYWGQGTLVTVSAASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSW
NSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPK
;
B,D ? 
3 'polypeptide(L)' no no CQHDLSTRRLKC CQHDLSTRRLKC E,F ? 
# 
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   ILE n 
1 3   LEU n 
1 4   LEU n 
1 5   THR n 
1 6   GLN n 
1 7   SER n 
1 8   PRO n 
1 9   VAL n 
1 10  ILE n 
1 11  LEU n 
1 12  SER n 
1 13  VAL n 
1 14  SER n 
1 15  PRO n 
1 16  GLY n 
1 17  GLU n 
1 18  ARG n 
1 19  VAL n 
1 20  SER n 
1 21  PHE n 
1 22  SER n 
1 23  CYS n 
1 24  ARG n 
1 25  ALA n 
1 26  SER n 
1 27  GLN n 
1 28  SER n 
1 29  ILE n 
1 30  GLY n 
1 31  THR n 
1 32  ASN n 
1 33  ILE n 
1 34  HIS n 
1 35  TRP n 
1 36  TYR n 
1 37  GLN n 
1 38  GLN n 
1 39  ARG n 
1 40  THR n 
1 41  ASN n 
1 42  GLY n 
1 43  SER n 
1 44  PRO n 
1 45  ARG n 
1 46  LEU n 
1 47  LEU n 
1 48  ILE n 
1 49  LYS n 
1 50  TYR n 
1 51  ALA n 
1 52  SER n 
1 53  GLU n 
1 54  SER n 
1 55  ILE n 
1 56  SER n 
1 57  GLY n 
1 58  ILE n 
1 59  PRO n 
1 60  SER n 
1 61  ARG n 
1 62  PHE n 
1 63  SER n 
1 64  GLY n 
1 65  SER n 
1 66  GLY n 
1 67  SER n 
1 68  GLY n 
1 69  THR n 
1 70  ASP n 
1 71  PHE n 
1 72  THR n 
1 73  LEU n 
1 74  SER n 
1 75  ILE n 
1 76  ASN n 
1 77  SER n 
1 78  VAL n 
1 79  GLU n 
1 80  SER n 
1 81  GLU n 
1 82  ASP n 
1 83  ILE n 
1 84  ALA n 
1 85  ASP n 
1 86  TYR n 
1 87  TYR n 
1 88  CYS n 
1 89  GLN n 
1 90  GLN n 
1 91  ASN n 
1 92  ASN n 
1 93  ASN n 
1 94  TRP n 
1 95  PRO n 
1 96  THR n 
1 97  THR n 
1 98  PHE n 
1 99  GLY n 
1 100 ALA n 
1 101 GLY n 
1 102 THR n 
1 103 LYS n 
1 104 LEU n 
1 105 GLU n 
1 106 LEU n 
1 107 LYS n 
1 108 ARG n 
1 109 THR n 
1 110 VAL n 
1 111 ALA n 
1 112 ALA n 
1 113 PRO n 
1 114 SER n 
1 115 VAL n 
1 116 PHE n 
1 117 ILE n 
1 118 PHE n 
1 119 PRO n 
1 120 PRO n 
1 121 SER n 
1 122 ASP n 
1 123 GLU n 
1 124 GLN n 
1 125 LEU n 
1 126 LYS n 
1 127 SER n 
1 128 GLY n 
1 129 THR n 
1 130 ALA n 
1 131 SER n 
1 132 VAL n 
1 133 VAL n 
1 134 CYS n 
1 135 LEU n 
1 136 LEU n 
1 137 ASN n 
1 138 ASN n 
1 139 PHE n 
1 140 TYR n 
1 141 PRO n 
1 142 ARG n 
1 143 GLU n 
1 144 ALA n 
1 145 LYS n 
1 146 VAL n 
1 147 GLN n 
1 148 TRP n 
1 149 LYS n 
1 150 VAL n 
1 151 ASP n 
1 152 ASN n 
1 153 ALA n 
1 154 LEU n 
1 155 GLN n 
1 156 SER n 
1 157 GLY n 
1 158 ASN n 
1 159 SER n 
1 160 GLN n 
1 161 GLU n 
1 162 SER n 
1 163 VAL n 
1 164 THR n 
1 165 GLU n 
1 166 GLN n 
1 167 ASP n 
1 168 SER n 
1 169 LYS n 
1 170 ASP n 
1 171 SER n 
1 172 THR n 
1 173 TYR n 
1 174 SER n 
1 175 LEU n 
1 176 SER n 
1 177 SER n 
1 178 THR n 
1 179 LEU n 
1 180 THR n 
1 181 LEU n 
1 182 SER n 
1 183 LYS n 
1 184 ALA n 
1 185 ASP n 
1 186 TYR n 
1 187 GLU n 
1 188 LYS n 
1 189 HIS n 
1 190 LYS n 
1 191 VAL n 
1 192 TYR n 
1 193 ALA n 
1 194 CYS n 
1 195 GLU n 
1 196 VAL n 
1 197 THR n 
1 198 HIS n 
1 199 GLN n 
1 200 GLY n 
1 201 LEU n 
1 202 SER n 
1 203 SER n 
1 204 PRO n 
1 205 VAL n 
1 206 THR n 
1 207 LYS n 
1 208 SER n 
1 209 PHE n 
1 210 ASN n 
1 211 ARG n 
1 212 GLY n 
1 213 ALA n 
2 1   GLN n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   LYS n 
2 6   GLN n 
2 7   SER n 
2 8   GLY n 
2 9   PRO n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  PRO n 
2 15  SER n 
2 16  GLN n 
2 17  SER n 
2 18  LEU n 
2 19  SER n 
2 20  ILE n 
2 21  THR n 
2 22  CYS n 
2 23  THR n 
2 24  VAL n 
2 25  SER n 
2 26  GLY n 
2 27  PHE n 
2 28  SER n 
2 29  LEU n 
2 30  THR n 
2 31  ASN n 
2 32  TYR n 
2 33  GLY n 
2 34  VAL n 
2 35  HIS n 
2 36  TRP n 
2 37  VAL n 
2 38  ARG n 
2 39  GLN n 
2 40  SER n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TRP n 
2 48  LEU n 
2 49  GLY n 
2 50  VAL n 
2 51  ILE n 
2 52  TRP n 
2 53  SER n 
2 54  GLY n 
2 55  GLY n 
2 56  ASN n 
2 57  THR n 
2 58  ASP n 
2 59  TYR n 
2 60  ASN n 
2 61  THR n 
2 62  PRO n 
2 63  PHE n 
2 64  THR n 
2 65  SER n 
2 66  ARG n 
2 67  LEU n 
2 68  SER n 
2 69  ILE n 
2 70  ASN n 
2 71  LYS n 
2 72  ASP n 
2 73  ASN n 
2 74  SER n 
2 75  LYS n 
2 76  SER n 
2 77  GLN n 
2 78  VAL n 
2 79  PHE n 
2 80  PHE n 
2 81  LYS n 
2 82  MET n 
2 83  ASN n 
2 84  SER n 
2 85  LEU n 
2 86  GLN n 
2 87  SER n 
2 88  ASN n 
2 89  ASP n 
2 90  THR n 
2 91  ALA n 
2 92  ILE n 
2 93  TYR n 
2 94  TYR n 
2 95  CYS n 
2 96  ALA n 
2 97  ARG n 
2 98  ALA n 
2 99  LEU n 
2 100 THR n 
2 101 TYR n 
2 102 TYR n 
2 103 ASP n 
2 104 TYR n 
2 105 GLU n 
2 106 PHE n 
2 107 ALA n 
2 108 TYR n 
2 109 TRP n 
2 110 GLY n 
2 111 GLN n 
2 112 GLY n 
2 113 THR n 
2 114 LEU n 
2 115 VAL n 
2 116 THR n 
2 117 VAL n 
2 118 SER n 
2 119 ALA n 
2 120 ALA n 
2 121 SER n 
2 122 THR n 
2 123 LYS n 
2 124 GLY n 
2 125 PRO n 
2 126 SER n 
2 127 VAL n 
2 128 PHE n 
2 129 PRO n 
2 130 LEU n 
2 131 ALA n 
2 132 PRO n 
2 133 SER n 
2 134 SER n 
2 135 LYS n 
2 136 SER n 
2 137 THR n 
2 138 SER n 
2 139 GLY n 
2 140 GLY n 
2 141 THR n 
2 142 ALA n 
2 143 ALA n 
2 144 LEU n 
2 145 GLY n 
2 146 CYS n 
2 147 LEU n 
2 148 VAL n 
2 149 LYS n 
2 150 ASP n 
2 151 TYR n 
2 152 PHE n 
2 153 PRO n 
2 154 GLU n 
2 155 PRO n 
2 156 VAL n 
2 157 THR n 
2 158 VAL n 
2 159 SER n 
2 160 TRP n 
2 161 ASN n 
2 162 SER n 
2 163 GLY n 
2 164 ALA n 
2 165 LEU n 
2 166 THR n 
2 167 SER n 
2 168 GLY n 
2 169 VAL n 
2 170 HIS n 
2 171 THR n 
2 172 PHE n 
2 173 PRO n 
2 174 ALA n 
2 175 VAL n 
2 176 LEU n 
2 177 GLN n 
2 178 SER n 
2 179 SER n 
2 180 GLY n 
2 181 LEU n 
2 182 TYR n 
2 183 SER n 
2 184 LEU n 
2 185 SER n 
2 186 SER n 
2 187 VAL n 
2 188 VAL n 
2 189 THR n 
2 190 VAL n 
2 191 PRO n 
2 192 SER n 
2 193 SER n 
2 194 SER n 
2 195 LEU n 
2 196 GLY n 
2 197 THR n 
2 198 GLN n 
2 199 THR n 
2 200 TYR n 
2 201 ILE n 
2 202 CYS n 
2 203 ASN n 
2 204 VAL n 
2 205 ASN n 
2 206 HIS n 
2 207 LYS n 
2 208 PRO n 
2 209 SER n 
2 210 ASN n 
2 211 THR n 
2 212 LYS n 
2 213 VAL n 
2 214 ASP n 
2 215 LYS n 
2 216 ARG n 
2 217 VAL n 
2 218 GLU n 
2 219 PRO n 
2 220 LYS n 
3 1   CYS n 
3 2   GLN n 
3 3   HIS n 
3 4   ASP n 
3 5   LEU n 
3 6   SER n 
3 7   THR n 
3 8   ARG n 
3 9   ARG n 
3 10  LEU n 
3 11  LYS n 
3 12  CYS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 213 'mouse, human' ? ? ? ? ? ? ? ? 'MUS MUSCULUS, HOMO SAPIENS' '10090, 9606' ? ? ? ? ? ? ? ? 
unidentified 32644 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 220 'mouse, human' ? ? ? ? ? ? ? ? 'MUS MUSCULUS, HOMO SAPIENS' '10090, 9606' ? ? ? ? ? ? ? ? 
unidentified 32644 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_src_syn.entity_id              3 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       ? 
_pdbx_entity_src_syn.pdbx_end_seq_num       ? 
_pdbx_entity_src_syn.organism_scientific    'synthetic construct' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       32630 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 5EUK 5EUK ? 1 ? 1 
2 PDB 5EUK 5EUK ? 2 ? 1 
3 PDB 5EUK 5EUK ? 3 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5EUK A 1 ? 213 ? 5EUK 1 ? 213 ? 1 213 
2 2 5EUK B 1 ? 220 ? 5EUK 1 ? 220 ? 1 220 
3 1 5EUK C 1 ? 213 ? 5EUK 1 ? 213 ? 1 213 
4 2 5EUK D 1 ? 220 ? 5EUK 1 ? 220 ? 1 220 
5 3 5EUK E 1 ? 12  ? 5EUK 1 ? 12  ? 1 12  
6 3 5EUK F 1 ? 12  ? 5EUK 1 ? 12  ? 1 12  
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
MRY non-polymer         . MESO-ERYTHRITOL        ? 'C4 H10 O4'      122.120 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION'        ? 'O4 P -3'        94.971  
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'    117.146 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   5EUK 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.87 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         57.20 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.3 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.1 M citric acid, 0.1 M sodium phosphate dibasic, 0.4 M potassium phosphate dibasic, 1.6 M sodium phosphate monobasic' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RIGAKU RAXIS IV++' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-10-07 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5EUK 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                2.50 
_reflns.d_resolution_low                 32.83 
_reflns.details                          ? 
_reflns.limit_h_max                      ? 
_reflns.limit_h_min                      ? 
_reflns.limit_k_max                      ? 
_reflns.limit_k_min                      ? 
_reflns.limit_l_max                      ? 
_reflns.limit_l_min                      ? 
_reflns.number_all                       ? 
_reflns.number_obs                       39428 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.2 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.8 
_reflns.pdbx_Rmerge_I_obs                0.126 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            11.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  2.5 
_reflns_shell.d_res_low                   2.56 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         1.8 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.percent_possible_all        92.9 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                0.775 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             3.0 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 5EUK 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.50 
_refine.ls_d_res_low                             32.83 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     39421 
_refine.ls_number_reflns_R_free                  1971 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.20 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1746 
_refine.ls_R_factor_R_free                       0.2337 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1714 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4GW1 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.27 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.35 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        6744 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_refine_hist.number_atoms_solvent             410 
_refine_hist.number_atoms_total               7210 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        32.83 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 6987 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.193  ? 9507 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 13.455 ? 2492 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.078  ? 1080 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 1212 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 2.4950 2.5574  . . 130 2476 93.00  . . . 0.3686 . 0.2567 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.5574 2.6265  . . 138 2611 100.00 . . . 0.2969 . 0.2215 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.6265 2.7038  . . 139 2651 100.00 . . . 0.2817 . 0.2155 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.7038 2.7910  . . 141 2663 100.00 . . . 0.2895 . 0.2106 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.7910 2.8907  . . 140 2671 100.00 . . . 0.3005 . 0.2064 . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.8907 3.0064  . . 138 2623 100.00 . . . 0.2696 . 0.1914 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.0064 3.1431  . . 143 2704 100.00 . . . 0.2389 . 0.1800 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.1431 3.3086  . . 140 2663 100.00 . . . 0.2312 . 0.1750 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.3086 3.5157  . . 140 2663 100.00 . . . 0.2261 . 0.1609 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.5157 3.7868  . . 142 2695 100.00 . . . 0.2237 . 0.1572 . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.7868 4.1672  . . 142 2700 100.00 . . . 0.2213 . 0.1483 . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.1672 4.7686  . . 143 2720 100.00 . . . 0.1850 . 0.1262 . . . . . . . . . . 
'X-RAY DIFFRACTION' 4.7686 6.0020  . . 145 2752 100.00 . . . 0.1860 . 0.1500 . . . . . . . . . . 
'X-RAY DIFFRACTION' 6.0020 32.8363 . . 150 2858 98.00  . . . 0.2179 . 0.1838 . . . . . . . . . . 
# 
_struct.entry_id                     5EUK 
_struct.title                        'Cetuximab Fab in complex with F3H meditope variant' 
_struct.pdbx_descriptor              'Cetuximab Fab light chain, Cetuximab Fab heavy chain, F3H meditope' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        5EUK 
_struct_keywords.text            'antibody, anti-EGFR, immune system' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
J N N 4 ? 
K N N 6 ? 
L N N 5 ? 
M N N 4 ? 
N N N 7 ? 
O N N 7 ? 
P N N 7 ? 
Q N N 7 ? 
R N N 7 ? 
S N N 7 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 79  ? ILE A 83  ? GLU A 79  ILE A 83  5 ? 5 
HELX_P HELX_P2  AA2 SER A 121 ? LYS A 126 ? SER A 121 LYS A 126 1 ? 6 
HELX_P HELX_P3  AA3 LYS A 183 ? LYS A 188 ? LYS A 183 LYS A 188 1 ? 6 
HELX_P HELX_P4  AA4 THR B 61  ? THR B 64  ? THR B 61  THR B 64  5 ? 4 
HELX_P HELX_P5  AA5 GLN B 86  ? THR B 90  ? GLN B 86  THR B 90  5 ? 5 
HELX_P HELX_P6  AA6 SER B 162 ? ALA B 164 ? SER B 162 ALA B 164 5 ? 3 
HELX_P HELX_P7  AA7 SER B 193 ? LEU B 195 ? SER B 193 LEU B 195 5 ? 3 
HELX_P HELX_P8  AA8 LYS B 207 ? ASN B 210 ? LYS B 207 ASN B 210 5 ? 4 
HELX_P HELX_P9  AA9 GLU C 79  ? ILE C 83  ? GLU C 79  ILE C 83  5 ? 5 
HELX_P HELX_P10 AB1 SER C 121 ? LYS C 126 ? SER C 121 LYS C 126 1 ? 6 
HELX_P HELX_P11 AB2 LYS C 183 ? LYS C 188 ? LYS C 183 LYS C 188 1 ? 6 
HELX_P HELX_P12 AB3 THR D 61  ? THR D 64  ? THR D 61  THR D 64  5 ? 4 
HELX_P HELX_P13 AB4 GLN D 86  ? THR D 90  ? GLN D 86  THR D 90  5 ? 5 
HELX_P HELX_P14 AB5 SER D 162 ? ALA D 164 ? SER D 162 ALA D 164 5 ? 3 
HELX_P HELX_P15 AB6 SER D 193 ? LEU D 195 ? SER D 193 LEU D 195 5 ? 3 
HELX_P HELX_P16 AB7 LYS D 207 ? ASN D 210 ? LYS D 207 ASN D 210 5 ? 4 
# 
_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 23  SG  ? ? ? 1_555 A CYS 88  SG ? ? A CYS 23  A CYS 88  1_555 ? ? ? ? ? ? ? 2.063 ? 
disulf2  disulf ?   ? A CYS 134 SG  ? ? ? 1_555 A CYS 194 SG ? ? A CYS 134 A CYS 194 1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf3  disulf ?   ? B CYS 22  SG  ? ? ? 1_555 B CYS 95  SG ? ? B CYS 22  B CYS 95  1_555 ? ? ? ? ? ? ? 2.066 ? 
disulf4  disulf ?   ? B CYS 146 SG  ? ? ? 1_555 B CYS 202 SG ? ? B CYS 146 B CYS 202 1_555 ? ? ? ? ? ? ? 2.012 ? 
disulf5  disulf ?   ? C CYS 23  SG  ? ? ? 1_555 C CYS 88  SG ? ? C CYS 23  C CYS 88  1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf6  disulf ?   ? C CYS 134 SG  ? ? ? 1_555 C CYS 194 SG ? ? C CYS 134 C CYS 194 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf7  disulf ?   ? D CYS 22  SG  ? ? ? 1_555 D CYS 95  SG ? ? D CYS 22  D CYS 95  1_555 ? ? ? ? ? ? ? 2.072 ? 
disulf8  disulf ?   ? D CYS 146 SG  ? ? ? 1_555 D CYS 202 SG ? ? D CYS 146 D CYS 202 1_555 ? ? ? ? ? ? ? 2.040 ? 
disulf9  disulf ?   ? E CYS 1   SG  ? ? ? 1_555 E CYS 12  SG ? ? E CYS 1   E CYS 12  1_555 ? ? ? ? ? ? ? 2.031 ? 
disulf10 disulf ?   ? F CYS 1   SG  ? ? ? 1_555 F CYS 12  SG ? ? F CYS 1   F CYS 12  1_555 ? ? ? ? ? ? ? 2.034 ? 
covale1  covale one ? B ASN 88  ND2 ? ? ? 1_555 I NAG .   C1 ? ? B ASN 88  B NAG 301 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale2  covale one ? D ASN 88  ND2 ? ? ? 1_555 L NAG .   C1 ? ? D ASN 88  D NAG 301 1_555 ? ? ? ? ? ? ? 1.444 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  SER 7   A . ? SER 7   A PRO 8   A ? PRO 8   A 1 -10.20 
2  TRP 94  A . ? TRP 94  A PRO 95  A ? PRO 95  A 1 -0.36  
3  TYR 140 A . ? TYR 140 A PRO 141 A ? PRO 141 A 1 9.68   
4  PHE 152 B . ? PHE 152 B PRO 153 B ? PRO 153 B 1 -8.37  
5  GLU 154 B . ? GLU 154 B PRO 155 B ? PRO 155 B 1 0.34   
6  SER 7   C . ? SER 7   C PRO 8   C ? PRO 8   C 1 -0.82  
7  TRP 94  C . ? TRP 94  C PRO 95  C ? PRO 95  C 1 5.17   
8  TYR 140 C . ? TYR 140 C PRO 141 C ? PRO 141 C 1 5.33   
9  PHE 152 D . ? PHE 152 D PRO 153 D ? PRO 153 D 1 -4.30  
10 GLU 154 D . ? GLU 154 D PRO 155 D ? PRO 155 D 1 -5.33  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 5 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 6 ? 
AA8 ? 4 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 3 ? 
AB3 ? 4 ? 
AB4 ? 6 ? 
AB5 ? 4 ? 
AB6 ? 4 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 6 ? 
AC1 ? 4 ? 
AC2 ? 4 ? 
AC3 ? 4 ? 
AC4 ? 3 ? 
AC5 ? 2 ? 
AC6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB8 3 4 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AB9 5 6 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 4   ? SER A 7   ? LEU A 4   SER A 7   
AA1 2 VAL A 19  ? ALA A 25  ? VAL A 19  ALA A 25  
AA1 3 ASP A 70  ? ILE A 75  ? ASP A 70  ILE A 75  
AA1 4 PHE A 62  ? SER A 67  ? PHE A 62  SER A 67  
AA2 1 ILE A 10  ? VAL A 13  ? ILE A 10  VAL A 13  
AA2 2 THR A 102 ? LEU A 106 ? THR A 102 LEU A 106 
AA2 3 ALA A 84  ? GLN A 90  ? ALA A 84  GLN A 90  
AA2 4 ILE A 33  ? GLN A 38  ? ILE A 33  GLN A 38  
AA2 5 ARG A 45  ? ILE A 48  ? ARG A 45  ILE A 48  
AA3 1 ILE A 10  ? VAL A 13  ? ILE A 10  VAL A 13  
AA3 2 THR A 102 ? LEU A 106 ? THR A 102 LEU A 106 
AA3 3 ALA A 84  ? GLN A 90  ? ALA A 84  GLN A 90  
AA3 4 THR A 97  ? PHE A 98  ? THR A 97  PHE A 98  
AA4 1 SER A 114 ? PHE A 118 ? SER A 114 PHE A 118 
AA4 2 THR A 129 ? PHE A 139 ? THR A 129 PHE A 139 
AA4 3 TYR A 173 ? SER A 182 ? TYR A 173 SER A 182 
AA4 4 SER A 159 ? VAL A 163 ? SER A 159 VAL A 163 
AA5 1 ALA A 153 ? GLN A 155 ? ALA A 153 GLN A 155 
AA5 2 LYS A 145 ? VAL A 150 ? LYS A 145 VAL A 150 
AA5 3 VAL A 191 ? THR A 197 ? VAL A 191 THR A 197 
AA5 4 VAL A 205 ? ASN A 210 ? VAL A 205 ASN A 210 
AA6 1 GLN B 3   ? GLN B 6   ? GLN B 3   GLN B 6   
AA6 2 LEU B 18  ? SER B 25  ? LEU B 18  SER B 25  
AA6 3 GLN B 77  ? MET B 82  ? GLN B 77  MET B 82  
AA6 4 LEU B 67  ? ASP B 72  ? LEU B 67  ASP B 72  
AA7 1 GLY B 10  ? VAL B 12  ? GLY B 10  VAL B 12  
AA7 2 THR B 113 ? VAL B 117 ? THR B 113 VAL B 117 
AA7 3 ALA B 91  ? ALA B 98  ? ALA B 91  ALA B 98  
AA7 4 VAL B 34  ? SER B 40  ? VAL B 34  SER B 40  
AA7 5 GLY B 44  ? ILE B 51  ? GLY B 44  ILE B 51  
AA7 6 THR B 57  ? TYR B 59  ? THR B 57  TYR B 59  
AA8 1 GLY B 10  ? VAL B 12  ? GLY B 10  VAL B 12  
AA8 2 THR B 113 ? VAL B 117 ? THR B 113 VAL B 117 
AA8 3 ALA B 91  ? ALA B 98  ? ALA B 91  ALA B 98  
AA8 4 PHE B 106 ? TRP B 109 ? PHE B 106 TRP B 109 
AA9 1 SER B 126 ? LEU B 130 ? SER B 126 LEU B 130 
AA9 2 THR B 141 ? TYR B 151 ? THR B 141 TYR B 151 
AA9 3 TYR B 182 ? PRO B 191 ? TYR B 182 PRO B 191 
AA9 4 VAL B 169 ? THR B 171 ? VAL B 169 THR B 171 
AB1 1 THR B 137 ? SER B 138 ? THR B 137 SER B 138 
AB1 2 THR B 141 ? TYR B 151 ? THR B 141 TYR B 151 
AB1 3 TYR B 182 ? PRO B 191 ? TYR B 182 PRO B 191 
AB1 4 VAL B 175 ? LEU B 176 ? VAL B 175 LEU B 176 
AB2 1 THR B 157 ? TRP B 160 ? THR B 157 TRP B 160 
AB2 2 ILE B 201 ? HIS B 206 ? ILE B 201 HIS B 206 
AB2 3 THR B 211 ? ARG B 216 ? THR B 211 ARG B 216 
AB3 1 LEU C 4   ? SER C 7   ? LEU C 4   SER C 7   
AB3 2 VAL C 19  ? ALA C 25  ? VAL C 19  ALA C 25  
AB3 3 ASP C 70  ? ILE C 75  ? ASP C 70  ILE C 75  
AB3 4 PHE C 62  ? SER C 67  ? PHE C 62  SER C 67  
AB4 1 ILE C 10  ? VAL C 13  ? ILE C 10  VAL C 13  
AB4 2 THR C 102 ? LEU C 106 ? THR C 102 LEU C 106 
AB4 3 ASP C 85  ? GLN C 90  ? ASP C 85  GLN C 90  
AB4 4 ILE C 33  ? GLN C 38  ? ILE C 33  GLN C 38  
AB4 5 ARG C 45  ? LYS C 49  ? ARG C 45  LYS C 49  
AB4 6 GLU C 53  ? SER C 54  ? GLU C 53  SER C 54  
AB5 1 ILE C 10  ? VAL C 13  ? ILE C 10  VAL C 13  
AB5 2 THR C 102 ? LEU C 106 ? THR C 102 LEU C 106 
AB5 3 ASP C 85  ? GLN C 90  ? ASP C 85  GLN C 90  
AB5 4 THR C 97  ? PHE C 98  ? THR C 97  PHE C 98  
AB6 1 SER C 114 ? PHE C 118 ? SER C 114 PHE C 118 
AB6 2 THR C 129 ? PHE C 139 ? THR C 129 PHE C 139 
AB6 3 TYR C 173 ? SER C 182 ? TYR C 173 SER C 182 
AB6 4 SER C 159 ? VAL C 163 ? SER C 159 VAL C 163 
AB7 1 ALA C 153 ? LEU C 154 ? ALA C 153 LEU C 154 
AB7 2 LYS C 145 ? VAL C 150 ? LYS C 145 VAL C 150 
AB7 3 VAL C 191 ? THR C 197 ? VAL C 191 THR C 197 
AB7 4 VAL C 205 ? ASN C 210 ? VAL C 205 ASN C 210 
AB8 1 GLN D 3   ? GLN D 6   ? GLN D 3   GLN D 6   
AB8 2 LEU D 18  ? SER D 25  ? LEU D 18  SER D 25  
AB8 3 GLN D 77  ? MET D 82  ? GLN D 77  MET D 82  
AB8 4 LEU D 67  ? ASP D 72  ? LEU D 67  ASP D 72  
AB9 1 GLY D 10  ? VAL D 12  ? GLY D 10  VAL D 12  
AB9 2 THR D 113 ? VAL D 117 ? THR D 113 VAL D 117 
AB9 3 ALA D 91  ? ALA D 98  ? ALA D 91  ALA D 98  
AB9 4 VAL D 34  ? SER D 40  ? VAL D 34  SER D 40  
AB9 5 GLY D 44  ? ILE D 51  ? GLY D 44  ILE D 51  
AB9 6 THR D 57  ? TYR D 59  ? THR D 57  TYR D 59  
AC1 1 GLY D 10  ? VAL D 12  ? GLY D 10  VAL D 12  
AC1 2 THR D 113 ? VAL D 117 ? THR D 113 VAL D 117 
AC1 3 ALA D 91  ? ALA D 98  ? ALA D 91  ALA D 98  
AC1 4 PHE D 106 ? TRP D 109 ? PHE D 106 TRP D 109 
AC2 1 SER D 126 ? LEU D 130 ? SER D 126 LEU D 130 
AC2 2 THR D 141 ? TYR D 151 ? THR D 141 TYR D 151 
AC2 3 TYR D 182 ? PRO D 191 ? TYR D 182 PRO D 191 
AC2 4 VAL D 169 ? THR D 171 ? VAL D 169 THR D 171 
AC3 1 SER D 126 ? LEU D 130 ? SER D 126 LEU D 130 
AC3 2 THR D 141 ? TYR D 151 ? THR D 141 TYR D 151 
AC3 3 TYR D 182 ? PRO D 191 ? TYR D 182 PRO D 191 
AC3 4 VAL D 175 ? LEU D 176 ? VAL D 175 LEU D 176 
AC4 1 THR D 157 ? TRP D 160 ? THR D 157 TRP D 160 
AC4 2 ILE D 201 ? HIS D 206 ? ILE D 201 HIS D 206 
AC4 3 THR D 211 ? ARG D 216 ? THR D 211 ARG D 216 
AC5 1 GLN E 2   ? ASP E 4   ? GLN E 2   ASP E 4   
AC5 2 ARG E 9   ? LYS E 11  ? ARG E 9   LYS E 11  
AC6 1 GLN F 2   ? ASP F 4   ? GLN F 2   ASP F 4   
AC6 2 ARG F 9   ? LYS F 11  ? ARG F 9   LYS F 11  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N THR A 5   ? N THR A 5   O ARG A 24  ? O ARG A 24  
AA1 2 3 N PHE A 21  ? N PHE A 21  O LEU A 73  ? O LEU A 73  
AA1 3 4 O SER A 74  ? O SER A 74  N SER A 63  ? N SER A 63  
AA2 1 2 N LEU A 11  ? N LEU A 11  O LYS A 103 ? O LYS A 103 
AA2 2 3 O LEU A 104 ? O LEU A 104 N ALA A 84  ? N ALA A 84  
AA2 3 4 O ASP A 85  ? O ASP A 85  N GLN A 38  ? N GLN A 38  
AA2 4 5 N TRP A 35  ? N TRP A 35  O LEU A 47  ? O LEU A 47  
AA3 1 2 N LEU A 11  ? N LEU A 11  O LYS A 103 ? O LYS A 103 
AA3 2 3 O LEU A 104 ? O LEU A 104 N ALA A 84  ? N ALA A 84  
AA3 3 4 N GLN A 90  ? N GLN A 90  O THR A 97  ? O THR A 97  
AA4 1 2 N PHE A 118 ? N PHE A 118 O VAL A 133 ? O VAL A 133 
AA4 2 3 N LEU A 136 ? N LEU A 136 O LEU A 175 ? O LEU A 175 
AA4 3 4 O THR A 178 ? O THR A 178 N GLN A 160 ? N GLN A 160 
AA5 1 2 O GLN A 155 ? O GLN A 155 N TRP A 148 ? N TRP A 148 
AA5 2 3 N LYS A 149 ? N LYS A 149 O ALA A 193 ? O ALA A 193 
AA5 3 4 N VAL A 196 ? N VAL A 196 O VAL A 205 ? O VAL A 205 
AA6 1 2 N LYS B 5   ? N LYS B 5   O THR B 23  ? O THR B 23  
AA6 2 3 N CYS B 22  ? N CYS B 22  O VAL B 78  ? O VAL B 78  
AA6 3 4 O PHE B 79  ? O PHE B 79  N ASN B 70  ? N ASN B 70  
AA7 1 2 N VAL B 12  ? N VAL B 12  O THR B 116 ? O THR B 116 
AA7 2 3 O VAL B 115 ? O VAL B 115 N ALA B 91  ? N ALA B 91  
AA7 3 4 O ALA B 96  ? O ALA B 96  N HIS B 35  ? N HIS B 35  
AA7 4 5 N TRP B 36  ? N TRP B 36  O LEU B 48  ? O LEU B 48  
AA7 5 6 N VAL B 50  ? N VAL B 50  O ASP B 58  ? O ASP B 58  
AA8 1 2 N VAL B 12  ? N VAL B 12  O THR B 116 ? O THR B 116 
AA8 2 3 O VAL B 115 ? O VAL B 115 N ALA B 91  ? N ALA B 91  
AA8 3 4 N ARG B 97  ? N ARG B 97  O TYR B 108 ? O TYR B 108 
AA9 1 2 N PHE B 128 ? N PHE B 128 O LEU B 147 ? O LEU B 147 
AA9 2 3 N VAL B 148 ? N VAL B 148 O LEU B 184 ? O LEU B 184 
AA9 3 4 O VAL B 187 ? O VAL B 187 N HIS B 170 ? N HIS B 170 
AB1 1 2 N SER B 138 ? N SER B 138 O THR B 141 ? O THR B 141 
AB1 2 3 N VAL B 148 ? N VAL B 148 O LEU B 184 ? O LEU B 184 
AB1 3 4 O SER B 183 ? O SER B 183 N VAL B 175 ? N VAL B 175 
AB2 1 2 N SER B 159 ? N SER B 159 O ASN B 203 ? O ASN B 203 
AB2 2 3 N VAL B 204 ? N VAL B 204 O VAL B 213 ? O VAL B 213 
AB3 1 2 N THR C 5   ? N THR C 5   O ARG C 24  ? O ARG C 24  
AB3 2 3 N CYS C 23  ? N CYS C 23  O PHE C 71  ? O PHE C 71  
AB3 3 4 O SER C 74  ? O SER C 74  N SER C 63  ? N SER C 63  
AB4 1 2 N LEU C 11  ? N LEU C 11  O LYS C 103 ? O LYS C 103 
AB4 2 3 O THR C 102 ? O THR C 102 N TYR C 86  ? N TYR C 86  
AB4 3 4 O ASP C 85  ? O ASP C 85  N GLN C 38  ? N GLN C 38  
AB4 4 5 N TRP C 35  ? N TRP C 35  O LEU C 47  ? O LEU C 47  
AB4 5 6 N LYS C 49  ? N LYS C 49  O GLU C 53  ? O GLU C 53  
AB5 1 2 N LEU C 11  ? N LEU C 11  O LYS C 103 ? O LYS C 103 
AB5 2 3 O THR C 102 ? O THR C 102 N TYR C 86  ? N TYR C 86  
AB5 3 4 N GLN C 90  ? N GLN C 90  O THR C 97  ? O THR C 97  
AB6 1 2 N SER C 114 ? N SER C 114 O ASN C 137 ? O ASN C 137 
AB6 2 3 N VAL C 132 ? N VAL C 132 O LEU C 179 ? O LEU C 179 
AB6 3 4 O THR C 178 ? O THR C 178 N GLN C 160 ? N GLN C 160 
AB7 1 2 O ALA C 153 ? O ALA C 153 N VAL C 150 ? N VAL C 150 
AB7 2 3 N GLN C 147 ? N GLN C 147 O GLU C 195 ? O GLU C 195 
AB7 3 4 N TYR C 192 ? N TYR C 192 O PHE C 209 ? O PHE C 209 
AB8 1 2 N GLN D 3   ? N GLN D 3   O SER D 25  ? O SER D 25  
AB8 2 3 N CYS D 22  ? N CYS D 22  O VAL D 78  ? O VAL D 78  
AB8 3 4 O PHE D 79  ? O PHE D 79  N ASN D 70  ? N ASN D 70  
AB9 1 2 N VAL D 12  ? N VAL D 12  O THR D 116 ? O THR D 116 
AB9 2 3 O VAL D 115 ? O VAL D 115 N ALA D 91  ? N ALA D 91  
AB9 3 4 O TYR D 94  ? O TYR D 94  N VAL D 37  ? N VAL D 37  
AB9 4 5 N TRP D 36  ? N TRP D 36  O LEU D 48  ? O LEU D 48  
AB9 5 6 N VAL D 50  ? N VAL D 50  O ASP D 58  ? O ASP D 58  
AC1 1 2 N VAL D 12  ? N VAL D 12  O THR D 116 ? O THR D 116 
AC1 2 3 O VAL D 115 ? O VAL D 115 N ALA D 91  ? N ALA D 91  
AC1 3 4 N ARG D 97  ? N ARG D 97  O TYR D 108 ? O TYR D 108 
AC2 1 2 N LEU D 130 ? N LEU D 130 O GLY D 145 ? O GLY D 145 
AC2 2 3 N TYR D 151 ? N TYR D 151 O TYR D 182 ? O TYR D 182 
AC2 3 4 O VAL D 187 ? O VAL D 187 N HIS D 170 ? N HIS D 170 
AC3 1 2 N LEU D 130 ? N LEU D 130 O GLY D 145 ? O GLY D 145 
AC3 2 3 N TYR D 151 ? N TYR D 151 O TYR D 182 ? O TYR D 182 
AC3 3 4 O SER D 183 ? O SER D 183 N VAL D 175 ? N VAL D 175 
AC4 1 2 N SER D 159 ? N SER D 159 O ASN D 203 ? O ASN D 203 
AC4 2 3 N VAL D 204 ? N VAL D 204 O VAL D 213 ? O VAL D 213 
AC5 1 2 N GLN E 2   ? N GLN E 2   O LYS E 11  ? O LYS E 11  
AC6 1 2 N GLN F 2   ? N GLN F 2   O LYS F 11  ? O LYS F 11  
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A PO4 301 ? 5 'binding site for residue PO4 A 301'                           
AC2 Software A PO4 302 ? 8 'binding site for residue PO4 A 302'                           
AC3 Software B PO4 302 ? 5 'binding site for residue PO4 B 302'                           
AC4 Software C MRY 301 ? 7 'binding site for residue MRY C 301'                           
AC5 Software D PO4 302 ? 4 'binding site for residue PO4 D 302'                           
AC6 Software B NAG 301 ? 4 'binding site for Mono-Saccharide NAG B 301 bound to ASN B 88' 
AC7 Software D NAG 301 ? 5 'binding site for Mono-Saccharide NAG D 301 bound to ASN D 88' 
# 
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 5 ARG A 39  ? ARG A 39  . ? 1_555 ? 
2  AC1 5 ARG A 45  ? ARG A 45  . ? 1_555 ? 
3  AC1 5 PRO A 59  ? PRO A 59  . ? 1_555 ? 
4  AC1 5 ARG A 61  ? ARG A 61  . ? 1_555 ? 
5  AC1 5 HOH N .   ? HOH A 421 . ? 1_555 ? 
6  AC2 8 GLN A 155 ? GLN A 155 . ? 1_555 ? 
7  AC2 8 LEU A 181 ? LEU A 181 . ? 1_555 ? 
8  AC2 8 ASP A 185 ? ASP A 185 . ? 1_555 ? 
9  AC2 8 HIS A 189 ? HIS A 189 . ? 1_555 ? 
10 AC2 8 ILE D 201 ? ILE D 201 . ? 3_545 ? 
11 AC2 8 ASN D 203 ? ASN D 203 . ? 3_545 ? 
12 AC2 8 ASP D 214 ? ASP D 214 . ? 3_545 ? 
13 AC2 8 HOH Q .   ? HOH D 423 . ? 3_545 ? 
14 AC3 5 ASN B 205 ? ASN B 205 . ? 1_555 ? 
15 AC3 5 LYS B 207 ? LYS B 207 . ? 1_555 ? 
16 AC3 5 ASN B 210 ? ASN B 210 . ? 1_555 ? 
17 AC3 5 LYS B 212 ? LYS B 212 . ? 1_555 ? 
18 AC3 5 HOH O .   ? HOH B 421 . ? 1_555 ? 
19 AC4 7 SER C 156 ? SER C 156 . ? 1_555 ? 
20 AC4 7 GLY C 157 ? GLY C 157 . ? 1_555 ? 
21 AC4 7 ASN C 158 ? ASN C 158 . ? 1_555 ? 
22 AC4 7 SER C 159 ? SER C 159 . ? 1_555 ? 
23 AC4 7 HOH P .   ? HOH C 410 . ? 1_555 ? 
24 AC4 7 HOH P .   ? HOH C 436 . ? 1_555 ? 
25 AC4 7 HOH P .   ? HOH C 489 . ? 1_555 ? 
26 AC5 4 ASN D 205 ? ASN D 205 . ? 1_555 ? 
27 AC5 4 LYS D 207 ? LYS D 207 . ? 1_555 ? 
28 AC5 4 ASN D 210 ? ASN D 210 . ? 1_555 ? 
29 AC5 4 LYS D 212 ? LYS D 212 . ? 1_555 ? 
30 AC6 4 ARG B 38  ? ARG B 38  . ? 1_555 ? 
31 AC6 4 LYS B 43  ? LYS B 43  . ? 1_555 ? 
32 AC6 4 ASN B 88  ? ASN B 88  . ? 1_555 ? 
33 AC6 4 HOH O .   ? HOH B 434 . ? 1_555 ? 
34 AC7 5 ARG D 38  ? ARG D 38  . ? 1_555 ? 
35 AC7 5 SER D 40  ? SER D 40  . ? 1_555 ? 
36 AC7 5 LYS D 43  ? LYS D 43  . ? 1_555 ? 
37 AC7 5 ASN D 88  ? ASN D 88  . ? 1_555 ? 
38 AC7 5 HOH Q .   ? HOH D 417 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5EUK 
_atom_sites.fract_transf_matrix[1][1]   0.015642 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012186 
_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]   0.004715 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP A 1 1   ? -14.296 -41.942 9.164  1.00 36.12 ? 1   ASP A N   1 
ATOM   2    C CA  . ASP A 1 1   ? -15.433 -41.071 9.444  1.00 30.43 ? 1   ASP A CA  1 
ATOM   3    C C   . ASP A 1 1   ? -15.007 -39.611 9.472  1.00 31.35 ? 1   ASP A C   1 
ATOM   4    O O   . ASP A 1 1   ? -13.860 -39.310 9.780  1.00 39.85 ? 1   ASP A O   1 
ATOM   5    C CB  . ASP A 1 1   ? -16.060 -41.423 10.794 1.00 35.69 ? 1   ASP A CB  1 
ATOM   6    C CG  . ASP A 1 1   ? -16.676 -42.816 10.818 1.00 41.55 ? 1   ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 1   ? -16.708 -43.463 9.748  1.00 34.07 ? 1   ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 1   ? -17.143 -43.243 11.909 1.00 35.37 ? 1   ASP A OD2 1 
ATOM   9    N N   . ILE A 1 2   ? -15.922 -38.701 9.148  1.00 29.99 ? 2   ILE A N   1 
ATOM   10   C CA  . ILE A 1 2   ? -15.643 -37.286 9.338  1.00 30.78 ? 2   ILE A CA  1 
ATOM   11   C C   . ILE A 1 2   ? -15.605 -36.953 10.836 1.00 33.06 ? 2   ILE A C   1 
ATOM   12   O O   . ILE A 1 2   ? -16.539 -37.275 11.582 1.00 25.64 ? 2   ILE A O   1 
ATOM   13   C CB  . ILE A 1 2   ? -16.696 -36.379 8.671  1.00 32.71 ? 2   ILE A CB  1 
ATOM   14   C CG1 . ILE A 1 2   ? -16.869 -36.750 7.203  1.00 33.97 ? 2   ILE A CG1 1 
ATOM   15   C CG2 . ILE A 1 2   ? -16.286 -34.917 8.811  1.00 25.86 ? 2   ILE A CG2 1 
ATOM   16   C CD1 . ILE A 1 2   ? -15.581 -36.741 6.437  1.00 27.50 ? 2   ILE A CD1 1 
ATOM   17   N N   . LEU A 1 3   ? -14.521 -36.319 11.271 1.00 31.71 ? 3   LEU A N   1 
ATOM   18   C CA  . LEU A 1 3   ? -14.421 -35.845 12.641 1.00 27.96 ? 3   LEU A CA  1 
ATOM   19   C C   . LEU A 1 3   ? -14.869 -34.384 12.704 1.00 30.91 ? 3   LEU A C   1 
ATOM   20   O O   . LEU A 1 3   ? -14.399 -33.531 11.946 1.00 27.23 ? 3   LEU A O   1 
ATOM   21   C CB  . LEU A 1 3   ? -13.000 -36.024 13.191 1.00 22.46 ? 3   LEU A CB  1 
ATOM   22   C CG  . LEU A 1 3   ? -12.701 -35.505 14.609 1.00 35.27 ? 3   LEU A CG  1 
ATOM   23   C CD1 . LEU A 1 3   ? -13.367 -36.349 15.706 1.00 25.10 ? 3   LEU A CD1 1 
ATOM   24   C CD2 . LEU A 1 3   ? -11.195 -35.401 14.857 1.00 29.39 ? 3   LEU A CD2 1 
ATOM   25   N N   . LEU A 1 4   ? -15.802 -34.114 13.606 1.00 21.75 ? 4   LEU A N   1 
ATOM   26   C CA  . LEU A 1 4   ? -16.293 -32.771 13.804 1.00 20.95 ? 4   LEU A CA  1 
ATOM   27   C C   . LEU A 1 4   ? -15.727 -32.256 15.108 1.00 28.80 ? 4   LEU A C   1 
ATOM   28   O O   . LEU A 1 4   ? -15.906 -32.874 16.162 1.00 24.94 ? 4   LEU A O   1 
ATOM   29   C CB  . LEU A 1 4   ? -17.819 -32.756 13.860 1.00 23.15 ? 4   LEU A CB  1 
ATOM   30   C CG  . LEU A 1 4   ? -18.531 -33.177 12.576 1.00 24.61 ? 4   LEU A CG  1 
ATOM   31   C CD1 . LEU A 1 4   ? -20.045 -33.155 12.800 1.00 26.44 ? 4   LEU A CD1 1 
ATOM   32   C CD2 . LEU A 1 4   ? -18.130 -32.274 11.405 1.00 16.92 ? 4   LEU A CD2 1 
ATOM   33   N N   . THR A 1 5   ? -15.039 -31.122 15.034 1.00 27.30 ? 5   THR A N   1 
ATOM   34   C CA  . THR A 1 5   ? -14.476 -30.525 16.220 1.00 24.98 ? 5   THR A CA  1 
ATOM   35   C C   . THR A 1 5   ? -15.246 -29.254 16.580 1.00 26.74 ? 5   THR A C   1 
ATOM   36   O O   . THR A 1 5   ? -15.310 -28.307 15.794 1.00 24.55 ? 5   THR A O   1 
ATOM   37   C CB  . THR A 1 5   ? -12.969 -30.256 16.033 1.00 30.60 ? 5   THR A CB  1 
ATOM   38   O OG1 . THR A 1 5   ? -12.315 -31.500 15.751 1.00 24.00 ? 5   THR A OG1 1 
ATOM   39   C CG2 . THR A 1 5   ? -12.369 -29.639 17.299 1.00 18.03 ? 5   THR A CG2 1 
ATOM   40   N N   . GLN A 1 6   ? -15.859 -29.265 17.763 1.00 28.62 ? 6   GLN A N   1 
ATOM   41   C CA  . GLN A 1 6   ? -16.609 -28.119 18.265 1.00 21.87 ? 6   GLN A CA  1 
ATOM   42   C C   . GLN A 1 6   ? -15.795 -27.386 19.309 1.00 26.33 ? 6   GLN A C   1 
ATOM   43   O O   . GLN A 1 6   ? -15.251 -27.997 20.227 1.00 21.43 ? 6   GLN A O   1 
ATOM   44   C CB  . GLN A 1 6   ? -17.934 -28.560 18.865 1.00 16.34 ? 6   GLN A CB  1 
ATOM   45   C CG  . GLN A 1 6   ? -18.874 -29.171 17.872 1.00 19.07 ? 6   GLN A CG  1 
ATOM   46   C CD  . GLN A 1 6   ? -20.262 -29.350 18.432 1.00 24.29 ? 6   GLN A CD  1 
ATOM   47   O OE1 . GLN A 1 6   ? -20.772 -30.475 18.510 1.00 18.99 ? 6   GLN A OE1 1 
ATOM   48   N NE2 . GLN A 1 6   ? -20.885 -28.242 18.842 1.00 16.07 ? 6   GLN A NE2 1 
ATOM   49   N N   . SER A 1 7   ? -15.699 -26.072 19.156 1.00 31.47 ? 7   SER A N   1 
ATOM   50   C CA  . SER A 1 7   ? -14.867 -25.268 20.041 1.00 36.01 ? 7   SER A CA  1 
ATOM   51   C C   . SER A 1 7   ? -15.532 -23.919 20.278 1.00 39.14 ? 7   SER A C   1 
ATOM   52   O O   . SER A 1 7   ? -16.311 -23.452 19.440 1.00 40.19 ? 7   SER A O   1 
ATOM   53   C CB  . SER A 1 7   ? -13.473 -25.061 19.438 1.00 36.87 ? 7   SER A CB  1 
ATOM   54   O OG  . SER A 1 7   ? -13.453 -23.924 18.594 1.00 46.40 ? 7   SER A OG  1 
ATOM   55   N N   . PRO A 1 8   ? -15.268 -23.311 21.441 1.00 36.42 ? 8   PRO A N   1 
ATOM   56   C CA  . PRO A 1 8   ? -14.568 -23.975 22.544 1.00 33.61 ? 8   PRO A CA  1 
ATOM   57   C C   . PRO A 1 8   ? -15.483 -24.975 23.237 1.00 35.57 ? 8   PRO A C   1 
ATOM   58   O O   . PRO A 1 8   ? -16.652 -25.119 22.866 1.00 35.64 ? 8   PRO A O   1 
ATOM   59   C CB  . PRO A 1 8   ? -14.291 -22.828 23.507 1.00 37.81 ? 8   PRO A CB  1 
ATOM   60   C CG  . PRO A 1 8   ? -15.419 -21.865 23.252 1.00 30.52 ? 8   PRO A CG  1 
ATOM   61   C CD  . PRO A 1 8   ? -15.632 -21.921 21.773 1.00 31.91 ? 8   PRO A CD  1 
ATOM   62   N N   . VAL A 1 9   ? -14.944 -25.649 24.241 1.00 27.82 ? 9   VAL A N   1 
ATOM   63   C CA  . VAL A 1 9   ? -15.710 -26.594 25.042 1.00 32.50 ? 9   VAL A CA  1 
ATOM   64   C C   . VAL A 1 9   ? -16.855 -25.921 25.833 1.00 30.91 ? 9   VAL A C   1 
ATOM   65   O O   . VAL A 1 9   ? -17.968 -26.448 25.903 1.00 24.44 ? 9   VAL A O   1 
ATOM   66   C CB  . VAL A 1 9   ? -14.755 -27.386 25.974 1.00 36.74 ? 9   VAL A CB  1 
ATOM   67   C CG1 . VAL A 1 9   ? -15.370 -27.608 27.307 1.00 37.83 ? 9   VAL A CG1 1 
ATOM   68   C CG2 . VAL A 1 9   ? -14.342 -28.708 25.344 1.00 26.31 ? 9   VAL A CG2 1 
ATOM   69   N N   . ILE A 1 10  ? -16.578 -24.754 26.417 1.00 31.64 ? 10  ILE A N   1 
ATOM   70   C CA  . ILE A 1 10  ? -17.582 -24.004 27.172 1.00 23.22 ? 10  ILE A CA  1 
ATOM   71   C C   . ILE A 1 10  ? -17.668 -22.571 26.679 1.00 21.83 ? 10  ILE A C   1 
ATOM   72   O O   . ILE A 1 10  ? -16.652 -21.940 26.410 1.00 28.41 ? 10  ILE A O   1 
ATOM   73   C CB  . ILE A 1 10  ? -17.236 -23.931 28.676 1.00 26.12 ? 10  ILE A CB  1 
ATOM   74   C CG1 . ILE A 1 10  ? -16.944 -25.312 29.240 1.00 36.69 ? 10  ILE A CG1 1 
ATOM   75   C CG2 . ILE A 1 10  ? -18.368 -23.318 29.471 1.00 25.34 ? 10  ILE A CG2 1 
ATOM   76   C CD1 . ILE A 1 10  ? -16.548 -25.293 30.703 1.00 54.78 ? 10  ILE A CD1 1 
ATOM   77   N N   . LEU A 1 11  ? -18.886 -22.061 26.553 1.00 20.29 ? 11  LEU A N   1 
ATOM   78   C CA  . LEU A 1 11  ? -19.100 -20.633 26.365 1.00 22.53 ? 11  LEU A CA  1 
ATOM   79   C C   . LEU A 1 11  ? -19.887 -20.047 27.529 1.00 25.94 ? 11  LEU A C   1 
ATOM   80   O O   . LEU A 1 11  ? -20.869 -20.631 27.983 1.00 29.18 ? 11  LEU A O   1 
ATOM   81   C CB  . LEU A 1 11  ? -19.841 -20.365 25.060 1.00 18.38 ? 11  LEU A CB  1 
ATOM   82   C CG  . LEU A 1 11  ? -18.977 -20.449 23.804 1.00 25.81 ? 11  LEU A CG  1 
ATOM   83   C CD1 . LEU A 1 11  ? -19.831 -20.321 22.554 1.00 26.49 ? 11  LEU A CD1 1 
ATOM   84   C CD2 . LEU A 1 11  ? -17.908 -19.373 23.849 1.00 22.88 ? 11  LEU A CD2 1 
ATOM   85   N N   . SER A 1 12  ? -19.456 -18.887 28.006 1.00 29.25 ? 12  SER A N   1 
ATOM   86   C CA  . SER A 1 12  ? -20.142 -18.196 29.088 1.00 24.56 ? 12  SER A CA  1 
ATOM   87   C C   . SER A 1 12  ? -20.417 -16.750 28.681 1.00 25.34 ? 12  SER A C   1 
ATOM   88   O O   . SER A 1 12  ? -19.494 -15.973 28.500 1.00 31.89 ? 12  SER A O   1 
ATOM   89   C CB  . SER A 1 12  ? -19.283 -18.240 30.354 1.00 32.17 ? 12  SER A CB  1 
ATOM   90   O OG  . SER A 1 12  ? -19.793 -17.380 31.361 1.00 48.27 ? 12  SER A OG  1 
ATOM   91   N N   . VAL A 1 13  ? -21.685 -16.389 28.519 1.00 21.04 ? 13  VAL A N   1 
ATOM   92   C CA  . VAL A 1 13  ? -22.032 -15.038 28.086 1.00 26.47 ? 13  VAL A CA  1 
ATOM   93   C C   . VAL A 1 13  ? -23.118 -14.422 28.969 1.00 29.36 ? 13  VAL A C   1 
ATOM   94   O O   . VAL A 1 13  ? -23.740 -15.115 29.767 1.00 29.56 ? 13  VAL A O   1 
ATOM   95   C CB  . VAL A 1 13  ? -22.502 -15.017 26.600 1.00 30.79 ? 13  VAL A CB  1 
ATOM   96   C CG1 . VAL A 1 13  ? -21.559 -15.834 25.709 1.00 26.20 ? 13  VAL A CG1 1 
ATOM   97   C CG2 . VAL A 1 13  ? -23.900 -15.547 26.478 1.00 21.03 ? 13  VAL A CG2 1 
ATOM   98   N N   . SER A 1 14  ? -23.346 -13.121 28.819 1.00 27.74 ? 14  SER A N   1 
ATOM   99   C CA  . SER A 1 14  ? -24.423 -12.452 29.539 1.00 28.76 ? 14  SER A CA  1 
ATOM   100  C C   . SER A 1 14  ? -25.655 -12.329 28.647 1.00 29.35 ? 14  SER A C   1 
ATOM   101  O O   . SER A 1 14  ? -25.531 -12.294 27.430 1.00 32.96 ? 14  SER A O   1 
ATOM   102  C CB  . SER A 1 14  ? -23.962 -11.082 30.011 1.00 30.13 ? 14  SER A CB  1 
ATOM   103  O OG  . SER A 1 14  ? -22.684 -11.173 30.626 1.00 37.45 ? 14  SER A OG  1 
ATOM   104  N N   . PRO A 1 15  ? -26.854 -12.279 29.246 1.00 27.42 ? 15  PRO A N   1 
ATOM   105  C CA  . PRO A 1 15  ? -28.077 -12.204 28.436 1.00 32.97 ? 15  PRO A CA  1 
ATOM   106  C C   . PRO A 1 15  ? -28.079 -10.994 27.522 1.00 31.71 ? 15  PRO A C   1 
ATOM   107  O O   . PRO A 1 15  ? -27.487 -9.972  27.861 1.00 35.25 ? 15  PRO A O   1 
ATOM   108  C CB  . PRO A 1 15  ? -29.182 -12.057 29.480 1.00 24.00 ? 15  PRO A CB  1 
ATOM   109  C CG  . PRO A 1 15  ? -28.607 -12.660 30.701 1.00 22.06 ? 15  PRO A CG  1 
ATOM   110  C CD  . PRO A 1 15  ? -27.153 -12.354 30.685 1.00 23.59 ? 15  PRO A CD  1 
ATOM   111  N N   . GLY A 1 16  ? -28.727 -11.128 26.367 1.00 37.57 ? 16  GLY A N   1 
ATOM   112  C CA  . GLY A 1 16  ? -28.801 -10.061 25.394 1.00 31.61 ? 16  GLY A CA  1 
ATOM   113  C C   . GLY A 1 16  ? -27.591 -9.991  24.487 1.00 33.00 ? 16  GLY A C   1 
ATOM   114  O O   . GLY A 1 16  ? -27.653 -9.344  23.444 1.00 40.65 ? 16  GLY A O   1 
ATOM   115  N N   . GLU A 1 17  ? -26.491 -10.633 24.885 1.00 25.89 ? 17  GLU A N   1 
ATOM   116  C CA  . GLU A 1 17  ? -25.287 -10.678 24.062 1.00 34.56 ? 17  GLU A CA  1 
ATOM   117  C C   . GLU A 1 17  ? -25.438 -11.675 22.914 1.00 36.40 ? 17  GLU A C   1 
ATOM   118  O O   . GLU A 1 17  ? -26.265 -12.584 22.969 1.00 29.73 ? 17  GLU A O   1 
ATOM   119  C CB  . GLU A 1 17  ? -24.051 -11.027 24.901 1.00 30.92 ? 17  GLU A CB  1 
ATOM   120  C CG  . GLU A 1 17  ? -23.517 -9.889  25.762 1.00 43.60 ? 17  GLU A CG  1 
ATOM   121  C CD  . GLU A 1 17  ? -22.387 -10.336 26.683 1.00 51.53 ? 17  GLU A CD  1 
ATOM   122  O OE1 . GLU A 1 17  ? -21.966 -11.507 26.568 1.00 43.52 ? 17  GLU A OE1 1 
ATOM   123  O OE2 . GLU A 1 17  ? -21.926 -9.521  27.520 1.00 46.26 ? 17  GLU A OE2 1 
ATOM   124  N N   . ARG A 1 18  ? -24.633 -11.488 21.875 1.00 32.96 ? 18  ARG A N   1 
ATOM   125  C CA  . ARG A 1 18  ? -24.608 -12.406 20.750 1.00 33.96 ? 18  ARG A CA  1 
ATOM   126  C C   . ARG A 1 18  ? -23.578 -13.487 21.046 1.00 31.00 ? 18  ARG A C   1 
ATOM   127  O O   . ARG A 1 18  ? -22.573 -13.225 21.712 1.00 31.34 ? 18  ARG A O   1 
ATOM   128  C CB  . ARG A 1 18  ? -24.248 -11.664 19.462 1.00 38.38 ? 18  ARG A CB  1 
ATOM   129  C CG  . ARG A 1 18  ? -24.420 -12.489 18.206 1.00 44.85 ? 18  ARG A CG  1 
ATOM   130  C CD  . ARG A 1 18  ? -24.084 -11.717 16.944 1.00 48.77 ? 18  ARG A CD  1 
ATOM   131  N NE  . ARG A 1 18  ? -24.257 -12.552 15.753 1.00 61.93 ? 18  ARG A NE  1 
ATOM   132  C CZ  . ARG A 1 18  ? -25.326 -12.519 14.956 1.00 65.98 ? 18  ARG A CZ  1 
ATOM   133  N NH1 . ARG A 1 18  ? -26.320 -11.676 15.208 1.00 57.99 ? 18  ARG A NH1 1 
ATOM   134  N NH2 . ARG A 1 18  ? -25.394 -13.317 13.891 1.00 51.92 ? 18  ARG A NH2 1 
ATOM   135  N N   . VAL A 1 19  ? -23.829 -14.701 20.561 1.00 27.93 ? 19  VAL A N   1 
ATOM   136  C CA  . VAL A 1 19  ? -22.901 -15.812 20.774 1.00 33.57 ? 19  VAL A CA  1 
ATOM   137  C C   . VAL A 1 19  ? -22.792 -16.727 19.543 1.00 23.12 ? 19  VAL A C   1 
ATOM   138  O O   . VAL A 1 19  ? -23.772 -16.941 18.812 1.00 26.46 ? 19  VAL A O   1 
ATOM   139  C CB  . VAL A 1 19  ? -23.265 -16.630 22.063 1.00 24.82 ? 19  VAL A CB  1 
ATOM   140  C CG1 . VAL A 1 19  ? -24.458 -17.506 21.836 1.00 20.53 ? 19  VAL A CG1 1 
ATOM   141  C CG2 . VAL A 1 19  ? -22.079 -17.467 22.528 1.00 25.65 ? 19  VAL A CG2 1 
ATOM   142  N N   . SER A 1 20  ? -21.594 -17.254 19.316 1.00 19.70 ? 20  SER A N   1 
ATOM   143  C CA  . SER A 1 20  ? -21.321 -18.104 18.160 1.00 23.11 ? 20  SER A CA  1 
ATOM   144  C C   . SER A 1 20  ? -20.646 -19.414 18.548 1.00 27.60 ? 20  SER A C   1 
ATOM   145  O O   . SER A 1 20  ? -19.714 -19.441 19.353 1.00 26.51 ? 20  SER A O   1 
ATOM   146  C CB  . SER A 1 20  ? -20.445 -17.377 17.134 1.00 22.96 ? 20  SER A CB  1 
ATOM   147  O OG  . SER A 1 20  ? -21.186 -16.364 16.478 1.00 33.25 ? 20  SER A OG  1 
ATOM   148  N N   . PHE A 1 21  ? -21.132 -20.498 17.959 1.00 25.30 ? 21  PHE A N   1 
ATOM   149  C CA  . PHE A 1 21  ? -20.567 -21.815 18.165 1.00 27.38 ? 21  PHE A CA  1 
ATOM   150  C C   . PHE A 1 21  ? -19.882 -22.270 16.879 1.00 31.12 ? 21  PHE A C   1 
ATOM   151  O O   . PHE A 1 21  ? -20.421 -22.137 15.781 1.00 24.11 ? 21  PHE A O   1 
ATOM   152  C CB  . PHE A 1 21  ? -21.657 -22.814 18.545 1.00 27.04 ? 21  PHE A CB  1 
ATOM   153  C CG  . PHE A 1 21  ? -22.479 -22.404 19.740 1.00 25.59 ? 21  PHE A CG  1 
ATOM   154  C CD1 . PHE A 1 21  ? -23.603 -21.613 19.590 1.00 20.86 ? 21  PHE A CD1 1 
ATOM   155  C CD2 . PHE A 1 21  ? -22.137 -22.830 21.014 1.00 26.82 ? 21  PHE A CD2 1 
ATOM   156  C CE1 . PHE A 1 21  ? -24.366 -21.245 20.694 1.00 26.91 ? 21  PHE A CE1 1 
ATOM   157  C CE2 . PHE A 1 21  ? -22.892 -22.464 22.114 1.00 22.97 ? 21  PHE A CE2 1 
ATOM   158  C CZ  . PHE A 1 21  ? -24.012 -21.671 21.952 1.00 20.17 ? 21  PHE A CZ  1 
ATOM   159  N N   . SER A 1 22  ? -18.690 -22.820 17.043 1.00 30.54 ? 22  SER A N   1 
ATOM   160  C CA  . SER A 1 22  ? -17.835 -23.192 15.941 1.00 22.76 ? 22  SER A CA  1 
ATOM   161  C C   . SER A 1 22  ? -17.898 -24.709 15.715 1.00 28.34 ? 22  SER A C   1 
ATOM   162  O O   . SER A 1 22  ? -17.775 -25.490 16.662 1.00 28.02 ? 22  SER A O   1 
ATOM   163  C CB  . SER A 1 22  ? -16.415 -22.732 16.289 1.00 19.60 ? 22  SER A CB  1 
ATOM   164  O OG  . SER A 1 22  ? -15.441 -23.218 15.402 1.00 34.07 ? 22  SER A OG  1 
ATOM   165  N N   . CYS A 1 23  ? -18.107 -25.130 14.468 1.00 24.79 ? 23  CYS A N   1 
ATOM   166  C CA  . CYS A 1 23  ? -18.023 -26.551 14.128 1.00 23.33 ? 23  CYS A CA  1 
ATOM   167  C C   . CYS A 1 23  ? -17.095 -26.733 12.948 1.00 28.44 ? 23  CYS A C   1 
ATOM   168  O O   . CYS A 1 23  ? -17.391 -26.289 11.841 1.00 29.97 ? 23  CYS A O   1 
ATOM   169  C CB  . CYS A 1 23  ? -19.399 -27.138 13.800 1.00 23.87 ? 23  CYS A CB  1 
ATOM   170  S SG  . CYS A 1 23  ? -19.409 -28.934 13.503 1.00 27.34 ? 23  CYS A SG  1 
ATOM   171  N N   . ARG A 1 24  ? -15.967 -27.387 13.184 1.00 25.85 ? 24  ARG A N   1 
ATOM   172  C CA  . ARG A 1 24  ? -14.999 -27.604 12.121 1.00 24.79 ? 24  ARG A CA  1 
ATOM   173  C C   . ARG A 1 24  ? -14.898 -29.068 11.709 1.00 25.74 ? 24  ARG A C   1 
ATOM   174  O O   . ARG A 1 24  ? -14.826 -29.963 12.552 1.00 24.83 ? 24  ARG A O   1 
ATOM   175  C CB  . ARG A 1 24  ? -13.631 -27.042 12.509 1.00 23.21 ? 24  ARG A CB  1 
ATOM   176  C CG  . ARG A 1 24  ? -13.621 -25.538 12.659 1.00 31.31 ? 24  ARG A CG  1 
ATOM   177  C CD  . ARG A 1 24  ? -12.284 -25.010 13.166 1.00 35.98 ? 24  ARG A CD  1 
ATOM   178  N NE  . ARG A 1 24  ? -12.133 -23.602 12.808 1.00 38.65 ? 24  ARG A NE  1 
ATOM   179  C CZ  . ARG A 1 24  ? -12.552 -22.586 13.559 1.00 37.77 ? 24  ARG A CZ  1 
ATOM   180  N NH1 . ARG A 1 24  ? -13.127 -22.812 14.740 1.00 39.31 ? 24  ARG A NH1 1 
ATOM   181  N NH2 . ARG A 1 24  ? -12.388 -21.340 13.132 1.00 31.46 ? 24  ARG A NH2 1 
ATOM   182  N N   . ALA A 1 25  ? -14.891 -29.292 10.400 1.00 26.25 ? 25  ALA A N   1 
ATOM   183  C CA  . ALA A 1 25  ? -14.846 -30.637 9.841  1.00 27.22 ? 25  ALA A CA  1 
ATOM   184  C C   . ALA A 1 25  ? -13.439 -31.040 9.389  1.00 28.34 ? 25  ALA A C   1 
ATOM   185  O O   . ALA A 1 25  ? -12.653 -30.208 8.938  1.00 30.52 ? 25  ALA A O   1 
ATOM   186  C CB  . ALA A 1 25  ? -15.831 -30.749 8.685  1.00 24.00 ? 25  ALA A CB  1 
ATOM   187  N N   . SER A 1 26  ? -13.134 -32.327 9.502  1.00 28.16 ? 26  SER A N   1 
ATOM   188  C CA  . SER A 1 26  ? -11.813 -32.846 9.160  1.00 27.04 ? 26  SER A CA  1 
ATOM   189  C C   . SER A 1 26  ? -11.583 -32.940 7.654  1.00 28.91 ? 26  SER A C   1 
ATOM   190  O O   . SER A 1 26  ? -10.514 -33.339 7.210  1.00 30.70 ? 26  SER A O   1 
ATOM   191  C CB  . SER A 1 26  ? -11.629 -34.230 9.787  1.00 33.24 ? 26  SER A CB  1 
ATOM   192  O OG  . SER A 1 26  ? -12.649 -35.125 9.342  1.00 35.23 ? 26  SER A OG  1 
ATOM   193  N N   . GLN A 1 27  ? -12.581 -32.540 6.878  1.00 32.77 ? 27  GLN A N   1 
ATOM   194  C CA  . GLN A 1 27  ? -12.614 -32.817 5.454  1.00 36.32 ? 27  GLN A CA  1 
ATOM   195  C C   . GLN A 1 27  ? -13.820 -32.063 4.918  1.00 35.69 ? 27  GLN A C   1 
ATOM   196  O O   . GLN A 1 27  ? -14.830 -31.972 5.603  1.00 32.72 ? 27  GLN A O   1 
ATOM   197  C CB  . GLN A 1 27  ? -12.804 -34.316 5.285  1.00 37.42 ? 27  GLN A CB  1 
ATOM   198  C CG  . GLN A 1 27  ? -12.708 -34.865 3.903  1.00 33.86 ? 27  GLN A CG  1 
ATOM   199  C CD  . GLN A 1 27  ? -12.957 -36.368 3.898  1.00 43.19 ? 27  GLN A CD  1 
ATOM   200  O OE1 . GLN A 1 27  ? -12.659 -37.063 4.874  1.00 38.37 ? 27  GLN A OE1 1 
ATOM   201  N NE2 . GLN A 1 27  ? -13.517 -36.871 2.808  1.00 47.82 ? 27  GLN A NE2 1 
ATOM   202  N N   . SER A 1 28  ? -13.726 -31.503 3.717  1.00 36.60 ? 28  SER A N   1 
ATOM   203  C CA  . SER A 1 28  ? -14.815 -30.667 3.215  1.00 37.46 ? 28  SER A CA  1 
ATOM   204  C C   . SER A 1 28  ? -16.129 -31.441 3.164  1.00 35.15 ? 28  SER A C   1 
ATOM   205  O O   . SER A 1 28  ? -16.152 -32.600 2.765  1.00 38.60 ? 28  SER A O   1 
ATOM   206  C CB  . SER A 1 28  ? -14.474 -30.084 1.846  1.00 35.79 ? 28  SER A CB  1 
ATOM   207  O OG  . SER A 1 28  ? -15.520 -29.241 1.392  1.00 37.53 ? 28  SER A OG  1 
ATOM   208  N N   . ILE A 1 29  ? -17.214 -30.809 3.598  1.00 37.00 ? 29  ILE A N   1 
ATOM   209  C CA  . ILE A 1 29  ? -18.510 -31.486 3.665  1.00 31.27 ? 29  ILE A CA  1 
ATOM   210  C C   . ILE A 1 29  ? -19.632 -30.628 3.119  1.00 31.83 ? 29  ILE A C   1 
ATOM   211  O O   . ILE A 1 29  ? -20.804 -30.894 3.394  1.00 27.40 ? 29  ILE A O   1 
ATOM   212  C CB  . ILE A 1 29  ? -18.898 -31.901 5.108  1.00 26.56 ? 29  ILE A CB  1 
ATOM   213  C CG1 . ILE A 1 29  ? -18.819 -30.697 6.056  1.00 28.12 ? 29  ILE A CG1 1 
ATOM   214  C CG2 . ILE A 1 29  ? -18.035 -33.048 5.591  1.00 27.64 ? 29  ILE A CG2 1 
ATOM   215  C CD1 . ILE A 1 29  ? -19.373 -30.964 7.449  1.00 20.73 ? 29  ILE A CD1 1 
ATOM   216  N N   . GLY A 1 30  ? -19.266 -29.598 2.356  1.00 32.41 ? 30  GLY A N   1 
ATOM   217  C CA  . GLY A 1 30  ? -20.236 -28.749 1.686  1.00 24.34 ? 30  GLY A CA  1 
ATOM   218  C C   . GLY A 1 30  ? -20.989 -27.880 2.669  1.00 29.20 ? 30  GLY A C   1 
ATOM   219  O O   . GLY A 1 30  ? -20.379 -27.160 3.447  1.00 29.87 ? 30  GLY A O   1 
ATOM   220  N N   . THR A 1 31  ? -22.314 -27.939 2.625  1.00 26.40 ? 31  THR A N   1 
ATOM   221  C CA  . THR A 1 31  ? -23.138 -27.279 3.625  1.00 27.23 ? 31  THR A CA  1 
ATOM   222  C C   . THR A 1 31  ? -23.991 -28.336 4.303  1.00 27.43 ? 31  THR A C   1 
ATOM   223  O O   . THR A 1 31  ? -25.075 -28.049 4.815  1.00 27.88 ? 31  THR A O   1 
ATOM   224  C CB  . THR A 1 31  ? -24.074 -26.218 3.005  1.00 26.15 ? 31  THR A CB  1 
ATOM   225  O OG1 . THR A 1 31  ? -24.722 -26.768 1.854  1.00 25.03 ? 31  THR A OG1 1 
ATOM   226  C CG2 . THR A 1 31  ? -23.299 -24.979 2.599  1.00 22.67 ? 31  THR A CG2 1 
ATOM   227  N N   . ASN A 1 32  ? -23.509 -29.571 4.270  1.00 24.66 ? 32  ASN A N   1 
ATOM   228  C CA  . ASN A 1 32  ? -24.251 -30.674 4.848  1.00 21.09 ? 32  ASN A CA  1 
ATOM   229  C C   . ASN A 1 32  ? -24.009 -30.765 6.345  1.00 25.71 ? 32  ASN A C   1 
ATOM   230  O O   . ASN A 1 32  ? -23.440 -31.736 6.837  1.00 24.23 ? 32  ASN A O   1 
ATOM   231  C CB  . ASN A 1 32  ? -23.889 -31.990 4.162  1.00 20.99 ? 32  ASN A CB  1 
ATOM   232  C CG  . ASN A 1 32  ? -25.078 -32.912 4.023  1.00 26.73 ? 32  ASN A CG  1 
ATOM   233  O OD1 . ASN A 1 32  ? -25.801 -33.173 4.991  1.00 26.52 ? 32  ASN A OD1 1 
ATOM   234  N ND2 . ASN A 1 32  ? -25.303 -33.400 2.809  1.00 25.40 ? 32  ASN A ND2 1 
ATOM   235  N N   . ILE A 1 33  ? -24.436 -29.736 7.064  1.00 26.42 ? 33  ILE A N   1 
ATOM   236  C CA  A ILE A 1 33  ? -24.304 -29.707 8.510  0.59 26.78 ? 33  ILE A CA  1 
ATOM   237  C CA  B ILE A 1 33  ? -24.304 -29.725 8.512  0.41 26.60 ? 33  ILE A CA  1 
ATOM   238  C C   . ILE A 1 33  ? -25.642 -29.343 9.162  1.00 27.19 ? 33  ILE A C   1 
ATOM   239  O O   . ILE A 1 33  ? -26.394 -28.511 8.649  1.00 21.24 ? 33  ILE A O   1 
ATOM   240  C CB  A ILE A 1 33  ? -23.162 -28.750 8.952  0.59 25.96 ? 33  ILE A CB  1 
ATOM   241  C CB  B ILE A 1 33  ? -23.165 -28.787 8.970  0.41 26.60 ? 33  ILE A CB  1 
ATOM   242  C CG1 A ILE A 1 33  ? -22.607 -29.152 10.317 0.59 25.99 ? 33  ILE A CG1 1 
ATOM   243  C CG1 B ILE A 1 33  ? -22.899 -28.934 10.466 0.41 25.95 ? 33  ILE A CG1 1 
ATOM   244  C CG2 A ILE A 1 33  ? -23.608 -27.297 8.946  0.59 25.83 ? 33  ILE A CG2 1 
ATOM   245  C CG2 B ILE A 1 33  ? -23.470 -27.347 8.622  0.41 25.91 ? 33  ILE A CG2 1 
ATOM   246  C CD1 A ILE A 1 33  ? -21.587 -30.263 10.247 0.59 25.06 ? 33  ILE A CD1 1 
ATOM   247  C CD1 B ILE A 1 33  ? -21.781 -28.056 10.963 0.41 26.78 ? 33  ILE A CD1 1 
ATOM   248  N N   . HIS A 1 34  ? -25.952 -29.988 10.279 1.00 28.61 ? 34  HIS A N   1 
ATOM   249  C CA  . HIS A 1 34  ? -27.181 -29.716 11.022 1.00 24.39 ? 34  HIS A CA  1 
ATOM   250  C C   . HIS A 1 34  ? -26.812 -29.387 12.460 1.00 24.17 ? 34  HIS A C   1 
ATOM   251  O O   . HIS A 1 34  ? -25.779 -29.837 12.958 1.00 27.77 ? 34  HIS A O   1 
ATOM   252  C CB  . HIS A 1 34  ? -28.110 -30.933 10.998 1.00 25.78 ? 34  HIS A CB  1 
ATOM   253  C CG  . HIS A 1 34  ? -28.390 -31.461 9.627  1.00 26.38 ? 34  HIS A CG  1 
ATOM   254  N ND1 . HIS A 1 34  ? -28.623 -30.636 8.544  1.00 20.38 ? 34  HIS A ND1 1 
ATOM   255  C CD2 . HIS A 1 34  ? -28.467 -32.727 9.152  1.00 24.22 ? 34  HIS A CD2 1 
ATOM   256  C CE1 . HIS A 1 34  ? -28.838 -31.375 7.469  1.00 22.76 ? 34  HIS A CE1 1 
ATOM   257  N NE2 . HIS A 1 34  ? -28.751 -32.647 7.815  1.00 20.26 ? 34  HIS A NE2 1 
ATOM   258  N N   . TRP A 1 35  ? -27.649 -28.606 13.132 1.00 17.60 ? 35  TRP A N   1 
ATOM   259  C CA  . TRP A 1 35  ? -27.367 -28.240 14.515 1.00 19.64 ? 35  TRP A CA  1 
ATOM   260  C C   . TRP A 1 35  ? -28.500 -28.654 15.449 1.00 23.74 ? 35  TRP A C   1 
ATOM   261  O O   . TRP A 1 35  ? -29.666 -28.595 15.075 1.00 25.92 ? 35  TRP A O   1 
ATOM   262  C CB  . TRP A 1 35  ? -27.155 -26.734 14.649 1.00 21.24 ? 35  TRP A CB  1 
ATOM   263  C CG  . TRP A 1 35  ? -25.938 -26.188 13.993 1.00 21.74 ? 35  TRP A CG  1 
ATOM   264  C CD1 . TRP A 1 35  ? -25.829 -25.744 12.706 1.00 21.44 ? 35  TRP A CD1 1 
ATOM   265  C CD2 . TRP A 1 35  ? -24.655 -25.993 14.598 1.00 23.57 ? 35  TRP A CD2 1 
ATOM   266  N NE1 . TRP A 1 35  ? -24.548 -25.295 12.469 1.00 24.43 ? 35  TRP A NE1 1 
ATOM   267  C CE2 . TRP A 1 35  ? -23.807 -25.436 13.612 1.00 25.14 ? 35  TRP A CE2 1 
ATOM   268  C CE3 . TRP A 1 35  ? -24.137 -26.244 15.871 1.00 21.91 ? 35  TRP A CE3 1 
ATOM   269  C CZ2 . TRP A 1 35  ? -22.472 -25.120 13.865 1.00 21.97 ? 35  TRP A CZ2 1 
ATOM   270  C CZ3 . TRP A 1 35  ? -22.810 -25.930 16.123 1.00 27.02 ? 35  TRP A CZ3 1 
ATOM   271  C CH2 . TRP A 1 35  ? -21.992 -25.375 15.119 1.00 26.79 ? 35  TRP A CH2 1 
ATOM   272  N N   . TYR A 1 36  ? -28.141 -29.027 16.674 1.00 20.38 ? 36  TYR A N   1 
ATOM   273  C CA  . TYR A 1 36  ? -29.098 -29.442 17.692 1.00 17.00 ? 36  TYR A CA  1 
ATOM   274  C C   . TYR A 1 36  ? -28.898 -28.758 19.055 1.00 20.99 ? 36  TYR A C   1 
ATOM   275  O O   . TYR A 1 36  ? -27.786 -28.400 19.435 1.00 18.83 ? 36  TYR A O   1 
ATOM   276  C CB  . TYR A 1 36  ? -29.028 -30.953 17.883 1.00 19.45 ? 36  TYR A CB  1 
ATOM   277  C CG  . TYR A 1 36  ? -29.353 -31.763 16.655 1.00 17.23 ? 36  TYR A CG  1 
ATOM   278  C CD1 . TYR A 1 36  ? -28.376 -32.058 15.725 1.00 20.90 ? 36  TYR A CD1 1 
ATOM   279  C CD2 . TYR A 1 36  ? -30.633 -32.239 16.429 1.00 16.61 ? 36  TYR A CD2 1 
ATOM   280  C CE1 . TYR A 1 36  ? -28.656 -32.809 14.602 1.00 22.42 ? 36  TYR A CE1 1 
ATOM   281  C CE2 . TYR A 1 36  ? -30.925 -32.991 15.303 1.00 22.66 ? 36  TYR A CE2 1 
ATOM   282  C CZ  . TYR A 1 36  ? -29.926 -33.268 14.392 1.00 19.05 ? 36  TYR A CZ  1 
ATOM   283  O OH  . TYR A 1 36  ? -30.183 -34.012 13.273 1.00 24.02 ? 36  TYR A OH  1 
ATOM   284  N N   . GLN A 1 37  ? -29.988 -28.597 19.798 1.00 22.73 ? 37  GLN A N   1 
ATOM   285  C CA  . GLN A 1 37  ? -29.914 -28.081 21.157 1.00 14.64 ? 37  GLN A CA  1 
ATOM   286  C C   . GLN A 1 37  ? -30.197 -29.215 22.143 1.00 21.57 ? 37  GLN A C   1 
ATOM   287  O O   . GLN A 1 37  ? -31.114 -30.004 21.925 1.00 21.32 ? 37  GLN A O   1 
ATOM   288  C CB  . GLN A 1 37  ? -30.951 -26.970 21.348 1.00 19.50 ? 37  GLN A CB  1 
ATOM   289  C CG  . GLN A 1 37  ? -31.030 -26.437 22.774 1.00 22.65 ? 37  GLN A CG  1 
ATOM   290  C CD  . GLN A 1 37  ? -32.138 -25.423 22.959 1.00 25.31 ? 37  GLN A CD  1 
ATOM   291  O OE1 . GLN A 1 37  ? -33.320 -25.755 22.835 1.00 21.20 ? 37  GLN A OE1 1 
ATOM   292  N NE2 . GLN A 1 37  ? -31.762 -24.170 23.254 1.00 21.70 ? 37  GLN A NE2 1 
ATOM   293  N N   . GLN A 1 38  ? -29.419 -29.326 23.217 1.00 16.09 ? 38  GLN A N   1 
ATOM   294  C CA  . GLN A 1 38  ? -29.822 -30.242 24.271 1.00 19.80 ? 38  GLN A CA  1 
ATOM   295  C C   . GLN A 1 38  ? -29.998 -29.560 25.630 1.00 22.29 ? 38  GLN A C   1 
ATOM   296  O O   . GLN A 1 38  ? -29.030 -29.214 26.295 1.00 22.32 ? 38  GLN A O   1 
ATOM   297  C CB  . GLN A 1 38  ? -28.895 -31.452 24.386 1.00 25.70 ? 38  GLN A CB  1 
ATOM   298  C CG  . GLN A 1 38  ? -29.502 -32.546 25.295 1.00 22.13 ? 38  GLN A CG  1 
ATOM   299  C CD  . GLN A 1 38  ? -28.788 -33.872 25.171 1.00 19.20 ? 38  GLN A CD  1 
ATOM   300  O OE1 . GLN A 1 38  ? -27.581 -33.917 24.936 1.00 23.96 ? 38  GLN A OE1 1 
ATOM   301  N NE2 . GLN A 1 38  ? -29.527 -34.958 25.316 1.00 14.51 ? 38  GLN A NE2 1 
ATOM   302  N N   . ARG A 1 39  ? -31.245 -29.367 26.037 1.00 18.77 ? 39  ARG A N   1 
ATOM   303  C CA  . ARG A 1 39  ? -31.500 -28.800 27.348 1.00 25.22 ? 39  ARG A CA  1 
ATOM   304  C C   . ARG A 1 39  ? -31.417 -29.877 28.427 1.00 22.73 ? 39  ARG A C   1 
ATOM   305  O O   . ARG A 1 39  ? -31.398 -31.067 28.122 1.00 20.25 ? 39  ARG A O   1 
ATOM   306  C CB  . ARG A 1 39  ? -32.862 -28.135 27.373 1.00 26.14 ? 39  ARG A CB  1 
ATOM   307  C CG  . ARG A 1 39  ? -32.890 -26.766 26.765 1.00 29.40 ? 39  ARG A CG  1 
ATOM   308  C CD  . ARG A 1 39  ? -34.311 -26.291 26.695 1.00 26.55 ? 39  ARG A CD  1 
ATOM   309  N NE  . ARG A 1 39  ? -34.465 -25.123 25.847 1.00 26.54 ? 39  ARG A NE  1 
ATOM   310  C CZ  . ARG A 1 39  ? -35.642 -24.663 25.444 1.00 46.59 ? 39  ARG A CZ  1 
ATOM   311  N NH1 . ARG A 1 39  ? -36.753 -25.288 25.813 1.00 33.86 ? 39  ARG A NH1 1 
ATOM   312  N NH2 . ARG A 1 39  ? -35.704 -23.586 24.670 1.00 48.45 ? 39  ARG A NH2 1 
ATOM   313  N N   . THR A 1 40  ? -31.360 -29.448 29.681 1.00 21.21 ? 40  THR A N   1 
ATOM   314  C CA  . THR A 1 40  ? -31.273 -30.373 30.808 1.00 24.16 ? 40  THR A CA  1 
ATOM   315  C C   . THR A 1 40  ? -32.428 -31.366 30.793 1.00 23.55 ? 40  THR A C   1 
ATOM   316  O O   . THR A 1 40  ? -33.590 -30.968 30.730 1.00 19.95 ? 40  THR A O   1 
ATOM   317  C CB  . THR A 1 40  ? -31.243 -29.616 32.146 1.00 19.49 ? 40  THR A CB  1 
ATOM   318  O OG1 . THR A 1 40  ? -30.054 -28.821 32.202 1.00 18.67 ? 40  THR A OG1 1 
ATOM   319  C CG2 . THR A 1 40  ? -31.268 -30.586 33.319 1.00 16.04 ? 40  THR A CG2 1 
ATOM   320  N N   . ASN A 1 41  ? -32.081 -32.654 30.809 1.00 23.48 ? 41  ASN A N   1 
ATOM   321  C CA  . ASN A 1 41  ? -33.044 -33.766 30.705 1.00 27.17 ? 41  ASN A CA  1 
ATOM   322  C C   . ASN A 1 41  ? -33.774 -33.975 29.376 1.00 27.53 ? 41  ASN A C   1 
ATOM   323  O O   . ASN A 1 41  ? -34.661 -34.823 29.288 1.00 26.77 ? 41  ASN A O   1 
ATOM   324  C CB  . ASN A 1 41  ? -34.050 -33.732 31.854 1.00 22.71 ? 41  ASN A CB  1 
ATOM   325  C CG  . ASN A 1 41  ? -33.414 -34.109 33.165 1.00 30.06 ? 41  ASN A CG  1 
ATOM   326  O OD1 . ASN A 1 41  ? -33.618 -33.455 34.192 1.00 24.72 ? 41  ASN A OD1 1 
ATOM   327  N ND2 . ASN A 1 41  ? -32.601 -35.161 33.128 1.00 22.78 ? 41  ASN A ND2 1 
ATOM   328  N N   . GLY A 1 42  ? -33.397 -33.227 28.344 1.00 18.29 ? 42  GLY A N   1 
ATOM   329  C CA  . GLY A 1 42  ? -34.104 -33.315 27.076 1.00 23.41 ? 42  GLY A CA  1 
ATOM   330  C C   . GLY A 1 42  ? -33.473 -34.247 26.060 1.00 21.67 ? 42  GLY A C   1 
ATOM   331  O O   . GLY A 1 42  ? -32.379 -34.772 26.259 1.00 22.42 ? 42  GLY A O   1 
ATOM   332  N N   . SER A 1 43  ? -34.186 -34.473 24.967 1.00 22.41 ? 43  SER A N   1 
ATOM   333  C CA  . SER A 1 43  ? -33.591 -35.101 23.797 1.00 16.91 ? 43  SER A CA  1 
ATOM   334  C C   . SER A 1 43  ? -33.189 -33.936 22.916 1.00 18.21 ? 43  SER A C   1 
ATOM   335  O O   . SER A 1 43  ? -33.711 -32.834 23.100 1.00 17.91 ? 43  SER A O   1 
ATOM   336  C CB  . SER A 1 43  ? -34.617 -35.969 23.080 1.00 16.62 ? 43  SER A CB  1 
ATOM   337  O OG  . SER A 1 43  ? -35.338 -36.762 23.994 1.00 24.63 ? 43  SER A OG  1 
ATOM   338  N N   . PRO A 1 44  ? -32.259 -34.157 21.966 1.00 19.01 ? 44  PRO A N   1 
ATOM   339  C CA  . PRO A 1 44  ? -31.864 -33.064 21.064 1.00 18.10 ? 44  PRO A CA  1 
ATOM   340  C C   . PRO A 1 44  ? -33.056 -32.467 20.306 1.00 17.30 ? 44  PRO A C   1 
ATOM   341  O O   . PRO A 1 44  ? -33.996 -33.177 19.942 1.00 17.81 ? 44  PRO A O   1 
ATOM   342  C CB  . PRO A 1 44  ? -30.902 -33.737 20.080 1.00 17.70 ? 44  PRO A CB  1 
ATOM   343  C CG  . PRO A 1 44  ? -30.400 -34.970 20.789 1.00 16.97 ? 44  PRO A CG  1 
ATOM   344  C CD  . PRO A 1 44  ? -31.524 -35.408 21.690 1.00 19.66 ? 44  PRO A CD  1 
ATOM   345  N N   . ARG A 1 45  ? -32.999 -31.155 20.113 1.00 14.64 ? 45  ARG A N   1 
ATOM   346  C CA  . ARG A 1 45  ? -33.974 -30.392 19.347 1.00 18.42 ? 45  ARG A CA  1 
ATOM   347  C C   . ARG A 1 45  ? -33.224 -29.824 18.124 1.00 21.71 ? 45  ARG A C   1 
ATOM   348  O O   . ARG A 1 45  ? -32.185 -29.176 18.267 1.00 21.94 ? 45  ARG A O   1 
ATOM   349  C CB  . ARG A 1 45  ? -34.555 -29.283 20.246 1.00 20.00 ? 45  ARG A CB  1 
ATOM   350  C CG  . ARG A 1 45  ? -35.458 -28.199 19.618 1.00 26.52 ? 45  ARG A CG  1 
ATOM   351  C CD  . ARG A 1 45  ? -35.444 -26.936 20.538 1.00 30.83 ? 45  ARG A CD  1 
ATOM   352  N NE  . ARG A 1 45  ? -36.397 -25.860 20.216 1.00 32.29 ? 45  ARG A NE  1 
ATOM   353  C CZ  . ARG A 1 45  ? -36.478 -24.686 20.858 1.00 35.09 ? 45  ARG A CZ  1 
ATOM   354  N NH1 . ARG A 1 45  ? -35.677 -24.406 21.871 1.00 27.69 ? 45  ARG A NH1 1 
ATOM   355  N NH2 . ARG A 1 45  ? -37.369 -23.775 20.486 1.00 40.64 ? 45  ARG A NH2 1 
ATOM   356  N N   . LEU A 1 46  ? -33.728 -30.119 16.929 1.00 21.91 ? 46  LEU A N   1 
ATOM   357  C CA  . LEU A 1 46  ? -33.154 -29.627 15.670 1.00 18.53 ? 46  LEU A CA  1 
ATOM   358  C C   . LEU A 1 46  ? -33.305 -28.111 15.495 1.00 19.54 ? 46  LEU A C   1 
ATOM   359  O O   . LEU A 1 46  ? -34.414 -27.601 15.460 1.00 24.49 ? 46  LEU A O   1 
ATOM   360  C CB  . LEU A 1 46  ? -33.822 -30.347 14.489 1.00 17.62 ? 46  LEU A CB  1 
ATOM   361  C CG  . LEU A 1 46  ? -33.439 -29.892 13.088 1.00 19.90 ? 46  LEU A CG  1 
ATOM   362  C CD1 . LEU A 1 46  ? -31.968 -30.230 12.812 1.00 23.30 ? 46  LEU A CD1 1 
ATOM   363  C CD2 . LEU A 1 46  ? -34.342 -30.516 12.070 1.00 17.10 ? 46  LEU A CD2 1 
ATOM   364  N N   . LEU A 1 47  ? -32.197 -27.390 15.364 1.00 21.69 ? 47  LEU A N   1 
ATOM   365  C CA  . LEU A 1 47  ? -32.253 -25.932 15.244 1.00 19.31 ? 47  LEU A CA  1 
ATOM   366  C C   . LEU A 1 47  ? -32.064 -25.438 13.808 1.00 33.13 ? 47  LEU A C   1 
ATOM   367  O O   . LEU A 1 47  ? -32.757 -24.525 13.342 1.00 35.94 ? 47  LEU A O   1 
ATOM   368  C CB  . LEU A 1 47  ? -31.162 -25.304 16.106 1.00 22.27 ? 47  LEU A CB  1 
ATOM   369  C CG  . LEU A 1 47  ? -31.197 -25.549 17.616 1.00 17.44 ? 47  LEU A CG  1 
ATOM   370  C CD1 . LEU A 1 47  ? -29.847 -25.186 18.238 1.00 13.26 ? 47  LEU A CD1 1 
ATOM   371  C CD2 . LEU A 1 47  ? -32.338 -24.757 18.242 1.00 12.94 ? 47  LEU A CD2 1 
ATOM   372  N N   . ILE A 1 48  ? -31.090 -26.020 13.120 1.00 29.20 ? 48  ILE A N   1 
ATOM   373  C CA  . ILE A 1 48  ? -30.743 -25.584 11.778 1.00 28.32 ? 48  ILE A CA  1 
ATOM   374  C C   . ILE A 1 48  ? -30.421 -26.805 10.926 1.00 27.72 ? 48  ILE A C   1 
ATOM   375  O O   . ILE A 1 48  ? -29.713 -27.710 11.370 1.00 27.52 ? 48  ILE A O   1 
ATOM   376  C CB  . ILE A 1 48  ? -29.494 -24.658 11.782 1.00 23.60 ? 48  ILE A CB  1 
ATOM   377  C CG1 . ILE A 1 48  ? -29.714 -23.412 12.636 1.00 22.98 ? 48  ILE A CG1 1 
ATOM   378  C CG2 . ILE A 1 48  ? -29.110 -24.261 10.361 1.00 20.02 ? 48  ILE A CG2 1 
ATOM   379  C CD1 . ILE A 1 48  ? -30.710 -22.454 12.072 1.00 25.63 ? 48  ILE A CD1 1 
ATOM   380  N N   . LYS A 1 49  ? -30.908 -26.850 9.717  1.00 21.71 ? 49  LYS A N   1 
ATOM   381  C CA  . LYS A 1 49  ? -30.484 -27.860 8.783  1.00 23.83 ? 49  LYS A CA  1 
ATOM   382  C C   . LYS A 1 49  ? -29.703 -27.269 7.626  1.00 26.98 ? 49  LYS A C   1 
ATOM   383  O O   . LYS A 1 49  ? -29.949 -26.188 7.222  1.00 25.94 ? 49  LYS A O   1 
ATOM   384  C CB  . LYS A 1 49  ? -31.681 -28.648 8.279  1.00 23.12 ? 49  LYS A CB  1 
ATOM   385  C CG  . LYS A 1 49  ? -32.566 -27.857 7.378  1.00 21.84 ? 49  LYS A CG  1 
ATOM   386  C CD  . LYS A 1 49  ? -33.722 -28.665 6.892  1.00 32.53 ? 49  LYS A CD  1 
ATOM   387  C CE  . LYS A 1 49  ? -34.891 -27.762 6.674  1.00 22.23 ? 49  LYS A CE  1 
ATOM   388  N NZ  . LYS A 1 49  ? -35.412 -27.888 5.328  1.00 28.12 ? 49  LYS A NZ  1 
ATOM   389  N N   . TYR A 1 50  ? -28.755 -28.026 7.111  1.00 24.96 ? 50  TYR A N   1 
ATOM   390  C CA  . TYR A 1 50  ? -27.967 -27.633 5.946  1.00 24.17 ? 50  TYR A CA  1 
ATOM   391  C C   . TYR A 1 50  ? -27.328 -26.259 6.127  1.00 26.98 ? 50  TYR A C   1 
ATOM   392  O O   . TYR A 1 50  ? -27.529 -25.351 5.321  1.00 29.81 ? 50  TYR A O   1 
ATOM   393  C CB  . TYR A 1 50  ? -28.806 -27.723 4.670  1.00 21.08 ? 50  TYR A CB  1 
ATOM   394  C CG  . TYR A 1 50  ? -29.187 -29.148 4.335  1.00 25.13 ? 50  TYR A CG  1 
ATOM   395  C CD1 . TYR A 1 50  ? -30.452 -29.650 4.656  1.00 22.23 ? 50  TYR A CD1 1 
ATOM   396  C CD2 . TYR A 1 50  ? -28.273 -30.007 3.719  1.00 18.98 ? 50  TYR A CD2 1 
ATOM   397  C CE1 . TYR A 1 50  ? -30.805 -30.962 4.351  1.00 18.00 ? 50  TYR A CE1 1 
ATOM   398  C CE2 . TYR A 1 50  ? -28.611 -31.324 3.423  1.00 11.92 ? 50  TYR A CE2 1 
ATOM   399  C CZ  . TYR A 1 50  ? -29.876 -31.792 3.744  1.00 20.12 ? 50  TYR A CZ  1 
ATOM   400  O OH  . TYR A 1 50  ? -30.217 -33.095 3.451  1.00 26.62 ? 50  TYR A OH  1 
ATOM   401  N N   . ALA A 1 51  ? -26.586 -26.128 7.223  1.00 21.66 ? 51  ALA A N   1 
ATOM   402  C CA  . ALA A 1 51  ? -25.807 -24.929 7.538  1.00 27.55 ? 51  ALA A CA  1 
ATOM   403  C C   . ALA A 1 51  ? -26.596 -23.689 7.917  1.00 26.96 ? 51  ALA A C   1 
ATOM   404  O O   . ALA A 1 51  ? -26.261 -23.031 8.904  1.00 19.65 ? 51  ALA A O   1 
ATOM   405  C CB  . ALA A 1 51  ? -24.796 -24.611 6.435  1.00 27.10 ? 51  ALA A CB  1 
ATOM   406  N N   . SER A 1 52  ? -27.646 -23.382 7.157  1.00 24.33 ? 52  SER A N   1 
ATOM   407  C CA  . SER A 1 52  ? -28.287 -22.074 7.282  1.00 26.32 ? 52  SER A CA  1 
ATOM   408  C C   . SER A 1 52  ? -29.806 -22.051 7.257  1.00 18.77 ? 52  SER A C   1 
ATOM   409  O O   . SER A 1 52  ? -30.405 -21.032 7.566  1.00 21.08 ? 52  SER A O   1 
ATOM   410  C CB  . SER A 1 52  ? -27.753 -21.121 6.203  1.00 29.14 ? 52  SER A CB  1 
ATOM   411  O OG  . SER A 1 52  ? -27.817 -21.715 4.905  1.00 38.42 ? 52  SER A OG  1 
ATOM   412  N N   . GLU A 1 53  ? -30.427 -23.163 6.892  1.00 22.83 ? 53  GLU A N   1 
ATOM   413  C CA  . GLU A 1 53  ? -31.872 -23.194 6.671  1.00 16.93 ? 53  GLU A CA  1 
ATOM   414  C C   . GLU A 1 53  ? -32.695 -23.246 7.946  1.00 28.26 ? 53  GLU A C   1 
ATOM   415  O O   . GLU A 1 53  ? -32.360 -23.963 8.897  1.00 33.03 ? 53  GLU A O   1 
ATOM   416  C CB  . GLU A 1 53  ? -32.243 -24.374 5.790  1.00 20.06 ? 53  GLU A CB  1 
ATOM   417  C CG  . GLU A 1 53  ? -31.532 -24.353 4.463  1.00 28.86 ? 53  GLU A CG  1 
ATOM   418  C CD  . GLU A 1 53  ? -31.870 -25.548 3.611  1.00 35.22 ? 53  GLU A CD  1 
ATOM   419  O OE1 . GLU A 1 53  ? -32.663 -26.401 4.082  1.00 34.27 ? 53  GLU A OE1 1 
ATOM   420  O OE2 . GLU A 1 53  ? -31.336 -25.630 2.477  1.00 32.08 ? 53  GLU A OE2 1 
ATOM   421  N N   . SER A 1 54  ? -33.786 -22.489 7.956  1.00 26.13 ? 54  SER A N   1 
ATOM   422  C CA  . SER A 1 54  ? -34.643 -22.416 9.121  1.00 26.99 ? 54  SER A CA  1 
ATOM   423  C C   . SER A 1 54  ? -35.411 -23.700 9.371  1.00 36.38 ? 54  SER A C   1 
ATOM   424  O O   . SER A 1 54  ? -35.685 -24.470 8.443  1.00 30.12 ? 54  SER A O   1 
ATOM   425  C CB  . SER A 1 54  ? -35.614 -21.248 8.996  1.00 30.84 ? 54  SER A CB  1 
ATOM   426  O OG  . SER A 1 54  ? -35.023 -20.062 9.497  1.00 52.30 ? 54  SER A OG  1 
ATOM   427  N N   . ILE A 1 55  ? -35.746 -23.914 10.641 1.00 33.91 ? 55  ILE A N   1 
ATOM   428  C CA  . ILE A 1 55  ? -36.609 -25.005 11.061 1.00 27.38 ? 55  ILE A CA  1 
ATOM   429  C C   . ILE A 1 55  ? -37.821 -24.353 11.691 1.00 27.14 ? 55  ILE A C   1 
ATOM   430  O O   . ILE A 1 55  ? -37.695 -23.355 12.401 1.00 31.23 ? 55  ILE A O   1 
ATOM   431  C CB  . ILE A 1 55  ? -35.907 -25.900 12.099 1.00 31.05 ? 55  ILE A CB  1 
ATOM   432  C CG1 . ILE A 1 55  ? -34.588 -26.404 11.537 1.00 23.87 ? 55  ILE A CG1 1 
ATOM   433  C CG2 . ILE A 1 55  ? -36.797 -27.071 12.498 1.00 26.59 ? 55  ILE A CG2 1 
ATOM   434  C CD1 . ILE A 1 55  ? -34.772 -27.294 10.350 1.00 24.18 ? 55  ILE A CD1 1 
ATOM   435  N N   . SER A 1 56  ? -39.003 -24.883 11.420 1.00 35.33 ? 56  SER A N   1 
ATOM   436  C CA  . SER A 1 56  ? -40.214 -24.230 11.886 1.00 32.82 ? 56  SER A CA  1 
ATOM   437  C C   . SER A 1 56  ? -40.353 -24.418 13.392 1.00 40.14 ? 56  SER A C   1 
ATOM   438  O O   . SER A 1 56  ? -40.102 -25.508 13.913 1.00 36.35 ? 56  SER A O   1 
ATOM   439  C CB  . SER A 1 56  ? -41.427 -24.815 11.184 1.00 36.33 ? 56  SER A CB  1 
ATOM   440  O OG  . SER A 1 56  ? -41.827 -26.004 11.841 1.00 47.63 ? 56  SER A OG  1 
ATOM   441  N N   . GLY A 1 57  ? -40.744 -23.355 14.089 1.00 33.09 ? 57  GLY A N   1 
ATOM   442  C CA  . GLY A 1 57  ? -40.918 -23.408 15.529 1.00 31.02 ? 57  GLY A CA  1 
ATOM   443  C C   . GLY A 1 57  ? -39.712 -22.918 16.309 1.00 33.51 ? 57  GLY A C   1 
ATOM   444  O O   . GLY A 1 57  ? -39.783 -22.714 17.518 1.00 38.50 ? 57  GLY A O   1 
ATOM   445  N N   . ILE A 1 58  ? -38.598 -22.736 15.611 1.00 39.65 ? 58  ILE A N   1 
ATOM   446  C CA  . ILE A 1 58  ? -37.355 -22.286 16.221 1.00 27.65 ? 58  ILE A CA  1 
ATOM   447  C C   . ILE A 1 58  ? -37.271 -20.772 16.129 1.00 24.70 ? 58  ILE A C   1 
ATOM   448  O O   . ILE A 1 58  ? -37.395 -20.215 15.045 1.00 38.16 ? 58  ILE A O   1 
ATOM   449  C CB  . ILE A 1 58  ? -36.138 -22.927 15.499 1.00 26.98 ? 58  ILE A CB  1 
ATOM   450  C CG1 . ILE A 1 58  ? -36.197 -24.458 15.601 1.00 25.75 ? 58  ILE A CG1 1 
ATOM   451  C CG2 . ILE A 1 58  ? -34.811 -22.395 16.045 1.00 23.43 ? 58  ILE A CG2 1 
ATOM   452  C CD1 . ILE A 1 58  ? -36.284 -24.976 17.021 1.00 22.69 ? 58  ILE A CD1 1 
ATOM   453  N N   . PRO A 1 59  ? -37.056 -20.099 17.265 1.00 22.13 ? 59  PRO A N   1 
ATOM   454  C CA  . PRO A 1 59  ? -36.929 -18.637 17.326 1.00 26.17 ? 59  PRO A CA  1 
ATOM   455  C C   . PRO A 1 59  ? -35.945 -18.086 16.290 1.00 30.26 ? 59  PRO A C   1 
ATOM   456  O O   . PRO A 1 59  ? -34.949 -18.732 15.986 1.00 28.32 ? 59  PRO A O   1 
ATOM   457  C CB  . PRO A 1 59  ? -36.368 -18.394 18.728 1.00 26.21 ? 59  PRO A CB  1 
ATOM   458  C CG  . PRO A 1 59  ? -36.845 -19.563 19.526 1.00 40.07 ? 59  PRO A CG  1 
ATOM   459  C CD  . PRO A 1 59  ? -36.849 -20.734 18.578 1.00 34.05 ? 59  PRO A CD  1 
ATOM   460  N N   . SER A 1 60  ? -36.212 -16.889 15.782 1.00 29.19 ? 60  SER A N   1 
ATOM   461  C CA  . SER A 1 60  ? -35.380 -16.299 14.740 1.00 35.04 ? 60  SER A CA  1 
ATOM   462  C C   . SER A 1 60  ? -33.972 -15.943 15.223 1.00 36.07 ? 60  SER A C   1 
ATOM   463  O O   . SER A 1 60  ? -33.080 -15.669 14.409 1.00 31.10 ? 60  SER A O   1 
ATOM   464  C CB  . SER A 1 60  ? -36.055 -15.051 14.176 1.00 31.30 ? 60  SER A CB  1 
ATOM   465  O OG  . SER A 1 60  ? -36.053 -14.024 15.154 1.00 37.75 ? 60  SER A OG  1 
ATOM   466  N N   . ARG A 1 61  ? -33.764 -15.936 16.538 1.00 33.30 ? 61  ARG A N   1 
ATOM   467  C CA  . ARG A 1 61  ? -32.457 -15.564 17.064 1.00 24.81 ? 61  ARG A CA  1 
ATOM   468  C C   . ARG A 1 61  ? -31.414 -16.627 16.717 1.00 33.03 ? 61  ARG A C   1 
ATOM   469  O O   . ARG A 1 61  ? -30.209 -16.371 16.782 1.00 23.40 ? 61  ARG A O   1 
ATOM   470  C CB  . ARG A 1 61  ? -32.513 -15.295 18.570 1.00 28.19 ? 61  ARG A CB  1 
ATOM   471  C CG  . ARG A 1 61  ? -32.714 -16.512 19.464 1.00 28.01 ? 61  ARG A CG  1 
ATOM   472  C CD  . ARG A 1 61  ? -32.777 -16.067 20.931 1.00 35.26 ? 61  ARG A CD  1 
ATOM   473  N NE  . ARG A 1 61  ? -33.112 -17.166 21.820 1.00 23.22 ? 61  ARG A NE  1 
ATOM   474  C CZ  . ARG A 1 61  ? -34.353 -17.489 22.156 1.00 36.41 ? 61  ARG A CZ  1 
ATOM   475  N NH1 . ARG A 1 61  ? -35.367 -16.776 21.685 1.00 37.77 ? 61  ARG A NH1 1 
ATOM   476  N NH2 . ARG A 1 61  ? -34.579 -18.519 22.962 1.00 34.29 ? 61  ARG A NH2 1 
ATOM   477  N N   . PHE A 1 62  ? -31.887 -17.813 16.338 1.00 21.28 ? 62  PHE A N   1 
ATOM   478  C CA  . PHE A 1 62  ? -31.005 -18.892 15.925 1.00 23.77 ? 62  PHE A CA  1 
ATOM   479  C C   . PHE A 1 62  ? -30.760 -18.855 14.426 1.00 27.07 ? 62  PHE A C   1 
ATOM   480  O O   . PHE A 1 62  ? -31.703 -18.943 13.639 1.00 34.04 ? 62  PHE A O   1 
ATOM   481  C CB  . PHE A 1 62  ? -31.608 -20.249 16.294 1.00 25.63 ? 62  PHE A CB  1 
ATOM   482  C CG  . PHE A 1 62  ? -31.668 -20.506 17.773 1.00 20.97 ? 62  PHE A CG  1 
ATOM   483  C CD1 . PHE A 1 62  ? -32.809 -20.202 18.500 1.00 26.15 ? 62  PHE A CD1 1 
ATOM   484  C CD2 . PHE A 1 62  ? -30.591 -21.065 18.431 1.00 20.77 ? 62  PHE A CD2 1 
ATOM   485  C CE1 . PHE A 1 62  ? -32.874 -20.428 19.875 1.00 26.54 ? 62  PHE A CE1 1 
ATOM   486  C CE2 . PHE A 1 62  ? -30.640 -21.303 19.808 1.00 31.27 ? 62  PHE A CE2 1 
ATOM   487  C CZ  . PHE A 1 62  ? -31.792 -20.979 20.533 1.00 23.46 ? 62  PHE A CZ  1 
ATOM   488  N N   . SER A 1 63  ? -29.495 -18.734 14.034 1.00 24.07 ? 63  SER A N   1 
ATOM   489  C CA  . SER A 1 63  ? -29.093 -18.867 12.629 1.00 27.64 ? 63  SER A CA  1 
ATOM   490  C C   . SER A 1 63  ? -27.742 -19.583 12.518 1.00 31.43 ? 63  SER A C   1 
ATOM   491  O O   . SER A 1 63  ? -27.012 -19.717 13.510 1.00 27.41 ? 63  SER A O   1 
ATOM   492  C CB  . SER A 1 63  ? -29.017 -17.501 11.944 1.00 21.64 ? 63  SER A CB  1 
ATOM   493  O OG  . SER A 1 63  ? -28.005 -16.699 12.527 1.00 33.38 ? 63  SER A OG  1 
ATOM   494  N N   . GLY A 1 64  ? -27.415 -20.048 11.316 1.00 25.69 ? 64  GLY A N   1 
ATOM   495  C CA  . GLY A 1 64  ? -26.134 -20.682 11.081 1.00 18.31 ? 64  GLY A CA  1 
ATOM   496  C C   . GLY A 1 64  ? -25.549 -20.349 9.726  1.00 22.55 ? 64  GLY A C   1 
ATOM   497  O O   . GLY A 1 64  ? -26.272 -20.023 8.785  1.00 23.51 ? 64  GLY A O   1 
ATOM   498  N N   . SER A 1 65  ? -24.229 -20.434 9.621  1.00 26.67 ? 65  SER A N   1 
ATOM   499  C CA  . SER A 1 65  ? -23.559 -20.162 8.360  1.00 25.29 ? 65  SER A CA  1 
ATOM   500  C C   . SER A 1 65  ? -22.339 -21.059 8.178  1.00 30.32 ? 65  SER A C   1 
ATOM   501  O O   . SER A 1 65  ? -21.989 -21.852 9.066  1.00 32.17 ? 65  SER A O   1 
ATOM   502  C CB  . SER A 1 65  ? -23.171 -18.684 8.264  1.00 23.80 ? 65  SER A CB  1 
ATOM   503  O OG  . SER A 1 65  ? -22.087 -18.395 9.128  1.00 37.99 ? 65  SER A OG  1 
ATOM   504  N N   . GLY A 1 66  ? -21.702 -20.929 7.020  1.00 24.61 ? 66  GLY A N   1 
ATOM   505  C CA  . GLY A 1 66  ? -20.523 -21.707 6.709  1.00 23.65 ? 66  GLY A CA  1 
ATOM   506  C C   . GLY A 1 66  ? -20.722 -22.685 5.562  1.00 30.69 ? 66  GLY A C   1 
ATOM   507  O O   . GLY A 1 66  ? -21.858 -23.000 5.167  1.00 20.21 ? 66  GLY A O   1 
ATOM   508  N N   . SER A 1 67  ? -19.587 -23.138 5.028  1.00 29.49 ? 67  SER A N   1 
ATOM   509  C CA  . SER A 1 67  ? -19.493 -24.195 4.020  1.00 31.13 ? 67  SER A CA  1 
ATOM   510  C C   . SER A 1 67  ? -18.036 -24.674 3.955  1.00 30.50 ? 67  SER A C   1 
ATOM   511  O O   . SER A 1 67  ? -17.126 -23.990 4.434  1.00 29.99 ? 67  SER A O   1 
ATOM   512  C CB  . SER A 1 67  ? -19.911 -23.704 2.643  1.00 29.62 ? 67  SER A CB  1 
ATOM   513  O OG  . SER A 1 67  ? -18.923 -22.835 2.133  1.00 46.13 ? 67  SER A OG  1 
ATOM   514  N N   . GLY A 1 68  ? -17.818 -25.851 3.378  1.00 21.66 ? 68  GLY A N   1 
ATOM   515  C CA  . GLY A 1 68  ? -16.497 -26.447 3.364  1.00 21.08 ? 68  GLY A CA  1 
ATOM   516  C C   . GLY A 1 68  ? -16.221 -27.176 4.664  1.00 28.76 ? 68  GLY A C   1 
ATOM   517  O O   . GLY A 1 68  ? -16.674 -28.301 4.858  1.00 29.99 ? 68  GLY A O   1 
ATOM   518  N N   . THR A 1 69  ? -15.475 -26.539 5.562  1.00 27.70 ? 69  THR A N   1 
ATOM   519  C CA  . THR A 1 69  ? -15.125 -27.177 6.825  1.00 31.03 ? 69  THR A CA  1 
ATOM   520  C C   . THR A 1 69  ? -15.344 -26.300 8.052  1.00 32.08 ? 69  THR A C   1 
ATOM   521  O O   . THR A 1 69  ? -15.224 -26.779 9.177  1.00 33.48 ? 69  THR A O   1 
ATOM   522  C CB  . THR A 1 69  ? -13.654 -27.630 6.843  1.00 26.49 ? 69  THR A CB  1 
ATOM   523  O OG1 . THR A 1 69  ? -12.812 -26.492 6.661  1.00 27.07 ? 69  THR A OG1 1 
ATOM   524  C CG2 . THR A 1 69  ? -13.382 -28.642 5.761  1.00 25.73 ? 69  THR A CG2 1 
ATOM   525  N N   . ASP A 1 70  ? -15.654 -25.026 7.843  1.00 27.01 ? 70  ASP A N   1 
ATOM   526  C CA  . ASP A 1 70  ? -15.747 -24.089 8.956  1.00 25.21 ? 70  ASP A CA  1 
ATOM   527  C C   . ASP A 1 70  ? -17.173 -23.535 9.091  1.00 32.71 ? 70  ASP A C   1 
ATOM   528  O O   . ASP A 1 70  ? -17.639 -22.764 8.238  1.00 31.94 ? 70  ASP A O   1 
ATOM   529  C CB  . ASP A 1 70  ? -14.725 -22.967 8.774  1.00 30.41 ? 70  ASP A CB  1 
ATOM   530  C CG  . ASP A 1 70  ? -14.579 -22.086 10.006 1.00 41.12 ? 70  ASP A CG  1 
ATOM   531  O OD1 . ASP A 1 70  ? -15.090 -22.462 11.084 1.00 46.40 ? 70  ASP A OD1 1 
ATOM   532  O OD2 . ASP A 1 70  ? -13.937 -21.011 9.895  1.00 40.18 ? 70  ASP A OD2 1 
ATOM   533  N N   . PHE A 1 71  ? -17.853 -23.938 10.170 1.00 24.87 ? 71  PHE A N   1 
ATOM   534  C CA  . PHE A 1 71  ? -19.271 -23.642 10.382 1.00 26.65 ? 71  PHE A CA  1 
ATOM   535  C C   . PHE A 1 71  ? -19.563 -22.877 11.667 1.00 30.03 ? 71  PHE A C   1 
ATOM   536  O O   . PHE A 1 71  ? -18.834 -22.988 12.664 1.00 24.21 ? 71  PHE A O   1 
ATOM   537  C CB  . PHE A 1 71  ? -20.079 -24.943 10.359 1.00 26.85 ? 71  PHE A CB  1 
ATOM   538  C CG  . PHE A 1 71  ? -19.955 -25.690 9.065  1.00 30.33 ? 71  PHE A CG  1 
ATOM   539  C CD1 . PHE A 1 71  ? -20.708 -25.318 7.964  1.00 26.87 ? 71  PHE A CD1 1 
ATOM   540  C CD2 . PHE A 1 71  ? -19.063 -26.738 8.940  1.00 23.64 ? 71  PHE A CD2 1 
ATOM   541  C CE1 . PHE A 1 71  ? -20.584 -25.987 6.776  1.00 24.09 ? 71  PHE A CE1 1 
ATOM   542  C CE2 . PHE A 1 71  ? -18.935 -27.408 7.753  1.00 27.59 ? 71  PHE A CE2 1 
ATOM   543  C CZ  . PHE A 1 71  ? -19.699 -27.033 6.666  1.00 26.14 ? 71  PHE A CZ  1 
ATOM   544  N N   . THR A 1 72  ? -20.647 -22.108 11.644 1.00 30.35 ? 72  THR A N   1 
ATOM   545  C CA  . THR A 1 72  ? -21.022 -21.302 12.802 1.00 24.89 ? 72  THR A CA  1 
ATOM   546  C C   . THR A 1 72  ? -22.515 -21.340 13.103 1.00 24.59 ? 72  THR A C   1 
ATOM   547  O O   . THR A 1 72  ? -23.335 -21.160 12.218 1.00 24.25 ? 72  THR A O   1 
ATOM   548  C CB  . THR A 1 72  ? -20.572 -19.831 12.646 1.00 23.01 ? 72  THR A CB  1 
ATOM   549  O OG1 . THR A 1 72  ? -19.148 -19.783 12.474 1.00 16.77 ? 72  THR A OG1 1 
ATOM   550  C CG2 . THR A 1 72  ? -20.971 -19.005 13.882 1.00 23.59 ? 72  THR A CG2 1 
ATOM   551  N N   . LEU A 1 73  ? -22.847 -21.587 14.368 1.00 27.63 ? 73  LEU A N   1 
ATOM   552  C CA  . LEU A 1 73  ? -24.211 -21.449 14.872 1.00 26.08 ? 73  LEU A CA  1 
ATOM   553  C C   . LEU A 1 73  ? -24.267 -20.165 15.682 1.00 23.13 ? 73  LEU A C   1 
ATOM   554  O O   . LEU A 1 73  ? -23.391 -19.902 16.497 1.00 25.06 ? 73  LEU A O   1 
ATOM   555  C CB  . LEU A 1 73  ? -24.592 -22.642 15.757 1.00 25.17 ? 73  LEU A CB  1 
ATOM   556  C CG  . LEU A 1 73  ? -25.942 -22.579 16.484 1.00 25.42 ? 73  LEU A CG  1 
ATOM   557  C CD1 . LEU A 1 73  ? -27.122 -22.619 15.506 1.00 20.14 ? 73  LEU A CD1 1 
ATOM   558  C CD2 . LEU A 1 73  ? -26.048 -23.704 17.503 1.00 23.88 ? 73  LEU A CD2 1 
ATOM   559  N N   . SER A 1 74  ? -25.285 -19.352 15.451 1.00 22.98 ? 74  SER A N   1 
ATOM   560  C CA  . SER A 1 74  ? -25.349 -18.067 16.121 1.00 22.56 ? 74  SER A CA  1 
ATOM   561  C C   . SER A 1 74  ? -26.670 -17.805 16.828 1.00 26.32 ? 74  SER A C   1 
ATOM   562  O O   . SER A 1 74  ? -27.741 -18.121 16.309 1.00 28.96 ? 74  SER A O   1 
ATOM   563  C CB  . SER A 1 74  ? -25.043 -16.940 15.140 1.00 29.51 ? 74  SER A CB  1 
ATOM   564  O OG  . SER A 1 74  ? -23.650 -16.883 14.886 1.00 32.87 ? 74  SER A OG  1 
ATOM   565  N N   . ILE A 1 75  ? -26.573 -17.246 18.028 1.00 25.11 ? 75  ILE A N   1 
ATOM   566  C CA  . ILE A 1 75  ? -27.734 -16.714 18.728 1.00 34.53 ? 75  ILE A CA  1 
ATOM   567  C C   . ILE A 1 75  ? -27.521 -15.213 18.902 1.00 32.19 ? 75  ILE A C   1 
ATOM   568  O O   . ILE A 1 75  ? -26.596 -14.794 19.611 1.00 35.74 ? 75  ILE A O   1 
ATOM   569  C CB  . ILE A 1 75  ? -27.933 -17.378 20.104 1.00 31.77 ? 75  ILE A CB  1 
ATOM   570  C CG1 . ILE A 1 75  ? -27.814 -18.897 19.985 1.00 27.24 ? 75  ILE A CG1 1 
ATOM   571  C CG2 . ILE A 1 75  ? -29.286 -16.978 20.690 1.00 26.38 ? 75  ILE A CG2 1 
ATOM   572  C CD1 . ILE A 1 75  ? -27.925 -19.619 21.300 1.00 28.28 ? 75  ILE A CD1 1 
ATOM   573  N N   . ASN A 1 76  ? -28.353 -14.402 18.251 1.00 32.90 ? 76  ASN A N   1 
ATOM   574  C CA  . ASN A 1 76  ? -28.064 -12.966 18.182 1.00 45.05 ? 76  ASN A CA  1 
ATOM   575  C C   . ASN A 1 76  ? -28.302 -12.197 19.480 1.00 42.95 ? 76  ASN A C   1 
ATOM   576  O O   . ASN A 1 76  ? -27.703 -11.144 19.699 1.00 47.84 ? 76  ASN A O   1 
ATOM   577  C CB  . ASN A 1 76  ? -28.750 -12.285 16.990 1.00 39.67 ? 76  ASN A CB  1 
ATOM   578  C CG  . ASN A 1 76  ? -30.231 -12.511 16.964 1.00 52.47 ? 76  ASN A CG  1 
ATOM   579  O OD1 . ASN A 1 76  ? -30.859 -12.683 18.009 1.00 50.50 ? 76  ASN A OD1 1 
ATOM   580  N ND2 . ASN A 1 76  ? -30.812 -12.510 15.761 1.00 56.61 ? 76  ASN A ND2 1 
ATOM   581  N N   . SER A 1 77  ? -29.166 -12.730 20.335 1.00 36.22 ? 77  SER A N   1 
ATOM   582  C CA  . SER A 1 77  ? -29.395 -12.144 21.647 1.00 36.94 ? 77  SER A CA  1 
ATOM   583  C C   . SER A 1 77  ? -29.863 -13.239 22.599 1.00 42.04 ? 77  SER A C   1 
ATOM   584  O O   . SER A 1 77  ? -31.049 -13.573 22.660 1.00 43.30 ? 77  SER A O   1 
ATOM   585  C CB  . SER A 1 77  ? -30.423 -11.018 21.562 1.00 29.44 ? 77  SER A CB  1 
ATOM   586  O OG  . SER A 1 77  ? -30.309 -10.148 22.672 1.00 42.37 ? 77  SER A OG  1 
ATOM   587  N N   . VAL A 1 78  ? -28.913 -13.787 23.344 1.00 32.17 ? 78  VAL A N   1 
ATOM   588  C CA  A VAL A 1 78  ? -29.170 -14.961 24.163 0.46 35.21 ? 78  VAL A CA  1 
ATOM   589  C CA  B VAL A 1 78  ? -29.162 -14.959 24.177 0.54 35.21 ? 78  VAL A CA  1 
ATOM   590  C C   . VAL A 1 78  ? -30.166 -14.699 25.296 1.00 36.84 ? 78  VAL A C   1 
ATOM   591  O O   . VAL A 1 78  ? -30.093 -13.690 25.991 1.00 38.81 ? 78  VAL A O   1 
ATOM   592  C CB  A VAL A 1 78  ? -27.844 -15.544 24.723 0.46 35.49 ? 78  VAL A CB  1 
ATOM   593  C CB  B VAL A 1 78  ? -27.847 -15.490 24.777 0.54 35.56 ? 78  VAL A CB  1 
ATOM   594  C CG1 A VAL A 1 78  ? -27.092 -14.486 25.512 0.46 33.46 ? 78  VAL A CG1 1 
ATOM   595  C CG1 B VAL A 1 78  ? -28.103 -16.723 25.626 0.54 36.33 ? 78  VAL A CG1 1 
ATOM   596  C CG2 A VAL A 1 78  ? -28.110 -16.772 25.575 0.46 36.41 ? 78  VAL A CG2 1 
ATOM   597  C CG2 B VAL A 1 78  ? -26.871 -15.805 23.674 0.54 31.71 ? 78  VAL A CG2 1 
ATOM   598  N N   . GLU A 1 79  ? -31.111 -15.617 25.459 1.00 35.96 ? 79  GLU A N   1 
ATOM   599  C CA  . GLU A 1 79  ? -32.020 -15.587 26.591 1.00 33.63 ? 79  GLU A CA  1 
ATOM   600  C C   . GLU A 1 79  ? -31.614 -16.697 27.557 1.00 32.80 ? 79  GLU A C   1 
ATOM   601  O O   . GLU A 1 79  ? -30.855 -17.595 27.193 1.00 31.31 ? 79  GLU A O   1 
ATOM   602  C CB  . GLU A 1 79  ? -33.456 -15.787 26.122 1.00 33.18 ? 79  GLU A CB  1 
ATOM   603  C CG  . GLU A 1 79  ? -33.928 -14.725 25.156 1.00 39.68 ? 79  GLU A CG  1 
ATOM   604  C CD  . GLU A 1 79  ? -35.338 -14.976 24.669 1.00 57.98 ? 79  GLU A CD  1 
ATOM   605  O OE1 . GLU A 1 79  ? -35.999 -15.888 25.215 1.00 54.61 ? 79  GLU A OE1 1 
ATOM   606  O OE2 . GLU A 1 79  ? -35.784 -14.265 23.740 1.00 65.64 ? 79  GLU A OE2 1 
ATOM   607  N N   . SER A 1 80  ? -32.115 -16.644 28.785 1.00 29.37 ? 80  SER A N   1 
ATOM   608  C CA  . SER A 1 80  ? -31.754 -17.637 29.797 1.00 37.27 ? 80  SER A CA  1 
ATOM   609  C C   . SER A 1 80  ? -32.233 -19.032 29.388 1.00 29.75 ? 80  SER A C   1 
ATOM   610  O O   . SER A 1 80  ? -31.645 -20.045 29.768 1.00 31.62 ? 80  SER A O   1 
ATOM   611  C CB  . SER A 1 80  ? -32.285 -17.248 31.185 1.00 32.12 ? 80  SER A CB  1 
ATOM   612  O OG  . SER A 1 80  ? -33.706 -17.232 31.210 1.00 45.98 ? 80  SER A OG  1 
ATOM   613  N N   . GLU A 1 81  ? -33.285 -19.071 28.585 1.00 24.68 ? 81  GLU A N   1 
ATOM   614  C CA  . GLU A 1 81  ? -33.825 -20.324 28.077 1.00 31.63 ? 81  GLU A CA  1 
ATOM   615  C C   . GLU A 1 81  ? -32.809 -21.025 27.173 1.00 30.39 ? 81  GLU A C   1 
ATOM   616  O O   . GLU A 1 81  ? -32.906 -22.220 26.932 1.00 33.85 ? 81  GLU A O   1 
ATOM   617  C CB  . GLU A 1 81  ? -35.134 -20.068 27.306 1.00 39.37 ? 81  GLU A CB  1 
ATOM   618  C CG  . GLU A 1 81  ? -36.334 -19.603 28.162 1.00 46.20 ? 81  GLU A CG  1 
ATOM   619  C CD  . GLU A 1 81  ? -36.196 -18.176 28.724 1.00 52.84 ? 81  GLU A CD  1 
ATOM   620  O OE1 . GLU A 1 81  ? -35.536 -17.321 28.080 1.00 41.82 ? 81  GLU A OE1 1 
ATOM   621  O OE2 . GLU A 1 81  ? -36.756 -17.914 29.818 1.00 44.65 ? 81  GLU A OE2 1 
ATOM   622  N N   . ASP A 1 82  ? -31.833 -20.275 26.676 1.00 25.69 ? 82  ASP A N   1 
ATOM   623  C CA  . ASP A 1 82  ? -30.844 -20.838 25.772 1.00 27.31 ? 82  ASP A CA  1 
ATOM   624  C C   . ASP A 1 82  ? -29.757 -21.655 26.468 1.00 23.83 ? 82  ASP A C   1 
ATOM   625  O O   . ASP A 1 82  ? -28.881 -22.200 25.794 1.00 24.79 ? 82  ASP A O   1 
ATOM   626  C CB  . ASP A 1 82  ? -30.211 -19.747 24.906 1.00 26.63 ? 82  ASP A CB  1 
ATOM   627  C CG  . ASP A 1 82  ? -31.231 -19.033 24.037 1.00 30.57 ? 82  ASP A CG  1 
ATOM   628  O OD1 . ASP A 1 82  ? -32.256 -19.662 23.685 1.00 24.93 ? 82  ASP A OD1 1 
ATOM   629  O OD2 . ASP A 1 82  ? -31.014 -17.844 23.713 1.00 28.86 ? 82  ASP A OD2 1 
ATOM   630  N N   . ILE A 1 83  ? -29.793 -21.727 27.802 1.00 26.23 ? 83  ILE A N   1 
ATOM   631  C CA  . ILE A 1 83  ? -28.869 -22.587 28.546 1.00 23.69 ? 83  ILE A CA  1 
ATOM   632  C C   . ILE A 1 83  ? -29.058 -24.021 28.070 1.00 19.02 ? 83  ILE A C   1 
ATOM   633  O O   . ILE A 1 83  ? -30.152 -24.560 28.154 1.00 21.77 ? 83  ILE A O   1 
ATOM   634  C CB  . ILE A 1 83  ? -29.090 -22.506 30.078 1.00 25.83 ? 83  ILE A CB  1 
ATOM   635  C CG1 . ILE A 1 83  ? -28.686 -21.127 30.605 1.00 27.30 ? 83  ILE A CG1 1 
ATOM   636  C CG2 . ILE A 1 83  ? -28.278 -23.590 30.800 1.00 26.15 ? 83  ILE A CG2 1 
ATOM   637  C CD1 . ILE A 1 83  ? -29.138 -20.848 32.040 1.00 28.13 ? 83  ILE A CD1 1 
ATOM   638  N N   . ALA A 1 84  ? -27.992 -24.612 27.544 1.00 20.13 ? 84  ALA A N   1 
ATOM   639  C CA  . ALA A 1 84  ? -28.044 -25.932 26.926 1.00 19.41 ? 84  ALA A CA  1 
ATOM   640  C C   . ALA A 1 84  ? -26.682 -26.289 26.374 1.00 19.34 ? 84  ALA A C   1 
ATOM   641  O O   . ALA A 1 84  ? -25.763 -25.475 26.376 1.00 17.59 ? 84  ALA A O   1 
ATOM   642  C CB  . ALA A 1 84  ? -29.067 -25.970 25.785 1.00 15.65 ? 84  ALA A CB  1 
ATOM   643  N N   . ASP A 1 85  ? -26.578 -27.514 25.876 1.00 18.25 ? 85  ASP A N   1 
ATOM   644  C CA  . ASP A 1 85  ? -25.468 -27.901 25.030 1.00 22.57 ? 85  ASP A CA  1 
ATOM   645  C C   . ASP A 1 85  ? -25.892 -27.837 23.558 1.00 21.11 ? 85  ASP A C   1 
ATOM   646  O O   . ASP A 1 85  ? -27.069 -27.964 23.225 1.00 20.88 ? 85  ASP A O   1 
ATOM   647  C CB  . ASP A 1 85  ? -24.980 -29.295 25.399 1.00 23.73 ? 85  ASP A CB  1 
ATOM   648  C CG  . ASP A 1 85  ? -24.741 -29.442 26.885 1.00 28.60 ? 85  ASP A CG  1 
ATOM   649  O OD1 . ASP A 1 85  ? -24.316 -28.448 27.518 1.00 33.69 ? 85  ASP A OD1 1 
ATOM   650  O OD2 . ASP A 1 85  ? -24.989 -30.540 27.424 1.00 29.85 ? 85  ASP A OD2 1 
ATOM   651  N N   . TYR A 1 86  ? -24.920 -27.638 22.680 1.00 25.65 ? 86  TYR A N   1 
ATOM   652  C CA  . TYR A 1 86  ? -25.194 -27.470 21.264 1.00 17.39 ? 86  TYR A CA  1 
ATOM   653  C C   . TYR A 1 86  ? -24.314 -28.400 20.456 1.00 22.53 ? 86  TYR A C   1 
ATOM   654  O O   . TYR A 1 86  ? -23.099 -28.436 20.656 1.00 26.90 ? 86  TYR A O   1 
ATOM   655  C CB  . TYR A 1 86  ? -25.005 -26.002 20.868 1.00 17.93 ? 86  TYR A CB  1 
ATOM   656  C CG  . TYR A 1 86  ? -26.098 -25.127 21.442 1.00 19.39 ? 86  TYR A CG  1 
ATOM   657  C CD1 . TYR A 1 86  ? -26.003 -24.610 22.736 1.00 17.49 ? 86  TYR A CD1 1 
ATOM   658  C CD2 . TYR A 1 86  ? -27.250 -24.864 20.713 1.00 15.44 ? 86  TYR A CD2 1 
ATOM   659  C CE1 . TYR A 1 86  ? -27.013 -23.831 23.268 1.00 16.90 ? 86  TYR A CE1 1 
ATOM   660  C CE2 . TYR A 1 86  ? -28.266 -24.085 21.236 1.00 18.19 ? 86  TYR A CE2 1 
ATOM   661  C CZ  . TYR A 1 86  ? -28.144 -23.570 22.514 1.00 19.55 ? 86  TYR A CZ  1 
ATOM   662  O OH  . TYR A 1 86  ? -29.161 -22.807 23.037 1.00 17.51 ? 86  TYR A OH  1 
ATOM   663  N N   . TYR A 1 87  ? -24.933 -29.170 19.562 1.00 20.15 ? 87  TYR A N   1 
ATOM   664  C CA  . TYR A 1 87  ? -24.212 -30.158 18.761 1.00 20.80 ? 87  TYR A CA  1 
ATOM   665  C C   . TYR A 1 87  ? -24.342 -29.875 17.263 1.00 23.78 ? 87  TYR A C   1 
ATOM   666  O O   . TYR A 1 87  ? -25.395 -29.422 16.784 1.00 23.11 ? 87  TYR A O   1 
ATOM   667  C CB  . TYR A 1 87  ? -24.724 -31.579 19.055 1.00 17.50 ? 87  TYR A CB  1 
ATOM   668  C CG  . TYR A 1 87  ? -24.477 -32.053 20.474 1.00 19.34 ? 87  TYR A CG  1 
ATOM   669  C CD1 . TYR A 1 87  ? -25.416 -31.829 21.475 1.00 16.62 ? 87  TYR A CD1 1 
ATOM   670  C CD2 . TYR A 1 87  ? -23.308 -32.717 20.814 1.00 17.52 ? 87  TYR A CD2 1 
ATOM   671  C CE1 . TYR A 1 87  ? -25.200 -32.253 22.780 1.00 16.17 ? 87  TYR A CE1 1 
ATOM   672  C CE2 . TYR A 1 87  ? -23.078 -33.143 22.107 1.00 16.51 ? 87  TYR A CE2 1 
ATOM   673  C CZ  . TYR A 1 87  ? -24.035 -32.907 23.088 1.00 15.47 ? 87  TYR A CZ  1 
ATOM   674  O OH  . TYR A 1 87  ? -23.831 -33.319 24.379 1.00 22.83 ? 87  TYR A OH  1 
ATOM   675  N N   . CYS A 1 88  ? -23.277 -30.145 16.518 1.00 22.34 ? 88  CYS A N   1 
ATOM   676  C CA  . CYS A 1 88  ? -23.369 -30.137 15.064 1.00 20.89 ? 88  CYS A CA  1 
ATOM   677  C C   . CYS A 1 88  ? -23.328 -31.570 14.519 1.00 20.98 ? 88  CYS A C   1 
ATOM   678  O O   . CYS A 1 88  ? -22.827 -32.479 15.172 1.00 18.51 ? 88  CYS A O   1 
ATOM   679  C CB  . CYS A 1 88  ? -22.257 -29.287 14.464 1.00 18.01 ? 88  CYS A CB  1 
ATOM   680  S SG  . CYS A 1 88  ? -20.630 -29.911 14.848 1.00 24.40 ? 88  CYS A SG  1 
ATOM   681  N N   . GLN A 1 89  ? -23.878 -31.764 13.327 1.00 21.31 ? 89  GLN A N   1 
ATOM   682  C CA  . GLN A 1 89  ? -23.978 -33.086 12.721 1.00 16.83 ? 89  GLN A CA  1 
ATOM   683  C C   . GLN A 1 89  ? -23.660 -32.961 11.242 1.00 21.05 ? 89  GLN A C   1 
ATOM   684  O O   . GLN A 1 89  ? -24.195 -32.068 10.576 1.00 23.39 ? 89  GLN A O   1 
ATOM   685  C CB  . GLN A 1 89  ? -25.400 -33.614 12.884 1.00 16.22 ? 89  GLN A CB  1 
ATOM   686  C CG  . GLN A 1 89  ? -25.657 -34.969 12.237 1.00 14.27 ? 89  GLN A CG  1 
ATOM   687  C CD  . GLN A 1 89  ? -27.118 -35.183 11.866 1.00 17.17 ? 89  GLN A CD  1 
ATOM   688  O OE1 . GLN A 1 89  ? -27.946 -34.277 12.002 1.00 19.14 ? 89  GLN A OE1 1 
ATOM   689  N NE2 . GLN A 1 89  ? -27.441 -36.382 11.381 1.00 14.69 ? 89  GLN A NE2 1 
ATOM   690  N N   . GLN A 1 90  ? -22.786 -33.827 10.723 1.00 22.19 ? 90  GLN A N   1 
ATOM   691  C CA  . GLN A 1 90  ? -22.481 -33.825 9.286  1.00 21.94 ? 90  GLN A CA  1 
ATOM   692  C C   . GLN A 1 90  ? -23.141 -35.008 8.626  1.00 21.51 ? 90  GLN A C   1 
ATOM   693  O O   . GLN A 1 90  ? -23.238 -36.074 9.221  1.00 21.82 ? 90  GLN A O   1 
ATOM   694  C CB  . GLN A 1 90  ? -20.968 -33.863 8.998  1.00 22.07 ? 90  GLN A CB  1 
ATOM   695  C CG  . GLN A 1 90  ? -20.259 -35.225 9.218  1.00 21.93 ? 90  GLN A CG  1 
ATOM   696  C CD  . GLN A 1 90  ? -20.468 -36.240 8.086  1.00 24.91 ? 90  GLN A CD  1 
ATOM   697  O OE1 . GLN A 1 90  ? -20.778 -35.878 6.943  1.00 22.63 ? 90  GLN A OE1 1 
ATOM   698  N NE2 . GLN A 1 90  ? -20.321 -37.522 8.414  1.00 24.15 ? 90  GLN A NE2 1 
ATOM   699  N N   . ASN A 1 91  ? -23.565 -34.836 7.382  1.00 25.31 ? 91  ASN A N   1 
ATOM   700  C CA  . ASN A 1 91  ? -24.108 -35.952 6.631  1.00 24.04 ? 91  ASN A CA  1 
ATOM   701  C C   . ASN A 1 91  ? -23.719 -35.929 5.145  1.00 27.82 ? 91  ASN A C   1 
ATOM   702  O O   . ASN A 1 91  ? -24.449 -36.414 4.271  1.00 28.07 ? 91  ASN A O   1 
ATOM   703  C CB  . ASN A 1 91  ? -25.615 -36.010 6.784  1.00 19.81 ? 91  ASN A CB  1 
ATOM   704  C CG  . ASN A 1 91  ? -26.185 -37.318 6.312  1.00 25.01 ? 91  ASN A CG  1 
ATOM   705  O OD1 . ASN A 1 91  ? -25.612 -38.386 6.555  1.00 24.35 ? 91  ASN A OD1 1 
ATOM   706  N ND2 . ASN A 1 91  ? -27.308 -37.245 5.609  1.00 20.64 ? 91  ASN A ND2 1 
ATOM   707  N N   . ASN A 1 92  ? -22.563 -35.358 4.858  1.00 25.88 ? 92  ASN A N   1 
ATOM   708  C CA  . ASN A 1 92  ? -22.049 -35.390 3.510  1.00 23.42 ? 92  ASN A CA  1 
ATOM   709  C C   . ASN A 1 92  ? -21.490 -36.781 3.236  1.00 22.72 ? 92  ASN A C   1 
ATOM   710  O O   . ASN A 1 92  ? -21.538 -37.256 2.106  1.00 25.34 ? 92  ASN A O   1 
ATOM   711  C CB  . ASN A 1 92  ? -20.989 -34.302 3.317  1.00 25.08 ? 92  ASN A CB  1 
ATOM   712  C CG  . ASN A 1 92  ? -20.502 -34.209 1.884  1.00 32.91 ? 92  ASN A CG  1 
ATOM   713  O OD1 . ASN A 1 92  ? -21.189 -33.667 1.013  1.00 29.14 ? 92  ASN A OD1 1 
ATOM   714  N ND2 . ASN A 1 92  ? -19.307 -34.730 1.634  1.00 27.48 ? 92  ASN A ND2 1 
ATOM   715  N N   . ASN A 1 93  ? -21.000 -37.428 4.297  1.00 27.01 ? 93  ASN A N   1 
ATOM   716  C CA  . ASN A 1 93  ? -20.353 -38.747 4.246  1.00 25.11 ? 93  ASN A CA  1 
ATOM   717  C C   . ASN A 1 93  ? -21.050 -39.737 5.158  1.00 27.23 ? 93  ASN A C   1 
ATOM   718  O O   . ASN A 1 93  ? -21.442 -39.393 6.270  1.00 24.02 ? 93  ASN A O   1 
ATOM   719  C CB  . ASN A 1 93  ? -18.894 -38.666 4.719  1.00 19.31 ? 93  ASN A CB  1 
ATOM   720  C CG  . ASN A 1 93  ? -17.996 -37.928 3.743  1.00 42.81 ? 93  ASN A CG  1 
ATOM   721  O OD1 . ASN A 1 93  ? -18.199 -36.740 3.447  1.00 42.19 ? 93  ASN A OD1 1 
ATOM   722  N ND2 . ASN A 1 93  ? -16.974 -38.623 3.252  1.00 49.40 ? 93  ASN A ND2 1 
ATOM   723  N N   . TRP A 1 94  ? -21.178 -40.976 4.703  1.00 27.12 ? 94  TRP A N   1 
ATOM   724  C CA  . TRP A 1 94  ? -21.730 -42.030 5.531  1.00 25.21 ? 94  TRP A CA  1 
ATOM   725  C C   . TRP A 1 94  ? -20.586 -42.596 6.373  1.00 27.75 ? 94  TRP A C   1 
ATOM   726  O O   . TRP A 1 94  ? -19.497 -42.790 5.846  1.00 29.84 ? 94  TRP A O   1 
ATOM   727  C CB  . TRP A 1 94  ? -22.342 -43.121 4.644  1.00 20.16 ? 94  TRP A CB  1 
ATOM   728  C CG  . TRP A 1 94  ? -23.124 -44.150 5.399  1.00 19.12 ? 94  TRP A CG  1 
ATOM   729  C CD1 . TRP A 1 94  ? -24.474 -44.188 5.567  1.00 19.39 ? 94  TRP A CD1 1 
ATOM   730  C CD2 . TRP A 1 94  ? -22.599 -45.283 6.110  1.00 23.30 ? 94  TRP A CD2 1 
ATOM   731  N NE1 . TRP A 1 94  ? -24.825 -45.270 6.326  1.00 16.92 ? 94  TRP A NE1 1 
ATOM   732  C CE2 . TRP A 1 94  ? -23.695 -45.959 6.677  1.00 24.59 ? 94  TRP A CE2 1 
ATOM   733  C CE3 . TRP A 1 94  ? -21.307 -45.789 6.322  1.00 21.69 ? 94  TRP A CE3 1 
ATOM   734  C CZ2 . TRP A 1 94  ? -23.547 -47.122 7.441  1.00 25.21 ? 94  TRP A CZ2 1 
ATOM   735  C CZ3 . TRP A 1 94  ? -21.157 -46.947 7.085  1.00 18.22 ? 94  TRP A CZ3 1 
ATOM   736  C CH2 . TRP A 1 94  ? -22.271 -47.598 7.636  1.00 22.16 ? 94  TRP A CH2 1 
ATOM   737  N N   . PRO A 1 95  ? -20.822 -42.852 7.681  1.00 26.12 ? 95  PRO A N   1 
ATOM   738  C CA  . PRO A 1 95  ? -22.096 -42.626 8.383  1.00 24.88 ? 95  PRO A CA  1 
ATOM   739  C C   . PRO A 1 95  ? -22.172 -41.198 8.905  1.00 20.06 ? 95  PRO A C   1 
ATOM   740  O O   . PRO A 1 95  ? -21.126 -40.564 9.029  1.00 20.41 ? 95  PRO A O   1 
ATOM   741  C CB  . PRO A 1 95  ? -22.013 -43.610 9.558  1.00 25.04 ? 95  PRO A CB  1 
ATOM   742  C CG  . PRO A 1 95  ? -20.520 -43.644 9.889  1.00 21.75 ? 95  PRO A CG  1 
ATOM   743  C CD  . PRO A 1 95  ? -19.799 -43.450 8.569  1.00 27.11 ? 95  PRO A CD  1 
ATOM   744  N N   . THR A 1 96  ? -23.375 -40.702 9.197  1.00 19.40 ? 96  THR A N   1 
ATOM   745  C CA  . THR A 1 96  ? -23.526 -39.378 9.786  1.00 15.41 ? 96  THR A CA  1 
ATOM   746  C C   . THR A 1 96  ? -22.823 -39.367 11.144 1.00 18.29 ? 96  THR A C   1 
ATOM   747  O O   . THR A 1 96  ? -22.868 -40.356 11.868 1.00 16.05 ? 96  THR A O   1 
ATOM   748  C CB  . THR A 1 96  ? -25.011 -38.970 9.907  1.00 20.27 ? 96  THR A CB  1 
ATOM   749  O OG1 . THR A 1 96  ? -25.112 -37.618 10.369 1.00 16.15 ? 96  THR A OG1 1 
ATOM   750  C CG2 . THR A 1 96  ? -25.769 -39.890 10.860 1.00 16.13 ? 96  THR A CG2 1 
ATOM   751  N N   . THR A 1 97  ? -22.118 -38.279 11.450 1.00 21.30 ? 97  THR A N   1 
ATOM   752  C CA  . THR A 1 97  ? -21.389 -38.157 12.712 1.00 17.33 ? 97  THR A CA  1 
ATOM   753  C C   . THR A 1 97  ? -21.652 -36.818 13.395 1.00 21.16 ? 97  THR A C   1 
ATOM   754  O O   . THR A 1 97  ? -21.956 -35.823 12.740 1.00 23.65 ? 97  THR A O   1 
ATOM   755  C CB  . THR A 1 97  ? -19.851 -38.315 12.525 1.00 21.81 ? 97  THR A CB  1 
ATOM   756  O OG1 . THR A 1 97  ? -19.383 -37.428 11.496 1.00 23.90 ? 97  THR A OG1 1 
ATOM   757  C CG2 . THR A 1 97  ? -19.494 -39.737 12.154 1.00 22.51 ? 97  THR A CG2 1 
ATOM   758  N N   . PHE A 1 98  ? -21.524 -36.790 14.716 1.00 19.48 ? 98  PHE A N   1 
ATOM   759  C CA  . PHE A 1 98  ? -21.817 -35.586 15.486 1.00 17.08 ? 98  PHE A CA  1 
ATOM   760  C C   . PHE A 1 98  ? -20.564 -35.095 16.148 1.00 17.59 ? 98  PHE A C   1 
ATOM   761  O O   . PHE A 1 98  ? -19.673 -35.887 16.450 1.00 24.98 ? 98  PHE A O   1 
ATOM   762  C CB  . PHE A 1 98  ? -22.802 -35.886 16.612 1.00 19.24 ? 98  PHE A CB  1 
ATOM   763  C CG  . PHE A 1 98  ? -24.152 -36.326 16.151 1.00 20.27 ? 98  PHE A CG  1 
ATOM   764  C CD1 . PHE A 1 98  ? -24.374 -37.644 15.789 1.00 18.01 ? 98  PHE A CD1 1 
ATOM   765  C CD2 . PHE A 1 98  ? -25.209 -35.436 16.125 1.00 17.36 ? 98  PHE A CD2 1 
ATOM   766  C CE1 . PHE A 1 98  ? -25.612 -38.059 15.385 1.00 16.79 ? 98  PHE A CE1 1 
ATOM   767  C CE2 . PHE A 1 98  ? -26.449 -35.845 15.727 1.00 16.53 ? 98  PHE A CE2 1 
ATOM   768  C CZ  . PHE A 1 98  ? -26.651 -37.160 15.351 1.00 19.96 ? 98  PHE A CZ  1 
ATOM   769  N N   . GLY A 1 99  ? -20.504 -33.794 16.407 1.00 14.62 ? 99  GLY A N   1 
ATOM   770  C CA  . GLY A 1 99  ? -19.436 -33.243 17.228 1.00 25.76 ? 99  GLY A CA  1 
ATOM   771  C C   . GLY A 1 99  ? -19.634 -33.581 18.700 1.00 17.98 ? 99  GLY A C   1 
ATOM   772  O O   . GLY A 1 99  ? -20.578 -34.289 19.061 1.00 23.19 ? 99  GLY A O   1 
ATOM   773  N N   . ALA A 1 100 ? -18.762 -33.065 19.553 1.00 14.17 ? 100 ALA A N   1 
ATOM   774  C CA  . ALA A 1 100 ? -18.777 -33.433 20.964 1.00 17.39 ? 100 ALA A CA  1 
ATOM   775  C C   . ALA A 1 100 ? -19.626 -32.474 21.794 1.00 25.51 ? 100 ALA A C   1 
ATOM   776  O O   . ALA A 1 100 ? -19.919 -32.739 22.957 1.00 22.80 ? 100 ALA A O   1 
ATOM   777  C CB  . ALA A 1 100 ? -17.356 -33.508 21.514 1.00 9.79  ? 100 ALA A CB  1 
ATOM   778  N N   . GLY A 1 101 ? -20.018 -31.356 21.188 1.00 21.99 ? 101 GLY A N   1 
ATOM   779  C CA  . GLY A 1 101 ? -20.878 -30.392 21.848 1.00 21.45 ? 101 GLY A CA  1 
ATOM   780  C C   . GLY A 1 101 ? -20.158 -29.233 22.518 1.00 25.18 ? 101 GLY A C   1 
ATOM   781  O O   . GLY A 1 101 ? -19.022 -29.366 22.962 1.00 25.20 ? 101 GLY A O   1 
ATOM   782  N N   . THR A 1 102 ? -20.841 -28.095 22.578 1.00 17.49 ? 102 THR A N   1 
ATOM   783  C CA  . THR A 1 102 ? -20.371 -26.928 23.294 1.00 21.73 ? 102 THR A CA  1 
ATOM   784  C C   . THR A 1 102 ? -21.413 -26.562 24.368 1.00 24.62 ? 102 THR A C   1 
ATOM   785  O O   . THR A 1 102 ? -22.622 -26.543 24.100 1.00 21.45 ? 102 THR A O   1 
ATOM   786  C CB  . THR A 1 102 ? -20.157 -25.743 22.314 1.00 22.97 ? 102 THR A CB  1 
ATOM   787  O OG1 . THR A 1 102 ? -19.049 -26.035 21.459 1.00 30.00 ? 102 THR A OG1 1 
ATOM   788  C CG2 . THR A 1 102 ? -19.867 -24.460 23.048 1.00 22.96 ? 102 THR A CG2 1 
ATOM   789  N N   . LYS A 1 103 ? -20.947 -26.292 25.583 1.00 21.30 ? 103 LYS A N   1 
ATOM   790  C CA  . LYS A 1 103 ? -21.825 -25.900 26.676 1.00 19.20 ? 103 LYS A CA  1 
ATOM   791  C C   . LYS A 1 103 ? -22.009 -24.384 26.688 1.00 24.54 ? 103 LYS A C   1 
ATOM   792  O O   . LYS A 1 103 ? -21.034 -23.630 26.614 1.00 26.01 ? 103 LYS A O   1 
ATOM   793  C CB  . LYS A 1 103 ? -21.232 -26.364 28.006 1.00 25.96 ? 103 LYS A CB  1 
ATOM   794  C CG  . LYS A 1 103 ? -22.033 -25.976 29.234 1.00 21.73 ? 103 LYS A CG  1 
ATOM   795  C CD  . LYS A 1 103 ? -21.912 -27.053 30.302 1.00 27.39 ? 103 LYS A CD  1 
ATOM   796  C CE  . LYS A 1 103 ? -22.557 -26.627 31.604 1.00 35.10 ? 103 LYS A CE  1 
ATOM   797  N NZ  . LYS A 1 103 ? -22.713 -27.764 32.559 1.00 37.02 ? 103 LYS A NZ  1 
ATOM   798  N N   . LEU A 1 104 ? -23.260 -23.938 26.762 1.00 22.54 ? 104 LEU A N   1 
ATOM   799  C CA  . LEU A 1 104 ? -23.548 -22.520 26.906 1.00 23.32 ? 104 LEU A CA  1 
ATOM   800  C C   . LEU A 1 104 ? -24.012 -22.192 28.335 1.00 20.92 ? 104 LEU A C   1 
ATOM   801  O O   . LEU A 1 104 ? -25.047 -22.659 28.782 1.00 21.42 ? 104 LEU A O   1 
ATOM   802  C CB  . LEU A 1 104 ? -24.584 -22.062 25.875 1.00 17.44 ? 104 LEU A CB  1 
ATOM   803  C CG  . LEU A 1 104 ? -24.937 -20.577 26.024 1.00 19.35 ? 104 LEU A CG  1 
ATOM   804  C CD1 . LEU A 1 104 ? -23.805 -19.705 25.499 1.00 19.11 ? 104 LEU A CD1 1 
ATOM   805  C CD2 . LEU A 1 104 ? -26.269 -20.207 25.383 1.00 17.95 ? 104 LEU A CD2 1 
ATOM   806  N N   . GLU A 1 105 ? -23.222 -21.397 29.046 1.00 27.46 ? 105 GLU A N   1 
ATOM   807  C CA  . GLU A 1 105 ? -23.565 -20.969 30.396 1.00 27.05 ? 105 GLU A CA  1 
ATOM   808  C C   . GLU A 1 105 ? -23.890 -19.483 30.401 1.00 26.05 ? 105 GLU A C   1 
ATOM   809  O O   . GLU A 1 105 ? -23.296 -18.705 29.651 1.00 24.28 ? 105 GLU A O   1 
ATOM   810  C CB  . GLU A 1 105 ? -22.400 -21.229 31.350 1.00 25.56 ? 105 GLU A CB  1 
ATOM   811  C CG  . GLU A 1 105 ? -21.783 -22.599 31.211 1.00 32.56 ? 105 GLU A CG  1 
ATOM   812  C CD  . GLU A 1 105 ? -21.024 -23.010 32.459 1.00 45.58 ? 105 GLU A CD  1 
ATOM   813  O OE1 . GLU A 1 105 ? -19.848 -22.606 32.582 1.00 39.51 ? 105 GLU A OE1 1 
ATOM   814  O OE2 . GLU A 1 105 ? -21.611 -23.727 33.315 1.00 49.92 ? 105 GLU A OE2 1 
ATOM   815  N N   . LEU A 1 106 ? -24.829 -19.089 31.253 1.00 25.43 ? 106 LEU A N   1 
ATOM   816  C CA  . LEU A 1 106 ? -25.200 -17.690 31.360 1.00 22.56 ? 106 LEU A CA  1 
ATOM   817  C C   . LEU A 1 106 ? -24.676 -17.026 32.615 1.00 29.93 ? 106 LEU A C   1 
ATOM   818  O O   . LEU A 1 106 ? -24.798 -17.571 33.719 1.00 33.01 ? 106 LEU A O   1 
ATOM   819  C CB  . LEU A 1 106 ? -26.705 -17.515 31.293 1.00 23.34 ? 106 LEU A CB  1 
ATOM   820  C CG  . LEU A 1 106 ? -27.077 -16.913 29.944 1.00 30.11 ? 106 LEU A CG  1 
ATOM   821  C CD1 . LEU A 1 106 ? -26.926 -18.022 28.936 1.00 36.14 ? 106 LEU A CD1 1 
ATOM   822  C CD2 . LEU A 1 106 ? -28.472 -16.321 29.942 1.00 26.37 ? 106 LEU A CD2 1 
ATOM   823  N N   . LYS A 1 107 ? -24.087 -15.848 32.441 1.00 26.70 ? 107 LYS A N   1 
ATOM   824  C CA  . LYS A 1 107 ? -23.726 -15.018 33.574 1.00 25.86 ? 107 LYS A CA  1 
ATOM   825  C C   . LYS A 1 107 ? -24.977 -14.312 34.085 1.00 28.75 ? 107 LYS A C   1 
ATOM   826  O O   . LYS A 1 107 ? -25.948 -14.095 33.353 1.00 26.89 ? 107 LYS A O   1 
ATOM   827  C CB  . LYS A 1 107 ? -22.677 -13.978 33.194 1.00 29.13 ? 107 LYS A CB  1 
ATOM   828  C CG  . LYS A 1 107 ? -21.325 -14.534 32.796 1.00 33.58 ? 107 LYS A CG  1 
ATOM   829  C CD  . LYS A 1 107 ? -20.319 -13.407 32.584 1.00 30.59 ? 107 LYS A CD  1 
ATOM   830  C CE  . LYS A 1 107 ? -19.078 -13.898 31.847 1.00 35.30 ? 107 LYS A CE  1 
ATOM   831  N NZ  . LYS A 1 107 ? -18.561 -15.143 32.465 1.00 49.42 ? 107 LYS A NZ  1 
ATOM   832  N N   . ARG A 1 108 ? -24.950 -13.981 35.362 1.00 22.83 ? 108 ARG A N   1 
ATOM   833  C CA  . ARG A 1 108 ? -25.958 -13.124 35.939 1.00 20.99 ? 108 ARG A CA  1 
ATOM   834  C C   . ARG A 1 108 ? -25.348 -12.438 37.149 1.00 23.59 ? 108 ARG A C   1 
ATOM   835  O O   . ARG A 1 108 ? -24.172 -12.631 37.462 1.00 22.98 ? 108 ARG A O   1 
ATOM   836  C CB  . ARG A 1 108 ? -27.192 -13.925 36.327 1.00 27.10 ? 108 ARG A CB  1 
ATOM   837  C CG  . ARG A 1 108 ? -26.929 -15.089 37.264 1.00 16.80 ? 108 ARG A CG  1 
ATOM   838  C CD  . ARG A 1 108 ? -28.185 -15.336 38.051 1.00 18.76 ? 108 ARG A CD  1 
ATOM   839  N NE  . ARG A 1 108 ? -28.407 -14.248 39.007 1.00 21.71 ? 108 ARG A NE  1 
ATOM   840  C CZ  . ARG A 1 108 ? -29.591 -13.910 39.521 1.00 21.11 ? 108 ARG A CZ  1 
ATOM   841  N NH1 . ARG A 1 108 ? -30.696 -14.549 39.164 1.00 20.72 ? 108 ARG A NH1 1 
ATOM   842  N NH2 . ARG A 1 108 ? -29.670 -12.912 40.391 1.00 20.89 ? 108 ARG A NH2 1 
ATOM   843  N N   . THR A 1 109 ? -26.144 -11.631 37.826 1.00 20.51 ? 109 THR A N   1 
ATOM   844  C CA  . THR A 1 109 ? -25.661 -10.959 39.016 1.00 22.53 ? 109 THR A CA  1 
ATOM   845  C C   . THR A 1 109 ? -25.512 -11.975 40.148 1.00 25.51 ? 109 THR A C   1 
ATOM   846  O O   . THR A 1 109 ? -26.184 -13.021 40.157 1.00 21.09 ? 109 THR A O   1 
ATOM   847  C CB  . THR A 1 109 ? -26.627 -9.866  39.446 1.00 19.81 ? 109 THR A CB  1 
ATOM   848  O OG1 . THR A 1 109 ? -27.813 -10.476 39.967 1.00 20.34 ? 109 THR A OG1 1 
ATOM   849  C CG2 . THR A 1 109 ? -26.985 -8.988  38.251 1.00 21.28 ? 109 THR A CG2 1 
ATOM   850  N N   . VAL A 1 110 ? -24.625 -11.663 41.090 1.00 17.03 ? 110 VAL A N   1 
ATOM   851  C CA  . VAL A 1 110 ? -24.454 -12.478 42.287 1.00 18.08 ? 110 VAL A CA  1 
ATOM   852  C C   . VAL A 1 110 ? -25.757 -12.592 43.090 1.00 15.51 ? 110 VAL A C   1 
ATOM   853  O O   . VAL A 1 110 ? -26.486 -11.623 43.244 1.00 20.54 ? 110 VAL A O   1 
ATOM   854  C CB  . VAL A 1 110 ? -23.299 -11.952 43.160 1.00 15.95 ? 110 VAL A CB  1 
ATOM   855  C CG1 . VAL A 1 110 ? -23.234 -12.704 44.481 1.00 14.28 ? 110 VAL A CG1 1 
ATOM   856  C CG2 . VAL A 1 110 ? -21.980 -12.084 42.403 1.00 12.38 ? 110 VAL A CG2 1 
ATOM   857  N N   . ALA A 1 111 ? -26.060 -13.799 43.547 1.00 16.77 ? 111 ALA A N   1 
ATOM   858  C CA  . ALA A 1 111 ? -27.251 -14.047 44.339 1.00 15.82 ? 111 ALA A CA  1 
ATOM   859  C C   . ALA A 1 111 ? -26.844 -14.990 45.458 1.00 17.21 ? 111 ALA A C   1 
ATOM   860  O O   . ALA A 1 111 ? -26.345 -16.087 45.198 1.00 19.62 ? 111 ALA A O   1 
ATOM   861  C CB  . ALA A 1 111 ? -28.345 -14.676 43.485 1.00 11.18 ? 111 ALA A CB  1 
ATOM   862  N N   . ALA A 1 112 ? -27.019 -14.556 46.696 1.00 12.16 ? 112 ALA A N   1 
ATOM   863  C CA  . ALA A 1 112 ? -26.656 -15.380 47.837 1.00 14.96 ? 112 ALA A CA  1 
ATOM   864  C C   . ALA A 1 112 ? -27.670 -16.522 47.945 1.00 15.03 ? 112 ALA A C   1 
ATOM   865  O O   . ALA A 1 112 ? -28.812 -16.349 47.551 1.00 15.10 ? 112 ALA A O   1 
ATOM   866  C CB  . ALA A 1 112 ? -26.643 -14.536 49.104 1.00 12.76 ? 112 ALA A CB  1 
ATOM   867  N N   . PRO A 1 113 ? -27.232 -17.701 48.414 1.00 12.78 ? 113 PRO A N   1 
ATOM   868  C CA  . PRO A 1 113 ? -28.166 -18.810 48.629 1.00 14.12 ? 113 PRO A CA  1 
ATOM   869  C C   . PRO A 1 113 ? -29.086 -18.567 49.816 1.00 18.05 ? 113 PRO A C   1 
ATOM   870  O O   . PRO A 1 113 ? -28.726 -17.833 50.729 1.00 17.15 ? 113 PRO A O   1 
ATOM   871  C CB  . PRO A 1 113 ? -27.244 -20.003 48.938 1.00 13.47 ? 113 PRO A CB  1 
ATOM   872  C CG  . PRO A 1 113 ? -25.936 -19.395 49.367 1.00 10.72 ? 113 PRO A CG  1 
ATOM   873  C CD  . PRO A 1 113 ? -25.826 -18.112 48.591 1.00 14.24 ? 113 PRO A CD  1 
ATOM   874  N N   . SER A 1 114 ? -30.271 -19.162 49.771 1.00 15.00 ? 114 SER A N   1 
ATOM   875  C CA  . SER A 1 114 ? -31.077 -19.371 50.955 1.00 13.04 ? 114 SER A CA  1 
ATOM   876  C C   . SER A 1 114 ? -30.686 -20.746 51.470 1.00 12.30 ? 114 SER A C   1 
ATOM   877  O O   . SER A 1 114 ? -30.613 -21.703 50.708 1.00 18.02 ? 114 SER A O   1 
ATOM   878  C CB  . SER A 1 114 ? -32.562 -19.357 50.605 1.00 12.58 ? 114 SER A CB  1 
ATOM   879  O OG  . SER A 1 114 ? -32.976 -18.079 50.158 1.00 26.19 ? 114 SER A OG  1 
ATOM   880  N N   . VAL A 1 115 ? -30.416 -20.847 52.759 1.00 17.94 ? 115 VAL A N   1 
ATOM   881  C CA  . VAL A 1 115 ? -29.984 -22.110 53.334 1.00 15.74 ? 115 VAL A CA  1 
ATOM   882  C C   . VAL A 1 115 ? -31.060 -22.692 54.222 1.00 16.82 ? 115 VAL A C   1 
ATOM   883  O O   . VAL A 1 115 ? -31.613 -21.995 55.058 1.00 21.83 ? 115 VAL A O   1 
ATOM   884  C CB  . VAL A 1 115 ? -28.743 -21.925 54.206 1.00 16.65 ? 115 VAL A CB  1 
ATOM   885  C CG1 . VAL A 1 115 ? -28.237 -23.283 54.679 1.00 14.55 ? 115 VAL A CG1 1 
ATOM   886  C CG2 . VAL A 1 115 ? -27.671 -21.169 53.450 1.00 13.46 ? 115 VAL A CG2 1 
ATOM   887  N N   . PHE A 1 116 ? -31.342 -23.976 54.049 1.00 19.57 ? 116 PHE A N   1 
ATOM   888  C CA  . PHE A 1 116 ? -32.279 -24.668 54.916 1.00 20.36 ? 116 PHE A CA  1 
ATOM   889  C C   . PHE A 1 116 ? -31.635 -25.971 55.354 1.00 22.34 ? 116 PHE A C   1 
ATOM   890  O O   . PHE A 1 116 ? -30.912 -26.590 54.573 1.00 22.51 ? 116 PHE A O   1 
ATOM   891  C CB  . PHE A 1 116 ? -33.585 -24.942 54.174 1.00 20.81 ? 116 PHE A CB  1 
ATOM   892  C CG  . PHE A 1 116 ? -34.158 -23.736 53.486 1.00 20.47 ? 116 PHE A CG  1 
ATOM   893  C CD1 . PHE A 1 116 ? -33.827 -23.449 52.172 1.00 20.27 ? 116 PHE A CD1 1 
ATOM   894  C CD2 . PHE A 1 116 ? -35.031 -22.895 54.146 1.00 24.70 ? 116 PHE A CD2 1 
ATOM   895  C CE1 . PHE A 1 116 ? -34.346 -22.341 51.532 1.00 20.60 ? 116 PHE A CE1 1 
ATOM   896  C CE2 . PHE A 1 116 ? -35.560 -21.790 53.514 1.00 24.37 ? 116 PHE A CE2 1 
ATOM   897  C CZ  . PHE A 1 116 ? -35.215 -21.512 52.206 1.00 21.25 ? 116 PHE A CZ  1 
ATOM   898  N N   . ILE A 1 117 ? -31.872 -26.383 56.597 1.00 18.01 ? 117 ILE A N   1 
ATOM   899  C CA  . ILE A 1 117 ? -31.337 -27.655 57.076 1.00 15.35 ? 117 ILE A CA  1 
ATOM   900  C C   . ILE A 1 117 ? -32.439 -28.626 57.504 1.00 15.26 ? 117 ILE A C   1 
ATOM   901  O O   . ILE A 1 117 ? -33.387 -28.253 58.171 1.00 25.41 ? 117 ILE A O   1 
ATOM   902  C CB  . ILE A 1 117 ? -30.306 -27.455 58.222 1.00 27.77 ? 117 ILE A CB  1 
ATOM   903  C CG1 . ILE A 1 117 ? -29.629 -28.785 58.591 1.00 13.70 ? 117 ILE A CG1 1 
ATOM   904  C CG2 . ILE A 1 117 ? -30.947 -26.771 59.424 1.00 19.83 ? 117 ILE A CG2 1 
ATOM   905  C CD1 . ILE A 1 117 ? -28.438 -28.607 59.482 1.00 16.68 ? 117 ILE A CD1 1 
ATOM   906  N N   . PHE A 1 118 ? -32.301 -29.880 57.114 1.00 16.42 ? 118 PHE A N   1 
ATOM   907  C CA  . PHE A 1 118 ? -33.310 -30.893 57.391 1.00 18.76 ? 118 PHE A CA  1 
ATOM   908  C C   . PHE A 1 118 ? -32.725 -32.052 58.186 1.00 19.18 ? 118 PHE A C   1 
ATOM   909  O O   . PHE A 1 118 ? -31.888 -32.792 57.677 1.00 18.73 ? 118 PHE A O   1 
ATOM   910  C CB  . PHE A 1 118 ? -33.852 -31.473 56.082 1.00 18.55 ? 118 PHE A CB  1 
ATOM   911  C CG  . PHE A 1 118 ? -34.514 -30.471 55.182 1.00 17.47 ? 118 PHE A CG  1 
ATOM   912  C CD1 . PHE A 1 118 ? -35.861 -30.159 55.338 1.00 15.43 ? 118 PHE A CD1 1 
ATOM   913  C CD2 . PHE A 1 118 ? -33.805 -29.873 54.156 1.00 15.88 ? 118 PHE A CD2 1 
ATOM   914  C CE1 . PHE A 1 118 ? -36.488 -29.254 54.484 1.00 17.52 ? 118 PHE A CE1 1 
ATOM   915  C CE2 . PHE A 1 118 ? -34.418 -28.972 53.306 1.00 16.27 ? 118 PHE A CE2 1 
ATOM   916  C CZ  . PHE A 1 118 ? -35.762 -28.662 53.461 1.00 17.38 ? 118 PHE A CZ  1 
ATOM   917  N N   . PRO A 1 119 ? -33.179 -32.227 59.429 1.00 23.05 ? 119 PRO A N   1 
ATOM   918  C CA  . PRO A 1 119 ? -32.852 -33.399 60.255 1.00 21.13 ? 119 PRO A CA  1 
ATOM   919  C C   . PRO A 1 119 ? -33.260 -34.683 59.555 1.00 18.33 ? 119 PRO A C   1 
ATOM   920  O O   . PRO A 1 119 ? -34.065 -34.626 58.638 1.00 23.55 ? 119 PRO A O   1 
ATOM   921  C CB  . PRO A 1 119 ? -33.743 -33.216 61.491 1.00 24.47 ? 119 PRO A CB  1 
ATOM   922  C CG  . PRO A 1 119 ? -34.053 -31.750 61.539 1.00 21.91 ? 119 PRO A CG  1 
ATOM   923  C CD  . PRO A 1 119 ? -34.063 -31.270 60.118 1.00 22.09 ? 119 PRO A CD  1 
ATOM   924  N N   . PRO A 1 120 ? -32.720 -35.831 59.986 1.00 22.42 ? 120 PRO A N   1 
ATOM   925  C CA  . PRO A 1 120 ? -33.217 -37.130 59.515 1.00 15.93 ? 120 PRO A CA  1 
ATOM   926  C C   . PRO A 1 120 ? -34.673 -37.321 59.914 1.00 24.16 ? 120 PRO A C   1 
ATOM   927  O O   . PRO A 1 120 ? -35.084 -36.859 60.981 1.00 18.96 ? 120 PRO A O   1 
ATOM   928  C CB  . PRO A 1 120 ? -32.368 -38.133 60.286 1.00 20.46 ? 120 PRO A CB  1 
ATOM   929  C CG  . PRO A 1 120 ? -31.214 -37.366 60.831 1.00 18.70 ? 120 PRO A CG  1 
ATOM   930  C CD  . PRO A 1 120 ? -31.626 -35.957 60.965 1.00 22.62 ? 120 PRO A CD  1 
ATOM   931  N N   . SER A 1 121 ? -35.450 -37.994 59.071 1.00 27.61 ? 121 SER A N   1 
ATOM   932  C CA  . SER A 1 121 ? -36.824 -38.344 59.436 1.00 26.11 ? 121 SER A CA  1 
ATOM   933  C C   . SER A 1 121 ? -36.800 -39.497 60.422 1.00 25.24 ? 121 SER A C   1 
ATOM   934  O O   . SER A 1 121 ? -35.888 -40.333 60.389 1.00 28.63 ? 121 SER A O   1 
ATOM   935  C CB  . SER A 1 121 ? -37.620 -38.771 58.203 1.00 25.06 ? 121 SER A CB  1 
ATOM   936  O OG  . SER A 1 121 ? -37.132 -39.999 57.690 1.00 28.18 ? 121 SER A OG  1 
ATOM   937  N N   . ASP A 1 122 ? -37.806 -39.553 61.290 1.00 26.75 ? 122 ASP A N   1 
ATOM   938  C CA  . ASP A 1 122 ? -37.978 -40.705 62.173 1.00 30.37 ? 122 ASP A CA  1 
ATOM   939  C C   . ASP A 1 122 ? -38.151 -41.956 61.325 1.00 30.31 ? 122 ASP A C   1 
ATOM   940  O O   . ASP A 1 122 ? -37.757 -43.049 61.722 1.00 30.28 ? 122 ASP A O   1 
ATOM   941  C CB  . ASP A 1 122 ? -39.180 -40.506 63.099 1.00 32.09 ? 122 ASP A CB  1 
ATOM   942  C CG  . ASP A 1 122 ? -38.963 -39.376 64.096 1.00 45.94 ? 122 ASP A CG  1 
ATOM   943  O OD1 . ASP A 1 122 ? -37.798 -39.163 64.500 1.00 47.05 ? 122 ASP A OD1 1 
ATOM   944  O OD2 . ASP A 1 122 ? -39.945 -38.694 64.469 1.00 52.16 ? 122 ASP A OD2 1 
ATOM   945  N N   . GLU A 1 123 ? -38.734 -41.767 60.144 1.00 23.70 ? 123 GLU A N   1 
ATOM   946  C CA  . GLU A 1 123 ? -38.903 -42.834 59.174 1.00 31.75 ? 123 GLU A CA  1 
ATOM   947  C C   . GLU A 1 123 ? -37.555 -43.415 58.777 1.00 28.00 ? 123 GLU A C   1 
ATOM   948  O O   . GLU A 1 123 ? -37.359 -44.630 58.837 1.00 32.37 ? 123 GLU A O   1 
ATOM   949  C CB  . GLU A 1 123 ? -39.645 -42.328 57.926 1.00 34.76 ? 123 GLU A CB  1 
ATOM   950  C CG  . GLU A 1 123 ? -41.123 -41.992 58.152 1.00 37.97 ? 123 GLU A CG  1 
ATOM   951  C CD  . GLU A 1 123 ? -41.360 -40.617 58.792 1.00 41.20 ? 123 GLU A CD  1 
ATOM   952  O OE1 . GLU A 1 123 ? -40.393 -39.973 59.246 1.00 34.59 ? 123 GLU A OE1 1 
ATOM   953  O OE2 . GLU A 1 123 ? -42.531 -40.176 58.843 1.00 50.92 ? 123 GLU A OE2 1 
ATOM   954  N N   . GLN A 1 124 ? -36.628 -42.554 58.372 1.00 24.66 ? 124 GLN A N   1 
ATOM   955  C CA  . GLN A 1 124 ? -35.303 -43.037 57.987 1.00 32.46 ? 124 GLN A CA  1 
ATOM   956  C C   . GLN A 1 124 ? -34.557 -43.672 59.166 1.00 30.25 ? 124 GLN A C   1 
ATOM   957  O O   . GLN A 1 124 ? -33.887 -44.695 59.009 1.00 29.91 ? 124 GLN A O   1 
ATOM   958  C CB  . GLN A 1 124 ? -34.453 -41.940 57.338 1.00 26.73 ? 124 GLN A CB  1 
ATOM   959  C CG  . GLN A 1 124 ? -33.097 -42.474 56.874 1.00 23.85 ? 124 GLN A CG  1 
ATOM   960  C CD  . GLN A 1 124 ? -32.166 -41.389 56.402 1.00 22.43 ? 124 GLN A CD  1 
ATOM   961  O OE1 . GLN A 1 124 ? -32.421 -40.204 56.609 1.00 26.86 ? 124 GLN A OE1 1 
ATOM   962  N NE2 . GLN A 1 124 ? -31.080 -41.784 55.753 1.00 24.26 ? 124 GLN A NE2 1 
ATOM   963  N N   . LEU A 1 125 ? -34.679 -43.059 60.340 1.00 28.41 ? 125 LEU A N   1 
ATOM   964  C CA  . LEU A 1 125 ? -33.998 -43.554 61.534 1.00 31.82 ? 125 LEU A CA  1 
ATOM   965  C C   . LEU A 1 125 ? -34.310 -45.027 61.840 1.00 35.59 ? 125 LEU A C   1 
ATOM   966  O O   . LEU A 1 125 ? -33.444 -45.754 62.338 1.00 33.83 ? 125 LEU A O   1 
ATOM   967  C CB  . LEU A 1 125 ? -34.310 -42.671 62.744 1.00 26.95 ? 125 LEU A CB  1 
ATOM   968  C CG  . LEU A 1 125 ? -33.577 -41.334 62.731 1.00 28.60 ? 125 LEU A CG  1 
ATOM   969  C CD1 . LEU A 1 125 ? -33.931 -40.509 63.935 1.00 29.08 ? 125 LEU A CD1 1 
ATOM   970  C CD2 . LEU A 1 125 ? -32.097 -41.580 62.685 1.00 33.31 ? 125 LEU A CD2 1 
ATOM   971  N N   . LYS A 1 126 ? -35.526 -45.465 61.514 1.00 28.06 ? 126 LYS A N   1 
ATOM   972  C CA  . LYS A 1 126 ? -35.916 -46.865 61.685 1.00 35.02 ? 126 LYS A CA  1 
ATOM   973  C C   . LYS A 1 126 ? -35.079 -47.862 60.876 1.00 34.75 ? 126 LYS A C   1 
ATOM   974  O O   . LYS A 1 126 ? -35.173 -49.061 61.106 1.00 41.52 ? 126 LYS A O   1 
ATOM   975  C CB  . LYS A 1 126 ? -37.395 -47.070 61.339 1.00 32.33 ? 126 LYS A CB  1 
ATOM   976  C CG  . LYS A 1 126 ? -38.375 -46.414 62.290 1.00 35.99 ? 126 LYS A CG  1 
ATOM   977  C CD  . LYS A 1 126 ? -39.794 -46.852 61.980 1.00 43.63 ? 126 LYS A CD  1 
ATOM   978  C CE  . LYS A 1 126 ? -40.789 -46.131 62.867 1.00 50.48 ? 126 LYS A CE  1 
ATOM   979  N NZ  . LYS A 1 126 ? -42.189 -46.300 62.389 1.00 59.34 ? 126 LYS A NZ  1 
ATOM   980  N N   . SER A 1 127 ? -34.279 -47.380 59.927 1.00 35.81 ? 127 SER A N   1 
ATOM   981  C CA  . SER A 1 127 ? -33.481 -48.266 59.080 1.00 31.01 ? 127 SER A CA  1 
ATOM   982  C C   . SER A 1 127 ? -32.027 -48.385 59.539 1.00 36.50 ? 127 SER A C   1 
ATOM   983  O O   . SER A 1 127 ? -31.264 -49.199 59.013 1.00 36.08 ? 127 SER A O   1 
ATOM   984  C CB  . SER A 1 127 ? -33.522 -47.791 57.624 1.00 43.75 ? 127 SER A CB  1 
ATOM   985  O OG  . SER A 1 127 ? -32.891 -46.525 57.478 1.00 45.14 ? 127 SER A OG  1 
ATOM   986  N N   . GLY A 1 128 ? -31.638 -47.570 60.512 1.00 32.44 ? 128 GLY A N   1 
ATOM   987  C CA  . GLY A 1 128 ? -30.283 -47.621 61.031 1.00 39.18 ? 128 GLY A CA  1 
ATOM   988  C C   . GLY A 1 128 ? -29.338 -46.722 60.259 1.00 42.67 ? 128 GLY A C   1 
ATOM   989  O O   . GLY A 1 128 ? -28.118 -46.931 60.243 1.00 35.33 ? 128 GLY A O   1 
ATOM   990  N N   . THR A 1 129 ? -29.916 -45.715 59.610 1.00 39.62 ? 129 THR A N   1 
ATOM   991  C CA  . THR A 1 129 ? -29.146 -44.727 58.868 1.00 37.75 ? 129 THR A CA  1 
ATOM   992  C C   . THR A 1 129 ? -29.749 -43.339 59.071 1.00 33.65 ? 129 THR A C   1 
ATOM   993  O O   . THR A 1 129 ? -30.967 -43.177 59.165 1.00 23.68 ? 129 THR A O   1 
ATOM   994  C CB  . THR A 1 129 ? -29.092 -45.071 57.364 1.00 38.66 ? 129 THR A CB  1 
ATOM   995  O OG1 . THR A 1 129 ? -28.683 -46.436 57.200 1.00 42.03 ? 129 THR A OG1 1 
ATOM   996  C CG2 . THR A 1 129 ? -28.117 -44.160 56.631 1.00 33.88 ? 129 THR A CG2 1 
ATOM   997  N N   . ALA A 1 130 ? -28.884 -42.339 59.154 1.00 32.52 ? 130 ALA A N   1 
ATOM   998  C CA  . ALA A 1 130 ? -29.336 -40.963 59.274 1.00 34.65 ? 130 ALA A CA  1 
ATOM   999  C C   . ALA A 1 130 ? -28.762 -40.087 58.149 1.00 28.10 ? 130 ALA A C   1 
ATOM   1000 O O   . ALA A 1 130 ? -27.551 -39.987 57.985 1.00 25.26 ? 130 ALA A O   1 
ATOM   1001 C CB  . ALA A 1 130 ? -28.972 -40.407 60.646 1.00 26.04 ? 130 ALA A CB  1 
ATOM   1002 N N   . SER A 1 131 ? -29.634 -39.466 57.365 1.00 27.18 ? 131 SER A N   1 
ATOM   1003 C CA  . SER A 1 131 ? -29.185 -38.482 56.391 1.00 19.98 ? 131 SER A CA  1 
ATOM   1004 C C   . SER A 1 131 ? -29.535 -37.119 56.925 1.00 21.33 ? 131 SER A C   1 
ATOM   1005 O O   . SER A 1 131 ? -30.666 -36.892 57.336 1.00 22.21 ? 131 SER A O   1 
ATOM   1006 C CB  . SER A 1 131 ? -29.872 -38.680 55.043 1.00 17.12 ? 131 SER A CB  1 
ATOM   1007 O OG  . SER A 1 131 ? -29.317 -39.772 54.343 1.00 26.66 ? 131 SER A OG  1 
ATOM   1008 N N   . VAL A 1 132 ? -28.571 -36.209 56.921 1.00 18.76 ? 132 VAL A N   1 
ATOM   1009 C CA  . VAL A 1 132 ? -28.848 -34.829 57.280 1.00 17.99 ? 132 VAL A CA  1 
ATOM   1010 C C   . VAL A 1 132 ? -28.628 -33.988 56.035 1.00 21.95 ? 132 VAL A C   1 
ATOM   1011 O O   . VAL A 1 132 ? -27.527 -33.949 55.489 1.00 25.23 ? 132 VAL A O   1 
ATOM   1012 C CB  . VAL A 1 132 ? -27.916 -34.329 58.390 1.00 20.92 ? 132 VAL A CB  1 
ATOM   1013 C CG1 . VAL A 1 132 ? -28.361 -32.960 58.862 1.00 23.69 ? 132 VAL A CG1 1 
ATOM   1014 C CG2 . VAL A 1 132 ? -27.892 -35.306 59.554 1.00 16.14 ? 132 VAL A CG2 1 
ATOM   1015 N N   . VAL A 1 133 ? -29.670 -33.318 55.570 1.00 21.51 ? 133 VAL A N   1 
ATOM   1016 C CA  . VAL A 1 133 ? -29.579 -32.593 54.315 1.00 20.47 ? 133 VAL A CA  1 
ATOM   1017 C C   . VAL A 1 133 ? -29.492 -31.102 54.572 1.00 18.15 ? 133 VAL A C   1 
ATOM   1018 O O   . VAL A 1 133 ? -30.228 -30.557 55.381 1.00 17.54 ? 133 VAL A O   1 
ATOM   1019 C CB  . VAL A 1 133 ? -30.789 -32.917 53.381 1.00 20.86 ? 133 VAL A CB  1 
ATOM   1020 C CG1 . VAL A 1 133 ? -30.784 -32.018 52.141 1.00 11.04 ? 133 VAL A CG1 1 
ATOM   1021 C CG2 . VAL A 1 133 ? -30.796 -34.398 53.001 1.00 14.05 ? 133 VAL A CG2 1 
ATOM   1022 N N   . CYS A 1 134 ? -28.577 -30.456 53.868 1.00 16.73 ? 134 CYS A N   1 
ATOM   1023 C CA  . CYS A 1 134 ? -28.440 -29.016 53.901 1.00 14.51 ? 134 CYS A CA  1 
ATOM   1024 C C   . CYS A 1 134 ? -28.640 -28.485 52.480 1.00 21.34 ? 134 CYS A C   1 
ATOM   1025 O O   . CYS A 1 134 ? -27.943 -28.894 51.548 1.00 20.56 ? 134 CYS A O   1 
ATOM   1026 C CB  . CYS A 1 134 ? -27.048 -28.659 54.410 1.00 22.20 ? 134 CYS A CB  1 
ATOM   1027 S SG  . CYS A 1 134 ? -26.633 -26.913 54.445 1.00 29.77 ? 134 CYS A SG  1 
ATOM   1028 N N   . LEU A 1 135 ? -29.599 -27.581 52.316 1.00 17.03 ? 135 LEU A N   1 
ATOM   1029 C CA  . LEU A 1 135 ? -29.970 -27.089 50.999 1.00 16.12 ? 135 LEU A CA  1 
ATOM   1030 C C   . LEU A 1 135 ? -29.484 -25.658 50.796 1.00 16.27 ? 135 LEU A C   1 
ATOM   1031 O O   . LEU A 1 135 ? -29.651 -24.816 51.669 1.00 22.15 ? 135 LEU A O   1 
ATOM   1032 C CB  . LEU A 1 135 ? -31.490 -27.160 50.835 1.00 12.63 ? 135 LEU A CB  1 
ATOM   1033 C CG  . LEU A 1 135 ? -32.084 -26.459 49.619 1.00 20.91 ? 135 LEU A CG  1 
ATOM   1034 C CD1 . LEU A 1 135 ? -31.787 -27.250 48.364 1.00 20.46 ? 135 LEU A CD1 1 
ATOM   1035 C CD2 . LEU A 1 135 ? -33.593 -26.248 49.785 1.00 20.13 ? 135 LEU A CD2 1 
ATOM   1036 N N   . LEU A 1 136 ? -28.862 -25.392 49.655 1.00 14.07 ? 136 LEU A N   1 
ATOM   1037 C CA  . LEU A 1 136 ? -28.488 -24.026 49.280 1.00 14.81 ? 136 LEU A CA  1 
ATOM   1038 C C   . LEU A 1 136 ? -29.298 -23.686 48.040 1.00 19.75 ? 136 LEU A C   1 
ATOM   1039 O O   . LEU A 1 136 ? -29.122 -24.292 46.980 1.00 16.16 ? 136 LEU A O   1 
ATOM   1040 C CB  . LEU A 1 136 ? -26.992 -23.913 48.981 1.00 16.68 ? 136 LEU A CB  1 
ATOM   1041 C CG  . LEU A 1 136 ? -25.963 -23.896 50.126 1.00 22.89 ? 136 LEU A CG  1 
ATOM   1042 C CD1 . LEU A 1 136 ? -26.046 -25.123 51.060 1.00 8.72  ? 136 LEU A CD1 1 
ATOM   1043 C CD2 . LEU A 1 136 ? -24.557 -23.740 49.544 1.00 11.13 ? 136 LEU A CD2 1 
ATOM   1044 N N   . ASN A 1 137 ? -30.210 -22.736 48.181 1.00 16.01 ? 137 ASN A N   1 
ATOM   1045 C CA  . ASN A 1 137 ? -31.201 -22.517 47.141 1.00 17.61 ? 137 ASN A CA  1 
ATOM   1046 C C   . ASN A 1 137 ? -30.979 -21.248 46.318 1.00 20.83 ? 137 ASN A C   1 
ATOM   1047 O O   . ASN A 1 137 ? -30.759 -20.159 46.874 1.00 14.73 ? 137 ASN A O   1 
ATOM   1048 C CB  . ASN A 1 137 ? -32.607 -22.525 47.746 1.00 16.70 ? 137 ASN A CB  1 
ATOM   1049 C CG  . ASN A 1 137 ? -33.657 -23.044 46.788 1.00 19.36 ? 137 ASN A CG  1 
ATOM   1050 O OD1 . ASN A 1 137 ? -33.420 -23.997 46.055 1.00 17.17 ? 137 ASN A OD1 1 
ATOM   1051 N ND2 . ASN A 1 137 ? -34.831 -22.417 46.794 1.00 18.71 ? 137 ASN A ND2 1 
ATOM   1052 N N   . ASN A 1 138 ? -31.020 -21.413 44.992 1.00 17.94 ? 138 ASN A N   1 
ATOM   1053 C CA  . ASN A 1 138 ? -31.072 -20.283 44.058 1.00 21.97 ? 138 ASN A CA  1 
ATOM   1054 C C   . ASN A 1 138 ? -29.967 -19.248 44.220 1.00 18.07 ? 138 ASN A C   1 
ATOM   1055 O O   . ASN A 1 138 ? -30.233 -18.106 44.572 1.00 21.49 ? 138 ASN A O   1 
ATOM   1056 C CB  . ASN A 1 138 ? -32.432 -19.589 44.142 1.00 14.63 ? 138 ASN A CB  1 
ATOM   1057 C CG  . ASN A 1 138 ? -33.564 -20.493 43.710 1.00 21.72 ? 138 ASN A CG  1 
ATOM   1058 O OD1 . ASN A 1 138 ? -33.373 -21.690 43.464 1.00 17.88 ? 138 ASN A OD1 1 
ATOM   1059 N ND2 . ASN A 1 138 ? -34.758 -19.930 43.623 1.00 27.39 ? 138 ASN A ND2 1 
ATOM   1060 N N   . PHE A 1 139 ? -28.731 -19.647 43.952 1.00 18.46 ? 139 PHE A N   1 
ATOM   1061 C CA  . PHE A 1 139 ? -27.594 -18.750 44.137 1.00 18.84 ? 139 PHE A CA  1 
ATOM   1062 C C   . PHE A 1 139 ? -26.748 -18.656 42.872 1.00 17.80 ? 139 PHE A C   1 
ATOM   1063 O O   . PHE A 1 139 ? -26.907 -19.452 41.943 1.00 13.23 ? 139 PHE A O   1 
ATOM   1064 C CB  . PHE A 1 139 ? -26.731 -19.209 45.323 1.00 15.19 ? 139 PHE A CB  1 
ATOM   1065 C CG  . PHE A 1 139 ? -26.176 -20.601 45.173 1.00 17.48 ? 139 PHE A CG  1 
ATOM   1066 C CD1 . PHE A 1 139 ? -26.886 -21.699 45.646 1.00 18.06 ? 139 PHE A CD1 1 
ATOM   1067 C CD2 . PHE A 1 139 ? -24.945 -20.813 44.553 1.00 14.60 ? 139 PHE A CD2 1 
ATOM   1068 C CE1 . PHE A 1 139 ? -26.379 -22.985 45.507 1.00 20.84 ? 139 PHE A CE1 1 
ATOM   1069 C CE2 . PHE A 1 139 ? -24.430 -22.084 44.410 1.00 16.55 ? 139 PHE A CE2 1 
ATOM   1070 C CZ  . PHE A 1 139 ? -25.144 -23.177 44.883 1.00 20.86 ? 139 PHE A CZ  1 
ATOM   1071 N N   . TYR A 1 140 ? -25.846 -17.676 42.850 1.00 16.95 ? 140 TYR A N   1 
ATOM   1072 C CA  . TYR A 1 140 ? -24.931 -17.473 41.725 1.00 17.97 ? 140 TYR A CA  1 
ATOM   1073 C C   . TYR A 1 140 ? -23.724 -16.706 42.225 1.00 17.53 ? 140 TYR A C   1 
ATOM   1074 O O   . TYR A 1 140 ? -23.880 -15.679 42.884 1.00 22.58 ? 140 TYR A O   1 
ATOM   1075 C CB  . TYR A 1 140 ? -25.604 -16.709 40.570 1.00 13.76 ? 140 TYR A CB  1 
ATOM   1076 C CG  . TYR A 1 140 ? -24.728 -16.687 39.333 1.00 20.82 ? 140 TYR A CG  1 
ATOM   1077 C CD1 . TYR A 1 140 ? -24.739 -17.748 38.429 1.00 21.31 ? 140 TYR A CD1 1 
ATOM   1078 C CD2 . TYR A 1 140 ? -23.859 -15.627 39.088 1.00 21.18 ? 140 TYR A CD2 1 
ATOM   1079 C CE1 . TYR A 1 140 ? -23.931 -17.746 37.319 1.00 20.93 ? 140 TYR A CE1 1 
ATOM   1080 C CE2 . TYR A 1 140 ? -23.041 -15.616 37.977 1.00 24.23 ? 140 TYR A CE2 1 
ATOM   1081 C CZ  . TYR A 1 140 ? -23.082 -16.677 37.099 1.00 26.07 ? 140 TYR A CZ  1 
ATOM   1082 O OH  . TYR A 1 140 ? -22.270 -16.667 35.998 1.00 33.55 ? 140 TYR A OH  1 
ATOM   1083 N N   . PRO A 1 141 ? -22.515 -17.170 41.887 1.00 20.10 ? 141 PRO A N   1 
ATOM   1084 C CA  . PRO A 1 141 ? -22.231 -18.233 40.918 1.00 16.11 ? 141 PRO A CA  1 
ATOM   1085 C C   . PRO A 1 141 ? -22.157 -19.600 41.596 1.00 17.33 ? 141 PRO A C   1 
ATOM   1086 O O   . PRO A 1 141 ? -22.390 -19.709 42.805 1.00 16.34 ? 141 PRO A O   1 
ATOM   1087 C CB  . PRO A 1 141 ? -20.853 -17.836 40.404 1.00 17.09 ? 141 PRO A CB  1 
ATOM   1088 C CG  . PRO A 1 141 ? -20.158 -17.287 41.667 1.00 14.64 ? 141 PRO A CG  1 
ATOM   1089 C CD  . PRO A 1 141 ? -21.280 -16.644 42.506 1.00 19.60 ? 141 PRO A CD  1 
ATOM   1090 N N   . ARG A 1 142 ? -21.816 -20.624 40.818 1.00 19.48 ? 142 ARG A N   1 
ATOM   1091 C CA  . ARG A 1 142 ? -21.839 -22.013 41.268 1.00 17.10 ? 142 ARG A CA  1 
ATOM   1092 C C   . ARG A 1 142 ? -20.969 -22.301 42.503 1.00 19.42 ? 142 ARG A C   1 
ATOM   1093 O O   . ARG A 1 142 ? -21.299 -23.160 43.317 1.00 29.61 ? 142 ARG A O   1 
ATOM   1094 C CB  . ARG A 1 142 ? -21.424 -22.918 40.109 1.00 23.33 ? 142 ARG A CB  1 
ATOM   1095 C CG  . ARG A 1 142 ? -21.687 -24.407 40.289 1.00 24.30 ? 142 ARG A CG  1 
ATOM   1096 C CD  . ARG A 1 142 ? -21.082 -25.175 39.106 1.00 27.43 ? 142 ARG A CD  1 
ATOM   1097 N NE  . ARG A 1 142 ? -21.815 -26.400 38.790 1.00 42.98 ? 142 ARG A NE  1 
ATOM   1098 C CZ  . ARG A 1 142 ? -21.539 -27.597 39.306 1.00 43.18 ? 142 ARG A CZ  1 
ATOM   1099 N NH1 . ARG A 1 142 ? -20.539 -27.740 40.171 1.00 33.32 ? 142 ARG A NH1 1 
ATOM   1100 N NH2 . ARG A 1 142 ? -22.265 -28.656 38.960 1.00 45.83 ? 142 ARG A NH2 1 
ATOM   1101 N N   . GLU A 1 143 ? -19.865 -21.588 42.656 1.00 16.21 ? 143 GLU A N   1 
ATOM   1102 C CA  . GLU A 1 143 ? -18.949 -21.884 43.755 1.00 19.92 ? 143 GLU A CA  1 
ATOM   1103 C C   . GLU A 1 143 ? -19.561 -21.602 45.138 1.00 21.10 ? 143 GLU A C   1 
ATOM   1104 O O   . GLU A 1 143 ? -20.057 -20.504 45.409 1.00 19.95 ? 143 GLU A O   1 
ATOM   1105 C CB  . GLU A 1 143 ? -17.616 -21.154 43.548 1.00 17.94 ? 143 GLU A CB  1 
ATOM   1106 C CG  . GLU A 1 143 ? -16.860 -20.769 44.813 1.00 34.11 ? 143 GLU A CG  1 
ATOM   1107 C CD  . GLU A 1 143 ? -16.194 -21.947 45.520 1.00 31.90 ? 143 GLU A CD  1 
ATOM   1108 O OE1 . GLU A 1 143 ? -15.876 -21.802 46.725 1.00 34.03 ? 143 GLU A OE1 1 
ATOM   1109 O OE2 . GLU A 1 143 ? -15.985 -23.005 44.884 1.00 25.23 ? 143 GLU A OE2 1 
ATOM   1110 N N   . ALA A 1 144 ? -19.539 -22.627 45.986 1.00 16.48 ? 144 ALA A N   1 
ATOM   1111 C CA  . ALA A 1 144 ? -19.996 -22.540 47.374 1.00 20.65 ? 144 ALA A CA  1 
ATOM   1112 C C   . ALA A 1 144 ? -19.268 -23.554 48.262 1.00 17.00 ? 144 ALA A C   1 
ATOM   1113 O O   . ALA A 1 144 ? -18.827 -24.601 47.794 1.00 24.85 ? 144 ALA A O   1 
ATOM   1114 C CB  . ALA A 1 144 ? -21.520 -22.753 47.472 1.00 12.23 ? 144 ALA A CB  1 
ATOM   1115 N N   . LYS A 1 145 ? -19.142 -23.231 49.541 1.00 19.77 ? 145 LYS A N   1 
ATOM   1116 C CA  . LYS A 1 145 ? -18.522 -24.126 50.507 1.00 19.89 ? 145 LYS A CA  1 
ATOM   1117 C C   . LYS A 1 145 ? -19.560 -24.513 51.539 1.00 24.37 ? 145 LYS A C   1 
ATOM   1118 O O   . LYS A 1 145 ? -20.217 -23.636 52.107 1.00 25.13 ? 145 LYS A O   1 
ATOM   1119 C CB  . LYS A 1 145 ? -17.372 -23.424 51.221 1.00 20.71 ? 145 LYS A CB  1 
ATOM   1120 C CG  . LYS A 1 145 ? -16.175 -23.110 50.349 1.00 31.58 ? 145 LYS A CG  1 
ATOM   1121 C CD  . LYS A 1 145 ? -15.525 -24.377 49.836 1.00 32.72 ? 145 LYS A CD  1 
ATOM   1122 C CE  . LYS A 1 145 ? -14.309 -24.044 48.989 1.00 32.76 ? 145 LYS A CE  1 
ATOM   1123 N NZ  . LYS A 1 145 ? -13.504 -25.257 48.709 1.00 45.20 ? 145 LYS A NZ  1 
ATOM   1124 N N   . VAL A 1 146 ? -19.719 -25.819 51.756 1.00 16.56 ? 146 VAL A N   1 
ATOM   1125 C CA  . VAL A 1 146 ? -20.515 -26.330 52.858 1.00 18.67 ? 146 VAL A CA  1 
ATOM   1126 C C   . VAL A 1 146 ? -19.604 -27.074 53.833 1.00 23.34 ? 146 VAL A C   1 
ATOM   1127 O O   . VAL A 1 146 ? -18.991 -28.090 53.479 1.00 21.19 ? 146 VAL A O   1 
ATOM   1128 C CB  . VAL A 1 146 ? -21.638 -27.289 52.390 1.00 21.24 ? 146 VAL A CB  1 
ATOM   1129 C CG1 . VAL A 1 146 ? -22.329 -27.928 53.597 1.00 18.74 ? 146 VAL A CG1 1 
ATOM   1130 C CG2 . VAL A 1 146 ? -22.643 -26.557 51.545 1.00 22.10 ? 146 VAL A CG2 1 
ATOM   1131 N N   . GLN A 1 147 ? -19.515 -26.561 55.054 1.00 15.73 ? 147 GLN A N   1 
ATOM   1132 C CA  . GLN A 1 147 ? -18.749 -27.206 56.113 1.00 21.35 ? 147 GLN A CA  1 
ATOM   1133 C C   . GLN A 1 147 ? -19.678 -27.785 57.186 1.00 19.21 ? 147 GLN A C   1 
ATOM   1134 O O   . GLN A 1 147 ? -20.550 -27.087 57.712 1.00 16.71 ? 147 GLN A O   1 
ATOM   1135 C CB  . GLN A 1 147 ? -17.767 -26.204 56.740 1.00 23.68 ? 147 GLN A CB  1 
ATOM   1136 C CG  . GLN A 1 147 ? -16.916 -26.747 57.873 1.00 27.71 ? 147 GLN A CG  1 
ATOM   1137 C CD  . GLN A 1 147 ? -15.917 -25.720 58.388 1.00 45.88 ? 147 GLN A CD  1 
ATOM   1138 O OE1 . GLN A 1 147 ? -16.088 -25.161 59.480 1.00 37.95 ? 147 GLN A OE1 1 
ATOM   1139 N NE2 . GLN A 1 147 ? -14.875 -25.450 57.592 1.00 33.90 ? 147 GLN A NE2 1 
ATOM   1140 N N   . TRP A 1 148 ? -19.485 -29.063 57.502 1.00 17.82 ? 148 TRP A N   1 
ATOM   1141 C CA  . TRP A 1 148 ? -20.323 -29.746 58.475 1.00 16.01 ? 148 TRP A CA  1 
ATOM   1142 C C   . TRP A 1 148 ? -19.656 -29.839 59.838 1.00 21.53 ? 148 TRP A C   1 
ATOM   1143 O O   . TRP A 1 148 ? -18.488 -30.208 59.946 1.00 19.37 ? 148 TRP A O   1 
ATOM   1144 C CB  . TRP A 1 148 ? -20.736 -31.144 57.997 1.00 15.26 ? 148 TRP A CB  1 
ATOM   1145 C CG  . TRP A 1 148 ? -21.820 -31.164 56.959 1.00 17.51 ? 148 TRP A CG  1 
ATOM   1146 C CD1 . TRP A 1 148 ? -21.654 -31.248 55.606 1.00 22.34 ? 148 TRP A CD1 1 
ATOM   1147 C CD2 . TRP A 1 148 ? -23.239 -31.104 57.186 1.00 19.44 ? 148 TRP A CD2 1 
ATOM   1148 N NE1 . TRP A 1 148 ? -22.877 -31.241 54.980 1.00 22.44 ? 148 TRP A NE1 1 
ATOM   1149 C CE2 . TRP A 1 148 ? -23.866 -31.158 55.925 1.00 22.97 ? 148 TRP A CE2 1 
ATOM   1150 C CE3 . TRP A 1 148 ? -24.037 -31.017 58.333 1.00 19.96 ? 148 TRP A CE3 1 
ATOM   1151 C CZ2 . TRP A 1 148 ? -25.256 -31.123 55.775 1.00 23.85 ? 148 TRP A CZ2 1 
ATOM   1152 C CZ3 . TRP A 1 148 ? -25.416 -30.987 58.188 1.00 20.15 ? 148 TRP A CZ3 1 
ATOM   1153 C CH2 . TRP A 1 148 ? -26.015 -31.037 56.913 1.00 21.95 ? 148 TRP A CH2 1 
ATOM   1154 N N   . LYS A 1 149 ? -20.416 -29.494 60.875 1.00 17.11 ? 149 LYS A N   1 
ATOM   1155 C CA  . LYS A 1 149 ? -19.965 -29.652 62.239 1.00 20.59 ? 149 LYS A CA  1 
ATOM   1156 C C   . LYS A 1 149 ? -20.987 -30.413 63.075 1.00 27.09 ? 149 LYS A C   1 
ATOM   1157 O O   . LYS A 1 149 ? -22.180 -30.108 63.048 1.00 26.97 ? 149 LYS A O   1 
ATOM   1158 C CB  . LYS A 1 149 ? -19.647 -28.293 62.870 1.00 24.10 ? 149 LYS A CB  1 
ATOM   1159 C CG  . LYS A 1 149 ? -18.161 -28.047 63.058 1.00 20.57 ? 149 LYS A CG  1 
ATOM   1160 C CD  . LYS A 1 149 ? -17.811 -26.588 62.889 1.00 26.27 ? 149 LYS A CD  1 
ATOM   1161 C CE  . LYS A 1 149 ? -16.300 -26.389 62.825 1.00 34.37 ? 149 LYS A CE  1 
ATOM   1162 N NZ  . LYS A 1 149 ? -15.933 -24.965 62.518 1.00 52.18 ? 149 LYS A NZ  1 
ATOM   1163 N N   . VAL A 1 150 ? -20.506 -31.415 63.802 1.00 22.06 ? 150 VAL A N   1 
ATOM   1164 C CA  . VAL A 1 150 ? -21.316 -32.157 64.751 1.00 21.11 ? 150 VAL A CA  1 
ATOM   1165 C C   . VAL A 1 150 ? -20.626 -32.042 66.108 1.00 29.26 ? 150 VAL A C   1 
ATOM   1166 O O   . VAL A 1 150 ? -19.513 -32.564 66.292 1.00 25.26 ? 150 VAL A O   1 
ATOM   1167 C CB  . VAL A 1 150 ? -21.394 -33.642 64.375 1.00 19.03 ? 150 VAL A CB  1 
ATOM   1168 C CG1 . VAL A 1 150 ? -22.190 -34.409 65.424 1.00 20.29 ? 150 VAL A CG1 1 
ATOM   1169 C CG2 . VAL A 1 150 ? -21.982 -33.815 62.996 1.00 17.62 ? 150 VAL A CG2 1 
ATOM   1170 N N   . ASP A 1 151 ? -21.267 -31.347 67.045 1.00 26.72 ? 151 ASP A N   1 
ATOM   1171 C CA  . ASP A 1 151 ? -20.662 -31.080 68.349 1.00 21.21 ? 151 ASP A CA  1 
ATOM   1172 C C   . ASP A 1 151 ? -19.287 -30.439 68.160 1.00 23.47 ? 151 ASP A C   1 
ATOM   1173 O O   . ASP A 1 151 ? -18.290 -30.899 68.706 1.00 27.85 ? 151 ASP A O   1 
ATOM   1174 C CB  . ASP A 1 151 ? -20.539 -32.373 69.171 1.00 27.49 ? 151 ASP A CB  1 
ATOM   1175 C CG  . ASP A 1 151 ? -21.891 -32.948 69.600 1.00 28.78 ? 151 ASP A CG  1 
ATOM   1176 O OD1 . ASP A 1 151 ? -22.833 -32.177 69.903 1.00 24.26 ? 151 ASP A OD1 1 
ATOM   1177 O OD2 . ASP A 1 151 ? -21.999 -34.193 69.649 1.00 31.37 ? 151 ASP A OD2 1 
ATOM   1178 N N   . ASN A 1 152 ? -19.235 -29.391 67.350 1.00 30.71 ? 152 ASN A N   1 
ATOM   1179 C CA  . ASN A 1 152 ? -17.977 -28.708 67.019 1.00 30.26 ? 152 ASN A CA  1 
ATOM   1180 C C   . ASN A 1 152 ? -16.876 -29.549 66.387 1.00 29.10 ? 152 ASN A C   1 
ATOM   1181 O O   . ASN A 1 152 ? -15.779 -29.046 66.145 1.00 34.05 ? 152 ASN A O   1 
ATOM   1182 C CB  . ASN A 1 152 ? -17.429 -27.920 68.209 1.00 27.30 ? 152 ASN A CB  1 
ATOM   1183 C CG  . ASN A 1 152 ? -18.178 -26.626 68.423 1.00 50.04 ? 152 ASN A CG  1 
ATOM   1184 O OD1 . ASN A 1 152 ? -18.771 -26.076 67.485 1.00 47.78 ? 152 ASN A OD1 1 
ATOM   1185 N ND2 . ASN A 1 152 ? -18.180 -26.138 69.658 1.00 58.52 ? 152 ASN A ND2 1 
ATOM   1186 N N   . ALA A 1 153 ? -17.153 -30.821 66.119 1.00 25.24 ? 153 ALA A N   1 
ATOM   1187 C CA  . ALA A 1 153 ? -16.210 -31.622 65.357 1.00 20.43 ? 153 ALA A CA  1 
ATOM   1188 C C   . ALA A 1 153 ? -16.450 -31.439 63.849 1.00 23.66 ? 153 ALA A C   1 
ATOM   1189 O O   . ALA A 1 153 ? -17.544 -31.692 63.324 1.00 18.17 ? 153 ALA A O   1 
ATOM   1190 C CB  . ALA A 1 153 ? -16.298 -33.072 65.750 1.00 23.27 ? 153 ALA A CB  1 
ATOM   1191 N N   . LEU A 1 154 ? -15.419 -30.958 63.170 1.00 20.00 ? 154 LEU A N   1 
ATOM   1192 C CA  . LEU A 1 154 ? -15.443 -30.833 61.731 1.00 19.40 ? 154 LEU A CA  1 
ATOM   1193 C C   . LEU A 1 154 ? -15.679 -32.205 61.096 1.00 21.40 ? 154 LEU A C   1 
ATOM   1194 O O   . LEU A 1 154 ? -14.983 -33.163 61.406 1.00 24.75 ? 154 LEU A O   1 
ATOM   1195 C CB  . LEU A 1 154 ? -14.128 -30.235 61.250 1.00 17.61 ? 154 LEU A CB  1 
ATOM   1196 C CG  . LEU A 1 154 ? -13.910 -30.193 59.737 1.00 25.93 ? 154 LEU A CG  1 
ATOM   1197 C CD1 . LEU A 1 154 ? -14.916 -29.280 59.038 1.00 23.52 ? 154 LEU A CD1 1 
ATOM   1198 C CD2 . LEU A 1 154 ? -12.477 -29.774 59.439 1.00 20.07 ? 154 LEU A CD2 1 
ATOM   1199 N N   . GLN A 1 155 ? -16.690 -32.306 60.238 1.00 23.62 ? 155 GLN A N   1 
ATOM   1200 C CA  . GLN A 1 155 ? -16.965 -33.560 59.547 1.00 22.88 ? 155 GLN A CA  1 
ATOM   1201 C C   . GLN A 1 155 ? -16.236 -33.554 58.221 1.00 24.12 ? 155 GLN A C   1 
ATOM   1202 O O   . GLN A 1 155 ? -16.249 -32.551 57.505 1.00 22.45 ? 155 GLN A O   1 
ATOM   1203 C CB  . GLN A 1 155 ? -18.465 -33.757 59.308 1.00 18.26 ? 155 GLN A CB  1 
ATOM   1204 C CG  . GLN A 1 155 ? -19.297 -33.829 60.569 1.00 19.30 ? 155 GLN A CG  1 
ATOM   1205 C CD  . GLN A 1 155 ? -18.872 -34.956 61.478 1.00 22.88 ? 155 GLN A CD  1 
ATOM   1206 O OE1 . GLN A 1 155 ? -19.127 -36.128 61.195 1.00 25.41 ? 155 GLN A OE1 1 
ATOM   1207 N NE2 . GLN A 1 155 ? -18.224 -34.610 62.585 1.00 21.31 ? 155 GLN A NE2 1 
ATOM   1208 N N   . SER A 1 156 ? -15.607 -34.677 57.893 1.00 17.98 ? 156 SER A N   1 
ATOM   1209 C CA  . SER A 1 156 ? -14.922 -34.790 56.624 1.00 19.71 ? 156 SER A CA  1 
ATOM   1210 C C   . SER A 1 156 ? -15.060 -36.178 56.020 1.00 24.23 ? 156 SER A C   1 
ATOM   1211 O O   . SER A 1 156 ? -14.971 -37.202 56.725 1.00 22.69 ? 156 SER A O   1 
ATOM   1212 C CB  . SER A 1 156 ? -13.446 -34.442 56.778 1.00 20.31 ? 156 SER A CB  1 
ATOM   1213 O OG  . SER A 1 156 ? -12.797 -34.586 55.525 1.00 27.72 ? 156 SER A OG  1 
ATOM   1214 N N   . GLY A 1 157 ? -15.274 -36.201 54.708 1.00 17.42 ? 157 GLY A N   1 
ATOM   1215 C CA  . GLY A 1 157 ? -15.377 -37.444 53.973 1.00 23.62 ? 157 GLY A CA  1 
ATOM   1216 C C   . GLY A 1 157 ? -16.731 -38.126 54.045 1.00 22.77 ? 157 GLY A C   1 
ATOM   1217 O O   . GLY A 1 157 ? -16.966 -39.088 53.316 1.00 26.85 ? 157 GLY A O   1 
ATOM   1218 N N   . ASN A 1 158 ? -17.616 -37.643 54.917 1.00 19.92 ? 158 ASN A N   1 
ATOM   1219 C CA  . ASN A 1 158 ? -18.920 -38.284 55.111 1.00 22.79 ? 158 ASN A CA  1 
ATOM   1220 C C   . ASN A 1 158 ? -20.115 -37.468 54.605 1.00 27.75 ? 158 ASN A C   1 
ATOM   1221 O O   . ASN A 1 158 ? -21.239 -37.632 55.074 1.00 31.47 ? 158 ASN A O   1 
ATOM   1222 C CB  . ASN A 1 158 ? -19.117 -38.743 56.570 1.00 12.73 ? 158 ASN A CB  1 
ATOM   1223 C CG  . ASN A 1 158 ? -19.007 -37.602 57.566 1.00 21.73 ? 158 ASN A CG  1 
ATOM   1224 O OD1 . ASN A 1 158 ? -18.653 -36.473 57.206 1.00 22.61 ? 158 ASN A OD1 1 
ATOM   1225 N ND2 . ASN A 1 158 ? -19.290 -37.891 58.828 1.00 22.00 ? 158 ASN A ND2 1 
ATOM   1226 N N   . SER A 1 159 ? -19.871 -36.594 53.639 1.00 26.29 ? 159 SER A N   1 
ATOM   1227 C CA  . SER A 1 159 ? -20.956 -35.860 53.017 1.00 23.57 ? 159 SER A CA  1 
ATOM   1228 C C   . SER A 1 159 ? -20.823 -35.906 51.490 1.00 24.79 ? 159 SER A C   1 
ATOM   1229 O O   . SER A 1 159 ? -19.719 -36.027 50.958 1.00 27.31 ? 159 SER A O   1 
ATOM   1230 C CB  . SER A 1 159 ? -20.975 -34.416 53.519 1.00 16.76 ? 159 SER A CB  1 
ATOM   1231 O OG  . SER A 1 159 ? -19.871 -33.697 53.001 1.00 25.65 ? 159 SER A OG  1 
ATOM   1232 N N   . GLN A 1 160 ? -21.944 -35.827 50.788 1.00 19.44 ? 160 GLN A N   1 
ATOM   1233 C CA  . GLN A 1 160 ? -21.910 -35.726 49.340 1.00 22.67 ? 160 GLN A CA  1 
ATOM   1234 C C   . GLN A 1 160 ? -22.707 -34.518 48.868 1.00 24.00 ? 160 GLN A C   1 
ATOM   1235 O O   . GLN A 1 160 ? -23.751 -34.166 49.435 1.00 16.31 ? 160 GLN A O   1 
ATOM   1236 C CB  . GLN A 1 160 ? -22.436 -36.997 48.683 1.00 23.96 ? 160 GLN A CB  1 
ATOM   1237 C CG  . GLN A 1 160 ? -21.506 -38.206 48.835 1.00 25.01 ? 160 GLN A CG  1 
ATOM   1238 C CD  . GLN A 1 160 ? -22.092 -39.452 48.194 1.00 29.30 ? 160 GLN A CD  1 
ATOM   1239 O OE1 . GLN A 1 160 ? -23.271 -39.763 48.387 1.00 32.25 ? 160 GLN A OE1 1 
ATOM   1240 N NE2 . GLN A 1 160 ? -21.285 -40.155 47.404 1.00 24.75 ? 160 GLN A NE2 1 
ATOM   1241 N N   . GLU A 1 161 ? -22.192 -33.872 47.830 1.00 24.82 ? 161 GLU A N   1 
ATOM   1242 C CA  . GLU A 1 161 ? -22.818 -32.699 47.269 1.00 18.54 ? 161 GLU A CA  1 
ATOM   1243 C C   . GLU A 1 161 ? -23.406 -32.989 45.908 1.00 27.05 ? 161 GLU A C   1 
ATOM   1244 O O   . GLU A 1 161 ? -22.922 -33.854 45.185 1.00 28.31 ? 161 GLU A O   1 
ATOM   1245 C CB  . GLU A 1 161 ? -21.811 -31.578 47.145 1.00 19.62 ? 161 GLU A CB  1 
ATOM   1246 C CG  . GLU A 1 161 ? -21.543 -30.855 48.442 1.00 35.75 ? 161 GLU A CG  1 
ATOM   1247 C CD  . GLU A 1 161 ? -20.680 -29.633 48.224 1.00 42.33 ? 161 GLU A CD  1 
ATOM   1248 O OE1 . GLU A 1 161 ? -20.462 -29.262 47.041 1.00 33.77 ? 161 GLU A OE1 1 
ATOM   1249 O OE2 . GLU A 1 161 ? -20.220 -29.050 49.231 1.00 37.20 ? 161 GLU A OE2 1 
ATOM   1250 N N   . SER A 1 162 ? -24.460 -32.256 45.571 1.00 26.19 ? 162 SER A N   1 
ATOM   1251 C CA  . SER A 1 162 ? -25.064 -32.335 44.258 1.00 15.13 ? 162 SER A CA  1 
ATOM   1252 C C   . SER A 1 162 ? -25.570 -30.948 43.878 1.00 17.70 ? 162 SER A C   1 
ATOM   1253 O O   . SER A 1 162 ? -26.164 -30.240 44.700 1.00 22.68 ? 162 SER A O   1 
ATOM   1254 C CB  . SER A 1 162 ? -26.191 -33.355 44.256 1.00 15.67 ? 162 SER A CB  1 
ATOM   1255 O OG  . SER A 1 162 ? -26.773 -33.444 42.972 1.00 25.68 ? 162 SER A OG  1 
ATOM   1256 N N   . VAL A 1 163 ? -25.291 -30.549 42.643 1.00 21.08 ? 163 VAL A N   1 
ATOM   1257 C CA  . VAL A 1 163 ? -25.634 -29.226 42.146 1.00 16.63 ? 163 VAL A CA  1 
ATOM   1258 C C   . VAL A 1 163 ? -26.533 -29.372 40.934 1.00 18.71 ? 163 VAL A C   1 
ATOM   1259 O O   . VAL A 1 163 ? -26.214 -30.115 40.014 1.00 17.91 ? 163 VAL A O   1 
ATOM   1260 C CB  . VAL A 1 163 ? -24.369 -28.426 41.740 1.00 21.69 ? 163 VAL A CB  1 
ATOM   1261 C CG1 . VAL A 1 163 ? -24.749 -27.033 41.231 1.00 22.96 ? 163 VAL A CG1 1 
ATOM   1262 C CG2 . VAL A 1 163 ? -23.411 -28.315 42.914 1.00 26.07 ? 163 VAL A CG2 1 
ATOM   1263 N N   . THR A 1 164 ? -27.667 -28.682 40.936 1.00 18.10 ? 164 THR A N   1 
ATOM   1264 C CA  . THR A 1 164 ? -28.522 -28.676 39.764 1.00 20.27 ? 164 THR A CA  1 
ATOM   1265 C C   . THR A 1 164 ? -27.794 -28.009 38.615 1.00 21.89 ? 164 THR A C   1 
ATOM   1266 O O   . THR A 1 164 ? -26.824 -27.276 38.818 1.00 23.35 ? 164 THR A O   1 
ATOM   1267 C CB  . THR A 1 164 ? -29.813 -27.881 39.991 1.00 24.67 ? 164 THR A CB  1 
ATOM   1268 O OG1 . THR A 1 164 ? -29.504 -26.634 40.625 1.00 20.90 ? 164 THR A OG1 1 
ATOM   1269 C CG2 . THR A 1 164 ? -30.782 -28.679 40.863 1.00 21.51 ? 164 THR A CG2 1 
ATOM   1270 N N   . GLU A 1 165 ? -28.251 -28.269 37.398 1.00 22.43 ? 165 GLU A N   1 
ATOM   1271 C CA  . GLU A 1 165 ? -27.790 -27.486 36.260 1.00 21.48 ? 165 GLU A CA  1 
ATOM   1272 C C   . GLU A 1 165 ? -28.399 -26.108 36.394 1.00 20.00 ? 165 GLU A C   1 
ATOM   1273 O O   . GLU A 1 165 ? -29.254 -25.879 37.241 1.00 21.91 ? 165 GLU A O   1 
ATOM   1274 C CB  . GLU A 1 165 ? -28.190 -28.134 34.931 1.00 19.51 ? 165 GLU A CB  1 
ATOM   1275 C CG  . GLU A 1 165 ? -27.419 -29.421 34.604 1.00 26.89 ? 165 GLU A CG  1 
ATOM   1276 C CD  . GLU A 1 165 ? -25.905 -29.206 34.464 1.00 31.99 ? 165 GLU A CD  1 
ATOM   1277 O OE1 . GLU A 1 165 ? -25.455 -28.043 34.339 1.00 37.55 ? 165 GLU A OE1 1 
ATOM   1278 O OE2 . GLU A 1 165 ? -25.158 -30.211 34.475 1.00 28.49 ? 165 GLU A OE2 1 
ATOM   1279 N N   . GLN A 1 166 ? -27.940 -25.179 35.575 1.00 23.16 ? 166 GLN A N   1 
ATOM   1280 C CA  . GLN A 1 166 ? -28.425 -23.808 35.646 1.00 22.66 ? 166 GLN A CA  1 
ATOM   1281 C C   . GLN A 1 166 ? -29.915 -23.736 35.329 1.00 19.16 ? 166 GLN A C   1 
ATOM   1282 O O   . GLN A 1 166 ? -30.416 -24.404 34.424 1.00 23.29 ? 166 GLN A O   1 
ATOM   1283 C CB  . GLN A 1 166 ? -27.633 -22.912 34.693 1.00 28.49 ? 166 GLN A CB  1 
ATOM   1284 C CG  . GLN A 1 166 ? -27.273 -21.555 35.259 1.00 27.80 ? 166 GLN A CG  1 
ATOM   1285 C CD  . GLN A 1 166 ? -26.257 -20.834 34.390 1.00 31.92 ? 166 GLN A CD  1 
ATOM   1286 O OE1 . GLN A 1 166 ? -25.665 -21.429 33.485 1.00 32.42 ? 166 GLN A OE1 1 
ATOM   1287 N NE2 . GLN A 1 166 ? -26.055 -19.548 34.655 1.00 23.68 ? 166 GLN A NE2 1 
ATOM   1288 N N   . ASP A 1 167 ? -30.618 -22.914 36.088 1.00 24.03 ? 167 ASP A N   1 
ATOM   1289 C CA  . ASP A 1 167 ? -32.052 -22.784 35.948 1.00 19.98 ? 167 ASP A CA  1 
ATOM   1290 C C   . ASP A 1 167 ? -32.363 -21.950 34.712 1.00 22.74 ? 167 ASP A C   1 
ATOM   1291 O O   . ASP A 1 167 ? -31.727 -20.930 34.472 1.00 24.25 ? 167 ASP A O   1 
ATOM   1292 C CB  . ASP A 1 167 ? -32.638 -22.142 37.203 1.00 21.44 ? 167 ASP A CB  1 
ATOM   1293 C CG  . ASP A 1 167 ? -34.139 -22.185 37.222 1.00 29.13 ? 167 ASP A CG  1 
ATOM   1294 O OD1 . ASP A 1 167 ? -34.767 -21.205 36.767 1.00 27.99 ? 167 ASP A OD1 1 
ATOM   1295 O OD2 . ASP A 1 167 ? -34.687 -23.204 37.698 1.00 43.08 ? 167 ASP A OD2 1 
ATOM   1296 N N   . SER A 1 168 ? -33.341 -22.381 33.926 1.00 26.09 ? 168 SER A N   1 
ATOM   1297 C CA  . SER A 1 168 ? -33.615 -21.715 32.658 1.00 24.93 ? 168 SER A CA  1 
ATOM   1298 C C   . SER A 1 168 ? -34.356 -20.403 32.824 1.00 26.07 ? 168 SER A C   1 
ATOM   1299 O O   . SER A 1 168 ? -34.447 -19.627 31.876 1.00 26.06 ? 168 SER A O   1 
ATOM   1300 C CB  . SER A 1 168 ? -34.396 -22.620 31.716 1.00 24.94 ? 168 SER A CB  1 
ATOM   1301 O OG  . SER A 1 168 ? -35.701 -22.807 32.189 1.00 30.99 ? 168 SER A OG  1 
ATOM   1302 N N   . LYS A 1 169 ? -34.885 -20.145 34.017 1.00 24.27 ? 169 LYS A N   1 
ATOM   1303 C CA  . LYS A 1 169 ? -35.617 -18.896 34.234 1.00 18.13 ? 169 LYS A CA  1 
ATOM   1304 C C   . LYS A 1 169 ? -34.770 -17.822 34.891 1.00 22.01 ? 169 LYS A C   1 
ATOM   1305 O O   . LYS A 1 169 ? -34.656 -16.737 34.358 1.00 28.11 ? 169 LYS A O   1 
ATOM   1306 C CB  . LYS A 1 169 ? -36.891 -19.135 35.034 1.00 24.44 ? 169 LYS A CB  1 
ATOM   1307 N N   . ASP A 1 170 ? -34.170 -18.117 36.044 1.00 29.03 ? 170 ASP A N   1 
ATOM   1308 C CA  . ASP A 1 170 ? -33.381 -17.108 36.761 1.00 16.92 ? 170 ASP A CA  1 
ATOM   1309 C C   . ASP A 1 170 ? -31.859 -17.311 36.688 1.00 19.56 ? 170 ASP A C   1 
ATOM   1310 O O   . ASP A 1 170 ? -31.104 -16.548 37.290 1.00 16.60 ? 170 ASP A O   1 
ATOM   1311 C CB  . ASP A 1 170 ? -33.847 -16.962 38.226 1.00 14.97 ? 170 ASP A CB  1 
ATOM   1312 C CG  . ASP A 1 170 ? -33.746 -18.269 39.034 1.00 29.45 ? 170 ASP A CG  1 
ATOM   1313 O OD1 . ASP A 1 170 ? -32.749 -19.011 38.885 1.00 25.94 ? 170 ASP A OD1 1 
ATOM   1314 O OD2 . ASP A 1 170 ? -34.670 -18.553 39.836 1.00 32.13 ? 170 ASP A OD2 1 
ATOM   1315 N N   . SER A 1 171 ? -31.420 -18.343 35.972 1.00 14.98 ? 171 SER A N   1 
ATOM   1316 C CA  . SER A 1 171 ? -29.985 -18.624 35.809 1.00 20.07 ? 171 SER A CA  1 
ATOM   1317 C C   . SER A 1 171 ? -29.203 -18.941 37.093 1.00 23.65 ? 171 SER A C   1 
ATOM   1318 O O   . SER A 1 171 ? -27.979 -18.772 37.126 1.00 21.38 ? 171 SER A O   1 
ATOM   1319 C CB  . SER A 1 171 ? -29.288 -17.467 35.087 1.00 11.06 ? 171 SER A CB  1 
ATOM   1320 O OG  . SER A 1 171 ? -29.752 -17.353 33.763 1.00 23.01 ? 171 SER A OG  1 
ATOM   1321 N N   . THR A 1 172 ? -29.886 -19.389 38.145 1.00 15.85 ? 172 THR A N   1 
ATOM   1322 C CA  . THR A 1 172 ? -29.178 -19.706 39.388 1.00 17.28 ? 172 THR A CA  1 
ATOM   1323 C C   . THR A 1 172 ? -28.930 -21.207 39.527 1.00 21.08 ? 172 THR A C   1 
ATOM   1324 O O   . THR A 1 172 ? -29.381 -22.016 38.714 1.00 19.95 ? 172 THR A O   1 
ATOM   1325 C CB  . THR A 1 172 ? -29.934 -19.214 40.665 1.00 18.27 ? 172 THR A CB  1 
ATOM   1326 O OG1 . THR A 1 172 ? -31.088 -20.029 40.891 1.00 19.04 ? 172 THR A OG1 1 
ATOM   1327 C CG2 . THR A 1 172 ? -30.357 -17.763 40.548 1.00 17.14 ? 172 THR A CG2 1 
ATOM   1328 N N   . TYR A 1 173 ? -28.223 -21.566 40.585 1.00 14.52 ? 173 TYR A N   1 
ATOM   1329 C CA  . TYR A 1 173 ? -27.967 -22.944 40.897 1.00 13.01 ? 173 TYR A CA  1 
ATOM   1330 C C   . TYR A 1 173 ? -28.549 -23.228 42.253 1.00 17.88 ? 173 TYR A C   1 
ATOM   1331 O O   . TYR A 1 173 ? -28.738 -22.320 43.066 1.00 20.77 ? 173 TYR A O   1 
ATOM   1332 C CB  . TYR A 1 173 ? -26.461 -23.194 40.949 1.00 14.50 ? 173 TYR A CB  1 
ATOM   1333 C CG  . TYR A 1 173 ? -25.736 -22.971 39.647 1.00 18.43 ? 173 TYR A CG  1 
ATOM   1334 C CD1 . TYR A 1 173 ? -25.670 -23.977 38.682 1.00 22.71 ? 173 TYR A CD1 1 
ATOM   1335 C CD2 . TYR A 1 173 ? -25.112 -21.761 39.383 1.00 19.47 ? 173 TYR A CD2 1 
ATOM   1336 C CE1 . TYR A 1 173 ? -25.001 -23.777 37.486 1.00 27.45 ? 173 TYR A CE1 1 
ATOM   1337 C CE2 . TYR A 1 173 ? -24.442 -21.549 38.193 1.00 27.39 ? 173 TYR A CE2 1 
ATOM   1338 C CZ  . TYR A 1 173 ? -24.387 -22.559 37.249 1.00 29.43 ? 173 TYR A CZ  1 
ATOM   1339 O OH  . TYR A 1 173 ? -23.732 -22.343 36.068 1.00 35.64 ? 173 TYR A OH  1 
ATOM   1340 N N   . SER A 1 174 ? -28.814 -24.501 42.505 1.00 15.83 ? 174 SER A N   1 
ATOM   1341 C CA  . SER A 1 174 ? -29.141 -24.939 43.842 1.00 14.29 ? 174 SER A CA  1 
ATOM   1342 C C   . SER A 1 174 ? -28.253 -26.116 44.182 1.00 19.56 ? 174 SER A C   1 
ATOM   1343 O O   . SER A 1 174 ? -27.814 -26.841 43.294 1.00 19.45 ? 174 SER A O   1 
ATOM   1344 C CB  . SER A 1 174 ? -30.626 -25.286 43.965 1.00 14.51 ? 174 SER A CB  1 
ATOM   1345 O OG  . SER A 1 174 ? -31.390 -24.097 44.086 1.00 14.03 ? 174 SER A OG  1 
ATOM   1346 N N   . LEU A 1 175 ? -27.980 -26.293 45.471 1.00 22.06 ? 175 LEU A N   1 
ATOM   1347 C CA  . LEU A 1 175 ? -27.001 -27.270 45.926 1.00 19.73 ? 175 LEU A CA  1 
ATOM   1348 C C   . LEU A 1 175 ? -27.530 -28.009 47.128 1.00 23.31 ? 175 LEU A C   1 
ATOM   1349 O O   . LEU A 1 175 ? -28.084 -27.406 48.045 1.00 20.03 ? 175 LEU A O   1 
ATOM   1350 C CB  . LEU A 1 175 ? -25.693 -26.575 46.318 1.00 19.16 ? 175 LEU A CB  1 
ATOM   1351 C CG  . LEU A 1 175 ? -24.507 -27.460 46.716 1.00 18.24 ? 175 LEU A CG  1 
ATOM   1352 C CD1 . LEU A 1 175 ? -23.207 -26.839 46.250 1.00 16.43 ? 175 LEU A CD1 1 
ATOM   1353 C CD2 . LEU A 1 175 ? -24.469 -27.686 48.211 1.00 15.95 ? 175 LEU A CD2 1 
ATOM   1354 N N   . SER A 1 176 ? -27.328 -29.315 47.133 1.00 20.33 ? 176 SER A N   1 
ATOM   1355 C CA  . SER A 1 176 ? -27.687 -30.115 48.279 1.00 19.40 ? 176 SER A CA  1 
ATOM   1356 C C   . SER A 1 176 ? -26.410 -30.726 48.817 1.00 24.35 ? 176 SER A C   1 
ATOM   1357 O O   . SER A 1 176 ? -25.635 -31.316 48.067 1.00 25.76 ? 176 SER A O   1 
ATOM   1358 C CB  . SER A 1 176 ? -28.665 -31.234 47.879 1.00 18.81 ? 176 SER A CB  1 
ATOM   1359 O OG  . SER A 1 176 ? -28.005 -32.292 47.180 1.00 17.56 ? 176 SER A OG  1 
ATOM   1360 N N   . SER A 1 177 ? -26.191 -30.573 50.112 1.00 18.59 ? 177 SER A N   1 
ATOM   1361 C CA  . SER A 1 177 ? -25.141 -31.301 50.805 1.00 19.06 ? 177 SER A CA  1 
ATOM   1362 C C   . SER A 1 177 ? -25.805 -32.282 51.780 1.00 22.74 ? 177 SER A C   1 
ATOM   1363 O O   . SER A 1 177 ? -26.606 -31.879 52.618 1.00 23.29 ? 177 SER A O   1 
ATOM   1364 C CB  . SER A 1 177 ? -24.218 -30.329 51.540 1.00 17.36 ? 177 SER A CB  1 
ATOM   1365 O OG  . SER A 1 177 ? -23.165 -31.001 52.198 1.00 19.53 ? 177 SER A OG  1 
ATOM   1366 N N   . THR A 1 178 ? -25.491 -33.565 51.640 1.00 19.13 ? 178 THR A N   1 
ATOM   1367 C CA  . THR A 1 178 ? -26.090 -34.614 52.457 1.00 18.26 ? 178 THR A CA  1 
ATOM   1368 C C   . THR A 1 178 ? -25.035 -35.293 53.356 1.00 23.05 ? 178 THR A C   1 
ATOM   1369 O O   . THR A 1 178 ? -24.094 -35.918 52.877 1.00 17.94 ? 178 THR A O   1 
ATOM   1370 C CB  . THR A 1 178 ? -26.822 -35.656 51.560 1.00 22.60 ? 178 THR A CB  1 
ATOM   1371 O OG1 . THR A 1 178 ? -27.755 -34.982 50.701 1.00 27.51 ? 178 THR A OG1 1 
ATOM   1372 C CG2 . THR A 1 178 ? -27.562 -36.701 52.390 1.00 16.60 ? 178 THR A CG2 1 
ATOM   1373 N N   . LEU A 1 179 ? -25.189 -35.130 54.666 1.00 20.99 ? 179 LEU A N   1 
ATOM   1374 C CA  . LEU A 1 179 ? -24.296 -35.749 55.643 1.00 17.37 ? 179 LEU A CA  1 
ATOM   1375 C C   . LEU A 1 179 ? -24.891 -37.077 56.076 1.00 18.90 ? 179 LEU A C   1 
ATOM   1376 O O   . LEU A 1 179 ? -26.039 -37.123 56.496 1.00 21.53 ? 179 LEU A O   1 
ATOM   1377 C CB  . LEU A 1 179 ? -24.133 -34.837 56.857 1.00 17.43 ? 179 LEU A CB  1 
ATOM   1378 C CG  . LEU A 1 179 ? -23.299 -35.350 58.034 1.00 16.77 ? 179 LEU A CG  1 
ATOM   1379 C CD1 . LEU A 1 179 ? -21.800 -35.278 57.757 1.00 13.81 ? 179 LEU A CD1 1 
ATOM   1380 C CD2 . LEU A 1 179 ? -23.658 -34.557 59.281 1.00 13.21 ? 179 LEU A CD2 1 
ATOM   1381 N N   . THR A 1 180 ? -24.121 -38.154 55.959 1.00 18.00 ? 180 THR A N   1 
ATOM   1382 C CA  . THR A 1 180 ? -24.610 -39.496 56.284 1.00 21.39 ? 180 THR A CA  1 
ATOM   1383 C C   . THR A 1 180 ? -23.883 -40.176 57.457 1.00 23.88 ? 180 THR A C   1 
ATOM   1384 O O   . THR A 1 180 ? -22.662 -40.291 57.460 1.00 34.25 ? 180 THR A O   1 
ATOM   1385 C CB  . THR A 1 180 ? -24.593 -40.409 55.047 1.00 21.39 ? 180 THR A CB  1 
ATOM   1386 O OG1 . THR A 1 180 ? -25.513 -39.886 54.095 1.00 33.66 ? 180 THR A OG1 1 
ATOM   1387 C CG2 . THR A 1 180 ? -25.036 -41.812 55.407 1.00 29.06 ? 180 THR A CG2 1 
ATOM   1388 N N   . LEU A 1 181 ? -24.659 -40.603 58.451 1.00 29.73 ? 181 LEU A N   1 
ATOM   1389 C CA  . LEU A 1 181 ? -24.153 -41.235 59.669 1.00 32.45 ? 181 LEU A CA  1 
ATOM   1390 C C   . LEU A 1 181 ? -24.945 -42.494 59.957 1.00 36.47 ? 181 LEU A C   1 
ATOM   1391 O O   . LEU A 1 181 ? -26.097 -42.625 59.536 1.00 31.66 ? 181 LEU A O   1 
ATOM   1392 C CB  . LEU A 1 181 ? -24.355 -40.330 60.881 1.00 31.68 ? 181 LEU A CB  1 
ATOM   1393 C CG  . LEU A 1 181 ? -24.031 -38.846 60.855 1.00 35.04 ? 181 LEU A CG  1 
ATOM   1394 C CD1 . LEU A 1 181 ? -24.849 -38.185 61.928 1.00 38.30 ? 181 LEU A CD1 1 
ATOM   1395 C CD2 . LEU A 1 181 ? -22.559 -38.636 61.128 1.00 44.38 ? 181 LEU A CD2 1 
ATOM   1396 N N   . SER A 1 182 ? -24.341 -43.400 60.716 1.00 39.24 ? 182 SER A N   1 
ATOM   1397 C CA  . SER A 1 182 ? -25.068 -44.540 61.249 1.00 40.04 ? 182 SER A CA  1 
ATOM   1398 C C   . SER A 1 182 ? -26.104 -44.009 62.238 1.00 33.39 ? 182 SER A C   1 
ATOM   1399 O O   . SER A 1 182 ? -25.964 -42.892 62.735 1.00 35.27 ? 182 SER A O   1 
ATOM   1400 C CB  . SER A 1 182 ? -24.099 -45.502 61.934 1.00 35.90 ? 182 SER A CB  1 
ATOM   1401 O OG  . SER A 1 182 ? -23.491 -44.895 63.058 1.00 35.57 ? 182 SER A OG  1 
ATOM   1402 N N   . LYS A 1 183 ? -27.154 -44.776 62.509 1.00 31.07 ? 183 LYS A N   1 
ATOM   1403 C CA  . LYS A 1 183 ? -28.116 -44.323 63.503 1.00 31.04 ? 183 LYS A CA  1 
ATOM   1404 C C   . LYS A 1 183 ? -27.429 -44.211 64.853 1.00 31.80 ? 183 LYS A C   1 
ATOM   1405 O O   . LYS A 1 183 ? -27.692 -43.275 65.611 1.00 30.56 ? 183 LYS A O   1 
ATOM   1406 C CB  . LYS A 1 183 ? -29.326 -45.250 63.614 1.00 26.03 ? 183 LYS A CB  1 
ATOM   1407 C CG  . LYS A 1 183 ? -30.349 -44.748 64.631 1.00 29.93 ? 183 LYS A CG  1 
ATOM   1408 C CD  . LYS A 1 183 ? -31.457 -45.753 64.915 1.00 35.10 ? 183 LYS A CD  1 
ATOM   1409 C CE  . LYS A 1 183 ? -32.327 -45.276 66.082 1.00 48.71 ? 183 LYS A CE  1 
ATOM   1410 N NZ  . LYS A 1 183 ? -33.223 -46.349 66.635 1.00 54.71 ? 183 LYS A NZ  1 
ATOM   1411 N N   . ALA A 1 184 ? -26.539 -45.163 65.142 1.00 39.02 ? 184 ALA A N   1 
ATOM   1412 C CA  . ALA A 1 184 ? -25.857 -45.199 66.439 1.00 40.06 ? 184 ALA A CA  1 
ATOM   1413 C C   . ALA A 1 184 ? -25.072 -43.916 66.655 1.00 35.04 ? 184 ALA A C   1 
ATOM   1414 O O   . ALA A 1 184 ? -25.244 -43.262 67.680 1.00 29.38 ? 184 ALA A O   1 
ATOM   1415 C CB  . ALA A 1 184 ? -24.942 -46.427 66.565 1.00 28.36 ? 184 ALA A CB  1 
ATOM   1416 N N   . ASP A 1 185 ? -24.239 -43.563 65.669 1.00 34.89 ? 185 ASP A N   1 
ATOM   1417 C CA  . ASP A 1 185 ? -23.450 -42.330 65.681 1.00 29.91 ? 185 ASP A CA  1 
ATOM   1418 C C   . ASP A 1 185 ? -24.338 -41.104 65.835 1.00 32.78 ? 185 ASP A C   1 
ATOM   1419 O O   . ASP A 1 185 ? -24.063 -40.235 66.663 1.00 31.53 ? 185 ASP A O   1 
ATOM   1420 C CB  . ASP A 1 185 ? -22.615 -42.184 64.398 1.00 40.38 ? 185 ASP A CB  1 
ATOM   1421 C CG  . ASP A 1 185 ? -21.337 -43.034 64.417 1.00 47.82 ? 185 ASP A CG  1 
ATOM   1422 O OD1 . ASP A 1 185 ? -21.056 -43.663 65.464 1.00 49.32 ? 185 ASP A OD1 1 
ATOM   1423 O OD2 . ASP A 1 185 ? -20.605 -43.063 63.397 1.00 42.71 ? 185 ASP A OD2 1 
ATOM   1424 N N   . TYR A 1 186 ? -25.396 -41.036 65.029 1.00 31.96 ? 186 TYR A N   1 
ATOM   1425 C CA  . TYR A 1 186 ? -26.310 -39.909 65.067 1.00 20.50 ? 186 TYR A CA  1 
ATOM   1426 C C   . TYR A 1 186 ? -26.849 -39.740 66.467 1.00 25.17 ? 186 TYR A C   1 
ATOM   1427 O O   . TYR A 1 186 ? -26.887 -38.631 66.992 1.00 28.48 ? 186 TYR A O   1 
ATOM   1428 C CB  . TYR A 1 186 ? -27.462 -40.080 64.063 1.00 28.20 ? 186 TYR A CB  1 
ATOM   1429 C CG  . TYR A 1 186 ? -28.483 -38.960 64.133 1.00 24.15 ? 186 TYR A CG  1 
ATOM   1430 C CD1 . TYR A 1 186 ? -28.185 -37.695 63.647 1.00 24.08 ? 186 TYR A CD1 1 
ATOM   1431 C CD2 . TYR A 1 186 ? -29.738 -39.160 64.695 1.00 27.60 ? 186 TYR A CD2 1 
ATOM   1432 C CE1 . TYR A 1 186 ? -29.101 -36.666 63.717 1.00 25.71 ? 186 TYR A CE1 1 
ATOM   1433 C CE2 . TYR A 1 186 ? -30.664 -38.133 64.761 1.00 22.47 ? 186 TYR A CE2 1 
ATOM   1434 C CZ  . TYR A 1 186 ? -30.338 -36.891 64.279 1.00 25.57 ? 186 TYR A CZ  1 
ATOM   1435 O OH  . TYR A 1 186 ? -31.247 -35.864 64.356 1.00 16.51 ? 186 TYR A OH  1 
ATOM   1436 N N   . GLU A 1 187 ? -27.252 -40.846 67.082 1.00 30.82 ? 187 GLU A N   1 
ATOM   1437 C CA  . GLU A 1 187 ? -27.825 -40.784 68.426 1.00 33.15 ? 187 GLU A CA  1 
ATOM   1438 C C   . GLU A 1 187 ? -26.831 -40.312 69.503 1.00 29.37 ? 187 GLU A C   1 
ATOM   1439 O O   . GLU A 1 187 ? -27.220 -39.674 70.480 1.00 27.44 ? 187 GLU A O   1 
ATOM   1440 C CB  . GLU A 1 187 ? -28.477 -42.119 68.811 1.00 26.88 ? 187 GLU A CB  1 
ATOM   1441 C CG  . GLU A 1 187 ? -29.738 -42.478 68.004 1.00 30.36 ? 187 GLU A CG  1 
ATOM   1442 C CD  . GLU A 1 187 ? -30.863 -41.450 68.129 1.00 36.86 ? 187 GLU A CD  1 
ATOM   1443 O OE1 . GLU A 1 187 ? -30.794 -40.584 69.034 1.00 36.41 ? 187 GLU A OE1 1 
ATOM   1444 O OE2 . GLU A 1 187 ? -31.821 -41.505 67.312 1.00 31.44 ? 187 GLU A OE2 1 
ATOM   1445 N N   . LYS A 1 188 ? -25.549 -40.599 69.308 1.00 28.98 ? 188 LYS A N   1 
ATOM   1446 C CA  . LYS A 1 188 ? -24.531 -40.206 70.286 1.00 34.14 ? 188 LYS A CA  1 
ATOM   1447 C C   . LYS A 1 188 ? -24.153 -38.721 70.290 1.00 36.76 ? 188 LYS A C   1 
ATOM   1448 O O   . LYS A 1 188 ? -23.254 -38.326 71.028 1.00 37.84 ? 188 LYS A O   1 
ATOM   1449 C CB  . LYS A 1 188 ? -23.256 -41.032 70.102 1.00 34.09 ? 188 LYS A CB  1 
ATOM   1450 C CG  . LYS A 1 188 ? -23.403 -42.507 70.392 1.00 32.09 ? 188 LYS A CG  1 
ATOM   1451 C CD  . LYS A 1 188 ? -22.085 -43.211 70.136 1.00 36.98 ? 188 LYS A CD  1 
ATOM   1452 C CE  . LYS A 1 188 ? -22.167 -44.709 70.400 1.00 48.99 ? 188 LYS A CE  1 
ATOM   1453 N NZ  . LYS A 1 188 ? -22.197 -45.520 69.136 1.00 46.11 ? 188 LYS A NZ  1 
ATOM   1454 N N   . HIS A 1 189 ? -24.822 -37.900 69.482 1.00 34.95 ? 189 HIS A N   1 
ATOM   1455 C CA  . HIS A 1 189 ? -24.440 -36.494 69.367 1.00 25.04 ? 189 HIS A CA  1 
ATOM   1456 C C   . HIS A 1 189 ? -25.638 -35.563 69.407 1.00 31.54 ? 189 HIS A C   1 
ATOM   1457 O O   . HIS A 1 189 ? -26.773 -36.007 69.271 1.00 33.83 ? 189 HIS A O   1 
ATOM   1458 C CB  . HIS A 1 189 ? -23.640 -36.273 68.091 1.00 28.59 ? 189 HIS A CB  1 
ATOM   1459 C CG  . HIS A 1 189 ? -22.353 -37.041 68.038 1.00 34.79 ? 189 HIS A CG  1 
ATOM   1460 N ND1 . HIS A 1 189 ? -22.173 -38.142 67.225 1.00 37.79 ? 189 HIS A ND1 1 
ATOM   1461 C CD2 . HIS A 1 189 ? -21.177 -36.860 68.687 1.00 29.46 ? 189 HIS A CD2 1 
ATOM   1462 C CE1 . HIS A 1 189 ? -20.944 -38.605 67.377 1.00 37.42 ? 189 HIS A CE1 1 
ATOM   1463 N NE2 . HIS A 1 189 ? -20.320 -37.846 68.258 1.00 37.00 ? 189 HIS A NE2 1 
ATOM   1464 N N   . LYS A 1 190 ? -25.400 -34.266 69.583 1.00 29.61 ? 190 LYS A N   1 
ATOM   1465 C CA  . LYS A 1 190 ? -26.528 -33.350 69.711 1.00 32.66 ? 190 LYS A CA  1 
ATOM   1466 C C   . LYS A 1 190 ? -26.642 -32.241 68.652 1.00 30.69 ? 190 LYS A C   1 
ATOM   1467 O O   . LYS A 1 190 ? -27.709 -32.044 68.072 1.00 32.74 ? 190 LYS A O   1 
ATOM   1468 C CB  . LYS A 1 190 ? -26.570 -32.738 71.115 1.00 30.44 ? 190 LYS A CB  1 
ATOM   1469 C CG  . LYS A 1 190 ? -27.862 -31.974 71.407 1.00 30.28 ? 190 LYS A CG  1 
ATOM   1470 C CD  . LYS A 1 190 ? -27.771 -31.194 72.717 1.00 43.93 ? 190 LYS A CD  1 
ATOM   1471 C CE  . LYS A 1 190 ? -28.685 -29.978 72.707 1.00 47.80 ? 190 LYS A CE  1 
ATOM   1472 N NZ  . LYS A 1 190 ? -28.150 -28.892 73.572 1.00 47.27 ? 190 LYS A NZ  1 
ATOM   1473 N N   . VAL A 1 191 ? -25.565 -31.500 68.426 1.00 28.46 ? 191 VAL A N   1 
ATOM   1474 C CA  . VAL A 1 191 ? -25.652 -30.284 67.617 1.00 27.23 ? 191 VAL A CA  1 
ATOM   1475 C C   . VAL A 1 191 ? -25.123 -30.511 66.202 1.00 26.51 ? 191 VAL A C   1 
ATOM   1476 O O   . VAL A 1 191 ? -23.934 -30.767 66.008 1.00 27.23 ? 191 VAL A O   1 
ATOM   1477 C CB  . VAL A 1 191 ? -24.930 -29.091 68.305 1.00 22.91 ? 191 VAL A CB  1 
ATOM   1478 C CG1 . VAL A 1 191 ? -24.756 -27.927 67.361 1.00 15.49 ? 191 VAL A CG1 1 
ATOM   1479 C CG2 . VAL A 1 191 ? -25.710 -28.649 69.527 1.00 25.96 ? 191 VAL A CG2 1 
ATOM   1480 N N   . TYR A 1 192 ? -26.024 -30.415 65.227 1.00 25.30 ? 192 TYR A N   1 
ATOM   1481 C CA  . TYR A 1 192 ? -25.711 -30.624 63.808 1.00 23.83 ? 192 TYR A CA  1 
ATOM   1482 C C   . TYR A 1 192 ? -25.774 -29.311 63.062 1.00 22.76 ? 192 TYR A C   1 
ATOM   1483 O O   . TYR A 1 192 ? -26.825 -28.690 62.975 1.00 24.17 ? 192 TYR A O   1 
ATOM   1484 C CB  . TYR A 1 192 ? -26.677 -31.637 63.188 1.00 21.59 ? 192 TYR A CB  1 
ATOM   1485 C CG  . TYR A 1 192 ? -26.490 -33.017 63.773 1.00 25.31 ? 192 TYR A CG  1 
ATOM   1486 C CD1 . TYR A 1 192 ? -25.656 -33.936 63.162 1.00 20.60 ? 192 TYR A CD1 1 
ATOM   1487 C CD2 . TYR A 1 192 ? -27.108 -33.382 64.960 1.00 28.18 ? 192 TYR A CD2 1 
ATOM   1488 C CE1 . TYR A 1 192 ? -25.461 -35.186 63.695 1.00 25.37 ? 192 TYR A CE1 1 
ATOM   1489 C CE2 . TYR A 1 192 ? -26.913 -34.635 65.513 1.00 24.32 ? 192 TYR A CE2 1 
ATOM   1490 C CZ  . TYR A 1 192 ? -26.087 -35.527 64.874 1.00 28.12 ? 192 TYR A CZ  1 
ATOM   1491 O OH  . TYR A 1 192 ? -25.883 -36.766 65.409 1.00 26.77 ? 192 TYR A OH  1 
ATOM   1492 N N   . ALA A 1 193 ? -24.634 -28.871 62.548 1.00 23.70 ? 193 ALA A N   1 
ATOM   1493 C CA  . ALA A 1 193 ? -24.570 -27.584 61.878 1.00 23.04 ? 193 ALA A CA  1 
ATOM   1494 C C   . ALA A 1 193 ? -23.900 -27.680 60.523 1.00 21.11 ? 193 ALA A C   1 
ATOM   1495 O O   . ALA A 1 193 ? -22.837 -28.276 60.376 1.00 27.14 ? 193 ALA A O   1 
ATOM   1496 C CB  . ALA A 1 193 ? -23.867 -26.553 62.749 1.00 22.73 ? 193 ALA A CB  1 
ATOM   1497 N N   . CYS A 1 194 ? -24.546 -27.106 59.522 1.00 15.78 ? 194 CYS A N   1 
ATOM   1498 C CA  . CYS A 1 194 ? -23.885 -26.932 58.264 1.00 22.29 ? 194 CYS A CA  1 
ATOM   1499 C C   . CYS A 1 194 ? -23.643 -25.446 58.117 1.00 22.46 ? 194 CYS A C   1 
ATOM   1500 O O   . CYS A 1 194 ? -24.496 -24.621 58.466 1.00 24.84 ? 194 CYS A O   1 
ATOM   1501 C CB  . CYS A 1 194 ? -24.676 -27.541 57.099 1.00 28.83 ? 194 CYS A CB  1 
ATOM   1502 S SG  . CYS A 1 194 ? -25.905 -26.495 56.315 1.00 37.35 ? 194 CYS A SG  1 
ATOM   1503 N N   . GLU A 1 195 ? -22.443 -25.127 57.653 1.00 17.44 ? 195 GLU A N   1 
ATOM   1504 C CA  . GLU A 1 195 ? -22.005 -23.762 57.490 1.00 21.79 ? 195 GLU A CA  1 
ATOM   1505 C C   . GLU A 1 195 ? -21.760 -23.489 56.013 1.00 28.05 ? 195 GLU A C   1 
ATOM   1506 O O   . GLU A 1 195 ? -21.098 -24.275 55.317 1.00 21.76 ? 195 GLU A O   1 
ATOM   1507 C CB  . GLU A 1 195 ? -20.718 -23.531 58.266 1.00 28.52 ? 195 GLU A CB  1 
ATOM   1508 C CG  . GLU A 1 195 ? -20.598 -22.130 58.799 1.00 28.01 ? 195 GLU A CG  1 
ATOM   1509 C CD  . GLU A 1 195 ? -19.169 -21.704 58.945 1.00 32.83 ? 195 GLU A CD  1 
ATOM   1510 O OE1 . GLU A 1 195 ? -18.377 -22.012 58.020 1.00 39.63 ? 195 GLU A OE1 1 
ATOM   1511 O OE2 . GLU A 1 195 ? -18.842 -21.076 59.976 1.00 29.55 ? 195 GLU A OE2 1 
ATOM   1512 N N   . VAL A 1 196 ? -22.296 -22.370 55.543 1.00 20.85 ? 196 VAL A N   1 
ATOM   1513 C CA  . VAL A 1 196 ? -22.283 -22.077 54.128 1.00 18.85 ? 196 VAL A CA  1 
ATOM   1514 C C   . VAL A 1 196 ? -21.503 -20.805 53.840 1.00 20.51 ? 196 VAL A C   1 
ATOM   1515 O O   . VAL A 1 196 ? -21.678 -19.786 54.500 1.00 23.45 ? 196 VAL A O   1 
ATOM   1516 C CB  . VAL A 1 196 ? -23.717 -21.983 53.595 1.00 22.90 ? 196 VAL A CB  1 
ATOM   1517 C CG1 . VAL A 1 196 ? -23.751 -21.392 52.183 1.00 11.20 ? 196 VAL A CG1 1 
ATOM   1518 C CG2 . VAL A 1 196 ? -24.387 -23.367 53.682 1.00 18.50 ? 196 VAL A CG2 1 
ATOM   1519 N N   . THR A 1 197 ? -20.621 -20.890 52.857 1.00 19.27 ? 197 THR A N   1 
ATOM   1520 C CA  . THR A 1 197 ? -19.829 -19.762 52.435 1.00 23.20 ? 197 THR A CA  1 
ATOM   1521 C C   . THR A 1 197 ? -20.113 -19.501 50.971 1.00 23.20 ? 197 THR A C   1 
ATOM   1522 O O   . THR A 1 197 ? -20.115 -20.424 50.153 1.00 26.56 ? 197 THR A O   1 
ATOM   1523 C CB  . THR A 1 197 ? -18.316 -20.048 52.602 1.00 26.66 ? 197 THR A CB  1 
ATOM   1524 O OG1 . THR A 1 197 ? -18.010 -20.210 53.996 1.00 27.24 ? 197 THR A OG1 1 
ATOM   1525 C CG2 . THR A 1 197 ? -17.485 -18.907 52.010 1.00 20.00 ? 197 THR A CG2 1 
ATOM   1526 N N   . HIS A 1 198 ? -20.347 -18.243 50.632 1.00 18.15 ? 198 HIS A N   1 
ATOM   1527 C CA  . HIS A 1 198 ? -20.621 -17.887 49.252 1.00 18.51 ? 198 HIS A CA  1 
ATOM   1528 C C   . HIS A 1 198 ? -20.271 -16.439 49.013 1.00 16.45 ? 198 HIS A C   1 
ATOM   1529 O O   . HIS A 1 198 ? -20.355 -15.619 49.925 1.00 16.64 ? 198 HIS A O   1 
ATOM   1530 C CB  . HIS A 1 198 ? -22.099 -18.109 48.933 1.00 16.26 ? 198 HIS A CB  1 
ATOM   1531 C CG  . HIS A 1 198 ? -22.436 -17.904 47.494 1.00 13.08 ? 198 HIS A CG  1 
ATOM   1532 N ND1 . HIS A 1 198 ? -22.792 -16.678 46.987 1.00 11.75 ? 198 HIS A ND1 1 
ATOM   1533 C CD2 . HIS A 1 198 ? -22.457 -18.765 46.453 1.00 13.89 ? 198 HIS A CD2 1 
ATOM   1534 C CE1 . HIS A 1 198 ? -23.028 -16.795 45.695 1.00 14.36 ? 198 HIS A CE1 1 
ATOM   1535 N NE2 . HIS A 1 198 ? -22.835 -18.053 45.345 1.00 10.68 ? 198 HIS A NE2 1 
ATOM   1536 N N   . GLN A 1 199 ? -19.893 -16.129 47.779 1.00 17.63 ? 199 GLN A N   1 
ATOM   1537 C CA  . GLN A 1 199 ? -19.549 -14.759 47.376 1.00 22.45 ? 199 GLN A CA  1 
ATOM   1538 C C   . GLN A 1 199 ? -20.619 -13.716 47.744 1.00 23.16 ? 199 GLN A C   1 
ATOM   1539 O O   . GLN A 1 199 ? -20.284 -12.582 48.074 1.00 22.37 ? 199 GLN A O   1 
ATOM   1540 C CB  . GLN A 1 199 ? -19.269 -14.716 45.865 1.00 21.47 ? 199 GLN A CB  1 
ATOM   1541 C CG  . GLN A 1 199 ? -18.817 -13.374 45.315 1.00 20.00 ? 199 GLN A CG  1 
ATOM   1542 C CD  . GLN A 1 199 ? -18.451 -13.433 43.830 1.00 29.29 ? 199 GLN A CD  1 
ATOM   1543 O OE1 . GLN A 1 199 ? -18.358 -14.510 43.234 1.00 29.28 ? 199 GLN A OE1 1 
ATOM   1544 N NE2 . GLN A 1 199 ? -18.241 -12.266 43.228 1.00 33.89 ? 199 GLN A NE2 1 
ATOM   1545 N N   . GLY A 1 200 ? -21.896 -14.104 47.689 1.00 15.28 ? 200 GLY A N   1 
ATOM   1546 C CA  . GLY A 1 200 ? -22.990 -13.203 47.999 1.00 17.12 ? 200 GLY A CA  1 
ATOM   1547 C C   . GLY A 1 200 ? -23.285 -13.015 49.481 1.00 24.30 ? 200 GLY A C   1 
ATOM   1548 O O   . GLY A 1 200 ? -24.107 -12.177 49.862 1.00 27.97 ? 200 GLY A O   1 
ATOM   1549 N N   . LEU A 1 201 ? -22.626 -13.799 50.324 1.00 18.63 ? 201 LEU A N   1 
ATOM   1550 C CA  . LEU A 1 201 ? -22.793 -13.655 51.757 1.00 18.71 ? 201 LEU A CA  1 
ATOM   1551 C C   . LEU A 1 201 ? -21.674 -12.793 52.316 1.00 23.95 ? 201 LEU A C   1 
ATOM   1552 O O   . LEU A 1 201 ? -20.512 -12.939 51.938 1.00 26.19 ? 201 LEU A O   1 
ATOM   1553 C CB  . LEU A 1 201 ? -22.802 -15.019 52.429 1.00 18.11 ? 201 LEU A CB  1 
ATOM   1554 C CG  . LEU A 1 201 ? -23.976 -15.892 51.983 1.00 18.52 ? 201 LEU A CG  1 
ATOM   1555 C CD1 . LEU A 1 201 ? -23.853 -17.256 52.611 1.00 17.46 ? 201 LEU A CD1 1 
ATOM   1556 C CD2 . LEU A 1 201 ? -25.285 -15.235 52.361 1.00 11.13 ? 201 LEU A CD2 1 
ATOM   1557 N N   . SER A 1 202 ? -22.021 -11.869 53.200 1.00 25.02 ? 202 SER A N   1 
ATOM   1558 C CA  . SER A 1 202 ? -20.997 -10.999 53.751 1.00 31.56 ? 202 SER A CA  1 
ATOM   1559 C C   . SER A 1 202 ? -20.275 -11.706 54.897 1.00 24.83 ? 202 SER A C   1 
ATOM   1560 O O   . SER A 1 202 ? -19.210 -11.281 55.315 1.00 41.62 ? 202 SER A O   1 
ATOM   1561 C CB  . SER A 1 202 ? -21.571 -9.640  54.164 1.00 22.82 ? 202 SER A CB  1 
ATOM   1562 O OG  . SER A 1 202 ? -22.442 -9.756  55.264 1.00 29.77 ? 202 SER A OG  1 
ATOM   1563 N N   . SER A 1 203 ? -20.863 -12.785 55.398 1.00 20.75 ? 203 SER A N   1 
ATOM   1564 C CA  . SER A 1 203 ? -20.180 -13.681 56.329 1.00 27.39 ? 203 SER A CA  1 
ATOM   1565 C C   . SER A 1 203 ? -20.884 -15.041 56.268 1.00 25.35 ? 203 SER A C   1 
ATOM   1566 O O   . SER A 1 203 ? -22.014 -15.112 55.796 1.00 24.35 ? 203 SER A O   1 
ATOM   1567 C CB  . SER A 1 203 ? -20.133 -13.104 57.753 1.00 24.28 ? 203 SER A CB  1 
ATOM   1568 O OG  . SER A 1 203 ? -21.411 -12.756 58.222 1.00 28.83 ? 203 SER A OG  1 
ATOM   1569 N N   . PRO A 1 204 ? -20.208 -16.129 56.698 1.00 30.61 ? 204 PRO A N   1 
ATOM   1570 C CA  . PRO A 1 204 ? -20.825 -17.458 56.554 1.00 22.81 ? 204 PRO A CA  1 
ATOM   1571 C C   . PRO A 1 204 ? -22.167 -17.566 57.271 1.00 22.53 ? 204 PRO A C   1 
ATOM   1572 O O   . PRO A 1 204 ? -22.355 -16.968 58.324 1.00 26.00 ? 204 PRO A O   1 
ATOM   1573 C CB  . PRO A 1 204 ? -19.799 -18.394 57.195 1.00 25.24 ? 204 PRO A CB  1 
ATOM   1574 C CG  . PRO A 1 204 ? -18.500 -17.676 57.071 1.00 27.31 ? 204 PRO A CG  1 
ATOM   1575 C CD  . PRO A 1 204 ? -18.822 -16.216 57.201 1.00 24.95 ? 204 PRO A CD  1 
ATOM   1576 N N   . VAL A 1 205 ? -23.095 -18.301 56.677 1.00 18.90 ? 205 VAL A N   1 
ATOM   1577 C CA  . VAL A 1 205 ? -24.403 -18.523 57.274 1.00 18.12 ? 205 VAL A CA  1 
ATOM   1578 C C   . VAL A 1 205 ? -24.443 -19.931 57.839 1.00 15.92 ? 205 VAL A C   1 
ATOM   1579 O O   . VAL A 1 205 ? -24.058 -20.887 57.173 1.00 23.54 ? 205 VAL A O   1 
ATOM   1580 C CB  . VAL A 1 205 ? -25.531 -18.383 56.229 1.00 15.10 ? 205 VAL A CB  1 
ATOM   1581 C CG1 . VAL A 1 205 ? -26.853 -18.749 56.829 1.00 20.44 ? 205 VAL A CG1 1 
ATOM   1582 C CG2 . VAL A 1 205 ? -25.576 -16.972 55.687 1.00 20.73 ? 205 VAL A CG2 1 
ATOM   1583 N N   . THR A 1 206 ? -24.900 -20.059 59.073 1.00 17.37 ? 206 THR A N   1 
ATOM   1584 C CA  . THR A 1 206 ? -24.951 -21.349 59.723 1.00 19.61 ? 206 THR A CA  1 
ATOM   1585 C C   . THR A 1 206 ? -26.406 -21.718 59.994 1.00 21.55 ? 206 THR A C   1 
ATOM   1586 O O   . THR A 1 206 ? -27.157 -20.933 60.555 1.00 24.56 ? 206 THR A O   1 
ATOM   1587 C CB  . THR A 1 206 ? -24.172 -21.336 61.055 1.00 18.83 ? 206 THR A CB  1 
ATOM   1588 O OG1 . THR A 1 206 ? -22.792 -21.070 60.803 1.00 17.57 ? 206 THR A OG1 1 
ATOM   1589 C CG2 . THR A 1 206 ? -24.276 -22.689 61.745 1.00 21.10 ? 206 THR A CG2 1 
ATOM   1590 N N   . LYS A 1 207 ? -26.799 -22.910 59.598 1.00 19.41 ? 207 LYS A N   1 
ATOM   1591 C CA  . LYS A 1 207 ? -28.084 -23.454 59.909 1.00 20.00 ? 207 LYS A CA  1 
ATOM   1592 C C   . LYS A 1 207 ? -27.873 -24.700 60.731 1.00 29.00 ? 207 LYS A C   1 
ATOM   1593 O O   . LYS A 1 207 ? -27.040 -25.473 60.450 1.00 23.74 ? 207 LYS A O   1 
ATOM   1594 C CB  . LYS A 1 207 ? -28.843 -23.777 58.645 1.00 17.25 ? 207 LYS A CB  1 
ATOM   1595 C CG  . LYS A 1 207 ? -29.600 -22.645 58.013 1.00 20.33 ? 207 LYS A CG  1 
ATOM   1596 C CD  . LYS A 1 207 ? -30.196 -21.737 59.048 1.00 24.19 ? 207 LYS A CD  1 
ATOM   1597 C CE  . LYS A 1 207 ? -31.286 -20.857 58.538 1.00 20.21 ? 207 LYS A CE  1 
ATOM   1598 N NZ  . LYS A 1 207 ? -30.689 -19.652 57.983 1.00 31.55 ? 207 LYS A NZ  1 
ATOM   1599 N N   . SER A 1 208 ? -28.618 -24.876 61.795 1.00 29.20 ? 208 SER A N   1 
ATOM   1600 C CA  . SER A 1 208 ? -28.354 -25.990 62.696 1.00 30.14 ? 208 SER A CA  1 
ATOM   1601 C C   . SER A 1 208 ? -29.536 -26.380 63.542 1.00 24.37 ? 208 SER A C   1 
ATOM   1602 O O   . SER A 1 208 ? -30.521 -25.664 63.631 1.00 29.12 ? 208 SER A O   1 
ATOM   1603 C CB  . SER A 1 208 ? -27.200 -25.654 63.619 1.00 23.77 ? 208 SER A CB  1 
ATOM   1604 O OG  . SER A 1 208 ? -27.537 -24.549 64.410 1.00 24.03 ? 208 SER A OG  1 
ATOM   1605 N N   . PHE A 1 209 ? -29.424 -27.535 64.175 1.00 28.65 ? 209 PHE A N   1 
ATOM   1606 C CA  . PHE A 1 209 ? -30.480 -27.994 65.045 1.00 26.50 ? 209 PHE A CA  1 
ATOM   1607 C C   . PHE A 1 209 ? -29.896 -28.847 66.152 1.00 32.03 ? 209 PHE A C   1 
ATOM   1608 O O   . PHE A 1 209 ? -28.764 -29.327 66.043 1.00 32.91 ? 209 PHE A O   1 
ATOM   1609 C CB  . PHE A 1 209 ? -31.547 -28.757 64.254 1.00 21.26 ? 209 PHE A CB  1 
ATOM   1610 C CG  . PHE A 1 209 ? -31.059 -30.034 63.635 1.00 26.36 ? 209 PHE A CG  1 
ATOM   1611 C CD1 . PHE A 1 209 ? -30.553 -30.046 62.339 1.00 26.23 ? 209 PHE A CD1 1 
ATOM   1612 C CD2 . PHE A 1 209 ? -31.123 -31.233 64.336 1.00 28.59 ? 209 PHE A CD2 1 
ATOM   1613 C CE1 . PHE A 1 209 ? -30.108 -31.224 61.757 1.00 22.89 ? 209 PHE A CE1 1 
ATOM   1614 C CE2 . PHE A 1 209 ? -30.676 -32.417 63.764 1.00 25.04 ? 209 PHE A CE2 1 
ATOM   1615 C CZ  . PHE A 1 209 ? -30.170 -32.410 62.469 1.00 29.05 ? 209 PHE A CZ  1 
ATOM   1616 N N   . ASN A 1 210 ? -30.656 -29.002 67.231 1.00 34.66 ? 210 ASN A N   1 
ATOM   1617 C CA  . ASN A 1 210 ? -30.344 -29.992 68.240 1.00 32.91 ? 210 ASN A CA  1 
ATOM   1618 C C   . ASN A 1 210 ? -31.264 -31.178 68.027 1.00 32.59 ? 210 ASN A C   1 
ATOM   1619 O O   . ASN A 1 210 ? -32.485 -31.011 67.917 1.00 37.94 ? 210 ASN A O   1 
ATOM   1620 C CB  . ASN A 1 210 ? -30.547 -29.414 69.646 1.00 37.06 ? 210 ASN A CB  1 
ATOM   1621 C CG  . ASN A 1 210 ? -29.804 -28.121 69.850 1.00 38.18 ? 210 ASN A CG  1 
ATOM   1622 O OD1 . ASN A 1 210 ? -28.844 -27.826 69.138 1.00 43.96 ? 210 ASN A OD1 1 
ATOM   1623 N ND2 . ASN A 1 210 ? -30.246 -27.331 70.817 1.00 43.32 ? 210 ASN A ND2 1 
ATOM   1624 N N   . ARG A 1 211 ? -30.679 -32.368 67.963 1.00 25.40 ? 211 ARG A N   1 
ATOM   1625 C CA  . ARG A 1 211 ? -31.461 -33.580 67.800 1.00 31.09 ? 211 ARG A CA  1 
ATOM   1626 C C   . ARG A 1 211 ? -32.565 -33.692 68.876 1.00 36.64 ? 211 ARG A C   1 
ATOM   1627 O O   . ARG A 1 211 ? -32.277 -33.858 70.063 1.00 35.77 ? 211 ARG A O   1 
ATOM   1628 C CB  . ARG A 1 211 ? -30.559 -34.810 67.814 1.00 22.00 ? 211 ARG A CB  1 
ATOM   1629 C CG  . ARG A 1 211 ? -31.342 -36.105 67.834 1.00 27.60 ? 211 ARG A CG  1 
ATOM   1630 C CD  . ARG A 1 211 ? -30.453 -37.327 67.935 1.00 27.66 ? 211 ARG A CD  1 
ATOM   1631 N NE  . ARG A 1 211 ? -29.379 -37.162 68.898 1.00 25.41 ? 211 ARG A NE  1 
ATOM   1632 C CZ  . ARG A 1 211 ? -29.550 -37.143 70.218 1.00 38.60 ? 211 ARG A CZ  1 
ATOM   1633 N NH1 . ARG A 1 211 ? -30.767 -37.262 70.747 1.00 30.43 ? 211 ARG A NH1 1 
ATOM   1634 N NH2 . ARG A 1 211 ? -28.502 -36.991 71.017 1.00 36.82 ? 211 ARG A NH2 1 
ATOM   1635 N N   . GLY A 1 212 ? -33.826 -33.573 68.463 1.00 35.64 ? 212 GLY A N   1 
ATOM   1636 C CA  . GLY A 1 212 ? -34.947 -33.637 69.392 1.00 40.75 ? 212 GLY A CA  1 
ATOM   1637 C C   . GLY A 1 212 ? -35.090 -32.415 70.282 1.00 33.72 ? 212 GLY A C   1 
ATOM   1638 O O   . GLY A 1 212 ? -35.460 -31.321 69.827 1.00 41.65 ? 212 GLY A O   1 
ATOM   1639 N N   . GLN B 2 1   ? -50.131 -34.835 15.613 1.00 38.26 ? 1   GLN B N   1 
ATOM   1640 C CA  . GLN B 2 1   ? -48.828 -34.543 16.199 1.00 30.07 ? 1   GLN B CA  1 
ATOM   1641 C C   . GLN B 2 1   ? -47.868 -35.726 16.021 1.00 30.53 ? 1   GLN B C   1 
ATOM   1642 O O   . GLN B 2 1   ? -48.202 -36.853 16.390 1.00 33.47 ? 1   GLN B O   1 
ATOM   1643 C CB  . GLN B 2 1   ? -48.996 -34.217 17.685 1.00 30.29 ? 1   GLN B CB  1 
ATOM   1644 N N   . VAL B 2 2   ? -46.693 -35.482 15.441 1.00 25.28 ? 2   VAL B N   1 
ATOM   1645 C CA  . VAL B 2 2   ? -45.678 -36.530 15.339 1.00 24.45 ? 2   VAL B CA  1 
ATOM   1646 C C   . VAL B 2 2   ? -45.011 -36.808 16.687 1.00 28.76 ? 2   VAL B C   1 
ATOM   1647 O O   . VAL B 2 2   ? -44.485 -35.894 17.321 1.00 30.57 ? 2   VAL B O   1 
ATOM   1648 C CB  . VAL B 2 2   ? -44.577 -36.167 14.330 1.00 32.18 ? 2   VAL B CB  1 
ATOM   1649 C CG1 . VAL B 2 2   ? -43.369 -37.115 14.476 1.00 22.73 ? 2   VAL B CG1 1 
ATOM   1650 C CG2 . VAL B 2 2   ? -45.130 -36.206 12.923 1.00 28.99 ? 2   VAL B CG2 1 
ATOM   1651 N N   . GLN B 2 3   ? -45.031 -38.068 17.115 1.00 23.43 ? 3   GLN B N   1 
ATOM   1652 C CA  . GLN B 2 3   ? -44.413 -38.480 18.374 1.00 26.57 ? 3   GLN B CA  1 
ATOM   1653 C C   . GLN B 2 3   ? -43.689 -39.826 18.238 1.00 27.93 ? 3   GLN B C   1 
ATOM   1654 O O   . GLN B 2 3   ? -44.028 -40.651 17.386 1.00 26.77 ? 3   GLN B O   1 
ATOM   1655 C CB  . GLN B 2 3   ? -45.468 -38.605 19.471 1.00 27.09 ? 3   GLN B CB  1 
ATOM   1656 C CG  . GLN B 2 3   ? -46.166 -37.309 19.821 1.00 40.14 ? 3   GLN B CG  1 
ATOM   1657 C CD  . GLN B 2 3   ? -47.085 -37.448 21.024 1.00 49.39 ? 3   GLN B CD  1 
ATOM   1658 O OE1 . GLN B 2 3   ? -47.606 -38.529 21.300 1.00 46.37 ? 3   GLN B OE1 1 
ATOM   1659 N NE2 . GLN B 2 3   ? -47.287 -36.348 21.746 1.00 59.46 ? 3   GLN B NE2 1 
ATOM   1660 N N   . LEU B 2 4   ? -42.684 -40.037 19.081 1.00 22.68 ? 4   LEU B N   1 
ATOM   1661 C CA  . LEU B 2 4   ? -42.058 -41.348 19.222 1.00 25.86 ? 4   LEU B CA  1 
ATOM   1662 C C   . LEU B 2 4   ? -41.927 -41.630 20.720 1.00 27.51 ? 4   LEU B C   1 
ATOM   1663 O O   . LEU B 2 4   ? -41.422 -40.795 21.471 1.00 25.87 ? 4   LEU B O   1 
ATOM   1664 C CB  . LEU B 2 4   ? -40.691 -41.419 18.517 1.00 19.60 ? 4   LEU B CB  1 
ATOM   1665 C CG  . LEU B 2 4   ? -40.557 -41.144 17.003 1.00 19.83 ? 4   LEU B CG  1 
ATOM   1666 C CD1 . LEU B 2 4   ? -40.658 -39.663 16.667 1.00 19.85 ? 4   LEU B CD1 1 
ATOM   1667 C CD2 . LEU B 2 4   ? -39.257 -41.688 16.444 1.00 16.51 ? 4   LEU B CD2 1 
ATOM   1668 N N   . LYS B 2 5   ? -42.420 -42.784 21.166 1.00 29.20 ? 5   LYS B N   1 
ATOM   1669 C CA  . LYS B 2 5   ? -42.340 -43.132 22.581 1.00 23.82 ? 5   LYS B CA  1 
ATOM   1670 C C   . LYS B 2 5   ? -41.602 -44.432 22.723 1.00 25.98 ? 5   LYS B C   1 
ATOM   1671 O O   . LYS B 2 5   ? -41.936 -45.422 22.078 1.00 22.88 ? 5   LYS B O   1 
ATOM   1672 C CB  . LYS B 2 5   ? -43.728 -43.217 23.210 1.00 33.62 ? 5   LYS B CB  1 
ATOM   1673 C CG  . LYS B 2 5   ? -44.583 -41.998 22.941 1.00 30.69 ? 5   LYS B CG  1 
ATOM   1674 C CD  . LYS B 2 5   ? -45.904 -42.067 23.683 1.00 59.98 ? 5   LYS B CD  1 
ATOM   1675 C CE  . LYS B 2 5   ? -46.821 -40.934 23.246 1.00 56.01 ? 5   LYS B CE  1 
ATOM   1676 N NZ  . LYS B 2 5   ? -46.056 -39.657 23.083 1.00 53.69 ? 5   LYS B NZ  1 
ATOM   1677 N N   . GLN B 2 6   ? -40.560 -44.412 23.543 1.00 23.72 ? 6   GLN B N   1 
ATOM   1678 C CA  . GLN B 2 6   ? -39.701 -45.565 23.686 1.00 19.39 ? 6   GLN B CA  1 
ATOM   1679 C C   . GLN B 2 6   ? -40.088 -46.311 24.952 1.00 27.36 ? 6   GLN B C   1 
ATOM   1680 O O   . GLN B 2 6   ? -40.658 -45.722 25.868 1.00 21.76 ? 6   GLN B O   1 
ATOM   1681 C CB  . GLN B 2 6   ? -38.244 -45.123 23.776 1.00 25.06 ? 6   GLN B CB  1 
ATOM   1682 C CG  . GLN B 2 6   ? -37.684 -44.538 22.509 1.00 20.00 ? 6   GLN B CG  1 
ATOM   1683 C CD  . GLN B 2 6   ? -36.309 -43.915 22.712 1.00 20.96 ? 6   GLN B CD  1 
ATOM   1684 O OE1 . GLN B 2 6   ? -36.093 -42.759 22.370 1.00 19.33 ? 6   GLN B OE1 1 
ATOM   1685 N NE2 . GLN B 2 6   ? -35.375 -44.686 23.251 1.00 17.37 ? 6   GLN B NE2 1 
ATOM   1686 N N   . SER B 2 7   ? -39.782 -47.605 25.003 1.00 18.03 ? 7   SER B N   1 
ATOM   1687 C CA  . SER B 2 7   ? -39.963 -48.362 26.233 1.00 19.98 ? 7   SER B CA  1 
ATOM   1688 C C   . SER B 2 7   ? -38.995 -47.869 27.320 1.00 30.81 ? 7   SER B C   1 
ATOM   1689 O O   . SER B 2 7   ? -37.935 -47.293 27.022 1.00 26.73 ? 7   SER B O   1 
ATOM   1690 C CB  . SER B 2 7   ? -39.792 -49.860 25.987 1.00 21.07 ? 7   SER B CB  1 
ATOM   1691 O OG  . SER B 2 7   ? -38.681 -50.130 25.155 1.00 28.65 ? 7   SER B OG  1 
ATOM   1692 N N   . GLY B 2 8   ? -39.368 -48.100 28.577 1.00 29.22 ? 8   GLY B N   1 
ATOM   1693 C CA  . GLY B 2 8   ? -38.637 -47.580 29.724 1.00 19.32 ? 8   GLY B CA  1 
ATOM   1694 C C   . GLY B 2 8   ? -37.213 -48.059 29.977 1.00 20.35 ? 8   GLY B C   1 
ATOM   1695 O O   . GLY B 2 8   ? -36.756 -49.074 29.451 1.00 21.71 ? 8   GLY B O   1 
ATOM   1696 N N   . PRO B 2 9   ? -36.509 -47.336 30.847 1.00 21.23 ? 9   PRO B N   1 
ATOM   1697 C CA  . PRO B 2 9   ? -35.081 -47.540 31.076 1.00 21.90 ? 9   PRO B CA  1 
ATOM   1698 C C   . PRO B 2 9   ? -34.851 -48.763 31.942 1.00 32.27 ? 9   PRO B C   1 
ATOM   1699 O O   . PRO B 2 9   ? -35.781 -49.248 32.606 1.00 31.86 ? 9   PRO B O   1 
ATOM   1700 C CB  . PRO B 2 9   ? -34.688 -46.283 31.842 1.00 24.54 ? 9   PRO B CB  1 
ATOM   1701 C CG  . PRO B 2 9   ? -35.939 -45.943 32.640 1.00 20.98 ? 9   PRO B CG  1 
ATOM   1702 C CD  . PRO B 2 9   ? -37.110 -46.429 31.844 1.00 24.76 ? 9   PRO B CD  1 
ATOM   1703 N N   . GLY B 2 10  ? -33.624 -49.263 31.941 1.00 28.12 ? 10  GLY B N   1 
ATOM   1704 C CA  . GLY B 2 10  ? -33.329 -50.411 32.763 1.00 27.08 ? 10  GLY B CA  1 
ATOM   1705 C C   . GLY B 2 10  ? -31.946 -50.994 32.619 1.00 29.04 ? 10  GLY B C   1 
ATOM   1706 O O   . GLY B 2 10  ? -31.097 -50.522 31.850 1.00 28.16 ? 10  GLY B O   1 
ATOM   1707 N N   . LEU B 2 11  ? -31.757 -52.069 33.367 1.00 25.93 ? 11  LEU B N   1 
ATOM   1708 C CA  . LEU B 2 11  ? -30.485 -52.715 33.522 1.00 25.97 ? 11  LEU B CA  1 
ATOM   1709 C C   . LEU B 2 11  ? -30.323 -53.809 32.465 1.00 29.55 ? 11  LEU B C   1 
ATOM   1710 O O   . LEU B 2 11  ? -31.280 -54.475 32.095 1.00 30.99 ? 11  LEU B O   1 
ATOM   1711 C CB  . LEU B 2 11  ? -30.436 -53.313 34.923 1.00 19.37 ? 11  LEU B CB  1 
ATOM   1712 C CG  . LEU B 2 11  ? -29.082 -53.600 35.544 1.00 33.13 ? 11  LEU B CG  1 
ATOM   1713 C CD1 . LEU B 2 11  ? -28.192 -52.402 35.362 1.00 31.90 ? 11  LEU B CD1 1 
ATOM   1714 C CD2 . LEU B 2 11  ? -29.264 -53.921 37.022 1.00 28.05 ? 11  LEU B CD2 1 
ATOM   1715 N N   . VAL B 2 12  ? -29.103 -53.973 31.972 1.00 28.88 ? 12  VAL B N   1 
ATOM   1716 C CA  . VAL B 2 12  ? -28.748 -55.106 31.136 1.00 25.54 ? 12  VAL B CA  1 
ATOM   1717 C C   . VAL B 2 12  ? -27.459 -55.695 31.698 1.00 31.35 ? 12  VAL B C   1 
ATOM   1718 O O   . VAL B 2 12  ? -26.471 -54.975 31.865 1.00 27.56 ? 12  VAL B O   1 
ATOM   1719 C CB  . VAL B 2 12  ? -28.521 -54.682 29.664 1.00 29.93 ? 12  VAL B CB  1 
ATOM   1720 C CG1 . VAL B 2 12  ? -27.922 -55.823 28.849 1.00 31.89 ? 12  VAL B CG1 1 
ATOM   1721 C CG2 . VAL B 2 12  ? -29.815 -54.209 29.038 1.00 23.92 ? 12  VAL B CG2 1 
ATOM   1722 N N   . GLN B 2 13  ? -27.470 -56.993 32.002 1.00 34.18 ? 13  GLN B N   1 
ATOM   1723 C CA  . GLN B 2 13  ? -26.269 -57.664 32.500 1.00 35.72 ? 13  GLN B CA  1 
ATOM   1724 C C   . GLN B 2 13  ? -25.191 -57.656 31.416 1.00 37.26 ? 13  GLN B C   1 
ATOM   1725 O O   . GLN B 2 13  ? -25.497 -57.613 30.227 1.00 33.52 ? 13  GLN B O   1 
ATOM   1726 C CB  . GLN B 2 13  ? -26.569 -59.105 32.950 1.00 33.72 ? 13  GLN B CB  1 
ATOM   1727 C CG  . GLN B 2 13  ? -27.615 -59.254 34.065 1.00 36.39 ? 13  GLN B CG  1 
ATOM   1728 C CD  . GLN B 2 13  ? -27.277 -58.464 35.342 1.00 47.85 ? 13  GLN B CD  1 
ATOM   1729 O OE1 . GLN B 2 13  ? -28.126 -57.749 35.896 1.00 37.98 ? 13  GLN B OE1 1 
ATOM   1730 N NE2 . GLN B 2 13  ? -26.042 -58.601 35.814 1.00 42.99 ? 13  GLN B NE2 1 
ATOM   1731 N N   . PRO B 2 14  ? -23.919 -57.658 31.825 1.00 36.15 ? 14  PRO B N   1 
ATOM   1732 C CA  . PRO B 2 14  ? -22.827 -57.795 30.860 1.00 28.59 ? 14  PRO B CA  1 
ATOM   1733 C C   . PRO B 2 14  ? -23.015 -59.018 29.974 1.00 35.69 ? 14  PRO B C   1 
ATOM   1734 O O   . PRO B 2 14  ? -23.528 -60.040 30.437 1.00 39.33 ? 14  PRO B O   1 
ATOM   1735 C CB  . PRO B 2 14  ? -21.607 -57.951 31.755 1.00 32.17 ? 14  PRO B CB  1 
ATOM   1736 C CG  . PRO B 2 14  ? -21.953 -57.130 32.948 1.00 36.22 ? 14  PRO B CG  1 
ATOM   1737 C CD  . PRO B 2 14  ? -23.426 -57.333 33.171 1.00 28.10 ? 14  PRO B CD  1 
ATOM   1738 N N   . SER B 2 15  ? -22.633 -58.874 28.705 1.00 41.96 ? 15  SER B N   1 
ATOM   1739 C CA  . SER B 2 15  ? -22.776 -59.904 27.668 1.00 39.01 ? 15  SER B CA  1 
ATOM   1740 C C   . SER B 2 15  ? -24.219 -60.256 27.296 1.00 37.26 ? 15  SER B C   1 
ATOM   1741 O O   . SER B 2 15  ? -24.454 -61.255 26.624 1.00 45.11 ? 15  SER B O   1 
ATOM   1742 C CB  . SER B 2 15  ? -21.995 -61.172 28.022 1.00 39.67 ? 15  SER B CB  1 
ATOM   1743 O OG  . SER B 2 15  ? -22.785 -62.040 28.811 1.00 54.37 ? 15  SER B OG  1 
ATOM   1744 N N   . GLN B 2 16  ? -25.176 -59.433 27.713 1.00 41.35 ? 16  GLN B N   1 
ATOM   1745 C CA  . GLN B 2 16  ? -26.589 -59.662 27.392 1.00 34.13 ? 16  GLN B CA  1 
ATOM   1746 C C   . GLN B 2 16  ? -27.113 -58.715 26.318 1.00 33.74 ? 16  GLN B C   1 
ATOM   1747 O O   . GLN B 2 16  ? -26.405 -57.813 25.870 1.00 44.04 ? 16  GLN B O   1 
ATOM   1748 C CB  . GLN B 2 16  ? -27.445 -59.510 28.640 1.00 43.29 ? 16  GLN B CB  1 
ATOM   1749 C CG  . GLN B 2 16  ? -27.146 -60.535 29.702 1.00 46.27 ? 16  GLN B CG  1 
ATOM   1750 C CD  . GLN B 2 16  ? -27.912 -61.815 29.477 1.00 57.85 ? 16  GLN B CD  1 
ATOM   1751 O OE1 . GLN B 2 16  ? -27.633 -62.566 28.540 1.00 57.53 ? 16  GLN B OE1 1 
ATOM   1752 N NE2 . GLN B 2 16  ? -28.897 -62.072 30.335 1.00 61.76 ? 16  GLN B NE2 1 
ATOM   1753 N N   . SER B 2 17  ? -28.366 -58.911 25.916 1.00 33.62 ? 17  SER B N   1 
ATOM   1754 C CA  . SER B 2 17  ? -28.938 -58.150 24.808 1.00 35.93 ? 17  SER B CA  1 
ATOM   1755 C C   . SER B 2 17  ? -29.884 -57.028 25.226 1.00 36.54 ? 17  SER B C   1 
ATOM   1756 O O   . SER B 2 17  ? -30.604 -57.134 26.214 1.00 34.76 ? 17  SER B O   1 
ATOM   1757 C CB  . SER B 2 17  ? -29.641 -59.078 23.820 1.00 34.09 ? 17  SER B CB  1 
ATOM   1758 O OG  . SER B 2 17  ? -30.588 -59.887 24.487 1.00 48.97 ? 17  SER B OG  1 
ATOM   1759 N N   . LEU B 2 18  ? -29.874 -55.955 24.442 1.00 36.26 ? 18  LEU B N   1 
ATOM   1760 C CA  . LEU B 2 18  ? -30.726 -54.810 24.680 1.00 23.38 ? 18  LEU B CA  1 
ATOM   1761 C C   . LEU B 2 18  ? -31.941 -54.889 23.759 1.00 25.98 ? 18  LEU B C   1 
ATOM   1762 O O   . LEU B 2 18  ? -31.796 -55.151 22.579 1.00 29.24 ? 18  LEU B O   1 
ATOM   1763 C CB  . LEU B 2 18  ? -29.933 -53.524 24.432 1.00 23.04 ? 18  LEU B CB  1 
ATOM   1764 C CG  . LEU B 2 18  ? -30.689 -52.203 24.591 1.00 26.92 ? 18  LEU B CG  1 
ATOM   1765 C CD1 . LEU B 2 18  ? -31.422 -52.169 25.922 1.00 18.86 ? 18  LEU B CD1 1 
ATOM   1766 C CD2 . LEU B 2 18  ? -29.743 -51.026 24.480 1.00 19.10 ? 18  LEU B CD2 1 
ATOM   1767 N N   . SER B 2 19  ? -33.138 -54.692 24.303 1.00 21.31 ? 19  SER B N   1 
ATOM   1768 C CA  . SER B 2 19  ? -34.332 -54.606 23.480 1.00 22.51 ? 19  SER B CA  1 
ATOM   1769 C C   . SER B 2 19  ? -35.087 -53.330 23.826 1.00 27.07 ? 19  SER B C   1 
ATOM   1770 O O   . SER B 2 19  ? -35.469 -53.122 24.980 1.00 23.49 ? 19  SER B O   1 
ATOM   1771 C CB  . SER B 2 19  ? -35.236 -55.822 23.677 1.00 27.94 ? 19  SER B CB  1 
ATOM   1772 O OG  . SER B 2 19  ? -34.670 -56.987 23.103 1.00 32.95 ? 19  SER B OG  1 
ATOM   1773 N N   . ILE B 2 20  ? -35.281 -52.471 22.828 1.00 21.78 ? 20  ILE B N   1 
ATOM   1774 C CA  . ILE B 2 20  ? -36.062 -51.256 22.996 1.00 19.45 ? 20  ILE B CA  1 
ATOM   1775 C C   . ILE B 2 20  ? -37.123 -51.154 21.922 1.00 24.64 ? 20  ILE B C   1 
ATOM   1776 O O   . ILE B 2 20  ? -36.864 -51.430 20.746 1.00 28.66 ? 20  ILE B O   1 
ATOM   1777 C CB  . ILE B 2 20  ? -35.176 -50.013 22.936 1.00 24.99 ? 20  ILE B CB  1 
ATOM   1778 C CG1 . ILE B 2 20  ? -34.038 -50.121 23.960 1.00 23.94 ? 20  ILE B CG1 1 
ATOM   1779 C CG2 . ILE B 2 20  ? -36.005 -48.749 23.151 1.00 17.25 ? 20  ILE B CG2 1 
ATOM   1780 C CD1 . ILE B 2 20  ? -33.024 -49.006 23.822 1.00 22.68 ? 20  ILE B CD1 1 
ATOM   1781 N N   . THR B 2 21  ? -38.329 -50.775 22.325 1.00 26.53 ? 21  THR B N   1 
ATOM   1782 C CA  . THR B 2 21  ? -39.423 -50.601 21.373 1.00 21.09 ? 21  THR B CA  1 
ATOM   1783 C C   . THR B 2 21  ? -39.717 -49.123 21.210 1.00 25.13 ? 21  THR B C   1 
ATOM   1784 O O   . THR B 2 21  ? -39.816 -48.392 22.202 1.00 24.38 ? 21  THR B O   1 
ATOM   1785 C CB  . THR B 2 21  ? -40.705 -51.335 21.816 1.00 24.15 ? 21  THR B CB  1 
ATOM   1786 O OG1 . THR B 2 21  ? -40.535 -52.740 21.614 1.00 23.52 ? 21  THR B OG1 1 
ATOM   1787 C CG2 . THR B 2 21  ? -41.932 -50.854 21.020 1.00 27.36 ? 21  THR B CG2 1 
ATOM   1788 N N   . CYS B 2 22  ? -39.836 -48.691 19.956 1.00 18.78 ? 22  CYS B N   1 
ATOM   1789 C CA  . CYS B 2 22  ? -40.220 -47.324 19.622 1.00 21.30 ? 22  CYS B CA  1 
ATOM   1790 C C   . CYS B 2 22  ? -41.620 -47.383 19.033 1.00 26.56 ? 22  CYS B C   1 
ATOM   1791 O O   . CYS B 2 22  ? -41.858 -48.066 18.030 1.00 23.34 ? 22  CYS B O   1 
ATOM   1792 C CB  . CYS B 2 22  ? -39.243 -46.732 18.589 1.00 26.57 ? 22  CYS B CB  1 
ATOM   1793 S SG  . CYS B 2 22  ? -39.442 -44.958 18.216 1.00 28.69 ? 22  CYS B SG  1 
ATOM   1794 N N   . THR B 2 23  ? -42.555 -46.690 19.670 1.00 26.86 ? 23  THR B N   1 
ATOM   1795 C CA  . THR B 2 23  ? -43.917 -46.629 19.153 1.00 25.99 ? 23  THR B CA  1 
ATOM   1796 C C   . THR B 2 23  ? -44.185 -45.235 18.621 1.00 25.67 ? 23  THR B C   1 
ATOM   1797 O O   . THR B 2 23  ? -44.161 -44.258 19.371 1.00 31.41 ? 23  THR B O   1 
ATOM   1798 C CB  . THR B 2 23  ? -44.973 -46.981 20.209 1.00 25.96 ? 23  THR B CB  1 
ATOM   1799 O OG1 . THR B 2 23  ? -44.754 -48.316 20.694 1.00 27.83 ? 23  THR B OG1 1 
ATOM   1800 C CG2 . THR B 2 23  ? -46.370 -46.888 19.595 1.00 21.96 ? 23  THR B CG2 1 
ATOM   1801 N N   . VAL B 2 24  ? -44.429 -45.145 17.321 1.00 21.94 ? 24  VAL B N   1 
ATOM   1802 C CA  . VAL B 2 24  ? -44.582 -43.858 16.681 1.00 24.86 ? 24  VAL B CA  1 
ATOM   1803 C C   . VAL B 2 24  ? -46.045 -43.577 16.416 1.00 26.05 ? 24  VAL B C   1 
ATOM   1804 O O   . VAL B 2 24  ? -46.849 -44.501 16.276 1.00 25.53 ? 24  VAL B O   1 
ATOM   1805 C CB  . VAL B 2 24  ? -43.815 -43.802 15.342 1.00 30.56 ? 24  VAL B CB  1 
ATOM   1806 C CG1 . VAL B 2 24  ? -42.388 -44.316 15.522 1.00 22.58 ? 24  VAL B CG1 1 
ATOM   1807 C CG2 . VAL B 2 24  ? -44.557 -44.586 14.246 1.00 21.14 ? 24  VAL B CG2 1 
ATOM   1808 N N   . SER B 2 25  ? -46.384 -42.292 16.359 1.00 22.26 ? 25  SER B N   1 
ATOM   1809 C CA  . SER B 2 25  ? -47.726 -41.862 15.998 1.00 18.44 ? 25  SER B CA  1 
ATOM   1810 C C   . SER B 2 25  ? -47.635 -40.478 15.358 1.00 25.35 ? 25  SER B C   1 
ATOM   1811 O O   . SER B 2 25  ? -46.658 -39.757 15.569 1.00 32.08 ? 25  SER B O   1 
ATOM   1812 C CB  . SER B 2 25  ? -48.638 -41.840 17.218 1.00 15.26 ? 25  SER B CB  1 
ATOM   1813 O OG  . SER B 2 25  ? -48.192 -40.881 18.156 1.00 30.88 ? 25  SER B OG  1 
ATOM   1814 N N   . GLY B 2 26  ? -48.641 -40.118 14.567 1.00 23.25 ? 26  GLY B N   1 
ATOM   1815 C CA  . GLY B 2 26  ? -48.610 -38.885 13.800 1.00 26.45 ? 26  GLY B CA  1 
ATOM   1816 C C   . GLY B 2 26  ? -48.030 -39.090 12.406 1.00 28.12 ? 26  GLY B C   1 
ATOM   1817 O O   . GLY B 2 26  ? -47.932 -38.151 11.616 1.00 25.87 ? 26  GLY B O   1 
ATOM   1818 N N   . PHE B 2 27  ? -47.622 -40.321 12.113 1.00 18.92 ? 27  PHE B N   1 
ATOM   1819 C CA  . PHE B 2 27  ? -47.132 -40.678 10.784 1.00 22.89 ? 27  PHE B CA  1 
ATOM   1820 C C   . PHE B 2 27  ? -47.091 -42.196 10.624 1.00 21.63 ? 27  PHE B C   1 
ATOM   1821 O O   . PHE B 2 27  ? -47.347 -42.941 11.563 1.00 26.23 ? 27  PHE B O   1 
ATOM   1822 C CB  . PHE B 2 27  ? -45.757 -40.044 10.485 1.00 20.77 ? 27  PHE B CB  1 
ATOM   1823 C CG  . PHE B 2 27  ? -44.631 -40.575 11.335 1.00 27.15 ? 27  PHE B CG  1 
ATOM   1824 C CD1 . PHE B 2 27  ? -44.422 -40.083 12.628 1.00 28.80 ? 27  PHE B CD1 1 
ATOM   1825 C CD2 . PHE B 2 27  ? -43.779 -41.566 10.846 1.00 24.18 ? 27  PHE B CD2 1 
ATOM   1826 C CE1 . PHE B 2 27  ? -43.386 -40.566 13.417 1.00 23.52 ? 27  PHE B CE1 1 
ATOM   1827 C CE2 . PHE B 2 27  ? -42.740 -42.058 11.622 1.00 24.13 ? 27  PHE B CE2 1 
ATOM   1828 C CZ  . PHE B 2 27  ? -42.537 -41.557 12.914 1.00 23.01 ? 27  PHE B CZ  1 
ATOM   1829 N N   . SER B 2 28  ? -46.758 -42.652 9.431  1.00 28.52 ? 28  SER B N   1 
ATOM   1830 C CA  . SER B 2 28  ? -46.796 -44.071 9.128  1.00 28.62 ? 28  SER B CA  1 
ATOM   1831 C C   . SER B 2 28  ? -45.390 -44.579 8.814  1.00 29.05 ? 28  SER B C   1 
ATOM   1832 O O   . SER B 2 28  ? -44.625 -43.932 8.091  1.00 27.58 ? 28  SER B O   1 
ATOM   1833 C CB  . SER B 2 28  ? -47.753 -44.336 7.960  1.00 17.60 ? 28  SER B CB  1 
ATOM   1834 O OG  . SER B 2 28  ? -47.578 -45.644 7.452  1.00 25.65 ? 28  SER B OG  1 
ATOM   1835 N N   . LEU B 2 29  ? -45.056 -45.740 9.360  1.00 23.62 ? 29  LEU B N   1 
ATOM   1836 C CA  . LEU B 2 29  ? -43.740 -46.328 9.150  1.00 27.64 ? 29  LEU B CA  1 
ATOM   1837 C C   . LEU B 2 29  ? -43.565 -46.761 7.708  1.00 28.26 ? 29  LEU B C   1 
ATOM   1838 O O   . LEU B 2 29  ? -42.455 -47.073 7.282  1.00 29.55 ? 29  LEU B O   1 
ATOM   1839 C CB  . LEU B 2 29  ? -43.518 -47.516 10.092 1.00 21.54 ? 29  LEU B CB  1 
ATOM   1840 C CG  . LEU B 2 29  ? -43.434 -47.143 11.579 1.00 28.42 ? 29  LEU B CG  1 
ATOM   1841 C CD1 . LEU B 2 29  ? -43.407 -48.377 12.470 1.00 30.78 ? 29  LEU B CD1 1 
ATOM   1842 C CD2 . LEU B 2 29  ? -42.227 -46.278 11.849 1.00 17.71 ? 29  LEU B CD2 1 
ATOM   1843 N N   . THR B 2 30  ? -44.661 -46.786 6.957  1.00 27.38 ? 30  THR B N   1 
ATOM   1844 C CA  . THR B 2 30  ? -44.590 -47.116 5.538  1.00 33.02 ? 30  THR B CA  1 
ATOM   1845 C C   . THR B 2 30  ? -44.071 -45.934 4.727  1.00 26.83 ? 30  THR B C   1 
ATOM   1846 O O   . THR B 2 30  ? -43.557 -46.128 3.633  1.00 26.57 ? 30  THR B O   1 
ATOM   1847 C CB  . THR B 2 30  ? -45.944 -47.558 4.980  1.00 32.92 ? 30  THR B CB  1 
ATOM   1848 O OG1 . THR B 2 30  ? -46.874 -46.469 5.078  1.00 35.96 ? 30  THR B OG1 1 
ATOM   1849 C CG2 . THR B 2 30  ? -46.461 -48.764 5.758  1.00 31.79 ? 30  THR B CG2 1 
ATOM   1850 N N   . ASN B 2 31  ? -44.185 -44.725 5.285  1.00 26.91 ? 31  ASN B N   1 
ATOM   1851 C CA  . ASN B 2 31  ? -43.687 -43.503 4.636  1.00 34.20 ? 31  ASN B CA  1 
ATOM   1852 C C   . ASN B 2 31  ? -42.399 -42.934 5.219  1.00 28.05 ? 31  ASN B C   1 
ATOM   1853 O O   . ASN B 2 31  ? -41.805 -42.035 4.634  1.00 30.29 ? 31  ASN B O   1 
ATOM   1854 C CB  . ASN B 2 31  ? -44.736 -42.392 4.669  1.00 29.79 ? 31  ASN B CB  1 
ATOM   1855 C CG  . ASN B 2 31  ? -46.030 -42.803 4.026  1.00 33.68 ? 31  ASN B CG  1 
ATOM   1856 O OD1 . ASN B 2 31  ? -46.033 -43.476 2.994  1.00 42.46 ? 31  ASN B OD1 1 
ATOM   1857 N ND2 . ASN B 2 31  ? -47.142 -42.415 4.635  1.00 27.04 ? 31  ASN B ND2 1 
ATOM   1858 N N   . TYR B 2 32  ? -41.975 -43.413 6.382  1.00 25.90 ? 32  TYR B N   1 
ATOM   1859 C CA  . TYR B 2 32  ? -40.757 -42.869 6.978  1.00 22.60 ? 32  TYR B CA  1 
ATOM   1860 C C   . TYR B 2 32  ? -39.810 -43.911 7.527  1.00 27.32 ? 32  TYR B C   1 
ATOM   1861 O O   . TYR B 2 32  ? -40.228 -44.971 8.002  1.00 29.93 ? 32  TYR B O   1 
ATOM   1862 C CB  . TYR B 2 32  ? -41.080 -41.856 8.073  1.00 22.05 ? 32  TYR B CB  1 
ATOM   1863 C CG  . TYR B 2 32  ? -41.672 -40.582 7.557  1.00 26.05 ? 32  TYR B CG  1 
ATOM   1864 C CD1 . TYR B 2 32  ? -40.860 -39.505 7.231  1.00 24.41 ? 32  TYR B CD1 1 
ATOM   1865 C CD2 . TYR B 2 32  ? -43.047 -40.454 7.387  1.00 29.37 ? 32  TYR B CD2 1 
ATOM   1866 C CE1 . TYR B 2 32  ? -41.403 -38.324 6.750  1.00 31.33 ? 32  TYR B CE1 1 
ATOM   1867 C CE2 . TYR B 2 32  ? -43.601 -39.279 6.911  1.00 28.72 ? 32  TYR B CE2 1 
ATOM   1868 C CZ  . TYR B 2 32  ? -42.775 -38.219 6.591  1.00 32.95 ? 32  TYR B CZ  1 
ATOM   1869 O OH  . TYR B 2 32  ? -43.317 -37.052 6.107  1.00 42.89 ? 32  TYR B OH  1 
ATOM   1870 N N   . GLY B 2 33  ? -38.522 -43.589 7.461  1.00 35.60 ? 33  GLY B N   1 
ATOM   1871 C CA  . GLY B 2 33  ? -37.501 -44.379 8.119  1.00 28.73 ? 33  GLY B CA  1 
ATOM   1872 C C   . GLY B 2 33  ? -37.391 -43.964 9.572  1.00 25.50 ? 33  GLY B C   1 
ATOM   1873 O O   . GLY B 2 33  ? -37.674 -42.814 9.931  1.00 19.53 ? 33  GLY B O   1 
ATOM   1874 N N   . VAL B 2 34  ? -36.987 -44.906 10.415 1.00 22.97 ? 34  VAL B N   1 
ATOM   1875 C CA  . VAL B 2 34  ? -36.781 -44.614 11.831 1.00 25.07 ? 34  VAL B CA  1 
ATOM   1876 C C   . VAL B 2 34  ? -35.337 -44.912 12.203 1.00 23.73 ? 34  VAL B C   1 
ATOM   1877 O O   . VAL B 2 34  ? -34.833 -46.015 11.943 1.00 22.61 ? 34  VAL B O   1 
ATOM   1878 C CB  . VAL B 2 34  ? -37.784 -45.373 12.722 1.00 23.31 ? 34  VAL B CB  1 
ATOM   1879 C CG1 . VAL B 2 34  ? -37.347 -45.333 14.179 1.00 20.49 ? 34  VAL B CG1 1 
ATOM   1880 C CG2 . VAL B 2 34  ? -39.168 -44.778 12.556 1.00 15.37 ? 34  VAL B CG2 1 
ATOM   1881 N N   . HIS B 2 35  ? -34.666 -43.908 12.770 1.00 18.83 ? 35  HIS B N   1 
ATOM   1882 C CA  . HIS B 2 35  ? -33.237 -44.010 13.060 1.00 23.32 ? 35  HIS B CA  1 
ATOM   1883 C C   . HIS B 2 35  ? -32.988 -44.279 14.533 1.00 24.87 ? 35  HIS B C   1 
ATOM   1884 O O   . HIS B 2 35  ? -33.817 -43.943 15.381 1.00 22.32 ? 35  HIS B O   1 
ATOM   1885 C CB  . HIS B 2 35  ? -32.508 -42.713 12.695 1.00 23.65 ? 35  HIS B CB  1 
ATOM   1886 C CG  . HIS B 2 35  ? -32.532 -42.379 11.239 1.00 22.97 ? 35  HIS B CG  1 
ATOM   1887 N ND1 . HIS B 2 35  ? -31.449 -42.591 10.413 1.00 16.00 ? 35  HIS B ND1 1 
ATOM   1888 C CD2 . HIS B 2 35  ? -33.495 -41.816 10.465 1.00 18.41 ? 35  HIS B CD2 1 
ATOM   1889 C CE1 . HIS B 2 35  ? -31.750 -42.189 9.188  1.00 26.66 ? 35  HIS B CE1 1 
ATOM   1890 N NE2 . HIS B 2 35  ? -32.984 -41.711 9.196  1.00 22.31 ? 35  HIS B NE2 1 
ATOM   1891 N N   . TRP B 2 36  ? -31.826 -44.853 14.833 1.00 24.30 ? 36  TRP B N   1 
ATOM   1892 C CA  . TRP B 2 36  ? -31.399 -45.043 16.214 1.00 15.86 ? 36  TRP B CA  1 
ATOM   1893 C C   . TRP B 2 36  ? -30.048 -44.370 16.454 1.00 22.06 ? 36  TRP B C   1 
ATOM   1894 O O   . TRP B 2 36  ? -29.083 -44.558 15.695 1.00 22.90 ? 36  TRP B O   1 
ATOM   1895 C CB  . TRP B 2 36  ? -31.341 -46.528 16.558 1.00 19.25 ? 36  TRP B CB  1 
ATOM   1896 C CG  . TRP B 2 36  ? -32.691 -47.132 16.541 1.00 24.01 ? 36  TRP B CG  1 
ATOM   1897 C CD1 . TRP B 2 36  ? -33.368 -47.596 15.452 1.00 23.50 ? 36  TRP B CD1 1 
ATOM   1898 C CD2 . TRP B 2 36  ? -33.568 -47.304 17.661 1.00 24.37 ? 36  TRP B CD2 1 
ATOM   1899 N NE1 . TRP B 2 36  ? -34.605 -48.061 15.825 1.00 27.52 ? 36  TRP B NE1 1 
ATOM   1900 C CE2 . TRP B 2 36  ? -34.750 -47.892 17.178 1.00 26.99 ? 36  TRP B CE2 1 
ATOM   1901 C CE3 . TRP B 2 36  ? -33.463 -47.029 19.019 1.00 20.46 ? 36  TRP B CE3 1 
ATOM   1902 C CZ2 . TRP B 2 36  ? -35.817 -48.206 18.011 1.00 26.46 ? 36  TRP B CZ2 1 
ATOM   1903 C CZ3 . TRP B 2 36  ? -34.521 -47.335 19.841 1.00 24.96 ? 36  TRP B CZ3 1 
ATOM   1904 C CH2 . TRP B 2 36  ? -35.681 -47.922 19.339 1.00 25.36 ? 36  TRP B CH2 1 
ATOM   1905 N N   . VAL B 2 37  ? -30.008 -43.565 17.509 1.00 20.98 ? 37  VAL B N   1 
ATOM   1906 C CA  . VAL B 2 37  ? -28.835 -42.804 17.910 1.00 19.76 ? 37  VAL B CA  1 
ATOM   1907 C C   . VAL B 2 37  ? -28.699 -43.022 19.400 1.00 21.58 ? 37  VAL B C   1 
ATOM   1908 O O   . VAL B 2 37  ? -29.702 -43.053 20.113 1.00 25.83 ? 37  VAL B O   1 
ATOM   1909 C CB  . VAL B 2 37  ? -29.056 -41.275 17.682 1.00 20.10 ? 37  VAL B CB  1 
ATOM   1910 C CG1 . VAL B 2 37  ? -27.858 -40.459 18.177 1.00 18.23 ? 37  VAL B CG1 1 
ATOM   1911 C CG2 . VAL B 2 37  ? -29.368 -40.972 16.229 1.00 14.10 ? 37  VAL B CG2 1 
ATOM   1912 N N   . ARG B 2 38  ? -27.478 -43.173 19.888 1.00 15.33 ? 38  ARG B N   1 
ATOM   1913 C CA  . ARG B 2 38  ? -27.286 -43.244 21.323 1.00 16.95 ? 38  ARG B CA  1 
ATOM   1914 C C   . ARG B 2 38  ? -26.378 -42.128 21.804 1.00 23.61 ? 38  ARG B C   1 
ATOM   1915 O O   . ARG B 2 38  ? -25.715 -41.456 21.007 1.00 20.55 ? 38  ARG B O   1 
ATOM   1916 C CB  . ARG B 2 38  ? -26.736 -44.606 21.751 1.00 19.98 ? 38  ARG B CB  1 
ATOM   1917 C CG  . ARG B 2 38  ? -25.280 -44.836 21.368 1.00 20.55 ? 38  ARG B CG  1 
ATOM   1918 C CD  . ARG B 2 38  ? -24.792 -46.120 21.959 1.00 19.05 ? 38  ARG B CD  1 
ATOM   1919 N NE  . ARG B 2 38  ? -23.423 -46.413 21.562 1.00 29.12 ? 38  ARG B NE  1 
ATOM   1920 C CZ  . ARG B 2 38  ? -22.768 -47.503 21.944 1.00 29.56 ? 38  ARG B CZ  1 
ATOM   1921 N NH1 . ARG B 2 38  ? -23.374 -48.378 22.732 1.00 28.84 ? 38  ARG B NH1 1 
ATOM   1922 N NH2 . ARG B 2 38  ? -21.522 -47.716 21.544 1.00 25.66 ? 38  ARG B NH2 1 
ATOM   1923 N N   . GLN B 2 39  ? -26.346 -41.947 23.117 1.00 22.43 ? 39  GLN B N   1 
ATOM   1924 C CA  . GLN B 2 39  ? -25.521 -40.913 23.717 1.00 22.86 ? 39  GLN B CA  1 
ATOM   1925 C C   . GLN B 2 39  ? -24.776 -41.513 24.893 1.00 23.19 ? 39  GLN B C   1 
ATOM   1926 O O   . GLN B 2 39  ? -25.382 -41.815 25.919 1.00 23.81 ? 39  GLN B O   1 
ATOM   1927 C CB  . GLN B 2 39  ? -26.401 -39.754 24.177 1.00 19.56 ? 39  GLN B CB  1 
ATOM   1928 C CG  . GLN B 2 39  ? -25.642 -38.486 24.492 1.00 23.53 ? 39  GLN B CG  1 
ATOM   1929 C CD  . GLN B 2 39  ? -26.560 -37.294 24.737 1.00 30.34 ? 39  GLN B CD  1 
ATOM   1930 O OE1 . GLN B 2 39  ? -27.684 -37.443 25.237 1.00 27.98 ? 39  GLN B OE1 1 
ATOM   1931 N NE2 . GLN B 2 39  ? -26.081 -36.097 24.383 1.00 23.98 ? 39  GLN B NE2 1 
ATOM   1932 N N   . SER B 2 40  ? -23.467 -41.699 24.742 1.00 23.08 ? 40  SER B N   1 
ATOM   1933 C CA  . SER B 2 40  ? -22.666 -42.362 25.772 1.00 19.08 ? 40  SER B CA  1 
ATOM   1934 C C   . SER B 2 40  ? -21.728 -41.370 26.428 1.00 29.23 ? 40  SER B C   1 
ATOM   1935 O O   . SER B 2 40  ? -21.411 -40.336 25.836 1.00 36.24 ? 40  SER B O   1 
ATOM   1936 C CB  . SER B 2 40  ? -21.862 -43.522 25.181 1.00 19.27 ? 40  SER B CB  1 
ATOM   1937 O OG  . SER B 2 40  ? -20.775 -43.046 24.415 1.00 29.63 ? 40  SER B OG  1 
ATOM   1938 N N   . PRO B 2 41  ? -21.293 -41.669 27.664 1.00 26.60 ? 41  PRO B N   1 
ATOM   1939 C CA  . PRO B 2 41  ? -20.363 -40.795 28.380 1.00 34.06 ? 41  PRO B CA  1 
ATOM   1940 C C   . PRO B 2 41  ? -19.072 -40.517 27.605 1.00 35.97 ? 41  PRO B C   1 
ATOM   1941 O O   . PRO B 2 41  ? -18.607 -39.375 27.592 1.00 39.43 ? 41  PRO B O   1 
ATOM   1942 C CB  . PRO B 2 41  ? -20.075 -41.591 29.656 1.00 22.97 ? 41  PRO B CB  1 
ATOM   1943 C CG  . PRO B 2 41  ? -21.323 -42.313 29.899 1.00 20.67 ? 41  PRO B CG  1 
ATOM   1944 C CD  . PRO B 2 41  ? -21.848 -42.703 28.557 1.00 25.48 ? 41  PRO B CD  1 
ATOM   1945 N N   . GLY B 2 42  ? -18.513 -41.545 26.974 1.00 26.46 ? 42  GLY B N   1 
ATOM   1946 C CA  . GLY B 2 42  ? -17.253 -41.411 26.275 1.00 36.12 ? 42  GLY B CA  1 
ATOM   1947 C C   . GLY B 2 42  ? -17.407 -40.897 24.857 1.00 43.57 ? 42  GLY B C   1 
ATOM   1948 O O   . GLY B 2 42  ? -16.939 -39.804 24.543 1.00 51.33 ? 42  GLY B O   1 
ATOM   1949 N N   . LYS B 2 43  ? -18.075 -41.674 24.008 1.00 46.25 ? 43  LYS B N   1 
ATOM   1950 C CA  . LYS B 2 43  ? -18.227 -41.323 22.595 1.00 43.30 ? 43  LYS B CA  1 
ATOM   1951 C C   . LYS B 2 43  ? -19.211 -40.190 22.269 1.00 36.52 ? 43  LYS B C   1 
ATOM   1952 O O   . LYS B 2 43  ? -19.136 -39.609 21.188 1.00 47.38 ? 43  LYS B O   1 
ATOM   1953 C CB  . LYS B 2 43  ? -18.556 -42.570 21.767 1.00 42.75 ? 43  LYS B CB  1 
ATOM   1954 C CG  . LYS B 2 43  ? -17.393 -43.531 21.616 1.00 47.43 ? 43  LYS B CG  1 
ATOM   1955 C CD  . LYS B 2 43  ? -17.344 -44.116 20.206 1.00 56.84 ? 43  LYS B CD  1 
ATOM   1956 C CE  . LYS B 2 43  ? -16.142 -45.028 20.024 1.00 54.93 ? 43  LYS B CE  1 
ATOM   1957 N NZ  . LYS B 2 43  ? -16.220 -45.831 18.770 1.00 56.79 ? 43  LYS B NZ  1 
ATOM   1958 N N   . GLY B 2 44  ? -20.124 -39.876 23.183 1.00 31.87 ? 44  GLY B N   1 
ATOM   1959 C CA  . GLY B 2 44  ? -21.122 -38.856 22.910 1.00 25.52 ? 44  GLY B CA  1 
ATOM   1960 C C   . GLY B 2 44  ? -22.190 -39.381 21.964 1.00 25.20 ? 44  GLY B C   1 
ATOM   1961 O O   . GLY B 2 44  ? -22.544 -40.560 22.033 1.00 24.06 ? 44  GLY B O   1 
ATOM   1962 N N   . LEU B 2 45  ? -22.695 -38.519 21.078 1.00 20.55 ? 45  LEU B N   1 
ATOM   1963 C CA  . LEU B 2 45  ? -23.722 -38.915 20.110 1.00 19.16 ? 45  LEU B CA  1 
ATOM   1964 C C   . LEU B 2 45  ? -23.146 -39.756 18.973 1.00 19.74 ? 45  LEU B C   1 
ATOM   1965 O O   . LEU B 2 45  ? -22.122 -39.423 18.369 1.00 22.78 ? 45  LEU B O   1 
ATOM   1966 C CB  . LEU B 2 45  ? -24.445 -37.699 19.530 1.00 19.94 ? 45  LEU B CB  1 
ATOM   1967 C CG  . LEU B 2 45  ? -25.309 -36.872 20.485 1.00 19.98 ? 45  LEU B CG  1 
ATOM   1968 C CD1 . LEU B 2 45  ? -25.502 -35.473 19.934 1.00 16.96 ? 45  LEU B CD1 1 
ATOM   1969 C CD2 . LEU B 2 45  ? -26.646 -37.537 20.736 1.00 17.41 ? 45  LEU B CD2 1 
ATOM   1970 N N   . GLU B 2 46  ? -23.843 -40.833 18.668 1.00 21.37 ? 46  GLU B N   1 
ATOM   1971 C CA  . GLU B 2 46  ? -23.327 -41.848 17.792 1.00 19.91 ? 46  GLU B CA  1 
ATOM   1972 C C   . GLU B 2 46  ? -24.532 -42.442 17.086 1.00 20.56 ? 46  GLU B C   1 
ATOM   1973 O O   . GLU B 2 46  ? -25.448 -42.939 17.739 1.00 24.25 ? 46  GLU B O   1 
ATOM   1974 C CB  . GLU B 2 46  ? -22.636 -42.897 18.656 1.00 18.95 ? 46  GLU B CB  1 
ATOM   1975 C CG  . GLU B 2 46  ? -21.949 -44.019 17.933 1.00 21.35 ? 46  GLU B CG  1 
ATOM   1976 C CD  . GLU B 2 46  ? -21.173 -44.906 18.901 1.00 37.30 ? 46  GLU B CD  1 
ATOM   1977 O OE1 . GLU B 2 46  ? -21.526 -44.942 20.107 1.00 33.65 ? 46  GLU B OE1 1 
ATOM   1978 O OE2 . GLU B 2 46  ? -20.203 -45.559 18.461 1.00 43.64 ? 46  GLU B OE2 1 
ATOM   1979 N N   . TRP B 2 47  ? -24.559 -42.358 15.759 1.00 20.65 ? 47  TRP B N   1 
ATOM   1980 C CA  . TRP B 2 47  ? -25.650 -42.936 14.994 1.00 19.91 ? 47  TRP B CA  1 
ATOM   1981 C C   . TRP B 2 47  ? -25.432 -44.439 14.897 1.00 19.18 ? 47  TRP B C   1 
ATOM   1982 O O   . TRP B 2 47  ? -24.336 -44.883 14.586 1.00 25.78 ? 47  TRP B O   1 
ATOM   1983 C CB  . TRP B 2 47  ? -25.687 -42.291 13.612 1.00 25.33 ? 47  TRP B CB  1 
ATOM   1984 C CG  . TRP B 2 47  ? -26.759 -42.772 12.668 1.00 19.80 ? 47  TRP B CG  1 
ATOM   1985 C CD1 . TRP B 2 47  ? -28.053 -42.343 12.606 1.00 18.78 ? 47  TRP B CD1 1 
ATOM   1986 C CD2 . TRP B 2 47  ? -26.602 -43.730 11.613 1.00 18.83 ? 47  TRP B CD2 1 
ATOM   1987 N NE1 . TRP B 2 47  ? -28.716 -42.990 11.591 1.00 19.70 ? 47  TRP B NE1 1 
ATOM   1988 C CE2 . TRP B 2 47  ? -27.849 -43.843 10.965 1.00 20.61 ? 47  TRP B CE2 1 
ATOM   1989 C CE3 . TRP B 2 47  ? -25.528 -44.509 11.160 1.00 21.79 ? 47  TRP B CE3 1 
ATOM   1990 C CZ2 . TRP B 2 47  ? -28.054 -44.703 9.880  1.00 24.84 ? 47  TRP B CZ2 1 
ATOM   1991 C CZ3 . TRP B 2 47  ? -25.728 -45.364 10.078 1.00 18.16 ? 47  TRP B CZ3 1 
ATOM   1992 C CH2 . TRP B 2 47  ? -26.988 -45.456 9.454  1.00 24.21 ? 47  TRP B CH2 1 
ATOM   1993 N N   . LEU B 2 48  ? -26.468 -45.222 15.170 1.00 18.07 ? 48  LEU B N   1 
ATOM   1994 C CA  . LEU B 2 48  ? -26.344 -46.676 15.157 1.00 20.59 ? 48  LEU B CA  1 
ATOM   1995 C C   . LEU B 2 48  ? -26.903 -47.344 13.881 1.00 24.03 ? 48  LEU B C   1 
ATOM   1996 O O   . LEU B 2 48  ? -26.323 -48.293 13.358 1.00 20.92 ? 48  LEU B O   1 
ATOM   1997 C CB  . LEU B 2 48  ? -27.009 -47.255 16.407 1.00 20.01 ? 48  LEU B CB  1 
ATOM   1998 C CG  . LEU B 2 48  ? -26.476 -46.709 17.741 1.00 23.65 ? 48  LEU B CG  1 
ATOM   1999 C CD1 . LEU B 2 48  ? -27.363 -47.108 18.921 1.00 18.95 ? 48  LEU B CD1 1 
ATOM   2000 C CD2 . LEU B 2 48  ? -25.046 -47.161 17.991 1.00 19.30 ? 48  LEU B CD2 1 
ATOM   2001 N N   . GLY B 2 49  ? -28.033 -46.854 13.386 1.00 29.04 ? 49  GLY B N   1 
ATOM   2002 C CA  . GLY B 2 49  ? -28.637 -47.413 12.187 1.00 23.20 ? 49  GLY B CA  1 
ATOM   2003 C C   . GLY B 2 49  ? -30.039 -46.898 11.936 1.00 22.78 ? 49  GLY B C   1 
ATOM   2004 O O   . GLY B 2 49  ? -30.500 -45.973 12.596 1.00 24.00 ? 49  GLY B O   1 
ATOM   2005 N N   . VAL B 2 50  ? -30.730 -47.525 10.993 1.00 28.10 ? 50  VAL B N   1 
ATOM   2006 C CA  . VAL B 2 50  ? -32.012 -47.034 10.512 1.00 19.40 ? 50  VAL B CA  1 
ATOM   2007 C C   . VAL B 2 50  ? -32.780 -48.183 9.876  1.00 18.34 ? 50  VAL B C   1 
ATOM   2008 O O   . VAL B 2 50  ? -32.199 -49.041 9.234  1.00 24.10 ? 50  VAL B O   1 
ATOM   2009 C CB  . VAL B 2 50  ? -31.797 -45.906 9.472  1.00 17.76 ? 50  VAL B CB  1 
ATOM   2010 C CG1 . VAL B 2 50  ? -30.745 -46.310 8.478  1.00 19.99 ? 50  VAL B CG1 1 
ATOM   2011 C CG2 . VAL B 2 50  ? -33.092 -45.544 8.755  1.00 19.53 ? 50  VAL B CG2 1 
ATOM   2012 N N   . ILE B 2 51  ? -34.083 -48.236 10.102 1.00 26.12 ? 51  ILE B N   1 
ATOM   2013 C CA  . ILE B 2 51  ? -34.927 -49.109 9.313  1.00 21.84 ? 51  ILE B CA  1 
ATOM   2014 C C   . ILE B 2 51  ? -35.775 -48.237 8.402  1.00 25.99 ? 51  ILE B C   1 
ATOM   2015 O O   . ILE B 2 51  ? -36.445 -47.305 8.863  1.00 25.14 ? 51  ILE B O   1 
ATOM   2016 C CB  . ILE B 2 51  ? -35.777 -50.067 10.164 1.00 23.28 ? 51  ILE B CB  1 
ATOM   2017 C CG1 . ILE B 2 51  ? -36.478 -51.083 9.255  1.00 23.07 ? 51  ILE B CG1 1 
ATOM   2018 C CG2 . ILE B 2 51  ? -36.762 -49.314 11.063 1.00 21.24 ? 51  ILE B CG2 1 
ATOM   2019 C CD1 . ILE B 2 51  ? -36.815 -52.400 9.948  1.00 18.04 ? 51  ILE B CD1 1 
ATOM   2020 N N   . TRP B 2 52  ? -35.693 -48.515 7.102  1.00 25.15 ? 52  TRP B N   1 
ATOM   2021 C CA  . TRP B 2 52  ? -36.335 -47.688 6.078  1.00 23.42 ? 52  TRP B CA  1 
ATOM   2022 C C   . TRP B 2 52  ? -37.783 -48.075 5.858  1.00 25.31 ? 52  TRP B C   1 
ATOM   2023 O O   . TRP B 2 52  ? -38.219 -49.160 6.242  1.00 24.57 ? 52  TRP B O   1 
ATOM   2024 C CB  . TRP B 2 52  ? -35.586 -47.799 4.746  1.00 24.16 ? 52  TRP B CB  1 
ATOM   2025 C CG  . TRP B 2 52  ? -34.205 -47.287 4.797  1.00 24.07 ? 52  TRP B CG  1 
ATOM   2026 C CD1 . TRP B 2 52  ? -33.054 -48.018 4.715  1.00 26.10 ? 52  TRP B CD1 1 
ATOM   2027 C CD2 . TRP B 2 52  ? -33.805 -45.926 4.976  1.00 26.11 ? 52  TRP B CD2 1 
ATOM   2028 N NE1 . TRP B 2 52  ? -31.965 -47.196 4.828  1.00 23.04 ? 52  TRP B NE1 1 
ATOM   2029 C CE2 . TRP B 2 52  ? -32.397 -45.903 4.974  1.00 26.07 ? 52  TRP B CE2 1 
ATOM   2030 C CE3 . TRP B 2 52  ? -34.501 -44.719 5.123  1.00 26.02 ? 52  TRP B CE3 1 
ATOM   2031 C CZ2 . TRP B 2 52  ? -31.668 -44.723 5.126  1.00 26.98 ? 52  TRP B CZ2 1 
ATOM   2032 C CZ3 . TRP B 2 52  ? -33.782 -43.555 5.270  1.00 24.09 ? 52  TRP B CZ3 1 
ATOM   2033 C CH2 . TRP B 2 52  ? -32.378 -43.561 5.275  1.00 22.88 ? 52  TRP B CH2 1 
ATOM   2034 N N   . SER B 2 53  ? -38.518 -47.183 5.205  1.00 36.67 ? 53  SER B N   1 
ATOM   2035 C CA  . SER B 2 53  ? -39.929 -47.409 4.880  1.00 32.63 ? 53  SER B CA  1 
ATOM   2036 C C   . SER B 2 53  ? -40.218 -48.813 4.356  1.00 32.34 ? 53  SER B C   1 
ATOM   2037 O O   . SER B 2 53  ? -41.128 -49.493 4.842  1.00 28.49 ? 53  SER B O   1 
ATOM   2038 C CB  . SER B 2 53  ? -40.385 -46.375 3.863  1.00 33.73 ? 53  SER B CB  1 
ATOM   2039 O OG  . SER B 2 53  ? -40.295 -45.082 4.424  1.00 36.31 ? 53  SER B OG  1 
ATOM   2040 N N   . GLY B 2 54  ? -39.423 -49.247 3.383  1.00 28.40 ? 54  GLY B N   1 
ATOM   2041 C CA  . GLY B 2 54  ? -39.624 -50.539 2.752  1.00 18.47 ? 54  GLY B CA  1 
ATOM   2042 C C   . GLY B 2 54  ? -39.042 -51.702 3.520  1.00 27.29 ? 54  GLY B C   1 
ATOM   2043 O O   . GLY B 2 54  ? -39.086 -52.837 3.047  1.00 29.72 ? 54  GLY B O   1 
ATOM   2044 N N   . GLY B 2 55  ? -38.476 -51.429 4.695  1.00 31.86 ? 55  GLY B N   1 
ATOM   2045 C CA  . GLY B 2 55  ? -37.967 -52.489 5.559  1.00 21.81 ? 55  GLY B CA  1 
ATOM   2046 C C   . GLY B 2 55  ? -36.474 -52.777 5.501  1.00 20.28 ? 55  GLY B C   1 
ATOM   2047 O O   . GLY B 2 55  ? -35.965 -53.585 6.271  1.00 30.36 ? 55  GLY B O   1 
ATOM   2048 N N   . ASN B 2 56  ? -35.769 -52.146 4.571  1.00 25.57 ? 56  ASN B N   1 
ATOM   2049 C CA  . ASN B 2 56  ? -34.320 -52.279 4.487  1.00 24.18 ? 56  ASN B CA  1 
ATOM   2050 C C   . ASN B 2 56  ? -33.651 -51.647 5.699  1.00 24.34 ? 56  ASN B C   1 
ATOM   2051 O O   . ASN B 2 56  ? -34.159 -50.670 6.256  1.00 24.14 ? 56  ASN B O   1 
ATOM   2052 C CB  . ASN B 2 56  ? -33.804 -51.590 3.224  1.00 32.96 ? 56  ASN B CB  1 
ATOM   2053 C CG  . ASN B 2 56  ? -34.146 -52.347 1.960  1.00 33.04 ? 56  ASN B CG  1 
ATOM   2054 O OD1 . ASN B 2 56  ? -34.275 -53.574 1.970  1.00 29.55 ? 56  ASN B OD1 1 
ATOM   2055 N ND2 . ASN B 2 56  ? -34.270 -51.619 0.853  1.00 32.05 ? 56  ASN B ND2 1 
ATOM   2056 N N   . THR B 2 57  ? -32.508 -52.186 6.105  1.00 22.19 ? 57  THR B N   1 
ATOM   2057 C CA  . THR B 2 57  ? -31.762 -51.586 7.202  1.00 21.56 ? 57  THR B CA  1 
ATOM   2058 C C   . THR B 2 57  ? -30.311 -51.288 6.846  1.00 18.29 ? 57  THR B C   1 
ATOM   2059 O O   . THR B 2 57  ? -29.702 -51.999 6.066  1.00 24.91 ? 57  THR B O   1 
ATOM   2060 C CB  . THR B 2 57  ? -31.771 -52.475 8.460  1.00 22.39 ? 57  THR B CB  1 
ATOM   2061 O OG1 . THR B 2 57  ? -31.278 -53.779 8.133  1.00 19.27 ? 57  THR B OG1 1 
ATOM   2062 C CG2 . THR B 2 57  ? -33.180 -52.585 9.035  1.00 22.85 ? 57  THR B CG2 1 
ATOM   2063 N N   . ASP B 2 58  ? -29.773 -50.220 7.421  1.00 18.81 ? 58  ASP B N   1 
ATOM   2064 C CA  . ASP B 2 58  ? -28.337 -49.973 7.421  1.00 20.69 ? 58  ASP B CA  1 
ATOM   2065 C C   . ASP B 2 58  ? -27.900 -49.925 8.866  1.00 27.37 ? 58  ASP B C   1 
ATOM   2066 O O   . ASP B 2 58  ? -28.633 -49.414 9.724  1.00 25.73 ? 58  ASP B O   1 
ATOM   2067 C CB  . ASP B 2 58  ? -28.007 -48.628 6.777  1.00 26.93 ? 58  ASP B CB  1 
ATOM   2068 C CG  . ASP B 2 58  ? -28.573 -48.496 5.378  1.00 29.50 ? 58  ASP B CG  1 
ATOM   2069 O OD1 . ASP B 2 58  ? -28.564 -49.497 4.631  1.00 26.21 ? 58  ASP B OD1 1 
ATOM   2070 O OD2 . ASP B 2 58  ? -29.032 -47.389 5.021  1.00 32.88 ? 58  ASP B OD2 1 
ATOM   2071 N N   . TYR B 2 59  ? -26.712 -50.444 9.148  1.00 26.09 ? 59  TYR B N   1 
ATOM   2072 C CA  . TYR B 2 59  ? -26.121 -50.299 10.478 1.00 22.86 ? 59  TYR B CA  1 
ATOM   2073 C C   . TYR B 2 59  ? -24.777 -49.604 10.385 1.00 19.95 ? 59  TYR B C   1 
ATOM   2074 O O   . TYR B 2 59  ? -23.978 -49.912 9.501  1.00 21.63 ? 59  TYR B O   1 
ATOM   2075 C CB  . TYR B 2 59  ? -25.956 -51.660 11.147 1.00 26.62 ? 59  TYR B CB  1 
ATOM   2076 C CG  . TYR B 2 59  ? -27.234 -52.437 11.180 1.00 19.08 ? 59  TYR B CG  1 
ATOM   2077 C CD1 . TYR B 2 59  ? -28.401 -51.874 11.672 1.00 18.20 ? 59  TYR B CD1 1 
ATOM   2078 C CD2 . TYR B 2 59  ? -27.280 -53.736 10.706 1.00 22.81 ? 59  TYR B CD2 1 
ATOM   2079 C CE1 . TYR B 2 59  ? -29.586 -52.595 11.682 1.00 25.37 ? 59  TYR B CE1 1 
ATOM   2080 C CE2 . TYR B 2 59  ? -28.457 -54.461 10.710 1.00 21.39 ? 59  TYR B CE2 1 
ATOM   2081 C CZ  . TYR B 2 59  ? -29.601 -53.893 11.198 1.00 21.54 ? 59  TYR B CZ  1 
ATOM   2082 O OH  . TYR B 2 59  ? -30.764 -54.630 11.189 1.00 27.66 ? 59  TYR B OH  1 
ATOM   2083 N N   . ASN B 2 60  ? -24.526 -48.665 11.289 1.00 16.96 ? 60  ASN B N   1 
ATOM   2084 C CA  . ASN B 2 60  ? -23.202 -48.056 11.376 1.00 22.48 ? 60  ASN B CA  1 
ATOM   2085 C C   . ASN B 2 60  ? -22.182 -49.187 11.488 1.00 21.53 ? 60  ASN B C   1 
ATOM   2086 O O   . ASN B 2 60  ? -22.491 -50.237 12.049 1.00 25.02 ? 60  ASN B O   1 
ATOM   2087 C CB  . ASN B 2 60  ? -23.102 -47.085 12.566 1.00 18.43 ? 60  ASN B CB  1 
ATOM   2088 C CG  . ASN B 2 60  ? -21.945 -46.109 12.422 1.00 23.64 ? 60  ASN B CG  1 
ATOM   2089 O OD1 . ASN B 2 60  ? -21.118 -46.261 11.533 1.00 30.74 ? 60  ASN B OD1 1 
ATOM   2090 N ND2 . ASN B 2 60  ? -21.876 -45.112 13.301 1.00 21.73 ? 60  ASN B ND2 1 
ATOM   2091 N N   . THR B 2 61  ? -20.994 -48.991 10.924 1.00 22.00 ? 61  THR B N   1 
ATOM   2092 C CA  . THR B 2 61  ? -20.016 -50.080 10.776 1.00 26.07 ? 61  THR B CA  1 
ATOM   2093 C C   . THR B 2 61  ? -19.729 -50.965 12.008 1.00 26.40 ? 61  THR B C   1 
ATOM   2094 O O   . THR B 2 61  ? -19.788 -52.192 11.909 1.00 27.39 ? 61  THR B O   1 
ATOM   2095 C CB  . THR B 2 61  ? -18.671 -49.568 10.238 1.00 31.01 ? 61  THR B CB  1 
ATOM   2096 O OG1 . THR B 2 61  ? -18.908 -48.574 9.238  1.00 33.45 ? 61  THR B OG1 1 
ATOM   2097 C CG2 . THR B 2 61  ? -17.872 -50.729 9.657  1.00 28.82 ? 61  THR B CG2 1 
ATOM   2098 N N   . PRO B 2 62  ? -19.421 -50.352 13.170 1.00 27.40 ? 62  PRO B N   1 
ATOM   2099 C CA  . PRO B 2 62  ? -19.069 -51.211 14.300 1.00 21.61 ? 62  PRO B CA  1 
ATOM   2100 C C   . PRO B 2 62  ? -20.235 -51.974 14.949 1.00 25.99 ? 62  PRO B C   1 
ATOM   2101 O O   . PRO B 2 62  ? -20.003 -52.653 15.950 1.00 33.57 ? 62  PRO B O   1 
ATOM   2102 C CB  . PRO B 2 62  ? -18.451 -50.228 15.294 1.00 26.56 ? 62  PRO B CB  1 
ATOM   2103 C CG  . PRO B 2 62  ? -19.092 -48.950 14.998 1.00 26.19 ? 62  PRO B CG  1 
ATOM   2104 C CD  . PRO B 2 62  ? -19.317 -48.923 13.523 1.00 21.04 ? 62  PRO B CD  1 
ATOM   2105 N N   . PHE B 2 63  ? -21.446 -51.889 14.403 1.00 22.28 ? 63  PHE B N   1 
ATOM   2106 C CA  . PHE B 2 63  ? -22.587 -52.595 14.992 1.00 23.10 ? 63  PHE B CA  1 
ATOM   2107 C C   . PHE B 2 63  ? -23.244 -53.529 13.973 1.00 30.65 ? 63  PHE B C   1 
ATOM   2108 O O   . PHE B 2 63  ? -24.284 -54.134 14.245 1.00 32.18 ? 63  PHE B O   1 
ATOM   2109 C CB  . PHE B 2 63  ? -23.613 -51.614 15.562 1.00 21.56 ? 63  PHE B CB  1 
ATOM   2110 C CG  . PHE B 2 63  ? -23.011 -50.532 16.407 1.00 22.72 ? 63  PHE B CG  1 
ATOM   2111 C CD1 . PHE B 2 63  ? -22.684 -49.303 15.854 1.00 21.58 ? 63  PHE B CD1 1 
ATOM   2112 C CD2 . PHE B 2 63  ? -22.773 -50.741 17.756 1.00 26.20 ? 63  PHE B CD2 1 
ATOM   2113 C CE1 . PHE B 2 63  ? -22.118 -48.300 16.637 1.00 25.80 ? 63  PHE B CE1 1 
ATOM   2114 C CE2 . PHE B 2 63  ? -22.213 -49.748 18.542 1.00 26.43 ? 63  PHE B CE2 1 
ATOM   2115 C CZ  . PHE B 2 63  ? -21.883 -48.528 17.986 1.00 29.06 ? 63  PHE B CZ  1 
ATOM   2116 N N   . THR B 2 64  ? -22.627 -53.624 12.800 1.00 28.98 ? 64  THR B N   1 
ATOM   2117 C CA  . THR B 2 64  ? -22.983 -54.596 11.766 1.00 29.79 ? 64  THR B CA  1 
ATOM   2118 C C   . THR B 2 64  ? -23.396 -55.959 12.329 1.00 34.55 ? 64  THR B C   1 
ATOM   2119 O O   . THR B 2 64  ? -24.447 -56.498 11.984 1.00 36.02 ? 64  THR B O   1 
ATOM   2120 C CB  . THR B 2 64  ? -21.756 -54.831 10.852 1.00 35.41 ? 64  THR B CB  1 
ATOM   2121 O OG1 . THR B 2 64  ? -21.470 -53.640 10.109 1.00 37.87 ? 64  THR B OG1 1 
ATOM   2122 C CG2 . THR B 2 64  ? -21.976 -56.001 9.901  1.00 33.80 ? 64  THR B CG2 1 
ATOM   2123 N N   . SER B 2 65  ? -22.567 -56.503 13.218 1.00 37.87 ? 65  SER B N   1 
ATOM   2124 C CA  . SER B 2 65  ? -22.708 -57.891 13.640 1.00 36.04 ? 65  SER B CA  1 
ATOM   2125 C C   . SER B 2 65  ? -23.401 -58.081 14.981 1.00 36.33 ? 65  SER B C   1 
ATOM   2126 O O   . SER B 2 65  ? -23.444 -59.193 15.502 1.00 38.49 ? 65  SER B O   1 
ATOM   2127 C CB  . SER B 2 65  ? -21.345 -58.574 13.686 1.00 35.60 ? 65  SER B CB  1 
ATOM   2128 O OG  . SER B 2 65  ? -20.602 -58.127 14.802 1.00 42.66 ? 65  SER B OG  1 
ATOM   2129 N N   . ARG B 2 66  ? -23.943 -57.019 15.557 1.00 37.82 ? 66  ARG B N   1 
ATOM   2130 C CA  . ARG B 2 66  ? -24.658 -57.209 16.804 1.00 38.22 ? 66  ARG B CA  1 
ATOM   2131 C C   . ARG B 2 66  ? -25.911 -56.366 16.905 1.00 33.52 ? 66  ARG B C   1 
ATOM   2132 O O   . ARG B 2 66  ? -26.562 -56.335 17.939 1.00 41.67 ? 66  ARG B O   1 
ATOM   2133 C CB  . ARG B 2 66  ? -23.739 -56.981 18.008 1.00 37.29 ? 66  ARG B CB  1 
ATOM   2134 C CG  . ARG B 2 66  ? -23.122 -55.601 18.105 1.00 33.19 ? 66  ARG B CG  1 
ATOM   2135 C CD  . ARG B 2 66  ? -22.521 -55.447 19.485 1.00 31.30 ? 66  ARG B CD  1 
ATOM   2136 N NE  . ARG B 2 66  ? -22.001 -54.114 19.742 1.00 32.48 ? 66  ARG B NE  1 
ATOM   2137 C CZ  . ARG B 2 66  ? -22.073 -53.521 20.929 1.00 31.39 ? 66  ARG B CZ  1 
ATOM   2138 N NH1 . ARG B 2 66  ? -22.662 -54.145 21.941 1.00 22.21 ? 66  ARG B NH1 1 
ATOM   2139 N NH2 . ARG B 2 66  ? -21.571 -52.305 21.099 1.00 27.71 ? 66  ARG B NH2 1 
ATOM   2140 N N   . LEU B 2 67  ? -26.265 -55.699 15.821 1.00 26.93 ? 67  LEU B N   1 
ATOM   2141 C CA  . LEU B 2 67  ? -27.467 -54.890 15.822 1.00 20.77 ? 67  LEU B CA  1 
ATOM   2142 C C   . LEU B 2 67  ? -28.505 -55.458 14.866 1.00 24.26 ? 67  LEU B C   1 
ATOM   2143 O O   . LEU B 2 67  ? -28.200 -55.819 13.731 1.00 36.61 ? 67  LEU B O   1 
ATOM   2144 C CB  . LEU B 2 67  ? -27.117 -53.445 15.462 1.00 25.32 ? 67  LEU B CB  1 
ATOM   2145 C CG  . LEU B 2 67  ? -28.218 -52.381 15.457 1.00 34.16 ? 67  LEU B CG  1 
ATOM   2146 C CD1 . LEU B 2 67  ? -29.023 -52.481 16.736 1.00 29.33 ? 67  LEU B CD1 1 
ATOM   2147 C CD2 . LEU B 2 67  ? -27.626 -50.974 15.294 1.00 23.25 ? 67  LEU B CD2 1 
ATOM   2148 N N   . SER B 2 68  ? -29.739 -55.555 15.328 1.00 23.65 ? 68  SER B N   1 
ATOM   2149 C CA  . SER B 2 68  ? -30.828 -55.900 14.441 1.00 20.24 ? 68  SER B CA  1 
ATOM   2150 C C   . SER B 2 68  ? -31.971 -54.932 14.682 1.00 25.19 ? 68  SER B C   1 
ATOM   2151 O O   . SER B 2 68  ? -32.309 -54.642 15.825 1.00 26.06 ? 68  SER B O   1 
ATOM   2152 C CB  . SER B 2 68  ? -31.274 -57.333 14.691 1.00 26.01 ? 68  SER B CB  1 
ATOM   2153 O OG  . SER B 2 68  ? -32.631 -57.379 15.095 1.00 35.68 ? 68  SER B OG  1 
ATOM   2154 N N   . ILE B 2 69  ? -32.555 -54.415 13.607 1.00 18.98 ? 69  ILE B N   1 
ATOM   2155 C CA  . ILE B 2 69  ? -33.724 -53.549 13.726 1.00 23.07 ? 69  ILE B CA  1 
ATOM   2156 C C   . ILE B 2 69  ? -34.900 -54.118 12.928 1.00 22.77 ? 69  ILE B C   1 
ATOM   2157 O O   . ILE B 2 69  ? -34.737 -54.538 11.786 1.00 26.45 ? 69  ILE B O   1 
ATOM   2158 C CB  . ILE B 2 69  ? -33.420 -52.102 13.248 1.00 27.79 ? 69  ILE B CB  1 
ATOM   2159 C CG1 . ILE B 2 69  ? -32.168 -51.541 13.921 1.00 22.83 ? 69  ILE B CG1 1 
ATOM   2160 C CG2 . ILE B 2 69  ? -34.597 -51.183 13.514 1.00 27.30 ? 69  ILE B CG2 1 
ATOM   2161 C CD1 . ILE B 2 69  ? -31.753 -50.199 13.366 1.00 24.95 ? 69  ILE B CD1 1 
ATOM   2162 N N   . ASN B 2 70  ? -36.081 -54.145 13.537 1.00 26.93 ? 70  ASN B N   1 
ATOM   2163 C CA  . ASN B 2 70  ? -37.298 -54.593 12.855 1.00 24.71 ? 70  ASN B CA  1 
ATOM   2164 C C   . ASN B 2 70  ? -38.452 -53.683 13.200 1.00 30.10 ? 70  ASN B C   1 
ATOM   2165 O O   . ASN B 2 70  ? -38.331 -52.774 14.033 1.00 33.86 ? 70  ASN B O   1 
ATOM   2166 C CB  . ASN B 2 70  ? -37.682 -56.023 13.238 1.00 23.08 ? 70  ASN B CB  1 
ATOM   2167 C CG  . ASN B 2 70  ? -36.604 -57.024 12.908 1.00 28.62 ? 70  ASN B CG  1 
ATOM   2168 O OD1 . ASN B 2 70  ? -35.571 -57.070 13.573 1.00 39.42 ? 70  ASN B OD1 1 
ATOM   2169 N ND2 . ASN B 2 70  ? -36.833 -57.835 11.880 1.00 35.38 ? 70  ASN B ND2 1 
ATOM   2170 N N   . LYS B 2 71  ? -39.587 -53.937 12.571 1.00 22.85 ? 71  LYS B N   1 
ATOM   2171 C CA  . LYS B 2 71  ? -40.750 -53.128 12.830 1.00 29.25 ? 71  LYS B CA  1 
ATOM   2172 C C   . LYS B 2 71  ? -42.006 -53.885 12.483 1.00 33.18 ? 71  LYS B C   1 
ATOM   2173 O O   . LYS B 2 71  ? -41.957 -54.934 11.842 1.00 27.36 ? 71  LYS B O   1 
ATOM   2174 C CB  . LYS B 2 71  ? -40.683 -51.838 12.021 1.00 34.24 ? 71  LYS B CB  1 
ATOM   2175 C CG  . LYS B 2 71  ? -40.812 -52.056 10.531 1.00 29.77 ? 71  LYS B CG  1 
ATOM   2176 C CD  . LYS B 2 71  ? -40.560 -50.766 9.778  1.00 26.73 ? 71  LYS B CD  1 
ATOM   2177 C CE  . LYS B 2 71  ? -40.917 -50.904 8.311  1.00 23.77 ? 71  LYS B CE  1 
ATOM   2178 N NZ  . LYS B 2 71  ? -41.282 -49.569 7.797  1.00 24.62 ? 71  LYS B NZ  1 
ATOM   2179 N N   . ASP B 2 72  ? -43.126 -53.334 12.932 1.00 32.74 ? 72  ASP B N   1 
ATOM   2180 C CA  . ASP B 2 72  ? -44.448 -53.834 12.619 1.00 21.90 ? 72  ASP B CA  1 
ATOM   2181 C C   . ASP B 2 72  ? -45.219 -52.597 12.202 1.00 32.09 ? 72  ASP B C   1 
ATOM   2182 O O   . ASP B 2 72  ? -45.735 -51.872 13.054 1.00 37.65 ? 72  ASP B O   1 
ATOM   2183 C CB  . ASP B 2 72  ? -45.074 -54.467 13.865 1.00 35.90 ? 72  ASP B CB  1 
ATOM   2184 C CG  . ASP B 2 72  ? -46.457 -55.064 13.606 1.00 44.97 ? 72  ASP B CG  1 
ATOM   2185 O OD1 . ASP B 2 72  ? -47.315 -54.401 12.973 1.00 39.30 ? 72  ASP B OD1 1 
ATOM   2186 O OD2 . ASP B 2 72  ? -46.685 -56.210 14.054 1.00 45.08 ? 72  ASP B OD2 1 
ATOM   2187 N N   . ASN B 2 73  ? -45.274 -52.350 10.893 1.00 37.90 ? 73  ASN B N   1 
ATOM   2188 C CA  . ASN B 2 73  ? -45.955 -51.181 10.333 1.00 32.27 ? 73  ASN B CA  1 
ATOM   2189 C C   . ASN B 2 73  ? -47.352 -50.955 10.892 1.00 39.39 ? 73  ASN B C   1 
ATOM   2190 O O   . ASN B 2 73  ? -47.716 -49.822 11.236 1.00 36.06 ? 73  ASN B O   1 
ATOM   2191 C CB  . ASN B 2 73  ? -46.038 -51.278 8.812  1.00 31.23 ? 73  ASN B CB  1 
ATOM   2192 C CG  . ASN B 2 73  ? -44.726 -50.974 8.142  1.00 37.99 ? 73  ASN B CG  1 
ATOM   2193 O OD1 . ASN B 2 73  ? -43.887 -50.269 8.699  1.00 33.58 ? 73  ASN B OD1 1 
ATOM   2194 N ND2 . ASN B 2 73  ? -44.533 -51.509 6.940  1.00 36.68 ? 73  ASN B ND2 1 
ATOM   2195 N N   . SER B 2 74  ? -48.124 -52.036 10.985 1.00 42.23 ? 74  SER B N   1 
ATOM   2196 C CA  . SER B 2 74  ? -49.506 -51.959 11.446 1.00 38.97 ? 74  SER B CA  1 
ATOM   2197 C C   . SER B 2 74  ? -49.599 -51.505 12.898 1.00 38.48 ? 74  SER B C   1 
ATOM   2198 O O   . SER B 2 74  ? -50.492 -50.725 13.251 1.00 42.99 ? 74  SER B O   1 
ATOM   2199 C CB  . SER B 2 74  ? -50.236 -53.293 11.232 1.00 40.64 ? 74  SER B CB  1 
ATOM   2200 O OG  . SER B 2 74  ? -49.432 -54.400 11.591 1.00 44.83 ? 74  SER B OG  1 
ATOM   2201 N N   . LYS B 2 75  ? -48.657 -51.918 13.712 1.00 34.30 ? 75  LYS B N   1 
ATOM   2202 C CA  . LYS B 2 75  ? -48.665 -51.539 15.099 1.00 33.68 ? 75  LYS B CA  1 
ATOM   2203 C C   . LYS B 2 75  ? -47.898 -50.269 15.362 1.00 38.17 ? 75  LYS B C   1 
ATOM   2204 O O   . LYS B 2 75  ? -47.829 -49.806 16.477 1.00 34.02 ? 75  LYS B O   1 
ATOM   2205 C CB  . LYS B 2 75  ? -48.136 -52.654 15.933 1.00 30.36 ? 75  LYS B CB  1 
ATOM   2206 C CG  . LYS B 2 75  ? -49.168 -53.716 16.139 1.00 45.11 ? 75  LYS B CG  1 
ATOM   2207 C CD  . LYS B 2 75  ? -48.581 -55.100 16.143 1.00 47.88 ? 75  LYS B CD  1 
ATOM   2208 C CE  . LYS B 2 75  ? -47.915 -55.427 17.453 1.00 53.81 ? 75  LYS B CE  1 
ATOM   2209 N NZ  . LYS B 2 75  ? -47.924 -56.888 17.705 1.00 62.77 ? 75  LYS B NZ  1 
ATOM   2210 N N   . SER B 2 76  ? -47.338 -49.722 14.297 1.00 31.47 ? 76  SER B N   1 
ATOM   2211 C CA  . SER B 2 76  ? -46.521 -48.516 14.368 1.00 32.45 ? 76  SER B CA  1 
ATOM   2212 C C   . SER B 2 76  ? -45.342 -48.679 15.326 1.00 32.37 ? 76  SER B C   1 
ATOM   2213 O O   . SER B 2 76  ? -44.945 -47.726 15.998 1.00 30.07 ? 76  SER B O   1 
ATOM   2214 C CB  . SER B 2 76  ? -47.357 -47.303 14.776 1.00 27.62 ? 76  SER B CB  1 
ATOM   2215 O OG  . SER B 2 76  ? -48.158 -46.839 13.705 1.00 34.33 ? 76  SER B OG  1 
ATOM   2216 N N   . GLN B 2 77  ? -44.781 -49.881 15.381 1.00 27.25 ? 77  GLN B N   1 
ATOM   2217 C CA  . GLN B 2 77  ? -43.703 -50.156 16.316 1.00 32.17 ? 77  GLN B CA  1 
ATOM   2218 C C   . GLN B 2 77  ? -42.412 -50.491 15.604 1.00 31.84 ? 77  GLN B C   1 
ATOM   2219 O O   . GLN B 2 77  ? -42.407 -51.215 14.615 1.00 28.83 ? 77  GLN B O   1 
ATOM   2220 C CB  . GLN B 2 77  ? -44.082 -51.290 17.269 1.00 30.52 ? 77  GLN B CB  1 
ATOM   2221 C CG  . GLN B 2 77  ? -45.205 -50.929 18.223 1.00 31.18 ? 77  GLN B CG  1 
ATOM   2222 C CD  . GLN B 2 77  ? -45.686 -52.121 19.038 1.00 37.50 ? 77  GLN B CD  1 
ATOM   2223 O OE1 . GLN B 2 77  ? -46.092 -51.975 20.194 1.00 33.03 ? 77  GLN B OE1 1 
ATOM   2224 N NE2 . GLN B 2 77  ? -45.651 -53.304 18.433 1.00 34.28 ? 77  GLN B NE2 1 
ATOM   2225 N N   . VAL B 2 78  ? -41.315 -49.954 16.124 1.00 34.73 ? 78  VAL B N   1 
ATOM   2226 C CA  . VAL B 2 78  ? -39.987 -50.264 15.615 1.00 29.38 ? 78  VAL B CA  1 
ATOM   2227 C C   . VAL B 2 78  ? -39.178 -50.921 16.731 1.00 32.16 ? 78  VAL B C   1 
ATOM   2228 O O   . VAL B 2 78  ? -39.089 -50.374 17.841 1.00 28.57 ? 78  VAL B O   1 
ATOM   2229 C CB  . VAL B 2 78  ? -39.272 -49.001 15.124 1.00 21.60 ? 78  VAL B CB  1 
ATOM   2230 C CG1 . VAL B 2 78  ? -37.834 -49.322 14.712 1.00 20.69 ? 78  VAL B CG1 1 
ATOM   2231 C CG2 . VAL B 2 78  ? -40.039 -48.387 13.981 1.00 22.80 ? 78  VAL B CG2 1 
ATOM   2232 N N   . PHE B 2 79  ? -38.595 -52.085 16.447 1.00 22.87 ? 79  PHE B N   1 
ATOM   2233 C CA  . PHE B 2 79  ? -37.855 -52.821 17.473 1.00 27.06 ? 79  PHE B CA  1 
ATOM   2234 C C   . PHE B 2 79  ? -36.351 -52.798 17.258 1.00 25.20 ? 79  PHE B C   1 
ATOM   2235 O O   . PHE B 2 79  ? -35.855 -53.151 16.200 1.00 26.91 ? 79  PHE B O   1 
ATOM   2236 C CB  . PHE B 2 79  ? -38.308 -54.279 17.561 1.00 29.36 ? 79  PHE B CB  1 
ATOM   2237 C CG  . PHE B 2 79  ? -39.785 -54.457 17.511 1.00 28.93 ? 79  PHE B CG  1 
ATOM   2238 C CD1 . PHE B 2 79  ? -40.396 -54.907 16.346 1.00 26.62 ? 79  PHE B CD1 1 
ATOM   2239 C CD2 . PHE B 2 79  ? -40.569 -54.176 18.617 1.00 30.17 ? 79  PHE B CD2 1 
ATOM   2240 C CE1 . PHE B 2 79  ? -41.769 -55.073 16.289 1.00 34.17 ? 79  PHE B CE1 1 
ATOM   2241 C CE2 . PHE B 2 79  ? -41.945 -54.338 18.568 1.00 29.72 ? 79  PHE B CE2 1 
ATOM   2242 C CZ  . PHE B 2 79  ? -42.547 -54.787 17.409 1.00 31.64 ? 79  PHE B CZ  1 
ATOM   2243 N N   . PHE B 2 80  ? -35.635 -52.423 18.306 1.00 27.63 ? 80  PHE B N   1 
ATOM   2244 C CA  . PHE B 2 80  ? -34.193 -52.312 18.285 1.00 25.06 ? 80  PHE B CA  1 
ATOM   2245 C C   . PHE B 2 80  ? -33.647 -53.393 19.208 1.00 27.34 ? 80  PHE B C   1 
ATOM   2246 O O   . PHE B 2 80  ? -34.064 -53.510 20.365 1.00 32.78 ? 80  PHE B O   1 
ATOM   2247 C CB  . PHE B 2 80  ? -33.829 -50.910 18.787 1.00 26.10 ? 80  PHE B CB  1 
ATOM   2248 C CG  . PHE B 2 80  ? -32.359 -50.676 19.039 1.00 26.44 ? 80  PHE B CG  1 
ATOM   2249 C CD1 . PHE B 2 80  ? -31.570 -50.083 18.077 1.00 17.44 ? 80  PHE B CD1 1 
ATOM   2250 C CD2 . PHE B 2 80  ? -31.792 -50.969 20.274 1.00 24.61 ? 80  PHE B CD2 1 
ATOM   2251 C CE1 . PHE B 2 80  ? -30.234 -49.826 18.320 1.00 21.83 ? 80  PHE B CE1 1 
ATOM   2252 C CE2 . PHE B 2 80  ? -30.451 -50.715 20.523 1.00 23.20 ? 80  PHE B CE2 1 
ATOM   2253 C CZ  . PHE B 2 80  ? -29.671 -50.143 19.547 1.00 23.49 ? 80  PHE B CZ  1 
ATOM   2254 N N   . LYS B 2 81  ? -32.730 -54.196 18.690 1.00 25.25 ? 81  LYS B N   1 
ATOM   2255 C CA  . LYS B 2 81  ? -32.057 -55.207 19.491 1.00 23.26 ? 81  LYS B CA  1 
ATOM   2256 C C   . LYS B 2 81  ? -30.555 -55.138 19.250 1.00 28.44 ? 81  LYS B C   1 
ATOM   2257 O O   . LYS B 2 81  ? -30.099 -54.997 18.110 1.00 26.96 ? 81  LYS B O   1 
ATOM   2258 C CB  . LYS B 2 81  ? -32.592 -56.618 19.200 1.00 23.32 ? 81  LYS B CB  1 
ATOM   2259 C CG  . LYS B 2 81  ? -31.976 -57.702 20.095 1.00 32.78 ? 81  LYS B CG  1 
ATOM   2260 C CD  . LYS B 2 81  ? -32.658 -59.062 19.942 1.00 33.45 ? 81  LYS B CD  1 
ATOM   2261 C CE  . LYS B 2 81  ? -32.241 -60.018 21.058 1.00 39.79 ? 81  LYS B CE  1 
ATOM   2262 N NZ  . LYS B 2 81  ? -31.494 -61.215 20.560 1.00 56.12 ? 81  LYS B NZ  1 
ATOM   2263 N N   . MET B 2 82  ? -29.788 -55.219 20.330 1.00 27.70 ? 82  MET B N   1 
ATOM   2264 C CA  . MET B 2 82  ? -28.340 -55.208 20.217 1.00 29.98 ? 82  MET B CA  1 
ATOM   2265 C C   . MET B 2 82  ? -27.749 -56.235 21.172 1.00 30.88 ? 82  MET B C   1 
ATOM   2266 O O   . MET B 2 82  ? -28.005 -56.191 22.372 1.00 33.94 ? 82  MET B O   1 
ATOM   2267 C CB  . MET B 2 82  ? -27.771 -53.811 20.494 1.00 29.29 ? 82  MET B CB  1 
ATOM   2268 C CG  . MET B 2 82  ? -26.288 -53.666 20.156 1.00 30.04 ? 82  MET B CG  1 
ATOM   2269 S SD  . MET B 2 82  ? -25.649 -52.001 20.470 1.00 37.46 ? 82  MET B SD  1 
ATOM   2270 C CE  . MET B 2 82  ? -25.833 -51.921 22.253 1.00 30.87 ? 82  MET B CE  1 
ATOM   2271 N N   . ASN B 2 83  ? -26.962 -57.155 20.623 1.00 25.39 ? 83  ASN B N   1 
ATOM   2272 C CA  . ASN B 2 83  ? -26.433 -58.291 21.366 1.00 31.89 ? 83  ASN B CA  1 
ATOM   2273 C C   . ASN B 2 83  ? -25.153 -57.986 22.140 1.00 34.20 ? 83  ASN B C   1 
ATOM   2274 O O   . ASN B 2 83  ? -24.445 -57.011 21.853 1.00 29.06 ? 83  ASN B O   1 
ATOM   2275 C CB  . ASN B 2 83  ? -26.186 -59.473 20.416 1.00 28.56 ? 83  ASN B CB  1 
ATOM   2276 C CG  . ASN B 2 83  ? -27.453 -59.924 19.705 1.00 44.82 ? 83  ASN B CG  1 
ATOM   2277 O OD1 . ASN B 2 83  ? -28.368 -60.476 20.331 1.00 49.55 ? 83  ASN B OD1 1 
ATOM   2278 N ND2 . ASN B 2 83  ? -27.512 -59.702 18.388 1.00 50.25 ? 83  ASN B ND2 1 
ATOM   2279 N N   . SER B 2 84  ? -24.887 -58.851 23.116 1.00 29.85 ? 84  SER B N   1 
ATOM   2280 C CA  . SER B 2 84  ? -23.687 -58.834 23.955 1.00 37.58 ? 84  SER B CA  1 
ATOM   2281 C C   . SER B 2 84  ? -23.187 -57.449 24.377 1.00 37.14 ? 84  SER B C   1 
ATOM   2282 O O   . SER B 2 84  ? -22.191 -56.947 23.839 1.00 33.56 ? 84  SER B O   1 
ATOM   2283 C CB  . SER B 2 84  ? -22.563 -59.631 23.288 1.00 39.80 ? 84  SER B CB  1 
ATOM   2284 O OG  . SER B 2 84  ? -22.160 -59.008 22.090 1.00 44.07 ? 84  SER B OG  1 
ATOM   2285 N N   . LEU B 2 85  ? -23.871 -56.845 25.345 1.00 31.09 ? 85  LEU B N   1 
ATOM   2286 C CA  . LEU B 2 85  ? -23.498 -55.512 25.807 1.00 36.55 ? 85  LEU B CA  1 
ATOM   2287 C C   . LEU B 2 85  ? -22.333 -55.547 26.789 1.00 39.07 ? 85  LEU B C   1 
ATOM   2288 O O   . LEU B 2 85  ? -22.124 -56.537 27.496 1.00 36.26 ? 85  LEU B O   1 
ATOM   2289 C CB  . LEU B 2 85  ? -24.697 -54.791 26.417 1.00 31.74 ? 85  LEU B CB  1 
ATOM   2290 C CG  . LEU B 2 85  ? -25.482 -53.913 25.437 1.00 38.74 ? 85  LEU B CG  1 
ATOM   2291 C CD1 . LEU B 2 85  ? -26.253 -54.754 24.437 1.00 34.05 ? 85  LEU B CD1 1 
ATOM   2292 C CD2 . LEU B 2 85  ? -26.421 -52.944 26.155 1.00 30.76 ? 85  LEU B CD2 1 
ATOM   2293 N N   . GLN B 2 86  ? -21.561 -54.471 26.816 1.00 31.14 ? 86  GLN B N   1 
ATOM   2294 C CA  . GLN B 2 86  ? -20.490 -54.339 27.790 1.00 31.32 ? 86  GLN B CA  1 
ATOM   2295 C C   . GLN B 2 86  ? -20.685 -53.016 28.491 1.00 37.65 ? 86  GLN B C   1 
ATOM   2296 O O   . GLN B 2 86  ? -21.577 -52.250 28.130 1.00 37.30 ? 86  GLN B O   1 
ATOM   2297 C CB  . GLN B 2 86  ? -19.118 -54.390 27.119 1.00 34.44 ? 86  GLN B CB  1 
ATOM   2298 C CG  . GLN B 2 86  ? -18.839 -55.695 26.373 1.00 51.01 ? 86  GLN B CG  1 
ATOM   2299 C CD  . GLN B 2 86  ? -19.057 -56.942 27.233 1.00 49.91 ? 86  GLN B CD  1 
ATOM   2300 O OE1 . GLN B 2 86  ? -18.866 -56.921 28.457 1.00 46.30 ? 86  GLN B OE1 1 
ATOM   2301 N NE2 . GLN B 2 86  ? -19.469 -58.034 26.590 1.00 48.22 ? 86  GLN B NE2 1 
ATOM   2302 N N   . SER B 2 87  ? -19.863 -52.749 29.495 1.00 32.40 ? 87  SER B N   1 
ATOM   2303 C CA  . SER B 2 87  ? -20.013 -51.528 30.260 1.00 37.88 ? 87  SER B CA  1 
ATOM   2304 C C   . SER B 2 87  ? -20.065 -50.267 29.409 1.00 29.11 ? 87  SER B C   1 
ATOM   2305 O O   . SER B 2 87  ? -20.884 -49.397 29.652 1.00 28.04 ? 87  SER B O   1 
ATOM   2306 C CB  . SER B 2 87  ? -18.939 -51.421 31.343 1.00 37.56 ? 87  SER B CB  1 
ATOM   2307 O OG  . SER B 2 87  ? -19.371 -52.087 32.517 1.00 52.94 ? 87  SER B OG  1 
ATOM   2308 N N   . ASN B 2 88  ? -19.220 -50.163 28.396 1.00 31.27 ? 88  ASN B N   1 
ATOM   2309 C CA  . ASN B 2 88  ? -19.248 -48.940 27.604 1.00 29.77 ? 88  ASN B CA  1 
ATOM   2310 C C   . ASN B 2 88  ? -20.442 -48.847 26.650 1.00 28.11 ? 88  ASN B C   1 
ATOM   2311 O O   . ASN B 2 88  ? -20.535 -47.926 25.855 1.00 32.54 ? 88  ASN B O   1 
ATOM   2312 C CB  . ASN B 2 88  ? -17.916 -48.670 26.898 1.00 29.93 ? 88  ASN B CB  1 
ATOM   2313 C CG  . ASN B 2 88  ? -17.545 -49.734 25.898 1.00 40.81 ? 88  ASN B CG  1 
ATOM   2314 O OD1 . ASN B 2 88  ? -18.356 -50.590 25.534 1.00 40.84 ? 88  ASN B OD1 1 
ATOM   2315 N ND2 . ASN B 2 88  ? -16.289 -49.682 25.439 1.00 51.39 ? 88  ASN B ND2 1 
ATOM   2316 N N   . ASP B 2 89  ? -21.366 -49.797 26.735 1.00 29.87 ? 89  ASP B N   1 
ATOM   2317 C CA  . ASP B 2 89  ? -22.613 -49.681 25.989 1.00 26.34 ? 89  ASP B CA  1 
ATOM   2318 C C   . ASP B 2 89  ? -23.682 -49.020 26.845 1.00 25.35 ? 89  ASP B C   1 
ATOM   2319 O O   . ASP B 2 89  ? -24.819 -48.841 26.418 1.00 20.95 ? 89  ASP B O   1 
ATOM   2320 C CB  . ASP B 2 89  ? -23.075 -51.035 25.462 1.00 27.79 ? 89  ASP B CB  1 
ATOM   2321 C CG  . ASP B 2 89  ? -22.153 -51.579 24.390 1.00 31.36 ? 89  ASP B CG  1 
ATOM   2322 O OD1 . ASP B 2 89  ? -21.772 -50.793 23.489 1.00 32.32 ? 89  ASP B OD1 1 
ATOM   2323 O OD2 . ASP B 2 89  ? -21.800 -52.778 24.460 1.00 29.33 ? 89  ASP B OD2 1 
ATOM   2324 N N   . THR B 2 90  ? -23.294 -48.651 28.060 1.00 26.82 ? 90  THR B N   1 
ATOM   2325 C CA  . THR B 2 90  ? -24.145 -47.833 28.902 1.00 27.36 ? 90  THR B CA  1 
ATOM   2326 C C   . THR B 2 90  ? -24.326 -46.507 28.197 1.00 24.52 ? 90  THR B C   1 
ATOM   2327 O O   . THR B 2 90  ? -23.353 -45.804 27.930 1.00 24.51 ? 90  THR B O   1 
ATOM   2328 C CB  . THR B 2 90  ? -23.520 -47.589 30.293 1.00 22.38 ? 90  THR B CB  1 
ATOM   2329 O OG1 . THR B 2 90  ? -23.437 -48.836 30.998 1.00 26.15 ? 90  THR B OG1 1 
ATOM   2330 C CG2 . THR B 2 90  ? -24.361 -46.587 31.096 1.00 14.74 ? 90  THR B CG2 1 
ATOM   2331 N N   . ALA B 2 91  ? -25.576 -46.177 27.891 1.00 21.50 ? 91  ALA B N   1 
ATOM   2332 C CA  . ALA B 2 91  ? -25.885 -44.955 27.169 1.00 19.67 ? 91  ALA B CA  1 
ATOM   2333 C C   . ALA B 2 91  ? -27.375 -44.653 27.226 1.00 22.60 ? 91  ALA B C   1 
ATOM   2334 O O   . ALA B 2 91  ? -28.178 -45.483 27.678 1.00 19.47 ? 91  ALA B O   1 
ATOM   2335 C CB  . ALA B 2 91  ? -25.441 -45.092 25.719 1.00 21.06 ? 91  ALA B CB  1 
ATOM   2336 N N   . ILE B 2 92  ? -27.737 -43.454 26.779 1.00 16.15 ? 92  ILE B N   1 
ATOM   2337 C CA  . ILE B 2 92  ? -29.123 -43.166 26.471 1.00 20.88 ? 92  ILE B CA  1 
ATOM   2338 C C   . ILE B 2 92  ? -29.339 -43.478 24.997 1.00 19.25 ? 92  ILE B C   1 
ATOM   2339 O O   . ILE B 2 92  ? -28.671 -42.915 24.130 1.00 17.82 ? 92  ILE B O   1 
ATOM   2340 C CB  . ILE B 2 92  ? -29.494 -41.700 26.703 1.00 17.11 ? 92  ILE B CB  1 
ATOM   2341 C CG1 . ILE B 2 92  ? -29.235 -41.299 28.145 1.00 17.21 ? 92  ILE B CG1 1 
ATOM   2342 C CG2 . ILE B 2 92  ? -30.951 -41.469 26.338 1.00 17.98 ? 92  ILE B CG2 1 
ATOM   2343 C CD1 . ILE B 2 92  ? -29.150 -39.808 28.321 1.00 22.81 ? 92  ILE B CD1 1 
ATOM   2344 N N   . TYR B 2 93  ? -30.270 -44.383 24.729 1.00 17.19 ? 93  TYR B N   1 
ATOM   2345 C CA  . TYR B 2 93  ? -30.621 -44.760 23.378 1.00 18.09 ? 93  TYR B CA  1 
ATOM   2346 C C   . TYR B 2 93  ? -31.852 -43.990 22.921 1.00 21.77 ? 93  TYR B C   1 
ATOM   2347 O O   . TYR B 2 93  ? -32.783 -43.770 23.698 1.00 24.56 ? 93  TYR B O   1 
ATOM   2348 C CB  . TYR B 2 93  ? -30.850 -46.269 23.312 1.00 15.44 ? 93  TYR B CB  1 
ATOM   2349 C CG  . TYR B 2 93  ? -29.572 -47.026 23.519 1.00 19.80 ? 93  TYR B CG  1 
ATOM   2350 C CD1 . TYR B 2 93  ? -29.053 -47.219 24.793 1.00 20.32 ? 93  TYR B CD1 1 
ATOM   2351 C CD2 . TYR B 2 93  ? -28.852 -47.510 22.441 1.00 18.12 ? 93  TYR B CD2 1 
ATOM   2352 C CE1 . TYR B 2 93  ? -27.859 -47.891 24.982 1.00 22.89 ? 93  TYR B CE1 1 
ATOM   2353 C CE2 . TYR B 2 93  ? -27.671 -48.181 22.620 1.00 17.58 ? 93  TYR B CE2 1 
ATOM   2354 C CZ  . TYR B 2 93  ? -27.173 -48.367 23.883 1.00 22.71 ? 93  TYR B CZ  1 
ATOM   2355 O OH  . TYR B 2 93  ? -25.980 -49.043 24.037 1.00 28.04 ? 93  TYR B OH  1 
ATOM   2356 N N   . TYR B 2 94  ? -31.851 -43.574 21.659 1.00 19.67 ? 94  TYR B N   1 
ATOM   2357 C CA  . TYR B 2 94  ? -32.961 -42.804 21.115 1.00 21.65 ? 94  TYR B CA  1 
ATOM   2358 C C   . TYR B 2 94  ? -33.433 -43.368 19.801 1.00 21.20 ? 94  TYR B C   1 
ATOM   2359 O O   . TYR B 2 94  ? -32.645 -43.931 19.043 1.00 22.82 ? 94  TYR B O   1 
ATOM   2360 C CB  . TYR B 2 94  ? -32.536 -41.374 20.808 1.00 17.17 ? 94  TYR B CB  1 
ATOM   2361 C CG  . TYR B 2 94  ? -32.045 -40.536 21.945 1.00 17.16 ? 94  TYR B CG  1 
ATOM   2362 C CD1 . TYR B 2 94  ? -32.898 -39.670 22.612 1.00 17.12 ? 94  TYR B CD1 1 
ATOM   2363 C CD2 . TYR B 2 94  ? -30.710 -40.545 22.305 1.00 20.68 ? 94  TYR B CD2 1 
ATOM   2364 C CE1 . TYR B 2 94  ? -32.439 -38.860 23.630 1.00 15.59 ? 94  TYR B CE1 1 
ATOM   2365 C CE2 . TYR B 2 94  ? -30.241 -39.732 23.326 1.00 20.70 ? 94  TYR B CE2 1 
ATOM   2366 C CZ  . TYR B 2 94  ? -31.110 -38.896 23.981 1.00 15.51 ? 94  TYR B CZ  1 
ATOM   2367 O OH  . TYR B 2 94  ? -30.640 -38.102 24.998 1.00 26.97 ? 94  TYR B OH  1 
ATOM   2368 N N   . CYS B 2 95  ? -34.711 -43.165 19.502 1.00 19.55 ? 95  CYS B N   1 
ATOM   2369 C CA  . CYS B 2 95  ? -35.183 -43.340 18.131 1.00 21.41 ? 95  CYS B CA  1 
ATOM   2370 C C   . CYS B 2 95  ? -35.522 -41.964 17.554 1.00 21.75 ? 95  CYS B C   1 
ATOM   2371 O O   . CYS B 2 95  ? -35.923 -41.046 18.280 1.00 21.23 ? 95  CYS B O   1 
ATOM   2372 C CB  . CYS B 2 95  ? -36.354 -44.329 18.034 1.00 22.83 ? 95  CYS B CB  1 
ATOM   2373 S SG  . CYS B 2 95  ? -37.844 -43.867 18.940 1.00 30.22 ? 95  CYS B SG  1 
ATOM   2374 N N   . ALA B 2 96  ? -35.325 -41.803 16.257 1.00 16.62 ? 96  ALA B N   1 
ATOM   2375 C CA  . ALA B 2 96  ? -35.531 -40.498 15.663 1.00 16.04 ? 96  ALA B CA  1 
ATOM   2376 C C   . ALA B 2 96  ? -36.162 -40.604 14.296 1.00 21.73 ? 96  ALA B C   1 
ATOM   2377 O O   . ALA B 2 96  ? -36.083 -41.652 13.647 1.00 20.83 ? 96  ALA B O   1 
ATOM   2378 C CB  . ALA B 2 96  ? -34.228 -39.750 15.579 1.00 15.49 ? 96  ALA B CB  1 
ATOM   2379 N N   . ARG B 2 97  ? -36.799 -39.513 13.873 1.00 22.11 ? 97  ARG B N   1 
ATOM   2380 C CA  . ARG B 2 97  ? -37.342 -39.415 12.534 1.00 20.96 ? 97  ARG B CA  1 
ATOM   2381 C C   . ARG B 2 97  ? -36.821 -38.155 11.872 1.00 26.82 ? 97  ARG B C   1 
ATOM   2382 O O   . ARG B 2 97  ? -36.669 -37.118 12.518 1.00 23.28 ? 97  ARG B O   1 
ATOM   2383 C CB  . ARG B 2 97  ? -38.864 -39.396 12.544 1.00 19.77 ? 97  ARG B CB  1 
ATOM   2384 C CG  . ARG B 2 97  ? -39.466 -39.900 11.250 1.00 22.22 ? 97  ARG B CG  1 
ATOM   2385 C CD  . ARG B 2 97  ? -40.798 -39.250 10.958 1.00 25.34 ? 97  ARG B CD  1 
ATOM   2386 N NE  . ARG B 2 97  ? -40.627 -37.973 10.277 1.00 28.52 ? 97  ARG B NE  1 
ATOM   2387 C CZ  . ARG B 2 97  ? -41.628 -37.205 9.871  1.00 26.79 ? 97  ARG B CZ  1 
ATOM   2388 N NH1 . ARG B 2 97  ? -42.879 -37.581 10.096 1.00 31.60 ? 97  ARG B NH1 1 
ATOM   2389 N NH2 . ARG B 2 97  ? -41.378 -36.066 9.238  1.00 29.25 ? 97  ARG B NH2 1 
ATOM   2390 N N   . ALA B 2 98  ? -36.542 -38.254 10.576 1.00 27.91 ? 98  ALA B N   1 
ATOM   2391 C CA  . ALA B 2 98  ? -36.024 -37.125 9.827  1.00 25.54 ? 98  ALA B CA  1 
ATOM   2392 C C   . ALA B 2 98  ? -37.163 -36.249 9.313  1.00 23.55 ? 98  ALA B C   1 
ATOM   2393 O O   . ALA B 2 98  ? -38.331 -36.628 9.397  1.00 24.86 ? 98  ALA B O   1 
ATOM   2394 C CB  . ALA B 2 98  ? -35.144 -37.615 8.685  1.00 19.40 ? 98  ALA B CB  1 
ATOM   2395 N N   . LEU B 2 99  ? -36.825 -35.086 8.761  1.00 21.57 ? 99  LEU B N   1 
ATOM   2396 C CA  . LEU B 2 99  ? -37.815 -34.235 8.089  1.00 29.47 ? 99  LEU B CA  1 
ATOM   2397 C C   . LEU B 2 99  ? -38.428 -34.891 6.845  1.00 31.81 ? 99  LEU B C   1 
ATOM   2398 O O   . LEU B 2 99  ? -39.641 -34.841 6.651  1.00 33.03 ? 99  LEU B O   1 
ATOM   2399 C CB  . LEU B 2 99  ? -37.200 -32.895 7.695  1.00 23.18 ? 99  LEU B CB  1 
ATOM   2400 C CG  . LEU B 2 99  ? -37.236 -31.756 8.708  1.00 29.08 ? 99  LEU B CG  1 
ATOM   2401 C CD1 . LEU B 2 99  ? -36.693 -30.509 8.057  1.00 25.42 ? 99  LEU B CD1 1 
ATOM   2402 C CD2 . LEU B 2 99  ? -38.642 -31.513 9.255  1.00 18.98 ? 99  LEU B CD2 1 
ATOM   2403 N N   . THR B 2 100 ? -37.590 -35.489 5.999  1.00 32.18 ? 100 THR B N   1 
ATOM   2404 C CA  . THR B 2 100 ? -38.076 -36.166 4.798  1.00 29.05 ? 100 THR B CA  1 
ATOM   2405 C C   . THR B 2 100 ? -37.774 -37.652 4.891  1.00 26.91 ? 100 THR B C   1 
ATOM   2406 O O   . THR B 2 100 ? -36.998 -38.077 5.749  1.00 28.93 ? 100 THR B O   1 
ATOM   2407 C CB  . THR B 2 100 ? -37.474 -35.565 3.516  1.00 37.00 ? 100 THR B CB  1 
ATOM   2408 O OG1 . THR B 2 100 ? -36.049 -35.579 3.613  1.00 45.18 ? 100 THR B OG1 1 
ATOM   2409 C CG2 . THR B 2 100 ? -37.929 -34.132 3.346  1.00 40.31 ? 100 THR B CG2 1 
ATOM   2410 N N   . TYR B 2 101 ? -38.400 -38.442 4.030  1.00 24.66 ? 101 TYR B N   1 
ATOM   2411 C CA  . TYR B 2 101 ? -38.296 -39.893 4.125  1.00 27.42 ? 101 TYR B CA  1 
ATOM   2412 C C   . TYR B 2 101 ? -36.880 -40.465 3.933  1.00 27.06 ? 101 TYR B C   1 
ATOM   2413 O O   . TYR B 2 101 ? -36.585 -41.554 4.434  1.00 31.38 ? 101 TYR B O   1 
ATOM   2414 C CB  . TYR B 2 101 ? -39.277 -40.580 3.168  1.00 25.02 ? 101 TYR B CB  1 
ATOM   2415 C CG  . TYR B 2 101 ? -38.849 -40.570 1.714  1.00 27.83 ? 101 TYR B CG  1 
ATOM   2416 C CD1 . TYR B 2 101 ? -38.082 -41.598 1.186  1.00 22.90 ? 101 TYR B CD1 1 
ATOM   2417 C CD2 . TYR B 2 101 ? -39.221 -39.533 0.870  1.00 25.20 ? 101 TYR B CD2 1 
ATOM   2418 C CE1 . TYR B 2 101 ? -37.692 -41.594 -0.152 1.00 26.45 ? 101 TYR B CE1 1 
ATOM   2419 C CE2 . TYR B 2 101 ? -38.839 -39.517 -0.464 1.00 28.27 ? 101 TYR B CE2 1 
ATOM   2420 C CZ  . TYR B 2 101 ? -38.072 -40.549 -0.975 1.00 30.50 ? 101 TYR B CZ  1 
ATOM   2421 O OH  . TYR B 2 101 ? -37.692 -40.529 -2.308 1.00 23.99 ? 101 TYR B OH  1 
ATOM   2422 N N   . TYR B 2 102 ? -36.015 -39.749 3.216  1.00 24.84 ? 102 TYR B N   1 
ATOM   2423 C CA  . TYR B 2 102 ? -34.701 -40.306 2.847  1.00 22.76 ? 102 TYR B CA  1 
ATOM   2424 C C   . TYR B 2 102 ? -33.539 -39.675 3.617  1.00 23.16 ? 102 TYR B C   1 
ATOM   2425 O O   . TYR B 2 102 ? -32.387 -40.090 3.467  1.00 24.25 ? 102 TYR B O   1 
ATOM   2426 C CB  . TYR B 2 102 ? -34.438 -40.082 1.345  1.00 23.85 ? 102 TYR B CB  1 
ATOM   2427 C CG  . TYR B 2 102 ? -34.531 -38.621 0.960  1.00 24.27 ? 102 TYR B CG  1 
ATOM   2428 C CD1 . TYR B 2 102 ? -33.443 -37.768 1.108  1.00 22.13 ? 102 TYR B CD1 1 
ATOM   2429 C CD2 . TYR B 2 102 ? -35.726 -38.087 0.514  1.00 22.70 ? 102 TYR B CD2 1 
ATOM   2430 C CE1 . TYR B 2 102 ? -33.533 -36.434 0.796  1.00 25.65 ? 102 TYR B CE1 1 
ATOM   2431 C CE2 . TYR B 2 102 ? -35.832 -36.755 0.192  1.00 28.44 ? 102 TYR B CE2 1 
ATOM   2432 C CZ  . TYR B 2 102 ? -34.731 -35.927 0.333  1.00 32.69 ? 102 TYR B CZ  1 
ATOM   2433 O OH  . TYR B 2 102 ? -34.846 -34.593 0.014  1.00 26.02 ? 102 TYR B OH  1 
ATOM   2434 N N   . ASP B 2 103 ? -33.839 -38.660 4.420  1.00 23.13 ? 103 ASP B N   1 
ATOM   2435 C CA  . ASP B 2 103 ? -32.814 -37.754 4.931  1.00 17.60 ? 103 ASP B CA  1 
ATOM   2436 C C   . ASP B 2 103 ? -32.393 -38.057 6.385  1.00 28.93 ? 103 ASP B C   1 
ATOM   2437 O O   . ASP B 2 103 ? -32.860 -39.017 6.999  1.00 22.81 ? 103 ASP B O   1 
ATOM   2438 C CB  . ASP B 2 103 ? -33.318 -36.316 4.802  1.00 22.76 ? 103 ASP B CB  1 
ATOM   2439 C CG  . ASP B 2 103 ? -32.230 -35.347 4.403  1.00 24.97 ? 103 ASP B CG  1 
ATOM   2440 O OD1 . ASP B 2 103 ? -31.056 -35.617 4.717  1.00 24.38 ? 103 ASP B OD1 1 
ATOM   2441 O OD2 . ASP B 2 103 ? -32.552 -34.311 3.780  1.00 23.79 ? 103 ASP B OD2 1 
ATOM   2442 N N   . TYR B 2 104 ? -31.516 -37.226 6.936  1.00 25.30 ? 104 TYR B N   1 
ATOM   2443 C CA  . TYR B 2 104 ? -30.873 -37.542 8.200  1.00 19.74 ? 104 TYR B CA  1 
ATOM   2444 C C   . TYR B 2 104 ? -30.922 -36.381 9.183  1.00 19.58 ? 104 TYR B C   1 
ATOM   2445 O O   . TYR B 2 104 ? -30.318 -36.448 10.247 1.00 24.38 ? 104 TYR B O   1 
ATOM   2446 C CB  . TYR B 2 104 ? -29.412 -37.965 7.965  1.00 19.62 ? 104 TYR B CB  1 
ATOM   2447 C CG  . TYR B 2 104 ? -29.242 -39.324 7.302  1.00 22.82 ? 104 TYR B CG  1 
ATOM   2448 C CD1 . TYR B 2 104 ? -28.963 -40.460 8.049  1.00 19.69 ? 104 TYR B CD1 1 
ATOM   2449 C CD2 . TYR B 2 104 ? -29.357 -39.465 5.923  1.00 27.10 ? 104 TYR B CD2 1 
ATOM   2450 C CE1 . TYR B 2 104 ? -28.805 -41.691 7.446  1.00 24.12 ? 104 TYR B CE1 1 
ATOM   2451 C CE2 . TYR B 2 104 ? -29.202 -40.687 5.308  1.00 24.58 ? 104 TYR B CE2 1 
ATOM   2452 C CZ  . TYR B 2 104 ? -28.924 -41.798 6.064  1.00 28.75 ? 104 TYR B CZ  1 
ATOM   2453 O OH  . TYR B 2 104 ? -28.769 -43.012 5.429  1.00 22.60 ? 104 TYR B OH  1 
ATOM   2454 N N   . GLU B 2 105 ? -31.616 -35.308 8.836  1.00 19.00 ? 105 GLU B N   1 
ATOM   2455 C CA  . GLU B 2 105 ? -31.786 -34.237 9.795  1.00 19.30 ? 105 GLU B CA  1 
ATOM   2456 C C   . GLU B 2 105 ? -32.930 -34.617 10.744 1.00 29.89 ? 105 GLU B C   1 
ATOM   2457 O O   . GLU B 2 105 ? -34.094 -34.705 10.349 1.00 26.15 ? 105 GLU B O   1 
ATOM   2458 C CB  . GLU B 2 105 ? -31.977 -32.870 9.119  1.00 23.47 ? 105 GLU B CB  1 
ATOM   2459 C CG  . GLU B 2 105 ? -33.353 -32.566 8.542  1.00 25.66 ? 105 GLU B CG  1 
ATOM   2460 C CD  . GLU B 2 105 ? -33.584 -33.216 7.197  1.00 30.71 ? 105 GLU B CD  1 
ATOM   2461 O OE1 . GLU B 2 105 ? -33.565 -32.487 6.185  1.00 36.41 ? 105 GLU B OE1 1 
ATOM   2462 O OE2 . GLU B 2 105 ? -33.799 -34.449 7.149  1.00 32.03 ? 105 GLU B OE2 1 
ATOM   2463 N N   . PHE B 2 106 ? -32.580 -34.879 12.001 1.00 24.07 ? 106 PHE B N   1 
ATOM   2464 C CA  . PHE B 2 106 ? -33.527 -35.471 12.934 1.00 23.11 ? 106 PHE B CA  1 
ATOM   2465 C C   . PHE B 2 106 ? -34.375 -34.467 13.699 1.00 22.09 ? 106 PHE B C   1 
ATOM   2466 O O   . PHE B 2 106 ? -33.936 -33.879 14.686 1.00 20.25 ? 106 PHE B O   1 
ATOM   2467 C CB  . PHE B 2 106 ? -32.795 -36.392 13.884 1.00 22.67 ? 106 PHE B CB  1 
ATOM   2468 C CG  . PHE B 2 106 ? -31.910 -37.387 13.185 1.00 21.00 ? 106 PHE B CG  1 
ATOM   2469 C CD1 . PHE B 2 106 ? -32.452 -38.316 12.320 1.00 18.07 ? 106 PHE B CD1 1 
ATOM   2470 C CD2 . PHE B 2 106 ? -30.538 -37.396 13.407 1.00 23.33 ? 106 PHE B CD2 1 
ATOM   2471 C CE1 . PHE B 2 106 ? -31.653 -39.235 11.681 1.00 21.71 ? 106 PHE B CE1 1 
ATOM   2472 C CE2 . PHE B 2 106 ? -29.730 -38.310 12.778 1.00 24.09 ? 106 PHE B CE2 1 
ATOM   2473 C CZ  . PHE B 2 106 ? -30.287 -39.235 11.903 1.00 26.28 ? 106 PHE B CZ  1 
ATOM   2474 N N   . ALA B 2 107 ? -35.601 -34.283 13.225 1.00 19.96 ? 107 ALA B N   1 
ATOM   2475 C CA  . ALA B 2 107 ? -36.501 -33.299 13.803 1.00 21.23 ? 107 ALA B CA  1 
ATOM   2476 C C   . ALA B 2 107 ? -37.410 -33.889 14.884 1.00 24.57 ? 107 ALA B C   1 
ATOM   2477 O O   . ALA B 2 107 ? -38.071 -33.161 15.611 1.00 23.35 ? 107 ALA B O   1 
ATOM   2478 C CB  . ALA B 2 107 ? -37.328 -32.646 12.714 1.00 22.99 ? 107 ALA B CB  1 
ATOM   2479 N N   . TYR B 2 108 ? -37.448 -35.209 14.985 1.00 26.13 ? 108 TYR B N   1 
ATOM   2480 C CA  . TYR B 2 108 ? -38.323 -35.854 15.952 1.00 22.40 ? 108 TYR B CA  1 
ATOM   2481 C C   . TYR B 2 108 ? -37.562 -36.934 16.697 1.00 22.64 ? 108 TYR B C   1 
ATOM   2482 O O   . TYR B 2 108 ? -36.989 -37.833 16.085 1.00 25.72 ? 108 TYR B O   1 
ATOM   2483 C CB  . TYR B 2 108 ? -39.573 -36.422 15.271 1.00 20.23 ? 108 TYR B CB  1 
ATOM   2484 C CG  . TYR B 2 108 ? -40.287 -35.385 14.439 1.00 26.79 ? 108 TYR B CG  1 
ATOM   2485 C CD1 . TYR B 2 108 ? -40.156 -35.368 13.048 1.00 22.43 ? 108 TYR B CD1 1 
ATOM   2486 C CD2 . TYR B 2 108 ? -41.063 -34.396 15.042 1.00 21.62 ? 108 TYR B CD2 1 
ATOM   2487 C CE1 . TYR B 2 108 ? -40.782 -34.410 12.285 1.00 21.21 ? 108 TYR B CE1 1 
ATOM   2488 C CE2 . TYR B 2 108 ? -41.702 -33.428 14.284 1.00 27.34 ? 108 TYR B CE2 1 
ATOM   2489 C CZ  . TYR B 2 108 ? -41.551 -33.441 12.897 1.00 31.89 ? 108 TYR B CZ  1 
ATOM   2490 O OH  . TYR B 2 108 ? -42.163 -32.489 12.121 1.00 28.08 ? 108 TYR B OH  1 
ATOM   2491 N N   . TRP B 2 109 ? -37.558 -36.835 18.023 1.00 22.12 ? 109 TRP B N   1 
ATOM   2492 C CA  . TRP B 2 109 ? -36.821 -37.766 18.869 1.00 18.11 ? 109 TRP B CA  1 
ATOM   2493 C C   . TRP B 2 109 ? -37.708 -38.460 19.883 1.00 17.05 ? 109 TRP B C   1 
ATOM   2494 O O   . TRP B 2 109 ? -38.639 -37.863 20.432 1.00 19.17 ? 109 TRP B O   1 
ATOM   2495 C CB  . TRP B 2 109 ? -35.736 -37.020 19.620 1.00 16.67 ? 109 TRP B CB  1 
ATOM   2496 C CG  . TRP B 2 109 ? -34.662 -36.481 18.761 1.00 20.86 ? 109 TRP B CG  1 
ATOM   2497 C CD1 . TRP B 2 109 ? -34.737 -35.399 17.945 1.00 18.54 ? 109 TRP B CD1 1 
ATOM   2498 C CD2 . TRP B 2 109 ? -33.326 -36.988 18.643 1.00 23.13 ? 109 TRP B CD2 1 
ATOM   2499 N NE1 . TRP B 2 109 ? -33.529 -35.192 17.324 1.00 20.72 ? 109 TRP B NE1 1 
ATOM   2500 C CE2 . TRP B 2 109 ? -32.648 -36.158 17.731 1.00 24.28 ? 109 TRP B CE2 1 
ATOM   2501 C CE3 . TRP B 2 109 ? -32.638 -38.064 19.220 1.00 17.46 ? 109 TRP B CE3 1 
ATOM   2502 C CZ2 . TRP B 2 109 ? -31.314 -36.368 17.379 1.00 24.09 ? 109 TRP B CZ2 1 
ATOM   2503 C CZ3 . TRP B 2 109 ? -31.308 -38.269 18.875 1.00 14.89 ? 109 TRP B CZ3 1 
ATOM   2504 C CH2 . TRP B 2 109 ? -30.664 -37.427 17.965 1.00 23.53 ? 109 TRP B CH2 1 
ATOM   2505 N N   . GLY B 2 110 ? -37.417 -39.730 20.136 1.00 18.24 ? 110 GLY B N   1 
ATOM   2506 C CA  . GLY B 2 110 ? -37.977 -40.392 21.302 1.00 20.46 ? 110 GLY B CA  1 
ATOM   2507 C C   . GLY B 2 110 ? -37.466 -39.698 22.562 1.00 24.21 ? 110 GLY B C   1 
ATOM   2508 O O   . GLY B 2 110 ? -36.534 -38.874 22.512 1.00 18.33 ? 110 GLY B O   1 
ATOM   2509 N N   . GLN B 2 111 ? -38.064 -40.023 23.701 1.00 20.10 ? 111 GLN B N   1 
ATOM   2510 C CA  . GLN B 2 111 ? -37.663 -39.381 24.949 1.00 23.71 ? 111 GLN B CA  1 
ATOM   2511 C C   . GLN B 2 111 ? -36.334 -39.950 25.460 1.00 19.35 ? 111 GLN B C   1 
ATOM   2512 O O   . GLN B 2 111 ? -35.732 -39.410 26.383 1.00 19.94 ? 111 GLN B O   1 
ATOM   2513 C CB  . GLN B 2 111 ? -38.786 -39.459 26.005 1.00 14.16 ? 111 GLN B CB  1 
ATOM   2514 C CG  . GLN B 2 111 ? -38.874 -40.758 26.785 1.00 12.52 ? 111 GLN B CG  1 
ATOM   2515 C CD  . GLN B 2 111 ? -39.548 -41.887 26.025 1.00 22.79 ? 111 GLN B CD  1 
ATOM   2516 O OE1 . GLN B 2 111 ? -39.666 -41.867 24.790 1.00 21.36 ? 111 GLN B OE1 1 
ATOM   2517 N NE2 . GLN B 2 111 ? -39.998 -42.887 26.766 1.00 17.73 ? 111 GLN B NE2 1 
ATOM   2518 N N   . GLY B 2 112 ? -35.867 -41.021 24.822 1.00 21.55 ? 112 GLY B N   1 
ATOM   2519 C CA  . GLY B 2 112 ? -34.619 -41.671 25.192 1.00 19.49 ? 112 GLY B CA  1 
ATOM   2520 C C   . GLY B 2 112 ? -34.848 -42.787 26.198 1.00 23.91 ? 112 GLY B C   1 
ATOM   2521 O O   . GLY B 2 112 ? -35.839 -42.771 26.931 1.00 24.27 ? 112 GLY B O   1 
ATOM   2522 N N   . THR B 2 113 ? -33.936 -43.756 26.225 1.00 20.83 ? 113 THR B N   1 
ATOM   2523 C CA  . THR B 2 113 ? -34.019 -44.891 27.136 1.00 12.57 ? 113 THR B CA  1 
ATOM   2524 C C   . THR B 2 113 ? -32.649 -45.127 27.761 1.00 21.26 ? 113 THR B C   1 
ATOM   2525 O O   . THR B 2 113 ? -31.741 -45.662 27.106 1.00 23.40 ? 113 THR B O   1 
ATOM   2526 C CB  . THR B 2 113 ? -34.453 -46.186 26.404 1.00 19.65 ? 113 THR B CB  1 
ATOM   2527 O OG1 . THR B 2 113 ? -35.724 -45.997 25.761 1.00 19.94 ? 113 THR B OG1 1 
ATOM   2528 C CG2 . THR B 2 113 ? -34.539 -47.350 27.386 1.00 18.96 ? 113 THR B CG2 1 
ATOM   2529 N N   . LEU B 2 114 ? -32.488 -44.719 29.018 1.00 20.86 ? 114 LEU B N   1 
ATOM   2530 C CA  . LEU B 2 114 ? -31.210 -44.886 29.709 1.00 15.45 ? 114 LEU B CA  1 
ATOM   2531 C C   . LEU B 2 114 ? -30.961 -46.355 30.031 1.00 17.21 ? 114 LEU B C   1 
ATOM   2532 O O   . LEU B 2 114 ? -31.660 -46.965 30.845 1.00 21.38 ? 114 LEU B O   1 
ATOM   2533 C CB  . LEU B 2 114 ? -31.141 -44.040 30.987 1.00 15.68 ? 114 LEU B CB  1 
ATOM   2534 C CG  . LEU B 2 114 ? -29.893 -44.245 31.857 1.00 18.80 ? 114 LEU B CG  1 
ATOM   2535 C CD1 . LEU B 2 114 ? -28.614 -44.057 31.051 1.00 15.95 ? 114 LEU B CD1 1 
ATOM   2536 C CD2 . LEU B 2 114 ? -29.886 -43.300 33.060 1.00 20.67 ? 114 LEU B CD2 1 
ATOM   2537 N N   . VAL B 2 115 ? -29.956 -46.920 29.387 1.00 18.05 ? 115 VAL B N   1 
ATOM   2538 C CA  . VAL B 2 115 ? -29.623 -48.301 29.617 1.00 18.18 ? 115 VAL B CA  1 
ATOM   2539 C C   . VAL B 2 115 ? -28.318 -48.363 30.369 1.00 23.31 ? 115 VAL B C   1 
ATOM   2540 O O   . VAL B 2 115 ? -27.344 -47.710 29.983 1.00 24.82 ? 115 VAL B O   1 
ATOM   2541 C CB  . VAL B 2 115 ? -29.492 -49.067 28.303 1.00 18.99 ? 115 VAL B CB  1 
ATOM   2542 C CG1 . VAL B 2 115 ? -29.033 -50.491 28.570 1.00 26.42 ? 115 VAL B CG1 1 
ATOM   2543 C CG2 . VAL B 2 115 ? -30.818 -49.055 27.563 1.00 16.42 ? 115 VAL B CG2 1 
ATOM   2544 N N   . THR B 2 116 ? -28.310 -49.137 31.454 1.00 22.52 ? 116 THR B N   1 
ATOM   2545 C CA  . THR B 2 116 ? -27.113 -49.333 32.257 1.00 19.01 ? 116 THR B CA  1 
ATOM   2546 C C   . THR B 2 116 ? -26.624 -50.778 32.114 1.00 26.02 ? 116 THR B C   1 
ATOM   2547 O O   . THR B 2 116 ? -27.376 -51.732 32.334 1.00 24.89 ? 116 THR B O   1 
ATOM   2548 C CB  . THR B 2 116 ? -27.373 -48.984 33.756 1.00 26.26 ? 116 THR B CB  1 
ATOM   2549 O OG1 . THR B 2 116 ? -27.857 -47.637 33.874 1.00 22.60 ? 116 THR B OG1 1 
ATOM   2550 C CG2 . THR B 2 116 ? -26.094 -49.135 34.589 1.00 20.37 ? 116 THR B CG2 1 
ATOM   2551 N N   . VAL B 2 117 ? -25.371 -50.947 31.714 1.00 24.64 ? 117 VAL B N   1 
ATOM   2552 C CA  . VAL B 2 117 ? -24.796 -52.282 31.664 1.00 22.56 ? 117 VAL B CA  1 
ATOM   2553 C C   . VAL B 2 117 ? -24.024 -52.509 32.947 1.00 23.82 ? 117 VAL B C   1 
ATOM   2554 O O   . VAL B 2 117 ? -23.024 -51.855 33.208 1.00 25.55 ? 117 VAL B O   1 
ATOM   2555 C CB  . VAL B 2 117 ? -23.878 -52.467 30.460 1.00 32.14 ? 117 VAL B CB  1 
ATOM   2556 C CG1 . VAL B 2 117 ? -23.378 -53.912 30.395 1.00 27.77 ? 117 VAL B CG1 1 
ATOM   2557 C CG2 . VAL B 2 117 ? -24.624 -52.085 29.183 1.00 28.21 ? 117 VAL B CG2 1 
ATOM   2558 N N   . SER B 2 118 ? -24.521 -53.413 33.775 1.00 31.57 ? 118 SER B N   1 
ATOM   2559 C CA  . SER B 2 118 ? -23.919 -53.645 35.076 1.00 26.85 ? 118 SER B CA  1 
ATOM   2560 C C   . SER B 2 118 ? -24.266 -55.032 35.551 1.00 33.14 ? 118 SER B C   1 
ATOM   2561 O O   . SER B 2 118 ? -25.335 -55.559 35.238 1.00 38.97 ? 118 SER B O   1 
ATOM   2562 C CB  . SER B 2 118 ? -24.405 -52.617 36.099 1.00 26.49 ? 118 SER B CB  1 
ATOM   2563 O OG  . SER B 2 118 ? -23.996 -52.978 37.408 1.00 32.43 ? 118 SER B OG  1 
ATOM   2564 N N   . ALA B 2 119 ? -23.359 -55.626 36.310 1.00 38.77 ? 119 ALA B N   1 
ATOM   2565 C CA  . ALA B 2 119 ? -23.601 -56.951 36.850 1.00 39.41 ? 119 ALA B CA  1 
ATOM   2566 C C   . ALA B 2 119 ? -24.549 -56.922 38.057 1.00 42.90 ? 119 ALA B C   1 
ATOM   2567 O O   . ALA B 2 119 ? -25.055 -57.963 38.474 1.00 46.01 ? 119 ALA B O   1 
ATOM   2568 C CB  . ALA B 2 119 ? -22.296 -57.620 37.200 1.00 43.20 ? 119 ALA B CB  1 
ATOM   2569 N N   . ALA B 2 120 ? -24.806 -55.736 38.608 1.00 35.38 ? 120 ALA B N   1 
ATOM   2570 C CA  . ALA B 2 120 ? -25.632 -55.643 39.819 1.00 33.12 ? 120 ALA B CA  1 
ATOM   2571 C C   . ALA B 2 120 ? -27.098 -56.003 39.601 1.00 31.98 ? 120 ALA B C   1 
ATOM   2572 O O   . ALA B 2 120 ? -27.485 -56.513 38.553 1.00 35.96 ? 120 ALA B O   1 
ATOM   2573 C CB  . ALA B 2 120 ? -25.517 -54.270 40.466 1.00 27.07 ? 120 ALA B CB  1 
ATOM   2574 N N   . SER B 2 121 ? -27.919 -55.735 40.604 1.00 29.11 ? 121 SER B N   1 
ATOM   2575 C CA  . SER B 2 121 ? -29.337 -56.023 40.472 1.00 29.11 ? 121 SER B CA  1 
ATOM   2576 C C   . SER B 2 121 ? -30.160 -54.780 40.744 1.00 29.68 ? 121 SER B C   1 
ATOM   2577 O O   . SER B 2 121 ? -29.678 -53.823 41.343 1.00 27.52 ? 121 SER B O   1 
ATOM   2578 C CB  . SER B 2 121 ? -29.765 -57.170 41.383 1.00 29.16 ? 121 SER B CB  1 
ATOM   2579 O OG  . SER B 2 121 ? -29.346 -56.928 42.699 1.00 30.39 ? 121 SER B OG  1 
ATOM   2580 N N   . THR B 2 122 ? -31.400 -54.803 40.273 1.00 26.60 ? 122 THR B N   1 
ATOM   2581 C CA  . THR B 2 122 ? -32.283 -53.659 40.377 1.00 25.12 ? 122 THR B CA  1 
ATOM   2582 C C   . THR B 2 122 ? -32.813 -53.552 41.793 1.00 27.17 ? 122 THR B C   1 
ATOM   2583 O O   . THR B 2 122 ? -33.141 -54.554 42.428 1.00 33.03 ? 122 THR B O   1 
ATOM   2584 C CB  . THR B 2 122 ? -33.450 -53.768 39.382 1.00 26.04 ? 122 THR B CB  1 
ATOM   2585 O OG1 . THR B 2 122 ? -32.931 -54.071 38.081 1.00 27.18 ? 122 THR B OG1 1 
ATOM   2586 C CG2 . THR B 2 122 ? -34.197 -52.469 39.305 1.00 26.19 ? 122 THR B CG2 1 
ATOM   2587 N N   . LYS B 2 123 ? -32.876 -52.328 42.293 1.00 29.01 ? 123 LYS B N   1 
ATOM   2588 C CA  . LYS B 2 123 ? -33.334 -52.090 43.644 1.00 22.30 ? 123 LYS B CA  1 
ATOM   2589 C C   . LYS B 2 123 ? -34.099 -50.778 43.703 1.00 16.51 ? 123 LYS B C   1 
ATOM   2590 O O   . LYS B 2 123 ? -33.583 -49.739 43.307 1.00 20.57 ? 123 LYS B O   1 
ATOM   2591 C CB  . LYS B 2 123 ? -32.140 -52.058 44.596 1.00 23.99 ? 123 LYS B CB  1 
ATOM   2592 C CG  . LYS B 2 123 ? -32.555 -51.928 46.052 1.00 26.58 ? 123 LYS B CG  1 
ATOM   2593 C CD  . LYS B 2 123 ? -31.372 -51.773 46.981 1.00 22.73 ? 123 LYS B CD  1 
ATOM   2594 C CE  . LYS B 2 123 ? -31.872 -51.492 48.390 1.00 24.08 ? 123 LYS B CE  1 
ATOM   2595 N NZ  . LYS B 2 123 ? -32.866 -50.374 48.398 1.00 24.61 ? 123 LYS B NZ  1 
ATOM   2596 N N   . GLY B 2 124 ? -35.334 -50.831 44.184 1.00 16.98 ? 124 GLY B N   1 
ATOM   2597 C CA  . GLY B 2 124 ? -36.147 -49.635 44.309 1.00 16.77 ? 124 GLY B CA  1 
ATOM   2598 C C   . GLY B 2 124 ? -35.679 -48.725 45.435 1.00 18.03 ? 124 GLY B C   1 
ATOM   2599 O O   . GLY B 2 124 ? -35.011 -49.173 46.368 1.00 20.51 ? 124 GLY B O   1 
ATOM   2600 N N   . PRO B 2 125 ? -36.030 -47.434 45.360 1.00 13.95 ? 125 PRO B N   1 
ATOM   2601 C CA  . PRO B 2 125 ? -35.624 -46.481 46.396 1.00 15.60 ? 125 PRO B CA  1 
ATOM   2602 C C   . PRO B 2 125 ? -36.562 -46.520 47.593 1.00 17.42 ? 125 PRO B C   1 
ATOM   2603 O O   . PRO B 2 125 ? -37.723 -46.877 47.424 1.00 13.88 ? 125 PRO B O   1 
ATOM   2604 C CB  . PRO B 2 125 ? -35.796 -45.136 45.699 1.00 13.87 ? 125 PRO B CB  1 
ATOM   2605 C CG  . PRO B 2 125 ? -36.985 -45.363 44.794 1.00 12.59 ? 125 PRO B CG  1 
ATOM   2606 C CD  . PRO B 2 125 ? -36.883 -46.808 44.336 1.00 13.90 ? 125 PRO B CD  1 
ATOM   2607 N N   . SER B 2 126 ? -36.048 -46.192 48.778 1.00 18.20 ? 126 SER B N   1 
ATOM   2608 C CA  . SER B 2 126 ? -36.872 -45.803 49.912 1.00 11.55 ? 126 SER B CA  1 
ATOM   2609 C C   . SER B 2 126 ? -37.047 -44.299 49.806 1.00 15.95 ? 126 SER B C   1 
ATOM   2610 O O   . SER B 2 126 ? -36.121 -43.593 49.413 1.00 16.27 ? 126 SER B O   1 
ATOM   2611 C CB  . SER B 2 126 ? -36.174 -46.125 51.231 1.00 19.67 ? 126 SER B CB  1 
ATOM   2612 O OG  . SER B 2 126 ? -35.937 -47.515 51.379 1.00 26.03 ? 126 SER B OG  1 
ATOM   2613 N N   . VAL B 2 127 ? -38.221 -43.799 50.165 1.00 14.78 ? 127 VAL B N   1 
ATOM   2614 C CA  . VAL B 2 127 ? -38.506 -42.382 50.023 1.00 11.93 ? 127 VAL B CA  1 
ATOM   2615 C C   . VAL B 2 127 ? -38.789 -41.774 51.388 1.00 15.61 ? 127 VAL B C   1 
ATOM   2616 O O   . VAL B 2 127 ? -39.701 -42.195 52.074 1.00 13.77 ? 127 VAL B O   1 
ATOM   2617 C CB  . VAL B 2 127 ? -39.697 -42.165 49.089 1.00 15.84 ? 127 VAL B CB  1 
ATOM   2618 C CG1 . VAL B 2 127 ? -39.898 -40.688 48.814 1.00 10.69 ? 127 VAL B CG1 1 
ATOM   2619 C CG2 . VAL B 2 127 ? -39.482 -42.947 47.778 1.00 18.13 ? 127 VAL B CG2 1 
ATOM   2620 N N   . PHE B 2 128 ? -37.991 -40.779 51.777 1.00 19.72 ? 128 PHE B N   1 
ATOM   2621 C CA  . PHE B 2 128 ? -38.120 -40.158 53.093 1.00 20.92 ? 128 PHE B CA  1 
ATOM   2622 C C   . PHE B 2 128 ? -38.491 -38.677 53.014 1.00 17.82 ? 128 PHE B C   1 
ATOM   2623 O O   . PHE B 2 128 ? -38.076 -37.983 52.094 1.00 18.41 ? 128 PHE B O   1 
ATOM   2624 C CB  . PHE B 2 128 ? -36.840 -40.368 53.903 1.00 17.88 ? 128 PHE B CB  1 
ATOM   2625 C CG  . PHE B 2 128 ? -36.502 -41.812 54.116 1.00 18.65 ? 128 PHE B CG  1 
ATOM   2626 C CD1 . PHE B 2 128 ? -37.311 -42.612 54.904 1.00 15.88 ? 128 PHE B CD1 1 
ATOM   2627 C CD2 . PHE B 2 128 ? -35.379 -42.374 53.523 1.00 19.60 ? 128 PHE B CD2 1 
ATOM   2628 C CE1 . PHE B 2 128 ? -37.009 -43.948 55.104 1.00 17.59 ? 128 PHE B CE1 1 
ATOM   2629 C CE2 . PHE B 2 128 ? -35.070 -43.716 53.720 1.00 15.80 ? 128 PHE B CE2 1 
ATOM   2630 C CZ  . PHE B 2 128 ? -35.892 -44.500 54.503 1.00 21.69 ? 128 PHE B CZ  1 
ATOM   2631 N N   . PRO B 2 129 ? -39.294 -38.190 53.972 1.00 15.27 ? 129 PRO B N   1 
ATOM   2632 C CA  . PRO B 2 129 ? -39.680 -36.779 53.908 1.00 14.41 ? 129 PRO B CA  1 
ATOM   2633 C C   . PRO B 2 129 ? -38.547 -35.856 54.349 1.00 14.30 ? 129 PRO B C   1 
ATOM   2634 O O   . PRO B 2 129 ? -37.750 -36.207 55.216 1.00 14.49 ? 129 PRO B O   1 
ATOM   2635 C CB  . PRO B 2 129 ? -40.844 -36.694 54.899 1.00 9.66  ? 129 PRO B CB  1 
ATOM   2636 C CG  . PRO B 2 129 ? -40.504 -37.714 55.923 1.00 17.16 ? 129 PRO B CG  1 
ATOM   2637 C CD  . PRO B 2 129 ? -39.868 -38.860 55.151 1.00 17.98 ? 129 PRO B CD  1 
ATOM   2638 N N   . LEU B 2 130 ? -38.464 -34.690 53.724 1.00 15.82 ? 130 LEU B N   1 
ATOM   2639 C CA  . LEU B 2 130 ? -37.575 -33.635 54.189 1.00 17.48 ? 130 LEU B CA  1 
ATOM   2640 C C   . LEU B 2 130 ? -38.507 -32.544 54.647 1.00 12.01 ? 130 LEU B C   1 
ATOM   2641 O O   . LEU B 2 130 ? -39.007 -31.758 53.843 1.00 17.56 ? 130 LEU B O   1 
ATOM   2642 C CB  . LEU B 2 130 ? -36.646 -33.155 53.071 1.00 17.99 ? 130 LEU B CB  1 
ATOM   2643 C CG  . LEU B 2 130 ? -35.607 -34.179 52.642 1.00 15.64 ? 130 LEU B CG  1 
ATOM   2644 C CD1 . LEU B 2 130 ? -34.785 -33.646 51.503 1.00 17.14 ? 130 LEU B CD1 1 
ATOM   2645 C CD2 . LEU B 2 130 ? -34.723 -34.517 53.824 1.00 13.14 ? 130 LEU B CD2 1 
ATOM   2646 N N   . ALA B 2 131 ? -38.781 -32.545 55.945 1.00 13.07 ? 131 ALA B N   1 
ATOM   2647 C CA  . ALA B 2 131 ? -39.909 -31.801 56.494 1.00 20.59 ? 131 ALA B CA  1 
ATOM   2648 C C   . ALA B 2 131 ? -39.574 -30.339 56.683 1.00 21.83 ? 131 ALA B C   1 
ATOM   2649 O O   . ALA B 2 131 ? -38.516 -30.005 57.214 1.00 25.27 ? 131 ALA B O   1 
ATOM   2650 C CB  . ALA B 2 131 ? -40.355 -32.403 57.803 1.00 12.31 ? 131 ALA B CB  1 
ATOM   2651 N N   . PRO B 2 132 ? -40.498 -29.459 56.281 1.00 24.36 ? 132 PRO B N   1 
ATOM   2652 C CA  . PRO B 2 132 ? -40.363 -28.030 56.576 1.00 26.46 ? 132 PRO B CA  1 
ATOM   2653 C C   . PRO B 2 132 ? -40.483 -27.798 58.072 1.00 24.63 ? 132 PRO B C   1 
ATOM   2654 O O   . PRO B 2 132 ? -41.174 -28.552 58.743 1.00 32.05 ? 132 PRO B O   1 
ATOM   2655 C CB  . PRO B 2 132 ? -41.581 -27.420 55.884 1.00 22.21 ? 132 PRO B CB  1 
ATOM   2656 C CG  . PRO B 2 132 ? -42.617 -28.505 55.951 1.00 25.19 ? 132 PRO B CG  1 
ATOM   2657 C CD  . PRO B 2 132 ? -41.840 -29.798 55.775 1.00 27.88 ? 132 PRO B CD  1 
ATOM   2658 N N   . SER B 2 133 ? -39.817 -26.774 58.585 1.00 41.20 ? 133 SER B N   1 
ATOM   2659 C CA  . SER B 2 133 ? -40.000 -26.343 59.969 1.00 48.26 ? 133 SER B CA  1 
ATOM   2660 C C   . SER B 2 133 ? -39.585 -24.890 60.041 1.00 51.10 ? 133 SER B C   1 
ATOM   2661 O O   . SER B 2 133 ? -39.588 -24.203 59.027 1.00 46.27 ? 133 SER B O   1 
ATOM   2662 C CB  . SER B 2 133 ? -39.136 -27.162 60.921 1.00 49.29 ? 133 SER B CB  1 
ATOM   2663 O OG  . SER B 2 133 ? -37.798 -26.704 60.900 1.00 56.04 ? 133 SER B OG  1 
ATOM   2664 N N   . SER B 2 134 ? -39.204 -24.431 61.230 1.00 58.75 ? 134 SER B N   1 
ATOM   2665 C CA  . SER B 2 134 ? -38.603 -23.106 61.383 1.00 61.36 ? 134 SER B CA  1 
ATOM   2666 C C   . SER B 2 134 ? -37.157 -23.096 60.862 1.00 64.18 ? 134 SER B C   1 
ATOM   2667 O O   . SER B 2 134 ? -36.680 -22.083 60.346 1.00 56.74 ? 134 SER B O   1 
ATOM   2668 C CB  . SER B 2 134 ? -38.648 -22.667 62.842 1.00 49.04 ? 134 SER B CB  1 
ATOM   2669 O OG  . SER B 2 134 ? -38.058 -23.645 63.678 1.00 60.49 ? 134 SER B OG  1 
ATOM   2670 N N   . LYS B 2 135 ? -36.476 -24.237 60.991 1.00 67.13 ? 135 LYS B N   1 
ATOM   2671 C CA  . LYS B 2 135 ? -35.095 -24.408 60.516 1.00 65.40 ? 135 LYS B CA  1 
ATOM   2672 C C   . LYS B 2 135 ? -35.033 -24.389 58.985 1.00 68.00 ? 135 LYS B C   1 
ATOM   2673 O O   . LYS B 2 135 ? -33.945 -24.331 58.374 1.00 50.17 ? 135 LYS B O   1 
ATOM   2674 C CB  . LYS B 2 135 ? -34.499 -25.722 61.044 1.00 57.22 ? 135 LYS B CB  1 
ATOM   2675 C CG  . LYS B 2 135 ? -34.368 -25.783 62.559 1.00 55.12 ? 135 LYS B CG  1 
ATOM   2676 C CD  . LYS B 2 135 ? -33.471 -24.668 63.059 1.00 53.09 ? 135 LYS B CD  1 
ATOM   2677 C CE  . LYS B 2 135 ? -33.346 -24.699 64.572 1.00 46.87 ? 135 LYS B CE  1 
ATOM   2678 N NZ  . LYS B 2 135 ? -32.359 -23.686 65.049 1.00 39.26 ? 135 LYS B NZ  1 
ATOM   2679 N N   . SER B 2 136 ? -36.214 -24.444 58.375 1.00 56.98 ? 136 SER B N   1 
ATOM   2680 C CA  . SER B 2 136 ? -36.322 -24.360 56.930 1.00 56.99 ? 136 SER B CA  1 
ATOM   2681 C C   . SER B 2 136 ? -37.440 -23.396 56.463 1.00 54.20 ? 136 SER B C   1 
ATOM   2682 O O   . SER B 2 136 ? -38.040 -23.607 55.401 1.00 38.91 ? 136 SER B O   1 
ATOM   2683 C CB  . SER B 2 136 ? -36.457 -25.765 56.316 1.00 35.31 ? 136 SER B CB  1 
ATOM   2684 O OG  . SER B 2 136 ? -37.776 -26.026 55.881 1.00 34.04 ? 136 SER B OG  1 
ATOM   2685 N N   . THR B 2 137 ? -37.700 -22.347 57.259 1.00 47.92 ? 137 THR B N   1 
ATOM   2686 C CA  . THR B 2 137 ? -38.654 -21.276 56.895 1.00 56.63 ? 137 THR B CA  1 
ATOM   2687 C C   . THR B 2 137 ? -38.101 -19.864 57.145 1.00 65.76 ? 137 THR B C   1 
ATOM   2688 O O   . THR B 2 137 ? -38.082 -19.386 58.291 1.00 66.73 ? 137 THR B O   1 
ATOM   2689 C CB  . THR B 2 137 ? -40.037 -21.386 57.628 1.00 52.85 ? 137 THR B CB  1 
ATOM   2690 O OG1 . THR B 2 137 ? -40.720 -22.586 57.236 1.00 54.30 ? 137 THR B OG1 1 
ATOM   2691 C CG2 . THR B 2 137 ? -40.930 -20.183 57.292 1.00 43.13 ? 137 THR B CG2 1 
ATOM   2692 N N   . SER B 2 138 ? -37.677 -19.192 56.073 1.00 54.37 ? 138 SER B N   1 
ATOM   2693 C CA  . SER B 2 138 ? -37.157 -17.832 56.193 1.00 62.64 ? 138 SER B CA  1 
ATOM   2694 C C   . SER B 2 138 ? -37.940 -16.829 55.332 1.00 56.46 ? 138 SER B C   1 
ATOM   2695 O O   . SER B 2 138 ? -38.043 -16.979 54.106 1.00 51.07 ? 138 SER B O   1 
ATOM   2696 C CB  . SER B 2 138 ? -35.654 -17.788 55.862 1.00 58.87 ? 138 SER B CB  1 
ATOM   2697 O OG  . SER B 2 138 ? -34.999 -16.709 56.530 1.00 64.57 ? 138 SER B OG  1 
ATOM   2698 N N   . GLY B 2 139 ? -38.492 -15.809 55.990 1.00 56.69 ? 139 GLY B N   1 
ATOM   2699 C CA  . GLY B 2 139 ? -39.212 -14.738 55.315 1.00 41.42 ? 139 GLY B CA  1 
ATOM   2700 C C   . GLY B 2 139 ? -40.497 -15.166 54.628 1.00 40.88 ? 139 GLY B C   1 
ATOM   2701 O O   . GLY B 2 139 ? -40.753 -14.787 53.483 1.00 46.45 ? 139 GLY B O   1 
ATOM   2702 N N   . GLY B 2 140 ? -41.312 -15.957 55.321 1.00 34.49 ? 140 GLY B N   1 
ATOM   2703 C CA  . GLY B 2 140 ? -42.550 -16.445 54.740 1.00 39.00 ? 140 GLY B CA  1 
ATOM   2704 C C   . GLY B 2 140 ? -42.409 -17.582 53.733 1.00 30.92 ? 140 GLY B C   1 
ATOM   2705 O O   . GLY B 2 140 ? -43.410 -18.113 53.271 1.00 31.21 ? 140 GLY B O   1 
ATOM   2706 N N   . THR B 2 141 ? -41.180 -17.959 53.396 1.00 29.02 ? 141 THR B N   1 
ATOM   2707 C CA  . THR B 2 141 ? -40.939 -19.042 52.447 1.00 25.61 ? 141 THR B CA  1 
ATOM   2708 C C   . THR B 2 141 ? -40.445 -20.307 53.151 1.00 31.53 ? 141 THR B C   1 
ATOM   2709 O O   . THR B 2 141 ? -39.499 -20.257 53.943 1.00 35.58 ? 141 THR B O   1 
ATOM   2710 C CB  . THR B 2 141 ? -39.941 -18.598 51.349 1.00 24.35 ? 141 THR B CB  1 
ATOM   2711 O OG1 . THR B 2 141 ? -40.611 -17.713 50.446 1.00 23.75 ? 141 THR B OG1 1 
ATOM   2712 C CG2 . THR B 2 141 ? -39.394 -19.792 50.568 1.00 17.74 ? 141 THR B CG2 1 
ATOM   2713 N N   . ALA B 2 142 ? -41.093 -21.436 52.881 1.00 20.05 ? 142 ALA B N   1 
ATOM   2714 C CA  . ALA B 2 142 ? -40.653 -22.712 53.456 1.00 23.71 ? 142 ALA B CA  1 
ATOM   2715 C C   . ALA B 2 142 ? -40.084 -23.661 52.395 1.00 24.02 ? 142 ALA B C   1 
ATOM   2716 O O   . ALA B 2 142 ? -40.524 -23.675 51.235 1.00 26.02 ? 142 ALA B O   1 
ATOM   2717 C CB  . ALA B 2 142 ? -41.795 -23.390 54.234 1.00 20.89 ? 142 ALA B CB  1 
ATOM   2718 N N   . ALA B 2 143 ? -39.111 -24.466 52.795 1.00 21.68 ? 143 ALA B N   1 
ATOM   2719 C CA  . ALA B 2 143 ? -38.538 -25.462 51.903 1.00 19.54 ? 143 ALA B CA  1 
ATOM   2720 C C   . ALA B 2 143 ? -38.880 -26.856 52.395 1.00 17.65 ? 143 ALA B C   1 
ATOM   2721 O O   . ALA B 2 143 ? -38.886 -27.126 53.586 1.00 20.05 ? 143 ALA B O   1 
ATOM   2722 C CB  . ALA B 2 143 ? -37.042 -25.283 51.778 1.00 17.63 ? 143 ALA B CB  1 
ATOM   2723 N N   . LEU B 2 144 ? -39.176 -27.744 51.468 1.00 17.45 ? 144 LEU B N   1 
ATOM   2724 C CA  . LEU B 2 144 ? -39.517 -29.097 51.834 1.00 17.84 ? 144 LEU B CA  1 
ATOM   2725 C C   . LEU B 2 144 ? -39.136 -30.009 50.680 1.00 19.98 ? 144 LEU B C   1 
ATOM   2726 O O   . LEU B 2 144 ? -39.039 -29.573 49.524 1.00 17.93 ? 144 LEU B O   1 
ATOM   2727 C CB  . LEU B 2 144 ? -41.003 -29.196 52.205 1.00 16.81 ? 144 LEU B CB  1 
ATOM   2728 C CG  . LEU B 2 144 ? -42.035 -28.955 51.112 1.00 17.10 ? 144 LEU B CG  1 
ATOM   2729 C CD1 . LEU B 2 144 ? -42.309 -30.256 50.402 1.00 20.38 ? 144 LEU B CD1 1 
ATOM   2730 C CD2 . LEU B 2 144 ? -43.317 -28.408 51.694 1.00 25.48 ? 144 LEU B CD2 1 
ATOM   2731 N N   . GLY B 2 145 ? -38.924 -31.276 50.991 1.00 15.30 ? 145 GLY B N   1 
ATOM   2732 C CA  . GLY B 2 145 ? -38.471 -32.187 49.972 1.00 14.13 ? 145 GLY B CA  1 
ATOM   2733 C C   . GLY B 2 145 ? -38.653 -33.646 50.322 1.00 16.63 ? 145 GLY B C   1 
ATOM   2734 O O   . GLY B 2 145 ? -39.235 -34.002 51.350 1.00 13.29 ? 145 GLY B O   1 
ATOM   2735 N N   . CYS B 2 146 ? -38.146 -34.482 49.426 1.00 17.05 ? 146 CYS B N   1 
ATOM   2736 C CA  . CYS B 2 146 ? -38.155 -35.921 49.570 1.00 16.87 ? 146 CYS B CA  1 
ATOM   2737 C C   . CYS B 2 146 ? -36.761 -36.435 49.341 1.00 19.65 ? 146 CYS B C   1 
ATOM   2738 O O   . CYS B 2 146 ? -36.095 -36.050 48.366 1.00 20.43 ? 146 CYS B O   1 
ATOM   2739 C CB  . CYS B 2 146 ? -39.090 -36.546 48.538 1.00 19.12 ? 146 CYS B CB  1 
ATOM   2740 S SG  . CYS B 2 146 ? -40.776 -36.520 49.091 1.00 34.15 ? 146 CYS B SG  1 
ATOM   2741 N N   . LEU B 2 147 ? -36.318 -37.306 50.235 1.00 15.33 ? 147 LEU B N   1 
ATOM   2742 C CA  . LEU B 2 147 ? -35.054 -38.003 50.045 1.00 17.22 ? 147 LEU B CA  1 
ATOM   2743 C C   . LEU B 2 147 ? -35.345 -39.341 49.374 1.00 15.73 ? 147 LEU B C   1 
ATOM   2744 O O   . LEU B 2 147 ? -36.110 -40.149 49.889 1.00 21.13 ? 147 LEU B O   1 
ATOM   2745 C CB  . LEU B 2 147 ? -34.341 -38.187 51.384 1.00 18.13 ? 147 LEU B CB  1 
ATOM   2746 C CG  . LEU B 2 147 ? -33.075 -39.042 51.441 1.00 20.46 ? 147 LEU B CG  1 
ATOM   2747 C CD1 . LEU B 2 147 ? -31.924 -38.414 50.664 1.00 14.85 ? 147 LEU B CD1 1 
ATOM   2748 C CD2 . LEU B 2 147 ? -32.680 -39.273 52.895 1.00 19.76 ? 147 LEU B CD2 1 
ATOM   2749 N N   . VAL B 2 148 ? -34.772 -39.538 48.194 1.00 17.36 ? 148 VAL B N   1 
ATOM   2750 C CA  . VAL B 2 148 ? -34.999 -40.742 47.411 1.00 11.93 ? 148 VAL B CA  1 
ATOM   2751 C C   . VAL B 2 148 ? -33.718 -41.558 47.422 1.00 21.25 ? 148 VAL B C   1 
ATOM   2752 O O   . VAL B 2 148 ? -32.765 -41.259 46.701 1.00 24.55 ? 148 VAL B O   1 
ATOM   2753 C CB  . VAL B 2 148 ? -35.399 -40.388 45.979 1.00 20.59 ? 148 VAL B CB  1 
ATOM   2754 C CG1 . VAL B 2 148 ? -35.666 -41.652 45.166 1.00 13.61 ? 148 VAL B CG1 1 
ATOM   2755 C CG2 . VAL B 2 148 ? -36.621 -39.470 46.003 1.00 13.59 ? 148 VAL B CG2 1 
ATOM   2756 N N   . LYS B 2 149 ? -33.700 -42.593 48.253 1.00 18.48 ? 149 LYS B N   1 
ATOM   2757 C CA  . LYS B 2 149 ? -32.443 -43.181 48.685 1.00 18.66 ? 149 LYS B CA  1 
ATOM   2758 C C   . LYS B 2 149 ? -32.268 -44.642 48.284 1.00 18.36 ? 149 LYS B C   1 
ATOM   2759 O O   . LYS B 2 149 ? -33.229 -45.407 48.246 1.00 20.66 ? 149 LYS B O   1 
ATOM   2760 C CB  . LYS B 2 149 ? -32.315 -43.011 50.205 1.00 20.56 ? 149 LYS B CB  1 
ATOM   2761 C CG  . LYS B 2 149 ? -30.976 -43.388 50.789 1.00 23.97 ? 149 LYS B CG  1 
ATOM   2762 C CD  . LYS B 2 149 ? -30.680 -42.578 52.028 1.00 23.42 ? 149 LYS B CD  1 
ATOM   2763 C CE  . LYS B 2 149 ? -29.693 -43.304 52.917 1.00 23.74 ? 149 LYS B CE  1 
ATOM   2764 N NZ  . LYS B 2 149 ? -28.731 -44.090 52.123 1.00 27.35 ? 149 LYS B NZ  1 
ATOM   2765 N N   . ASP B 2 150 ? -31.028 -45.001 47.959 1.00 27.67 ? 150 ASP B N   1 
ATOM   2766 C CA  . ASP B 2 150 ? -30.615 -46.396 47.739 1.00 22.44 ? 150 ASP B CA  1 
ATOM   2767 C C   . ASP B 2 150 ? -31.319 -47.145 46.613 1.00 17.48 ? 150 ASP B C   1 
ATOM   2768 O O   . ASP B 2 150 ? -31.897 -48.205 46.829 1.00 27.10 ? 150 ASP B O   1 
ATOM   2769 C CB  . ASP B 2 150 ? -30.692 -47.186 49.055 1.00 16.27 ? 150 ASP B CB  1 
ATOM   2770 C CG  . ASP B 2 150 ? -29.812 -46.580 50.137 1.00 26.15 ? 150 ASP B CG  1 
ATOM   2771 O OD1 . ASP B 2 150 ? -28.831 -45.896 49.770 1.00 25.12 ? 150 ASP B OD1 1 
ATOM   2772 O OD2 . ASP B 2 150 ? -30.097 -46.774 51.341 1.00 30.07 ? 150 ASP B OD2 1 
ATOM   2773 N N   . TYR B 2 151 ? -31.259 -46.611 45.404 1.00 18.22 ? 151 TYR B N   1 
ATOM   2774 C CA  . TYR B 2 151 ? -31.845 -47.315 44.268 1.00 16.69 ? 151 TYR B CA  1 
ATOM   2775 C C   . TYR B 2 151 ? -30.786 -47.627 43.218 1.00 17.24 ? 151 TYR B C   1 
ATOM   2776 O O   . TYR B 2 151 ? -29.669 -47.111 43.283 1.00 16.98 ? 151 TYR B O   1 
ATOM   2777 C CB  . TYR B 2 151 ? -32.997 -46.515 43.652 1.00 14.34 ? 151 TYR B CB  1 
ATOM   2778 C CG  . TYR B 2 151 ? -32.591 -45.158 43.117 1.00 12.77 ? 151 TYR B CG  1 
ATOM   2779 C CD1 . TYR B 2 151 ? -32.544 -44.048 43.955 1.00 13.18 ? 151 TYR B CD1 1 
ATOM   2780 C CD2 . TYR B 2 151 ? -32.256 -44.986 41.771 1.00 11.42 ? 151 TYR B CD2 1 
ATOM   2781 C CE1 . TYR B 2 151 ? -32.171 -42.796 43.475 1.00 13.47 ? 151 TYR B CE1 1 
ATOM   2782 C CE2 . TYR B 2 151 ? -31.904 -43.741 41.269 1.00 13.02 ? 151 TYR B CE2 1 
ATOM   2783 C CZ  . TYR B 2 151 ? -31.853 -42.647 42.129 1.00 18.15 ? 151 TYR B CZ  1 
ATOM   2784 O OH  . TYR B 2 151 ? -31.487 -41.406 41.654 1.00 15.50 ? 151 TYR B OH  1 
ATOM   2785 N N   . PHE B 2 152 ? -31.148 -48.490 42.272 1.00 14.45 ? 152 PHE B N   1 
ATOM   2786 C CA  . PHE B 2 152 ? -30.300 -48.840 41.145 1.00 15.77 ? 152 PHE B CA  1 
ATOM   2787 C C   . PHE B 2 152 ? -31.118 -49.553 40.062 1.00 20.95 ? 152 PHE B C   1 
ATOM   2788 O O   . PHE B 2 152 ? -32.005 -50.356 40.368 1.00 19.38 ? 152 PHE B O   1 
ATOM   2789 C CB  . PHE B 2 152 ? -29.159 -49.753 41.592 1.00 13.11 ? 152 PHE B CB  1 
ATOM   2790 C CG  . PHE B 2 152 ? -28.092 -49.908 40.564 1.00 15.89 ? 152 PHE B CG  1 
ATOM   2791 C CD1 . PHE B 2 152 ? -28.068 -51.013 39.720 1.00 22.11 ? 152 PHE B CD1 1 
ATOM   2792 C CD2 . PHE B 2 152 ? -27.121 -48.924 40.410 1.00 19.46 ? 152 PHE B CD2 1 
ATOM   2793 C CE1 . PHE B 2 152 ? -27.075 -51.143 38.747 1.00 25.92 ? 152 PHE B CE1 1 
ATOM   2794 C CE2 . PHE B 2 152 ? -26.131 -49.043 39.446 1.00 21.94 ? 152 PHE B CE2 1 
ATOM   2795 C CZ  . PHE B 2 152 ? -26.111 -50.156 38.612 1.00 19.08 ? 152 PHE B CZ  1 
ATOM   2796 N N   . PRO B 2 153 ? -30.836 -49.252 38.787 1.00 18.72 ? 153 PRO B N   1 
ATOM   2797 C CA  . PRO B 2 153 ? -29.946 -48.189 38.316 1.00 21.36 ? 153 PRO B CA  1 
ATOM   2798 C C   . PRO B 2 153 ? -30.716 -46.878 38.204 1.00 17.96 ? 153 PRO B C   1 
ATOM   2799 O O   . PRO B 2 153 ? -31.888 -46.849 38.551 1.00 17.48 ? 153 PRO B O   1 
ATOM   2800 C CB  . PRO B 2 153 ? -29.603 -48.662 36.902 1.00 25.48 ? 153 PRO B CB  1 
ATOM   2801 C CG  . PRO B 2 153 ? -30.880 -49.274 36.439 1.00 18.65 ? 153 PRO B CG  1 
ATOM   2802 C CD  . PRO B 2 153 ? -31.386 -50.026 37.658 1.00 17.77 ? 153 PRO B CD  1 
ATOM   2803 N N   . GLU B 2 154 ? -30.068 -45.822 37.721 1.00 21.63 ? 154 GLU B N   1 
ATOM   2804 C CA  . GLU B 2 154 ? -30.766 -44.627 37.269 1.00 17.03 ? 154 GLU B CA  1 
ATOM   2805 C C   . GLU B 2 154 ? -31.665 -45.052 36.105 1.00 21.54 ? 154 GLU B C   1 
ATOM   2806 O O   . GLU B 2 154 ? -31.455 -46.119 35.514 1.00 21.15 ? 154 GLU B O   1 
ATOM   2807 C CB  . GLU B 2 154 ? -29.759 -43.564 36.823 1.00 18.87 ? 154 GLU B CB  1 
ATOM   2808 C CG  . GLU B 2 154 ? -29.229 -42.662 37.953 1.00 21.96 ? 154 GLU B CG  1 
ATOM   2809 C CD  . GLU B 2 154 ? -29.990 -41.335 38.066 1.00 26.10 ? 154 GLU B CD  1 
ATOM   2810 O OE1 . GLU B 2 154 ? -29.550 -40.344 37.450 1.00 31.34 ? 154 GLU B OE1 1 
ATOM   2811 O OE2 . GLU B 2 154 ? -31.025 -41.278 38.773 1.00 25.81 ? 154 GLU B OE2 1 
ATOM   2812 N N   . PRO B 2 155 ? -32.681 -44.236 35.769 1.00 22.65 ? 155 PRO B N   1 
ATOM   2813 C CA  . PRO B 2 155 ? -33.078 -42.954 36.355 1.00 23.57 ? 155 PRO B CA  1 
ATOM   2814 C C   . PRO B 2 155 ? -34.213 -43.151 37.338 1.00 21.79 ? 155 PRO B C   1 
ATOM   2815 O O   . PRO B 2 155 ? -34.746 -44.261 37.459 1.00 22.62 ? 155 PRO B O   1 
ATOM   2816 C CB  . PRO B 2 155 ? -33.608 -42.191 35.142 1.00 15.11 ? 155 PRO B CB  1 
ATOM   2817 C CG  . PRO B 2 155 ? -34.251 -43.242 34.348 1.00 13.05 ? 155 PRO B CG  1 
ATOM   2818 C CD  . PRO B 2 155 ? -33.478 -44.521 34.569 1.00 19.37 ? 155 PRO B CD  1 
ATOM   2819 N N   . VAL B 2 156 ? -34.575 -42.082 38.032 1.00 17.53 ? 156 VAL B N   1 
ATOM   2820 C CA  . VAL B 2 156 ? -35.785 -42.083 38.829 1.00 19.24 ? 156 VAL B CA  1 
ATOM   2821 C C   . VAL B 2 156 ? -36.513 -40.790 38.509 1.00 18.02 ? 156 VAL B C   1 
ATOM   2822 O O   . VAL B 2 156 ? -35.883 -39.770 38.262 1.00 21.34 ? 156 VAL B O   1 
ATOM   2823 C CB  . VAL B 2 156 ? -35.482 -42.246 40.345 1.00 22.43 ? 156 VAL B CB  1 
ATOM   2824 C CG1 . VAL B 2 156 ? -34.741 -41.039 40.894 1.00 16.70 ? 156 VAL B CG1 1 
ATOM   2825 C CG2 . VAL B 2 156 ? -36.750 -42.469 41.113 1.00 21.24 ? 156 VAL B CG2 1 
ATOM   2826 N N   . THR B 2 157 ? -37.841 -40.817 38.469 1.00 21.49 ? 157 THR B N   1 
ATOM   2827 C CA  . THR B 2 157 ? -38.576 -39.584 38.197 1.00 16.73 ? 157 THR B CA  1 
ATOM   2828 C C   . THR B 2 157 ? -39.246 -39.079 39.458 1.00 19.46 ? 157 THR B C   1 
ATOM   2829 O O   . THR B 2 157 ? -39.700 -39.855 40.293 1.00 20.31 ? 157 THR B O   1 
ATOM   2830 C CB  . THR B 2 157 ? -39.601 -39.713 37.034 1.00 23.56 ? 157 THR B CB  1 
ATOM   2831 O OG1 . THR B 2 157 ? -40.606 -40.673 37.371 1.00 36.43 ? 157 THR B OG1 1 
ATOM   2832 C CG2 . THR B 2 157 ? -38.914 -40.161 35.768 1.00 25.01 ? 157 THR B CG2 1 
ATOM   2833 N N   . VAL B 2 158 ? -39.266 -37.764 39.606 1.00 19.67 ? 158 VAL B N   1 
ATOM   2834 C CA  . VAL B 2 158 ? -39.910 -37.144 40.739 1.00 18.35 ? 158 VAL B CA  1 
ATOM   2835 C C   . VAL B 2 158 ? -40.735 -35.986 40.230 1.00 23.78 ? 158 VAL B C   1 
ATOM   2836 O O   . VAL B 2 158 ? -40.251 -35.165 39.455 1.00 21.87 ? 158 VAL B O   1 
ATOM   2837 C CB  . VAL B 2 158 ? -38.900 -36.593 41.761 1.00 16.09 ? 158 VAL B CB  1 
ATOM   2838 C CG1 . VAL B 2 158 ? -39.638 -35.930 42.922 1.00 15.00 ? 158 VAL B CG1 1 
ATOM   2839 C CG2 . VAL B 2 158 ? -37.995 -37.689 42.263 1.00 19.45 ? 158 VAL B CG2 1 
ATOM   2840 N N   . SER B 2 159 ? -41.986 -35.925 40.675 1.00 20.97 ? 159 SER B N   1 
ATOM   2841 C CA  . SER B 2 159 ? -42.821 -34.770 40.438 1.00 20.16 ? 159 SER B CA  1 
ATOM   2842 C C   . SER B 2 159 ? -43.507 -34.430 41.748 1.00 22.69 ? 159 SER B C   1 
ATOM   2843 O O   . SER B 2 159 ? -43.439 -35.192 42.715 1.00 19.16 ? 159 SER B O   1 
ATOM   2844 C CB  . SER B 2 159 ? -43.851 -35.048 39.341 1.00 20.49 ? 159 SER B CB  1 
ATOM   2845 O OG  . SER B 2 159 ? -44.848 -35.930 39.802 1.00 28.82 ? 159 SER B OG  1 
ATOM   2846 N N   . TRP B 2 160 ? -44.155 -33.273 41.782 1.00 21.18 ? 160 TRP B N   1 
ATOM   2847 C CA  . TRP B 2 160 ? -44.860 -32.845 42.967 1.00 19.95 ? 160 TRP B CA  1 
ATOM   2848 C C   . TRP B 2 160 ? -46.337 -32.625 42.687 1.00 18.66 ? 160 TRP B C   1 
ATOM   2849 O O   . TRP B 2 160 ? -46.705 -32.050 41.653 1.00 22.16 ? 160 TRP B O   1 
ATOM   2850 C CB  . TRP B 2 160 ? -44.203 -31.598 43.516 1.00 17.70 ? 160 TRP B CB  1 
ATOM   2851 C CG  . TRP B 2 160 ? -42.868 -31.913 44.155 1.00 24.03 ? 160 TRP B CG  1 
ATOM   2852 C CD1 . TRP B 2 160 ? -41.654 -32.001 43.535 1.00 16.15 ? 160 TRP B CD1 1 
ATOM   2853 C CD2 . TRP B 2 160 ? -42.629 -32.181 45.543 1.00 18.59 ? 160 TRP B CD2 1 
ATOM   2854 N NE1 . TRP B 2 160 ? -40.678 -32.297 44.450 1.00 13.94 ? 160 TRP B NE1 1 
ATOM   2855 C CE2 . TRP B 2 160 ? -41.246 -32.411 45.689 1.00 16.88 ? 160 TRP B CE2 1 
ATOM   2856 C CE3 . TRP B 2 160 ? -43.449 -32.247 46.670 1.00 16.46 ? 160 TRP B CE3 1 
ATOM   2857 C CZ2 . TRP B 2 160 ? -40.667 -32.708 46.920 1.00 15.10 ? 160 TRP B CZ2 1 
ATOM   2858 C CZ3 . TRP B 2 160 ? -42.875 -32.540 47.887 1.00 18.66 ? 160 TRP B CZ3 1 
ATOM   2859 C CH2 . TRP B 2 160 ? -41.493 -32.763 48.006 1.00 19.69 ? 160 TRP B CH2 1 
ATOM   2860 N N   . ASN B 2 161 ? -47.168 -33.102 43.612 1.00 19.28 ? 161 ASN B N   1 
ATOM   2861 C CA  . ASN B 2 161 ? -48.621 -33.021 43.493 1.00 20.25 ? 161 ASN B CA  1 
ATOM   2862 C C   . ASN B 2 161 ? -49.080 -33.421 42.100 1.00 19.93 ? 161 ASN B C   1 
ATOM   2863 O O   . ASN B 2 161 ? -49.719 -32.644 41.394 1.00 23.15 ? 161 ASN B O   1 
ATOM   2864 C CB  . ASN B 2 161 ? -49.105 -31.624 43.866 1.00 16.38 ? 161 ASN B CB  1 
ATOM   2865 C CG  . ASN B 2 161 ? -48.811 -31.284 45.307 1.00 17.08 ? 161 ASN B CG  1 
ATOM   2866 O OD1 . ASN B 2 161 ? -48.247 -32.096 46.043 1.00 27.43 ? 161 ASN B OD1 1 
ATOM   2867 N ND2 . ASN B 2 161 ? -49.185 -30.082 45.725 1.00 17.61 ? 161 ASN B ND2 1 
ATOM   2868 N N   . SER B 2 162 ? -48.678 -34.621 41.697 1.00 21.14 ? 162 SER B N   1 
ATOM   2869 C CA  . SER B 2 162 ? -49.053 -35.215 40.405 1.00 26.07 ? 162 SER B CA  1 
ATOM   2870 C C   . SER B 2 162 ? -48.832 -34.329 39.194 1.00 18.87 ? 162 SER B C   1 
ATOM   2871 O O   . SER B 2 162 ? -49.602 -34.385 38.249 1.00 36.62 ? 162 SER B O   1 
ATOM   2872 C CB  . SER B 2 162 ? -50.512 -35.677 40.429 1.00 27.29 ? 162 SER B CB  1 
ATOM   2873 O OG  . SER B 2 162 ? -50.739 -36.547 41.526 1.00 25.29 ? 162 SER B OG  1 
ATOM   2874 N N   . GLY B 2 163 ? -47.787 -33.517 39.218 1.00 22.11 ? 163 GLY B N   1 
ATOM   2875 C CA  . GLY B 2 163 ? -47.521 -32.624 38.110 1.00 20.77 ? 163 GLY B CA  1 
ATOM   2876 C C   . GLY B 2 163 ? -48.050 -31.206 38.298 1.00 23.33 ? 163 GLY B C   1 
ATOM   2877 O O   . GLY B 2 163 ? -47.627 -30.304 37.582 1.00 25.72 ? 163 GLY B O   1 
ATOM   2878 N N   . ALA B 2 164 ? -48.957 -30.995 39.252 1.00 20.02 ? 164 ALA B N   1 
ATOM   2879 C CA  . ALA B 2 164 ? -49.539 -29.664 39.463 1.00 18.11 ? 164 ALA B CA  1 
ATOM   2880 C C   . ALA B 2 164 ? -48.585 -28.646 40.083 1.00 23.49 ? 164 ALA B C   1 
ATOM   2881 O O   . ALA B 2 164 ? -48.833 -27.451 39.996 1.00 32.06 ? 164 ALA B O   1 
ATOM   2882 C CB  . ALA B 2 164 ? -50.817 -29.754 40.306 1.00 13.00 ? 164 ALA B CB  1 
ATOM   2883 N N   . LEU B 2 165 ? -47.528 -29.111 40.745 1.00 22.12 ? 165 LEU B N   1 
ATOM   2884 C CA  . LEU B 2 165 ? -46.544 -28.203 41.344 1.00 21.95 ? 165 LEU B CA  1 
ATOM   2885 C C   . LEU B 2 165 ? -45.185 -28.341 40.651 1.00 17.74 ? 165 LEU B C   1 
ATOM   2886 O O   . LEU B 2 165 ? -44.559 -29.407 40.694 1.00 18.03 ? 165 LEU B O   1 
ATOM   2887 C CB  . LEU B 2 165 ? -46.420 -28.433 42.859 1.00 14.27 ? 165 LEU B CB  1 
ATOM   2888 C CG  . LEU B 2 165 ? -45.419 -27.559 43.632 1.00 24.90 ? 165 LEU B CG  1 
ATOM   2889 C CD1 . LEU B 2 165 ? -45.682 -26.072 43.468 1.00 17.26 ? 165 LEU B CD1 1 
ATOM   2890 C CD2 . LEU B 2 165 ? -45.381 -27.917 45.122 1.00 21.78 ? 165 LEU B CD2 1 
ATOM   2891 N N   . THR B 2 166 ? -44.742 -27.267 40.003 1.00 19.20 ? 166 THR B N   1 
ATOM   2892 C CA  . THR B 2 166 ? -43.482 -27.279 39.259 1.00 18.42 ? 166 THR B CA  1 
ATOM   2893 C C   . THR B 2 166 ? -42.627 -26.062 39.561 1.00 20.89 ? 166 THR B C   1 
ATOM   2894 O O   . THR B 2 166 ? -41.412 -26.085 39.411 1.00 25.81 ? 166 THR B O   1 
ATOM   2895 C CB  . THR B 2 166 ? -43.712 -27.313 37.730 1.00 21.29 ? 166 THR B CB  1 
ATOM   2896 O OG1 . THR B 2 166 ? -44.681 -26.321 37.363 1.00 20.32 ? 166 THR B OG1 1 
ATOM   2897 C CG2 . THR B 2 166 ? -44.195 -28.684 37.291 1.00 18.73 ? 166 THR B CG2 1 
ATOM   2898 N N   . SER B 2 167 ? -43.271 -24.985 39.971 1.00 19.27 ? 167 SER B N   1 
ATOM   2899 C CA  . SER B 2 167 ? -42.551 -23.780 40.285 1.00 20.31 ? 167 SER B CA  1 
ATOM   2900 C C   . SER B 2 167 ? -41.780 -23.949 41.618 1.00 30.44 ? 167 SER B C   1 
ATOM   2901 O O   . SER B 2 167 ? -42.344 -24.333 42.652 1.00 18.07 ? 167 SER B O   1 
ATOM   2902 C CB  . SER B 2 167 ? -43.534 -22.608 40.317 1.00 16.69 ? 167 SER B CB  1 
ATOM   2903 O OG  . SER B 2 167 ? -43.103 -21.601 41.209 1.00 34.58 ? 167 SER B OG  1 
ATOM   2904 N N   . GLY B 2 168 ? -40.478 -23.681 41.579 1.00 31.12 ? 168 GLY B N   1 
ATOM   2905 C CA  . GLY B 2 168 ? -39.663 -23.751 42.778 1.00 18.91 ? 168 GLY B CA  1 
ATOM   2906 C C   . GLY B 2 168 ? -39.193 -25.163 43.059 1.00 24.67 ? 168 GLY B C   1 
ATOM   2907 O O   . GLY B 2 168 ? -38.635 -25.429 44.122 1.00 22.51 ? 168 GLY B O   1 
ATOM   2908 N N   . VAL B 2 169 ? -39.426 -26.070 42.109 1.00 24.05 ? 169 VAL B N   1 
ATOM   2909 C CA  . VAL B 2 169 ? -38.959 -27.449 42.245 1.00 22.06 ? 169 VAL B CA  1 
ATOM   2910 C C   . VAL B 2 169 ? -37.520 -27.660 41.757 1.00 25.56 ? 169 VAL B C   1 
ATOM   2911 O O   . VAL B 2 169 ? -37.175 -27.352 40.605 1.00 28.90 ? 169 VAL B O   1 
ATOM   2912 C CB  . VAL B 2 169 ? -39.858 -28.428 41.502 1.00 20.84 ? 169 VAL B CB  1 
ATOM   2913 C CG1 . VAL B 2 169 ? -39.306 -29.857 41.629 1.00 22.76 ? 169 VAL B CG1 1 
ATOM   2914 C CG2 . VAL B 2 169 ? -41.281 -28.335 42.034 1.00 18.95 ? 169 VAL B CG2 1 
ATOM   2915 N N   . HIS B 2 170 ? -36.681 -28.197 42.633 1.00 20.04 ? 170 HIS B N   1 
ATOM   2916 C CA  . HIS B 2 170 ? -35.346 -28.629 42.229 1.00 16.95 ? 170 HIS B CA  1 
ATOM   2917 C C   . HIS B 2 170 ? -35.179 -30.091 42.550 1.00 19.92 ? 170 HIS B C   1 
ATOM   2918 O O   . HIS B 2 170 ? -35.241 -30.500 43.715 1.00 18.51 ? 170 HIS B O   1 
ATOM   2919 C CB  . HIS B 2 170 ? -34.262 -27.832 42.946 1.00 12.46 ? 170 HIS B CB  1 
ATOM   2920 C CG  . HIS B 2 170 ? -34.327 -26.369 42.655 1.00 17.84 ? 170 HIS B CG  1 
ATOM   2921 N ND1 . HIS B 2 170 ? -34.252 -25.872 41.381 1.00 18.02 ? 170 HIS B ND1 1 
ATOM   2922 C CD2 . HIS B 2 170 ? -34.489 -25.311 43.484 1.00 15.98 ? 170 HIS B CD2 1 
ATOM   2923 C CE1 . HIS B 2 170 ? -34.356 -24.548 41.428 1.00 18.75 ? 170 HIS B CE1 1 
ATOM   2924 N NE2 . HIS B 2 170 ? -34.495 -24.189 42.686 1.00 21.48 ? 170 HIS B NE2 1 
ATOM   2925 N N   . THR B 2 171 ? -34.977 -30.889 41.518 1.00 17.27 ? 171 THR B N   1 
ATOM   2926 C CA  . THR B 2 171 ? -34.642 -32.281 41.742 1.00 20.42 ? 171 THR B CA  1 
ATOM   2927 C C   . THR B 2 171 ? -33.167 -32.475 41.424 1.00 20.58 ? 171 THR B C   1 
ATOM   2928 O O   . THR B 2 171 ? -32.731 -32.270 40.292 1.00 22.09 ? 171 THR B O   1 
ATOM   2929 C CB  . THR B 2 171 ? -35.511 -33.197 40.896 1.00 16.58 ? 171 THR B CB  1 
ATOM   2930 O OG1 . THR B 2 171 ? -36.871 -33.067 41.329 1.00 22.57 ? 171 THR B OG1 1 
ATOM   2931 C CG2 . THR B 2 171 ? -35.051 -34.641 41.046 1.00 16.48 ? 171 THR B CG2 1 
ATOM   2932 N N   . PHE B 2 172 ? -32.394 -32.852 42.433 1.00 17.37 ? 172 PHE B N   1 
ATOM   2933 C CA  . PHE B 2 172 ? -30.942 -32.912 42.285 1.00 17.15 ? 172 PHE B CA  1 
ATOM   2934 C C   . PHE B 2 172 ? -30.473 -34.076 41.403 1.00 23.87 ? 172 PHE B C   1 
ATOM   2935 O O   . PHE B 2 172 ? -31.131 -35.118 41.311 1.00 19.02 ? 172 PHE B O   1 
ATOM   2936 C CB  . PHE B 2 172 ? -30.255 -32.862 43.660 1.00 14.60 ? 172 PHE B CB  1 
ATOM   2937 C CG  . PHE B 2 172 ? -30.385 -31.523 44.324 1.00 16.43 ? 172 PHE B CG  1 
ATOM   2938 C CD1 . PHE B 2 172 ? -29.617 -30.449 43.897 1.00 23.73 ? 172 PHE B CD1 1 
ATOM   2939 C CD2 . PHE B 2 172 ? -31.308 -31.311 45.320 1.00 9.79  ? 172 PHE B CD2 1 
ATOM   2940 C CE1 . PHE B 2 172 ? -29.755 -29.189 44.481 1.00 23.21 ? 172 PHE B CE1 1 
ATOM   2941 C CE2 . PHE B 2 172 ? -31.443 -30.060 45.905 1.00 15.36 ? 172 PHE B CE2 1 
ATOM   2942 C CZ  . PHE B 2 172 ? -30.673 -29.003 45.491 1.00 14.68 ? 172 PHE B CZ  1 
ATOM   2943 N N   . PRO B 2 173 ? -29.366 -33.872 40.686 1.00 19.06 ? 173 PRO B N   1 
ATOM   2944 C CA  . PRO B 2 173 ? -28.743 -34.998 39.997 1.00 21.35 ? 173 PRO B CA  1 
ATOM   2945 C C   . PRO B 2 173 ? -28.399 -36.057 41.034 1.00 24.84 ? 173 PRO B C   1 
ATOM   2946 O O   . PRO B 2 173 ? -27.965 -35.695 42.134 1.00 22.76 ? 173 PRO B O   1 
ATOM   2947 C CB  . PRO B 2 173 ? -27.474 -34.376 39.416 1.00 19.98 ? 173 PRO B CB  1 
ATOM   2948 C CG  . PRO B 2 173 ? -27.840 -32.967 39.173 1.00 17.65 ? 173 PRO B CG  1 
ATOM   2949 C CD  . PRO B 2 173 ? -28.751 -32.588 40.317 1.00 23.02 ? 173 PRO B CD  1 
ATOM   2950 N N   . ALA B 2 174 ? -28.626 -37.328 40.715 1.00 22.53 ? 174 ALA B N   1 
ATOM   2951 C CA  . ALA B 2 174 ? -28.296 -38.401 41.641 1.00 19.28 ? 174 ALA B CA  1 
ATOM   2952 C C   . ALA B 2 174 ? -26.792 -38.471 41.862 1.00 24.28 ? 174 ALA B C   1 
ATOM   2953 O O   . ALA B 2 174 ? -25.999 -38.060 41.015 1.00 22.04 ? 174 ALA B O   1 
ATOM   2954 C CB  . ALA B 2 174 ? -28.797 -39.731 41.114 1.00 21.77 ? 174 ALA B CB  1 
ATOM   2955 N N   . VAL B 2 175 ? -26.412 -38.974 43.024 1.00 26.51 ? 175 VAL B N   1 
ATOM   2956 C CA  . VAL B 2 175 ? -25.030 -39.265 43.312 1.00 21.18 ? 175 VAL B CA  1 
ATOM   2957 C C   . VAL B 2 175 ? -24.934 -40.742 43.632 1.00 22.99 ? 175 VAL B C   1 
ATOM   2958 O O   . VAL B 2 175 ? -25.871 -41.342 44.171 1.00 26.29 ? 175 VAL B O   1 
ATOM   2959 C CB  . VAL B 2 175 ? -24.496 -38.430 44.489 1.00 28.56 ? 175 VAL B CB  1 
ATOM   2960 C CG1 . VAL B 2 175 ? -24.800 -36.935 44.267 1.00 19.99 ? 175 VAL B CG1 1 
ATOM   2961 C CG2 . VAL B 2 175 ? -25.068 -38.928 45.822 1.00 26.42 ? 175 VAL B CG2 1 
ATOM   2962 N N   . LEU B 2 176 ? -23.812 -41.337 43.258 1.00 23.81 ? 176 LEU B N   1 
ATOM   2963 C CA  . LEU B 2 176 ? -23.543 -42.735 43.541 1.00 20.18 ? 176 LEU B CA  1 
ATOM   2964 C C   . LEU B 2 176 ? -22.892 -42.817 44.925 1.00 24.92 ? 176 LEU B C   1 
ATOM   2965 O O   . LEU B 2 176 ? -21.934 -42.102 45.217 1.00 26.88 ? 176 LEU B O   1 
ATOM   2966 C CB  . LEU B 2 176 ? -22.617 -43.302 42.465 1.00 17.98 ? 176 LEU B CB  1 
ATOM   2967 C CG  . LEU B 2 176 ? -22.474 -44.826 42.418 1.00 30.01 ? 176 LEU B CG  1 
ATOM   2968 C CD1 . LEU B 2 176 ? -23.790 -45.501 41.988 1.00 20.75 ? 176 LEU B CD1 1 
ATOM   2969 C CD2 . LEU B 2 176 ? -21.336 -45.226 41.500 1.00 23.94 ? 176 LEU B CD2 1 
ATOM   2970 N N   . GLN B 2 177 ? -23.428 -43.665 45.790 1.00 24.88 ? 177 GLN B N   1 
ATOM   2971 C CA  . GLN B 2 177 ? -22.870 -43.827 47.128 1.00 20.51 ? 177 GLN B CA  1 
ATOM   2972 C C   . GLN B 2 177 ? -21.833 -44.957 47.095 1.00 24.57 ? 177 GLN B C   1 
ATOM   2973 O O   . GLN B 2 177 ? -21.692 -45.660 46.091 1.00 22.35 ? 177 GLN B O   1 
ATOM   2974 C CB  . GLN B 2 177 ? -23.987 -44.123 48.137 1.00 21.79 ? 177 GLN B CB  1 
ATOM   2975 C CG  . GLN B 2 177 ? -25.109 -43.065 48.179 1.00 23.05 ? 177 GLN B CG  1 
ATOM   2976 C CD  . GLN B 2 177 ? -26.413 -43.575 48.823 1.00 25.52 ? 177 GLN B CD  1 
ATOM   2977 O OE1 . GLN B 2 177 ? -26.846 -43.072 49.858 1.00 27.07 ? 177 GLN B OE1 1 
ATOM   2978 N NE2 . GLN B 2 177 ? -27.041 -44.568 48.198 1.00 25.59 ? 177 GLN B NE2 1 
ATOM   2979 N N   . SER B 2 178 ? -21.104 -45.134 48.190 1.00 31.24 ? 178 SER B N   1 
ATOM   2980 C CA  . SER B 2 178 ? -20.068 -46.163 48.242 1.00 32.59 ? 178 SER B CA  1 
ATOM   2981 C C   . SER B 2 178 ? -20.708 -47.555 48.153 1.00 30.45 ? 178 SER B C   1 
ATOM   2982 O O   . SER B 2 178 ? -20.070 -48.537 47.764 1.00 33.95 ? 178 SER B O   1 
ATOM   2983 C CB  . SER B 2 178 ? -19.231 -46.030 49.523 1.00 29.58 ? 178 SER B CB  1 
ATOM   2984 O OG  . SER B 2 178 ? -19.949 -46.506 50.650 1.00 33.16 ? 178 SER B OG  1 
ATOM   2985 N N   . SER B 2 179 ? -21.982 -47.629 48.516 1.00 24.73 ? 179 SER B N   1 
ATOM   2986 C CA  . SER B 2 179 ? -22.735 -48.868 48.407 1.00 25.97 ? 179 SER B CA  1 
ATOM   2987 C C   . SER B 2 179 ? -22.947 -49.268 46.950 1.00 25.92 ? 179 SER B C   1 
ATOM   2988 O O   . SER B 2 179 ? -23.374 -50.381 46.673 1.00 21.15 ? 179 SER B O   1 
ATOM   2989 C CB  . SER B 2 179 ? -24.095 -48.696 49.054 1.00 17.93 ? 179 SER B CB  1 
ATOM   2990 O OG  . SER B 2 179 ? -24.878 -47.804 48.279 1.00 23.75 ? 179 SER B OG  1 
ATOM   2991 N N   . GLY B 2 180 ? -22.667 -48.356 46.025 1.00 20.50 ? 180 GLY B N   1 
ATOM   2992 C CA  . GLY B 2 180 ? -22.914 -48.617 44.621 1.00 22.40 ? 180 GLY B CA  1 
ATOM   2993 C C   . GLY B 2 180 ? -24.361 -48.331 44.246 1.00 22.04 ? 180 GLY B C   1 
ATOM   2994 O O   . GLY B 2 180 ? -24.804 -48.696 43.156 1.00 21.92 ? 180 GLY B O   1 
ATOM   2995 N N   . LEU B 2 181 ? -25.083 -47.678 45.156 1.00 16.71 ? 181 LEU B N   1 
ATOM   2996 C CA  . LEU B 2 181 ? -26.489 -47.344 44.981 1.00 15.76 ? 181 LEU B CA  1 
ATOM   2997 C C   . LEU B 2 181 ? -26.641 -45.837 44.899 1.00 19.72 ? 181 LEU B C   1 
ATOM   2998 O O   . LEU B 2 181 ? -25.849 -45.103 45.495 1.00 21.62 ? 181 LEU B O   1 
ATOM   2999 C CB  . LEU B 2 181 ? -27.302 -47.851 46.171 1.00 20.69 ? 181 LEU B CB  1 
ATOM   3000 C CG  . LEU B 2 181 ? -27.391 -49.364 46.372 1.00 19.25 ? 181 LEU B CG  1 
ATOM   3001 C CD1 . LEU B 2 181 ? -28.310 -49.670 47.530 1.00 16.33 ? 181 LEU B CD1 1 
ATOM   3002 C CD2 . LEU B 2 181 ? -27.890 -50.019 45.096 1.00 13.62 ? 181 LEU B CD2 1 
ATOM   3003 N N   . TYR B 2 182 ? -27.654 -45.376 44.168 1.00 17.37 ? 182 TYR B N   1 
ATOM   3004 C CA  . TYR B 2 182 ? -27.865 -43.946 43.978 1.00 17.28 ? 182 TYR B CA  1 
ATOM   3005 C C   . TYR B 2 182 ? -28.778 -43.329 45.018 1.00 16.97 ? 182 TYR B C   1 
ATOM   3006 O O   . TYR B 2 182 ? -29.637 -43.994 45.591 1.00 15.31 ? 182 TYR B O   1 
ATOM   3007 C CB  . TYR B 2 182 ? -28.445 -43.643 42.598 1.00 15.15 ? 182 TYR B CB  1 
ATOM   3008 C CG  . TYR B 2 182 ? -27.500 -43.867 41.445 1.00 21.90 ? 182 TYR B CG  1 
ATOM   3009 C CD1 . TYR B 2 182 ? -27.502 -45.068 40.751 1.00 13.14 ? 182 TYR B CD1 1 
ATOM   3010 C CD2 . TYR B 2 182 ? -26.619 -42.865 41.034 1.00 17.54 ? 182 TYR B CD2 1 
ATOM   3011 C CE1 . TYR B 2 182 ? -26.663 -45.271 39.703 1.00 18.60 ? 182 TYR B CE1 1 
ATOM   3012 C CE2 . TYR B 2 182 ? -25.765 -43.065 39.979 1.00 11.50 ? 182 TYR B CE2 1 
ATOM   3013 C CZ  . TYR B 2 182 ? -25.794 -44.273 39.317 1.00 19.57 ? 182 TYR B CZ  1 
ATOM   3014 O OH  . TYR B 2 182 ? -24.955 -44.503 38.255 1.00 24.77 ? 182 TYR B OH  1 
ATOM   3015 N N   . SER B 2 183 ? -28.601 -42.030 45.214 1.00 15.81 ? 183 SER B N   1 
ATOM   3016 C CA  . SER B 2 183 ? -29.445 -41.268 46.104 1.00 21.78 ? 183 SER B CA  1 
ATOM   3017 C C   . SER B 2 183 ? -29.647 -39.836 45.555 1.00 23.36 ? 183 SER B C   1 
ATOM   3018 O O   . SER B 2 183 ? -28.733 -39.255 44.978 1.00 25.85 ? 183 SER B O   1 
ATOM   3019 C CB  . SER B 2 183 ? -28.809 -41.247 47.491 1.00 16.11 ? 183 SER B CB  1 
ATOM   3020 O OG  . SER B 2 183 ? -29.563 -40.466 48.391 1.00 30.40 ? 183 SER B OG  1 
ATOM   3021 N N   . LEU B 2 184 ? -30.850 -39.285 45.700 1.00 24.05 ? 184 LEU B N   1 
ATOM   3022 C CA  . LEU B 2 184 ? -31.086 -37.882 45.373 1.00 19.41 ? 184 LEU B CA  1 
ATOM   3023 C C   . LEU B 2 184 ? -32.133 -37.258 46.288 1.00 20.28 ? 184 LEU B C   1 
ATOM   3024 O O   . LEU B 2 184 ? -32.936 -37.965 46.902 1.00 20.71 ? 184 LEU B O   1 
ATOM   3025 C CB  . LEU B 2 184 ? -31.487 -37.708 43.899 1.00 20.90 ? 184 LEU B CB  1 
ATOM   3026 C CG  . LEU B 2 184 ? -32.821 -38.213 43.316 1.00 18.39 ? 184 LEU B CG  1 
ATOM   3027 C CD1 . LEU B 2 184 ? -34.009 -37.411 43.781 1.00 19.56 ? 184 LEU B CD1 1 
ATOM   3028 C CD2 . LEU B 2 184 ? -32.771 -38.198 41.800 1.00 20.70 ? 184 LEU B CD2 1 
ATOM   3029 N N   . SER B 2 185 ? -32.122 -35.930 46.363 1.00 16.30 ? 185 SER B N   1 
ATOM   3030 C CA  . SER B 2 185 ? -33.213 -35.178 46.977 1.00 16.71 ? 185 SER B CA  1 
ATOM   3031 C C   . SER B 2 185 ? -33.935 -34.319 45.947 1.00 20.76 ? 185 SER B C   1 
ATOM   3032 O O   . SER B 2 185 ? -33.341 -33.857 44.972 1.00 20.49 ? 185 SER B O   1 
ATOM   3033 C CB  . SER B 2 185 ? -32.719 -34.288 48.117 1.00 16.39 ? 185 SER B CB  1 
ATOM   3034 O OG  . SER B 2 185 ? -32.508 -35.031 49.309 1.00 30.82 ? 185 SER B OG  1 
ATOM   3035 N N   . SER B 2 186 ? -35.228 -34.118 46.170 1.00 16.71 ? 186 SER B N   1 
ATOM   3036 C CA  . SER B 2 186 ? -36.015 -33.219 45.359 1.00 12.34 ? 186 SER B CA  1 
ATOM   3037 C C   . SER B 2 186 ? -36.628 -32.271 46.333 1.00 15.85 ? 186 SER B C   1 
ATOM   3038 O O   . SER B 2 186 ? -37.192 -32.710 47.319 1.00 21.48 ? 186 SER B O   1 
ATOM   3039 C CB  . SER B 2 186 ? -37.122 -33.978 44.635 1.00 17.80 ? 186 SER B CB  1 
ATOM   3040 O OG  . SER B 2 186 ? -37.821 -33.113 43.767 1.00 16.04 ? 186 SER B OG  1 
ATOM   3041 N N   . VAL B 2 187 ? -36.520 -30.974 46.077 1.00 15.67 ? 187 VAL B N   1 
ATOM   3042 C CA  . VAL B 2 187 ? -37.029 -29.991 47.018 1.00 18.66 ? 187 VAL B CA  1 
ATOM   3043 C C   . VAL B 2 187 ? -37.905 -28.999 46.311 1.00 13.87 ? 187 VAL B C   1 
ATOM   3044 O O   . VAL B 2 187 ? -37.871 -28.887 45.088 1.00 16.88 ? 187 VAL B O   1 
ATOM   3045 C CB  . VAL B 2 187 ? -35.890 -29.220 47.766 1.00 16.15 ? 187 VAL B CB  1 
ATOM   3046 C CG1 . VAL B 2 187 ? -34.973 -30.193 48.467 1.00 16.16 ? 187 VAL B CG1 1 
ATOM   3047 C CG2 . VAL B 2 187 ? -35.105 -28.339 46.802 1.00 14.98 ? 187 VAL B CG2 1 
ATOM   3048 N N   . VAL B 2 188 ? -38.690 -28.273 47.092 1.00 10.67 ? 188 VAL B N   1 
ATOM   3049 C CA  . VAL B 2 188 ? -39.545 -27.245 46.547 1.00 9.96  ? 188 VAL B CA  1 
ATOM   3050 C C   . VAL B 2 188 ? -39.707 -26.202 47.622 1.00 19.86 ? 188 VAL B C   1 
ATOM   3051 O O   . VAL B 2 188 ? -39.680 -26.525 48.821 1.00 19.50 ? 188 VAL B O   1 
ATOM   3052 C CB  . VAL B 2 188 ? -40.916 -27.814 46.113 1.00 17.21 ? 188 VAL B CB  1 
ATOM   3053 C CG1 . VAL B 2 188 ? -41.614 -28.522 47.267 1.00 13.10 ? 188 VAL B CG1 1 
ATOM   3054 C CG2 . VAL B 2 188 ? -41.810 -26.721 45.524 1.00 17.98 ? 188 VAL B CG2 1 
ATOM   3055 N N   . THR B 2 189 ? -39.822 -24.946 47.206 1.00 13.41 ? 189 THR B N   1 
ATOM   3056 C CA  . THR B 2 189 ? -40.143 -23.882 48.137 1.00 18.21 ? 189 THR B CA  1 
ATOM   3057 C C   . THR B 2 189 ? -41.585 -23.405 47.935 1.00 17.24 ? 189 THR B C   1 
ATOM   3058 O O   . THR B 2 189 ? -42.054 -23.236 46.816 1.00 20.76 ? 189 THR B O   1 
ATOM   3059 C CB  . THR B 2 189 ? -39.128 -22.712 48.077 1.00 21.30 ? 189 THR B CB  1 
ATOM   3060 O OG1 . THR B 2 189 ? -38.895 -22.325 46.713 1.00 20.41 ? 189 THR B OG1 1 
ATOM   3061 C CG2 . THR B 2 189 ? -37.820 -23.138 48.691 1.00 16.38 ? 189 THR B CG2 1 
ATOM   3062 N N   . VAL B 2 190 ? -42.289 -23.219 49.040 1.00 17.53 ? 190 VAL B N   1 
ATOM   3063 C CA  . VAL B 2 190 ? -43.699 -22.851 49.011 1.00 18.70 ? 190 VAL B CA  1 
ATOM   3064 C C   . VAL B 2 190 ? -43.943 -21.796 50.073 1.00 18.13 ? 190 VAL B C   1 
ATOM   3065 O O   . VAL B 2 190 ? -43.128 -21.637 50.987 1.00 25.15 ? 190 VAL B O   1 
ATOM   3066 C CB  . VAL B 2 190 ? -44.606 -24.078 49.299 1.00 21.41 ? 190 VAL B CB  1 
ATOM   3067 C CG1 . VAL B 2 190 ? -44.362 -25.182 48.266 1.00 12.80 ? 190 VAL B CG1 1 
ATOM   3068 C CG2 . VAL B 2 190 ? -44.388 -24.593 50.734 1.00 16.06 ? 190 VAL B CG2 1 
ATOM   3069 N N   . PRO B 2 191 ? -45.046 -21.049 49.951 1.00 19.63 ? 191 PRO B N   1 
ATOM   3070 C CA  . PRO B 2 191 ? -45.369 -20.133 51.049 1.00 26.71 ? 191 PRO B CA  1 
ATOM   3071 C C   . PRO B 2 191 ? -45.542 -20.912 52.348 1.00 21.06 ? 191 PRO B C   1 
ATOM   3072 O O   . PRO B 2 191 ? -46.199 -21.941 52.335 1.00 22.46 ? 191 PRO B O   1 
ATOM   3073 C CB  . PRO B 2 191 ? -46.705 -19.537 50.606 1.00 19.94 ? 191 PRO B CB  1 
ATOM   3074 C CG  . PRO B 2 191 ? -46.640 -19.586 49.113 1.00 14.63 ? 191 PRO B CG  1 
ATOM   3075 C CD  . PRO B 2 191 ? -45.975 -20.895 48.819 1.00 17.12 ? 191 PRO B CD  1 
ATOM   3076 N N   . SER B 2 192 ? -44.950 -20.447 53.441 1.00 19.73 ? 192 SER B N   1 
ATOM   3077 C CA  . SER B 2 192 ? -45.134 -21.131 54.713 1.00 28.31 ? 192 SER B CA  1 
ATOM   3078 C C   . SER B 2 192 ? -46.614 -21.150 55.127 1.00 24.49 ? 192 SER B C   1 
ATOM   3079 O O   . SER B 2 192 ? -47.063 -22.117 55.736 1.00 26.23 ? 192 SER B O   1 
ATOM   3080 C CB  . SER B 2 192 ? -44.255 -20.517 55.814 1.00 28.10 ? 192 SER B CB  1 
ATOM   3081 O OG  . SER B 2 192 ? -44.632 -19.180 56.087 1.00 32.77 ? 192 SER B OG  1 
ATOM   3082 N N   . SER B 2 193 ? -47.370 -20.103 54.774 1.00 21.74 ? 193 SER B N   1 
ATOM   3083 C CA  . SER B 2 193 ? -48.808 -20.041 55.107 1.00 22.43 ? 193 SER B CA  1 
ATOM   3084 C C   . SER B 2 193 ? -49.656 -21.134 54.458 1.00 21.16 ? 193 SER B C   1 
ATOM   3085 O O   . SER B 2 193 ? -50.799 -21.351 54.859 1.00 32.41 ? 193 SER B O   1 
ATOM   3086 C CB  . SER B 2 193 ? -49.427 -18.661 54.817 1.00 16.79 ? 193 SER B CB  1 
ATOM   3087 O OG  . SER B 2 193 ? -49.311 -18.288 53.452 1.00 24.71 ? 193 SER B OG  1 
ATOM   3088 N N   . SER B 2 194 ? -49.108 -21.829 53.471 1.00 20.53 ? 194 SER B N   1 
ATOM   3089 C CA  . SER B 2 194 ? -49.884 -22.848 52.782 1.00 20.13 ? 194 SER B CA  1 
ATOM   3090 C C   . SER B 2 194 ? -49.659 -24.224 53.389 1.00 30.39 ? 194 SER B C   1 
ATOM   3091 O O   . SER B 2 194 ? -50.333 -25.186 53.016 1.00 30.34 ? 194 SER B O   1 
ATOM   3092 C CB  . SER B 2 194 ? -49.540 -22.879 51.290 1.00 20.35 ? 194 SER B CB  1 
ATOM   3093 O OG  . SER B 2 194 ? -48.326 -23.584 51.079 1.00 25.36 ? 194 SER B OG  1 
ATOM   3094 N N   . LEU B 2 195 ? -48.702 -24.318 54.312 1.00 26.58 ? 195 LEU B N   1 
ATOM   3095 C CA  . LEU B 2 195 ? -48.369 -25.595 54.925 1.00 25.87 ? 195 LEU B CA  1 
ATOM   3096 C C   . LEU B 2 195 ? -49.546 -26.206 55.658 1.00 26.43 ? 195 LEU B C   1 
ATOM   3097 O O   . LEU B 2 195 ? -49.682 -27.421 55.704 1.00 38.12 ? 195 LEU B O   1 
ATOM   3098 C CB  . LEU B 2 195 ? -47.199 -25.456 55.884 1.00 22.86 ? 195 LEU B CB  1 
ATOM   3099 C CG  . LEU B 2 195 ? -45.838 -25.255 55.241 1.00 24.26 ? 195 LEU B CG  1 
ATOM   3100 C CD1 . LEU B 2 195 ? -44.795 -25.117 56.338 1.00 21.00 ? 195 LEU B CD1 1 
ATOM   3101 C CD2 . LEU B 2 195 ? -45.519 -26.411 54.312 1.00 23.10 ? 195 LEU B CD2 1 
ATOM   3102 N N   . GLY B 2 196 ? -50.394 -25.366 56.238 1.00 30.57 ? 196 GLY B N   1 
ATOM   3103 C CA  . GLY B 2 196 ? -51.580 -25.856 56.913 1.00 38.72 ? 196 GLY B CA  1 
ATOM   3104 C C   . GLY B 2 196 ? -52.657 -26.273 55.931 1.00 42.28 ? 196 GLY B C   1 
ATOM   3105 O O   . GLY B 2 196 ? -53.313 -27.300 56.101 1.00 47.69 ? 196 GLY B O   1 
ATOM   3106 N N   . THR B 2 197 ? -52.813 -25.473 54.884 1.00 37.51 ? 197 THR B N   1 
ATOM   3107 C CA  . THR B 2 197 ? -53.882 -25.643 53.910 1.00 40.13 ? 197 THR B CA  1 
ATOM   3108 C C   . THR B 2 197 ? -53.612 -26.730 52.865 1.00 38.31 ? 197 THR B C   1 
ATOM   3109 O O   . THR B 2 197 ? -54.462 -27.584 52.622 1.00 37.47 ? 197 THR B O   1 
ATOM   3110 C CB  . THR B 2 197 ? -54.128 -24.318 53.177 1.00 43.64 ? 197 THR B CB  1 
ATOM   3111 O OG1 . THR B 2 197 ? -54.320 -23.280 54.146 1.00 43.47 ? 197 THR B OG1 1 
ATOM   3112 C CG2 . THR B 2 197 ? -55.337 -24.417 52.249 1.00 40.52 ? 197 THR B CG2 1 
ATOM   3113 N N   . GLN B 2 198 ? -52.447 -26.706 52.263 1.00 36.34 ? 198 GLN B N   1 
ATOM   3114 C CA  . GLN B 2 198 ? -52.097 -27.527 51.123 1.00 25.05 ? 198 GLN B CA  1 
ATOM   3115 C C   . GLN B 2 198 ? -51.409 -28.828 51.459 1.00 24.49 ? 198 GLN B C   1 
ATOM   3116 O O   . GLN B 2 198 ? -50.657 -28.893 52.377 1.00 24.64 ? 198 GLN B O   1 
ATOM   3117 C CB  . GLN B 2 198 ? -51.170 -26.731 50.227 1.00 31.16 ? 198 GLN B CB  1 
ATOM   3118 C CG  . GLN B 2 198 ? -51.843 -25.727 49.353 1.00 38.14 ? 198 GLN B CG  1 
ATOM   3119 C CD  . GLN B 2 198 ? -52.751 -26.359 48.336 1.00 53.72 ? 198 GLN B CD  1 
ATOM   3120 O OE1 . GLN B 2 198 ? -52.519 -27.484 47.874 1.00 43.43 ? 198 GLN B OE1 1 
ATOM   3121 N NE2 . GLN B 2 198 ? -53.794 -25.642 47.980 1.00 41.59 ? 198 GLN B NE2 1 
ATOM   3122 N N   . THR B 2 199 ? -51.669 -29.864 50.695 1.00 23.59 ? 199 THR B N   1 
ATOM   3123 C CA  . THR B 2 199 ? -50.968 -31.125 50.857 1.00 24.18 ? 199 THR B CA  1 
ATOM   3124 C C   . THR B 2 199 ? -49.829 -31.195 49.849 1.00 21.10 ? 199 THR B C   1 
ATOM   3125 O O   . THR B 2 199 ? -50.001 -30.861 48.675 1.00 20.87 ? 199 THR B O   1 
ATOM   3126 C CB  . THR B 2 199 ? -51.922 -32.312 50.659 1.00 25.37 ? 199 THR B CB  1 
ATOM   3127 O OG1 . THR B 2 199 ? -52.272 -32.420 49.275 1.00 19.69 ? 199 THR B OG1 1 
ATOM   3128 C CG2 . THR B 2 199 ? -53.183 -32.091 51.474 1.00 28.52 ? 199 THR B CG2 1 
ATOM   3129 N N   . TYR B 2 200 ? -48.656 -31.616 50.304 1.00 21.36 ? 200 TYR B N   1 
ATOM   3130 C CA  . TYR B 2 200 ? -47.508 -31.694 49.410 1.00 15.97 ? 200 TYR B CA  1 
ATOM   3131 C C   . TYR B 2 200 ? -47.010 -33.118 49.292 1.00 20.47 ? 200 TYR B C   1 
ATOM   3132 O O   . TYR B 2 200 ? -46.657 -33.756 50.290 1.00 16.00 ? 200 TYR B O   1 
ATOM   3133 C CB  . TYR B 2 200 ? -46.402 -30.749 49.855 1.00 13.27 ? 200 TYR B CB  1 
ATOM   3134 C CG  . TYR B 2 200 ? -46.784 -29.289 49.710 1.00 16.62 ? 200 TYR B CG  1 
ATOM   3135 C CD1 . TYR B 2 200 ? -46.701 -28.647 48.484 1.00 13.94 ? 200 TYR B CD1 1 
ATOM   3136 C CD2 . TYR B 2 200 ? -47.243 -28.565 50.791 1.00 13.84 ? 200 TYR B CD2 1 
ATOM   3137 C CE1 . TYR B 2 200 ? -47.053 -27.335 48.344 1.00 12.94 ? 200 TYR B CE1 1 
ATOM   3138 C CE2 . TYR B 2 200 ? -47.597 -27.251 50.667 1.00 17.79 ? 200 TYR B CE2 1 
ATOM   3139 C CZ  . TYR B 2 200 ? -47.500 -26.634 49.441 1.00 18.10 ? 200 TYR B CZ  1 
ATOM   3140 O OH  . TYR B 2 200 ? -47.856 -25.315 49.319 1.00 8.04  ? 200 TYR B OH  1 
ATOM   3141 N N   . ILE B 2 201 ? -46.993 -33.614 48.056 1.00 19.33 ? 201 ILE B N   1 
ATOM   3142 C CA  . ILE B 2 201 ? -46.681 -35.005 47.801 1.00 13.69 ? 201 ILE B CA  1 
ATOM   3143 C C   . ILE B 2 201 ? -45.647 -35.112 46.712 1.00 19.56 ? 201 ILE B C   1 
ATOM   3144 O O   . ILE B 2 201 ? -45.858 -34.617 45.600 1.00 19.44 ? 201 ILE B O   1 
ATOM   3145 C CB  . ILE B 2 201 ? -47.946 -35.789 47.356 1.00 18.85 ? 201 ILE B CB  1 
ATOM   3146 C CG1 . ILE B 2 201 ? -48.974 -35.803 48.500 1.00 21.03 ? 201 ILE B CG1 1 
ATOM   3147 C CG2 . ILE B 2 201 ? -47.564 -37.196 46.899 1.00 15.49 ? 201 ILE B CG2 1 
ATOM   3148 C CD1 . ILE B 2 201 ? -49.950 -36.944 48.474 1.00 22.10 ? 201 ILE B CD1 1 
ATOM   3149 N N   . CYS B 2 202 ? -44.524 -35.755 47.013 1.00 17.36 ? 202 CYS B N   1 
ATOM   3150 C CA  . CYS B 2 202 ? -43.579 -36.062 45.947 1.00 21.05 ? 202 CYS B CA  1 
ATOM   3151 C C   . CYS B 2 202 ? -43.918 -37.413 45.313 1.00 14.02 ? 202 CYS B C   1 
ATOM   3152 O O   . CYS B 2 202 ? -44.056 -38.413 46.006 1.00 19.27 ? 202 CYS B O   1 
ATOM   3153 C CB  . CYS B 2 202 ? -42.130 -36.011 46.437 1.00 21.75 ? 202 CYS B CB  1 
ATOM   3154 S SG  . CYS B 2 202 ? -41.671 -37.371 47.502 1.00 25.94 ? 202 CYS B SG  1 
ATOM   3155 N N   . ASN B 2 203 ? -44.082 -37.425 43.994 1.00 16.16 ? 203 ASN B N   1 
ATOM   3156 C CA  . ASN B 2 203 ? -44.414 -38.654 43.266 1.00 20.84 ? 203 ASN B CA  1 
ATOM   3157 C C   . ASN B 2 203 ? -43.163 -39.265 42.709 1.00 22.60 ? 203 ASN B C   1 
ATOM   3158 O O   . ASN B 2 203 ? -42.521 -38.689 41.843 1.00 24.17 ? 203 ASN B O   1 
ATOM   3159 C CB  . ASN B 2 203 ? -45.380 -38.362 42.135 1.00 8.36  ? 203 ASN B CB  1 
ATOM   3160 C CG  . ASN B 2 203 ? -46.488 -37.463 42.573 1.00 20.90 ? 203 ASN B CG  1 
ATOM   3161 O OD1 . ASN B 2 203 ? -46.549 -36.308 42.171 1.00 23.84 ? 203 ASN B OD1 1 
ATOM   3162 N ND2 . ASN B 2 203 ? -47.356 -37.967 43.444 1.00 19.00 ? 203 ASN B ND2 1 
ATOM   3163 N N   . VAL B 2 204 ? -42.810 -40.433 43.215 1.00 20.47 ? 204 VAL B N   1 
ATOM   3164 C CA  . VAL B 2 204 ? -41.548 -41.040 42.851 1.00 20.04 ? 204 VAL B CA  1 
ATOM   3165 C C   . VAL B 2 204 ? -41.795 -42.292 42.024 1.00 22.20 ? 204 VAL B C   1 
ATOM   3166 O O   . VAL B 2 204 ? -42.527 -43.183 42.436 1.00 19.07 ? 204 VAL B O   1 
ATOM   3167 C CB  . VAL B 2 204 ? -40.697 -41.357 44.102 1.00 15.11 ? 204 VAL B CB  1 
ATOM   3168 C CG1 . VAL B 2 204 ? -39.433 -42.067 43.708 1.00 13.90 ? 204 VAL B CG1 1 
ATOM   3169 C CG2 . VAL B 2 204 ? -40.388 -40.069 44.858 1.00 14.58 ? 204 VAL B CG2 1 
ATOM   3170 N N   . ASN B 2 205 ? -41.186 -42.342 40.845 1.00 21.97 ? 205 ASN B N   1 
ATOM   3171 C CA  . ASN B 2 205 ? -41.277 -43.515 40.003 1.00 20.81 ? 205 ASN B CA  1 
ATOM   3172 C C   . ASN B 2 205 ? -39.897 -44.018 39.631 1.00 22.21 ? 205 ASN B C   1 
ATOM   3173 O O   . ASN B 2 205 ? -39.100 -43.304 39.022 1.00 22.54 ? 205 ASN B O   1 
ATOM   3174 C CB  . ASN B 2 205 ? -42.104 -43.225 38.750 1.00 27.70 ? 205 ASN B CB  1 
ATOM   3175 C CG  . ASN B 2 205 ? -42.560 -44.497 38.047 1.00 31.18 ? 205 ASN B CG  1 
ATOM   3176 O OD1 . ASN B 2 205 ? -42.205 -45.595 38.457 1.00 32.68 ? 205 ASN B OD1 1 
ATOM   3177 N ND2 . ASN B 2 205 ? -43.371 -44.351 36.999 1.00 30.82 ? 205 ASN B ND2 1 
ATOM   3178 N N   . HIS B 2 206 ? -39.603 -45.241 40.042 1.00 19.79 ? 206 HIS B N   1 
ATOM   3179 C CA  . HIS B 2 206 ? -38.392 -45.911 39.607 1.00 22.81 ? 206 HIS B CA  1 
ATOM   3180 C C   . HIS B 2 206 ? -38.822 -46.984 38.624 1.00 24.23 ? 206 HIS B C   1 
ATOM   3181 O O   . HIS B 2 206 ? -39.088 -48.122 39.009 1.00 23.89 ? 206 HIS B O   1 
ATOM   3182 C CB  . HIS B 2 206 ? -37.649 -46.533 40.791 1.00 16.79 ? 206 HIS B CB  1 
ATOM   3183 C CG  . HIS B 2 206 ? -36.297 -47.075 40.442 1.00 22.07 ? 206 HIS B CG  1 
ATOM   3184 N ND1 . HIS B 2 206 ? -35.940 -48.388 40.663 1.00 20.76 ? 206 HIS B ND1 1 
ATOM   3185 C CD2 . HIS B 2 206 ? -35.208 -46.476 39.899 1.00 14.43 ? 206 HIS B CD2 1 
ATOM   3186 C CE1 . HIS B 2 206 ? -34.690 -48.574 40.279 1.00 16.98 ? 206 HIS B CE1 1 
ATOM   3187 N NE2 . HIS B 2 206 ? -34.226 -47.430 39.807 1.00 17.83 ? 206 HIS B NE2 1 
ATOM   3188 N N   . LYS B 2 207 ? -38.921 -46.600 37.358 1.00 23.61 ? 207 LYS B N   1 
ATOM   3189 C CA  . LYS B 2 207 ? -39.304 -47.540 36.314 1.00 25.81 ? 207 LYS B CA  1 
ATOM   3190 C C   . LYS B 2 207 ? -38.498 -48.854 36.249 1.00 20.90 ? 207 LYS B C   1 
ATOM   3191 O O   . LYS B 2 207 ? -39.098 -49.903 36.074 1.00 29.93 ? 207 LYS B O   1 
ATOM   3192 C CB  . LYS B 2 207 ? -39.388 -46.838 34.958 1.00 26.07 ? 207 LYS B CB  1 
ATOM   3193 C CG  . LYS B 2 207 ? -40.803 -46.398 34.619 1.00 29.77 ? 207 LYS B CG  1 
ATOM   3194 C CD  . LYS B 2 207 ? -40.854 -45.248 33.634 1.00 36.29 ? 207 LYS B CD  1 
ATOM   3195 C CE  . LYS B 2 207 ? -42.301 -44.917 33.288 1.00 50.56 ? 207 LYS B CE  1 
ATOM   3196 N NZ  . LYS B 2 207 ? -42.438 -43.584 32.650 1.00 37.41 ? 207 LYS B NZ  1 
ATOM   3197 N N   . PRO B 2 208 ? -37.159 -48.816 36.430 1.00 21.79 ? 208 PRO B N   1 
ATOM   3198 C CA  . PRO B 2 208 ? -36.435 -50.099 36.370 1.00 20.91 ? 208 PRO B CA  1 
ATOM   3199 C C   . PRO B 2 208 ? -36.846 -51.165 37.413 1.00 23.70 ? 208 PRO B C   1 
ATOM   3200 O O   . PRO B 2 208 ? -36.585 -52.351 37.199 1.00 22.18 ? 208 PRO B O   1 
ATOM   3201 C CB  . PRO B 2 208 ? -34.974 -49.689 36.597 1.00 17.36 ? 208 PRO B CB  1 
ATOM   3202 C CG  . PRO B 2 208 ? -34.908 -48.266 36.220 1.00 22.85 ? 208 PRO B CG  1 
ATOM   3203 C CD  . PRO B 2 208 ? -36.232 -47.676 36.583 1.00 21.67 ? 208 PRO B CD  1 
ATOM   3204 N N   . SER B 2 209 ? -37.459 -50.755 38.520 1.00 23.84 ? 209 SER B N   1 
ATOM   3205 C CA  . SER B 2 209 ? -37.837 -51.697 39.581 1.00 26.68 ? 209 SER B CA  1 
ATOM   3206 C C   . SER B 2 209 ? -39.346 -51.697 39.808 1.00 31.48 ? 209 SER B C   1 
ATOM   3207 O O   . SER B 2 209 ? -39.844 -52.331 40.742 1.00 22.09 ? 209 SER B O   1 
ATOM   3208 C CB  . SER B 2 209 ? -37.129 -51.374 40.902 1.00 21.64 ? 209 SER B CB  1 
ATOM   3209 O OG  . SER B 2 209 ? -37.659 -50.215 41.510 1.00 24.99 ? 209 SER B OG  1 
ATOM   3210 N N   . ASN B 2 210 ? -40.069 -50.988 38.942 1.00 30.05 ? 210 ASN B N   1 
ATOM   3211 C CA  . ASN B 2 210 ? -41.529 -50.873 39.049 1.00 33.05 ? 210 ASN B CA  1 
ATOM   3212 C C   . ASN B 2 210 ? -41.981 -50.376 40.414 1.00 31.49 ? 210 ASN B C   1 
ATOM   3213 O O   . ASN B 2 210 ? -43.006 -50.806 40.926 1.00 34.85 ? 210 ASN B O   1 
ATOM   3214 C CB  . ASN B 2 210 ? -42.197 -52.205 38.719 1.00 34.75 ? 210 ASN B CB  1 
ATOM   3215 C CG  . ASN B 2 210 ? -41.933 -52.635 37.299 1.00 47.21 ? 210 ASN B CG  1 
ATOM   3216 O OD1 . ASN B 2 210 ? -42.078 -51.840 36.356 1.00 40.89 ? 210 ASN B OD1 1 
ATOM   3217 N ND2 . ASN B 2 210 ? -41.526 -53.891 37.129 1.00 40.52 ? 210 ASN B ND2 1 
ATOM   3218 N N   . THR B 2 211 ? -41.195 -49.477 40.996 1.00 35.92 ? 211 THR B N   1 
ATOM   3219 C CA  . THR B 2 211 ? -41.525 -48.889 42.273 1.00 26.61 ? 211 THR B CA  1 
ATOM   3220 C C   . THR B 2 211 ? -42.125 -47.507 42.064 1.00 29.34 ? 211 THR B C   1 
ATOM   3221 O O   . THR B 2 211 ? -41.457 -46.585 41.595 1.00 25.66 ? 211 THR B O   1 
ATOM   3222 C CB  . THR B 2 211 ? -40.295 -48.760 43.168 1.00 27.29 ? 211 THR B CB  1 
ATOM   3223 O OG1 . THR B 2 211 ? -39.689 -50.046 43.341 1.00 32.14 ? 211 THR B OG1 1 
ATOM   3224 C CG2 . THR B 2 211 ? -40.687 -48.176 44.542 1.00 24.89 ? 211 THR B CG2 1 
ATOM   3225 N N   . LYS B 2 212 ? -43.404 -47.382 42.389 1.00 27.37 ? 212 LYS B N   1 
ATOM   3226 C CA  . LYS B 2 212 ? -44.052 -46.082 42.437 1.00 28.13 ? 212 LYS B CA  1 
ATOM   3227 C C   . LYS B 2 212 ? -44.403 -45.765 43.881 1.00 20.50 ? 212 LYS B C   1 
ATOM   3228 O O   . LYS B 2 212 ? -45.037 -46.564 44.561 1.00 17.69 ? 212 LYS B O   1 
ATOM   3229 C CB  . LYS B 2 212 ? -45.289 -46.052 41.538 1.00 17.17 ? 212 LYS B CB  1 
ATOM   3230 C CG  . LYS B 2 212 ? -44.987 -45.612 40.132 1.00 28.00 ? 212 LYS B CG  1 
ATOM   3231 C CD  . LYS B 2 212 ? -46.198 -45.718 39.201 1.00 33.34 ? 212 LYS B CD  1 
ATOM   3232 C CE  . LYS B 2 212 ? -47.378 -44.888 39.697 1.00 31.07 ? 212 LYS B CE  1 
ATOM   3233 N NZ  . LYS B 2 212 ? -48.378 -44.624 38.612 1.00 38.36 ? 212 LYS B NZ  1 
ATOM   3234 N N   . VAL B 2 213 ? -43.960 -44.607 44.351 1.00 18.81 ? 213 VAL B N   1 
ATOM   3235 C CA  . VAL B 2 213 ? -44.264 -44.185 45.706 1.00 20.28 ? 213 VAL B CA  1 
ATOM   3236 C C   . VAL B 2 213 ? -44.746 -42.752 45.723 1.00 18.16 ? 213 VAL B C   1 
ATOM   3237 O O   . VAL B 2 213 ? -44.161 -41.895 45.078 1.00 20.90 ? 213 VAL B O   1 
ATOM   3238 C CB  . VAL B 2 213 ? -43.045 -44.312 46.634 1.00 19.04 ? 213 VAL B CB  1 
ATOM   3239 C CG1 . VAL B 2 213 ? -43.344 -43.692 47.999 1.00 19.42 ? 213 VAL B CG1 1 
ATOM   3240 C CG2 . VAL B 2 213 ? -42.654 -45.766 46.791 1.00 14.84 ? 213 VAL B CG2 1 
ATOM   3241 N N   . ASP B 2 214 ? -45.825 -42.502 46.457 1.00 22.14 ? 214 ASP B N   1 
ATOM   3242 C CA  . ASP B 2 214 ? -46.256 -41.138 46.751 1.00 19.35 ? 214 ASP B CA  1 
ATOM   3243 C C   . ASP B 2 214 ? -45.978 -40.864 48.223 1.00 20.66 ? 214 ASP B C   1 
ATOM   3244 O O   . ASP B 2 214 ? -46.580 -41.485 49.106 1.00 21.57 ? 214 ASP B O   1 
ATOM   3245 C CB  . ASP B 2 214 ? -47.744 -40.941 46.451 1.00 16.82 ? 214 ASP B CB  1 
ATOM   3246 C CG  . ASP B 2 214 ? -48.036 -40.876 44.951 1.00 25.57 ? 214 ASP B CG  1 
ATOM   3247 O OD1 . ASP B 2 214 ? -47.096 -40.610 44.157 1.00 21.02 ? 214 ASP B OD1 1 
ATOM   3248 O OD2 . ASP B 2 214 ? -49.206 -41.089 44.562 1.00 24.03 ? 214 ASP B OD2 1 
ATOM   3249 N N   . LYS B 2 215 ? -45.067 -39.935 48.481 1.00 17.79 ? 215 LYS B N   1 
ATOM   3250 C CA  . LYS B 2 215 ? -44.707 -39.574 49.839 1.00 15.71 ? 215 LYS B CA  1 
ATOM   3251 C C   . LYS B 2 215 ? -45.270 -38.220 50.189 1.00 14.87 ? 215 LYS B C   1 
ATOM   3252 O O   . LYS B 2 215 ? -44.911 -37.227 49.571 1.00 18.82 ? 215 LYS B O   1 
ATOM   3253 C CB  . LYS B 2 215 ? -43.192 -39.506 49.994 1.00 16.87 ? 215 LYS B CB  1 
ATOM   3254 C CG  . LYS B 2 215 ? -42.754 -39.132 51.414 1.00 18.11 ? 215 LYS B CG  1 
ATOM   3255 C CD  . LYS B 2 215 ? -42.757 -40.356 52.316 1.00 20.67 ? 215 LYS B CD  1 
ATOM   3256 C CE  . LYS B 2 215 ? -43.178 -40.015 53.722 1.00 18.11 ? 215 LYS B CE  1 
ATOM   3257 N NZ  . LYS B 2 215 ? -43.317 -41.279 54.484 1.00 20.27 ? 215 LYS B NZ  1 
ATOM   3258 N N   . ARG B 2 216 ? -46.134 -38.182 51.192 1.00 13.02 ? 216 ARG B N   1 
ATOM   3259 C CA  . ARG B 2 216 ? -46.646 -36.928 51.715 1.00 16.39 ? 216 ARG B CA  1 
ATOM   3260 C C   . ARG B 2 216 ? -45.624 -36.325 52.666 1.00 14.27 ? 216 ARG B C   1 
ATOM   3261 O O   . ARG B 2 216 ? -45.063 -37.030 53.498 1.00 15.99 ? 216 ARG B O   1 
ATOM   3262 C CB  . ARG B 2 216 ? -47.977 -37.169 52.439 1.00 21.66 ? 216 ARG B CB  1 
ATOM   3263 C CG  . ARG B 2 216 ? -48.432 -36.031 53.330 1.00 18.03 ? 216 ARG B CG  1 
ATOM   3264 C CD  . ARG B 2 216 ? -49.080 -34.915 52.533 1.00 17.95 ? 216 ARG B CD  1 
ATOM   3265 N NE  . ARG B 2 216 ? -49.665 -33.932 53.438 1.00 30.89 ? 216 ARG B NE  1 
ATOM   3266 C CZ  . ARG B 2 216 ? -50.873 -34.042 53.985 1.00 36.12 ? 216 ARG B CZ  1 
ATOM   3267 N NH1 . ARG B 2 216 ? -51.633 -35.095 53.700 1.00 27.71 ? 216 ARG B NH1 1 
ATOM   3268 N NH2 . ARG B 2 216 ? -51.320 -33.098 54.809 1.00 31.25 ? 216 ARG B NH2 1 
ATOM   3269 N N   . VAL B 2 217 ? -45.389 -35.023 52.541 1.00 16.40 ? 217 VAL B N   1 
ATOM   3270 C CA  . VAL B 2 217 ? -44.378 -34.334 53.348 1.00 18.13 ? 217 VAL B CA  1 
ATOM   3271 C C   . VAL B 2 217 ? -45.023 -33.225 54.182 1.00 25.67 ? 217 VAL B C   1 
ATOM   3272 O O   . VAL B 2 217 ? -45.592 -32.275 53.630 1.00 20.90 ? 217 VAL B O   1 
ATOM   3273 C CB  . VAL B 2 217 ? -43.289 -33.706 52.469 1.00 14.25 ? 217 VAL B CB  1 
ATOM   3274 C CG1 . VAL B 2 217 ? -42.329 -32.904 53.319 1.00 17.76 ? 217 VAL B CG1 1 
ATOM   3275 C CG2 . VAL B 2 217 ? -42.544 -34.796 51.675 1.00 9.62  ? 217 VAL B CG2 1 
ATOM   3276 N N   . GLU B 2 218 ? -44.916 -33.342 55.508 1.00 22.19 ? 218 GLU B N   1 
ATOM   3277 C CA  . GLU B 2 218 ? -45.639 -32.480 56.450 1.00 29.42 ? 218 GLU B CA  1 
ATOM   3278 C C   . GLU B 2 218 ? -44.674 -31.872 57.439 1.00 24.42 ? 218 GLU B C   1 
ATOM   3279 O O   . GLU B 2 218 ? -43.624 -32.439 57.692 1.00 24.63 ? 218 GLU B O   1 
ATOM   3280 C CB  . GLU B 2 218 ? -46.675 -33.298 57.232 1.00 28.03 ? 218 GLU B CB  1 
ATOM   3281 C CG  . GLU B 2 218 ? -47.986 -33.515 56.506 1.00 39.22 ? 218 GLU B CG  1 
ATOM   3282 C CD  . GLU B 2 218 ? -48.824 -34.621 57.138 1.00 53.34 ? 218 GLU B CD  1 
ATOM   3283 O OE1 . GLU B 2 218 ? -49.852 -35.021 56.538 1.00 48.57 ? 218 GLU B OE1 1 
ATOM   3284 O OE2 . GLU B 2 218 ? -48.452 -35.099 58.232 1.00 40.81 ? 218 GLU B OE2 1 
ATOM   3285 N N   . PRO B 2 219 ? -45.037 -30.720 58.023 1.00 35.66 ? 219 PRO B N   1 
ATOM   3286 C CA  . PRO B 2 219 ? -44.227 -30.114 59.090 1.00 27.19 ? 219 PRO B CA  1 
ATOM   3287 C C   . PRO B 2 219 ? -44.166 -31.043 60.295 1.00 30.86 ? 219 PRO B C   1 
ATOM   3288 O O   . PRO B 2 219 ? -45.187 -31.663 60.582 1.00 31.41 ? 219 PRO B O   1 
ATOM   3289 C CB  . PRO B 2 219 ? -45.022 -28.862 59.461 1.00 20.91 ? 219 PRO B CB  1 
ATOM   3290 C CG  . PRO B 2 219 ? -45.881 -28.574 58.263 1.00 27.96 ? 219 PRO B CG  1 
ATOM   3291 C CD  . PRO B 2 219 ? -46.220 -29.906 57.683 1.00 21.77 ? 219 PRO B CD  1 
ATOM   3292 N N   . LYS B 2 220 ? -43.020 -31.143 60.978 1.00 40.20 ? 220 LYS B N   1 
ATOM   3293 C CA  . LYS B 2 220 ? -42.919 -31.995 62.170 1.00 39.05 ? 220 LYS B CA  1 
ATOM   3294 C C   . LYS B 2 220 ? -43.127 -31.206 63.449 1.00 43.52 ? 220 LYS B C   1 
ATOM   3295 O O   . LYS B 2 220 ? -44.212 -31.233 64.031 1.00 54.33 ? 220 LYS B O   1 
ATOM   3296 C CB  . LYS B 2 220 ? -41.582 -32.738 62.230 1.00 50.10 ? 220 LYS B CB  1 
ATOM   3297 C CG  . LYS B 2 220 ? -41.704 -34.247 62.000 1.00 59.89 ? 220 LYS B CG  1 
ATOM   3298 C CD  . LYS B 2 220 ? -40.469 -35.010 62.489 1.00 60.63 ? 220 LYS B CD  1 
ATOM   3299 C CE  . LYS B 2 220 ? -40.319 -34.935 64.004 1.00 55.10 ? 220 LYS B CE  1 
ATOM   3300 N NZ  . LYS B 2 220 ? -39.451 -36.020 64.553 1.00 52.25 ? 220 LYS B NZ  1 
ATOM   3301 N N   . ASP C 1 1   ? -17.110 0.717   6.118  1.00 33.00 ? 1   ASP C N   1 
ATOM   3302 C CA  . ASP C 1 1   ? -15.967 -0.148  6.350  1.00 29.34 ? 1   ASP C CA  1 
ATOM   3303 C C   . ASP C 1 1   ? -16.359 -1.621  6.432  1.00 41.42 ? 1   ASP C C   1 
ATOM   3304 O O   . ASP C 1 1   ? -17.527 -1.956  6.639  1.00 40.55 ? 1   ASP C O   1 
ATOM   3305 C CB  . ASP C 1 1   ? -15.248 0.252   7.640  1.00 32.87 ? 1   ASP C CB  1 
ATOM   3306 C CG  . ASP C 1 1   ? -14.673 1.638   7.583  1.00 47.21 ? 1   ASP C CG  1 
ATOM   3307 O OD1 . ASP C 1 1   ? -14.783 2.284   6.521  1.00 40.68 ? 1   ASP C OD1 1 
ATOM   3308 O OD2 . ASP C 1 1   ? -14.099 2.075   8.612  1.00 59.78 ? 1   ASP C OD2 1 
ATOM   3309 N N   . ILE C 1 2   ? -15.369 -2.493  6.260  1.00 31.19 ? 2   ILE C N   1 
ATOM   3310 C CA  . ILE C 1 2   ? -15.568 -3.918  6.466  1.00 32.48 ? 2   ILE C CA  1 
ATOM   3311 C C   . ILE C 1 2   ? -15.625 -4.204  7.964  1.00 29.82 ? 2   ILE C C   1 
ATOM   3312 O O   . ILE C 1 2   ? -14.713 -3.821  8.709  1.00 26.94 ? 2   ILE C O   1 
ATOM   3313 C CB  . ILE C 1 2   ? -14.408 -4.727  5.853  1.00 30.11 ? 2   ILE C CB  1 
ATOM   3314 C CG1 . ILE C 1 2   ? -14.357 -4.507  4.339  1.00 31.25 ? 2   ILE C CG1 1 
ATOM   3315 C CG2 . ILE C 1 2   ? -14.543 -6.213  6.187  1.00 19.29 ? 2   ILE C CG2 1 
ATOM   3316 C CD1 . ILE C 1 2   ? -15.508 -5.122  3.595  1.00 24.55 ? 2   ILE C CD1 1 
ATOM   3317 N N   . LEU C 1 3   ? -16.685 -4.874  8.409  1.00 25.41 ? 3   LEU C N   1 
ATOM   3318 C CA  . LEU C 1 3   ? -16.750 -5.312  9.799  1.00 25.07 ? 3   LEU C CA  1 
ATOM   3319 C C   . LEU C 1 3   ? -16.129 -6.702  9.971  1.00 25.74 ? 3   LEU C C   1 
ATOM   3320 O O   . LEU C 1 3   ? -16.395 -7.617  9.190  1.00 32.19 ? 3   LEU C O   1 
ATOM   3321 C CB  . LEU C 1 3   ? -18.191 -5.302  10.317 1.00 24.10 ? 3   LEU C CB  1 
ATOM   3322 C CG  . LEU C 1 3   ? -18.276 -5.478  11.845 1.00 39.68 ? 3   LEU C CG  1 
ATOM   3323 C CD1 . LEU C 1 3   ? -17.777 -4.219  12.567 1.00 24.62 ? 3   LEU C CD1 1 
ATOM   3324 C CD2 . LEU C 1 3   ? -19.686 -5.887  12.335 1.00 21.37 ? 3   LEU C CD2 1 
ATOM   3325 N N   . LEU C 1 4   ? -15.283 -6.855  10.979 1.00 22.44 ? 4   LEU C N   1 
ATOM   3326 C CA  . LEU C 1 4   ? -14.748 -8.166  11.297 1.00 21.52 ? 4   LEU C CA  1 
ATOM   3327 C C   . LEU C 1 4   ? -15.332 -8.625  12.625 1.00 31.42 ? 4   LEU C C   1 
ATOM   3328 O O   . LEU C 1 4   ? -15.253 -7.916  13.639 1.00 22.32 ? 4   LEU C O   1 
ATOM   3329 C CB  . LEU C 1 4   ? -13.224 -8.136  11.387 1.00 22.07 ? 4   LEU C CB  1 
ATOM   3330 C CG  . LEU C 1 4   ? -12.417 -7.660  10.175 1.00 23.71 ? 4   LEU C CG  1 
ATOM   3331 C CD1 . LEU C 1 4   ? -10.932 -7.776  10.467 1.00 23.74 ? 4   LEU C CD1 1 
ATOM   3332 C CD2 . LEU C 1 4   ? -12.780 -8.412  8.908  1.00 16.86 ? 4   LEU C CD2 1 
ATOM   3333 N N   . THR C 1 5   ? -15.922 -9.812  12.617 1.00 21.28 ? 5   THR C N   1 
ATOM   3334 C CA  . THR C 1 5   ? -16.516 -10.353 13.819 1.00 20.35 ? 5   THR C CA  1 
ATOM   3335 C C   . THR C 1 5   ? -15.669 -11.507 14.301 1.00 21.32 ? 5   THR C C   1 
ATOM   3336 O O   . THR C 1 5   ? -15.599 -12.540 13.642 1.00 30.29 ? 5   THR C O   1 
ATOM   3337 C CB  . THR C 1 5   ? -17.963 -10.834 13.567 1.00 26.40 ? 5   THR C CB  1 
ATOM   3338 O OG1 . THR C 1 5   ? -18.736 -9.760  13.029 1.00 31.79 ? 5   THR C OG1 1 
ATOM   3339 C CG2 . THR C 1 5   ? -18.617 -11.272 14.851 1.00 19.67 ? 5   THR C CG2 1 
ATOM   3340 N N   . GLN C 1 6   ? -15.015 -11.334 15.441 1.00 17.98 ? 6   GLN C N   1 
ATOM   3341 C CA  . GLN C 1 6   ? -14.210 -12.414 15.997 1.00 24.56 ? 6   GLN C CA  1 
ATOM   3342 C C   . GLN C 1 6   ? -14.997 -13.183 17.044 1.00 32.43 ? 6   GLN C C   1 
ATOM   3343 O O   . GLN C 1 6   ? -15.809 -12.606 17.763 1.00 32.36 ? 6   GLN C O   1 
ATOM   3344 C CB  . GLN C 1 6   ? -12.918 -11.881 16.607 1.00 21.27 ? 6   GLN C CB  1 
ATOM   3345 C CG  . GLN C 1 6   ? -11.917 -11.425 15.594 1.00 18.97 ? 6   GLN C CG  1 
ATOM   3346 C CD  . GLN C 1 6   ? -10.656 -10.908 16.238 1.00 20.37 ? 6   GLN C CD  1 
ATOM   3347 O OE1 . GLN C 1 6   ? -10.424 -9.704  16.297 1.00 21.51 ? 6   GLN C OE1 1 
ATOM   3348 N NE2 . GLN C 1 6   ? -9.834  -11.819 16.733 1.00 22.05 ? 6   GLN C NE2 1 
ATOM   3349 N N   . SER C 1 7   ? -14.772 -14.488 17.120 1.00 26.50 ? 7   SER C N   1 
ATOM   3350 C CA  . SER C 1 7   ? -15.464 -15.296 18.118 1.00 28.00 ? 7   SER C CA  1 
ATOM   3351 C C   . SER C 1 7   ? -14.628 -16.507 18.540 1.00 30.73 ? 7   SER C C   1 
ATOM   3352 O O   . SER C 1 7   ? -13.895 -17.081 17.729 1.00 33.60 ? 7   SER C O   1 
ATOM   3353 C CB  . SER C 1 7   ? -16.839 -15.736 17.599 1.00 31.34 ? 7   SER C CB  1 
ATOM   3354 O OG  . SER C 1 7   ? -16.726 -16.833 16.706 1.00 36.05 ? 7   SER C OG  1 
ATOM   3355 N N   . PRO C 1 8   ? -14.731 -16.897 19.817 1.00 32.29 ? 8   PRO C N   1 
ATOM   3356 C CA  . PRO C 1 8   ? -15.570 -16.232 20.820 1.00 34.85 ? 8   PRO C CA  1 
ATOM   3357 C C   . PRO C 1 8   ? -14.868 -15.012 21.405 1.00 29.01 ? 8   PRO C C   1 
ATOM   3358 O O   . PRO C 1 8   ? -13.690 -14.780 21.135 1.00 27.00 ? 8   PRO C O   1 
ATOM   3359 C CB  . PRO C 1 8   ? -15.710 -17.298 21.904 1.00 26.93 ? 8   PRO C CB  1 
ATOM   3360 C CG  . PRO C 1 8   ? -14.392 -18.007 21.861 1.00 26.18 ? 8   PRO C CG  1 
ATOM   3361 C CD  . PRO C 1 8   ? -14.014 -18.056 20.385 1.00 24.40 ? 8   PRO C CD  1 
ATOM   3362 N N   . VAL C 1 9   ? -15.599 -14.234 22.189 1.00 27.16 ? 9   VAL C N   1 
ATOM   3363 C CA  . VAL C 1 9   ? -15.013 -13.114 22.906 1.00 30.88 ? 9   VAL C CA  1 
ATOM   3364 C C   . VAL C 1 9   ? -13.942 -13.631 23.873 1.00 29.11 ? 9   VAL C C   1 
ATOM   3365 O O   . VAL C 1 9   ? -12.853 -13.064 23.979 1.00 29.91 ? 9   VAL C O   1 
ATOM   3366 C CB  . VAL C 1 9   ? -16.095 -12.335 23.669 1.00 32.05 ? 9   VAL C CB  1 
ATOM   3367 C CG1 . VAL C 1 9   ? -15.475 -11.273 24.549 1.00 40.98 ? 9   VAL C CG1 1 
ATOM   3368 C CG2 . VAL C 1 9   ? -17.079 -11.730 22.697 1.00 21.53 ? 9   VAL C CG2 1 
ATOM   3369 N N   . ILE C 1 10  ? -14.257 -14.723 24.561 1.00 27.41 ? 10  ILE C N   1 
ATOM   3370 C CA  . ILE C 1 10  ? -13.325 -15.342 25.488 1.00 25.60 ? 10  ILE C CA  1 
ATOM   3371 C C   . ILE C 1 10  ? -13.162 -16.815 25.166 1.00 31.18 ? 10  ILE C C   1 
ATOM   3372 O O   . ILE C 1 10  ? -14.146 -17.568 25.091 1.00 26.09 ? 10  ILE C O   1 
ATOM   3373 C CB  . ILE C 1 10  ? -13.817 -15.252 26.940 1.00 25.33 ? 10  ILE C CB  1 
ATOM   3374 C CG1 . ILE C 1 10  ? -14.133 -13.810 27.327 1.00 31.56 ? 10  ILE C CG1 1 
ATOM   3375 C CG2 . ILE C 1 10  ? -12.787 -15.849 27.873 1.00 24.10 ? 10  ILE C CG2 1 
ATOM   3376 C CD1 . ILE C 1 10  ? -14.624 -13.675 28.743 1.00 39.44 ? 10  ILE C CD1 1 
ATOM   3377 N N   . LEU C 1 11  ? -11.913 -17.227 24.994 1.00 26.07 ? 11  LEU C N   1 
ATOM   3378 C CA  . LEU C 1 11  ? -11.611 -18.589 24.602 1.00 21.09 ? 11  LEU C CA  1 
ATOM   3379 C C   . LEU C 1 11  ? -10.828 -19.296 25.698 1.00 21.91 ? 11  LEU C C   1 
ATOM   3380 O O   . LEU C 1 11  ? -9.627  -19.107 25.833 1.00 26.82 ? 11  LEU C O   1 
ATOM   3381 C CB  . LEU C 1 11  ? -10.837 -18.586 23.280 1.00 22.30 ? 11  LEU C CB  1 
ATOM   3382 C CG  . LEU C 1 11  ? -10.360 -19.911 22.698 1.00 27.36 ? 11  LEU C CG  1 
ATOM   3383 C CD1 . LEU C 1 11  ? -11.499 -20.917 22.694 1.00 35.39 ? 11  LEU C CD1 1 
ATOM   3384 C CD2 . LEU C 1 11  ? -9.835  -19.691 21.285 1.00 31.16 ? 11  LEU C CD2 1 
ATOM   3385 N N   . SER C 1 12  ? -11.521 -20.108 26.485 1.00 24.12 ? 12  SER C N   1 
ATOM   3386 C CA  . SER C 1 12  ? -10.882 -20.846 27.566 1.00 26.61 ? 12  SER C CA  1 
ATOM   3387 C C   . SER C 1 12  ? -10.549 -22.269 27.109 1.00 25.13 ? 12  SER C C   1 
ATOM   3388 O O   . SER C 1 12  ? -11.419 -22.986 26.615 1.00 26.55 ? 12  SER C O   1 
ATOM   3389 C CB  . SER C 1 12  ? -11.808 -20.868 28.794 1.00 23.87 ? 12  SER C CB  1 
ATOM   3390 O OG  . SER C 1 12  ? -11.193 -21.494 29.907 1.00 34.20 ? 12  SER C OG  1 
ATOM   3391 N N   . VAL C 1 13  ? -9.292  -22.673 27.258 1.00 20.19 ? 13  VAL C N   1 
ATOM   3392 C CA  . VAL C 1 13  ? -8.870  -24.000 26.814 1.00 27.01 ? 13  VAL C CA  1 
ATOM   3393 C C   . VAL C 1 13  ? -7.822  -24.614 27.717 1.00 26.51 ? 13  VAL C C   1 
ATOM   3394 O O   . VAL C 1 13  ? -7.124  -23.911 28.436 1.00 30.78 ? 13  VAL C O   1 
ATOM   3395 C CB  . VAL C 1 13  ? -8.260  -23.982 25.389 1.00 32.02 ? 13  VAL C CB  1 
ATOM   3396 C CG1 . VAL C 1 13  ? -9.305  -23.641 24.342 1.00 33.52 ? 13  VAL C CG1 1 
ATOM   3397 C CG2 . VAL C 1 13  ? -7.079  -23.020 25.330 1.00 28.22 ? 13  VAL C CG2 1 
ATOM   3398 N N   . SER C 1 14  ? -7.693  -25.934 27.640 1.00 30.24 ? 14  SER C N   1 
ATOM   3399 C CA  . SER C 1 14  ? -6.712  -26.664 28.434 1.00 33.69 ? 14  SER C CA  1 
ATOM   3400 C C   . SER C 1 14  ? -5.372  -26.711 27.707 1.00 30.30 ? 14  SER C C   1 
ATOM   3401 O O   . SER C 1 14  ? -5.326  -26.830 26.495 1.00 36.68 ? 14  SER C O   1 
ATOM   3402 C CB  . SER C 1 14  ? -7.209  -28.080 28.728 1.00 28.86 ? 14  SER C CB  1 
ATOM   3403 O OG  . SER C 1 14  ? -8.503  -28.044 29.298 1.00 41.88 ? 14  SER C OG  1 
ATOM   3404 N N   . PRO C 1 15  ? -4.268  -26.621 28.453 1.00 38.06 ? 15  PRO C N   1 
ATOM   3405 C CA  . PRO C 1 15  ? -2.955  -26.578 27.800 1.00 31.45 ? 15  PRO C CA  1 
ATOM   3406 C C   . PRO C 1 15  ? -2.664  -27.835 26.981 1.00 31.36 ? 15  PRO C C   1 
ATOM   3407 O O   . PRO C 1 15  ? -3.075  -28.931 27.368 1.00 34.65 ? 15  PRO C O   1 
ATOM   3408 C CB  . PRO C 1 15  ? -1.979  -26.446 28.980 1.00 27.77 ? 15  PRO C CB  1 
ATOM   3409 C CG  . PRO C 1 15  ? -2.733  -26.950 30.157 1.00 26.88 ? 15  PRO C CG  1 
ATOM   3410 C CD  . PRO C 1 15  ? -4.163  -26.596 29.923 1.00 32.65 ? 15  PRO C CD  1 
ATOM   3411 N N   . GLY C 1 16  ? -1.974  -27.669 25.855 1.00 31.69 ? 16  GLY C N   1 
ATOM   3412 C CA  . GLY C 1 16  ? -1.660  -28.782 24.976 1.00 22.75 ? 16  GLY C CA  1 
ATOM   3413 C C   . GLY C 1 16  ? -2.754  -29.073 23.964 1.00 31.60 ? 16  GLY C C   1 
ATOM   3414 O O   . GLY C 1 16  ? -2.534  -29.810 23.010 1.00 30.82 ? 16  GLY C O   1 
ATOM   3415 N N   . GLU C 1 17  ? -3.934  -28.495 24.171 1.00 32.13 ? 17  GLU C N   1 
ATOM   3416 C CA  . GLU C 1 17  ? -5.040  -28.650 23.232 1.00 30.50 ? 17  GLU C CA  1 
ATOM   3417 C C   . GLU C 1 17  ? -4.832  -27.872 21.931 1.00 33.30 ? 17  GLU C C   1 
ATOM   3418 O O   . GLU C 1 17  ? -3.935  -27.038 21.819 1.00 27.40 ? 17  GLU C O   1 
ATOM   3419 C CB  . GLU C 1 17  ? -6.354  -28.198 23.872 1.00 32.04 ? 17  GLU C CB  1 
ATOM   3420 C CG  . GLU C 1 17  ? -6.938  -29.162 24.885 1.00 34.83 ? 17  GLU C CG  1 
ATOM   3421 C CD  . GLU C 1 17  ? -8.301  -28.718 25.373 1.00 38.39 ? 17  GLU C CD  1 
ATOM   3422 O OE1 . GLU C 1 17  ? -8.529  -27.491 25.453 1.00 38.51 ? 17  GLU C OE1 1 
ATOM   3423 O OE2 . GLU C 1 17  ? -9.147  -29.592 25.671 1.00 51.69 ? 17  GLU C OE2 1 
ATOM   3424 N N   . ARG C 1 18  ? -5.678  -28.156 20.948 1.00 48.22 ? 18  ARG C N   1 
ATOM   3425 C CA  . ARG C 1 18  ? -5.719  -27.373 19.720 1.00 48.38 ? 18  ARG C CA  1 
ATOM   3426 C C   . ARG C 1 18  ? -6.702  -26.218 19.902 1.00 37.46 ? 18  ARG C C   1 
ATOM   3427 O O   . ARG C 1 18  ? -7.744  -26.373 20.541 1.00 34.39 ? 18  ARG C O   1 
ATOM   3428 C CB  . ARG C 1 18  ? -6.112  -28.251 18.531 1.00 43.57 ? 18  ARG C CB  1 
ATOM   3429 C CG  . ARG C 1 18  ? -6.120  -27.518 17.204 1.00 53.20 ? 18  ARG C CG  1 
ATOM   3430 C CD  . ARG C 1 18  ? -5.955  -28.478 16.038 1.00 56.82 ? 18  ARG C CD  1 
ATOM   3431 N NE  . ARG C 1 18  ? -6.020  -27.784 14.755 1.00 62.35 ? 18  ARG C NE  1 
ATOM   3432 C CZ  . ARG C 1 18  ? -4.983  -27.188 14.173 1.00 63.88 ? 18  ARG C CZ  1 
ATOM   3433 N NH1 . ARG C 1 18  ? -3.796  -27.196 14.761 1.00 58.75 ? 18  ARG C NH1 1 
ATOM   3434 N NH2 . ARG C 1 18  ? -5.132  -26.578 13.005 1.00 56.54 ? 18  ARG C NH2 1 
ATOM   3435 N N   . VAL C 1 19  ? -6.363  -25.059 19.351 1.00 26.54 ? 19  VAL C N   1 
ATOM   3436 C CA  . VAL C 1 19  ? -7.115  -23.841 19.611 1.00 25.85 ? 19  VAL C CA  1 
ATOM   3437 C C   . VAL C 1 19  ? -7.458  -23.129 18.311 1.00 23.96 ? 19  VAL C C   1 
ATOM   3438 O O   . VAL C 1 19  ? -6.602  -22.977 17.434 1.00 27.64 ? 19  VAL C O   1 
ATOM   3439 C CB  . VAL C 1 19  ? -6.305  -22.916 20.541 1.00 32.83 ? 19  VAL C CB  1 
ATOM   3440 C CG1 . VAL C 1 19  ? -6.863  -21.514 20.553 1.00 24.89 ? 19  VAL C CG1 1 
ATOM   3441 C CG2 . VAL C 1 19  ? -6.261  -23.504 21.941 1.00 35.27 ? 19  VAL C CG2 1 
ATOM   3442 N N   . SER C 1 20  ? -8.712  -22.701 18.172 1.00 30.26 ? 20  SER C N   1 
ATOM   3443 C CA  . SER C 1 20  ? -9.135  -22.061 16.926 1.00 24.14 ? 20  SER C CA  1 
ATOM   3444 C C   . SER C 1 20  ? -9.891  -20.757 17.102 1.00 32.62 ? 20  SER C C   1 
ATOM   3445 O O   . SER C 1 20  ? -11.038 -20.730 17.560 1.00 35.41 ? 20  SER C O   1 
ATOM   3446 C CB  . SER C 1 20  ? -9.928  -23.027 16.064 1.00 26.89 ? 20  SER C CB  1 
ATOM   3447 O OG  . SER C 1 20  ? -9.078  -24.064 15.605 1.00 38.45 ? 20  SER C OG  1 
ATOM   3448 N N   . PHE C 1 21  ? -9.231  -19.669 16.724 1.00 32.84 ? 21  PHE C N   1 
ATOM   3449 C CA  . PHE C 1 21  ? -9.857  -18.363 16.776 1.00 30.04 ? 21  PHE C CA  1 
ATOM   3450 C C   . PHE C 1 21  ? -10.611 -18.139 15.485 1.00 28.89 ? 21  PHE C C   1 
ATOM   3451 O O   . PHE C 1 21  ? -10.141 -18.499 14.408 1.00 27.89 ? 21  PHE C O   1 
ATOM   3452 C CB  . PHE C 1 21  ? -8.814  -17.276 16.967 1.00 23.50 ? 21  PHE C CB  1 
ATOM   3453 C CG  . PHE C 1 21  ? -7.920  -17.496 18.162 1.00 22.30 ? 21  PHE C CG  1 
ATOM   3454 C CD1 . PHE C 1 21  ? -6.721  -18.161 18.032 1.00 24.31 ? 21  PHE C CD1 1 
ATOM   3455 C CD2 . PHE C 1 21  ? -8.272  -17.016 19.400 1.00 18.15 ? 21  PHE C CD2 1 
ATOM   3456 C CE1 . PHE C 1 21  ? -5.894  -18.344 19.118 1.00 26.61 ? 21  PHE C CE1 1 
ATOM   3457 C CE2 . PHE C 1 21  ? -7.454  -17.191 20.484 1.00 21.64 ? 21  PHE C CE2 1 
ATOM   3458 C CZ  . PHE C 1 21  ? -6.265  -17.857 20.351 1.00 26.20 ? 21  PHE C CZ  1 
ATOM   3459 N N   . SER C 1 22  ? -11.785 -17.535 15.589 1.00 27.96 ? 22  SER C N   1 
ATOM   3460 C CA  . SER C 1 22  ? -12.643 -17.380 14.427 1.00 28.97 ? 22  SER C CA  1 
ATOM   3461 C C   . SER C 1 22  ? -12.821 -15.910 14.071 1.00 23.49 ? 22  SER C C   1 
ATOM   3462 O O   . SER C 1 22  ? -13.060 -15.080 14.942 1.00 27.26 ? 22  SER C O   1 
ATOM   3463 C CB  . SER C 1 22  ? -13.982 -18.060 14.687 1.00 22.34 ? 22  SER C CB  1 
ATOM   3464 O OG  . SER C 1 22  ? -14.954 -17.613 13.785 1.00 31.53 ? 22  SER C OG  1 
ATOM   3465 N N   . CYS C 1 23  ? -12.682 -15.598 12.787 1.00 19.86 ? 23  CYS C N   1 
ATOM   3466 C CA  . CYS C 1 23  ? -12.834 -14.230 12.296 1.00 25.20 ? 23  CYS C CA  1 
ATOM   3467 C C   . CYS C 1 23  ? -13.724 -14.239 11.049 1.00 34.21 ? 23  CYS C C   1 
ATOM   3468 O O   . CYS C 1 23  ? -13.394 -14.866 10.033 1.00 32.60 ? 23  CYS C O   1 
ATOM   3469 C CB  . CYS C 1 23  ? -11.463 -13.609 11.982 1.00 21.30 ? 23  CYS C CB  1 
ATOM   3470 S SG  . CYS C 1 23  ? -11.458 -11.854 11.468 1.00 28.44 ? 23  CYS C SG  1 
ATOM   3471 N N   . ARG C 1 24  ? -14.859 -13.560 11.125 1.00 24.89 ? 24  ARG C N   1 
ATOM   3472 C CA  . ARG C 1 24  ? -15.770 -13.536 9.998  1.00 25.35 ? 24  ARG C CA  1 
ATOM   3473 C C   . ARG C 1 24  ? -15.845 -12.112 9.465  1.00 30.86 ? 24  ARG C C   1 
ATOM   3474 O O   . ARG C 1 24  ? -15.998 -11.159 10.241 1.00 27.44 ? 24  ARG C O   1 
ATOM   3475 C CB  . ARG C 1 24  ? -17.155 -14.031 10.425 1.00 29.53 ? 24  ARG C CB  1 
ATOM   3476 C CG  . ARG C 1 24  ? -18.074 -14.379 9.262  1.00 49.82 ? 24  ARG C CG  1 
ATOM   3477 C CD  . ARG C 1 24  ? -19.367 -15.089 9.703  1.00 49.09 ? 24  ARG C CD  1 
ATOM   3478 N NE  . ARG C 1 24  ? -19.899 -15.927 8.625  1.00 63.23 ? 24  ARG C NE  1 
ATOM   3479 C CZ  . ARG C 1 24  ? -20.679 -15.493 7.636  1.00 62.55 ? 24  ARG C CZ  1 
ATOM   3480 N NH1 . ARG C 1 24  ? -21.042 -14.218 7.570  1.00 63.14 ? 24  ARG C NH1 1 
ATOM   3481 N NH2 . ARG C 1 24  ? -21.099 -16.344 6.709  1.00 54.43 ? 24  ARG C NH2 1 
ATOM   3482 N N   . ALA C 1 25  ? -15.724 -11.963 8.147  1.00 27.13 ? 25  ALA C N   1 
ATOM   3483 C CA  . ALA C 1 25  ? -15.805 -10.645 7.523  1.00 25.76 ? 25  ALA C CA  1 
ATOM   3484 C C   . ALA C 1 25  ? -17.225 -10.338 7.039  1.00 33.23 ? 25  ALA C C   1 
ATOM   3485 O O   . ALA C 1 25  ? -17.977 -11.243 6.673  1.00 37.43 ? 25  ALA C O   1 
ATOM   3486 C CB  . ALA C 1 25  ? -14.804 -10.520 6.400  1.00 23.58 ? 25  ALA C CB  1 
ATOM   3487 N N   . SER C 1 26  ? -17.584 -9.056  7.049  1.00 32.32 ? 26  SER C N   1 
ATOM   3488 C CA  . SER C 1 26  ? -18.938 -8.628  6.720  1.00 28.55 ? 26  SER C CA  1 
ATOM   3489 C C   . SER C 1 26  ? -19.237 -8.792  5.230  1.00 38.52 ? 26  SER C C   1 
ATOM   3490 O O   . SER C 1 26  ? -20.392 -8.695  4.806  1.00 38.34 ? 26  SER C O   1 
ATOM   3491 C CB  . SER C 1 26  ? -19.194 -7.186  7.186  1.00 27.00 ? 26  SER C CB  1 
ATOM   3492 O OG  . SER C 1 26  ? -18.337 -6.254  6.548  1.00 33.90 ? 26  SER C OG  1 
ATOM   3493 N N   . GLN C 1 27  ? -18.187 -9.048  4.456  1.00 31.51 ? 27  GLN C N   1 
ATOM   3494 C CA  . GLN C 1 27  ? -18.294 -9.367  3.032  1.00 35.67 ? 27  GLN C CA  1 
ATOM   3495 C C   . GLN C 1 27  ? -16.998 -10.052 2.584  1.00 35.04 ? 27  GLN C C   1 
ATOM   3496 O O   . GLN C 1 27  ? -16.030 -10.104 3.340  1.00 34.74 ? 27  GLN C O   1 
ATOM   3497 C CB  . GLN C 1 27  ? -18.540 -8.104  2.207  1.00 34.99 ? 27  GLN C CB  1 
ATOM   3498 C CG  . GLN C 1 27  ? -17.282 -7.423  1.746  1.00 36.91 ? 27  GLN C CG  1 
ATOM   3499 C CD  . GLN C 1 27  ? -17.549 -6.109  1.041  1.00 51.25 ? 27  GLN C CD  1 
ATOM   3500 O OE1 . GLN C 1 27  ? -18.426 -5.342  1.449  1.00 45.80 ? 27  GLN C OE1 1 
ATOM   3501 N NE2 . GLN C 1 27  ? -16.788 -5.839  -0.028 1.00 42.28 ? 27  GLN C NE2 1 
ATOM   3502 N N   . SER C 1 28  ? -16.963 -10.573 1.364  1.00 32.56 ? 28  SER C N   1 
ATOM   3503 C CA  . SER C 1 28  ? -15.764 -11.270 0.900  1.00 35.49 ? 28  SER C CA  1 
ATOM   3504 C C   . SER C 1 28  ? -14.519 -10.385 0.831  1.00 32.88 ? 28  SER C C   1 
ATOM   3505 O O   . SER C 1 28  ? -14.576 -9.234  0.403  1.00 29.29 ? 28  SER C O   1 
ATOM   3506 C CB  . SER C 1 28  ? -15.992 -11.932 -0.454 1.00 32.00 ? 28  SER C CB  1 
ATOM   3507 O OG  . SER C 1 28  ? -14.885 -12.752 -0.781 1.00 43.35 ? 28  SER C OG  1 
ATOM   3508 N N   . ILE C 1 29  ? -13.396 -10.947 1.263  1.00 30.11 ? 29  ILE C N   1 
ATOM   3509 C CA  . ILE C 1 29  ? -12.129 -10.239 1.277  1.00 24.29 ? 29  ILE C CA  1 
ATOM   3510 C C   . ILE C 1 29  ? -10.978 -11.134 0.845  1.00 25.24 ? 29  ILE C C   1 
ATOM   3511 O O   . ILE C 1 29  ? -9.826  -10.861 1.169  1.00 28.13 ? 29  ILE C O   1 
ATOM   3512 C CB  . ILE C 1 29  ? -11.801 -9.683  2.681  1.00 21.16 ? 29  ILE C CB  1 
ATOM   3513 C CG1 . ILE C 1 29  ? -11.915 -10.782 3.726  1.00 20.18 ? 29  ILE C CG1 1 
ATOM   3514 C CG2 . ILE C 1 29  ? -12.672 -8.477  3.026  1.00 23.15 ? 29  ILE C CG2 1 
ATOM   3515 C CD1 . ILE C 1 29  ? -11.374 -10.379 5.067  1.00 28.30 ? 29  ILE C CD1 1 
ATOM   3516 N N   . GLY C 1 30  ? -11.293 -12.211 0.135  1.00 23.99 ? 30  GLY C N   1 
ATOM   3517 C CA  . GLY C 1 30  ? -10.269 -13.077 -0.425 1.00 19.43 ? 30  GLY C CA  1 
ATOM   3518 C C   . GLY C 1 30  ? -9.443  -13.775 0.633  1.00 23.04 ? 30  GLY C C   1 
ATOM   3519 O O   . GLY C 1 30  ? -9.971  -14.539 1.443  1.00 32.96 ? 30  GLY C O   1 
ATOM   3520 N N   . THR C 1 31  ? -8.142  -13.522 0.629  1.00 18.49 ? 31  THR C N   1 
ATOM   3521 C CA  . THR C 1 31  ? -7.288  -14.017 1.700  1.00 21.15 ? 31  THR C CA  1 
ATOM   3522 C C   . THR C 1 31  ? -6.580  -12.844 2.372  1.00 20.38 ? 31  THR C C   1 
ATOM   3523 O O   . THR C 1 31  ? -5.511  -12.998 2.942  1.00 19.65 ? 31  THR C O   1 
ATOM   3524 C CB  . THR C 1 31  ? -6.254  -15.050 1.193  1.00 27.38 ? 31  THR C CB  1 
ATOM   3525 O OG1 . THR C 1 31  ? -5.417  -14.455 0.195  1.00 25.20 ? 31  THR C OG1 1 
ATOM   3526 C CG2 . THR C 1 31  ? -6.946  -16.270 0.606  1.00 21.12 ? 31  THR C CG2 1 
ATOM   3527 N N   . ASN C 1 32  ? -7.201  -11.671 2.303  1.00 25.83 ? 32  ASN C N   1 
ATOM   3528 C CA  . ASN C 1 32  ? -6.576  -10.439 2.756  1.00 19.96 ? 32  ASN C CA  1 
ATOM   3529 C C   . ASN C 1 32  ? -6.805  -10.172 4.241  1.00 20.07 ? 32  ASN C C   1 
ATOM   3530 O O   . ASN C 1 32  ? -7.383  -9.159  4.631  1.00 25.60 ? 32  ASN C O   1 
ATOM   3531 C CB  . ASN C 1 32  ? -7.063  -9.268  1.918  1.00 19.30 ? 32  ASN C CB  1 
ATOM   3532 C CG  . ASN C 1 32  ? -5.980  -8.235  1.682  1.00 28.97 ? 32  ASN C CG  1 
ATOM   3533 O OD1 . ASN C 1 32  ? -5.259  -7.845  2.604  1.00 32.34 ? 32  ASN C OD1 1 
ATOM   3534 N ND2 . ASN C 1 32  ? -5.856  -7.785  0.438  1.00 34.15 ? 32  ASN C ND2 1 
ATOM   3535 N N   . ILE C 1 33  ? -6.333  -11.094 5.067  1.00 19.35 ? 33  ILE C N   1 
ATOM   3536 C CA  . ILE C 1 33  ? -6.526  -11.006 6.503  1.00 18.03 ? 33  ILE C CA  1 
ATOM   3537 C C   . ILE C 1 33  ? -5.180  -11.252 7.179  1.00 22.90 ? 33  ILE C C   1 
ATOM   3538 O O   . ILE C 1 33  ? -4.400  -12.086 6.732  1.00 19.31 ? 33  ILE C O   1 
ATOM   3539 C CB  . ILE C 1 33  ? -7.598  -12.011 6.974  1.00 19.56 ? 33  ILE C CB  1 
ATOM   3540 C CG1 . ILE C 1 33  ? -8.004  -11.762 8.420  1.00 26.00 ? 33  ILE C CG1 1 
ATOM   3541 C CG2 . ILE C 1 33  ? -7.117  -13.427 6.796  1.00 28.61 ? 33  ILE C CG2 1 
ATOM   3542 C CD1 . ILE C 1 33  ? -9.289  -10.936 8.541  1.00 32.17 ? 33  ILE C CD1 1 
ATOM   3543 N N   . HIS C 1 34  ? -4.883  -10.474 8.215  1.00 19.52 ? 34  HIS C N   1 
ATOM   3544 C CA  . HIS C 1 34  ? -3.668  -10.665 9.002  1.00 17.96 ? 34  HIS C CA  1 
ATOM   3545 C C   . HIS C 1 34  ? -4.024  -10.906 10.477 1.00 20.47 ? 34  HIS C C   1 
ATOM   3546 O O   . HIS C 1 34  ? -5.064  -10.457 10.955 1.00 16.79 ? 34  HIS C O   1 
ATOM   3547 C CB  . HIS C 1 34  ? -2.738  -9.465  8.865  1.00 21.99 ? 34  HIS C CB  1 
ATOM   3548 C CG  . HIS C 1 34  ? -2.510  -9.030  7.448  1.00 27.81 ? 34  HIS C CG  1 
ATOM   3549 N ND1 . HIS C 1 34  ? -2.085  -9.892  6.457  1.00 24.86 ? 34  HIS C ND1 1 
ATOM   3550 C CD2 . HIS C 1 34  ? -2.638  -7.819  6.855  1.00 21.94 ? 34  HIS C CD2 1 
ATOM   3551 C CE1 . HIS C 1 34  ? -1.961  -9.232  5.323  1.00 22.28 ? 34  HIS C CE1 1 
ATOM   3552 N NE2 . HIS C 1 34  ? -2.291  -7.969  5.539  1.00 26.03 ? 34  HIS C NE2 1 
ATOM   3553 N N   . TRP C 1 35  ? -3.176  -11.649 11.181 1.00 21.14 ? 35  TRP C N   1 
ATOM   3554 C CA  . TRP C 1 35  ? -3.422  -11.960 12.577 1.00 21.14 ? 35  TRP C CA  1 
ATOM   3555 C C   . TRP C 1 35  ? -2.317  -11.423 13.467 1.00 19.46 ? 35  TRP C C   1 
ATOM   3556 O O   . TRP C 1 35  ? -1.140  -11.450 13.107 1.00 23.16 ? 35  TRP C O   1 
ATOM   3557 C CB  . TRP C 1 35  ? -3.566  -13.465 12.786 1.00 21.52 ? 35  TRP C CB  1 
ATOM   3558 C CG  . TRP C 1 35  ? -4.787  -14.070 12.192 1.00 23.91 ? 35  TRP C CG  1 
ATOM   3559 C CD1 . TRP C 1 35  ? -4.917  -14.573 10.935 1.00 20.78 ? 35  TRP C CD1 1 
ATOM   3560 C CD2 . TRP C 1 35  ? -6.057  -14.267 12.839 1.00 28.02 ? 35  TRP C CD2 1 
ATOM   3561 N NE1 . TRP C 1 35  ? -6.185  -15.073 10.756 1.00 28.10 ? 35  TRP C NE1 1 
ATOM   3562 C CE2 . TRP C 1 35  ? -6.904  -14.895 11.905 1.00 20.80 ? 35  TRP C CE2 1 
ATOM   3563 C CE3 . TRP C 1 35  ? -6.551  -13.981 14.118 1.00 28.24 ? 35  TRP C CE3 1 
ATOM   3564 C CZ2 . TRP C 1 35  ? -8.218  -15.232 12.202 1.00 26.60 ? 35  TRP C CZ2 1 
ATOM   3565 C CZ3 . TRP C 1 35  ? -7.859  -14.319 14.414 1.00 22.13 ? 35  TRP C CZ3 1 
ATOM   3566 C CH2 . TRP C 1 35  ? -8.677  -14.939 13.462 1.00 30.00 ? 35  TRP C CH2 1 
ATOM   3567 N N   . TYR C 1 36  ? -2.709  -10.960 14.645 1.00 21.40 ? 36  TYR C N   1 
ATOM   3568 C CA  . TYR C 1 36  ? -1.781  -10.354 15.589 1.00 16.56 ? 36  TYR C CA  1 
ATOM   3569 C C   . TYR C 1 36  ? -1.951  -10.931 16.975 1.00 16.72 ? 36  TYR C C   1 
ATOM   3570 O O   . TYR C 1 36  ? -3.005  -11.457 17.326 1.00 16.64 ? 36  TYR C O   1 
ATOM   3571 C CB  . TYR C 1 36  ? -2.015  -8.849  15.668 1.00 16.97 ? 36  TYR C CB  1 
ATOM   3572 C CG  . TYR C 1 36  ? -1.730  -8.116  14.388 1.00 20.30 ? 36  TYR C CG  1 
ATOM   3573 C CD1 . TYR C 1 36  ? -2.729  -7.927  13.437 1.00 18.72 ? 36  TYR C CD1 1 
ATOM   3574 C CD2 . TYR C 1 36  ? -0.458  -7.612  14.124 1.00 16.72 ? 36  TYR C CD2 1 
ATOM   3575 C CE1 . TYR C 1 36  ? -2.468  -7.265  12.258 1.00 17.11 ? 36  TYR C CE1 1 
ATOM   3576 C CE2 . TYR C 1 36  ? -0.190  -6.943  12.951 1.00 18.93 ? 36  TYR C CE2 1 
ATOM   3577 C CZ  . TYR C 1 36  ? -1.198  -6.768  12.015 1.00 24.57 ? 36  TYR C CZ  1 
ATOM   3578 O OH  . TYR C 1 36  ? -0.936  -6.088  10.834 1.00 20.19 ? 36  TYR C OH  1 
ATOM   3579 N N   . GLN C 1 37  ? -0.903  -10.814 17.775 1.00 19.53 ? 37  GLN C N   1 
ATOM   3580 C CA  . GLN C 1 37  ? -0.964  -11.239 19.158 1.00 21.20 ? 37  GLN C CA  1 
ATOM   3581 C C   . GLN C 1 37  ? -0.678  -10.041 20.046 1.00 20.97 ? 37  GLN C C   1 
ATOM   3582 O O   . GLN C 1 37  ? 0.240   -9.283  19.782 1.00 26.36 ? 37  GLN C O   1 
ATOM   3583 C CB  . GLN C 1 37  ? 0.062   -12.332 19.420 1.00 19.40 ? 37  GLN C CB  1 
ATOM   3584 C CG  . GLN C 1 37  ? 0.155   -12.752 20.878 1.00 18.43 ? 37  GLN C CG  1 
ATOM   3585 C CD  . GLN C 1 37  ? 1.336   -13.661 21.130 1.00 26.75 ? 37  GLN C CD  1 
ATOM   3586 O OE1 . GLN C 1 37  ? 2.479   -13.210 21.144 1.00 23.66 ? 37  GLN C OE1 1 
ATOM   3587 N NE2 . GLN C 1 37  ? 1.071   -14.954 21.307 1.00 21.29 ? 37  GLN C NE2 1 
ATOM   3588 N N   . GLN C 1 38  ? -1.470  -9.842  21.090 1.00 22.12 ? 38  GLN C N   1 
ATOM   3589 C CA  . GLN C 1 38  ? -1.107  -8.814  22.059 1.00 24.96 ? 38  GLN C CA  1 
ATOM   3590 C C   . GLN C 1 38  ? -1.010  -9.383  23.456 1.00 21.77 ? 38  GLN C C   1 
ATOM   3591 O O   . GLN C 1 38  ? -2.020  -9.676  24.088 1.00 20.99 ? 38  GLN C O   1 
ATOM   3592 C CB  . GLN C 1 38  ? -2.044  -7.608  22.026 1.00 20.99 ? 38  GLN C CB  1 
ATOM   3593 C CG  . GLN C 1 38  ? -1.507  -6.446  22.848 1.00 17.25 ? 38  GLN C CG  1 
ATOM   3594 C CD  . GLN C 1 38  ? -2.235  -5.156  22.573 1.00 22.62 ? 38  GLN C CD  1 
ATOM   3595 O OE1 . GLN C 1 38  ? -3.459  -5.139  22.435 1.00 20.85 ? 38  GLN C OE1 1 
ATOM   3596 N NE2 . GLN C 1 38  ? -1.489  -4.066  22.481 1.00 22.05 ? 38  GLN C NE2 1 
ATOM   3597 N N   . ARG C 1 39  ? 0.229   -9.553  23.905 1.00 18.39 ? 39  ARG C N   1 
ATOM   3598 C CA  . ARG C 1 39  ? 0.536   -9.974  25.256 1.00 18.63 ? 39  ARG C CA  1 
ATOM   3599 C C   . ARG C 1 39  ? 0.456   -8.779  26.185 1.00 21.98 ? 39  ARG C C   1 
ATOM   3600 O O   . ARG C 1 39  ? 0.538   -7.637  25.736 1.00 22.65 ? 39  ARG C O   1 
ATOM   3601 C CB  . ARG C 1 39  ? 1.949   -10.535 25.311 1.00 21.18 ? 39  ARG C CB  1 
ATOM   3602 C CG  . ARG C 1 39  ? 2.119   -11.890 24.683 1.00 22.79 ? 39  ARG C CG  1 
ATOM   3603 C CD  . ARG C 1 39  ? 3.573   -12.243 24.641 1.00 20.16 ? 39  ARG C CD  1 
ATOM   3604 N NE  . ARG C 1 39  ? 3.777   -13.583 24.116 1.00 37.74 ? 39  ARG C NE  1 
ATOM   3605 C CZ  . ARG C 1 39  ? 4.961   -14.070 23.759 1.00 47.83 ? 39  ARG C CZ  1 
ATOM   3606 N NH1 . ARG C 1 39  ? 6.045   -13.315 23.873 1.00 36.91 ? 39  ARG C NH1 1 
ATOM   3607 N NH2 . ARG C 1 39  ? 5.056   -15.307 23.285 1.00 55.59 ? 39  ARG C NH2 1 
ATOM   3608 N N   . THR C 1 40  ? 0.324   -9.052  27.480 1.00 22.38 ? 40  THR C N   1 
ATOM   3609 C CA  . THR C 1 40  ? 0.192   -8.008  28.494 1.00 23.25 ? 40  THR C CA  1 
ATOM   3610 C C   . THR C 1 40  ? 1.296   -6.933  28.431 1.00 23.90 ? 40  THR C C   1 
ATOM   3611 O O   . THR C 1 40  ? 2.483   -7.242  28.359 1.00 18.72 ? 40  THR C O   1 
ATOM   3612 C CB  . THR C 1 40  ? 0.123   -8.634  29.908 1.00 31.87 ? 40  THR C CB  1 
ATOM   3613 O OG1 . THR C 1 40  ? -0.992  -9.539  29.988 1.00 21.68 ? 40  THR C OG1 1 
ATOM   3614 C CG2 . THR C 1 40  ? -0.002  -7.549  30.973 1.00 20.03 ? 40  THR C CG2 1 
ATOM   3615 N N   . ASN C 1 41  ? 0.879   -5.668  28.450 1.00 21.32 ? 41  ASN C N   1 
ATOM   3616 C CA  . ASN C 1 41  ? 1.778   -4.515  28.291 1.00 24.04 ? 41  ASN C CA  1 
ATOM   3617 C C   . ASN C 1 41  ? 2.505   -4.418  26.944 1.00 34.17 ? 41  ASN C C   1 
ATOM   3618 O O   . ASN C 1 41  ? 3.201   -3.432  26.694 1.00 30.87 ? 41  ASN C O   1 
ATOM   3619 C CB  . ASN C 1 41  ? 2.793   -4.403  29.434 1.00 20.22 ? 41  ASN C CB  1 
ATOM   3620 C CG  . ASN C 1 41  ? 2.134   -4.298  30.796 1.00 30.56 ? 41  ASN C CG  1 
ATOM   3621 O OD1 . ASN C 1 41  ? 2.368   -5.134  31.662 1.00 26.42 ? 41  ASN C OD1 1 
ATOM   3622 N ND2 . ASN C 1 41  ? 1.302   -3.276  30.989 1.00 28.44 ? 41  ASN C ND2 1 
ATOM   3623 N N   . GLY C 1 42  ? 2.329   -5.410  26.073 1.00 18.22 ? 42  GLY C N   1 
ATOM   3624 C CA  . GLY C 1 42  ? 3.022   -5.412  24.796 1.00 29.55 ? 42  GLY C CA  1 
ATOM   3625 C C   . GLY C 1 42  ? 2.362   -4.666  23.642 1.00 20.61 ? 42  GLY C C   1 
ATOM   3626 O O   . GLY C 1 42  ? 1.237   -4.188  23.748 1.00 18.53 ? 42  GLY C O   1 
ATOM   3627 N N   . SER C 1 43  ? 3.089   -4.566  22.533 1.00 19.79 ? 43  SER C N   1 
ATOM   3628 C CA  . SER C 1 43  ? 2.526   -4.070  21.284 1.00 20.03 ? 43  SER C CA  1 
ATOM   3629 C C   . SER C 1 43  ? 2.051   -5.292  20.521 1.00 16.37 ? 43  SER C C   1 
ATOM   3630 O O   . SER C 1 43  ? 2.480   -6.394  20.815 1.00 18.05 ? 43  SER C O   1 
ATOM   3631 C CB  . SER C 1 43  ? 3.576   -3.299  20.487 1.00 17.24 ? 43  SER C CB  1 
ATOM   3632 O OG  . SER C 1 43  ? 3.928   -2.090  21.137 1.00 23.61 ? 43  SER C OG  1 
ATOM   3633 N N   . PRO C 1 44  ? 1.146   -5.113  19.554 1.00 19.86 ? 44  PRO C N   1 
ATOM   3634 C CA  . PRO C 1 44  ? 0.752   -6.270  18.740 1.00 22.77 ? 44  PRO C CA  1 
ATOM   3635 C C   . PRO C 1 44  ? 1.953   -6.914  18.021 1.00 19.73 ? 44  PRO C C   1 
ATOM   3636 O O   . PRO C 1 44  ? 2.848   -6.213  17.558 1.00 22.26 ? 44  PRO C O   1 
ATOM   3637 C CB  . PRO C 1 44  ? -0.222  -5.666  17.725 1.00 20.48 ? 44  PRO C CB  1 
ATOM   3638 C CG  . PRO C 1 44  ? -0.753  -4.425  18.401 1.00 21.58 ? 44  PRO C CG  1 
ATOM   3639 C CD  . PRO C 1 44  ? 0.385   -3.897  19.216 1.00 21.63 ? 44  PRO C CD  1 
ATOM   3640 N N   . ARG C 1 45  ? 1.979   -8.239  17.969 1.00 17.26 ? 45  ARG C N   1 
ATOM   3641 C CA  . ARG C 1 45  ? 2.974   -8.970  17.201 1.00 21.39 ? 45  ARG C CA  1 
ATOM   3642 C C   . ARG C 1 45  ? 2.271   -9.676  16.052 1.00 20.20 ? 45  ARG C C   1 
ATOM   3643 O O   . ARG C 1 45  ? 1.403   -10.527 16.269 1.00 23.21 ? 45  ARG C O   1 
ATOM   3644 C CB  . ARG C 1 45  ? 3.729   -9.979  18.086 1.00 21.33 ? 45  ARG C CB  1 
ATOM   3645 C CG  . ARG C 1 45  ? 4.537   -11.014 17.313 1.00 28.03 ? 45  ARG C CG  1 
ATOM   3646 C CD  . ARG C 1 45  ? 5.609   -11.742 18.149 1.00 28.02 ? 45  ARG C CD  1 
ATOM   3647 N NE  . ARG C 1 45  ? 5.115   -12.834 18.999 1.00 40.41 ? 45  ARG C NE  1 
ATOM   3648 C CZ  . ARG C 1 45  ? 5.731   -14.010 19.157 1.00 38.48 ? 45  ARG C CZ  1 
ATOM   3649 N NH1 . ARG C 1 45  ? 6.859   -14.270 18.499 1.00 40.85 ? 45  ARG C NH1 1 
ATOM   3650 N NH2 . ARG C 1 45  ? 5.223   -14.937 19.969 1.00 33.61 ? 45  ARG C NH2 1 
ATOM   3651 N N   . LEU C 1 46  ? 2.626   -9.298  14.829 1.00 18.97 ? 46  LEU C N   1 
ATOM   3652 C CA  . LEU C 1 46  ? 2.156   -9.980  13.625 1.00 20.11 ? 46  LEU C CA  1 
ATOM   3653 C C   . LEU C 1 46  ? 2.502   -11.476 13.664 1.00 23.25 ? 46  LEU C C   1 
ATOM   3654 O O   . LEU C 1 46  ? 3.652   -11.852 13.928 1.00 24.08 ? 46  LEU C O   1 
ATOM   3655 C CB  . LEU C 1 46  ? 2.799   -9.339  12.396 1.00 22.14 ? 46  LEU C CB  1 
ATOM   3656 C CG  . LEU C 1 46  ? 2.558   -9.966  11.026 1.00 19.93 ? 46  LEU C CG  1 
ATOM   3657 C CD1 . LEU C 1 46  ? 1.200   -9.540  10.479 1.00 17.17 ? 46  LEU C CD1 1 
ATOM   3658 C CD2 . LEU C 1 46  ? 3.689   -9.570  10.085 1.00 22.74 ? 46  LEU C CD2 1 
ATOM   3659 N N   . LEU C 1 47  ? 1.507   -12.321 13.393 1.00 22.65 ? 47  LEU C N   1 
ATOM   3660 C CA  . LEU C 1 47  ? 1.660   -13.778 13.502 1.00 23.60 ? 47  LEU C CA  1 
ATOM   3661 C C   . LEU C 1 47  ? 1.530   -14.506 12.176 1.00 27.04 ? 47  LEU C C   1 
ATOM   3662 O O   . LEU C 1 47  ? 2.262   -15.454 11.898 1.00 33.02 ? 47  LEU C O   1 
ATOM   3663 C CB  . LEU C 1 47  ? 0.569   -14.340 14.399 1.00 22.69 ? 47  LEU C CB  1 
ATOM   3664 C CG  . LEU C 1 47  ? 0.611   -14.039 15.877 1.00 22.32 ? 47  LEU C CG  1 
ATOM   3665 C CD1 . LEU C 1 47  ? -0.737  -14.433 16.465 1.00 24.39 ? 47  LEU C CD1 1 
ATOM   3666 C CD2 . LEU C 1 47  ? 1.735   -14.844 16.491 1.00 26.58 ? 47  LEU C CD2 1 
ATOM   3667 N N   . ILE C 1 48  ? 0.550   -14.077 11.388 1.00 22.52 ? 48  ILE C N   1 
ATOM   3668 C CA  . ILE C 1 48  ? 0.204   -14.699 10.124 1.00 16.80 ? 48  ILE C CA  1 
ATOM   3669 C C   . ILE C 1 48  ? -0.143  -13.577 9.150  1.00 23.13 ? 48  ILE C C   1 
ATOM   3670 O O   . ILE C 1 48  ? -0.796  -12.604 9.526  1.00 25.70 ? 48  ILE C O   1 
ATOM   3671 C CB  . ILE C 1 48  ? -1.034  -15.624 10.288 1.00 17.41 ? 48  ILE C CB  1 
ATOM   3672 C CG1 . ILE C 1 48  ? -0.707  -16.849 11.153 1.00 23.28 ? 48  ILE C CG1 1 
ATOM   3673 C CG2 . ILE C 1 48  ? -1.581  -16.063 8.950  1.00 19.00 ? 48  ILE C CG2 1 
ATOM   3674 C CD1 . ILE C 1 48  ? 0.379   -17.726 10.594 1.00 20.60 ? 48  ILE C CD1 1 
ATOM   3675 N N   . LYS C 1 49  ? 0.297   -13.688 7.902  1.00 23.35 ? 49  LYS C N   1 
ATOM   3676 C CA  . LYS C 1 49  ? -0.118  -12.719 6.897  1.00 23.22 ? 49  LYS C CA  1 
ATOM   3677 C C   . LYS C 1 49  ? -0.878  -13.387 5.749  1.00 25.66 ? 49  LYS C C   1 
ATOM   3678 O O   . LYS C 1 49  ? -0.601  -14.530 5.388  1.00 26.85 ? 49  LYS C O   1 
ATOM   3679 C CB  . LYS C 1 49  ? 1.072   -11.911 6.382  1.00 22.29 ? 49  LYS C CB  1 
ATOM   3680 C CG  . LYS C 1 49  ? 2.049   -12.679 5.512  1.00 20.40 ? 49  LYS C CG  1 
ATOM   3681 C CD  . LYS C 1 49  ? 3.291   -11.833 5.215  1.00 15.53 ? 49  LYS C CD  1 
ATOM   3682 C CE  . LYS C 1 49  ? 4.387   -12.653 4.534  1.00 20.79 ? 49  LYS C CE  1 
ATOM   3683 N NZ  . LYS C 1 49  ? 4.099   -12.913 3.075  1.00 19.26 ? 49  LYS C NZ  1 
ATOM   3684 N N   . TYR C 1 50  ? -1.851  -12.666 5.198  1.00 24.62 ? 50  TYR C N   1 
ATOM   3685 C CA  . TYR C 1 50  ? -2.633  -13.141 4.058  1.00 25.01 ? 50  TYR C CA  1 
ATOM   3686 C C   . TYR C 1 50  ? -3.273  -14.509 4.294  1.00 27.29 ? 50  TYR C C   1 
ATOM   3687 O O   . TYR C 1 50  ? -3.069  -15.441 3.516  1.00 34.14 ? 50  TYR C O   1 
ATOM   3688 C CB  . TYR C 1 50  ? -1.794  -13.121 2.769  1.00 23.83 ? 50  TYR C CB  1 
ATOM   3689 C CG  . TYR C 1 50  ? -1.536  -11.717 2.282  1.00 29.25 ? 50  TYR C CG  1 
ATOM   3690 C CD1 . TYR C 1 50  ? -0.263  -11.140 2.383  1.00 24.47 ? 50  TYR C CD1 1 
ATOM   3691 C CD2 . TYR C 1 50  ? -2.577  -10.940 1.753  1.00 22.72 ? 50  TYR C CD2 1 
ATOM   3692 C CE1 . TYR C 1 50  ? -0.027  -9.829  1.940  1.00 21.13 ? 50  TYR C CE1 1 
ATOM   3693 C CE2 . TYR C 1 50  ? -2.353  -9.626  1.323  1.00 24.00 ? 50  TYR C CE2 1 
ATOM   3694 C CZ  . TYR C 1 50  ? -1.076  -9.085  1.420  1.00 30.30 ? 50  TYR C CZ  1 
ATOM   3695 O OH  . TYR C 1 50  ? -0.848  -7.797  0.998  1.00 30.48 ? 50  TYR C OH  1 
ATOM   3696 N N   . ALA C 1 51  ? -4.040  -14.601 5.378  1.00 21.95 ? 51  ALA C N   1 
ATOM   3697 C CA  . ALA C 1 51  ? -4.764  -15.810 5.762  1.00 23.58 ? 51  ALA C CA  1 
ATOM   3698 C C   . ALA C 1 51  ? -3.899  -16.921 6.330  1.00 25.43 ? 51  ALA C C   1 
ATOM   3699 O O   . ALA C 1 51  ? -4.188  -17.421 7.423  1.00 24.38 ? 51  ALA C O   1 
ATOM   3700 C CB  . ALA C 1 51  ? -5.638  -16.345 4.606  1.00 22.68 ? 51  ALA C CB  1 
ATOM   3701 N N   . SER C 1 52  ? -2.836  -17.286 5.610  1.00 19.70 ? 52  SER C N   1 
ATOM   3702 C CA  . SER C 1 52  ? -2.133  -18.536 5.887  1.00 24.71 ? 52  SER C CA  1 
ATOM   3703 C C   . SER C 1 52  ? -0.612  -18.492 5.841  1.00 26.56 ? 52  SER C C   1 
ATOM   3704 O O   . SER C 1 52  ? 0.030   -19.506 6.101  1.00 27.81 ? 52  SER C O   1 
ATOM   3705 C CB  . SER C 1 52  ? -2.582  -19.605 4.900  1.00 19.55 ? 52  SER C CB  1 
ATOM   3706 O OG  . SER C 1 52  ? -1.886  -19.453 3.675  1.00 26.73 ? 52  SER C OG  1 
ATOM   3707 N N   . GLU C 1 53  ? -0.026  -17.352 5.496  1.00 24.67 ? 53  GLU C N   1 
ATOM   3708 C CA  . GLU C 1 53  ? 1.418   -17.312 5.252  1.00 21.34 ? 53  GLU C CA  1 
ATOM   3709 C C   . GLU C 1 53  ? 2.183   -16.974 6.510  1.00 22.35 ? 53  GLU C C   1 
ATOM   3710 O O   . GLU C 1 53  ? 1.796   -16.082 7.241  1.00 25.49 ? 53  GLU C O   1 
ATOM   3711 C CB  . GLU C 1 53  ? 1.762   -16.292 4.171  1.00 28.68 ? 53  GLU C CB  1 
ATOM   3712 C CG  . GLU C 1 53  ? 1.047   -16.499 2.848  1.00 28.34 ? 53  GLU C CG  1 
ATOM   3713 C CD  . GLU C 1 53  ? 1.325   -15.370 1.889  1.00 29.48 ? 53  GLU C CD  1 
ATOM   3714 O OE1 . GLU C 1 53  ? 1.912   -14.358 2.329  1.00 27.95 ? 53  GLU C OE1 1 
ATOM   3715 O OE2 . GLU C 1 53  ? 0.958   -15.479 0.703  1.00 35.00 ? 53  GLU C OE2 1 
ATOM   3716 N N   . SER C 1 54  ? 3.287   -17.669 6.752  1.00 27.51 ? 54  SER C N   1 
ATOM   3717 C CA  . SER C 1 54  ? 4.024   -17.498 7.998  1.00 30.84 ? 54  SER C CA  1 
ATOM   3718 C C   . SER C 1 54  ? 4.891   -16.243 8.048  1.00 31.69 ? 54  SER C C   1 
ATOM   3719 O O   . SER C 1 54  ? 5.159   -15.607 7.025  1.00 34.91 ? 54  SER C O   1 
ATOM   3720 C CB  . SER C 1 54  ? 4.882   -18.727 8.291  1.00 30.92 ? 54  SER C CB  1 
ATOM   3721 O OG  . SER C 1 54  ? 5.833   -18.914 7.270  1.00 42.08 ? 54  SER C OG  1 
ATOM   3722 N N   . ILE C 1 55  ? 5.327   -15.916 9.262  1.00 30.45 ? 55  ILE C N   1 
ATOM   3723 C CA  . ILE C 1 55  ? 6.144   -14.745 9.544  1.00 28.80 ? 55  ILE C CA  1 
ATOM   3724 C C   . ILE C 1 55  ? 7.438   -15.176 10.219 1.00 31.37 ? 55  ILE C C   1 
ATOM   3725 O O   . ILE C 1 55  ? 7.420   -16.004 11.131 1.00 32.44 ? 55  ILE C O   1 
ATOM   3726 C CB  . ILE C 1 55  ? 5.415   -13.785 10.495 1.00 23.13 ? 55  ILE C CB  1 
ATOM   3727 C CG1 . ILE C 1 55  ? 4.033   -13.445 9.945  1.00 16.89 ? 55  ILE C CG1 1 
ATOM   3728 C CG2 . ILE C 1 55  ? 6.253   -12.535 10.734 1.00 24.06 ? 55  ILE C CG2 1 
ATOM   3729 C CD1 . ILE C 1 55  ? 4.084   -12.838 8.557  1.00 21.96 ? 55  ILE C CD1 1 
ATOM   3730 N N   . SER C 1 56  ? 8.562   -14.622 9.777  1.00 32.67 ? 56  SER C N   1 
ATOM   3731 C CA  . SER C 1 56  ? 9.851   -14.990 10.356 1.00 37.46 ? 56  SER C CA  1 
ATOM   3732 C C   . SER C 1 56  ? 9.927   -14.692 11.849 1.00 41.39 ? 56  SER C C   1 
ATOM   3733 O O   . SER C 1 56  ? 9.818   -13.541 12.274 1.00 36.89 ? 56  SER C O   1 
ATOM   3734 C CB  . SER C 1 56  ? 11.000  -14.279 9.648  1.00 44.70 ? 56  SER C CB  1 
ATOM   3735 O OG  . SER C 1 56  ? 12.188  -14.398 10.415 1.00 48.62 ? 56  SER C OG  1 
ATOM   3736 N N   . GLY C 1 57  ? 10.118  -15.745 12.637 1.00 40.13 ? 57  GLY C N   1 
ATOM   3737 C CA  . GLY C 1 57  ? 10.284  -15.612 14.069 1.00 32.11 ? 57  GLY C CA  1 
ATOM   3738 C C   . GLY C 1 57  ? 9.118   -16.160 14.861 1.00 35.58 ? 57  GLY C C   1 
ATOM   3739 O O   . GLY C 1 57  ? 9.199   -16.272 16.086 1.00 29.47 ? 57  GLY C O   1 
ATOM   3740 N N   . ILE C 1 58  ? 8.032   -16.495 14.167 1.00 38.16 ? 58  ILE C N   1 
ATOM   3741 C CA  . ILE C 1 58  ? 6.815   -16.963 14.830 1.00 33.54 ? 58  ILE C CA  1 
ATOM   3742 C C   . ILE C 1 58  ? 6.810   -18.486 14.888 1.00 33.82 ? 58  ILE C C   1 
ATOM   3743 O O   . ILE C 1 58  ? 6.925   -19.147 13.851 1.00 39.03 ? 58  ILE C O   1 
ATOM   3744 C CB  . ILE C 1 58  ? 5.533   -16.467 14.113 1.00 28.25 ? 58  ILE C CB  1 
ATOM   3745 C CG1 . ILE C 1 58  ? 5.517   -14.935 14.004 1.00 28.40 ? 58  ILE C CG1 1 
ATOM   3746 C CG2 . ILE C 1 58  ? 4.290   -17.008 14.799 1.00 20.06 ? 58  ILE C CG2 1 
ATOM   3747 C CD1 . ILE C 1 58  ? 5.607   -14.213 15.323 1.00 27.00 ? 58  ILE C CD1 1 
ATOM   3748 N N   . PRO C 1 59  ? 6.695   -19.049 16.105 1.00 34.64 ? 59  PRO C N   1 
ATOM   3749 C CA  . PRO C 1 59  ? 6.736   -20.511 16.269 1.00 35.00 ? 59  PRO C CA  1 
ATOM   3750 C C   . PRO C 1 59  ? 5.731   -21.232 15.364 1.00 33.44 ? 59  PRO C C   1 
ATOM   3751 O O   . PRO C 1 59  ? 4.614   -20.758 15.153 1.00 33.06 ? 59  PRO C O   1 
ATOM   3752 C CB  . PRO C 1 59  ? 6.422   -20.728 17.768 1.00 28.47 ? 59  PRO C CB  1 
ATOM   3753 C CG  . PRO C 1 59  ? 5.977   -19.393 18.301 1.00 36.24 ? 59  PRO C CG  1 
ATOM   3754 C CD  . PRO C 1 59  ? 6.569   -18.342 17.392 1.00 30.32 ? 59  PRO C CD  1 
ATOM   3755 N N   . SER C 1 60  ? 6.151   -22.375 14.839 1.00 35.32 ? 60  SER C N   1 
ATOM   3756 C CA  . SER C 1 60  ? 5.413   -23.095 13.813 1.00 32.15 ? 60  SER C CA  1 
ATOM   3757 C C   . SER C 1 60  ? 4.055   -23.585 14.286 1.00 31.36 ? 60  SER C C   1 
ATOM   3758 O O   . SER C 1 60  ? 3.225   -23.991 13.472 1.00 33.10 ? 60  SER C O   1 
ATOM   3759 C CB  . SER C 1 60  ? 6.231   -24.285 13.306 1.00 34.65 ? 60  SER C CB  1 
ATOM   3760 O OG  . SER C 1 60  ? 6.433   -25.240 14.341 1.00 43.55 ? 60  SER C OG  1 
ATOM   3761 N N   . ARG C 1 61  ? 3.817   -23.546 15.594 1.00 31.58 ? 61  ARG C N   1 
ATOM   3762 C CA  . ARG C 1 61  ? 2.532   -24.010 16.117 1.00 35.04 ? 61  ARG C CA  1 
ATOM   3763 C C   . ARG C 1 61  ? 1.395   -23.049 15.759 1.00 35.16 ? 61  ARG C C   1 
ATOM   3764 O O   . ARG C 1 61  ? 0.227   -23.408 15.845 1.00 39.51 ? 61  ARG C O   1 
ATOM   3765 C CB  . ARG C 1 61  ? 2.594   -24.253 17.625 1.00 33.28 ? 61  ARG C CB  1 
ATOM   3766 C CG  . ARG C 1 61  ? 2.801   -23.005 18.449 1.00 39.26 ? 61  ARG C CG  1 
ATOM   3767 C CD  . ARG C 1 61  ? 2.675   -23.308 19.932 1.00 35.85 ? 61  ARG C CD  1 
ATOM   3768 N NE  . ARG C 1 61  ? 2.902   -22.112 20.716 1.00 34.46 ? 61  ARG C NE  1 
ATOM   3769 C CZ  . ARG C 1 61  ? 4.107   -21.663 21.041 1.00 42.45 ? 61  ARG C CZ  1 
ATOM   3770 N NH1 . ARG C 1 61  ? 5.184   -22.334 20.656 1.00 37.97 ? 61  ARG C NH1 1 
ATOM   3771 N NH2 . ARG C 1 61  ? 4.233   -20.547 21.751 1.00 40.58 ? 61  ARG C NH2 1 
ATOM   3772 N N   . PHE C 1 62  ? 1.753   -21.833 15.356 1.00 30.87 ? 62  PHE C N   1 
ATOM   3773 C CA  . PHE C 1 62  ? 0.793   -20.886 14.800 1.00 26.20 ? 62  PHE C CA  1 
ATOM   3774 C C   . PHE C 1 62  ? 0.596   -21.165 13.306 1.00 29.92 ? 62  PHE C C   1 
ATOM   3775 O O   . PHE C 1 62  ? 1.571   -21.289 12.550 1.00 26.24 ? 62  PHE C O   1 
ATOM   3776 C CB  . PHE C 1 62  ? 1.276   -19.452 15.005 1.00 21.70 ? 62  PHE C CB  1 
ATOM   3777 C CG  . PHE C 1 62  ? 1.267   -18.999 16.455 1.00 30.89 ? 62  PHE C CG  1 
ATOM   3778 C CD1 . PHE C 1 62  ? 2.431   -19.016 17.225 1.00 35.41 ? 62  PHE C CD1 1 
ATOM   3779 C CD2 . PHE C 1 62  ? 0.096   -18.543 17.039 1.00 26.35 ? 62  PHE C CD2 1 
ATOM   3780 C CE1 . PHE C 1 62  ? 2.420   -18.597 18.555 1.00 30.68 ? 62  PHE C CE1 1 
ATOM   3781 C CE2 . PHE C 1 62  ? 0.075   -18.125 18.359 1.00 39.17 ? 62  PHE C CE2 1 
ATOM   3782 C CZ  . PHE C 1 62  ? 1.245   -18.153 19.125 1.00 33.06 ? 62  PHE C CZ  1 
ATOM   3783 N N   . SER C 1 63  ? -0.659  -21.273 12.886 1.00 23.81 ? 63  SER C N   1 
ATOM   3784 C CA  . SER C 1 63  ? -0.981  -21.353 11.465 1.00 26.15 ? 63  SER C CA  1 
ATOM   3785 C C   . SER C 1 63  ? -2.337  -20.681 11.239 1.00 32.48 ? 63  SER C C   1 
ATOM   3786 O O   . SER C 1 63  ? -3.034  -20.332 12.204 1.00 25.46 ? 63  SER C O   1 
ATOM   3787 C CB  . SER C 1 63  ? -1.012  -22.826 10.976 1.00 28.57 ? 63  SER C CB  1 
ATOM   3788 O OG  . SER C 1 63  ? -2.245  -23.476 11.275 1.00 25.07 ? 63  SER C OG  1 
ATOM   3789 N N   . GLY C 1 64  ? -2.704  -20.511 9.971  1.00 22.74 ? 64  GLY C N   1 
ATOM   3790 C CA  . GLY C 1 64  ? -3.934  -19.822 9.627  1.00 25.39 ? 64  GLY C CA  1 
ATOM   3791 C C   . GLY C 1 64  ? -4.558  -20.329 8.344  1.00 27.92 ? 64  GLY C C   1 
ATOM   3792 O O   . GLY C 1 64  ? -3.877  -20.876 7.485  1.00 29.22 ? 64  GLY C O   1 
ATOM   3793 N N   . SER C 1 65  ? -5.862  -20.150 8.207  1.00 24.45 ? 65  SER C N   1 
ATOM   3794 C CA  . SER C 1 65  ? -6.570  -20.704 7.062  1.00 24.25 ? 65  SER C CA  1 
ATOM   3795 C C   . SER C 1 65  ? -7.845  -19.931 6.750  1.00 20.96 ? 65  SER C C   1 
ATOM   3796 O O   . SER C 1 65  ? -8.303  -19.109 7.538  1.00 24.57 ? 65  SER C O   1 
ATOM   3797 C CB  . SER C 1 65  ? -6.908  -22.175 7.311  1.00 25.08 ? 65  SER C CB  1 
ATOM   3798 O OG  . SER C 1 65  ? -7.903  -22.277 8.324  1.00 34.39 ? 65  SER C OG  1 
ATOM   3799 N N   . GLY C 1 66  ? -8.413  -20.210 5.586  1.00 24.22 ? 66  GLY C N   1 
ATOM   3800 C CA  . GLY C 1 66  ? -9.657  -19.594 5.188  1.00 23.95 ? 66  GLY C CA  1 
ATOM   3801 C C   . GLY C 1 66  ? -9.538  -18.667 4.000  1.00 26.42 ? 66  GLY C C   1 
ATOM   3802 O O   . GLY C 1 66  ? -8.445  -18.210 3.647  1.00 28.28 ? 66  GLY C O   1 
ATOM   3803 N N   . SER C 1 67  ? -10.678 -18.402 3.373  1.00 28.60 ? 67  SER C N   1 
ATOM   3804 C CA  . SER C 1 67  ? -10.763 -17.442 2.279  1.00 28.59 ? 67  SER C CA  1 
ATOM   3805 C C   . SER C 1 67  ? -12.209 -17.031 2.116  1.00 32.91 ? 67  SER C C   1 
ATOM   3806 O O   . SER C 1 67  ? -13.119 -17.751 2.542  1.00 37.13 ? 67  SER C O   1 
ATOM   3807 C CB  . SER C 1 67  ? -10.267 -18.043 0.975  1.00 23.67 ? 67  SER C CB  1 
ATOM   3808 O OG  . SER C 1 67  ? -11.124 -19.084 0.566  1.00 47.72 ? 67  SER C OG  1 
ATOM   3809 N N   . GLY C 1 68  ? -12.425 -15.873 1.505  1.00 27.92 ? 68  GLY C N   1 
ATOM   3810 C CA  . GLY C 1 68  ? -13.769 -15.359 1.342  1.00 22.41 ? 68  GLY C CA  1 
ATOM   3811 C C   . GLY C 1 68  ? -14.172 -14.566 2.558  1.00 32.72 ? 68  GLY C C   1 
ATOM   3812 O O   . GLY C 1 68  ? -13.820 -13.387 2.670  1.00 33.67 ? 68  GLY C O   1 
ATOM   3813 N N   . THR C 1 69  ? -14.889 -15.207 3.481  1.00 27.35 ? 69  THR C N   1 
ATOM   3814 C CA  . THR C 1 69  ? -15.404 -14.508 4.661  1.00 32.27 ? 69  THR C CA  1 
ATOM   3815 C C   . THR C 1 69  ? -15.031 -15.164 5.983  1.00 29.68 ? 69  THR C C   1 
ATOM   3816 O O   . THR C 1 69  ? -14.990 -14.493 7.003  1.00 34.25 ? 69  THR C O   1 
ATOM   3817 C CB  . THR C 1 69  ? -16.949 -14.340 4.621  1.00 37.69 ? 69  THR C CB  1 
ATOM   3818 O OG1 . THR C 1 69  ? -17.584 -15.600 4.873  1.00 37.21 ? 69  THR C OG1 1 
ATOM   3819 C CG2 . THR C 1 69  ? -17.398 -13.794 3.278  1.00 30.19 ? 69  THR C CG2 1 
ATOM   3820 N N   . ASP C 1 70  ? -14.776 -16.469 5.967  1.00 31.33 ? 70  ASP C N   1 
ATOM   3821 C CA  . ASP C 1 70  ? -14.471 -17.200 7.195  1.00 28.39 ? 70  ASP C CA  1 
ATOM   3822 C C   . ASP C 1 70  ? -12.987 -17.502 7.360  1.00 28.48 ? 70  ASP C C   1 
ATOM   3823 O O   . ASP C 1 70  ? -12.388 -18.194 6.534  1.00 26.08 ? 70  ASP C O   1 
ATOM   3824 C CB  . ASP C 1 70  ? -15.276 -18.502 7.270  1.00 31.07 ? 70  ASP C CB  1 
ATOM   3825 C CG  . ASP C 1 70  ? -16.780 -18.267 7.277  1.00 37.82 ? 70  ASP C CG  1 
ATOM   3826 O OD1 . ASP C 1 70  ? -17.228 -17.161 7.654  1.00 34.21 ? 70  ASP C OD1 1 
ATOM   3827 O OD2 . ASP C 1 70  ? -17.514 -19.205 6.896  1.00 41.92 ? 70  ASP C OD2 1 
ATOM   3828 N N   . PHE C 1 71  ? -12.391 -16.988 8.433  1.00 26.57 ? 71  PHE C N   1 
ATOM   3829 C CA  . PHE C 1 71  ? -10.954 -17.169 8.633  1.00 26.72 ? 71  PHE C CA  1 
ATOM   3830 C C   . PHE C 1 71  ? -10.666 -17.771 10.007 1.00 28.89 ? 71  PHE C C   1 
ATOM   3831 O O   . PHE C 1 71  ? -11.447 -17.611 10.953 1.00 27.71 ? 71  PHE C O   1 
ATOM   3832 C CB  . PHE C 1 71  ? -10.179 -15.857 8.387  1.00 18.90 ? 71  PHE C CB  1 
ATOM   3833 C CG  . PHE C 1 71  ? -10.467 -15.227 7.044  1.00 24.57 ? 71  PHE C CG  1 
ATOM   3834 C CD1 . PHE C 1 71  ? -9.629  -15.447 5.961  1.00 25.05 ? 71  PHE C CD1 1 
ATOM   3835 C CD2 . PHE C 1 71  ? -11.597 -14.440 6.855  1.00 28.62 ? 71  PHE C CD2 1 
ATOM   3836 C CE1 . PHE C 1 71  ? -9.896  -14.877 4.725  1.00 23.43 ? 71  PHE C CE1 1 
ATOM   3837 C CE2 . PHE C 1 71  ? -11.877 -13.876 5.616  1.00 25.78 ? 71  PHE C CE2 1 
ATOM   3838 C CZ  . PHE C 1 71  ? -11.024 -14.093 4.555  1.00 24.43 ? 71  PHE C CZ  1 
ATOM   3839 N N   . THR C 1 72  ? -9.551  -18.485 10.099 1.00 22.89 ? 72  THR C N   1 
ATOM   3840 C CA  . THR C 1 72  ? -9.218  -19.216 11.307 1.00 27.08 ? 72  THR C CA  1 
ATOM   3841 C C   . THR C 1 72  ? -7.754  -19.008 11.675 1.00 28.45 ? 72  THR C C   1 
ATOM   3842 O O   . THR C 1 72  ? -6.866  -19.114 10.826 1.00 29.19 ? 72  THR C O   1 
ATOM   3843 C CB  . THR C 1 72  ? -9.480  -20.729 11.113 1.00 26.61 ? 72  THR C CB  1 
ATOM   3844 O OG1 . THR C 1 72  ? -10.861 -20.937 10.807 1.00 25.86 ? 72  THR C OG1 1 
ATOM   3845 C CG2 . THR C 1 72  ? -9.117  -21.515 12.371 1.00 27.02 ? 72  THR C CG2 1 
ATOM   3846 N N   . LEU C 1 73  ? -7.499  -18.699 12.939 1.00 29.90 ? 73  LEU C N   1 
ATOM   3847 C CA  . LEU C 1 73  ? -6.132  -18.716 13.446 1.00 30.22 ? 73  LEU C CA  1 
ATOM   3848 C C   . LEU C 1 73  ? -5.997  -19.955 14.323 1.00 30.94 ? 73  LEU C C   1 
ATOM   3849 O O   . LEU C 1 73  ? -6.889  -20.247 15.130 1.00 26.84 ? 73  LEU C O   1 
ATOM   3850 C CB  . LEU C 1 73  ? -5.812  -17.455 14.245 1.00 25.50 ? 73  LEU C CB  1 
ATOM   3851 C CG  . LEU C 1 73  ? -4.424  -17.462 14.892 1.00 29.71 ? 73  LEU C CG  1 
ATOM   3852 C CD1 . LEU C 1 73  ? -3.340  -17.257 13.837 1.00 29.63 ? 73  LEU C CD1 1 
ATOM   3853 C CD2 . LEU C 1 73  ? -4.302  -16.441 16.020 1.00 22.70 ? 73  LEU C CD2 1 
ATOM   3854 N N   . SER C 1 74  ? -4.903  -20.694 14.151 1.00 27.47 ? 74  SER C N   1 
ATOM   3855 C CA  . SER C 1 74  ? -4.738  -21.967 14.844 1.00 28.41 ? 74  SER C CA  1 
ATOM   3856 C C   . SER C 1 74  ? -3.436  -22.098 15.608 1.00 28.40 ? 74  SER C C   1 
ATOM   3857 O O   . SER C 1 74  ? -2.364  -21.801 15.088 1.00 30.04 ? 74  SER C O   1 
ATOM   3858 C CB  . SER C 1 74  ? -4.864  -23.128 13.862 1.00 28.58 ? 74  SER C CB  1 
ATOM   3859 O OG  . SER C 1 74  ? -6.203  -23.563 13.806 1.00 34.29 ? 74  SER C OG  1 
ATOM   3860 N N   . ILE C 1 75  ? -3.540  -22.534 16.858 1.00 34.07 ? 75  ILE C N   1 
ATOM   3861 C CA  . ILE C 1 75  ? -2.368  -22.916 17.637 1.00 32.47 ? 75  ILE C CA  1 
ATOM   3862 C C   . ILE C 1 75  ? -2.509  -24.393 17.944 1.00 38.73 ? 75  ILE C C   1 
ATOM   3863 O O   . ILE C 1 75  ? -3.371  -24.780 18.733 1.00 38.45 ? 75  ILE C O   1 
ATOM   3864 C CB  . ILE C 1 75  ? -2.280  -22.143 18.956 1.00 33.86 ? 75  ILE C CB  1 
ATOM   3865 C CG1 . ILE C 1 75  ? -2.547  -20.655 18.728 1.00 32.23 ? 75  ILE C CG1 1 
ATOM   3866 C CG2 . ILE C 1 75  ? -0.919  -22.357 19.609 1.00 36.01 ? 75  ILE C CG2 1 
ATOM   3867 C CD1 . ILE C 1 75  ? -2.488  -19.843 19.991 1.00 26.46 ? 75  ILE C CD1 1 
ATOM   3868 N N   . ASN C 1 76  ? -1.680  -25.221 17.314 1.00 39.19 ? 76  ASN C N   1 
ATOM   3869 C CA  . ASN C 1 76  ? -1.872  -26.669 17.396 1.00 51.35 ? 76  ASN C CA  1 
ATOM   3870 C C   . ASN C 1 76  ? -1.763  -27.246 18.816 1.00 48.63 ? 76  ASN C C   1 
ATOM   3871 O O   . ASN C 1 76  ? -2.586  -28.069 19.224 1.00 52.58 ? 76  ASN C O   1 
ATOM   3872 C CB  . ASN C 1 76  ? -0.993  -27.431 16.382 1.00 34.23 ? 76  ASN C CB  1 
ATOM   3873 C CG  . ASN C 1 76  ? 0.497   -27.317 16.671 1.00 49.62 ? 76  ASN C CG  1 
ATOM   3874 O OD1 . ASN C 1 76  ? 0.913   -26.958 17.773 1.00 53.35 ? 76  ASN C OD1 1 
ATOM   3875 N ND2 . ASN C 1 76  ? 1.312   -27.637 15.671 1.00 56.79 ? 76  ASN C ND2 1 
ATOM   3876 N N   . SER C 1 77  ? -0.760  -26.804 19.567 1.00 33.67 ? 77  SER C N   1 
ATOM   3877 C CA  . SER C 1 77  ? -0.606  -27.243 20.950 1.00 32.91 ? 77  SER C CA  1 
ATOM   3878 C C   . SER C 1 77  ? -0.352  -26.045 21.851 1.00 34.92 ? 77  SER C C   1 
ATOM   3879 O O   . SER C 1 77  ? 0.795   -25.636 22.057 1.00 33.90 ? 77  SER C O   1 
ATOM   3880 C CB  . SER C 1 77  ? 0.530   -28.254 21.077 1.00 29.77 ? 77  SER C CB  1 
ATOM   3881 O OG  . SER C 1 77  ? 0.584   -28.777 22.388 1.00 36.83 ? 77  SER C OG  1 
ATOM   3882 N N   . VAL C 1 78  ? -1.435  -25.492 22.386 1.00 25.13 ? 78  VAL C N   1 
ATOM   3883 C CA  . VAL C 1 78  ? -1.379  -24.244 23.137 1.00 32.15 ? 78  VAL C CA  1 
ATOM   3884 C C   . VAL C 1 78  ? -0.517  -24.335 24.407 1.00 35.63 ? 78  VAL C C   1 
ATOM   3885 O O   . VAL C 1 78  ? -0.492  -25.358 25.093 1.00 33.85 ? 78  VAL C O   1 
ATOM   3886 C CB  . VAL C 1 78  ? -2.803  -23.724 23.454 1.00 36.71 ? 78  VAL C CB  1 
ATOM   3887 C CG1 . VAL C 1 78  ? -3.489  -24.614 24.481 1.00 27.62 ? 78  VAL C CG1 1 
ATOM   3888 C CG2 . VAL C 1 78  ? -2.759  -22.276 23.918 1.00 37.74 ? 78  VAL C CG2 1 
ATOM   3889 N N   . GLU C 1 79  ? 0.217   -23.263 24.687 1.00 39.01 ? 79  GLU C N   1 
ATOM   3890 C CA  . GLU C 1 79  ? 1.093   -23.190 25.852 1.00 37.94 ? 79  GLU C CA  1 
ATOM   3891 C C   . GLU C 1 79  ? 0.708   -21.967 26.678 1.00 30.18 ? 79  GLU C C   1 
ATOM   3892 O O   . GLU C 1 79  ? 0.070   -21.046 26.165 1.00 27.72 ? 79  GLU C O   1 
ATOM   3893 C CB  . GLU C 1 79  ? 2.550   -23.071 25.406 1.00 37.50 ? 79  GLU C CB  1 
ATOM   3894 C CG  . GLU C 1 79  ? 2.921   -23.991 24.246 1.00 40.65 ? 79  GLU C CG  1 
ATOM   3895 C CD  . GLU C 1 79  ? 4.363   -23.821 23.789 1.00 48.42 ? 79  GLU C CD  1 
ATOM   3896 O OE1 . GLU C 1 79  ? 4.939   -22.734 24.020 1.00 41.23 ? 79  GLU C OE1 1 
ATOM   3897 O OE2 . GLU C 1 79  ? 4.919   -24.778 23.198 1.00 44.80 ? 79  GLU C OE2 1 
ATOM   3898 N N   . SER C 1 80  ? 1.094   -21.949 27.949 1.00 28.48 ? 80  SER C N   1 
ATOM   3899 C CA  . SER C 1 80  ? 0.763   -20.818 28.806 1.00 28.95 ? 80  SER C CA  1 
ATOM   3900 C C   . SER C 1 80  ? 1.429   -19.527 28.343 1.00 25.00 ? 80  SER C C   1 
ATOM   3901 O O   . SER C 1 80  ? 0.919   -18.443 28.594 1.00 30.15 ? 80  SER C O   1 
ATOM   3902 C CB  . SER C 1 80  ? 1.104   -21.120 30.261 1.00 35.80 ? 80  SER C CB  1 
ATOM   3903 O OG  . SER C 1 80  ? 2.297   -21.869 30.330 1.00 43.39 ? 80  SER C OG  1 
ATOM   3904 N N   . GLU C 1 81  ? 2.545   -19.635 27.633 1.00 28.47 ? 81  GLU C N   1 
ATOM   3905 C CA  . GLU C 1 81  ? 3.153   -18.455 27.019 1.00 27.24 ? 81  GLU C CA  1 
ATOM   3906 C C   . GLU C 1 81  ? 2.299   -17.866 25.889 1.00 29.84 ? 81  GLU C C   1 
ATOM   3907 O O   . GLU C 1 81  ? 2.569   -16.767 25.409 1.00 29.29 ? 81  GLU C O   1 
ATOM   3908 C CB  . GLU C 1 81  ? 4.563   -18.763 26.522 1.00 31.94 ? 81  GLU C CB  1 
ATOM   3909 C CG  . GLU C 1 81  ? 4.672   -20.020 25.686 1.00 42.01 ? 81  GLU C CG  1 
ATOM   3910 C CD  . GLU C 1 81  ? 6.100   -20.311 25.232 1.00 63.35 ? 81  GLU C CD  1 
ATOM   3911 O OE1 . GLU C 1 81  ? 6.448   -19.984 24.068 1.00 63.48 ? 81  GLU C OE1 1 
ATOM   3912 O OE2 . GLU C 1 81  ? 6.874   -20.878 26.038 1.00 75.32 ? 81  GLU C OE2 1 
ATOM   3913 N N   . ASP C 1 82  ? 1.257   -18.587 25.481 1.00 28.67 ? 82  ASP C N   1 
ATOM   3914 C CA  . ASP C 1 82  ? 0.347   -18.088 24.455 1.00 28.88 ? 82  ASP C CA  1 
ATOM   3915 C C   . ASP C 1 82  ? -0.802  -17.250 25.020 1.00 25.16 ? 82  ASP C C   1 
ATOM   3916 O O   . ASP C 1 82  ? -1.625  -16.749 24.265 1.00 28.32 ? 82  ASP C O   1 
ATOM   3917 C CB  . ASP C 1 82  ? -0.203  -19.233 23.598 1.00 25.20 ? 82  ASP C CB  1 
ATOM   3918 C CG  . ASP C 1 82  ? 0.887   -19.958 22.828 1.00 28.71 ? 82  ASP C CG  1 
ATOM   3919 O OD1 . ASP C 1 82  ? 1.893   -19.306 22.450 1.00 31.56 ? 82  ASP C OD1 1 
ATOM   3920 O OD2 . ASP C 1 82  ? 0.735   -21.179 22.597 1.00 27.98 ? 82  ASP C OD2 1 
ATOM   3921 N N   . ILE C 1 83  ? -0.864  -17.107 26.339 1.00 23.61 ? 83  ILE C N   1 
ATOM   3922 C CA  . ILE C 1 83  ? -1.852  -16.231 26.954 1.00 18.71 ? 83  ILE C CA  1 
ATOM   3923 C C   . ILE C 1 83  ? -1.683  -14.813 26.421 1.00 18.11 ? 83  ILE C C   1 
ATOM   3924 O O   . ILE C 1 83  ? -0.656  -14.176 26.642 1.00 14.67 ? 83  ILE C O   1 
ATOM   3925 C CB  . ILE C 1 83  ? -1.756  -16.252 28.501 1.00 27.44 ? 83  ILE C CB  1 
ATOM   3926 C CG1 . ILE C 1 83  ? -2.206  -17.618 29.049 1.00 34.63 ? 83  ILE C CG1 1 
ATOM   3927 C CG2 . ILE C 1 83  ? -2.609  -15.135 29.122 1.00 22.74 ? 83  ILE C CG2 1 
ATOM   3928 C CD1 . ILE C 1 83  ? -1.821  -17.876 30.507 1.00 28.24 ? 83  ILE C CD1 1 
ATOM   3929 N N   . ALA C 1 84  ? -2.693  -14.340 25.694 1.00 20.17 ? 84  ALA C N   1 
ATOM   3930 C CA  . ALA C 1 84  ? -2.670  -13.018 25.093 1.00 17.15 ? 84  ALA C CA  1 
ATOM   3931 C C   . ALA C 1 84  ? -4.018  -12.752 24.473 1.00 23.50 ? 84  ALA C C   1 
ATOM   3932 O O   . ALA C 1 84  ? -4.906  -13.598 24.514 1.00 21.22 ? 84  ALA C O   1 
ATOM   3933 C CB  . ALA C 1 84  ? -1.600  -12.941 24.012 1.00 14.65 ? 84  ALA C CB  1 
ATOM   3934 N N   . ASP C 1 85  ? -4.177  -11.565 23.899 1.00 25.33 ? 85  ASP C N   1 
ATOM   3935 C CA  . ASP C 1 85  ? -5.320  -11.303 23.046 1.00 21.09 ? 85  ASP C CA  1 
ATOM   3936 C C   . ASP C 1 85  ? -4.908  -11.530 21.600 1.00 24.59 ? 85  ASP C C   1 
ATOM   3937 O O   . ASP C 1 85  ? -3.731  -11.394 21.255 1.00 27.28 ? 85  ASP C O   1 
ATOM   3938 C CB  . ASP C 1 85  ? -5.818  -9.888  23.257 1.00 26.97 ? 85  ASP C CB  1 
ATOM   3939 C CG  . ASP C 1 85  ? -6.263  -9.653  24.678 1.00 30.87 ? 85  ASP C CG  1 
ATOM   3940 O OD1 . ASP C 1 85  ? -6.674  -10.635 25.333 1.00 27.72 ? 85  ASP C OD1 1 
ATOM   3941 O OD2 . ASP C 1 85  ? -6.195  -8.494  25.139 1.00 33.38 ? 85  ASP C OD2 1 
ATOM   3942 N N   . TYR C 1 86  ? -5.872  -11.890 20.761 1.00 21.20 ? 86  TYR C N   1 
ATOM   3943 C CA  . TYR C 1 86  ? -5.598  -12.190 19.362 1.00 21.34 ? 86  TYR C CA  1 
ATOM   3944 C C   . TYR C 1 86  ? -6.513  -11.414 18.424 1.00 20.23 ? 86  TYR C C   1 
ATOM   3945 O O   . TYR C 1 86  ? -7.731  -11.411 18.582 1.00 22.78 ? 86  TYR C O   1 
ATOM   3946 C CB  . TYR C 1 86  ? -5.679  -13.699 19.117 1.00 23.66 ? 86  TYR C CB  1 
ATOM   3947 C CG  . TYR C 1 86  ? -4.566  -14.453 19.806 1.00 24.59 ? 86  TYR C CG  1 
ATOM   3948 C CD1 . TYR C 1 86  ? -4.714  -14.915 21.111 1.00 19.69 ? 86  TYR C CD1 1 
ATOM   3949 C CD2 . TYR C 1 86  ? -3.353  -14.670 19.165 1.00 21.25 ? 86  TYR C CD2 1 
ATOM   3950 C CE1 . TYR C 1 86  ? -3.694  -15.601 21.749 1.00 19.26 ? 86  TYR C CE1 1 
ATOM   3951 C CE2 . TYR C 1 86  ? -2.320  -15.346 19.798 1.00 25.09 ? 86  TYR C CE2 1 
ATOM   3952 C CZ  . TYR C 1 86  ? -2.493  -15.813 21.091 1.00 26.24 ? 86  TYR C CZ  1 
ATOM   3953 O OH  . TYR C 1 86  ? -1.464  -16.494 21.719 1.00 23.03 ? 86  TYR C OH  1 
ATOM   3954 N N   . TYR C 1 87  ? -5.909  -10.742 17.450 1.00 23.21 ? 87  TYR C N   1 
ATOM   3955 C CA  . TYR C 1 87  ? -6.653  -9.850  16.568 1.00 23.62 ? 87  TYR C CA  1 
ATOM   3956 C C   . TYR C 1 87  ? -6.539  -10.252 15.114 1.00 22.68 ? 87  TYR C C   1 
ATOM   3957 O O   . TYR C 1 87  ? -5.490  -10.722 14.663 1.00 24.40 ? 87  TYR C O   1 
ATOM   3958 C CB  . TYR C 1 87  ? -6.184  -8.392  16.724 1.00 18.72 ? 87  TYR C CB  1 
ATOM   3959 C CG  . TYR C 1 87  ? -6.500  -7.800  18.077 1.00 22.20 ? 87  TYR C CG  1 
ATOM   3960 C CD1 . TYR C 1 87  ? -5.583  -7.869  19.114 1.00 24.01 ? 87  TYR C CD1 1 
ATOM   3961 C CD2 . TYR C 1 87  ? -7.722  -7.192  18.323 1.00 23.70 ? 87  TYR C CD2 1 
ATOM   3962 C CE1 . TYR C 1 87  ? -5.864  -7.343  20.353 1.00 26.54 ? 87  TYR C CE1 1 
ATOM   3963 C CE2 . TYR C 1 87  ? -8.012  -6.663  19.569 1.00 29.45 ? 87  TYR C CE2 1 
ATOM   3964 C CZ  . TYR C 1 87  ? -7.074  -6.744  20.577 1.00 23.42 ? 87  TYR C CZ  1 
ATOM   3965 O OH  . TYR C 1 87  ? -7.336  -6.222  21.813 1.00 31.05 ? 87  TYR C OH  1 
ATOM   3966 N N   . CYS C 1 88  ? -7.623  -10.049 14.380 1.00 16.23 ? 88  CYS C N   1 
ATOM   3967 C CA  . CYS C 1 88  ? -7.553  -10.137 12.941 1.00 19.60 ? 88  CYS C CA  1 
ATOM   3968 C C   . CYS C 1 88  ? -7.706  -8.748  12.293 1.00 26.31 ? 88  CYS C C   1 
ATOM   3969 O O   . CYS C 1 88  ? -8.312  -7.831  12.859 1.00 21.37 ? 88  CYS C O   1 
ATOM   3970 C CB  . CYS C 1 88  ? -8.574  -11.145 12.409 1.00 20.27 ? 88  CYS C CB  1 
ATOM   3971 S SG  . CYS C 1 88  ? -10.284 -10.644 12.599 1.00 26.79 ? 88  CYS C SG  1 
ATOM   3972 N N   . GLN C 1 89  ? -7.126  -8.607  11.106 1.00 23.52 ? 89  GLN C N   1 
ATOM   3973 C CA  . GLN C 1 89  ? -7.140  -7.351  10.364 1.00 20.86 ? 89  GLN C CA  1 
ATOM   3974 C C   . GLN C 1 89  ? -7.436  -7.678  8.913  1.00 21.76 ? 89  GLN C C   1 
ATOM   3975 O O   . GLN C 1 89  ? -6.909  -8.654  8.392  1.00 21.31 ? 89  GLN C O   1 
ATOM   3976 C CB  . GLN C 1 89  ? -5.775  -6.668  10.464 1.00 19.86 ? 89  GLN C CB  1 
ATOM   3977 C CG  . GLN C 1 89  ? -5.496  -5.639  9.374  1.00 19.55 ? 89  GLN C CG  1 
ATOM   3978 C CD  . GLN C 1 89  ? -4.003  -5.308  9.255  1.00 23.43 ? 89  GLN C CD  1 
ATOM   3979 O OE1 . GLN C 1 89  ? -3.152  -6.179  9.419  1.00 20.87 ? 89  GLN C OE1 1 
ATOM   3980 N NE2 . GLN C 1 89  ? -3.687  -4.047  8.975  1.00 22.35 ? 89  GLN C NE2 1 
ATOM   3981 N N   . GLN C 1 90  ? -8.290  -6.888  8.268  1.00 19.48 ? 90  GLN C N   1 
ATOM   3982 C CA  . GLN C 1 90  ? -8.517  -7.048  6.836  1.00 17.54 ? 90  GLN C CA  1 
ATOM   3983 C C   . GLN C 1 90  ? -7.944  -5.846  6.114  1.00 20.67 ? 90  GLN C C   1 
ATOM   3984 O O   . GLN C 1 90  ? -7.970  -4.730  6.645  1.00 17.84 ? 90  GLN C O   1 
ATOM   3985 C CB  . GLN C 1 90  ? -10.008 -7.216  6.505  1.00 18.70 ? 90  GLN C CB  1 
ATOM   3986 C CG  . GLN C 1 90  ? -10.870 -5.966  6.651  1.00 15.90 ? 90  GLN C CG  1 
ATOM   3987 C CD  . GLN C 1 90  ? -10.725 -4.972  5.489  1.00 24.10 ? 90  GLN C CD  1 
ATOM   3988 O OE1 . GLN C 1 90  ? -10.448 -5.356  4.344  1.00 16.53 ? 90  GLN C OE1 1 
ATOM   3989 N NE2 . GLN C 1 90  ? -10.886 -3.680  5.796  1.00 24.44 ? 90  GLN C NE2 1 
ATOM   3990 N N   . ASN C 1 91  ? -7.447  -6.067  4.897  1.00 24.73 ? 91  ASN C N   1 
ATOM   3991 C CA  . ASN C 1 91  ? -7.017  -4.963  4.037  1.00 23.73 ? 91  ASN C CA  1 
ATOM   3992 C C   . ASN C 1 91  ? -7.393  -5.137  2.557  1.00 26.23 ? 91  ASN C C   1 
ATOM   3993 O O   . ASN C 1 91  ? -6.714  -4.640  1.665  1.00 27.30 ? 91  ASN C O   1 
ATOM   3994 C CB  . ASN C 1 91  ? -5.519  -4.702  4.186  1.00 20.67 ? 91  ASN C CB  1 
ATOM   3995 C CG  . ASN C 1 91  ? -5.091  -3.393  3.554  1.00 24.69 ? 91  ASN C CG  1 
ATOM   3996 O OD1 . ASN C 1 91  ? -5.741  -2.352  3.724  1.00 24.32 ? 91  ASN C OD1 1 
ATOM   3997 N ND2 . ASN C 1 91  ? -4.006  -3.443  2.796  1.00 22.25 ? 91  ASN C ND2 1 
ATOM   3998 N N   . ASN C 1 92  ? -8.487  -5.838  2.297  1.00 27.55 ? 92  ASN C N   1 
ATOM   3999 C CA  . ASN C 1 92  ? -9.031  -5.894  0.944  1.00 27.92 ? 92  ASN C CA  1 
ATOM   4000 C C   . ASN C 1 92  ? -9.731  -4.572  0.587  1.00 30.73 ? 92  ASN C C   1 
ATOM   4001 O O   . ASN C 1 92  ? -9.621  -4.072  -0.535 1.00 28.98 ? 92  ASN C O   1 
ATOM   4002 C CB  . ASN C 1 92  ? -9.982  -7.085  0.797  1.00 24.97 ? 92  ASN C CB  1 
ATOM   4003 C CG  . ASN C 1 92  ? -10.494 -7.258  -0.630 1.00 26.33 ? 92  ASN C CG  1 
ATOM   4004 O OD1 . ASN C 1 92  ? -9.809  -7.815  -1.491 1.00 22.37 ? 92  ASN C OD1 1 
ATOM   4005 N ND2 . ASN C 1 92  ? -11.715 -6.802  -0.873 1.00 28.53 ? 92  ASN C ND2 1 
ATOM   4006 N N   . ASN C 1 93  ? -10.445 -4.006  1.553  1.00 24.24 ? 93  ASN C N   1 
ATOM   4007 C CA  . ASN C 1 93  ? -11.113 -2.732  1.353  1.00 27.89 ? 93  ASN C CA  1 
ATOM   4008 C C   . ASN C 1 93  ? -10.507 -1.629  2.203  1.00 24.69 ? 93  ASN C C   1 
ATOM   4009 O O   . ASN C 1 93  ? -10.066 -1.879  3.308  1.00 28.41 ? 93  ASN C O   1 
ATOM   4010 C CB  . ASN C 1 93  ? -12.615 -2.865  1.599  1.00 26.12 ? 93  ASN C CB  1 
ATOM   4011 C CG  . ASN C 1 93  ? -13.305 -3.674  0.510  1.00 44.95 ? 93  ASN C CG  1 
ATOM   4012 O OD1 . ASN C 1 93  ? -13.248 -4.912  0.493  1.00 44.22 ? 93  ASN C OD1 1 
ATOM   4013 N ND2 . ASN C 1 93  ? -13.946 -2.976  -0.421 1.00 44.59 ? 93  ASN C ND2 1 
ATOM   4014 N N   . TRP C 1 94  ? -10.446 -0.420  1.657  1.00 28.08 ? 94  TRP C N   1 
ATOM   4015 C CA  . TRP C 1 94  ? -9.893  0.718   2.374  1.00 23.86 ? 94  TRP C CA  1 
ATOM   4016 C C   . TRP C 1 94  ? -11.007 1.356   3.179  1.00 23.64 ? 94  TRP C C   1 
ATOM   4017 O O   . TRP C 1 94  ? -12.075 1.637   2.643  1.00 29.11 ? 94  TRP C O   1 
ATOM   4018 C CB  . TRP C 1 94  ? -9.293  1.746   1.399  1.00 20.08 ? 94  TRP C CB  1 
ATOM   4019 C CG  . TRP C 1 94  ? -8.517  2.860   2.058  1.00 22.66 ? 94  TRP C CG  1 
ATOM   4020 C CD1 . TRP C 1 94  ? -7.160  2.933   2.221  1.00 27.48 ? 94  TRP C CD1 1 
ATOM   4021 C CD2 . TRP C 1 94  ? -9.055  4.051   2.657  1.00 23.77 ? 94  TRP C CD2 1 
ATOM   4022 N NE1 . TRP C 1 94  ? -6.822  4.099   2.870  1.00 19.37 ? 94  TRP C NE1 1 
ATOM   4023 C CE2 . TRP C 1 94  ? -7.965  4.799   3.152  1.00 18.80 ? 94  TRP C CE2 1 
ATOM   4024 C CE3 . TRP C 1 94  ? -10.350 4.559   2.817  1.00 22.01 ? 94  TRP C CE3 1 
ATOM   4025 C CZ2 . TRP C 1 94  ? -8.134  6.028   3.787  1.00 19.13 ? 94  TRP C CZ2 1 
ATOM   4026 C CZ3 . TRP C 1 94  ? -10.514 5.777   3.458  1.00 20.94 ? 94  TRP C CZ3 1 
ATOM   4027 C CH2 . TRP C 1 94  ? -9.414  6.497   3.930  1.00 20.72 ? 94  TRP C CH2 1 
ATOM   4028 N N   . PRO C 1 95  ? -10.743 1.637   4.463  1.00 29.12 ? 95  PRO C N   1 
ATOM   4029 C CA  . PRO C 1 95  ? -9.420  1.462   5.080  1.00 18.40 ? 95  PRO C CA  1 
ATOM   4030 C C   . PRO C 1 95  ? -9.261  0.126   5.786  1.00 17.81 ? 95  PRO C C   1 
ATOM   4031 O O   . PRO C 1 95  ? -10.244 -0.589  6.027  1.00 19.21 ? 95  PRO C O   1 
ATOM   4032 C CB  . PRO C 1 95  ? -9.383  2.591   6.103  1.00 27.44 ? 95  PRO C CB  1 
ATOM   4033 C CG  . PRO C 1 95  ? -10.845 2.674   6.581  1.00 31.18 ? 95  PRO C CG  1 
ATOM   4034 C CD  . PRO C 1 95  ? -11.709 2.272   5.384  1.00 29.45 ? 95  PRO C CD  1 
ATOM   4035 N N   . THR C 1 96  ? -8.022  -0.205  6.124  1.00 17.70 ? 96  THR C N   1 
ATOM   4036 C CA  . THR C 1 96  ? -7.767  -1.411  6.882  1.00 17.32 ? 96  THR C CA  1 
ATOM   4037 C C   . THR C 1 96  ? -8.500  -1.334  8.225  1.00 21.69 ? 96  THR C C   1 
ATOM   4038 O O   . THR C 1 96  ? -8.546  -0.281  8.863  1.00 21.96 ? 96  THR C O   1 
ATOM   4039 C CB  . THR C 1 96  ? -6.260  -1.666  7.052  1.00 16.15 ? 96  THR C CB  1 
ATOM   4040 O OG1 . THR C 1 96  ? -6.047  -2.956  7.626  1.00 11.77 ? 96  THR C OG1 1 
ATOM   4041 C CG2 . THR C 1 96  ? -5.620  -0.611  7.913  1.00 14.77 ? 96  THR C CG2 1 
ATOM   4042 N N   . THR C 1 97  ? -9.124  -2.438  8.621  1.00 20.48 ? 97  THR C N   1 
ATOM   4043 C CA  . THR C 1 97  ? -9.882  -2.471  9.854  1.00 17.56 ? 97  THR C CA  1 
ATOM   4044 C C   . THR C 1 97  ? -9.547  -3.728  10.628 1.00 24.15 ? 97  THR C C   1 
ATOM   4045 O O   . THR C 1 97  ? -9.174  -4.746  10.045 1.00 21.11 ? 97  THR C O   1 
ATOM   4046 C CB  . THR C 1 97  ? -11.404 -2.409  9.597  1.00 20.34 ? 97  THR C CB  1 
ATOM   4047 O OG1 . THR C 1 97  ? -11.779 -3.435  8.675  1.00 23.46 ? 97  THR C OG1 1 
ATOM   4048 C CG2 . THR C 1 97  ? -11.801 -1.063  9.022  1.00 19.96 ? 97  THR C CG2 1 
ATOM   4049 N N   . PHE C 1 98  ? -9.679  -3.644  11.947 1.00 23.51 ? 98  PHE C N   1 
ATOM   4050 C CA  . PHE C 1 98  ? -9.340  -4.752  12.832 1.00 23.02 ? 98  PHE C CA  1 
ATOM   4051 C C   . PHE C 1 98  ? -10.589 -5.335  13.497 1.00 21.12 ? 98  PHE C C   1 
ATOM   4052 O O   . PHE C 1 98  ? -11.574 -4.626  13.699 1.00 22.92 ? 98  PHE C O   1 
ATOM   4053 C CB  . PHE C 1 98  ? -8.385  -4.276  13.927 1.00 14.40 ? 98  PHE C CB  1 
ATOM   4054 C CG  . PHE C 1 98  ? -7.018  -3.898  13.442 1.00 13.64 ? 98  PHE C CG  1 
ATOM   4055 C CD1 . PHE C 1 98  ? -6.764  -2.625  12.963 1.00 16.68 ? 98  PHE C CD1 1 
ATOM   4056 C CD2 . PHE C 1 98  ? -5.969  -4.799  13.517 1.00 16.86 ? 98  PHE C CD2 1 
ATOM   4057 C CE1 . PHE C 1 98  ? -5.491  -2.255  12.548 1.00 12.58 ? 98  PHE C CE1 1 
ATOM   4058 C CE2 . PHE C 1 98  ? -4.690  -4.445  13.099 1.00 13.84 ? 98  PHE C CE2 1 
ATOM   4059 C CZ  . PHE C 1 98  ? -4.450  -3.169  12.611 1.00 15.34 ? 98  PHE C CZ  1 
ATOM   4060 N N   . GLY C 1 99  ? -10.537 -6.617  13.854 1.00 21.64 ? 99  GLY C N   1 
ATOM   4061 C CA  . GLY C 1 99  ? -11.570 -7.220  14.687 1.00 24.06 ? 99  GLY C CA  1 
ATOM   4062 C C   . GLY C 1 99  ? -11.506 -6.707  16.125 1.00 24.55 ? 99  GLY C C   1 
ATOM   4063 O O   . GLY C 1 99  ? -10.636 -5.902  16.473 1.00 24.59 ? 99  GLY C O   1 
ATOM   4064 N N   . ALA C 1 100 ? -12.421 -7.173  16.970 1.00 26.13 ? 100 ALA C N   1 
ATOM   4065 C CA  . ALA C 1 100 ? -12.508 -6.685  18.347 1.00 20.43 ? 100 ALA C CA  1 
ATOM   4066 C C   . ALA C 1 100 ? -11.598 -7.485  19.272 1.00 26.29 ? 100 ALA C C   1 
ATOM   4067 O O   . ALA C 1 100 ? -11.312 -7.076  20.398 1.00 21.28 ? 100 ALA C O   1 
ATOM   4068 C CB  . ALA C 1 100 ? -13.939 -6.727  18.839 1.00 8.25  ? 100 ALA C CB  1 
ATOM   4069 N N   . GLY C 1 101 ? -11.154 -8.640  18.797 1.00 26.02 ? 101 GLY C N   1 
ATOM   4070 C CA  . GLY C 1 101 ? -10.213 -9.443  19.553 1.00 21.23 ? 101 GLY C CA  1 
ATOM   4071 C C   . GLY C 1 101 ? -10.857 -10.610 20.264 1.00 21.78 ? 101 GLY C C   1 
ATOM   4072 O O   . GLY C 1 101 ? -12.059 -10.613 20.521 1.00 25.74 ? 101 GLY C O   1 
ATOM   4073 N N   . THR C 1 102 ? -10.040 -11.612 20.564 1.00 24.39 ? 102 THR C N   1 
ATOM   4074 C CA  . THR C 1 102 ? -10.449 -12.756 21.368 1.00 27.13 ? 102 THR C CA  1 
ATOM   4075 C C   . THR C 1 102 ? -9.408  -12.966 22.459 1.00 22.86 ? 102 THR C C   1 
ATOM   4076 O O   . THR C 1 102 ? -8.221  -13.085 22.167 1.00 23.14 ? 102 THR C O   1 
ATOM   4077 C CB  . THR C 1 102 ? -10.570 -14.049 20.511 1.00 30.12 ? 102 THR C CB  1 
ATOM   4078 O OG1 . THR C 1 102 ? -11.783 -14.010 19.745 1.00 33.49 ? 102 THR C OG1 1 
ATOM   4079 C CG2 . THR C 1 102 ? -10.560 -15.307 21.396 1.00 26.36 ? 102 THR C CG2 1 
ATOM   4080 N N   . LYS C 1 103 ? -9.865  -12.994 23.710 1.00 29.45 ? 103 LYS C N   1 
ATOM   4081 C CA  . LYS C 1 103 ? -9.037  -13.260 24.896 1.00 27.58 ? 103 LYS C CA  1 
ATOM   4082 C C   . LYS C 1 103 ? -8.744  -14.751 25.002 1.00 22.95 ? 103 LYS C C   1 
ATOM   4083 O O   . LYS C 1 103 ? -9.670  -15.557 25.074 1.00 29.18 ? 103 LYS C O   1 
ATOM   4084 C CB  . LYS C 1 103 ? -9.825  -12.840 26.147 1.00 31.37 ? 103 LYS C CB  1 
ATOM   4085 C CG  . LYS C 1 103 ? -9.114  -11.927 27.137 1.00 23.66 ? 103 LYS C CG  1 
ATOM   4086 C CD  . LYS C 1 103 ? -8.306  -12.710 28.129 1.00 30.94 ? 103 LYS C CD  1 
ATOM   4087 C CE  . LYS C 1 103 ? -7.833  -11.817 29.261 1.00 34.09 ? 103 LYS C CE  1 
ATOM   4088 N NZ  . LYS C 1 103 ? -8.929  -11.345 30.143 1.00 30.49 ? 103 LYS C NZ  1 
ATOM   4089 N N   . LEU C 1 104 ? -7.475  -15.134 25.016 1.00 23.51 ? 104 LEU C N   1 
ATOM   4090 C CA  . LEU C 1 104 ? -7.126  -16.532 25.275 1.00 20.58 ? 104 LEU C CA  1 
ATOM   4091 C C   . LEU C 1 104 ? -6.836  -16.736 26.756 1.00 21.81 ? 104 LEU C C   1 
ATOM   4092 O O   . LEU C 1 104 ? -5.954  -16.085 27.321 1.00 20.54 ? 104 LEU C O   1 
ATOM   4093 C CB  . LEU C 1 104 ? -5.920  -16.973 24.445 1.00 16.75 ? 104 LEU C CB  1 
ATOM   4094 C CG  . LEU C 1 104 ? -5.488  -18.441 24.563 1.00 24.18 ? 104 LEU C CG  1 
ATOM   4095 C CD1 . LEU C 1 104 ? -6.619  -19.397 24.193 1.00 18.92 ? 104 LEU C CD1 1 
ATOM   4096 C CD2 . LEU C 1 104 ? -4.227  -18.729 23.725 1.00 19.62 ? 104 LEU C CD2 1 
ATOM   4097 N N   . GLU C 1 105 ? -7.597  -17.631 27.376 1.00 23.58 ? 105 GLU C N   1 
ATOM   4098 C CA  . GLU C 1 105 ? -7.388  -18.000 28.775 1.00 31.31 ? 105 GLU C CA  1 
ATOM   4099 C C   . GLU C 1 105 ? -6.983  -19.458 28.897 1.00 28.96 ? 105 GLU C C   1 
ATOM   4100 O O   . GLU C 1 105 ? -7.464  -20.318 28.151 1.00 24.32 ? 105 GLU C O   1 
ATOM   4101 C CB  . GLU C 1 105 ? -8.666  -17.801 29.578 1.00 26.84 ? 105 GLU C CB  1 
ATOM   4102 C CG  . GLU C 1 105 ? -9.238  -16.403 29.519 1.00 37.68 ? 105 GLU C CG  1 
ATOM   4103 C CD  . GLU C 1 105 ? -10.213 -16.152 30.656 1.00 43.81 ? 105 GLU C CD  1 
ATOM   4104 O OE1 . GLU C 1 105 ? -11.059 -17.033 30.933 1.00 36.14 ? 105 GLU C OE1 1 
ATOM   4105 O OE2 . GLU C 1 105 ? -10.111 -15.084 31.287 1.00 46.21 ? 105 GLU C OE2 1 
ATOM   4106 N N   . LEU C 1 106 ? -6.115  -19.748 29.852 1.00 22.59 ? 106 LEU C N   1 
ATOM   4107 C CA  . LEU C 1 106 ? -5.735  -21.133 30.068 1.00 25.25 ? 106 LEU C CA  1 
ATOM   4108 C C   . LEU C 1 106 ? -6.307  -21.740 31.337 1.00 26.43 ? 106 LEU C C   1 
ATOM   4109 O O   . LEU C 1 106 ? -6.344  -21.110 32.384 1.00 28.06 ? 106 LEU C O   1 
ATOM   4110 C CB  . LEU C 1 106 ? -4.227  -21.329 29.984 1.00 25.87 ? 106 LEU C CB  1 
ATOM   4111 C CG  . LEU C 1 106 ? -3.895  -21.878 28.590 1.00 28.80 ? 106 LEU C CG  1 
ATOM   4112 C CD1 . LEU C 1 106 ? -4.129  -20.805 27.519 1.00 31.55 ? 106 LEU C CD1 1 
ATOM   4113 C CD2 . LEU C 1 106 ? -2.489  -22.421 28.521 1.00 33.21 ? 106 LEU C CD2 1 
ATOM   4114 N N   . LYS C 1 107 ? -6.791  -22.967 31.209 1.00 27.88 ? 107 LYS C N   1 
ATOM   4115 C CA  . LYS C 1 107 ? -7.272  -23.722 32.343 1.00 27.73 ? 107 LYS C CA  1 
ATOM   4116 C C   . LYS C 1 107 ? -6.080  -24.362 33.026 1.00 33.88 ? 107 LYS C C   1 
ATOM   4117 O O   . LYS C 1 107 ? -5.076  -24.669 32.382 1.00 29.78 ? 107 LYS C O   1 
ATOM   4118 C CB  . LYS C 1 107 ? -8.252  -24.801 31.885 1.00 27.40 ? 107 LYS C CB  1 
ATOM   4119 C CG  . LYS C 1 107 ? -9.629  -24.273 31.506 1.00 30.35 ? 107 LYS C CG  1 
ATOM   4120 C CD  . LYS C 1 107 ? -10.414 -25.324 30.746 1.00 44.83 ? 107 LYS C CD  1 
ATOM   4121 C CE  . LYS C 1 107 ? -11.665 -24.729 30.123 1.00 51.86 ? 107 LYS C CE  1 
ATOM   4122 N NZ  . LYS C 1 107 ? -12.265 -25.669 29.136 1.00 48.66 ? 107 LYS C NZ  1 
ATOM   4123 N N   . ARG C 1 108 ? -6.188  -24.536 34.336 1.00 25.50 ? 108 ARG C N   1 
ATOM   4124 C CA  . ARG C 1 108 ? -5.203  -25.285 35.083 1.00 21.51 ? 108 ARG C CA  1 
ATOM   4125 C C   . ARG C 1 108 ? -5.841  -25.766 36.385 1.00 24.38 ? 108 ARG C C   1 
ATOM   4126 O O   . ARG C 1 108 ? -6.972  -25.412 36.711 1.00 27.48 ? 108 ARG C O   1 
ATOM   4127 C CB  . ARG C 1 108 ? -3.948  -24.445 35.355 1.00 18.36 ? 108 ARG C CB  1 
ATOM   4128 C CG  . ARG C 1 108 ? -4.192  -23.168 36.143 1.00 18.68 ? 108 ARG C CG  1 
ATOM   4129 C CD  . ARG C 1 108 ? -2.995  -22.834 37.024 1.00 20.15 ? 108 ARG C CD  1 
ATOM   4130 N NE  . ARG C 1 108 ? -2.886  -23.751 38.160 1.00 17.35 ? 108 ARG C NE  1 
ATOM   4131 C CZ  . ARG C 1 108 ? -1.737  -24.115 38.718 1.00 21.87 ? 108 ARG C CZ  1 
ATOM   4132 N NH1 . ARG C 1 108 ? -0.585  -23.645 38.253 1.00 26.67 ? 108 ARG C NH1 1 
ATOM   4133 N NH2 . ARG C 1 108 ? -1.732  -24.966 39.734 1.00 22.20 ? 108 ARG C NH2 1 
ATOM   4134 N N   . THR C 1 109 ? -5.109  -26.587 37.117 1.00 18.66 ? 109 THR C N   1 
ATOM   4135 C CA  . THR C 1 109 ? -5.589  -27.095 38.378 1.00 20.36 ? 109 THR C CA  1 
ATOM   4136 C C   . THR C 1 109 ? -5.691  -25.958 39.376 1.00 22.15 ? 109 THR C C   1 
ATOM   4137 O O   . THR C 1 109 ? -4.864  -25.043 39.385 1.00 26.79 ? 109 THR C O   1 
ATOM   4138 C CB  . THR C 1 109 ? -4.643  -28.179 38.948 1.00 25.23 ? 109 THR C CB  1 
ATOM   4139 O OG1 . THR C 1 109 ? -3.340  -27.619 39.125 1.00 19.23 ? 109 THR C OG1 1 
ATOM   4140 C CG2 . THR C 1 109 ? -4.561  -29.374 38.007 1.00 11.70 ? 109 THR C CG2 1 
ATOM   4141 N N   . VAL C 1 110 ? -6.734  -26.022 40.189 1.00 16.31 ? 110 VAL C N   1 
ATOM   4142 C CA  . VAL C 1 110 ? -6.887  -25.180 41.361 1.00 19.25 ? 110 VAL C CA  1 
ATOM   4143 C C   . VAL C 1 110 ? -5.576  -25.033 42.161 1.00 22.03 ? 110 VAL C C   1 
ATOM   4144 O O   . VAL C 1 110 ? -4.899  -26.012 42.454 1.00 23.23 ? 110 VAL C O   1 
ATOM   4145 C CB  . VAL C 1 110 ? -7.978  -25.760 42.286 1.00 18.70 ? 110 VAL C CB  1 
ATOM   4146 C CG1 . VAL C 1 110 ? -8.130  -24.923 43.525 1.00 22.47 ? 110 VAL C CG1 1 
ATOM   4147 C CG2 . VAL C 1 110 ? -9.305  -25.873 41.539 1.00 14.58 ? 110 VAL C CG2 1 
ATOM   4148 N N   . ALA C 1 111 ? -5.228  -23.795 42.491 1.00 19.58 ? 111 ALA C N   1 
ATOM   4149 C CA  . ALA C 1 111 ? -4.112  -23.502 43.371 1.00 18.52 ? 111 ALA C CA  1 
ATOM   4150 C C   . ALA C 1 111 ? -4.554  -22.436 44.360 1.00 22.76 ? 111 ALA C C   1 
ATOM   4151 O O   . ALA C 1 111 ? -5.044  -21.378 43.967 1.00 22.52 ? 111 ALA C O   1 
ATOM   4152 C CB  . ALA C 1 111 ? -2.920  -23.012 42.584 1.00 16.41 ? 111 ALA C CB  1 
ATOM   4153 N N   . ALA C 1 112 ? -4.386  -22.729 45.646 1.00 23.63 ? 112 ALA C N   1 
ATOM   4154 C CA  . ALA C 1 112 ? -4.781  -21.818 46.704 1.00 19.51 ? 112 ALA C CA  1 
ATOM   4155 C C   . ALA C 1 112 ? -3.811  -20.645 46.760 1.00 20.90 ? 112 ALA C C   1 
ATOM   4156 O O   . ALA C 1 112 ? -2.628  -20.806 46.479 1.00 25.77 ? 112 ALA C O   1 
ATOM   4157 C CB  . ALA C 1 112 ? -4.807  -22.549 48.023 1.00 27.31 ? 112 ALA C CB  1 
ATOM   4158 N N   . PRO C 1 113 ? -4.309  -19.450 47.120 1.00 22.95 ? 113 PRO C N   1 
ATOM   4159 C CA  . PRO C 1 113 ? -3.426  -18.289 47.203 1.00 21.41 ? 113 PRO C CA  1 
ATOM   4160 C C   . PRO C 1 113 ? -2.616  -18.309 48.473 1.00 22.84 ? 113 PRO C C   1 
ATOM   4161 O O   . PRO C 1 113 ? -3.125  -18.704 49.529 1.00 24.15 ? 113 PRO C O   1 
ATOM   4162 C CB  . PRO C 1 113 ? -4.405  -17.114 47.272 1.00 19.24 ? 113 PRO C CB  1 
ATOM   4163 C CG  . PRO C 1 113 ? -5.594  -17.683 47.958 1.00 21.88 ? 113 PRO C CG  1 
ATOM   4164 C CD  . PRO C 1 113 ? -5.707  -19.085 47.411 1.00 28.86 ? 113 PRO C CD  1 
ATOM   4165 N N   . SER C 1 114 ? -1.361  -17.895 48.355 1.00 18.74 ? 114 SER C N   1 
ATOM   4166 C CA  . SER C 1 114 ? -0.564  -17.518 49.507 1.00 17.75 ? 114 SER C CA  1 
ATOM   4167 C C   . SER C 1 114 ? -0.926  -16.074 49.849 1.00 22.28 ? 114 SER C C   1 
ATOM   4168 O O   . SER C 1 114 ? -0.945  -15.207 48.966 1.00 21.00 ? 114 SER C O   1 
ATOM   4169 C CB  . SER C 1 114 ? 0.916   -17.625 49.175 1.00 9.99  ? 114 SER C CB  1 
ATOM   4170 O OG  . SER C 1 114 ? 1.226   -18.952 48.818 1.00 20.55 ? 114 SER C OG  1 
ATOM   4171 N N   . VAL C 1 115 ? -1.218  -15.826 51.121 1.00 14.95 ? 115 VAL C N   1 
ATOM   4172 C CA  . VAL C 1 115 ? -1.688  -14.519 51.574 1.00 16.54 ? 115 VAL C CA  1 
ATOM   4173 C C   . VAL C 1 115 ? -0.602  -13.801 52.395 1.00 19.10 ? 115 VAL C C   1 
ATOM   4174 O O   . VAL C 1 115 ? 0.163   -14.450 53.101 1.00 15.11 ? 115 VAL C O   1 
ATOM   4175 C CB  . VAL C 1 115 ? -2.980  -14.668 52.433 1.00 16.39 ? 115 VAL C CB  1 
ATOM   4176 C CG1 . VAL C 1 115 ? -3.560  -13.311 52.805 1.00 11.95 ? 115 VAL C CG1 1 
ATOM   4177 C CG2 . VAL C 1 115 ? -4.010  -15.507 51.701 1.00 10.39 ? 115 VAL C CG2 1 
ATOM   4178 N N   . PHE C 1 116 ? -0.542  -12.472 52.295 1.00 14.24 ? 116 PHE C N   1 
ATOM   4179 C CA  . PHE C 1 116 ? 0.437   -11.660 53.017 1.00 14.06 ? 116 PHE C CA  1 
ATOM   4180 C C   . PHE C 1 116 ? -0.179  -10.313 53.335 1.00 23.23 ? 116 PHE C C   1 
ATOM   4181 O O   . PHE C 1 116 ? -0.824  -9.701  52.465 1.00 21.03 ? 116 PHE C O   1 
ATOM   4182 C CB  . PHE C 1 116 ? 1.668   -11.370 52.154 1.00 13.75 ? 116 PHE C CB  1 
ATOM   4183 C CG  . PHE C 1 116 ? 2.417   -12.588 51.691 1.00 12.43 ? 116 PHE C CG  1 
ATOM   4184 C CD1 . PHE C 1 116 ? 2.104   -13.194 50.491 1.00 10.98 ? 116 PHE C CD1 1 
ATOM   4185 C CD2 . PHE C 1 116 ? 3.469   -13.084 52.431 1.00 11.93 ? 116 PHE C CD2 1 
ATOM   4186 C CE1 . PHE C 1 116 ? 2.806   -14.293 50.051 1.00 14.92 ? 116 PHE C CE1 1 
ATOM   4187 C CE2 . PHE C 1 116 ? 4.187   -14.175 51.992 1.00 15.48 ? 116 PHE C CE2 1 
ATOM   4188 C CZ  . PHE C 1 116 ? 3.851   -14.787 50.800 1.00 13.73 ? 116 PHE C CZ  1 
ATOM   4189 N N   . ILE C 1 117 ? 0.031   -9.842  54.563 1.00 18.69 ? 117 ILE C N   1 
ATOM   4190 C CA  . ILE C 1 117 ? -0.465  -8.532  54.960 1.00 20.50 ? 117 ILE C CA  1 
ATOM   4191 C C   . ILE C 1 117 ? 0.687   -7.568  55.242 1.00 21.35 ? 117 ILE C C   1 
ATOM   4192 O O   . ILE C 1 117 ? 1.718   -7.969  55.768 1.00 23.24 ? 117 ILE C O   1 
ATOM   4193 C CB  . ILE C 1 117 ? -1.431  -8.617  56.164 1.00 23.24 ? 117 ILE C CB  1 
ATOM   4194 C CG1 . ILE C 1 117 ? -2.177  -7.295  56.351 1.00 16.20 ? 117 ILE C CG1 1 
ATOM   4195 C CG2 . ILE C 1 117 ? -0.700  -9.027  57.427 1.00 14.57 ? 117 ILE C CG2 1 
ATOM   4196 C CD1 . ILE C 1 117 ? -3.276  -7.360  57.390 1.00 21.02 ? 117 ILE C CD1 1 
ATOM   4197 N N   . PHE C 1 118 ? 0.499   -6.309  54.856 1.00 21.91 ? 118 PHE C N   1 
ATOM   4198 C CA  . PHE C 1 118 ? 1.508   -5.260  54.990 1.00 18.12 ? 118 PHE C CA  1 
ATOM   4199 C C   . PHE C 1 118 ? 0.905   -4.027  55.674 1.00 21.86 ? 118 PHE C C   1 
ATOM   4200 O O   . PHE C 1 118 ? -0.023  -3.410  55.154 1.00 20.03 ? 118 PHE C O   1 
ATOM   4201 C CB  . PHE C 1 118 ? 2.000   -4.812  53.619 1.00 15.41 ? 118 PHE C CB  1 
ATOM   4202 C CG  . PHE C 1 118 ? 2.610   -5.899  52.790 1.00 21.59 ? 118 PHE C CG  1 
ATOM   4203 C CD1 . PHE C 1 118 ? 3.902   -6.357  53.048 1.00 21.97 ? 118 PHE C CD1 1 
ATOM   4204 C CD2 . PHE C 1 118 ? 1.916   -6.433  51.715 1.00 21.50 ? 118 PHE C CD2 1 
ATOM   4205 C CE1 . PHE C 1 118 ? 4.483   -7.353  52.264 1.00 17.38 ? 118 PHE C CE1 1 
ATOM   4206 C CE2 . PHE C 1 118 ? 2.483   -7.424  50.923 1.00 20.51 ? 118 PHE C CE2 1 
ATOM   4207 C CZ  . PHE C 1 118 ? 3.773   -7.888  51.201 1.00 23.07 ? 118 PHE C CZ  1 
ATOM   4208 N N   . PRO C 1 119 ? 1.453   -3.643  56.829 1.00 22.21 ? 119 PRO C N   1 
ATOM   4209 C CA  . PRO C 1 119 ? 0.942   -2.480  57.555 1.00 20.81 ? 119 PRO C CA  1 
ATOM   4210 C C   . PRO C 1 119 ? 1.355   -1.244  56.813 1.00 22.91 ? 119 PRO C C   1 
ATOM   4211 O O   . PRO C 1 119 ? 2.310   -1.320  56.059 1.00 23.52 ? 119 PRO C O   1 
ATOM   4212 C CB  . PRO C 1 119 ? 1.701   -2.534  58.891 1.00 21.70 ? 119 PRO C CB  1 
ATOM   4213 C CG  . PRO C 1 119 ? 2.338   -3.893  58.942 1.00 28.11 ? 119 PRO C CG  1 
ATOM   4214 C CD  . PRO C 1 119 ? 2.586   -4.271  57.523 1.00 26.09 ? 119 PRO C CD  1 
ATOM   4215 N N   . PRO C 1 120 ? 0.660   -0.120  57.027 1.00 25.74 ? 120 PRO C N   1 
ATOM   4216 C CA  . PRO C 1 120 ? 1.083   1.156   56.443 1.00 22.53 ? 120 PRO C CA  1 
ATOM   4217 C C   . PRO C 1 120 ? 2.481   1.508   56.923 1.00 20.91 ? 120 PRO C C   1 
ATOM   4218 O O   . PRO C 1 120 ? 2.859   1.113   58.015 1.00 23.37 ? 120 PRO C O   1 
ATOM   4219 C CB  . PRO C 1 120 ? 0.088   2.152   57.023 1.00 16.50 ? 120 PRO C CB  1 
ATOM   4220 C CG  . PRO C 1 120 ? -0.407  1.506   58.251 1.00 20.74 ? 120 PRO C CG  1 
ATOM   4221 C CD  . PRO C 1 120 ? -0.453  0.048   57.970 1.00 20.10 ? 120 PRO C CD  1 
ATOM   4222 N N   . SER C 1 121 ? 3.236   2.230   56.105 1.00 22.90 ? 121 SER C N   1 
ATOM   4223 C CA  . SER C 1 121 ? 4.582   2.633   56.471 1.00 26.67 ? 121 SER C CA  1 
ATOM   4224 C C   . SER C 1 121 ? 4.456   3.864   57.335 1.00 25.20 ? 121 SER C C   1 
ATOM   4225 O O   . SER C 1 121 ? 3.436   4.552   57.286 1.00 26.66 ? 121 SER C O   1 
ATOM   4226 C CB  . SER C 1 121 ? 5.394   2.972   55.220 1.00 21.13 ? 121 SER C CB  1 
ATOM   4227 O OG  . SER C 1 121 ? 4.921   4.174   54.634 1.00 18.60 ? 121 SER C OG  1 
ATOM   4228 N N   . ASP C 1 122 ? 5.487   4.134   58.127 1.00 26.01 ? 122 ASP C N   1 
ATOM   4229 C CA  . ASP C 1 122 ? 5.527   5.343   58.936 1.00 25.60 ? 122 ASP C CA  1 
ATOM   4230 C C   . ASP C 1 122 ? 5.634   6.571   58.049 1.00 26.13 ? 122 ASP C C   1 
ATOM   4231 O O   . ASP C 1 122 ? 5.129   7.638   58.398 1.00 28.99 ? 122 ASP C O   1 
ATOM   4232 C CB  . ASP C 1 122 ? 6.709   5.303   59.907 1.00 33.69 ? 122 ASP C CB  1 
ATOM   4233 C CG  . ASP C 1 122 ? 6.489   4.337   61.048 1.00 37.50 ? 122 ASP C CG  1 
ATOM   4234 O OD1 . ASP C 1 122 ? 5.342   3.871   61.226 1.00 47.56 ? 122 ASP C OD1 1 
ATOM   4235 O OD2 . ASP C 1 122 ? 7.458   4.052   61.778 1.00 42.73 ? 122 ASP C OD2 1 
ATOM   4236 N N   . GLU C 1 123 ? 6.294   6.420   56.901 1.00 26.29 ? 123 GLU C N   1 
ATOM   4237 C CA  A GLU C 1 123 ? 6.455   7.532   55.963 0.53 28.86 ? 123 GLU C CA  1 
ATOM   4238 C CA  B GLU C 1 123 ? 6.458   7.522   55.960 0.47 28.68 ? 123 GLU C CA  1 
ATOM   4239 C C   . GLU C 1 123 ? 5.107   7.994   55.410 1.00 27.40 ? 123 GLU C C   1 
ATOM   4240 O O   . GLU C 1 123 ? 4.873   9.197   55.239 1.00 23.79 ? 123 GLU C O   1 
ATOM   4241 C CB  A GLU C 1 123 ? 7.402   7.159   54.817 0.53 28.43 ? 123 GLU C CB  1 
ATOM   4242 C CB  B GLU C 1 123 ? 7.386   7.115   54.814 0.47 28.37 ? 123 GLU C CB  1 
ATOM   4243 C CG  A GLU C 1 123 ? 7.779   8.334   53.911 0.53 27.94 ? 123 GLU C CG  1 
ATOM   4244 C CG  B GLU C 1 123 ? 8.813   6.776   55.246 0.47 36.83 ? 123 GLU C CG  1 
ATOM   4245 C CD  A GLU C 1 123 ? 8.841   7.979   52.871 0.53 34.79 ? 123 GLU C CD  1 
ATOM   4246 C CD  B GLU C 1 123 ? 9.012   5.299   55.558 0.47 34.79 ? 123 GLU C CD  1 
ATOM   4247 O OE1 A GLU C 1 123 ? 8.667   6.974   52.144 0.53 29.53 ? 123 GLU C OE1 1 
ATOM   4248 O OE1 B GLU C 1 123 ? 8.526   4.829   56.613 0.47 32.64 ? 123 GLU C OE1 1 
ATOM   4249 O OE2 A GLU C 1 123 ? 9.853   8.708   52.782 0.53 28.67 ? 123 GLU C OE2 1 
ATOM   4250 O OE2 B GLU C 1 123 ? 9.665   4.611   54.744 0.47 27.91 ? 123 GLU C OE2 1 
ATOM   4251 N N   . GLN C 1 124 ? 4.214   7.045   55.140 1.00 19.59 ? 124 GLN C N   1 
ATOM   4252 C CA  . GLN C 1 124 ? 2.905   7.402   54.619 1.00 19.73 ? 124 GLN C CA  1 
ATOM   4253 C C   . GLN C 1 124 ? 2.060   8.085   55.686 1.00 22.24 ? 124 GLN C C   1 
ATOM   4254 O O   . GLN C 1 124 ? 1.347   9.043   55.392 1.00 21.66 ? 124 GLN C O   1 
ATOM   4255 C CB  . GLN C 1 124 ? 2.166   6.179   54.061 1.00 20.99 ? 124 GLN C CB  1 
ATOM   4256 C CG  . GLN C 1 124 ? 0.896   6.561   53.313 1.00 19.04 ? 124 GLN C CG  1 
ATOM   4257 C CD  . GLN C 1 124 ? -0.022  5.396   53.024 1.00 18.55 ? 124 GLN C CD  1 
ATOM   4258 O OE1 . GLN C 1 124 ? 0.224   4.268   53.443 1.00 21.01 ? 124 GLN C OE1 1 
ATOM   4259 N NE2 . GLN C 1 124 ? -1.099  5.671   52.307 1.00 23.19 ? 124 GLN C NE2 1 
ATOM   4260 N N   . LEU C 1 125 ? 2.146   7.592   56.922 1.00 21.43 ? 125 LEU C N   1 
ATOM   4261 C CA  . LEU C 1 125 ? 1.329   8.115   58.014 1.00 24.58 ? 125 LEU C CA  1 
ATOM   4262 C C   . LEU C 1 125 ? 1.456   9.635   58.201 1.00 30.10 ? 125 LEU C C   1 
ATOM   4263 O O   . LEU C 1 125 ? 0.483   10.298  58.575 1.00 32.19 ? 125 LEU C O   1 
ATOM   4264 C CB  . LEU C 1 125 ? 1.589   7.362   59.324 1.00 17.52 ? 125 LEU C CB  1 
ATOM   4265 C CG  . LEU C 1 125 ? 1.137   5.902   59.375 1.00 24.07 ? 125 LEU C CG  1 
ATOM   4266 C CD1 . LEU C 1 125 ? 1.492   5.269   60.714 1.00 14.47 ? 125 LEU C CD1 1 
ATOM   4267 C CD2 . LEU C 1 125 ? -0.359  5.755   59.088 1.00 18.02 ? 125 LEU C CD2 1 
ATOM   4268 N N   . LYS C 1 126 ? 2.633   10.187  57.906 1.00 33.31 ? 126 LYS C N   1 
ATOM   4269 C CA  . LYS C 1 126 ? 2.842   11.635  57.975 1.00 29.21 ? 126 LYS C CA  1 
ATOM   4270 C C   . LYS C 1 126 ? 1.911   12.380  57.020 1.00 28.62 ? 126 LYS C C   1 
ATOM   4271 O O   . LYS C 1 126 ? 1.688   13.581  57.169 1.00 36.33 ? 126 LYS C O   1 
ATOM   4272 C CB  . LYS C 1 126 ? 4.298   12.004  57.650 1.00 30.72 ? 126 LYS C CB  1 
ATOM   4273 C CG  . LYS C 1 126 ? 5.363   11.264  58.449 1.00 34.67 ? 126 LYS C CG  1 
ATOM   4274 C CD  . LYS C 1 126 ? 6.748   11.494  57.847 1.00 47.78 ? 126 LYS C CD  1 
ATOM   4275 C CE  . LYS C 1 126 ? 7.789   10.544  58.452 1.00 59.69 ? 126 LYS C CE  1 
ATOM   4276 N NZ  . LYS C 1 126 ? 9.114   10.614  57.758 1.00 59.46 ? 126 LYS C NZ  1 
ATOM   4277 N N   . SER C 1 127 ? 1.373   11.684  56.029 1.00 23.89 ? 127 SER C N   1 
ATOM   4278 C CA  . SER C 1 127 ? 0.508   12.364  55.076 1.00 33.38 ? 127 SER C CA  1 
ATOM   4279 C C   . SER C 1 127 ? -0.957  12.377  55.534 1.00 28.95 ? 127 SER C C   1 
ATOM   4280 O O   . SER C 1 127 ? -1.797  13.031  54.928 1.00 40.51 ? 127 SER C O   1 
ATOM   4281 C CB  . SER C 1 127 ? 0.673   11.793  53.654 1.00 27.43 ? 127 SER C CB  1 
ATOM   4282 O OG  . SER C 1 127 ? -0.019  10.568  53.467 1.00 30.53 ? 127 SER C OG  1 
ATOM   4283 N N   . GLY C 1 128 ? -1.257  11.667  56.615 1.00 24.24 ? 128 GLY C N   1 
ATOM   4284 C CA  . GLY C 1 128 ? -2.608  11.647  57.142 1.00 24.73 ? 128 GLY C CA  1 
ATOM   4285 C C   . GLY C 1 128 ? -3.472  10.530  56.580 1.00 28.55 ? 128 GLY C C   1 
ATOM   4286 O O   . GLY C 1 128 ? -4.672  10.483  56.840 1.00 24.92 ? 128 GLY C O   1 
ATOM   4287 N N   . THR C 1 129 ? -2.861  9.634   55.808 1.00 27.45 ? 129 THR C N   1 
ATOM   4288 C CA  . THR C 1 129 ? -3.554  8.485   55.239 1.00 22.61 ? 129 THR C CA  1 
ATOM   4289 C C   . THR C 1 129 ? -2.787  7.206   55.552 1.00 23.63 ? 129 THR C C   1 
ATOM   4290 O O   . THR C 1 129 ? -1.559  7.203   55.545 1.00 29.59 ? 129 THR C O   1 
ATOM   4291 C CB  . THR C 1 129 ? -3.733  8.639   53.694 1.00 27.79 ? 129 THR C CB  1 
ATOM   4292 O OG1 . THR C 1 129 ? -4.836  9.510   53.410 1.00 28.68 ? 129 THR C OG1 1 
ATOM   4293 C CG2 . THR C 1 129 ? -4.024  7.304   53.029 1.00 31.77 ? 129 THR C CG2 1 
ATOM   4294 N N   . ALA C 1 130 ? -3.503  6.126   55.837 1.00 16.64 ? 130 ALA C N   1 
ATOM   4295 C CA  . ALA C 1 130 ? -2.874  4.828   56.014 1.00 16.72 ? 130 ALA C CA  1 
ATOM   4296 C C   . ALA C 1 130 ? -3.405  3.856   54.985 1.00 20.95 ? 130 ALA C C   1 
ATOM   4297 O O   . ALA C 1 130 ? -4.606  3.607   54.943 1.00 20.54 ? 130 ALA C O   1 
ATOM   4298 C CB  . ALA C 1 130 ? -3.138  4.291   57.408 1.00 14.50 ? 130 ALA C CB  1 
ATOM   4299 N N   . SER C 1 131 ? -2.519  3.302   54.156 1.00 25.53 ? 131 SER C N   1 
ATOM   4300 C CA  . SER C 1 131 ? -2.904  2.220   53.249 1.00 14.77 ? 131 SER C CA  1 
ATOM   4301 C C   . SER C 1 131 ? -2.521  0.894   53.887 1.00 17.65 ? 131 SER C C   1 
ATOM   4302 O O   . SER C 1 131 ? -1.395  0.728   54.347 1.00 22.83 ? 131 SER C O   1 
ATOM   4303 C CB  . SER C 1 131 ? -2.223  2.365   51.884 1.00 14.05 ? 131 SER C CB  1 
ATOM   4304 O OG  . SER C 1 131 ? -2.539  3.593   51.241 1.00 10.50 ? 131 SER C OG  1 
ATOM   4305 N N   . VAL C 1 132 ? -3.459  -0.042  53.946 1.00 15.23 ? 132 VAL C N   1 
ATOM   4306 C CA  . VAL C 1 132 ? -3.146  -1.373  54.439 1.00 14.19 ? 132 VAL C CA  1 
ATOM   4307 C C   . VAL C 1 132 ? -3.383  -2.365  53.309 1.00 19.88 ? 132 VAL C C   1 
ATOM   4308 O O   . VAL C 1 132 ? -4.462  -2.380  52.713 1.00 19.31 ? 132 VAL C O   1 
ATOM   4309 C CB  . VAL C 1 132 ? -4.021  -1.759  55.640 1.00 18.05 ? 132 VAL C CB  1 
ATOM   4310 C CG1 . VAL C 1 132 ? -3.552  -3.095  56.234 1.00 16.92 ? 132 VAL C CG1 1 
ATOM   4311 C CG2 . VAL C 1 132 ? -4.008  -0.651  56.687 1.00 15.87 ? 132 VAL C CG2 1 
ATOM   4312 N N   . VAL C 1 133 ? -2.377  -3.186  53.012 1.00 18.36 ? 133 VAL C N   1 
ATOM   4313 C CA  . VAL C 1 133 ? -2.388  -3.978  51.795 1.00 15.67 ? 133 VAL C CA  1 
ATOM   4314 C C   . VAL C 1 133 ? -2.354  -5.475  52.051 1.00 18.54 ? 133 VAL C C   1 
ATOM   4315 O O   . VAL C 1 133 ? -1.588  -5.960  52.885 1.00 23.43 ? 133 VAL C O   1 
ATOM   4316 C CB  . VAL C 1 133 ? -1.218  -3.579  50.841 1.00 17.06 ? 133 VAL C CB  1 
ATOM   4317 C CG1 . VAL C 1 133 ? -1.143  -4.507  49.619 1.00 7.65  ? 133 VAL C CG1 1 
ATOM   4318 C CG2 . VAL C 1 133 ? -1.379  -2.151  50.398 1.00 16.26 ? 133 VAL C CG2 1 
ATOM   4319 N N   . CYS C 1 134 ? -3.185  -6.196  51.301 1.00 20.30 ? 134 CYS C N   1 
ATOM   4320 C CA  . CYS C 1 134 ? -3.281  -7.649  51.378 1.00 25.04 ? 134 CYS C CA  1 
ATOM   4321 C C   . CYS C 1 134 ? -2.925  -8.228  50.023 1.00 20.20 ? 134 CYS C C   1 
ATOM   4322 O O   . CYS C 1 134 ? -3.506  -7.842  49.017 1.00 20.24 ? 134 CYS C O   1 
ATOM   4323 C CB  . CYS C 1 134 ? -4.712  -8.051  51.743 1.00 23.41 ? 134 CYS C CB  1 
ATOM   4324 S SG  . CYS C 1 134 ? -4.961  -9.752  52.279 1.00 28.26 ? 134 CYS C SG  1 
ATOM   4325 N N   . LEU C 1 135 ? -1.965  -9.147  50.003 1.00 19.47 ? 135 LEU C N   1 
ATOM   4326 C CA  . LEU C 1 135 ? -1.541  -9.799  48.775 1.00 15.51 ? 135 LEU C CA  1 
ATOM   4327 C C   . LEU C 1 135 ? -2.066  -11.226 48.740 1.00 13.79 ? 135 LEU C C   1 
ATOM   4328 O O   . LEU C 1 135 ? -1.938  -11.967 49.708 1.00 20.16 ? 135 LEU C O   1 
ATOM   4329 C CB  . LEU C 1 135 ? -0.010  -9.815  48.682 1.00 11.87 ? 135 LEU C CB  1 
ATOM   4330 C CG  . LEU C 1 135 ? 0.640   -10.587 47.520 1.00 17.60 ? 135 LEU C CG  1 
ATOM   4331 C CD1 . LEU C 1 135 ? 0.186   -10.038 46.157 1.00 15.84 ? 135 LEU C CD1 1 
ATOM   4332 C CD2 . LEU C 1 135 ? 2.170   -10.574 47.618 1.00 12.62 ? 135 LEU C CD2 1 
ATOM   4333 N N   . LEU C 1 136 ? -2.665  -11.612 47.626 1.00 15.73 ? 136 LEU C N   1 
ATOM   4334 C CA  . LEU C 1 136 ? -2.982  -13.013 47.388 1.00 15.49 ? 136 LEU C CA  1 
ATOM   4335 C C   . LEU C 1 136 ? -2.132  -13.451 46.224 1.00 17.19 ? 136 LEU C C   1 
ATOM   4336 O O   . LEU C 1 136 ? -2.312  -12.967 45.108 1.00 17.05 ? 136 LEU C O   1 
ATOM   4337 C CB  . LEU C 1 136 ? -4.452  -13.194 47.039 1.00 16.20 ? 136 LEU C CB  1 
ATOM   4338 C CG  . LEU C 1 136 ? -5.498  -13.162 48.149 1.00 14.67 ? 136 LEU C CG  1 
ATOM   4339 C CD1 . LEU C 1 136 ? -5.487  -11.876 48.973 1.00 12.48 ? 136 LEU C CD1 1 
ATOM   4340 C CD2 . LEU C 1 136 ? -6.842  -13.355 47.492 1.00 19.33 ? 136 LEU C CD2 1 
ATOM   4341 N N   . ASN C 1 137 ? -1.197  -14.359 46.471 1.00 19.53 ? 137 ASN C N   1 
ATOM   4342 C CA  . ASN C 1 137 ? -0.237  -14.710 45.431 1.00 16.99 ? 137 ASN C CA  1 
ATOM   4343 C C   . ASN C 1 137 ? -0.521  -16.027 44.708 1.00 22.26 ? 137 ASN C C   1 
ATOM   4344 O O   . ASN C 1 137 ? -0.840  -17.040 45.335 1.00 21.66 ? 137 ASN C O   1 
ATOM   4345 C CB  . ASN C 1 137 ? 1.180   -14.727 45.988 1.00 19.08 ? 137 ASN C CB  1 
ATOM   4346 C CG  . ASN C 1 137 ? 2.192   -14.168 45.008 1.00 28.92 ? 137 ASN C CG  1 
ATOM   4347 O OD1 . ASN C 1 137 ? 1.870   -13.294 44.198 1.00 22.82 ? 137 ASN C OD1 1 
ATOM   4348 N ND2 . ASN C 1 137 ? 3.425   -14.666 45.079 1.00 22.35 ? 137 ASN C ND2 1 
ATOM   4349 N N   . ASN C 1 138 ? -0.420  -15.972 43.378 1.00 19.48 ? 138 ASN C N   1 
ATOM   4350 C CA  . ASN C 1 138 ? -0.329  -17.148 42.511 1.00 20.12 ? 138 ASN C CA  1 
ATOM   4351 C C   . ASN C 1 138 ? -1.416  -18.191 42.686 1.00 18.36 ? 138 ASN C C   1 
ATOM   4352 O O   . ASN C 1 138 ? -1.132  -19.308 43.098 1.00 21.28 ? 138 ASN C O   1 
ATOM   4353 C CB  . ASN C 1 138 ? 1.053   -17.813 42.655 1.00 20.62 ? 138 ASN C CB  1 
ATOM   4354 C CG  . ASN C 1 138 ? 2.190   -16.871 42.297 1.00 23.27 ? 138 ASN C CG  1 
ATOM   4355 O OD1 . ASN C 1 138 ? 1.979   -15.848 41.656 1.00 22.62 ? 138 ASN C OD1 1 
ATOM   4356 N ND2 . ASN C 1 138 ? 3.397   -17.211 42.715 1.00 27.87 ? 138 ASN C ND2 1 
ATOM   4357 N N   . PHE C 1 139 ? -2.649  -17.845 42.342 1.00 16.63 ? 139 PHE C N   1 
ATOM   4358 C CA  . PHE C 1 139 ? -3.776  -18.731 42.619 1.00 19.52 ? 139 PHE C CA  1 
ATOM   4359 C C   . PHE C 1 139 ? -4.620  -18.989 41.380 1.00 20.57 ? 139 PHE C C   1 
ATOM   4360 O O   . PHE C 1 139 ? -4.493  -18.294 40.372 1.00 20.19 ? 139 PHE C O   1 
ATOM   4361 C CB  . PHE C 1 139 ? -4.642  -18.169 43.761 1.00 20.04 ? 139 PHE C CB  1 
ATOM   4362 C CG  . PHE C 1 139 ? -5.174  -16.793 43.501 1.00 20.25 ? 139 PHE C CG  1 
ATOM   4363 C CD1 . PHE C 1 139 ? -4.512  -15.678 43.985 1.00 20.03 ? 139 PHE C CD1 1 
ATOM   4364 C CD2 . PHE C 1 139 ? -6.332  -16.611 42.764 1.00 20.95 ? 139 PHE C CD2 1 
ATOM   4365 C CE1 . PHE C 1 139 ? -5.001  -14.404 43.744 1.00 18.63 ? 139 PHE C CE1 1 
ATOM   4366 C CE2 . PHE C 1 139 ? -6.816  -15.349 42.514 1.00 17.72 ? 139 PHE C CE2 1 
ATOM   4367 C CZ  . PHE C 1 139 ? -6.150  -14.244 43.008 1.00 19.68 ? 139 PHE C CZ  1 
ATOM   4368 N N   . TYR C 1 140 ? -5.478  -19.998 41.460 1.00 19.12 ? 140 TYR C N   1 
ATOM   4369 C CA  . TYR C 1 140 ? -6.374  -20.324 40.357 1.00 19.47 ? 140 TYR C CA  1 
ATOM   4370 C C   . TYR C 1 140 ? -7.570  -21.095 40.903 1.00 23.97 ? 140 TYR C C   1 
ATOM   4371 O O   . TYR C 1 140 ? -7.392  -22.044 41.674 1.00 21.92 ? 140 TYR C O   1 
ATOM   4372 C CB  . TYR C 1 140 ? -5.656  -21.140 39.275 1.00 15.71 ? 140 TYR C CB  1 
ATOM   4373 C CG  . TYR C 1 140 ? -6.508  -21.308 38.045 1.00 20.33 ? 140 TYR C CG  1 
ATOM   4374 C CD1 . TYR C 1 140 ? -6.388  -20.439 36.968 1.00 19.67 ? 140 TYR C CD1 1 
ATOM   4375 C CD2 . TYR C 1 140 ? -7.479  -22.299 37.981 1.00 18.77 ? 140 TYR C CD2 1 
ATOM   4376 C CE1 . TYR C 1 140 ? -7.191  -20.572 35.855 1.00 17.71 ? 140 TYR C CE1 1 
ATOM   4377 C CE2 . TYR C 1 140 ? -8.299  -22.429 36.887 1.00 15.97 ? 140 TYR C CE2 1 
ATOM   4378 C CZ  . TYR C 1 140 ? -8.148  -21.576 35.821 1.00 18.34 ? 140 TYR C CZ  1 
ATOM   4379 O OH  . TYR C 1 140 ? -8.964  -21.730 34.721 1.00 20.20 ? 140 TYR C OH  1 
ATOM   4380 N N   . PRO C 1 141 ? -8.788  -20.712 40.489 1.00 17.06 ? 141 PRO C N   1 
ATOM   4381 C CA  . PRO C 1 141 ? -9.114  -19.697 39.480 1.00 20.47 ? 141 PRO C CA  1 
ATOM   4382 C C   . PRO C 1 141 ? -9.142  -18.257 40.005 1.00 24.39 ? 141 PRO C C   1 
ATOM   4383 O O   . PRO C 1 141 ? -8.932  -17.999 41.197 1.00 21.71 ? 141 PRO C O   1 
ATOM   4384 C CB  . PRO C 1 141 ? -10.526 -20.088 39.065 1.00 22.13 ? 141 PRO C CB  1 
ATOM   4385 C CG  . PRO C 1 141 ? -11.130 -20.568 40.341 1.00 20.08 ? 141 PRO C CG  1 
ATOM   4386 C CD  . PRO C 1 141 ? -10.004 -21.323 41.049 1.00 19.16 ? 141 PRO C CD  1 
ATOM   4387 N N   . ARG C 1 142 ? -9.435  -17.341 39.087 1.00 19.93 ? 142 ARG C N   1 
ATOM   4388 C CA  . ARG C 1 142 ? -9.375  -15.904 39.315 1.00 25.69 ? 142 ARG C CA  1 
ATOM   4389 C C   . ARG C 1 142 ? -10.211 -15.421 40.507 1.00 28.06 ? 142 ARG C C   1 
ATOM   4390 O O   . ARG C 1 142 ? -9.768  -14.559 41.264 1.00 25.20 ? 142 ARG C O   1 
ATOM   4391 C CB  . ARG C 1 142 ? -9.837  -15.193 38.046 1.00 23.13 ? 142 ARG C CB  1 
ATOM   4392 C CG  . ARG C 1 142 ? -9.444  -13.737 37.917 1.00 33.41 ? 142 ARG C CG  1 
ATOM   4393 C CD  . ARG C 1 142 ? -10.007 -13.179 36.603 1.00 33.40 ? 142 ARG C CD  1 
ATOM   4394 N NE  . ARG C 1 142 ? -9.530  -11.833 36.300 1.00 33.56 ? 142 ARG C NE  1 
ATOM   4395 C CZ  . ARG C 1 142 ? -9.942  -10.733 36.925 1.00 57.36 ? 142 ARG C CZ  1 
ATOM   4396 N NH1 . ARG C 1 142 ? -10.835 -10.814 37.905 1.00 54.02 ? 142 ARG C NH1 1 
ATOM   4397 N NH2 . ARG C 1 142 ? -9.454  -9.548  36.577 1.00 53.39 ? 142 ARG C NH2 1 
ATOM   4398 N N   . GLU C 1 143 ? -11.407 -15.980 40.671 1.00 23.72 ? 143 GLU C N   1 
ATOM   4399 C CA  A GLU C 1 143 ? -12.340 -15.528 41.697 0.52 26.73 ? 143 GLU C CA  1 
ATOM   4400 C CA  B GLU C 1 143 ? -12.328 -15.508 41.702 0.48 26.53 ? 143 GLU C CA  1 
ATOM   4401 C C   . GLU C 1 143 ? -11.822 -15.756 43.116 1.00 23.46 ? 143 GLU C C   1 
ATOM   4402 O O   . GLU C 1 143 ? -11.448 -16.869 43.472 1.00 30.50 ? 143 GLU C O   1 
ATOM   4403 C CB  A GLU C 1 143 ? -13.701 -16.206 41.516 0.52 26.67 ? 143 GLU C CB  1 
ATOM   4404 C CB  B GLU C 1 143 ? -13.711 -16.136 41.537 0.48 26.67 ? 143 GLU C CB  1 
ATOM   4405 C CG  A GLU C 1 143 ? -14.445 -15.799 40.240 0.52 32.68 ? 143 GLU C CG  1 
ATOM   4406 C CG  B GLU C 1 143 ? -14.729 -15.673 42.584 0.48 30.93 ? 143 GLU C CG  1 
ATOM   4407 C CD  A GLU C 1 143 ? -13.877 -16.437 38.977 0.52 31.54 ? 143 GLU C CD  1 
ATOM   4408 C CD  B GLU C 1 143 ? -14.984 -14.170 42.533 0.48 35.66 ? 143 GLU C CD  1 
ATOM   4409 O OE1 A GLU C 1 143 ? -13.173 -17.464 39.083 0.52 24.19 ? 143 GLU C OE1 1 
ATOM   4410 O OE1 B GLU C 1 143 ? -15.378 -13.671 41.456 0.48 36.53 ? 143 GLU C OE1 1 
ATOM   4411 O OE2 A GLU C 1 143 ? -14.138 -15.907 37.876 0.52 23.99 ? 143 GLU C OE2 1 
ATOM   4412 O OE2 B GLU C 1 143 ? -14.781 -13.488 43.563 0.48 28.23 ? 143 GLU C OE2 1 
ATOM   4413 N N   . ALA C 1 144 ? -11.818 -14.697 43.916 1.00 22.66 ? 144 ALA C N   1 
ATOM   4414 C CA  . ALA C 1 144 ? -11.371 -14.763 45.301 1.00 25.10 ? 144 ALA C CA  1 
ATOM   4415 C C   . ALA C 1 144 ? -12.029 -13.635 46.082 1.00 25.91 ? 144 ALA C C   1 
ATOM   4416 O O   . ALA C 1 144 ? -12.330 -12.583 45.518 1.00 34.14 ? 144 ALA C O   1 
ATOM   4417 C CB  . ALA C 1 144 ? -9.860  -14.640 45.373 1.00 22.17 ? 144 ALA C CB  1 
ATOM   4418 N N   . LYS C 1 145 ? -12.264 -13.848 47.372 1.00 21.79 ? 145 LYS C N   1 
ATOM   4419 C CA  . LYS C 1 145 ? -12.836 -12.796 48.193 1.00 18.80 ? 145 LYS C CA  1 
ATOM   4420 C C   . LYS C 1 145 ? -11.905 -12.409 49.338 1.00 22.43 ? 145 LYS C C   1 
ATOM   4421 O O   . LYS C 1 145 ? -11.464 -13.252 50.116 1.00 23.64 ? 145 LYS C O   1 
ATOM   4422 C CB  . LYS C 1 145 ? -14.202 -13.212 48.719 1.00 20.67 ? 145 LYS C CB  1 
ATOM   4423 C CG  . LYS C 1 145 ? -15.037 -12.073 49.252 1.00 21.52 ? 145 LYS C CG  1 
ATOM   4424 C CD  . LYS C 1 145 ? -16.493 -12.501 49.455 1.00 26.19 ? 145 LYS C CD  1 
ATOM   4425 C CE  . LYS C 1 145 ? -17.229 -11.558 50.379 1.00 28.63 ? 145 LYS C CE  1 
ATOM   4426 N NZ  . LYS C 1 145 ? -18.695 -11.697 50.241 1.00 28.33 ? 145 LYS C NZ  1 
ATOM   4427 N N   . VAL C 1 146 ? -11.598 -11.121 49.414 1.00 25.10 ? 146 VAL C N   1 
ATOM   4428 C CA  . VAL C 1 146 ? -10.879 -10.547 50.534 1.00 17.27 ? 146 VAL C CA  1 
ATOM   4429 C C   . VAL C 1 146 ? -11.838 -9.722  51.376 1.00 18.92 ? 146 VAL C C   1 
ATOM   4430 O O   . VAL C 1 146 ? -12.496 -8.819  50.862 1.00 17.80 ? 146 VAL C O   1 
ATOM   4431 C CB  . VAL C 1 146 ? -9.790  -9.590  50.045 1.00 15.13 ? 146 VAL C CB  1 
ATOM   4432 C CG1 . VAL C 1 146 ? -9.115  -8.894  51.235 1.00 17.56 ? 146 VAL C CG1 1 
ATOM   4433 C CG2 . VAL C 1 146 ? -8.782  -10.338 49.200 1.00 19.32 ? 146 VAL C CG2 1 
ATOM   4434 N N   . GLN C 1 147 ? -11.916 -10.028 52.667 1.00 18.31 ? 147 GLN C N   1 
ATOM   4435 C CA  . GLN C 1 147 ? -12.634 -9.172  53.608 1.00 26.21 ? 147 GLN C CA  1 
ATOM   4436 C C   . GLN C 1 147 ? -11.674 -8.556  54.617 1.00 21.55 ? 147 GLN C C   1 
ATOM   4437 O O   . GLN C 1 147 ? -10.778 -9.232  55.115 1.00 23.53 ? 147 GLN C O   1 
ATOM   4438 C CB  . GLN C 1 147 ? -13.745 -9.951  54.328 1.00 19.89 ? 147 GLN C CB  1 
ATOM   4439 C CG  . GLN C 1 147 ? -14.832 -10.477 53.388 1.00 27.36 ? 147 GLN C CG  1 
ATOM   4440 C CD  . GLN C 1 147 ? -15.912 -11.266 54.104 1.00 31.88 ? 147 GLN C CD  1 
ATOM   4441 O OE1 . GLN C 1 147 ? -15.626 -12.164 54.902 1.00 32.60 ? 147 GLN C OE1 1 
ATOM   4442 N NE2 . GLN C 1 147 ? -17.167 -10.930 53.824 1.00 32.44 ? 147 GLN C NE2 1 
ATOM   4443 N N   . TRP C 1 148 ? -11.855 -7.269  54.897 1.00 22.38 ? 148 TRP C N   1 
ATOM   4444 C CA  . TRP C 1 148 ? -11.049 -6.566  55.898 1.00 21.33 ? 148 TRP C CA  1 
ATOM   4445 C C   . TRP C 1 148 ? -11.805 -6.413  57.210 1.00 17.49 ? 148 TRP C C   1 
ATOM   4446 O O   . TRP C 1 148 ? -12.898 -5.856  57.252 1.00 18.12 ? 148 TRP C O   1 
ATOM   4447 C CB  . TRP C 1 148 ? -10.638 -5.168  55.412 1.00 14.26 ? 148 TRP C CB  1 
ATOM   4448 C CG  . TRP C 1 148 ? -9.620  -5.164  54.317 1.00 22.55 ? 148 TRP C CG  1 
ATOM   4449 C CD1 . TRP C 1 148 ? -9.862  -5.100  52.975 1.00 22.51 ? 148 TRP C CD1 1 
ATOM   4450 C CD2 . TRP C 1 148 ? -8.197  -5.214  54.463 1.00 17.55 ? 148 TRP C CD2 1 
ATOM   4451 N NE1 . TRP C 1 148 ? -8.683  -5.111  52.280 1.00 22.32 ? 148 TRP C NE1 1 
ATOM   4452 C CE2 . TRP C 1 148 ? -7.643  -5.182  53.171 1.00 18.69 ? 148 TRP C CE2 1 
ATOM   4453 C CE3 . TRP C 1 148 ? -7.339  -5.292  55.558 1.00 15.23 ? 148 TRP C CE3 1 
ATOM   4454 C CZ2 . TRP C 1 148 ? -6.270  -5.232  52.942 1.00 17.10 ? 148 TRP C CZ2 1 
ATOM   4455 C CZ3 . TRP C 1 148 ? -5.987  -5.328  55.332 1.00 20.77 ? 148 TRP C CZ3 1 
ATOM   4456 C CH2 . TRP C 1 148 ? -5.461  -5.303  54.031 1.00 16.83 ? 148 TRP C CH2 1 
ATOM   4457 N N   . LYS C 1 149 ? -11.218 -6.908  58.286 1.00 21.89 ? 149 LYS C N   1 
ATOM   4458 C CA  . LYS C 1 149 ? -11.779 -6.665  59.604 1.00 25.83 ? 149 LYS C CA  1 
ATOM   4459 C C   . LYS C 1 149 ? -10.785 -5.856  60.421 1.00 22.47 ? 149 LYS C C   1 
ATOM   4460 O O   . LYS C 1 149 ? -9.620  -6.212  60.510 1.00 27.83 ? 149 LYS C O   1 
ATOM   4461 C CB  . LYS C 1 149 ? -12.151 -7.980  60.293 1.00 20.18 ? 149 LYS C CB  1 
ATOM   4462 C CG  . LYS C 1 149 ? -12.895 -8.935  59.376 1.00 21.67 ? 149 LYS C CG  1 
ATOM   4463 C CD  . LYS C 1 149 ? -13.799 -9.908  60.127 1.00 20.86 ? 149 LYS C CD  1 
ATOM   4464 C CE  . LYS C 1 149 ? -14.521 -10.818 59.133 1.00 33.02 ? 149 LYS C CE  1 
ATOM   4465 N NZ  . LYS C 1 149 ? -14.899 -12.147 59.705 1.00 37.20 ? 149 LYS C NZ  1 
ATOM   4466 N N   . VAL C 1 150 ? -11.249 -4.747  60.976 1.00 20.70 ? 150 VAL C N   1 
ATOM   4467 C CA  . VAL C 1 150 ? -10.449 -3.919  61.858 1.00 20.54 ? 150 VAL C CA  1 
ATOM   4468 C C   . VAL C 1 150 ? -11.058 -3.969  63.252 1.00 22.67 ? 150 VAL C C   1 
ATOM   4469 O O   . VAL C 1 150 ? -12.195 -3.524  63.443 1.00 23.74 ? 150 VAL C O   1 
ATOM   4470 C CB  . VAL C 1 150 ? -10.475 -2.468  61.389 1.00 18.75 ? 150 VAL C CB  1 
ATOM   4471 C CG1 . VAL C 1 150 ? -9.637  -1.612  62.318 1.00 15.71 ? 150 VAL C CG1 1 
ATOM   4472 C CG2 . VAL C 1 150 ? -9.999  -2.373  59.957 1.00 19.50 ? 150 VAL C CG2 1 
ATOM   4473 N N   . ASP C 1 151 ? -10.318 -4.512  64.218 1.00 28.45 ? 151 ASP C N   1 
ATOM   4474 C CA  . ASP C 1 151 ? -10.872 -4.782  65.558 1.00 25.85 ? 151 ASP C CA  1 
ATOM   4475 C C   . ASP C 1 151 ? -12.219 -5.502  65.440 1.00 26.07 ? 151 ASP C C   1 
ATOM   4476 O O   . ASP C 1 151 ? -13.174 -5.190  66.142 1.00 26.95 ? 151 ASP C O   1 
ATOM   4477 C CB  . ASP C 1 151 ? -11.005 -3.494  66.383 1.00 25.26 ? 151 ASP C CB  1 
ATOM   4478 C CG  . ASP C 1 151 ? -9.680  -3.026  66.968 1.00 22.15 ? 151 ASP C CG  1 
ATOM   4479 O OD1 . ASP C 1 151 ? -8.776  -3.863  67.137 1.00 28.30 ? 151 ASP C OD1 1 
ATOM   4480 O OD2 . ASP C 1 151 ? -9.546  -1.826  67.276 1.00 26.63 ? 151 ASP C OD2 1 
ATOM   4481 N N   . ASN C 1 152 ? -12.268 -6.438  64.498 1.00 25.76 ? 152 ASN C N   1 
ATOM   4482 C CA  . ASN C 1 152 ? -13.429 -7.278  64.211 1.00 25.76 ? 152 ASN C CA  1 
ATOM   4483 C C   . ASN C 1 152 ? -14.637 -6.637  63.536 1.00 27.96 ? 152 ASN C C   1 
ATOM   4484 O O   . ASN C 1 152 ? -15.665 -7.299  63.356 1.00 24.30 ? 152 ASN C O   1 
ATOM   4485 C CB  . ASN C 1 152 ? -13.854 -8.110  65.424 1.00 31.11 ? 152 ASN C CB  1 
ATOM   4486 C CG  . ASN C 1 152 ? -13.304 -9.518  65.363 1.00 48.64 ? 152 ASN C CG  1 
ATOM   4487 O OD1 . ASN C 1 152 ? -13.676 -10.308 64.483 1.00 47.97 ? 152 ASN C OD1 1 
ATOM   4488 N ND2 . ASN C 1 152 ? -12.396 -9.837  66.280 1.00 45.72 ? 152 ASN C ND2 1 
ATOM   4489 N N   . ALA C 1 153 ? -14.526 -5.370  63.150 1.00 19.39 ? 153 ALA C N   1 
ATOM   4490 C CA  . ALA C 1 153 ? -15.580 -4.780  62.346 1.00 19.90 ? 153 ALA C CA  1 
ATOM   4491 C C   . ALA C 1 153 ? -15.276 -5.043  60.870 1.00 22.58 ? 153 ALA C C   1 
ATOM   4492 O O   . ALA C 1 153 ? -14.178 -4.752  60.401 1.00 16.68 ? 153 ALA C O   1 
ATOM   4493 C CB  . ALA C 1 153 ? -15.712 -3.276  62.627 1.00 14.16 ? 153 ALA C CB  1 
ATOM   4494 N N   . LEU C 1 154 ? -16.236 -5.622  60.153 1.00 19.28 ? 154 LEU C N   1 
ATOM   4495 C CA  . LEU C 1 154 ? -16.115 -5.770  58.711 1.00 16.10 ? 154 LEU C CA  1 
ATOM   4496 C C   . LEU C 1 154 ? -16.034 -4.395  58.069 1.00 21.64 ? 154 LEU C C   1 
ATOM   4497 O O   . LEU C 1 154 ? -16.825 -3.506  58.389 1.00 26.42 ? 154 LEU C O   1 
ATOM   4498 C CB  . LEU C 1 154 ? -17.289 -6.558  58.130 1.00 18.07 ? 154 LEU C CB  1 
ATOM   4499 C CG  . LEU C 1 154 ? -17.331 -6.747  56.603 1.00 18.12 ? 154 LEU C CG  1 
ATOM   4500 C CD1 . LEU C 1 154 ? -16.152 -7.590  56.093 1.00 22.10 ? 154 LEU C CD1 1 
ATOM   4501 C CD2 . LEU C 1 154 ? -18.649 -7.366  56.140 1.00 15.35 ? 154 LEU C CD2 1 
ATOM   4502 N N   . GLN C 1 155 ? -15.064 -4.210  57.179 1.00 21.31 ? 155 GLN C N   1 
ATOM   4503 C CA  . GLN C 1 155 ? -14.955 -2.960  56.437 1.00 19.02 ? 155 GLN C CA  1 
ATOM   4504 C C   . GLN C 1 155 ? -15.730 -3.063  55.129 1.00 25.61 ? 155 GLN C C   1 
ATOM   4505 O O   . GLN C 1 155 ? -15.782 -4.121  54.487 1.00 22.88 ? 155 GLN C O   1 
ATOM   4506 C CB  . GLN C 1 155 ? -13.495 -2.625  56.157 1.00 18.42 ? 155 GLN C CB  1 
ATOM   4507 C CG  . GLN C 1 155 ? -12.635 -2.575  57.414 1.00 14.20 ? 155 GLN C CG  1 
ATOM   4508 C CD  . GLN C 1 155 ? -13.001 -1.424  58.323 1.00 15.45 ? 155 GLN C CD  1 
ATOM   4509 O OE1 . GLN C 1 155 ? -12.971 -0.265  57.921 1.00 16.09 ? 155 GLN C OE1 1 
ATOM   4510 N NE2 . GLN C 1 155 ? -13.337 -1.738  59.566 1.00 23.21 ? 155 GLN C NE2 1 
ATOM   4511 N N   . SER C 1 156 ? -16.358 -1.962  54.750 1.00 21.43 ? 156 SER C N   1 
ATOM   4512 C CA  . SER C 1 156 ? -17.064 -1.905  53.499 1.00 17.18 ? 156 SER C CA  1 
ATOM   4513 C C   . SER C 1 156 ? -16.916 -0.521  52.910 1.00 21.41 ? 156 SER C C   1 
ATOM   4514 O O   . SER C 1 156 ? -17.083 0.480   53.608 1.00 21.01 ? 156 SER C O   1 
ATOM   4515 C CB  . SER C 1 156 ? -18.534 -2.224  53.702 1.00 14.16 ? 156 SER C CB  1 
ATOM   4516 O OG  . SER C 1 156 ? -19.199 -2.325  52.443 1.00 16.09 ? 156 SER C OG  1 
ATOM   4517 N N   . GLY C 1 157 ? -16.582 -0.471  51.627 1.00 19.93 ? 157 GLY C N   1 
ATOM   4518 C CA  . GLY C 1 157 ? -16.539 0.783   50.907 1.00 18.06 ? 157 GLY C CA  1 
ATOM   4519 C C   . GLY C 1 157 ? -15.195 1.484   50.944 1.00 16.99 ? 157 GLY C C   1 
ATOM   4520 O O   . GLY C 1 157 ? -15.028 2.504   50.277 1.00 21.96 ? 157 GLY C O   1 
ATOM   4521 N N   . ASN C 1 158 ? -14.253 0.964   51.733 1.00 16.61 ? 158 ASN C N   1 
ATOM   4522 C CA  . ASN C 1 158 ? -12.920 1.554   51.824 1.00 17.60 ? 158 ASN C CA  1 
ATOM   4523 C C   . ASN C 1 158 ? -11.786 0.636   51.337 1.00 20.99 ? 158 ASN C C   1 
ATOM   4524 O O   . ASN C 1 158 ? -10.636 0.725   51.801 1.00 19.52 ? 158 ASN C O   1 
ATOM   4525 C CB  . ASN C 1 158 ? -12.642 2.088   53.224 1.00 12.14 ? 158 ASN C CB  1 
ATOM   4526 C CG  . ASN C 1 158 ? -12.822 1.040   54.304 1.00 20.43 ? 158 ASN C CG  1 
ATOM   4527 O OD1 . ASN C 1 158 ? -13.041 -0.138  54.019 1.00 21.53 ? 158 ASN C OD1 1 
ATOM   4528 N ND2 . ASN C 1 158 ? -12.722 1.467   55.567 1.00 16.84 ? 158 ASN C ND2 1 
ATOM   4529 N N   . SER C 1 159 ? -12.105 -0.235  50.391 1.00 13.47 ? 159 SER C N   1 
ATOM   4530 C CA  . SER C 1 159 ? -11.078 -1.062  49.789 1.00 21.47 ? 159 SER C CA  1 
ATOM   4531 C C   . SER C 1 159 ? -11.180 -1.151  48.254 1.00 18.39 ? 159 SER C C   1 
ATOM   4532 O O   . SER C 1 159 ? -12.271 -1.086  47.661 1.00 15.48 ? 159 SER C O   1 
ATOM   4533 C CB  . SER C 1 159 ? -11.064 -2.454  50.435 1.00 15.72 ? 159 SER C CB  1 
ATOM   4534 O OG  . SER C 1 159 ? -12.327 -3.074  50.303 1.00 22.87 ? 159 SER C OG  1 
ATOM   4535 N N   . GLN C 1 160 ? -10.021 -1.267  47.621 1.00 17.73 ? 160 GLN C N   1 
ATOM   4536 C CA  . GLN C 1 160 ? -9.944  -1.491  46.171 1.00 21.78 ? 160 GLN C CA  1 
ATOM   4537 C C   . GLN C 1 160 ? -9.070  -2.719  45.872 1.00 17.04 ? 160 GLN C C   1 
ATOM   4538 O O   . GLN C 1 160 ? -8.040  -2.927  46.501 1.00 20.48 ? 160 GLN C O   1 
ATOM   4539 C CB  . GLN C 1 160 ? -9.414  -0.245  45.444 1.00 16.91 ? 160 GLN C CB  1 
ATOM   4540 C CG  . GLN C 1 160 ? -10.346 0.956   45.494 1.00 17.01 ? 160 GLN C CG  1 
ATOM   4541 C CD  . GLN C 1 160 ? -9.975  2.063   44.489 1.00 32.47 ? 160 GLN C CD  1 
ATOM   4542 O OE1 . GLN C 1 160 ? -9.033  2.832   44.712 1.00 27.23 ? 160 GLN C OE1 1 
ATOM   4543 N NE2 . GLN C 1 160 ? -10.728 2.147   43.385 1.00 17.53 ? 160 GLN C NE2 1 
ATOM   4544 N N   . GLU C 1 161 ? -9.513  -3.555  44.946 1.00 15.39 ? 161 GLU C N   1 
ATOM   4545 C CA  . GLU C 1 161 ? -8.748  -4.737  44.565 1.00 19.58 ? 161 GLU C CA  1 
ATOM   4546 C C   . GLU C 1 161 ? -8.163  -4.516  43.187 1.00 24.30 ? 161 GLU C C   1 
ATOM   4547 O O   . GLU C 1 161 ? -8.590  -3.623  42.451 1.00 21.88 ? 161 GLU C O   1 
ATOM   4548 C CB  . GLU C 1 161 ? -9.631  -5.985  44.519 1.00 18.58 ? 161 GLU C CB  1 
ATOM   4549 C CG  . GLU C 1 161 ? -10.201 -6.455  45.853 1.00 32.15 ? 161 GLU C CG  1 
ATOM   4550 C CD  . GLU C 1 161 ? -11.010 -7.728  45.682 1.00 37.49 ? 161 GLU C CD  1 
ATOM   4551 O OE1 . GLU C 1 161 ? -11.162 -8.157  44.513 1.00 32.27 ? 161 GLU C OE1 1 
ATOM   4552 O OE2 . GLU C 1 161 ? -11.489 -8.299  46.697 1.00 38.47 ? 161 GLU C OE2 1 
ATOM   4553 N N   . SER C 1 162 ? -7.194  -5.347  42.832 1.00 23.28 ? 162 SER C N   1 
ATOM   4554 C CA  . SER C 1 162 ? -6.576  -5.279  41.521 1.00 17.48 ? 162 SER C CA  1 
ATOM   4555 C C   . SER C 1 162 ? -6.023  -6.657  41.210 1.00 18.34 ? 162 SER C C   1 
ATOM   4556 O O   . SER C 1 162 ? -5.383  -7.279  42.057 1.00 21.00 ? 162 SER C O   1 
ATOM   4557 C CB  . SER C 1 162 ? -5.475  -4.230  41.514 1.00 17.17 ? 162 SER C CB  1 
ATOM   4558 O OG  . SER C 1 162 ? -4.864  -4.133  40.247 1.00 24.07 ? 162 SER C OG  1 
ATOM   4559 N N   . VAL C 1 163 ? -6.310  -7.157  40.015 1.00 15.21 ? 163 VAL C N   1 
ATOM   4560 C CA  . VAL C 1 163 ? -5.885  -8.501  39.647 1.00 21.88 ? 163 VAL C CA  1 
ATOM   4561 C C   . VAL C 1 163 ? -4.983  -8.451  38.432 1.00 19.56 ? 163 VAL C C   1 
ATOM   4562 O O   . VAL C 1 163 ? -5.274  -7.741  37.472 1.00 21.21 ? 163 VAL C O   1 
ATOM   4563 C CB  . VAL C 1 163 ? -7.079  -9.419  39.345 1.00 21.83 ? 163 VAL C CB  1 
ATOM   4564 C CG1 . VAL C 1 163 ? -6.596  -10.822 39.027 1.00 25.83 ? 163 VAL C CG1 1 
ATOM   4565 C CG2 . VAL C 1 163 ? -8.017  -9.442  40.516 1.00 23.22 ? 163 VAL C CG2 1 
ATOM   4566 N N   . THR C 1 164 ? -3.876  -9.186  38.487 1.00 19.96 ? 164 THR C N   1 
ATOM   4567 C CA  . THR C 1 164 ? -2.974  -9.295  37.346 1.00 20.18 ? 164 THR C CA  1 
ATOM   4568 C C   . THR C 1 164 ? -3.650  -10.066 36.223 1.00 22.03 ? 164 THR C C   1 
ATOM   4569 O O   . THR C 1 164 ? -4.648  -10.753 36.434 1.00 26.42 ? 164 THR C O   1 
ATOM   4570 C CB  . THR C 1 164 ? -1.698  -10.032 37.726 1.00 15.18 ? 164 THR C CB  1 
ATOM   4571 O OG1 . THR C 1 164 ? -2.039  -11.224 38.429 1.00 20.47 ? 164 THR C OG1 1 
ATOM   4572 C CG2 . THR C 1 164 ? -0.828  -9.169  38.627 1.00 18.62 ? 164 THR C CG2 1 
ATOM   4573 N N   . GLU C 1 165 ? -3.123  -9.955  35.017 1.00 24.85 ? 165 GLU C N   1 
ATOM   4574 C CA  . GLU C 1 165 ? -3.561  -10.856 33.957 1.00 28.84 ? 165 GLU C CA  1 
ATOM   4575 C C   . GLU C 1 165 ? -3.005  -12.240 34.251 1.00 23.98 ? 165 GLU C C   1 
ATOM   4576 O O   . GLU C 1 165 ? -2.113  -12.389 35.072 1.00 22.45 ? 165 GLU C O   1 
ATOM   4577 C CB  . GLU C 1 165 ? -3.099  -10.361 32.582 1.00 23.71 ? 165 GLU C CB  1 
ATOM   4578 C CG  . GLU C 1 165 ? -3.907  -9.150  32.083 1.00 35.16 ? 165 GLU C CG  1 
ATOM   4579 C CD  . GLU C 1 165 ? -5.401  -9.454  31.923 1.00 33.68 ? 165 GLU C CD  1 
ATOM   4580 O OE1 . GLU C 1 165 ? -5.756  -10.625 31.664 1.00 39.01 ? 165 GLU C OE1 1 
ATOM   4581 O OE2 . GLU C 1 165 ? -6.224  -8.523  32.059 1.00 37.95 ? 165 GLU C OE2 1 
ATOM   4582 N N   . GLN C 1 166 ? -3.535  -13.259 33.597 1.00 30.34 ? 166 GLN C N   1 
ATOM   4583 C CA  . GLN C 1 166 ? -3.055  -14.604 33.862 1.00 26.67 ? 166 GLN C CA  1 
ATOM   4584 C C   . GLN C 1 166 ? -1.574  -14.736 33.504 1.00 28.10 ? 166 GLN C C   1 
ATOM   4585 O O   . GLN C 1 166 ? -1.120  -14.223 32.485 1.00 27.02 ? 166 GLN C O   1 
ATOM   4586 C CB  . GLN C 1 166 ? -3.892  -15.625 33.115 1.00 22.87 ? 166 GLN C CB  1 
ATOM   4587 C CG  . GLN C 1 166 ? -3.809  -16.989 33.723 1.00 30.16 ? 166 GLN C CG  1 
ATOM   4588 C CD  . GLN C 1 166 ? -4.648  -17.986 32.976 1.00 25.52 ? 166 GLN C CD  1 
ATOM   4589 O OE1 . GLN C 1 166 ? -5.130  -17.703 31.881 1.00 28.88 ? 166 GLN C OE1 1 
ATOM   4590 N NE2 . GLN C 1 166 ? -4.824  -19.165 33.557 1.00 22.35 ? 166 GLN C NE2 1 
ATOM   4591 N N   . ASP C 1 167 ? -0.830  -15.417 34.364 1.00 28.92 ? 167 ASP C N   1 
ATOM   4592 C CA  . ASP C 1 167 ? 0.624   -15.461 34.280 1.00 27.55 ? 167 ASP C CA  1 
ATOM   4593 C C   . ASP C 1 167 ? 1.146   -16.418 33.194 1.00 20.92 ? 167 ASP C C   1 
ATOM   4594 O O   . ASP C 1 167 ? 0.706   -17.549 33.094 1.00 28.37 ? 167 ASP C O   1 
ATOM   4595 C CB  . ASP C 1 167 ? 1.183   -15.834 35.656 1.00 32.13 ? 167 ASP C CB  1 
ATOM   4596 C CG  . ASP C 1 167 ? 2.682   -15.658 35.744 1.00 31.31 ? 167 ASP C CG  1 
ATOM   4597 O OD1 . ASP C 1 167 ? 3.403   -16.624 35.402 1.00 26.23 ? 167 ASP C OD1 1 
ATOM   4598 O OD2 . ASP C 1 167 ? 3.129   -14.561 36.163 1.00 32.90 ? 167 ASP C OD2 1 
ATOM   4599 N N   . SER C 1 168 ? 2.098   -15.980 32.386 1.00 26.30 ? 168 SER C N   1 
ATOM   4600 C CA  . SER C 1 168 ? 2.451   -16.777 31.210 1.00 26.45 ? 168 SER C CA  1 
ATOM   4601 C C   . SER C 1 168 ? 3.302   -17.995 31.522 1.00 29.99 ? 168 SER C C   1 
ATOM   4602 O O   . SER C 1 168 ? 3.513   -18.832 30.648 1.00 30.90 ? 168 SER C O   1 
ATOM   4603 C CB  . SER C 1 168 ? 3.077   -15.934 30.084 1.00 24.09 ? 168 SER C CB  1 
ATOM   4604 O OG  . SER C 1 168 ? 4.194   -15.196 30.528 1.00 23.12 ? 168 SER C OG  1 
ATOM   4605 N N   . LYS C 1 169 ? 3.770   -18.123 32.761 1.00 25.92 ? 169 LYS C N   1 
ATOM   4606 C CA  . LYS C 1 169 ? 4.525   -19.322 33.117 1.00 26.53 ? 169 LYS C CA  1 
ATOM   4607 C C   . LYS C 1 169 ? 3.650   -20.406 33.747 1.00 28.30 ? 169 LYS C C   1 
ATOM   4608 O O   . LYS C 1 169 ? 3.627   -21.536 33.257 1.00 30.31 ? 169 LYS C O   1 
ATOM   4609 C CB  . LYS C 1 169 ? 5.749   -18.992 33.985 1.00 22.17 ? 169 LYS C CB  1 
ATOM   4610 N N   . ASP C 1 170 ? 2.908   -20.056 34.800 1.00 26.41 ? 170 ASP C N   1 
ATOM   4611 C CA  . ASP C 1 170 ? 2.174   -21.051 35.602 1.00 22.06 ? 170 ASP C CA  1 
ATOM   4612 C C   . ASP C 1 170 ? 0.655   -20.912 35.563 1.00 19.44 ? 170 ASP C C   1 
ATOM   4613 O O   . ASP C 1 170 ? -0.053  -21.657 36.235 1.00 17.64 ? 170 ASP C O   1 
ATOM   4614 C CB  . ASP C 1 170 ? 2.643   -21.025 37.062 1.00 19.12 ? 170 ASP C CB  1 
ATOM   4615 C CG  . ASP C 1 170 ? 2.445   -19.655 37.732 1.00 32.48 ? 170 ASP C CG  1 
ATOM   4616 O OD1 . ASP C 1 170 ? 1.717   -18.791 37.186 1.00 26.67 ? 170 ASP C OD1 1 
ATOM   4617 O OD2 . ASP C 1 170 ? 3.033   -19.438 38.816 1.00 34.59 ? 170 ASP C OD2 1 
ATOM   4618 N N   . SER C 1 171 ? 0.176   -19.931 34.806 1.00 20.70 ? 171 SER C N   1 
ATOM   4619 C CA  . SER C 1 171 ? -1.260  -19.708 34.575 1.00 23.43 ? 171 SER C CA  1 
ATOM   4620 C C   . SER C 1 171 ? -2.079  -19.270 35.801 1.00 24.63 ? 171 SER C C   1 
ATOM   4621 O O   . SER C 1 171 ? -3.304  -19.405 35.804 1.00 18.36 ? 171 SER C O   1 
ATOM   4622 C CB  . SER C 1 171 ? -1.909  -20.930 33.918 1.00 16.61 ? 171 SER C CB  1 
ATOM   4623 O OG  . SER C 1 171 ? -1.281  -21.230 32.692 1.00 22.68 ? 171 SER C OG  1 
ATOM   4624 N N   . THR C 1 172 ? -1.417  -18.735 36.822 1.00 14.78 ? 172 THR C N   1 
ATOM   4625 C CA  . THR C 1 172 ? -2.127  -18.242 37.988 1.00 18.59 ? 172 THR C CA  1 
ATOM   4626 C C   . THR C 1 172 ? -2.385  -16.744 37.938 1.00 21.46 ? 172 THR C C   1 
ATOM   4627 O O   . THR C 1 172 ? -1.858  -16.030 37.081 1.00 27.37 ? 172 THR C O   1 
ATOM   4628 C CB  . THR C 1 172 ? -1.353  -18.512 39.276 1.00 18.87 ? 172 THR C CB  1 
ATOM   4629 O OG1 . THR C 1 172 ? -0.179  -17.692 39.303 1.00 19.00 ? 172 THR C OG1 1 
ATOM   4630 C CG2 . THR C 1 172 ? -0.990  -19.977 39.394 1.00 15.99 ? 172 THR C CG2 1 
ATOM   4631 N N   . TYR C 1 173 ? -3.191  -16.278 38.884 1.00 17.36 ? 173 TYR C N   1 
ATOM   4632 C CA  . TYR C 1 173 ? -3.449  -14.859 39.059 1.00 19.65 ? 173 TYR C CA  1 
ATOM   4633 C C   . TYR C 1 173 ? -2.870  -14.432 40.384 1.00 20.42 ? 173 TYR C C   1 
ATOM   4634 O O   . TYR C 1 173 ? -2.662  -15.261 41.271 1.00 22.23 ? 173 TYR C O   1 
ATOM   4635 C CB  . TYR C 1 173 ? -4.959  -14.576 39.066 1.00 20.22 ? 173 TYR C CB  1 
ATOM   4636 C CG  . TYR C 1 173 ? -5.655  -15.001 37.808 1.00 22.16 ? 173 TYR C CG  1 
ATOM   4637 C CD1 . TYR C 1 173 ? -5.833  -14.107 36.758 1.00 25.85 ? 173 TYR C CD1 1 
ATOM   4638 C CD2 . TYR C 1 173 ? -6.116  -16.304 37.653 1.00 23.24 ? 173 TYR C CD2 1 
ATOM   4639 C CE1 . TYR C 1 173 ? -6.464  -14.493 35.580 1.00 22.08 ? 173 TYR C CE1 1 
ATOM   4640 C CE2 . TYR C 1 173 ? -6.747  -16.708 36.486 1.00 27.06 ? 173 TYR C CE2 1 
ATOM   4641 C CZ  . TYR C 1 173 ? -6.922  -15.794 35.450 1.00 28.51 ? 173 TYR C CZ  1 
ATOM   4642 O OH  . TYR C 1 173 ? -7.541  -16.183 34.290 1.00 31.31 ? 173 TYR C OH  1 
ATOM   4643 N N   . SER C 1 174 ? -2.614  -13.137 40.522 1.00 20.00 ? 174 SER C N   1 
ATOM   4644 C CA  . SER C 1 174 ? -2.357  -12.570 41.835 1.00 16.53 ? 174 SER C CA  1 
ATOM   4645 C C   . SER C 1 174 ? -3.302  -11.393 42.056 1.00 19.08 ? 174 SER C C   1 
ATOM   4646 O O   . SER C 1 174 ? -3.752  -10.762 41.097 1.00 24.36 ? 174 SER C O   1 
ATOM   4647 C CB  . SER C 1 174 ? -0.887  -12.174 41.991 1.00 18.44 ? 174 SER C CB  1 
ATOM   4648 O OG  . SER C 1 174 ? -0.071  -13.333 42.080 1.00 17.13 ? 174 SER C OG  1 
ATOM   4649 N N   . LEU C 1 175 ? -3.629  -11.125 43.314 1.00 18.52 ? 175 LEU C N   1 
ATOM   4650 C CA  . LEU C 1 175 ? -4.520  -10.024 43.675 1.00 17.65 ? 175 LEU C CA  1 
ATOM   4651 C C   . LEU C 1 175 ? -3.931  -9.223  44.843 1.00 19.62 ? 175 LEU C C   1 
ATOM   4652 O O   . LEU C 1 175 ? -3.315  -9.764  45.761 1.00 13.80 ? 175 LEU C O   1 
ATOM   4653 C CB  . LEU C 1 175 ? -5.921  -10.549 44.024 1.00 12.95 ? 175 LEU C CB  1 
ATOM   4654 C CG  . LEU C 1 175 ? -7.058  -9.610  44.490 1.00 22.44 ? 175 LEU C CG  1 
ATOM   4655 C CD1 . LEU C 1 175 ? -8.442  -10.251 44.261 1.00 12.12 ? 175 LEU C CD1 1 
ATOM   4656 C CD2 . LEU C 1 175 ? -6.933  -9.205  45.946 1.00 12.83 ? 175 LEU C CD2 1 
ATOM   4657 N N   . SER C 1 176 ? -4.132  -7.918  44.796 1.00 19.47 ? 176 SER C N   1 
ATOM   4658 C CA  . SER C 1 176 ? -3.799  -7.085  45.919 1.00 20.06 ? 176 SER C CA  1 
ATOM   4659 C C   . SER C 1 176 ? -5.031  -6.279  46.301 1.00 20.28 ? 176 SER C C   1 
ATOM   4660 O O   . SER C 1 176 ? -5.681  -5.679  45.448 1.00 20.93 ? 176 SER C O   1 
ATOM   4661 C CB  . SER C 1 176 ? -2.645  -6.165  45.575 1.00 15.25 ? 176 SER C CB  1 
ATOM   4662 O OG  . SER C 1 176 ? -3.105  -5.148  44.729 1.00 27.89 ? 176 SER C OG  1 
ATOM   4663 N N   . SER C 1 177 ? -5.346  -6.283  47.590 1.00 17.96 ? 177 SER C N   1 
ATOM   4664 C CA  . SER C 1 177 ? -6.441  -5.500  48.136 1.00 18.80 ? 177 SER C CA  1 
ATOM   4665 C C   . SER C 1 177 ? -5.823  -4.392  48.978 1.00 18.89 ? 177 SER C C   1 
ATOM   4666 O O   . SER C 1 177 ? -4.927  -4.644  49.781 1.00 19.85 ? 177 SER C O   1 
ATOM   4667 C CB  . SER C 1 177 ? -7.350  -6.408  48.981 1.00 19.87 ? 177 SER C CB  1 
ATOM   4668 O OG  . SER C 1 177 ? -8.490  -5.731  49.473 1.00 19.75 ? 177 SER C OG  1 
ATOM   4669 N N   . THR C 1 178 ? -6.267  -3.161  48.753 1.00 20.35 ? 178 THR C N   1 
ATOM   4670 C CA  . THR C 1 178 ? -5.791  -2.014  49.516 1.00 14.29 ? 178 THR C CA  1 
ATOM   4671 C C   . THR C 1 178 ? -6.921  -1.406  50.333 1.00 17.52 ? 178 THR C C   1 
ATOM   4672 O O   . THR C 1 178 ? -7.898  -0.899  49.772 1.00 14.21 ? 178 THR C O   1 
ATOM   4673 C CB  . THR C 1 178 ? -5.236  -0.908  48.620 1.00 9.85  ? 178 THR C CB  1 
ATOM   4674 O OG1 . THR C 1 178 ? -4.107  -1.397  47.903 1.00 21.89 ? 178 THR C OG1 1 
ATOM   4675 C CG2 . THR C 1 178 ? -4.803  0.282   49.462 1.00 15.41 ? 178 THR C CG2 1 
ATOM   4676 N N   . LEU C 1 179 ? -6.765  -1.449  51.655 1.00 15.93 ? 179 LEU C N   1 
ATOM   4677 C CA  . LEU C 1 179 ? -7.681  -0.796  52.585 1.00 13.98 ? 179 LEU C CA  1 
ATOM   4678 C C   . LEU C 1 179 ? -7.167  0.609   52.854 1.00 14.28 ? 179 LEU C C   1 
ATOM   4679 O O   . LEU C 1 179 ? -6.030  0.777   53.292 1.00 18.71 ? 179 LEU C O   1 
ATOM   4680 C CB  . LEU C 1 179 ? -7.740  -1.592  53.896 1.00 13.37 ? 179 LEU C CB  1 
ATOM   4681 C CG  . LEU C 1 179 ? -8.648  -1.076  55.015 1.00 15.75 ? 179 LEU C CG  1 
ATOM   4682 C CD1 . LEU C 1 179 ? -10.102 -1.439  54.728 1.00 17.54 ? 179 LEU C CD1 1 
ATOM   4683 C CD2 . LEU C 1 179 ? -8.201  -1.580  56.388 1.00 12.46 ? 179 LEU C CD2 1 
ATOM   4684 N N   . THR C 1 180 ? -7.978  1.614   52.539 1.00 18.29 ? 180 THR C N   1 
ATOM   4685 C CA  . THR C 1 180 ? -7.592  3.004   52.780 1.00 15.19 ? 180 THR C CA  1 
ATOM   4686 C C   . THR C 1 180 ? -8.331  3.575   53.973 1.00 19.33 ? 180 THR C C   1 
ATOM   4687 O O   . THR C 1 180 ? -9.553  3.443   54.096 1.00 27.03 ? 180 THR C O   1 
ATOM   4688 C CB  . THR C 1 180 ? -7.795  3.900   51.547 1.00 15.87 ? 180 THR C CB  1 
ATOM   4689 O OG1 . THR C 1 180 ? -7.059  3.363   50.438 1.00 25.44 ? 180 THR C OG1 1 
ATOM   4690 C CG2 . THR C 1 180 ? -7.279  5.308   51.834 1.00 11.24 ? 180 THR C CG2 1 
ATOM   4691 N N   . LEU C 1 181 ? -7.597  4.164   54.880 1.00 18.26 ? 181 LEU C N   1 
ATOM   4692 C CA  . LEU C 1 181 ? -8.070  4.668   56.141 1.00 18.83 ? 181 LEU C CA  1 
ATOM   4693 C C   . LEU C 1 181 ? -7.402  5.961   56.444 1.00 19.44 ? 181 LEU C C   1 
ATOM   4694 O O   . LEU C 1 181 ? -6.314  6.171   56.078 1.00 19.48 ? 181 LEU C O   1 
ATOM   4695 C CB  . LEU C 1 181 ? -7.703  3.721   57.258 1.00 18.24 ? 181 LEU C CB  1 
ATOM   4696 C CG  . LEU C 1 181 ? -8.349  2.404   57.571 1.00 28.83 ? 181 LEU C CG  1 
ATOM   4697 C CD1 . LEU C 1 181 ? -7.652  1.715   58.715 1.00 24.06 ? 181 LEU C CD1 1 
ATOM   4698 C CD2 . LEU C 1 181 ? -9.810  2.554   57.873 1.00 30.14 ? 181 LEU C CD2 1 
ATOM   4699 N N   . SER C 1 182 ? -8.053  6.819   57.191 1.00 23.91 ? 182 SER C N   1 
ATOM   4700 C CA  . SER C 1 182 ? -7.416  8.061   57.631 1.00 23.66 ? 182 SER C CA  1 
ATOM   4701 C C   . SER C 1 182 ? -6.391  7.708   58.707 1.00 24.51 ? 182 SER C C   1 
ATOM   4702 O O   . SER C 1 182 ? -6.518  6.676   59.381 1.00 20.80 ? 182 SER C O   1 
ATOM   4703 C CB  . SER C 1 182 ? -8.454  9.041   58.167 1.00 19.75 ? 182 SER C CB  1 
ATOM   4704 O OG  . SER C 1 182 ? -9.056  8.558   59.339 1.00 30.23 ? 182 SER C OG  1 
ATOM   4705 N N   . LYS C 1 183 ? -5.366  8.538   58.857 1.00 22.21 ? 183 LYS C N   1 
ATOM   4706 C CA  . LYS C 1 183 ? -4.382  8.319   59.922 1.00 26.76 ? 183 LYS C CA  1 
ATOM   4707 C C   . LYS C 1 183 ? -5.057  8.224   61.299 1.00 29.64 ? 183 LYS C C   1 
ATOM   4708 O O   . LYS C 1 183 ? -4.683  7.398   62.133 1.00 22.15 ? 183 LYS C O   1 
ATOM   4709 C CB  . LYS C 1 183 ? -3.320  9.421   59.939 1.00 28.45 ? 183 LYS C CB  1 
ATOM   4710 C CG  . LYS C 1 183 ? -2.200  9.172   60.951 1.00 26.49 ? 183 LYS C CG  1 
ATOM   4711 C CD  . LYS C 1 183 ? -1.414  10.444  61.276 1.00 33.11 ? 183 LYS C CD  1 
ATOM   4712 C CE  . LYS C 1 183 ? -0.356  10.182  62.357 1.00 41.26 ? 183 LYS C CE  1 
ATOM   4713 N NZ  . LYS C 1 183 ? -0.054  11.386  63.205 1.00 43.61 ? 183 LYS C NZ  1 
ATOM   4714 N N   . ALA C 1 184 ? -6.069  9.058   61.520 1.00 24.78 ? 184 ALA C N   1 
ATOM   4715 C CA  . ALA C 1 184 ? -6.765  9.084   62.803 1.00 28.64 ? 184 ALA C CA  1 
ATOM   4716 C C   . ALA C 1 184 ? -7.486  7.765   63.092 1.00 32.09 ? 184 ALA C C   1 
ATOM   4717 O O   . ALA C 1 184 ? -7.361  7.211   64.187 1.00 25.75 ? 184 ALA C O   1 
ATOM   4718 C CB  . ALA C 1 184 ? -7.747  10.260  62.862 1.00 22.05 ? 184 ALA C CB  1 
ATOM   4719 N N   . ASP C 1 185 ? -8.244  7.277   62.110 1.00 30.67 ? 185 ASP C N   1 
ATOM   4720 C CA  . ASP C 1 185 ? -8.955  6.021   62.259 1.00 25.46 ? 185 ASP C CA  1 
ATOM   4721 C C   . ASP C 1 185 ? -7.964  4.894   62.505 1.00 24.56 ? 185 ASP C C   1 
ATOM   4722 O O   . ASP C 1 185 ? -8.190  4.037   63.359 1.00 24.00 ? 185 ASP C O   1 
ATOM   4723 C CB  . ASP C 1 185 ? -9.818  5.722   61.020 1.00 33.96 ? 185 ASP C CB  1 
ATOM   4724 C CG  . ASP C 1 185 ? -11.177 6.412   61.070 1.00 37.48 ? 185 ASP C CG  1 
ATOM   4725 O OD1 . ASP C 1 185 ? -11.539 6.942   62.149 1.00 40.56 ? 185 ASP C OD1 1 
ATOM   4726 O OD2 . ASP C 1 185 ? -11.889 6.407   60.037 1.00 35.97 ? 185 ASP C OD2 1 
ATOM   4727 N N   . TYR C 1 186 ? -6.866  4.906   61.754 1.00 21.10 ? 186 TYR C N   1 
ATOM   4728 C CA  . TYR C 1 186 ? -5.869  3.854   61.867 1.00 21.16 ? 186 TYR C CA  1 
ATOM   4729 C C   . TYR C 1 186 ? -5.296  3.811   63.280 1.00 23.05 ? 186 TYR C C   1 
ATOM   4730 O O   . TYR C 1 186 ? -5.101  2.734   63.840 1.00 22.93 ? 186 TYR C O   1 
ATOM   4731 C CB  . TYR C 1 186 ? -4.750  4.029   60.831 1.00 20.12 ? 186 TYR C CB  1 
ATOM   4732 C CG  . TYR C 1 186 ? -3.628  3.032   60.990 1.00 20.78 ? 186 TYR C CG  1 
ATOM   4733 C CD1 . TYR C 1 186 ? -3.811  1.690   60.676 1.00 21.82 ? 186 TYR C CD1 1 
ATOM   4734 C CD2 . TYR C 1 186 ? -2.379  3.428   61.461 1.00 24.25 ? 186 TYR C CD2 1 
ATOM   4735 C CE1 . TYR C 1 186 ? -2.773  0.763   60.834 1.00 18.57 ? 186 TYR C CE1 1 
ATOM   4736 C CE2 . TYR C 1 186 ? -1.335  2.510   61.614 1.00 18.82 ? 186 TYR C CE2 1 
ATOM   4737 C CZ  . TYR C 1 186 ? -1.542  1.187   61.303 1.00 19.32 ? 186 TYR C CZ  1 
ATOM   4738 O OH  . TYR C 1 186 ? -0.511  0.293   61.461 1.00 22.92 ? 186 TYR C OH  1 
ATOM   4739 N N   . GLU C 1 187 ? -5.046  4.987   63.853 1.00 27.92 ? 187 GLU C N   1 
ATOM   4740 C CA  . GLU C 1 187 ? -4.484  5.097   65.200 1.00 24.47 ? 187 GLU C CA  1 
ATOM   4741 C C   . GLU C 1 187 ? -5.451  4.680   66.306 1.00 24.16 ? 187 GLU C C   1 
ATOM   4742 O O   . GLU C 1 187 ? -5.030  4.343   67.399 1.00 32.81 ? 187 GLU C O   1 
ATOM   4743 C CB  . GLU C 1 187 ? -3.977  6.517   65.471 1.00 27.18 ? 187 GLU C CB  1 
ATOM   4744 C CG  . GLU C 1 187 ? -2.786  6.956   64.630 1.00 32.55 ? 187 GLU C CG  1 
ATOM   4745 C CD  . GLU C 1 187 ? -1.541  6.093   64.826 1.00 40.96 ? 187 GLU C CD  1 
ATOM   4746 O OE1 . GLU C 1 187 ? -1.462  5.347   65.832 1.00 38.30 ? 187 GLU C OE1 1 
ATOM   4747 O OE2 . GLU C 1 187 ? -0.634  6.157   63.961 1.00 42.32 ? 187 GLU C OE2 1 
ATOM   4748 N N   . LYS C 1 188 ? -6.744  4.702   66.025 1.00 24.32 ? 188 LYS C N   1 
ATOM   4749 C CA  . LYS C 1 188 ? -7.744  4.337   67.031 1.00 28.05 ? 188 LYS C CA  1 
ATOM   4750 C C   . LYS C 1 188 ? -7.987  2.836   67.171 1.00 26.83 ? 188 LYS C C   1 
ATOM   4751 O O   . LYS C 1 188 ? -8.763  2.410   68.017 1.00 27.98 ? 188 LYS C O   1 
ATOM   4752 C CB  . LYS C 1 188 ? -9.078  5.038   66.746 1.00 27.20 ? 188 LYS C CB  1 
ATOM   4753 C CG  . LYS C 1 188 ? -9.078  6.511   67.107 1.00 33.67 ? 188 LYS C CG  1 
ATOM   4754 C CD  . LYS C 1 188 ? -10.391 7.193   66.746 1.00 36.95 ? 188 LYS C CD  1 
ATOM   4755 C CE  . LYS C 1 188 ? -10.376 8.675   67.136 1.00 39.76 ? 188 LYS C CE  1 
ATOM   4756 N NZ  . LYS C 1 188 ? -9.465  9.511   66.288 1.00 28.77 ? 188 LYS C NZ  1 
ATOM   4757 N N   . HIS C 1 189 ? -7.335  2.030   66.347 1.00 26.44 ? 189 HIS C N   1 
ATOM   4758 C CA  . HIS C 1 189 ? -7.636  0.604   66.341 1.00 24.12 ? 189 HIS C CA  1 
ATOM   4759 C C   . HIS C 1 189 ? -6.384  -0.255  66.433 1.00 23.95 ? 189 HIS C C   1 
ATOM   4760 O O   . HIS C 1 189 ? -5.273  0.237   66.240 1.00 24.26 ? 189 HIS C O   1 
ATOM   4761 C CB  . HIS C 1 189 ? -8.479  0.256   65.117 1.00 23.17 ? 189 HIS C CB  1 
ATOM   4762 C CG  . HIS C 1 189 ? -9.834  0.889   65.133 1.00 31.07 ? 189 HIS C CG  1 
ATOM   4763 N ND1 . HIS C 1 189 ? -10.176 1.947   64.320 1.00 36.44 ? 189 HIS C ND1 1 
ATOM   4764 C CD2 . HIS C 1 189 ? -10.931 0.628   65.890 1.00 27.66 ? 189 HIS C CD2 1 
ATOM   4765 C CE1 . HIS C 1 189 ? -11.426 2.301   64.563 1.00 29.28 ? 189 HIS C CE1 1 
ATOM   4766 N NE2 . HIS C 1 189 ? -11.903 1.517   65.514 1.00 27.96 ? 189 HIS C NE2 1 
ATOM   4767 N N   . LYS C 1 190 ? -6.560  -1.533  66.733 1.00 19.25 ? 190 LYS C N   1 
ATOM   4768 C CA  . LYS C 1 190 ? -5.408  -2.368  67.026 1.00 25.53 ? 190 LYS C CA  1 
ATOM   4769 C C   . LYS C 1 190 ? -5.198  -3.510  66.050 1.00 20.90 ? 190 LYS C C   1 
ATOM   4770 O O   . LYS C 1 190 ? -4.109  -3.663  65.499 1.00 28.50 ? 190 LYS C O   1 
ATOM   4771 C CB  . LYS C 1 190 ? -5.479  -2.927  68.457 1.00 30.10 ? 190 LYS C CB  1 
ATOM   4772 C CG  . LYS C 1 190 ? -4.153  -3.525  68.937 1.00 31.35 ? 190 LYS C CG  1 
ATOM   4773 C CD  . LYS C 1 190 ? -4.281  -4.316  70.231 1.00 44.03 ? 190 LYS C CD  1 
ATOM   4774 C CE  . LYS C 1 190 ? -2.931  -4.907  70.637 1.00 45.58 ? 190 LYS C CE  1 
ATOM   4775 N NZ  . LYS C 1 190 ? -2.965  -5.548  71.982 1.00 47.19 ? 190 LYS C NZ  1 
ATOM   4776 N N   . VAL C 1 191 ? -6.219  -4.332  65.863 1.00 17.17 ? 191 VAL C N   1 
ATOM   4777 C CA  . VAL C 1 191 ? -6.061  -5.552  65.090 1.00 19.64 ? 191 VAL C CA  1 
ATOM   4778 C C   . VAL C 1 191 ? -6.516  -5.399  63.651 1.00 22.81 ? 191 VAL C C   1 
ATOM   4779 O O   . VAL C 1 191 ? -7.706  -5.235  63.384 1.00 22.93 ? 191 VAL C O   1 
ATOM   4780 C CB  . VAL C 1 191 ? -6.863  -6.710  65.700 1.00 21.83 ? 191 VAL C CB  1 
ATOM   4781 C CG1 . VAL C 1 191 ? -6.673  -7.973  64.861 1.00 16.21 ? 191 VAL C CG1 1 
ATOM   4782 C CG2 . VAL C 1 191 ? -6.452  -6.940  67.139 1.00 23.20 ? 191 VAL C CG2 1 
ATOM   4783 N N   . TYR C 1 192 ? -5.570  -5.495  62.725 1.00 19.54 ? 192 TYR C N   1 
ATOM   4784 C CA  . TYR C 1 192 ? -5.876  -5.434  61.304 1.00 17.70 ? 192 TYR C CA  1 
ATOM   4785 C C   . TYR C 1 192 ? -5.796  -6.813  60.657 1.00 18.02 ? 192 TYR C C   1 
ATOM   4786 O O   . TYR C 1 192 ? -4.887  -7.589  60.914 1.00 20.96 ? 192 TYR C O   1 
ATOM   4787 C CB  . TYR C 1 192 ? -4.974  -4.408  60.618 1.00 15.87 ? 192 TYR C CB  1 
ATOM   4788 C CG  . TYR C 1 192 ? -5.281  -3.032  61.122 1.00 19.17 ? 192 TYR C CG  1 
ATOM   4789 C CD1 . TYR C 1 192 ? -6.217  -2.236  60.480 1.00 15.00 ? 192 TYR C CD1 1 
ATOM   4790 C CD2 . TYR C 1 192 ? -4.686  -2.549  62.287 1.00 20.23 ? 192 TYR C CD2 1 
ATOM   4791 C CE1 . TYR C 1 192 ? -6.520  -0.983  60.949 1.00 19.58 ? 192 TYR C CE1 1 
ATOM   4792 C CE2 . TYR C 1 192 ? -4.992  -1.303  62.772 1.00 21.74 ? 192 TYR C CE2 1 
ATOM   4793 C CZ  . TYR C 1 192 ? -5.915  -0.522  62.102 1.00 23.03 ? 192 TYR C CZ  1 
ATOM   4794 O OH  . TYR C 1 192 ? -6.230  0.730   62.579 1.00 23.64 ? 192 TYR C OH  1 
ATOM   4795 N N   . ALA C 1 193 ? -6.769  -7.126  59.821 1.00 18.13 ? 193 ALA C N   1 
ATOM   4796 C CA  . ALA C 1 193 ? -6.878  -8.475  59.296 1.00 16.85 ? 193 ALA C CA  1 
ATOM   4797 C C   . ALA C 1 193 ? -7.450  -8.484  57.903 1.00 20.69 ? 193 ALA C C   1 
ATOM   4798 O O   . ALA C 1 193 ? -8.315  -7.674  57.555 1.00 23.44 ? 193 ALA C O   1 
ATOM   4799 C CB  . ALA C 1 193 ? -7.749  -9.333  60.218 1.00 11.53 ? 193 ALA C CB  1 
ATOM   4800 N N   . CYS C 1 194 ? -6.973  -9.410  57.096 1.00 16.55 ? 194 CYS C N   1 
ATOM   4801 C CA  . CYS C 1 194 ? -7.676  -9.687  55.864 1.00 23.84 ? 194 CYS C CA  1 
ATOM   4802 C C   . CYS C 1 194 ? -7.974  -11.164 55.823 1.00 19.16 ? 194 CYS C C   1 
ATOM   4803 O O   . CYS C 1 194 ? -7.104  -11.997 56.073 1.00 24.77 ? 194 CYS C O   1 
ATOM   4804 C CB  . CYS C 1 194 ? -6.910  -9.211  54.617 1.00 27.95 ? 194 CYS C CB  1 
ATOM   4805 S SG  . CYS C 1 194 ? -5.373  -10.074 54.250 1.00 33.10 ? 194 CYS C SG  1 
ATOM   4806 N N   . GLU C 1 195 ? -9.227  -11.476 55.535 1.00 21.27 ? 195 GLU C N   1 
ATOM   4807 C CA  . GLU C 1 195 ? -9.670  -12.848 55.467 1.00 22.82 ? 195 GLU C CA  1 
ATOM   4808 C C   . GLU C 1 195 ? -9.838  -13.174 54.008 1.00 19.84 ? 195 GLU C C   1 
ATOM   4809 O O   . GLU C 1 195 ? -10.290 -12.343 53.221 1.00 26.82 ? 195 GLU C O   1 
ATOM   4810 C CB  . GLU C 1 195 ? -10.997 -12.997 56.194 1.00 25.44 ? 195 GLU C CB  1 
ATOM   4811 C CG  . GLU C 1 195 ? -11.358 -14.416 56.525 1.00 29.59 ? 195 GLU C CG  1 
ATOM   4812 C CD  . GLU C 1 195 ? -12.667 -14.500 57.293 1.00 38.29 ? 195 GLU C CD  1 
ATOM   4813 O OE1 . GLU C 1 195 ? -13.157 -13.434 57.740 1.00 33.03 ? 195 GLU C OE1 1 
ATOM   4814 O OE2 . GLU C 1 195 ? -13.205 -15.623 57.442 1.00 36.53 ? 195 GLU C OE2 1 
ATOM   4815 N N   . VAL C 1 196 ? -9.474  -14.384 53.634 1.00 18.29 ? 196 VAL C N   1 
ATOM   4816 C CA  . VAL C 1 196 ? -9.511  -14.735 52.237 1.00 16.89 ? 196 VAL C CA  1 
ATOM   4817 C C   . VAL C 1 196 ? -10.319 -16.005 52.038 1.00 20.32 ? 196 VAL C C   1 
ATOM   4818 O O   . VAL C 1 196 ? -10.094 -17.011 52.713 1.00 25.33 ? 196 VAL C O   1 
ATOM   4819 C CB  . VAL C 1 196 ? -8.080  -14.902 51.659 1.00 19.25 ? 196 VAL C CB  1 
ATOM   4820 C CG1 . VAL C 1 196 ? -8.139  -15.243 50.182 1.00 19.14 ? 196 VAL C CG1 1 
ATOM   4821 C CG2 . VAL C 1 196 ? -7.249  -13.632 51.881 1.00 11.57 ? 196 VAL C CG2 1 
ATOM   4822 N N   . THR C 1 197 ? -11.265 -15.961 51.109 1.00 19.67 ? 197 THR C N   1 
ATOM   4823 C CA  . THR C 1 197 ? -11.969 -17.168 50.705 1.00 20.75 ? 197 THR C CA  1 
ATOM   4824 C C   . THR C 1 197 ? -11.695 -17.419 49.230 1.00 21.47 ? 197 THR C C   1 
ATOM   4825 O O   . THR C 1 197 ? -11.629 -16.490 48.436 1.00 27.41 ? 197 THR C O   1 
ATOM   4826 C CB  . THR C 1 197 ? -13.492 -17.055 50.957 1.00 18.22 ? 197 THR C CB  1 
ATOM   4827 O OG1 . THR C 1 197 ? -14.005 -15.942 50.221 1.00 24.72 ? 197 THR C OG1 1 
ATOM   4828 C CG2 . THR C 1 197 ? -13.761 -16.840 52.414 1.00 17.13 ? 197 THR C CG2 1 
ATOM   4829 N N   . HIS C 1 198 ? -11.529 -18.682 48.874 1.00 22.58 ? 198 HIS C N   1 
ATOM   4830 C CA  . HIS C 1 198 ? -11.191 -19.057 47.515 1.00 23.09 ? 198 HIS C CA  1 
ATOM   4831 C C   . HIS C 1 198 ? -11.469 -20.548 47.348 1.00 27.98 ? 198 HIS C C   1 
ATOM   4832 O O   . HIS C 1 198 ? -11.398 -21.307 48.316 1.00 24.00 ? 198 HIS C O   1 
ATOM   4833 C CB  . HIS C 1 198 ? -9.712  -18.749 47.243 1.00 23.68 ? 198 HIS C CB  1 
ATOM   4834 C CG  . HIS C 1 198 ? -9.230  -19.215 45.906 1.00 19.65 ? 198 HIS C CG  1 
ATOM   4835 N ND1 . HIS C 1 198 ? -8.638  -20.442 45.719 1.00 19.20 ? 198 HIS C ND1 1 
ATOM   4836 C CD2 . HIS C 1 198 ? -9.245  -18.617 44.689 1.00 21.48 ? 198 HIS C CD2 1 
ATOM   4837 C CE1 . HIS C 1 198 ? -8.308  -20.583 44.446 1.00 21.69 ? 198 HIS C CE1 1 
ATOM   4838 N NE2 . HIS C 1 198 ? -8.666  -19.488 43.799 1.00 19.77 ? 198 HIS C NE2 1 
ATOM   4839 N N   . GLN C 1 199 ? -11.790 -20.954 46.121 1.00 21.44 ? 199 GLN C N   1 
ATOM   4840 C CA  . GLN C 1 199 ? -12.069 -22.351 45.815 1.00 25.22 ? 199 GLN C CA  1 
ATOM   4841 C C   . GLN C 1 199 ? -11.024 -23.347 46.337 1.00 25.24 ? 199 GLN C C   1 
ATOM   4842 O O   . GLN C 1 199 ? -11.370 -24.429 46.802 1.00 31.70 ? 199 GLN C O   1 
ATOM   4843 C CB  . GLN C 1 199 ? -12.247 -22.540 44.316 1.00 24.20 ? 199 GLN C CB  1 
ATOM   4844 C CG  . GLN C 1 199 ? -12.537 -23.963 43.942 1.00 27.98 ? 199 GLN C CG  1 
ATOM   4845 C CD  . GLN C 1 199 ? -12.862 -24.096 42.485 1.00 35.68 ? 199 GLN C CD  1 
ATOM   4846 O OE1 . GLN C 1 199 ? -13.191 -23.110 41.826 1.00 47.54 ? 199 GLN C OE1 1 
ATOM   4847 N NE2 . GLN C 1 199 ? -12.764 -25.310 41.961 1.00 33.17 ? 199 GLN C NE2 1 
ATOM   4848 N N   . GLY C 1 200 ? -9.752  -22.978 46.262 1.00 23.68 ? 200 GLY C N   1 
ATOM   4849 C CA  . GLY C 1 200 ? -8.688  -23.805 46.790 1.00 17.78 ? 200 GLY C CA  1 
ATOM   4850 C C   . GLY C 1 200 ? -8.521  -23.728 48.296 1.00 21.72 ? 200 GLY C C   1 
ATOM   4851 O O   . GLY C 1 200 ? -7.570  -24.275 48.838 1.00 25.47 ? 200 GLY C O   1 
ATOM   4852 N N   . LEU C 1 201 ? -9.424  -23.045 48.986 1.00 24.66 ? 201 LEU C N   1 
ATOM   4853 C CA  . LEU C 1 201 ? -9.356  -23.041 50.455 1.00 31.01 ? 201 LEU C CA  1 
ATOM   4854 C C   . LEU C 1 201 ? -10.544 -23.769 51.114 1.00 27.73 ? 201 LEU C C   1 
ATOM   4855 O O   . LEU C 1 201 ? -11.707 -23.424 50.902 1.00 24.25 ? 201 LEU C O   1 
ATOM   4856 C CB  . LEU C 1 201 ? -9.195  -21.622 51.008 1.00 26.47 ? 201 LEU C CB  1 
ATOM   4857 C CG  . LEU C 1 201 ? -7.922  -20.887 50.585 1.00 25.43 ? 201 LEU C CG  1 
ATOM   4858 C CD1 . LEU C 1 201 ? -7.969  -19.450 51.082 1.00 22.22 ? 201 LEU C CD1 1 
ATOM   4859 C CD2 . LEU C 1 201 ? -6.664  -21.595 51.074 1.00 13.18 ? 201 LEU C CD2 1 
ATOM   4860 N N   . SER C 1 202 ? -10.228 -24.795 51.895 1.00 30.77 ? 202 SER C N   1 
ATOM   4861 C CA  . SER C 1 202 ? -11.240 -25.569 52.611 1.00 32.78 ? 202 SER C CA  1 
ATOM   4862 C C   . SER C 1 202 ? -11.922 -24.684 53.645 1.00 31.25 ? 202 SER C C   1 
ATOM   4863 O O   . SER C 1 202 ? -13.127 -24.763 53.837 1.00 37.75 ? 202 SER C O   1 
ATOM   4864 C CB  . SER C 1 202 ? -10.591 -26.763 53.304 1.00 31.07 ? 202 SER C CB  1 
ATOM   4865 O OG  . SER C 1 202 ? -9.444  -26.343 54.030 1.00 39.38 ? 202 SER C OG  1 
ATOM   4866 N N   . SER C 1 203 ? -11.135 -23.845 54.308 1.00 24.59 ? 203 SER C N   1 
ATOM   4867 C CA  . SER C 1 203 ? -11.658 -22.871 55.250 1.00 32.55 ? 203 SER C CA  1 
ATOM   4868 C C   . SER C 1 203 ? -10.882 -21.563 55.033 1.00 31.46 ? 203 SER C C   1 
ATOM   4869 O O   . SER C 1 203 ? -9.779  -21.599 54.489 1.00 31.67 ? 203 SER C O   1 
ATOM   4870 C CB  . SER C 1 203 ? -11.493 -23.399 56.677 1.00 29.30 ? 203 SER C CB  1 
ATOM   4871 O OG  . SER C 1 203 ? -10.263 -22.973 57.235 1.00 40.07 ? 203 SER C OG  1 
ATOM   4872 N N   . PRO C 1 204 ? -11.444 -20.405 55.449 1.00 29.35 ? 204 PRO C N   1 
ATOM   4873 C CA  . PRO C 1 204 ? -10.798 -19.129 55.109 1.00 16.14 ? 204 PRO C CA  1 
ATOM   4874 C C   . PRO C 1 204 ? -9.414  -18.996 55.710 1.00 19.76 ? 204 PRO C C   1 
ATOM   4875 O O   . PRO C 1 204 ? -9.105  -19.658 56.698 1.00 35.77 ? 204 PRO C O   1 
ATOM   4876 C CB  . PRO C 1 204 ? -11.711 -18.084 55.746 1.00 20.81 ? 204 PRO C CB  1 
ATOM   4877 C CG  . PRO C 1 204 ? -12.983 -18.791 56.055 1.00 31.70 ? 204 PRO C CG  1 
ATOM   4878 C CD  . PRO C 1 204 ? -12.608 -20.205 56.330 1.00 29.22 ? 204 PRO C CD  1 
ATOM   4879 N N   . VAL C 1 205 ? -8.579  -18.161 55.113 1.00 25.61 ? 205 VAL C N   1 
ATOM   4880 C CA  . VAL C 1 205 ? -7.266  -17.902 55.674 1.00 20.66 ? 205 VAL C CA  1 
ATOM   4881 C C   . VAL C 1 205 ? -7.179  -16.455 56.123 1.00 22.53 ? 205 VAL C C   1 
ATOM   4882 O O   . VAL C 1 205 ? -7.619  -15.555 55.417 1.00 24.19 ? 205 VAL C O   1 
ATOM   4883 C CB  . VAL C 1 205 ? -6.157  -18.234 54.674 1.00 23.27 ? 205 VAL C CB  1 
ATOM   4884 C CG1 . VAL C 1 205 ? -4.830  -17.593 55.092 1.00 15.25 ? 205 VAL C CG1 1 
ATOM   4885 C CG2 . VAL C 1 205 ? -6.042  -19.729 54.536 1.00 19.49 ? 205 VAL C CG2 1 
ATOM   4886 N N   . THR C 1 206 ? -6.653  -16.242 57.322 1.00 20.68 ? 206 THR C N   1 
ATOM   4887 C CA  . THR C 1 206 ? -6.570  -14.908 57.875 1.00 20.10 ? 206 THR C CA  1 
ATOM   4888 C C   . THR C 1 206 ? -5.114  -14.553 58.181 1.00 26.10 ? 206 THR C C   1 
ATOM   4889 O O   . THR C 1 206 ? -4.352  -15.371 58.695 1.00 18.91 ? 206 THR C O   1 
ATOM   4890 C CB  . THR C 1 206 ? -7.468  -14.771 59.129 1.00 20.06 ? 206 THR C CB  1 
ATOM   4891 O OG1 . THR C 1 206 ? -8.814  -15.122 58.777 1.00 27.89 ? 206 THR C OG1 1 
ATOM   4892 C CG2 . THR C 1 206 ? -7.451  -13.345 59.665 1.00 12.15 ? 206 THR C CG2 1 
ATOM   4893 N N   . LYS C 1 207 ? -4.734  -13.334 57.831 1.00 21.73 ? 207 LYS C N   1 
ATOM   4894 C CA  . LYS C 1 207 ? -3.409  -12.849 58.120 1.00 15.55 ? 207 LYS C CA  1 
ATOM   4895 C C   . LYS C 1 207 ? -3.644  -11.523 58.800 1.00 17.61 ? 207 LYS C C   1 
ATOM   4896 O O   . LYS C 1 207 ? -4.521  -10.776 58.387 1.00 22.53 ? 207 LYS C O   1 
ATOM   4897 C CB  . LYS C 1 207 ? -2.642  -12.657 56.814 1.00 16.28 ? 207 LYS C CB  1 
ATOM   4898 C CG  . LYS C 1 207 ? -1.382  -13.493 56.688 1.00 26.38 ? 207 LYS C CG  1 
ATOM   4899 C CD  . LYS C 1 207 ? -1.646  -14.997 56.657 1.00 26.25 ? 207 LYS C CD  1 
ATOM   4900 C CE  . LYS C 1 207 ? -0.320  -15.768 56.697 1.00 29.13 ? 207 LYS C CE  1 
ATOM   4901 N NZ  . LYS C 1 207 ? -0.514  -17.242 56.805 1.00 24.62 ? 207 LYS C NZ  1 
ATOM   4902 N N   . SER C 1 208 ? -2.889  -11.218 59.843 1.00 19.23 ? 208 SER C N   1 
ATOM   4903 C CA  . SER C 1 208 ? -3.138  -10.000 60.603 1.00 18.86 ? 208 SER C CA  1 
ATOM   4904 C C   . SER C 1 208 ? -1.876  -9.379  61.198 1.00 19.86 ? 208 SER C C   1 
ATOM   4905 O O   . SER C 1 208 ? -0.821  -9.989  61.218 1.00 30.26 ? 208 SER C O   1 
ATOM   4906 C CB  . SER C 1 208 ? -4.154  -10.282 61.723 1.00 19.74 ? 208 SER C CB  1 
ATOM   4907 O OG  . SER C 1 208 ? -3.848  -11.491 62.374 1.00 31.03 ? 208 SER C OG  1 
ATOM   4908 N N   . PHE C 1 209 ? -1.988  -8.154  61.683 1.00 14.59 ? 209 PHE C N   1 
ATOM   4909 C CA  . PHE C 1 209 ? -0.926  -7.563  62.453 1.00 23.35 ? 209 PHE C CA  1 
ATOM   4910 C C   . PHE C 1 209 ? -1.596  -6.693  63.490 1.00 26.85 ? 209 PHE C C   1 
ATOM   4911 O O   . PHE C 1 209 ? -2.734  -6.270  63.275 1.00 29.94 ? 209 PHE C O   1 
ATOM   4912 C CB  . PHE C 1 209 ? 0.037   -6.763  61.566 1.00 24.33 ? 209 PHE C CB  1 
ATOM   4913 C CG  . PHE C 1 209 ? -0.563  -5.505  60.974 1.00 27.78 ? 209 PHE C CG  1 
ATOM   4914 C CD1 . PHE C 1 209 ? -1.133  -5.526  59.705 1.00 23.96 ? 209 PHE C CD1 1 
ATOM   4915 C CD2 . PHE C 1 209 ? -0.529  -4.302  61.672 1.00 24.84 ? 209 PHE C CD2 1 
ATOM   4916 C CE1 . PHE C 1 209 ? -1.669  -4.376  59.146 1.00 20.65 ? 209 PHE C CE1 1 
ATOM   4917 C CE2 . PHE C 1 209 ? -1.067  -3.143  61.119 1.00 22.98 ? 209 PHE C CE2 1 
ATOM   4918 C CZ  . PHE C 1 209 ? -1.637  -3.184  59.854 1.00 23.40 ? 209 PHE C CZ  1 
ATOM   4919 N N   . ASN C 1 210 ? -0.924  -6.473  64.620 1.00 25.98 ? 210 ASN C N   1 
ATOM   4920 C CA  . ASN C 1 210 ? -1.355  -5.485  65.597 1.00 21.92 ? 210 ASN C CA  1 
ATOM   4921 C C   . ASN C 1 210 ? -0.578  -4.201  65.369 1.00 31.55 ? 210 ASN C C   1 
ATOM   4922 O O   . ASN C 1 210 ? 0.650   -4.219  65.353 1.00 33.36 ? 210 ASN C O   1 
ATOM   4923 C CB  . ASN C 1 210 ? -1.113  -5.988  67.016 1.00 28.64 ? 210 ASN C CB  1 
ATOM   4924 C CG  . ASN C 1 210 ? -1.917  -7.221  67.335 1.00 33.97 ? 210 ASN C CG  1 
ATOM   4925 O OD1 . ASN C 1 210 ? -3.028  -7.404  66.830 1.00 34.24 ? 210 ASN C OD1 1 
ATOM   4926 N ND2 . ASN C 1 210 ? -1.361  -8.084  68.172 1.00 26.60 ? 210 ASN C ND2 1 
ATOM   4927 N N   . ARG C 1 211 ? -1.291  -3.095  65.176 1.00 24.76 ? 211 ARG C N   1 
ATOM   4928 C CA  . ARG C 1 211 ? -0.652  -1.799  65.018 1.00 26.83 ? 211 ARG C CA  1 
ATOM   4929 C C   . ARG C 1 211 ? 0.263   -1.547  66.206 1.00 33.19 ? 211 ARG C C   1 
ATOM   4930 O O   . ARG C 1 211 ? -0.165  -1.669  67.346 1.00 27.92 ? 211 ARG C O   1 
ATOM   4931 C CB  . ARG C 1 211 ? -1.699  -0.689  64.929 1.00 20.44 ? 211 ARG C CB  1 
ATOM   4932 C CG  . ARG C 1 211 ? -1.103  0.705   64.819 1.00 17.56 ? 211 ARG C CG  1 
ATOM   4933 C CD  . ARG C 1 211 ? -2.159  1.803   64.980 1.00 22.48 ? 211 ARG C CD  1 
ATOM   4934 N NE  . ARG C 1 211 ? -2.987  1.637   66.174 1.00 22.84 ? 211 ARG C NE  1 
ATOM   4935 C CZ  . ARG C 1 211 ? -2.579  1.877   67.419 1.00 26.20 ? 211 ARG C CZ  1 
ATOM   4936 N NH1 . ARG C 1 211 ? -1.343  2.295   67.653 1.00 24.93 ? 211 ARG C NH1 1 
ATOM   4937 N NH2 . ARG C 1 211 ? -3.414  1.697   68.432 1.00 24.85 ? 211 ARG C NH2 1 
ATOM   4938 N N   . GLY C 1 212 ? 1.523   -1.211  65.937 1.00 45.68 ? 212 GLY C N   1 
ATOM   4939 C CA  . GLY C 1 212 ? 2.466   -0.910  67.002 1.00 46.05 ? 212 GLY C CA  1 
ATOM   4940 C C   . GLY C 1 212 ? 3.273   -2.120  67.430 1.00 49.47 ? 212 GLY C C   1 
ATOM   4941 O O   . GLY C 1 212 ? 4.498   -2.054  67.520 1.00 60.21 ? 212 GLY C O   1 
ATOM   4942 N N   . ALA C 1 213 ? 2.586   -3.228  67.696 1.00 58.54 ? 213 ALA C N   1 
ATOM   4943 C CA  . ALA C 1 213 ? 3.247   -4.463  68.102 1.00 57.11 ? 213 ALA C CA  1 
ATOM   4944 C C   . ALA C 1 213 ? 4.259   -4.888  67.048 1.00 53.56 ? 213 ALA C C   1 
ATOM   4945 O O   . ALA C 1 213 ? 3.887   -5.308  65.955 1.00 55.55 ? 213 ALA C O   1 
ATOM   4946 C CB  . ALA C 1 213 ? 2.220   -5.572  68.353 1.00 46.41 ? 213 ALA C CB  1 
ATOM   4947 O OXT . ALA C 1 213 ? 5.470   -4.801  67.269 1.00 67.48 ? 213 ALA C OXT 1 
ATOM   4948 N N   . GLN D 2 1   ? 18.776  -4.364  13.018 1.00 43.14 ? 1   GLN D N   1 
ATOM   4949 C CA  . GLN D 2 1   ? 17.678  -4.260  13.975 1.00 45.87 ? 1   GLN D CA  1 
ATOM   4950 C C   . GLN D 2 1   ? 16.677  -3.156  13.600 1.00 40.57 ? 1   GLN D C   1 
ATOM   4951 O O   . GLN D 2 1   ? 16.931  -1.980  13.857 1.00 36.47 ? 1   GLN D O   1 
ATOM   4952 C CB  . GLN D 2 1   ? 18.234  -4.006  15.384 1.00 28.05 ? 1   GLN D CB  1 
ATOM   4953 N N   . VAL D 2 2   ? 15.546  -3.533  12.998 1.00 37.29 ? 2   VAL D N   1 
ATOM   4954 C CA  . VAL D 2 2   ? 14.463  -2.577  12.711 1.00 37.28 ? 2   VAL D CA  1 
ATOM   4955 C C   . VAL D 2 2   ? 13.683  -2.170  13.968 1.00 35.93 ? 2   VAL D C   1 
ATOM   4956 O O   . VAL D 2 2   ? 13.067  -3.017  14.607 1.00 39.27 ? 2   VAL D O   1 
ATOM   4957 C CB  . VAL D 2 2   ? 13.424  -3.154  11.722 1.00 31.27 ? 2   VAL D CB  1 
ATOM   4958 C CG1 . VAL D 2 2   ? 12.247  -2.188  11.575 1.00 27.27 ? 2   VAL D CG1 1 
ATOM   4959 C CG2 . VAL D 2 2   ? 14.050  -3.445  10.377 1.00 32.72 ? 2   VAL D CG2 1 
ATOM   4960 N N   . GLN D 2 3   ? 13.684  -0.884  14.314 1.00 31.26 ? 3   GLN D N   1 
ATOM   4961 C CA  . GLN D 2 3   ? 12.971  -0.429  15.508 1.00 33.52 ? 3   GLN D CA  1 
ATOM   4962 C C   . GLN D 2 3   ? 12.271  0.918   15.336 1.00 34.91 ? 3   GLN D C   1 
ATOM   4963 O O   . GLN D 2 3   ? 12.778  1.810   14.647 1.00 34.54 ? 3   GLN D O   1 
ATOM   4964 C CB  . GLN D 2 3   ? 13.909  -0.385  16.725 1.00 31.68 ? 3   GLN D CB  1 
ATOM   4965 C CG  . GLN D 2 3   ? 14.338  -1.765  17.224 1.00 46.39 ? 3   GLN D CG  1 
ATOM   4966 C CD  . GLN D 2 3   ? 15.174  -1.728  18.503 1.00 54.81 ? 3   GLN D CD  1 
ATOM   4967 O OE1 . GLN D 2 3   ? 15.684  -0.680  18.905 1.00 52.26 ? 3   GLN D OE1 1 
ATOM   4968 N NE2 . GLN D 2 3   ? 15.311  -2.884  19.149 1.00 62.05 ? 3   GLN D NE2 1 
ATOM   4969 N N   . LEU D 2 4   ? 11.102  1.052   15.966 1.00 31.36 ? 4   LEU D N   1 
ATOM   4970 C CA  . LEU D 2 4   ? 10.403  2.335   16.043 1.00 33.24 ? 4   LEU D CA  1 
ATOM   4971 C C   . LEU D 2 4   ? 10.242  2.702   17.507 1.00 27.00 ? 4   LEU D C   1 
ATOM   4972 O O   . LEU D 2 4   ? 9.749   1.902   18.288 1.00 27.82 ? 4   LEU D O   1 
ATOM   4973 C CB  . LEU D 2 4   ? 9.029   2.289   15.344 1.00 28.03 ? 4   LEU D CB  1 
ATOM   4974 C CG  . LEU D 2 4   ? 8.988   1.935   13.848 1.00 31.49 ? 4   LEU D CG  1 
ATOM   4975 C CD1 . LEU D 2 4   ? 9.001   0.430   13.657 1.00 29.40 ? 4   LEU D CD1 1 
ATOM   4976 C CD2 . LEU D 2 4   ? 7.792   2.565   13.106 1.00 24.93 ? 4   LEU D CD2 1 
ATOM   4977 N N   . LYS D 2 5   ? 10.670  3.905   17.878 1.00 31.41 ? 5   LYS D N   1 
ATOM   4978 C CA  . LYS D 2 5   ? 10.600  4.355   19.270 1.00 29.53 ? 5   LYS D CA  1 
ATOM   4979 C C   . LYS D 2 5   ? 9.853   5.677   19.371 1.00 28.42 ? 5   LYS D C   1 
ATOM   4980 O O   . LYS D 2 5   ? 10.191  6.658   18.695 1.00 28.57 ? 5   LYS D O   1 
ATOM   4981 C CB  . LYS D 2 5   ? 12.004  4.497   19.851 1.00 28.04 ? 5   LYS D CB  1 
ATOM   4982 C CG  . LYS D 2 5   ? 12.856  3.260   19.625 1.00 44.60 ? 5   LYS D CG  1 
ATOM   4983 C CD  . LYS D 2 5   ? 14.253  3.411   20.204 1.00 58.34 ? 5   LYS D CD  1 
ATOM   4984 C CE  . LYS D 2 5   ? 14.953  2.062   20.248 1.00 58.95 ? 5   LYS D CE  1 
ATOM   4985 N NZ  . LYS D 2 5   ? 14.099  1.030   20.918 1.00 54.61 ? 5   LYS D NZ  1 
ATOM   4986 N N   . GLN D 2 6   ? 8.834   5.709   20.219 1.00 24.02 ? 6   GLN D N   1 
ATOM   4987 C CA  . GLN D 2 6   ? 7.938   6.862   20.250 1.00 23.41 ? 6   GLN D CA  1 
ATOM   4988 C C   . GLN D 2 6   ? 8.261   7.778   21.424 1.00 24.62 ? 6   GLN D C   1 
ATOM   4989 O O   . GLN D 2 6   ? 8.956   7.384   22.351 1.00 23.17 ? 6   GLN D O   1 
ATOM   4990 C CB  . GLN D 2 6   ? 6.483   6.394   20.303 1.00 21.73 ? 6   GLN D CB  1 
ATOM   4991 C CG  . GLN D 2 6   ? 6.241   5.109   19.522 1.00 27.17 ? 6   GLN D CG  1 
ATOM   4992 C CD  . GLN D 2 6   ? 4.774   4.780   19.385 1.00 27.37 ? 6   GLN D CD  1 
ATOM   4993 O OE1 . GLN D 2 6   ? 4.400   3.713   18.883 1.00 24.77 ? 6   GLN D OE1 1 
ATOM   4994 N NE2 . GLN D 2 6   ? 3.927   5.698   19.833 1.00 26.36 ? 6   GLN D NE2 1 
ATOM   4995 N N   . SER D 2 7   ? 7.778   9.012   21.379 1.00 24.67 ? 7   SER D N   1 
ATOM   4996 C CA  . SER D 2 7   ? 7.973   9.910   22.508 1.00 25.80 ? 7   SER D CA  1 
ATOM   4997 C C   . SER D 2 7   ? 7.088   9.476   23.690 1.00 37.47 ? 7   SER D C   1 
ATOM   4998 O O   . SER D 2 7   ? 6.136   8.702   23.518 1.00 28.78 ? 7   SER D O   1 
ATOM   4999 C CB  . SER D 2 7   ? 7.704   11.354  22.103 1.00 22.53 ? 7   SER D CB  1 
ATOM   5000 O OG  . SER D 2 7   ? 6.601   11.410  21.233 1.00 29.01 ? 7   SER D OG  1 
ATOM   5001 N N   . GLY D 2 8   ? 7.412   9.974   24.882 1.00 30.16 ? 8   GLY D N   1 
ATOM   5002 C CA  . GLY D 2 8   ? 6.776   9.526   26.112 1.00 28.87 ? 8   GLY D CA  1 
ATOM   5003 C C   . GLY D 2 8   ? 5.283   9.788   26.256 1.00 30.70 ? 8   GLY D C   1 
ATOM   5004 O O   . GLY D 2 8   ? 4.709   10.610  25.535 1.00 25.30 ? 8   GLY D O   1 
ATOM   5005 N N   . PRO D 2 9   ? 4.646   9.095   27.216 1.00 27.61 ? 9   PRO D N   1 
ATOM   5006 C CA  . PRO D 2 9   ? 3.220   9.255   27.490 1.00 25.26 ? 9   PRO D CA  1 
ATOM   5007 C C   . PRO D 2 9   ? 2.951   10.593  28.174 1.00 32.83 ? 9   PRO D C   1 
ATOM   5008 O O   . PRO D 2 9   ? 3.865   11.246  28.689 1.00 24.15 ? 9   PRO D O   1 
ATOM   5009 C CB  . PRO D 2 9   ? 2.945   8.126   28.473 1.00 21.97 ? 9   PRO D CB  1 
ATOM   5010 C CG  . PRO D 2 9   ? 4.198   8.033   29.245 1.00 18.64 ? 9   PRO D CG  1 
ATOM   5011 C CD  . PRO D 2 9   ? 5.289   8.233   28.221 1.00 25.16 ? 9   PRO D CD  1 
ATOM   5012 N N   . GLY D 2 10  ? 1.690   11.002  28.188 1.00 28.36 ? 10  GLY D N   1 
ATOM   5013 C CA  . GLY D 2 10  ? 1.354   12.235  28.848 1.00 23.38 ? 10  GLY D CA  1 
ATOM   5014 C C   . GLY D 2 10  ? -0.076  12.672  28.706 1.00 24.36 ? 10  GLY D C   1 
ATOM   5015 O O   . GLY D 2 10  ? -0.863  12.101  27.950 1.00 29.61 ? 10  GLY D O   1 
ATOM   5016 N N   . LEU D 2 11  ? -0.382  13.720  29.450 1.00 25.61 ? 11  LEU D N   1 
ATOM   5017 C CA  . LEU D 2 11  ? -1.701  14.307  29.534 1.00 27.94 ? 11  LEU D CA  1 
ATOM   5018 C C   . LEU D 2 11  ? -1.868  15.368  28.439 1.00 28.95 ? 11  LEU D C   1 
ATOM   5019 O O   . LEU D 2 11  ? -0.918  16.073  28.110 1.00 32.75 ? 11  LEU D O   1 
ATOM   5020 C CB  . LEU D 2 11  ? -1.837  14.937  30.925 1.00 15.86 ? 11  LEU D CB  1 
ATOM   5021 C CG  . LEU D 2 11  ? -3.188  15.482  31.358 1.00 25.56 ? 11  LEU D CG  1 
ATOM   5022 C CD1 . LEU D 2 11  ? -4.229  14.386  31.358 1.00 27.69 ? 11  LEU D CD1 1 
ATOM   5023 C CD2 . LEU D 2 11  ? -3.030  16.066  32.729 1.00 30.16 ? 11  LEU D CD2 1 
ATOM   5024 N N   . VAL D 2 12  ? -3.060  15.462  27.860 1.00 26.69 ? 12  VAL D N   1 
ATOM   5025 C CA  . VAL D 2 12  ? -3.391  16.557  26.942 1.00 29.47 ? 12  VAL D CA  1 
ATOM   5026 C C   . VAL D 2 12  ? -4.757  17.142  27.316 1.00 34.83 ? 12  VAL D C   1 
ATOM   5027 O O   . VAL D 2 12  ? -5.719  16.407  27.545 1.00 35.43 ? 12  VAL D O   1 
ATOM   5028 C CB  . VAL D 2 12  ? -3.386  16.091  25.454 1.00 33.17 ? 12  VAL D CB  1 
ATOM   5029 C CG1 . VAL D 2 12  ? -4.239  14.857  25.279 1.00 46.44 ? 12  VAL D CG1 1 
ATOM   5030 C CG2 . VAL D 2 12  ? -3.868  17.197  24.522 1.00 35.13 ? 12  VAL D CG2 1 
ATOM   5031 N N   . GLN D 2 13  ? -4.836  18.463  27.412 1.00 35.55 ? 13  GLN D N   1 
ATOM   5032 C CA  . GLN D 2 13  ? -6.077  19.121  27.810 1.00 37.20 ? 13  GLN D CA  1 
ATOM   5033 C C   . GLN D 2 13  ? -7.140  18.991  26.724 1.00 37.20 ? 13  GLN D C   1 
ATOM   5034 O O   . GLN D 2 13  ? -6.817  19.029  25.541 1.00 36.89 ? 13  GLN D O   1 
ATOM   5035 C CB  . GLN D 2 13  ? -5.810  20.596  28.114 1.00 36.04 ? 13  GLN D CB  1 
ATOM   5036 C CG  . GLN D 2 13  ? -4.785  20.813  29.214 1.00 40.78 ? 13  GLN D CG  1 
ATOM   5037 C CD  . GLN D 2 13  ? -5.248  20.246  30.552 1.00 52.71 ? 13  GLN D CD  1 
ATOM   5038 O OE1 . GLN D 2 13  ? -6.415  20.393  30.919 1.00 56.43 ? 13  GLN D OE1 1 
ATOM   5039 N NE2 . GLN D 2 13  ? -4.338  19.586  31.282 1.00 40.03 ? 13  GLN D NE2 1 
ATOM   5040 N N   . PRO D 2 14  ? -8.411  18.820  27.126 1.00 35.76 ? 14  PRO D N   1 
ATOM   5041 C CA  . PRO D 2 14  ? -9.510  18.796  26.159 1.00 35.07 ? 14  PRO D CA  1 
ATOM   5042 C C   . PRO D 2 14  ? -9.429  19.981  25.202 1.00 43.31 ? 14  PRO D C   1 
ATOM   5043 O O   . PRO D 2 14  ? -9.118  21.102  25.623 1.00 40.48 ? 14  PRO D O   1 
ATOM   5044 C CB  . PRO D 2 14  ? -10.748 18.897  27.046 1.00 36.79 ? 14  PRO D CB  1 
ATOM   5045 C CG  . PRO D 2 14  ? -10.338 18.240  28.322 1.00 32.00 ? 14  PRO D CG  1 
ATOM   5046 C CD  . PRO D 2 14  ? -8.888  18.607  28.505 1.00 41.06 ? 14  PRO D CD  1 
ATOM   5047 N N   . SER D 2 15  ? -9.676  19.700  23.925 1.00 37.38 ? 15  SER D N   1 
ATOM   5048 C CA  . SER D 2 15  ? -9.555  20.664  22.826 1.00 41.47 ? 15  SER D CA  1 
ATOM   5049 C C   . SER D 2 15  ? -8.121  21.002  22.379 1.00 36.52 ? 15  SER D C   1 
ATOM   5050 O O   . SER D 2 15  ? -7.947  21.564  21.305 1.00 45.34 ? 15  SER D O   1 
ATOM   5051 C CB  . SER D 2 15  ? -10.364 21.944  23.093 1.00 38.95 ? 15  SER D CB  1 
ATOM   5052 O OG  . SER D 2 15  ? -11.729 21.636  23.319 1.00 52.37 ? 15  SER D OG  1 
ATOM   5053 N N   . GLN D 2 16  ? -7.105  20.672  23.175 1.00 32.71 ? 16  GLN D N   1 
ATOM   5054 C CA  . GLN D 2 16  ? -5.717  20.882  22.727 1.00 38.88 ? 16  GLN D CA  1 
ATOM   5055 C C   . GLN D 2 16  ? -5.268  19.787  21.756 1.00 39.97 ? 16  GLN D C   1 
ATOM   5056 O O   . GLN D 2 16  ? -6.012  18.839  21.487 1.00 42.80 ? 16  GLN D O   1 
ATOM   5057 C CB  . GLN D 2 16  ? -4.726  20.960  23.895 1.00 42.23 ? 16  GLN D CB  1 
ATOM   5058 C CG  . GLN D 2 16  ? -5.065  21.967  24.970 1.00 44.39 ? 16  GLN D CG  1 
ATOM   5059 C CD  . GLN D 2 16  ? -5.391  23.332  24.417 1.00 54.84 ? 16  GLN D CD  1 
ATOM   5060 O OE1 . GLN D 2 16  ? -4.495  24.134  24.157 1.00 60.84 ? 16  GLN D OE1 1 
ATOM   5061 N NE2 . GLN D 2 16  ? -6.682  23.612  24.243 1.00 53.86 ? 16  GLN D NE2 1 
ATOM   5062 N N   . SER D 2 17  ? -4.046  19.914  21.245 1.00 38.84 ? 17  SER D N   1 
ATOM   5063 C CA  . SER D 2 17  ? -3.546  18.994  20.226 1.00 37.30 ? 17  SER D CA  1 
ATOM   5064 C C   . SER D 2 17  ? -2.638  17.931  20.826 1.00 36.01 ? 17  SER D C   1 
ATOM   5065 O O   . SER D 2 17  ? -2.127  18.094  21.925 1.00 35.18 ? 17  SER D O   1 
ATOM   5066 C CB  . SER D 2 17  ? -2.762  19.756  19.168 1.00 33.06 ? 17  SER D CB  1 
ATOM   5067 O OG  . SER D 2 17  ? -1.575  20.265  19.745 1.00 36.61 ? 17  SER D OG  1 
ATOM   5068 N N   . LEU D 2 18  ? -2.422  16.855  20.081 1.00 31.59 ? 18  LEU D N   1 
ATOM   5069 C CA  . LEU D 2 18  ? -1.587  15.764  20.542 1.00 24.52 ? 18  LEU D CA  1 
ATOM   5070 C C   . LEU D 2 18  ? -0.422  15.607  19.582 1.00 31.10 ? 18  LEU D C   1 
ATOM   5071 O O   . LEU D 2 18  ? -0.620  15.535  18.376 1.00 34.93 ? 18  LEU D O   1 
ATOM   5072 C CB  . LEU D 2 18  ? -2.407  14.483  20.596 1.00 21.95 ? 18  LEU D CB  1 
ATOM   5073 C CG  . LEU D 2 18  ? -1.719  13.132  20.478 1.00 25.51 ? 18  LEU D CG  1 
ATOM   5074 C CD1 . LEU D 2 18  ? -0.675  12.937  21.557 1.00 26.47 ? 18  LEU D CD1 1 
ATOM   5075 C CD2 . LEU D 2 18  ? -2.785  12.039  20.549 1.00 27.70 ? 18  LEU D CD2 1 
ATOM   5076 N N   . SER D 2 19  ? 0.794   15.556  20.115 1.00 27.59 ? 19  SER D N   1 
ATOM   5077 C CA  . SER D 2 19  ? 1.976   15.432  19.278 1.00 25.95 ? 19  SER D CA  1 
ATOM   5078 C C   . SER D 2 19  ? 2.858   14.277  19.694 1.00 21.50 ? 19  SER D C   1 
ATOM   5079 O O   . SER D 2 19  ? 3.425   14.279  20.777 1.00 22.78 ? 19  SER D O   1 
ATOM   5080 C CB  . SER D 2 19  ? 2.785   16.725  19.293 1.00 29.15 ? 19  SER D CB  1 
ATOM   5081 O OG  . SER D 2 19  ? 2.165   17.702  18.483 1.00 38.24 ? 19  SER D OG  1 
ATOM   5082 N N   . ILE D 2 20  ? 2.977   13.289  18.816 1.00 26.15 ? 20  ILE D N   1 
ATOM   5083 C CA  . ILE D 2 20  ? 3.866   12.165  19.064 1.00 24.66 ? 20  ILE D CA  1 
ATOM   5084 C C   . ILE D 2 20  ? 4.957   12.104  18.009 1.00 24.46 ? 20  ILE D C   1 
ATOM   5085 O O   . ILE D 2 20  ? 4.696   12.326  16.830 1.00 25.27 ? 20  ILE D O   1 
ATOM   5086 C CB  . ILE D 2 20  ? 3.100   10.850  19.091 1.00 19.08 ? 20  ILE D CB  1 
ATOM   5087 C CG1 . ILE D 2 20  ? 1.963   10.943  20.110 1.00 18.29 ? 20  ILE D CG1 1 
ATOM   5088 C CG2 . ILE D 2 20  ? 4.041   9.696   19.422 1.00 17.29 ? 20  ILE D CG2 1 
ATOM   5089 C CD1 . ILE D 2 20  ? 0.950   9.838   19.984 1.00 20.76 ? 20  ILE D CD1 1 
ATOM   5090 N N   . THR D 2 21  ? 6.184   11.833  18.444 1.00 24.04 ? 21  THR D N   1 
ATOM   5091 C CA  . THR D 2 21  ? 7.291   11.608  17.528 1.00 20.66 ? 21  THR D CA  1 
ATOM   5092 C C   . THR D 2 21  ? 7.668   10.136  17.439 1.00 24.47 ? 21  THR D C   1 
ATOM   5093 O O   . THR D 2 21  ? 7.937   9.499   18.460 1.00 22.07 ? 21  THR D O   1 
ATOM   5094 C CB  . THR D 2 21  ? 8.526   12.394  17.964 1.00 21.55 ? 21  THR D CB  1 
ATOM   5095 O OG1 . THR D 2 21  ? 8.251   13.793  17.840 1.00 27.41 ? 21  THR D OG1 1 
ATOM   5096 C CG2 . THR D 2 21  ? 9.734   12.029  17.089 1.00 26.19 ? 21  THR D CG2 1 
ATOM   5097 N N   . CYS D 2 22  ? 7.696   9.607   16.214 1.00 26.80 ? 22  CYS D N   1 
ATOM   5098 C CA  . CYS D 2 22  ? 8.216   8.265   15.955 1.00 21.30 ? 22  CYS D CA  1 
ATOM   5099 C C   . CYS D 2 22  ? 9.601   8.347   15.336 1.00 26.99 ? 22  CYS D C   1 
ATOM   5100 O O   . CYS D 2 22  ? 9.795   9.001   14.315 1.00 31.03 ? 22  CYS D O   1 
ATOM   5101 C CB  . CYS D 2 22  ? 7.286   7.484   15.030 1.00 17.42 ? 22  CYS D CB  1 
ATOM   5102 S SG  . CYS D 2 22  ? 7.764   5.746   14.736 1.00 24.68 ? 22  CYS D SG  1 
ATOM   5103 N N   . THR D 2 23  ? 10.556  7.663   15.954 1.00 24.40 ? 23  THR D N   1 
ATOM   5104 C CA  . THR D 2 23  ? 11.952  7.707   15.540 1.00 21.68 ? 23  THR D CA  1 
ATOM   5105 C C   . THR D 2 23  ? 12.405  6.312   15.112 1.00 31.92 ? 23  THR D C   1 
ATOM   5106 O O   . THR D 2 23  ? 12.514  5.406   15.939 1.00 35.45 ? 23  THR D O   1 
ATOM   5107 C CB  . THR D 2 23  ? 12.854  8.168   16.706 1.00 26.19 ? 23  THR D CB  1 
ATOM   5108 O OG1 . THR D 2 23  ? 12.439  9.465   17.163 1.00 34.23 ? 23  THR D OG1 1 
ATOM   5109 C CG2 . THR D 2 23  ? 14.317  8.198   16.280 1.00 15.12 ? 23  THR D CG2 1 
ATOM   5110 N N   . VAL D 2 24  ? 12.678  6.130   13.828 1.00 30.13 ? 24  VAL D N   1 
ATOM   5111 C CA  . VAL D 2 24  ? 13.003  4.797   13.335 1.00 33.66 ? 24  VAL D CA  1 
ATOM   5112 C C   . VAL D 2 24  ? 14.498  4.570   13.151 1.00 28.47 ? 24  VAL D C   1 
ATOM   5113 O O   . VAL D 2 24  ? 15.278  5.515   13.031 1.00 26.97 ? 24  VAL D O   1 
ATOM   5114 C CB  . VAL D 2 24  ? 12.300  4.497   11.990 1.00 34.04 ? 24  VAL D CB  1 
ATOM   5115 C CG1 . VAL D 2 24  ? 10.825  4.885   12.064 1.00 26.56 ? 24  VAL D CG1 1 
ATOM   5116 C CG2 . VAL D 2 24  ? 13.010  5.201   10.836 1.00 20.76 ? 24  VAL D CG2 1 
ATOM   5117 N N   . SER D 2 25  ? 14.878  3.300   13.114 1.00 25.94 ? 25  SER D N   1 
ATOM   5118 C CA  . SER D 2 25  ? 16.250  2.888   12.843 1.00 24.19 ? 25  SER D CA  1 
ATOM   5119 C C   . SER D 2 25  ? 16.233  1.477   12.258 1.00 31.78 ? 25  SER D C   1 
ATOM   5120 O O   . SER D 2 25  ? 15.363  0.671   12.599 1.00 37.37 ? 25  SER D O   1 
ATOM   5121 C CB  . SER D 2 25  ? 17.069  2.911   14.131 1.00 26.29 ? 25  SER D CB  1 
ATOM   5122 O OG  . SER D 2 25  ? 16.501  2.037   15.087 1.00 33.83 ? 25  SER D OG  1 
ATOM   5123 N N   . GLY D 2 26  ? 17.184  1.171   11.381 1.00 30.63 ? 26  GLY D N   1 
ATOM   5124 C CA  . GLY D 2 26  ? 17.238  -0.142  10.762 1.00 21.76 ? 26  GLY D CA  1 
ATOM   5125 C C   . GLY D 2 26  ? 16.605  -0.156  9.383  1.00 25.40 ? 26  GLY D C   1 
ATOM   5126 O O   . GLY D 2 26  ? 16.500  -1.213  8.753  1.00 23.62 ? 26  GLY D O   1 
ATOM   5127 N N   . PHE D 2 27  ? 16.178  1.021   8.927  1.00 21.14 ? 27  PHE D N   1 
ATOM   5128 C CA  . PHE D 2 27  ? 15.583  1.207   7.600  1.00 21.76 ? 27  PHE D CA  1 
ATOM   5129 C C   . PHE D 2 27  ? 15.380  2.697   7.397  1.00 25.51 ? 27  PHE D C   1 
ATOM   5130 O O   . PHE D 2 27  ? 15.347  3.463   8.358  1.00 30.42 ? 27  PHE D O   1 
ATOM   5131 C CB  . PHE D 2 27  ? 14.226  0.492   7.461  1.00 21.35 ? 27  PHE D CB  1 
ATOM   5132 C CG  . PHE D 2 27  ? 13.079  1.207   8.153  1.00 20.96 ? 27  PHE D CG  1 
ATOM   5133 C CD1 . PHE D 2 27  ? 12.800  0.972   9.492  1.00 21.75 ? 27  PHE D CD1 1 
ATOM   5134 C CD2 . PHE D 2 27  ? 12.281  2.108   7.459  1.00 26.87 ? 27  PHE D CD2 1 
ATOM   5135 C CE1 . PHE D 2 27  ? 11.754  1.617   10.129 1.00 20.82 ? 27  PHE D CE1 1 
ATOM   5136 C CE2 . PHE D 2 27  ? 11.227  2.763   8.092  1.00 28.77 ? 27  PHE D CE2 1 
ATOM   5137 C CZ  . PHE D 2 27  ? 10.964  2.509   9.434  1.00 27.09 ? 27  PHE D CZ  1 
ATOM   5138 N N   . SER D 2 28  ? 15.213  3.109   6.150  1.00 27.60 ? 28  SER D N   1 
ATOM   5139 C CA  . SER D 2 28  ? 15.065  4.523   5.841  1.00 30.12 ? 28  SER D CA  1 
ATOM   5140 C C   . SER D 2 28  ? 13.606  4.927   5.585  1.00 34.79 ? 28  SER D C   1 
ATOM   5141 O O   . SER D 2 28  ? 12.808  4.154   5.048  1.00 29.19 ? 28  SER D O   1 
ATOM   5142 C CB  . SER D 2 28  ? 15.951  4.890   4.650  1.00 29.12 ? 28  SER D CB  1 
ATOM   5143 O OG  . SER D 2 28  ? 15.643  6.184   4.162  1.00 38.73 ? 28  SER D OG  1 
ATOM   5144 N N   . LEU D 2 29  ? 13.264  6.149   5.973  1.00 32.43 ? 29  LEU D N   1 
ATOM   5145 C CA  . LEU D 2 29  ? 11.918  6.645   5.763  1.00 26.73 ? 29  LEU D CA  1 
ATOM   5146 C C   . LEU D 2 29  ? 11.684  6.859   4.281  1.00 33.87 ? 29  LEU D C   1 
ATOM   5147 O O   . LEU D 2 29  ? 10.541  6.926   3.830  1.00 38.33 ? 29  LEU D O   1 
ATOM   5148 C CB  . LEU D 2 29  ? 11.681  7.931   6.554  1.00 27.88 ? 29  LEU D CB  1 
ATOM   5149 C CG  . LEU D 2 29  ? 11.693  7.719   8.069  1.00 25.03 ? 29  LEU D CG  1 
ATOM   5150 C CD1 . LEU D 2 29  ? 11.522  9.035   8.797  1.00 25.09 ? 29  LEU D CD1 1 
ATOM   5151 C CD2 . LEU D 2 29  ? 10.607  6.730   8.467  1.00 18.61 ? 29  LEU D CD2 1 
ATOM   5152 N N   . THR D 2 30  ? 12.772  6.945   3.518  1.00 33.97 ? 30  THR D N   1 
ATOM   5153 C CA  . THR D 2 30  ? 12.674  7.072   2.064  1.00 37.28 ? 30  THR D CA  1 
ATOM   5154 C C   . THR D 2 30  ? 12.324  5.746   1.392  1.00 31.67 ? 30  THR D C   1 
ATOM   5155 O O   . THR D 2 30  ? 11.996  5.732   0.215  1.00 29.83 ? 30  THR D O   1 
ATOM   5156 C CB  . THR D 2 30  ? 13.973  7.619   1.427  1.00 26.86 ? 30  THR D CB  1 
ATOM   5157 O OG1 . THR D 2 30  ? 15.026  6.666   1.607  1.00 35.59 ? 30  THR D OG1 1 
ATOM   5158 C CG2 . THR D 2 30  ? 14.374  8.935   2.054  1.00 29.98 ? 30  THR D CG2 1 
ATOM   5159 N N   . ASN D 2 31  ? 12.407  4.640   2.133  1.00 28.67 ? 31  ASN D N   1 
ATOM   5160 C CA  . ASN D 2 31  ? 12.081  3.317   1.590  1.00 26.20 ? 31  ASN D CA  1 
ATOM   5161 C C   . ASN D 2 31  ? 10.775  2.688   2.096  1.00 32.13 ? 31  ASN D C   1 
ATOM   5162 O O   . ASN D 2 31  ? 10.238  1.798   1.456  1.00 31.90 ? 31  ASN D O   1 
ATOM   5163 C CB  . ASN D 2 31  ? 13.224  2.335   1.832  1.00 28.89 ? 31  ASN D CB  1 
ATOM   5164 C CG  . ASN D 2 31  ? 14.451  2.661   1.024  1.00 30.44 ? 31  ASN D CG  1 
ATOM   5165 O OD1 . ASN D 2 31  ? 14.355  3.256   -0.039 1.00 33.10 ? 31  ASN D OD1 1 
ATOM   5166 N ND2 . ASN D 2 31  ? 15.620  2.274   1.527  1.00 29.71 ? 31  ASN D ND2 1 
ATOM   5167 N N   . TYR D 2 32  ? 10.277  3.124   3.250  1.00 35.29 ? 32  TYR D N   1 
ATOM   5168 C CA  . TYR D 2 32  ? 9.050   2.544   3.816  1.00 28.90 ? 32  TYR D CA  1 
ATOM   5169 C C   . TYR D 2 32  ? 8.077   3.600   4.331  1.00 23.12 ? 32  TYR D C   1 
ATOM   5170 O O   . TYR D 2 32  ? 8.488   4.631   4.850  1.00 28.53 ? 32  TYR D O   1 
ATOM   5171 C CB  . TYR D 2 32  ? 9.390   1.589   4.950  1.00 25.35 ? 32  TYR D CB  1 
ATOM   5172 C CG  . TYR D 2 32  ? 10.108  0.324   4.537  1.00 27.91 ? 32  TYR D CG  1 
ATOM   5173 C CD1 . TYR D 2 32  ? 9.406   -0.865  4.345  1.00 21.32 ? 32  TYR D CD1 1 
ATOM   5174 C CD2 . TYR D 2 32  ? 11.489  0.311   4.358  1.00 23.55 ? 32  TYR D CD2 1 
ATOM   5175 C CE1 . TYR D 2 32  ? 10.058  -2.025  3.982  1.00 24.65 ? 32  TYR D CE1 1 
ATOM   5176 C CE2 . TYR D 2 32  ? 12.150  -0.846  3.990  1.00 23.77 ? 32  TYR D CE2 1 
ATOM   5177 C CZ  . TYR D 2 32  ? 11.428  -2.014  3.809  1.00 23.22 ? 32  TYR D CZ  1 
ATOM   5178 O OH  . TYR D 2 32  ? 12.069  -3.171  3.449  1.00 27.47 ? 32  TYR D OH  1 
ATOM   5179 N N   . GLY D 2 33  ? 6.786   3.355   4.158  1.00 21.81 ? 33  GLY D N   1 
ATOM   5180 C CA  . GLY D 2 33  ? 5.787   4.202   4.776  1.00 24.17 ? 33  GLY D CA  1 
ATOM   5181 C C   . GLY D 2 33  ? 5.738   3.935   6.274  1.00 24.09 ? 33  GLY D C   1 
ATOM   5182 O O   . GLY D 2 33  ? 6.095   2.846   6.733  1.00 24.50 ? 33  GLY D O   1 
ATOM   5183 N N   . VAL D 2 34  ? 5.303   4.925   7.042  1.00 23.12 ? 34  VAL D N   1 
ATOM   5184 C CA  . VAL D 2 34  ? 5.075   4.724   8.475  1.00 19.28 ? 34  VAL D CA  1 
ATOM   5185 C C   . VAL D 2 34  ? 3.615   4.998   8.798  1.00 18.82 ? 34  VAL D C   1 
ATOM   5186 O O   . VAL D 2 34  ? 3.083   6.054   8.472  1.00 23.10 ? 34  VAL D O   1 
ATOM   5187 C CB  . VAL D 2 34  ? 6.021   5.588   9.339  1.00 23.33 ? 34  VAL D CB  1 
ATOM   5188 C CG1 . VAL D 2 34  ? 5.509   5.704   10.784 1.00 20.74 ? 34  VAL D CG1 1 
ATOM   5189 C CG2 . VAL D 2 34  ? 7.435   5.016   9.301  1.00 18.40 ? 34  VAL D CG2 1 
ATOM   5190 N N   . HIS D 2 35  ? 2.962   4.029   9.424  1.00 28.35 ? 35  HIS D N   1 
ATOM   5191 C CA  . HIS D 2 35  ? 1.539   4.137   9.712  1.00 24.96 ? 35  HIS D CA  1 
ATOM   5192 C C   . HIS D 2 35  ? 1.315   4.508   11.159 1.00 26.68 ? 35  HIS D C   1 
ATOM   5193 O O   . HIS D 2 35  ? 2.224   4.385   11.982 1.00 23.13 ? 35  HIS D O   1 
ATOM   5194 C CB  . HIS D 2 35  ? 0.855   2.806   9.441  1.00 23.93 ? 35  HIS D CB  1 
ATOM   5195 C CG  . HIS D 2 35  ? 0.960   2.349   8.022  1.00 24.80 ? 35  HIS D CG  1 
ATOM   5196 N ND1 . HIS D 2 35  ? -0.143  2.129   7.227  1.00 26.73 ? 35  HIS D ND1 1 
ATOM   5197 C CD2 . HIS D 2 35  ? 2.040   2.064   7.256  1.00 18.94 ? 35  HIS D CD2 1 
ATOM   5198 C CE1 . HIS D 2 35  ? 0.251   1.724   6.032  1.00 31.95 ? 35  HIS D CE1 1 
ATOM   5199 N NE2 . HIS D 2 35  ? 1.572   1.673   6.026  1.00 27.51 ? 35  HIS D NE2 1 
ATOM   5200 N N   . TRP D 2 36  ? 0.098   4.955   11.467 1.00 24.38 ? 36  TRP D N   1 
ATOM   5201 C CA  . TRP D 2 36  ? -0.289  5.206   12.848 1.00 19.43 ? 36  TRP D CA  1 
ATOM   5202 C C   . TRP D 2 36  ? -1.596  4.502   13.182 1.00 27.60 ? 36  TRP D C   1 
ATOM   5203 O O   . TRP D 2 36  ? -2.595  4.628   12.474 1.00 27.11 ? 36  TRP D O   1 
ATOM   5204 C CB  . TRP D 2 36  ? -0.371  6.706   13.149 1.00 22.33 ? 36  TRP D CB  1 
ATOM   5205 C CG  . TRP D 2 36  ? 0.974   7.364   13.025 1.00 28.12 ? 36  TRP D CG  1 
ATOM   5206 C CD1 . TRP D 2 36  ? 1.607   7.711   11.866 1.00 24.03 ? 36  TRP D CD1 1 
ATOM   5207 C CD2 . TRP D 2 36  ? 1.870   7.721   14.091 1.00 25.42 ? 36  TRP D CD2 1 
ATOM   5208 N NE1 . TRP D 2 36  ? 2.830   8.269   12.140 1.00 23.97 ? 36  TRP D NE1 1 
ATOM   5209 C CE2 . TRP D 2 36  ? 3.017   8.288   13.499 1.00 21.15 ? 36  TRP D CE2 1 
ATOM   5210 C CE3 . TRP D 2 36  ? 1.810   7.624   15.485 1.00 23.24 ? 36  TRP D CE3 1 
ATOM   5211 C CZ2 . TRP D 2 36  ? 4.092   8.752   14.249 1.00 19.85 ? 36  TRP D CZ2 1 
ATOM   5212 C CZ3 . TRP D 2 36  ? 2.883   8.084   16.230 1.00 23.72 ? 36  TRP D CZ3 1 
ATOM   5213 C CH2 . TRP D 2 36  ? 4.004   8.646   15.612 1.00 24.17 ? 36  TRP D CH2 1 
ATOM   5214 N N   . VAL D 2 37  ? -1.561  3.743   14.269 1.00 28.34 ? 37  VAL D N   1 
ATOM   5215 C CA  . VAL D 2 37  ? -2.700  3.002   14.756 1.00 27.30 ? 37  VAL D CA  1 
ATOM   5216 C C   . VAL D 2 37  ? -2.901  3.371   16.225 1.00 25.09 ? 37  VAL D C   1 
ATOM   5217 O O   . VAL D 2 37  ? -1.935  3.595   16.952 1.00 28.92 ? 37  VAL D O   1 
ATOM   5218 C CB  . VAL D 2 37  ? -2.442  1.486   14.606 1.00 22.83 ? 37  VAL D CB  1 
ATOM   5219 C CG1 . VAL D 2 37  ? -3.530  0.651   15.306 1.00 18.51 ? 37  VAL D CG1 1 
ATOM   5220 C CG2 . VAL D 2 37  ? -2.326  1.125   13.128 1.00 18.67 ? 37  VAL D CG2 1 
ATOM   5221 N N   . ARG D 2 38  ? -4.151  3.454   16.663 1.00 18.58 ? 38  ARG D N   1 
ATOM   5222 C CA  . ARG D 2 38  ? -4.423  3.659   18.072 1.00 21.49 ? 38  ARG D CA  1 
ATOM   5223 C C   . ARG D 2 38  ? -5.306  2.554   18.628 1.00 24.71 ? 38  ARG D C   1 
ATOM   5224 O O   . ARG D 2 38  ? -6.045  1.904   17.889 1.00 34.69 ? 38  ARG D O   1 
ATOM   5225 C CB  . ARG D 2 38  ? -5.033  5.037   18.322 1.00 22.53 ? 38  ARG D CB  1 
ATOM   5226 C CG  . ARG D 2 38  ? -6.492  5.163   17.939 1.00 22.42 ? 38  ARG D CG  1 
ATOM   5227 C CD  . ARG D 2 38  ? -6.993  6.560   18.235 1.00 18.14 ? 38  ARG D CD  1 
ATOM   5228 N NE  . ARG D 2 38  ? -8.413  6.698   17.962 1.00 26.11 ? 38  ARG D NE  1 
ATOM   5229 C CZ  . ARG D 2 38  ? -9.097  7.818   18.139 1.00 22.79 ? 38  ARG D CZ  1 
ATOM   5230 N NH1 . ARG D 2 38  ? -8.488  8.903   18.582 1.00 19.17 ? 38  ARG D NH1 1 
ATOM   5231 N NH2 . ARG D 2 38  ? -10.388 7.845   17.862 1.00 30.09 ? 38  ARG D NH2 1 
ATOM   5232 N N   . GLN D 2 39  ? -5.212  2.333   19.934 1.00 24.11 ? 39  GLN D N   1 
ATOM   5233 C CA  . GLN D 2 39  ? -6.040  1.338   20.606 1.00 23.45 ? 39  GLN D CA  1 
ATOM   5234 C C   . GLN D 2 39  ? -6.820  2.028   21.719 1.00 26.14 ? 39  GLN D C   1 
ATOM   5235 O O   . GLN D 2 39  ? -6.254  2.370   22.749 1.00 28.61 ? 39  GLN D O   1 
ATOM   5236 C CB  . GLN D 2 39  ? -5.148  0.238   21.180 1.00 23.83 ? 39  GLN D CB  1 
ATOM   5237 C CG  . GLN D 2 39  ? -5.864  -1.023  21.627 1.00 23.76 ? 39  GLN D CG  1 
ATOM   5238 C CD  . GLN D 2 39  ? -4.913  -2.205  21.759 1.00 26.81 ? 39  GLN D CD  1 
ATOM   5239 O OE1 . GLN D 2 39  ? -3.723  -2.042  22.075 1.00 27.36 ? 39  GLN D OE1 1 
ATOM   5240 N NE2 . GLN D 2 39  ? -5.428  -3.404  21.495 1.00 27.96 ? 39  GLN D NE2 1 
ATOM   5241 N N   . SER D 2 40  ? -8.109  2.262   21.504 1.00 32.43 ? 40  SER D N   1 
ATOM   5242 C CA  . SER D 2 40  ? -8.916  2.985   22.489 1.00 32.01 ? 40  SER D CA  1 
ATOM   5243 C C   . SER D 2 40  ? -9.797  2.028   23.279 1.00 38.69 ? 40  SER D C   1 
ATOM   5244 O O   . SER D 2 40  ? -10.156 0.964   22.778 1.00 38.40 ? 40  SER D O   1 
ATOM   5245 C CB  . SER D 2 40  ? -9.764  4.069   21.818 1.00 31.27 ? 40  SER D CB  1 
ATOM   5246 O OG  . SER D 2 40  ? -10.847 3.517   21.091 1.00 35.36 ? 40  SER D OG  1 
ATOM   5247 N N   . PRO D 2 41  ? -10.134 2.398   24.525 1.00 44.22 ? 41  PRO D N   1 
ATOM   5248 C CA  . PRO D 2 41  ? -10.960 1.531   25.368 1.00 39.38 ? 41  PRO D CA  1 
ATOM   5249 C C   . PRO D 2 41  ? -12.273 1.129   24.710 1.00 41.08 ? 41  PRO D C   1 
ATOM   5250 O O   . PRO D 2 41  ? -12.696 -0.017  24.844 1.00 50.67 ? 41  PRO D O   1 
ATOM   5251 C CB  . PRO D 2 41  ? -11.205 2.382   26.628 1.00 38.59 ? 41  PRO D CB  1 
ATOM   5252 C CG  . PRO D 2 41  ? -10.735 3.759   26.293 1.00 35.03 ? 41  PRO D CG  1 
ATOM   5253 C CD  . PRO D 2 41  ? -9.672  3.586   25.263 1.00 43.92 ? 41  PRO D CD  1 
ATOM   5254 N N   . GLY D 2 42  ? -12.892 2.050   23.982 1.00 38.05 ? 42  GLY D N   1 
ATOM   5255 C CA  . GLY D 2 42  ? -14.168 1.779   23.347 1.00 41.47 ? 42  GLY D CA  1 
ATOM   5256 C C   . GLY D 2 42  ? -14.080 1.054   22.012 1.00 56.08 ? 42  GLY D C   1 
ATOM   5257 O O   . GLY D 2 42  ? -14.710 0.012   21.821 1.00 56.76 ? 42  GLY D O   1 
ATOM   5258 N N   . LYS D 2 43  ? -13.289 1.595   21.088 1.00 42.32 ? 43  LYS D N   1 
ATOM   5259 C CA  . LYS D 2 43  ? -13.266 1.097   19.714 1.00 45.40 ? 43  LYS D CA  1 
ATOM   5260 C C   . LYS D 2 43  ? -12.092 0.208   19.348 1.00 36.16 ? 43  LYS D C   1 
ATOM   5261 O O   . LYS D 2 43  ? -11.899 -0.080  18.177 1.00 38.59 ? 43  LYS D O   1 
ATOM   5262 C CB  . LYS D 2 43  ? -13.277 2.268   18.743 1.00 46.12 ? 43  LYS D CB  1 
ATOM   5263 C CG  . LYS D 2 43  ? -14.388 3.265   18.984 1.00 48.47 ? 43  LYS D CG  1 
ATOM   5264 C CD  . LYS D 2 43  ? -14.381 4.354   17.920 1.00 52.93 ? 43  LYS D CD  1 
ATOM   5265 C CE  . LYS D 2 43  ? -15.470 4.140   16.873 1.00 63.56 ? 43  LYS D CE  1 
ATOM   5266 N NZ  . LYS D 2 43  ? -15.428 5.186   15.803 1.00 50.73 ? 43  LYS D NZ  1 
ATOM   5267 N N   . GLY D 2 44  ? -11.292 -0.193  20.327 1.00 38.92 ? 44  GLY D N   1 
ATOM   5268 C CA  . GLY D 2 44  ? -10.196 -1.106  20.066 1.00 32.72 ? 44  GLY D CA  1 
ATOM   5269 C C   . GLY D 2 44  ? -9.187  -0.561  19.082 1.00 27.99 ? 44  GLY D C   1 
ATOM   5270 O O   . GLY D 2 44  ? -8.869  0.631   19.112 1.00 30.23 ? 44  GLY D O   1 
ATOM   5271 N N   . LEU D 2 45  ? -8.691  -1.434  18.207 1.00 24.86 ? 45  LEU D N   1 
ATOM   5272 C CA  . LEU D 2 45  ? -7.657  -1.073  17.238 1.00 21.07 ? 45  LEU D CA  1 
ATOM   5273 C C   . LEU D 2 45  ? -8.192  -0.315  16.025 1.00 22.39 ? 45  LEU D C   1 
ATOM   5274 O O   . LEU D 2 45  ? -9.145  -0.728  15.376 1.00 21.05 ? 45  LEU D O   1 
ATOM   5275 C CB  . LEU D 2 45  ? -6.904  -2.322  16.784 1.00 21.35 ? 45  LEU D CB  1 
ATOM   5276 C CG  . LEU D 2 45  ? -5.969  -2.932  17.832 1.00 25.42 ? 45  LEU D CG  1 
ATOM   5277 C CD1 . LEU D 2 45  ? -5.625  -4.348  17.431 1.00 21.57 ? 45  LEU D CD1 1 
ATOM   5278 C CD2 . LEU D 2 45  ? -4.709  -2.090  18.035 1.00 20.02 ? 45  LEU D CD2 1 
ATOM   5279 N N   . GLU D 2 46  ? -7.534  0.787   15.701 1.00 25.06 ? 46  GLU D N   1 
ATOM   5280 C CA  . GLU D 2 46  ? -8.059  1.711   14.713 1.00 27.04 ? 46  GLU D CA  1 
ATOM   5281 C C   . GLU D 2 46  ? -6.927  2.320   13.893 1.00 31.46 ? 46  GLU D C   1 
ATOM   5282 O O   . GLU D 2 46  ? -6.054  3.010   14.435 1.00 26.26 ? 46  GLU D O   1 
ATOM   5283 C CB  . GLU D 2 46  ? -8.829  2.807   15.449 1.00 25.78 ? 46  GLU D CB  1 
ATOM   5284 C CG  . GLU D 2 46  ? -9.685  3.703   14.594 1.00 30.06 ? 46  GLU D CG  1 
ATOM   5285 C CD  . GLU D 2 46  ? -10.612 4.573   15.444 1.00 40.69 ? 46  GLU D CD  1 
ATOM   5286 O OE1 . GLU D 2 46  ? -10.370 4.703   16.675 1.00 36.89 ? 46  GLU D OE1 1 
ATOM   5287 O OE2 . GLU D 2 46  ? -11.589 5.118   14.882 1.00 38.53 ? 46  GLU D OE2 1 
ATOM   5288 N N   . TRP D 2 47  ? -6.940  2.066   12.586 1.00 24.90 ? 47  TRP D N   1 
ATOM   5289 C CA  . TRP D 2 47  ? -5.939  2.629   11.698 1.00 19.16 ? 47  TRP D CA  1 
ATOM   5290 C C   . TRP D 2 47  ? -6.219  4.103   11.496 1.00 21.82 ? 47  TRP D C   1 
ATOM   5291 O O   . TRP D 2 47  ? -7.357  4.492   11.248 1.00 26.83 ? 47  TRP D O   1 
ATOM   5292 C CB  . TRP D 2 47  ? -5.968  1.899   10.368 1.00 25.19 ? 47  TRP D CB  1 
ATOM   5293 C CG  . TRP D 2 47  ? -4.972  2.388   9.351  1.00 21.85 ? 47  TRP D CG  1 
ATOM   5294 C CD1 . TRP D 2 47  ? -3.646  2.044   9.252  1.00 21.23 ? 47  TRP D CD1 1 
ATOM   5295 C CD2 . TRP D 2 47  ? -5.237  3.273   8.269  1.00 18.64 ? 47  TRP D CD2 1 
ATOM   5296 N NE1 . TRP D 2 47  ? -3.075  2.678   8.177  1.00 23.93 ? 47  TRP D NE1 1 
ATOM   5297 C CE2 . TRP D 2 47  ? -4.030  3.435   7.553  1.00 23.90 ? 47  TRP D CE2 1 
ATOM   5298 C CE3 . TRP D 2 47  ? -6.379  3.944   7.829  1.00 20.73 ? 47  TRP D CE3 1 
ATOM   5299 C CZ2 . TRP D 2 47  ? -3.934  4.248   6.418  1.00 26.71 ? 47  TRP D CZ2 1 
ATOM   5300 C CZ3 . TRP D 2 47  ? -6.283  4.761   6.697  1.00 27.39 ? 47  TRP D CZ3 1 
ATOM   5301 C CH2 . TRP D 2 47  ? -5.067  4.901   6.006  1.00 22.64 ? 47  TRP D CH2 1 
ATOM   5302 N N   . LEU D 2 48  ? -5.181  4.926   11.597 1.00 22.57 ? 48  LEU D N   1 
ATOM   5303 C CA  . LEU D 2 48  ? -5.372  6.371   11.614 1.00 24.14 ? 48  LEU D CA  1 
ATOM   5304 C C   . LEU D 2 48  ? -4.869  7.038   10.338 1.00 26.16 ? 48  LEU D C   1 
ATOM   5305 O O   . LEU D 2 48  ? -5.584  7.831   9.714  1.00 26.47 ? 48  LEU D O   1 
ATOM   5306 C CB  . LEU D 2 48  ? -4.695  6.988   12.845 1.00 23.61 ? 48  LEU D CB  1 
ATOM   5307 C CG  . LEU D 2 48  ? -5.286  6.647   14.213 1.00 21.12 ? 48  LEU D CG  1 
ATOM   5308 C CD1 . LEU D 2 48  ? -4.497  7.316   15.322 1.00 20.85 ? 48  LEU D CD1 1 
ATOM   5309 C CD2 . LEU D 2 48  ? -6.738  7.075   14.288 1.00 21.99 ? 48  LEU D CD2 1 
ATOM   5310 N N   . GLY D 2 49  ? -3.637  6.722   9.955  1.00 22.97 ? 49  GLY D N   1 
ATOM   5311 C CA  . GLY D 2 49  ? -3.034  7.343   8.795  1.00 22.81 ? 49  GLY D CA  1 
ATOM   5312 C C   . GLY D 2 49  ? -1.708  6.733   8.414  1.00 24.05 ? 49  GLY D C   1 
ATOM   5313 O O   . GLY D 2 49  ? -1.190  5.854   9.105  1.00 26.33 ? 49  GLY D O   1 
ATOM   5314 N N   . VAL D 2 50  ? -1.157  7.213   7.305  1.00 24.42 ? 50  VAL D N   1 
ATOM   5315 C CA  . VAL D 2 50  ? 0.143   6.772   6.823  1.00 18.47 ? 50  VAL D CA  1 
ATOM   5316 C C   . VAL D 2 50  ? 0.835   7.927   6.122  1.00 20.56 ? 50  VAL D C   1 
ATOM   5317 O O   . VAL D 2 50  ? 0.187   8.742   5.468  1.00 22.58 ? 50  VAL D O   1 
ATOM   5318 C CB  . VAL D 2 50  ? 0.013   5.557   5.849  1.00 23.42 ? 50  VAL D CB  1 
ATOM   5319 C CG1 . VAL D 2 50  ? -1.002  5.841   4.736  1.00 21.18 ? 50  VAL D CG1 1 
ATOM   5320 C CG2 . VAL D 2 50  ? 1.360   5.167   5.269  1.00 20.86 ? 50  VAL D CG2 1 
ATOM   5321 N N   . ILE D 2 51  ? 2.148   8.015   6.293  1.00 21.32 ? 51  ILE D N   1 
ATOM   5322 C CA  . ILE D 2 51  ? 2.975   8.841   5.431  1.00 20.67 ? 51  ILE D CA  1 
ATOM   5323 C C   . ILE D 2 51  ? 3.896   7.914   4.640  1.00 21.25 ? 51  ILE D C   1 
ATOM   5324 O O   . ILE D 2 51  ? 4.642   7.114   5.216  1.00 22.80 ? 51  ILE D O   1 
ATOM   5325 C CB  . ILE D 2 51  ? 3.762   9.918   6.208  1.00 22.18 ? 51  ILE D CB  1 
ATOM   5326 C CG1 . ILE D 2 51  ? 4.519   10.824  5.232  1.00 23.34 ? 51  ILE D CG1 1 
ATOM   5327 C CG2 . ILE D 2 51  ? 4.725   9.295   7.203  1.00 17.87 ? 51  ILE D CG2 1 
ATOM   5328 C CD1 . ILE D 2 51  ? 4.999   12.095  5.853  1.00 19.22 ? 51  ILE D CD1 1 
ATOM   5329 N N   . TRP D 2 52  ? 3.800   7.994   3.318  1.00 22.72 ? 52  TRP D N   1 
ATOM   5330 C CA  . TRP D 2 52  ? 4.542   7.099   2.427  1.00 23.18 ? 52  TRP D CA  1 
ATOM   5331 C C   . TRP D 2 52  ? 5.954   7.598   2.157  1.00 25.35 ? 52  TRP D C   1 
ATOM   5332 O O   . TRP D 2 52  ? 6.290   8.733   2.478  1.00 24.58 ? 52  TRP D O   1 
ATOM   5333 C CB  . TRP D 2 52  ? 3.804   6.923   1.098  1.00 20.58 ? 52  TRP D CB  1 
ATOM   5334 C CG  . TRP D 2 52  ? 2.391   6.420   1.241  1.00 30.58 ? 52  TRP D CG  1 
ATOM   5335 C CD1 . TRP D 2 52  ? 1.244   7.156   1.128  1.00 26.14 ? 52  TRP D CD1 1 
ATOM   5336 C CD2 . TRP D 2 52  ? 1.974   5.075   1.523  1.00 28.69 ? 52  TRP D CD2 1 
ATOM   5337 N NE1 . TRP D 2 52  ? 0.150   6.359   1.327  1.00 26.33 ? 52  TRP D NE1 1 
ATOM   5338 C CE2 . TRP D 2 52  ? 0.565   5.076   1.568  1.00 27.40 ? 52  TRP D CE2 1 
ATOM   5339 C CE3 . TRP D 2 52  ? 2.655   3.873   1.746  1.00 28.80 ? 52  TRP D CE3 1 
ATOM   5340 C CZ2 . TRP D 2 52  ? -0.180  3.923   1.818  1.00 30.74 ? 52  TRP D CZ2 1 
ATOM   5341 C CZ3 . TRP D 2 52  ? 1.913   2.724   1.995  1.00 29.38 ? 52  TRP D CZ3 1 
ATOM   5342 C CH2 . TRP D 2 52  ? 0.509   2.760   2.030  1.00 27.46 ? 52  TRP D CH2 1 
ATOM   5343 N N   . SER D 2 53  ? 6.765   6.735   1.554  1.00 29.74 ? 53  SER D N   1 
ATOM   5344 C CA  . SER D 2 53  ? 8.162   7.026   1.242  1.00 27.31 ? 53  SER D CA  1 
ATOM   5345 C C   . SER D 2 53  ? 8.384   8.399   0.637  1.00 32.57 ? 53  SER D C   1 
ATOM   5346 O O   . SER D 2 53  ? 9.249   9.145   1.091  1.00 32.81 ? 53  SER D O   1 
ATOM   5347 C CB  . SER D 2 53  ? 8.711   5.966   0.293  1.00 30.68 ? 53  SER D CB  1 
ATOM   5348 O OG  . SER D 2 53  ? 8.915   4.746   0.983  1.00 35.67 ? 53  SER D OG  1 
ATOM   5349 N N   . GLY D 2 54  ? 7.594   8.728   -0.383 1.00 28.45 ? 54  GLY D N   1 
ATOM   5350 C CA  . GLY D 2 54  ? 7.724   9.996   -1.075 1.00 24.28 ? 54  GLY D CA  1 
ATOM   5351 C C   . GLY D 2 54  ? 7.043   11.192  -0.426 1.00 33.19 ? 54  GLY D C   1 
ATOM   5352 O O   . GLY D 2 54  ? 6.998   12.274  -1.011 1.00 35.82 ? 54  GLY D O   1 
ATOM   5353 N N   . GLY D 2 55  ? 6.502   11.015  0.774  1.00 30.45 ? 55  GLY D N   1 
ATOM   5354 C CA  . GLY D 2 55  ? 5.931   12.139  1.494  1.00 20.61 ? 55  GLY D CA  1 
ATOM   5355 C C   . GLY D 2 55  ? 4.424   12.287  1.401  1.00 23.81 ? 55  GLY D C   1 
ATOM   5356 O O   . GLY D 2 55  ? 3.853   13.088  2.133  1.00 26.72 ? 55  GLY D O   1 
ATOM   5357 N N   . ASN D 2 56  ? 3.777   11.543  0.503  1.00 25.56 ? 56  ASN D N   1 
ATOM   5358 C CA  . ASN D 2 56  ? 2.316   11.504  0.452  1.00 21.63 ? 56  ASN D CA  1 
ATOM   5359 C C   . ASN D 2 56  ? 1.720   10.978  1.762  1.00 31.97 ? 56  ASN D C   1 
ATOM   5360 O O   . ASN D 2 56  ? 2.334   10.147  2.448  1.00 27.08 ? 56  ASN D O   1 
ATOM   5361 C CB  . ASN D 2 56  ? 1.831   10.604  -0.687 1.00 33.19 ? 56  ASN D CB  1 
ATOM   5362 C CG  . ASN D 2 56  ? 1.906   11.271  -2.050 1.00 33.90 ? 56  ASN D CG  1 
ATOM   5363 O OD1 . ASN D 2 56  ? 1.773   12.488  -2.178 1.00 29.79 ? 56  ASN D OD1 1 
ATOM   5364 N ND2 . ASN D 2 56  ? 2.112   10.461  -3.082 1.00 32.55 ? 56  ASN D ND2 1 
ATOM   5365 N N   . THR D 2 57  ? 0.524   11.452  2.108  1.00 23.94 ? 57  THR D N   1 
ATOM   5366 C CA  . THR D 2 57  ? -0.164  10.952  3.290  1.00 20.75 ? 57  THR D CA  1 
ATOM   5367 C C   . THR D 2 57  ? -1.591  10.574  2.969  1.00 27.22 ? 57  THR D C   1 
ATOM   5368 O O   . THR D 2 57  ? -2.248  11.231  2.166  1.00 29.63 ? 57  THR D O   1 
ATOM   5369 C CB  . THR D 2 57  ? -0.229  12.001  4.412  1.00 24.82 ? 57  THR D CB  1 
ATOM   5370 O OG1 . THR D 2 57  ? -0.833  13.198  3.904  1.00 30.70 ? 57  THR D OG1 1 
ATOM   5371 C CG2 . THR D 2 57  ? 1.169   12.299  4.967  1.00 22.99 ? 57  THR D CG2 1 
ATOM   5372 N N   . ASP D 2 58  ? -2.058  9.505   3.602  1.00 25.81 ? 58  ASP D N   1 
ATOM   5373 C CA  . ASP D 2 58  ? -3.465  9.161   3.616  1.00 18.05 ? 58  ASP D CA  1 
ATOM   5374 C C   . ASP D 2 58  ? -3.922  9.217   5.063  1.00 30.94 ? 58  ASP D C   1 
ATOM   5375 O O   . ASP D 2 58  ? -3.175  8.833   5.964  1.00 25.71 ? 58  ASP D O   1 
ATOM   5376 C CB  . ASP D 2 58  ? -3.674  7.738   3.103  1.00 21.27 ? 58  ASP D CB  1 
ATOM   5377 C CG  . ASP D 2 58  ? -3.387  7.593   1.623  1.00 33.75 ? 58  ASP D CG  1 
ATOM   5378 O OD1 . ASP D 2 58  ? -3.850  8.450   0.829  1.00 25.64 ? 58  ASP D OD1 1 
ATOM   5379 O OD2 . ASP D 2 58  ? -2.703  6.605   1.267  1.00 26.94 ? 58  ASP D OD2 1 
ATOM   5380 N N   . TYR D 2 59  ? -5.145  9.686   5.289  1.00 26.82 ? 59  TYR D N   1 
ATOM   5381 C CA  . TYR D 2 59  ? -5.727  9.668   6.627  1.00 27.21 ? 59  TYR D CA  1 
ATOM   5382 C C   . TYR D 2 59  ? -7.054  8.909   6.630  1.00 29.09 ? 59  TYR D C   1 
ATOM   5383 O O   . TYR D 2 59  ? -7.839  8.992   5.676  1.00 22.28 ? 59  TYR D O   1 
ATOM   5384 C CB  . TYR D 2 59  ? -5.940  11.095  7.136  1.00 27.59 ? 59  TYR D CB  1 
ATOM   5385 C CG  . TYR D 2 59  ? -4.687  11.932  7.126  1.00 24.69 ? 59  TYR D CG  1 
ATOM   5386 C CD1 . TYR D 2 59  ? -3.514  11.475  7.717  1.00 31.79 ? 59  TYR D CD1 1 
ATOM   5387 C CD2 . TYR D 2 59  ? -4.669  13.177  6.517  1.00 24.99 ? 59  TYR D CD2 1 
ATOM   5388 C CE1 . TYR D 2 59  ? -2.354  12.247  7.702  1.00 28.81 ? 59  TYR D CE1 1 
ATOM   5389 C CE2 . TYR D 2 59  ? -3.528  13.949  6.502  1.00 30.15 ? 59  TYR D CE2 1 
ATOM   5390 C CZ  . TYR D 2 59  ? -2.373  13.482  7.095  1.00 28.29 ? 59  TYR D CZ  1 
ATOM   5391 O OH  . TYR D 2 59  ? -1.239  14.257  7.071  1.00 32.54 ? 59  TYR D OH  1 
ATOM   5392 N N   . ASN D 2 60  ? -7.310  8.153   7.690  1.00 24.36 ? 60  ASN D N   1 
ATOM   5393 C CA  . ASN D 2 60  ? -8.604  7.504   7.784  1.00 24.91 ? 60  ASN D CA  1 
ATOM   5394 C C   . ASN D 2 60  ? -9.684  8.575   7.883  1.00 32.49 ? 60  ASN D C   1 
ATOM   5395 O O   . ASN D 2 60  ? -9.528  9.563   8.607  1.00 27.71 ? 60  ASN D O   1 
ATOM   5396 C CB  . ASN D 2 60  ? -8.670  6.539   8.960  1.00 29.68 ? 60  ASN D CB  1 
ATOM   5397 C CG  . ASN D 2 60  ? -9.824  5.570   8.837  1.00 27.60 ? 60  ASN D CG  1 
ATOM   5398 O OD1 . ASN D 2 60  ? -10.713 5.756   8.008  1.00 20.51 ? 60  ASN D OD1 1 
ATOM   5399 N ND2 . ASN D 2 60  ? -9.817  4.532   9.659  1.00 19.70 ? 60  ASN D ND2 1 
ATOM   5400 N N   . THR D 2 61  ? -10.758 8.374   7.123  1.00 31.85 ? 61  THR D N   1 
ATOM   5401 C CA  . THR D 2 61  ? -11.812 9.373   6.925  1.00 29.93 ? 61  THR D CA  1 
ATOM   5402 C C   . THR D 2 61  ? -12.249 10.198  8.158  1.00 32.05 ? 61  THR D C   1 
ATOM   5403 O O   . THR D 2 61  ? -12.272 11.427  8.093  1.00 27.91 ? 61  THR D O   1 
ATOM   5404 C CB  . THR D 2 61  ? -13.024 8.753   6.204  1.00 27.86 ? 61  THR D CB  1 
ATOM   5405 O OG1 . THR D 2 61  ? -12.674 8.509   4.839  1.00 37.12 ? 61  THR D OG1 1 
ATOM   5406 C CG2 . THR D 2 61  ? -14.219 9.689   6.246  1.00 27.97 ? 61  THR D CG2 1 
ATOM   5407 N N   . PRO D 2 62  ? -12.560 9.542   9.293  1.00 31.21 ? 62  PRO D N   1 
ATOM   5408 C CA  . PRO D 2 62  ? -12.983 10.377  10.425 1.00 28.44 ? 62  PRO D CA  1 
ATOM   5409 C C   . PRO D 2 62  ? -11.859 11.204  11.045 1.00 27.51 ? 62  PRO D C   1 
ATOM   5410 O O   . PRO D 2 62  ? -12.096 11.844  12.061 1.00 37.89 ? 62  PRO D O   1 
ATOM   5411 C CB  . PRO D 2 62  ? -13.495 9.356   11.437 1.00 29.55 ? 62  PRO D CB  1 
ATOM   5412 C CG  . PRO D 2 62  ? -12.751 8.120   11.126 1.00 31.32 ? 62  PRO D CG  1 
ATOM   5413 C CD  . PRO D 2 62  ? -12.575 8.107   9.637  1.00 30.12 ? 62  PRO D CD  1 
ATOM   5414 N N   . PHE D 2 63  ? -10.671 11.218  10.452 1.00 23.47 ? 63  PHE D N   1 
ATOM   5415 C CA  . PHE D 2 63  ? -9.582  11.997  11.020 1.00 22.61 ? 63  PHE D CA  1 
ATOM   5416 C C   . PHE D 2 63  ? -8.998  13.018  10.047 1.00 32.69 ? 63  PHE D C   1 
ATOM   5417 O O   . PHE D 2 63  ? -8.190  13.862  10.444 1.00 33.92 ? 63  PHE D O   1 
ATOM   5418 C CB  . PHE D 2 63  ? -8.498  11.069  11.573 1.00 20.78 ? 63  PHE D CB  1 
ATOM   5419 C CG  . PHE D 2 63  ? -9.006  10.124  12.631 1.00 31.68 ? 63  PHE D CG  1 
ATOM   5420 C CD1 . PHE D 2 63  ? -9.483  8.866   12.294 1.00 25.64 ? 63  PHE D CD1 1 
ATOM   5421 C CD2 . PHE D 2 63  ? -9.032  10.506  13.963 1.00 26.73 ? 63  PHE D CD2 1 
ATOM   5422 C CE1 . PHE D 2 63  ? -9.966  8.007   13.267 1.00 23.57 ? 63  PHE D CE1 1 
ATOM   5423 C CE2 . PHE D 2 63  ? -9.506  9.650   14.930 1.00 27.38 ? 63  PHE D CE2 1 
ATOM   5424 C CZ  . PHE D 2 63  ? -9.975  8.396   14.575 1.00 26.48 ? 63  PHE D CZ  1 
ATOM   5425 N N   . THR D 2 64  ? -9.445  12.957  8.792  1.00 32.83 ? 64  THR D N   1 
ATOM   5426 C CA  . THR D 2 64  ? -8.881  13.759  7.705  1.00 26.75 ? 64  THR D CA  1 
ATOM   5427 C C   . THR D 2 64  ? -8.743  15.244  8.030  1.00 32.44 ? 64  THR D C   1 
ATOM   5428 O O   . THR D 2 64  ? -7.779  15.888  7.616  1.00 40.29 ? 64  THR D O   1 
ATOM   5429 C CB  . THR D 2 64  ? -9.657  13.570  6.371  1.00 29.86 ? 64  THR D CB  1 
ATOM   5430 O OG1 . THR D 2 64  ? -11.064 13.530  6.622  1.00 40.32 ? 64  THR D OG1 1 
ATOM   5431 C CG2 . THR D 2 64  ? -9.260  12.263  5.698  1.00 27.95 ? 64  THR D CG2 1 
ATOM   5432 N N   . SER D 2 65  ? -9.677  15.778  8.807  1.00 36.71 ? 65  SER D N   1 
ATOM   5433 C CA  . SER D 2 65  ? -9.679  17.204  9.088  1.00 33.77 ? 65  SER D CA  1 
ATOM   5434 C C   . SER D 2 65  ? -9.054  17.578  10.433 1.00 34.07 ? 65  SER D C   1 
ATOM   5435 O O   . SER D 2 65  ? -9.171  18.719  10.878 1.00 33.80 ? 65  SER D O   1 
ATOM   5436 C CB  . SER D 2 65  ? -11.100 17.751  9.022  1.00 32.82 ? 65  SER D CB  1 
ATOM   5437 O OG  . SER D 2 65  ? -11.853 17.297  10.126 1.00 42.17 ? 65  SER D OG  1 
ATOM   5438 N N   . ARG D 2 66  ? -8.387  16.642  11.094 1.00 37.25 ? 66  ARG D N   1 
ATOM   5439 C CA  . ARG D 2 66  ? -7.746  17.003  12.353 1.00 38.75 ? 66  ARG D CA  1 
ATOM   5440 C C   . ARG D 2 66  ? -6.422  16.310  12.586 1.00 28.32 ? 66  ARG D C   1 
ATOM   5441 O O   . ARG D 2 66  ? -5.863  16.366  13.680 1.00 29.83 ? 66  ARG D O   1 
ATOM   5442 C CB  . ARG D 2 66  ? -8.696  16.777  13.531 1.00 32.38 ? 66  ARG D CB  1 
ATOM   5443 C CG  . ARG D 2 66  ? -8.982  15.330  13.897 1.00 32.48 ? 66  ARG D CG  1 
ATOM   5444 C CD  . ARG D 2 66  ? -10.075 15.338  14.958 1.00 40.65 ? 66  ARG D CD  1 
ATOM   5445 N NE  . ARG D 2 66  ? -10.298 14.044  15.575 1.00 34.48 ? 66  ARG D NE  1 
ATOM   5446 C CZ  . ARG D 2 66  ? -10.063 13.782  16.856 1.00 38.30 ? 66  ARG D CZ  1 
ATOM   5447 N NH1 . ARG D 2 66  ? -9.597  14.731  17.660 1.00 34.30 ? 66  ARG D NH1 1 
ATOM   5448 N NH2 . ARG D 2 66  ? -10.294 12.567  17.333 1.00 43.79 ? 66  ARG D NH2 1 
ATOM   5449 N N   . LEU D 2 67  ? -5.909  15.677  11.545 1.00 27.75 ? 67  LEU D N   1 
ATOM   5450 C CA  . LEU D 2 67  ? -4.694  14.895  11.674 1.00 28.05 ? 67  LEU D CA  1 
ATOM   5451 C C   . LEU D 2 67  ? -3.664  15.337  10.647 1.00 30.50 ? 67  LEU D C   1 
ATOM   5452 O O   . LEU D 2 67  ? -3.991  15.635  9.496  1.00 36.80 ? 67  LEU D O   1 
ATOM   5453 C CB  . LEU D 2 67  ? -5.026  13.418  11.501 1.00 26.92 ? 67  LEU D CB  1 
ATOM   5454 C CG  . LEU D 2 67  ? -3.906  12.394  11.511 1.00 30.65 ? 67  LEU D CG  1 
ATOM   5455 C CD1 . LEU D 2 67  ? -3.105  12.534  12.783 1.00 30.91 ? 67  LEU D CD1 1 
ATOM   5456 C CD2 . LEU D 2 67  ? -4.509  11.018  11.403 1.00 27.77 ? 67  LEU D CD2 1 
ATOM   5457 N N   . SER D 2 68  ? -2.413  15.407  11.064 1.00 25.25 ? 68  SER D N   1 
ATOM   5458 C CA  . SER D 2 68  ? -1.364  15.700  10.123 1.00 23.46 ? 68  SER D CA  1 
ATOM   5459 C C   . SER D 2 68  ? -0.150  14.839  10.452 1.00 30.67 ? 68  SER D C   1 
ATOM   5460 O O   . SER D 2 68  ? 0.214   14.670  11.620 1.00 33.82 ? 68  SER D O   1 
ATOM   5461 C CB  . SER D 2 68  ? -1.026  17.189  10.143 1.00 25.07 ? 68  SER D CB  1 
ATOM   5462 O OG  . SER D 2 68  ? 0.071   17.446  10.993 1.00 37.77 ? 68  SER D OG  1 
ATOM   5463 N N   . ILE D 2 69  ? 0.454   14.265  9.420  1.00 21.44 ? 69  ILE D N   1 
ATOM   5464 C CA  . ILE D 2 69  ? 1.615   13.430  9.598  1.00 18.23 ? 69  ILE D CA  1 
ATOM   5465 C C   . ILE D 2 69  ? 2.721   13.952  8.710  1.00 24.55 ? 69  ILE D C   1 
ATOM   5466 O O   . ILE D 2 69  ? 2.553   14.086  7.488  1.00 27.27 ? 69  ILE D O   1 
ATOM   5467 C CB  . ILE D 2 69  ? 1.317   11.973  9.240  1.00 22.85 ? 69  ILE D CB  1 
ATOM   5468 C CG1 . ILE D 2 69  ? 0.131   11.452  10.056 1.00 23.62 ? 69  ILE D CG1 1 
ATOM   5469 C CG2 . ILE D 2 69  ? 2.551   11.107  9.451  1.00 18.40 ? 69  ILE D CG2 1 
ATOM   5470 C CD1 . ILE D 2 69  ? -0.196  10.003  9.793  1.00 20.71 ? 69  ILE D CD1 1 
ATOM   5471 N N   . ASN D 2 70  ? 3.853   14.259  9.329  1.00 25.24 ? 70  ASN D N   1 
ATOM   5472 C CA  . ASN D 2 70  ? 5.001   14.791  8.613  1.00 25.10 ? 70  ASN D CA  1 
ATOM   5473 C C   . ASN D 2 70  ? 6.235   13.983  8.950  1.00 31.10 ? 70  ASN D C   1 
ATOM   5474 O O   . ASN D 2 70  ? 6.211   13.158  9.867  1.00 31.18 ? 70  ASN D O   1 
ATOM   5475 C CB  . ASN D 2 70  ? 5.215   16.262  8.976  1.00 25.79 ? 70  ASN D CB  1 
ATOM   5476 C CG  . ASN D 2 70  ? 4.187   17.164  8.332  1.00 32.61 ? 70  ASN D CG  1 
ATOM   5477 O OD1 . ASN D 2 70  ? 4.306   17.501  7.153  1.00 50.89 ? 70  ASN D OD1 1 
ATOM   5478 N ND2 . ASN D 2 70  ? 3.151   17.535  9.084  1.00 28.78 ? 70  ASN D ND2 1 
ATOM   5479 N N   . LYS D 2 71  ? 7.316   14.211  8.215  1.00 31.83 ? 71  LYS D N   1 
ATOM   5480 C CA  . LYS D 2 71  ? 8.571   13.559  8.546  1.00 25.30 ? 71  LYS D CA  1 
ATOM   5481 C C   . LYS D 2 71  ? 9.788   14.371  8.142  1.00 28.97 ? 71  LYS D C   1 
ATOM   5482 O O   . LYS D 2 71  ? 9.697   15.343  7.400  1.00 25.01 ? 71  LYS D O   1 
ATOM   5483 C CB  . LYS D 2 71  ? 8.653   12.179  7.901  1.00 32.00 ? 71  LYS D CB  1 
ATOM   5484 C CG  . LYS D 2 71  ? 8.523   12.189  6.398  1.00 27.41 ? 71  LYS D CG  1 
ATOM   5485 C CD  . LYS D 2 71  ? 8.603   10.779  5.840  1.00 35.30 ? 71  LYS D CD  1 
ATOM   5486 C CE  . LYS D 2 71  ? 8.641   10.783  4.314  1.00 28.96 ? 71  LYS D CE  1 
ATOM   5487 N NZ  . LYS D 2 71  ? 9.090   9.476   3.828  1.00 26.65 ? 71  LYS D NZ  1 
ATOM   5488 N N   . ASP D 2 72  ? 10.928  13.953  8.672  1.00 29.80 ? 72  ASP D N   1 
ATOM   5489 C CA  . ASP D 2 72  ? 12.220  14.488  8.309  1.00 27.76 ? 72  ASP D CA  1 
ATOM   5490 C C   . ASP D 2 72  ? 13.026  13.249  7.971  1.00 36.51 ? 72  ASP D C   1 
ATOM   5491 O O   . ASP D 2 72  ? 13.424  12.502  8.872  1.00 32.60 ? 72  ASP D O   1 
ATOM   5492 C CB  . ASP D 2 72  ? 12.827  15.226  9.503  1.00 35.97 ? 72  ASP D CB  1 
ATOM   5493 C CG  . ASP D 2 72  ? 14.219  15.777  9.221  1.00 42.74 ? 72  ASP D CG  1 
ATOM   5494 O OD1 . ASP D 2 72  ? 15.029  15.097  8.558  1.00 36.86 ? 72  ASP D OD1 1 
ATOM   5495 O OD2 . ASP D 2 72  ? 14.514  16.901  9.683  1.00 51.46 ? 72  ASP D OD2 1 
ATOM   5496 N N   . ASN D 2 73  ? 13.254  13.017  6.679  1.00 35.88 ? 73  ASN D N   1 
ATOM   5497 C CA  . ASN D 2 73  ? 13.952  11.808  6.248  1.00 36.30 ? 73  ASN D CA  1 
ATOM   5498 C C   . ASN D 2 73  ? 15.343  11.682  6.851  1.00 37.98 ? 73  ASN D C   1 
ATOM   5499 O O   . ASN D 2 73  ? 15.751  10.594  7.255  1.00 36.80 ? 73  ASN D O   1 
ATOM   5500 C CB  . ASN D 2 73  ? 14.029  11.730  4.722  1.00 35.73 ? 73  ASN D CB  1 
ATOM   5501 C CG  . ASN D 2 73  ? 12.697  11.431  4.093  1.00 36.39 ? 73  ASN D CG  1 
ATOM   5502 O OD1 . ASN D 2 73  ? 11.931  10.618  4.603  1.00 43.78 ? 73  ASN D OD1 1 
ATOM   5503 N ND2 . ASN D 2 73  ? 12.404  12.090  2.980  1.00 33.70 ? 73  ASN D ND2 1 
ATOM   5504 N N   . SER D 2 74  ? 16.057  12.805  6.926  1.00 36.82 ? 74  SER D N   1 
ATOM   5505 C CA  . SER D 2 74  ? 17.439  12.825  7.427  1.00 34.80 ? 74  SER D CA  1 
ATOM   5506 C C   . SER D 2 74  ? 17.545  12.470  8.909  1.00 36.47 ? 74  SER D C   1 
ATOM   5507 O O   . SER D 2 74  ? 18.454  11.735  9.311  1.00 30.31 ? 74  SER D O   1 
ATOM   5508 C CB  . SER D 2 74  ? 18.104  14.178  7.149  1.00 36.30 ? 74  SER D CB  1 
ATOM   5509 O OG  . SER D 2 74  ? 17.430  15.245  7.790  1.00 46.27 ? 74  SER D OG  1 
ATOM   5510 N N   . LYS D 2 75  ? 16.614  12.988  9.713  1.00 36.02 ? 75  LYS D N   1 
ATOM   5511 C CA  . LYS D 2 75  ? 16.596  12.708  11.151 1.00 33.18 ? 75  LYS D CA  1 
ATOM   5512 C C   . LYS D 2 75  ? 15.916  11.383  11.506 1.00 31.46 ? 75  LYS D C   1 
ATOM   5513 O O   . LYS D 2 75  ? 15.868  11.008  12.671 1.00 34.03 ? 75  LYS D O   1 
ATOM   5514 C CB  . LYS D 2 75  ? 15.970  13.867  11.941 1.00 35.66 ? 75  LYS D CB  1 
ATOM   5515 C CG  . LYS D 2 75  ? 16.688  15.200  11.731 1.00 38.45 ? 75  LYS D CG  1 
ATOM   5516 C CD  . LYS D 2 75  ? 16.134  16.302  12.618 1.00 41.35 ? 75  LYS D CD  1 
ATOM   5517 C CE  . LYS D 2 75  ? 14.608  16.298  12.633 1.00 56.83 ? 75  LYS D CE  1 
ATOM   5518 N NZ  . LYS D 2 75  ? 14.008  17.589  13.095 1.00 52.57 ? 75  LYS D NZ  1 
ATOM   5519 N N   . SER D 2 76  ? 15.406  10.674  10.503 1.00 33.73 ? 76  SER D N   1 
ATOM   5520 C CA  . SER D 2 76  ? 14.800  9.359   10.704 1.00 26.75 ? 76  SER D CA  1 
ATOM   5521 C C   . SER D 2 76  ? 13.586  9.465   11.630 1.00 25.57 ? 76  SER D C   1 
ATOM   5522 O O   . SER D 2 76  ? 13.269  8.532   12.375 1.00 21.97 ? 76  SER D O   1 
ATOM   5523 C CB  . SER D 2 76  ? 15.831  8.377   11.272 1.00 24.94 ? 76  SER D CB  1 
ATOM   5524 O OG  . SER D 2 76  ? 15.843  7.158   10.551 1.00 36.90 ? 76  SER D OG  1 
ATOM   5525 N N   . GLN D 2 77  ? 12.915  10.614  11.576 1.00 23.75 ? 77  GLN D N   1 
ATOM   5526 C CA  . GLN D 2 77  ? 11.780  10.892  12.449 1.00 28.70 ? 77  GLN D CA  1 
ATOM   5527 C C   . GLN D 2 77  ? 10.470  11.184  11.715 1.00 27.50 ? 77  GLN D C   1 
ATOM   5528 O O   . GLN D 2 77  ? 10.444  11.948  10.757 1.00 31.97 ? 77  GLN D O   1 
ATOM   5529 C CB  . GLN D 2 77  ? 12.105  12.076  13.355 1.00 32.67 ? 77  GLN D CB  1 
ATOM   5530 C CG  . GLN D 2 77  ? 13.199  11.803  14.364 1.00 31.49 ? 77  GLN D CG  1 
ATOM   5531 C CD  . GLN D 2 77  ? 13.435  12.990  15.273 1.00 36.47 ? 77  GLN D CD  1 
ATOM   5532 O OE1 . GLN D 2 77  ? 13.455  14.138  14.825 1.00 32.30 ? 77  GLN D OE1 1 
ATOM   5533 N NE2 . GLN D 2 77  ? 13.602  12.721  16.562 1.00 41.07 ? 77  GLN D NE2 1 
ATOM   5534 N N   . VAL D 2 78  ? 9.384   10.591  12.204 1.00 27.68 ? 78  VAL D N   1 
ATOM   5535 C CA  . VAL D 2 78  ? 8.025   10.867  11.725 1.00 25.90 ? 78  VAL D CA  1 
ATOM   5536 C C   . VAL D 2 78  ? 7.214   11.621  12.784 1.00 26.97 ? 78  VAL D C   1 
ATOM   5537 O O   . VAL D 2 78  ? 7.262   11.275  13.964 1.00 30.27 ? 78  VAL D O   1 
ATOM   5538 C CB  . VAL D 2 78  ? 7.277   9.551   11.371 1.00 26.59 ? 78  VAL D CB  1 
ATOM   5539 C CG1 . VAL D 2 78  ? 5.834   9.841   10.969 1.00 19.45 ? 78  VAL D CG1 1 
ATOM   5540 C CG2 . VAL D 2 78  ? 8.010   8.801   10.254 1.00 19.33 ? 78  VAL D CG2 1 
ATOM   5541 N N   . PHE D 2 79  ? 6.465   12.639  12.365 1.00 26.13 ? 79  PHE D N   1 
ATOM   5542 C CA  . PHE D 2 79  ? 5.707   13.472  13.303 1.00 24.88 ? 79  PHE D CA  1 
ATOM   5543 C C   . PHE D 2 79  ? 4.178   13.346  13.161 1.00 31.18 ? 79  PHE D C   1 
ATOM   5544 O O   . PHE D 2 79  ? 3.602   13.657  12.115 1.00 29.74 ? 79  PHE D O   1 
ATOM   5545 C CB  . PHE D 2 79  ? 6.115   14.938  13.160 1.00 21.40 ? 79  PHE D CB  1 
ATOM   5546 C CG  . PHE D 2 79  ? 7.603   15.151  13.064 1.00 28.23 ? 79  PHE D CG  1 
ATOM   5547 C CD1 . PHE D 2 79  ? 8.197   15.449  11.847 1.00 26.30 ? 79  PHE D CD1 1 
ATOM   5548 C CD2 . PHE D 2 79  ? 8.410   15.050  14.191 1.00 34.95 ? 79  PHE D CD2 1 
ATOM   5549 C CE1 . PHE D 2 79  ? 9.557   15.646  11.756 1.00 33.07 ? 79  PHE D CE1 1 
ATOM   5550 C CE2 . PHE D 2 79  ? 9.776   15.246  14.106 1.00 26.99 ? 79  PHE D CE2 1 
ATOM   5551 C CZ  . PHE D 2 79  ? 10.351  15.546  12.887 1.00 35.97 ? 79  PHE D CZ  1 
ATOM   5552 N N   . PHE D 2 80  ? 3.535   12.901  14.235 1.00 22.86 ? 80  PHE D N   1 
ATOM   5553 C CA  . PHE D 2 80  ? 2.096   12.710  14.280 1.00 23.31 ? 80  PHE D CA  1 
ATOM   5554 C C   . PHE D 2 80  ? 1.511   13.856  15.073 1.00 28.50 ? 80  PHE D C   1 
ATOM   5555 O O   . PHE D 2 80  ? 1.960   14.134  16.182 1.00 33.15 ? 80  PHE D O   1 
ATOM   5556 C CB  . PHE D 2 80  ? 1.798   11.389  14.987 1.00 25.02 ? 80  PHE D CB  1 
ATOM   5557 C CG  . PHE D 2 80  ? 0.335   11.109  15.208 1.00 25.16 ? 80  PHE D CG  1 
ATOM   5558 C CD1 . PHE D 2 80  ? -0.373  10.334  14.310 1.00 22.02 ? 80  PHE D CD1 1 
ATOM   5559 C CD2 . PHE D 2 80  ? -0.319  11.573  16.349 1.00 29.18 ? 80  PHE D CD2 1 
ATOM   5560 C CE1 . PHE D 2 80  ? -1.711  10.043  14.531 1.00 25.94 ? 80  PHE D CE1 1 
ATOM   5561 C CE2 . PHE D 2 80  ? -1.665  11.290  16.572 1.00 22.74 ? 80  PHE D CE2 1 
ATOM   5562 C CZ  . PHE D 2 80  ? -2.356  10.526  15.668 1.00 24.58 ? 80  PHE D CZ  1 
ATOM   5563 N N   . LYS D 2 81  ? 0.508   14.525  14.516 1.00 26.78 ? 81  LYS D N   1 
ATOM   5564 C CA  . LYS D 2 81  ? -0.164  15.592  15.240 1.00 27.85 ? 81  LYS D CA  1 
ATOM   5565 C C   . LYS D 2 81  ? -1.674  15.507  15.030 1.00 32.58 ? 81  LYS D C   1 
ATOM   5566 O O   . LYS D 2 81  ? -2.133  15.345  13.897 1.00 31.63 ? 81  LYS D O   1 
ATOM   5567 C CB  . LYS D 2 81  ? 0.395   16.956  14.834 1.00 25.67 ? 81  LYS D CB  1 
ATOM   5568 C CG  . LYS D 2 81  ? -0.207  18.136  15.589 1.00 30.79 ? 81  LYS D CG  1 
ATOM   5569 C CD  . LYS D 2 81  ? 0.502   19.444  15.247 1.00 30.95 ? 81  LYS D CD  1 
ATOM   5570 C CE  . LYS D 2 81  ? -0.462  20.626  15.156 1.00 42.22 ? 81  LYS D CE  1 
ATOM   5571 N NZ  . LYS D 2 81  ? -1.074  21.019  16.466 1.00 31.84 ? 81  LYS D NZ  1 
ATOM   5572 N N   . MET D 2 82  ? -2.438  15.583  16.122 1.00 27.13 ? 82  MET D N   1 
ATOM   5573 C CA  . MET D 2 82  ? -3.894  15.494  16.047 1.00 28.85 ? 82  MET D CA  1 
ATOM   5574 C C   . MET D 2 82  ? -4.582  16.581  16.865 1.00 33.93 ? 82  MET D C   1 
ATOM   5575 O O   . MET D 2 82  ? -4.288  16.772  18.036 1.00 40.78 ? 82  MET D O   1 
ATOM   5576 C CB  . MET D 2 82  ? -4.396  14.118  16.479 1.00 26.28 ? 82  MET D CB  1 
ATOM   5577 C CG  . MET D 2 82  ? -5.895  13.937  16.290 1.00 27.54 ? 82  MET D CG  1 
ATOM   5578 S SD  . MET D 2 82  ? -6.412  12.210  16.390 1.00 35.61 ? 82  MET D SD  1 
ATOM   5579 C CE  . MET D 2 82  ? -6.963  12.095  18.095 1.00 30.87 ? 82  MET D CE  1 
ATOM   5580 N N   . ASN D 2 83  ? -5.521  17.276  16.239 1.00 40.18 ? 83  ASN D N   1 
ATOM   5581 C CA  . ASN D 2 83  ? -6.118  18.466  16.826 1.00 38.12 ? 83  ASN D CA  1 
ATOM   5582 C C   . ASN D 2 83  ? -7.418  18.209  17.577 1.00 35.61 ? 83  ASN D C   1 
ATOM   5583 O O   . ASN D 2 83  ? -8.147  17.248  17.297 1.00 28.57 ? 83  ASN D O   1 
ATOM   5584 C CB  . ASN D 2 83  ? -6.362  19.509  15.733 1.00 34.59 ? 83  ASN D CB  1 
ATOM   5585 C CG  . ASN D 2 83  ? -5.077  19.951  15.055 1.00 47.76 ? 83  ASN D CG  1 
ATOM   5586 O OD1 . ASN D 2 83  ? -4.026  20.064  15.695 1.00 45.92 ? 83  ASN D OD1 1 
ATOM   5587 N ND2 . ASN D 2 83  ? -5.154  20.203  13.751 1.00 54.27 ? 83  ASN D ND2 1 
ATOM   5588 N N   . SER D 2 84  ? -7.697  19.099  18.524 1.00 29.71 ? 84  SER D N   1 
ATOM   5589 C CA  . SER D 2 84  ? -8.954  19.108  19.259 1.00 42.14 ? 84  SER D CA  1 
ATOM   5590 C C   . SER D 2 84  ? -9.315  17.753  19.844 1.00 41.13 ? 84  SER D C   1 
ATOM   5591 O O   . SER D 2 84  ? -10.280 17.120  19.412 1.00 40.99 ? 84  SER D O   1 
ATOM   5592 C CB  . SER D 2 84  ? -10.087 19.620  18.374 1.00 45.52 ? 84  SER D CB  1 
ATOM   5593 O OG  . SER D 2 84  ? -9.967  21.018  18.181 1.00 50.66 ? 84  SER D OG  1 
ATOM   5594 N N   . LEU D 2 85  ? -8.537  17.313  20.828 1.00 38.20 ? 85  LEU D N   1 
ATOM   5595 C CA  . LEU D 2 85  ? -8.773  16.018  21.445 1.00 41.21 ? 85  LEU D CA  1 
ATOM   5596 C C   . LEU D 2 85  ? -9.922  16.069  22.438 1.00 33.87 ? 85  LEU D C   1 
ATOM   5597 O O   . LEU D 2 85  ? -10.006 16.968  23.274 1.00 33.61 ? 85  LEU D O   1 
ATOM   5598 C CB  . LEU D 2 85  ? -7.504  15.487  22.114 1.00 38.12 ? 85  LEU D CB  1 
ATOM   5599 C CG  . LEU D 2 85  ? -6.696  14.516  21.252 1.00 35.99 ? 85  LEU D CG  1 
ATOM   5600 C CD1 . LEU D 2 85  ? -6.091  15.214  20.053 1.00 32.34 ? 85  LEU D CD1 1 
ATOM   5601 C CD2 . LEU D 2 85  ? -5.620  13.849  22.076 1.00 35.91 ? 85  LEU D CD2 1 
ATOM   5602 N N   . GLN D 2 86  ? -10.819 15.099  22.332 1.00 31.95 ? 86  GLN D N   1 
ATOM   5603 C CA  . GLN D 2 86  ? -11.883 14.975  23.311 1.00 37.16 ? 86  GLN D CA  1 
ATOM   5604 C C   . GLN D 2 86  ? -11.527 13.832  24.241 1.00 35.20 ? 86  GLN D C   1 
ATOM   5605 O O   . GLN D 2 86  ? -10.589 13.080  23.991 1.00 35.20 ? 86  GLN D O   1 
ATOM   5606 C CB  . GLN D 2 86  ? -13.241 14.728  22.640 1.00 34.88 ? 86  GLN D CB  1 
ATOM   5607 C CG  . GLN D 2 86  ? -13.584 15.701  21.499 1.00 43.68 ? 86  GLN D CG  1 
ATOM   5608 C CD  . GLN D 2 86  ? -13.377 17.165  21.876 1.00 50.10 ? 86  GLN D CD  1 
ATOM   5609 O OE1 . GLN D 2 86  ? -13.678 17.591  22.995 1.00 45.13 ? 86  GLN D OE1 1 
ATOM   5610 N NE2 . GLN D 2 86  ? -12.838 17.936  20.941 1.00 53.30 ? 86  GLN D NE2 1 
ATOM   5611 N N   . SER D 2 87  ? -12.283 13.716  25.316 1.00 35.70 ? 87  SER D N   1 
ATOM   5612 C CA  . SER D 2 87  ? -12.095 12.662  26.284 1.00 31.64 ? 87  SER D CA  1 
ATOM   5613 C C   . SER D 2 87  ? -11.910 11.287  25.641 1.00 29.81 ? 87  SER D C   1 
ATOM   5614 O O   . SER D 2 87  ? -11.006 10.549  26.012 1.00 31.66 ? 87  SER D O   1 
ATOM   5615 C CB  . SER D 2 87  ? -13.277 12.643  27.249 1.00 23.74 ? 87  SER D CB  1 
ATOM   5616 O OG  . SER D 2 87  ? -13.014 11.773  28.333 1.00 46.74 ? 87  SER D OG  1 
ATOM   5617 N N   . ASN D 2 88  ? -12.730 10.951  24.654 1.00 27.85 ? 88  ASN D N   1 
ATOM   5618 C CA  . ASN D 2 88  ? -12.616 9.622   24.050 1.00 34.11 ? 88  ASN D CA  1 
ATOM   5619 C C   . ASN D 2 88  ? -11.453 9.442   23.071 1.00 36.55 ? 88  ASN D C   1 
ATOM   5620 O O   . ASN D 2 88  ? -11.388 8.440   22.369 1.00 33.91 ? 88  ASN D O   1 
ATOM   5621 C CB  . ASN D 2 88  ? -13.935 9.154   23.411 1.00 22.71 ? 88  ASN D CB  1 
ATOM   5622 C CG  . ASN D 2 88  ? -14.350 9.994   22.221 1.00 39.68 ? 88  ASN D CG  1 
ATOM   5623 O OD1 . ASN D 2 88  ? -13.574 10.797  21.690 1.00 44.51 ? 88  ASN D OD1 1 
ATOM   5624 N ND2 . ASN D 2 88  ? -15.592 9.813   21.800 1.00 45.62 ? 88  ASN D ND2 1 
ATOM   5625 N N   . ASP D 2 89  ? -10.550 10.413  23.009 1.00 31.73 ? 89  ASP D N   1 
ATOM   5626 C CA  . ASP D 2 89  ? -9.352  10.260  22.194 1.00 30.60 ? 89  ASP D CA  1 
ATOM   5627 C C   . ASP D 2 89  ? -8.226  9.706   23.071 1.00 30.54 ? 89  ASP D C   1 
ATOM   5628 O O   . ASP D 2 89  ? -7.094  9.496   22.612 1.00 19.12 ? 89  ASP D O   1 
ATOM   5629 C CB  . ASP D 2 89  ? -8.965  11.580  21.513 1.00 33.87 ? 89  ASP D CB  1 
ATOM   5630 C CG  . ASP D 2 89  ? -9.885  11.926  20.352 1.00 32.34 ? 89  ASP D CG  1 
ATOM   5631 O OD1 . ASP D 2 89  ? -10.220 11.013  19.573 1.00 33.15 ? 89  ASP D OD1 1 
ATOM   5632 O OD2 . ASP D 2 89  ? -10.288 13.103  20.219 1.00 35.46 ? 89  ASP D OD2 1 
ATOM   5633 N N   . THR D 2 90  ? -8.568  9.472   24.338 1.00 25.20 ? 90  THR D N   1 
ATOM   5634 C CA  . THR D 2 90  ? -7.716  8.754   25.273 1.00 21.44 ? 90  THR D CA  1 
ATOM   5635 C C   . THR D 2 90  ? -7.500  7.363   24.716 1.00 17.81 ? 90  THR D C   1 
ATOM   5636 O O   . THR D 2 90  ? -8.461  6.632   24.494 1.00 20.63 ? 90  THR D O   1 
ATOM   5637 C CB  . THR D 2 90  ? -8.391  8.671   26.675 1.00 21.40 ? 90  THR D CB  1 
ATOM   5638 O OG1 . THR D 2 90  ? -8.380  9.966   27.281 1.00 34.07 ? 90  THR D OG1 1 
ATOM   5639 C CG2 . THR D 2 90  ? -7.661  7.715   27.592 1.00 14.81 ? 90  THR D CG2 1 
ATOM   5640 N N   . ALA D 2 91  ? -6.241  7.009   24.477 1.00 19.56 ? 91  ALA D N   1 
ATOM   5641 C CA  . ALA D 2 91  ? -5.904  5.752   23.823 1.00 22.84 ? 91  ALA D CA  1 
ATOM   5642 C C   . ALA D 2 91  ? -4.407  5.517   23.836 1.00 20.97 ? 91  ALA D C   1 
ATOM   5643 O O   . ALA D 2 91  ? -3.638  6.404   24.204 1.00 21.19 ? 91  ALA D O   1 
ATOM   5644 C CB  . ALA D 2 91  ? -6.426  5.756   22.360 1.00 19.51 ? 91  ALA D CB  1 
ATOM   5645 N N   . ILE D 2 92  ? -3.991  4.318   23.436 1.00 15.39 ? 92  ILE D N   1 
ATOM   5646 C CA  . ILE D 2 92  ? -2.581  4.088   23.173 1.00 19.64 ? 92  ILE D CA  1 
ATOM   5647 C C   . ILE D 2 92  ? -2.342  4.273   21.675 1.00 28.19 ? 92  ILE D C   1 
ATOM   5648 O O   . ILE D 2 92  ? -2.970  3.585   20.857 1.00 23.18 ? 92  ILE D O   1 
ATOM   5649 C CB  . ILE D 2 92  ? -2.107  2.698   23.620 1.00 18.01 ? 92  ILE D CB  1 
ATOM   5650 C CG1 . ILE D 2 92  ? -2.344  2.510   25.122 1.00 32.14 ? 92  ILE D CG1 1 
ATOM   5651 C CG2 . ILE D 2 92  ? -0.637  2.520   23.301 1.00 15.22 ? 92  ILE D CG2 1 
ATOM   5652 C CD1 . ILE D 2 92  ? -2.102  1.091   25.621 1.00 30.01 ? 92  ILE D CD1 1 
ATOM   5653 N N   . TYR D 2 93  ? -1.443  5.205   21.332 1.00 22.56 ? 93  TYR D N   1 
ATOM   5654 C CA  . TYR D 2 93  ? -1.105  5.513   19.938 1.00 20.24 ? 93  TYR D CA  1 
ATOM   5655 C C   . TYR D 2 93  ? 0.180   4.833   19.511 1.00 17.35 ? 93  TYR D C   1 
ATOM   5656 O O   . TYR D 2 93  ? 1.193   4.972   20.180 1.00 21.06 ? 93  TYR D O   1 
ATOM   5657 C CB  . TYR D 2 93  ? -1.005  7.031   19.741 1.00 15.66 ? 93  TYR D CB  1 
ATOM   5658 C CG  . TYR D 2 93  ? -2.354  7.710   19.852 1.00 20.82 ? 93  TYR D CG  1 
ATOM   5659 C CD1 . TYR D 2 93  ? -2.931  7.964   21.092 1.00 24.30 ? 93  TYR D CD1 1 
ATOM   5660 C CD2 . TYR D 2 93  ? -3.070  8.056   18.717 1.00 20.10 ? 93  TYR D CD2 1 
ATOM   5661 C CE1 . TYR D 2 93  ? -4.167  8.562   21.190 1.00 20.68 ? 93  TYR D CE1 1 
ATOM   5662 C CE2 . TYR D 2 93  ? -4.299  8.645   18.807 1.00 17.18 ? 93  TYR D CE2 1 
ATOM   5663 C CZ  . TYR D 2 93  ? -4.847  8.895   20.040 1.00 21.58 ? 93  TYR D CZ  1 
ATOM   5664 O OH  . TYR D 2 93  ? -6.082  9.487   20.108 1.00 23.55 ? 93  TYR D OH  1 
ATOM   5665 N N   . TYR D 2 94  ? 0.130   4.087   18.412 1.00 16.73 ? 94  TYR D N   1 
ATOM   5666 C CA  . TYR D 2 94  ? 1.309   3.378   17.899 1.00 22.35 ? 94  TYR D CA  1 
ATOM   5667 C C   . TYR D 2 94  ? 1.726   3.914   16.539 1.00 23.70 ? 94  TYR D C   1 
ATOM   5668 O O   . TYR D 2 94  ? 0.883   4.284   15.714 1.00 20.73 ? 94  TYR D O   1 
ATOM   5669 C CB  . TYR D 2 94  ? 1.048   1.869   17.709 1.00 16.82 ? 94  TYR D CB  1 
ATOM   5670 C CG  . TYR D 2 94  ? 0.599   1.110   18.933 1.00 18.68 ? 94  TYR D CG  1 
ATOM   5671 C CD1 . TYR D 2 94  ? 1.514   0.436   19.729 1.00 20.53 ? 94  TYR D CD1 1 
ATOM   5672 C CD2 . TYR D 2 94  ? -0.739  1.050   19.283 1.00 19.77 ? 94  TYR D CD2 1 
ATOM   5673 C CE1 . TYR D 2 94  ? 1.114   -0.266  20.844 1.00 17.71 ? 94  TYR D CE1 1 
ATOM   5674 C CE2 . TYR D 2 94  ? -1.147  0.348   20.396 1.00 24.52 ? 94  TYR D CE2 1 
ATOM   5675 C CZ  . TYR D 2 94  ? -0.215  -0.307  21.174 1.00 21.04 ? 94  TYR D CZ  1 
ATOM   5676 O OH  . TYR D 2 94  ? -0.621  -1.000  22.289 1.00 25.21 ? 94  TYR D OH  1 
ATOM   5677 N N   . CYS D 2 95  ? 3.027   3.930   16.292 1.00 18.69 ? 95  CYS D N   1 
ATOM   5678 C CA  . CYS D 2 95  ? 3.504   4.021   14.927 1.00 23.80 ? 95  CYS D CA  1 
ATOM   5679 C C   . CYS D 2 95  ? 3.896   2.605   14.496 1.00 24.25 ? 95  CYS D C   1 
ATOM   5680 O O   . CYS D 2 95  ? 4.280   1.786   15.335 1.00 20.98 ? 95  CYS D O   1 
ATOM   5681 C CB  . CYS D 2 95  ? 4.656   5.030   14.783 1.00 18.84 ? 95  CYS D CB  1 
ATOM   5682 S SG  . CYS D 2 95  ? 6.239   4.623   15.577 1.00 27.71 ? 95  CYS D SG  1 
ATOM   5683 N N   . ALA D 2 96  ? 3.777   2.314   13.205 1.00 19.45 ? 96  ALA D N   1 
ATOM   5684 C CA  . ALA D 2 96  ? 4.036   0.969   12.708 1.00 21.90 ? 96  ALA D CA  1 
ATOM   5685 C C   . ALA D 2 96  ? 4.624   0.943   11.281 1.00 21.23 ? 96  ALA D C   1 
ATOM   5686 O O   . ALA D 2 96  ? 4.395   1.855   10.479 1.00 22.53 ? 96  ALA D O   1 
ATOM   5687 C CB  . ALA D 2 96  ? 2.758   0.139   12.783 1.00 18.16 ? 96  ALA D CB  1 
ATOM   5688 N N   . ARG D 2 97  ? 5.395   -0.100  10.978 1.00 24.65 ? 97  ARG D N   1 
ATOM   5689 C CA  . ARG D 2 97  ? 5.952   -0.297  9.640  1.00 19.83 ? 97  ARG D CA  1 
ATOM   5690 C C   . ARG D 2 97  ? 5.482   -1.627  9.072  1.00 18.82 ? 97  ARG D C   1 
ATOM   5691 O O   . ARG D 2 97  ? 5.452   -2.632  9.781  1.00 23.72 ? 97  ARG D O   1 
ATOM   5692 C CB  . ARG D 2 97  ? 7.483   -0.277  9.660  1.00 21.28 ? 97  ARG D CB  1 
ATOM   5693 C CG  . ARG D 2 97  ? 8.115   0.279   8.367  1.00 24.78 ? 97  ARG D CG  1 
ATOM   5694 C CD  . ARG D 2 97  ? 9.459   -0.362  8.062  1.00 17.83 ? 97  ARG D CD  1 
ATOM   5695 N NE  . ARG D 2 97  ? 9.263   -1.725  7.604  1.00 23.73 ? 97  ARG D NE  1 
ATOM   5696 C CZ  . ARG D 2 97  ? 10.225  -2.532  7.173  1.00 21.76 ? 97  ARG D CZ  1 
ATOM   5697 N NH1 . ARG D 2 97  ? 11.479  -2.122  7.143  1.00 23.33 ? 97  ARG D NH1 1 
ATOM   5698 N NH2 . ARG D 2 97  ? 9.927   -3.755  6.763  1.00 19.48 ? 97  ARG D NH2 1 
ATOM   5699 N N   . ALA D 2 98  ? 5.113   -1.628  7.795  1.00 17.69 ? 98  ALA D N   1 
ATOM   5700 C CA  . ALA D 2 98  ? 4.716   -2.852  7.114  1.00 19.28 ? 98  ALA D CA  1 
ATOM   5701 C C   . ALA D 2 98  ? 5.951   -3.653  6.695  1.00 20.69 ? 98  ALA D C   1 
ATOM   5702 O O   . ALA D 2 98  ? 7.058   -3.130  6.690  1.00 20.27 ? 98  ALA D O   1 
ATOM   5703 C CB  . ALA D 2 98  ? 3.838   -2.530  5.916  1.00 19.98 ? 98  ALA D CB  1 
ATOM   5704 N N   . LEU D 2 99  ? 5.762   -4.926  6.356  1.00 24.91 ? 99  LEU D N   1 
ATOM   5705 C CA  . LEU D 2 99  ? 6.848   -5.752  5.825  1.00 27.05 ? 99  LEU D CA  1 
ATOM   5706 C C   . LEU D 2 99  ? 7.338   -5.176  4.506  1.00 30.31 ? 99  LEU D C   1 
ATOM   5707 O O   . LEU D 2 99  ? 8.493   -5.344  4.107  1.00 30.34 ? 99  LEU D O   1 
ATOM   5708 C CB  . LEU D 2 99  ? 6.332   -7.156  5.540  1.00 30.59 ? 99  LEU D CB  1 
ATOM   5709 C CG  . LEU D 2 99  ? 6.642   -8.271  6.528  1.00 33.34 ? 99  LEU D CG  1 
ATOM   5710 C CD1 . LEU D 2 99  ? 5.957   -9.541  6.050  1.00 27.88 ? 99  LEU D CD1 1 
ATOM   5711 C CD2 . LEU D 2 99  ? 8.138   -8.479  6.643  1.00 29.40 ? 99  LEU D CD2 1 
ATOM   5712 N N   . THR D 2 100 ? 6.426   -4.482  3.840  1.00 34.02 ? 100 THR D N   1 
ATOM   5713 C CA  . THR D 2 100 ? 6.588   -4.096  2.454  1.00 32.82 ? 100 THR D CA  1 
ATOM   5714 C C   . THR D 2 100 ? 6.320   -2.603  2.284  1.00 32.36 ? 100 THR D C   1 
ATOM   5715 O O   . THR D 2 100 ? 5.452   -2.048  2.964  1.00 33.20 ? 100 THR D O   1 
ATOM   5716 C CB  . THR D 2 100 ? 5.583   -4.859  1.607  1.00 35.85 ? 100 THR D CB  1 
ATOM   5717 O OG1 . THR D 2 100 ? 5.855   -6.264  1.682  1.00 41.20 ? 100 THR D OG1 1 
ATOM   5718 C CG2 . THR D 2 100 ? 5.716   -4.444  0.241  1.00 33.25 ? 100 THR D CG2 1 
ATOM   5719 N N   . TYR D 2 101 ? 7.056   -1.948  1.388  1.00 25.06 ? 101 TYR D N   1 
ATOM   5720 C CA  . TYR D 2 101 ? 6.926   -0.505  1.240  1.00 27.89 ? 101 TYR D CA  1 
ATOM   5721 C C   . TYR D 2 101 ? 5.494   -0.036  0.971  1.00 26.72 ? 101 TYR D C   1 
ATOM   5722 O O   . TYR D 2 101 ? 5.103   1.038   1.420  1.00 28.24 ? 101 TYR D O   1 
ATOM   5723 C CB  . TYR D 2 101 ? 7.901   0.050   0.183  1.00 22.59 ? 101 TYR D CB  1 
ATOM   5724 C CG  . TYR D 2 101 ? 7.509   -0.166  -1.258 1.00 25.78 ? 101 TYR D CG  1 
ATOM   5725 C CD1 . TYR D 2 101 ? 6.595   0.671   -1.893 1.00 24.51 ? 101 TYR D CD1 1 
ATOM   5726 C CD2 . TYR D 2 101 ? 8.087   -1.190  -2.003 1.00 27.48 ? 101 TYR D CD2 1 
ATOM   5727 C CE1 . TYR D 2 101 ? 6.249   0.468   -3.228 1.00 32.74 ? 101 TYR D CE1 1 
ATOM   5728 C CE2 . TYR D 2 101 ? 7.751   -1.396  -3.332 1.00 20.86 ? 101 TYR D CE2 1 
ATOM   5729 C CZ  . TYR D 2 101 ? 6.833   -0.574  -3.943 1.00 28.61 ? 101 TYR D CZ  1 
ATOM   5730 O OH  . TYR D 2 101 ? 6.505   -0.789  -5.271 1.00 25.21 ? 101 TYR D OH  1 
ATOM   5731 N N   . TYR D 2 102 ? 4.721   -0.846  0.253  1.00 26.63 ? 102 TYR D N   1 
ATOM   5732 C CA  . TYR D 2 102 ? 3.386   -0.452  -0.202 1.00 25.72 ? 102 TYR D CA  1 
ATOM   5733 C C   . TYR D 2 102 ? 2.247   -1.081  0.619  1.00 21.51 ? 102 TYR D C   1 
ATOM   5734 O O   . TYR D 2 102 ? 1.076   -0.713  0.467  1.00 20.31 ? 102 TYR D O   1 
ATOM   5735 C CB  . TYR D 2 102 ? 3.212   -0.814  -1.687 1.00 19.09 ? 102 TYR D CB  1 
ATOM   5736 C CG  . TYR D 2 102 ? 3.405   -2.289  -1.962 1.00 17.56 ? 102 TYR D CG  1 
ATOM   5737 C CD1 . TYR D 2 102 ? 2.398   -3.201  -1.688 1.00 17.02 ? 102 TYR D CD1 1 
ATOM   5738 C CD2 . TYR D 2 102 ? 4.603   -2.770  -2.471 1.00 20.68 ? 102 TYR D CD2 1 
ATOM   5739 C CE1 . TYR D 2 102 ? 2.568   -4.545  -1.913 1.00 18.95 ? 102 TYR D CE1 1 
ATOM   5740 C CE2 . TYR D 2 102 ? 4.779   -4.124  -2.714 1.00 25.80 ? 102 TYR D CE2 1 
ATOM   5741 C CZ  . TYR D 2 102 ? 3.754   -5.008  -2.428 1.00 24.66 ? 102 TYR D CZ  1 
ATOM   5742 O OH  . TYR D 2 102 ? 3.917   -6.361  -2.655 1.00 21.47 ? 102 TYR D OH  1 
ATOM   5743 N N   . ASP D 2 103 ? 2.583   -2.041  1.467  1.00 16.09 ? 103 ASP D N   1 
ATOM   5744 C CA  . ASP D 2 103 ? 1.552   -2.872  2.092  1.00 25.02 ? 103 ASP D CA  1 
ATOM   5745 C C   . ASP D 2 103 ? 1.106   -2.412  3.487  1.00 25.49 ? 103 ASP D C   1 
ATOM   5746 O O   . ASP D 2 103 ? 1.565   -1.398  4.004  1.00 29.72 ? 103 ASP D O   1 
ATOM   5747 C CB  . ASP D 2 103 ? 1.992   -4.341  2.128  1.00 26.21 ? 103 ASP D CB  1 
ATOM   5748 C CG  . ASP D 2 103 ? 0.826   -5.302  1.936  1.00 34.05 ? 103 ASP D CG  1 
ATOM   5749 O OD1 . ASP D 2 103 ? -0.334  -4.878  2.161  1.00 34.41 ? 103 ASP D OD1 1 
ATOM   5750 O OD2 . ASP D 2 103 ? 1.059   -6.476  1.564  1.00 26.31 ? 103 ASP D OD2 1 
ATOM   5751 N N   . TYR D 2 104 ? 0.205   -3.175  4.090  1.00 25.26 ? 104 TYR D N   1 
ATOM   5752 C CA  . TYR D 2 104 ? -0.383  -2.793  5.361  1.00 24.33 ? 104 TYR D CA  1 
ATOM   5753 C C   . TYR D 2 104 ? -0.242  -3.869  6.440  1.00 24.46 ? 104 TYR D C   1 
ATOM   5754 O O   . TYR D 2 104 ? -0.933  -3.824  7.453  1.00 25.38 ? 104 TYR D O   1 
ATOM   5755 C CB  . TYR D 2 104 ? -1.860  -2.451  5.172  1.00 19.56 ? 104 TYR D CB  1 
ATOM   5756 C CG  . TYR D 2 104 ? -2.133  -1.185  4.400  1.00 23.11 ? 104 TYR D CG  1 
ATOM   5757 C CD1 . TYR D 2 104 ? -1.928  -1.128  3.023  1.00 24.18 ? 104 TYR D CD1 1 
ATOM   5758 C CD2 . TYR D 2 104 ? -2.636  -0.054  5.035  1.00 20.92 ? 104 TYR D CD2 1 
ATOM   5759 C CE1 . TYR D 2 104 ? -2.192  0.020   2.308  1.00 22.43 ? 104 TYR D CE1 1 
ATOM   5760 C CE2 . TYR D 2 104 ? -2.906  1.109   4.321  1.00 24.85 ? 104 TYR D CE2 1 
ATOM   5761 C CZ  . TYR D 2 104 ? -2.678  1.136   2.953  1.00 29.05 ? 104 TYR D CZ  1 
ATOM   5762 O OH  . TYR D 2 104 ? -2.931  2.272   2.221  1.00 28.94 ? 104 TYR D OH  1 
ATOM   5763 N N   . GLU D 2 105 ? 0.621   -4.852  6.218  1.00 23.72 ? 105 GLU D N   1 
ATOM   5764 C CA  . GLU D 2 105 ? 0.787   -5.900  7.218  1.00 23.46 ? 105 GLU D CA  1 
ATOM   5765 C C   . GLU D 2 105 ? 1.895   -5.501  8.193  1.00 27.67 ? 105 GLU D C   1 
ATOM   5766 O O   . GLU D 2 105 ? 3.077   -5.464  7.842  1.00 27.74 ? 105 GLU D O   1 
ATOM   5767 C CB  . GLU D 2 105 ? 0.971   -7.296  6.594  1.00 21.55 ? 105 GLU D CB  1 
ATOM   5768 C CG  . GLU D 2 105 ? 2.349   -7.643  6.063  1.00 37.45 ? 105 GLU D CG  1 
ATOM   5769 C CD  . GLU D 2 105 ? 2.695   -6.965  4.748  1.00 34.55 ? 105 GLU D CD  1 
ATOM   5770 O OE1 . GLU D 2 105 ? 2.749   -7.680  3.727  1.00 36.48 ? 105 GLU D OE1 1 
ATOM   5771 O OE2 . GLU D 2 105 ? 2.941   -5.735  4.736  1.00 31.68 ? 105 GLU D OE2 1 
ATOM   5772 N N   . PHE D 2 106 ? 1.483   -5.163  9.412  1.00 21.08 ? 106 PHE D N   1 
ATOM   5773 C CA  . PHE D 2 106 ? 2.336   -4.442  10.345 1.00 22.87 ? 106 PHE D CA  1 
ATOM   5774 C C   . PHE D 2 106 ? 3.244   -5.368  11.141 1.00 22.53 ? 106 PHE D C   1 
ATOM   5775 O O   . PHE D 2 106 ? 2.865   -5.882  12.186 1.00 21.43 ? 106 PHE D O   1 
ATOM   5776 C CB  . PHE D 2 106 ? 1.490   -3.560  11.265 1.00 17.48 ? 106 PHE D CB  1 
ATOM   5777 C CG  . PHE D 2 106 ? 0.599   -2.601  10.518 1.00 17.51 ? 106 PHE D CG  1 
ATOM   5778 C CD1 . PHE D 2 106 ? -0.773  -2.661  10.646 1.00 16.78 ? 106 PHE D CD1 1 
ATOM   5779 C CD2 . PHE D 2 106 ? 1.142   -1.638  9.677  1.00 25.32 ? 106 PHE D CD2 1 
ATOM   5780 C CE1 . PHE D 2 106 ? -1.590  -1.769  9.961  1.00 21.17 ? 106 PHE D CE1 1 
ATOM   5781 C CE2 . PHE D 2 106 ? 0.326   -0.736  8.981  1.00 23.83 ? 106 PHE D CE2 1 
ATOM   5782 C CZ  . PHE D 2 106 ? -1.037  -0.808  9.122  1.00 22.00 ? 106 PHE D CZ  1 
ATOM   5783 N N   . ALA D 2 107 ? 4.454   -5.558  10.630 1.00 20.52 ? 107 ALA D N   1 
ATOM   5784 C CA  . ALA D 2 107 ? 5.420   -6.435  11.260 1.00 19.68 ? 107 ALA D CA  1 
ATOM   5785 C C   . ALA D 2 107 ? 6.235   -5.729  12.357 1.00 23.96 ? 107 ALA D C   1 
ATOM   5786 O O   . ALA D 2 107 ? 6.739   -6.376  13.266 1.00 26.80 ? 107 ALA D O   1 
ATOM   5787 C CB  . ALA D 2 107 ? 6.329   -7.037  10.203 1.00 16.23 ? 107 ALA D CB  1 
ATOM   5788 N N   . TYR D 2 108 ? 6.360   -4.408  12.271 1.00 22.99 ? 108 TYR D N   1 
ATOM   5789 C CA  . TYR D 2 108 ? 7.167   -3.645  13.232 1.00 22.64 ? 108 TYR D CA  1 
ATOM   5790 C C   . TYR D 2 108 ? 6.371   -2.527  13.895 1.00 21.08 ? 108 TYR D C   1 
ATOM   5791 O O   . TYR D 2 108 ? 5.771   -1.692  13.214 1.00 21.37 ? 108 TYR D O   1 
ATOM   5792 C CB  . TYR D 2 108 ? 8.459   -3.114  12.571 1.00 26.21 ? 108 TYR D CB  1 
ATOM   5793 C CG  . TYR D 2 108 ? 9.263   -4.210  11.888 1.00 31.45 ? 108 TYR D CG  1 
ATOM   5794 C CD1 . TYR D 2 108 ? 9.135   -4.449  10.511 1.00 29.71 ? 108 TYR D CD1 1 
ATOM   5795 C CD2 . TYR D 2 108 ? 10.116  -5.034  12.622 1.00 23.83 ? 108 TYR D CD2 1 
ATOM   5796 C CE1 . TYR D 2 108 ? 9.857   -5.461  9.885  1.00 24.17 ? 108 TYR D CE1 1 
ATOM   5797 C CE2 . TYR D 2 108 ? 10.829  -6.047  12.016 1.00 24.22 ? 108 TYR D CE2 1 
ATOM   5798 C CZ  . TYR D 2 108 ? 10.699  -6.259  10.645 1.00 37.69 ? 108 TYR D CZ  1 
ATOM   5799 O OH  . TYR D 2 108 ? 11.414  -7.273  10.043 1.00 42.42 ? 108 TYR D OH  1 
ATOM   5800 N N   . TRP D 2 109 ? 6.350   -2.524  15.229 1.00 30.50 ? 109 TRP D N   1 
ATOM   5801 C CA  . TRP D 2 109 ? 5.575   -1.522  15.978 1.00 24.50 ? 109 TRP D CA  1 
ATOM   5802 C C   . TRP D 2 109 ? 6.437   -0.691  16.898 1.00 17.17 ? 109 TRP D C   1 
ATOM   5803 O O   . TRP D 2 109 ? 7.512   -1.128  17.307 1.00 26.51 ? 109 TRP D O   1 
ATOM   5804 C CB  . TRP D 2 109 ? 4.487   -2.189  16.809 1.00 19.28 ? 109 TRP D CB  1 
ATOM   5805 C CG  . TRP D 2 109 ? 3.458   -2.899  15.988 1.00 16.19 ? 109 TRP D CG  1 
ATOM   5806 C CD1 . TRP D 2 109 ? 3.644   -4.015  15.227 1.00 17.48 ? 109 TRP D CD1 1 
ATOM   5807 C CD2 . TRP D 2 109 ? 2.072   -2.553  15.866 1.00 15.42 ? 109 TRP D CD2 1 
ATOM   5808 N NE1 . TRP D 2 109 ? 2.461   -4.387  14.645 1.00 18.95 ? 109 TRP D NE1 1 
ATOM   5809 C CE2 . TRP D 2 109 ? 1.480   -3.504  15.021 1.00 20.32 ? 109 TRP D CE2 1 
ATOM   5810 C CE3 . TRP D 2 109 ? 1.275   -1.538  16.401 1.00 20.89 ? 109 TRP D CE3 1 
ATOM   5811 C CZ2 . TRP D 2 109 ? 0.129   -3.461  14.679 1.00 23.32 ? 109 TRP D CZ2 1 
ATOM   5812 C CZ3 . TRP D 2 109 ? -0.071  -1.493  16.062 1.00 21.34 ? 109 TRP D CZ3 1 
ATOM   5813 C CH2 . TRP D 2 109 ? -0.628  -2.449  15.208 1.00 24.25 ? 109 TRP D CH2 1 
ATOM   5814 N N   . GLY D 2 110 ? 5.962   0.510   17.215 1.00 20.29 ? 110 GLY D N   1 
ATOM   5815 C CA  . GLY D 2 110 ? 6.550   1.316   18.270 1.00 19.29 ? 110 GLY D CA  1 
ATOM   5816 C C   . GLY D 2 110 ? 6.076   0.766   19.603 1.00 22.10 ? 110 GLY D C   1 
ATOM   5817 O O   . GLY D 2 110 ? 5.228   -0.139  19.630 1.00 21.25 ? 110 GLY D O   1 
ATOM   5818 N N   . GLN D 2 111 ? 6.593   1.294   20.708 1.00 17.69 ? 111 GLN D N   1 
ATOM   5819 C CA  . GLN D 2 111 ? 6.189   0.775   22.017 1.00 18.29 ? 111 GLN D CA  1 
ATOM   5820 C C   . GLN D 2 111 ? 4.830   1.315   22.438 1.00 19.36 ? 111 GLN D C   1 
ATOM   5821 O O   . GLN D 2 111 ? 4.223   0.825   23.395 1.00 17.96 ? 111 GLN D O   1 
ATOM   5822 C CB  . GLN D 2 111 ? 7.245   1.036   23.101 1.00 8.78  ? 111 GLN D CB  1 
ATOM   5823 C CG  . GLN D 2 111 ? 7.250   2.428   23.658 1.00 14.49 ? 111 GLN D CG  1 
ATOM   5824 C CD  . GLN D 2 111 ? 8.151   3.388   22.899 1.00 21.96 ? 111 GLN D CD  1 
ATOM   5825 O OE1 . GLN D 2 111 ? 8.615   3.113   21.778 1.00 26.17 ? 111 GLN D OE1 1 
ATOM   5826 N NE2 . GLN D 2 111 ? 8.406   4.532   23.515 1.00 21.55 ? 111 GLN D NE2 1 
ATOM   5827 N N   . GLY D 2 112 ? 4.349   2.315   21.703 1.00 22.48 ? 112 GLY D N   1 
ATOM   5828 C CA  . GLY D 2 112 ? 3.058   2.917   21.979 1.00 23.59 ? 112 GLY D CA  1 
ATOM   5829 C C   . GLY D 2 112 ? 3.174   4.058   22.974 1.00 25.52 ? 112 GLY D C   1 
ATOM   5830 O O   . GLY D 2 112 ? 4.017   4.038   23.867 1.00 27.46 ? 112 GLY D O   1 
ATOM   5831 N N   . THR D 2 113 ? 2.333   5.069   22.805 1.00 25.21 ? 113 THR D N   1 
ATOM   5832 C CA  . THR D 2 113 ? 2.330   6.219   23.693 1.00 20.43 ? 113 THR D CA  1 
ATOM   5833 C C   . THR D 2 113 ? 0.951   6.351   24.293 1.00 19.29 ? 113 THR D C   1 
ATOM   5834 O O   . THR D 2 113 ? 0.000   6.674   23.566 1.00 21.99 ? 113 THR D O   1 
ATOM   5835 C CB  . THR D 2 113 ? 2.642   7.508   22.923 1.00 22.89 ? 113 THR D CB  1 
ATOM   5836 O OG1 . THR D 2 113 ? 3.936   7.398   22.313 1.00 29.89 ? 113 THR D OG1 1 
ATOM   5837 C CG2 . THR D 2 113 ? 2.613   8.712   23.853 1.00 18.98 ? 113 THR D CG2 1 
ATOM   5838 N N   . LEU D 2 114 ? 0.831   6.087   25.600 1.00 18.46 ? 114 LEU D N   1 
ATOM   5839 C CA  . LEU D 2 114 ? -0.460  6.220   26.293 1.00 16.32 ? 114 LEU D CA  1 
ATOM   5840 C C   . LEU D 2 114 ? -0.778  7.689   26.481 1.00 19.62 ? 114 LEU D C   1 
ATOM   5841 O O   . LEU D 2 114 ? -0.041  8.426   27.143 1.00 23.72 ? 114 LEU D O   1 
ATOM   5842 C CB  . LEU D 2 114 ? -0.492  5.464   27.638 1.00 13.22 ? 114 LEU D CB  1 
ATOM   5843 C CG  . LEU D 2 114 ? -1.682  5.649   28.600 1.00 21.08 ? 114 LEU D CG  1 
ATOM   5844 C CD1 . LEU D 2 114 ? -3.024  5.563   27.892 1.00 20.23 ? 114 LEU D CD1 1 
ATOM   5845 C CD2 . LEU D 2 114 ? -1.646  4.641   29.750 1.00 20.67 ? 114 LEU D CD2 1 
ATOM   5846 N N   . VAL D 2 115 ? -1.877  8.112   25.878 1.00 22.86 ? 115 VAL D N   1 
ATOM   5847 C CA  . VAL D 2 115 ? -2.256  9.518   25.860 1.00 21.54 ? 115 VAL D CA  1 
ATOM   5848 C C   . VAL D 2 115 ? -3.577  9.694   26.602 1.00 25.76 ? 115 VAL D C   1 
ATOM   5849 O O   . VAL D 2 115 ? -4.590  9.090   26.236 1.00 25.94 ? 115 VAL D O   1 
ATOM   5850 C CB  . VAL D 2 115 ? -2.398  10.010  24.403 1.00 20.50 ? 115 VAL D CB  1 
ATOM   5851 C CG1 . VAL D 2 115 ? -2.788  11.483  24.347 1.00 26.28 ? 115 VAL D CG1 1 
ATOM   5852 C CG2 . VAL D 2 115 ? -1.104  9.757   23.634 1.00 16.64 ? 115 VAL D CG2 1 
ATOM   5853 N N   . THR D 2 116 ? -3.558  10.508  27.653 1.00 22.55 ? 116 THR D N   1 
ATOM   5854 C CA  . THR D 2 116 ? -4.752  10.744  28.450 1.00 25.45 ? 116 THR D CA  1 
ATOM   5855 C C   . THR D 2 116 ? -5.286  12.130  28.154 1.00 30.04 ? 116 THR D C   1 
ATOM   5856 O O   . THR D 2 116 ? -4.520  13.094  28.089 1.00 27.80 ? 116 THR D O   1 
ATOM   5857 C CB  . THR D 2 116 ? -4.466  10.598  29.963 1.00 25.31 ? 116 THR D CB  1 
ATOM   5858 O OG1 . THR D 2 116 ? -3.957  9.287   30.227 1.00 18.90 ? 116 THR D OG1 1 
ATOM   5859 C CG2 . THR D 2 116 ? -5.741  10.811  30.795 1.00 24.28 ? 116 THR D CG2 1 
ATOM   5860 N N   . VAL D 2 117 ? -6.596  12.218  27.936 1.00 28.77 ? 117 VAL D N   1 
ATOM   5861 C CA  . VAL D 2 117 ? -7.249  13.509  27.771 1.00 22.95 ? 117 VAL D CA  1 
ATOM   5862 C C   . VAL D 2 117 ? -8.050  13.825  29.024 1.00 30.35 ? 117 VAL D C   1 
ATOM   5863 O O   . VAL D 2 117 ? -9.017  13.135  29.353 1.00 28.87 ? 117 VAL D O   1 
ATOM   5864 C CB  . VAL D 2 117 ? -8.159  13.552  26.539 1.00 27.55 ? 117 VAL D CB  1 
ATOM   5865 C CG1 . VAL D 2 117 ? -8.754  14.943  26.364 1.00 29.33 ? 117 VAL D CG1 1 
ATOM   5866 C CG2 . VAL D 2 117 ? -7.384  13.167  25.313 1.00 27.84 ? 117 VAL D CG2 1 
ATOM   5867 N N   . SER D 2 118 ? -7.621  14.861  29.735 1.00 31.74 ? 118 SER D N   1 
ATOM   5868 C CA  . SER D 2 118 ? -8.272  15.255  30.971 1.00 26.59 ? 118 SER D CA  1 
ATOM   5869 C C   . SER D 2 118 ? -7.926  16.703  31.254 1.00 32.39 ? 118 SER D C   1 
ATOM   5870 O O   . SER D 2 118 ? -6.879  17.195  30.833 1.00 31.68 ? 118 SER D O   1 
ATOM   5871 C CB  . SER D 2 118 ? -7.808  14.368  32.136 1.00 31.19 ? 118 SER D CB  1 
ATOM   5872 O OG  . SER D 2 118 ? -8.731  14.373  33.215 1.00 35.29 ? 118 SER D OG  1 
ATOM   5873 N N   . ALA D 2 119 ? -8.824  17.389  31.954 1.00 36.52 ? 119 ALA D N   1 
ATOM   5874 C CA  . ALA D 2 119 ? -8.566  18.747  32.400 1.00 38.00 ? 119 ALA D CA  1 
ATOM   5875 C C   . ALA D 2 119 ? -7.677  18.772  33.658 1.00 41.87 ? 119 ALA D C   1 
ATOM   5876 O O   . ALA D 2 119 ? -7.120  19.811  34.019 1.00 45.48 ? 119 ALA D O   1 
ATOM   5877 C CB  . ALA D 2 119 ? -9.882  19.471  32.643 1.00 35.30 ? 119 ALA D CB  1 
ATOM   5878 N N   . ALA D 2 120 ? -7.533  17.618  34.304 1.00 30.12 ? 120 ALA D N   1 
ATOM   5879 C CA  . ALA D 2 120 ? -6.703  17.473  35.508 1.00 37.66 ? 120 ALA D CA  1 
ATOM   5880 C C   . ALA D 2 120 ? -5.218  17.863  35.355 1.00 30.45 ? 120 ALA D C   1 
ATOM   5881 O O   . ALA D 2 120 ? -4.743  18.137  34.255 1.00 32.85 ? 120 ALA D O   1 
ATOM   5882 C CB  . ALA D 2 120 ? -6.825  16.046  36.052 1.00 34.52 ? 120 ALA D CB  1 
ATOM   5883 N N   . SER D 2 121 ? -4.490  17.883  36.469 1.00 35.75 ? 121 SER D N   1 
ATOM   5884 C CA  . SER D 2 121 ? -3.062  18.206  36.446 1.00 30.51 ? 121 SER D CA  1 
ATOM   5885 C C   . SER D 2 121 ? -2.243  16.939  36.552 1.00 31.62 ? 121 SER D C   1 
ATOM   5886 O O   . SER D 2 121 ? -2.727  15.914  37.029 1.00 33.71 ? 121 SER D O   1 
ATOM   5887 C CB  . SER D 2 121 ? -2.665  19.127  37.606 1.00 32.38 ? 121 SER D CB  1 
ATOM   5888 O OG  . SER D 2 121 ? -3.476  20.282  37.669 1.00 47.10 ? 121 SER D OG  1 
ATOM   5889 N N   . THR D 2 122 ? -0.997  17.024  36.105 1.00 29.23 ? 122 THR D N   1 
ATOM   5890 C CA  . THR D 2 122 ? -0.057  15.924  36.219 1.00 31.03 ? 122 THR D CA  1 
ATOM   5891 C C   . THR D 2 122 ? 0.473   15.891  37.647 1.00 30.21 ? 122 THR D C   1 
ATOM   5892 O O   . THR D 2 122 ? 0.683   16.942  38.251 1.00 26.41 ? 122 THR D O   1 
ATOM   5893 C CB  . THR D 2 122 ? 1.085   16.093  35.213 1.00 21.28 ? 122 THR D CB  1 
ATOM   5894 O OG1 . THR D 2 122 ? 0.537   16.028  33.895 1.00 32.89 ? 122 THR D OG1 1 
ATOM   5895 C CG2 . THR D 2 122 ? 2.088   14.990  35.344 1.00 23.94 ? 122 THR D CG2 1 
ATOM   5896 N N   . LYS D 2 123 ? 0.656   14.693  38.194 1.00 22.44 ? 123 LYS D N   1 
ATOM   5897 C CA  . LYS D 2 123 ? 1.141   14.550  39.562 1.00 24.46 ? 123 LYS D CA  1 
ATOM   5898 C C   . LYS D 2 123 ? 2.022   13.316  39.719 1.00 19.81 ? 123 LYS D C   1 
ATOM   5899 O O   . LYS D 2 123 ? 1.612   12.209  39.373 1.00 19.95 ? 123 LYS D O   1 
ATOM   5900 C CB  . LYS D 2 123 ? -0.029  14.501  40.547 1.00 21.26 ? 123 LYS D CB  1 
ATOM   5901 C CG  . LYS D 2 123 ? 0.399   14.576  41.990 1.00 24.92 ? 123 LYS D CG  1 
ATOM   5902 C CD  . LYS D 2 123 ? -0.775  14.374  42.959 1.00 32.19 ? 123 LYS D CD  1 
ATOM   5903 C CE  . LYS D 2 123 ? -0.283  14.318  44.415 1.00 33.68 ? 123 LYS D CE  1 
ATOM   5904 N NZ  . LYS D 2 123 ? 0.857   13.349  44.621 1.00 28.10 ? 123 LYS D NZ  1 
ATOM   5905 N N   . GLY D 2 124 ? 3.237   13.514  40.222 1.00 15.95 ? 124 GLY D N   1 
ATOM   5906 C CA  . GLY D 2 124 ? 4.135   12.403  40.476 1.00 16.68 ? 124 GLY D CA  1 
ATOM   5907 C C   . GLY D 2 124 ? 3.617   11.579  41.646 1.00 19.04 ? 124 GLY D C   1 
ATOM   5908 O O   . GLY D 2 124 ? 2.867   12.082  42.474 1.00 16.66 ? 124 GLY D O   1 
ATOM   5909 N N   . PRO D 2 125 ? 3.999   10.301  41.710 1.00 15.07 ? 125 PRO D N   1 
ATOM   5910 C CA  . PRO D 2 125 ? 3.493   9.445   42.780 1.00 16.59 ? 125 PRO D CA  1 
ATOM   5911 C C   . PRO D 2 125 ? 4.367   9.545   44.029 1.00 25.43 ? 125 PRO D C   1 
ATOM   5912 O O   . PRO D 2 125 ? 5.501   10.028  43.970 1.00 19.11 ? 125 PRO D O   1 
ATOM   5913 C CB  . PRO D 2 125 ? 3.632   8.043   42.181 1.00 19.36 ? 125 PRO D CB  1 
ATOM   5914 C CG  . PRO D 2 125 ? 4.839   8.148   41.282 1.00 10.99 ? 125 PRO D CG  1 
ATOM   5915 C CD  . PRO D 2 125 ? 4.832   9.558   40.742 1.00 13.32 ? 125 PRO D CD  1 
ATOM   5916 N N   . SER D 2 126 ? 3.825   9.093   45.153 1.00 21.53 ? 126 SER D N   1 
ATOM   5917 C CA  . SER D 2 126 ? 4.629   8.845   46.336 1.00 25.91 ? 126 SER D CA  1 
ATOM   5918 C C   . SER D 2 126 ? 4.864   7.345   46.375 1.00 24.23 ? 126 SER D C   1 
ATOM   5919 O O   . SER D 2 126 ? 3.959   6.570   46.043 1.00 22.68 ? 126 SER D O   1 
ATOM   5920 C CB  . SER D 2 126 ? 3.894   9.307   47.585 1.00 20.79 ? 126 SER D CB  1 
ATOM   5921 O OG  . SER D 2 126 ? 3.394   10.616  47.382 1.00 33.50 ? 126 SER D OG  1 
ATOM   5922 N N   . VAL D 2 127 ? 6.080   6.937   46.736 1.00 18.78 ? 127 VAL D N   1 
ATOM   5923 C CA  . VAL D 2 127 ? 6.406   5.520   46.808 1.00 17.88 ? 127 VAL D CA  1 
ATOM   5924 C C   . VAL D 2 127 ? 6.641   5.098   48.252 1.00 22.23 ? 127 VAL D C   1 
ATOM   5925 O O   . VAL D 2 127 ? 7.415   5.716   48.960 1.00 19.05 ? 127 VAL D O   1 
ATOM   5926 C CB  . VAL D 2 127 ? 7.630   5.190   45.964 1.00 15.59 ? 127 VAL D CB  1 
ATOM   5927 C CG1 . VAL D 2 127 ? 7.849   3.678   45.922 1.00 13.46 ? 127 VAL D CG1 1 
ATOM   5928 C CG2 . VAL D 2 127 ? 7.472   5.756   44.560 1.00 15.44 ? 127 VAL D CG2 1 
ATOM   5929 N N   . PHE D 2 128 ? 5.955   4.040   48.674 1.00 20.01 ? 128 PHE D N   1 
ATOM   5930 C CA  . PHE D 2 128 ? 6.040   3.550   50.032 1.00 13.41 ? 128 PHE D CA  1 
ATOM   5931 C C   . PHE D 2 128 ? 6.372   2.078   49.990 1.00 21.76 ? 128 PHE D C   1 
ATOM   5932 O O   . PHE D 2 128 ? 5.977   1.381   49.056 1.00 20.73 ? 128 PHE D O   1 
ATOM   5933 C CB  . PHE D 2 128 ? 4.710   3.749   50.762 1.00 18.72 ? 128 PHE D CB  1 
ATOM   5934 C CG  . PHE D 2 128 ? 4.242   5.174   50.809 1.00 16.76 ? 128 PHE D CG  1 
ATOM   5935 C CD1 . PHE D 2 128 ? 5.011   6.155   51.419 1.00 16.73 ? 128 PHE D CD1 1 
ATOM   5936 C CD2 . PHE D 2 128 ? 3.026   5.533   50.257 1.00 14.24 ? 128 PHE D CD2 1 
ATOM   5937 C CE1 . PHE D 2 128 ? 4.572   7.487   51.474 1.00 16.34 ? 128 PHE D CE1 1 
ATOM   5938 C CE2 . PHE D 2 128 ? 2.589   6.871   50.309 1.00 25.54 ? 128 PHE D CE2 1 
ATOM   5939 C CZ  . PHE D 2 128 ? 3.372   7.842   50.927 1.00 12.41 ? 128 PHE D CZ  1 
ATOM   5940 N N   . PRO D 2 129 ? 7.114   1.593   51.002 1.00 31.56 ? 129 PRO D N   1 
ATOM   5941 C CA  . PRO D 2 129 ? 7.519   0.186   51.102 1.00 20.82 ? 129 PRO D CA  1 
ATOM   5942 C C   . PRO D 2 129 ? 6.372   -0.722  51.525 1.00 20.92 ? 129 PRO D C   1 
ATOM   5943 O O   . PRO D 2 129 ? 5.607   -0.342  52.402 1.00 16.73 ? 129 PRO D O   1 
ATOM   5944 C CB  . PRO D 2 129 ? 8.545   0.217   52.239 1.00 18.91 ? 129 PRO D CB  1 
ATOM   5945 C CG  . PRO D 2 129 ? 8.095   1.355   53.095 1.00 19.18 ? 129 PRO D CG  1 
ATOM   5946 C CD  . PRO D 2 129 ? 7.654   2.394   52.118 1.00 18.92 ? 129 PRO D CD  1 
ATOM   5947 N N   . LEU D 2 130 ? 6.264   -1.903  50.922 1.00 21.31 ? 130 LEU D N   1 
ATOM   5948 C CA  . LEU D 2 130 ? 5.398   -2.946  51.460 1.00 20.53 ? 130 LEU D CA  1 
ATOM   5949 C C   . LEU D 2 130 ? 6.320   -3.984  52.062 1.00 21.51 ? 130 LEU D C   1 
ATOM   5950 O O   . LEU D 2 130 ? 6.853   -4.855  51.364 1.00 23.92 ? 130 LEU D O   1 
ATOM   5951 C CB  . LEU D 2 130 ? 4.493   -3.559  50.390 1.00 19.41 ? 130 LEU D CB  1 
ATOM   5952 C CG  . LEU D 2 130 ? 3.407   -2.657  49.784 1.00 22.29 ? 130 LEU D CG  1 
ATOM   5953 C CD1 . LEU D 2 130 ? 2.851   -3.285  48.530 1.00 25.78 ? 130 LEU D CD1 1 
ATOM   5954 C CD2 . LEU D 2 130 ? 2.276   -2.390  50.762 1.00 19.54 ? 130 LEU D CD2 1 
ATOM   5955 N N   . ALA D 2 131 ? 6.513   -3.871  53.370 1.00 21.56 ? 131 ALA D N   1 
ATOM   5956 C CA  . ALA D 2 131 ? 7.561   -4.599  54.061 1.00 21.95 ? 131 ALA D CA  1 
ATOM   5957 C C   . ALA D 2 131 ? 7.018   -5.679  54.969 1.00 27.88 ? 131 ALA D C   1 
ATOM   5958 O O   . ALA D 2 131 ? 6.031   -5.473  55.677 1.00 27.88 ? 131 ALA D O   1 
ATOM   5959 C CB  . ALA D 2 131 ? 8.395   -3.644  54.864 1.00 27.77 ? 131 ALA D CB  1 
ATOM   5960 N N   . PRO D 2 132 ? 7.684   -6.839  54.961 1.00 36.39 ? 132 PRO D N   1 
ATOM   5961 C CA  . PRO D 2 132 ? 7.416   -7.959  55.867 1.00 27.51 ? 132 PRO D CA  1 
ATOM   5962 C C   . PRO D 2 132 ? 8.005   -7.700  57.249 1.00 28.90 ? 132 PRO D C   1 
ATOM   5963 O O   . PRO D 2 132 ? 7.552   -8.313  58.218 1.00 50.44 ? 132 PRO D O   1 
ATOM   5964 C CB  . PRO D 2 132 ? 8.142   -9.117  55.195 1.00 29.02 ? 132 PRO D CB  1 
ATOM   5965 C CG  . PRO D 2 132 ? 9.297   -8.468  54.481 1.00 34.55 ? 132 PRO D CG  1 
ATOM   5966 C CD  . PRO D 2 132 ? 8.777   -7.129  54.018 1.00 29.53 ? 132 PRO D CD  1 
ATOM   5967 N N   . GLY D 2 140 ? 9.460   -20.319 54.370 1.00 29.26 ? 140 GLY D N   1 
ATOM   5968 C CA  . GLY D 2 140 ? 10.329  -19.169 54.544 1.00 29.21 ? 140 GLY D CA  1 
ATOM   5969 C C   . GLY D 2 140 ? 10.377  -18.280 53.312 1.00 29.55 ? 140 GLY D C   1 
ATOM   5970 O O   . GLY D 2 140 ? 11.449  -17.800 52.913 1.00 28.65 ? 140 GLY D O   1 
ATOM   5971 N N   . THR D 2 141 ? 9.215   -18.069 52.694 1.00 17.72 ? 141 THR D N   1 
ATOM   5972 C CA  . THR D 2 141 ? 9.109   -17.124 51.588 1.00 17.91 ? 141 THR D CA  1 
ATOM   5973 C C   . THR D 2 141 ? 8.525   -15.827 52.111 1.00 22.43 ? 141 THR D C   1 
ATOM   5974 O O   . THR D 2 141 ? 7.528   -15.824 52.817 1.00 24.01 ? 141 THR D O   1 
ATOM   5975 C CB  . THR D 2 141 ? 8.203   -17.628 50.451 1.00 24.91 ? 141 THR D CB  1 
ATOM   5976 O OG1 . THR D 2 141 ? 8.824   -18.742 49.788 1.00 27.61 ? 141 THR D OG1 1 
ATOM   5977 C CG2 . THR D 2 141 ? 7.967   -16.521 49.454 1.00 18.52 ? 141 THR D CG2 1 
ATOM   5978 N N   . ALA D 2 142 ? 9.161   -14.719 51.777 1.00 21.99 ? 142 ALA D N   1 
ATOM   5979 C CA  . ALA D 2 142 ? 8.649   -13.428 52.169 1.00 21.22 ? 142 ALA D CA  1 
ATOM   5980 C C   . ALA D 2 142 ? 8.110   -12.703 50.941 1.00 26.02 ? 142 ALA D C   1 
ATOM   5981 O O   . ALA D 2 142 ? 8.498   -12.997 49.804 1.00 19.07 ? 142 ALA D O   1 
ATOM   5982 C CB  . ALA D 2 142 ? 9.731   -12.614 52.834 1.00 19.67 ? 142 ALA D CB  1 
ATOM   5983 N N   . ALA D 2 143 ? 7.214   -11.753 51.172 1.00 22.93 ? 143 ALA D N   1 
ATOM   5984 C CA  . ALA D 2 143 ? 6.722   -10.920 50.095 1.00 18.03 ? 143 ALA D CA  1 
ATOM   5985 C C   . ALA D 2 143 ? 7.149   -9.513  50.407 1.00 18.87 ? 143 ALA D C   1 
ATOM   5986 O O   . ALA D 2 143 ? 7.162   -9.113  51.553 1.00 22.78 ? 143 ALA D O   1 
ATOM   5987 C CB  . ALA D 2 143 ? 5.197   -11.024 49.977 1.00 21.00 ? 143 ALA D CB  1 
ATOM   5988 N N   . LEU D 2 144 ? 7.513   -8.771  49.376 1.00 19.86 ? 144 LEU D N   1 
ATOM   5989 C CA  . LEU D 2 144 ? 8.022   -7.427  49.524 1.00 22.73 ? 144 LEU D CA  1 
ATOM   5990 C C   . LEU D 2 144 ? 7.338   -6.650  48.451 1.00 19.75 ? 144 LEU D C   1 
ATOM   5991 O O   . LEU D 2 144 ? 7.016   -7.213  47.404 1.00 15.16 ? 144 LEU D O   1 
ATOM   5992 C CB  . LEU D 2 144 ? 9.519   -7.386  49.228 1.00 26.08 ? 144 LEU D CB  1 
ATOM   5993 C CG  . LEU D 2 144 ? 10.505  -7.892  50.253 1.00 27.63 ? 144 LEU D CG  1 
ATOM   5994 C CD1 . LEU D 2 144 ? 11.816  -8.151  49.560 1.00 29.30 ? 144 LEU D CD1 1 
ATOM   5995 C CD2 . LEU D 2 144 ? 10.686  -6.829  51.269 1.00 37.29 ? 144 LEU D CD2 1 
ATOM   5996 N N   . GLY D 2 145 ? 7.151   -5.354  48.671 1.00 19.71 ? 145 GLY D N   1 
ATOM   5997 C CA  . GLY D 2 145 ? 6.564   -4.554  47.623 1.00 15.44 ? 145 GLY D CA  1 
ATOM   5998 C C   . GLY D 2 145 ? 6.723   -3.057  47.720 1.00 16.85 ? 145 GLY D C   1 
ATOM   5999 O O   . GLY D 2 145 ? 7.336   -2.542  48.659 1.00 17.60 ? 145 GLY D O   1 
ATOM   6000 N N   . CYS D 2 146 ? 6.164   -2.372  46.722 1.00 15.49 ? 146 CYS D N   1 
ATOM   6001 C CA  . CYS D 2 146 ? 6.151   -0.919  46.645 1.00 20.20 ? 146 CYS D CA  1 
ATOM   6002 C C   . CYS D 2 146 ? 4.750   -0.424  46.321 1.00 23.41 ? 146 CYS D C   1 
ATOM   6003 O O   . CYS D 2 146 ? 4.088   -0.934  45.417 1.00 18.06 ? 146 CYS D O   1 
ATOM   6004 C CB  . CYS D 2 146 ? 7.133   -0.404  45.586 1.00 20.83 ? 146 CYS D CB  1 
ATOM   6005 S SG  . CYS D 2 146 ? 8.835   -0.269  46.183 1.00 36.48 ? 146 CYS D SG  1 
ATOM   6006 N N   . LEU D 2 147 ? 4.311   0.574   47.077 1.00 26.41 ? 147 LEU D N   1 
ATOM   6007 C CA  . LEU D 2 147 ? 3.011   1.188   46.882 1.00 19.83 ? 147 LEU D CA  1 
ATOM   6008 C C   . LEU D 2 147 ? 3.231   2.500   46.160 1.00 19.85 ? 147 LEU D C   1 
ATOM   6009 O O   . LEU D 2 147 ? 3.822   3.440   46.700 1.00 19.94 ? 147 LEU D O   1 
ATOM   6010 C CB  . LEU D 2 147 ? 2.335   1.422   48.232 1.00 21.15 ? 147 LEU D CB  1 
ATOM   6011 C CG  . LEU D 2 147 ? 0.951   2.065   48.261 1.00 21.91 ? 147 LEU D CG  1 
ATOM   6012 C CD1 . LEU D 2 147 ? -0.043  1.241   47.476 1.00 17.33 ? 147 LEU D CD1 1 
ATOM   6013 C CD2 . LEU D 2 147 ? 0.516   2.190   49.700 1.00 20.91 ? 147 LEU D CD2 1 
ATOM   6014 N N   . VAL D 2 148 ? 2.804   2.538   44.907 1.00 20.53 ? 148 VAL D N   1 
ATOM   6015 C CA  . VAL D 2 148 ? 2.984   3.710   44.067 1.00 16.84 ? 148 VAL D CA  1 
ATOM   6016 C C   . VAL D 2 148 ? 1.663   4.456   44.048 1.00 23.13 ? 148 VAL D C   1 
ATOM   6017 O O   . VAL D 2 148 ? 0.700   4.033   43.404 1.00 24.66 ? 148 VAL D O   1 
ATOM   6018 C CB  . VAL D 2 148 ? 3.437   3.301   42.665 1.00 20.91 ? 148 VAL D CB  1 
ATOM   6019 C CG1 . VAL D 2 148 ? 3.723   4.523   41.820 1.00 19.90 ? 148 VAL D CG1 1 
ATOM   6020 C CG2 . VAL D 2 148 ? 4.681   2.409   42.770 1.00 12.57 ? 148 VAL D CG2 1 
ATOM   6021 N N   . LYS D 2 149 ? 1.619   5.562   44.782 1.00 20.42 ? 149 LYS D N   1 
ATOM   6022 C CA  . LYS D 2 149 ? 0.350   6.151   45.175 1.00 19.35 ? 149 LYS D CA  1 
ATOM   6023 C C   . LYS D 2 149 ? 0.166   7.612   44.770 1.00 18.50 ? 149 LYS D C   1 
ATOM   6024 O O   . LYS D 2 149 ? 1.083   8.420   44.874 1.00 20.45 ? 149 LYS D O   1 
ATOM   6025 C CB  . LYS D 2 149 ? 0.172   5.998   46.692 1.00 27.95 ? 149 LYS D CB  1 
ATOM   6026 C CG  . LYS D 2 149 ? -1.198  6.397   47.202 1.00 25.57 ? 149 LYS D CG  1 
ATOM   6027 C CD  . LYS D 2 149 ? -1.473  5.819   48.567 1.00 26.37 ? 149 LYS D CD  1 
ATOM   6028 C CE  . LYS D 2 149 ? -2.932  6.000   48.922 1.00 19.17 ? 149 LYS D CE  1 
ATOM   6029 N NZ  . LYS D 2 149 ? -3.303  7.429   48.802 1.00 28.63 ? 149 LYS D NZ  1 
ATOM   6030 N N   . ASP D 2 150 ? -1.044  7.923   44.308 1.00 23.18 ? 150 ASP D N   1 
ATOM   6031 C CA  . ASP D 2 150 ? -1.500  9.297   44.071 1.00 21.57 ? 150 ASP D CA  1 
ATOM   6032 C C   . ASP D 2 150 ? -0.736  9.975   42.944 1.00 22.74 ? 150 ASP D C   1 
ATOM   6033 O O   . ASP D 2 150 ? -0.148  11.049  43.127 1.00 22.60 ? 150 ASP D O   1 
ATOM   6034 C CB  . ASP D 2 150 ? -1.431  10.146  45.348 1.00 17.62 ? 150 ASP D CB  1 
ATOM   6035 C CG  . ASP D 2 150 ? -2.366  9.644   46.437 1.00 24.19 ? 150 ASP D CG  1 
ATOM   6036 O OD1 . ASP D 2 150 ? -3.398  9.011   46.112 1.00 27.06 ? 150 ASP D OD1 1 
ATOM   6037 O OD2 . ASP D 2 150 ? -2.077  9.886   47.626 1.00 26.45 ? 150 ASP D OD2 1 
ATOM   6038 N N   . TYR D 2 151 ? -0.754  9.342   41.775 1.00 19.39 ? 151 TYR D N   1 
ATOM   6039 C CA  . TYR D 2 151 ? -0.175  9.934   40.597 1.00 12.27 ? 151 TYR D CA  1 
ATOM   6040 C C   . TYR D 2 151 ? -1.232  10.079  39.509 1.00 20.87 ? 151 TYR D C   1 
ATOM   6041 O O   . TYR D 2 151 ? -2.267  9.407   39.531 1.00 25.48 ? 151 TYR D O   1 
ATOM   6042 C CB  . TYR D 2 151 ? 0.998   9.098   40.101 1.00 15.34 ? 151 TYR D CB  1 
ATOM   6043 C CG  . TYR D 2 151 ? 0.631   7.728   39.572 1.00 17.56 ? 151 TYR D CG  1 
ATOM   6044 C CD1 . TYR D 2 151 ? 0.587   6.615   40.413 1.00 12.87 ? 151 TYR D CD1 1 
ATOM   6045 C CD2 . TYR D 2 151 ? 0.353   7.538   38.223 1.00 13.69 ? 151 TYR D CD2 1 
ATOM   6046 C CE1 . TYR D 2 151 ? 0.265   5.362   39.927 1.00 11.66 ? 151 TYR D CE1 1 
ATOM   6047 C CE2 . TYR D 2 151 ? 0.040   6.289   37.733 1.00 20.55 ? 151 TYR D CE2 1 
ATOM   6048 C CZ  . TYR D 2 151 ? -0.005  5.202   38.586 1.00 16.81 ? 151 TYR D CZ  1 
ATOM   6049 O OH  . TYR D 2 151 ? -0.326  3.965   38.066 1.00 20.66 ? 151 TYR D OH  1 
ATOM   6050 N N   . PHE D 2 152 ? -0.954  10.967  38.563 1.00 15.46 ? 152 PHE D N   1 
ATOM   6051 C CA  . PHE D 2 152 ? -1.789  11.157  37.396 1.00 19.12 ? 152 PHE D CA  1 
ATOM   6052 C C   . PHE D 2 152 ? -0.951  11.801  36.293 1.00 21.48 ? 152 PHE D C   1 
ATOM   6053 O O   . PHE D 2 152 ? -0.135  12.681  36.558 1.00 22.43 ? 152 PHE D O   1 
ATOM   6054 C CB  . PHE D 2 152 ? -2.983  12.063  37.720 1.00 18.36 ? 152 PHE D CB  1 
ATOM   6055 C CG  . PHE D 2 152 ? -4.035  12.074  36.647 1.00 25.42 ? 152 PHE D CG  1 
ATOM   6056 C CD1 . PHE D 2 152 ? -3.999  13.014  35.619 1.00 23.23 ? 152 PHE D CD1 1 
ATOM   6057 C CD2 . PHE D 2 152 ? -5.043  11.125  36.648 1.00 18.95 ? 152 PHE D CD2 1 
ATOM   6058 C CE1 . PHE D 2 152 ? -4.969  13.015  34.628 1.00 22.35 ? 152 PHE D CE1 1 
ATOM   6059 C CE2 . PHE D 2 152 ? -6.007  11.113  35.653 1.00 25.89 ? 152 PHE D CE2 1 
ATOM   6060 C CZ  . PHE D 2 152 ? -5.976  12.063  34.649 1.00 16.07 ? 152 PHE D CZ  1 
ATOM   6061 N N   . PRO D 2 153 ? -1.141  11.359  35.048 1.00 17.90 ? 153 PRO D N   1 
ATOM   6062 C CA  . PRO D 2 153 ? -2.013  10.254  34.648 1.00 21.43 ? 153 PRO D CA  1 
ATOM   6063 C C   . PRO D 2 153 ? -1.241  8.946   34.610 1.00 18.74 ? 153 PRO D C   1 
ATOM   6064 O O   . PRO D 2 153 ? -0.089  8.888   35.014 1.00 15.83 ? 153 PRO D O   1 
ATOM   6065 C CB  . PRO D 2 153 ? -2.391  10.632  33.218 1.00 21.40 ? 153 PRO D CB  1 
ATOM   6066 C CG  . PRO D 2 153 ? -1.123  11.271  32.696 1.00 20.12 ? 153 PRO D CG  1 
ATOM   6067 C CD  . PRO D 2 153 ? -0.557  12.046  33.882 1.00 19.90 ? 153 PRO D CD  1 
ATOM   6068 N N   . GLU D 2 154 ? -1.880  7.903   34.102 1.00 22.07 ? 154 GLU D N   1 
ATOM   6069 C CA  . GLU D 2 154 ? -1.169  6.684   33.749 1.00 21.99 ? 154 GLU D CA  1 
ATOM   6070 C C   . GLU D 2 154 ? -0.186  7.019   32.610 1.00 26.30 ? 154 GLU D C   1 
ATOM   6071 O O   . GLU D 2 154 ? -0.340  8.049   31.942 1.00 21.46 ? 154 GLU D O   1 
ATOM   6072 C CB  . GLU D 2 154 ? -2.176  5.631   33.290 1.00 20.96 ? 154 GLU D CB  1 
ATOM   6073 C CG  . GLU D 2 154 ? -2.889  4.894   34.407 1.00 24.19 ? 154 GLU D CG  1 
ATOM   6074 C CD  . GLU D 2 154 ? -2.192  3.598   34.743 1.00 39.27 ? 154 GLU D CD  1 
ATOM   6075 O OE1 . GLU D 2 154 ? -2.772  2.563   34.385 1.00 42.48 ? 154 GLU D OE1 1 
ATOM   6076 O OE2 . GLU D 2 154 ? -1.083  3.605   35.363 1.00 38.69 ? 154 GLU D OE2 1 
ATOM   6077 N N   . PRO D 2 155 ? 0.852   6.183   32.405 1.00 24.47 ? 155 PRO D N   1 
ATOM   6078 C CA  . PRO D 2 155 ? 1.241   5.020   33.210 1.00 22.90 ? 155 PRO D CA  1 
ATOM   6079 C C   . PRO D 2 155 ? 2.454   5.304   34.092 1.00 24.56 ? 155 PRO D C   1 
ATOM   6080 O O   . PRO D 2 155 ? 3.119   6.343   33.989 1.00 19.07 ? 155 PRO D O   1 
ATOM   6081 C CB  . PRO D 2 155 ? 1.673   4.032   32.141 1.00 18.02 ? 155 PRO D CB  1 
ATOM   6082 C CG  . PRO D 2 155 ? 2.404   4.943   31.152 1.00 18.69 ? 155 PRO D CG  1 
ATOM   6083 C CD  . PRO D 2 155 ? 1.644   6.254   31.163 1.00 19.16 ? 155 PRO D CD  1 
ATOM   6084 N N   . VAL D 2 156 ? 2.762   4.353   34.957 1.00 27.33 ? 156 VAL D N   1 
ATOM   6085 C CA  . VAL D 2 156 ? 4.003   4.411   35.699 1.00 23.36 ? 156 VAL D CA  1 
ATOM   6086 C C   . VAL D 2 156 ? 4.659   3.067   35.445 1.00 23.86 ? 156 VAL D C   1 
ATOM   6087 O O   . VAL D 2 156 ? 3.962   2.064   35.283 1.00 25.30 ? 156 VAL D O   1 
ATOM   6088 C CB  . VAL D 2 156 ? 3.744   4.673   37.211 1.00 24.28 ? 156 VAL D CB  1 
ATOM   6089 C CG1 . VAL D 2 156 ? 3.085   3.491   37.854 1.00 21.89 ? 156 VAL D CG1 1 
ATOM   6090 C CG2 . VAL D 2 156 ? 5.035   5.010   37.933 1.00 23.20 ? 156 VAL D CG2 1 
ATOM   6091 N N   . THR D 2 157 ? 5.980   3.030   35.346 1.00 23.43 ? 157 THR D N   1 
ATOM   6092 C CA  . THR D 2 157 ? 6.636   1.736   35.193 1.00 25.36 ? 157 THR D CA  1 
ATOM   6093 C C   . THR D 2 157 ? 7.442   1.415   36.430 1.00 21.99 ? 157 THR D C   1 
ATOM   6094 O O   . THR D 2 157 ? 8.002   2.301   37.064 1.00 21.25 ? 157 THR D O   1 
ATOM   6095 C CB  . THR D 2 157 ? 7.589   1.701   34.008 1.00 26.62 ? 157 THR D CB  1 
ATOM   6096 O OG1 . THR D 2 157 ? 8.690   2.568   34.288 1.00 26.75 ? 157 THR D OG1 1 
ATOM   6097 C CG2 . THR D 2 157 ? 6.881   2.129   32.726 1.00 17.26 ? 157 THR D CG2 1 
ATOM   6098 N N   . VAL D 2 158 ? 7.482   0.132   36.768 1.00 22.27 ? 158 VAL D N   1 
ATOM   6099 C CA  . VAL D 2 158 ? 8.177   -0.336  37.955 1.00 18.69 ? 158 VAL D CA  1 
ATOM   6100 C C   . VAL D 2 158 ? 9.020   -1.544  37.617 1.00 23.53 ? 158 VAL D C   1 
ATOM   6101 O O   . VAL D 2 158 ? 8.536   -2.513  37.019 1.00 24.98 ? 158 VAL D O   1 
ATOM   6102 C CB  . VAL D 2 158 ? 7.205   -0.757  39.080 1.00 15.85 ? 158 VAL D CB  1 
ATOM   6103 C CG1 . VAL D 2 158 ? 7.979   -1.135  40.341 1.00 13.40 ? 158 VAL D CG1 1 
ATOM   6104 C CG2 . VAL D 2 158 ? 6.215   0.348   39.370 1.00 19.80 ? 158 VAL D CG2 1 
ATOM   6105 N N   . SER D 2 159 ? 10.283  -1.502  38.019 1.00 21.70 ? 159 SER D N   1 
ATOM   6106 C CA  . SER D 2 159 ? 11.141  -2.656  37.853 1.00 22.38 ? 159 SER D CA  1 
ATOM   6107 C C   . SER D 2 159 ? 11.774  -2.902  39.204 1.00 22.54 ? 159 SER D C   1 
ATOM   6108 O O   . SER D 2 159 ? 11.647  -2.077  40.098 1.00 23.18 ? 159 SER D O   1 
ATOM   6109 C CB  . SER D 2 159 ? 12.204  -2.390  36.778 1.00 17.81 ? 159 SER D CB  1 
ATOM   6110 O OG  . SER D 2 159 ? 13.105  -1.398  37.217 1.00 22.70 ? 159 SER D OG  1 
ATOM   6111 N N   . TRP D 2 160 ? 12.441  -4.037  39.358 1.00 24.63 ? 160 TRP D N   1 
ATOM   6112 C CA  . TRP D 2 160 ? 13.150  -4.341  40.589 1.00 16.51 ? 160 TRP D CA  1 
ATOM   6113 C C   . TRP D 2 160 ? 14.635  -4.597  40.328 1.00 20.87 ? 160 TRP D C   1 
ATOM   6114 O O   . TRP D 2 160 ? 14.990  -5.288  39.363 1.00 21.40 ? 160 TRP D O   1 
ATOM   6115 C CB  . TRP D 2 160 ? 12.529  -5.565  41.242 1.00 17.81 ? 160 TRP D CB  1 
ATOM   6116 C CG  . TRP D 2 160 ? 11.207  -5.284  41.843 1.00 28.22 ? 160 TRP D CG  1 
ATOM   6117 C CD1 . TRP D 2 160 ? 9.983   -5.314  41.215 1.00 21.04 ? 160 TRP D CD1 1 
ATOM   6118 C CD2 . TRP D 2 160 ? 10.954  -4.916  43.200 1.00 20.41 ? 160 TRP D CD2 1 
ATOM   6119 N NE1 . TRP D 2 160 ? 8.994   -4.988  42.105 1.00 19.85 ? 160 TRP D NE1 1 
ATOM   6120 C CE2 . TRP D 2 160 ? 9.558   -4.740  43.331 1.00 22.09 ? 160 TRP D CE2 1 
ATOM   6121 C CE3 . TRP D 2 160 ? 11.771  -4.725  44.321 1.00 19.38 ? 160 TRP D CE3 1 
ATOM   6122 C CZ2 . TRP D 2 160 ? 8.958   -4.376  44.548 1.00 20.67 ? 160 TRP D CZ2 1 
ATOM   6123 C CZ3 . TRP D 2 160 ? 11.184  -4.359  45.517 1.00 18.02 ? 160 TRP D CZ3 1 
ATOM   6124 C CH2 . TRP D 2 160 ? 9.786   -4.194  45.626 1.00 19.13 ? 160 TRP D CH2 1 
ATOM   6125 N N   . ASN D 2 161 ? 15.481  -4.048  41.203 1.00 19.39 ? 161 ASN D N   1 
ATOM   6126 C CA  . ASN D 2 161 ? 16.931  -4.224  41.133 1.00 25.36 ? 161 ASN D CA  1 
ATOM   6127 C C   . ASN D 2 161 ? 17.476  -3.887  39.749 1.00 22.61 ? 161 ASN D C   1 
ATOM   6128 O O   . ASN D 2 161 ? 18.221  -4.656  39.155 1.00 20.62 ? 161 ASN D O   1 
ATOM   6129 C CB  . ASN D 2 161 ? 17.332  -5.637  41.574 1.00 15.39 ? 161 ASN D CB  1 
ATOM   6130 C CG  . ASN D 2 161 ? 17.183  -5.841  43.069 1.00 16.88 ? 161 ASN D CG  1 
ATOM   6131 O OD1 . ASN D 2 161 ? 16.768  -4.936  43.794 1.00 28.75 ? 161 ASN D OD1 1 
ATOM   6132 N ND2 . ASN D 2 161 ? 17.520  -7.023  43.541 1.00 13.08 ? 161 ASN D ND2 1 
ATOM   6133 N N   . SER D 2 162 ? 17.060  -2.733  39.240 1.00 19.91 ? 162 SER D N   1 
ATOM   6134 C CA  . SER D 2 162 ? 17.407  -2.283  37.895 1.00 21.43 ? 162 SER D CA  1 
ATOM   6135 C C   . SER D 2 162 ? 17.142  -3.286  36.778 1.00 20.43 ? 162 SER D C   1 
ATOM   6136 O O   . SER D 2 162 ? 17.791  -3.235  35.740 1.00 24.63 ? 162 SER D O   1 
ATOM   6137 C CB  . SER D 2 162 ? 18.860  -1.818  37.842 1.00 21.64 ? 162 SER D CB  1 
ATOM   6138 O OG  . SER D 2 162 ? 19.084  -0.841  38.842 1.00 34.15 ? 162 SER D OG  1 
ATOM   6139 N N   . GLY D 2 163 ? 16.177  -4.173  36.974 1.00 19.02 ? 163 GLY D N   1 
ATOM   6140 C CA  . GLY D 2 163 ? 15.818  -5.129  35.941 1.00 17.17 ? 163 GLY D CA  1 
ATOM   6141 C C   . GLY D 2 163 ? 16.362  -6.527  36.193 1.00 26.70 ? 163 GLY D C   1 
ATOM   6142 O O   . GLY D 2 163 ? 15.901  -7.488  35.588 1.00 32.12 ? 163 GLY D O   1 
ATOM   6143 N N   . ALA D 2 164 ? 17.331  -6.647  37.097 1.00 23.15 ? 164 ALA D N   1 
ATOM   6144 C CA  . ALA D 2 164 ? 17.961  -7.936  37.379 1.00 21.78 ? 164 ALA D CA  1 
ATOM   6145 C C   . ALA D 2 164 ? 16.997  -8.915  38.021 1.00 23.89 ? 164 ALA D C   1 
ATOM   6146 O O   . ALA D 2 164 ? 17.271  -10.109 38.064 1.00 25.61 ? 164 ALA D O   1 
ATOM   6147 C CB  . ALA D 2 164 ? 19.183  -7.760  38.272 1.00 13.50 ? 164 ALA D CB  1 
ATOM   6148 N N   . LEU D 2 165 ? 15.889  -8.406  38.549 1.00 20.52 ? 165 LEU D N   1 
ATOM   6149 C CA  . LEU D 2 165 ? 14.962  -9.219  39.336 1.00 22.95 ? 165 LEU D CA  1 
ATOM   6150 C C   . LEU D 2 165 ? 13.582  -9.222  38.693 1.00 26.79 ? 165 LEU D C   1 
ATOM   6151 O O   . LEU D 2 165 ? 12.813  -8.257  38.804 1.00 25.74 ? 165 LEU D O   1 
ATOM   6152 C CB  . LEU D 2 165 ? 14.884  -8.700  40.784 1.00 17.40 ? 165 LEU D CB  1 
ATOM   6153 C CG  . LEU D 2 165 ? 13.882  -9.396  41.714 1.00 25.92 ? 165 LEU D CG  1 
ATOM   6154 C CD1 . LEU D 2 165 ? 14.010  -10.901 41.611 1.00 21.65 ? 165 LEU D CD1 1 
ATOM   6155 C CD2 . LEU D 2 165 ? 14.079  -8.947  43.166 1.00 20.95 ? 165 LEU D CD2 1 
ATOM   6156 N N   . THR D 2 166 ? 13.264  -10.315 38.019 1.00 20.06 ? 166 THR D N   1 
ATOM   6157 C CA  . THR D 2 166 ? 11.993  -10.407 37.322 1.00 23.93 ? 166 THR D CA  1 
ATOM   6158 C C   . THR D 2 166 ? 11.165  -11.563 37.861 1.00 22.60 ? 166 THR D C   1 
ATOM   6159 O O   . THR D 2 166 ? 9.936   -11.546 37.829 1.00 29.17 ? 166 THR D O   1 
ATOM   6160 C CB  . THR D 2 166 ? 12.238  -10.613 35.836 1.00 26.76 ? 166 THR D CB  1 
ATOM   6161 O OG1 . THR D 2 166 ? 13.236  -11.628 35.681 1.00 25.06 ? 166 THR D OG1 1 
ATOM   6162 C CG2 . THR D 2 166 ? 12.725  -9.317  35.192 1.00 19.51 ? 166 THR D CG2 1 
ATOM   6163 N N   . SER D 2 167 ? 11.847  -12.567 38.380 1.00 21.54 ? 167 SER D N   1 
ATOM   6164 C CA  . SER D 2 167 ? 11.177  -13.784 38.808 1.00 30.27 ? 167 SER D CA  1 
ATOM   6165 C C   . SER D 2 167 ? 10.335  -13.585 40.075 1.00 24.89 ? 167 SER D C   1 
ATOM   6166 O O   . SER D 2 167 ? 10.840  -13.139 41.114 1.00 30.60 ? 167 SER D O   1 
ATOM   6167 C CB  . SER D 2 167 ? 12.212  -14.890 39.014 1.00 35.37 ? 167 SER D CB  1 
ATOM   6168 O OG  . SER D 2 167 ? 11.582  -16.154 39.060 1.00 47.86 ? 167 SER D OG  1 
ATOM   6169 N N   . GLY D 2 168 ? 9.049   -13.906 39.983 1.00 26.01 ? 168 GLY D N   1 
ATOM   6170 C CA  . GLY D 2 168 ? 8.155   -13.761 41.119 1.00 21.12 ? 168 GLY D CA  1 
ATOM   6171 C C   . GLY D 2 168 ? 7.723   -12.322 41.356 1.00 23.78 ? 168 GLY D C   1 
ATOM   6172 O O   . GLY D 2 168 ? 7.118   -12.016 42.383 1.00 20.78 ? 168 GLY D O   1 
ATOM   6173 N N   . VAL D 2 169 ? 8.052   -11.438 40.413 1.00 19.09 ? 169 VAL D N   1 
ATOM   6174 C CA  . VAL D 2 169 ? 7.564   -10.068 40.434 1.00 19.28 ? 169 VAL D CA  1 
ATOM   6175 C C   . VAL D 2 169 ? 6.140   -10.016 39.888 1.00 17.79 ? 169 VAL D C   1 
ATOM   6176 O O   . VAL D 2 169 ? 5.839   -10.622 38.866 1.00 28.61 ? 169 VAL D O   1 
ATOM   6177 C CB  . VAL D 2 169 ? 8.462   -9.143  39.600 1.00 18.92 ? 169 VAL D CB  1 
ATOM   6178 C CG1 . VAL D 2 169 ? 7.893   -7.739  39.567 1.00 18.18 ? 169 VAL D CG1 1 
ATOM   6179 C CG2 . VAL D 2 169 ? 9.878   -9.133  40.146 1.00 14.39 ? 169 VAL D CG2 1 
ATOM   6180 N N   . HIS D 2 170 ? 5.250   -9.344  40.602 1.00 21.40 ? 170 HIS D N   1 
ATOM   6181 C CA  . HIS D 2 170 ? 3.919   -9.045  40.078 1.00 16.39 ? 170 HIS D CA  1 
ATOM   6182 C C   . HIS D 2 170 ? 3.705   -7.557  40.226 1.00 19.64 ? 170 HIS D C   1 
ATOM   6183 O O   . HIS D 2 170 ? 3.806   -7.013  41.328 1.00 19.41 ? 170 HIS D O   1 
ATOM   6184 C CB  . HIS D 2 170 ? 2.810   -9.785  40.831 1.00 13.66 ? 170 HIS D CB  1 
ATOM   6185 C CG  . HIS D 2 170 ? 2.835   -11.269 40.641 1.00 22.41 ? 170 HIS D CG  1 
ATOM   6186 N ND1 . HIS D 2 170 ? 2.760   -11.863 39.396 1.00 27.93 ? 170 HIS D ND1 1 
ATOM   6187 C CD2 . HIS D 2 170 ? 2.938   -12.280 41.536 1.00 19.99 ? 170 HIS D CD2 1 
ATOM   6188 C CE1 . HIS D 2 170 ? 2.817   -13.175 39.534 1.00 20.65 ? 170 HIS D CE1 1 
ATOM   6189 N NE2 . HIS D 2 170 ? 2.928   -13.454 40.821 1.00 25.59 ? 170 HIS D NE2 1 
ATOM   6190 N N   . THR D 2 171 ? 3.454   -6.895  39.106 1.00 15.90 ? 171 THR D N   1 
ATOM   6191 C CA  . THR D 2 171 ? 3.111   -5.490  39.123 1.00 18.41 ? 171 THR D CA  1 
ATOM   6192 C C   . THR D 2 171 ? 1.662   -5.346  38.709 1.00 19.53 ? 171 THR D C   1 
ATOM   6193 O O   . THR D 2 171 ? 1.278   -5.691  37.598 1.00 22.61 ? 171 THR D O   1 
ATOM   6194 C CB  . THR D 2 171 ? 4.033   -4.693  38.214 1.00 17.89 ? 171 THR D CB  1 
ATOM   6195 O OG1 . THR D 2 171 ? 5.366   -4.799  38.726 1.00 24.29 ? 171 THR D OG1 1 
ATOM   6196 C CG2 . THR D 2 171 ? 3.615   -3.234  38.187 1.00 15.65 ? 171 THR D CG2 1 
ATOM   6197 N N   . PHE D 2 172 ? 0.846   -4.864  39.629 1.00 23.19 ? 172 PHE D N   1 
ATOM   6198 C CA  . PHE D 2 172 ? -0.595  -4.863  39.424 1.00 19.14 ? 172 PHE D CA  1 
ATOM   6199 C C   . PHE D 2 172 ? -1.067  -3.735  38.496 1.00 21.32 ? 172 PHE D C   1 
ATOM   6200 O O   . PHE D 2 172 ? -0.379  -2.716  38.325 1.00 21.65 ? 172 PHE D O   1 
ATOM   6201 C CB  . PHE D 2 172 ? -1.305  -4.819  40.784 1.00 22.56 ? 172 PHE D CB  1 
ATOM   6202 C CG  . PHE D 2 172 ? -1.147  -6.084  41.586 1.00 16.60 ? 172 PHE D CG  1 
ATOM   6203 C CD1 . PHE D 2 172 ? -2.031  -7.147  41.411 1.00 18.36 ? 172 PHE D CD1 1 
ATOM   6204 C CD2 . PHE D 2 172 ? -0.117  -6.221  42.499 1.00 18.90 ? 172 PHE D CD2 1 
ATOM   6205 C CE1 . PHE D 2 172 ? -1.894  -8.322  42.135 1.00 16.30 ? 172 PHE D CE1 1 
ATOM   6206 C CE2 . PHE D 2 172 ? 0.022   -7.389  43.241 1.00 18.40 ? 172 PHE D CE2 1 
ATOM   6207 C CZ  . PHE D 2 172 ? -0.870  -8.436  43.061 1.00 25.33 ? 172 PHE D CZ  1 
ATOM   6208 N N   . PRO D 2 173 ? -2.232  -3.929  37.863 1.00 21.56 ? 173 PRO D N   1 
ATOM   6209 C CA  . PRO D 2 173 ? -2.797  -2.824  37.095 1.00 18.32 ? 173 PRO D CA  1 
ATOM   6210 C C   . PRO D 2 173 ? -3.170  -1.717  38.060 1.00 23.51 ? 173 PRO D C   1 
ATOM   6211 O O   . PRO D 2 173 ? -3.744  -2.014  39.113 1.00 22.11 ? 173 PRO D O   1 
ATOM   6212 C CB  . PRO D 2 173 ? -4.073  -3.426  36.500 1.00 12.01 ? 173 PRO D CB  1 
ATOM   6213 C CG  . PRO D 2 173 ? -3.910  -4.898  36.595 1.00 13.76 ? 173 PRO D CG  1 
ATOM   6214 C CD  . PRO D 2 173 ? -3.063  -5.144  37.786 1.00 19.74 ? 173 PRO D CD  1 
ATOM   6215 N N   . ALA D 2 174 ? -2.852  -0.474  37.708 1.00 20.89 ? 174 ALA D N   1 
ATOM   6216 C CA  . ALA D 2 174 ? -3.283  0.696   38.478 1.00 24.40 ? 174 ALA D CA  1 
ATOM   6217 C C   . ALA D 2 174 ? -4.798  0.725   38.695 1.00 21.50 ? 174 ALA D C   1 
ATOM   6218 O O   . ALA D 2 174 ? -5.572  0.371   37.804 1.00 20.64 ? 174 ALA D O   1 
ATOM   6219 C CB  . ALA D 2 174 ? -2.844  1.980   37.767 1.00 20.35 ? 174 ALA D CB  1 
ATOM   6220 N N   . VAL D 2 175 ? -5.215  1.170   39.871 1.00 17.51 ? 175 VAL D N   1 
ATOM   6221 C CA  . VAL D 2 175 ? -6.618  1.474   40.097 1.00 19.62 ? 175 VAL D CA  1 
ATOM   6222 C C   . VAL D 2 175 ? -6.829  2.975   40.180 1.00 22.80 ? 175 VAL D C   1 
ATOM   6223 O O   . VAL D 2 175 ? -5.960  3.715   40.657 1.00 24.42 ? 175 VAL D O   1 
ATOM   6224 C CB  . VAL D 2 175 ? -7.188  0.821   41.383 1.00 18.86 ? 175 VAL D CB  1 
ATOM   6225 C CG1 . VAL D 2 175 ? -6.954  -0.678  41.366 1.00 14.47 ? 175 VAL D CG1 1 
ATOM   6226 C CG2 . VAL D 2 175 ? -6.617  1.484   42.658 1.00 23.57 ? 175 VAL D CG2 1 
ATOM   6227 N N   . LEU D 2 176 ? -7.989  3.413   39.696 1.00 21.27 ? 176 LEU D N   1 
ATOM   6228 C CA  . LEU D 2 176 ? -8.431  4.780   39.861 1.00 16.75 ? 176 LEU D CA  1 
ATOM   6229 C C   . LEU D 2 176 ? -9.081  4.966   41.242 1.00 20.83 ? 176 LEU D C   1 
ATOM   6230 O O   . LEU D 2 176 ? -10.066 4.306   41.580 1.00 24.16 ? 176 LEU D O   1 
ATOM   6231 C CB  . LEU D 2 176 ? -9.399  5.146   38.739 1.00 22.14 ? 176 LEU D CB  1 
ATOM   6232 C CG  . LEU D 2 176 ? -9.809  6.619   38.657 1.00 25.88 ? 176 LEU D CG  1 
ATOM   6233 C CD1 . LEU D 2 176 ? -8.598  7.527   38.837 1.00 22.52 ? 176 LEU D CD1 1 
ATOM   6234 C CD2 . LEU D 2 176 ? -10.476 6.884   37.329 1.00 15.96 ? 176 LEU D CD2 1 
ATOM   6235 N N   . GLN D 2 177 ? -8.505  5.852   42.050 1.00 24.35 ? 177 GLN D N   1 
ATOM   6236 C CA  . GLN D 2 177 ? -9.022  6.127   43.389 1.00 20.17 ? 177 GLN D CA  1 
ATOM   6237 C C   . GLN D 2 177 ? -10.171 7.122   43.336 1.00 25.25 ? 177 GLN D C   1 
ATOM   6238 O O   . GLN D 2 177 ? -10.321 7.848   42.357 1.00 28.91 ? 177 GLN D O   1 
ATOM   6239 C CB  . GLN D 2 177 ? -7.920  6.692   44.270 1.00 19.41 ? 177 GLN D CB  1 
ATOM   6240 C CG  . GLN D 2 177 ? -6.959  5.673   44.798 1.00 18.92 ? 177 GLN D CG  1 
ATOM   6241 C CD  . GLN D 2 177 ? -5.600  6.275   45.056 1.00 23.83 ? 177 GLN D CD  1 
ATOM   6242 O OE1 . GLN D 2 177 ? -4.884  5.852   45.953 1.00 30.05 ? 177 GLN D OE1 1 
ATOM   6243 N NE2 . GLN D 2 177 ? -5.237  7.273   44.262 1.00 24.29 ? 177 GLN D NE2 1 
ATOM   6244 N N   . SER D 2 178 ? -10.966 7.186   44.400 1.00 28.95 ? 178 SER D N   1 
ATOM   6245 C CA  . SER D 2 178 ? -12.112 8.086   44.414 1.00 26.56 ? 178 SER D CA  1 
ATOM   6246 C C   . SER D 2 178 ? -11.635 9.528   44.272 1.00 25.79 ? 178 SER D C   1 
ATOM   6247 O O   . SER D 2 178 ? -12.379 10.405  43.846 1.00 38.40 ? 178 SER D O   1 
ATOM   6248 C CB  . SER D 2 178 ? -12.948 7.897   45.683 1.00 35.48 ? 178 SER D CB  1 
ATOM   6249 O OG  . SER D 2 178 ? -12.252 8.310   46.844 1.00 51.28 ? 178 SER D OG  1 
ATOM   6250 N N   . SER D 2 179 ? -10.371 9.752   44.600 1.00 25.52 ? 179 SER D N   1 
ATOM   6251 C CA  . SER D 2 179 ? -9.758  11.067  44.507 1.00 18.02 ? 179 SER D CA  1 
ATOM   6252 C C   . SER D 2 179 ? -9.448  11.446  43.065 1.00 22.85 ? 179 SER D C   1 
ATOM   6253 O O   . SER D 2 179 ? -9.171  12.611  42.776 1.00 24.66 ? 179 SER D O   1 
ATOM   6254 C CB  . SER D 2 179 ? -8.454  11.079  45.306 1.00 17.95 ? 179 SER D CB  1 
ATOM   6255 O OG  . SER D 2 179 ? -7.444  10.369  44.609 1.00 23.54 ? 179 SER D OG  1 
ATOM   6256 N N   . GLY D 2 180 ? -9.455  10.460  42.170 1.00 23.15 ? 180 GLY D N   1 
ATOM   6257 C CA  . GLY D 2 180 ? -9.111  10.698  40.775 1.00 20.76 ? 180 GLY D CA  1 
ATOM   6258 C C   . GLY D 2 180 ? -7.643  10.475  40.438 1.00 21.08 ? 180 GLY D C   1 
ATOM   6259 O O   . GLY D 2 180 ? -7.236  10.561  39.284 1.00 23.05 ? 180 GLY D O   1 
ATOM   6260 N N   . LEU D 2 181 ? -6.844  10.187  41.454 1.00 22.58 ? 181 LEU D N   1 
ATOM   6261 C CA  . LEU D 2 181 ? -5.443  9.861   41.256 1.00 21.38 ? 181 LEU D CA  1 
ATOM   6262 C C   . LEU D 2 181 ? -5.323  8.346   41.155 1.00 20.58 ? 181 LEU D C   1 
ATOM   6263 O O   . LEU D 2 181 ? -6.201  7.628   41.647 1.00 21.61 ? 181 LEU D O   1 
ATOM   6264 C CB  . LEU D 2 181 ? -4.617  10.395  42.435 1.00 22.77 ? 181 LEU D CB  1 
ATOM   6265 C CG  . LEU D 2 181 ? -4.727  11.908  42.659 1.00 20.40 ? 181 LEU D CG  1 
ATOM   6266 C CD1 . LEU D 2 181 ? -3.964  12.364  43.899 1.00 16.03 ? 181 LEU D CD1 1 
ATOM   6267 C CD2 . LEU D 2 181 ? -4.253  12.663  41.395 1.00 16.24 ? 181 LEU D CD2 1 
ATOM   6268 N N   . TYR D 2 182 ? -4.265  7.848   40.508 1.00 17.45 ? 182 TYR D N   1 
ATOM   6269 C CA  . TYR D 2 182 ? -4.068  6.397   40.448 1.00 20.65 ? 182 TYR D CA  1 
ATOM   6270 C C   . TYR D 2 182 ? -3.212  5.887   41.589 1.00 19.53 ? 182 TYR D C   1 
ATOM   6271 O O   . TYR D 2 182 ? -2.483  6.641   42.229 1.00 17.32 ? 182 TYR D O   1 
ATOM   6272 C CB  . TYR D 2 182 ? -3.449  5.934   39.127 1.00 12.06 ? 182 TYR D CB  1 
ATOM   6273 C CG  . TYR D 2 182 ? -4.375  6.050   37.950 1.00 20.09 ? 182 TYR D CG  1 
ATOM   6274 C CD1 . TYR D 2 182 ? -4.384  7.197   37.176 1.00 25.24 ? 182 TYR D CD1 1 
ATOM   6275 C CD2 . TYR D 2 182 ? -5.235  5.019   37.603 1.00 17.03 ? 182 TYR D CD2 1 
ATOM   6276 C CE1 . TYR D 2 182 ? -5.221  7.330   36.106 1.00 19.49 ? 182 TYR D CE1 1 
ATOM   6277 C CE2 . TYR D 2 182 ? -6.087  5.145   36.524 1.00 16.80 ? 182 TYR D CE2 1 
ATOM   6278 C CZ  . TYR D 2 182 ? -6.067  6.309   35.781 1.00 21.36 ? 182 TYR D CZ  1 
ATOM   6279 O OH  . TYR D 2 182 ? -6.887  6.479   34.703 1.00 26.14 ? 182 TYR D OH  1 
ATOM   6280 N N   . SER D 2 183 ? -3.299  4.585   41.810 1.00 14.44 ? 183 SER D N   1 
ATOM   6281 C CA  . SER D 2 183 ? -2.435  3.914   42.742 1.00 15.54 ? 183 SER D CA  1 
ATOM   6282 C C   . SER D 2 183 ? -2.132  2.550   42.158 1.00 20.41 ? 183 SER D C   1 
ATOM   6283 O O   . SER D 2 183 ? -2.969  1.979   41.469 1.00 15.76 ? 183 SER D O   1 
ATOM   6284 C CB  . SER D 2 183 ? -3.147  3.746   44.071 1.00 15.05 ? 183 SER D CB  1 
ATOM   6285 O OG  . SER D 2 183 ? -2.214  3.654   45.121 1.00 32.77 ? 183 SER D OG  1 
ATOM   6286 N N   . LEU D 2 184 ? -0.926  2.041   42.399 1.00 22.59 ? 184 LEU D N   1 
ATOM   6287 C CA  . LEU D 2 184 ? -0.632  0.641   42.107 1.00 22.13 ? 184 LEU D CA  1 
ATOM   6288 C C   . LEU D 2 184 ? 0.374   0.083   43.069 1.00 18.92 ? 184 LEU D C   1 
ATOM   6289 O O   . LEU D 2 184 ? 1.030   0.821   43.797 1.00 22.96 ? 184 LEU D O   1 
ATOM   6290 C CB  . LEU D 2 184 ? -0.171  0.409   40.659 1.00 18.90 ? 184 LEU D CB  1 
ATOM   6291 C CG  . LEU D 2 184 ? 1.116   0.939   40.029 1.00 21.73 ? 184 LEU D CG  1 
ATOM   6292 C CD1 . LEU D 2 184 ? 2.370   0.200   40.452 1.00 15.86 ? 184 LEU D CD1 1 
ATOM   6293 C CD2 . LEU D 2 184 ? 0.942   0.817   38.534 1.00 23.63 ? 184 LEU D CD2 1 
ATOM   6294 N N   . SER D 2 185 ? 0.470   -1.238  43.077 1.00 22.61 ? 185 SER D N   1 
ATOM   6295 C CA  . SER D 2 185 ? 1.463   -1.920  43.877 1.00 21.10 ? 185 SER D CA  1 
ATOM   6296 C C   . SER D 2 185 ? 2.224   -2.871  42.990 1.00 21.50 ? 185 SER D C   1 
ATOM   6297 O O   . SER D 2 185 ? 1.700   -3.352  41.974 1.00 15.55 ? 185 SER D O   1 
ATOM   6298 C CB  . SER D 2 185 ? 0.822   -2.678  45.024 1.00 22.96 ? 185 SER D CB  1 
ATOM   6299 O OG  . SER D 2 185 ? 0.292   -1.781  45.978 1.00 38.11 ? 185 SER D OG  1 
ATOM   6300 N N   . SER D 2 186 ? 3.477   -3.099  43.373 1.00 16.25 ? 186 SER D N   1 
ATOM   6301 C CA  . SER D 2 186 ? 4.320   -4.094  42.746 1.00 15.97 ? 186 SER D CA  1 
ATOM   6302 C C   . SER D 2 186 ? 4.954   -4.894  43.859 1.00 15.37 ? 186 SER D C   1 
ATOM   6303 O O   . SER D 2 186 ? 5.537   -4.331  44.780 1.00 11.97 ? 186 SER D O   1 
ATOM   6304 C CB  . SER D 2 186 ? 5.404   -3.449  41.879 1.00 15.52 ? 186 SER D CB  1 
ATOM   6305 O OG  . SER D 2 186 ? 6.287   -4.435  41.386 1.00 15.13 ? 186 SER D OG  1 
ATOM   6306 N N   . VAL D 2 187 ? 4.818   -6.208  43.778 1.00 14.50 ? 187 VAL D N   1 
ATOM   6307 C CA  . VAL D 2 187 ? 5.395   -7.080  44.780 1.00 15.58 ? 187 VAL D CA  1 
ATOM   6308 C C   . VAL D 2 187 ? 6.296   -8.152  44.159 1.00 21.28 ? 187 VAL D C   1 
ATOM   6309 O O   . VAL D 2 187 ? 6.283   -8.409  42.946 1.00 19.50 ? 187 VAL D O   1 
ATOM   6310 C CB  . VAL D 2 187 ? 4.296   -7.771  45.599 1.00 15.38 ? 187 VAL D CB  1 
ATOM   6311 C CG1 . VAL D 2 187 ? 3.488   -6.731  46.362 1.00 12.59 ? 187 VAL D CG1 1 
ATOM   6312 C CG2 . VAL D 2 187 ? 3.397   -8.604  44.680 1.00 15.43 ? 187 VAL D CG2 1 
ATOM   6313 N N   . VAL D 2 188 ? 7.075   -8.783  45.011 1.00 15.46 ? 188 VAL D N   1 
ATOM   6314 C CA  . VAL D 2 188 ? 7.952   -9.845  44.587 1.00 16.69 ? 188 VAL D CA  1 
ATOM   6315 C C   . VAL D 2 188 ? 8.077   -10.752 45.797 1.00 16.71 ? 188 VAL D C   1 
ATOM   6316 O O   . VAL D 2 188 ? 7.981   -10.302 46.951 1.00 14.50 ? 188 VAL D O   1 
ATOM   6317 C CB  . VAL D 2 188 ? 9.347   -9.290  44.128 1.00 23.83 ? 188 VAL D CB  1 
ATOM   6318 C CG1 . VAL D 2 188 ? 10.039  -8.512  45.256 1.00 13.55 ? 188 VAL D CG1 1 
ATOM   6319 C CG2 . VAL D 2 188 ? 10.245  -10.398 43.583 1.00 14.87 ? 188 VAL D CG2 1 
ATOM   6320 N N   . THR D 2 189 ? 8.249   -12.037 45.543 1.00 14.74 ? 189 THR D N   1 
ATOM   6321 C CA  . THR D 2 189 ? 8.484   -12.960 46.629 1.00 13.72 ? 189 THR D CA  1 
ATOM   6322 C C   . THR D 2 189 ? 9.938   -13.380 46.606 1.00 22.63 ? 189 THR D C   1 
ATOM   6323 O O   . THR D 2 189 ? 10.531  -13.593 45.534 1.00 22.58 ? 189 THR D O   1 
ATOM   6324 C CB  . THR D 2 189 ? 7.549   -14.163 46.559 1.00 13.50 ? 189 THR D CB  1 
ATOM   6325 O OG1 . THR D 2 189 ? 7.577   -14.719 45.235 1.00 16.73 ? 189 THR D OG1 1 
ATOM   6326 C CG2 . THR D 2 189 ? 6.136   -13.701 46.879 1.00 14.25 ? 189 THR D CG2 1 
ATOM   6327 N N   . VAL D 2 190 ? 10.527  -13.446 47.797 1.00 21.51 ? 190 VAL D N   1 
ATOM   6328 C CA  . VAL D 2 190 ? 11.944  -13.756 47.938 1.00 16.39 ? 190 VAL D CA  1 
ATOM   6329 C C   . VAL D 2 190 ? 12.195  -14.703 49.112 1.00 17.66 ? 190 VAL D C   1 
ATOM   6330 O O   . VAL D 2 190 ? 11.392  -14.774 50.045 1.00 17.77 ? 190 VAL D O   1 
ATOM   6331 C CB  . VAL D 2 190 ? 12.793  -12.466 48.117 1.00 12.56 ? 190 VAL D CB  1 
ATOM   6332 C CG1 . VAL D 2 190 ? 12.590  -11.524 46.952 1.00 17.94 ? 190 VAL D CG1 1 
ATOM   6333 C CG2 . VAL D 2 190 ? 12.487  -11.789 49.416 1.00 11.66 ? 190 VAL D CG2 1 
ATOM   6334 N N   . PRO D 2 191 ? 13.323  -15.428 49.081 1.00 17.05 ? 191 PRO D N   1 
ATOM   6335 C CA  . PRO D 2 191 ? 13.666  -16.237 50.259 1.00 17.89 ? 191 PRO D CA  1 
ATOM   6336 C C   . PRO D 2 191 ? 13.848  -15.331 51.458 1.00 24.23 ? 191 PRO D C   1 
ATOM   6337 O O   . PRO D 2 191 ? 14.625  -14.380 51.366 1.00 25.38 ? 191 PRO D O   1 
ATOM   6338 C CB  . PRO D 2 191 ? 15.001  -16.857 49.879 1.00 12.00 ? 191 PRO D CB  1 
ATOM   6339 C CG  . PRO D 2 191 ? 15.014  -16.814 48.353 1.00 20.74 ? 191 PRO D CG  1 
ATOM   6340 C CD  . PRO D 2 191 ? 14.317  -15.554 48.002 1.00 9.29  ? 191 PRO D CD  1 
ATOM   6341 N N   . SER D 2 192 ? 13.148  -15.598 52.555 1.00 19.44 ? 192 SER D N   1 
ATOM   6342 C CA  . SER D 2 192 ? 13.197  -14.665 53.669 1.00 22.27 ? 192 SER D CA  1 
ATOM   6343 C C   . SER D 2 192 ? 14.598  -14.532 54.258 1.00 22.41 ? 192 SER D C   1 
ATOM   6344 O O   . SER D 2 192 ? 14.905  -13.516 54.875 1.00 23.48 ? 192 SER D O   1 
ATOM   6345 C CB  . SER D 2 192 ? 12.159  -14.993 54.747 1.00 17.33 ? 192 SER D CB  1 
ATOM   6346 O OG  . SER D 2 192 ? 12.383  -16.269 55.294 1.00 31.51 ? 192 SER D OG  1 
ATOM   6347 N N   . SER D 2 193 ? 15.455  -15.531 54.048 1.00 17.52 ? 193 SER D N   1 
ATOM   6348 C CA  . SER D 2 193 ? 16.819  -15.463 54.592 1.00 21.80 ? 193 SER D CA  1 
ATOM   6349 C C   . SER D 2 193 ? 17.768  -14.578 53.772 1.00 22.56 ? 193 SER D C   1 
ATOM   6350 O O   . SER D 2 193 ? 18.922  -14.384 54.138 1.00 28.25 ? 193 SER D O   1 
ATOM   6351 C CB  . SER D 2 193 ? 17.429  -16.850 54.812 1.00 19.66 ? 193 SER D CB  1 
ATOM   6352 O OG  . SER D 2 193 ? 17.525  -17.568 53.601 1.00 27.32 ? 193 SER D OG  1 
ATOM   6353 N N   . SER D 2 194 ? 17.275  -14.032 52.670 1.00 20.79 ? 194 SER D N   1 
ATOM   6354 C CA  . SER D 2 194 ? 18.067  -13.089 51.898 1.00 26.09 ? 194 SER D CA  1 
ATOM   6355 C C   . SER D 2 194 ? 17.746  -11.619 52.244 1.00 23.96 ? 194 SER D C   1 
ATOM   6356 O O   . SER D 2 194 ? 18.392  -10.702 51.747 1.00 28.80 ? 194 SER D O   1 
ATOM   6357 C CB  . SER D 2 194 ? 17.890  -13.358 50.400 1.00 20.59 ? 194 SER D CB  1 
ATOM   6358 O OG  . SER D 2 194 ? 16.558  -13.081 49.994 1.00 22.65 ? 194 SER D OG  1 
ATOM   6359 N N   . LEU D 2 195 ? 16.759  -11.403 53.104 1.00 23.11 ? 195 LEU D N   1 
ATOM   6360 C CA  . LEU D 2 195 ? 16.342  -10.051 53.459 1.00 28.32 ? 195 LEU D CA  1 
ATOM   6361 C C   . LEU D 2 195 ? 17.427  -9.221  54.127 1.00 31.37 ? 195 LEU D C   1 
ATOM   6362 O O   . LEU D 2 195 ? 17.391  -7.990  54.083 1.00 33.61 ? 195 LEU D O   1 
ATOM   6363 C CB  . LEU D 2 195 ? 15.119  -10.087 54.360 1.00 24.02 ? 195 LEU D CB  1 
ATOM   6364 C CG  . LEU D 2 195 ? 13.877  -10.597 53.652 1.00 25.40 ? 195 LEU D CG  1 
ATOM   6365 C CD1 . LEU D 2 195 ? 12.662  -10.310 54.512 1.00 22.90 ? 195 LEU D CD1 1 
ATOM   6366 C CD2 . LEU D 2 195 ? 13.767  -9.950  52.274 1.00 21.25 ? 195 LEU D CD2 1 
ATOM   6367 N N   . GLY D 2 196 ? 18.390  -9.895  54.744 1.00 37.33 ? 196 GLY D N   1 
ATOM   6368 C CA  . GLY D 2 196 ? 19.442  -9.214  55.471 1.00 30.74 ? 196 GLY D CA  1 
ATOM   6369 C C   . GLY D 2 196 ? 20.611  -8.836  54.590 1.00 31.28 ? 196 GLY D C   1 
ATOM   6370 O O   . GLY D 2 196 ? 21.148  -7.739  54.707 1.00 44.84 ? 196 GLY D O   1 
ATOM   6371 N N   . THR D 2 197 ? 20.992  -9.737  53.695 1.00 28.97 ? 197 THR D N   1 
ATOM   6372 C CA  . THR D 2 197 ? 22.206  -9.572  52.896 1.00 31.62 ? 197 THR D CA  1 
ATOM   6373 C C   . THR D 2 197 ? 21.987  -9.040  51.486 1.00 33.80 ? 197 THR D C   1 
ATOM   6374 O O   . THR D 2 197 ? 22.906  -8.476  50.891 1.00 31.82 ? 197 THR D O   1 
ATOM   6375 C CB  . THR D 2 197 ? 22.941  -10.909 52.760 1.00 41.26 ? 197 THR D CB  1 
ATOM   6376 O OG1 . THR D 2 197 ? 21.989  -11.927 52.421 1.00 37.17 ? 197 THR D OG1 1 
ATOM   6377 C CG2 . THR D 2 197 ? 23.647  -11.270 54.069 1.00 39.24 ? 197 THR D CG2 1 
ATOM   6378 N N   . GLN D 2 198 ? 20.787  -9.239  50.946 1.00 29.41 ? 198 GLN D N   1 
ATOM   6379 C CA  . GLN D 2 198 ? 20.496  -8.835  49.571 1.00 31.25 ? 198 GLN D CA  1 
ATOM   6380 C C   . GLN D 2 198 ? 19.556  -7.639  49.525 1.00 29.41 ? 198 GLN D C   1 
ATOM   6381 O O   . GLN D 2 198 ? 18.510  -7.650  50.172 1.00 28.09 ? 198 GLN D O   1 
ATOM   6382 C CB  . GLN D 2 198 ? 19.859  -9.989  48.806 1.00 31.46 ? 198 GLN D CB  1 
ATOM   6383 C CG  . GLN D 2 198 ? 19.351  -9.595  47.449 1.00 29.86 ? 198 GLN D CG  1 
ATOM   6384 C CD  . GLN D 2 198 ? 20.465  -9.476  46.437 1.00 33.70 ? 198 GLN D CD  1 
ATOM   6385 O OE1 . GLN D 2 198 ? 21.330  -10.346 46.349 1.00 43.04 ? 198 GLN D OE1 1 
ATOM   6386 N NE2 . GLN D 2 198 ? 20.453  -8.399  45.665 1.00 31.65 ? 198 GLN D NE2 1 
ATOM   6387 N N   . THR D 2 199 ? 19.911  -6.613  48.760 1.00 24.59 ? 199 THR D N   1 
ATOM   6388 C CA  . THR D 2 199 ? 19.057  -5.437  48.711 1.00 32.83 ? 199 THR D CA  1 
ATOM   6389 C C   . THR D 2 199 ? 17.994  -5.575  47.631 1.00 26.01 ? 199 THR D C   1 
ATOM   6390 O O   . THR D 2 199 ? 18.240  -6.150  46.570 1.00 24.73 ? 199 THR D O   1 
ATOM   6391 C CB  . THR D 2 199 ? 19.837  -4.123  48.529 1.00 25.78 ? 199 THR D CB  1 
ATOM   6392 O OG1 . THR D 2 199 ? 20.249  -3.995  47.171 1.00 33.55 ? 199 THR D OG1 1 
ATOM   6393 C CG2 . THR D 2 199 ? 21.051  -4.097  49.418 1.00 32.33 ? 199 THR D CG2 1 
ATOM   6394 N N   . TYR D 2 200 ? 16.803  -5.062  47.939 1.00 26.14 ? 200 TYR D N   1 
ATOM   6395 C CA  . TYR D 2 200 ? 15.667  -5.098  47.024 1.00 22.51 ? 200 TYR D CA  1 
ATOM   6396 C C   . TYR D 2 200 ? 15.174  -3.691  46.785 1.00 21.75 ? 200 TYR D C   1 
ATOM   6397 O O   . TYR D 2 200 ? 14.686  -3.012  47.689 1.00 30.55 ? 200 TYR D O   1 
ATOM   6398 C CB  . TYR D 2 200 ? 14.552  -5.971  47.586 1.00 19.89 ? 200 TYR D CB  1 
ATOM   6399 C CG  . TYR D 2 200 ? 14.975  -7.415  47.659 1.00 24.60 ? 200 TYR D CG  1 
ATOM   6400 C CD1 . TYR D 2 200 ? 15.000  -8.200  46.512 1.00 26.01 ? 200 TYR D CD1 1 
ATOM   6401 C CD2 . TYR D 2 200 ? 15.370  -7.991  48.859 1.00 18.61 ? 200 TYR D CD2 1 
ATOM   6402 C CE1 . TYR D 2 200 ? 15.397  -9.514  46.555 1.00 23.77 ? 200 TYR D CE1 1 
ATOM   6403 C CE2 . TYR D 2 200 ? 15.774  -9.310  48.909 1.00 19.43 ? 200 TYR D CE2 1 
ATOM   6404 C CZ  . TYR D 2 200 ? 15.786  -10.067 47.752 1.00 21.20 ? 200 TYR D CZ  1 
ATOM   6405 O OH  . TYR D 2 200 ? 16.186  -11.382 47.769 1.00 15.35 ? 200 TYR D OH  1 
ATOM   6406 N N   . ILE D 2 201 ? 15.333  -3.233  45.561 1.00 22.23 ? 201 ILE D N   1 
ATOM   6407 C CA  . ILE D 2 201 ? 14.929  -1.888  45.225 1.00 21.54 ? 201 ILE D CA  1 
ATOM   6408 C C   . ILE D 2 201 ? 13.851  -1.915  44.167 1.00 21.48 ? 201 ILE D C   1 
ATOM   6409 O O   . ILE D 2 201 ? 13.991  -2.588  43.154 1.00 21.32 ? 201 ILE D O   1 
ATOM   6410 C CB  . ILE D 2 201 ? 16.130  -1.108  44.691 1.00 21.91 ? 201 ILE D CB  1 
ATOM   6411 C CG1 . ILE D 2 201 ? 17.240  -1.108  45.743 1.00 25.15 ? 201 ILE D CG1 1 
ATOM   6412 C CG2 . ILE D 2 201 ? 15.725  0.304   44.280 1.00 17.75 ? 201 ILE D CG2 1 
ATOM   6413 C CD1 . ILE D 2 201 ? 18.475  -0.410  45.284 1.00 40.53 ? 201 ILE D CD1 1 
ATOM   6414 N N   . CYS D 2 202 ? 12.764  -1.193  44.387 1.00 20.90 ? 202 CYS D N   1 
ATOM   6415 C CA  . CYS D 2 202 ? 11.858  -0.989  43.276 1.00 22.65 ? 202 CYS D CA  1 
ATOM   6416 C C   . CYS D 2 202 ? 12.200  0.322   42.585 1.00 17.99 ? 202 CYS D C   1 
ATOM   6417 O O   . CYS D 2 202 ? 12.466  1.339   43.229 1.00 19.17 ? 202 CYS D O   1 
ATOM   6418 C CB  . CYS D 2 202 ? 10.382  -1.052  43.686 1.00 25.31 ? 202 CYS D CB  1 
ATOM   6419 S SG  . CYS D 2 202 ? 9.786   0.418   44.514 1.00 34.04 ? 202 CYS D SG  1 
ATOM   6420 N N   . ASN D 2 203 ? 12.201  0.269   41.263 1.00 14.71 ? 203 ASN D N   1 
ATOM   6421 C CA  . ASN D 2 203 ? 12.560  1.399   40.437 1.00 17.18 ? 203 ASN D CA  1 
ATOM   6422 C C   . ASN D 2 203 ? 11.305  1.958   39.814 1.00 21.87 ? 203 ASN D C   1 
ATOM   6423 O O   . ASN D 2 203 ? 10.771  1.407   38.850 1.00 20.14 ? 203 ASN D O   1 
ATOM   6424 C CB  . ASN D 2 203 ? 13.540  0.960   39.348 1.00 18.82 ? 203 ASN D CB  1 
ATOM   6425 C CG  . ASN D 2 203 ? 14.716  0.182   39.910 1.00 20.72 ? 203 ASN D CG  1 
ATOM   6426 O OD1 . ASN D 2 203 ? 14.876  -1.007  39.642 1.00 18.94 ? 203 ASN D OD1 1 
ATOM   6427 N ND2 . ASN D 2 203 ? 15.539  0.852   40.709 1.00 20.54 ? 203 ASN D ND2 1 
ATOM   6428 N N   . VAL D 2 204 ? 10.827  3.053   40.380 1.00 23.41 ? 204 VAL D N   1 
ATOM   6429 C CA  . VAL D 2 204 ? 9.592   3.640   39.916 1.00 21.13 ? 204 VAL D CA  1 
ATOM   6430 C C   . VAL D 2 204 ? 9.888   4.817   39.033 1.00 19.02 ? 204 VAL D C   1 
ATOM   6431 O O   . VAL D 2 204 ? 10.683  5.674   39.386 1.00 20.11 ? 204 VAL D O   1 
ATOM   6432 C CB  . VAL D 2 204 ? 8.756   4.118   41.089 1.00 18.64 ? 204 VAL D CB  1 
ATOM   6433 C CG1 . VAL D 2 204 ? 7.455   4.733   40.587 1.00 10.29 ? 204 VAL D CG1 1 
ATOM   6434 C CG2 . VAL D 2 204 ? 8.525   2.958   42.051 1.00 15.10 ? 204 VAL D CG2 1 
ATOM   6435 N N   . ASN D 2 205 ? 9.247   4.844   37.873 1.00 28.17 ? 205 ASN D N   1 
ATOM   6436 C CA  . ASN D 2 205 ? 9.382   5.951   36.948 1.00 25.20 ? 205 ASN D CA  1 
ATOM   6437 C C   . ASN D 2 205 ? 8.018   6.362   36.423 1.00 22.78 ? 205 ASN D C   1 
ATOM   6438 O O   . ASN D 2 205 ? 7.329   5.583   35.759 1.00 25.93 ? 205 ASN D O   1 
ATOM   6439 C CB  . ASN D 2 205 ? 10.298  5.572   35.782 1.00 23.21 ? 205 ASN D CB  1 
ATOM   6440 C CG  . ASN D 2 205 ? 10.611  6.753   34.872 1.00 29.65 ? 205 ASN D CG  1 
ATOM   6441 O OD1 . ASN D 2 205 ? 10.006  7.821   34.976 1.00 26.28 ? 205 ASN D OD1 1 
ATOM   6442 N ND2 . ASN D 2 205 ? 11.557  6.556   33.968 1.00 25.36 ? 205 ASN D ND2 1 
ATOM   6443 N N   . HIS D 2 206 ? 7.636   7.592   36.733 1.00 22.17 ? 206 HIS D N   1 
ATOM   6444 C CA  . HIS D 2 206 ? 6.428   8.178   36.187 1.00 18.82 ? 206 HIS D CA  1 
ATOM   6445 C C   . HIS D 2 206 ? 6.850   9.195   35.147 1.00 20.15 ? 206 HIS D C   1 
ATOM   6446 O O   . HIS D 2 206 ? 7.106   10.347  35.479 1.00 24.32 ? 206 HIS D O   1 
ATOM   6447 C CB  . HIS D 2 206 ? 5.635   8.882   37.290 1.00 20.63 ? 206 HIS D CB  1 
ATOM   6448 C CG  . HIS D 2 206 ? 4.304   9.398   36.839 1.00 18.60 ? 206 HIS D CG  1 
ATOM   6449 N ND1 . HIS D 2 206 ? 3.968   10.732  36.900 1.00 18.84 ? 206 HIS D ND1 1 
ATOM   6450 C CD2 . HIS D 2 206 ? 3.232   8.760   36.321 1.00 15.39 ? 206 HIS D CD2 1 
ATOM   6451 C CE1 . HIS D 2 206 ? 2.742   10.892  36.434 1.00 16.51 ? 206 HIS D CE1 1 
ATOM   6452 N NE2 . HIS D 2 206 ? 2.273   9.713   36.075 1.00 13.94 ? 206 HIS D NE2 1 
ATOM   6453 N N   . LYS D 2 207 ? 6.933   8.777   33.890 1.00 24.21 ? 207 LYS D N   1 
ATOM   6454 C CA  . LYS D 2 207 ? 7.404   9.669   32.820 1.00 22.04 ? 207 LYS D CA  1 
ATOM   6455 C C   . LYS D 2 207 ? 6.590   10.946  32.552 1.00 25.31 ? 207 LYS D C   1 
ATOM   6456 O O   . LYS D 2 207 ? 7.182   11.981  32.262 1.00 34.71 ? 207 LYS D O   1 
ATOM   6457 C CB  . LYS D 2 207 ? 7.658   8.898   31.519 1.00 21.75 ? 207 LYS D CB  1 
ATOM   6458 C CG  . LYS D 2 207 ? 8.933   8.080   31.542 1.00 22.99 ? 207 LYS D CG  1 
ATOM   6459 C CD  . LYS D 2 207 ? 8.932   7.010   30.472 1.00 31.54 ? 207 LYS D CD  1 
ATOM   6460 C CE  . LYS D 2 207 ? 10.229  6.212   30.495 1.00 33.51 ? 207 LYS D CE  1 
ATOM   6461 N NZ  . LYS D 2 207 ? 10.300  5.249   29.354 1.00 37.62 ? 207 LYS D NZ  1 
ATOM   6462 N N   . PRO D 2 208 ? 5.244   10.887  32.638 1.00 23.10 ? 208 PRO D N   1 
ATOM   6463 C CA  . PRO D 2 208 ? 4.494   12.131  32.425 1.00 23.76 ? 208 PRO D CA  1 
ATOM   6464 C C   . PRO D 2 208 ? 4.864   13.269  33.382 1.00 26.14 ? 208 PRO D C   1 
ATOM   6465 O O   . PRO D 2 208 ? 4.662   14.435  33.041 1.00 24.85 ? 208 PRO D O   1 
ATOM   6466 C CB  . PRO D 2 208 ? 3.049   11.704  32.666 1.00 21.14 ? 208 PRO D CB  1 
ATOM   6467 C CG  . PRO D 2 208 ? 3.029   10.289  32.336 1.00 21.45 ? 208 PRO D CG  1 
ATOM   6468 C CD  . PRO D 2 208 ? 4.340   9.727   32.728 1.00 15.11 ? 208 PRO D CD  1 
ATOM   6469 N N   . SER D 2 209 ? 5.405   12.948  34.552 1.00 21.70 ? 209 SER D N   1 
ATOM   6470 C CA  . SER D 2 209 ? 5.782   13.996  35.498 1.00 21.98 ? 209 SER D CA  1 
ATOM   6471 C C   . SER D 2 209 ? 7.295   14.030  35.715 1.00 29.43 ? 209 SER D C   1 
ATOM   6472 O O   . SER D 2 209 ? 7.782   14.696  36.634 1.00 23.81 ? 209 SER D O   1 
ATOM   6473 C CB  . SER D 2 209 ? 5.089   13.781  36.842 1.00 20.43 ? 209 SER D CB  1 
ATOM   6474 O OG  . SER D 2 209 ? 5.746   12.764  37.583 1.00 25.64 ? 209 SER D OG  1 
ATOM   6475 N N   . ASN D 2 210 ? 8.033   13.299  34.886 1.00 22.24 ? 210 ASN D N   1 
ATOM   6476 C CA  . ASN D 2 210 ? 9.480   13.146  35.094 1.00 30.37 ? 210 ASN D CA  1 
ATOM   6477 C C   . ASN D 2 210 ? 9.932   12.737  36.518 1.00 25.68 ? 210 ASN D C   1 
ATOM   6478 O O   . ASN D 2 210 ? 11.057  13.026  36.920 1.00 37.12 ? 210 ASN D O   1 
ATOM   6479 C CB  . ASN D 2 210 ? 10.219  14.413  34.633 1.00 31.02 ? 210 ASN D CB  1 
ATOM   6480 C CG  . ASN D 2 210 ? 9.946   14.748  33.165 1.00 43.12 ? 210 ASN D CG  1 
ATOM   6481 O OD1 . ASN D 2 210 ? 10.053  13.889  32.285 1.00 29.75 ? 210 ASN D OD1 1 
ATOM   6482 N ND2 . ASN D 2 210 ? 9.578   15.996  32.901 1.00 38.27 ? 210 ASN D ND2 1 
ATOM   6483 N N   . THR D 2 211 ? 9.067   12.063  37.274 1.00 22.50 ? 211 THR D N   1 
ATOM   6484 C CA  . THR D 2 211 ? 9.429   11.596  38.616 1.00 17.86 ? 211 THR D CA  1 
ATOM   6485 C C   . THR D 2 211 ? 10.015  10.196  38.590 1.00 19.12 ? 211 THR D C   1 
ATOM   6486 O O   . THR D 2 211 ? 9.375   9.255   38.123 1.00 22.76 ? 211 THR D O   1 
ATOM   6487 C CB  . THR D 2 211 ? 8.219   11.587  39.559 1.00 20.15 ? 211 THR D CB  1 
ATOM   6488 O OG1 . THR D 2 211 ? 7.661   12.904  39.624 1.00 24.61 ? 211 THR D OG1 1 
ATOM   6489 C CG2 . THR D 2 211 ? 8.623   11.119  40.973 1.00 16.50 ? 211 THR D CG2 1 
ATOM   6490 N N   . LYS D 2 212 ? 11.242  10.066  39.083 1.00 23.47 ? 212 LYS D N   1 
ATOM   6491 C CA  . LYS D 2 212 ? 11.894  8.765   39.231 1.00 20.10 ? 212 LYS D CA  1 
ATOM   6492 C C   . LYS D 2 212 ? 12.294  8.513   40.693 1.00 20.93 ? 212 LYS D C   1 
ATOM   6493 O O   . LYS D 2 212 ? 12.919  9.357   41.343 1.00 16.32 ? 212 LYS D O   1 
ATOM   6494 C CB  . LYS D 2 212 ? 13.125  8.649   38.327 1.00 19.39 ? 212 LYS D CB  1 
ATOM   6495 C CG  . LYS D 2 212 ? 12.805  8.674   36.837 1.00 35.31 ? 212 LYS D CG  1 
ATOM   6496 C CD  . LYS D 2 212 ? 13.995  8.216   35.986 1.00 30.77 ? 212 LYS D CD  1 
ATOM   6497 C CE  . LYS D 2 212 ? 15.192  9.121   36.192 1.00 39.18 ? 212 LYS D CE  1 
ATOM   6498 N NZ  . LYS D 2 212 ? 16.468  8.529   35.665 1.00 39.14 ? 212 LYS D NZ  1 
ATOM   6499 N N   . VAL D 2 213 ? 11.923  7.343   41.204 1.00 19.37 ? 213 VAL D N   1 
ATOM   6500 C CA  . VAL D 2 213 ? 12.242  6.970   42.562 1.00 17.51 ? 213 VAL D CA  1 
ATOM   6501 C C   . VAL D 2 213 ? 12.801  5.561   42.621 1.00 22.05 ? 213 VAL D C   1 
ATOM   6502 O O   . VAL D 2 213 ? 12.221  4.634   42.062 1.00 24.29 ? 213 VAL D O   1 
ATOM   6503 C CB  . VAL D 2 213 ? 11.005  7.058   43.486 1.00 22.32 ? 213 VAL D CB  1 
ATOM   6504 C CG1 . VAL D 2 213 ? 11.354  6.597   44.919 1.00 13.58 ? 213 VAL D CG1 1 
ATOM   6505 C CG2 . VAL D 2 213 ? 10.461  8.469   43.510 1.00 13.27 ? 213 VAL D CG2 1 
ATOM   6506 N N   . ASP D 2 214 ? 13.937  5.412   43.296 1.00 20.31 ? 214 ASP D N   1 
ATOM   6507 C CA  . ASP D 2 214 ? 14.469  4.102   43.626 1.00 18.87 ? 214 ASP D CA  1 
ATOM   6508 C C   . ASP D 2 214 ? 14.206  3.896   45.108 1.00 24.38 ? 214 ASP D C   1 
ATOM   6509 O O   . ASP D 2 214 ? 14.677  4.671   45.942 1.00 22.76 ? 214 ASP D O   1 
ATOM   6510 C CB  . ASP D 2 214 ? 15.968  4.032   43.361 1.00 19.72 ? 214 ASP D CB  1 
ATOM   6511 C CG  . ASP D 2 214 ? 16.312  4.125   41.879 1.00 30.95 ? 214 ASP D CG  1 
ATOM   6512 O OD1 . ASP D 2 214 ? 15.519  3.629   41.041 1.00 22.90 ? 214 ASP D OD1 1 
ATOM   6513 O OD2 . ASP D 2 214 ? 17.385  4.689   41.553 1.00 28.16 ? 214 ASP D OD2 1 
ATOM   6514 N N   . LYS D 2 215 ? 13.448  2.856   45.442 1.00 20.83 ? 215 LYS D N   1 
ATOM   6515 C CA  . LYS D 2 215 ? 13.050  2.631   46.824 1.00 22.67 ? 215 LYS D CA  1 
ATOM   6516 C C   . LYS D 2 215 ? 13.528  1.281   47.304 1.00 21.86 ? 215 LYS D C   1 
ATOM   6517 O O   . LYS D 2 215 ? 13.232  0.261   46.684 1.00 22.16 ? 215 LYS D O   1 
ATOM   6518 C CB  . LYS D 2 215 ? 11.527  2.727   46.980 1.00 14.43 ? 215 LYS D CB  1 
ATOM   6519 C CG  . LYS D 2 215 ? 11.044  2.465   48.420 1.00 20.23 ? 215 LYS D CG  1 
ATOM   6520 C CD  . LYS D 2 215 ? 11.289  3.661   49.347 1.00 19.95 ? 215 LYS D CD  1 
ATOM   6521 C CE  . LYS D 2 215 ? 11.018  3.324   50.805 1.00 21.58 ? 215 LYS D CE  1 
ATOM   6522 N NZ  . LYS D 2 215 ? 11.057  4.515   51.714 1.00 25.20 ? 215 LYS D NZ  1 
ATOM   6523 N N   . ARG D 2 216 ? 14.264  1.280   48.413 1.00 24.05 ? 216 ARG D N   1 
ATOM   6524 C CA  . ARG D 2 216 ? 14.687  0.035   49.032 1.00 24.23 ? 216 ARG D CA  1 
ATOM   6525 C C   . ARG D 2 216 ? 13.578  -0.427  49.958 1.00 21.08 ? 216 ARG D C   1 
ATOM   6526 O O   . ARG D 2 216 ? 12.954  0.390   50.632 1.00 21.42 ? 216 ARG D O   1 
ATOM   6527 C CB  . ARG D 2 216 ? 15.982  0.215   49.827 1.00 24.46 ? 216 ARG D CB  1 
ATOM   6528 C CG  . ARG D 2 216 ? 16.333  -1.048  50.594 1.00 23.56 ? 216 ARG D CG  1 
ATOM   6529 C CD  . ARG D 2 216 ? 17.709  -1.078  51.201 1.00 26.39 ? 216 ARG D CD  1 
ATOM   6530 N NE  . ARG D 2 216 ? 17.973  -2.440  51.668 1.00 36.66 ? 216 ARG D NE  1 
ATOM   6531 C CZ  . ARG D 2 216 ? 18.675  -2.743  52.757 1.00 31.85 ? 216 ARG D CZ  1 
ATOM   6532 N NH1 . ARG D 2 216 ? 19.197  -1.781  53.503 1.00 36.18 ? 216 ARG D NH1 1 
ATOM   6533 N NH2 . ARG D 2 216 ? 18.852  -4.011  53.101 1.00 34.48 ? 216 ARG D NH2 1 
ATOM   6534 N N   . VAL D 2 217 ? 13.322  -1.731  49.982 1.00 21.59 ? 217 VAL D N   1 
ATOM   6535 C CA  . VAL D 2 217 ? 12.248  -2.276  50.800 1.00 18.89 ? 217 VAL D CA  1 
ATOM   6536 C C   . VAL D 2 217 ? 12.822  -3.382  51.667 1.00 18.56 ? 217 VAL D C   1 
ATOM   6537 O O   . VAL D 2 217 ? 13.413  -4.333  51.162 1.00 22.14 ? 217 VAL D O   1 
ATOM   6538 C CB  . VAL D 2 217 ? 11.086  -2.832  49.932 1.00 17.83 ? 217 VAL D CB  1 
ATOM   6539 C CG1 . VAL D 2 217 ? 9.966   -3.340  50.815 1.00 23.23 ? 217 VAL D CG1 1 
ATOM   6540 C CG2 . VAL D 2 217 ? 10.565  -1.763  48.985 1.00 14.16 ? 217 VAL D CG2 1 
ATOM   6541 N N   . GLU D 2 218 ? 12.679  -3.235  52.975 1.00 23.40 ? 218 GLU D N   1 
ATOM   6542 C CA  . GLU D 2 218 ? 13.240  -4.186  53.929 1.00 28.19 ? 218 GLU D CA  1 
ATOM   6543 C C   . GLU D 2 218 ? 12.325  -4.228  55.135 1.00 28.57 ? 218 GLU D C   1 
ATOM   6544 O O   . GLU D 2 218 ? 11.512  -3.314  55.309 1.00 28.84 ? 218 GLU D O   1 
ATOM   6545 C CB  . GLU D 2 218 ? 14.631  -3.745  54.351 1.00 16.61 ? 218 GLU D CB  1 
ATOM   6546 C CG  . GLU D 2 218 ? 14.669  -2.350  54.881 1.00 26.33 ? 218 GLU D CG  1 
ATOM   6547 C CD  . GLU D 2 218 ? 16.064  -1.955  55.314 1.00 41.16 ? 218 GLU D CD  1 
ATOM   6548 O OE1 . GLU D 2 218 ? 16.401  -0.751  55.235 1.00 44.04 ? 218 GLU D OE1 1 
ATOM   6549 O OE2 . GLU D 2 218 ? 16.826  -2.857  55.728 1.00 48.58 ? 218 GLU D OE2 1 
ATOM   6550 N N   . PRO D 2 219 ? 12.434  -5.284  55.967 1.00 31.11 ? 219 PRO D N   1 
ATOM   6551 C CA  . PRO D 2 219 ? 11.536  -5.371  57.130 1.00 33.99 ? 219 PRO D CA  1 
ATOM   6552 C C   . PRO D 2 219 ? 11.801  -4.245  58.112 1.00 25.52 ? 219 PRO D C   1 
ATOM   6553 O O   . PRO D 2 219 ? 12.961  -3.936  58.358 1.00 24.02 ? 219 PRO D O   1 
ATOM   6554 C CB  . PRO D 2 219 ? 11.890  -6.723  57.753 1.00 34.49 ? 219 PRO D CB  1 
ATOM   6555 C CG  . PRO D 2 219 ? 13.251  -7.051  57.229 1.00 26.37 ? 219 PRO D CG  1 
ATOM   6556 C CD  . PRO D 2 219 ? 13.315  -6.461  55.863 1.00 29.14 ? 219 PRO D CD  1 
ATOM   6557 N N   . LYS D 2 220 ? 10.737  -3.636  58.638 1.00 38.31 ? 220 LYS D N   1 
ATOM   6558 C CA  . LYS D 2 220 ? 10.854  -2.502  59.565 1.00 41.01 ? 220 LYS D CA  1 
ATOM   6559 C C   . LYS D 2 220 ? 11.297  -2.925  60.975 1.00 33.33 ? 220 LYS D C   1 
ATOM   6560 O O   . LYS D 2 220 ? 11.557  -4.110  61.241 1.00 30.52 ? 220 LYS D O   1 
ATOM   6561 C CB  . LYS D 2 220 ? 9.537   -1.729  59.642 1.00 38.90 ? 220 LYS D CB  1 
ATOM   6562 C CG  . LYS D 2 220 ? 9.516   -0.620  60.696 1.00 57.09 ? 220 LYS D CG  1 
ATOM   6563 C CD  . LYS D 2 220 ? 8.101   -0.305  61.189 1.00 51.47 ? 220 LYS D CD  1 
ATOM   6564 C CE  . LYS D 2 220 ? 8.100   -0.044  62.701 1.00 61.09 ? 220 LYS D CE  1 
ATOM   6565 N NZ  . LYS D 2 220 ? 6.801   0.473   63.226 1.00 60.54 ? 220 LYS D NZ  1 
ATOM   6566 N N   . CYS E 3 1   ? -15.123 -32.687 26.701 1.00 59.54 ? 1   CYS E N   1 
ATOM   6567 C CA  . CYS E 3 1   ? -15.902 -32.797 27.935 1.00 59.70 ? 1   CYS E CA  1 
ATOM   6568 C C   . CYS E 3 1   ? -16.370 -34.228 28.206 1.00 62.72 ? 1   CYS E C   1 
ATOM   6569 O O   . CYS E 3 1   ? -15.836 -35.195 27.651 1.00 71.55 ? 1   CYS E O   1 
ATOM   6570 C CB  . CYS E 3 1   ? -17.121 -31.864 27.889 1.00 52.00 ? 1   CYS E CB  1 
ATOM   6571 S SG  . CYS E 3 1   ? -16.892 -30.189 28.597 1.00 59.99 ? 1   CYS E SG  1 
ATOM   6572 N N   . GLN E 3 2   ? -17.373 -34.349 29.072 1.00 55.88 ? 2   GLN E N   1 
ATOM   6573 C CA  . GLN E 3 2   ? -17.978 -35.635 29.403 1.00 46.82 ? 2   GLN E CA  1 
ATOM   6574 C C   . GLN E 3 2   ? -19.495 -35.531 29.356 1.00 38.79 ? 2   GLN E C   1 
ATOM   6575 O O   . GLN E 3 2   ? -20.066 -34.530 29.773 1.00 38.49 ? 2   GLN E O   1 
ATOM   6576 C CB  . GLN E 3 2   ? -17.520 -36.089 30.783 1.00 41.22 ? 2   GLN E CB  1 
ATOM   6577 C CG  . GLN E 3 2   ? -16.122 -36.673 30.786 1.00 57.97 ? 2   GLN E CG  1 
ATOM   6578 C CD  . GLN E 3 2   ? -16.067 -38.045 30.126 1.00 71.27 ? 2   GLN E CD  1 
ATOM   6579 O OE1 . GLN E 3 2   ? -16.760 -38.977 30.551 1.00 65.75 ? 2   GLN E OE1 1 
ATOM   6580 N NE2 . GLN E 3 2   ? -15.246 -38.174 29.077 1.00 56.84 ? 2   GLN E NE2 1 
ATOM   6581 N N   . HIS E 3 3   ? -20.149 -36.562 28.838 1.00 36.56 ? 3   HIS E N   1 
ATOM   6582 C CA  . HIS E 3 3   ? -21.603 -36.538 28.703 1.00 33.19 ? 3   HIS E CA  1 
ATOM   6583 C C   . HIS E 3 3   ? -22.275 -37.275 29.861 1.00 28.33 ? 3   HIS E C   1 
ATOM   6584 O O   . HIS E 3 3   ? -22.128 -38.488 30.002 1.00 32.39 ? 3   HIS E O   1 
ATOM   6585 C CB  . HIS E 3 3   ? -22.025 -37.112 27.348 1.00 27.79 ? 3   HIS E CB  1 
ATOM   6586 C CG  . HIS E 3 3   ? -21.269 -36.534 26.192 1.00 34.37 ? 3   HIS E CG  1 
ATOM   6587 N ND1 . HIS E 3 3   ? -19.967 -36.882 25.905 1.00 32.78 ? 3   HIS E ND1 1 
ATOM   6588 C CD2 . HIS E 3 3   ? -21.628 -35.622 25.259 1.00 34.79 ? 3   HIS E CD2 1 
ATOM   6589 C CE1 . HIS E 3 3   ? -19.558 -36.213 24.843 1.00 32.67 ? 3   HIS E CE1 1 
ATOM   6590 N NE2 . HIS E 3 3   ? -20.547 -35.441 24.431 1.00 27.59 ? 3   HIS E NE2 1 
ATOM   6591 N N   . ASP E 3 4   ? -23.003 -36.521 30.685 1.00 26.86 ? 4   ASP E N   1 
ATOM   6592 C CA  . ASP E 3 4   ? -23.611 -37.018 31.918 1.00 20.76 ? 4   ASP E CA  1 
ATOM   6593 C C   . ASP E 3 4   ? -25.002 -37.579 31.628 1.00 24.75 ? 4   ASP E C   1 
ATOM   6594 O O   . ASP E 3 4   ? -25.886 -36.845 31.198 1.00 25.77 ? 4   ASP E O   1 
ATOM   6595 C CB  . ASP E 3 4   ? -23.680 -35.867 32.932 1.00 30.94 ? 4   ASP E CB  1 
ATOM   6596 C CG  . ASP E 3 4   ? -24.202 -36.290 34.298 1.00 30.63 ? 4   ASP E CG  1 
ATOM   6597 O OD1 . ASP E 3 4   ? -24.462 -37.487 34.514 1.00 34.68 ? 4   ASP E OD1 1 
ATOM   6598 O OD2 . ASP E 3 4   ? -24.343 -35.401 35.164 1.00 38.83 ? 4   ASP E OD2 1 
ATOM   6599 N N   . LEU E 3 5   ? -25.190 -38.877 31.867 1.00 22.49 ? 5   LEU E N   1 
ATOM   6600 C CA  . LEU E 3 5   ? -26.429 -39.563 31.508 1.00 20.62 ? 5   LEU E CA  1 
ATOM   6601 C C   . LEU E 3 5   ? -27.579 -39.247 32.448 1.00 31.77 ? 5   LEU E C   1 
ATOM   6602 O O   . LEU E 3 5   ? -28.738 -39.502 32.112 1.00 33.96 ? 5   LEU E O   1 
ATOM   6603 C CB  . LEU E 3 5   ? -26.231 -41.074 31.456 1.00 18.12 ? 5   LEU E CB  1 
ATOM   6604 C CG  . LEU E 3 5   ? -25.148 -41.597 30.524 1.00 22.49 ? 5   LEU E CG  1 
ATOM   6605 C CD1 . LEU E 3 5   ? -25.225 -43.105 30.450 1.00 25.18 ? 5   LEU E CD1 1 
ATOM   6606 C CD2 . LEU E 3 5   ? -25.270 -40.982 29.143 1.00 29.11 ? 5   LEU E CD2 1 
ATOM   6607 N N   . SER E 3 6   ? -27.263 -38.710 33.626 1.00 27.73 ? 6   SER E N   1 
ATOM   6608 C CA  . SER E 3 6   ? -28.292 -38.296 34.577 1.00 32.39 ? 6   SER E CA  1 
ATOM   6609 C C   . SER E 3 6   ? -28.976 -37.009 34.121 1.00 28.59 ? 6   SER E C   1 
ATOM   6610 O O   . SER E 3 6   ? -30.198 -36.937 34.078 1.00 26.87 ? 6   SER E O   1 
ATOM   6611 C CB  . SER E 3 6   ? -27.696 -38.085 35.978 1.00 31.94 ? 6   SER E CB  1 
ATOM   6612 O OG  . SER E 3 6   ? -27.259 -39.298 36.551 1.00 26.65 ? 6   SER E OG  1 
ATOM   6613 N N   . THR E 3 7   ? -28.182 -35.992 33.798 1.00 29.31 ? 7   THR E N   1 
ATOM   6614 C CA  . THR E 3 7   ? -28.727 -34.682 33.439 1.00 28.63 ? 7   THR E CA  1 
ATOM   6615 C C   . THR E 3 7   ? -28.860 -34.499 31.934 1.00 31.66 ? 7   THR E C   1 
ATOM   6616 O O   . THR E 3 7   ? -29.532 -33.571 31.477 1.00 31.63 ? 7   THR E O   1 
ATOM   6617 C CB  . THR E 3 7   ? -27.865 -33.520 33.991 1.00 35.04 ? 7   THR E CB  1 
ATOM   6618 O OG1 . THR E 3 7   ? -26.595 -33.481 33.315 1.00 35.25 ? 7   THR E OG1 1 
ATOM   6619 C CG2 . THR E 3 7   ? -27.660 -33.674 35.500 1.00 34.79 ? 7   THR E CG2 1 
ATOM   6620 N N   . ARG E 3 8   ? -28.227 -35.387 31.175 1.00 18.90 ? 8   ARG E N   1 
ATOM   6621 C CA  . ARG E 3 8   ? -28.160 -35.251 29.728 1.00 29.52 ? 8   ARG E CA  1 
ATOM   6622 C C   . ARG E 3 8   ? -27.469 -33.953 29.339 1.00 25.57 ? 8   ARG E C   1 
ATOM   6623 O O   . ARG E 3 8   ? -27.777 -33.358 28.319 1.00 30.71 ? 8   ARG E O   1 
ATOM   6624 C CB  . ARG E 3 8   ? -29.554 -35.336 29.092 1.00 30.20 ? 8   ARG E CB  1 
ATOM   6625 C CG  . ARG E 3 8   ? -30.278 -36.616 29.400 1.00 21.59 ? 8   ARG E CG  1 
ATOM   6626 C CD  . ARG E 3 8   ? -31.417 -36.784 28.460 1.00 25.79 ? 8   ARG E CD  1 
ATOM   6627 N NE  . ARG E 3 8   ? -32.223 -37.950 28.791 1.00 30.48 ? 8   ARG E NE  1 
ATOM   6628 C CZ  . ARG E 3 8   ? -33.256 -38.377 28.071 1.00 26.75 ? 8   ARG E CZ  1 
ATOM   6629 N NH1 . ARG E 3 8   ? -33.602 -37.737 26.957 1.00 22.94 ? 8   ARG E NH1 1 
ATOM   6630 N NH2 . ARG E 3 8   ? -33.929 -39.453 28.464 1.00 25.33 ? 8   ARG E NH2 1 
ATOM   6631 N N   . ARG E 3 9   ? -26.530 -33.518 30.164 1.00 24.19 ? 9   ARG E N   1 
ATOM   6632 C CA  . ARG E 3 9   ? -25.803 -32.300 29.895 1.00 20.63 ? 9   ARG E CA  1 
ATOM   6633 C C   . ARG E 3 9   ? -24.311 -32.563 29.927 1.00 24.20 ? 9   ARG E C   1 
ATOM   6634 O O   . ARG E 3 9   ? -23.850 -33.514 30.563 1.00 25.82 ? 9   ARG E O   1 
ATOM   6635 C CB  . ARG E 3 9   ? -26.166 -31.241 30.929 1.00 21.71 ? 9   ARG E CB  1 
ATOM   6636 C CG  . ARG E 3 9   ? -27.580 -30.744 30.822 1.00 25.37 ? 9   ARG E CG  1 
ATOM   6637 C CD  . ARG E 3 9   ? -27.805 -29.978 29.534 1.00 23.20 ? 9   ARG E CD  1 
ATOM   6638 N NE  . ARG E 3 9   ? -26.824 -28.913 29.323 1.00 21.73 ? 9   ARG E NE  1 
ATOM   6639 C CZ  . ARG E 3 9   ? -26.783 -27.776 30.016 1.00 27.01 ? 9   ARG E CZ  1 
ATOM   6640 N NH1 . ARG E 3 9   ? -27.651 -27.538 31.005 1.00 21.88 ? 9   ARG E NH1 1 
ATOM   6641 N NH2 . ARG E 3 9   ? -25.859 -26.874 29.726 1.00 24.96 ? 9   ARG E NH2 1 
ATOM   6642 N N   . LEU E 3 10  ? -23.555 -31.725 29.232 1.00 24.86 ? 10  LEU E N   1 
ATOM   6643 C CA  . LEU E 3 10  ? -22.109 -31.811 29.290 1.00 24.68 ? 10  LEU E CA  1 
ATOM   6644 C C   . LEU E 3 10  ? -21.653 -31.458 30.687 1.00 25.16 ? 10  LEU E C   1 
ATOM   6645 O O   . LEU E 3 10  ? -22.236 -30.606 31.354 1.00 31.46 ? 10  LEU E O   1 
ATOM   6646 C CB  . LEU E 3 10  ? -21.452 -30.874 28.278 1.00 28.51 ? 10  LEU E CB  1 
ATOM   6647 C CG  . LEU E 3 10  ? -21.555 -31.178 26.785 1.00 28.74 ? 10  LEU E CG  1 
ATOM   6648 C CD1 . LEU E 3 10  ? -20.792 -30.121 26.013 1.00 28.87 ? 10  LEU E CD1 1 
ATOM   6649 C CD2 . LEU E 3 10  ? -21.021 -32.557 26.475 1.00 30.07 ? 10  LEU E CD2 1 
ATOM   6650 N N   . LYS E 3 11  ? -20.603 -32.127 31.124 1.00 28.56 ? 11  LYS E N   1 
ATOM   6651 C CA  . LYS E 3 11  ? -20.057 -31.921 32.447 1.00 32.81 ? 11  LYS E CA  1 
ATOM   6652 C C   . LYS E 3 11  ? -18.552 -31.781 32.293 1.00 39.63 ? 11  LYS E C   1 
ATOM   6653 O O   . LYS E 3 11  ? -17.901 -32.624 31.674 1.00 36.78 ? 11  LYS E O   1 
ATOM   6654 C CB  . LYS E 3 11  ? -20.393 -33.123 33.327 1.00 33.16 ? 11  LYS E CB  1 
ATOM   6655 C CG  . LYS E 3 11  ? -20.144 -32.952 34.816 1.00 39.45 ? 11  LYS E CG  1 
ATOM   6656 C CD  . LYS E 3 11  ? -20.558 -34.226 35.548 1.00 43.74 ? 11  LYS E CD  1 
ATOM   6657 C CE  . LYS E 3 11  ? -20.582 -34.043 37.058 1.00 55.13 ? 11  LYS E CE  1 
ATOM   6658 N NZ  . LYS E 3 11  ? -21.637 -33.088 37.493 1.00 54.67 ? 11  LYS E NZ  1 
ATOM   6659 N N   . CYS E 3 12  ? -18.002 -30.700 32.832 1.00 53.88 ? 12  CYS E N   1 
ATOM   6660 C CA  . CYS E 3 12  ? -16.568 -30.457 32.734 1.00 56.30 ? 12  CYS E CA  1 
ATOM   6661 C C   . CYS E 3 12  ? -15.930 -30.424 34.124 1.00 74.35 ? 12  CYS E C   1 
ATOM   6662 O O   . CYS E 3 12  ? -16.615 -30.271 35.143 1.00 79.99 ? 12  CYS E O   1 
ATOM   6663 C CB  . CYS E 3 12  ? -16.290 -29.162 31.955 1.00 49.21 ? 12  CYS E CB  1 
ATOM   6664 S SG  . CYS E 3 12  ? -17.082 -29.069 30.280 1.00 67.97 ? 12  CYS E SG  1 
ATOM   6665 O OXT . CYS E 3 12  ? -14.713 -30.571 34.261 1.00 93.75 ? 12  CYS E OXT 1 
ATOM   6666 N N   . CYS F 3 1   ? -16.044 -7.413  24.865 1.00 63.57 ? 1   CYS F N   1 
ATOM   6667 C CA  . CYS F 3 1   ? -15.285 -7.037  26.058 1.00 62.58 ? 1   CYS F CA  1 
ATOM   6668 C C   . CYS F 3 1   ? -14.761 -5.600  26.002 1.00 64.66 ? 1   CYS F C   1 
ATOM   6669 O O   . CYS F 3 1   ? -15.103 -4.836  25.095 1.00 70.76 ? 1   CYS F O   1 
ATOM   6670 C CB  . CYS F 3 1   ? -14.114 -7.993  26.270 1.00 54.30 ? 1   CYS F CB  1 
ATOM   6671 S SG  . CYS F 3 1   ? -14.471 -9.399  27.328 1.00 70.82 ? 1   CYS F SG  1 
ATOM   6672 N N   . GLN F 3 2   ? -13.912 -5.247  26.966 1.00 58.02 ? 2   GLN F N   1 
ATOM   6673 C CA  . GLN F 3 2   ? -13.367 -3.894  27.061 1.00 50.84 ? 2   GLN F CA  1 
ATOM   6674 C C   . GLN F 3 2   ? -11.845 -3.843  26.926 1.00 50.26 ? 2   GLN F C   1 
ATOM   6675 O O   . GLN F 3 2   ? -11.135 -4.746  27.376 1.00 43.91 ? 2   GLN F O   1 
ATOM   6676 C CB  . GLN F 3 2   ? -13.764 -3.257  28.385 1.00 52.91 ? 2   GLN F CB  1 
ATOM   6677 C CG  . GLN F 3 2   ? -13.835 -1.752  28.327 1.00 52.54 ? 2   GLN F CG  1 
ATOM   6678 C CD  . GLN F 3 2   ? -15.047 -1.282  27.552 1.00 67.25 ? 2   GLN F CD  1 
ATOM   6679 O OE1 . GLN F 3 2   ? -16.048 -1.997  27.456 1.00 72.22 ? 2   GLN F OE1 1 
ATOM   6680 N NE2 . GLN F 3 2   ? -14.968 -0.077  26.995 1.00 54.24 ? 2   GLN F NE2 1 
ATOM   6681 N N   . HIS F 3 3   ? -11.352 -2.761  26.329 1.00 46.09 ? 3   HIS F N   1 
ATOM   6682 C CA  . HIS F 3 3   ? -9.929  -2.608  26.053 1.00 43.06 ? 3   HIS F CA  1 
ATOM   6683 C C   . HIS F 3 3   ? -9.233  -1.751  27.109 1.00 32.96 ? 3   HIS F C   1 
ATOM   6684 O O   . HIS F 3 3   ? -9.422  -0.542  27.162 1.00 32.93 ? 3   HIS F O   1 
ATOM   6685 C CB  . HIS F 3 3   ? -9.716  -2.016  24.655 1.00 43.61 ? 3   HIS F CB  1 
ATOM   6686 C CG  . HIS F 3 3   ? -10.256 -2.866  23.545 1.00 43.66 ? 3   HIS F CG  1 
ATOM   6687 N ND1 . HIS F 3 3   ? -11.550 -2.752  23.080 1.00 47.30 ? 3   HIS F ND1 1 
ATOM   6688 C CD2 . HIS F 3 3   ? -9.674  -3.840  22.806 1.00 43.20 ? 3   HIS F CD2 1 
ATOM   6689 C CE1 . HIS F 3 3   ? -11.742 -3.625  22.106 1.00 46.38 ? 3   HIS F CE1 1 
ATOM   6690 N NE2 . HIS F 3 3   ? -10.620 -4.296  21.919 1.00 35.33 ? 3   HIS F NE2 1 
ATOM   6691 N N   . ASP F 3 4   ? -8.409  -2.396  27.927 1.00 34.15 ? 4   ASP F N   1 
ATOM   6692 C CA  . ASP F 3 4   ? -7.774  -1.775  29.084 1.00 27.79 ? 4   ASP F CA  1 
ATOM   6693 C C   . ASP F 3 4   ? -6.426  -1.143  28.733 1.00 25.72 ? 4   ASP F C   1 
ATOM   6694 O O   . ASP F 3 4   ? -5.470  -1.842  28.414 1.00 29.34 ? 4   ASP F O   1 
ATOM   6695 C CB  . ASP F 3 4   ? -7.592  -2.849  30.167 1.00 37.54 ? 4   ASP F CB  1 
ATOM   6696 C CG  . ASP F 3 4   ? -7.143  -2.289  31.514 1.00 35.28 ? 4   ASP F CG  1 
ATOM   6697 O OD1 . ASP F 3 4   ? -6.921  -1.071  31.653 1.00 35.75 ? 4   ASP F OD1 1 
ATOM   6698 O OD2 . ASP F 3 4   ? -7.002  -3.098  32.449 1.00 49.80 ? 4   ASP F OD2 1 
ATOM   6699 N N   . LEU F 3 5   ? -6.351  0.180   28.824 1.00 31.40 ? 5   LEU F N   1 
ATOM   6700 C CA  . LEU F 3 5   ? -5.128  0.920   28.501 1.00 35.20 ? 5   LEU F CA  1 
ATOM   6701 C C   . LEU F 3 5   ? -3.988  0.694   29.493 1.00 37.23 ? 5   LEU F C   1 
ATOM   6702 O O   . LEU F 3 5   ? -2.827  0.991   29.193 1.00 42.67 ? 5   LEU F O   1 
ATOM   6703 C CB  . LEU F 3 5   ? -5.425  2.417   28.410 1.00 30.28 ? 5   LEU F CB  1 
ATOM   6704 C CG  . LEU F 3 5   ? -6.513  2.784   27.410 1.00 32.00 ? 5   LEU F CG  1 
ATOM   6705 C CD1 . LEU F 3 5   ? -6.709  4.287   27.368 1.00 23.31 ? 5   LEU F CD1 1 
ATOM   6706 C CD2 . LEU F 3 5   ? -6.163  2.219   26.031 1.00 28.98 ? 5   LEU F CD2 1 
ATOM   6707 N N   . SER F 3 6   ? -4.319  0.188   30.678 1.00 38.40 ? 6   SER F N   1 
ATOM   6708 C CA  . SER F 3 6   ? -3.314  -0.077  31.701 1.00 38.93 ? 6   SER F CA  1 
ATOM   6709 C C   . SER F 3 6   ? -2.528  -1.334  31.362 1.00 36.61 ? 6   SER F C   1 
ATOM   6710 O O   . SER F 3 6   ? -1.312  -1.358  31.464 1.00 43.15 ? 6   SER F O   1 
ATOM   6711 C CB  . SER F 3 6   ? -3.968  -0.233  33.076 1.00 47.66 ? 6   SER F CB  1 
ATOM   6712 O OG  . SER F 3 6   ? -4.811  0.864   33.378 1.00 54.79 ? 6   SER F OG  1 
ATOM   6713 N N   . THR F 3 7   ? -3.233  -2.375  30.946 1.00 32.56 ? 7   THR F N   1 
ATOM   6714 C CA  . THR F 3 7   ? -2.621  -3.676  30.736 1.00 31.74 ? 7   THR F CA  1 
ATOM   6715 C C   . THR F 3 7   ? -2.434  -4.012  29.249 1.00 37.18 ? 7   THR F C   1 
ATOM   6716 O O   . THR F 3 7   ? -1.741  -4.967  28.894 1.00 33.53 ? 7   THR F O   1 
ATOM   6717 C CB  . THR F 3 7   ? -3.453  -4.774  31.435 1.00 35.82 ? 7   THR F CB  1 
ATOM   6718 O OG1 . THR F 3 7   ? -4.819  -4.667  31.021 1.00 34.74 ? 7   THR F OG1 1 
ATOM   6719 C CG2 . THR F 3 7   ? -3.387  -4.605  32.956 1.00 31.35 ? 7   THR F CG2 1 
ATOM   6720 N N   . ARG F 3 8   ? -3.046  -3.205  28.389 1.00 29.04 ? 8   ARG F N   1 
ATOM   6721 C CA  . ARG F 3 8   ? -3.115  -3.493  26.964 1.00 35.35 ? 8   ARG F CA  1 
ATOM   6722 C C   . ARG F 3 8   ? -3.779  -4.839  26.728 1.00 33.20 ? 8   ARG F C   1 
ATOM   6723 O O   . ARG F 3 8   ? -3.534  -5.491  25.719 1.00 43.14 ? 8   ARG F O   1 
ATOM   6724 C CB  . ARG F 3 8   ? -1.736  -3.423  26.295 1.00 31.96 ? 8   ARG F CB  1 
ATOM   6725 C CG  . ARG F 3 8   ? -0.980  -2.133  26.606 1.00 33.94 ? 8   ARG F CG  1 
ATOM   6726 C CD  . ARG F 3 8   ? 0.122   -1.881  25.604 1.00 28.75 ? 8   ARG F CD  1 
ATOM   6727 N NE  . ARG F 3 8   ? 0.940   -0.716  25.932 1.00 27.64 ? 8   ARG F NE  1 
ATOM   6728 C CZ  . ARG F 3 8   ? 1.943   -0.280  25.172 1.00 31.25 ? 8   ARG F CZ  1 
ATOM   6729 N NH1 . ARG F 3 8   ? 2.234   -0.912  24.035 1.00 29.27 ? 8   ARG F NH1 1 
ATOM   6730 N NH2 . ARG F 3 8   ? 2.646   0.787   25.534 1.00 17.95 ? 8   ARG F NH2 1 
ATOM   6731 N N   . ARG F 3 9   ? -4.641  -5.242  27.654 1.00 31.68 ? 9   ARG F N   1 
ATOM   6732 C CA  . ARG F 3 9   ? -5.356  -6.505  27.517 1.00 34.93 ? 9   ARG F CA  1 
ATOM   6733 C C   . ARG F 3 9   ? -6.864  -6.328  27.479 1.00 31.82 ? 9   ARG F C   1 
ATOM   6734 O O   . ARG F 3 9   ? -7.406  -5.381  28.055 1.00 35.86 ? 9   ARG F O   1 
ATOM   6735 C CB  . ARG F 3 9   ? -4.975  -7.477  28.634 1.00 26.04 ? 9   ARG F CB  1 
ATOM   6736 C CG  . ARG F 3 9   ? -3.585  -8.033  28.501 1.00 28.97 ? 9   ARG F CG  1 
ATOM   6737 C CD  . ARG F 3 9   ? -3.428  -8.860  27.229 1.00 23.40 ? 9   ARG F CD  1 
ATOM   6738 N NE  . ARG F 3 9   ? -4.308  -10.022 27.188 1.00 23.32 ? 9   ARG F NE  1 
ATOM   6739 C CZ  . ARG F 3 9   ? -4.155  -11.114 27.937 1.00 33.55 ? 9   ARG F CZ  1 
ATOM   6740 N NH1 . ARG F 3 9   ? -3.159  -11.202 28.812 1.00 23.09 ? 9   ARG F NH1 1 
ATOM   6741 N NH2 . ARG F 3 9   ? -5.011  -12.123 27.815 1.00 31.80 ? 9   ARG F NH2 1 
ATOM   6742 N N   . LEU F 3 10  ? -7.536  -7.243  26.789 1.00 29.92 ? 10  LEU F N   1 
ATOM   6743 C CA  . LEU F 3 10  ? -8.990  -7.313  26.848 1.00 38.23 ? 10  LEU F CA  1 
ATOM   6744 C C   . LEU F 3 10  ? -9.440  -7.552  28.296 1.00 39.10 ? 10  LEU F C   1 
ATOM   6745 O O   . LEU F 3 10  ? -8.860  -8.357  29.034 1.00 36.00 ? 10  LEU F O   1 
ATOM   6746 C CB  . LEU F 3 10  ? -9.525  -8.407  25.915 1.00 34.16 ? 10  LEU F CB  1 
ATOM   6747 C CG  . LEU F 3 10  ? -9.511  -8.108  24.414 1.00 36.75 ? 10  LEU F CG  1 
ATOM   6748 C CD1 . LEU F 3 10  ? -9.855  -9.361  23.614 1.00 32.18 ? 10  LEU F CD1 1 
ATOM   6749 C CD2 . LEU F 3 10  ? -10.474 -6.990  24.085 1.00 31.74 ? 10  LEU F CD2 1 
ATOM   6750 N N   . LYS F 3 11  ? -10.478 -6.830  28.684 1.00 38.84 ? 11  LYS F N   1 
ATOM   6751 C CA  . LYS F 3 11  ? -10.939 -6.771  30.059 1.00 43.87 ? 11  LYS F CA  1 
ATOM   6752 C C   . LYS F 3 11  ? -12.403 -7.147  30.040 1.00 50.21 ? 11  LYS F C   1 
ATOM   6753 O O   . LYS F 3 11  ? -13.244 -6.349  29.633 1.00 57.04 ? 11  LYS F O   1 
ATOM   6754 C CB  . LYS F 3 11  ? -10.784 -5.333  30.539 1.00 42.97 ? 11  LYS F CB  1 
ATOM   6755 C CG  . LYS F 3 11  ? -11.388 -5.037  31.872 1.00 42.03 ? 11  LYS F CG  1 
ATOM   6756 C CD  . LYS F 3 11  ? -10.379 -5.278  32.956 1.00 53.74 ? 11  LYS F CD  1 
ATOM   6757 C CE  . LYS F 3 11  ? -10.909 -4.812  34.294 1.00 61.02 ? 11  LYS F CE  1 
ATOM   6758 N NZ  . LYS F 3 11  ? -10.139 -5.447  35.392 1.00 57.29 ? 11  LYS F NZ  1 
ATOM   6759 N N   . CYS F 3 12  ? -12.733 -8.357  30.460 1.00 53.39 ? 12  CYS F N   1 
ATOM   6760 C CA  . CYS F 3 12  ? -14.060 -8.870  30.131 1.00 58.25 ? 12  CYS F CA  1 
ATOM   6761 C C   . CYS F 3 12  ? -15.101 -8.840  31.259 1.00 67.70 ? 12  CYS F C   1 
ATOM   6762 O O   . CYS F 3 12  ? -14.800 -8.559  32.423 1.00 69.65 ? 12  CYS F O   1 
ATOM   6763 C CB  . CYS F 3 12  ? -13.925 -10.259 29.516 1.00 60.08 ? 12  CYS F CB  1 
ATOM   6764 S SG  . CYS F 3 12  ? -12.797 -10.264 28.094 1.00 57.95 ? 12  CYS F SG  1 
ATOM   6765 O OXT . CYS F 3 12  ? -16.285 -9.073  31.014 1.00 66.04 ? 12  CYS F OXT 1 
HETATM 6766 P P   . PO4 G 4 .   ? -37.660 -21.346 22.730 0.67 59.37 ? 301 PO4 A P   1 
HETATM 6767 O O1  . PO4 G 4 .   ? -38.690 -21.640 21.653 0.67 45.41 ? 301 PO4 A O1  1 
HETATM 6768 O O2  . PO4 G 4 .   ? -37.564 -19.847 22.961 0.67 33.50 ? 301 PO4 A O2  1 
HETATM 6769 O O3  . PO4 G 4 .   ? -36.311 -21.890 22.291 0.67 40.44 ? 301 PO4 A O3  1 
HETATM 6770 O O4  . PO4 G 4 .   ? -38.090 -22.025 24.016 0.67 39.25 ? 301 PO4 A O4  1 
HETATM 6771 P P   . PO4 H 4 .   ? -19.655 -38.670 63.865 0.63 35.73 ? 302 PO4 A P   1 
HETATM 6772 O O1  . PO4 H 4 .   ? -19.303 -38.995 62.431 0.63 29.33 ? 302 PO4 A O1  1 
HETATM 6773 O O2  . PO4 H 4 .   ? -20.123 -37.232 63.953 0.63 24.78 ? 302 PO4 A O2  1 
HETATM 6774 O O3  . PO4 H 4 .   ? -20.762 -39.590 64.338 0.63 45.18 ? 302 PO4 A O3  1 
HETATM 6775 O O4  . PO4 H 4 .   ? -18.447 -38.887 64.742 0.63 25.84 ? 302 PO4 A O4  1 
HETATM 6776 C C1  . NAG I 5 .   ? -16.163 -49.929 24.024 1.00 58.97 ? 301 NAG B C1  1 
HETATM 6777 C C2  . NAG I 5 .   ? -16.011 -48.705 23.074 1.00 53.57 ? 301 NAG B C2  1 
HETATM 6778 C C3  . NAG I 5 .   ? -15.644 -49.097 21.643 1.00 57.03 ? 301 NAG B C3  1 
HETATM 6779 C C4  . NAG I 5 .   ? -14.415 -50.045 21.671 1.00 62.63 ? 301 NAG B C4  1 
HETATM 6780 C C5  . NAG I 5 .   ? -14.776 -51.236 22.533 1.00 64.95 ? 301 NAG B C5  1 
HETATM 6781 C C6  . NAG I 5 .   ? -13.687 -52.284 22.595 1.00 80.19 ? 301 NAG B C6  1 
HETATM 6782 C C7  . NAG I 5 .   ? -17.517 -46.863 23.814 1.00 49.64 ? 301 NAG B C7  1 
HETATM 6783 C C8  . NAG I 5 .   ? -18.868 -46.233 23.644 1.00 38.04 ? 301 NAG B C8  1 
HETATM 6784 N N2  . NAG I 5 .   ? -17.290 -47.942 23.050 1.00 56.80 ? 301 NAG B N2  1 
HETATM 6785 O O3  . NAG I 5 .   ? -15.352 -47.970 20.853 1.00 58.06 ? 301 NAG B O3  1 
HETATM 6786 O O4  . NAG I 5 .   ? -14.075 -50.450 20.360 1.00 67.11 ? 301 NAG B O4  1 
HETATM 6787 O O5  . NAG I 5 .   ? -14.994 -50.770 23.859 1.00 59.51 ? 301 NAG B O5  1 
HETATM 6788 O O6  . NAG I 5 .   ? -14.180 -53.468 23.211 1.00 83.93 ? 301 NAG B O6  1 
HETATM 6789 O O7  . NAG I 5 .   ? -16.691 -46.422 24.598 1.00 47.22 ? 301 NAG B O7  1 
HETATM 6790 P P   . PO4 J 4 .   ? -43.914 -48.446 36.623 0.66 63.14 ? 302 PO4 B P   1 
HETATM 6791 O O1  . PO4 J 4 .   ? -42.801 -48.866 35.680 0.66 51.36 ? 302 PO4 B O1  1 
HETATM 6792 O O2  . PO4 J 4 .   ? -44.624 -47.241 36.036 0.66 40.58 ? 302 PO4 B O2  1 
HETATM 6793 O O3  . PO4 J 4 .   ? -44.902 -49.583 36.793 0.66 48.81 ? 302 PO4 B O3  1 
HETATM 6794 O O4  . PO4 J 4 .   ? -43.323 -48.108 37.979 0.66 32.96 ? 302 PO4 B O4  1 
HETATM 6795 O OAB . MRY K 6 .   ? -19.541 -4.868  50.304 0.85 26.98 ? 301 MRY C OAB 1 
HETATM 6796 C CAA . MRY K 6 .   ? -18.349 -4.302  50.702 0.85 27.02 ? 301 MRY C CAA 1 
HETATM 6797 C CAC . MRY K 6 .   ? -17.561 -3.785  49.549 0.85 34.95 ? 301 MRY C CAC 1 
HETATM 6798 O OAD . MRY K 6 .   ? -18.378 -2.954  48.815 0.85 39.45 ? 301 MRY C OAD 1 
HETATM 6799 C CAE . MRY K 6 .   ? -16.389 -3.009  50.060 0.85 23.28 ? 301 MRY C CAE 1 
HETATM 6800 O OAF . MRY K 6 .   ? -15.557 -3.819  50.806 0.85 33.51 ? 301 MRY C OAF 1 
HETATM 6801 C CAG . MRY K 6 .   ? -15.623 -2.443  48.910 0.85 34.86 ? 301 MRY C CAG 1 
HETATM 6802 O OAH . MRY K 6 .   ? -14.832 -1.375  49.310 0.85 21.62 ? 301 MRY C OAH 1 
HETATM 6803 C C1  . NAG L 5 .   ? -15.734 9.743   20.365 1.00 53.29 ? 301 NAG D C1  1 
HETATM 6804 C C2  . NAG L 5 .   ? -15.588 8.409   19.584 1.00 57.95 ? 301 NAG D C2  1 
HETATM 6805 C C3  . NAG L 5 .   ? -16.006 8.576   18.106 1.00 59.46 ? 301 NAG D C3  1 
HETATM 6806 C C4  . NAG L 5 .   ? -17.311 9.339   17.969 1.00 54.34 ? 301 NAG D C4  1 
HETATM 6807 C C5  . NAG L 5 .   ? -17.209 10.637  18.747 1.00 64.75 ? 301 NAG D C5  1 
HETATM 6808 C C6  . NAG L 5 .   ? -18.453 11.486  18.681 1.00 70.47 ? 301 NAG D C6  1 
HETATM 6809 C C7  . NAG L 5 .   ? -13.887 6.779   20.299 1.00 50.96 ? 301 NAG D C7  1 
HETATM 6810 C C8  . NAG L 5 .   ? -12.429 6.418   20.270 1.00 44.61 ? 301 NAG D C8  1 
HETATM 6811 N N2  . NAG L 5 .   ? -14.223 7.904   19.670 1.00 52.96 ? 301 NAG D N2  1 
HETATM 6812 O O3  . NAG L 5 .   ? -16.129 7.284   17.514 1.00 60.61 ? 301 NAG D O3  1 
HETATM 6813 O O4  . NAG L 5 .   ? -17.569 9.653   16.601 1.00 63.53 ? 301 NAG D O4  1 
HETATM 6814 O O5  . NAG L 5 .   ? -17.002 10.313  20.125 1.00 61.83 ? 301 NAG D O5  1 
HETATM 6815 O O6  . NAG L 5 .   ? -18.230 12.740  19.309 1.00 69.71 ? 301 NAG D O6  1 
HETATM 6816 O O7  . NAG L 5 .   ? -14.712 6.072   20.875 1.00 60.86 ? 301 NAG D O7  1 
HETATM 6817 P P   . PO4 M 4 .   ? 11.911  10.302  32.941 0.78 45.21 ? 302 PO4 D P   1 
HETATM 6818 O O1  . PO4 M 4 .   ? 11.164  10.917  31.784 0.78 39.06 ? 302 PO4 D O1  1 
HETATM 6819 O O2  . PO4 M 4 .   ? 12.988  11.229  33.465 0.78 29.70 ? 302 PO4 D O2  1 
HETATM 6820 O O3  . PO4 M 4 .   ? 12.524  9.002   32.463 0.78 39.25 ? 302 PO4 D O3  1 
HETATM 6821 O O4  . PO4 M 4 .   ? 10.909  10.055  34.040 0.78 35.01 ? 302 PO4 D O4  1 
HETATM 6822 O O   . HOH N 7 .   ? -31.014 -26.035 33.303 1.00 25.44 ? 401 HOH A O   1 
HETATM 6823 O O   . HOH N 7 .   ? -24.050 -37.987 52.378 1.00 30.10 ? 402 HOH A O   1 
HETATM 6824 O O   . HOH N 7 .   ? -37.881 -21.198 12.222 1.00 37.47 ? 403 HOH A O   1 
HETATM 6825 O O   . HOH N 7 .   ? -33.844 -19.444 13.615 1.00 28.74 ? 404 HOH A O   1 
HETATM 6826 O O   . HOH N 7 .   ? -27.997 -14.793 32.961 1.00 37.23 ? 405 HOH A O   1 
HETATM 6827 O O   . HOH N 7 .   ? -21.230 -45.593 66.678 1.00 33.54 ? 406 HOH A O   1 
HETATM 6828 O O   . HOH N 7 .   ? -20.226 -12.271 25.260 1.00 29.98 ? 407 HOH A O   1 
HETATM 6829 O O   . HOH N 7 .   ? -33.535 -37.087 32.158 1.00 31.57 ? 408 HOH A O   1 
HETATM 6830 O O   . HOH N 7 .   ? -22.657 -25.243 34.778 1.00 27.87 ? 409 HOH A O   1 
HETATM 6831 O O   . HOH N 7 .   ? -20.856 -40.634 58.932 1.00 27.62 ? 410 HOH A O   1 
HETATM 6832 O O   . HOH N 7 .   ? -18.427 -27.700 49.951 1.00 13.98 ? 411 HOH A O   1 
HETATM 6833 O O   . HOH N 7 .   ? -14.875 -20.168 48.137 1.00 30.53 ? 412 HOH A O   1 
HETATM 6834 O O   . HOH N 7 .   ? -19.249 -18.299 45.872 1.00 24.35 ? 413 HOH A O   1 
HETATM 6835 O O   . HOH N 7 .   ? -32.560 -35.882 56.232 1.00 23.93 ? 414 HOH A O   1 
HETATM 6836 O O   . HOH N 7 .   ? -29.803 -19.353 9.218  1.00 26.43 ? 415 HOH A O   1 
HETATM 6837 O O   . HOH N 7 .   ? -25.603 -32.650 26.336 1.00 26.95 ? 416 HOH A O   1 
HETATM 6838 O O   . HOH N 7 .   ? -34.496 -38.835 56.787 1.00 32.40 ? 417 HOH A O   1 
HETATM 6839 O O   . HOH N 7 .   ? -14.013 -18.711 10.874 1.00 29.92 ? 418 HOH A O   1 
HETATM 6840 O O   . HOH N 7 .   ? -23.832 -21.790 4.217  1.00 32.55 ? 419 HOH A O   1 
HETATM 6841 O O   . HOH N 7 .   ? -15.782 -31.577 18.727 1.00 27.73 ? 420 HOH A O   1 
HETATM 6842 O O   . HOH N 7 .   ? -33.847 -22.163 23.658 1.00 20.98 ? 421 HOH A O   1 
HETATM 6843 O O   . HOH N 7 .   ? -26.228 -25.865 33.257 1.00 31.76 ? 422 HOH A O   1 
HETATM 6844 O O   . HOH N 7 .   ? -25.157 -38.971 49.935 1.00 29.50 ? 423 HOH A O   1 
HETATM 6845 O O   . HOH N 7 .   ? -43.907 -39.549 56.743 1.00 30.14 ? 424 HOH A O   1 
HETATM 6846 O O   . HOH N 7 .   ? -17.531 -30.584 56.337 1.00 23.67 ? 425 HOH A O   1 
HETATM 6847 O O   . HOH N 7 .   ? -11.857 -20.743 8.297  1.00 35.15 ? 426 HOH A O   1 
HETATM 6848 O O   . HOH N 7 .   ? -24.265 -27.930 37.393 1.00 31.26 ? 427 HOH A O   1 
HETATM 6849 O O   . HOH N 7 .   ? -33.569 -30.709 24.673 1.00 23.15 ? 428 HOH A O   1 
HETATM 6850 O O   . HOH N 7 .   ? -34.493 -27.970 23.699 1.00 30.93 ? 429 HOH A O   1 
HETATM 6851 O O   . HOH N 7 .   ? -21.363 -42.665 60.879 1.00 31.89 ? 430 HOH A O   1 
HETATM 6852 O O   . HOH N 7 .   ? -17.272 -35.634 51.940 1.00 25.19 ? 431 HOH A O   1 
HETATM 6853 O O   . HOH N 7 .   ? -14.039 -39.292 1.782  1.00 36.99 ? 432 HOH A O   1 
HETATM 6854 O O   . HOH N 7 .   ? -28.434 -15.269 14.760 1.00 36.15 ? 433 HOH A O   1 
HETATM 6855 O O   . HOH N 7 .   ? -30.750 -26.671 29.711 1.00 25.90 ? 434 HOH A O   1 
HETATM 6856 O O   . HOH N 7 .   ? -23.464 -23.744 10.339 1.00 26.10 ? 435 HOH A O   1 
HETATM 6857 O O   . HOH N 7 .   ? -21.826 -11.932 38.640 1.00 26.25 ? 436 HOH A O   1 
HETATM 6858 O O   . HOH N 7 .   ? -26.308 -34.085 48.316 1.00 19.96 ? 437 HOH A O   1 
HETATM 6859 O O   . HOH N 7 .   ? -27.554 -45.318 6.324  1.00 25.13 ? 438 HOH A O   1 
HETATM 6860 O O   . HOH N 7 .   ? -36.284 -18.861 11.603 1.00 39.43 ? 439 HOH A O   1 
HETATM 6861 O O   . HOH N 7 .   ? -11.764 -37.168 7.456  1.00 38.98 ? 440 HOH A O   1 
HETATM 6862 O O   . HOH N 7 .   ? -20.324 -13.865 23.163 1.00 36.23 ? 441 HOH A O   1 
HETATM 6863 O O   . HOH N 7 .   ? -24.580 -23.908 32.883 1.00 32.92 ? 442 HOH A O   1 
HETATM 6864 O O   . HOH N 7 .   ? -22.141 -41.475 14.299 1.00 23.88 ? 443 HOH A O   1 
HETATM 6865 O O   . HOH N 7 .   ? -34.569 -24.775 34.613 1.00 29.42 ? 444 HOH A O   1 
HETATM 6866 O O   . HOH N 7 .   ? -18.120 -40.262 8.392  1.00 28.34 ? 445 HOH A O   1 
HETATM 6867 O O   . HOH N 7 .   ? -19.665 -25.570 18.762 1.00 24.06 ? 446 HOH A O   1 
HETATM 6868 O O   . HOH N 7 .   ? -36.866 -28.765 16.178 1.00 24.72 ? 447 HOH A O   1 
HETATM 6869 O O   . HOH N 7 .   ? -33.272 -12.350 21.434 1.00 42.20 ? 448 HOH A O   1 
HETATM 6870 O O   . HOH N 7 .   ? -18.370 -22.805 55.050 1.00 29.86 ? 449 HOH A O   1 
HETATM 6871 O O   . HOH N 7 .   ? -40.915 -37.438 60.403 1.00 39.30 ? 450 HOH A O   1 
HETATM 6872 O O   . HOH N 7 .   ? -13.123 -28.079 66.408 1.00 30.43 ? 451 HOH A O   1 
HETATM 6873 O O   . HOH N 7 .   ? -21.711 -14.033 14.915 1.00 39.31 ? 452 HOH A O   1 
HETATM 6874 O O   . HOH N 7 .   ? -16.935 -19.986 18.987 1.00 43.91 ? 453 HOH A O   1 
HETATM 6875 O O   . HOH N 7 .   ? -17.218 -16.993 44.090 1.00 20.69 ? 454 HOH A O   1 
HETATM 6876 O O   . HOH N 7 .   ? -22.328 -37.395 -0.644 1.00 32.45 ? 455 HOH A O   1 
HETATM 6877 O O   . HOH N 7 .   ? -20.190 -30.309 52.120 1.00 43.54 ? 456 HOH A O   1 
HETATM 6878 O O   . HOH N 7 .   ? -13.852 -25.847 16.127 1.00 29.03 ? 457 HOH A O   1 
HETATM 6879 O O   . HOH N 7 .   ? -22.910 -48.313 69.150 1.00 31.98 ? 458 HOH A O   1 
HETATM 6880 O O   . HOH N 7 .   ? -34.765 -19.683 47.752 1.00 23.64 ? 459 HOH A O   1 
HETATM 6881 O O   . HOH N 7 .   ? -19.041 -16.619 20.542 1.00 29.11 ? 460 HOH A O   1 
HETATM 6882 O O   . HOH N 7 .   ? -29.069 -49.515 57.140 1.00 30.54 ? 461 HOH A O   1 
HETATM 6883 O O   . HOH N 7 .   ? -18.284 -34.197 55.433 1.00 31.14 ? 462 HOH A O   1 
HETATM 6884 O O   . HOH N 7 .   ? -34.311 -22.192 12.553 1.00 29.03 ? 463 HOH A O   1 
HETATM 6885 O O   . HOH N 7 .   ? -23.516 -29.587 0.546  1.00 24.86 ? 464 HOH A O   1 
HETATM 6886 O O   . HOH N 7 .   ? -21.585 -28.476 65.833 1.00 22.47 ? 465 HOH A O   1 
HETATM 6887 O O   . HOH N 7 .   ? -20.138 -25.665 44.342 1.00 23.33 ? 466 HOH A O   1 
HETATM 6888 O O   . HOH N 7 .   ? -24.293 -13.979 57.300 1.00 31.50 ? 467 HOH A O   1 
HETATM 6889 O O   . HOH N 7 .   ? -23.645 -26.383 -0.879 1.00 27.78 ? 468 HOH A O   1 
HETATM 6890 O O   . HOH N 7 .   ? -19.588 -34.771 46.698 1.00 22.88 ? 469 HOH A O   1 
HETATM 6891 O O   . HOH N 7 .   ? -24.876 -8.479  54.104 1.00 33.86 ? 470 HOH A O   1 
HETATM 6892 O O   . HOH N 7 .   ? -25.602 -17.583 60.609 1.00 18.09 ? 471 HOH A O   1 
HETATM 6893 O O   . HOH N 7 .   ? -12.018 -31.905 12.775 1.00 30.29 ? 472 HOH A O   1 
HETATM 6894 O O   . HOH N 7 .   ? -38.712 -27.499 19.232 1.00 38.54 ? 473 HOH A O   1 
HETATM 6895 O O   . HOH N 7 .   ? -31.542 -22.998 40.911 1.00 17.51 ? 474 HOH A O   1 
HETATM 6896 O O   . HOH N 7 .   ? -21.501 -41.190 54.826 1.00 37.48 ? 475 HOH A O   1 
HETATM 6897 O O   . HOH N 7 .   ? -20.019 -41.671 2.000  1.00 32.00 ? 476 HOH A O   1 
HETATM 6898 O O   . HOH N 7 .   ? -25.603 -42.483 8.124  1.00 24.34 ? 477 HOH A O   1 
HETATM 6899 O O   . HOH N 7 .   ? -23.938 -32.613 40.843 1.00 31.28 ? 478 HOH A O   1 
HETATM 6900 O O   . HOH N 7 .   ? -31.373 -24.504 39.472 1.00 33.11 ? 479 HOH A O   1 
HETATM 6901 O O   . HOH N 7 .   ? -15.465 -33.540 53.190 1.00 25.40 ? 480 HOH A O   1 
HETATM 6902 O O   . HOH N 7 .   ? -27.488 -40.703 51.889 1.00 45.50 ? 481 HOH A O   1 
HETATM 6903 O O   . HOH N 7 .   ? -11.486 -32.096 1.691  1.00 42.77 ? 482 HOH A O   1 
HETATM 6904 O O   . HOH N 7 .   ? -27.296 -25.033 2.266  1.00 27.40 ? 483 HOH A O   1 
HETATM 6905 O O   . HOH N 7 .   ? -18.742 -42.792 2.858  1.00 41.23 ? 484 HOH A O   1 
HETATM 6906 O O   . HOH N 7 .   ? -19.234 -39.680 51.277 1.00 34.89 ? 485 HOH A O   1 
HETATM 6907 O O   . HOH N 7 .   ? -16.319 -38.370 14.495 1.00 34.92 ? 486 HOH A O   1 
HETATM 6908 O O   . HOH N 7 .   ? -22.553 -8.064  57.905 1.00 25.71 ? 487 HOH A O   1 
HETATM 6909 O O   . HOH N 7 .   ? -31.796 -28.485 1.209  1.00 22.00 ? 488 HOH A O   1 
HETATM 6910 O O   . HOH N 7 .   ? -21.318 -25.389 65.719 1.00 23.35 ? 489 HOH A O   1 
HETATM 6911 O O   . HOH N 7 .   ? -21.482 -35.574 -1.511 1.00 36.40 ? 490 HOH A O   1 
HETATM 6912 O O   . HOH N 7 .   ? -15.731 -20.227 57.696 1.00 36.11 ? 491 HOH A O   1 
HETATM 6913 O O   . HOH N 7 .   ? -21.814 -19.957 34.916 1.00 33.74 ? 492 HOH A O   1 
HETATM 6914 O O   . HOH N 7 .   ? -17.616 -31.564 54.061 1.00 26.18 ? 493 HOH A O   1 
HETATM 6915 O O   . HOH N 7 .   ? -37.015 -32.815 25.088 1.00 23.03 ? 494 HOH A O   1 
HETATM 6916 O O   . HOH N 7 .   ? -17.566 -45.409 6.376  1.00 33.76 ? 495 HOH A O   1 
HETATM 6917 O O   . HOH N 7 .   ? -17.486 -14.836 51.359 1.00 25.11 ? 496 HOH A O   1 
HETATM 6918 O O   . HOH N 7 .   ? -16.904 -18.862 61.560 1.00 41.44 ? 497 HOH A O   1 
HETATM 6919 O O   . HOH N 7 .   ? -21.975 -9.587  49.933 1.00 36.13 ? 498 HOH A O   1 
HETATM 6920 O O   . HOH N 7 .   ? -20.744 -20.103 37.657 1.00 28.95 ? 499 HOH A O   1 
HETATM 6921 O O   . HOH N 7 .   ? -31.837 -36.638 73.918 1.00 34.78 ? 500 HOH A O   1 
HETATM 6922 O O   . HOH N 7 .   ? -32.557 -26.783 36.527 1.00 49.46 ? 501 HOH A O   1 
HETATM 6923 O O   . HOH N 7 .   ? -21.492 -39.842 52.257 1.00 34.64 ? 502 HOH A O   1 
HETATM 6924 O O   . HOH N 7 .   ? -17.287 -18.965 48.486 1.00 20.93 ? 503 HOH A O   1 
HETATM 6925 O O   . HOH N 7 .   ? -26.376 -36.466 47.577 1.00 20.18 ? 504 HOH A O   1 
HETATM 6926 O O   . HOH N 7 .   ? -16.315 -28.662 49.553 1.00 40.76 ? 505 HOH A O   1 
HETATM 6927 O O   . HOH N 7 .   ? -29.495 -36.945 74.883 1.00 36.94 ? 506 HOH A O   1 
HETATM 6928 O O   . HOH N 7 .   ? -15.189 -36.942 50.299 1.00 34.42 ? 507 HOH A O   1 
HETATM 6929 O O   . HOH N 7 .   ? -40.645 -35.832 59.375 1.00 42.87 ? 508 HOH A O   1 
HETATM 6930 O O   . HOH N 7 .   ? -18.367 -39.825 16.205 1.00 30.52 ? 509 HOH A O   1 
HETATM 6931 O O   . HOH N 7 .   ? -36.045 -30.191 26.316 1.00 21.50 ? 510 HOH A O   1 
HETATM 6932 O O   . HOH O 7 .   ? -47.368 -41.452 6.748  1.00 35.20 ? 401 HOH B O   1 
HETATM 6933 O O   . HOH O 7 .   ? -27.462 -59.829 16.030 1.00 40.13 ? 402 HOH B O   1 
HETATM 6934 O O   . HOH O 7 .   ? -37.580 -43.750 4.132  1.00 35.40 ? 403 HOH B O   1 
HETATM 6935 O O   . HOH O 7 .   ? -29.482 -59.155 17.036 1.00 47.23 ? 404 HOH B O   1 
HETATM 6936 O O   . HOH O 7 .   ? -22.273 -43.030 22.006 1.00 28.75 ? 405 HOH B O   1 
HETATM 6937 O O   . HOH O 7 .   ? -37.156 -23.058 44.976 1.00 21.55 ? 406 HOH B O   1 
HETATM 6938 O O   . HOH O 7 .   ? -32.704 -39.475 38.008 1.00 17.92 ? 407 HOH B O   1 
HETATM 6939 O O   . HOH O 7 .   ? -36.980 -40.654 8.677  1.00 25.46 ? 408 HOH B O   1 
HETATM 6940 O O   . HOH O 7 .   ? -21.077 -39.206 15.996 1.00 17.88 ? 409 HOH B O   1 
HETATM 6941 O O   . HOH O 7 .   ? -29.872 -61.742 26.191 1.00 43.83 ? 410 HOH B O   1 
HETATM 6942 O O   . HOH O 7 .   ? -48.356 -31.661 53.104 1.00 20.71 ? 411 HOH B O   1 
HETATM 6943 O O   . HOH O 7 .   ? -36.951 -50.769 27.404 1.00 31.08 ? 412 HOH B O   1 
HETATM 6944 O O   . HOH O 7 .   ? -30.572 -47.586 33.206 1.00 23.82 ? 413 HOH B O   1 
HETATM 6945 O O   . HOH O 7 .   ? -46.807 -46.777 11.096 1.00 31.26 ? 414 HOH B O   1 
HETATM 6946 O O   . HOH O 7 .   ? -18.637 -47.482 19.534 1.00 35.79 ? 415 HOH B O   1 
HETATM 6947 O O   . HOH O 7 .   ? -28.771 -34.769 5.892  1.00 24.70 ? 416 HOH B O   1 
HETATM 6948 O O   . HOH O 7 .   ? -14.612 -39.011 25.690 1.00 40.65 ? 417 HOH B O   1 
HETATM 6949 O O   . HOH O 7 .   ? -38.410 -54.296 22.321 1.00 32.49 ? 418 HOH B O   1 
HETATM 6950 O O   . HOH O 7 .   ? -43.961 -31.709 39.353 1.00 24.83 ? 419 HOH B O   1 
HETATM 6951 O O   . HOH O 7 .   ? -49.940 -37.000 44.098 1.00 30.79 ? 420 HOH B O   1 
HETATM 6952 O O   . HOH O 7 .   ? -47.469 -49.505 37.733 1.00 39.64 ? 421 HOH B O   1 
HETATM 6953 O O   . HOH O 7 .   ? -17.033 -46.751 8.409  1.00 35.17 ? 422 HOH B O   1 
HETATM 6954 O O   . HOH O 7 .   ? -30.304 -37.842 38.322 1.00 28.03 ? 423 HOH B O   1 
HETATM 6955 O O   . HOH O 7 .   ? -21.155 -36.234 21.018 1.00 24.76 ? 424 HOH B O   1 
HETATM 6956 O O   . HOH O 7 .   ? -24.967 -46.981 37.031 1.00 31.37 ? 425 HOH B O   1 
HETATM 6957 O O   . HOH O 7 .   ? -34.893 -40.887 7.112  1.00 21.09 ? 426 HOH B O   1 
HETATM 6958 O O   . HOH O 7 .   ? -26.374 -46.850 50.664 1.00 31.70 ? 427 HOH B O   1 
HETATM 6959 O O   . HOH O 7 .   ? -27.579 -46.069 36.160 1.00 21.49 ? 428 HOH B O   1 
HETATM 6960 O O   . HOH O 7 .   ? -28.632 -54.461 6.843  1.00 29.76 ? 429 HOH B O   1 
HETATM 6961 O O   . HOH O 7 .   ? -41.366 -37.537 19.902 1.00 20.89 ? 430 HOH B O   1 
HETATM 6962 O O   . HOH O 7 .   ? -40.763 -42.552 54.639 1.00 26.63 ? 431 HOH B O   1 
HETATM 6963 O O   . HOH O 7 .   ? -19.543 -52.218 18.681 1.00 33.43 ? 432 HOH B O   1 
HETATM 6964 O O   . HOH O 7 .   ? -18.368 -45.946 11.988 1.00 34.64 ? 433 HOH B O   1 
HETATM 6965 O O   . HOH O 7 .   ? -19.500 -49.840 22.143 1.00 36.68 ? 434 HOH B O   1 
HETATM 6966 O O   . HOH O 7 .   ? -34.588 -43.494 30.427 1.00 21.92 ? 435 HOH B O   1 
HETATM 6967 O O   . HOH O 7 .   ? -22.918 -48.894 41.062 1.00 31.09 ? 436 HOH B O   1 
HETATM 6968 O O   . HOH O 7 .   ? -42.420 -20.683 43.806 1.00 39.09 ? 437 HOH B O   1 
HETATM 6969 O O   . HOH O 7 .   ? -22.143 -49.255 33.981 1.00 29.94 ? 438 HOH B O   1 
HETATM 6970 O O   . HOH O 7 .   ? -37.027 -55.406 8.194  1.00 34.34 ? 439 HOH B O   1 
HETATM 6971 O O   . HOH O 7 .   ? -36.355 -53.475 44.556 1.00 32.00 ? 440 HOH B O   1 
HETATM 6972 O O   . HOH O 7 .   ? -40.640 -28.546 38.162 1.00 34.93 ? 441 HOH B O   1 
HETATM 6973 O O   . HOH O 7 .   ? -34.634 -29.932 38.835 1.00 28.31 ? 442 HOH B O   1 
HETATM 6974 O O   . HOH O 7 .   ? -41.835 -34.835 4.797  1.00 43.00 ? 443 HOH B O   1 
HETATM 6975 O O   . HOH O 7 .   ? -29.106 -43.794 2.671  1.00 22.84 ? 444 HOH B O   1 
HETATM 6976 O O   . HOH O 7 .   ? -26.398 -61.181 23.955 1.00 32.30 ? 445 HOH B O   1 
HETATM 6977 O O   . HOH O 7 .   ? -38.352 -33.094 38.723 1.00 25.85 ? 446 HOH B O   1 
HETATM 6978 O O   . HOH O 7 .   ? -42.480 -52.079 4.879  1.00 38.02 ? 447 HOH B O   1 
HETATM 6979 O O   . HOH O 7 .   ? -29.790 -58.569 31.144 1.00 35.97 ? 448 HOH B O   1 
HETATM 6980 O O   . HOH O 7 .   ? -28.713 -37.651 48.575 1.00 39.70 ? 449 HOH B O   1 
HETATM 6981 O O   . HOH O 7 .   ? -37.303 -44.337 35.957 1.00 30.29 ? 450 HOH B O   1 
HETATM 6982 O O   . HOH O 7 .   ? -21.140 -42.784 50.009 1.00 33.30 ? 451 HOH B O   1 
HETATM 6983 O O   . HOH O 7 .   ? -27.862 -36.436 45.358 1.00 41.27 ? 452 HOH B O   1 
HETATM 6984 O O   . HOH O 7 .   ? -51.000 -38.992 45.705 1.00 22.58 ? 453 HOH B O   1 
HETATM 6985 O O   . HOH O 7 .   ? -49.132 -57.916 13.724 1.00 41.04 ? 454 HOH B O   1 
HETATM 6986 O O   . HOH O 7 .   ? -44.311 -23.112 44.839 1.00 27.17 ? 455 HOH B O   1 
HETATM 6987 O O   . HOH O 7 .   ? -36.598 -55.122 20.275 1.00 32.76 ? 456 HOH B O   1 
HETATM 6988 O O   . HOH O 7 .   ? -18.708 -52.802 23.525 1.00 40.98 ? 457 HOH B O   1 
HETATM 6989 O O   . HOH O 7 .   ? -30.943 -54.524 4.984  1.00 30.37 ? 458 HOH B O   1 
HETATM 6990 O O   . HOH O 7 .   ? -37.784 -36.547 37.276 1.00 26.76 ? 459 HOH B O   1 
HETATM 6991 O O   . HOH O 7 .   ? -38.878 -34.327 19.098 1.00 26.86 ? 460 HOH B O   1 
HETATM 6992 O O   . HOH O 7 .   ? -33.979 -26.807 38.508 1.00 21.26 ? 461 HOH B O   1 
HETATM 6993 O O   . HOH O 7 .   ? -37.198 -28.995 38.044 1.00 35.74 ? 462 HOH B O   1 
HETATM 6994 O O   . HOH O 7 .   ? -32.865 -54.806 -0.429 1.00 29.62 ? 463 HOH B O   1 
HETATM 6995 O O   . HOH O 7 .   ? -36.586 -50.151 2.420  1.00 33.71 ? 464 HOH B O   1 
HETATM 6996 O O   . HOH O 7 .   ? -49.826 -30.197 56.955 1.00 41.29 ? 465 HOH B O   1 
HETATM 6997 O O   . HOH O 7 .   ? -22.065 -39.804 41.273 1.00 32.56 ? 466 HOH B O   1 
HETATM 6998 O O   . HOH O 7 .   ? -20.436 -54.906 36.842 1.00 39.94 ? 467 HOH B O   1 
HETATM 6999 O O   . HOH O 7 .   ? -45.583 -42.359 42.132 1.00 25.56 ? 468 HOH B O   1 
HETATM 7000 O O   . HOH O 7 .   ? -44.217 -36.209 56.433 1.00 23.47 ? 469 HOH B O   1 
HETATM 7001 O O   . HOH O 7 .   ? -19.869 -51.212 46.219 1.00 30.72 ? 470 HOH B O   1 
HETATM 7002 O O   . HOH O 7 .   ? -25.582 -52.457 7.084  1.00 24.18 ? 471 HOH B O   1 
HETATM 7003 O O   . HOH O 7 .   ? -25.911 -51.107 4.830  1.00 32.88 ? 472 HOH B O   1 
HETATM 7004 O O   . HOH O 7 .   ? -40.804 -19.896 46.208 1.00 28.70 ? 473 HOH B O   1 
HETATM 7005 O O   . HOH O 7 .   ? -41.872 -43.403 1.781  1.00 33.00 ? 474 HOH B O   1 
HETATM 7006 O O   . HOH O 7 .   ? -23.702 -64.904 27.733 1.00 35.08 ? 475 HOH B O   1 
HETATM 7007 O O   . HOH O 7 .   ? -39.573 -22.842 38.627 1.00 38.36 ? 476 HOH B O   1 
HETATM 7008 O O   . HOH O 7 .   ? -19.643 -43.052 14.484 1.00 36.28 ? 477 HOH B O   1 
HETATM 7009 O O   . HOH O 7 .   ? -50.912 -37.221 58.948 1.00 31.16 ? 478 HOH B O   1 
HETATM 7010 O O   . HOH O 7 .   ? -47.645 -56.723 9.982  1.00 42.60 ? 479 HOH B O   1 
HETATM 7011 O O   . HOH O 7 .   ? -34.235 -33.466 37.553 1.00 34.33 ? 480 HOH B O   1 
HETATM 7012 O O   . HOH O 7 .   ? -27.362 -63.793 25.392 1.00 44.97 ? 481 HOH B O   1 
HETATM 7013 O O   . HOH O 7 .   ? -46.860 -54.729 9.008  1.00 43.54 ? 482 HOH B O   1 
HETATM 7014 O O   . HOH O 7 .   ? -37.467 -24.087 39.547 1.00 33.28 ? 483 HOH B O   1 
HETATM 7015 O O   . HOH O 7 .   ? -32.219 -36.696 38.244 1.00 31.40 ? 484 HOH B O   1 
HETATM 7016 O O   . HOH O 7 .   ? -30.431 -45.845 1.813  1.00 30.76 ? 485 HOH B O   1 
HETATM 7017 O O   . HOH O 7 .   ? -29.278 -62.974 22.975 1.00 45.86 ? 486 HOH B O   1 
HETATM 7018 O O   . HOH O 7 .   ? -37.064 -34.442 37.718 1.00 35.80 ? 487 HOH B O   1 
HETATM 7019 O O   . HOH O 7 .   ? -18.503 -50.227 19.397 1.00 37.87 ? 488 HOH B O   1 
HETATM 7020 O O   . HOH O 7 .   ? -45.183 -41.305 39.935 1.00 30.69 ? 489 HOH B O   1 
HETATM 7021 O O   . HOH O 7 .   ? -52.773 -29.738 43.576 1.00 28.49 ? 490 HOH B O   1 
HETATM 7022 O O   . HOH O 7 .   ? -40.908 -31.010 38.741 1.00 34.89 ? 491 HOH B O   1 
HETATM 7023 O O   . HOH O 7 .   ? -22.790 -46.671 34.713 1.00 32.46 ? 492 HOH B O   1 
HETATM 7024 O O   . HOH O 7 .   ? -38.061 -53.249 28.734 1.00 41.70 ? 493 HOH B O   1 
HETATM 7025 O O   . HOH O 7 .   ? -47.405 -23.222 42.661 1.00 22.05 ? 494 HOH B O   1 
HETATM 7026 O O   . HOH O 7 .   ? -26.867 -55.652 7.441  1.00 36.56 ? 495 HOH B O   1 
HETATM 7027 O O   . HOH O 7 .   ? -46.692 -22.644 45.049 1.00 19.73 ? 496 HOH B O   1 
HETATM 7028 O O   . HOH O 7 .   ? -47.578 -20.406 45.486 1.00 29.66 ? 497 HOH B O   1 
HETATM 7029 O O   . HOH P 7 .   ? 11.839  8.548   53.023 1.00 45.16 ? 401 HOH C O   1 
HETATM 7030 O O   . HOH P 7 .   ? -3.378  -2.717  46.567 1.00 47.39 ? 402 HOH C O   1 
HETATM 7031 O O   . HOH P 7 .   ? 4.998   -19.157 38.437 1.00 35.71 ? 403 HOH C O   1 
HETATM 7032 O O   . HOH P 7 .   ? -12.881 7.934   59.105 1.00 26.75 ? 404 HOH C O   1 
HETATM 7033 O O   . HOH P 7 .   ? 0.645   12.029  65.023 1.00 40.62 ? 405 HOH C O   1 
HETATM 7034 O O   . HOH P 7 .   ? -5.034  3.442   49.746 1.00 19.49 ? 406 HOH C O   1 
HETATM 7035 O O   . HOH P 7 .   ? -6.915  9.100   53.819 1.00 36.85 ? 407 HOH C O   1 
HETATM 7036 O O   . HOH P 7 .   ? 7.619   -18.169 10.774 1.00 38.58 ? 408 HOH C O   1 
HETATM 7037 O O   . HOH P 7 .   ? -16.980 -21.023 5.678  1.00 31.66 ? 409 HOH C O   1 
HETATM 7038 O O   . HOH P 7 .   ? -18.639 -0.791  48.234 1.00 40.61 ? 410 HOH C O   1 
HETATM 7039 O O   . HOH P 7 .   ? -11.273 8.607   63.671 1.00 26.80 ? 411 HOH C O   1 
HETATM 7040 O O   . HOH P 7 .   ? -4.918  -12.617 30.869 1.00 27.13 ? 412 HOH C O   1 
HETATM 7041 O O   . HOH P 7 .   ? -9.123  -3.634  -2.760 1.00 36.23 ? 413 HOH C O   1 
HETATM 7042 O O   . HOH P 7 .   ? -7.663  -8.952  -1.636 1.00 28.66 ? 414 HOH C O   1 
HETATM 7043 O O   . HOH P 7 .   ? -10.175 -8.927  66.732 1.00 38.00 ? 415 HOH C O   1 
HETATM 7044 O O   . HOH P 7 .   ? -14.337 -19.898 25.819 1.00 23.74 ? 416 HOH C O   1 
HETATM 7045 O O   . HOH P 7 .   ? -18.818 -9.331  10.612 1.00 28.19 ? 417 HOH C O   1 
HETATM 7046 O O   . HOH P 7 .   ? -8.635  1.321   48.966 1.00 21.48 ? 418 HOH C O   1 
HETATM 7047 O O   . HOH P 7 .   ? 5.519   -16.349 41.775 1.00 36.89 ? 419 HOH C O   1 
HETATM 7048 O O   . HOH P 7 .   ? -19.046 -11.124 0.141  1.00 40.13 ? 420 HOH C O   1 
HETATM 7049 O O   . HOH P 7 .   ? -5.748  -6.493  23.745 1.00 28.34 ? 421 HOH C O   1 
HETATM 7050 O O   . HOH P 7 .   ? 7.084   -18.766 21.994 1.00 47.11 ? 422 HOH C O   1 
HETATM 7051 O O   . HOH P 7 .   ? -13.870 -5.441  53.560 1.00 22.14 ? 423 HOH C O   1 
HETATM 7052 O O   . HOH P 7 .   ? 3.179   -17.147 22.318 1.00 31.62 ? 424 HOH C O   1 
HETATM 7053 O O   . HOH P 7 .   ? 0.576   -0.581  53.465 1.00 19.68 ? 425 HOH C O   1 
HETATM 7054 O O   . HOH P 7 .   ? 3.683   -19.903 12.165 1.00 32.64 ? 426 HOH C O   1 
HETATM 7055 O O   . HOH P 7 .   ? -8.689  -8.939  32.665 1.00 47.41 ? 427 HOH C O   1 
HETATM 7056 O O   . HOH P 7 .   ? 2.536   3.151   53.761 1.00 17.62 ? 428 HOH C O   1 
HETATM 7057 O O   . HOH P 7 .   ? -13.562 4.568   8.136  1.00 35.48 ? 429 HOH C O   1 
HETATM 7058 O O   . HOH P 7 .   ? 2.656   -11.991 36.226 1.00 25.04 ? 430 HOH C O   1 
HETATM 7059 O O   . HOH P 7 .   ? -9.525  -17.637 58.933 1.00 36.23 ? 431 HOH C O   1 
HETATM 7060 O O   . HOH P 7 .   ? 7.753   -21.948 21.008 1.00 36.02 ? 432 HOH C O   1 
HETATM 7061 O O   . HOH P 7 .   ? -11.000 -8.058  35.060 1.00 53.96 ? 433 HOH C O   1 
HETATM 7062 O O   . HOH P 7 .   ? 4.574   -7.490  26.784 1.00 29.65 ? 434 HOH C O   1 
HETATM 7063 O O   . HOH P 7 .   ? -6.685  -22.661 10.651 1.00 38.73 ? 435 HOH C O   1 
HETATM 7064 O O   . HOH P 7 .   ? -13.596 -2.339  52.518 1.00 18.35 ? 436 HOH C O   1 
HETATM 7065 O O   . HOH P 7 .   ? -11.614 4.652   55.318 1.00 19.92 ? 437 HOH C O   1 
HETATM 7066 O O   . HOH P 7 .   ? 3.307   -10.693 21.639 1.00 26.12 ? 438 HOH C O   1 
HETATM 7067 O O   . HOH P 7 .   ? -1.269  -24.749 14.016 1.00 33.35 ? 439 HOH C O   1 
HETATM 7068 O O   . HOH P 7 .   ? -0.131  -11.969 28.143 1.00 24.91 ? 440 HOH C O   1 
HETATM 7069 O O   . HOH P 7 .   ? -0.441  -13.168 37.329 1.00 20.26 ? 441 HOH C O   1 
HETATM 7070 O O   . HOH P 7 .   ? -7.050  -10.633 35.077 1.00 31.48 ? 442 HOH C O   1 
HETATM 7071 O O   . HOH P 7 .   ? -11.552 -6.621  49.460 1.00 32.99 ? 443 HOH C O   1 
HETATM 7072 O O   . HOH P 7 .   ? -10.696 5.997   57.459 1.00 24.76 ? 444 HOH C O   1 
HETATM 7073 O O   . HOH P 7 .   ? -6.234  12.420  58.099 1.00 30.27 ? 445 HOH C O   1 
HETATM 7074 O O   . HOH P 7 .   ? 2.406   -8.762  22.302 1.00 24.73 ? 446 HOH C O   1 
HETATM 7075 O O   . HOH P 7 .   ? 2.891   -13.389 33.117 1.00 27.31 ? 447 HOH C O   1 
HETATM 7076 O O   . HOH P 7 .   ? -12.906 -1.116  5.305  1.00 33.43 ? 448 HOH C O   1 
HETATM 7077 O O   . HOH P 7 .   ? 0.206   -14.909 39.397 1.00 17.13 ? 449 HOH C O   1 
HETATM 7078 O O   . HOH P 7 .   ? -6.678  -16.623 8.463  1.00 23.28 ? 450 HOH C O   1 
HETATM 7079 O O   . HOH P 7 .   ? -0.068  -31.496 22.764 1.00 35.18 ? 451 HOH C O   1 
HETATM 7080 O O   . HOH P 7 .   ? 8.411   -12.221 14.336 1.00 36.89 ? 452 HOH C O   1 
HETATM 7081 O O   . HOH P 7 .   ? -10.630 -22.214 7.550  1.00 35.17 ? 453 HOH C O   1 
HETATM 7082 O O   . HOH P 7 .   ? -0.130  -21.080 8.456  1.00 32.98 ? 454 HOH C O   1 
HETATM 7083 O O   . HOH P 7 .   ? -6.427  11.348  59.880 1.00 34.35 ? 455 HOH C O   1 
HETATM 7084 O O   . HOH P 7 .   ? -12.954 -19.141 44.270 1.00 31.60 ? 456 HOH C O   1 
HETATM 7085 O O   . HOH P 7 .   ? 0.044   -3.089  33.530 1.00 26.48 ? 457 HOH C O   1 
HETATM 7086 O O   . HOH P 7 .   ? 2.063   1.274   62.181 1.00 33.94 ? 458 HOH C O   1 
HETATM 7087 O O   . HOH P 7 .   ? 2.005   -21.218 4.930  1.00 39.43 ? 459 HOH C O   1 
HETATM 7088 O O   . HOH P 7 .   ? -14.804 -10.425 19.677 1.00 37.34 ? 460 HOH C O   1 
HETATM 7089 O O   . HOH P 7 .   ? -11.304 10.312  59.818 1.00 34.27 ? 461 HOH C O   1 
HETATM 7090 O O   . HOH P 7 .   ? -6.757  8.751   66.982 1.00 36.13 ? 462 HOH C O   1 
HETATM 7091 O O   . HOH P 7 .   ? -10.034 -7.931  63.397 1.00 29.73 ? 463 HOH C O   1 
HETATM 7092 O O   . HOH P 7 .   ? -1.177  -13.424 60.697 1.00 24.76 ? 464 HOH C O   1 
HETATM 7093 O O   . HOH P 7 .   ? -4.880  -23.476 10.012 1.00 39.57 ? 465 HOH C O   1 
HETATM 7094 O O   . HOH P 7 .   ? -12.928 -4.212  -2.874 1.00 41.84 ? 466 HOH C O   1 
HETATM 7095 O O   . HOH P 7 .   ? -13.676 -20.456 1.007  1.00 30.87 ? 467 HOH C O   1 
HETATM 7096 O O   . HOH P 7 .   ? -2.224  -23.746 31.447 1.00 37.99 ? 468 HOH C O   1 
HETATM 7097 O O   . HOH P 7 .   ? 6.319   -10.578 14.130 1.00 31.80 ? 469 HOH C O   1 
HETATM 7098 O O   . HOH P 7 .   ? 0.447   -19.660 45.901 1.00 27.88 ? 470 HOH C O   1 
HETATM 7099 O O   . HOH P 7 .   ? -13.990 3.843   3.200  1.00 37.38 ? 471 HOH C O   1 
HETATM 7100 O O   . HOH P 7 .   ? -2.380  -2.272  44.507 1.00 32.59 ? 472 HOH C O   1 
HETATM 7101 O O   . HOH P 7 .   ? -10.874 -14.722 16.927 1.00 23.50 ? 473 HOH C O   1 
HETATM 7102 O O   . HOH P 7 .   ? -14.415 -4.374  12.390 1.00 20.23 ? 474 HOH C O   1 
HETATM 7103 O O   . HOH P 7 .   ? -15.803 -15.896 58.888 1.00 34.12 ? 475 HOH C O   1 
HETATM 7104 O O   . HOH P 7 .   ? -17.125 -15.352 25.180 1.00 33.46 ? 476 HOH C O   1 
HETATM 7105 O O   . HOH P 7 .   ? -13.513 -21.012 50.427 1.00 31.37 ? 477 HOH C O   1 
HETATM 7106 O O   . HOH P 7 .   ? 7.365   1.862   58.790 1.00 44.23 ? 478 HOH C O   1 
HETATM 7107 O O   . HOH P 7 .   ? -6.105  0.871   69.600 1.00 23.13 ? 479 HOH C O   1 
HETATM 7108 O O   . HOH P 7 .   ? -6.003  1.808   5.041  1.00 21.97 ? 480 HOH C O   1 
HETATM 7109 O O   . HOH P 7 .   ? -1.122  8.514   51.202 1.00 34.93 ? 481 HOH C O   1 
HETATM 7110 O O   . HOH P 7 .   ? 1.879   -7.689  65.012 1.00 33.37 ? 482 HOH C O   1 
HETATM 7111 O O   . HOH P 7 .   ? -16.697 -13.620 57.682 1.00 37.62 ? 483 HOH C O   1 
HETATM 7112 O O   . HOH P 7 .   ? -14.122 -1.646  45.260 1.00 30.23 ? 484 HOH C O   1 
HETATM 7113 O O   . HOH P 7 .   ? 8.081   -12.029 16.748 1.00 35.91 ? 485 HOH C O   1 
HETATM 7114 O O   . HOH P 7 .   ? -16.984 -16.466 49.562 1.00 19.49 ? 486 HOH C O   1 
HETATM 7115 O O   . HOH P 7 .   ? 5.588   -16.081 3.993  1.00 39.37 ? 487 HOH C O   1 
HETATM 7116 O O   . HOH P 7 .   ? -12.110 -2.987  43.293 1.00 22.08 ? 488 HOH C O   1 
HETATM 7117 O O   . HOH P 7 .   ? -17.748 -5.911  52.826 1.00 36.78 ? 489 HOH C O   1 
HETATM 7118 O O   . HOH P 7 .   ? 5.848   -6.096  22.513 1.00 32.84 ? 490 HOH C O   1 
HETATM 7119 O O   . HOH P 7 .   ? 12.067  2.638   54.143 1.00 28.30 ? 491 HOH C O   1 
HETATM 7120 O O   . HOH P 7 .   ? 8.756   -23.830 15.975 1.00 41.36 ? 492 HOH C O   1 
HETATM 7121 O O   . HOH P 7 .   ? 2.661   -1.685  63.005 1.00 29.17 ? 493 HOH C O   1 
HETATM 7122 O O   . HOH P 7 .   ? -14.637 -10.577 42.273 1.00 40.09 ? 494 HOH C O   1 
HETATM 7123 O O   . HOH P 7 .   ? -20.103 -8.883  51.007 1.00 33.36 ? 495 HOH C O   1 
HETATM 7124 O O   . HOH P 7 .   ? 3.920   -19.983 4.476  1.00 44.63 ? 496 HOH C O   1 
HETATM 7125 O O   . HOH P 7 .   ? 7.586   -12.885 7.092  1.00 35.49 ? 497 HOH C O   1 
HETATM 7126 O O   . HOH P 7 .   ? -16.899 -7.938  52.325 1.00 35.73 ? 498 HOH C O   1 
HETATM 7127 O O   . HOH P 7 .   ? 6.011   -14.030 37.810 1.00 31.88 ? 499 HOH C O   1 
HETATM 7128 O O   . HOH P 7 .   ? -14.766 -13.551 64.347 1.00 49.26 ? 500 HOH C O   1 
HETATM 7129 O O   . HOH P 7 .   ? 12.546  10.850  52.593 1.00 37.89 ? 501 HOH C O   1 
HETATM 7130 O O   . HOH P 7 .   ? -11.161 2.925   49.100 1.00 32.37 ? 502 HOH C O   1 
HETATM 7131 O O   . HOH P 7 .   ? -0.743  -12.838 63.404 1.00 39.84 ? 503 HOH C O   1 
HETATM 7132 O O   . HOH P 7 .   ? -4.640  12.406  61.954 1.00 45.91 ? 504 HOH C O   1 
HETATM 7133 O O   . HOH P 7 .   ? 8.921   -15.015 6.118  1.00 30.62 ? 505 HOH C O   1 
HETATM 7134 O O   . HOH P 7 .   ? -12.481 -7.544  -4.425 1.00 37.68 ? 506 HOH C O   1 
HETATM 7135 O O   . HOH P 7 .   ? -15.372 -17.980 59.451 1.00 32.99 ? 507 HOH C O   1 
HETATM 7136 O O   . HOH P 7 .   ? 13.134  6.527   54.534 1.00 33.77 ? 508 HOH C O   1 
HETATM 7137 O O   . HOH P 7 .   ? 6.652   -6.509  27.866 1.00 43.03 ? 509 HOH C O   1 
HETATM 7138 O O   . HOH P 7 .   ? 3.548   -8.058  62.687 1.00 29.65 ? 510 HOH C O   1 
HETATM 7139 O O   . HOH P 7 .   ? -13.555 -0.749  13.057 1.00 29.11 ? 511 HOH C O   1 
HETATM 7140 O O   . HOH P 7 .   ? 4.883   -8.471  23.956 1.00 25.09 ? 512 HOH C O   1 
HETATM 7141 O O   . HOH Q 7 .   ? 9.489   -1.196  17.185 1.00 32.15 ? 401 HOH D O   1 
HETATM 7142 O O   . HOH Q 7 .   ? 0.622   2.136   34.977 1.00 20.62 ? 402 HOH D O   1 
HETATM 7143 O O   . HOH Q 7 .   ? 17.331  -6.658  51.914 1.00 30.97 ? 403 HOH D O   1 
HETATM 7144 O O   . HOH Q 7 .   ? 14.470  4.271   16.741 1.00 34.42 ? 404 HOH D O   1 
HETATM 7145 O O   . HOH Q 7 .   ? 10.781  -1.181  56.163 1.00 34.02 ? 405 HOH D O   1 
HETATM 7146 O O   . HOH Q 7 .   ? -2.362  -5.665  3.204  1.00 28.57 ? 406 HOH D O   1 
HETATM 7147 O O   . HOH Q 7 .   ? 14.081  4.976   39.600 1.00 30.46 ? 407 HOH D O   1 
HETATM 7148 O O   . HOH Q 7 .   ? -5.667  9.784   46.785 1.00 20.03 ? 408 HOH D O   1 
HETATM 7149 O O   . HOH Q 7 .   ? -12.375 11.918  14.568 1.00 39.86 ? 409 HOH D O   1 
HETATM 7150 O O   . HOH Q 7 .   ? 5.058   -7.696  14.715 1.00 28.75 ? 410 HOH D O   1 
HETATM 7151 O O   . HOH Q 7 .   ? -4.213  4.487   2.829  1.00 27.00 ? 411 HOH D O   1 
HETATM 7152 O O   . HOH Q 7 .   ? -0.984  9.143   29.509 1.00 21.70 ? 412 HOH D O   1 
HETATM 7153 O O   . HOH Q 7 .   ? -9.506  3.232   18.826 1.00 30.57 ? 413 HOH D O   1 
HETATM 7154 O O   . HOH Q 7 .   ? 10.949  1.674   36.188 1.00 14.63 ? 414 HOH D O   1 
HETATM 7155 O O   . HOH Q 7 .   ? 10.656  0.603   20.476 1.00 28.64 ? 415 HOH D O   1 
HETATM 7156 O O   . HOH Q 7 .   ? -8.143  8.571   33.500 1.00 38.61 ? 416 HOH D O   1 
HETATM 7157 O O   . HOH Q 7 .   ? -12.684 9.764   18.350 1.00 39.04 ? 417 HOH D O   1 
HETATM 7158 O O   . HOH Q 7 .   ? -9.580  -3.977  18.823 1.00 34.53 ? 418 HOH D O   1 
HETATM 7159 O O   . HOH Q 7 .   ? -4.496  7.950   32.588 1.00 27.16 ? 419 HOH D O   1 
HETATM 7160 O O   . HOH Q 7 .   ? 0.525   1.045   -1.607 1.00 29.82 ? 420 HOH D O   1 
HETATM 7161 O O   . HOH Q 7 .   ? 16.177  -4.623  50.607 1.00 26.23 ? 421 HOH D O   1 
HETATM 7162 O O   . HOH Q 7 .   ? 15.175  7.448   7.511  1.00 36.34 ? 422 HOH D O   1 
HETATM 7163 O O   . HOH Q 7 .   ? 18.170  -0.782  41.468 1.00 26.91 ? 423 HOH D O   1 
HETATM 7164 O O   . HOH Q 7 .   ? 6.902   -4.685  36.407 1.00 21.89 ? 424 HOH D O   1 
HETATM 7165 O O   . HOH Q 7 .   ? -10.028 23.462  19.522 1.00 33.60 ? 425 HOH D O   1 
HETATM 7166 O O   . HOH Q 7 .   ? 6.045   15.499  17.948 1.00 38.46 ? 426 HOH D O   1 
HETATM 7167 O O   . HOH Q 7 .   ? 14.326  -0.504  23.252 1.00 35.17 ? 427 HOH D O   1 
HETATM 7168 O O   . HOH Q 7 .   ? -2.458  2.388   -0.548 1.00 30.71 ? 428 HOH D O   1 
HETATM 7169 O O   . HOH Q 7 .   ? -6.224  22.054  19.121 1.00 31.65 ? 429 HOH D O   1 
HETATM 7170 O O   . HOH Q 7 .   ? 11.310  -0.738  54.162 1.00 23.00 ? 430 HOH D O   1 
HETATM 7171 O O   . HOH Q 7 .   ? 11.155  9.567   19.705 1.00 32.14 ? 431 HOH D O   1 
HETATM 7172 O O   . HOH Q 7 .   ? -8.033  22.739  30.819 1.00 34.28 ? 432 HOH D O   1 
HETATM 7173 O O   . HOH Q 7 .   ? -2.685  20.035  26.358 1.00 33.61 ? 433 HOH D O   1 
HETATM 7174 O O   . HOH Q 7 .   ? 5.578   -14.537 43.185 1.00 21.63 ? 434 HOH D O   1 
HETATM 7175 O O   . HOH Q 7 .   ? -13.234 7.317   15.727 1.00 33.41 ? 435 HOH D O   1 
HETATM 7176 O O   . HOH Q 7 .   ? -10.567 -0.975  12.885 1.00 15.53 ? 436 HOH D O   1 
HETATM 7177 O O   . HOH Q 7 .   ? 3.392   0.862   3.941  1.00 25.67 ? 437 HOH D O   1 
HETATM 7178 O O   . HOH Q 7 .   ? 2.884   4.968   27.301 1.00 14.82 ? 438 HOH D O   1 
HETATM 7179 O O   . HOH Q 7 .   ? -13.026 12.993  19.286 1.00 37.44 ? 439 HOH D O   1 
HETATM 7180 O O   . HOH Q 7 .   ? 5.701   6.499   32.577 1.00 22.46 ? 440 HOH D O   1 
HETATM 7181 O O   . HOH Q 7 .   ? 10.099  2.657   -1.321 1.00 37.57 ? 441 HOH D O   1 
HETATM 7182 O O   . HOH Q 7 .   ? -5.072  15.180  38.619 1.00 27.55 ? 442 HOH D O   1 
HETATM 7183 O O   . HOH Q 7 .   ? -9.402  0.946   11.457 1.00 22.92 ? 443 HOH D O   1 
HETATM 7184 O O   . HOH Q 7 .   ? 10.055  12.451  1.259  1.00 44.39 ? 444 HOH D O   1 
HETATM 7185 O O   . HOH Q 7 .   ? 15.986  1.052   4.201  1.00 29.94 ? 445 HOH D O   1 
HETATM 7186 O O   . HOH Q 7 .   ? 6.716   11.948  28.807 1.00 34.17 ? 446 HOH D O   1 
HETATM 7187 O O   . HOH Q 7 .   ? -9.683  10.379  30.151 1.00 42.48 ? 447 HOH D O   1 
HETATM 7188 O O   . HOH Q 7 .   ? -11.667 2.428   10.627 1.00 26.04 ? 448 HOH D O   1 
HETATM 7189 O O   . HOH Q 7 .   ? 2.917   15.418  43.969 1.00 31.75 ? 449 HOH D O   1 
HETATM 7190 O O   . HOH Q 7 .   ? 8.805   12.422  25.896 1.00 40.95 ? 450 HOH D O   1 
HETATM 7191 O O   . HOH Q 7 .   ? 2.840   0.756   51.995 1.00 26.50 ? 451 HOH D O   1 
HETATM 7192 O O   . HOH Q 7 .   ? -10.500 5.229   46.635 1.00 32.31 ? 452 HOH D O   1 
HETATM 7193 O O   . HOH Q 7 .   ? 12.311  -5.706  36.857 1.00 29.56 ? 453 HOH D O   1 
HETATM 7194 O O   . HOH Q 7 .   ? -0.008  9.557   49.789 1.00 33.38 ? 454 HOH D O   1 
HETATM 7195 O O   . HOH Q 7 .   ? 1.231   7.753   -2.049 1.00 22.42 ? 455 HOH D O   1 
HETATM 7196 O O   . HOH Q 7 .   ? 2.451   16.117  5.187  1.00 28.37 ? 456 HOH D O   1 
HETATM 7197 O O   . HOH Q 7 .   ? 14.288  1.062   54.011 1.00 36.59 ? 457 HOH D O   1 
HETATM 7198 O O   . HOH Q 7 .   ? 15.034  -6.389  12.048 1.00 40.76 ? 458 HOH D O   1 
HETATM 7199 O O   . HOH Q 7 .   ? 20.292  -6.343  11.245 1.00 45.17 ? 459 HOH D O   1 
HETATM 7200 O O   . HOH Q 7 .   ? -14.129 16.012  26.150 1.00 28.10 ? 460 HOH D O   1 
HETATM 7201 O O   . HOH Q 7 .   ? 12.819  -13.904 43.340 1.00 25.67 ? 461 HOH D O   1 
HETATM 7202 O O   . HOH Q 7 .   ? 13.718  -6.032  14.636 1.00 41.52 ? 462 HOH D O   1 
HETATM 7203 O O   . HOH Q 7 .   ? -1.263  20.060  24.200 1.00 29.12 ? 463 HOH D O   1 
HETATM 7204 O O   . HOH Q 7 .   ? -1.400  7.381   -1.495 1.00 25.54 ? 464 HOH D O   1 
HETATM 7205 O O   . HOH Q 7 .   ? 13.507  10.709  29.662 1.00 41.76 ? 465 HOH D O   1 
HETATM 7206 O O   . HOH Q 7 .   ? 4.832   15.326  4.192  1.00 36.59 ? 466 HOH D O   1 
HETATM 7207 O O   . HOH Q 7 .   ? 8.203   -13.297 35.707 1.00 37.01 ? 467 HOH D O   1 
HETATM 7208 O O   . HOH Q 7 .   ? -7.791  14.675  40.628 1.00 38.91 ? 468 HOH D O   1 
HETATM 7209 O O   . HOH Q 7 .   ? -7.465  13.679  38.250 1.00 28.79 ? 469 HOH D O   1 
HETATM 7210 O O   . HOH Q 7 .   ? 4.736   15.956  16.496 1.00 50.06 ? 470 HOH D O   1 
HETATM 7211 O O   . HOH Q 7 .   ? 11.618  -17.250 46.710 1.00 22.16 ? 471 HOH D O   1 
HETATM 7212 O O   . HOH Q 7 .   ? 8.630   -9.043  35.781 1.00 36.61 ? 472 HOH D O   1 
HETATM 7213 O O   . HOH Q 7 .   ? 10.137  -17.129 44.933 1.00 24.40 ? 473 HOH D O   1 
HETATM 7214 O O   . HOH Q 7 .   ? -0.087  -0.682  35.427 1.00 31.68 ? 474 HOH D O   1 
HETATM 7215 O O   . HOH Q 7 .   ? -1.899  4.418   -1.483 1.00 33.91 ? 475 HOH D O   1 
HETATM 7216 O O   . HOH Q 7 .   ? 5.497   14.007  44.025 1.00 37.99 ? 476 HOH D O   1 
HETATM 7217 O O   . HOH Q 7 .   ? 11.251  -16.351 42.975 1.00 34.18 ? 477 HOH D O   1 
HETATM 7218 O O   . HOH Q 7 .   ? -6.382  23.540  32.936 1.00 39.55 ? 478 HOH D O   1 
HETATM 7219 O O   . HOH Q 7 .   ? 9.328   -1.630  20.908 1.00 38.75 ? 479 HOH D O   1 
HETATM 7220 O O   . HOH Q 7 .   ? -13.603 9.778   15.341 1.00 40.47 ? 480 HOH D O   1 
HETATM 7221 O O   . HOH Q 7 .   ? 8.997   -0.039  56.437 1.00 29.56 ? 481 HOH D O   1 
HETATM 7222 O O   . HOH Q 7 .   ? 9.483   -6.903  36.345 1.00 32.13 ? 482 HOH D O   1 
HETATM 7223 O O   . HOH R 7 .   ? -30.867 -38.922 31.647 1.00 28.05 ? 101 HOH E O   1 
HETATM 7224 O O   . HOH R 7 .   ? -25.135 -24.750 30.468 1.00 29.12 ? 102 HOH E O   1 
HETATM 7225 O O   . HOH R 7 .   ? -24.552 -36.335 37.789 1.00 30.12 ? 103 HOH E O   1 
HETATM 7226 O O   . HOH R 7 .   ? -32.036 -39.108 35.459 1.00 28.95 ? 104 HOH E O   1 
HETATM 7227 O O   . HOH R 7 .   ? -24.639 -35.299 27.771 1.00 34.70 ? 105 HOH E O   1 
HETATM 7228 O O   . HOH R 7 .   ? -31.071 -34.606 36.485 1.00 33.15 ? 106 HOH E O   1 
HETATM 7229 O O   . HOH S 7 .   ? -15.410 -7.498  23.045 1.00 44.00 ? 101 HOH F O   1 
HETATM 7230 O O   . HOH S 7 .   ? -0.190  0.780   28.974 1.00 26.78 ? 102 HOH F O   1 
HETATM 7231 O O   . HOH S 7 .   ? -11.824 -10.288 32.069 1.00 44.61 ? 103 HOH F 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   1   1   ASP ASP A . n 
A 1 2   ILE 2   2   2   ILE ILE A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   GLN 6   6   6   GLN GLN A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  SER 12  12  12  SER SER A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  SER 20  20  20  SER SER A . n 
A 1 21  PHE 21  21  21  PHE PHE A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  CYS 23  23  23  CYS CYS A . n 
A 1 24  ARG 24  24  24  ARG ARG A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  SER 26  26  26  SER SER A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  THR 31  31  31  THR THR A . n 
A 1 32  ASN 32  32  32  ASN ASN A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  TRP 35  35  35  TRP TRP A . n 
A 1 36  TYR 36  36  36  TYR TYR A . n 
A 1 37  GLN 37  37  37  GLN GLN A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  ASN 41  41  41  ASN ASN A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  ILE 48  48  48  ILE ILE A . n 
A 1 49  LYS 49  49  49  LYS LYS A . n 
A 1 50  TYR 50  50  50  TYR TYR A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  ILE 58  58  58  ILE ILE A . n 
A 1 59  PRO 59  59  59  PRO PRO A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  PHE 62  62  62  PHE PHE A . n 
A 1 63  SER 63  63  63  SER SER A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  ASP 70  70  70  ASP ASP A . n 
A 1 71  PHE 71  71  71  PHE PHE A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ILE 75  75  75  ILE ILE A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  TYR 87  87  87  TYR TYR A . n 
A 1 88  CYS 88  88  88  CYS CYS A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  GLN 90  90  90  GLN GLN A . n 
A 1 91  ASN 91  91  91  ASN ASN A . n 
A 1 92  ASN 92  92  92  ASN ASN A . n 
A 1 93  ASN 93  93  93  ASN ASN A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 THR 102 102 102 THR THR A . n 
A 1 103 LYS 103 103 103 LYS LYS A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 LYS 107 107 107 LYS LYS A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 SER 114 114 114 SER SER A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 PRO 119 119 119 PRO PRO A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 GLN 124 124 124 GLN GLN A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 SER 127 127 127 SER SER A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 CYS 134 134 134 CYS CYS A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 ASN 137 137 137 ASN ASN A . n 
A 1 138 ASN 138 138 138 ASN ASN A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 ARG 142 142 142 ARG ARG A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 VAL 146 146 146 VAL VAL A . n 
A 1 147 GLN 147 147 147 GLN GLN A . n 
A 1 148 TRP 148 148 148 TRP TRP A . n 
A 1 149 LYS 149 149 149 LYS LYS A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 GLY 157 157 157 GLY GLY A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 GLN 160 160 160 GLN GLN A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 VAL 163 163 163 VAL VAL A . n 
A 1 164 THR 164 164 164 THR THR A . n 
A 1 165 GLU 165 165 165 GLU GLU A . n 
A 1 166 GLN 166 166 166 GLN GLN A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 ASP 170 170 170 ASP ASP A . n 
A 1 171 SER 171 171 171 SER SER A . n 
A 1 172 THR 172 172 172 THR THR A . n 
A 1 173 TYR 173 173 173 TYR TYR A . n 
A 1 174 SER 174 174 174 SER SER A . n 
A 1 175 LEU 175 175 175 LEU LEU A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 THR 180 180 180 THR THR A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 LYS 183 183 183 LYS LYS A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 HIS 189 189 189 HIS HIS A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 CYS 194 194 194 CYS CYS A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 THR 197 197 197 THR THR A . n 
A 1 198 HIS 198 198 198 HIS HIS A . n 
A 1 199 GLN 199 199 199 GLN GLN A . n 
A 1 200 GLY 200 200 200 GLY GLY A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 SER 202 202 202 SER SER A . n 
A 1 203 SER 203 203 203 SER SER A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 VAL 205 205 205 VAL VAL A . n 
A 1 206 THR 206 206 206 THR THR A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 PHE 209 209 209 PHE PHE A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 ARG 211 211 211 ARG ARG A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 ALA 213 213 ?   ?   ?   A . n 
B 2 1   GLN 1   1   1   GLN GLN B . n 
B 2 2   VAL 2   2   2   VAL VAL B . n 
B 2 3   GLN 3   3   3   GLN GLN B . n 
B 2 4   LEU 4   4   4   LEU LEU B . n 
B 2 5   LYS 5   5   5   LYS LYS B . n 
B 2 6   GLN 6   6   6   GLN GLN B . n 
B 2 7   SER 7   7   7   SER SER B . n 
B 2 8   GLY 8   8   8   GLY GLY B . n 
B 2 9   PRO 9   9   9   PRO PRO B . n 
B 2 10  GLY 10  10  10  GLY GLY B . n 
B 2 11  LEU 11  11  11  LEU LEU B . n 
B 2 12  VAL 12  12  12  VAL VAL B . n 
B 2 13  GLN 13  13  13  GLN GLN B . n 
B 2 14  PRO 14  14  14  PRO PRO B . n 
B 2 15  SER 15  15  15  SER SER B . n 
B 2 16  GLN 16  16  16  GLN GLN B . n 
B 2 17  SER 17  17  17  SER SER B . n 
B 2 18  LEU 18  18  18  LEU LEU B . n 
B 2 19  SER 19  19  19  SER SER B . n 
B 2 20  ILE 20  20  20  ILE ILE B . n 
B 2 21  THR 21  21  21  THR THR B . n 
B 2 22  CYS 22  22  22  CYS CYS B . n 
B 2 23  THR 23  23  23  THR THR B . n 
B 2 24  VAL 24  24  24  VAL VAL B . n 
B 2 25  SER 25  25  25  SER SER B . n 
B 2 26  GLY 26  26  26  GLY GLY B . n 
B 2 27  PHE 27  27  27  PHE PHE B . n 
B 2 28  SER 28  28  28  SER SER B . n 
B 2 29  LEU 29  29  29  LEU LEU B . n 
B 2 30  THR 30  30  30  THR THR B . n 
B 2 31  ASN 31  31  31  ASN ASN B . n 
B 2 32  TYR 32  32  32  TYR TYR B . n 
B 2 33  GLY 33  33  33  GLY GLY B . n 
B 2 34  VAL 34  34  34  VAL VAL B . n 
B 2 35  HIS 35  35  35  HIS HIS B . n 
B 2 36  TRP 36  36  36  TRP TRP B . n 
B 2 37  VAL 37  37  37  VAL VAL B . n 
B 2 38  ARG 38  38  38  ARG ARG B . n 
B 2 39  GLN 39  39  39  GLN GLN B . n 
B 2 40  SER 40  40  40  SER SER B . n 
B 2 41  PRO 41  41  41  PRO PRO B . n 
B 2 42  GLY 42  42  42  GLY GLY B . n 
B 2 43  LYS 43  43  43  LYS LYS B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  LEU 45  45  45  LEU LEU B . n 
B 2 46  GLU 46  46  46  GLU GLU B . n 
B 2 47  TRP 47  47  47  TRP TRP B . n 
B 2 48  LEU 48  48  48  LEU LEU B . n 
B 2 49  GLY 49  49  49  GLY GLY B . n 
B 2 50  VAL 50  50  50  VAL VAL B . n 
B 2 51  ILE 51  51  51  ILE ILE B . n 
B 2 52  TRP 52  52  52  TRP TRP B . n 
B 2 53  SER 53  53  53  SER SER B . n 
B 2 54  GLY 54  54  54  GLY GLY B . n 
B 2 55  GLY 55  55  55  GLY GLY B . n 
B 2 56  ASN 56  56  56  ASN ASN B . n 
B 2 57  THR 57  57  57  THR THR B . n 
B 2 58  ASP 58  58  58  ASP ASP B . n 
B 2 59  TYR 59  59  59  TYR TYR B . n 
B 2 60  ASN 60  60  60  ASN ASN B . n 
B 2 61  THR 61  61  61  THR THR B . n 
B 2 62  PRO 62  62  62  PRO PRO B . n 
B 2 63  PHE 63  63  63  PHE PHE B . n 
B 2 64  THR 64  64  64  THR THR B . n 
B 2 65  SER 65  65  65  SER SER B . n 
B 2 66  ARG 66  66  66  ARG ARG B . n 
B 2 67  LEU 67  67  67  LEU LEU B . n 
B 2 68  SER 68  68  68  SER SER B . n 
B 2 69  ILE 69  69  69  ILE ILE B . n 
B 2 70  ASN 70  70  70  ASN ASN B . n 
B 2 71  LYS 71  71  71  LYS LYS B . n 
B 2 72  ASP 72  72  72  ASP ASP B . n 
B 2 73  ASN 73  73  73  ASN ASN B . n 
B 2 74  SER 74  74  74  SER SER B . n 
B 2 75  LYS 75  75  75  LYS LYS B . n 
B 2 76  SER 76  76  76  SER SER B . n 
B 2 77  GLN 77  77  77  GLN GLN B . n 
B 2 78  VAL 78  78  78  VAL VAL B . n 
B 2 79  PHE 79  79  79  PHE PHE B . n 
B 2 80  PHE 80  80  80  PHE PHE B . n 
B 2 81  LYS 81  81  81  LYS LYS B . n 
B 2 82  MET 82  82  82  MET MET B . n 
B 2 83  ASN 83  83  83  ASN ASN B . n 
B 2 84  SER 84  84  84  SER SER B . n 
B 2 85  LEU 85  85  85  LEU LEU B . n 
B 2 86  GLN 86  86  86  GLN GLN B . n 
B 2 87  SER 87  87  87  SER SER B . n 
B 2 88  ASN 88  88  88  ASN ASN B . n 
B 2 89  ASP 89  89  89  ASP ASP B . n 
B 2 90  THR 90  90  90  THR THR B . n 
B 2 91  ALA 91  91  91  ALA ALA B . n 
B 2 92  ILE 92  92  92  ILE ILE B . n 
B 2 93  TYR 93  93  93  TYR TYR B . n 
B 2 94  TYR 94  94  94  TYR TYR B . n 
B 2 95  CYS 95  95  95  CYS CYS B . n 
B 2 96  ALA 96  96  96  ALA ALA B . n 
B 2 97  ARG 97  97  97  ARG ARG B . n 
B 2 98  ALA 98  98  98  ALA ALA B . n 
B 2 99  LEU 99  99  99  LEU LEU B . n 
B 2 100 THR 100 100 100 THR THR B . n 
B 2 101 TYR 101 101 101 TYR TYR B . n 
B 2 102 TYR 102 102 102 TYR TYR B . n 
B 2 103 ASP 103 103 103 ASP ASP B . n 
B 2 104 TYR 104 104 104 TYR TYR B . n 
B 2 105 GLU 105 105 105 GLU GLU B . n 
B 2 106 PHE 106 106 106 PHE PHE B . n 
B 2 107 ALA 107 107 107 ALA ALA B . n 
B 2 108 TYR 108 108 108 TYR TYR B . n 
B 2 109 TRP 109 109 109 TRP TRP B . n 
B 2 110 GLY 110 110 110 GLY GLY B . n 
B 2 111 GLN 111 111 111 GLN GLN B . n 
B 2 112 GLY 112 112 112 GLY GLY B . n 
B 2 113 THR 113 113 113 THR THR B . n 
B 2 114 LEU 114 114 114 LEU LEU B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 THR 116 116 116 THR THR B . n 
B 2 117 VAL 117 117 117 VAL VAL B . n 
B 2 118 SER 118 118 118 SER SER B . n 
B 2 119 ALA 119 119 119 ALA ALA B . n 
B 2 120 ALA 120 120 120 ALA ALA B . n 
B 2 121 SER 121 121 121 SER SER B . n 
B 2 122 THR 122 122 122 THR THR B . n 
B 2 123 LYS 123 123 123 LYS LYS B . n 
B 2 124 GLY 124 124 124 GLY GLY B . n 
B 2 125 PRO 125 125 125 PRO PRO B . n 
B 2 126 SER 126 126 126 SER SER B . n 
B 2 127 VAL 127 127 127 VAL VAL B . n 
B 2 128 PHE 128 128 128 PHE PHE B . n 
B 2 129 PRO 129 129 129 PRO PRO B . n 
B 2 130 LEU 130 130 130 LEU LEU B . n 
B 2 131 ALA 131 131 131 ALA ALA B . n 
B 2 132 PRO 132 132 132 PRO PRO B . n 
B 2 133 SER 133 133 133 SER SER B . n 
B 2 134 SER 134 134 134 SER SER B . n 
B 2 135 LYS 135 135 135 LYS LYS B . n 
B 2 136 SER 136 136 136 SER SER B . n 
B 2 137 THR 137 137 137 THR THR B . n 
B 2 138 SER 138 138 138 SER SER B . n 
B 2 139 GLY 139 139 139 GLY GLY B . n 
B 2 140 GLY 140 140 140 GLY GLY B . n 
B 2 141 THR 141 141 141 THR THR B . n 
B 2 142 ALA 142 142 142 ALA ALA B . n 
B 2 143 ALA 143 143 143 ALA ALA B . n 
B 2 144 LEU 144 144 144 LEU LEU B . n 
B 2 145 GLY 145 145 145 GLY GLY B . n 
B 2 146 CYS 146 146 146 CYS CYS B . n 
B 2 147 LEU 147 147 147 LEU LEU B . n 
B 2 148 VAL 148 148 148 VAL VAL B . n 
B 2 149 LYS 149 149 149 LYS LYS B . n 
B 2 150 ASP 150 150 150 ASP ASP B . n 
B 2 151 TYR 151 151 151 TYR TYR B . n 
B 2 152 PHE 152 152 152 PHE PHE B . n 
B 2 153 PRO 153 153 153 PRO PRO B . n 
B 2 154 GLU 154 154 154 GLU GLU B . n 
B 2 155 PRO 155 155 155 PRO PRO B . n 
B 2 156 VAL 156 156 156 VAL VAL B . n 
B 2 157 THR 157 157 157 THR THR B . n 
B 2 158 VAL 158 158 158 VAL VAL B . n 
B 2 159 SER 159 159 159 SER SER B . n 
B 2 160 TRP 160 160 160 TRP TRP B . n 
B 2 161 ASN 161 161 161 ASN ASN B . n 
B 2 162 SER 162 162 162 SER SER B . n 
B 2 163 GLY 163 163 163 GLY GLY B . n 
B 2 164 ALA 164 164 164 ALA ALA B . n 
B 2 165 LEU 165 165 165 LEU LEU B . n 
B 2 166 THR 166 166 166 THR THR B . n 
B 2 167 SER 167 167 167 SER SER B . n 
B 2 168 GLY 168 168 168 GLY GLY B . n 
B 2 169 VAL 169 169 169 VAL VAL B . n 
B 2 170 HIS 170 170 170 HIS HIS B . n 
B 2 171 THR 171 171 171 THR THR B . n 
B 2 172 PHE 172 172 172 PHE PHE B . n 
B 2 173 PRO 173 173 173 PRO PRO B . n 
B 2 174 ALA 174 174 174 ALA ALA B . n 
B 2 175 VAL 175 175 175 VAL VAL B . n 
B 2 176 LEU 176 176 176 LEU LEU B . n 
B 2 177 GLN 177 177 177 GLN GLN B . n 
B 2 178 SER 178 178 178 SER SER B . n 
B 2 179 SER 179 179 179 SER SER B . n 
B 2 180 GLY 180 180 180 GLY GLY B . n 
B 2 181 LEU 181 181 181 LEU LEU B . n 
B 2 182 TYR 182 182 182 TYR TYR B . n 
B 2 183 SER 183 183 183 SER SER B . n 
B 2 184 LEU 184 184 184 LEU LEU B . n 
B 2 185 SER 185 185 185 SER SER B . n 
B 2 186 SER 186 186 186 SER SER B . n 
B 2 187 VAL 187 187 187 VAL VAL B . n 
B 2 188 VAL 188 188 188 VAL VAL B . n 
B 2 189 THR 189 189 189 THR THR B . n 
B 2 190 VAL 190 190 190 VAL VAL B . n 
B 2 191 PRO 191 191 191 PRO PRO B . n 
B 2 192 SER 192 192 192 SER SER B . n 
B 2 193 SER 193 193 193 SER SER B . n 
B 2 194 SER 194 194 194 SER SER B . n 
B 2 195 LEU 195 195 195 LEU LEU B . n 
B 2 196 GLY 196 196 196 GLY GLY B . n 
B 2 197 THR 197 197 197 THR THR B . n 
B 2 198 GLN 198 198 198 GLN GLN B . n 
B 2 199 THR 199 199 199 THR THR B . n 
B 2 200 TYR 200 200 200 TYR TYR B . n 
B 2 201 ILE 201 201 201 ILE ILE B . n 
B 2 202 CYS 202 202 202 CYS CYS B . n 
B 2 203 ASN 203 203 203 ASN ASN B . n 
B 2 204 VAL 204 204 204 VAL VAL B . n 
B 2 205 ASN 205 205 205 ASN ASN B . n 
B 2 206 HIS 206 206 206 HIS HIS B . n 
B 2 207 LYS 207 207 207 LYS LYS B . n 
B 2 208 PRO 208 208 208 PRO PRO B . n 
B 2 209 SER 209 209 209 SER SER B . n 
B 2 210 ASN 210 210 210 ASN ASN B . n 
B 2 211 THR 211 211 211 THR THR B . n 
B 2 212 LYS 212 212 212 LYS LYS B . n 
B 2 213 VAL 213 213 213 VAL VAL B . n 
B 2 214 ASP 214 214 214 ASP ASP B . n 
B 2 215 LYS 215 215 215 LYS LYS B . n 
B 2 216 ARG 216 216 216 ARG ARG B . n 
B 2 217 VAL 217 217 217 VAL VAL B . n 
B 2 218 GLU 218 218 218 GLU GLU B . n 
B 2 219 PRO 219 219 219 PRO PRO B . n 
B 2 220 LYS 220 220 220 LYS LYS B . n 
C 1 1   ASP 1   1   1   ASP ASP C . n 
C 1 2   ILE 2   2   2   ILE ILE C . n 
C 1 3   LEU 3   3   3   LEU LEU C . n 
C 1 4   LEU 4   4   4   LEU LEU C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   GLN 6   6   6   GLN GLN C . n 
C 1 7   SER 7   7   7   SER SER C . n 
C 1 8   PRO 8   8   8   PRO PRO C . n 
C 1 9   VAL 9   9   9   VAL VAL C . n 
C 1 10  ILE 10  10  10  ILE ILE C . n 
C 1 11  LEU 11  11  11  LEU LEU C . n 
C 1 12  SER 12  12  12  SER SER C . n 
C 1 13  VAL 13  13  13  VAL VAL C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  PRO 15  15  15  PRO PRO C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  GLU 17  17  17  GLU GLU C . n 
C 1 18  ARG 18  18  18  ARG ARG C . n 
C 1 19  VAL 19  19  19  VAL VAL C . n 
C 1 20  SER 20  20  20  SER SER C . n 
C 1 21  PHE 21  21  21  PHE PHE C . n 
C 1 22  SER 22  22  22  SER SER C . n 
C 1 23  CYS 23  23  23  CYS CYS C . n 
C 1 24  ARG 24  24  24  ARG ARG C . n 
C 1 25  ALA 25  25  25  ALA ALA C . n 
C 1 26  SER 26  26  26  SER SER C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  ILE 29  29  29  ILE ILE C . n 
C 1 30  GLY 30  30  30  GLY GLY C . n 
C 1 31  THR 31  31  31  THR THR C . n 
C 1 32  ASN 32  32  32  ASN ASN C . n 
C 1 33  ILE 33  33  33  ILE ILE C . n 
C 1 34  HIS 34  34  34  HIS HIS C . n 
C 1 35  TRP 35  35  35  TRP TRP C . n 
C 1 36  TYR 36  36  36  TYR TYR C . n 
C 1 37  GLN 37  37  37  GLN GLN C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  ARG 39  39  39  ARG ARG C . n 
C 1 40  THR 40  40  40  THR THR C . n 
C 1 41  ASN 41  41  41  ASN ASN C . n 
C 1 42  GLY 42  42  42  GLY GLY C . n 
C 1 43  SER 43  43  43  SER SER C . n 
C 1 44  PRO 44  44  44  PRO PRO C . n 
C 1 45  ARG 45  45  45  ARG ARG C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  LEU 47  47  47  LEU LEU C . n 
C 1 48  ILE 48  48  48  ILE ILE C . n 
C 1 49  LYS 49  49  49  LYS LYS C . n 
C 1 50  TYR 50  50  50  TYR TYR C . n 
C 1 51  ALA 51  51  51  ALA ALA C . n 
C 1 52  SER 52  52  52  SER SER C . n 
C 1 53  GLU 53  53  53  GLU GLU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ILE 55  55  55  ILE ILE C . n 
C 1 56  SER 56  56  56  SER SER C . n 
C 1 57  GLY 57  57  57  GLY GLY C . n 
C 1 58  ILE 58  58  58  ILE ILE C . n 
C 1 59  PRO 59  59  59  PRO PRO C . n 
C 1 60  SER 60  60  60  SER SER C . n 
C 1 61  ARG 61  61  61  ARG ARG C . n 
C 1 62  PHE 62  62  62  PHE PHE C . n 
C 1 63  SER 63  63  63  SER SER C . n 
C 1 64  GLY 64  64  64  GLY GLY C . n 
C 1 65  SER 65  65  65  SER SER C . n 
C 1 66  GLY 66  66  66  GLY GLY C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  GLY 68  68  68  GLY GLY C . n 
C 1 69  THR 69  69  69  THR THR C . n 
C 1 70  ASP 70  70  70  ASP ASP C . n 
C 1 71  PHE 71  71  71  PHE PHE C . n 
C 1 72  THR 72  72  72  THR THR C . n 
C 1 73  LEU 73  73  73  LEU LEU C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ILE 75  75  75  ILE ILE C . n 
C 1 76  ASN 76  76  76  ASN ASN C . n 
C 1 77  SER 77  77  77  SER SER C . n 
C 1 78  VAL 78  78  78  VAL VAL C . n 
C 1 79  GLU 79  79  79  GLU GLU C . n 
C 1 80  SER 80  80  80  SER SER C . n 
C 1 81  GLU 81  81  81  GLU GLU C . n 
C 1 82  ASP 82  82  82  ASP ASP C . n 
C 1 83  ILE 83  83  83  ILE ILE C . n 
C 1 84  ALA 84  84  84  ALA ALA C . n 
C 1 85  ASP 85  85  85  ASP ASP C . n 
C 1 86  TYR 86  86  86  TYR TYR C . n 
C 1 87  TYR 87  87  87  TYR TYR C . n 
C 1 88  CYS 88  88  88  CYS CYS C . n 
C 1 89  GLN 89  89  89  GLN GLN C . n 
C 1 90  GLN 90  90  90  GLN GLN C . n 
C 1 91  ASN 91  91  91  ASN ASN C . n 
C 1 92  ASN 92  92  92  ASN ASN C . n 
C 1 93  ASN 93  93  93  ASN ASN C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  PRO 95  95  95  PRO PRO C . n 
C 1 96  THR 96  96  96  THR THR C . n 
C 1 97  THR 97  97  97  THR THR C . n 
C 1 98  PHE 98  98  98  PHE PHE C . n 
C 1 99  GLY 99  99  99  GLY GLY C . n 
C 1 100 ALA 100 100 100 ALA ALA C . n 
C 1 101 GLY 101 101 101 GLY GLY C . n 
C 1 102 THR 102 102 102 THR THR C . n 
C 1 103 LYS 103 103 103 LYS LYS C . n 
C 1 104 LEU 104 104 104 LEU LEU C . n 
C 1 105 GLU 105 105 105 GLU GLU C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 LYS 107 107 107 LYS LYS C . n 
C 1 108 ARG 108 108 108 ARG ARG C . n 
C 1 109 THR 109 109 109 THR THR C . n 
C 1 110 VAL 110 110 110 VAL VAL C . n 
C 1 111 ALA 111 111 111 ALA ALA C . n 
C 1 112 ALA 112 112 112 ALA ALA C . n 
C 1 113 PRO 113 113 113 PRO PRO C . n 
C 1 114 SER 114 114 114 SER SER C . n 
C 1 115 VAL 115 115 115 VAL VAL C . n 
C 1 116 PHE 116 116 116 PHE PHE C . n 
C 1 117 ILE 117 117 117 ILE ILE C . n 
C 1 118 PHE 118 118 118 PHE PHE C . n 
C 1 119 PRO 119 119 119 PRO PRO C . n 
C 1 120 PRO 120 120 120 PRO PRO C . n 
C 1 121 SER 121 121 121 SER SER C . n 
C 1 122 ASP 122 122 122 ASP ASP C . n 
C 1 123 GLU 123 123 123 GLU GLU C . n 
C 1 124 GLN 124 124 124 GLN GLN C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 LYS 126 126 126 LYS LYS C . n 
C 1 127 SER 127 127 127 SER SER C . n 
C 1 128 GLY 128 128 128 GLY GLY C . n 
C 1 129 THR 129 129 129 THR THR C . n 
C 1 130 ALA 130 130 130 ALA ALA C . n 
C 1 131 SER 131 131 131 SER SER C . n 
C 1 132 VAL 132 132 132 VAL VAL C . n 
C 1 133 VAL 133 133 133 VAL VAL C . n 
C 1 134 CYS 134 134 134 CYS CYS C . n 
C 1 135 LEU 135 135 135 LEU LEU C . n 
C 1 136 LEU 136 136 136 LEU LEU C . n 
C 1 137 ASN 137 137 137 ASN ASN C . n 
C 1 138 ASN 138 138 138 ASN ASN C . n 
C 1 139 PHE 139 139 139 PHE PHE C . n 
C 1 140 TYR 140 140 140 TYR TYR C . n 
C 1 141 PRO 141 141 141 PRO PRO C . n 
C 1 142 ARG 142 142 142 ARG ARG C . n 
C 1 143 GLU 143 143 143 GLU GLU C . n 
C 1 144 ALA 144 144 144 ALA ALA C . n 
C 1 145 LYS 145 145 145 LYS LYS C . n 
C 1 146 VAL 146 146 146 VAL VAL C . n 
C 1 147 GLN 147 147 147 GLN GLN C . n 
C 1 148 TRP 148 148 148 TRP TRP C . n 
C 1 149 LYS 149 149 149 LYS LYS C . n 
C 1 150 VAL 150 150 150 VAL VAL C . n 
C 1 151 ASP 151 151 151 ASP ASP C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 ALA 153 153 153 ALA ALA C . n 
C 1 154 LEU 154 154 154 LEU LEU C . n 
C 1 155 GLN 155 155 155 GLN GLN C . n 
C 1 156 SER 156 156 156 SER SER C . n 
C 1 157 GLY 157 157 157 GLY GLY C . n 
C 1 158 ASN 158 158 158 ASN ASN C . n 
C 1 159 SER 159 159 159 SER SER C . n 
C 1 160 GLN 160 160 160 GLN GLN C . n 
C 1 161 GLU 161 161 161 GLU GLU C . n 
C 1 162 SER 162 162 162 SER SER C . n 
C 1 163 VAL 163 163 163 VAL VAL C . n 
C 1 164 THR 164 164 164 THR THR C . n 
C 1 165 GLU 165 165 165 GLU GLU C . n 
C 1 166 GLN 166 166 166 GLN GLN C . n 
C 1 167 ASP 167 167 167 ASP ASP C . n 
C 1 168 SER 168 168 168 SER SER C . n 
C 1 169 LYS 169 169 169 LYS LYS C . n 
C 1 170 ASP 170 170 170 ASP ASP C . n 
C 1 171 SER 171 171 171 SER SER C . n 
C 1 172 THR 172 172 172 THR THR C . n 
C 1 173 TYR 173 173 173 TYR TYR C . n 
C 1 174 SER 174 174 174 SER SER C . n 
C 1 175 LEU 175 175 175 LEU LEU C . n 
C 1 176 SER 176 176 176 SER SER C . n 
C 1 177 SER 177 177 177 SER SER C . n 
C 1 178 THR 178 178 178 THR THR C . n 
C 1 179 LEU 179 179 179 LEU LEU C . n 
C 1 180 THR 180 180 180 THR THR C . n 
C 1 181 LEU 181 181 181 LEU LEU C . n 
C 1 182 SER 182 182 182 SER SER C . n 
C 1 183 LYS 183 183 183 LYS LYS C . n 
C 1 184 ALA 184 184 184 ALA ALA C . n 
C 1 185 ASP 185 185 185 ASP ASP C . n 
C 1 186 TYR 186 186 186 TYR TYR C . n 
C 1 187 GLU 187 187 187 GLU GLU C . n 
C 1 188 LYS 188 188 188 LYS LYS C . n 
C 1 189 HIS 189 189 189 HIS HIS C . n 
C 1 190 LYS 190 190 190 LYS LYS C . n 
C 1 191 VAL 191 191 191 VAL VAL C . n 
C 1 192 TYR 192 192 192 TYR TYR C . n 
C 1 193 ALA 193 193 193 ALA ALA C . n 
C 1 194 CYS 194 194 194 CYS CYS C . n 
C 1 195 GLU 195 195 195 GLU GLU C . n 
C 1 196 VAL 196 196 196 VAL VAL C . n 
C 1 197 THR 197 197 197 THR THR C . n 
C 1 198 HIS 198 198 198 HIS HIS C . n 
C 1 199 GLN 199 199 199 GLN GLN C . n 
C 1 200 GLY 200 200 200 GLY GLY C . n 
C 1 201 LEU 201 201 201 LEU LEU C . n 
C 1 202 SER 202 202 202 SER SER C . n 
C 1 203 SER 203 203 203 SER SER C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 VAL 205 205 205 VAL VAL C . n 
C 1 206 THR 206 206 206 THR THR C . n 
C 1 207 LYS 207 207 207 LYS LYS C . n 
C 1 208 SER 208 208 208 SER SER C . n 
C 1 209 PHE 209 209 209 PHE PHE C . n 
C 1 210 ASN 210 210 210 ASN ASN C . n 
C 1 211 ARG 211 211 211 ARG ARG C . n 
C 1 212 GLY 212 212 212 GLY GLY C . n 
C 1 213 ALA 213 213 213 ALA ALA C . n 
D 2 1   GLN 1   1   1   GLN GLN D . n 
D 2 2   VAL 2   2   2   VAL VAL D . n 
D 2 3   GLN 3   3   3   GLN GLN D . n 
D 2 4   LEU 4   4   4   LEU LEU D . n 
D 2 5   LYS 5   5   5   LYS LYS D . n 
D 2 6   GLN 6   6   6   GLN GLN D . n 
D 2 7   SER 7   7   7   SER SER D . n 
D 2 8   GLY 8   8   8   GLY GLY D . n 
D 2 9   PRO 9   9   9   PRO PRO D . n 
D 2 10  GLY 10  10  10  GLY GLY D . n 
D 2 11  LEU 11  11  11  LEU LEU D . n 
D 2 12  VAL 12  12  12  VAL VAL D . n 
D 2 13  GLN 13  13  13  GLN GLN D . n 
D 2 14  PRO 14  14  14  PRO PRO D . n 
D 2 15  SER 15  15  15  SER SER D . n 
D 2 16  GLN 16  16  16  GLN GLN D . n 
D 2 17  SER 17  17  17  SER SER D . n 
D 2 18  LEU 18  18  18  LEU LEU D . n 
D 2 19  SER 19  19  19  SER SER D . n 
D 2 20  ILE 20  20  20  ILE ILE D . n 
D 2 21  THR 21  21  21  THR THR D . n 
D 2 22  CYS 22  22  22  CYS CYS D . n 
D 2 23  THR 23  23  23  THR THR D . n 
D 2 24  VAL 24  24  24  VAL VAL D . n 
D 2 25  SER 25  25  25  SER SER D . n 
D 2 26  GLY 26  26  26  GLY GLY D . n 
D 2 27  PHE 27  27  27  PHE PHE D . n 
D 2 28  SER 28  28  28  SER SER D . n 
D 2 29  LEU 29  29  29  LEU LEU D . n 
D 2 30  THR 30  30  30  THR THR D . n 
D 2 31  ASN 31  31  31  ASN ASN D . n 
D 2 32  TYR 32  32  32  TYR TYR D . n 
D 2 33  GLY 33  33  33  GLY GLY D . n 
D 2 34  VAL 34  34  34  VAL VAL D . n 
D 2 35  HIS 35  35  35  HIS HIS D . n 
D 2 36  TRP 36  36  36  TRP TRP D . n 
D 2 37  VAL 37  37  37  VAL VAL D . n 
D 2 38  ARG 38  38  38  ARG ARG D . n 
D 2 39  GLN 39  39  39  GLN GLN D . n 
D 2 40  SER 40  40  40  SER SER D . n 
D 2 41  PRO 41  41  41  PRO PRO D . n 
D 2 42  GLY 42  42  42  GLY GLY D . n 
D 2 43  LYS 43  43  43  LYS LYS D . n 
D 2 44  GLY 44  44  44  GLY GLY D . n 
D 2 45  LEU 45  45  45  LEU LEU D . n 
D 2 46  GLU 46  46  46  GLU GLU D . n 
D 2 47  TRP 47  47  47  TRP TRP D . n 
D 2 48  LEU 48  48  48  LEU LEU D . n 
D 2 49  GLY 49  49  49  GLY GLY D . n 
D 2 50  VAL 50  50  50  VAL VAL D . n 
D 2 51  ILE 51  51  51  ILE ILE D . n 
D 2 52  TRP 52  52  52  TRP TRP D . n 
D 2 53  SER 53  53  53  SER SER D . n 
D 2 54  GLY 54  54  54  GLY GLY D . n 
D 2 55  GLY 55  55  55  GLY GLY D . n 
D 2 56  ASN 56  56  56  ASN ASN D . n 
D 2 57  THR 57  57  57  THR THR D . n 
D 2 58  ASP 58  58  58  ASP ASP D . n 
D 2 59  TYR 59  59  59  TYR TYR D . n 
D 2 60  ASN 60  60  60  ASN ASN D . n 
D 2 61  THR 61  61  61  THR THR D . n 
D 2 62  PRO 62  62  62  PRO PRO D . n 
D 2 63  PHE 63  63  63  PHE PHE D . n 
D 2 64  THR 64  64  64  THR THR D . n 
D 2 65  SER 65  65  65  SER SER D . n 
D 2 66  ARG 66  66  66  ARG ARG D . n 
D 2 67  LEU 67  67  67  LEU LEU D . n 
D 2 68  SER 68  68  68  SER SER D . n 
D 2 69  ILE 69  69  69  ILE ILE D . n 
D 2 70  ASN 70  70  70  ASN ASN D . n 
D 2 71  LYS 71  71  71  LYS LYS D . n 
D 2 72  ASP 72  72  72  ASP ASP D . n 
D 2 73  ASN 73  73  73  ASN ASN D . n 
D 2 74  SER 74  74  74  SER SER D . n 
D 2 75  LYS 75  75  75  LYS LYS D . n 
D 2 76  SER 76  76  76  SER SER D . n 
D 2 77  GLN 77  77  77  GLN GLN D . n 
D 2 78  VAL 78  78  78  VAL VAL D . n 
D 2 79  PHE 79  79  79  PHE PHE D . n 
D 2 80  PHE 80  80  80  PHE PHE D . n 
D 2 81  LYS 81  81  81  LYS LYS D . n 
D 2 82  MET 82  82  82  MET MET D . n 
D 2 83  ASN 83  83  83  ASN ASN D . n 
D 2 84  SER 84  84  84  SER SER D . n 
D 2 85  LEU 85  85  85  LEU LEU D . n 
D 2 86  GLN 86  86  86  GLN GLN D . n 
D 2 87  SER 87  87  87  SER SER D . n 
D 2 88  ASN 88  88  88  ASN ASN D . n 
D 2 89  ASP 89  89  89  ASP ASP D . n 
D 2 90  THR 90  90  90  THR THR D . n 
D 2 91  ALA 91  91  91  ALA ALA D . n 
D 2 92  ILE 92  92  92  ILE ILE D . n 
D 2 93  TYR 93  93  93  TYR TYR D . n 
D 2 94  TYR 94  94  94  TYR TYR D . n 
D 2 95  CYS 95  95  95  CYS CYS D . n 
D 2 96  ALA 96  96  96  ALA ALA D . n 
D 2 97  ARG 97  97  97  ARG ARG D . n 
D 2 98  ALA 98  98  98  ALA ALA D . n 
D 2 99  LEU 99  99  99  LEU LEU D . n 
D 2 100 THR 100 100 100 THR THR D . n 
D 2 101 TYR 101 101 101 TYR TYR D . n 
D 2 102 TYR 102 102 102 TYR TYR D . n 
D 2 103 ASP 103 103 103 ASP ASP D . n 
D 2 104 TYR 104 104 104 TYR TYR D . n 
D 2 105 GLU 105 105 105 GLU GLU D . n 
D 2 106 PHE 106 106 106 PHE PHE D . n 
D 2 107 ALA 107 107 107 ALA ALA D . n 
D 2 108 TYR 108 108 108 TYR TYR D . n 
D 2 109 TRP 109 109 109 TRP TRP D . n 
D 2 110 GLY 110 110 110 GLY GLY D . n 
D 2 111 GLN 111 111 111 GLN GLN D . n 
D 2 112 GLY 112 112 112 GLY GLY D . n 
D 2 113 THR 113 113 113 THR THR D . n 
D 2 114 LEU 114 114 114 LEU LEU D . n 
D 2 115 VAL 115 115 115 VAL VAL D . n 
D 2 116 THR 116 116 116 THR THR D . n 
D 2 117 VAL 117 117 117 VAL VAL D . n 
D 2 118 SER 118 118 118 SER SER D . n 
D 2 119 ALA 119 119 119 ALA ALA D . n 
D 2 120 ALA 120 120 120 ALA ALA D . n 
D 2 121 SER 121 121 121 SER SER D . n 
D 2 122 THR 122 122 122 THR THR D . n 
D 2 123 LYS 123 123 123 LYS LYS D . n 
D 2 124 GLY 124 124 124 GLY GLY D . n 
D 2 125 PRO 125 125 125 PRO PRO D . n 
D 2 126 SER 126 126 126 SER SER D . n 
D 2 127 VAL 127 127 127 VAL VAL D . n 
D 2 128 PHE 128 128 128 PHE PHE D . n 
D 2 129 PRO 129 129 129 PRO PRO D . n 
D 2 130 LEU 130 130 130 LEU LEU D . n 
D 2 131 ALA 131 131 131 ALA ALA D . n 
D 2 132 PRO 132 132 132 PRO PRO D . n 
D 2 133 SER 133 133 ?   ?   ?   D . n 
D 2 134 SER 134 134 ?   ?   ?   D . n 
D 2 135 LYS 135 135 ?   ?   ?   D . n 
D 2 136 SER 136 136 ?   ?   ?   D . n 
D 2 137 THR 137 137 ?   ?   ?   D . n 
D 2 138 SER 138 138 ?   ?   ?   D . n 
D 2 139 GLY 139 139 ?   ?   ?   D . n 
D 2 140 GLY 140 140 140 GLY GLY D . n 
D 2 141 THR 141 141 141 THR THR D . n 
D 2 142 ALA 142 142 142 ALA ALA D . n 
D 2 143 ALA 143 143 143 ALA ALA D . n 
D 2 144 LEU 144 144 144 LEU LEU D . n 
D 2 145 GLY 145 145 145 GLY GLY D . n 
D 2 146 CYS 146 146 146 CYS CYS D . n 
D 2 147 LEU 147 147 147 LEU LEU D . n 
D 2 148 VAL 148 148 148 VAL VAL D . n 
D 2 149 LYS 149 149 149 LYS LYS D . n 
D 2 150 ASP 150 150 150 ASP ASP D . n 
D 2 151 TYR 151 151 151 TYR TYR D . n 
D 2 152 PHE 152 152 152 PHE PHE D . n 
D 2 153 PRO 153 153 153 PRO PRO D . n 
D 2 154 GLU 154 154 154 GLU GLU D . n 
D 2 155 PRO 155 155 155 PRO PRO D . n 
D 2 156 VAL 156 156 156 VAL VAL D . n 
D 2 157 THR 157 157 157 THR THR D . n 
D 2 158 VAL 158 158 158 VAL VAL D . n 
D 2 159 SER 159 159 159 SER SER D . n 
D 2 160 TRP 160 160 160 TRP TRP D . n 
D 2 161 ASN 161 161 161 ASN ASN D . n 
D 2 162 SER 162 162 162 SER SER D . n 
D 2 163 GLY 163 163 163 GLY GLY D . n 
D 2 164 ALA 164 164 164 ALA ALA D . n 
D 2 165 LEU 165 165 165 LEU LEU D . n 
D 2 166 THR 166 166 166 THR THR D . n 
D 2 167 SER 167 167 167 SER SER D . n 
D 2 168 GLY 168 168 168 GLY GLY D . n 
D 2 169 VAL 169 169 169 VAL VAL D . n 
D 2 170 HIS 170 170 170 HIS HIS D . n 
D 2 171 THR 171 171 171 THR THR D . n 
D 2 172 PHE 172 172 172 PHE PHE D . n 
D 2 173 PRO 173 173 173 PRO PRO D . n 
D 2 174 ALA 174 174 174 ALA ALA D . n 
D 2 175 VAL 175 175 175 VAL VAL D . n 
D 2 176 LEU 176 176 176 LEU LEU D . n 
D 2 177 GLN 177 177 177 GLN GLN D . n 
D 2 178 SER 178 178 178 SER SER D . n 
D 2 179 SER 179 179 179 SER SER D . n 
D 2 180 GLY 180 180 180 GLY GLY D . n 
D 2 181 LEU 181 181 181 LEU LEU D . n 
D 2 182 TYR 182 182 182 TYR TYR D . n 
D 2 183 SER 183 183 183 SER SER D . n 
D 2 184 LEU 184 184 184 LEU LEU D . n 
D 2 185 SER 185 185 185 SER SER D . n 
D 2 186 SER 186 186 186 SER SER D . n 
D 2 187 VAL 187 187 187 VAL VAL D . n 
D 2 188 VAL 188 188 188 VAL VAL D . n 
D 2 189 THR 189 189 189 THR THR D . n 
D 2 190 VAL 190 190 190 VAL VAL D . n 
D 2 191 PRO 191 191 191 PRO PRO D . n 
D 2 192 SER 192 192 192 SER SER D . n 
D 2 193 SER 193 193 193 SER SER D . n 
D 2 194 SER 194 194 194 SER SER D . n 
D 2 195 LEU 195 195 195 LEU LEU D . n 
D 2 196 GLY 196 196 196 GLY GLY D . n 
D 2 197 THR 197 197 197 THR THR D . n 
D 2 198 GLN 198 198 198 GLN GLN D . n 
D 2 199 THR 199 199 199 THR THR D . n 
D 2 200 TYR 200 200 200 TYR TYR D . n 
D 2 201 ILE 201 201 201 ILE ILE D . n 
D 2 202 CYS 202 202 202 CYS CYS D . n 
D 2 203 ASN 203 203 203 ASN ASN D . n 
D 2 204 VAL 204 204 204 VAL VAL D . n 
D 2 205 ASN 205 205 205 ASN ASN D . n 
D 2 206 HIS 206 206 206 HIS HIS D . n 
D 2 207 LYS 207 207 207 LYS LYS D . n 
D 2 208 PRO 208 208 208 PRO PRO D . n 
D 2 209 SER 209 209 209 SER SER D . n 
D 2 210 ASN 210 210 210 ASN ASN D . n 
D 2 211 THR 211 211 211 THR THR D . n 
D 2 212 LYS 212 212 212 LYS LYS D . n 
D 2 213 VAL 213 213 213 VAL VAL D . n 
D 2 214 ASP 214 214 214 ASP ASP D . n 
D 2 215 LYS 215 215 215 LYS LYS D . n 
D 2 216 ARG 216 216 216 ARG ARG D . n 
D 2 217 VAL 217 217 217 VAL VAL D . n 
D 2 218 GLU 218 218 218 GLU GLU D . n 
D 2 219 PRO 219 219 219 PRO PRO D . n 
D 2 220 LYS 220 220 220 LYS LYS D . n 
E 3 1   CYS 1   1   1   CYS CYS E . n 
E 3 2   GLN 2   2   2   GLN GLN E . n 
E 3 3   HIS 3   3   3   HIS HIS E . n 
E 3 4   ASP 4   4   4   ASP ASP E . n 
E 3 5   LEU 5   5   5   LEU LEU E . n 
E 3 6   SER 6   6   6   SER SER E . n 
E 3 7   THR 7   7   7   THR THR E . n 
E 3 8   ARG 8   8   8   ARG ARG E . n 
E 3 9   ARG 9   9   9   ARG ARG E . n 
E 3 10  LEU 10  10  10  LEU LEU E . n 
E 3 11  LYS 11  11  11  LYS LYS E . n 
E 3 12  CYS 12  12  12  CYS CYS E . n 
F 3 1   CYS 1   1   1   CYS CYS F . n 
F 3 2   GLN 2   2   2   GLN GLN F . n 
F 3 3   HIS 3   3   3   HIS HIS F . n 
F 3 4   ASP 4   4   4   ASP ASP F . n 
F 3 5   LEU 5   5   5   LEU LEU F . n 
F 3 6   SER 6   6   6   SER SER F . n 
F 3 7   THR 7   7   7   THR THR F . n 
F 3 8   ARG 8   8   8   ARG ARG F . n 
F 3 9   ARG 9   9   9   ARG ARG F . n 
F 3 10  LEU 10  10  10  LEU LEU F . n 
F 3 11  LYS 11  11  11  LYS LYS F . n 
F 3 12  CYS 12  12  12  CYS CYS F . 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 
G 4 PO4 1   301 2   PO4 PO4 A . 
H 4 PO4 1   302 3   PO4 PO4 A . 
I 5 NAG 1   301 222 NAG NAG B . 
J 4 PO4 1   302 4   PO4 PO4 B . 
K 6 MRY 1   301 1   MRY MRY C . 
L 5 NAG 1   301 222 NAG NAG D . 
M 4 PO4 1   302 1   PO4 PO4 D . 
N 7 HOH 1   401 21  HOH HOH A . 
N 7 HOH 2   402 78  HOH HOH A . 
N 7 HOH 3   403 261 HOH HOH A . 
N 7 HOH 4   404 139 HOH HOH A . 
N 7 HOH 5   405 306 HOH HOH A . 
N 7 HOH 6   406 218 HOH HOH A . 
N 7 HOH 7   407 210 HOH HOH A . 
N 7 HOH 8   408 376 HOH HOH A . 
N 7 HOH 9   409 287 HOH HOH A . 
N 7 HOH 10  410 9   HOH HOH A . 
N 7 HOH 11  411 5   HOH HOH A . 
N 7 HOH 12  412 368 HOH HOH A . 
N 7 HOH 13  413 19  HOH HOH A . 
N 7 HOH 14  414 127 HOH HOH A . 
N 7 HOH 15  415 69  HOH HOH A . 
N 7 HOH 16  416 25  HOH HOH A . 
N 7 HOH 17  417 365 HOH HOH A . 
N 7 HOH 18  418 85  HOH HOH A . 
N 7 HOH 19  419 234 HOH HOH A . 
N 7 HOH 20  420 90  HOH HOH A . 
N 7 HOH 21  421 6   HOH HOH A . 
N 7 HOH 22  422 52  HOH HOH A . 
N 7 HOH 23  423 149 HOH HOH A . 
N 7 HOH 24  424 164 HOH HOH A . 
N 7 HOH 25  425 54  HOH HOH A . 
N 7 HOH 26  426 162 HOH HOH A . 
N 7 HOH 27  427 163 HOH HOH A . 
N 7 HOH 28  428 47  HOH HOH A . 
N 7 HOH 29  429 259 HOH HOH A . 
N 7 HOH 30  430 137 HOH HOH A . 
N 7 HOH 31  431 96  HOH HOH A . 
N 7 HOH 32  432 180 HOH HOH A . 
N 7 HOH 33  433 339 HOH HOH A . 
N 7 HOH 34  434 97  HOH HOH A . 
N 7 HOH 35  435 110 HOH HOH A . 
N 7 HOH 36  436 268 HOH HOH A . 
N 7 HOH 37  437 3   HOH HOH A . 
N 7 HOH 38  438 32  HOH HOH A . 
N 7 HOH 39  439 281 HOH HOH A . 
N 7 HOH 40  440 184 HOH HOH A . 
N 7 HOH 41  441 135 HOH HOH A . 
N 7 HOH 42  442 284 HOH HOH A . 
N 7 HOH 43  443 99  HOH HOH A . 
N 7 HOH 44  444 344 HOH HOH A . 
N 7 HOH 45  445 77  HOH HOH A . 
N 7 HOH 46  446 76  HOH HOH A . 
N 7 HOH 47  447 105 HOH HOH A . 
N 7 HOH 48  448 192 HOH HOH A . 
N 7 HOH 49  449 272 HOH HOH A . 
N 7 HOH 50  450 225 HOH HOH A . 
N 7 HOH 51  451 117 HOH HOH A . 
N 7 HOH 52  452 326 HOH HOH A . 
N 7 HOH 53  453 408 HOH HOH A . 
N 7 HOH 54  454 107 HOH HOH A . 
N 7 HOH 55  455 141 HOH HOH A . 
N 7 HOH 56  456 345 HOH HOH A . 
N 7 HOH 57  457 233 HOH HOH A . 
N 7 HOH 58  458 121 HOH HOH A . 
N 7 HOH 59  459 148 HOH HOH A . 
N 7 HOH 60  460 62  HOH HOH A . 
N 7 HOH 61  461 153 HOH HOH A . 
N 7 HOH 62  462 264 HOH HOH A . 
N 7 HOH 63  463 72  HOH HOH A . 
N 7 HOH 64  464 84  HOH HOH A . 
N 7 HOH 65  465 64  HOH HOH A . 
N 7 HOH 66  466 103 HOH HOH A . 
N 7 HOH 67  467 354 HOH HOH A . 
N 7 HOH 68  468 189 HOH HOH A . 
N 7 HOH 69  469 86  HOH HOH A . 
N 7 HOH 70  470 413 HOH HOH A . 
N 7 HOH 71  471 106 HOH HOH A . 
N 7 HOH 72  472 197 HOH HOH A . 
N 7 HOH 73  473 310 HOH HOH A . 
N 7 HOH 74  474 34  HOH HOH A . 
N 7 HOH 75  475 182 HOH HOH A . 
N 7 HOH 76  476 304 HOH HOH A . 
N 7 HOH 77  477 215 HOH HOH A . 
N 7 HOH 78  478 278 HOH HOH A . 
N 7 HOH 79  479 307 HOH HOH A . 
N 7 HOH 80  480 36  HOH HOH A . 
N 7 HOH 81  481 410 HOH HOH A . 
N 7 HOH 82  482 380 HOH HOH A . 
N 7 HOH 83  483 373 HOH HOH A . 
N 7 HOH 84  484 384 HOH HOH A . 
N 7 HOH 85  485 191 HOH HOH A . 
N 7 HOH 86  486 415 HOH HOH A . 
N 7 HOH 87  487 333 HOH HOH A . 
N 7 HOH 88  488 33  HOH HOH A . 
N 7 HOH 89  489 170 HOH HOH A . 
N 7 HOH 90  490 231 HOH HOH A . 
N 7 HOH 91  491 263 HOH HOH A . 
N 7 HOH 92  492 209 HOH HOH A . 
N 7 HOH 93  493 143 HOH HOH A . 
N 7 HOH 94  494 112 HOH HOH A . 
N 7 HOH 95  495 409 HOH HOH A . 
N 7 HOH 96  496 212 HOH HOH A . 
N 7 HOH 97  497 196 HOH HOH A . 
N 7 HOH 98  498 389 HOH HOH A . 
N 7 HOH 99  499 246 HOH HOH A . 
N 7 HOH 100 500 247 HOH HOH A . 
N 7 HOH 101 501 419 HOH HOH A . 
N 7 HOH 102 502 214 HOH HOH A . 
N 7 HOH 103 503 115 HOH HOH A . 
N 7 HOH 104 504 227 HOH HOH A . 
N 7 HOH 105 505 398 HOH HOH A . 
N 7 HOH 106 506 270 HOH HOH A . 
N 7 HOH 107 507 244 HOH HOH A . 
N 7 HOH 108 508 386 HOH HOH A . 
N 7 HOH 109 509 222 HOH HOH A . 
N 7 HOH 110 510 181 HOH HOH A . 
O 7 HOH 1   401 378 HOH HOH B . 
O 7 HOH 2   402 254 HOH HOH B . 
O 7 HOH 3   403 266 HOH HOH B . 
O 7 HOH 4   404 332 HOH HOH B . 
O 7 HOH 5   405 41  HOH HOH B . 
O 7 HOH 6   406 20  HOH HOH B . 
O 7 HOH 7   407 4   HOH HOH B . 
O 7 HOH 8   408 113 HOH HOH B . 
O 7 HOH 9   409 51  HOH HOH B . 
O 7 HOH 10  410 318 HOH HOH B . 
O 7 HOH 11  411 17  HOH HOH B . 
O 7 HOH 12  412 190 HOH HOH B . 
O 7 HOH 13  413 11  HOH HOH B . 
O 7 HOH 14  414 167 HOH HOH B . 
O 7 HOH 15  415 299 HOH HOH B . 
O 7 HOH 16  416 23  HOH HOH B . 
O 7 HOH 17  417 102 HOH HOH B . 
O 7 HOH 18  418 336 HOH HOH B . 
O 7 HOH 19  419 79  HOH HOH B . 
O 7 HOH 20  420 194 HOH HOH B . 
O 7 HOH 21  421 403 HOH HOH B . 
O 7 HOH 22  422 358 HOH HOH B . 
O 7 HOH 23  423 73  HOH HOH B . 
O 7 HOH 24  424 147 HOH HOH B . 
O 7 HOH 25  425 173 HOH HOH B . 
O 7 HOH 26  426 50  HOH HOH B . 
O 7 HOH 27  427 371 HOH HOH B . 
O 7 HOH 28  428 42  HOH HOH B . 
O 7 HOH 29  429 100 HOH HOH B . 
O 7 HOH 30  430 22  HOH HOH B . 
O 7 HOH 31  431 46  HOH HOH B . 
O 7 HOH 32  432 301 HOH HOH B . 
O 7 HOH 33  433 188 HOH HOH B . 
O 7 HOH 34  434 91  HOH HOH B . 
O 7 HOH 35  435 59  HOH HOH B . 
O 7 HOH 36  436 172 HOH HOH B . 
O 7 HOH 37  437 362 HOH HOH B . 
O 7 HOH 38  438 171 HOH HOH B . 
O 7 HOH 39  439 418 HOH HOH B . 
O 7 HOH 40  440 154 HOH HOH B . 
O 7 HOH 41  441 145 HOH HOH B . 
O 7 HOH 42  442 237 HOH HOH B . 
O 7 HOH 43  443 294 HOH HOH B . 
O 7 HOH 44  444 48  HOH HOH B . 
O 7 HOH 45  445 116 HOH HOH B . 
O 7 HOH 46  446 128 HOH HOH B . 
O 7 HOH 47  447 343 HOH HOH B . 
O 7 HOH 48  448 323 HOH HOH B . 
O 7 HOH 49  449 235 HOH HOH B . 
O 7 HOH 50  450 92  HOH HOH B . 
O 7 HOH 51  451 277 HOH HOH B . 
O 7 HOH 52  452 405 HOH HOH B . 
O 7 HOH 53  453 201 HOH HOH B . 
O 7 HOH 54  454 223 HOH HOH B . 
O 7 HOH 55  455 239 HOH HOH B . 
O 7 HOH 56  456 360 HOH HOH B . 
O 7 HOH 57  457 308 HOH HOH B . 
O 7 HOH 58  458 83  HOH HOH B . 
O 7 HOH 59  459 126 HOH HOH B . 
O 7 HOH 60  460 302 HOH HOH B . 
O 7 HOH 61  461 35  HOH HOH B . 
O 7 HOH 62  462 420 HOH HOH B . 
O 7 HOH 63  463 288 HOH HOH B . 
O 7 HOH 64  464 289 HOH HOH B . 
O 7 HOH 65  465 311 HOH HOH B . 
O 7 HOH 66  466 251 HOH HOH B . 
O 7 HOH 67  467 396 HOH HOH B . 
O 7 HOH 68  468 168 HOH HOH B . 
O 7 HOH 69  469 144 HOH HOH B . 
O 7 HOH 70  470 193 HOH HOH B . 
O 7 HOH 71  471 293 HOH HOH B . 
O 7 HOH 72  472 406 HOH HOH B . 
O 7 HOH 73  473 74  HOH HOH B . 
O 7 HOH 74  474 347 HOH HOH B . 
O 7 HOH 75  475 382 HOH HOH B . 
O 7 HOH 76  476 397 HOH HOH B . 
O 7 HOH 77  477 275 HOH HOH B . 
O 7 HOH 78  478 370 HOH HOH B . 
O 7 HOH 79  479 327 HOH HOH B . 
O 7 HOH 80  480 377 HOH HOH B . 
O 7 HOH 81  481 402 HOH HOH B . 
O 7 HOH 82  482 334 HOH HOH B . 
O 7 HOH 83  483 383 HOH HOH B . 
O 7 HOH 84  484 120 HOH HOH B . 
O 7 HOH 85  485 217 HOH HOH B . 
O 7 HOH 86  486 387 HOH HOH B . 
O 7 HOH 87  487 305 HOH HOH B . 
O 7 HOH 88  488 296 HOH HOH B . 
O 7 HOH 89  489 260 HOH HOH B . 
O 7 HOH 90  490 226 HOH HOH B . 
O 7 HOH 91  491 241 HOH HOH B . 
O 7 HOH 92  492 330 HOH HOH B . 
O 7 HOH 93  493 417 HOH HOH B . 
O 7 HOH 94  494 37  HOH HOH B . 
O 7 HOH 95  495 274 HOH HOH B . 
O 7 HOH 96  496 156 HOH HOH B . 
O 7 HOH 97  497 242 HOH HOH B . 
P 7 HOH 1   401 291 HOH HOH C . 
P 7 HOH 2   402 369 HOH HOH C . 
P 7 HOH 3   403 279 HOH HOH C . 
P 7 HOH 4   404 202 HOH HOH C . 
P 7 HOH 5   405 88  HOH HOH C . 
P 7 HOH 6   406 8   HOH HOH C . 
P 7 HOH 7   407 395 HOH HOH C . 
P 7 HOH 8   408 175 HOH HOH C . 
P 7 HOH 9   409 82  HOH HOH C . 
P 7 HOH 10  410 375 HOH HOH C . 
P 7 HOH 11  411 63  HOH HOH C . 
P 7 HOH 12  412 66  HOH HOH C . 
P 7 HOH 13  413 240 HOH HOH C . 
P 7 HOH 14  414 200 HOH HOH C . 
P 7 HOH 15  415 178 HOH HOH C . 
P 7 HOH 16  416 95  HOH HOH C . 
P 7 HOH 17  417 158 HOH HOH C . 
P 7 HOH 18  418 138 HOH HOH C . 
P 7 HOH 19  419 338 HOH HOH C . 
P 7 HOH 20  420 152 HOH HOH C . 
P 7 HOH 21  421 14  HOH HOH C . 
P 7 HOH 22  422 374 HOH HOH C . 
P 7 HOH 23  423 70  HOH HOH C . 
P 7 HOH 24  424 18  HOH HOH C . 
P 7 HOH 25  425 43  HOH HOH C . 
P 7 HOH 26  426 186 HOH HOH C . 
P 7 HOH 27  427 385 HOH HOH C . 
P 7 HOH 28  428 2   HOH HOH C . 
P 7 HOH 29  429 257 HOH HOH C . 
P 7 HOH 30  430 10  HOH HOH C . 
P 7 HOH 31  431 350 HOH HOH C . 
P 7 HOH 32  432 265 HOH HOH C . 
P 7 HOH 33  433 422 HOH HOH C . 
P 7 HOH 34  434 125 HOH HOH C . 
P 7 HOH 35  435 391 HOH HOH C . 
P 7 HOH 36  436 45  HOH HOH C . 
P 7 HOH 37  437 15  HOH HOH C . 
P 7 HOH 38  438 57  HOH HOH C . 
P 7 HOH 39  439 195 HOH HOH C . 
P 7 HOH 40  440 16  HOH HOH C . 
P 7 HOH 41  441 133 HOH HOH C . 
P 7 HOH 42  442 276 HOH HOH C . 
P 7 HOH 43  443 303 HOH HOH C . 
P 7 HOH 44  444 101 HOH HOH C . 
P 7 HOH 45  445 319 HOH HOH C . 
P 7 HOH 46  446 205 HOH HOH C . 
P 7 HOH 47  447 157 HOH HOH C . 
P 7 HOH 48  448 340 HOH HOH C . 
P 7 HOH 49  449 28  HOH HOH C . 
P 7 HOH 50  450 131 HOH HOH C . 
P 7 HOH 51  451 174 HOH HOH C . 
P 7 HOH 52  452 367 HOH HOH C . 
P 7 HOH 53  453 199 HOH HOH C . 
P 7 HOH 54  454 228 HOH HOH C . 
P 7 HOH 55  455 221 HOH HOH C . 
P 7 HOH 56  456 55  HOH HOH C . 
P 7 HOH 57  457 185 HOH HOH C . 
P 7 HOH 58  458 142 HOH HOH C . 
P 7 HOH 59  459 357 HOH HOH C . 
P 7 HOH 60  460 342 HOH HOH C . 
P 7 HOH 61  461 295 HOH HOH C . 
P 7 HOH 62  462 89  HOH HOH C . 
P 7 HOH 63  463 238 HOH HOH C . 
P 7 HOH 64  464 53  HOH HOH C . 
P 7 HOH 65  465 316 HOH HOH C . 
P 7 HOH 66  466 325 HOH HOH C . 
P 7 HOH 67  467 273 HOH HOH C . 
P 7 HOH 68  468 329 HOH HOH C . 
P 7 HOH 69  469 165 HOH HOH C . 
P 7 HOH 70  470 151 HOH HOH C . 
P 7 HOH 71  471 123 HOH HOH C . 
P 7 HOH 72  472 224 HOH HOH C . 
P 7 HOH 73  473 136 HOH HOH C . 
P 7 HOH 74  474 49  HOH HOH C . 
P 7 HOH 75  475 134 HOH HOH C . 
P 7 HOH 76  476 262 HOH HOH C . 
P 7 HOH 77  477 219 HOH HOH C . 
P 7 HOH 78  478 280 HOH HOH C . 
P 7 HOH 79  479 80  HOH HOH C . 
P 7 HOH 80  480 12  HOH HOH C . 
P 7 HOH 81  481 30  HOH HOH C . 
P 7 HOH 82  482 150 HOH HOH C . 
P 7 HOH 83  483 160 HOH HOH C . 
P 7 HOH 84  484 130 HOH HOH C . 
P 7 HOH 85  485 364 HOH HOH C . 
P 7 HOH 86  486 198 HOH HOH C . 
P 7 HOH 87  487 356 HOH HOH C . 
P 7 HOH 88  488 98  HOH HOH C . 
P 7 HOH 89  489 372 HOH HOH C . 
P 7 HOH 90  490 230 HOH HOH C . 
P 7 HOH 91  491 114 HOH HOH C . 
P 7 HOH 92  492 423 HOH HOH C . 
P 7 HOH 93  493 111 HOH HOH C . 
P 7 HOH 94  494 283 HOH HOH C . 
P 7 HOH 95  495 312 HOH HOH C . 
P 7 HOH 96  496 351 HOH HOH C . 
P 7 HOH 97  497 269 HOH HOH C . 
P 7 HOH 98  498 314 HOH HOH C . 
P 7 HOH 99  499 379 HOH HOH C . 
P 7 HOH 100 500 346 HOH HOH C . 
P 7 HOH 101 501 337 HOH HOH C . 
P 7 HOH 102 502 282 HOH HOH C . 
P 7 HOH 103 503 392 HOH HOH C . 
P 7 HOH 104 504 421 HOH HOH C . 
P 7 HOH 105 505 216 HOH HOH C . 
P 7 HOH 106 506 400 HOH HOH C . 
P 7 HOH 107 507 176 HOH HOH C . 
P 7 HOH 108 508 220 HOH HOH C . 
P 7 HOH 109 509 324 HOH HOH C . 
P 7 HOH 110 510 248 HOH HOH C . 
P 7 HOH 111 511 255 HOH HOH C . 
P 7 HOH 112 512 243 HOH HOH C . 
Q 7 HOH 1   401 207 HOH HOH D . 
Q 7 HOH 2   402 7   HOH HOH D . 
Q 7 HOH 3   403 211 HOH HOH D . 
Q 7 HOH 4   404 140 HOH HOH D . 
Q 7 HOH 5   405 236 HOH HOH D . 
Q 7 HOH 6   406 44  HOH HOH D . 
Q 7 HOH 7   407 271 HOH HOH D . 
Q 7 HOH 8   408 119 HOH HOH D . 
Q 7 HOH 9   409 399 HOH HOH D . 
Q 7 HOH 10  410 341 HOH HOH D . 
Q 7 HOH 11  411 1   HOH HOH D . 
Q 7 HOH 12  412 31  HOH HOH D . 
Q 7 HOH 13  413 13  HOH HOH D . 
Q 7 HOH 14  414 65  HOH HOH D . 
Q 7 HOH 15  415 81  HOH HOH D . 
Q 7 HOH 16  416 118 HOH HOH D . 
Q 7 HOH 17  417 313 HOH HOH D . 
Q 7 HOH 18  418 393 HOH HOH D . 
Q 7 HOH 19  419 27  HOH HOH D . 
Q 7 HOH 20  420 204 HOH HOH D . 
Q 7 HOH 21  421 124 HOH HOH D . 
Q 7 HOH 22  422 407 HOH HOH D . 
Q 7 HOH 23  423 166 HOH HOH D . 
Q 7 HOH 24  424 67  HOH HOH D . 
Q 7 HOH 25  425 177 HOH HOH D . 
Q 7 HOH 26  426 252 HOH HOH D . 
Q 7 HOH 27  427 87  HOH HOH D . 
Q 7 HOH 28  428 366 HOH HOH D . 
Q 7 HOH 29  429 245 HOH HOH D . 
Q 7 HOH 30  430 132 HOH HOH D . 
Q 7 HOH 31  431 61  HOH HOH D . 
Q 7 HOH 32  432 104 HOH HOH D . 
Q 7 HOH 33  433 179 HOH HOH D . 
Q 7 HOH 34  434 38  HOH HOH D . 
Q 7 HOH 35  435 75  HOH HOH D . 
Q 7 HOH 36  436 40  HOH HOH D . 
Q 7 HOH 37  437 39  HOH HOH D . 
Q 7 HOH 38  438 56  HOH HOH D . 
Q 7 HOH 39  439 309 HOH HOH D . 
Q 7 HOH 40  440 58  HOH HOH D . 
Q 7 HOH 41  441 414 HOH HOH D . 
Q 7 HOH 42  442 68  HOH HOH D . 
Q 7 HOH 43  443 169 HOH HOH D . 
Q 7 HOH 44  444 348 HOH HOH D . 
Q 7 HOH 45  445 298 HOH HOH D . 
Q 7 HOH 46  446 412 HOH HOH D . 
Q 7 HOH 47  447 381 HOH HOH D . 
Q 7 HOH 48  448 187 HOH HOH D . 
Q 7 HOH 49  449 122 HOH HOH D . 
Q 7 HOH 50  450 94  HOH HOH D . 
Q 7 HOH 51  451 206 HOH HOH D . 
Q 7 HOH 52  452 93  HOH HOH D . 
Q 7 HOH 53  453 109 HOH HOH D . 
Q 7 HOH 54  454 213 HOH HOH D . 
Q 7 HOH 55  455 24  HOH HOH D . 
Q 7 HOH 56  456 129 HOH HOH D . 
Q 7 HOH 57  457 249 HOH HOH D . 
Q 7 HOH 58  458 416 HOH HOH D . 
Q 7 HOH 59  459 361 HOH HOH D . 
Q 7 HOH 60  460 155 HOH HOH D . 
Q 7 HOH 61  461 26  HOH HOH D . 
Q 7 HOH 62  462 335 HOH HOH D . 
Q 7 HOH 63  463 161 HOH HOH D . 
Q 7 HOH 64  464 208 HOH HOH D . 
Q 7 HOH 65  465 349 HOH HOH D . 
Q 7 HOH 66  466 328 HOH HOH D . 
Q 7 HOH 67  467 363 HOH HOH D . 
Q 7 HOH 68  468 352 HOH HOH D . 
Q 7 HOH 69  469 250 HOH HOH D . 
Q 7 HOH 70  470 404 HOH HOH D . 
Q 7 HOH 71  471 29  HOH HOH D . 
Q 7 HOH 72  472 394 HOH HOH D . 
Q 7 HOH 73  473 159 HOH HOH D . 
Q 7 HOH 74  474 146 HOH HOH D . 
Q 7 HOH 75  475 285 HOH HOH D . 
Q 7 HOH 76  476 322 HOH HOH D . 
Q 7 HOH 77  477 229 HOH HOH D . 
Q 7 HOH 78  478 331 HOH HOH D . 
Q 7 HOH 79  479 256 HOH HOH D . 
Q 7 HOH 80  480 411 HOH HOH D . 
Q 7 HOH 81  481 297 HOH HOH D . 
Q 7 HOH 82  482 253 HOH HOH D . 
R 7 HOH 1   101 71  HOH HOH E . 
R 7 HOH 2   102 203 HOH HOH E . 
R 7 HOH 3   103 183 HOH HOH E . 
R 7 HOH 4   104 60  HOH HOH E . 
R 7 HOH 5   105 300 HOH HOH E . 
R 7 HOH 6   106 232 HOH HOH E . 
S 7 HOH 1   101 320 HOH HOH F . 
S 7 HOH 2   102 108 HOH HOH F . 
S 7 HOH 3   103 321 HOH HOH F . 
# 
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 trimeric 3 
2 author_and_software_defined_assembly PISA trimeric 3 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,G,H,I,J,N,O,R 
2 1 C,D,F,K,L,M,P,Q,S   
# 
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)' 6190  ? 
1 MORE         -43   ? 
1 'SSA (A^2)'  18550 ? 
2 'ABSA (A^2)' 5760  ? 
2 MORE         -28   ? 
2 'SSA (A^2)'  18570 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2016-10-26 
2 'Structure model' 1 1 2016-11-09 
3 'Structure model' 1 2 2017-12-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'  
2 3 'Structure model' 'Database references'  
3 3 'Structure model' 'Derived calculations' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' citation              
2 3 'Structure model' pdbx_struct_oper_list 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_citation.journal_abbrev'                  
2 3 'Structure model' '_citation.page_first'                      
3 3 'Structure model' '_citation.page_last'                       
4 3 'Structure model' '_citation.pdbx_database_id_DOI'            
5 3 'Structure model' '_citation.pdbx_database_id_PubMed'         
6 3 'Structure model' '_citation.title'                           
7 3 'Structure model' '_pdbx_struct_oper_list.symmetry_operation' 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? dev_1426 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .        4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 476 ? ? O A HOH 484 ? ? 1.90 
2  1 O   A HOH 450 ? ? O A HOH 508 ? ? 1.93 
3  1 N   F CYS 1   ? ? O F HOH 101 ? ? 1.93 
4  1 O   D TRP 109 ? ? O D HOH 401 ? ? 1.98 
5  1 OE2 C GLU 123 ? A O C HOH 401 ? ? 2.01 
6  1 O   D HOH 426 ? ? O D HOH 470 ? ? 2.01 
7  1 OG1 C THR 178 ? ? O C HOH 402 ? ? 2.01 
8  1 OD2 C ASP 170 ? ? O C HOH 403 ? ? 2.02 
9  1 OD2 C ASP 185 ? ? O C HOH 404 ? ? 2.05 
10 1 NZ  C LYS 183 ? ? O C HOH 405 ? ? 2.05 
11 1 O   A HOH 426 ? ? O C HOH 453 ? ? 2.06 
12 1 O   A GLN 166 ? ? O A HOH 401 ? ? 2.07 
13 1 O   C HOH 481 ? ? O D HOH 454 ? ? 2.08 
14 1 O   C HOH 435 ? ? O C HOH 465 ? ? 2.08 
15 1 O   C HOH 445 ? ? O C HOH 455 ? ? 2.09 
16 1 O   A HOH 474 ? ? O A HOH 479 ? ? 2.09 
17 1 O   D HOH 405 ? ? O D HOH 430 ? ? 2.12 
18 1 O   B HOH 446 ? ? O B HOH 487 ? ? 2.12 
19 1 O   A THR 178 ? ? O A HOH 402 ? ? 2.13 
20 1 O   D HOH 405 ? ? O D HOH 481 ? ? 2.14 
21 1 OG1 C THR 180 ? ? O C HOH 406 ? ? 2.14 
22 1 OG1 C THR 129 ? ? O C HOH 407 ? ? 2.16 
23 1 O   A ILE 55  ? ? O A HOH 403 ? ? 2.17 
24 1 O   A HOH 455 ? ? O A HOH 490 ? ? 2.19 
# 
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 GLN A 27  ? ? -173.70 142.99  
2  1 ALA A 51  ? ? 70.28   -45.67  
3  1 ALA A 84  ? ? 177.51  175.06  
4  1 ASN A 91  ? ? -142.54 29.26   
5  1 ASN A 152 ? ? 57.74   3.27    
6  1 SER B 84  ? ? 39.00   76.21   
7  1 ALA B 120 ? ? -68.40  -169.80 
8  1 SER B 133 ? ? -156.50 -156.15 
9  1 ASN C 41  ? ? 63.06   -3.87   
10 1 ALA C 51  ? ? 73.98   -51.74  
11 1 SER D 15  ? ? 75.28   -15.33  
12 1 ARG D 66  ? ? -143.69 11.80   
13 1 ALA D 120 ? ? -57.84  172.59  
14 1 ASN D 210 ? ? 49.77   25.78   
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 169 ? CG  ? A LYS 169 CG  
2  1 Y 1 A LYS 169 ? CD  ? A LYS 169 CD  
3  1 Y 1 A LYS 169 ? CE  ? A LYS 169 CE  
4  1 Y 1 A LYS 169 ? NZ  ? A LYS 169 NZ  
5  1 Y 1 B GLN 1   ? CG  ? B GLN 1   CG  
6  1 Y 1 B GLN 1   ? CD  ? B GLN 1   CD  
7  1 Y 1 B GLN 1   ? OE1 ? B GLN 1   OE1 
8  1 Y 1 B GLN 1   ? NE2 ? B GLN 1   NE2 
9  1 Y 1 C LYS 169 ? CG  ? C LYS 169 CG  
10 1 Y 1 C LYS 169 ? CD  ? C LYS 169 CD  
11 1 Y 1 C LYS 169 ? CE  ? C LYS 169 CE  
12 1 Y 1 C LYS 169 ? NZ  ? C LYS 169 NZ  
13 1 Y 1 D GLN 1   ? CG  ? D GLN 1   CG  
14 1 Y 1 D GLN 1   ? CD  ? D GLN 1   CD  
15 1 Y 1 D GLN 1   ? OE1 ? D GLN 1   OE1 
16 1 Y 1 D GLN 1   ? NE2 ? D GLN 1   NE2 
# 
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 ALA 213 ? A ALA 213 
2 1 Y 1 D SER 133 ? D SER 133 
3 1 Y 1 D SER 134 ? D SER 134 
4 1 Y 1 D LYS 135 ? D LYS 135 
5 1 Y 1 D SER 136 ? D SER 136 
6 1 Y 1 D THR 137 ? D THR 137 
7 1 Y 1 D SER 138 ? D SER 138 
8 1 Y 1 D GLY 139 ? D GLY 139 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'PHOSPHATE ION'        PO4 
5 N-ACETYL-D-GLUCOSAMINE NAG 
6 MESO-ERYTHRITOL        MRY 
7 water                  HOH 
# 
