data_3LAQ
# 
_entry.id   3LAQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3LAQ         
RCSB  RCSB057045   
WWPDB D_1000057045 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 2FD6 . unspecified 
PDB 3BT1 . unspecified 
PDB 3BT2 . unspecified 
PDB 2FAT . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3LAQ 
_pdbx_database_status.recvd_initial_deposition_date   2010-01-06 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
_audit_author.name           'Huang, M.' 
_audit_author.pdbx_ordinal   1 
# 
_citation.id                        primary 
_citation.title                     
;Structure-based engineering of species selectivity in the interaction between urokinase and its receptor: implication for preclinical cancer therapy.
;
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_volume            285 
_citation.page_first                10982 
_citation.page_last                 10992 
_citation.year                      2010 
_citation.journal_id_ASTM           JBCHA3 
_citation.country                   US 
_citation.journal_id_ISSN           0021-9258 
_citation.journal_id_CSD            0071 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20133942 
_citation.pdbx_database_id_DOI      10.1074/jbc.M109.093492 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Lin, L.'       1 
primary 'Gardsvoll, H.' 2 
primary 'Huai, Q.'      3 
primary 'Huang, M.'     4 
primary 'Ploug, M.'     5 
# 
_cell.entry_id           3LAQ 
_cell.length_a           61.421 
_cell.length_b           137.248 
_cell.length_c           65.785 
_cell.angle_alpha        90.00 
_cell.angle_beta         106.17 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3LAQ 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Urokinase-type plasminogen activator'             14997.969 2  3.4.21.73 ? 'UNP residues 21-154' ? 
2 polymer     man 'Urokinase plasminogen activator surface receptor' 30170.777 2  ?         ? 'UNP residues 24-300' ? 
3 non-polymer man N-ACETYL-D-GLUCOSAMINE                             221.208   10 ?         ? ?                     ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;U-plasminogen activator, uPA, Urokinase-type plasminogen activator long chain A, Urokinase-type plasminogen activator short chain A, Urokinase-type plasminogen activator chain B
;
2 'uPAR, U-PAR' 
# 
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 
;GSVLGAPDESNCGCQNGGVCVSYKYFSRIRRCSCPRKFQGEHCEIDASKTCYHGNGDSYRGKANTDTKGRPCLAWNAPAV
LQKPYNAHRPDAISLGLGKHNYCRNPDNQKRPWCYVQIGLRQFVQECMVHDCSL
;
;GSVLGAPDESNCGCQNGGVCVSYKYFSRIRRCSCPRKFQGEHCEIDASKTCYHGNGDSYRGKANTDTKGRPCLAWNAPAV
LQKPYNAHRPDAISLGLGKHNYCRNPDNQKRPWCYVQIGLRQFVQECMVHDCSL
;
A,B ? 
2 'polypeptide(L)' no no 
;LQCMQCESNQSCLVEECALGQDLCRTTVLREWQDDRELEVVTRGCAHSEKTNRTMSYRMGSMIISLTETVCATNLCNRPR
PGARGRAFPQGRYLECASCTSLDQSCERGREQSLQCRYPTEHCIEVVTLQSTERSLKDEDYTRGCGSLPGCPGTAGFHSN
QTFHFLKCCNYTHCNGGPVLDLQSFPPNGFQCYSCEGNNTLGCSSEEASLINCRGPMNQCLVATGLDVLGNRSYTVRGCA
TASWCQGSHVADSFPTHLNVSVSCCHGSGCNSPTGGA
;
;LQCMQCESNQSCLVEECALGQDLCRTTVLREWQDDRELEVVTRGCAHSEKTNRTMSYRMGSMIISLTETVCATNLCNRPR
PGARGRAFPQGRYLECASCTSLDQSCERGREQSLQCRYPTEHCIEVVTLQSTERSLKDEDYTRGCGSLPGCPGTAGFHSN
QTFHFLKCCNYTHCNGGPVLDLQSFPPNGFQCYSCEGNNTLGCSSEEASLINCRGPMNQCLVATGLDVLGNRSYTVRGCA
TASWCQGSHVADSFPTHLNVSVSCCHGSGCNSPTGGA
;
U,V ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   VAL n 
1 4   LEU n 
1 5   GLY n 
1 6   ALA n 
1 7   PRO n 
1 8   ASP n 
1 9   GLU n 
1 10  SER n 
1 11  ASN n 
1 12  CYS n 
1 13  GLY n 
1 14  CYS n 
1 15  GLN n 
1 16  ASN n 
1 17  GLY n 
1 18  GLY n 
1 19  VAL n 
1 20  CYS n 
1 21  VAL n 
1 22  SER n 
1 23  TYR n 
1 24  LYS n 
1 25  TYR n 
1 26  PHE n 
1 27  SER n 
1 28  ARG n 
1 29  ILE n 
1 30  ARG n 
1 31  ARG n 
1 32  CYS n 
1 33  SER n 
1 34  CYS n 
1 35  PRO n 
1 36  ARG n 
1 37  LYS n 
1 38  PHE n 
1 39  GLN n 
1 40  GLY n 
1 41  GLU n 
1 42  HIS n 
1 43  CYS n 
1 44  GLU n 
1 45  ILE n 
1 46  ASP n 
1 47  ALA n 
1 48  SER n 
1 49  LYS n 
1 50  THR n 
1 51  CYS n 
1 52  TYR n 
1 53  HIS n 
1 54  GLY n 
1 55  ASN n 
1 56  GLY n 
1 57  ASP n 
1 58  SER n 
1 59  TYR n 
1 60  ARG n 
1 61  GLY n 
1 62  LYS n 
1 63  ALA n 
1 64  ASN n 
1 65  THR n 
1 66  ASP n 
1 67  THR n 
1 68  LYS n 
1 69  GLY n 
1 70  ARG n 
1 71  PRO n 
1 72  CYS n 
1 73  LEU n 
1 74  ALA n 
1 75  TRP n 
1 76  ASN n 
1 77  ALA n 
1 78  PRO n 
1 79  ALA n 
1 80  VAL n 
1 81  LEU n 
1 82  GLN n 
1 83  LYS n 
1 84  PRO n 
1 85  TYR n 
1 86  ASN n 
1 87  ALA n 
1 88  HIS n 
1 89  ARG n 
1 90  PRO n 
1 91  ASP n 
1 92  ALA n 
1 93  ILE n 
1 94  SER n 
1 95  LEU n 
1 96  GLY n 
1 97  LEU n 
1 98  GLY n 
1 99  LYS n 
1 100 HIS n 
1 101 ASN n 
1 102 TYR n 
1 103 CYS n 
1 104 ARG n 
1 105 ASN n 
1 106 PRO n 
1 107 ASP n 
1 108 ASN n 
1 109 GLN n 
1 110 LYS n 
1 111 ARG n 
1 112 PRO n 
1 113 TRP n 
1 114 CYS n 
1 115 TYR n 
1 116 VAL n 
1 117 GLN n 
1 118 ILE n 
1 119 GLY n 
1 120 LEU n 
1 121 ARG n 
1 122 GLN n 
1 123 PHE n 
1 124 VAL n 
1 125 GLN n 
1 126 GLU n 
1 127 CYS n 
1 128 MET n 
1 129 VAL n 
1 130 HIS n 
1 131 ASP n 
1 132 CYS n 
1 133 SER n 
1 134 LEU n 
2 1   LEU n 
2 2   GLN n 
2 3   CYS n 
2 4   MET n 
2 5   GLN n 
2 6   CYS n 
2 7   GLU n 
2 8   SER n 
2 9   ASN n 
2 10  GLN n 
2 11  SER n 
2 12  CYS n 
2 13  LEU n 
2 14  VAL n 
2 15  GLU n 
2 16  GLU n 
2 17  CYS n 
2 18  ALA n 
2 19  LEU n 
2 20  GLY n 
2 21  GLN n 
2 22  ASP n 
2 23  LEU n 
2 24  CYS n 
2 25  ARG n 
2 26  THR n 
2 27  THR n 
2 28  VAL n 
2 29  LEU n 
2 30  ARG n 
2 31  GLU n 
2 32  TRP n 
2 33  GLN n 
2 34  ASP n 
2 35  ASP n 
2 36  ARG n 
2 37  GLU n 
2 38  LEU n 
2 39  GLU n 
2 40  VAL n 
2 41  VAL n 
2 42  THR n 
2 43  ARG n 
2 44  GLY n 
2 45  CYS n 
2 46  ALA n 
2 47  HIS n 
2 48  SER n 
2 49  GLU n 
2 50  LYS n 
2 51  THR n 
2 52  ASN n 
2 53  ARG n 
2 54  THR n 
2 55  MET n 
2 56  SER n 
2 57  TYR n 
2 58  ARG n 
2 59  MET n 
2 60  GLY n 
2 61  SER n 
2 62  MET n 
2 63  ILE n 
2 64  ILE n 
2 65  SER n 
2 66  LEU n 
2 67  THR n 
2 68  GLU n 
2 69  THR n 
2 70  VAL n 
2 71  CYS n 
2 72  ALA n 
2 73  THR n 
2 74  ASN n 
2 75  LEU n 
2 76  CYS n 
2 77  ASN n 
2 78  ARG n 
2 79  PRO n 
2 80  ARG n 
2 81  PRO n 
2 82  GLY n 
2 83  ALA n 
2 84  ARG n 
2 85  GLY n 
2 86  ARG n 
2 87  ALA n 
2 88  PHE n 
2 89  PRO n 
2 90  GLN n 
2 91  GLY n 
2 92  ARG n 
2 93  TYR n 
2 94  LEU n 
2 95  GLU n 
2 96  CYS n 
2 97  ALA n 
2 98  SER n 
2 99  CYS n 
2 100 THR n 
2 101 SER n 
2 102 LEU n 
2 103 ASP n 
2 104 GLN n 
2 105 SER n 
2 106 CYS n 
2 107 GLU n 
2 108 ARG n 
2 109 GLY n 
2 110 ARG n 
2 111 GLU n 
2 112 GLN n 
2 113 SER n 
2 114 LEU n 
2 115 GLN n 
2 116 CYS n 
2 117 ARG n 
2 118 TYR n 
2 119 PRO n 
2 120 THR n 
2 121 GLU n 
2 122 HIS n 
2 123 CYS n 
2 124 ILE n 
2 125 GLU n 
2 126 VAL n 
2 127 VAL n 
2 128 THR n 
2 129 LEU n 
2 130 GLN n 
2 131 SER n 
2 132 THR n 
2 133 GLU n 
2 134 ARG n 
2 135 SER n 
2 136 LEU n 
2 137 LYS n 
2 138 ASP n 
2 139 GLU n 
2 140 ASP n 
2 141 TYR n 
2 142 THR n 
2 143 ARG n 
2 144 GLY n 
2 145 CYS n 
2 146 GLY n 
2 147 SER n 
2 148 LEU n 
2 149 PRO n 
2 150 GLY n 
2 151 CYS n 
2 152 PRO n 
2 153 GLY n 
2 154 THR n 
2 155 ALA n 
2 156 GLY n 
2 157 PHE n 
2 158 HIS n 
2 159 SER n 
2 160 ASN n 
2 161 GLN n 
2 162 THR n 
2 163 PHE n 
2 164 HIS n 
2 165 PHE n 
2 166 LEU n 
2 167 LYS n 
2 168 CYS n 
2 169 CYS n 
2 170 ASN n 
2 171 TYR n 
2 172 THR n 
2 173 HIS n 
2 174 CYS n 
2 175 ASN n 
2 176 GLY n 
2 177 GLY n 
2 178 PRO n 
2 179 VAL n 
2 180 LEU n 
2 181 ASP n 
2 182 LEU n 
2 183 GLN n 
2 184 SER n 
2 185 PHE n 
2 186 PRO n 
2 187 PRO n 
2 188 ASN n 
2 189 GLY n 
2 190 PHE n 
2 191 GLN n 
2 192 CYS n 
2 193 TYR n 
2 194 SER n 
2 195 CYS n 
2 196 GLU n 
2 197 GLY n 
2 198 ASN n 
2 199 ASN n 
2 200 THR n 
2 201 LEU n 
2 202 GLY n 
2 203 CYS n 
2 204 SER n 
2 205 SER n 
2 206 GLU n 
2 207 GLU n 
2 208 ALA n 
2 209 SER n 
2 210 LEU n 
2 211 ILE n 
2 212 ASN n 
2 213 CYS n 
2 214 ARG n 
2 215 GLY n 
2 216 PRO n 
2 217 MET n 
2 218 ASN n 
2 219 GLN n 
2 220 CYS n 
2 221 LEU n 
2 222 VAL n 
2 223 ALA n 
2 224 THR n 
2 225 GLY n 
2 226 LEU n 
2 227 ASP n 
2 228 VAL n 
2 229 LEU n 
2 230 GLY n 
2 231 ASN n 
2 232 ARG n 
2 233 SER n 
2 234 TYR n 
2 235 THR n 
2 236 VAL n 
2 237 ARG n 
2 238 GLY n 
2 239 CYS n 
2 240 ALA n 
2 241 THR n 
2 242 ALA n 
2 243 SER n 
2 244 TRP n 
2 245 CYS n 
2 246 GLN n 
2 247 GLY n 
2 248 SER n 
2 249 HIS n 
2 250 VAL n 
2 251 ALA n 
2 252 ASP n 
2 253 SER n 
2 254 PHE n 
2 255 PRO n 
2 256 THR n 
2 257 HIS n 
2 258 LEU n 
2 259 ASN n 
2 260 VAL n 
2 261 SER n 
2 262 VAL n 
2 263 SER n 
2 264 CYS n 
2 265 CYS n 
2 266 HIS n 
2 267 GLY n 
2 268 SER n 
2 269 GLY n 
2 270 CYS n 
2 271 ASN n 
2 272 SER n 
2 273 PRO n 
2 274 THR n 
2 275 GLY n 
2 276 GLY n 
2 277 ALA n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample ? ? ? mouse ? Plau  ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? Drosophila 7215 ? ? ? ? ? ? 'S2 cells' ? ? ? ? ? ? 
? plasmid ? ? ? pMT ? ? 
2 1 sample ? ? ? mouse ? Plaur ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? Drosophila 7215 ? ? ? ? ? ? 'S2 cells' ? ? ? ? ? ? 
? plasmid ? ? ? pMT ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP UROK_MOUSE P06869 1 
;GSVLGAPDESNCGCQNGGVCVSYKYFSRIRRCSCPRKFQGEHCEIDASKTCYHGNGDSYRGKANTDTKGRPCLAWNAPAV
LQKPYNAHRPDAISLGLGKHNYCRNPDNQKRPWCYVQIGLRQFVQECMVHDCSL
;
21 ? 
2 UNP UPAR_MOUSE P35456 2 
;LQCMQCESNQSCLVEECALGQDLCRTTVLREWQDDRELEVVTRGCAHSEKTNRTMSYRMGSMIISLTETVCATNLCNRPR
PGARGRAFPQGRYLECASCTSLDQSCERGREQSLQCRYPTEHCIEVVTLQSTERSLKDEDYTRGCGSLPGCPGTAGFHSN
QTFHFLKCCNYTHCNGGPVLDLQSFPPNGFQCYSCEGNNTLGCSSEEASLINCRGPMNQCLVATGLDVLGNRSYTVRGCA
TASWCQGSHVADSFPTHLNVSVSCCHGSGCNSPTGGA
;
24 ? 
# 
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 3LAQ A 1 ? 134 ? P06869 21 ? 154 ? 1 134 
2 2 3LAQ U 1 ? 277 ? P35456 24 ? 300 ? 1 277 
3 1 3LAQ B 1 ? 134 ? P06869 21 ? 154 ? 1 134 
4 2 3LAQ V 1 ? 277 ? P35456 24 ? 300 ? 1 277 
# 
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 
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 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          3LAQ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.95 
_exptl_crystal.density_percent_sol   58.28 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              5.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    
'5-7 % (w/v) PEG 3350, 50 mM Bis-Tris at pH 5.5., VAPOR DIFFUSION, SITTING DROP, temperature 293K' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           160 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315r' 
_diffrn_detector.pdbx_collection_date   2006-08 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    GRAPHITE 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'NSLS BEAMLINE X29A' 
_diffrn_source.pdbx_synchrotron_site       NSLS 
_diffrn_source.pdbx_synchrotron_beamline   X29A 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0 
# 
_reflns.entry_id                     3LAQ 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             50 
_reflns.d_resolution_high            3.2 
_reflns.number_obs                   17190 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         89.5 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             3.2 
_reflns_shell.d_res_low              3.21 
_reflns_shell.percent_possible_all   54.4 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 3LAQ 
_refine.ls_number_reflns_obs                     15297 
_refine.ls_number_reflns_all                     14272 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             44.74 
_refine.ls_d_res_high                            3.20 
_refine.ls_percent_reflns_obs                    93.3 
_refine.ls_R_factor_obs                          0.237 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.231 
_refine.ls_R_factor_R_free                       0.341 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.300 
_refine.ls_number_reflns_R_free                  853 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.894 
_refine.correlation_coeff_Fo_to_Fc_free          0.771 
_refine.B_iso_mean                               34.72 
_refine.aniso_B[1][1]                            2.02000 
_refine.aniso_B[2][2]                            -2.84000 
_refine.aniso_B[3][3]                            0.39000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.77000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.715 
_refine.overall_SU_ML                            0.577 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             70.075 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_TLS_residual_ADP_flag               'LIKELY RESIDUAL' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        5895 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         140 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               6035 
_refine_hist.d_res_high                       3.20 
_refine_hist.d_res_low                        44.74 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.014  0.021  ? 6203 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.800  1.967  ? 8419 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       8.270  5.000  ? 758  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       39.794 23.741 ? 294  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       24.301 15.000 ? 984  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       21.217 15.000 ? 52   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.122  0.200  ? 905  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.021  ? 4776 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.547  1.500  ? 3803 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.120  2.000  ? 6108 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.739  3.000  ? 2400 'X-RAY DIFFRACTION' ? 
r_scangle_it                 3.092  4.500  ? 2311 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       3.20 
_refine_ls_shell.d_res_low                        3.28 
_refine_ls_shell.number_reflns_R_work             760 
_refine_ls_shell.R_factor_R_work                  0.2560 
_refine_ls_shell.percent_reflns_obs               63.27 
_refine_ls_shell.R_factor_R_free                  0.3800 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             48 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_pdbx_refine.pdbx_refine_id                              'X-RAY DIFFRACTION' 
_pdbx_refine.entry_id                                    3LAQ 
_pdbx_refine.R_factor_all_no_cutoff                      ? 
_pdbx_refine.R_factor_obs_no_cutoff                      ? 
_pdbx_refine.free_R_factor_no_cutoff                     ? 
_pdbx_refine.free_R_error_no_cutoff                      ? 
_pdbx_refine.free_R_val_test_set_size_perc_no_cutoff     ? 
_pdbx_refine.free_R_val_test_set_ct_no_cutoff            ? 
_pdbx_refine.R_factor_all_4sig_cutoff                    ? 
_pdbx_refine.R_factor_obs_4sig_cutoff                    ? 
_pdbx_refine.free_R_factor_4sig_cutoff                   ? 
_pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff   ? 
_pdbx_refine.free_R_val_test_set_ct_4sig_cutoff          ? 
_pdbx_refine.number_reflns_obs_4sig_cutoff               ? 
# 
_struct.entry_id                  3LAQ 
_struct.title                     'Structure-based engineering of species selectivity in the uPA-uPAR interaction' 
_struct.pdbx_descriptor           
'Urokinase-type plasminogen activator (E.C.3.4.21.73), Urokinase plasminogen activator surface receptor' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3LAQ 
_struct_keywords.pdbx_keywords   'Hydrolase/Hydrolase Receptor' 
_struct_keywords.text            
;uPA, uPAR, ATF, suPAR, smuPAR, mATF, Disulfide bond, EGF-like domain, Hydrolase, Kringle, Plasminogen activation, Protease, Secreted, Serine protease, Zymogen, Cell membrane, Glycoprotein, GPI-anchor, Lipoprotein, Membrane, Receptor, Hydrolase-Hydrolase Receptor complex
;
# 
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 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 3 ? 
M N N 3 ? 
N N N 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 LYS A 24  ? SER A 27  ? LYS A 24  SER A 27  5 ? 4 
HELX_P HELX_P2 2 ALA A 79  ? LYS A 83  ? ALA A 79  LYS A 83  5 ? 5 
HELX_P HELX_P3 3 SER B 248 ? SER B 253 ? SER U 248 SER U 253 1 ? 6 
HELX_P HELX_P4 4 SER B 268 ? SER B 272 ? SER U 268 SER U 272 5 ? 5 
HELX_P HELX_P5 5 ALA C 77  ? GLN C 82  ? ALA B 77  GLN B 82  1 ? 6 
HELX_P HELX_P6 6 ASP C 91  ? LEU C 95  ? ASP B 91  LEU B 95  5 ? 5 
HELX_P HELX_P7 7 LEU D 102 ? GLN D 104 ? LEU V 102 GLN V 104 5 ? 3 
HELX_P HELX_P8 8 VAL D 250 ? PHE D 254 ? VAL V 250 PHE V 254 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 12  SG  ? ? ? 1_555 A CYS 20  SG ? ? A CYS 12  A CYS 20   1_555 ? ? ? ? ? ? ? 2.059 ? 
disulf2  disulf ? ? A CYS 14  SG  ? ? ? 1_555 A CYS 32  SG ? ? A CYS 14  A CYS 32   1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf3  disulf ? ? A CYS 34  SG  ? ? ? 1_555 A CYS 43  SG ? ? A CYS 34  A CYS 43   1_555 ? ? ? ? ? ? ? 2.074 ? 
disulf4  disulf ? ? A CYS 51  SG  ? ? ? 1_555 A CYS 132 SG ? ? A CYS 51  A CYS 132  1_555 ? ? ? ? ? ? ? 2.100 ? 
disulf5  disulf ? ? A CYS 72  SG  ? ? ? 1_555 A CYS 114 SG ? ? A CYS 72  A CYS 114  1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf6  disulf ? ? A CYS 103 SG  ? ? ? 1_555 A CYS 127 SG ? ? A CYS 103 A CYS 127  1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf7  disulf ? ? B CYS 3   SG  ? ? ? 1_555 B CYS 24  SG ? ? U CYS 3   U CYS 24   1_555 ? ? ? ? ? ? ? 2.005 ? 
disulf8  disulf ? ? B CYS 6   SG  ? ? ? 1_555 B CYS 12  SG ? ? U CYS 6   U CYS 12   1_555 ? ? ? ? ? ? ? 2.114 ? 
disulf9  disulf ? ? B CYS 17  SG  ? ? ? 1_555 B CYS 45  SG ? ? U CYS 17  U CYS 45   1_555 ? ? ? ? ? ? ? 2.069 ? 
disulf10 disulf ? ? B CYS 71  SG  ? ? ? 1_555 B CYS 76  SG ? ? U CYS 71  U CYS 76   1_555 ? ? ? ? ? ? ? 2.069 ? 
disulf11 disulf ? ? B CYS 96  SG  ? ? ? 1_555 B CYS 123 SG ? ? U CYS 96  U CYS 123  1_555 ? ? ? ? ? ? ? 2.061 ? 
disulf12 disulf ? ? B CYS 99  SG  ? ? ? 1_555 B CYS 106 SG ? ? U CYS 99  U CYS 106  1_555 ? ? ? ? ? ? ? 2.052 ? 
disulf13 disulf ? ? B CYS 116 SG  ? ? ? 1_555 B CYS 145 SG ? ? U CYS 116 U CYS 145  1_555 ? ? ? ? ? ? ? 2.055 ? 
disulf14 disulf ? ? B CYS 151 SG  ? ? ? 1_555 B CYS 168 SG ? ? U CYS 151 U CYS 168  1_555 ? ? ? ? ? ? ? 2.053 ? 
disulf15 disulf ? ? B CYS 169 SG  ? ? ? 1_555 B CYS 174 SG ? ? U CYS 169 U CYS 174  1_555 ? ? ? ? ? ? ? 2.034 ? 
disulf16 disulf ? ? B CYS 192 SG  ? ? ? 1_555 B CYS 220 SG ? ? U CYS 192 U CYS 220  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf17 disulf ? ? B CYS 195 SG  ? ? ? 1_555 B CYS 203 SG ? ? U CYS 195 U CYS 203  1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf18 disulf ? ? B CYS 213 SG  ? ? ? 1_555 B CYS 239 SG ? ? U CYS 213 U CYS 239  1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf19 disulf ? ? B CYS 245 SG  ? ? ? 1_555 B CYS 264 SG ? ? U CYS 245 U CYS 264  1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf20 disulf ? ? B CYS 265 SG  ? ? ? 1_555 B CYS 270 SG ? ? U CYS 265 U CYS 270  1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf21 disulf ? ? C CYS 12  SG  ? ? ? 1_555 C CYS 20  SG ? ? B CYS 12  B CYS 20   1_555 ? ? ? ? ? ? ? 2.061 ? 
disulf22 disulf ? ? C CYS 14  SG  ? ? ? 1_555 C CYS 32  SG ? ? B CYS 14  B CYS 32   1_555 ? ? ? ? ? ? ? 2.081 ? 
disulf23 disulf ? ? C CYS 34  SG  ? ? ? 1_555 C CYS 43  SG ? ? B CYS 34  B CYS 43   1_555 ? ? ? ? ? ? ? 2.067 ? 
disulf24 disulf ? ? C CYS 51  SG  ? ? ? 1_555 C CYS 132 SG ? ? B CYS 51  B CYS 132  1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf25 disulf ? ? C CYS 72  SG  ? ? ? 1_555 C CYS 114 SG ? ? B CYS 72  B CYS 114  1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf26 disulf ? ? C CYS 103 SG  ? ? ? 1_555 C CYS 127 SG ? ? B CYS 103 B CYS 127  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf27 disulf ? ? D CYS 3   SG  ? ? ? 1_555 D CYS 24  SG ? ? V CYS 3   V CYS 24   1_555 ? ? ? ? ? ? ? 2.069 ? 
disulf28 disulf ? ? D CYS 6   SG  ? ? ? 1_555 D CYS 12  SG ? ? V CYS 6   V CYS 12   1_555 ? ? ? ? ? ? ? 2.158 ? 
disulf29 disulf ? ? D CYS 17  SG  ? ? ? 1_555 D CYS 45  SG ? ? V CYS 17  V CYS 45   1_555 ? ? ? ? ? ? ? 2.078 ? 
disulf30 disulf ? ? D CYS 71  SG  ? ? ? 1_555 D CYS 76  SG ? ? V CYS 71  V CYS 76   1_555 ? ? ? ? ? ? ? 2.019 ? 
disulf31 disulf ? ? D CYS 96  SG  ? ? ? 1_555 D CYS 123 SG ? ? V CYS 96  V CYS 123  1_555 ? ? ? ? ? ? ? 2.037 ? 
disulf32 disulf ? ? D CYS 99  SG  ? ? ? 1_555 D CYS 106 SG ? ? V CYS 99  V CYS 106  1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf33 disulf ? ? D CYS 116 SG  ? ? ? 1_555 D CYS 145 SG ? ? V CYS 116 V CYS 145  1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf34 disulf ? ? D CYS 151 SG  ? ? ? 1_555 D CYS 168 SG ? ? V CYS 151 V CYS 168  1_555 ? ? ? ? ? ? ? 2.064 ? 
disulf35 disulf ? ? D CYS 169 SG  ? ? ? 1_555 D CYS 174 SG ? ? V CYS 169 V CYS 174  1_555 ? ? ? ? ? ? ? 2.027 ? 
disulf36 disulf ? ? D CYS 192 SG  ? ? ? 1_555 D CYS 220 SG ? ? V CYS 192 V CYS 220  1_555 ? ? ? ? ? ? ? 2.057 ? 
disulf37 disulf ? ? D CYS 195 SG  ? ? ? 1_555 D CYS 203 SG ? ? V CYS 195 V CYS 203  1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf38 disulf ? ? D CYS 213 SG  ? ? ? 1_555 D CYS 239 SG ? ? V CYS 213 V CYS 239  1_555 ? ? ? ? ? ? ? 2.056 ? 
disulf39 disulf ? ? D CYS 245 SG  ? ? ? 1_555 D CYS 264 SG ? ? V CYS 245 V CYS 264  1_555 ? ? ? ? ? ? ? 2.081 ? 
disulf40 disulf ? ? D CYS 265 SG  ? ? ? 1_555 D CYS 270 SG ? ? V CYS 265 V CYS 270  1_555 ? ? ? ? ? ? ? 2.026 ? 
covale1  covale ? ? B ASN 52  ND2 ? ? ? 1_555 E NAG .   C1 ? ? U ASN 52  U NAG 1052 1_555 ? ? ? ? ? ? ? 1.312 ? 
covale2  covale ? ? B ASN 170 ND2 ? ? ? 1_555 H NAG .   C1 ? ? U ASN 170 U NAG 1170 1_555 ? ? ? ? ? ? ? 1.346 ? 
covale3  covale ? ? D ASN 52  ND2 ? ? ? 1_555 J NAG .   C1 ? ? V ASN 52  V NAG 1052 1_555 ? ? ? ? ? ? ? 1.430 ? 
covale4  covale ? ? D ASN 160 ND2 ? ? ? 1_555 M NAG .   C1 ? ? V ASN 160 V NAG 1160 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale5  covale ? ? B ASN 259 ND2 ? ? ? 1_555 I NAG .   C1 ? ? U ASN 259 U NAG 1259 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale6  covale ? ? D ASN 259 ND2 ? ? ? 1_555 N NAG .   C1 ? ? V ASN 259 V NAG 1259 1_555 ? ? ? ? ? ? ? 1.454 ? 
covale7  covale ? ? D ASN 170 ND2 ? ? ? 1_555 L NAG .   C1 ? ? V ASN 170 V NAG 1170 1_555 ? ? ? ? ? ? ? 1.557 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2  ? 
B ? 2  ? 
C ? 2  ? 
D ? 2  ? 
E ? 6  ? 
F ? 11 ? 
G ? 2  ? 
H ? 2  ? 
I ? 2  ? 
J ? 2  ? 
K ? 2  ? 
L ? 2  ? 
M ? 6  ? 
N ? 11 ? 
O ? 2  ? 
P ? 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 
A 1  2  ? anti-parallel 
B 1  2  ? anti-parallel 
C 1  2  ? anti-parallel 
D 1  2  ? anti-parallel 
E 1  2  ? anti-parallel 
E 2  3  ? anti-parallel 
E 3  4  ? anti-parallel 
E 4  5  ? anti-parallel 
E 5  6  ? anti-parallel 
F 1  2  ? anti-parallel 
F 2  3  ? anti-parallel 
F 3  4  ? anti-parallel 
F 4  5  ? anti-parallel 
F 5  6  ? anti-parallel 
F 6  7  ? anti-parallel 
F 7  8  ? anti-parallel 
F 8  9  ? anti-parallel 
F 9  10 ? anti-parallel 
F 10 11 ? anti-parallel 
G 1  2  ? anti-parallel 
H 1  2  ? anti-parallel 
I 1  2  ? anti-parallel 
J 1  2  ? anti-parallel 
K 1  2  ? anti-parallel 
L 1  2  ? anti-parallel 
M 1  2  ? anti-parallel 
M 2  3  ? anti-parallel 
M 3  4  ? anti-parallel 
M 4  5  ? anti-parallel 
M 5  6  ? anti-parallel 
N 1  2  ? anti-parallel 
N 2  3  ? anti-parallel 
N 3  4  ? anti-parallel 
N 4  5  ? anti-parallel 
N 5  6  ? anti-parallel 
N 6  7  ? anti-parallel 
N 7  8  ? anti-parallel 
N 8  9  ? anti-parallel 
N 9  10 ? anti-parallel 
N 10 11 ? anti-parallel 
O 1  2  ? anti-parallel 
P 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 
A 1  CYS A 20  ? SER A 22  ? CYS A 20  SER A 22  
A 2  ARG A 30  ? CYS A 32  ? ARG A 30  CYS A 32  
B 1  PHE A 38  ? GLN A 39  ? PHE A 38  GLN A 39  
B 2  ILE A 45  ? ASP A 46  ? ILE A 45  ASP A 46  
C 1  TRP A 113 ? ILE A 118 ? TRP A 113 ILE A 118 
C 2  ARG A 121 ? GLU A 126 ? ARG A 121 GLU A 126 
D 1  GLN B 2   ? GLN B 5   ? GLN U 2   GLN U 5   
D 2  LEU B 13  ? GLU B 16  ? LEU U 13  GLU U 16  
E 1  LEU B 38  ? CYS B 45  ? LEU U 38  CYS U 45  
E 2  CYS B 24  ? TRP B 32  ? CYS U 24  TRP U 32  
E 3  MET B 62  ? GLU B 68  ? MET U 62  GLU U 68  
E 4  ARG B 53  ? MET B 59  ? ARG U 53  MET U 59  
E 5  TYR B 141 ? SER B 147 ? TYR U 141 SER U 147 
E 6  CYS B 99  ? THR B 100 ? CYS U 99  THR U 100 
F 1  LEU B 38  ? CYS B 45  ? LEU U 38  CYS U 45  
F 2  CYS B 24  ? TRP B 32  ? CYS U 24  TRP U 32  
F 3  MET B 62  ? GLU B 68  ? MET U 62  GLU U 68  
F 4  ARG B 53  ? MET B 59  ? ARG U 53  MET U 59  
F 5  TYR B 141 ? SER B 147 ? TYR U 141 SER U 147 
F 6  CYS B 123 ? GLN B 130 ? CYS U 123 GLN U 130 
F 7  THR B 162 ? CYS B 169 ? THR U 162 CYS U 169 
F 8  GLY B 153 ? HIS B 158 ? GLY U 153 HIS U 158 
F 9  VAL B 236 ? ALA B 240 ? VAL U 236 ALA U 240 
F 10 GLN B 219 ? ALA B 223 ? GLN U 219 ALA U 223 
F 11 VAL B 262 ? CYS B 265 ? VAL U 262 CYS U 265 
G 1  GLU B 95  ? ALA B 97  ? GLU U 95  ALA U 97  
G 2  SER B 113 ? GLN B 115 ? SER U 113 GLN U 115 
H 1  GLN B 191 ? SER B 194 ? GLN U 191 SER U 194 
H 2  SER B 209 ? ASN B 212 ? SER U 209 ASN U 212 
I 1  VAL C 19  ? CYS C 20  ? VAL B 19  CYS B 20  
I 2  CYS C 32  ? SER C 33  ? CYS B 32  SER B 33  
J 1  PHE C 38  ? GLN C 39  ? PHE B 38  GLN B 39  
J 2  ILE C 45  ? ASP C 46  ? ILE B 45  ASP B 46  
K 1  TRP C 113 ? VAL C 116 ? TRP B 113 VAL B 116 
K 2  PHE C 123 ? GLU C 126 ? PHE B 123 GLU B 126 
L 1  GLN D 2   ? GLN D 5   ? GLN V 2   GLN V 5   
L 2  LEU D 13  ? GLU D 16  ? LEU V 13  GLU V 16  
M 1  GLU D 39  ? CYS D 45  ? GLU V 39  CYS V 45  
M 2  CYS D 24  ? ARG D 30  ? CYS V 24  ARG V 30  
M 3  MET D 62  ? CYS D 71  ? MET V 62  CYS V 71  
M 4  ARG D 53  ? MET D 59  ? ARG V 53  MET V 59  
M 5  TYR D 141 ? SER D 147 ? TYR V 141 SER V 147 
M 6  CYS D 99  ? THR D 100 ? CYS V 99  THR V 100 
N 1  GLU D 39  ? CYS D 45  ? GLU V 39  CYS V 45  
N 2  CYS D 24  ? ARG D 30  ? CYS V 24  ARG V 30  
N 3  MET D 62  ? CYS D 71  ? MET V 62  CYS V 71  
N 4  ARG D 53  ? MET D 59  ? ARG V 53  MET V 59  
N 5  TYR D 141 ? SER D 147 ? TYR V 141 SER V 147 
N 6  HIS D 122 ? LEU D 129 ? HIS V 122 LEU V 129 
N 7  PHE D 163 ? CYS D 169 ? PHE V 163 CYS V 169 
N 8  GLY D 153 ? HIS D 158 ? GLY V 153 HIS V 158 
N 9  TYR D 234 ? ALA D 240 ? TYR V 234 ALA V 240 
N 10 GLN D 219 ? GLY D 225 ? GLN V 219 GLY V 225 
N 11 VAL D 262 ? CYS D 264 ? VAL V 262 CYS V 264 
O 1  GLU D 95  ? CYS D 96  ? GLU V 95  CYS V 96  
O 2  LEU D 114 ? GLN D 115 ? LEU V 114 GLN V 115 
P 1  PRO D 187 ? TYR D 193 ? PRO V 187 TYR V 193 
P 2  LEU D 210 ? ARG D 214 ? LEU V 210 ARG V 214 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1  2  N VAL A 21  ? N VAL A 21  O ARG A 31  ? O ARG A 31  
B 1  2  N GLN A 39  ? N GLN A 39  O ILE A 45  ? O ILE A 45  
C 1  2  N VAL A 116 ? N VAL A 116 O PHE A 123 ? O PHE A 123 
D 1  2  N GLN B 5   ? N GLN U 5   O LEU B 13  ? O LEU U 13  
E 1  2  O VAL B 40  ? O VAL U 40  N LEU B 29  ? N LEU U 29  
E 2  3  N VAL B 28  ? N VAL U 28  O THR B 67  ? O THR U 67  
E 3  4  O GLU B 68  ? O GLU U 68  N ARG B 53  ? N ARG U 53  
E 4  5  N SER B 56  ? N SER U 56  O CYS B 145 ? O CYS U 145 
E 5  6  O ARG B 143 ? O ARG U 143 N CYS B 99  ? N CYS U 99  
F 1  2  O VAL B 40  ? O VAL U 40  N LEU B 29  ? N LEU U 29  
F 2  3  N VAL B 28  ? N VAL U 28  O THR B 67  ? O THR U 67  
F 3  4  O GLU B 68  ? O GLU U 68  N ARG B 53  ? N ARG U 53  
F 4  5  N SER B 56  ? N SER U 56  O CYS B 145 ? O CYS U 145 
F 5  6  O THR B 142 ? O THR U 142 N VAL B 126 ? N VAL U 126 
F 6  7  N VAL B 127 ? N VAL U 127 O PHE B 165 ? O PHE U 165 
F 7  8  O LEU B 166 ? O LEU U 166 N ALA B 155 ? N ALA U 155 
F 8  9  N HIS B 158 ? N HIS U 158 O CYS B 239 ? O CYS U 239 
F 9  10 O GLY B 238 ? O GLY U 238 N LEU B 221 ? N LEU U 221 
F 10 11 N CYS B 220 ? N CYS U 220 O CYS B 265 ? O CYS U 265 
G 1  2  N CYS B 96  ? N CYS U 96  O LEU B 114 ? O LEU U 114 
H 1  2  N CYS B 192 ? N CYS U 192 O ILE B 211 ? O ILE U 211 
I 1  2  N VAL C 19  ? N VAL B 19  O SER C 33  ? O SER B 33  
J 1  2  N GLN C 39  ? N GLN B 39  O ILE C 45  ? O ILE B 45  
K 1  2  N CYS C 114 ? N CYS B 114 O GLN C 125 ? O GLN B 125 
L 1  2  N CYS D 3   ? N CYS V 3   O GLU D 15  ? O GLU V 15  
M 1  2  O THR D 42  ? O THR V 42  N THR D 27  ? N THR V 27  
M 2  3  N CYS D 24  ? N CYS V 24  O CYS D 71  ? O CYS V 71  
M 3  4  O ILE D 64  ? O ILE V 64  N TYR D 57  ? N TYR V 57  
M 4  5  N THR D 54  ? N THR V 54  O SER D 147 ? O SER V 147 
M 5  6  O ARG D 143 ? O ARG V 143 N CYS D 99  ? N CYS V 99  
N 1  2  O THR D 42  ? O THR V 42  N THR D 27  ? N THR V 27  
N 2  3  N CYS D 24  ? N CYS V 24  O CYS D 71  ? O CYS V 71  
N 3  4  O ILE D 64  ? O ILE V 64  N TYR D 57  ? N TYR V 57  
N 4  5  N THR D 54  ? N THR V 54  O SER D 147 ? O SER V 147 
N 5  6  O GLY D 144 ? O GLY V 144 N ILE D 124 ? N ILE V 124 
N 6  7  N CYS D 123 ? N CYS V 123 O CYS D 169 ? O CYS V 169 
N 7  8  O HIS D 164 ? O HIS V 164 N PHE D 157 ? N PHE V 157 
N 8  9  N HIS D 158 ? N HIS V 158 O CYS D 239 ? O CYS V 239 
N 9  10 O ALA D 240 ? O ALA V 240 N GLN D 219 ? N GLN V 219 
N 10 11 N VAL D 222 ? N VAL V 222 O SER D 263 ? O SER V 263 
O 1  2  N CYS D 96  ? N CYS V 96  O LEU D 114 ? O LEU V 114 
P 1  2  N CYS D 192 ? N CYS V 192 O ILE D 211 ? O ILE V 211 
# 
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 ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG U 1052' 
AC2 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG U 1053' 
AC3 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG U 1160' 
AC4 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG U 1170' 
AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG U 1259' 
AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG V 1052' 
AC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG V 1053' 
AC8 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG V 1170' 
AC9 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG V 1160' 
BC1 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG V 1259' 
# 
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 3 ASN B 52  ? ASN U 52   . ? 1_555 ? 
2  AC1 3 VAL B 70  ? VAL U 70   . ? 1_555 ? 
3  AC1 3 NAG F .   ? NAG U 1053 . ? 1_555 ? 
4  AC2 1 NAG E .   ? NAG U 1052 . ? 1_555 ? 
5  AC3 1 ASN B 160 ? ASN U 160  . ? 1_555 ? 
6  AC4 1 ASN B 170 ? ASN U 170  . ? 1_555 ? 
7  AC5 3 LEU B 19  ? LEU U 19   . ? 1_555 ? 
8  AC5 3 LEU B 258 ? LEU U 258  . ? 1_555 ? 
9  AC5 3 ASN B 259 ? ASN U 259  . ? 1_555 ? 
10 AC6 3 ASN D 52  ? ASN V 52   . ? 1_555 ? 
11 AC6 3 THR D 69  ? THR V 69   . ? 1_555 ? 
12 AC6 3 NAG K .   ? NAG V 1053 . ? 1_555 ? 
13 AC7 1 NAG J .   ? NAG V 1052 . ? 1_555 ? 
14 AC8 3 HIS C 53  ? HIS B 53   . ? 1_655 ? 
15 AC8 3 CYS C 132 ? CYS B 132  . ? 1_655 ? 
16 AC8 3 ASN D 170 ? ASN V 170  . ? 1_555 ? 
17 AC9 2 ASN D 160 ? ASN V 160  . ? 1_555 ? 
18 AC9 2 GLN D 161 ? GLN V 161  . ? 1_555 ? 
19 BC1 2 LEU D 258 ? LEU V 258  . ? 1_555 ? 
20 BC1 2 ASN D 259 ? ASN V 259  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3LAQ 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3LAQ 
_atom_sites.fract_transf_matrix[1][1]   0.016281 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004721 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007286 
_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]   0.015827 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
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   . GLU A 1 9   ? 33.196  -6.265  27.411  1.00 70.31 ? 9    GLU A N   1 
ATOM   2    C CA  . GLU A 1 9   ? 32.936  -5.265  28.502  1.00 70.24 ? 9    GLU A CA  1 
ATOM   3    C C   . GLU A 1 9   ? 31.514  -4.612  28.467  1.00 69.62 ? 9    GLU A C   1 
ATOM   4    O O   . GLU A 1 9   ? 30.597  -5.070  27.745  1.00 69.29 ? 9    GLU A O   1 
ATOM   5    C CB  . GLU A 1 9   ? 34.067  -4.205  28.581  1.00 70.43 ? 9    GLU A CB  1 
ATOM   6    C CG  . GLU A 1 9   ? 35.445  -4.731  29.081  1.00 71.87 ? 9    GLU A CG  1 
ATOM   7    C CD  . GLU A 1 9   ? 36.395  -3.617  29.609  1.00 74.33 ? 9    GLU A CD  1 
ATOM   8    O OE1 . GLU A 1 9   ? 35.905  -2.610  30.195  1.00 75.36 ? 9    GLU A OE1 1 
ATOM   9    O OE2 . GLU A 1 9   ? 37.636  -3.760  29.454  1.00 73.97 ? 9    GLU A OE2 1 
ATOM   10   N N   . SER A 1 10  ? 31.359  -3.549  29.268  1.00 68.74 ? 10   SER A N   1 
ATOM   11   C CA  . SER A 1 10  ? 30.052  -3.007  29.668  1.00 67.40 ? 10   SER A CA  1 
ATOM   12   C C   . SER A 1 10  ? 29.995  -1.507  29.483  1.00 66.02 ? 10   SER A C   1 
ATOM   13   O O   . SER A 1 10  ? 29.265  -1.042  28.629  1.00 65.93 ? 10   SER A O   1 
ATOM   14   C CB  . SER A 1 10  ? 29.760  -3.330  31.140  1.00 67.47 ? 10   SER A CB  1 
ATOM   15   O OG  . SER A 1 10  ? 29.914  -4.717  31.402  1.00 68.74 ? 10   SER A OG  1 
ATOM   16   N N   . ASN A 1 11  ? 30.758  -0.773  30.300  1.00 63.89 ? 11   ASN A N   1 
ATOM   17   C CA  . ASN A 1 11  ? 30.815  0.697   30.288  1.00 61.97 ? 11   ASN A CA  1 
ATOM   18   C C   . ASN A 1 11  ? 29.881  1.374   29.284  1.00 60.94 ? 11   ASN A C   1 
ATOM   19   O O   . ASN A 1 11  ? 30.332  2.075   28.369  1.00 60.90 ? 11   ASN A O   1 
ATOM   20   C CB  . ASN A 1 11  ? 32.260  1.193   30.115  1.00 61.86 ? 11   ASN A CB  1 
ATOM   21   C CG  . ASN A 1 11  ? 33.070  0.337   29.154  1.00 61.12 ? 11   ASN A CG  1 
ATOM   22   O OD1 . ASN A 1 11  ? 34.179  -0.081  29.479  1.00 60.88 ? 11   ASN A OD1 1 
ATOM   23   N ND2 . ASN A 1 11  ? 32.518  0.063   27.976  1.00 59.22 ? 11   ASN A ND2 1 
ATOM   24   N N   . CYS A 1 12  ? 28.580  1.133   29.466  1.00 59.38 ? 12   CYS A N   1 
ATOM   25   C CA  . CYS A 1 12  ? 27.507  1.749   28.685  1.00 57.79 ? 12   CYS A CA  1 
ATOM   26   C C   . CYS A 1 12  ? 26.313  1.957   29.600  1.00 57.13 ? 12   CYS A C   1 
ATOM   27   O O   . CYS A 1 12  ? 25.300  2.515   29.187  1.00 57.38 ? 12   CYS A O   1 
ATOM   28   C CB  . CYS A 1 12  ? 27.072  0.845   27.529  1.00 57.42 ? 12   CYS A CB  1 
ATOM   29   S SG  . CYS A 1 12  ? 28.213  0.725   26.100  1.00 57.03 ? 12   CYS A SG  1 
ATOM   30   N N   . GLY A 1 13  ? 26.443  1.512   30.849  1.00 56.25 ? 13   GLY A N   1 
ATOM   31   C CA  . GLY A 1 13  ? 25.325  1.455   31.804  1.00 54.84 ? 13   GLY A CA  1 
ATOM   32   C C   . GLY A 1 13  ? 24.936  0.011   32.083  1.00 53.73 ? 13   GLY A C   1 
ATOM   33   O O   . GLY A 1 13  ? 23.898  -0.275  32.680  1.00 53.71 ? 13   GLY A O   1 
ATOM   34   N N   . CYS A 1 14  ? 25.800  -0.898  31.657  1.00 52.43 ? 14   CYS A N   1 
ATOM   35   C CA  . CYS A 1 14  ? 25.509  -2.305  31.686  1.00 51.14 ? 14   CYS A CA  1 
ATOM   36   C C   . CYS A 1 14  ? 25.798  -2.916  33.034  1.00 50.31 ? 14   CYS A C   1 
ATOM   37   O O   . CYS A 1 14  ? 26.887  -3.433  33.314  1.00 49.89 ? 14   CYS A O   1 
ATOM   38   C CB  . CYS A 1 14  ? 26.244  -3.007  30.559  1.00 51.24 ? 14   CYS A CB  1 
ATOM   39   S SG  . CYS A 1 14  ? 25.264  -2.936  29.067  1.00 51.73 ? 14   CYS A SG  1 
ATOM   40   N N   . GLN A 1 15  ? 24.785  -2.835  33.880  1.00 49.40 ? 15   GLN A N   1 
ATOM   41   C CA  . GLN A 1 15  ? 24.862  -3.409  35.197  1.00 48.45 ? 15   GLN A CA  1 
ATOM   42   C C   . GLN A 1 15  ? 25.035  -4.936  35.109  1.00 47.66 ? 15   GLN A C   1 
ATOM   43   O O   . GLN A 1 15  ? 24.757  -5.551  34.058  1.00 47.67 ? 15   GLN A O   1 
ATOM   44   C CB  . GLN A 1 15  ? 23.651  -2.978  36.041  1.00 48.44 ? 15   GLN A CB  1 
ATOM   45   C CG  . GLN A 1 15  ? 23.837  -1.645  36.799  1.00 49.34 ? 15   GLN A CG  1 
ATOM   46   C CD  . GLN A 1 15  ? 24.777  -1.764  38.032  1.00 51.89 ? 15   GLN A CD  1 
ATOM   47   O OE1 . GLN A 1 15  ? 26.010  -1.790  37.899  1.00 51.82 ? 15   GLN A OE1 1 
ATOM   48   N NE2 . GLN A 1 15  ? 24.185  -1.826  39.234  1.00 52.25 ? 15   GLN A NE2 1 
ATOM   49   N N   . ASN A 1 16  ? 25.533  -5.513  36.212  1.00 46.45 ? 16   ASN A N   1 
ATOM   50   C CA  . ASN A 1 16  ? 25.805  -6.948  36.376  1.00 44.71 ? 16   ASN A CA  1 
ATOM   51   C C   . ASN A 1 16  ? 26.734  -7.542  35.316  1.00 44.31 ? 16   ASN A C   1 
ATOM   52   O O   . ASN A 1 16  ? 27.795  -6.978  35.017  1.00 44.26 ? 16   ASN A O   1 
ATOM   53   C CB  . ASN A 1 16  ? 24.498  -7.727  36.520  1.00 44.14 ? 16   ASN A CB  1 
ATOM   54   C CG  . ASN A 1 16  ? 23.732  -7.329  37.768  1.00 42.72 ? 16   ASN A CG  1 
ATOM   55   O OD1 . ASN A 1 16  ? 23.887  -7.949  38.807  1.00 42.30 ? 16   ASN A OD1 1 
ATOM   56   N ND2 . ASN A 1 16  ? 22.937  -6.270  37.682  1.00 39.96 ? 16   ASN A ND2 1 
ATOM   57   N N   . GLY A 1 17  ? 26.348  -8.679  34.758  1.00 43.74 ? 17   GLY A N   1 
ATOM   58   C CA  . GLY A 1 17  ? 27.130  -9.277  33.687  1.00 43.45 ? 17   GLY A CA  1 
ATOM   59   C C   . GLY A 1 17  ? 26.783  -8.719  32.314  1.00 43.16 ? 17   GLY A C   1 
ATOM   60   O O   . GLY A 1 17  ? 27.084  -9.351  31.304  1.00 43.11 ? 17   GLY A O   1 
ATOM   61   N N   . GLY A 1 18  ? 26.152  -7.542  32.282  1.00 42.78 ? 18   GLY A N   1 
ATOM   62   C CA  . GLY A 1 18  ? 25.754  -6.885  31.045  1.00 42.40 ? 18   GLY A CA  1 
ATOM   63   C C   . GLY A 1 18  ? 26.884  -6.760  30.044  1.00 42.47 ? 18   GLY A C   1 
ATOM   64   O O   . GLY A 1 18  ? 28.012  -6.447  30.411  1.00 42.06 ? 18   GLY A O   1 
ATOM   65   N N   . VAL A 1 19  ? 26.583  -7.031  28.774  1.00 42.89 ? 19   VAL A N   1 
ATOM   66   C CA  . VAL A 1 19  ? 27.561  -6.843  27.688  1.00 43.25 ? 19   VAL A CA  1 
ATOM   67   C C   . VAL A 1 19  ? 27.114  -5.743  26.714  1.00 43.45 ? 19   VAL A C   1 
ATOM   68   O O   . VAL A 1 19  ? 25.982  -5.747  26.211  1.00 43.08 ? 19   VAL A O   1 
ATOM   69   C CB  . VAL A 1 19  ? 27.904  -8.166  26.944  1.00 43.08 ? 19   VAL A CB  1 
ATOM   70   C CG1 . VAL A 1 19  ? 28.452  -7.892  25.556  1.00 42.76 ? 19   VAL A CG1 1 
ATOM   71   C CG2 . VAL A 1 19  ? 28.901  -8.976  27.744  1.00 43.03 ? 19   VAL A CG2 1 
ATOM   72   N N   . CYS A 1 20  ? 28.012  -4.793  26.474  1.00 43.61 ? 20   CYS A N   1 
ATOM   73   C CA  . CYS A 1 20  ? 27.674  -3.691  25.616  1.00 43.82 ? 20   CYS A CA  1 
ATOM   74   C C   . CYS A 1 20  ? 27.939  -4.063  24.183  1.00 42.37 ? 20   CYS A C   1 
ATOM   75   O O   . CYS A 1 20  ? 29.088  -4.281  23.792  1.00 41.90 ? 20   CYS A O   1 
ATOM   76   C CB  . CYS A 1 20  ? 28.428  -2.417  25.990  1.00 44.69 ? 20   CYS A CB  1 
ATOM   77   S SG  . CYS A 1 20  ? 27.659  -1.012  25.143  1.00 50.50 ? 20   CYS A SG  1 
ATOM   78   N N   . VAL A 1 21  ? 26.849  -4.141  23.421  1.00 41.26 ? 21   VAL A N   1 
ATOM   79   C CA  . VAL A 1 21  ? 26.889  -4.310  21.964  1.00 39.96 ? 21   VAL A CA  1 
ATOM   80   C C   . VAL A 1 21  ? 26.209  -3.112  21.288  1.00 39.10 ? 21   VAL A C   1 
ATOM   81   O O   . VAL A 1 21  ? 25.094  -2.743  21.649  1.00 38.91 ? 21   VAL A O   1 
ATOM   82   C CB  . VAL A 1 21  ? 26.252  -5.664  21.520  1.00 40.05 ? 21   VAL A CB  1 
ATOM   83   C CG1 . VAL A 1 21  ? 26.136  -6.638  22.711  1.00 39.82 ? 21   VAL A CG1 1 
ATOM   84   C CG2 . VAL A 1 21  ? 24.891  -5.475  20.875  1.00 39.85 ? 21   VAL A CG2 1 
ATOM   85   N N   . SER A 1 22  ? 26.895  -2.490  20.335  1.00 38.33 ? 22   SER A N   1 
ATOM   86   C CA  . SER A 1 22  ? 26.347  -1.326  19.609  1.00 37.92 ? 22   SER A CA  1 
ATOM   87   C C   . SER A 1 22  ? 25.917  -1.677  18.171  1.00 37.00 ? 22   SER A C   1 
ATOM   88   O O   . SER A 1 22  ? 25.855  -2.846  17.816  1.00 37.24 ? 22   SER A O   1 
ATOM   89   C CB  . SER A 1 22  ? 27.350  -0.163  19.608  1.00 38.38 ? 22   SER A CB  1 
ATOM   90   O OG  . SER A 1 22  ? 28.240  -0.213  18.493  1.00 38.67 ? 22   SER A OG  1 
ATOM   91   N N   . TYR A 1 23  ? 25.648  -0.680  17.334  1.00 35.72 ? 23   TYR A N   1 
ATOM   92   C CA  . TYR A 1 23  ? 25.077  -0.956  16.016  1.00 34.57 ? 23   TYR A CA  1 
ATOM   93   C C   . TYR A 1 23  ? 25.347  0.098   14.950  1.00 33.25 ? 23   TYR A C   1 
ATOM   94   O O   . TYR A 1 23  ? 24.572  1.042   14.802  1.00 32.87 ? 23   TYR A O   1 
ATOM   95   C CB  . TYR A 1 23  ? 23.578  -1.151  16.159  1.00 34.84 ? 23   TYR A CB  1 
ATOM   96   C CG  . TYR A 1 23  ? 23.195  -2.487  16.720  1.00 36.42 ? 23   TYR A CG  1 
ATOM   97   C CD1 . TYR A 1 23  ? 23.438  -3.653  16.008  1.00 37.62 ? 23   TYR A CD1 1 
ATOM   98   C CD2 . TYR A 1 23  ? 22.581  -2.590  17.973  1.00 38.92 ? 23   TYR A CD2 1 
ATOM   99   C CE1 . TYR A 1 23  ? 23.079  -4.903  16.531  1.00 40.17 ? 23   TYR A CE1 1 
ATOM   100  C CE2 . TYR A 1 23  ? 22.202  -3.837  18.504  1.00 40.16 ? 23   TYR A CE2 1 
ATOM   101  C CZ  . TYR A 1 23  ? 22.459  -4.990  17.774  1.00 40.46 ? 23   TYR A CZ  1 
ATOM   102  O OH  . TYR A 1 23  ? 22.104  -6.226  18.271  1.00 40.62 ? 23   TYR A OH  1 
ATOM   103  N N   . LYS A 1 24  ? 26.406  -0.096  14.172  1.00 31.92 ? 24   LYS A N   1 
ATOM   104  C CA  . LYS A 1 24  ? 26.921  0.987   13.340  1.00 31.26 ? 24   LYS A CA  1 
ATOM   105  C C   . LYS A 1 24  ? 25.910  1.680   12.430  1.00 30.89 ? 24   LYS A C   1 
ATOM   106  O O   . LYS A 1 24  ? 25.766  2.897   12.505  1.00 31.18 ? 24   LYS A O   1 
ATOM   107  C CB  . LYS A 1 24  ? 28.216  0.627   12.597  1.00 31.12 ? 24   LYS A CB  1 
ATOM   108  C CG  . LYS A 1 24  ? 28.159  -0.513  11.613  1.00 30.83 ? 24   LYS A CG  1 
ATOM   109  C CD  . LYS A 1 24  ? 29.504  -1.220  11.624  1.00 30.94 ? 24   LYS A CD  1 
ATOM   110  C CE  . LYS A 1 24  ? 29.828  -1.841  10.293  1.00 31.65 ? 24   LYS A CE  1 
ATOM   111  N NZ  . LYS A 1 24  ? 28.863  -2.890  9.869   1.00 31.30 ? 24   LYS A NZ  1 
ATOM   112  N N   . TYR A 1 25  ? 25.201  0.919   11.603  1.00 30.12 ? 25   TYR A N   1 
ATOM   113  C CA  . TYR A 1 25  ? 24.259  1.507   10.655  1.00 29.34 ? 25   TYR A CA  1 
ATOM   114  C C   . TYR A 1 25  ? 23.082  2.171   11.354  1.00 29.55 ? 25   TYR A C   1 
ATOM   115  O O   . TYR A 1 25  ? 22.383  3.003   10.786  1.00 29.48 ? 25   TYR A O   1 
ATOM   116  C CB  . TYR A 1 25  ? 23.751  0.454   9.666   1.00 29.18 ? 25   TYR A CB  1 
ATOM   117  C CG  . TYR A 1 25  ? 24.831  -0.163  8.819   1.00 26.82 ? 25   TYR A CG  1 
ATOM   118  C CD1 . TYR A 1 25  ? 25.609  0.619   7.969   1.00 25.39 ? 25   TYR A CD1 1 
ATOM   119  C CD2 . TYR A 1 25  ? 25.071  -1.519  8.863   1.00 24.86 ? 25   TYR A CD2 1 
ATOM   120  C CE1 . TYR A 1 25  ? 26.605  0.067   7.187   1.00 24.56 ? 25   TYR A CE1 1 
ATOM   121  C CE2 . TYR A 1 25  ? 26.072  -2.087  8.094   1.00 25.16 ? 25   TYR A CE2 1 
ATOM   122  C CZ  . TYR A 1 25  ? 26.838  -1.290  7.253   1.00 24.83 ? 25   TYR A CZ  1 
ATOM   123  O OH  . TYR A 1 25  ? 27.829  -1.858  6.479   1.00 23.87 ? 25   TYR A OH  1 
ATOM   124  N N   . PHE A 1 26  ? 22.857  1.801   12.598  1.00 29.79 ? 26   PHE A N   1 
ATOM   125  C CA  . PHE A 1 26  ? 21.774  2.418   13.329  1.00 30.24 ? 26   PHE A CA  1 
ATOM   126  C C   . PHE A 1 26  ? 22.280  3.366   14.400  1.00 30.43 ? 26   PHE A C   1 
ATOM   127  O O   . PHE A 1 26  ? 21.953  3.230   15.569  1.00 30.64 ? 26   PHE A O   1 
ATOM   128  C CB  . PHE A 1 26  ? 20.840  1.361   13.890  1.00 30.09 ? 26   PHE A CB  1 
ATOM   129  C CG  . PHE A 1 26  ? 20.178  0.562   12.840  1.00 29.94 ? 26   PHE A CG  1 
ATOM   130  C CD1 . PHE A 1 26  ? 20.923  -0.261  12.004  1.00 29.07 ? 26   PHE A CD1 1 
ATOM   131  C CD2 . PHE A 1 26  ? 18.809  0.642   12.661  1.00 31.33 ? 26   PHE A CD2 1 
ATOM   132  C CE1 . PHE A 1 26  ? 20.319  -1.002  11.024  1.00 28.62 ? 26   PHE A CE1 1 
ATOM   133  C CE2 . PHE A 1 26  ? 18.186  -0.113  11.664  1.00 31.12 ? 26   PHE A CE2 1 
ATOM   134  C CZ  . PHE A 1 26  ? 18.950  -0.936  10.852  1.00 29.70 ? 26   PHE A CZ  1 
ATOM   135  N N   . SER A 1 27  ? 23.087  4.327   13.969  1.00 30.56 ? 27   SER A N   1 
ATOM   136  C CA  . SER A 1 27  ? 23.526  5.439   14.808  1.00 30.57 ? 27   SER A CA  1 
ATOM   137  C C   . SER A 1 27  ? 24.101  5.086   16.215  1.00 30.83 ? 27   SER A C   1 
ATOM   138  O O   . SER A 1 27  ? 23.733  5.683   17.219  1.00 30.44 ? 27   SER A O   1 
ATOM   139  C CB  . SER A 1 27  ? 22.433  6.525   14.853  1.00 30.43 ? 27   SER A CB  1 
ATOM   140  O OG  . SER A 1 27  ? 21.153  5.991   14.573  1.00 28.60 ? 27   SER A OG  1 
ATOM   141  N N   . ARG A 1 28  ? 25.029  4.127   16.240  1.00 31.48 ? 28   ARG A N   1 
ATOM   142  C CA  . ARG A 1 28  ? 25.738  3.659   17.442  1.00 32.64 ? 28   ARG A CA  1 
ATOM   143  C C   . ARG A 1 28  ? 24.835  3.438   18.659  1.00 32.73 ? 28   ARG A C   1 
ATOM   144  O O   . ARG A 1 28  ? 25.320  3.397   19.786  1.00 32.78 ? 28   ARG A O   1 
ATOM   145  C CB  . ARG A 1 28  ? 26.923  4.560   17.799  1.00 32.88 ? 28   ARG A CB  1 
ATOM   146  C CG  . ARG A 1 28  ? 27.547  5.280   16.619  1.00 37.31 ? 28   ARG A CG  1 
ATOM   147  C CD  . ARG A 1 28  ? 28.600  4.460   15.825  1.00 45.74 ? 28   ARG A CD  1 
ATOM   148  N NE  . ARG A 1 28  ? 28.716  3.035   16.209  1.00 50.75 ? 28   ARG A NE  1 
ATOM   149  C CZ  . ARG A 1 28  ? 29.656  2.187   15.750  1.00 52.40 ? 28   ARG A CZ  1 
ATOM   150  N NH1 . ARG A 1 28  ? 30.577  2.592   14.861  1.00 51.19 ? 28   ARG A NH1 1 
ATOM   151  N NH2 . ARG A 1 28  ? 29.675  0.922   16.184  1.00 52.67 ? 28   ARG A NH2 1 
ATOM   152  N N   . ILE A 1 29  ? 23.527  3.308   18.412  1.00 33.13 ? 29   ILE A N   1 
ATOM   153  C CA  . ILE A 1 29  ? 22.550  2.834   19.393  1.00 33.39 ? 29   ILE A CA  1 
ATOM   154  C C   . ILE A 1 29  ? 23.087  1.566   20.039  1.00 34.69 ? 29   ILE A C   1 
ATOM   155  O O   . ILE A 1 29  ? 23.762  0.764   19.384  1.00 34.84 ? 29   ILE A O   1 
ATOM   156  C CB  . ILE A 1 29  ? 21.151  2.581   18.755  1.00 32.90 ? 29   ILE A CB  1 
ATOM   157  C CG1 . ILE A 1 29  ? 20.080  2.452   19.818  1.00 31.94 ? 29   ILE A CG1 1 
ATOM   158  C CG2 . ILE A 1 29  ? 21.131  1.344   17.895  1.00 31.96 ? 29   ILE A CG2 1 
ATOM   159  C CD1 . ILE A 1 29  ? 18.704  2.685   19.284  1.00 31.32 ? 29   ILE A CD1 1 
ATOM   160  N N   . ARG A 1 30  ? 22.823  1.409   21.333  1.00 35.98 ? 30   ARG A N   1 
ATOM   161  C CA  . ARG A 1 30  ? 23.403  0.317   22.094  1.00 37.42 ? 30   ARG A CA  1 
ATOM   162  C C   . ARG A 1 30  ? 22.285  -0.472  22.699  1.00 37.95 ? 30   ARG A C   1 
ATOM   163  O O   . ARG A 1 30  ? 21.207  0.067   22.899  1.00 38.52 ? 30   ARG A O   1 
ATOM   164  C CB  . ARG A 1 30  ? 24.311  0.827   23.218  1.00 37.53 ? 30   ARG A CB  1 
ATOM   165  C CG  . ARG A 1 30  ? 25.443  1.739   22.778  1.00 39.54 ? 30   ARG A CG  1 
ATOM   166  C CD  . ARG A 1 30  ? 25.087  3.211   23.028  1.00 43.65 ? 30   ARG A CD  1 
ATOM   167  N NE  . ARG A 1 30  ? 25.028  3.520   24.454  1.00 46.13 ? 30   ARG A NE  1 
ATOM   168  C CZ  . ARG A 1 30  ? 26.033  4.046   25.147  1.00 47.89 ? 30   ARG A CZ  1 
ATOM   169  N NH1 . ARG A 1 30  ? 27.190  4.341   24.543  1.00 47.74 ? 30   ARG A NH1 1 
ATOM   170  N NH2 . ARG A 1 30  ? 25.877  4.283   26.448  1.00 49.04 ? 30   ARG A NH2 1 
ATOM   171  N N   . ARG A 1 31  ? 22.532  -1.753  22.964  1.00 38.64 ? 31   ARG A N   1 
ATOM   172  C CA  . ARG A 1 31  ? 21.665  -2.532  23.827  1.00 39.07 ? 31   ARG A CA  1 
ATOM   173  C C   . ARG A 1 31  ? 22.582  -3.392  24.644  1.00 39.35 ? 31   ARG A C   1 
ATOM   174  O O   . ARG A 1 31  ? 23.730  -3.639  24.259  1.00 38.93 ? 31   ARG A O   1 
ATOM   175  C CB  . ARG A 1 31  ? 20.653  -3.361  23.023  1.00 39.23 ? 31   ARG A CB  1 
ATOM   176  C CG  . ARG A 1 31  ? 20.817  -4.855  23.104  1.00 39.84 ? 31   ARG A CG  1 
ATOM   177  C CD  . ARG A 1 31  ? 20.351  -5.546  21.832  1.00 41.32 ? 31   ARG A CD  1 
ATOM   178  N NE  . ARG A 1 31  ? 20.214  -6.997  22.023  1.00 41.62 ? 31   ARG A NE  1 
ATOM   179  C CZ  . ARG A 1 31  ? 21.202  -7.879  21.910  1.00 40.23 ? 31   ARG A CZ  1 
ATOM   180  N NH1 . ARG A 1 31  ? 22.431  -7.485  21.604  1.00 39.08 ? 31   ARG A NH1 1 
ATOM   181  N NH2 . ARG A 1 31  ? 20.956  -9.159  22.117  1.00 40.03 ? 31   ARG A NH2 1 
ATOM   182  N N   . CYS A 1 32  ? 22.068  -3.817  25.788  1.00 40.12 ? 32   CYS A N   1 
ATOM   183  C CA  . CYS A 1 32  ? 22.811  -4.623  26.738  1.00 41.39 ? 32   CYS A CA  1 
ATOM   184  C C   . CYS A 1 32  ? 22.452  -6.115  26.540  1.00 40.48 ? 32   CYS A C   1 
ATOM   185  O O   . CYS A 1 32  ? 21.294  -6.446  26.304  1.00 40.86 ? 32   CYS A O   1 
ATOM   186  C CB  . CYS A 1 32  ? 22.493  -4.115  28.158  1.00 42.03 ? 32   CYS A CB  1 
ATOM   187  S SG  . CYS A 1 32  ? 23.819  -4.330  29.451  1.00 48.83 ? 32   CYS A SG  1 
ATOM   188  N N   . SER A 1 33  ? 23.435  -7.015  26.599  1.00 39.48 ? 33   SER A N   1 
ATOM   189  C CA  . SER A 1 33  ? 23.142  -8.446  26.441  1.00 38.22 ? 33   SER A CA  1 
ATOM   190  C C   . SER A 1 33  ? 23.160  -9.134  27.791  1.00 36.84 ? 33   SER A C   1 
ATOM   191  O O   . SER A 1 33  ? 24.214  -9.491  28.288  1.00 36.16 ? 33   SER A O   1 
ATOM   192  C CB  . SER A 1 33  ? 24.143  -9.120  25.501  1.00 38.76 ? 33   SER A CB  1 
ATOM   193  O OG  . SER A 1 33  ? 25.332  -9.467  26.202  1.00 39.69 ? 33   SER A OG  1 
ATOM   194  N N   . CYS A 1 34  ? 21.982  -9.328  28.364  1.00 35.77 ? 34   CYS A N   1 
ATOM   195  C CA  . CYS A 1 34  ? 21.868  -9.723  29.762  1.00 35.19 ? 34   CYS A CA  1 
ATOM   196  C C   . CYS A 1 34  ? 22.066  -11.223 30.023  1.00 34.78 ? 34   CYS A C   1 
ATOM   197  O O   . CYS A 1 34  ? 21.804  -12.056 29.139  1.00 35.24 ? 34   CYS A O   1 
ATOM   198  C CB  . CYS A 1 34  ? 20.531  -9.247  30.340  1.00 34.94 ? 34   CYS A CB  1 
ATOM   199  S SG  . CYS A 1 34  ? 20.274  -7.430  30.373  1.00 35.03 ? 34   CYS A SG  1 
ATOM   200  N N   . PRO A 1 35  ? 22.554  -11.572 31.232  1.00 33.84 ? 35   PRO A N   1 
ATOM   201  C CA  . PRO A 1 35  ? 22.533  -12.942 31.703  1.00 33.13 ? 35   PRO A CA  1 
ATOM   202  C C   . PRO A 1 35  ? 21.149  -13.262 32.224  1.00 32.74 ? 35   PRO A C   1 
ATOM   203  O O   . PRO A 1 35  ? 20.316  -12.365 32.338  1.00 32.49 ? 35   PRO A O   1 
ATOM   204  C CB  . PRO A 1 35  ? 23.530  -12.925 32.851  1.00 32.96 ? 35   PRO A CB  1 
ATOM   205  C CG  . PRO A 1 35  ? 24.322  -11.710 32.643  1.00 33.28 ? 35   PRO A CG  1 
ATOM   206  C CD  . PRO A 1 35  ? 23.369  -10.733 32.115  1.00 33.58 ? 35   PRO A CD  1 
ATOM   207  N N   . ARG A 1 36  ? 20.905  -14.529 32.551  1.00 32.57 ? 36   ARG A N   1 
ATOM   208  C CA  . ARG A 1 36  ? 19.537  -14.983 32.824  1.00 32.06 ? 36   ARG A CA  1 
ATOM   209  C C   . ARG A 1 36  ? 18.884  -14.254 33.978  1.00 30.95 ? 36   ARG A C   1 
ATOM   210  O O   . ARG A 1 36  ? 17.703  -13.927 33.893  1.00 30.62 ? 36   ARG A O   1 
ATOM   211  C CB  . ARG A 1 36  ? 19.404  -16.529 32.951  1.00 32.62 ? 36   ARG A CB  1 
ATOM   212  C CG  . ARG A 1 36  ? 19.915  -17.210 34.237  1.00 34.28 ? 36   ARG A CG  1 
ATOM   213  C CD  . ARG A 1 36  ? 19.190  -18.593 34.501  1.00 36.84 ? 36   ARG A CD  1 
ATOM   214  N NE  . ARG A 1 36  ? 20.110  -19.691 34.906  1.00 38.13 ? 36   ARG A NE  1 
ATOM   215  C CZ  . ARG A 1 36  ? 20.205  -20.237 36.127  1.00 37.60 ? 36   ARG A CZ  1 
ATOM   216  N NH1 . ARG A 1 36  ? 19.434  -19.829 37.125  1.00 35.67 ? 36   ARG A NH1 1 
ATOM   217  N NH2 . ARG A 1 36  ? 21.072  -21.222 36.345  1.00 38.21 ? 36   ARG A NH2 1 
ATOM   218  N N   . LYS A 1 37  ? 19.669  -13.971 35.019  1.00 29.92 ? 37   LYS A N   1 
ATOM   219  C CA  . LYS A 1 37  ? 19.156  -13.366 36.261  1.00 28.87 ? 37   LYS A CA  1 
ATOM   220  C C   . LYS A 1 37  ? 18.628  -11.936 36.097  1.00 27.55 ? 37   LYS A C   1 
ATOM   221  O O   . LYS A 1 37  ? 17.621  -11.568 36.701  1.00 26.45 ? 37   LYS A O   1 
ATOM   222  C CB  . LYS A 1 37  ? 20.224  -13.418 37.364  1.00 29.16 ? 37   LYS A CB  1 
ATOM   223  C CG  . LYS A 1 37  ? 19.663  -13.713 38.761  1.00 30.37 ? 37   LYS A CG  1 
ATOM   224  C CD  . LYS A 1 37  ? 20.555  -13.186 39.922  1.00 33.12 ? 37   LYS A CD  1 
ATOM   225  C CE  . LYS A 1 37  ? 21.902  -13.945 40.111  1.00 33.75 ? 37   LYS A CE  1 
ATOM   226  N NZ  . LYS A 1 37  ? 21.790  -15.346 40.643  1.00 32.46 ? 37   LYS A NZ  1 
ATOM   227  N N   . PHE A 1 38  ? 19.295  -11.153 35.254  1.00 26.78 ? 38   PHE A N   1 
ATOM   228  C CA  . PHE A 1 38  ? 19.019  -9.725  35.153  1.00 26.50 ? 38   PHE A CA  1 
ATOM   229  C C   . PHE A 1 38  ? 18.409  -9.279  33.846  1.00 26.31 ? 38   PHE A C   1 
ATOM   230  O O   . PHE A 1 38  ? 19.072  -9.207  32.825  1.00 26.61 ? 38   PHE A O   1 
ATOM   231  C CB  . PHE A 1 38  ? 20.273  -8.923  35.471  1.00 26.48 ? 38   PHE A CB  1 
ATOM   232  C CG  . PHE A 1 38  ? 20.883  -9.298  36.789  1.00 27.57 ? 38   PHE A CG  1 
ATOM   233  C CD1 . PHE A 1 38  ? 20.417  -8.723  37.976  1.00 26.01 ? 38   PHE A CD1 1 
ATOM   234  C CD2 . PHE A 1 38  ? 21.893  -10.273 36.855  1.00 28.16 ? 38   PHE A CD2 1 
ATOM   235  C CE1 . PHE A 1 38  ? 20.942  -9.095  39.183  1.00 24.52 ? 38   PHE A CE1 1 
ATOM   236  C CE2 . PHE A 1 38  ? 22.434  -10.647 38.074  1.00 26.49 ? 38   PHE A CE2 1 
ATOM   237  C CZ  . PHE A 1 38  ? 21.950  -10.056 39.236  1.00 26.04 ? 38   PHE A CZ  1 
ATOM   238  N N   . GLN A 1 39  ? 17.127  -8.970  33.896  1.00 26.07 ? 39   GLN A N   1 
ATOM   239  C CA  . GLN A 1 39  ? 16.401  -8.534  32.734  1.00 26.17 ? 39   GLN A CA  1 
ATOM   240  C C   . GLN A 1 39  ? 16.533  -7.040  32.600  1.00 26.94 ? 39   GLN A C   1 
ATOM   241  O O   . GLN A 1 39  ? 17.247  -6.416  33.392  1.00 27.57 ? 39   GLN A O   1 
ATOM   242  C CB  . GLN A 1 39  ? 14.961  -8.935  32.889  1.00 25.55 ? 39   GLN A CB  1 
ATOM   243  C CG  . GLN A 1 39  ? 14.825  -10.430 33.095  1.00 25.05 ? 39   GLN A CG  1 
ATOM   244  C CD  . GLN A 1 39  ? 13.391  -10.826 33.251  1.00 25.41 ? 39   GLN A CD  1 
ATOM   245  O OE1 . GLN A 1 39  ? 13.032  -12.004 33.162  1.00 23.87 ? 39   GLN A OE1 1 
ATOM   246  N NE2 . GLN A 1 39  ? 12.539  -9.826  33.472  1.00 26.68 ? 39   GLN A NE2 1 
ATOM   247  N N   . GLY A 1 40  ? 15.881  -6.455  31.597  1.00 27.38 ? 40   GLY A N   1 
ATOM   248  C CA  . GLY A 1 40  ? 15.820  -4.986  31.507  1.00 28.07 ? 40   GLY A CA  1 
ATOM   249  C C   . GLY A 1 40  ? 17.006  -4.311  30.838  1.00 28.54 ? 40   GLY A C   1 
ATOM   250  O O   . GLY A 1 40  ? 18.083  -4.898  30.721  1.00 28.92 ? 40   GLY A O   1 
ATOM   251  N N   . GLU A 1 41  ? 16.796  -3.060  30.427  1.00 28.73 ? 41   GLU A N   1 
ATOM   252  C CA  . GLU A 1 41  ? 17.637  -2.353  29.454  1.00 28.92 ? 41   GLU A CA  1 
ATOM   253  C C   . GLU A 1 41  ? 19.035  -2.068  29.934  1.00 29.05 ? 41   GLU A C   1 
ATOM   254  O O   . GLU A 1 41  ? 19.820  -1.475  29.223  1.00 29.31 ? 41   GLU A O   1 
ATOM   255  C CB  . GLU A 1 41  ? 16.949  -1.049  29.068  1.00 29.05 ? 41   GLU A CB  1 
ATOM   256  C CG  . GLU A 1 41  ? 17.781  -0.046  28.293  1.00 30.72 ? 41   GLU A CG  1 
ATOM   257  C CD  . GLU A 1 41  ? 17.154  1.359   28.272  1.00 34.16 ? 41   GLU A CD  1 
ATOM   258  O OE1 . GLU A 1 41  ? 17.917  2.346   28.085  1.00 35.35 ? 41   GLU A OE1 1 
ATOM   259  O OE2 . GLU A 1 41  ? 15.909  1.481   28.451  1.00 35.16 ? 41   GLU A OE2 1 
ATOM   260  N N   . HIS A 1 42  ? 19.355  -2.470  31.147  1.00 29.62 ? 42   HIS A N   1 
ATOM   261  C CA  . HIS A 1 42  ? 20.710  -2.301  31.629  1.00 30.57 ? 42   HIS A CA  1 
ATOM   262  C C   . HIS A 1 42  ? 21.160  -3.528  32.391  1.00 30.61 ? 42   HIS A C   1 
ATOM   263  O O   . HIS A 1 42  ? 22.306  -3.620  32.853  1.00 30.89 ? 42   HIS A O   1 
ATOM   264  C CB  . HIS A 1 42  ? 20.797  -1.060  32.498  1.00 30.86 ? 42   HIS A CB  1 
ATOM   265  C CG  . HIS A 1 42  ? 20.418  0.195   31.778  1.00 33.20 ? 42   HIS A CG  1 
ATOM   266  N ND1 . HIS A 1 42  ? 19.227  0.856   32.007  1.00 34.89 ? 42   HIS A ND1 1 
ATOM   267  C CD2 . HIS A 1 42  ? 21.059  0.896   30.811  1.00 34.88 ? 42   HIS A CD2 1 
ATOM   268  C CE1 . HIS A 1 42  ? 19.162  1.925   31.233  1.00 35.75 ? 42   HIS A CE1 1 
ATOM   269  N NE2 . HIS A 1 42  ? 20.257  1.967   30.491  1.00 36.42 ? 42   HIS A NE2 1 
ATOM   270  N N   . CYS A 1 43  ? 20.253  -4.495  32.474  1.00 30.47 ? 43   CYS A N   1 
ATOM   271  C CA  . CYS A 1 43  ? 20.451  -5.646  33.313  1.00 30.27 ? 43   CYS A CA  1 
ATOM   272  C C   . CYS A 1 43  ? 20.410  -5.011  34.675  1.00 29.13 ? 43   CYS A C   1 
ATOM   273  O O   . CYS A 1 43  ? 21.314  -5.117  35.471  1.00 29.27 ? 43   CYS A O   1 
ATOM   274  C CB  . CYS A 1 43  ? 21.774  -6.334  32.975  1.00 30.66 ? 43   CYS A CB  1 
ATOM   275  S SG  . CYS A 1 43  ? 22.019  -6.609  31.135  1.00 34.68 ? 43   CYS A SG  1 
ATOM   276  N N   . GLU A 1 44  ? 19.315  -4.309  34.888  1.00 28.11 ? 44   GLU A N   1 
ATOM   277  C CA  . GLU A 1 44  ? 19.097  -3.491  36.040  1.00 27.40 ? 44   GLU A CA  1 
ATOM   278  C C   . GLU A 1 44  ? 18.150  -4.225  36.956  1.00 26.38 ? 44   GLU A C   1 
ATOM   279  O O   . GLU A 1 44  ? 17.846  -3.757  38.049  1.00 25.86 ? 44   GLU A O   1 
ATOM   280  C CB  . GLU A 1 44  ? 18.424  -2.218  35.556  1.00 28.01 ? 44   GLU A CB  1 
ATOM   281  C CG  . GLU A 1 44  ? 17.175  -2.497  34.702  1.00 30.57 ? 44   GLU A CG  1 
ATOM   282  C CD  . GLU A 1 44  ? 17.078  -1.634  33.443  1.00 33.70 ? 44   GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 44  ? 18.087  -0.994  33.074  1.00 32.64 ? 44   GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 44  ? 15.982  -1.610  32.816  1.00 35.54 ? 44   GLU A OE2 1 
ATOM   285  N N   . ILE A 1 45  ? 17.677  -5.379  36.483  1.00 25.68 ? 45   ILE A N   1 
ATOM   286  C CA  . ILE A 1 45  ? 16.550  -6.105  37.091  1.00 24.39 ? 45   ILE A CA  1 
ATOM   287  C C   . ILE A 1 45  ? 16.909  -7.502  37.609  1.00 24.19 ? 45   ILE A C   1 
ATOM   288  O O   . ILE A 1 45  ? 17.240  -8.366  36.821  1.00 24.29 ? 45   ILE A O   1 
ATOM   289  C CB  . ILE A 1 45  ? 15.393  -6.227  36.080  1.00 23.72 ? 45   ILE A CB  1 
ATOM   290  C CG1 . ILE A 1 45  ? 15.111  -4.869  35.436  1.00 22.12 ? 45   ILE A CG1 1 
ATOM   291  C CG2 . ILE A 1 45  ? 14.179  -6.779  36.753  1.00 23.70 ? 45   ILE A CG2 1 
ATOM   292  C CD1 . ILE A 1 45  ? 13.662  -4.508  35.339  1.00 20.21 ? 45   ILE A CD1 1 
ATOM   293  N N   . ASP A 1 46  ? 16.852  -7.723  38.922  1.00 24.15 ? 46   ASP A N   1 
ATOM   294  C CA  . ASP A 1 46  ? 17.097  -9.067  39.464  1.00 24.43 ? 46   ASP A CA  1 
ATOM   295  C C   . ASP A 1 46  ? 15.776  -9.772  39.515  1.00 24.69 ? 46   ASP A C   1 
ATOM   296  O O   . ASP A 1 46  ? 14.954  -9.540  40.398  1.00 24.75 ? 46   ASP A O   1 
ATOM   297  C CB  . ASP A 1 46  ? 17.764  -9.065  40.856  1.00 24.48 ? 46   ASP A CB  1 
ATOM   298  C CG  . ASP A 1 46  ? 18.070  -10.484 41.381  1.00 23.95 ? 46   ASP A CG  1 
ATOM   299  O OD1 . ASP A 1 46  ? 17.550  -11.470 40.810  1.00 22.68 ? 46   ASP A OD1 1 
ATOM   300  O OD2 . ASP A 1 46  ? 18.835  -10.606 42.370  1.00 23.76 ? 46   ASP A OD2 1 
ATOM   301  N N   . ALA A 1 47  ? 15.576  -10.639 38.544  1.00 25.18 ? 47   ALA A N   1 
ATOM   302  C CA  . ALA A 1 47  ? 14.286  -11.244 38.358  1.00 25.79 ? 47   ALA A CA  1 
ATOM   303  C C   . ALA A 1 47  ? 14.082  -12.444 39.270  1.00 26.39 ? 47   ALA A C   1 
ATOM   304  O O   . ALA A 1 47  ? 13.003  -13.026 39.272  1.00 26.45 ? 47   ALA A O   1 
ATOM   305  C CB  . ALA A 1 47  ? 14.117  -11.617 36.909  1.00 25.69 ? 47   ALA A CB  1 
ATOM   306  N N   . SER A 1 48  ? 15.123  -12.812 40.026  1.00 27.47 ? 48   SER A N   1 
ATOM   307  C CA  . SER A 1 48  ? 15.043  -13.884 41.022  1.00 28.47 ? 48   SER A CA  1 
ATOM   308  C C   . SER A 1 48  ? 14.389  -13.402 42.333  1.00 29.34 ? 48   SER A C   1 
ATOM   309  O O   . SER A 1 48  ? 13.612  -14.125 42.959  1.00 29.20 ? 48   SER A O   1 
ATOM   310  C CB  . SER A 1 48  ? 16.426  -14.485 41.291  1.00 28.59 ? 48   SER A CB  1 
ATOM   311  O OG  . SER A 1 48  ? 17.274  -13.623 42.039  1.00 29.09 ? 48   SER A OG  1 
ATOM   312  N N   . LYS A 1 49  ? 14.689  -12.169 42.726  1.00 30.41 ? 49   LYS A N   1 
ATOM   313  C CA  . LYS A 1 49  ? 14.079  -11.570 43.900  1.00 31.86 ? 49   LYS A CA  1 
ATOM   314  C C   . LYS A 1 49  ? 12.553  -11.724 43.993  1.00 32.42 ? 49   LYS A C   1 
ATOM   315  O O   . LYS A 1 49  ? 11.802  -11.396 43.084  1.00 32.40 ? 49   LYS A O   1 
ATOM   316  C CB  . LYS A 1 49  ? 14.485  -10.099 44.047  1.00 32.28 ? 49   LYS A CB  1 
ATOM   317  C CG  . LYS A 1 49  ? 15.700  -9.868  44.948  1.00 34.02 ? 49   LYS A CG  1 
ATOM   318  C CD  . LYS A 1 49  ? 15.499  -8.625  45.818  1.00 36.34 ? 49   LYS A CD  1 
ATOM   319  C CE  . LYS A 1 49  ? 16.301  -8.714  47.139  1.00 38.51 ? 49   LYS A CE  1 
ATOM   320  N NZ  . LYS A 1 49  ? 15.792  -9.723  48.147  1.00 39.78 ? 49   LYS A NZ  1 
ATOM   321  N N   . THR A 1 50  ? 12.126  -12.199 45.151  1.00 33.42 ? 50   THR A N   1 
ATOM   322  C CA  . THR A 1 50  ? 10.764  -12.596 45.392  1.00 33.99 ? 50   THR A CA  1 
ATOM   323  C C   . THR A 1 50  ? 10.183  -11.880 46.629  1.00 34.30 ? 50   THR A C   1 
ATOM   324  O O   . THR A 1 50  ? 8.977   -11.639 46.699  1.00 33.94 ? 50   THR A O   1 
ATOM   325  C CB  . THR A 1 50  ? 10.751  -14.119 45.558  1.00 34.22 ? 50   THR A CB  1 
ATOM   326  O OG1 . THR A 1 50  ? 9.424   -14.558 45.849  1.00 35.97 ? 50   THR A OG1 1 
ATOM   327  C CG2 . THR A 1 50  ? 11.750  -14.581 46.662  1.00 33.37 ? 50   THR A CG2 1 
ATOM   328  N N   . CYS A 1 51  ? 11.052  -11.587 47.606  1.00 34.81 ? 51   CYS A N   1 
ATOM   329  C CA  . CYS A 1 51  ? 10.767  -10.669 48.709  1.00 35.37 ? 51   CYS A CA  1 
ATOM   330  C C   . CYS A 1 51  ? 11.684  -9.426  48.633  1.00 34.55 ? 51   CYS A C   1 
ATOM   331  O O   . CYS A 1 51  ? 12.599  -9.369  47.815  1.00 34.12 ? 51   CYS A O   1 
ATOM   332  C CB  . CYS A 1 51  ? 10.844  -11.381 50.084  1.00 36.07 ? 51   CYS A CB  1 
ATOM   333  S SG  . CYS A 1 51  ? 12.462  -12.091 50.744  1.00 41.39 ? 51   CYS A SG  1 
ATOM   334  N N   . TYR A 1 52  ? 11.425  -8.423  49.468  1.00 34.21 ? 52   TYR A N   1 
ATOM   335  C CA  . TYR A 1 52  ? 12.345  -7.278  49.612  1.00 33.70 ? 52   TYR A CA  1 
ATOM   336  C C   . TYR A 1 52  ? 12.963  -7.110  51.034  1.00 33.66 ? 52   TYR A C   1 
ATOM   337  O O   . TYR A 1 52  ? 12.386  -7.537  52.040  1.00 33.33 ? 52   TYR A O   1 
ATOM   338  C CB  . TYR A 1 52  ? 11.633  -6.008  49.232  1.00 33.40 ? 52   TYR A CB  1 
ATOM   339  C CG  . TYR A 1 52  ? 10.709  -5.504  50.312  1.00 32.68 ? 52   TYR A CG  1 
ATOM   340  C CD1 . TYR A 1 52  ? 11.151  -4.573  51.281  1.00 31.03 ? 52   TYR A CD1 1 
ATOM   341  C CD2 . TYR A 1 52  ? 9.401   -5.952  50.377  1.00 32.21 ? 52   TYR A CD2 1 
ATOM   342  C CE1 . TYR A 1 52  ? 10.299  -4.095  52.260  1.00 29.15 ? 52   TYR A CE1 1 
ATOM   343  C CE2 . TYR A 1 52  ? 8.543   -5.485  51.366  1.00 31.91 ? 52   TYR A CE2 1 
ATOM   344  C CZ  . TYR A 1 52  ? 8.995   -4.558  52.288  1.00 30.22 ? 52   TYR A CZ  1 
ATOM   345  O OH  . TYR A 1 52  ? 8.108   -4.124  53.228  1.00 31.15 ? 52   TYR A OH  1 
ATOM   346  N N   . HIS A 1 53  ? 14.114  -6.446  51.094  1.00 33.36 ? 53   HIS A N   1 
ATOM   347  C CA  . HIS A 1 53  ? 14.942  -6.439  52.276  1.00 33.18 ? 53   HIS A CA  1 
ATOM   348  C C   . HIS A 1 53  ? 14.898  -5.130  53.012  1.00 33.27 ? 53   HIS A C   1 
ATOM   349  O O   . HIS A 1 53  ? 15.342  -4.105  52.521  1.00 33.17 ? 53   HIS A O   1 
ATOM   350  C CB  . HIS A 1 53  ? 16.377  -6.759  51.910  1.00 33.20 ? 53   HIS A CB  1 
ATOM   351  C CG  . HIS A 1 53  ? 16.719  -8.201  52.055  1.00 34.95 ? 53   HIS A CG  1 
ATOM   352  N ND1 . HIS A 1 53  ? 16.201  -9.172  51.227  1.00 35.78 ? 53   HIS A ND1 1 
ATOM   353  C CD2 . HIS A 1 53  ? 17.523  -8.844  52.940  1.00 37.87 ? 53   HIS A CD2 1 
ATOM   354  C CE1 . HIS A 1 53  ? 16.673  -10.351 51.595  1.00 38.31 ? 53   HIS A CE1 1 
ATOM   355  N NE2 . HIS A 1 53  ? 17.478  -10.180 52.633  1.00 38.13 ? 53   HIS A NE2 1 
ATOM   356  N N   . GLY A 1 54  ? 14.382  -5.187  54.228  1.00 33.79 ? 54   GLY A N   1 
ATOM   357  C CA  . GLY A 1 54  ? 14.306  -4.025  55.092  1.00 33.81 ? 54   GLY A CA  1 
ATOM   358  C C   . GLY A 1 54  ? 13.123  -3.188  54.699  1.00 33.86 ? 54   GLY A C   1 
ATOM   359  O O   . GLY A 1 54  ? 11.974  -3.569  54.921  1.00 34.07 ? 54   GLY A O   1 
ATOM   360  N N   . ASN A 1 55  ? 13.411  -2.050  54.094  1.00 33.71 ? 55   ASN A N   1 
ATOM   361  C CA  . ASN A 1 55  ? 12.373  -1.129  53.707  1.00 33.86 ? 55   ASN A CA  1 
ATOM   362  C C   . ASN A 1 55  ? 12.064  -1.165  52.202  1.00 34.13 ? 55   ASN A C   1 
ATOM   363  O O   . ASN A 1 55  ? 10.939  -0.869  51.768  1.00 34.17 ? 55   ASN A O   1 
ATOM   364  C CB  . ASN A 1 55  ? 12.775  0.263   54.144  1.00 33.72 ? 55   ASN A CB  1 
ATOM   365  C CG  . ASN A 1 55  ? 12.852  1.203   53.000  1.00 34.09 ? 55   ASN A CG  1 
ATOM   366  O OD1 . ASN A 1 55  ? 11.830  1.679   52.501  1.00 34.79 ? 55   ASN A OD1 1 
ATOM   367  N ND2 . ASN A 1 55  ? 14.066  1.453   52.533  1.00 34.27 ? 55   ASN A ND2 1 
ATOM   368  N N   . GLY A 1 56  ? 13.074  -1.500  51.407  1.00 34.12 ? 56   GLY A N   1 
ATOM   369  C CA  . GLY A 1 56  ? 12.885  -1.621  49.990  1.00 33.82 ? 56   GLY A CA  1 
ATOM   370  C C   . GLY A 1 56  ? 13.792  -0.759  49.162  1.00 34.10 ? 56   GLY A C   1 
ATOM   371  O O   . GLY A 1 56  ? 14.002  -1.068  47.996  1.00 34.93 ? 56   GLY A O   1 
ATOM   372  N N   . ASP A 1 57  ? 14.332  0.321   49.732  1.00 33.84 ? 57   ASP A N   1 
ATOM   373  C CA  . ASP A 1 57  ? 15.168  1.272   48.968  1.00 33.40 ? 57   ASP A CA  1 
ATOM   374  C C   . ASP A 1 57  ? 16.056  0.543   47.939  1.00 32.76 ? 57   ASP A C   1 
ATOM   375  O O   . ASP A 1 57  ? 16.369  1.076   46.876  1.00 33.21 ? 57   ASP A O   1 
ATOM   376  C CB  . ASP A 1 57  ? 16.027  2.141   49.914  1.00 33.60 ? 57   ASP A CB  1 
ATOM   377  C CG  . ASP A 1 57  ? 15.811  3.672   49.710  1.00 35.03 ? 57   ASP A CG  1 
ATOM   378  O OD1 . ASP A 1 57  ? 16.706  4.472   50.091  1.00 36.25 ? 57   ASP A OD1 1 
ATOM   379  O OD2 . ASP A 1 57  ? 14.747  4.094   49.191  1.00 36.14 ? 57   ASP A OD2 1 
ATOM   380  N N   . SER A 1 58  ? 16.419  -0.696  48.250  1.00 31.72 ? 58   SER A N   1 
ATOM   381  C CA  . SER A 1 58  ? 17.259  -1.506  47.393  1.00 30.69 ? 58   SER A CA  1 
ATOM   382  C C   . SER A 1 58  ? 16.504  -2.374  46.360  1.00 30.12 ? 58   SER A C   1 
ATOM   383  O O   . SER A 1 58  ? 17.093  -2.794  45.351  1.00 29.84 ? 58   SER A O   1 
ATOM   384  C CB  . SER A 1 58  ? 18.099  -2.403  48.276  1.00 30.75 ? 58   SER A CB  1 
ATOM   385  O OG  . SER A 1 58  ? 19.075  -3.078  47.521  1.00 31.04 ? 58   SER A OG  1 
ATOM   386  N N   . TYR A 1 59  ? 15.221  -2.644  46.614  1.00 29.19 ? 59   TYR A N   1 
ATOM   387  C CA  . TYR A 1 59  ? 14.437  -3.599  45.826  1.00 28.45 ? 59   TYR A CA  1 
ATOM   388  C C   . TYR A 1 59  ? 14.393  -3.292  44.345  1.00 28.72 ? 59   TYR A C   1 
ATOM   389  O O   . TYR A 1 59  ? 13.938  -2.214  43.935  1.00 29.42 ? 59   TYR A O   1 
ATOM   390  C CB  . TYR A 1 59  ? 13.019  -3.676  46.335  1.00 27.90 ? 59   TYR A CB  1 
ATOM   391  C CG  . TYR A 1 59  ? 12.101  -4.551  45.510  1.00 27.58 ? 59   TYR A CG  1 
ATOM   392  C CD1 . TYR A 1 59  ? 12.174  -5.921  45.577  1.00 28.42 ? 59   TYR A CD1 1 
ATOM   393  C CD2 . TYR A 1 59  ? 11.129  -4.006  44.700  1.00 27.43 ? 59   TYR A CD2 1 
ATOM   394  C CE1 . TYR A 1 59  ? 11.302  -6.725  44.859  1.00 28.48 ? 59   TYR A CE1 1 
ATOM   395  C CE2 . TYR A 1 59  ? 10.261  -4.800  43.979  1.00 27.20 ? 59   TYR A CE2 1 
ATOM   396  C CZ  . TYR A 1 59  ? 10.349  -6.160  44.061  1.00 27.78 ? 59   TYR A CZ  1 
ATOM   397  O OH  . TYR A 1 59  ? 9.500   -6.975  43.331  1.00 28.19 ? 59   TYR A OH  1 
ATOM   398  N N   . ARG A 1 60  ? 14.855  -4.245  43.543  1.00 28.09 ? 60   ARG A N   1 
ATOM   399  C CA  . ARG A 1 60  ? 14.857  -4.073  42.110  1.00 27.34 ? 60   ARG A CA  1 
ATOM   400  C C   . ARG A 1 60  ? 14.053  -5.187  41.436  1.00 27.70 ? 60   ARG A C   1 
ATOM   401  O O   . ARG A 1 60  ? 14.243  -5.518  40.263  1.00 28.15 ? 60   ARG A O   1 
ATOM   402  C CB  . ARG A 1 60  ? 16.288  -3.972  41.596  1.00 26.66 ? 60   ARG A CB  1 
ATOM   403  C CG  . ARG A 1 60  ? 17.008  -2.730  42.099  1.00 26.23 ? 60   ARG A CG  1 
ATOM   404  C CD  . ARG A 1 60  ? 16.232  -1.435  41.813  1.00 24.99 ? 60   ARG A CD  1 
ATOM   405  N NE  . ARG A 1 60  ? 16.370  -0.443  42.890  1.00 23.50 ? 60   ARG A NE  1 
ATOM   406  C CZ  . ARG A 1 60  ? 17.299  0.511   42.933  1.00 21.73 ? 60   ARG A CZ  1 
ATOM   407  N NH1 . ARG A 1 60  ? 18.201  0.636   41.957  1.00 21.27 ? 60   ARG A NH1 1 
ATOM   408  N NH2 . ARG A 1 60  ? 17.316  1.347   43.953  1.00 19.48 ? 60   ARG A NH2 1 
ATOM   409  N N   . GLY A 1 61  ? 13.117  -5.762  42.175  1.00 27.45 ? 61   GLY A N   1 
ATOM   410  C CA  . GLY A 1 61  ? 12.409  -6.910  41.649  1.00 26.98 ? 61   GLY A CA  1 
ATOM   411  C C   . GLY A 1 61  ? 11.290  -6.463  40.748  1.00 26.76 ? 61   GLY A C   1 
ATOM   412  O O   . GLY A 1 61  ? 11.334  -5.357  40.206  1.00 26.82 ? 61   GLY A O   1 
ATOM   413  N N   . LYS A 1 62  ? 10.274  -7.321  40.634  1.00 26.30 ? 62   LYS A N   1 
ATOM   414  C CA  . LYS A 1 62  ? 9.271   -7.226  39.598  1.00 25.64 ? 62   LYS A CA  1 
ATOM   415  C C   . LYS A 1 62  ? 7.850   -7.345  40.093  1.00 26.13 ? 62   LYS A C   1 
ATOM   416  O O   . LYS A 1 62  ? 6.966   -7.793  39.343  1.00 26.15 ? 62   LYS A O   1 
ATOM   417  C CB  . LYS A 1 62  ? 9.515   -8.277  38.541  1.00 24.80 ? 62   LYS A CB  1 
ATOM   418  C CG  . LYS A 1 62  ? 10.912  -8.241  38.021  1.00 24.40 ? 62   LYS A CG  1 
ATOM   419  C CD  . LYS A 1 62  ? 10.994  -8.634  36.542  1.00 24.67 ? 62   LYS A CD  1 
ATOM   420  C CE  . LYS A 1 62  ? 10.789  -10.099 36.297  1.00 22.42 ? 62   LYS A CE  1 
ATOM   421  N NZ  . LYS A 1 62  ? 10.656  -10.276 34.870  1.00 23.45 ? 62   LYS A NZ  1 
ATOM   422  N N   . ALA A 1 63  ? 7.605   -6.937  41.333  1.00 26.36 ? 63   ALA A N   1 
ATOM   423  C CA  . ALA A 1 63  ? 6.222   -6.796  41.760  1.00 27.12 ? 63   ALA A CA  1 
ATOM   424  C C   . ALA A 1 63  ? 5.610   -5.719  40.900  1.00 27.83 ? 63   ALA A C   1 
ATOM   425  O O   . ALA A 1 63  ? 6.240   -4.693  40.655  1.00 28.51 ? 63   ALA A O   1 
ATOM   426  C CB  . ALA A 1 63  ? 6.145   -6.400  43.182  1.00 27.10 ? 63   ALA A CB  1 
ATOM   427  N N   . ASN A 1 64  ? 4.403   -5.935  40.405  1.00 28.31 ? 64   ASN A N   1 
ATOM   428  C CA  . ASN A 1 64  ? 3.757   -4.864  39.667  1.00 28.55 ? 64   ASN A CA  1 
ATOM   429  C C   . ASN A 1 64  ? 2.331   -4.608  40.102  1.00 28.78 ? 64   ASN A C   1 
ATOM   430  O O   . ASN A 1 64  ? 1.702   -3.713  39.597  1.00 29.48 ? 64   ASN A O   1 
ATOM   431  C CB  . ASN A 1 64  ? 3.822   -5.116  38.174  1.00 28.29 ? 64   ASN A CB  1 
ATOM   432  C CG  . ASN A 1 64  ? 3.269   -6.456  37.808  1.00 29.55 ? 64   ASN A CG  1 
ATOM   433  O OD1 . ASN A 1 64  ? 4.000   -7.344  37.393  1.00 31.05 ? 64   ASN A OD1 1 
ATOM   434  N ND2 . ASN A 1 64  ? 1.974   -6.636  38.002  1.00 31.84 ? 64   ASN A ND2 1 
ATOM   435  N N   . THR A 1 65  ? 1.784   -5.369  41.029  1.00 29.04 ? 65   THR A N   1 
ATOM   436  C CA  . THR A 1 65  ? 0.429   -5.019  41.423  1.00 29.33 ? 65   THR A CA  1 
ATOM   437  C C   . THR A 1 65  ? 0.366   -4.333  42.783  1.00 29.31 ? 65   THR A C   1 
ATOM   438  O O   . THR A 1 65  ? 1.390   -4.009  43.387  1.00 28.82 ? 65   THR A O   1 
ATOM   439  C CB  . THR A 1 65  ? -0.593  -6.184  41.251  1.00 29.44 ? 65   THR A CB  1 
ATOM   440  O OG1 . THR A 1 65  ? -0.208  -7.304  42.039  1.00 29.22 ? 65   THR A OG1 1 
ATOM   441  C CG2 . THR A 1 65  ? -0.666  -6.623  39.787  1.00 30.03 ? 65   THR A CG2 1 
ATOM   442  N N   . ASP A 1 66  ? -0.851  -4.080  43.234  1.00 29.36 ? 66   ASP A N   1 
ATOM   443  C CA  . ASP A 1 66  ? -1.042  -3.381  44.475  1.00 29.70 ? 66   ASP A CA  1 
ATOM   444  C C   . ASP A 1 66  ? -1.952  -4.184  45.388  1.00 29.64 ? 66   ASP A C   1 
ATOM   445  O O   . ASP A 1 66  ? -2.658  -5.103  44.963  1.00 29.72 ? 66   ASP A O   1 
ATOM   446  C CB  . ASP A 1 66  ? -1.585  -1.962  44.240  1.00 29.82 ? 66   ASP A CB  1 
ATOM   447  C CG  . ASP A 1 66  ? -3.103  -1.926  43.927  1.00 32.05 ? 66   ASP A CG  1 
ATOM   448  O OD1 . ASP A 1 66  ? -3.721  -2.992  43.674  1.00 34.68 ? 66   ASP A OD1 1 
ATOM   449  O OD2 . ASP A 1 66  ? -3.690  -0.812  43.924  1.00 33.74 ? 66   ASP A OD2 1 
ATOM   450  N N   . THR A 1 67  ? -1.933  -3.797  46.649  1.00 29.48 ? 67   THR A N   1 
ATOM   451  C CA  . THR A 1 67  ? -2.559  -4.509  47.724  1.00 29.36 ? 67   THR A CA  1 
ATOM   452  C C   . THR A 1 67  ? -4.094  -4.556  47.634  1.00 29.84 ? 67   THR A C   1 
ATOM   453  O O   . THR A 1 67  ? -4.766  -4.984  48.592  1.00 30.23 ? 67   THR A O   1 
ATOM   454  C CB  . THR A 1 67  ? -2.092  -3.880  49.027  1.00 29.29 ? 67   THR A CB  1 
ATOM   455  O OG1 . THR A 1 67  ? -1.964  -2.472  48.819  1.00 28.85 ? 67   THR A OG1 1 
ATOM   456  C CG2 . THR A 1 67  ? -0.716  -4.421  49.418  1.00 29.04 ? 67   THR A CG2 1 
ATOM   457  N N   . LYS A 1 68  ? -4.650  -4.129  46.494  1.00 29.92 ? 68   LYS A N   1 
ATOM   458  C CA  . LYS A 1 68  ? -6.087  -4.340  46.194  1.00 29.66 ? 68   LYS A CA  1 
ATOM   459  C C   . LYS A 1 68  ? -6.319  -5.127  44.894  1.00 29.53 ? 68   LYS A C   1 
ATOM   460  O O   . LYS A 1 68  ? -7.429  -5.602  44.642  1.00 29.55 ? 68   LYS A O   1 
ATOM   461  C CB  . LYS A 1 68  ? -6.876  -3.021  46.212  1.00 29.42 ? 68   LYS A CB  1 
ATOM   462  C CG  . LYS A 1 68  ? -7.261  -2.568  47.605  1.00 29.06 ? 68   LYS A CG  1 
ATOM   463  C CD  . LYS A 1 68  ? -7.689  -1.114  47.629  1.00 29.21 ? 68   LYS A CD  1 
ATOM   464  C CE  . LYS A 1 68  ? -8.015  -0.679  49.051  1.00 29.35 ? 68   LYS A CE  1 
ATOM   465  N NZ  . LYS A 1 68  ? -9.075  0.368   49.096  1.00 29.17 ? 68   LYS A NZ  1 
ATOM   466  N N   . GLY A 1 69  ? -5.263  -5.276  44.097  1.00 29.30 ? 69   GLY A N   1 
ATOM   467  C CA  . GLY A 1 69  ? -5.330  -5.989  42.828  1.00 29.69 ? 69   GLY A CA  1 
ATOM   468  C C   . GLY A 1 69  ? -4.705  -5.206  41.681  1.00 29.93 ? 69   GLY A C   1 
ATOM   469  O O   . GLY A 1 69  ? -3.822  -5.707  40.966  1.00 30.11 ? 69   GLY A O   1 
ATOM   470  N N   . ARG A 1 70  ? -5.172  -3.968  41.523  1.00 29.78 ? 70   ARG A N   1 
ATOM   471  C CA  . ARG A 1 70  ? -4.781  -3.034  40.442  1.00 29.18 ? 70   ARG A CA  1 
ATOM   472  C C   . ARG A 1 70  ? -3.326  -3.127  39.966  1.00 28.43 ? 70   ARG A C   1 
ATOM   473  O O   . ARG A 1 70  ? -2.429  -3.394  40.745  1.00 27.92 ? 70   ARG A O   1 
ATOM   474  C CB  . ARG A 1 70  ? -5.157  -1.598  40.850  1.00 29.23 ? 70   ARG A CB  1 
ATOM   475  C CG  . ARG A 1 70  ? -6.536  -1.539  41.555  1.00 30.04 ? 70   ARG A CG  1 
ATOM   476  C CD  . ARG A 1 70  ? -6.975  -0.130  41.930  1.00 31.68 ? 70   ARG A CD  1 
ATOM   477  N NE  . ARG A 1 70  ? -6.385  0.356   43.180  1.00 32.52 ? 70   ARG A NE  1 
ATOM   478  C CZ  . ARG A 1 70  ? -7.077  0.756   44.246  1.00 33.16 ? 70   ARG A CZ  1 
ATOM   479  N NH1 . ARG A 1 70  ? -8.412  0.745   44.253  1.00 33.14 ? 70   ARG A NH1 1 
ATOM   480  N NH2 . ARG A 1 70  ? -6.423  1.175   45.316  1.00 33.25 ? 70   ARG A NH2 1 
ATOM   481  N N   . PRO A 1 71  ? -3.098  -2.930  38.664  1.00 28.44 ? 71   PRO A N   1 
ATOM   482  C CA  . PRO A 1 71  ? -1.710  -2.956  38.191  1.00 28.34 ? 71   PRO A CA  1 
ATOM   483  C C   . PRO A 1 71  ? -1.040  -1.594  38.287  1.00 28.06 ? 71   PRO A C   1 
ATOM   484  O O   . PRO A 1 71  ? -1.704  -0.587  38.240  1.00 27.64 ? 71   PRO A O   1 
ATOM   485  C CB  . PRO A 1 71  ? -1.837  -3.405  36.722  1.00 28.21 ? 71   PRO A CB  1 
ATOM   486  C CG  . PRO A 1 71  ? -3.376  -3.535  36.438  1.00 28.17 ? 71   PRO A CG  1 
ATOM   487  C CD  . PRO A 1 71  ? -4.069  -2.826  37.555  1.00 28.38 ? 71   PRO A CD  1 
ATOM   488  N N   . CYS A 1 72  ? 0.275   -1.586  38.426  1.00 28.88 ? 72   CYS A N   1 
ATOM   489  C CA  . CYS A 1 72  ? 1.074   -0.361  38.511  1.00 30.10 ? 72   CYS A CA  1 
ATOM   490  C C   . CYS A 1 72  ? 1.133   0.295   37.173  1.00 29.95 ? 72   CYS A C   1 
ATOM   491  O O   . CYS A 1 72  ? 1.009   -0.380  36.156  1.00 30.24 ? 72   CYS A O   1 
ATOM   492  C CB  . CYS A 1 72  ? 2.540   -0.651  38.892  1.00 30.65 ? 72   CYS A CB  1 
ATOM   493  S SG  . CYS A 1 72  ? 2.874   -1.237  40.578  1.00 33.37 ? 72   CYS A SG  1 
ATOM   494  N N   . LEU A 1 73  ? 1.363   1.603   37.166  1.00 29.92 ? 73   LEU A N   1 
ATOM   495  C CA  . LEU A 1 73  ? 1.524   2.304   35.916  1.00 30.06 ? 73   LEU A CA  1 
ATOM   496  C C   . LEU A 1 73  ? 3.001   2.365   35.604  1.00 30.67 ? 73   LEU A C   1 
ATOM   497  O O   . LEU A 1 73  ? 3.827   2.394   36.509  1.00 31.06 ? 73   LEU A O   1 
ATOM   498  C CB  . LEU A 1 73  ? 0.862   3.686   35.948  1.00 29.59 ? 73   LEU A CB  1 
ATOM   499  C CG  . LEU A 1 73  ? -0.662  3.641   36.135  1.00 28.34 ? 73   LEU A CG  1 
ATOM   500  C CD1 . LEU A 1 73  ? -1.235  5.029   36.179  1.00 27.34 ? 73   LEU A CD1 1 
ATOM   501  C CD2 . LEU A 1 73  ? -1.362  2.808   35.081  1.00 26.10 ? 73   LEU A CD2 1 
ATOM   502  N N   . ALA A 1 74  ? 3.330   2.358   34.318  1.00 31.23 ? 74   ALA A N   1 
ATOM   503  C CA  . ALA A 1 74  ? 4.713   2.355   33.888  1.00 31.71 ? 74   ALA A CA  1 
ATOM   504  C C   . ALA A 1 74  ? 5.378   3.656   34.274  1.00 32.05 ? 74   ALA A C   1 
ATOM   505  O O   . ALA A 1 74  ? 4.799   4.723   34.083  1.00 32.02 ? 74   ALA A O   1 
ATOM   506  C CB  . ALA A 1 74  ? 4.782   2.162   32.394  1.00 31.95 ? 74   ALA A CB  1 
ATOM   507  N N   . TRP A 1 75  ? 6.588   3.572   34.818  1.00 32.47 ? 75   TRP A N   1 
ATOM   508  C CA  . TRP A 1 75  ? 7.389   4.772   35.055  1.00 33.04 ? 75   TRP A CA  1 
ATOM   509  C C   . TRP A 1 75  ? 7.583   5.560   33.759  1.00 33.15 ? 75   TRP A C   1 
ATOM   510  O O   . TRP A 1 75  ? 7.930   6.721   33.798  1.00 32.94 ? 75   TRP A O   1 
ATOM   511  C CB  . TRP A 1 75  ? 8.731   4.429   35.707  1.00 33.04 ? 75   TRP A CB  1 
ATOM   512  C CG  . TRP A 1 75  ? 8.583   3.546   36.915  1.00 33.76 ? 75   TRP A CG  1 
ATOM   513  C CD1 . TRP A 1 75  ? 8.854   2.222   36.983  1.00 35.43 ? 75   TRP A CD1 1 
ATOM   514  C CD2 . TRP A 1 75  ? 8.101   3.915   38.215  1.00 34.12 ? 75   TRP A CD2 1 
ATOM   515  N NE1 . TRP A 1 75  ? 8.575   1.729   38.240  1.00 33.74 ? 75   TRP A NE1 1 
ATOM   516  C CE2 . TRP A 1 75  ? 8.130   2.762   39.019  1.00 34.26 ? 75   TRP A CE2 1 
ATOM   517  C CE3 . TRP A 1 75  ? 7.673   5.113   38.788  1.00 34.68 ? 75   TRP A CE3 1 
ATOM   518  C CZ2 . TRP A 1 75  ? 7.742   2.776   40.368  1.00 34.42 ? 75   TRP A CZ2 1 
ATOM   519  C CZ3 . TRP A 1 75  ? 7.292   5.120   40.140  1.00 33.64 ? 75   TRP A CZ3 1 
ATOM   520  C CH2 . TRP A 1 75  ? 7.326   3.962   40.903  1.00 32.90 ? 75   TRP A CH2 1 
ATOM   521  N N   . ASN A 1 76  ? 7.347   4.901   32.625  1.00 33.89 ? 76   ASN A N   1 
ATOM   522  C CA  . ASN A 1 76  ? 7.231   5.514   31.302  1.00 34.47 ? 76   ASN A CA  1 
ATOM   523  C C   . ASN A 1 76  ? 6.070   6.425   31.160  1.00 34.24 ? 76   ASN A C   1 
ATOM   524  O O   . ASN A 1 76  ? 6.240   7.557   30.773  1.00 34.43 ? 76   ASN A O   1 
ATOM   525  C CB  . ASN A 1 76  ? 6.916   4.444   30.293  1.00 35.17 ? 76   ASN A CB  1 
ATOM   526  C CG  . ASN A 1 76  ? 8.096   4.017   29.529  1.00 38.37 ? 76   ASN A CG  1 
ATOM   527  O OD1 . ASN A 1 76  ? 8.025   3.023   28.787  1.00 41.45 ? 76   ASN A OD1 1 
ATOM   528  N ND2 . ASN A 1 76  ? 9.213   4.751   29.682  1.00 39.99 ? 76   ASN A ND2 1 
ATOM   529  N N   . ALA A 1 77  ? 4.883   5.882   31.437  1.00 34.28 ? 77   ALA A N   1 
ATOM   530  C CA  . ALA A 1 77  ? 3.577   6.480   31.132  1.00 34.39 ? 77   ALA A CA  1 
ATOM   531  C C   . ALA A 1 77  ? 3.559   7.968   30.923  1.00 34.88 ? 77   ALA A C   1 
ATOM   532  O O   . ALA A 1 77  ? 4.159   8.728   31.703  1.00 35.07 ? 77   ALA A O   1 
ATOM   533  C CB  . ALA A 1 77  ? 2.570   6.136   32.190  1.00 34.37 ? 77   ALA A CB  1 
ATOM   534  N N   . PRO A 1 78  ? 2.834   8.401   29.880  1.00 35.17 ? 78   PRO A N   1 
ATOM   535  C CA  . PRO A 1 78  ? 2.599   9.828   29.707  1.00 35.21 ? 78   PRO A CA  1 
ATOM   536  C C   . PRO A 1 78  ? 1.933   10.377  30.981  1.00 35.24 ? 78   PRO A C   1 
ATOM   537  O O   . PRO A 1 78  ? 2.288   11.462  31.459  1.00 35.02 ? 78   PRO A O   1 
ATOM   538  C CB  . PRO A 1 78  ? 1.650   9.878   28.503  1.00 35.30 ? 78   PRO A CB  1 
ATOM   539  C CG  . PRO A 1 78  ? 1.807   8.552   27.819  1.00 35.07 ? 78   PRO A CG  1 
ATOM   540  C CD  . PRO A 1 78  ? 2.089   7.587   28.902  1.00 34.97 ? 78   PRO A CD  1 
ATOM   541  N N   . ALA A 1 79  ? 1.001   9.592   31.532  1.00 35.33 ? 79   ALA A N   1 
ATOM   542  C CA  . ALA A 1 79  ? 0.369   9.869   32.821  1.00 35.28 ? 79   ALA A CA  1 
ATOM   543  C C   . ALA A 1 79  ? 1.423   10.194  33.889  1.00 35.26 ? 79   ALA A C   1 
ATOM   544  O O   . ALA A 1 79  ? 1.536   11.334  34.342  1.00 35.08 ? 79   ALA A O   1 
ATOM   545  C CB  . ALA A 1 79  ? -0.479  8.679   33.238  1.00 34.84 ? 79   ALA A CB  1 
ATOM   546  N N   . VAL A 1 80  ? 2.222   9.185   34.228  1.00 35.35 ? 80   VAL A N   1 
ATOM   547  C CA  . VAL A 1 80  ? 3.263   9.250   35.263  1.00 35.29 ? 80   VAL A CA  1 
ATOM   548  C C   . VAL A 1 80  ? 4.338   10.331  35.044  1.00 35.35 ? 80   VAL A C   1 
ATOM   549  O O   . VAL A 1 80  ? 4.937   10.829  36.008  1.00 35.61 ? 80   VAL A O   1 
ATOM   550  C CB  . VAL A 1 80  ? 3.948   7.857   35.421  1.00 35.33 ? 80   VAL A CB  1 
ATOM   551  C CG1 . VAL A 1 80  ? 5.073   7.884   36.466  1.00 34.89 ? 80   VAL A CG1 1 
ATOM   552  C CG2 . VAL A 1 80  ? 2.911   6.787   35.766  1.00 35.55 ? 80   VAL A CG2 1 
ATOM   553  N N   . LEU A 1 81  ? 4.594   10.698  33.794  1.00 35.00 ? 81   LEU A N   1 
ATOM   554  C CA  . LEU A 1 81  ? 5.628   11.697  33.540  1.00 34.64 ? 81   LEU A CA  1 
ATOM   555  C C   . LEU A 1 81  ? 5.344   13.086  34.142  1.00 34.23 ? 81   LEU A C   1 
ATOM   556  O O   . LEU A 1 81  ? 6.235   13.934  34.172  1.00 33.77 ? 81   LEU A O   1 
ATOM   557  C CB  . LEU A 1 81  ? 5.995   11.766  32.054  1.00 34.79 ? 81   LEU A CB  1 
ATOM   558  C CG  . LEU A 1 81  ? 7.237   10.944  31.692  1.00 34.53 ? 81   LEU A CG  1 
ATOM   559  C CD1 . LEU A 1 81  ? 7.268   10.621  30.221  1.00 34.99 ? 81   LEU A CD1 1 
ATOM   560  C CD2 . LEU A 1 81  ? 8.492   11.684  32.082  1.00 34.04 ? 81   LEU A CD2 1 
ATOM   561  N N   . GLN A 1 82  ? 4.121   13.294  34.634  1.00 33.91 ? 82   GLN A N   1 
ATOM   562  C CA  . GLN A 1 82  ? 3.792   14.495  35.406  1.00 33.93 ? 82   GLN A CA  1 
ATOM   563  C C   . GLN A 1 82  ? 4.212   14.300  36.854  1.00 33.67 ? 82   GLN A C   1 
ATOM   564  O O   . GLN A 1 82  ? 4.653   15.246  37.517  1.00 33.64 ? 82   GLN A O   1 
ATOM   565  C CB  . GLN A 1 82  ? 2.291   14.820  35.378  1.00 34.11 ? 82   GLN A CB  1 
ATOM   566  C CG  . GLN A 1 82  ? 1.521   14.377  34.133  1.00 35.47 ? 82   GLN A CG  1 
ATOM   567  C CD  . GLN A 1 82  ? 2.019   15.020  32.849  1.00 36.64 ? 82   GLN A CD  1 
ATOM   568  O OE1 . GLN A 1 82  ? 1.885   16.233  32.645  1.00 36.79 ? 82   GLN A OE1 1 
ATOM   569  N NE2 . GLN A 1 82  ? 2.587   14.201  31.967  1.00 36.95 ? 82   GLN A NE2 1 
ATOM   570  N N   . LYS A 1 83  ? 4.048   13.073  37.351  1.00 33.22 ? 83   LYS A N   1 
ATOM   571  C CA  . LYS A 1 83  ? 4.402   12.751  38.735  1.00 32.82 ? 83   LYS A CA  1 
ATOM   572  C C   . LYS A 1 83  ? 5.915   12.914  38.955  1.00 32.89 ? 83   LYS A C   1 
ATOM   573  O O   . LYS A 1 83  ? 6.690   12.758  38.010  1.00 33.10 ? 83   LYS A O   1 
ATOM   574  C CB  . LYS A 1 83  ? 3.910   11.353  39.087  1.00 32.19 ? 83   LYS A CB  1 
ATOM   575  C CG  . LYS A 1 83  ? 2.428   11.199  38.902  1.00 31.29 ? 83   LYS A CG  1 
ATOM   576  C CD  . LYS A 1 83  ? 1.700   11.627  40.147  1.00 32.28 ? 83   LYS A CD  1 
ATOM   577  C CE  . LYS A 1 83  ? 0.210   11.767  39.914  1.00 32.49 ? 83   LYS A CE  1 
ATOM   578  N NZ  . LYS A 1 83  ? -0.471  12.191  41.172  1.00 32.24 ? 83   LYS A NZ  1 
ATOM   579  N N   . PRO A 1 84  ? 6.336   13.259  40.188  1.00 32.69 ? 84   PRO A N   1 
ATOM   580  C CA  . PRO A 1 84  ? 7.730   13.660  40.401  1.00 32.67 ? 84   PRO A CA  1 
ATOM   581  C C   . PRO A 1 84  ? 8.728   12.528  40.192  1.00 32.57 ? 84   PRO A C   1 
ATOM   582  O O   . PRO A 1 84  ? 9.834   12.732  39.670  1.00 32.44 ? 84   PRO A O   1 
ATOM   583  C CB  . PRO A 1 84  ? 7.742   14.125  41.860  1.00 32.64 ? 84   PRO A CB  1 
ATOM   584  C CG  . PRO A 1 84  ? 6.316   14.435  42.167  1.00 33.01 ? 84   PRO A CG  1 
ATOM   585  C CD  . PRO A 1 84  ? 5.546   13.399  41.419  1.00 32.62 ? 84   PRO A CD  1 
ATOM   586  N N   . TYR A 1 85  ? 8.328   11.334  40.592  1.00 32.63 ? 85   TYR A N   1 
ATOM   587  C CA  . TYR A 1 85  ? 9.194   10.181  40.474  1.00 32.31 ? 85   TYR A CA  1 
ATOM   588  C C   . TYR A 1 85  ? 8.755   9.422   39.265  1.00 32.17 ? 85   TYR A C   1 
ATOM   589  O O   . TYR A 1 85  ? 7.689   8.798   39.268  1.00 31.81 ? 85   TYR A O   1 
ATOM   590  C CB  . TYR A 1 85  ? 9.105   9.334   41.741  1.00 32.38 ? 85   TYR A CB  1 
ATOM   591  C CG  . TYR A 1 85  ? 9.639   10.059  42.971  1.00 31.68 ? 85   TYR A CG  1 
ATOM   592  C CD1 . TYR A 1 85  ? 11.012  10.215  43.164  1.00 30.77 ? 85   TYR A CD1 1 
ATOM   593  C CD2 . TYR A 1 85  ? 8.779   10.597  43.919  1.00 30.30 ? 85   TYR A CD2 1 
ATOM   594  C CE1 . TYR A 1 85  ? 11.513  10.869  44.267  1.00 31.10 ? 85   TYR A CE1 1 
ATOM   595  C CE2 . TYR A 1 85  ? 9.278   11.255  45.035  1.00 31.32 ? 85   TYR A CE2 1 
ATOM   596  C CZ  . TYR A 1 85  ? 10.651  11.382  45.203  1.00 31.47 ? 85   TYR A CZ  1 
ATOM   597  O OH  . TYR A 1 85  ? 11.175  12.033  46.300  1.00 32.63 ? 85   TYR A OH  1 
ATOM   598  N N   . ASN A 1 86  ? 9.562   9.535   38.212  1.00 32.26 ? 86   ASN A N   1 
ATOM   599  C CA  . ASN A 1 86  ? 9.276   8.885   36.926  1.00 32.07 ? 86   ASN A CA  1 
ATOM   600  C C   . ASN A 1 86  ? 10.530  8.638   36.088  1.00 31.91 ? 86   ASN A C   1 
ATOM   601  O O   . ASN A 1 86  ? 11.592  9.154   36.390  1.00 31.96 ? 86   ASN A O   1 
ATOM   602  C CB  . ASN A 1 86  ? 8.207   9.662   36.143  1.00 32.01 ? 86   ASN A CB  1 
ATOM   603  C CG  . ASN A 1 86  ? 8.701   10.995  35.612  1.00 31.71 ? 86   ASN A CG  1 
ATOM   604  O OD1 . ASN A 1 86  ? 7.907   11.921  35.447  1.00 31.60 ? 86   ASN A OD1 1 
ATOM   605  N ND2 . ASN A 1 86  ? 10.003  11.097  35.318  1.00 30.61 ? 86   ASN A ND2 1 
ATOM   606  N N   . ALA A 1 87  ? 10.396  7.871   35.023  1.00 32.02 ? 87   ALA A N   1 
ATOM   607  C CA  . ALA A 1 87  ? 11.562  7.350   34.323  1.00 32.48 ? 87   ALA A CA  1 
ATOM   608  C C   . ALA A 1 87  ? 12.452  8.375   33.626  1.00 32.70 ? 87   ALA A C   1 
ATOM   609  O O   . ALA A 1 87  ? 13.582  8.059   33.243  1.00 32.91 ? 87   ALA A O   1 
ATOM   610  C CB  . ALA A 1 87  ? 11.151  6.253   33.352  1.00 32.72 ? 87   ALA A CB  1 
ATOM   611  N N   . HIS A 1 88  ? 11.968  9.591   33.441  1.00 33.04 ? 88   HIS A N   1 
ATOM   612  C CA  . HIS A 1 88  ? 12.812  10.569  32.771  1.00 33.58 ? 88   HIS A CA  1 
ATOM   613  C C   . HIS A 1 88  ? 13.747  11.277  33.740  1.00 33.82 ? 88   HIS A C   1 
ATOM   614  O O   . HIS A 1 88  ? 14.741  11.849  33.312  1.00 33.97 ? 88   HIS A O   1 
ATOM   615  C CB  . HIS A 1 88  ? 11.985  11.544  31.935  1.00 33.68 ? 88   HIS A CB  1 
ATOM   616  C CG  . HIS A 1 88  ? 11.556  10.988  30.610  1.00 34.05 ? 88   HIS A CG  1 
ATOM   617  N ND1 . HIS A 1 88  ? 10.890  11.742  29.668  1.00 34.48 ? 88   HIS A ND1 1 
ATOM   618  C CD2 . HIS A 1 88  ? 11.716  9.760   30.061  1.00 34.34 ? 88   HIS A CD2 1 
ATOM   619  C CE1 . HIS A 1 88  ? 10.643  10.998  28.604  1.00 34.16 ? 88   HIS A CE1 1 
ATOM   620  N NE2 . HIS A 1 88  ? 11.139  9.792   28.816  1.00 33.81 ? 88   HIS A NE2 1 
ATOM   621  N N   . ARG A 1 89  ? 13.437  11.221  35.037  1.00 34.19 ? 89   ARG A N   1 
ATOM   622  C CA  . ARG A 1 89  ? 14.314  11.743  36.085  1.00 34.61 ? 89   ARG A CA  1 
ATOM   623  C C   . ARG A 1 89  ? 15.749  11.595  35.653  1.00 34.93 ? 89   ARG A C   1 
ATOM   624  O O   . ARG A 1 89  ? 16.133  10.552  35.119  1.00 34.61 ? 89   ARG A O   1 
ATOM   625  C CB  . ARG A 1 89  ? 14.147  10.965  37.397  1.00 34.72 ? 89   ARG A CB  1 
ATOM   626  C CG  . ARG A 1 89  ? 12.975  11.361  38.274  1.00 35.69 ? 89   ARG A CG  1 
ATOM   627  C CD  . ARG A 1 89  ? 13.185  12.738  38.887  1.00 38.40 ? 89   ARG A CD  1 
ATOM   628  N NE  . ARG A 1 89  ? 14.144  12.706  39.988  1.00 39.24 ? 89   ARG A NE  1 
ATOM   629  C CZ  . ARG A 1 89  ? 13.812  12.562  41.267  1.00 38.78 ? 89   ARG A CZ  1 
ATOM   630  N NH1 . ARG A 1 89  ? 12.539  12.443  41.615  1.00 38.79 ? 89   ARG A NH1 1 
ATOM   631  N NH2 . ARG A 1 89  ? 14.757  12.540  42.194  1.00 38.69 ? 89   ARG A NH2 1 
ATOM   632  N N   . PRO A 1 90  ? 16.555  12.635  35.880  1.00 35.51 ? 90   PRO A N   1 
ATOM   633  C CA  . PRO A 1 90  ? 17.983  12.551  35.574  1.00 36.10 ? 90   PRO A CA  1 
ATOM   634  C C   . PRO A 1 90  ? 18.684  11.481  36.405  1.00 36.77 ? 90   PRO A C   1 
ATOM   635  O O   . PRO A 1 90  ? 19.733  10.985  36.008  1.00 37.06 ? 90   PRO A O   1 
ATOM   636  C CB  . PRO A 1 90  ? 18.508  13.942  35.942  1.00 35.91 ? 90   PRO A CB  1 
ATOM   637  C CG  . PRO A 1 90  ? 17.320  14.833  35.862  1.00 35.67 ? 90   PRO A CG  1 
ATOM   638  C CD  . PRO A 1 90  ? 16.152  13.991  36.287  1.00 35.66 ? 90   PRO A CD  1 
ATOM   639  N N   . ASP A 1 91  ? 18.084  11.123  37.536  1.00 37.59 ? 91   ASP A N   1 
ATOM   640  C CA  . ASP A 1 91  ? 18.673  10.197  38.507  1.00 38.37 ? 91   ASP A CA  1 
ATOM   641  C C   . ASP A 1 91  ? 18.121  8.783   38.371  1.00 38.61 ? 91   ASP A C   1 
ATOM   642  O O   . ASP A 1 91  ? 18.626  7.855   38.998  1.00 38.78 ? 91   ASP A O   1 
ATOM   643  C CB  . ASP A 1 91  ? 18.442  10.720  39.942  1.00 38.79 ? 91   ASP A CB  1 
ATOM   644  C CG  . ASP A 1 91  ? 17.071  11.427  40.121  1.00 40.03 ? 91   ASP A CG  1 
ATOM   645  O OD1 . ASP A 1 91  ? 16.025  10.738  40.042  1.00 41.65 ? 91   ASP A OD1 1 
ATOM   646  O OD2 . ASP A 1 91  ? 17.039  12.667  40.351  1.00 40.48 ? 91   ASP A OD2 1 
ATOM   647  N N   . ALA A 1 92  ? 17.094  8.638   37.531  1.00 39.11 ? 92   ALA A N   1 
ATOM   648  C CA  . ALA A 1 92  ? 16.241  7.432   37.442  1.00 39.17 ? 92   ALA A CA  1 
ATOM   649  C C   . ALA A 1 92  ? 16.982  6.100   37.366  1.00 39.13 ? 92   ALA A C   1 
ATOM   650  O O   . ALA A 1 92  ? 16.538  5.110   37.949  1.00 38.86 ? 92   ALA A O   1 
ATOM   651  C CB  . ALA A 1 92  ? 15.255  7.562   36.272  1.00 39.07 ? 92   ALA A CB  1 
ATOM   652  N N   . ILE A 1 93  ? 18.098  6.093   36.640  1.00 39.22 ? 93   ILE A N   1 
ATOM   653  C CA  . ILE A 1 93  ? 18.972  4.929   36.552  1.00 39.58 ? 93   ILE A CA  1 
ATOM   654  C C   . ILE A 1 93  ? 19.286  4.290   37.921  1.00 39.85 ? 93   ILE A C   1 
ATOM   655  O O   . ILE A 1 93  ? 18.862  3.161   38.185  1.00 39.87 ? 93   ILE A O   1 
ATOM   656  C CB  . ILE A 1 93  ? 20.273  5.250   35.785  1.00 39.70 ? 93   ILE A CB  1 
ATOM   657  C CG1 . ILE A 1 93  ? 20.834  6.621   36.211  1.00 39.85 ? 93   ILE A CG1 1 
ATOM   658  C CG2 . ILE A 1 93  ? 20.009  5.202   34.280  1.00 39.50 ? 93   ILE A CG2 1 
ATOM   659  C CD1 . ILE A 1 93  ? 22.348  6.667   36.325  1.00 39.53 ? 93   ILE A CD1 1 
ATOM   660  N N   . SER A 1 94  ? 19.998  5.011   38.788  1.00 40.01 ? 94   SER A N   1 
ATOM   661  C CA  . SER A 1 94  ? 20.393  4.489   40.097  1.00 40.17 ? 94   SER A CA  1 
ATOM   662  C C   . SER A 1 94  ? 19.207  4.128   41.008  1.00 40.14 ? 94   SER A C   1 
ATOM   663  O O   . SER A 1 94  ? 19.324  3.233   41.844  1.00 40.28 ? 94   SER A O   1 
ATOM   664  C CB  . SER A 1 94  ? 21.330  5.466   40.810  1.00 40.26 ? 94   SER A CB  1 
ATOM   665  O OG  . SER A 1 94  ? 20.609  6.559   41.351  1.00 40.49 ? 94   SER A OG  1 
ATOM   666  N N   . LEU A 1 95  ? 18.069  4.797   40.839  1.00 39.95 ? 95   LEU A N   1 
ATOM   667  C CA  . LEU A 1 95  ? 16.867  4.477   41.641  1.00 40.09 ? 95   LEU A CA  1 
ATOM   668  C C   . LEU A 1 95  ? 15.959  3.325   41.138  1.00 40.00 ? 95   LEU A C   1 
ATOM   669  O O   . LEU A 1 95  ? 14.910  3.055   41.730  1.00 39.74 ? 95   LEU A O   1 
ATOM   670  C CB  . LEU A 1 95  ? 15.984  5.713   41.834  1.00 40.21 ? 95   LEU A CB  1 
ATOM   671  C CG  . LEU A 1 95  ? 16.547  7.115   41.956  1.00 40.22 ? 95   LEU A CG  1 
ATOM   672  C CD1 . LEU A 1 95  ? 15.389  7.997   42.385  1.00 39.42 ? 95   LEU A CD1 1 
ATOM   673  C CD2 . LEU A 1 95  ? 17.739  7.181   42.926  1.00 39.88 ? 95   LEU A CD2 1 
ATOM   674  N N   . GLY A 1 96  ? 16.332  2.669   40.044  1.00 40.04 ? 96   GLY A N   1 
ATOM   675  C CA  . GLY A 1 96  ? 15.580  1.507   39.572  1.00 39.67 ? 96   GLY A CA  1 
ATOM   676  C C   . GLY A 1 96  ? 14.436  1.826   38.630  1.00 39.42 ? 96   GLY A C   1 
ATOM   677  O O   . GLY A 1 96  ? 14.009  0.953   37.877  1.00 39.59 ? 96   GLY A O   1 
ATOM   678  N N   . LEU A 1 97  ? 13.950  3.070   38.661  1.00 38.98 ? 97   LEU A N   1 
ATOM   679  C CA  . LEU A 1 97  ? 12.831  3.513   37.805  1.00 38.57 ? 97   LEU A CA  1 
ATOM   680  C C   . LEU A 1 97  ? 13.241  3.535   36.320  1.00 38.52 ? 97   LEU A C   1 
ATOM   681  O O   . LEU A 1 97  ? 14.254  4.152   35.936  1.00 38.94 ? 97   LEU A O   1 
ATOM   682  C CB  . LEU A 1 97  ? 12.331  4.895   38.243  1.00 38.37 ? 97   LEU A CB  1 
ATOM   683  C CG  . LEU A 1 97  ? 12.136  5.103   39.750  1.00 37.99 ? 97   LEU A CG  1 
ATOM   684  C CD1 . LEU A 1 97  ? 12.610  6.459   40.233  1.00 37.28 ? 97   LEU A CD1 1 
ATOM   685  C CD2 . LEU A 1 97  ? 10.708  4.877   40.150  1.00 36.77 ? 97   LEU A CD2 1 
ATOM   686  N N   . GLY A 1 98  ? 12.465  2.851   35.486  1.00 37.67 ? 98   GLY A N   1 
ATOM   687  C CA  . GLY A 1 98  ? 12.818  2.703   34.082  1.00 36.18 ? 98   GLY A CA  1 
ATOM   688  C C   . GLY A 1 98  ? 11.603  2.233   33.324  1.00 35.50 ? 98   GLY A C   1 
ATOM   689  O O   . GLY A 1 98  ? 10.491  2.219   33.875  1.00 35.59 ? 98   GLY A O   1 
ATOM   690  N N   . LYS A 1 99  ? 11.821  1.814   32.077  1.00 34.65 ? 99   LYS A N   1 
ATOM   691  C CA  . LYS A 1 99  ? 10.740  1.555   31.114  1.00 33.63 ? 99   LYS A CA  1 
ATOM   692  C C   . LYS A 1 99  ? 9.733   0.525   31.586  1.00 32.97 ? 99   LYS A C   1 
ATOM   693  O O   . LYS A 1 99  ? 8.857   0.122   30.833  1.00 32.94 ? 99   LYS A O   1 
ATOM   694  C CB  . LYS A 1 99  ? 11.302  1.194   29.725  1.00 33.95 ? 99   LYS A CB  1 
ATOM   695  C CG  . LYS A 1 99  ? 11.717  2.424   28.836  1.00 33.37 ? 99   LYS A CG  1 
ATOM   696  C CD  . LYS A 1 99  ? 12.343  1.961   27.526  1.00 32.72 ? 99   LYS A CD  1 
ATOM   697  C CE  . LYS A 1 99  ? 13.452  2.882   27.043  1.00 32.58 ? 99   LYS A CE  1 
ATOM   698  N NZ  . LYS A 1 99  ? 12.977  3.977   26.160  1.00 32.89 ? 99   LYS A NZ  1 
ATOM   699  N N   . HIS A 1 100 ? 9.832   0.145   32.858  1.00 32.29 ? 100  HIS A N   1 
ATOM   700  C CA  . HIS A 1 100 ? 8.959   -0.867  33.430  1.00 31.21 ? 100  HIS A CA  1 
ATOM   701  C C   . HIS A 1 100 ? 7.893   -0.288  34.287  1.00 31.01 ? 100  HIS A C   1 
ATOM   702  O O   . HIS A 1 100 ? 7.631   0.909   34.263  1.00 30.54 ? 100  HIS A O   1 
ATOM   703  C CB  . HIS A 1 100 ? 9.725   -1.865  34.266  1.00 30.83 ? 100  HIS A CB  1 
ATOM   704  C CG  . HIS A 1 100 ? 10.482  -1.239  35.386  1.00 29.70 ? 100  HIS A CG  1 
ATOM   705  N ND1 . HIS A 1 100 ? 11.836  -0.992  35.321  1.00 29.50 ? 100  HIS A ND1 1 
ATOM   706  C CD2 . HIS A 1 100 ? 10.078  -0.799  36.594  1.00 29.17 ? 100  HIS A CD2 1 
ATOM   707  C CE1 . HIS A 1 100 ? 12.233  -0.423  36.440  1.00 28.19 ? 100  HIS A CE1 1 
ATOM   708  N NE2 . HIS A 1 100 ? 11.186  -0.299  37.232  1.00 28.93 ? 100  HIS A NE2 1 
ATOM   709  N N   . ASN A 1 101 ? 7.328   -1.190  35.076  1.00 31.26 ? 101  ASN A N   1 
ATOM   710  C CA  . ASN A 1 101 ? 6.003   -1.092  35.623  1.00 31.62 ? 101  ASN A CA  1 
ATOM   711  C C   . ASN A 1 101 ? 6.091   -1.590  37.021  1.00 31.73 ? 101  ASN A C   1 
ATOM   712  O O   . ASN A 1 101 ? 5.085   -1.842  37.678  1.00 31.72 ? 101  ASN A O   1 
ATOM   713  C CB  . ASN A 1 101 ? 5.092   -2.045  34.856  1.00 31.87 ? 101  ASN A CB  1 
ATOM   714  C CG  . ASN A 1 101 ? 3.703   -2.099  35.438  1.00 33.69 ? 101  ASN A CG  1 
ATOM   715  O OD1 . ASN A 1 101 ? 3.145   -1.064  35.808  1.00 35.52 ? 101  ASN A OD1 1 
ATOM   716  N ND2 . ASN A 1 101 ? 3.144   -3.303  35.559  1.00 34.50 ? 101  ASN A ND2 1 
ATOM   717  N N   . TYR A 1 102 ? 7.316   -1.753  37.488  1.00 32.39 ? 102  TYR A N   1 
ATOM   718  C CA  . TYR A 1 102 ? 7.523   -2.489  38.720  1.00 32.88 ? 102  TYR A CA  1 
ATOM   719  C C   . TYR A 1 102 ? 7.306   -1.653  39.948  1.00 33.69 ? 102  TYR A C   1 
ATOM   720  O O   . TYR A 1 102 ? 6.611   -0.624  39.909  1.00 34.49 ? 102  TYR A O   1 
ATOM   721  C CB  . TYR A 1 102 ? 8.869   -3.204  38.725  1.00 32.29 ? 102  TYR A CB  1 
ATOM   722  C CG  . TYR A 1 102 ? 8.959   -4.121  37.540  1.00 31.75 ? 102  TYR A CG  1 
ATOM   723  C CD1 . TYR A 1 102 ? 7.854   -4.896  37.161  1.00 31.04 ? 102  TYR A CD1 1 
ATOM   724  C CD2 . TYR A 1 102 ? 10.114  -4.198  36.778  1.00 30.40 ? 102  TYR A CD2 1 
ATOM   725  C CE1 . TYR A 1 102 ? 7.901   -5.719  36.068  1.00 30.20 ? 102  TYR A CE1 1 
ATOM   726  C CE2 . TYR A 1 102 ? 10.171  -5.021  35.684  1.00 30.63 ? 102  TYR A CE2 1 
ATOM   727  C CZ  . TYR A 1 102 ? 9.058   -5.781  35.334  1.00 30.98 ? 102  TYR A CZ  1 
ATOM   728  O OH  . TYR A 1 102 ? 9.116   -6.621  34.247  1.00 32.69 ? 102  TYR A OH  1 
ATOM   729  N N   . CYS A 1 103 ? 7.846   -2.115  41.058  1.00 33.72 ? 103  CYS A N   1 
ATOM   730  C CA  . CYS A 1 103 ? 7.679   -1.393  42.265  1.00 33.75 ? 103  CYS A CA  1 
ATOM   731  C C   . CYS A 1 103 ? 8.976   -0.902  42.679  1.00 33.08 ? 103  CYS A C   1 
ATOM   732  O O   . CYS A 1 103 ? 9.989   -1.544  42.475  1.00 32.98 ? 103  CYS A O   1 
ATOM   733  C CB  . CYS A 1 103 ? 7.066   -2.253  43.305  1.00 34.01 ? 103  CYS A CB  1 
ATOM   734  S SG  . CYS A 1 103 ? 5.381   -1.949  43.055  1.00 39.61 ? 103  CYS A SG  1 
ATOM   735  N N   . ARG A 1 104 ? 8.957   0.296   43.206  1.00 32.71 ? 104  ARG A N   1 
ATOM   736  C CA  . ARG A 1 104 ? 10.175  0.853   43.680  1.00 32.67 ? 104  ARG A CA  1 
ATOM   737  C C   . ARG A 1 104 ? 9.785   1.596   44.925  1.00 32.39 ? 104  ARG A C   1 
ATOM   738  O O   . ARG A 1 104 ? 8.601   1.611   45.288  1.00 32.06 ? 104  ARG A O   1 
ATOM   739  C CB  . ARG A 1 104 ? 10.831  1.737   42.606  1.00 32.48 ? 104  ARG A CB  1 
ATOM   740  C CG  . ARG A 1 104 ? 11.276  0.985   41.343  1.00 33.01 ? 104  ARG A CG  1 
ATOM   741  C CD  . ARG A 1 104 ? 12.366  -0.036  41.627  1.00 35.93 ? 104  ARG A CD  1 
ATOM   742  N NE  . ARG A 1 104 ? 12.852  -0.757  40.443  1.00 38.56 ? 104  ARG A NE  1 
ATOM   743  C CZ  . ARG A 1 104 ? 12.619  -2.051  40.189  1.00 40.24 ? 104  ARG A CZ  1 
ATOM   744  N NH1 . ARG A 1 104 ? 11.892  -2.781  41.026  1.00 41.48 ? 104  ARG A NH1 1 
ATOM   745  N NH2 . ARG A 1 104 ? 13.117  -2.630  39.100  1.00 39.52 ? 104  ARG A NH2 1 
ATOM   746  N N   . ASN A 1 105 ? 10.790  2.164   45.583  1.00 32.04 ? 105  ASN A N   1 
ATOM   747  C CA  . ASN A 1 105 ? 10.598  3.026   46.708  1.00 31.76 ? 105  ASN A CA  1 
ATOM   748  C C   . ASN A 1 105 ? 11.813  3.913   46.765  1.00 31.88 ? 105  ASN A C   1 
ATOM   749  O O   . ASN A 1 105 ? 12.667  3.708   47.617  1.00 31.94 ? 105  ASN A O   1 
ATOM   750  C CB  . ASN A 1 105 ? 10.511  2.179   47.954  1.00 31.88 ? 105  ASN A CB  1 
ATOM   751  C CG  . ASN A 1 105 ? 10.447  2.992   49.197  1.00 31.92 ? 105  ASN A CG  1 
ATOM   752  O OD1 . ASN A 1 105 ? 10.027  4.140   49.178  1.00 32.11 ? 105  ASN A OD1 1 
ATOM   753  N ND2 . ASN A 1 105 ? 10.879  2.404   50.300  1.00 32.88 ? 105  ASN A ND2 1 
ATOM   754  N N   . PRO A 1 106 ? 11.905  4.893   45.840  1.00 32.08 ? 106  PRO A N   1 
ATOM   755  C CA  . PRO A 1 106 ? 13.097  5.752   45.611  1.00 32.13 ? 106  PRO A CA  1 
ATOM   756  C C   . PRO A 1 106 ? 13.315  6.838   46.677  1.00 32.22 ? 106  PRO A C   1 
ATOM   757  O O   . PRO A 1 106 ? 14.438  6.996   47.181  1.00 32.52 ? 106  PRO A O   1 
ATOM   758  C CB  . PRO A 1 106 ? 12.833  6.389   44.237  1.00 32.15 ? 106  PRO A CB  1 
ATOM   759  C CG  . PRO A 1 106 ? 11.455  5.891   43.792  1.00 32.09 ? 106  PRO A CG  1 
ATOM   760  C CD  . PRO A 1 106 ? 10.778  5.280   44.975  1.00 31.96 ? 106  PRO A CD  1 
ATOM   761  N N   . ASP A 1 107 ? 12.259  7.579   47.011  1.00 31.96 ? 107  ASP A N   1 
ATOM   762  C CA  . ASP A 1 107 ? 12.251  8.412   48.206  1.00 31.81 ? 107  ASP A CA  1 
ATOM   763  C C   . ASP A 1 107 ? 12.163  7.462   49.402  1.00 32.06 ? 107  ASP A C   1 
ATOM   764  O O   . ASP A 1 107 ? 12.359  6.252   49.255  1.00 32.26 ? 107  ASP A O   1 
ATOM   765  C CB  . ASP A 1 107 ? 11.042  9.337   48.178  1.00 31.51 ? 107  ASP A CB  1 
ATOM   766  C CG  . ASP A 1 107 ? 9.746   8.588   47.979  1.00 30.54 ? 107  ASP A CG  1 
ATOM   767  O OD1 . ASP A 1 107 ? 8.670   9.208   48.130  1.00 30.21 ? 107  ASP A OD1 1 
ATOM   768  O OD2 . ASP A 1 107 ? 9.800   7.379   47.675  1.00 28.77 ? 107  ASP A OD2 1 
ATOM   769  N N   . ASN A 1 108 ? 11.871  7.989   50.583  1.00 32.08 ? 108  ASN A N   1 
ATOM   770  C CA  . ASN A 1 108 ? 11.543  7.103   51.684  1.00 32.28 ? 108  ASN A CA  1 
ATOM   771  C C   . ASN A 1 108 ? 10.101  6.687   51.639  1.00 32.11 ? 108  ASN A C   1 
ATOM   772  O O   . ASN A 1 108 ? 9.310   7.287   50.920  1.00 31.91 ? 108  ASN A O   1 
ATOM   773  C CB  . ASN A 1 108 ? 11.889  7.717   53.023  1.00 32.58 ? 108  ASN A CB  1 
ATOM   774  C CG  . ASN A 1 108 ? 13.290  7.391   53.434  1.00 33.91 ? 108  ASN A CG  1 
ATOM   775  O OD1 . ASN A 1 108 ? 13.995  6.655   52.719  1.00 34.89 ? 108  ASN A OD1 1 
ATOM   776  N ND2 . ASN A 1 108 ? 13.721  7.924   54.585  1.00 34.32 ? 108  ASN A ND2 1 
ATOM   777  N N   . GLN A 1 109 ? 9.779   5.640   52.392  1.00 32.06 ? 109  GLN A N   1 
ATOM   778  C CA  . GLN A 1 109 ? 8.440   5.048   52.441  1.00 31.89 ? 109  GLN A CA  1 
ATOM   779  C C   . GLN A 1 109 ? 8.533   3.622   52.971  1.00 31.34 ? 109  GLN A C   1 
ATOM   780  O O   . GLN A 1 109 ? 9.322   2.822   52.466  1.00 31.53 ? 109  GLN A O   1 
ATOM   781  C CB  . GLN A 1 109 ? 7.763   5.047   51.063  1.00 31.97 ? 109  GLN A CB  1 
ATOM   782  C CG  . GLN A 1 109 ? 6.925   6.282   50.756  1.00 33.34 ? 109  GLN A CG  1 
ATOM   783  C CD  . GLN A 1 109 ? 5.616   6.327   51.536  1.00 36.49 ? 109  GLN A CD  1 
ATOM   784  O OE1 . GLN A 1 109 ? 4.536   6.308   50.932  1.00 38.35 ? 109  GLN A OE1 1 
ATOM   785  N NE2 . GLN A 1 109 ? 5.699   6.380   52.880  1.00 35.61 ? 109  GLN A NE2 1 
ATOM   786  N N   . LYS A 1 110 ? 7.733   3.311   53.987  1.00 30.49 ? 110  LYS A N   1 
ATOM   787  C CA  . LYS A 1 110 ? 7.711   1.973   54.578  1.00 29.50 ? 110  LYS A CA  1 
ATOM   788  C C   . LYS A 1 110 ? 8.172   0.890   53.590  1.00 28.93 ? 110  LYS A C   1 
ATOM   789  O O   . LYS A 1 110 ? 9.263   0.369   53.751  1.00 28.76 ? 110  LYS A O   1 
ATOM   790  C CB  . LYS A 1 110 ? 6.350   1.673   55.232  1.00 29.30 ? 110  LYS A CB  1 
ATOM   791  C CG  . LYS A 1 110 ? 5.131   2.356   54.585  1.00 29.72 ? 110  LYS A CG  1 
ATOM   792  C CD  . LYS A 1 110 ? 5.118   3.894   54.735  1.00 29.44 ? 110  LYS A CD  1 
ATOM   793  C CE  . LYS A 1 110 ? 4.431   4.373   56.019  1.00 29.83 ? 110  LYS A CE  1 
ATOM   794  N NZ  . LYS A 1 110 ? 5.205   4.086   57.257  1.00 28.51 ? 110  LYS A NZ  1 
ATOM   795  N N   . ARG A 1 111 ? 7.384   0.620   52.544  1.00 28.57 ? 111  ARG A N   1 
ATOM   796  C CA  . ARG A 1 111 ? 7.676   -0.424  51.538  1.00 28.11 ? 111  ARG A CA  1 
ATOM   797  C C   . ARG A 1 111 ? 7.716   0.123   50.108  1.00 27.71 ? 111  ARG A C   1 
ATOM   798  O O   . ARG A 1 111 ? 7.660   1.330   49.940  1.00 27.34 ? 111  ARG A O   1 
ATOM   799  C CB  . ARG A 1 111 ? 6.626   -1.518  51.624  1.00 28.25 ? 111  ARG A CB  1 
ATOM   800  C CG  . ARG A 1 111 ? 5.209   -1.014  51.493  1.00 29.61 ? 111  ARG A CG  1 
ATOM   801  C CD  . ARG A 1 111 ? 4.370   -1.970  50.654  1.00 32.29 ? 111  ARG A CD  1 
ATOM   802  N NE  . ARG A 1 111 ? 4.104   -3.310  51.216  1.00 33.59 ? 111  ARG A NE  1 
ATOM   803  C CZ  . ARG A 1 111 ? 4.030   -3.644  52.511  1.00 33.71 ? 111  ARG A CZ  1 
ATOM   804  N NH1 . ARG A 1 111 ? 4.215   -2.743  53.483  1.00 32.46 ? 111  ARG A NH1 1 
ATOM   805  N NH2 . ARG A 1 111 ? 3.762   -4.909  52.832  1.00 32.93 ? 111  ARG A NH2 1 
ATOM   806  N N   . PRO A 1 112 ? 7.835   -0.755  49.069  1.00 27.75 ? 112  PRO A N   1 
ATOM   807  C CA  . PRO A 1 112 ? 7.764   -0.212  47.710  1.00 27.70 ? 112  PRO A CA  1 
ATOM   808  C C   . PRO A 1 112 ? 6.351   -0.030  47.233  1.00 28.08 ? 112  PRO A C   1 
ATOM   809  O O   . PRO A 1 112 ? 5.450   -0.765  47.637  1.00 28.19 ? 112  PRO A O   1 
ATOM   810  C CB  . PRO A 1 112 ? 8.482   -1.258  46.854  1.00 27.09 ? 112  PRO A CB  1 
ATOM   811  C CG  . PRO A 1 112 ? 9.294   -2.050  47.807  1.00 26.99 ? 112  PRO A CG  1 
ATOM   812  C CD  . PRO A 1 112 ? 8.403   -2.113  49.023  1.00 27.91 ? 112  PRO A CD  1 
ATOM   813  N N   . TRP A 1 113 ? 6.187   0.957   46.359  1.00 28.75 ? 113  TRP A N   1 
ATOM   814  C CA  . TRP A 1 113 ? 4.885   1.449   45.923  1.00 29.01 ? 113  TRP A CA  1 
ATOM   815  C C   . TRP A 1 113 ? 4.932   1.704   44.428  1.00 29.40 ? 113  TRP A C   1 
ATOM   816  O O   . TRP A 1 113 ? 5.978   1.499   43.781  1.00 29.48 ? 113  TRP A O   1 
ATOM   817  C CB  . TRP A 1 113 ? 4.604   2.761   46.630  1.00 28.76 ? 113  TRP A CB  1 
ATOM   818  C CG  . TRP A 1 113 ? 5.757   3.720   46.514  1.00 29.02 ? 113  TRP A CG  1 
ATOM   819  C CD1 . TRP A 1 113 ? 6.817   3.853   47.374  1.00 29.11 ? 113  TRP A CD1 1 
ATOM   820  C CD2 . TRP A 1 113 ? 5.977   4.663   45.466  1.00 29.78 ? 113  TRP A CD2 1 
ATOM   821  N NE1 . TRP A 1 113 ? 7.681   4.825   46.928  1.00 29.00 ? 113  TRP A NE1 1 
ATOM   822  C CE2 . TRP A 1 113 ? 7.191   5.343   45.761  1.00 29.46 ? 113  TRP A CE2 1 
ATOM   823  C CE3 . TRP A 1 113 ? 5.265   5.011   44.310  1.00 29.10 ? 113  TRP A CE3 1 
ATOM   824  C CZ2 . TRP A 1 113 ? 7.704   6.343   44.942  1.00 29.22 ? 113  TRP A CZ2 1 
ATOM   825  C CZ3 . TRP A 1 113 ? 5.771   5.998   43.500  1.00 29.67 ? 113  TRP A CZ3 1 
ATOM   826  C CH2 . TRP A 1 113 ? 6.983   6.661   43.819  1.00 30.24 ? 113  TRP A CH2 1 
ATOM   827  N N   . CYS A 1 114 ? 3.809   2.170   43.886  1.00 29.76 ? 114  CYS A N   1 
ATOM   828  C CA  . CYS A 1 114 ? 3.757   2.605   42.493  1.00 30.24 ? 114  CYS A CA  1 
ATOM   829  C C   . CYS A 1 114 ? 2.500   3.374   42.215  1.00 29.38 ? 114  CYS A C   1 
ATOM   830  O O   . CYS A 1 114 ? 1.503   3.222   42.900  1.00 28.64 ? 114  CYS A O   1 
ATOM   831  C CB  . CYS A 1 114 ? 3.812   1.409   41.549  1.00 30.79 ? 114  CYS A CB  1 
ATOM   832  S SG  . CYS A 1 114 ? 2.362   0.336   41.750  1.00 33.83 ? 114  CYS A SG  1 
ATOM   833  N N   . TYR A 1 115 ? 2.559   4.167   41.159  1.00 29.53 ? 115  TYR A N   1 
ATOM   834  C CA  . TYR A 1 115 ? 1.461   5.038   40.787  1.00 29.83 ? 115  TYR A CA  1 
ATOM   835  C C   . TYR A 1 115 ? 0.344   4.262   40.106  1.00 30.16 ? 115  TYR A C   1 
ATOM   836  O O   . TYR A 1 115 ? 0.536   3.634   39.060  1.00 30.15 ? 115  TYR A O   1 
ATOM   837  C CB  . TYR A 1 115 ? 1.971   6.172   39.910  1.00 29.41 ? 115  TYR A CB  1 
ATOM   838  C CG  . TYR A 1 115 ? 2.845   7.155   40.653  1.00 29.15 ? 115  TYR A CG  1 
ATOM   839  C CD1 . TYR A 1 115 ? 2.360   7.870   41.776  1.00 29.23 ? 115  TYR A CD1 1 
ATOM   840  C CD2 . TYR A 1 115 ? 4.157   7.391   40.237  1.00 28.38 ? 115  TYR A CD2 1 
ATOM   841  C CE1 . TYR A 1 115 ? 3.183   8.798   42.453  1.00 29.21 ? 115  TYR A CE1 1 
ATOM   842  C CE2 . TYR A 1 115 ? 4.986   8.312   40.905  1.00 28.73 ? 115  TYR A CE2 1 
ATOM   843  C CZ  . TYR A 1 115 ? 4.497   9.010   42.001  1.00 29.52 ? 115  TYR A CZ  1 
ATOM   844  O OH  . TYR A 1 115 ? 5.340   9.904   42.632  1.00 31.03 ? 115  TYR A OH  1 
ATOM   845  N N   . VAL A 1 116 ? -0.824  4.308   40.721  1.00 30.36 ? 116  VAL A N   1 
ATOM   846  C CA  . VAL A 1 116 ? -1.888  3.412   40.354  1.00 30.86 ? 116  VAL A CA  1 
ATOM   847  C C   . VAL A 1 116 ? -3.041  4.221   39.853  1.00 31.15 ? 116  VAL A C   1 
ATOM   848  O O   . VAL A 1 116 ? -3.384  5.232   40.447  1.00 31.35 ? 116  VAL A O   1 
ATOM   849  C CB  . VAL A 1 116 ? -2.313  2.581   41.577  1.00 31.00 ? 116  VAL A CB  1 
ATOM   850  C CG1 . VAL A 1 116 ? -3.684  1.915   41.363  1.00 31.13 ? 116  VAL A CG1 1 
ATOM   851  C CG2 . VAL A 1 116 ? -1.230  1.552   41.907  1.00 30.60 ? 116  VAL A CG2 1 
ATOM   852  N N   . GLN A 1 117 ? -3.629  3.791   38.748  1.00 31.49 ? 117  GLN A N   1 
ATOM   853  C CA  . GLN A 1 117 ? -4.797  4.474   38.226  1.00 32.00 ? 117  GLN A CA  1 
ATOM   854  C C   . GLN A 1 117 ? -5.996  3.977   39.029  1.00 32.46 ? 117  GLN A C   1 
ATOM   855  O O   . GLN A 1 117 ? -6.096  2.784   39.294  1.00 33.13 ? 117  GLN A O   1 
ATOM   856  C CB  . GLN A 1 117 ? -4.949  4.145   36.745  1.00 31.77 ? 117  GLN A CB  1 
ATOM   857  C CG  . GLN A 1 117 ? -6.248  4.618   36.126  1.00 32.12 ? 117  GLN A CG  1 
ATOM   858  C CD  . GLN A 1 117 ? -6.178  6.042   35.638  1.00 32.65 ? 117  GLN A CD  1 
ATOM   859  O OE1 . GLN A 1 117 ? -5.144  6.481   35.107  1.00 32.44 ? 117  GLN A OE1 1 
ATOM   860  N NE2 . GLN A 1 117 ? -7.282  6.779   35.803  1.00 31.08 ? 117  GLN A NE2 1 
ATOM   861  N N   . ILE A 1 118 ? -6.875  4.878   39.457  1.00 32.62 ? 118  ILE A N   1 
ATOM   862  C CA  . ILE A 1 118 ? -8.133  4.495   40.125  1.00 32.91 ? 118  ILE A CA  1 
ATOM   863  C C   . ILE A 1 118 ? -9.147  5.564   39.779  1.00 33.17 ? 118  ILE A C   1 
ATOM   864  O O   . ILE A 1 118 ? -8.956  6.737   40.112  1.00 33.27 ? 118  ILE A O   1 
ATOM   865  C CB  . ILE A 1 118 ? -8.008  4.279   41.685  1.00 33.04 ? 118  ILE A CB  1 
ATOM   866  C CG1 . ILE A 1 118 ? -9.299  4.668   42.436  1.00 33.65 ? 118  ILE A CG1 1 
ATOM   867  C CG2 . ILE A 1 118 ? -6.852  5.073   42.290  1.00 33.16 ? 118  ILE A CG2 1 
ATOM   868  C CD1 . ILE A 1 118 ? -10.425 3.618   42.444  1.00 34.62 ? 118  ILE A CD1 1 
ATOM   869  N N   . GLY A 1 119 ? -10.223 5.154   39.107  1.00 33.42 ? 119  GLY A N   1 
ATOM   870  C CA  . GLY A 1 119 ? -11.068 6.094   38.386  1.00 33.44 ? 119  GLY A CA  1 
ATOM   871  C C   . GLY A 1 119 ? -10.185 6.944   37.481  1.00 33.63 ? 119  GLY A C   1 
ATOM   872  O O   . GLY A 1 119 ? -9.464  6.419   36.625  1.00 33.30 ? 119  GLY A O   1 
ATOM   873  N N   . LEU A 1 120 ? -10.199 8.254   37.716  1.00 33.83 ? 120  LEU A N   1 
ATOM   874  C CA  . LEU A 1 120 ? -9.499  9.205   36.856  1.00 33.93 ? 120  LEU A CA  1 
ATOM   875  C C   . LEU A 1 120 ? -8.073  9.528   37.305  1.00 34.03 ? 120  LEU A C   1 
ATOM   876  O O   . LEU A 1 120 ? -7.176  9.601   36.474  1.00 34.07 ? 120  LEU A O   1 
ATOM   877  C CB  . LEU A 1 120 ? -10.316 10.492  36.725  1.00 33.88 ? 120  LEU A CB  1 
ATOM   878  C CG  . LEU A 1 120 ? -10.319 11.194  35.363  1.00 33.59 ? 120  LEU A CG  1 
ATOM   879  C CD1 . LEU A 1 120 ? -11.600 11.975  35.220  1.00 32.68 ? 120  LEU A CD1 1 
ATOM   880  C CD2 . LEU A 1 120 ? -9.103  12.102  35.167  1.00 33.29 ? 120  LEU A CD2 1 
ATOM   881  N N   . ARG A 1 121 ? -7.877  9.726   38.607  1.00 34.26 ? 121  ARG A N   1 
ATOM   882  C CA  . ARG A 1 121 ? -6.594  10.170  39.166  1.00 34.54 ? 121  ARG A CA  1 
ATOM   883  C C   . ARG A 1 121 ? -5.467  9.136   39.195  1.00 34.87 ? 121  ARG A C   1 
ATOM   884  O O   . ARG A 1 121 ? -5.652  7.958   38.861  1.00 34.93 ? 121  ARG A O   1 
ATOM   885  C CB  . ARG A 1 121 ? -6.800  10.661  40.591  1.00 34.55 ? 121  ARG A CB  1 
ATOM   886  C CG  . ARG A 1 121 ? -7.042  12.131  40.723  1.00 34.62 ? 121  ARG A CG  1 
ATOM   887  C CD  . ARG A 1 121 ? -6.897  12.520  42.174  1.00 34.98 ? 121  ARG A CD  1 
ATOM   888  N NE  . ARG A 1 121 ? -7.406  13.861  42.442  1.00 35.73 ? 121  ARG A NE  1 
ATOM   889  C CZ  . ARG A 1 121 ? -7.414  14.446  43.640  1.00 35.80 ? 121  ARG A CZ  1 
ATOM   890  N NH1 . ARG A 1 121 ? -6.935  13.810  44.707  1.00 35.62 ? 121  ARG A NH1 1 
ATOM   891  N NH2 . ARG A 1 121 ? -7.903  15.677  43.771  1.00 35.93 ? 121  ARG A NH2 1 
ATOM   892  N N   . GLN A 1 122 ? -4.292  9.599   39.611  1.00 35.16 ? 122  GLN A N   1 
ATOM   893  C CA  . GLN A 1 122 ? -3.157  8.715   39.841  1.00 35.53 ? 122  GLN A CA  1 
ATOM   894  C C   . GLN A 1 122 ? -2.698  8.710   41.281  1.00 35.52 ? 122  GLN A C   1 
ATOM   895  O O   . GLN A 1 122 ? -1.712  9.366   41.633  1.00 35.52 ? 122  GLN A O   1 
ATOM   896  C CB  . GLN A 1 122 ? -1.975  9.069   38.944  1.00 35.63 ? 122  GLN A CB  1 
ATOM   897  C CG  . GLN A 1 122 ? -1.970  8.315   37.645  1.00 36.38 ? 122  GLN A CG  1 
ATOM   898  C CD  . GLN A 1 122 ? -2.743  9.031   36.559  1.00 36.82 ? 122  GLN A CD  1 
ATOM   899  O OE1 . GLN A 1 122 ? -3.953  9.260   36.673  1.00 36.41 ? 122  GLN A OE1 1 
ATOM   900  N NE2 . GLN A 1 122 ? -2.039  9.394   35.491  1.00 36.50 ? 122  GLN A NE2 1 
ATOM   901  N N   . PHE A 1 123 ? -3.412  7.951   42.101  1.00 35.59 ? 123  PHE A N   1 
ATOM   902  C CA  . PHE A 1 123 ? -2.975  7.644   43.455  1.00 35.74 ? 123  PHE A CA  1 
ATOM   903  C C   . PHE A 1 123 ? -1.674  6.807   43.497  1.00 35.56 ? 123  PHE A C   1 
ATOM   904  O O   . PHE A 1 123 ? -1.398  5.992   42.612  1.00 35.23 ? 123  PHE A O   1 
ATOM   905  C CB  . PHE A 1 123 ? -4.109  6.956   44.223  1.00 35.75 ? 123  PHE A CB  1 
ATOM   906  C CG  . PHE A 1 123 ? -5.243  7.875   44.590  1.00 36.36 ? 123  PHE A CG  1 
ATOM   907  C CD1 . PHE A 1 123 ? -6.049  8.446   43.608  1.00 36.53 ? 123  PHE A CD1 1 
ATOM   908  C CD2 . PHE A 1 123 ? -5.514  8.161   45.932  1.00 37.46 ? 123  PHE A CD2 1 
ATOM   909  C CE1 . PHE A 1 123 ? -7.107  9.295   43.959  1.00 37.64 ? 123  PHE A CE1 1 
ATOM   910  C CE2 . PHE A 1 123 ? -6.575  9.012   46.301  1.00 37.65 ? 123  PHE A CE2 1 
ATOM   911  C CZ  . PHE A 1 123 ? -7.371  9.581   45.314  1.00 37.70 ? 123  PHE A CZ  1 
ATOM   912  N N   . VAL A 1 124 ? -0.872  7.056   44.523  1.00 35.68 ? 124  VAL A N   1 
ATOM   913  C CA  . VAL A 1 124 ? 0.304   6.260   44.797  1.00 36.15 ? 124  VAL A CA  1 
ATOM   914  C C   . VAL A 1 124 ? -0.082  5.177   45.778  1.00 36.77 ? 124  VAL A C   1 
ATOM   915  O O   . VAL A 1 124 ? -0.350  5.449   46.945  1.00 36.86 ? 124  VAL A O   1 
ATOM   916  C CB  . VAL A 1 124 ? 1.441   7.098   45.393  1.00 36.19 ? 124  VAL A CB  1 
ATOM   917  C CG1 . VAL A 1 124 ? 0.877   8.203   46.290  1.00 36.53 ? 124  VAL A CG1 1 
ATOM   918  C CG2 . VAL A 1 124 ? 2.450   6.213   46.146  1.00 34.73 ? 124  VAL A CG2 1 
ATOM   919  N N   . GLN A 1 125 ? -0.110  3.944   45.291  1.00 37.67 ? 125  GLN A N   1 
ATOM   920  C CA  . GLN A 1 125 ? -0.499  2.806   46.106  1.00 38.39 ? 125  GLN A CA  1 
ATOM   921  C C   . GLN A 1 125 ? 0.680   1.903   46.409  1.00 39.26 ? 125  GLN A C   1 
ATOM   922  O O   . GLN A 1 125 ? 1.733   1.998   45.773  1.00 39.07 ? 125  GLN A O   1 
ATOM   923  C CB  . GLN A 1 125 ? -1.612  2.023   45.431  1.00 38.07 ? 125  GLN A CB  1 
ATOM   924  C CG  . GLN A 1 125 ? -2.866  2.814   45.261  1.00 38.00 ? 125  GLN A CG  1 
ATOM   925  C CD  . GLN A 1 125 ? -3.716  2.812   46.497  1.00 38.51 ? 125  GLN A CD  1 
ATOM   926  O OE1 . GLN A 1 125 ? -4.513  1.895   46.698  1.00 39.20 ? 125  GLN A OE1 1 
ATOM   927  N NE2 . GLN A 1 125 ? -3.569  3.847   47.336  1.00 38.67 ? 125  GLN A NE2 1 
ATOM   928  N N   . GLU A 1 126 ? 0.476   1.030   47.393  1.00 40.64 ? 126  GLU A N   1 
ATOM   929  C CA  . GLU A 1 126 ? 1.521   0.161   47.922  1.00 42.13 ? 126  GLU A CA  1 
ATOM   930  C C   . GLU A 1 126 ? 1.565   -1.223  47.254  1.00 42.62 ? 126  GLU A C   1 
ATOM   931  O O   . GLU A 1 126 ? 0.540   -1.908  47.142  1.00 43.02 ? 126  GLU A O   1 
ATOM   932  C CB  . GLU A 1 126 ? 1.313   -0.042  49.412  1.00 42.12 ? 126  GLU A CB  1 
ATOM   933  C CG  . GLU A 1 126 ? 1.002   1.184   50.198  1.00 43.70 ? 126  GLU A CG  1 
ATOM   934  C CD  . GLU A 1 126 ? 0.952   0.849   51.671  1.00 46.98 ? 126  GLU A CD  1 
ATOM   935  O OE1 . GLU A 1 126 ? -0.054  1.204   52.352  1.00 46.98 ? 126  GLU A OE1 1 
ATOM   936  O OE2 . GLU A 1 126 ? 1.925   0.190   52.128  1.00 47.86 ? 126  GLU A OE2 1 
ATOM   937  N N   . CYS A 1 127 ? 2.763   -1.642  46.864  1.00 42.82 ? 127  CYS A N   1 
ATOM   938  C CA  . CYS A 1 127 ? 2.947   -2.893  46.177  1.00 43.53 ? 127  CYS A CA  1 
ATOM   939  C C   . CYS A 1 127 ? 2.677   -4.134  47.040  1.00 44.29 ? 127  CYS A C   1 
ATOM   940  O O   . CYS A 1 127 ? 2.369   -4.020  48.225  1.00 44.34 ? 127  CYS A O   1 
ATOM   941  C CB  . CYS A 1 127 ? 4.364   -2.935  45.673  1.00 43.25 ? 127  CYS A CB  1 
ATOM   942  S SG  . CYS A 1 127 ? 4.449   -3.504  44.000  1.00 44.14 ? 127  CYS A SG  1 
ATOM   943  N N   . MET A 1 128 ? 2.800   -5.321  46.442  1.00 45.21 ? 128  MET A N   1 
ATOM   944  C CA  . MET A 1 128 ? 2.629   -6.565  47.185  1.00 46.10 ? 128  MET A CA  1 
ATOM   945  C C   . MET A 1 128 ? 3.864   -7.176  47.800  1.00 46.09 ? 128  MET A C   1 
ATOM   946  O O   . MET A 1 128 ? 3.859   -7.479  48.992  1.00 46.50 ? 128  MET A O   1 
ATOM   947  C CB  . MET A 1 128 ? 1.955   -7.639  46.356  1.00 46.60 ? 128  MET A CB  1 
ATOM   948  C CG  . MET A 1 128 ? 0.617   -7.977  46.932  1.00 48.74 ? 128  MET A CG  1 
ATOM   949  S SD  . MET A 1 128 ? -0.363  -6.584  46.445  1.00 52.51 ? 128  MET A SD  1 
ATOM   950  C CE  . MET A 1 128 ? -0.183  -6.838  44.691  1.00 53.33 ? 128  MET A CE  1 
ATOM   951  N N   . VAL A 1 129 ? 4.881   -7.424  46.980  1.00 45.64 ? 129  VAL A N   1 
ATOM   952  C CA  . VAL A 1 129 ? 6.131   -8.024  47.440  1.00 45.46 ? 129  VAL A CA  1 
ATOM   953  C C   . VAL A 1 129 ? 6.202   -8.320  48.949  1.00 45.50 ? 129  VAL A C   1 
ATOM   954  O O   . VAL A 1 129 ? 6.323   -7.402  49.756  1.00 45.65 ? 129  VAL A O   1 
ATOM   955  C CB  . VAL A 1 129 ? 7.313   -7.116  47.080  1.00 45.43 ? 129  VAL A CB  1 
ATOM   956  C CG1 . VAL A 1 129 ? 8.050   -7.642  45.881  1.00 45.24 ? 129  VAL A CG1 1 
ATOM   957  C CG2 . VAL A 1 129 ? 6.824   -5.716  46.831  1.00 45.96 ? 129  VAL A CG2 1 
ATOM   958  N N   . HIS A 1 130 ? 6.143   -9.595  49.334  1.00 45.49 ? 130  HIS A N   1 
ATOM   959  C CA  . HIS A 1 130 ? 6.256   -9.947  50.740  1.00 45.30 ? 130  HIS A CA  1 
ATOM   960  C C   . HIS A 1 130 ? 7.624   -9.562  51.236  1.00 45.28 ? 130  HIS A C   1 
ATOM   961  O O   . HIS A 1 130 ? 8.602   -9.606  50.504  1.00 44.69 ? 130  HIS A O   1 
ATOM   962  C CB  . HIS A 1 130 ? 6.023   -11.436 50.976  1.00 45.40 ? 130  HIS A CB  1 
ATOM   963  C CG  . HIS A 1 130 ? 5.502   -11.773 52.351  1.00 46.08 ? 130  HIS A CG  1 
ATOM   964  N ND1 . HIS A 1 130 ? 6.085   -12.731 53.160  1.00 45.13 ? 130  HIS A ND1 1 
ATOM   965  C CD2 . HIS A 1 130 ? 4.429   -11.306 53.042  1.00 45.72 ? 130  HIS A CD2 1 
ATOM   966  C CE1 . HIS A 1 130 ? 5.395   -12.839 54.283  1.00 44.87 ? 130  HIS A CE1 1 
ATOM   967  N NE2 . HIS A 1 130 ? 4.387   -11.986 54.237  1.00 44.67 ? 130  HIS A NE2 1 
ATOM   968  N N   . ASP A 1 131 ? 7.641   -9.140  52.493  1.00 45.81 ? 131  ASP A N   1 
ATOM   969  C CA  . ASP A 1 131 ? 8.831   -8.880  53.275  1.00 46.09 ? 131  ASP A CA  1 
ATOM   970  C C   . ASP A 1 131 ? 9.471   -10.217 53.644  1.00 46.22 ? 131  ASP A C   1 
ATOM   971  O O   . ASP A 1 131 ? 8.800   -11.248 53.692  1.00 45.73 ? 131  ASP A O   1 
ATOM   972  C CB  . ASP A 1 131 ? 8.371   -8.147  54.533  1.00 46.10 ? 131  ASP A CB  1 
ATOM   973  C CG  . ASP A 1 131 ? 9.496   -7.826  55.482  1.00 47.57 ? 131  ASP A CG  1 
ATOM   974  O OD1 . ASP A 1 131 ? 10.225  -6.845  55.226  1.00 48.44 ? 131  ASP A OD1 1 
ATOM   975  O OD2 . ASP A 1 131 ? 9.631   -8.533  56.512  1.00 50.06 ? 131  ASP A OD2 1 
ATOM   976  N N   . CYS A 1 132 ? 10.771  -10.215 53.874  1.00 47.13 ? 132  CYS A N   1 
ATOM   977  C CA  . CYS A 1 132 ? 11.394  -11.366 54.521  1.00 48.93 ? 132  CYS A CA  1 
ATOM   978  C C   . CYS A 1 132 ? 11.366  -11.172 56.081  1.00 49.74 ? 132  CYS A C   1 
ATOM   979  O O   . CYS A 1 132 ? 10.641  -11.857 56.838  1.00 50.44 ? 132  CYS A O   1 
ATOM   980  C CB  . CYS A 1 132 ? 12.804  -11.625 53.956  1.00 48.54 ? 132  CYS A CB  1 
ATOM   981  S SG  . CYS A 1 132 ? 13.138  -10.833 52.283  1.00 51.93 ? 132  CYS A SG  1 
ATOM   982  N N   . LEU B 2 1   ? 17.260  23.218  10.513  1.00 31.68 ? 1    LEU U N   1 
ATOM   983  C CA  . LEU B 2 1   ? 16.014  22.404  10.624  1.00 31.45 ? 1    LEU U CA  1 
ATOM   984  C C   . LEU B 2 1   ? 15.772  22.088  12.103  1.00 31.74 ? 1    LEU U C   1 
ATOM   985  O O   . LEU B 2 1   ? 16.652  21.534  12.779  1.00 31.95 ? 1    LEU U O   1 
ATOM   986  C CB  . LEU B 2 1   ? 16.168  21.103  9.816   1.00 31.13 ? 1    LEU U CB  1 
ATOM   987  C CG  . LEU B 2 1   ? 14.999  20.371  9.154   1.00 29.51 ? 1    LEU U CG  1 
ATOM   988  C CD1 . LEU B 2 1   ? 15.313  18.882  9.080   1.00 28.39 ? 1    LEU U CD1 1 
ATOM   989  C CD2 . LEU B 2 1   ? 13.700  20.583  9.865   1.00 27.85 ? 1    LEU U CD2 1 
ATOM   990  N N   . GLN B 2 2   ? 14.598  22.460  12.607  1.00 31.64 ? 2    GLN U N   1 
ATOM   991  C CA  . GLN B 2 2   ? 14.194  22.042  13.935  1.00 31.78 ? 2    GLN U CA  1 
ATOM   992  C C   . GLN B 2 2   ? 13.844  20.570  13.898  1.00 32.20 ? 2    GLN U C   1 
ATOM   993  O O   . GLN B 2 2   ? 13.147  20.110  13.002  1.00 31.84 ? 2    GLN U O   1 
ATOM   994  C CB  . GLN B 2 2   ? 13.016  22.853  14.460  1.00 31.29 ? 2    GLN U CB  1 
ATOM   995  C CG  . GLN B 2 2   ? 13.423  23.980  15.357  1.00 31.69 ? 2    GLN U CG  1 
ATOM   996  C CD  . GLN B 2 2   ? 12.251  24.847  15.805  1.00 34.52 ? 2    GLN U CD  1 
ATOM   997  O OE1 . GLN B 2 2   ? 11.276  25.047  15.070  1.00 36.71 ? 2    GLN U OE1 1 
ATOM   998  N NE2 . GLN B 2 2   ? 12.356  25.398  17.006  1.00 34.76 ? 2    GLN U NE2 1 
ATOM   999  N N   . CYS B 2 3   ? 14.358  19.837  14.876  1.00 33.05 ? 3    CYS U N   1 
ATOM   1000 C CA  . CYS B 2 3   ? 14.003  18.450  15.050  1.00 34.18 ? 3    CYS U CA  1 
ATOM   1001 C C   . CYS B 2 3   ? 14.219  17.929  16.452  1.00 33.86 ? 3    CYS U C   1 
ATOM   1002 O O   . CYS B 2 3   ? 15.263  18.177  17.027  1.00 34.23 ? 3    CYS U O   1 
ATOM   1003 C CB  . CYS B 2 3   ? 14.733  17.597  14.029  1.00 34.55 ? 3    CYS U CB  1 
ATOM   1004 S SG  . CYS B 2 3   ? 13.545  17.141  12.771  1.00 38.34 ? 3    CYS U SG  1 
ATOM   1005 N N   . MET B 2 4   ? 13.232  17.213  16.993  1.00 33.77 ? 4    MET U N   1 
ATOM   1006 C CA  . MET B 2 4   ? 13.320  16.662  18.350  1.00 33.98 ? 4    MET U CA  1 
ATOM   1007 C C   . MET B 2 4   ? 14.556  15.809  18.485  1.00 34.48 ? 4    MET U C   1 
ATOM   1008 O O   . MET B 2 4   ? 14.924  15.099  17.536  1.00 35.01 ? 4    MET U O   1 
ATOM   1009 C CB  . MET B 2 4   ? 12.129  15.786  18.674  1.00 33.61 ? 4    MET U CB  1 
ATOM   1010 C CG  . MET B 2 4   ? 10.832  16.376  18.305  1.00 33.90 ? 4    MET U CG  1 
ATOM   1011 S SD  . MET B 2 4   ? 9.990   17.071  19.704  1.00 36.66 ? 4    MET U SD  1 
ATOM   1012 C CE  . MET B 2 4   ? 10.880  18.590  19.979  1.00 36.84 ? 4    MET U CE  1 
ATOM   1013 N N   . GLN B 2 5   ? 15.192  15.883  19.653  1.00 34.50 ? 5    GLN U N   1 
ATOM   1014 C CA  . GLN B 2 5   ? 16.369  15.078  19.960  1.00 34.74 ? 5    GLN U CA  1 
ATOM   1015 C C   . GLN B 2 5   ? 16.186  14.526  21.343  1.00 34.95 ? 5    GLN U C   1 
ATOM   1016 O O   . GLN B 2 5   ? 15.610  15.187  22.189  1.00 35.28 ? 5    GLN U O   1 
ATOM   1017 C CB  . GLN B 2 5   ? 17.644  15.919  19.875  1.00 34.58 ? 5    GLN U CB  1 
ATOM   1018 C CG  . GLN B 2 5   ? 18.819  15.457  20.743  1.00 35.09 ? 5    GLN U CG  1 
ATOM   1019 C CD  . GLN B 2 5   ? 18.904  16.244  22.041  1.00 37.48 ? 5    GLN U CD  1 
ATOM   1020 O OE1 . GLN B 2 5   ? 19.621  17.256  22.154  1.00 37.22 ? 5    GLN U OE1 1 
ATOM   1021 N NE2 . GLN B 2 5   ? 18.140  15.804  23.024  1.00 38.85 ? 5    GLN U NE2 1 
ATOM   1022 N N   . CYS B 2 6   ? 16.660  13.308  21.568  1.00 35.31 ? 6    CYS U N   1 
ATOM   1023 C CA  . CYS B 2 6   ? 16.575  12.670  22.872  1.00 35.68 ? 6    CYS U CA  1 
ATOM   1024 C C   . CYS B 2 6   ? 17.027  11.229  22.795  1.00 35.62 ? 6    CYS U C   1 
ATOM   1025 O O   . CYS B 2 6   ? 16.428  10.419  22.110  1.00 35.06 ? 6    CYS U O   1 
ATOM   1026 C CB  . CYS B 2 6   ? 15.160  12.748  23.449  1.00 35.52 ? 6    CYS U CB  1 
ATOM   1027 S SG  . CYS B 2 6   ? 13.915  12.206  22.279  1.00 37.71 ? 6    CYS U SG  1 
ATOM   1028 N N   . GLU B 2 7   ? 18.110  10.948  23.509  1.00 36.12 ? 7    GLU U N   1 
ATOM   1029 C CA  . GLU B 2 7   ? 18.565  9.614   23.790  1.00 36.93 ? 7    GLU U CA  1 
ATOM   1030 C C   . GLU B 2 7   ? 17.516  8.859   24.613  1.00 36.96 ? 7    GLU U C   1 
ATOM   1031 O O   . GLU B 2 7   ? 16.452  9.397   24.943  1.00 36.76 ? 7    GLU U O   1 
ATOM   1032 C CB  . GLU B 2 7   ? 19.869  9.709   24.575  1.00 37.29 ? 7    GLU U CB  1 
ATOM   1033 C CG  . GLU B 2 7   ? 20.896  8.667   24.214  1.00 40.54 ? 7    GLU U CG  1 
ATOM   1034 C CD  . GLU B 2 7   ? 21.510  8.920   22.849  1.00 45.55 ? 7    GLU U CD  1 
ATOM   1035 O OE1 . GLU B 2 7   ? 21.399  10.072  22.352  1.00 47.54 ? 7    GLU U OE1 1 
ATOM   1036 O OE2 . GLU B 2 7   ? 22.100  7.969   22.270  1.00 47.49 ? 7    GLU U OE2 1 
ATOM   1037 N N   . SER B 2 8   ? 17.853  7.622   24.972  1.00 37.31 ? 8    SER U N   1 
ATOM   1038 C CA  . SER B 2 8   ? 16.914  6.649   25.524  1.00 37.74 ? 8    SER U CA  1 
ATOM   1039 C C   . SER B 2 8   ? 15.886  7.145   26.549  1.00 38.40 ? 8    SER U C   1 
ATOM   1040 O O   . SER B 2 8   ? 14.717  7.362   26.198  1.00 38.79 ? 8    SER U O   1 
ATOM   1041 C CB  . SER B 2 8   ? 17.671  5.469   26.109  1.00 37.45 ? 8    SER U CB  1 
ATOM   1042 O OG  . SER B 2 8   ? 16.748  4.462   26.478  1.00 37.53 ? 8    SER U OG  1 
ATOM   1043 N N   . ASN B 2 9   ? 16.324  7.303   27.802  1.00 38.48 ? 9    ASN U N   1 
ATOM   1044 C CA  . ASN B 2 9   ? 15.426  7.524   28.947  1.00 38.54 ? 9    ASN U CA  1 
ATOM   1045 C C   . ASN B 2 9   ? 15.149  9.013   29.134  1.00 38.07 ? 9    ASN U C   1 
ATOM   1046 O O   . ASN B 2 9   ? 14.509  9.439   30.117  1.00 37.93 ? 9    ASN U O   1 
ATOM   1047 C CB  . ASN B 2 9   ? 16.056  6.955   30.243  1.00 39.24 ? 9    ASN U CB  1 
ATOM   1048 C CG  . ASN B 2 9   ? 16.745  5.586   30.032  1.00 40.48 ? 9    ASN U CG  1 
ATOM   1049 O OD1 . ASN B 2 9   ? 17.927  5.400   30.380  1.00 40.84 ? 9    ASN U OD1 1 
ATOM   1050 N ND2 . ASN B 2 9   ? 16.003  4.629   29.462  1.00 40.72 ? 9    ASN U ND2 1 
ATOM   1051 N N   . GLN B 2 10  ? 15.672  9.802   28.199  1.00 37.16 ? 10   GLN U N   1 
ATOM   1052 C CA  . GLN B 2 10  ? 15.581  11.248  28.270  1.00 36.18 ? 10   GLN U CA  1 
ATOM   1053 C C   . GLN B 2 10  ? 14.246  11.701  27.766  1.00 35.29 ? 10   GLN U C   1 
ATOM   1054 O O   . GLN B 2 10  ? 13.523  10.929  27.162  1.00 35.22 ? 10   GLN U O   1 
ATOM   1055 C CB  . GLN B 2 10  ? 16.677  11.879  27.426  1.00 36.26 ? 10   GLN U CB  1 
ATOM   1056 C CG  . GLN B 2 10  ? 17.963  12.110  28.188  1.00 37.00 ? 10   GLN U CG  1 
ATOM   1057 C CD  . GLN B 2 10  ? 19.195  12.009  27.311  1.00 38.57 ? 10   GLN U CD  1 
ATOM   1058 O OE1 . GLN B 2 10  ? 20.286  11.658  27.783  1.00 39.65 ? 10   GLN U OE1 1 
ATOM   1059 N NE2 . GLN B 2 10  ? 19.032  12.305  26.024  1.00 38.93 ? 10   GLN U NE2 1 
ATOM   1060 N N   . SER B 2 11  ? 13.921  12.958  28.031  1.00 34.42 ? 11   SER U N   1 
ATOM   1061 C CA  . SER B 2 11  ? 12.790  13.608  27.399  1.00 33.59 ? 11   SER U CA  1 
ATOM   1062 C C   . SER B 2 11  ? 13.356  14.276  26.172  1.00 33.17 ? 11   SER U C   1 
ATOM   1063 O O   . SER B 2 11  ? 14.569  14.381  26.048  1.00 33.17 ? 11   SER U O   1 
ATOM   1064 C CB  . SER B 2 11  ? 12.212  14.659  28.327  1.00 33.49 ? 11   SER U CB  1 
ATOM   1065 O OG  . SER B 2 11  ? 13.184  15.650  28.556  1.00 33.10 ? 11   SER U OG  1 
ATOM   1066 N N   . CYS B 2 12  ? 12.497  14.736  25.268  1.00 32.73 ? 12   CYS U N   1 
ATOM   1067 C CA  . CYS B 2 12  ? 12.983  15.351  24.026  1.00 32.25 ? 12   CYS U CA  1 
ATOM   1068 C C   . CYS B 2 12  ? 13.041  16.847  24.020  1.00 30.87 ? 12   CYS U C   1 
ATOM   1069 O O   . CYS B 2 12  ? 12.165  17.541  24.542  1.00 30.99 ? 12   CYS U O   1 
ATOM   1070 C CB  . CYS B 2 12  ? 12.240  14.860  22.789  1.00 32.29 ? 12   CYS U CB  1 
ATOM   1071 S SG  . CYS B 2 12  ? 12.086  13.105  22.839  1.00 36.41 ? 12   CYS U SG  1 
ATOM   1072 N N   . LEU B 2 13  ? 14.109  17.303  23.386  1.00 29.44 ? 13   LEU U N   1 
ATOM   1073 C CA  . LEU B 2 13  ? 14.423  18.688  23.197  1.00 28.18 ? 13   LEU U CA  1 
ATOM   1074 C C   . LEU B 2 13  ? 14.114  19.064  21.763  1.00 27.22 ? 13   LEU U C   1 
ATOM   1075 O O   . LEU B 2 13  ? 14.045  18.203  20.913  1.00 27.33 ? 13   LEU U O   1 
ATOM   1076 C CB  . LEU B 2 13  ? 15.908  18.872  23.507  1.00 28.03 ? 13   LEU U CB  1 
ATOM   1077 C CG  . LEU B 2 13  ? 16.325  19.241  24.946  1.00 27.74 ? 13   LEU U CG  1 
ATOM   1078 C CD1 . LEU B 2 13  ? 15.283  18.937  26.042  1.00 24.90 ? 13   LEU U CD1 1 
ATOM   1079 C CD2 . LEU B 2 13  ? 17.708  18.662  25.265  1.00 27.80 ? 13   LEU U CD2 1 
ATOM   1080 N N   . VAL B 2 14  ? 13.904  20.340  21.497  1.00 26.44 ? 14   VAL U N   1 
ATOM   1081 C CA  . VAL B 2 14  ? 13.798  20.802  20.132  1.00 26.19 ? 14   VAL U CA  1 
ATOM   1082 C C   . VAL B 2 14  ? 15.182  21.193  19.673  1.00 26.62 ? 14   VAL U C   1 
ATOM   1083 O O   . VAL B 2 14  ? 15.575  22.329  19.802  1.00 26.66 ? 14   VAL U O   1 
ATOM   1084 C CB  . VAL B 2 14  ? 12.872  22.005  20.010  1.00 25.74 ? 14   VAL U CB  1 
ATOM   1085 C CG1 . VAL B 2 14  ? 12.843  22.481  18.617  1.00 25.48 ? 14   VAL U CG1 1 
ATOM   1086 C CG2 . VAL B 2 14  ? 11.486  21.633  20.405  1.00 25.71 ? 14   VAL U CG2 1 
ATOM   1087 N N   . GLU B 2 15  ? 15.930  20.227  19.165  1.00 27.52 ? 15   GLU U N   1 
ATOM   1088 C CA  . GLU B 2 15  ? 17.253  20.457  18.605  1.00 28.58 ? 15   GLU U CA  1 
ATOM   1089 C C   . GLU B 2 15  ? 17.022  21.139  17.271  1.00 28.41 ? 15   GLU U C   1 
ATOM   1090 O O   . GLU B 2 15  ? 15.887  21.269  16.847  1.00 28.14 ? 15   GLU U O   1 
ATOM   1091 C CB  . GLU B 2 15  ? 17.976  19.110  18.443  1.00 29.15 ? 15   GLU U CB  1 
ATOM   1092 C CG  . GLU B 2 15  ? 19.488  19.138  18.054  1.00 33.18 ? 15   GLU U CG  1 
ATOM   1093 C CD  . GLU B 2 15  ? 20.327  17.963  18.698  1.00 38.19 ? 15   GLU U CD  1 
ATOM   1094 O OE1 . GLU B 2 15  ? 20.804  17.034  17.965  1.00 38.60 ? 15   GLU U OE1 1 
ATOM   1095 O OE2 . GLU B 2 15  ? 20.509  17.981  19.949  1.00 38.99 ? 15   GLU U OE2 1 
ATOM   1096 N N   . GLU B 2 16  ? 18.086  21.587  16.618  1.00 28.71 ? 16   GLU U N   1 
ATOM   1097 C CA  . GLU B 2 16  ? 17.951  22.402  15.432  1.00 28.83 ? 16   GLU U CA  1 
ATOM   1098 C C   . GLU B 2 16  ? 19.221  22.326  14.631  1.00 29.17 ? 16   GLU U C   1 
ATOM   1099 O O   . GLU B 2 16  ? 20.235  22.873  15.044  1.00 28.91 ? 16   GLU U O   1 
ATOM   1100 C CB  . GLU B 2 16  ? 17.679  23.839  15.837  1.00 28.59 ? 16   GLU U CB  1 
ATOM   1101 C CG  . GLU B 2 16  ? 16.768  24.565  14.876  1.00 29.33 ? 16   GLU U CG  1 
ATOM   1102 C CD  . GLU B 2 16  ? 17.490  25.172  13.682  1.00 29.62 ? 16   GLU U CD  1 
ATOM   1103 O OE1 . GLU B 2 16  ? 16.907  26.067  13.038  1.00 30.22 ? 16   GLU U OE1 1 
ATOM   1104 O OE2 . GLU B 2 16  ? 18.635  24.775  13.387  1.00 29.65 ? 16   GLU U OE2 1 
ATOM   1105 N N   . CYS B 2 17  ? 19.151  21.673  13.475  1.00 30.00 ? 17   CYS U N   1 
ATOM   1106 C CA  . CYS B 2 17  ? 20.344  21.205  12.768  1.00 31.49 ? 17   CYS U CA  1 
ATOM   1107 C C   . CYS B 2 17  ? 21.129  22.309  12.096  1.00 32.01 ? 17   CYS U C   1 
ATOM   1108 O O   . CYS B 2 17  ? 20.604  23.385  11.873  1.00 32.34 ? 17   CYS U O   1 
ATOM   1109 C CB  . CYS B 2 17  ? 19.969  20.165  11.729  1.00 31.74 ? 17   CYS U CB  1 
ATOM   1110 S SG  . CYS B 2 17  ? 18.527  19.133  12.111  1.00 34.97 ? 17   CYS U SG  1 
ATOM   1111 N N   . ALA B 2 18  ? 22.390  22.046  11.771  1.00 33.04 ? 18   ALA U N   1 
ATOM   1112 C CA  . ALA B 2 18  ? 23.203  23.038  11.059  1.00 34.23 ? 18   ALA U CA  1 
ATOM   1113 C C   . ALA B 2 18  ? 23.367  22.672  9.597   1.00 35.02 ? 18   ALA U C   1 
ATOM   1114 O O   . ALA B 2 18  ? 23.089  21.535  9.197   1.00 35.01 ? 18   ALA U O   1 
ATOM   1115 C CB  . ALA B 2 18  ? 24.573  23.201  11.712  1.00 34.42 ? 18   ALA U CB  1 
ATOM   1116 N N   . LEU B 2 19  ? 23.821  23.643  8.805   1.00 36.14 ? 19   LEU U N   1 
ATOM   1117 C CA  . LEU B 2 19  ? 24.144  23.392  7.410   1.00 37.24 ? 19   LEU U CA  1 
ATOM   1118 C C   . LEU B 2 19  ? 24.980  22.122  7.372   1.00 37.86 ? 19   LEU U C   1 
ATOM   1119 O O   . LEU B 2 19  ? 26.132  22.092  7.829   1.00 37.91 ? 19   LEU U O   1 
ATOM   1120 C CB  . LEU B 2 19  ? 24.901  24.567  6.759   1.00 37.36 ? 19   LEU U CB  1 
ATOM   1121 C CG  . LEU B 2 19  ? 24.845  24.758  5.222   1.00 37.80 ? 19   LEU U CG  1 
ATOM   1122 C CD1 . LEU B 2 19  ? 25.788  25.880  4.770   1.00 38.01 ? 19   LEU U CD1 1 
ATOM   1123 C CD2 . LEU B 2 19  ? 25.090  23.481  4.376   1.00 37.39 ? 19   LEU U CD2 1 
ATOM   1124 N N   . GLY B 2 20  ? 24.353  21.070  6.850   1.00 38.59 ? 20   GLY U N   1 
ATOM   1125 C CA  . GLY B 2 20  ? 24.949  19.750  6.723   1.00 39.02 ? 20   GLY U CA  1 
ATOM   1126 C C   . GLY B 2 20  ? 23.911  18.708  7.069   1.00 39.25 ? 20   GLY U C   1 
ATOM   1127 O O   . GLY B 2 20  ? 23.814  17.674  6.401   1.00 39.44 ? 20   GLY U O   1 
ATOM   1128 N N   . GLN B 2 21  ? 23.134  18.992  8.113   1.00 39.45 ? 21   GLN U N   1 
ATOM   1129 C CA  . GLN B 2 21  ? 22.165  18.040  8.643   1.00 39.58 ? 21   GLN U CA  1 
ATOM   1130 C C   . GLN B 2 21  ? 20.777  18.478  8.210   1.00 38.98 ? 21   GLN U C   1 
ATOM   1131 O O   . GLN B 2 21  ? 20.366  19.615  8.474   1.00 38.51 ? 21   GLN U O   1 
ATOM   1132 C CB  . GLN B 2 21  ? 22.247  17.968  10.167  1.00 40.02 ? 21   GLN U CB  1 
ATOM   1133 C CG  . GLN B 2 21  ? 23.528  18.539  10.802  1.00 42.01 ? 21   GLN U CG  1 
ATOM   1134 C CD  . GLN B 2 21  ? 23.446  18.564  12.331  1.00 44.98 ? 21   GLN U CD  1 
ATOM   1135 O OE1 . GLN B 2 21  ? 23.885  19.523  12.987  1.00 46.20 ? 21   GLN U OE1 1 
ATOM   1136 N NE2 . GLN B 2 21  ? 22.862  17.509  12.903  1.00 45.01 ? 21   GLN U NE2 1 
ATOM   1137 N N   . ASP B 2 22  ? 20.065  17.581  7.529   1.00 38.46 ? 22   ASP U N   1 
ATOM   1138 C CA  . ASP B 2 22  ? 18.803  17.953  6.888   1.00 38.10 ? 22   ASP U CA  1 
ATOM   1139 C C   . ASP B 2 22  ? 17.752  16.866  6.969   1.00 37.62 ? 22   ASP U C   1 
ATOM   1140 O O   . ASP B 2 22  ? 16.822  16.808  6.158   1.00 37.58 ? 22   ASP U O   1 
ATOM   1141 C CB  . ASP B 2 22  ? 19.015  18.436  5.434   1.00 38.17 ? 22   ASP U CB  1 
ATOM   1142 C CG  . ASP B 2 22  ? 19.540  17.349  4.497   1.00 38.71 ? 22   ASP U CG  1 
ATOM   1143 O OD1 . ASP B 2 22  ? 20.409  17.687  3.662   1.00 40.12 ? 22   ASP U OD1 1 
ATOM   1144 O OD2 . ASP B 2 22  ? 19.087  16.181  4.558   1.00 39.04 ? 22   ASP U OD2 1 
ATOM   1145 N N   . LEU B 2 23  ? 17.894  16.014  7.968   1.00 36.96 ? 23   LEU U N   1 
ATOM   1146 C CA  . LEU B 2 23  ? 17.000  14.894  8.107   1.00 36.24 ? 23   LEU U CA  1 
ATOM   1147 C C   . LEU B 2 23  ? 16.788  14.628  9.573   1.00 36.17 ? 23   LEU U C   1 
ATOM   1148 O O   . LEU B 2 23  ? 17.610  15.037  10.391  1.00 36.37 ? 23   LEU U O   1 
ATOM   1149 C CB  . LEU B 2 23  ? 17.626  13.677  7.439   1.00 35.95 ? 23   LEU U CB  1 
ATOM   1150 C CG  . LEU B 2 23  ? 17.483  13.576  5.937   1.00 34.55 ? 23   LEU U CG  1 
ATOM   1151 C CD1 . LEU B 2 23  ? 17.997  12.231  5.501   1.00 34.00 ? 23   LEU U CD1 1 
ATOM   1152 C CD2 . LEU B 2 23  ? 16.022  13.737  5.584   1.00 33.54 ? 23   LEU U CD2 1 
ATOM   1153 N N   . CYS B 2 24  ? 15.708  13.927  9.916   1.00 35.71 ? 24   CYS U N   1 
ATOM   1154 C CA  . CYS B 2 24  ? 15.414  13.666  11.328  1.00 35.45 ? 24   CYS U CA  1 
ATOM   1155 C C   . CYS B 2 24  ? 15.312  12.238  11.716  1.00 34.44 ? 24   CYS U C   1 
ATOM   1156 O O   . CYS B 2 24  ? 14.306  11.577  11.463  1.00 34.98 ? 24   CYS U O   1 
ATOM   1157 C CB  . CYS B 2 24  ? 14.190  14.425  11.765  1.00 35.57 ? 24   CYS U CB  1 
ATOM   1158 S SG  . CYS B 2 24  ? 14.659  16.057  11.504  1.00 39.39 ? 24   CYS U SG  1 
ATOM   1159 N N   . ARG B 2 25  ? 16.377  11.785  12.361  1.00 33.01 ? 25   ARG U N   1 
ATOM   1160 C CA  . ARG B 2 25  ? 16.560  10.418  12.770  1.00 31.23 ? 25   ARG U CA  1 
ATOM   1161 C C   . ARG B 2 25  ? 15.525  10.087  13.819  1.00 30.31 ? 25   ARG U C   1 
ATOM   1162 O O   . ARG B 2 25  ? 15.124  10.962  14.592  1.00 29.66 ? 25   ARG U O   1 
ATOM   1163 C CB  . ARG B 2 25  ? 17.943  10.309  13.359  1.00 31.34 ? 25   ARG U CB  1 
ATOM   1164 C CG  . ARG B 2 25  ? 18.696  9.073   13.022  1.00 31.67 ? 25   ARG U CG  1 
ATOM   1165 C CD  . ARG B 2 25  ? 20.040  9.009   13.797  1.00 32.90 ? 25   ARG U CD  1 
ATOM   1166 N NE  . ARG B 2 25  ? 20.008  9.667   15.108  1.00 32.00 ? 25   ARG U NE  1 
ATOM   1167 C CZ  . ARG B 2 25  ? 19.256  9.289   16.137  1.00 30.60 ? 25   ARG U CZ  1 
ATOM   1168 N NH1 . ARG B 2 25  ? 18.438  8.251   16.048  1.00 27.70 ? 25   ARG U NH1 1 
ATOM   1169 N NH2 . ARG B 2 25  ? 19.317  9.980   17.260  1.00 33.11 ? 25   ARG U NH2 1 
ATOM   1170 N N   . THR B 2 26  ? 15.064  8.835   13.780  1.00 29.51 ? 26   THR U N   1 
ATOM   1171 C CA  . THR B 2 26  ? 14.157  8.240   14.763  1.00 28.87 ? 26   THR U CA  1 
ATOM   1172 C C   . THR B 2 26  ? 14.478  6.761   14.772  1.00 28.95 ? 26   THR U C   1 
ATOM   1173 O O   . THR B 2 26  ? 13.734  5.961   14.227  1.00 29.41 ? 26   THR U O   1 
ATOM   1174 C CB  . THR B 2 26  ? 12.683  8.397   14.382  1.00 28.32 ? 26   THR U CB  1 
ATOM   1175 O OG1 . THR B 2 26  ? 12.485  9.693   13.834  1.00 29.45 ? 26   THR U OG1 1 
ATOM   1176 C CG2 . THR B 2 26  ? 11.764  8.217   15.574  1.00 27.05 ? 26   THR U CG2 1 
ATOM   1177 N N   . THR B 2 27  ? 15.601  6.405   15.379  1.00 28.92 ? 27   THR U N   1 
ATOM   1178 C CA  . THR B 2 27  ? 16.000  5.017   15.518  1.00 28.92 ? 27   THR U CA  1 
ATOM   1179 C C   . THR B 2 27  ? 15.234  4.304   16.644  1.00 29.18 ? 27   THR U C   1 
ATOM   1180 O O   . THR B 2 27  ? 15.206  4.784   17.770  1.00 29.88 ? 27   THR U O   1 
ATOM   1181 C CB  . THR B 2 27  ? 17.478  4.934   15.813  1.00 28.51 ? 27   THR U CB  1 
ATOM   1182 O OG1 . THR B 2 27  ? 18.149  5.968   15.094  1.00 28.44 ? 27   THR U OG1 1 
ATOM   1183 C CG2 . THR B 2 27  ? 18.019  3.600   15.367  1.00 29.34 ? 27   THR U CG2 1 
ATOM   1184 N N   . VAL B 2 28  ? 14.614  3.164   16.337  1.00 28.96 ? 28   VAL U N   1 
ATOM   1185 C CA  . VAL B 2 28  ? 14.076  2.289   17.371  1.00 28.37 ? 28   VAL U CA  1 
ATOM   1186 C C   . VAL B 2 28  ? 14.790  0.935   17.373  1.00 28.66 ? 28   VAL U C   1 
ATOM   1187 O O   . VAL B 2 28  ? 15.129  0.422   16.317  1.00 28.30 ? 28   VAL U O   1 
ATOM   1188 C CB  . VAL B 2 28  ? 12.566  2.146   17.260  1.00 27.95 ? 28   VAL U CB  1 
ATOM   1189 C CG1 . VAL B 2 28  ? 12.121  2.386   15.870  1.00 27.53 ? 28   VAL U CG1 1 
ATOM   1190 C CG2 . VAL B 2 28  ? 12.116  0.791   17.760  1.00 27.85 ? 28   VAL U CG2 1 
ATOM   1191 N N   . LEU B 2 29  ? 15.074  0.418   18.572  1.00 29.31 ? 29   LEU U N   1 
ATOM   1192 C CA  . LEU B 2 29  ? 15.577  -0.946  18.792  1.00 30.20 ? 29   LEU U CA  1 
ATOM   1193 C C   . LEU B 2 29  ? 14.603  -1.728  19.676  1.00 31.31 ? 29   LEU U C   1 
ATOM   1194 O O   . LEU B 2 29  ? 14.244  -1.236  20.735  1.00 32.06 ? 29   LEU U O   1 
ATOM   1195 C CB  . LEU B 2 29  ? 16.952  -0.920  19.452  1.00 29.64 ? 29   LEU U CB  1 
ATOM   1196 C CG  . LEU B 2 29  ? 17.516  -2.242  20.003  1.00 29.41 ? 29   LEU U CG  1 
ATOM   1197 C CD1 . LEU B 2 29  ? 18.971  -2.489  19.568  1.00 27.84 ? 29   LEU U CD1 1 
ATOM   1198 C CD2 . LEU B 2 29  ? 17.392  -2.341  21.526  1.00 28.34 ? 29   LEU U CD2 1 
ATOM   1199 N N   . ARG B 2 30  ? 14.182  -2.927  19.250  1.00 32.24 ? 30   ARG U N   1 
ATOM   1200 C CA  . ARG B 2 30  ? 13.219  -3.759  19.994  1.00 33.17 ? 30   ARG U CA  1 
ATOM   1201 C C   . ARG B 2 30  ? 13.843  -5.107  20.288  1.00 33.37 ? 30   ARG U C   1 
ATOM   1202 O O   . ARG B 2 30  ? 14.805  -5.485  19.639  1.00 33.96 ? 30   ARG U O   1 
ATOM   1203 C CB  . ARG B 2 30  ? 11.962  -4.013  19.175  1.00 33.42 ? 30   ARG U CB  1 
ATOM   1204 C CG  . ARG B 2 30  ? 11.310  -2.798  18.587  1.00 36.55 ? 30   ARG U CG  1 
ATOM   1205 C CD  . ARG B 2 30  ? 9.940   -2.576  19.197  1.00 42.28 ? 30   ARG U CD  1 
ATOM   1206 N NE  . ARG B 2 30  ? 9.081   -1.752  18.338  1.00 45.97 ? 30   ARG U NE  1 
ATOM   1207 C CZ  . ARG B 2 30  ? 7.749   -1.716  18.414  1.00 48.55 ? 30   ARG U CZ  1 
ATOM   1208 N NH1 . ARG B 2 30  ? 7.098   -2.466  19.313  1.00 49.29 ? 30   ARG U NH1 1 
ATOM   1209 N NH2 . ARG B 2 30  ? 7.060   -0.936  17.582  1.00 49.43 ? 30   ARG U NH2 1 
ATOM   1210 N N   . GLU B 2 31  ? 13.298  -5.823  21.266  1.00 33.59 ? 31   GLU U N   1 
ATOM   1211 C CA  . GLU B 2 31  ? 13.652  -7.214  21.542  1.00 33.80 ? 31   GLU U CA  1 
ATOM   1212 C C   . GLU B 2 31  ? 12.397  -7.929  21.978  1.00 33.81 ? 31   GLU U C   1 
ATOM   1213 O O   . GLU B 2 31  ? 11.577  -7.383  22.725  1.00 33.89 ? 31   GLU U O   1 
ATOM   1214 C CB  . GLU B 2 31  ? 14.637  -7.335  22.699  1.00 34.21 ? 31   GLU U CB  1 
ATOM   1215 C CG  . GLU B 2 31  ? 16.042  -6.817  22.469  1.00 36.25 ? 31   GLU U CG  1 
ATOM   1216 C CD  . GLU B 2 31  ? 16.633  -6.177  23.737  1.00 39.55 ? 31   GLU U CD  1 
ATOM   1217 O OE1 . GLU B 2 31  ? 17.740  -6.612  24.181  1.00 39.27 ? 31   GLU U OE1 1 
ATOM   1218 O OE2 . GLU B 2 31  ? 15.973  -5.238  24.279  1.00 40.16 ? 31   GLU U OE2 1 
ATOM   1219 N N   . TRP B 2 32  ? 12.242  -9.158  21.518  1.00 33.85 ? 32   TRP U N   1 
ATOM   1220 C CA  . TRP B 2 32  ? 11.223  -10.022 22.063  1.00 33.75 ? 32   TRP U CA  1 
ATOM   1221 C C   . TRP B 2 32  ? 11.941  -11.263 22.536  1.00 33.93 ? 32   TRP U C   1 
ATOM   1222 O O   . TRP B 2 32  ? 12.948  -11.684 21.973  1.00 33.44 ? 32   TRP U O   1 
ATOM   1223 C CB  . TRP B 2 32  ? 10.151  -10.346 21.019  1.00 33.83 ? 32   TRP U CB  1 
ATOM   1224 C CG  . TRP B 2 32  ? 9.209   -11.488 21.375  1.00 33.66 ? 32   TRP U CG  1 
ATOM   1225 C CD1 . TRP B 2 32  ? 9.448   -12.827 21.226  1.00 33.08 ? 32   TRP U CD1 1 
ATOM   1226 C CD2 . TRP B 2 32  ? 7.885   -11.377 21.905  1.00 33.60 ? 32   TRP U CD2 1 
ATOM   1227 N NE1 . TRP B 2 32  ? 8.367   -13.551 21.646  1.00 32.99 ? 32   TRP U NE1 1 
ATOM   1228 C CE2 . TRP B 2 32  ? 7.391   -12.688 22.069  1.00 33.83 ? 32   TRP U CE2 1 
ATOM   1229 C CE3 . TRP B 2 32  ? 7.068   -10.295 22.266  1.00 34.90 ? 32   TRP U CE3 1 
ATOM   1230 C CZ2 . TRP B 2 32  ? 6.106   -12.951 22.576  1.00 35.13 ? 32   TRP U CZ2 1 
ATOM   1231 C CZ3 . TRP B 2 32  ? 5.786   -10.553 22.781  1.00 35.52 ? 32   TRP U CZ3 1 
ATOM   1232 C CH2 . TRP B 2 32  ? 5.318   -11.875 22.920  1.00 35.68 ? 32   TRP U CH2 1 
ATOM   1233 N N   . GLN B 2 33  ? 11.422  -11.811 23.612  1.00 34.34 ? 33   GLN U N   1 
ATOM   1234 C CA  . GLN B 2 33  ? 11.859  -13.065 24.117  1.00 35.03 ? 33   GLN U CA  1 
ATOM   1235 C C   . GLN B 2 33  ? 10.869  -13.351 25.206  1.00 35.98 ? 33   GLN U C   1 
ATOM   1236 O O   . GLN B 2 33  ? 10.419  -12.429 25.903  1.00 36.01 ? 33   GLN U O   1 
ATOM   1237 C CB  . GLN B 2 33  ? 13.238  -12.930 24.706  1.00 34.82 ? 33   GLN U CB  1 
ATOM   1238 C CG  . GLN B 2 33  ? 13.854  -14.239 25.074  1.00 35.17 ? 33   GLN U CG  1 
ATOM   1239 C CD  . GLN B 2 33  ? 14.994  -14.076 26.051  1.00 35.54 ? 33   GLN U CD  1 
ATOM   1240 O OE1 . GLN B 2 33  ? 14.999  -13.151 26.873  1.00 34.94 ? 33   GLN U OE1 1 
ATOM   1241 N NE2 . GLN B 2 33  ? 15.971  -14.983 25.976  1.00 35.39 ? 33   GLN U NE2 1 
ATOM   1242 N N   . ASP B 2 34  ? 10.509  -14.627 25.324  1.00 37.16 ? 34   ASP U N   1 
ATOM   1243 C CA  . ASP B 2 34  ? 9.620   -15.131 26.387  1.00 38.24 ? 34   ASP U CA  1 
ATOM   1244 C C   . ASP B 2 34  ? 8.543   -14.094 26.795  1.00 38.47 ? 34   ASP U C   1 
ATOM   1245 O O   . ASP B 2 34  ? 8.474   -13.647 27.949  1.00 38.96 ? 34   ASP U O   1 
ATOM   1246 C CB  . ASP B 2 34  ? 10.451  -15.660 27.582  1.00 38.42 ? 34   ASP U CB  1 
ATOM   1247 C CG  . ASP B 2 34  ? 11.399  -16.840 27.194  1.00 39.56 ? 34   ASP U CG  1 
ATOM   1248 O OD1 . ASP B 2 34  ? 12.431  -16.616 26.511  1.00 39.49 ? 34   ASP U OD1 1 
ATOM   1249 O OD2 . ASP B 2 34  ? 11.124  -17.997 27.604  1.00 41.13 ? 34   ASP U OD2 1 
ATOM   1250 N N   . ASP B 2 35  ? 7.723   -13.724 25.812  1.00 38.44 ? 35   ASP U N   1 
ATOM   1251 C CA  . ASP B 2 35  ? 6.803   -12.588 25.886  1.00 38.68 ? 35   ASP U CA  1 
ATOM   1252 C C   . ASP B 2 35  ? 7.227   -11.374 26.728  1.00 38.11 ? 35   ASP U C   1 
ATOM   1253 O O   . ASP B 2 35  ? 6.461   -10.912 27.586  1.00 38.29 ? 35   ASP U O   1 
ATOM   1254 C CB  . ASP B 2 35  ? 5.388   -13.035 26.265  1.00 39.11 ? 35   ASP U CB  1 
ATOM   1255 C CG  . ASP B 2 35  ? 4.358   -11.891 26.142  1.00 41.59 ? 35   ASP U CG  1 
ATOM   1256 O OD1 . ASP B 2 35  ? 4.510   -11.010 25.249  1.00 43.95 ? 35   ASP U OD1 1 
ATOM   1257 O OD2 . ASP B 2 35  ? 3.403   -11.858 26.953  1.00 43.65 ? 35   ASP U OD2 1 
ATOM   1258 N N   . ARG B 2 36  ? 8.434   -10.861 26.492  1.00 37.25 ? 36   ARG U N   1 
ATOM   1259 C CA  . ARG B 2 36  ? 8.815   -9.561  27.052  1.00 36.48 ? 36   ARG U CA  1 
ATOM   1260 C C   . ARG B 2 36  ? 9.371   -8.704  25.932  1.00 36.53 ? 36   ARG U C   1 
ATOM   1261 O O   . ARG B 2 36  ? 10.535  -8.906  25.539  1.00 37.01 ? 36   ARG U O   1 
ATOM   1262 C CB  . ARG B 2 36  ? 9.884   -9.657  28.151  1.00 35.93 ? 36   ARG U CB  1 
ATOM   1263 C CG  . ARG B 2 36  ? 9.849   -10.862 29.054  1.00 34.77 ? 36   ARG U CG  1 
ATOM   1264 C CD  . ARG B 2 36  ? 10.878  -10.731 30.179  1.00 31.94 ? 36   ARG U CD  1 
ATOM   1265 N NE  . ARG B 2 36  ? 12.202  -10.309 29.717  1.00 29.49 ? 36   ARG U NE  1 
ATOM   1266 C CZ  . ARG B 2 36  ? 13.158  -11.127 29.271  1.00 28.64 ? 36   ARG U CZ  1 
ATOM   1267 N NH1 . ARG B 2 36  ? 12.969  -12.450 29.203  1.00 27.40 ? 36   ARG U NH1 1 
ATOM   1268 N NH2 . ARG B 2 36  ? 14.316  -10.611 28.880  1.00 27.73 ? 36   ARG U NH2 1 
ATOM   1269 N N   . GLU B 2 37  ? 8.560   -7.771  25.406  1.00 35.94 ? 37   GLU U N   1 
ATOM   1270 C CA  . GLU B 2 37  ? 9.065   -6.778  24.435  1.00 35.18 ? 37   GLU U CA  1 
ATOM   1271 C C   . GLU B 2 37  ? 9.596   -5.577  25.198  1.00 34.05 ? 37   GLU U C   1 
ATOM   1272 O O   . GLU B 2 37  ? 8.940   -5.058  26.098  1.00 33.94 ? 37   GLU U O   1 
ATOM   1273 C CB  . GLU B 2 37  ? 8.055   -6.424  23.306  1.00 35.35 ? 37   GLU U CB  1 
ATOM   1274 C CG  . GLU B 2 37  ? 7.232   -5.104  23.417  1.00 38.15 ? 37   GLU U CG  1 
ATOM   1275 C CD  . GLU B 2 37  ? 7.094   -4.321  22.061  1.00 42.02 ? 37   GLU U CD  1 
ATOM   1276 O OE1 . GLU B 2 37  ? 5.939   -3.985  21.665  1.00 42.37 ? 37   GLU U OE1 1 
ATOM   1277 O OE2 . GLU B 2 37  ? 8.139   -4.030  21.401  1.00 42.18 ? 37   GLU U OE2 1 
ATOM   1278 N N   . LEU B 2 38  ? 10.821  -5.198  24.880  1.00 32.85 ? 38   LEU U N   1 
ATOM   1279 C CA  . LEU B 2 38  ? 11.440  -4.047  25.472  1.00 32.27 ? 38   LEU U CA  1 
ATOM   1280 C C   . LEU B 2 38  ? 11.975  -3.271  24.301  1.00 32.09 ? 38   LEU U C   1 
ATOM   1281 O O   . LEU B 2 38  ? 12.755  -3.823  23.517  1.00 32.00 ? 38   LEU U O   1 
ATOM   1282 C CB  . LEU B 2 38  ? 12.603  -4.471  26.379  1.00 32.49 ? 38   LEU U CB  1 
ATOM   1283 C CG  . LEU B 2 38  ? 13.793  -3.488  26.514  1.00 32.01 ? 38   LEU U CG  1 
ATOM   1284 C CD1 . LEU B 2 38  ? 13.596  -2.473  27.660  1.00 30.94 ? 38   LEU U CD1 1 
ATOM   1285 C CD2 . LEU B 2 38  ? 15.126  -4.184  26.633  1.00 29.87 ? 38   LEU U CD2 1 
ATOM   1286 N N   . GLU B 2 39  ? 11.592  -1.996  24.194  1.00 31.62 ? 39   GLU U N   1 
ATOM   1287 C CA  . GLU B 2 39  ? 11.969  -1.183  23.030  1.00 31.40 ? 39   GLU U CA  1 
ATOM   1288 C C   . GLU B 2 39  ? 12.592  0.187   23.344  1.00 30.22 ? 39   GLU U C   1 
ATOM   1289 O O   . GLU B 2 39  ? 12.037  0.962   24.108  1.00 30.32 ? 39   GLU U O   1 
ATOM   1290 C CB  . GLU B 2 39  ? 10.774  -1.094  22.082  1.00 31.90 ? 39   GLU U CB  1 
ATOM   1291 C CG  . GLU B 2 39  ? 10.450  0.263   21.557  1.00 35.50 ? 39   GLU U CG  1 
ATOM   1292 C CD  . GLU B 2 39  ? 9.020   0.647   21.924  1.00 41.71 ? 39   GLU U CD  1 
ATOM   1293 O OE1 . GLU B 2 39  ? 8.791   1.133   23.075  1.00 43.21 ? 39   GLU U OE1 1 
ATOM   1294 O OE2 . GLU B 2 39  ? 8.122   0.450   21.063  1.00 44.43 ? 39   GLU U OE2 1 
ATOM   1295 N N   . VAL B 2 40  ? 13.751  0.462   22.749  1.00 29.10 ? 40   VAL U N   1 
ATOM   1296 C CA  . VAL B 2 40  ? 14.511  1.699   22.981  1.00 28.22 ? 40   VAL U CA  1 
ATOM   1297 C C   . VAL B 2 40  ? 14.702  2.558   21.722  1.00 27.96 ? 40   VAL U C   1 
ATOM   1298 O O   . VAL B 2 40  ? 15.365  2.159   20.758  1.00 28.11 ? 40   VAL U O   1 
ATOM   1299 C CB  . VAL B 2 40  ? 15.877  1.468   23.763  1.00 28.24 ? 40   VAL U CB  1 
ATOM   1300 C CG1 . VAL B 2 40  ? 16.329  0.032   23.706  1.00 28.58 ? 40   VAL U CG1 1 
ATOM   1301 C CG2 . VAL B 2 40  ? 16.994  2.391   23.282  1.00 27.18 ? 40   VAL U CG2 1 
ATOM   1302 N N   . VAL B 2 41  ? 14.112  3.752   21.775  1.00 27.49 ? 41   VAL U N   1 
ATOM   1303 C CA  . VAL B 2 41  ? 14.113  4.750   20.711  1.00 26.83 ? 41   VAL U CA  1 
ATOM   1304 C C   . VAL B 2 41  ? 15.125  5.868   20.985  1.00 26.21 ? 41   VAL U C   1 
ATOM   1305 O O   . VAL B 2 41  ? 15.247  6.315   22.109  1.00 26.57 ? 41   VAL U O   1 
ATOM   1306 C CB  . VAL B 2 41  ? 12.736  5.425   20.646  1.00 26.85 ? 41   VAL U CB  1 
ATOM   1307 C CG1 . VAL B 2 41  ? 12.651  6.364   19.431  1.00 28.17 ? 41   VAL U CG1 1 
ATOM   1308 C CG2 . VAL B 2 41  ? 11.615  4.383   20.625  1.00 26.63 ? 41   VAL U CG2 1 
ATOM   1309 N N   . THR B 2 42  ? 15.858  6.303   19.972  1.00 25.53 ? 42   THR U N   1 
ATOM   1310 C CA  . THR B 2 42  ? 16.601  7.534   20.070  1.00 25.59 ? 42   THR U CA  1 
ATOM   1311 C C   . THR B 2 42  ? 16.312  8.380   18.850  1.00 26.21 ? 42   THR U C   1 
ATOM   1312 O O   . THR B 2 42  ? 16.211  7.871   17.749  1.00 26.51 ? 42   THR U O   1 
ATOM   1313 C CB  . THR B 2 42  ? 18.134  7.355   20.233  1.00 25.45 ? 42   THR U CB  1 
ATOM   1314 O OG1 . THR B 2 42  ? 18.685  6.671   19.107  1.00 25.18 ? 42   THR U OG1 1 
ATOM   1315 C CG2 . THR B 2 42  ? 18.481  6.607   21.496  1.00 25.60 ? 42   THR U CG2 1 
ATOM   1316 N N   . ARG B 2 43  ? 16.184  9.684   19.066  1.00 27.07 ? 43   ARG U N   1 
ATOM   1317 C CA  . ARG B 2 43  ? 15.899  10.651  18.017  1.00 27.54 ? 43   ARG U CA  1 
ATOM   1318 C C   . ARG B 2 43  ? 16.928  11.788  18.036  1.00 28.22 ? 43   ARG U C   1 
ATOM   1319 O O   . ARG B 2 43  ? 17.622  11.981  19.023  1.00 28.18 ? 43   ARG U O   1 
ATOM   1320 C CB  . ARG B 2 43  ? 14.501  11.227  18.199  1.00 27.12 ? 43   ARG U CB  1 
ATOM   1321 C CG  . ARG B 2 43  ? 13.498  10.242  18.627  1.00 26.34 ? 43   ARG U CG  1 
ATOM   1322 C CD  . ARG B 2 43  ? 12.399  10.981  19.269  1.00 27.01 ? 43   ARG U CD  1 
ATOM   1323 N NE  . ARG B 2 43  ? 11.131  10.602  18.678  1.00 29.41 ? 43   ARG U NE  1 
ATOM   1324 C CZ  . ARG B 2 43  ? 10.251  9.789   19.246  1.00 29.72 ? 43   ARG U CZ  1 
ATOM   1325 N NH1 . ARG B 2 43  ? 10.483  9.279   20.443  1.00 29.53 ? 43   ARG U NH1 1 
ATOM   1326 N NH2 . ARG B 2 43  ? 9.122   9.508   18.617  1.00 31.18 ? 43   ARG U NH2 1 
ATOM   1327 N N   . GLY B 2 44  ? 17.022  12.524  16.938  1.00 29.08 ? 44   GLY U N   1 
ATOM   1328 C CA  . GLY B 2 44  ? 17.967  13.609  16.833  1.00 30.78 ? 44   GLY U CA  1 
ATOM   1329 C C   . GLY B 2 44  ? 18.048  13.982  15.384  1.00 32.08 ? 44   GLY U C   1 
ATOM   1330 O O   . GLY B 2 44  ? 17.326  13.384  14.581  1.00 32.32 ? 44   GLY U O   1 
ATOM   1331 N N   . CYS B 2 45  ? 18.885  14.980  15.056  1.00 33.22 ? 45   CYS U N   1 
ATOM   1332 C CA  . CYS B 2 45  ? 19.142  15.356  13.656  1.00 34.69 ? 45   CYS U CA  1 
ATOM   1333 C C   . CYS B 2 45  ? 19.922  14.256  13.006  1.00 34.72 ? 45   CYS U C   1 
ATOM   1334 O O   . CYS B 2 45  ? 20.798  13.666  13.644  1.00 34.80 ? 45   CYS U O   1 
ATOM   1335 C CB  . CYS B 2 45  ? 19.921  16.669  13.508  1.00 34.60 ? 45   CYS U CB  1 
ATOM   1336 S SG  . CYS B 2 45  ? 18.958  18.185  13.899  1.00 39.32 ? 45   CYS U SG  1 
ATOM   1337 N N   . ALA B 2 46  ? 19.578  13.974  11.751  1.00 35.22 ? 46   ALA U N   1 
ATOM   1338 C CA  . ALA B 2 46  ? 20.270  12.971  10.969  1.00 36.10 ? 46   ALA U CA  1 
ATOM   1339 C C   . ALA B 2 46  ? 21.389  13.602  10.158  1.00 36.92 ? 46   ALA U C   1 
ATOM   1340 O O   . ALA B 2 46  ? 22.337  14.184  10.709  1.00 36.71 ? 46   ALA U O   1 
ATOM   1341 C CB  . ALA B 2 46  ? 19.312  12.262  10.072  1.00 35.89 ? 46   ALA U CB  1 
ATOM   1342 N N   . HIS B 2 47  ? 21.274  13.488  8.843   1.00 38.11 ? 47   HIS U N   1 
ATOM   1343 C CA  . HIS B 2 47  ? 22.279  14.054  7.973   1.00 39.25 ? 47   HIS U CA  1 
ATOM   1344 C C   . HIS B 2 47  ? 21.955  14.000  6.513   1.00 38.98 ? 47   HIS U C   1 
ATOM   1345 O O   . HIS B 2 47  ? 20.968  13.385  6.099   1.00 39.03 ? 47   HIS U O   1 
ATOM   1346 C CB  . HIS B 2 47  ? 23.629  13.390  8.198   1.00 39.96 ? 47   HIS U CB  1 
ATOM   1347 C CG  . HIS B 2 47  ? 24.598  14.265  8.918   1.00 42.64 ? 47   HIS U CG  1 
ATOM   1348 N ND1 . HIS B 2 47  ? 24.901  15.542  8.487   1.00 44.79 ? 47   HIS U ND1 1 
ATOM   1349 C CD2 . HIS B 2 47  ? 25.339  14.053  10.031  1.00 44.75 ? 47   HIS U CD2 1 
ATOM   1350 C CE1 . HIS B 2 47  ? 25.792  16.077  9.303   1.00 45.95 ? 47   HIS U CE1 1 
ATOM   1351 N NE2 . HIS B 2 47  ? 26.074  15.196  10.248  1.00 46.51 ? 47   HIS U NE2 1 
ATOM   1352 N N   . SER B 2 48  ? 22.835  14.651  5.754   1.00 38.73 ? 48   SER U N   1 
ATOM   1353 C CA  . SER B 2 48  ? 22.737  14.800  4.304   1.00 38.45 ? 48   SER U CA  1 
ATOM   1354 C C   . SER B 2 48  ? 22.127  13.564  3.641   1.00 38.09 ? 48   SER U C   1 
ATOM   1355 O O   . SER B 2 48  ? 21.085  13.643  2.995   1.00 37.09 ? 48   SER U O   1 
ATOM   1356 C CB  . SER B 2 48  ? 24.135  15.105  3.712   1.00 38.75 ? 48   SER U CB  1 
ATOM   1357 O OG  . SER B 2 48  ? 24.854  16.093  4.453   1.00 37.88 ? 48   SER U OG  1 
ATOM   1358 N N   . GLU B 2 49  ? 22.779  12.422  3.848   1.00 38.36 ? 49   GLU U N   1 
ATOM   1359 C CA  . GLU B 2 49  ? 22.409  11.196  3.163   1.00 38.83 ? 49   GLU U CA  1 
ATOM   1360 C C   . GLU B 2 49  ? 22.394  9.944   4.069   1.00 38.42 ? 49   GLU U C   1 
ATOM   1361 O O   . GLU B 2 49  ? 23.406  9.249   4.205   1.00 38.41 ? 49   GLU U O   1 
ATOM   1362 C CB  . GLU B 2 49  ? 23.331  10.972  1.948   1.00 39.37 ? 49   GLU U CB  1 
ATOM   1363 C CG  . GLU B 2 49  ? 23.975  12.249  1.336   1.00 40.92 ? 49   GLU U CG  1 
ATOM   1364 C CD  . GLU B 2 49  ? 23.081  13.006  0.336   1.00 42.59 ? 49   GLU U CD  1 
ATOM   1365 O OE1 . GLU B 2 49  ? 23.283  14.239  0.182   1.00 42.96 ? 49   GLU U OE1 1 
ATOM   1366 O OE2 . GLU B 2 49  ? 22.199  12.379  -0.302  1.00 42.28 ? 49   GLU U OE2 1 
ATOM   1367 N N   . LYS B 2 50  ? 21.243  9.687   4.694   1.00 37.89 ? 50   LYS U N   1 
ATOM   1368 C CA  . LYS B 2 50  ? 20.941  8.406   5.351   1.00 37.44 ? 50   LYS U CA  1 
ATOM   1369 C C   . LYS B 2 50  ? 19.577  7.981   4.845   1.00 37.48 ? 50   LYS U C   1 
ATOM   1370 O O   . LYS B 2 50  ? 18.815  8.823   4.349   1.00 37.81 ? 50   LYS U O   1 
ATOM   1371 C CB  . LYS B 2 50  ? 20.919  8.496   6.884   1.00 37.24 ? 50   LYS U CB  1 
ATOM   1372 C CG  . LYS B 2 50  ? 22.201  9.069   7.527   1.00 36.90 ? 50   LYS U CG  1 
ATOM   1373 C CD  . LYS B 2 50  ? 22.702  8.286   8.744   1.00 33.77 ? 50   LYS U CD  1 
ATOM   1374 C CE  . LYS B 2 50  ? 21.644  8.135   9.813   1.00 33.70 ? 50   LYS U CE  1 
ATOM   1375 N NZ  . LYS B 2 50  ? 21.862  6.874   10.589  1.00 33.34 ? 50   LYS U NZ  1 
ATOM   1376 N N   . THR B 2 51  ? 19.268  6.688   5.002   1.00 37.10 ? 51   THR U N   1 
ATOM   1377 C CA  . THR B 2 51  ? 18.214  5.978   4.235   1.00 36.21 ? 51   THR U CA  1 
ATOM   1378 C C   . THR B 2 51  ? 17.278  5.178   5.137   1.00 35.87 ? 51   THR U C   1 
ATOM   1379 O O   . THR B 2 51  ? 17.748  4.414   5.977   1.00 36.03 ? 51   THR U O   1 
ATOM   1380 C CB  . THR B 2 51  ? 18.850  4.939   3.246   1.00 36.17 ? 51   THR U CB  1 
ATOM   1381 O OG1 . THR B 2 51  ? 18.705  3.601   3.761   1.00 35.27 ? 51   THR U OG1 1 
ATOM   1382 C CG2 . THR B 2 51  ? 20.345  5.236   2.990   1.00 35.45 ? 51   THR U CG2 1 
ATOM   1383 N N   . ASN B 2 52  ? 15.969  5.306   4.958   1.00 35.27 ? 52   ASN U N   1 
ATOM   1384 C CA  . ASN B 2 52  ? 15.077  4.473   5.749   1.00 35.36 ? 52   ASN U CA  1 
ATOM   1385 C C   . ASN B 2 52  ? 15.563  3.030   5.742   1.00 34.34 ? 52   ASN U C   1 
ATOM   1386 O O   . ASN B 2 52  ? 15.471  2.353   4.734   1.00 34.70 ? 52   ASN U O   1 
ATOM   1387 C CB  . ASN B 2 52  ? 13.598  4.681   5.377   1.00 35.77 ? 52   ASN U CB  1 
ATOM   1388 C CG  . ASN B 2 52  ? 13.178  6.104   5.625   1.00 40.38 ? 52   ASN U CG  1 
ATOM   1389 O OD1 . ASN B 2 52  ? 13.936  6.840   6.211   1.00 44.25 ? 52   ASN U OD1 1 
ATOM   1390 N ND2 . ASN B 2 52  ? 12.026  6.517   5.196   1.00 48.08 ? 52   ASN U ND2 1 
ATOM   1391 N N   . ARG B 2 53  ? 16.155  2.595   6.857   1.00 33.34 ? 53   ARG U N   1 
ATOM   1392 C CA  . ARG B 2 53  ? 16.784  1.277   6.933   1.00 32.29 ? 53   ARG U CA  1 
ATOM   1393 C C   . ARG B 2 53  ? 16.238  0.384   8.025   1.00 32.22 ? 53   ARG U C   1 
ATOM   1394 O O   . ARG B 2 53  ? 15.710  0.873   9.012   1.00 32.36 ? 53   ARG U O   1 
ATOM   1395 C CB  . ARG B 2 53  ? 18.291  1.397   7.070   1.00 31.64 ? 53   ARG U CB  1 
ATOM   1396 C CG  . ARG B 2 53  ? 18.736  1.921   8.372   1.00 30.62 ? 53   ARG U CG  1 
ATOM   1397 C CD  . ARG B 2 53  ? 20.211  2.229   8.327   1.00 29.06 ? 53   ARG U CD  1 
ATOM   1398 N NE  . ARG B 2 53  ? 20.529  3.249   7.326   1.00 26.05 ? 53   ARG U NE  1 
ATOM   1399 C CZ  . ARG B 2 53  ? 21.703  3.858   7.230   1.00 24.34 ? 53   ARG U CZ  1 
ATOM   1400 N NH1 . ARG B 2 53  ? 22.670  3.576   8.074   1.00 24.99 ? 53   ARG U NH1 1 
ATOM   1401 N NH2 . ARG B 2 53  ? 21.917  4.759   6.298   1.00 25.28 ? 53   ARG U NH2 1 
ATOM   1402 N N   . THR B 2 54  ? 16.409  -0.928  7.833   1.00 32.30 ? 54   THR U N   1 
ATOM   1403 C CA  . THR B 2 54  ? 15.846  -1.997  8.682   1.00 32.24 ? 54   THR U CA  1 
ATOM   1404 C C   . THR B 2 54  ? 16.757  -3.218  8.816   1.00 32.49 ? 54   THR U C   1 
ATOM   1405 O O   . THR B 2 54  ? 17.396  -3.610  7.852   1.00 32.75 ? 54   THR U O   1 
ATOM   1406 C CB  . THR B 2 54  ? 14.533  -2.453  8.106   1.00 31.93 ? 54   THR U CB  1 
ATOM   1407 O OG1 . THR B 2 54  ? 13.563  -1.443  8.391   1.00 32.63 ? 54   THR U OG1 1 
ATOM   1408 C CG2 . THR B 2 54  ? 14.092  -3.792  8.692   1.00 31.82 ? 54   THR U CG2 1 
ATOM   1409 N N   . MET B 2 55  ? 16.814  -3.807  10.013  1.00 32.86 ? 55   MET U N   1 
ATOM   1410 C CA  . MET B 2 55  ? 17.630  -4.993  10.283  1.00 33.12 ? 55   MET U CA  1 
ATOM   1411 C C   . MET B 2 55  ? 16.986  -5.758  11.389  1.00 32.83 ? 55   MET U C   1 
ATOM   1412 O O   . MET B 2 55  ? 16.393  -5.165  12.267  1.00 33.08 ? 55   MET U O   1 
ATOM   1413 C CB  . MET B 2 55  ? 19.055  -4.596  10.680  1.00 33.61 ? 55   MET U CB  1 
ATOM   1414 C CG  . MET B 2 55  ? 19.819  -5.584  11.579  1.00 35.65 ? 55   MET U CG  1 
ATOM   1415 S SD  . MET B 2 55  ? 21.649  -5.620  11.324  1.00 41.81 ? 55   MET U SD  1 
ATOM   1416 C CE  . MET B 2 55  ? 22.255  -3.982  11.770  1.00 39.56 ? 55   MET U CE  1 
ATOM   1417 N N   . SER B 2 56  ? 17.069  -7.079  11.328  1.00 33.04 ? 56   SER U N   1 
ATOM   1418 C CA  . SER B 2 56  ? 16.665  -7.945  12.451  1.00 33.08 ? 56   SER U CA  1 
ATOM   1419 C C   . SER B 2 56  ? 17.356  -9.287  12.373  1.00 32.72 ? 56   SER U C   1 
ATOM   1420 O O   . SER B 2 56  ? 17.669  -9.772  11.295  1.00 32.81 ? 56   SER U O   1 
ATOM   1421 C CB  . SER B 2 56  ? 15.143  -8.132  12.546  1.00 32.95 ? 56   SER U CB  1 
ATOM   1422 O OG  . SER B 2 56  ? 14.602  -8.533  11.305  1.00 33.57 ? 56   SER U OG  1 
ATOM   1423 N N   . TYR B 2 57  ? 17.606  -9.864  13.538  1.00 32.64 ? 57   TYR U N   1 
ATOM   1424 C CA  . TYR B 2 57  ? 18.253  -11.166 13.654  1.00 32.53 ? 57   TYR U CA  1 
ATOM   1425 C C   . TYR B 2 57  ? 17.896  -11.803 14.996  1.00 32.46 ? 57   TYR U C   1 
ATOM   1426 O O   . TYR B 2 57  ? 17.236  -11.174 15.834  1.00 32.45 ? 57   TYR U O   1 
ATOM   1427 C CB  . TYR B 2 57  ? 19.769  -11.040 13.482  1.00 32.30 ? 57   TYR U CB  1 
ATOM   1428 C CG  . TYR B 2 57  ? 20.513  -10.494 14.673  1.00 32.40 ? 57   TYR U CG  1 
ATOM   1429 C CD1 . TYR B 2 57  ? 21.657  -11.131 15.144  1.00 32.63 ? 57   TYR U CD1 1 
ATOM   1430 C CD2 . TYR B 2 57  ? 20.089  -9.340  15.324  1.00 32.84 ? 57   TYR U CD2 1 
ATOM   1431 C CE1 . TYR B 2 57  ? 22.366  -10.637 16.229  1.00 33.41 ? 57   TYR U CE1 1 
ATOM   1432 C CE2 . TYR B 2 57  ? 20.787  -8.839  16.418  1.00 34.14 ? 57   TYR U CE2 1 
ATOM   1433 C CZ  . TYR B 2 57  ? 21.928  -9.490  16.867  1.00 34.08 ? 57   TYR U CZ  1 
ATOM   1434 O OH  . TYR B 2 57  ? 22.616  -8.996  17.954  1.00 33.31 ? 57   TYR U OH  1 
ATOM   1435 N N   . ARG B 2 58  ? 18.298  -13.054 15.193  1.00 32.21 ? 58   ARG U N   1 
ATOM   1436 C CA  . ARG B 2 58  ? 18.122  -13.649 16.504  1.00 31.88 ? 58   ARG U CA  1 
ATOM   1437 C C   . ARG B 2 58  ? 19.375  -14.216 17.135  1.00 31.72 ? 58   ARG U C   1 
ATOM   1438 O O   . ARG B 2 58  ? 20.180  -14.905 16.510  1.00 31.94 ? 58   ARG U O   1 
ATOM   1439 C CB  . ARG B 2 58  ? 16.940  -14.621 16.585  1.00 31.98 ? 58   ARG U CB  1 
ATOM   1440 C CG  . ARG B 2 58  ? 16.606  -15.492 15.379  1.00 32.82 ? 58   ARG U CG  1 
ATOM   1441 C CD  . ARG B 2 58  ? 15.668  -16.600 15.892  1.00 34.88 ? 58   ARG U CD  1 
ATOM   1442 N NE  . ARG B 2 58  ? 14.907  -17.294 14.854  1.00 35.53 ? 58   ARG U NE  1 
ATOM   1443 C CZ  . ARG B 2 58  ? 14.337  -18.485 15.020  1.00 35.05 ? 58   ARG U CZ  1 
ATOM   1444 N NH1 . ARG B 2 58  ? 14.445  -19.131 16.178  1.00 33.94 ? 58   ARG U NH1 1 
ATOM   1445 N NH2 . ARG B 2 58  ? 13.669  -19.037 14.020  1.00 35.22 ? 58   ARG U NH2 1 
ATOM   1446 N N   . MET B 2 59  ? 19.529  -13.868 18.397  1.00 31.73 ? 59   MET U N   1 
ATOM   1447 C CA  . MET B 2 59  ? 20.559  -14.398 19.255  1.00 31.81 ? 59   MET U CA  1 
ATOM   1448 C C   . MET B 2 59  ? 19.809  -15.281 20.252  1.00 31.26 ? 59   MET U C   1 
ATOM   1449 O O   . MET B 2 59  ? 18.801  -14.856 20.827  1.00 31.17 ? 59   MET U O   1 
ATOM   1450 C CB  . MET B 2 59  ? 21.272  -13.228 19.941  1.00 31.90 ? 59   MET U CB  1 
ATOM   1451 C CG  . MET B 2 59  ? 22.258  -13.610 21.015  1.00 34.19 ? 59   MET U CG  1 
ATOM   1452 S SD  . MET B 2 59  ? 23.283  -12.238 21.624  1.00 38.99 ? 59   MET U SD  1 
ATOM   1453 C CE  . MET B 2 59  ? 24.500  -13.196 22.555  1.00 38.74 ? 59   MET U CE  1 
ATOM   1454 N N   . GLY B 2 60  ? 20.263  -16.513 20.433  1.00 30.71 ? 60   GLY U N   1 
ATOM   1455 C CA  . GLY B 2 60  ? 19.572  -17.423 21.329  1.00 30.84 ? 60   GLY U CA  1 
ATOM   1456 C C   . GLY B 2 60  ? 18.070  -17.390 21.107  1.00 31.18 ? 60   GLY U C   1 
ATOM   1457 O O   . GLY B 2 60  ? 17.605  -17.333 19.970  1.00 31.38 ? 60   GLY U O   1 
ATOM   1458 N N   . SER B 2 61  ? 17.308  -17.394 22.197  1.00 31.48 ? 61   SER U N   1 
ATOM   1459 C CA  . SER B 2 61  ? 15.845  -17.476 22.136  1.00 31.46 ? 61   SER U CA  1 
ATOM   1460 C C   . SER B 2 61  ? 15.137  -16.153 21.876  1.00 31.32 ? 61   SER U C   1 
ATOM   1461 O O   . SER B 2 61  ? 13.925  -16.082 22.064  1.00 30.80 ? 61   SER U O   1 
ATOM   1462 C CB  . SER B 2 61  ? 15.320  -18.007 23.461  1.00 31.77 ? 61   SER U CB  1 
ATOM   1463 O OG  . SER B 2 61  ? 15.294  -16.965 24.431  1.00 32.42 ? 61   SER U OG  1 
ATOM   1464 N N   . MET B 2 62  ? 15.885  -15.114 21.482  1.00 31.72 ? 62   MET U N   1 
ATOM   1465 C CA  . MET B 2 62  ? 15.322  -13.759 21.255  1.00 32.26 ? 62   MET U CA  1 
ATOM   1466 C C   . MET B 2 62  ? 15.488  -13.195 19.826  1.00 31.57 ? 62   MET U C   1 
ATOM   1467 O O   . MET B 2 62  ? 16.328  -13.667 19.069  1.00 31.77 ? 62   MET U O   1 
ATOM   1468 C CB  . MET B 2 62  ? 15.819  -12.745 22.317  1.00 32.76 ? 62   MET U CB  1 
ATOM   1469 C CG  . MET B 2 62  ? 17.232  -12.151 22.139  1.00 35.20 ? 62   MET U CG  1 
ATOM   1470 S SD  . MET B 2 62  ? 17.381  -10.352 22.570  1.00 41.54 ? 62   MET U SD  1 
ATOM   1471 C CE  . MET B 2 62  ? 16.658  -10.241 24.227  1.00 41.59 ? 62   MET U CE  1 
ATOM   1472 N N   . ILE B 2 63  ? 14.675  -12.201 19.466  1.00 30.68 ? 63   ILE U N   1 
ATOM   1473 C CA  . ILE B 2 63  ? 14.844  -11.493 18.201  1.00 30.13 ? 63   ILE U CA  1 
ATOM   1474 C C   . ILE B 2 63  ? 14.979  -10.026 18.490  1.00 29.90 ? 63   ILE U C   1 
ATOM   1475 O O   . ILE B 2 63  ? 14.096  -9.423  19.109  1.00 30.08 ? 63   ILE U O   1 
ATOM   1476 C CB  . ILE B 2 63  ? 13.611  -11.554 17.302  1.00 30.24 ? 63   ILE U CB  1 
ATOM   1477 C CG1 . ILE B 2 63  ? 12.759  -12.775 17.621  1.00 31.42 ? 63   ILE U CG1 1 
ATOM   1478 C CG2 . ILE B 2 63  ? 14.006  -11.453 15.838  1.00 28.93 ? 63   ILE U CG2 1 
ATOM   1479 C CD1 . ILE B 2 63  ? 11.343  -12.395 17.964  1.00 33.43 ? 63   ILE U CD1 1 
ATOM   1480 N N   . ILE B 2 64  ? 16.065  -9.439  18.018  1.00 29.37 ? 64   ILE U N   1 
ATOM   1481 C CA  . ILE B 2 64  ? 16.209  -8.017  18.104  1.00 29.13 ? 64   ILE U CA  1 
ATOM   1482 C C   . ILE B 2 64  ? 15.855  -7.466  16.723  1.00 29.42 ? 64   ILE U C   1 
ATOM   1483 O O   . ILE B 2 64  ? 16.249  -8.037  15.702  1.00 29.83 ? 64   ILE U O   1 
ATOM   1484 C CB  . ILE B 2 64  ? 17.629  -7.613  18.572  1.00 29.05 ? 64   ILE U CB  1 
ATOM   1485 C CG1 . ILE B 2 64  ? 18.413  -6.938  17.459  1.00 29.99 ? 64   ILE U CG1 1 
ATOM   1486 C CG2 . ILE B 2 64  ? 18.409  -8.796  19.141  1.00 28.59 ? 64   ILE U CG2 1 
ATOM   1487 C CD1 . ILE B 2 64  ? 18.065  -5.478  17.288  1.00 31.87 ? 64   ILE U CD1 1 
ATOM   1488 N N   . SER B 2 65  ? 15.096  -6.374  16.680  1.00 29.46 ? 65   SER U N   1 
ATOM   1489 C CA  . SER B 2 65  ? 14.731  -5.750  15.403  1.00 28.98 ? 65   SER U CA  1 
ATOM   1490 C C   . SER B 2 65  ? 14.954  -4.235  15.365  1.00 28.53 ? 65   SER U C   1 
ATOM   1491 O O   . SER B 2 65  ? 14.066  -3.448  15.739  1.00 27.84 ? 65   SER U O   1 
ATOM   1492 C CB  . SER B 2 65  ? 13.281  -6.067  15.066  1.00 29.27 ? 65   SER U CB  1 
ATOM   1493 O OG  . SER B 2 65  ? 12.414  -5.328  15.909  1.00 30.32 ? 65   SER U OG  1 
ATOM   1494 N N   . LEU B 2 66  ? 16.147  -3.857  14.905  1.00 28.16 ? 66   LEU U N   1 
ATOM   1495 C CA  . LEU B 2 66  ? 16.504  -2.480  14.571  1.00 28.33 ? 66   LEU U CA  1 
ATOM   1496 C C   . LEU B 2 66  ? 15.766  -1.910  13.310  1.00 29.00 ? 66   LEU U C   1 
ATOM   1497 O O   . LEU B 2 66  ? 15.524  -2.606  12.318  1.00 28.80 ? 66   LEU U O   1 
ATOM   1498 C CB  . LEU B 2 66  ? 18.019  -2.402  14.378  1.00 28.08 ? 66   LEU U CB  1 
ATOM   1499 C CG  . LEU B 2 66  ? 18.979  -3.034  15.404  1.00 27.79 ? 66   LEU U CG  1 
ATOM   1500 C CD1 . LEU B 2 66  ? 20.200  -3.698  14.830  1.00 26.29 ? 66   LEU U CD1 1 
ATOM   1501 C CD2 . LEU B 2 66  ? 19.462  -2.021  16.365  1.00 29.91 ? 66   LEU U CD2 1 
ATOM   1502 N N   . THR B 2 67  ? 15.379  -0.640  13.387  1.00 29.91 ? 67   THR U N   1 
ATOM   1503 C CA  . THR B 2 67  ? 14.757  0.094   12.276  1.00 30.72 ? 67   THR U CA  1 
ATOM   1504 C C   . THR B 2 67  ? 15.146  1.564   12.399  1.00 31.61 ? 67   THR U C   1 
ATOM   1505 O O   . THR B 2 67  ? 15.219  2.093   13.513  1.00 32.02 ? 67   THR U O   1 
ATOM   1506 C CB  . THR B 2 67  ? 13.185  0.069   12.269  1.00 30.75 ? 67   THR U CB  1 
ATOM   1507 O OG1 . THR B 2 67  ? 12.674  1.282   12.849  1.00 29.87 ? 67   THR U OG1 1 
ATOM   1508 C CG2 . THR B 2 67  ? 12.585  -1.169  12.961  1.00 30.51 ? 67   THR U CG2 1 
ATOM   1509 N N   . GLU B 2 68  ? 15.373  2.225   11.266  1.00 32.33 ? 68   GLU U N   1 
ATOM   1510 C CA  . GLU B 2 68  ? 15.662  3.658   11.266  1.00 33.04 ? 68   GLU U CA  1 
ATOM   1511 C C   . GLU B 2 68  ? 14.782  4.406   10.263  1.00 32.89 ? 68   GLU U C   1 
ATOM   1512 O O   . GLU B 2 68  ? 14.516  3.902   9.181   1.00 33.00 ? 68   GLU U O   1 
ATOM   1513 C CB  . GLU B 2 68  ? 17.141  3.906   10.993  1.00 33.11 ? 68   GLU U CB  1 
ATOM   1514 C CG  . GLU B 2 68  ? 17.702  5.056   11.810  1.00 34.80 ? 68   GLU U CG  1 
ATOM   1515 C CD  . GLU B 2 68  ? 19.233  5.113   11.791  1.00 37.61 ? 68   GLU U CD  1 
ATOM   1516 O OE1 . GLU B 2 68  ? 19.846  4.855   12.860  1.00 38.83 ? 68   GLU U OE1 1 
ATOM   1517 O OE2 . GLU B 2 68  ? 19.823  5.418   10.720  1.00 37.11 ? 68   GLU U OE2 1 
ATOM   1518 N N   . THR B 2 69  ? 14.330  5.603   10.635  1.00 32.73 ? 69   THR U N   1 
ATOM   1519 C CA  . THR B 2 69  ? 13.386  6.358   9.823   1.00 32.25 ? 69   THR U CA  1 
ATOM   1520 C C   . THR B 2 69  ? 13.676  7.837   9.847   1.00 32.01 ? 69   THR U C   1 
ATOM   1521 O O   . THR B 2 69  ? 13.789  8.438   10.904  1.00 32.06 ? 69   THR U O   1 
ATOM   1522 C CB  . THR B 2 69  ? 11.946  6.108   10.261  1.00 32.13 ? 69   THR U CB  1 
ATOM   1523 O OG1 . THR B 2 69  ? 11.463  4.945   9.588   1.00 32.61 ? 69   THR U OG1 1 
ATOM   1524 C CG2 . THR B 2 69  ? 11.057  7.272   9.888   1.00 33.03 ? 69   THR U CG2 1 
ATOM   1525 N N   . VAL B 2 70  ? 13.752  8.419   8.659   1.00 31.92 ? 70   VAL U N   1 
ATOM   1526 C CA  . VAL B 2 70  ? 14.166  9.797   8.491   1.00 31.66 ? 70   VAL U CA  1 
ATOM   1527 C C   . VAL B 2 70  ? 13.180  10.626  7.640   1.00 31.90 ? 70   VAL U C   1 
ATOM   1528 O O   . VAL B 2 70  ? 12.462  10.092  6.799   1.00 31.65 ? 70   VAL U O   1 
ATOM   1529 C CB  . VAL B 2 70  ? 15.608  9.838   7.947   1.00 31.43 ? 70   VAL U CB  1 
ATOM   1530 C CG1 . VAL B 2 70  ? 16.486  8.922   8.764   1.00 30.97 ? 70   VAL U CG1 1 
ATOM   1531 C CG2 . VAL B 2 70  ? 15.671  9.390   6.504   1.00 31.74 ? 70   VAL U CG2 1 
ATOM   1532 N N   . CYS B 2 71  ? 13.136  11.929  7.912   1.00 32.64 ? 71   CYS U N   1 
ATOM   1533 C CA  . CYS B 2 71  ? 12.354  12.916  7.141   1.00 33.72 ? 71   CYS U CA  1 
ATOM   1534 C C   . CYS B 2 71  ? 12.879  14.340  7.327   1.00 33.67 ? 71   CYS U C   1 
ATOM   1535 O O   . CYS B 2 71  ? 13.453  14.683  8.377   1.00 33.70 ? 71   CYS U O   1 
ATOM   1536 C CB  . CYS B 2 71  ? 10.895  12.901  7.537   1.00 33.75 ? 71   CYS U CB  1 
ATOM   1537 S SG  . CYS B 2 71  ? 10.751  12.718  9.281   1.00 37.58 ? 71   CYS U SG  1 
ATOM   1538 N N   . ALA B 2 72  ? 12.652  15.163  6.298   1.00 33.66 ? 72   ALA U N   1 
ATOM   1539 C CA  . ALA B 2 72  ? 13.219  16.505  6.222   1.00 33.29 ? 72   ALA U CA  1 
ATOM   1540 C C   . ALA B 2 72  ? 12.216  17.621  6.547   1.00 33.01 ? 72   ALA U C   1 
ATOM   1541 O O   . ALA B 2 72  ? 12.299  18.707  5.972   1.00 33.01 ? 72   ALA U O   1 
ATOM   1542 C CB  . ALA B 2 72  ? 13.886  16.733  4.859   1.00 32.82 ? 72   ALA U CB  1 
ATOM   1543 N N   . THR B 2 73  ? 11.290  17.369  7.473   1.00 32.58 ? 73   THR U N   1 
ATOM   1544 C CA  . THR B 2 73  ? 10.403  18.443  7.941   1.00 32.52 ? 73   THR U CA  1 
ATOM   1545 C C   . THR B 2 73  ? 10.461  18.717  9.450   1.00 32.84 ? 73   THR U C   1 
ATOM   1546 O O   . THR B 2 73  ? 11.079  17.960  10.225  1.00 32.94 ? 73   THR U O   1 
ATOM   1547 C CB  . THR B 2 73  ? 8.957   18.240  7.521   1.00 32.12 ? 73   THR U CB  1 
ATOM   1548 O OG1 . THR B 2 73  ? 8.562   16.909  7.848   1.00 32.13 ? 73   THR U OG1 1 
ATOM   1549 C CG2 . THR B 2 73  ? 8.814   18.462  6.037   1.00 32.01 ? 73   THR U CG2 1 
ATOM   1550 N N   . ASN B 2 74  ? 9.811   19.809  9.854   1.00 32.66 ? 74   ASN U N   1 
ATOM   1551 C CA  . ASN B 2 74  ? 9.934   20.300  11.216  1.00 32.55 ? 74   ASN U CA  1 
ATOM   1552 C C   . ASN B 2 74  ? 9.317   19.438  12.303  1.00 32.85 ? 74   ASN U C   1 
ATOM   1553 O O   . ASN B 2 74  ? 8.081   19.382  12.440  1.00 32.92 ? 74   ASN U O   1 
ATOM   1554 C CB  . ASN B 2 74  ? 9.442   21.735  11.319  1.00 32.30 ? 74   ASN U CB  1 
ATOM   1555 C CG  . ASN B 2 74  ? 10.537  22.721  11.040  1.00 32.13 ? 74   ASN U CG  1 
ATOM   1556 O OD1 . ASN B 2 74  ? 11.614  22.330  10.602  1.00 31.80 ? 74   ASN U OD1 1 
ATOM   1557 N ND2 . ASN B 2 74  ? 10.286  24.008  11.303  1.00 31.97 ? 74   ASN U ND2 1 
ATOM   1558 N N   . LEU B 2 75  ? 10.212  18.787  13.065  1.00 32.87 ? 75   LEU U N   1 
ATOM   1559 C CA  . LEU B 2 75  ? 9.899   17.895  14.200  1.00 32.76 ? 75   LEU U CA  1 
ATOM   1560 C C   . LEU B 2 75  ? 9.053   16.730  13.760  1.00 33.21 ? 75   LEU U C   1 
ATOM   1561 O O   . LEU B 2 75  ? 8.010   16.439  14.343  1.00 32.79 ? 75   LEU U O   1 
ATOM   1562 C CB  . LEU B 2 75  ? 9.219   18.629  15.358  1.00 32.56 ? 75   LEU U CB  1 
ATOM   1563 C CG  . LEU B 2 75  ? 9.762   19.970  15.847  1.00 32.23 ? 75   LEU U CG  1 
ATOM   1564 C CD1 . LEU B 2 75  ? 8.937   20.440  17.027  1.00 31.27 ? 75   LEU U CD1 1 
ATOM   1565 C CD2 . LEU B 2 75  ? 11.221  19.875  16.212  1.00 31.80 ? 75   LEU U CD2 1 
ATOM   1566 N N   . CYS B 2 76  ? 9.521   16.068  12.709  1.00 34.17 ? 76   CYS U N   1 
ATOM   1567 C CA  . CYS B 2 76  ? 8.783   14.981  12.112  1.00 34.93 ? 76   CYS U CA  1 
ATOM   1568 C C   . CYS B 2 76  ? 9.045   13.660  12.835  1.00 35.00 ? 76   CYS U C   1 
ATOM   1569 O O   . CYS B 2 76  ? 8.409   12.666  12.523  1.00 35.26 ? 76   CYS U O   1 
ATOM   1570 C CB  . CYS B 2 76  ? 9.080   14.907  10.616  1.00 35.14 ? 76   CYS U CB  1 
ATOM   1571 S SG  . CYS B 2 76  ? 10.846  14.616  10.100  1.00 38.22 ? 76   CYS U SG  1 
ATOM   1572 N N   . ASN B 2 77  ? 9.991   13.651  13.777  1.00 35.07 ? 77   ASN U N   1 
ATOM   1573 C CA  . ASN B 2 77  ? 10.083  12.604  14.791  1.00 35.36 ? 77   ASN U CA  1 
ATOM   1574 C C   . ASN B 2 77  ? 9.294   13.085  15.992  1.00 36.50 ? 77   ASN U C   1 
ATOM   1575 O O   . ASN B 2 77  ? 9.334   14.263  16.265  1.00 36.97 ? 77   ASN U O   1 
ATOM   1576 C CB  . ASN B 2 77  ? 11.538  12.351  15.179  1.00 34.76 ? 77   ASN U CB  1 
ATOM   1577 C CG  . ASN B 2 77  ? 12.397  13.592  15.118  1.00 32.96 ? 77   ASN U CG  1 
ATOM   1578 O OD1 . ASN B 2 77  ? 11.901  14.682  14.923  1.00 30.68 ? 77   ASN U OD1 1 
ATOM   1579 N ND2 . ASN B 2 77  ? 13.704  13.422  15.278  1.00 31.61 ? 77   ASN U ND2 1 
ATOM   1580 N N   . ARG B 2 78  ? 8.559   12.234  16.711  1.00 37.85 ? 78   ARG U N   1 
ATOM   1581 C CA  . ARG B 2 78  ? 7.734   12.787  17.807  1.00 39.24 ? 78   ARG U CA  1 
ATOM   1582 C C   . ARG B 2 78  ? 7.471   11.966  19.103  1.00 41.11 ? 78   ARG U C   1 
ATOM   1583 O O   . ARG B 2 78  ? 8.409   11.684  19.844  1.00 40.60 ? 78   ARG U O   1 
ATOM   1584 C CB  . ARG B 2 78  ? 6.461   13.432  17.244  1.00 38.83 ? 78   ARG U CB  1 
ATOM   1585 C CG  . ARG B 2 78  ? 6.651   14.831  16.698  1.00 37.29 ? 78   ARG U CG  1 
ATOM   1586 C CD  . ARG B 2 78  ? 6.375   15.894  17.726  1.00 36.24 ? 78   ARG U CD  1 
ATOM   1587 N NE  . ARG B 2 78  ? 4.996   16.380  17.654  1.00 36.14 ? 78   ARG U NE  1 
ATOM   1588 C CZ  . ARG B 2 78  ? 4.414   17.153  18.571  1.00 35.89 ? 78   ARG U CZ  1 
ATOM   1589 N NH1 . ARG B 2 78  ? 5.083   17.537  19.652  1.00 36.36 ? 78   ARG U NH1 1 
ATOM   1590 N NH2 . ARG B 2 78  ? 3.155   17.541  18.411  1.00 35.05 ? 78   ARG U NH2 1 
ATOM   1591 N N   . PRO B 2 79  ? 6.200   11.605  19.409  1.00 43.31 ? 79   PRO U N   1 
ATOM   1592 C CA  . PRO B 2 79  ? 6.009   10.956  20.715  1.00 45.17 ? 79   PRO U CA  1 
ATOM   1593 C C   . PRO B 2 79  ? 6.043   9.412   20.639  1.00 47.30 ? 79   PRO U C   1 
ATOM   1594 O O   . PRO B 2 79  ? 6.904   8.756   21.278  1.00 47.55 ? 79   PRO U O   1 
ATOM   1595 C CB  . PRO B 2 79  ? 4.604   11.443  21.143  1.00 44.80 ? 79   PRO U CB  1 
ATOM   1596 C CG  . PRO B 2 79  ? 3.909   11.897  19.857  1.00 43.88 ? 79   PRO U CG  1 
ATOM   1597 C CD  . PRO B 2 79  ? 4.905   11.779  18.716  1.00 43.52 ? 79   PRO U CD  1 
ATOM   1598 N N   . ARG B 2 80  ? 5.083   8.870   19.872  1.00 49.21 ? 80   ARG U N   1 
ATOM   1599 C CA  . ARG B 2 80  ? 4.910   7.447   19.594  1.00 50.73 ? 80   ARG U CA  1 
ATOM   1600 C C   . ARG B 2 80  ? 6.110   6.963   18.746  1.00 51.53 ? 80   ARG U C   1 
ATOM   1601 O O   . ARG B 2 80  ? 6.865   7.811   18.258  1.00 51.79 ? 80   ARG U O   1 
ATOM   1602 C CB  . ARG B 2 80  ? 3.564   7.260   18.865  1.00 51.02 ? 80   ARG U CB  1 
ATOM   1603 C CG  . ARG B 2 80  ? 2.302   7.339   19.759  1.00 51.97 ? 80   ARG U CG  1 
ATOM   1604 C CD  . ARG B 2 80  ? 2.145   6.055   20.608  1.00 54.22 ? 80   ARG U CD  1 
ATOM   1605 N NE  . ARG B 2 80  ? 0.754   5.648   20.886  1.00 54.51 ? 80   ARG U NE  1 
ATOM   1606 C CZ  . ARG B 2 80  ? 0.062   4.763   20.163  1.00 54.21 ? 80   ARG U CZ  1 
ATOM   1607 N NH1 . ARG B 2 80  ? 0.615   4.198   19.088  1.00 53.89 ? 80   ARG U NH1 1 
ATOM   1608 N NH2 . ARG B 2 80  ? -1.187  4.454   20.508  1.00 52.59 ? 80   ARG U NH2 1 
ATOM   1609 N N   . PRO B 2 81  ? 6.301   5.617   18.568  1.00 52.28 ? 81   PRO U N   1 
ATOM   1610 C CA  . PRO B 2 81  ? 7.543   5.113   17.898  1.00 52.39 ? 81   PRO U CA  1 
ATOM   1611 C C   . PRO B 2 81  ? 7.642   5.413   16.394  1.00 52.38 ? 81   PRO U C   1 
ATOM   1612 O O   . PRO B 2 81  ? 6.642   5.316   15.673  1.00 52.49 ? 81   PRO U O   1 
ATOM   1613 C CB  . PRO B 2 81  ? 7.490   3.592   18.135  1.00 52.54 ? 81   PRO U CB  1 
ATOM   1614 C CG  . PRO B 2 81  ? 6.000   3.274   18.289  1.00 52.44 ? 81   PRO U CG  1 
ATOM   1615 C CD  . PRO B 2 81  ? 5.379   4.508   18.931  1.00 52.41 ? 81   PRO U CD  1 
ATOM   1616 N N   . TYR B 2 93  ? 7.891   -11.896 3.178   1.00 32.83 ? 93   TYR U N   1 
ATOM   1617 C CA  . TYR B 2 93  ? 8.743   -12.866 3.873   1.00 33.18 ? 93   TYR U CA  1 
ATOM   1618 C C   . TYR B 2 93  ? 9.658   -13.650 2.949   1.00 33.14 ? 93   TYR U C   1 
ATOM   1619 O O   . TYR B 2 93  ? 9.255   -14.058 1.861   1.00 33.56 ? 93   TYR U O   1 
ATOM   1620 C CB  . TYR B 2 93  ? 7.923   -13.893 4.648   1.00 33.34 ? 93   TYR U CB  1 
ATOM   1621 C CG  . TYR B 2 93  ? 6.433   -13.713 4.610   1.00 34.44 ? 93   TYR U CG  1 
ATOM   1622 C CD1 . TYR B 2 93  ? 5.763   -13.121 5.688   1.00 35.12 ? 93   TYR U CD1 1 
ATOM   1623 C CD2 . TYR B 2 93  ? 5.680   -14.166 3.507   1.00 33.80 ? 93   TYR U CD2 1 
ATOM   1624 C CE1 . TYR B 2 93  ? 4.382   -12.960 5.660   1.00 36.08 ? 93   TYR U CE1 1 
ATOM   1625 C CE2 . TYR B 2 93  ? 4.302   -14.011 3.467   1.00 34.01 ? 93   TYR U CE2 1 
ATOM   1626 C CZ  . TYR B 2 93  ? 3.656   -13.405 4.544   1.00 35.39 ? 93   TYR U CZ  1 
ATOM   1627 O OH  . TYR B 2 93  ? 2.288   -13.241 4.525   1.00 35.28 ? 93   TYR U OH  1 
ATOM   1628 N N   . LEU B 2 94  ? 10.871  -13.907 3.422   1.00 33.08 ? 94   LEU U N   1 
ATOM   1629 C CA  . LEU B 2 94  ? 11.907  -14.611 2.669   1.00 33.37 ? 94   LEU U CA  1 
ATOM   1630 C C   . LEU B 2 94  ? 12.964  -15.077 3.664   1.00 34.02 ? 94   LEU U C   1 
ATOM   1631 O O   . LEU B 2 94  ? 13.441  -14.277 4.468   1.00 34.66 ? 94   LEU U O   1 
ATOM   1632 C CB  . LEU B 2 94  ? 12.532  -13.667 1.621   1.00 33.01 ? 94   LEU U CB  1 
ATOM   1633 C CG  . LEU B 2 94  ? 13.968  -13.877 1.121   1.00 31.92 ? 94   LEU U CG  1 
ATOM   1634 C CD1 . LEU B 2 94  ? 14.092  -15.163 0.319   1.00 31.86 ? 94   LEU U CD1 1 
ATOM   1635 C CD2 . LEU B 2 94  ? 14.441  -12.687 0.305   1.00 30.01 ? 94   LEU U CD2 1 
ATOM   1636 N N   . GLU B 2 95  ? 13.348  -16.348 3.622   1.00 34.53 ? 95   GLU U N   1 
ATOM   1637 C CA  . GLU B 2 95  ? 14.258  -16.882 4.642   1.00 35.28 ? 95   GLU U CA  1 
ATOM   1638 C C   . GLU B 2 95  ? 15.765  -16.657 4.442   1.00 35.61 ? 95   GLU U C   1 
ATOM   1639 O O   . GLU B 2 95  ? 16.300  -16.816 3.346   1.00 35.02 ? 95   GLU U O   1 
ATOM   1640 C CB  . GLU B 2 95  ? 13.981  -18.357 4.915   1.00 35.54 ? 95   GLU U CB  1 
ATOM   1641 C CG  . GLU B 2 95  ? 13.246  -18.631 6.232   1.00 36.67 ? 95   GLU U CG  1 
ATOM   1642 C CD  . GLU B 2 95  ? 12.885  -20.119 6.435   1.00 39.05 ? 95   GLU U CD  1 
ATOM   1643 O OE1 . GLU B 2 95  ? 12.115  -20.420 7.382   1.00 38.93 ? 95   GLU U OE1 1 
ATOM   1644 O OE2 . GLU B 2 95  ? 13.361  -20.985 5.648   1.00 39.72 ? 95   GLU U OE2 1 
ATOM   1645 N N   . CYS B 2 96  ? 16.419  -16.287 5.551   1.00 36.61 ? 96   CYS U N   1 
ATOM   1646 C CA  . CYS B 2 96  ? 17.866  -16.037 5.644   1.00 37.21 ? 96   CYS U CA  1 
ATOM   1647 C C   . CYS B 2 96  ? 18.395  -16.567 6.960   1.00 37.01 ? 96   CYS U C   1 
ATOM   1648 O O   . CYS B 2 96  ? 17.710  -16.484 7.981   1.00 36.69 ? 96   CYS U O   1 
ATOM   1649 C CB  . CYS B 2 96  ? 18.165  -14.541 5.599   1.00 37.40 ? 96   CYS U CB  1 
ATOM   1650 S SG  . CYS B 2 96  ? 17.118  -13.548 4.487   1.00 40.01 ? 96   CYS U SG  1 
ATOM   1651 N N   . ALA B 2 97  ? 19.622  -17.082 6.931   1.00 37.26 ? 97   ALA U N   1 
ATOM   1652 C CA  . ALA B 2 97  ? 20.284  -17.615 8.126   1.00 37.89 ? 97   ALA U CA  1 
ATOM   1653 C C   . ALA B 2 97  ? 20.515  -16.526 9.181   1.00 38.11 ? 97   ALA U C   1 
ATOM   1654 O O   . ALA B 2 97  ? 20.782  -15.388 8.827   1.00 38.48 ? 97   ALA U O   1 
ATOM   1655 C CB  . ALA B 2 97  ? 21.606  -18.262 7.741   1.00 37.78 ? 97   ALA U CB  1 
ATOM   1656 N N   . SER B 2 98  ? 20.408  -16.860 10.465  1.00 38.23 ? 98   SER U N   1 
ATOM   1657 C CA  . SER B 2 98  ? 20.706  -15.879 11.519  1.00 38.56 ? 98   SER U CA  1 
ATOM   1658 C C   . SER B 2 98  ? 21.572  -16.399 12.647  1.00 38.81 ? 98   SER U C   1 
ATOM   1659 O O   . SER B 2 98  ? 21.746  -17.597 12.800  1.00 39.06 ? 98   SER U O   1 
ATOM   1660 C CB  . SER B 2 98  ? 19.432  -15.287 12.100  1.00 38.61 ? 98   SER U CB  1 
ATOM   1661 O OG  . SER B 2 98  ? 19.009  -14.191 11.319  1.00 39.10 ? 98   SER U OG  1 
ATOM   1662 N N   . CYS B 2 99  ? 22.102  -15.490 13.448  1.00 39.08 ? 99   CYS U N   1 
ATOM   1663 C CA  . CYS B 2 99  ? 23.090  -15.833 14.438  1.00 40.15 ? 99   CYS U CA  1 
ATOM   1664 C C   . CYS B 2 99  ? 23.895  -14.593 14.628  1.00 39.64 ? 99   CYS U C   1 
ATOM   1665 O O   . CYS B 2 99  ? 23.905  -13.750 13.757  1.00 39.66 ? 99   CYS U O   1 
ATOM   1666 C CB  . CYS B 2 99  ? 24.044  -16.862 13.875  1.00 40.71 ? 99   CYS U CB  1 
ATOM   1667 S SG  . CYS B 2 99  ? 24.823  -16.233 12.375  1.00 46.34 ? 99   CYS U SG  1 
ATOM   1668 N N   . THR B 2 100 ? 24.614  -14.511 15.741  1.00 39.75 ? 100  THR U N   1 
ATOM   1669 C CA  . THR B 2 100 ? 25.560  -13.436 15.986  1.00 39.68 ? 100  THR U CA  1 
ATOM   1670 C C   . THR B 2 100 ? 26.891  -14.044 16.330  1.00 40.21 ? 100  THR U C   1 
ATOM   1671 O O   . THR B 2 100 ? 26.945  -15.195 16.743  1.00 40.29 ? 100  THR U O   1 
ATOM   1672 C CB  . THR B 2 100 ? 25.122  -12.558 17.145  1.00 39.31 ? 100  THR U CB  1 
ATOM   1673 O OG1 . THR B 2 100 ? 26.271  -11.965 17.752  1.00 39.40 ? 100  THR U OG1 1 
ATOM   1674 C CG2 . THR B 2 100 ? 24.424  -13.363 18.166  1.00 38.77 ? 100  THR U CG2 1 
ATOM   1675 N N   . SER B 2 101 ? 27.964  -13.279 16.148  1.00 40.98 ? 101  SER U N   1 
ATOM   1676 C CA  . SER B 2 101 ? 29.267  -13.675 16.660  1.00 41.70 ? 101  SER U CA  1 
ATOM   1677 C C   . SER B 2 101 ? 29.188  -13.803 18.185  1.00 42.44 ? 101  SER U C   1 
ATOM   1678 O O   . SER B 2 101 ? 29.690  -14.781 18.749  1.00 42.93 ? 101  SER U O   1 
ATOM   1679 C CB  . SER B 2 101 ? 30.339  -12.659 16.293  1.00 41.52 ? 101  SER U CB  1 
ATOM   1680 O OG  . SER B 2 101 ? 30.555  -11.776 17.380  1.00 41.81 ? 101  SER U OG  1 
ATOM   1681 N N   . LEU B 2 102 ? 28.541  -12.833 18.835  1.00 42.89 ? 102  LEU U N   1 
ATOM   1682 C CA  . LEU B 2 102 ? 28.380  -12.814 20.289  1.00 43.85 ? 102  LEU U CA  1 
ATOM   1683 C C   . LEU B 2 102 ? 28.011  -14.119 21.036  1.00 44.66 ? 102  LEU U C   1 
ATOM   1684 O O   . LEU B 2 102 ? 28.617  -14.442 22.073  1.00 45.07 ? 102  LEU U O   1 
ATOM   1685 C CB  . LEU B 2 102 ? 27.386  -11.736 20.671  1.00 43.63 ? 102  LEU U CB  1 
ATOM   1686 C CG  . LEU B 2 102 ? 27.495  -11.365 22.145  1.00 44.49 ? 102  LEU U CG  1 
ATOM   1687 C CD1 . LEU B 2 102 ? 28.842  -10.668 22.495  1.00 44.96 ? 102  LEU U CD1 1 
ATOM   1688 C CD2 . LEU B 2 102 ? 26.319  -10.499 22.530  1.00 45.70 ? 102  LEU U CD2 1 
ATOM   1689 N N   . ASP B 2 103 ? 27.026  -14.864 20.540  1.00 45.30 ? 103  ASP U N   1 
ATOM   1690 C CA  . ASP B 2 103 ? 26.632  -16.112 21.199  1.00 46.09 ? 103  ASP U CA  1 
ATOM   1691 C C   . ASP B 2 103 ? 27.325  -17.346 20.629  1.00 46.27 ? 103  ASP U C   1 
ATOM   1692 O O   . ASP B 2 103 ? 26.868  -18.469 20.850  1.00 46.36 ? 103  ASP U O   1 
ATOM   1693 C CB  . ASP B 2 103 ? 25.113  -16.297 21.150  1.00 46.39 ? 103  ASP U CB  1 
ATOM   1694 C CG  . ASP B 2 103 ? 24.574  -16.356 19.728  1.00 48.09 ? 103  ASP U CG  1 
ATOM   1695 O OD1 . ASP B 2 103 ? 25.340  -16.039 18.789  1.00 50.00 ? 103  ASP U OD1 1 
ATOM   1696 O OD2 . ASP B 2 103 ? 23.381  -16.707 19.540  1.00 49.67 ? 103  ASP U OD2 1 
ATOM   1697 N N   . GLN B 2 104 ? 28.424  -17.133 19.906  1.00 46.68 ? 104  GLN U N   1 
ATOM   1698 C CA  . GLN B 2 104 ? 29.197  -18.210 19.257  1.00 47.43 ? 104  GLN U CA  1 
ATOM   1699 C C   . GLN B 2 104 ? 28.343  -19.117 18.345  1.00 47.53 ? 104  GLN U C   1 
ATOM   1700 O O   . GLN B 2 104 ? 28.514  -20.342 18.328  1.00 47.44 ? 104  GLN U O   1 
ATOM   1701 C CB  . GLN B 2 104 ? 29.978  -19.065 20.285  1.00 47.62 ? 104  GLN U CB  1 
ATOM   1702 C CG  . GLN B 2 104 ? 30.536  -18.337 21.526  1.00 48.86 ? 104  GLN U CG  1 
ATOM   1703 C CD  . GLN B 2 104 ? 31.656  -17.342 21.220  1.00 50.20 ? 104  GLN U CD  1 
ATOM   1704 O OE1 . GLN B 2 104 ? 32.180  -17.293 20.095  1.00 50.50 ? 104  GLN U OE1 1 
ATOM   1705 N NE2 . GLN B 2 104 ? 32.026  -16.537 22.230  1.00 49.06 ? 104  GLN U NE2 1 
ATOM   1706 N N   . SER B 2 105 ? 27.439  -18.514 17.580  1.00 47.73 ? 105  SER U N   1 
ATOM   1707 C CA  . SER B 2 105 ? 26.543  -19.286 16.734  1.00 48.25 ? 105  SER U CA  1 
ATOM   1708 C C   . SER B 2 105 ? 26.823  -19.146 15.237  1.00 48.97 ? 105  SER U C   1 
ATOM   1709 O O   . SER B 2 105 ? 26.588  -20.077 14.480  1.00 49.04 ? 105  SER U O   1 
ATOM   1710 C CB  . SER B 2 105 ? 25.108  -18.924 17.031  1.00 47.88 ? 105  SER U CB  1 
ATOM   1711 O OG  . SER B 2 105 ? 24.927  -17.553 16.798  1.00 47.35 ? 105  SER U OG  1 
ATOM   1712 N N   . CYS B 2 106 ? 27.332  -17.994 14.809  1.00 49.99 ? 106  CYS U N   1 
ATOM   1713 C CA  . CYS B 2 106 ? 27.719  -17.808 13.396  1.00 50.95 ? 106  CYS U CA  1 
ATOM   1714 C C   . CYS B 2 106 ? 29.006  -18.558 13.058  1.00 51.62 ? 106  CYS U C   1 
ATOM   1715 O O   . CYS B 2 106 ? 29.306  -18.768 11.886  1.00 51.68 ? 106  CYS U O   1 
ATOM   1716 C CB  . CYS B 2 106 ? 27.906  -16.317 13.020  1.00 50.83 ? 106  CYS U CB  1 
ATOM   1717 S SG  . CYS B 2 106 ? 26.443  -15.142 13.003  1.00 50.94 ? 106  CYS U SG  1 
ATOM   1718 N N   . GLU B 2 107 ? 29.766  -18.942 14.085  1.00 52.70 ? 107  GLU U N   1 
ATOM   1719 C CA  . GLU B 2 107 ? 31.077  -19.585 13.898  1.00 53.80 ? 107  GLU U CA  1 
ATOM   1720 C C   . GLU B 2 107 ? 30.972  -21.096 13.770  1.00 53.85 ? 107  GLU U C   1 
ATOM   1721 O O   . GLU B 2 107 ? 31.788  -21.724 13.077  1.00 54.23 ? 107  GLU U O   1 
ATOM   1722 C CB  . GLU B 2 107 ? 32.052  -19.235 15.029  1.00 54.07 ? 107  GLU U CB  1 
ATOM   1723 C CG  . GLU B 2 107 ? 32.574  -17.796 14.994  1.00 56.31 ? 107  GLU U CG  1 
ATOM   1724 C CD  . GLU B 2 107 ? 31.577  -16.760 15.552  1.00 58.98 ? 107  GLU U CD  1 
ATOM   1725 O OE1 . GLU B 2 107 ? 30.701  -17.124 16.384  1.00 59.93 ? 107  GLU U OE1 1 
ATOM   1726 O OE2 . GLU B 2 107 ? 31.687  -15.572 15.159  1.00 59.33 ? 107  GLU U OE2 1 
ATOM   1727 N N   . ARG B 2 108 ? 29.979  -21.677 14.441  1.00 53.71 ? 108  ARG U N   1 
ATOM   1728 C CA  . ARG B 2 108 ? 29.741  -23.112 14.332  1.00 53.72 ? 108  ARG U CA  1 
ATOM   1729 C C   . ARG B 2 108 ? 28.885  -23.454 13.095  1.00 53.45 ? 108  ARG U C   1 
ATOM   1730 O O   . ARG B 2 108 ? 27.940  -22.721 12.767  1.00 53.34 ? 108  ARG U O   1 
ATOM   1731 C CB  . ARG B 2 108 ? 29.136  -23.665 15.634  1.00 53.79 ? 108  ARG U CB  1 
ATOM   1732 C CG  . ARG B 2 108 ? 30.133  -23.718 16.806  1.00 54.20 ? 108  ARG U CG  1 
ATOM   1733 C CD  . ARG B 2 108 ? 31.091  -24.931 16.746  1.00 54.31 ? 108  ARG U CD  1 
ATOM   1734 N NE  . ARG B 2 108 ? 30.790  -25.914 17.789  1.00 54.12 ? 108  ARG U NE  1 
ATOM   1735 C CZ  . ARG B 2 108 ? 31.376  -25.961 18.989  1.00 54.06 ? 108  ARG U CZ  1 
ATOM   1736 N NH1 . ARG B 2 108 ? 32.321  -25.089 19.321  1.00 53.69 ? 108  ARG U NH1 1 
ATOM   1737 N NH2 . ARG B 2 108 ? 31.015  -26.892 19.866  1.00 53.89 ? 108  ARG U NH2 1 
ATOM   1738 N N   . GLY B 2 109 ? 29.244  -24.546 12.406  1.00 52.98 ? 109  GLY U N   1 
ATOM   1739 C CA  . GLY B 2 109 ? 28.464  -25.080 11.285  1.00 52.32 ? 109  GLY U CA  1 
ATOM   1740 C C   . GLY B 2 109 ? 27.034  -25.436 11.678  1.00 52.00 ? 109  GLY U C   1 
ATOM   1741 O O   . GLY B 2 109 ? 26.590  -26.571 11.464  1.00 52.08 ? 109  GLY U O   1 
ATOM   1742 N N   . ARG B 2 110 ? 26.343  -24.451 12.271  1.00 51.38 ? 110  ARG U N   1 
ATOM   1743 C CA  . ARG B 2 110 ? 24.911  -24.464 12.631  1.00 50.95 ? 110  ARG U CA  1 
ATOM   1744 C C   . ARG B 2 110 ? 24.535  -23.036 13.108  1.00 50.38 ? 110  ARG U C   1 
ATOM   1745 O O   . ARG B 2 110 ? 25.377  -22.363 13.707  1.00 50.84 ? 110  ARG U O   1 
ATOM   1746 C CB  . ARG B 2 110 ? 24.592  -25.538 13.697  1.00 50.94 ? 110  ARG U CB  1 
ATOM   1747 C CG  . ARG B 2 110 ? 25.115  -25.263 15.112  1.00 52.14 ? 110  ARG U CG  1 
ATOM   1748 C CD  . ARG B 2 110 ? 24.073  -24.522 15.974  1.00 54.24 ? 110  ARG U CD  1 
ATOM   1749 N NE  . ARG B 2 110 ? 24.673  -23.626 16.968  1.00 55.88 ? 110  ARG U NE  1 
ATOM   1750 C CZ  . ARG B 2 110 ? 25.103  -24.003 18.177  1.00 57.45 ? 110  ARG U CZ  1 
ATOM   1751 N NH1 . ARG B 2 110 ? 25.024  -25.280 18.571  1.00 57.34 ? 110  ARG U NH1 1 
ATOM   1752 N NH2 . ARG B 2 110 ? 25.624  -23.096 19.004  1.00 57.72 ? 110  ARG U NH2 1 
ATOM   1753 N N   . GLU B 2 111 ? 23.295  -22.584 12.859  1.00 49.34 ? 111  GLU U N   1 
ATOM   1754 C CA  . GLU B 2 111 ? 22.861  -21.181 13.114  1.00 48.05 ? 111  GLU U CA  1 
ATOM   1755 C C   . GLU B 2 111 ? 21.359  -20.960 12.891  1.00 46.93 ? 111  GLU U C   1 
ATOM   1756 O O   . GLU B 2 111 ? 20.928  -20.792 11.756  1.00 46.87 ? 111  GLU U O   1 
ATOM   1757 C CB  . GLU B 2 111 ? 23.646  -20.197 12.207  1.00 48.33 ? 111  GLU U CB  1 
ATOM   1758 C CG  . GLU B 2 111 ? 23.497  -20.439 10.665  1.00 49.07 ? 111  GLU U CG  1 
ATOM   1759 C CD  . GLU B 2 111 ? 24.474  -19.637 9.780   1.00 50.19 ? 111  GLU U CD  1 
ATOM   1760 O OE1 . GLU B 2 111 ? 24.868  -20.158 8.707   1.00 50.56 ? 111  GLU U OE1 1 
ATOM   1761 O OE2 . GLU B 2 111 ? 24.844  -18.495 10.138  1.00 49.92 ? 111  GLU U OE2 1 
ATOM   1762 N N   . GLN B 2 112 ? 20.557  -20.929 13.949  1.00 45.76 ? 112  GLN U N   1 
ATOM   1763 C CA  . GLN B 2 112 ? 19.093  -20.774 13.771  1.00 44.94 ? 112  GLN U CA  1 
ATOM   1764 C C   . GLN B 2 112 ? 18.706  -19.667 12.756  1.00 43.86 ? 112  GLN U C   1 
ATOM   1765 O O   . GLN B 2 112 ? 19.305  -18.604 12.738  1.00 43.97 ? 112  GLN U O   1 
ATOM   1766 C CB  . GLN B 2 112 ? 18.358  -20.613 15.125  1.00 45.24 ? 112  GLN U CB  1 
ATOM   1767 C CG  . GLN B 2 112 ? 18.283  -21.932 15.963  1.00 46.54 ? 112  GLN U CG  1 
ATOM   1768 C CD  . GLN B 2 112 ? 17.132  -21.991 17.000  1.00 47.75 ? 112  GLN U CD  1 
ATOM   1769 O OE1 . GLN B 2 112 ? 16.249  -22.856 16.916  1.00 47.48 ? 112  GLN U OE1 1 
ATOM   1770 N NE2 . GLN B 2 112 ? 17.161  -21.090 17.985  1.00 47.76 ? 112  GLN U NE2 1 
ATOM   1771 N N   . SER B 2 113 ? 17.716  -19.933 11.905  1.00 42.52 ? 113  SER U N   1 
ATOM   1772 C CA  . SER B 2 113 ? 17.340  -19.017 10.826  1.00 40.89 ? 113  SER U CA  1 
ATOM   1773 C C   . SER B 2 113 ? 15.986  -18.348 11.023  1.00 39.88 ? 113  SER U C   1 
ATOM   1774 O O   . SER B 2 113 ? 15.268  -18.626 11.971  1.00 39.24 ? 113  SER U O   1 
ATOM   1775 C CB  . SER B 2 113 ? 17.344  -19.751 9.496   1.00 41.19 ? 113  SER U CB  1 
ATOM   1776 O OG  . SER B 2 113 ? 16.306  -20.714 9.457   1.00 41.59 ? 113  SER U OG  1 
ATOM   1777 N N   . LEU B 2 114 ? 15.642  -17.489 10.072  1.00 39.19 ? 114  LEU U N   1 
ATOM   1778 C CA  . LEU B 2 114 ? 14.621  -16.462 10.250  1.00 38.51 ? 114  LEU U CA  1 
ATOM   1779 C C   . LEU B 2 114 ? 14.103  -16.078 8.891   1.00 38.04 ? 114  LEU U C   1 
ATOM   1780 O O   . LEU B 2 114 ? 14.723  -16.383 7.871   1.00 37.88 ? 114  LEU U O   1 
ATOM   1781 C CB  . LEU B 2 114 ? 15.282  -15.220 10.845  1.00 38.64 ? 114  LEU U CB  1 
ATOM   1782 C CG  . LEU B 2 114 ? 14.624  -14.083 11.635  1.00 38.62 ? 114  LEU U CG  1 
ATOM   1783 C CD1 . LEU B 2 114 ? 15.695  -13.077 11.943  1.00 38.40 ? 114  LEU U CD1 1 
ATOM   1784 C CD2 . LEU B 2 114 ? 13.485  -13.377 10.932  1.00 39.14 ? 114  LEU U CD2 1 
ATOM   1785 N N   . GLN B 2 115 ? 12.995  -15.353 8.887   1.00 37.38 ? 115  GLN U N   1 
ATOM   1786 C CA  . GLN B 2 115 ? 12.316  -15.010 7.659   1.00 37.03 ? 115  GLN U CA  1 
ATOM   1787 C C   . GLN B 2 115 ? 11.803  -13.583 7.696   1.00 36.72 ? 115  GLN U C   1 
ATOM   1788 O O   . GLN B 2 115 ? 10.982  -13.240 8.542   1.00 36.81 ? 115  GLN U O   1 
ATOM   1789 C CB  . GLN B 2 115 ? 11.144  -15.953 7.503   1.00 37.05 ? 115  GLN U CB  1 
ATOM   1790 C CG  . GLN B 2 115 ? 10.751  -16.239 6.096   1.00 37.41 ? 115  GLN U CG  1 
ATOM   1791 C CD  . GLN B 2 115 ? 9.348   -16.752 6.038   1.00 37.71 ? 115  GLN U CD  1 
ATOM   1792 O OE1 . GLN B 2 115 ? 8.652   -16.787 7.054   1.00 37.63 ? 115  GLN U OE1 1 
ATOM   1793 N NE2 . GLN B 2 115 ? 8.906   -17.137 4.849   1.00 37.78 ? 115  GLN U NE2 1 
ATOM   1794 N N   . CYS B 2 116 ? 12.262  -12.759 6.766   1.00 36.57 ? 116  CYS U N   1 
ATOM   1795 C CA  . CYS B 2 116 ? 11.954  -11.332 6.790   1.00 37.03 ? 116  CYS U CA  1 
ATOM   1796 C C   . CYS B 2 116 ? 10.463  -11.070 6.874   1.00 37.56 ? 116  CYS U C   1 
ATOM   1797 O O   . CYS B 2 116 ? 9.684   -11.803 6.275   1.00 37.68 ? 116  CYS U O   1 
ATOM   1798 C CB  . CYS B 2 116 ? 12.488  -10.652 5.539   1.00 36.87 ? 116  CYS U CB  1 
ATOM   1799 S SG  . CYS B 2 116 ? 14.177  -11.060 4.979   1.00 36.84 ? 116  CYS U SG  1 
ATOM   1800 N N   . ARG B 2 117 ? 10.051  -10.028 7.596   1.00 38.32 ? 117  ARG U N   1 
ATOM   1801 C CA  . ARG B 2 117 ? 8.613   -9.719  7.644   1.00 39.16 ? 117  ARG U CA  1 
ATOM   1802 C C   . ARG B 2 117 ? 8.154   -8.480  6.840   1.00 39.43 ? 117  ARG U C   1 
ATOM   1803 O O   . ARG B 2 117 ? 7.020   -8.007  6.984   1.00 39.64 ? 117  ARG U O   1 
ATOM   1804 C CB  . ARG B 2 117 ? 8.055   -9.724  9.080   1.00 39.26 ? 117  ARG U CB  1 
ATOM   1805 C CG  . ARG B 2 117 ? 6.714   -10.496 9.199   1.00 39.73 ? 117  ARG U CG  1 
ATOM   1806 C CD  . ARG B 2 117 ? 6.112   -10.798 7.798   1.00 40.11 ? 117  ARG U CD  1 
ATOM   1807 N NE  . ARG B 2 117 ? 4.663   -10.629 7.710   1.00 40.78 ? 117  ARG U NE  1 
ATOM   1808 C CZ  . ARG B 2 117 ? 4.000   -9.496  7.960   1.00 41.57 ? 117  ARG U CZ  1 
ATOM   1809 N NH1 . ARG B 2 117 ? 4.623   -8.386  8.354   1.00 41.62 ? 117  ARG U NH1 1 
ATOM   1810 N NH2 . ARG B 2 117 ? 2.685   -9.479  7.836   1.00 42.28 ? 117  ARG U NH2 1 
ATOM   1811 N N   . TYR B 2 118 ? 9.031   -7.975  5.984   1.00 39.63 ? 118  TYR U N   1 
ATOM   1812 C CA  . TYR B 2 118 ? 8.639   -6.979  5.007   1.00 39.64 ? 118  TYR U CA  1 
ATOM   1813 C C   . TYR B 2 118 ? 9.122   -7.449  3.662   1.00 39.33 ? 118  TYR U C   1 
ATOM   1814 O O   . TYR B 2 118 ? 10.288  -7.840  3.534   1.00 39.57 ? 118  TYR U O   1 
ATOM   1815 C CB  . TYR B 2 118 ? 9.254   -5.605  5.312   1.00 39.80 ? 118  TYR U CB  1 
ATOM   1816 C CG  . TYR B 2 118 ? 8.813   -4.981  6.627   1.00 40.98 ? 118  TYR U CG  1 
ATOM   1817 C CD1 . TYR B 2 118 ? 7.469   -5.027  7.036   1.00 41.84 ? 118  TYR U CD1 1 
ATOM   1818 C CD2 . TYR B 2 118 ? 9.738   -4.326  7.455   1.00 41.49 ? 118  TYR U CD2 1 
ATOM   1819 C CE1 . TYR B 2 118 ? 7.057   -4.457  8.243   1.00 43.01 ? 118  TYR U CE1 1 
ATOM   1820 C CE2 . TYR B 2 118 ? 9.345   -3.746  8.662   1.00 42.55 ? 118  TYR U CE2 1 
ATOM   1821 C CZ  . TYR B 2 118 ? 7.997   -3.812  9.055   1.00 44.41 ? 118  TYR U CZ  1 
ATOM   1822 O OH  . TYR B 2 118 ? 7.588   -3.239  10.259  1.00 45.99 ? 118  TYR U OH  1 
ATOM   1823 N N   . PRO B 2 119 ? 8.222   -7.470  2.661   1.00 38.82 ? 119  PRO U N   1 
ATOM   1824 C CA  . PRO B 2 119 ? 8.734   -7.347  1.296   1.00 38.17 ? 119  PRO U CA  1 
ATOM   1825 C C   . PRO B 2 119 ? 9.551   -6.051  1.182   1.00 37.71 ? 119  PRO U C   1 
ATOM   1826 O O   . PRO B 2 119 ? 9.184   -5.047  1.812   1.00 37.74 ? 119  PRO U O   1 
ATOM   1827 C CB  . PRO B 2 119 ? 7.458   -7.297  0.466   1.00 38.15 ? 119  PRO U CB  1 
ATOM   1828 C CG  . PRO B 2 119 ? 6.493   -8.205  1.243   1.00 38.20 ? 119  PRO U CG  1 
ATOM   1829 C CD  . PRO B 2 119 ? 6.847   -8.020  2.700   1.00 38.80 ? 119  PRO U CD  1 
ATOM   1830 N N   . THR B 2 120 ? 10.643  -6.108  0.404   1.00 37.16 ? 120  THR U N   1 
ATOM   1831 C CA  . THR B 2 120 ? 11.734  -5.080  0.268   1.00 36.66 ? 120  THR U CA  1 
ATOM   1832 C C   . THR B 2 120 ? 12.946  -5.351  1.135   1.00 36.68 ? 120  THR U C   1 
ATOM   1833 O O   . THR B 2 120 ? 14.030  -4.817  0.868   1.00 36.62 ? 120  THR U O   1 
ATOM   1834 C CB  . THR B 2 120 ? 11.352  -3.583  0.484   1.00 36.67 ? 120  THR U CB  1 
ATOM   1835 O OG1 . THR B 2 120 ? 10.895  -3.353  1.828   1.00 34.96 ? 120  THR U OG1 1 
ATOM   1836 C CG2 . THR B 2 120 ? 10.339  -3.110  -0.570  1.00 37.18 ? 120  THR U CG2 1 
ATOM   1837 N N   . GLU B 2 121 ? 12.745  -6.162  2.179   1.00 36.64 ? 121  GLU U N   1 
ATOM   1838 C CA  . GLU B 2 121 ? 13.821  -6.645  3.048   1.00 36.45 ? 121  GLU U CA  1 
ATOM   1839 C C   . GLU B 2 121 ? 14.792  -7.487  2.255   1.00 35.78 ? 121  GLU U C   1 
ATOM   1840 O O   . GLU B 2 121 ? 14.521  -7.832  1.128   1.00 35.88 ? 121  GLU U O   1 
ATOM   1841 C CB  . GLU B 2 121 ? 13.242  -7.494  4.163   1.00 36.72 ? 121  GLU U CB  1 
ATOM   1842 C CG  . GLU B 2 121 ? 12.792  -6.723  5.385   1.00 39.28 ? 121  GLU U CG  1 
ATOM   1843 C CD  . GLU B 2 121 ? 13.481  -7.224  6.679   1.00 42.84 ? 121  GLU U CD  1 
ATOM   1844 O OE1 . GLU B 2 121 ? 14.290  -8.177  6.580   1.00 42.89 ? 121  GLU U OE1 1 
ATOM   1845 O OE2 . GLU B 2 121 ? 13.235  -6.662  7.788   1.00 43.63 ? 121  GLU U OE2 1 
ATOM   1846 N N   . HIS B 2 122 ? 15.926  -7.829  2.831   1.00 35.44 ? 122  HIS U N   1 
ATOM   1847 C CA  . HIS B 2 122 ? 16.872  -8.663  2.119   1.00 35.62 ? 122  HIS U CA  1 
ATOM   1848 C C   . HIS B 2 122 ? 17.400  -9.749  3.001   1.00 35.98 ? 122  HIS U C   1 
ATOM   1849 O O   . HIS B 2 122 ? 16.832  -10.029 4.041   1.00 36.37 ? 122  HIS U O   1 
ATOM   1850 C CB  . HIS B 2 122 ? 18.030  -7.827  1.634   1.00 35.33 ? 122  HIS U CB  1 
ATOM   1851 C CG  . HIS B 2 122 ? 17.707  -7.024  0.421   1.00 36.03 ? 122  HIS U CG  1 
ATOM   1852 N ND1 . HIS B 2 122 ? 18.012  -7.454  -0.855  1.00 35.50 ? 122  HIS U ND1 1 
ATOM   1853 C CD2 . HIS B 2 122 ? 17.099  -5.823  0.284   1.00 36.18 ? 122  HIS U CD2 1 
ATOM   1854 C CE1 . HIS B 2 122 ? 17.613  -6.546  -1.726  1.00 35.44 ? 122  HIS U CE1 1 
ATOM   1855 N NE2 . HIS B 2 122 ? 17.055  -5.548  -1.061  1.00 36.64 ? 122  HIS U NE2 1 
ATOM   1856 N N   . CYS B 2 123 ? 18.485  -10.377 2.579   1.00 36.34 ? 123  CYS U N   1 
ATOM   1857 C CA  . CYS B 2 123 ? 19.252  -11.224 3.470   1.00 36.78 ? 123  CYS U CA  1 
ATOM   1858 C C   . CYS B 2 123 ? 20.562  -10.509 3.639   1.00 36.69 ? 123  CYS U C   1 
ATOM   1859 O O   . CYS B 2 123 ? 21.063  -9.945  2.664   1.00 37.00 ? 123  CYS U O   1 
ATOM   1860 C CB  . CYS B 2 123 ? 19.500  -12.572 2.827   1.00 36.92 ? 123  CYS U CB  1 
ATOM   1861 S SG  . CYS B 2 123 ? 18.047  -13.628 2.649   1.00 39.49 ? 123  CYS U SG  1 
ATOM   1862 N N   . ILE B 2 124 ? 21.126  -10.511 4.849   1.00 36.43 ? 124  ILE U N   1 
ATOM   1863 C CA  . ILE B 2 124 ? 22.415  -9.832  5.055   1.00 36.15 ? 124  ILE U CA  1 
ATOM   1864 C C   . ILE B 2 124 ? 23.420  -10.478 5.995   1.00 36.03 ? 124  ILE U C   1 
ATOM   1865 O O   . ILE B 2 124 ? 23.060  -11.096 6.993   1.00 35.68 ? 124  ILE U O   1 
ATOM   1866 C CB  . ILE B 2 124 ? 22.267  -8.333  5.456   1.00 36.12 ? 124  ILE U CB  1 
ATOM   1867 C CG1 . ILE B 2 124 ? 21.515  -8.170  6.784   1.00 36.41 ? 124  ILE U CG1 1 
ATOM   1868 C CG2 . ILE B 2 124 ? 21.642  -7.530  4.324   1.00 35.90 ? 124  ILE U CG2 1 
ATOM   1869 C CD1 . ILE B 2 124 ? 20.034  -7.792  6.659   1.00 35.19 ? 124  ILE U CD1 1 
ATOM   1870 N N   . GLU B 2 125 ? 24.688  -10.329 5.621   1.00 36.19 ? 125  GLU U N   1 
ATOM   1871 C CA  . GLU B 2 125 ? 25.826  -10.562 6.497   1.00 36.73 ? 125  GLU U CA  1 
ATOM   1872 C C   . GLU B 2 125 ? 26.551  -9.241  6.731   1.00 36.38 ? 125  GLU U C   1 
ATOM   1873 O O   . GLU B 2 125 ? 26.864  -8.518  5.783   1.00 36.43 ? 125  GLU U O   1 
ATOM   1874 C CB  . GLU B 2 125 ? 26.813  -11.560 5.880   1.00 37.05 ? 125  GLU U CB  1 
ATOM   1875 C CG  . GLU B 2 125 ? 26.698  -13.003 6.410   1.00 39.85 ? 125  GLU U CG  1 
ATOM   1876 C CD  . GLU B 2 125 ? 28.035  -13.796 6.423   1.00 43.32 ? 125  GLU U CD  1 
ATOM   1877 O OE1 . GLU B 2 125 ? 28.460  -14.205 7.530   1.00 44.72 ? 125  GLU U OE1 1 
ATOM   1878 O OE2 . GLU B 2 125 ? 28.656  -14.023 5.349   1.00 44.04 ? 125  GLU U OE2 1 
ATOM   1879 N N   . VAL B 2 126 ? 26.839  -8.931  7.987   1.00 36.04 ? 126  VAL U N   1 
ATOM   1880 C CA  . VAL B 2 126 ? 27.633  -7.753  8.300   1.00 35.65 ? 126  VAL U CA  1 
ATOM   1881 C C   . VAL B 2 126 ? 28.846  -8.097  9.164   1.00 36.25 ? 126  VAL U C   1 
ATOM   1882 O O   . VAL B 2 126 ? 28.718  -8.699  10.236  1.00 36.30 ? 126  VAL U O   1 
ATOM   1883 C CB  . VAL B 2 126 ? 26.748  -6.640  8.898   1.00 35.04 ? 126  VAL U CB  1 
ATOM   1884 C CG1 . VAL B 2 126 ? 25.710  -7.229  9.766   1.00 34.69 ? 126  VAL U CG1 1 
ATOM   1885 C CG2 . VAL B 2 126 ? 27.558  -5.603  9.629   1.00 33.85 ? 126  VAL U CG2 1 
ATOM   1886 N N   . VAL B 2 127 ? 30.026  -7.729  8.680   1.00 36.83 ? 127  VAL U N   1 
ATOM   1887 C CA  . VAL B 2 127 ? 31.238  -8.046  9.399   1.00 38.01 ? 127  VAL U CA  1 
ATOM   1888 C C   . VAL B 2 127 ? 31.978  -6.807  9.889   1.00 39.00 ? 127  VAL U C   1 
ATOM   1889 O O   . VAL B 2 127 ? 32.151  -5.860  9.134   1.00 39.20 ? 127  VAL U O   1 
ATOM   1890 C CB  . VAL B 2 127 ? 32.157  -8.945  8.557   1.00 38.04 ? 127  VAL U CB  1 
ATOM   1891 C CG1 . VAL B 2 127 ? 32.453  -8.310  7.225   1.00 37.38 ? 127  VAL U CG1 1 
ATOM   1892 C CG2 . VAL B 2 127 ? 33.449  -9.273  9.307   1.00 38.25 ? 127  VAL U CG2 1 
ATOM   1893 N N   . THR B 2 128 ? 32.384  -6.824  11.164  1.00 40.33 ? 128  THR U N   1 
ATOM   1894 C CA  . THR B 2 128 ? 33.237  -5.786  11.771  1.00 41.50 ? 128  THR U CA  1 
ATOM   1895 C C   . THR B 2 128 ? 34.395  -6.396  12.577  1.00 42.68 ? 128  THR U C   1 
ATOM   1896 O O   . THR B 2 128 ? 34.192  -6.915  13.687  1.00 43.07 ? 128  THR U O   1 
ATOM   1897 C CB  . THR B 2 128 ? 32.452  -4.843  12.707  1.00 41.11 ? 128  THR U CB  1 
ATOM   1898 O OG1 . THR B 2 128 ? 31.440  -4.151  11.972  1.00 40.70 ? 128  THR U OG1 1 
ATOM   1899 C CG2 . THR B 2 128 ? 33.388  -3.823  13.307  1.00 40.96 ? 128  THR U CG2 1 
ATOM   1900 N N   . LEU B 2 129 ? 35.604  -6.327  12.025  1.00 43.89 ? 129  LEU U N   1 
ATOM   1901 C CA  . LEU B 2 129 ? 36.777  -6.870  12.711  1.00 45.00 ? 129  LEU U CA  1 
ATOM   1902 C C   . LEU B 2 129 ? 37.734  -5.757  13.091  1.00 45.81 ? 129  LEU U C   1 
ATOM   1903 O O   . LEU B 2 129 ? 38.190  -4.995  12.223  1.00 45.94 ? 129  LEU U O   1 
ATOM   1904 C CB  . LEU B 2 129 ? 37.500  -7.920  11.860  1.00 45.04 ? 129  LEU U CB  1 
ATOM   1905 C CG  . LEU B 2 129 ? 36.762  -9.142  11.291  1.00 45.33 ? 129  LEU U CG  1 
ATOM   1906 C CD1 . LEU B 2 129 ? 37.784  -10.202 10.885  1.00 45.41 ? 129  LEU U CD1 1 
ATOM   1907 C CD2 . LEU B 2 129 ? 35.727  -9.740  12.259  1.00 45.50 ? 129  LEU U CD2 1 
ATOM   1908 N N   . GLN B 2 130 ? 38.033  -5.687  14.392  1.00 46.68 ? 130  GLN U N   1 
ATOM   1909 C CA  . GLN B 2 130 ? 38.838  -4.613  15.000  1.00 47.26 ? 130  GLN U CA  1 
ATOM   1910 C C   . GLN B 2 130 ? 39.920  -5.152  15.958  1.00 47.83 ? 130  GLN U C   1 
ATOM   1911 O O   . GLN B 2 130 ? 39.736  -6.195  16.597  1.00 48.28 ? 130  GLN U O   1 
ATOM   1912 C CB  . GLN B 2 130 ? 37.907  -3.645  15.719  1.00 46.79 ? 130  GLN U CB  1 
ATOM   1913 C CG  . GLN B 2 130 ? 36.643  -4.326  16.207  1.00 47.04 ? 130  GLN U CG  1 
ATOM   1914 C CD  . GLN B 2 130 ? 35.576  -3.359  16.699  1.00 48.66 ? 130  GLN U CD  1 
ATOM   1915 O OE1 . GLN B 2 130 ? 35.748  -2.131  16.674  1.00 48.02 ? 130  GLN U OE1 1 
ATOM   1916 N NE2 . GLN B 2 130 ? 34.457  -3.917  17.157  1.00 49.46 ? 130  GLN U NE2 1 
ATOM   1917 N N   . SER B 2 131 ? 41.045  -4.447  16.058  1.00 48.29 ? 131  SER U N   1 
ATOM   1918 C CA  . SER B 2 131 ? 42.143  -4.886  16.930  1.00 48.80 ? 131  SER U CA  1 
ATOM   1919 C C   . SER B 2 131 ? 42.234  -4.209  18.327  1.00 49.25 ? 131  SER U C   1 
ATOM   1920 O O   . SER B 2 131 ? 41.441  -3.311  18.660  1.00 49.49 ? 131  SER U O   1 
ATOM   1921 C CB  . SER B 2 131 ? 43.475  -4.817  16.182  1.00 48.59 ? 131  SER U CB  1 
ATOM   1922 O OG  . SER B 2 131 ? 43.635  -5.966  15.371  1.00 48.75 ? 131  SER U OG  1 
ATOM   1923 N N   . THR B 2 132 ? 43.194  -4.683  19.131  1.00 49.50 ? 132  THR U N   1 
ATOM   1924 C CA  . THR B 2 132 ? 43.486  -4.193  20.496  1.00 49.52 ? 132  THR U CA  1 
ATOM   1925 C C   . THR B 2 132 ? 42.237  -3.762  21.316  1.00 49.41 ? 132  THR U C   1 
ATOM   1926 O O   . THR B 2 132 ? 41.347  -4.592  21.530  1.00 49.51 ? 132  THR U O   1 
ATOM   1927 C CB  . THR B 2 132 ? 44.682  -3.173  20.502  1.00 49.79 ? 132  THR U CB  1 
ATOM   1928 O OG1 . THR B 2 132 ? 44.953  -2.739  19.163  1.00 50.19 ? 132  THR U OG1 1 
ATOM   1929 C CG2 . THR B 2 132 ? 45.966  -3.822  21.045  1.00 49.76 ? 132  THR U CG2 1 
ATOM   1930 N N   . GLU B 2 133 ? 42.157  -2.504  21.770  1.00 49.22 ? 133  GLU U N   1 
ATOM   1931 C CA  . GLU B 2 133 ? 41.018  -2.062  22.614  1.00 49.06 ? 133  GLU U CA  1 
ATOM   1932 C C   . GLU B 2 133 ? 39.916  -1.372  21.830  1.00 48.45 ? 133  GLU U C   1 
ATOM   1933 O O   . GLU B 2 133 ? 39.266  -0.467  22.361  1.00 48.48 ? 133  GLU U O   1 
ATOM   1934 C CB  . GLU B 2 133 ? 41.442  -1.142  23.771  1.00 49.27 ? 133  GLU U CB  1 
ATOM   1935 C CG  . GLU B 2 133 ? 42.268  -1.788  24.877  1.00 51.18 ? 133  GLU U CG  1 
ATOM   1936 C CD  . GLU B 2 133 ? 43.753  -1.498  24.722  1.00 54.04 ? 133  GLU U CD  1 
ATOM   1937 O OE1 . GLU B 2 133 ? 44.091  -0.573  23.943  1.00 55.28 ? 133  GLU U OE1 1 
ATOM   1938 O OE2 . GLU B 2 133 ? 44.581  -2.184  25.374  1.00 55.25 ? 133  GLU U OE2 1 
ATOM   1939 N N   . ARG B 2 134 ? 39.755  -1.785  20.570  1.00 47.67 ? 134  ARG U N   1 
ATOM   1940 C CA  . ARG B 2 134 ? 38.625  -1.448  19.674  1.00 46.83 ? 134  ARG U CA  1 
ATOM   1941 C C   . ARG B 2 134 ? 37.598  -0.354  20.035  1.00 46.03 ? 134  ARG U C   1 
ATOM   1942 O O   . ARG B 2 134 ? 36.850  -0.470  21.017  1.00 45.79 ? 134  ARG U O   1 
ATOM   1943 C CB  . ARG B 2 134 ? 37.863  -2.724  19.325  1.00 47.15 ? 134  ARG U CB  1 
ATOM   1944 C CG  . ARG B 2 134 ? 37.272  -3.494  20.498  1.00 47.70 ? 134  ARG U CG  1 
ATOM   1945 C CD  . ARG B 2 134 ? 36.564  -4.746  19.980  1.00 49.44 ? 134  ARG U CD  1 
ATOM   1946 N NE  . ARG B 2 134 ? 36.924  -5.941  20.747  1.00 50.84 ? 134  ARG U NE  1 
ATOM   1947 C CZ  . ARG B 2 134 ? 38.038  -6.661  20.584  1.00 50.81 ? 134  ARG U CZ  1 
ATOM   1948 N NH1 . ARG B 2 134 ? 38.950  -6.328  19.668  1.00 50.16 ? 134  ARG U NH1 1 
ATOM   1949 N NH2 . ARG B 2 134 ? 38.238  -7.726  21.354  1.00 50.72 ? 134  ARG U NH2 1 
ATOM   1950 N N   . SER B 2 135 ? 37.525  0.662   19.177  1.00 45.05 ? 135  SER U N   1 
ATOM   1951 C CA  . SER B 2 135 ? 36.623  1.812   19.357  1.00 44.13 ? 135  SER U CA  1 
ATOM   1952 C C   . SER B 2 135 ? 35.127  1.524   19.278  1.00 43.47 ? 135  SER U C   1 
ATOM   1953 O O   . SER B 2 135 ? 34.343  2.341   19.742  1.00 43.19 ? 135  SER U O   1 
ATOM   1954 C CB  . SER B 2 135 ? 36.955  2.916   18.353  1.00 44.07 ? 135  SER U CB  1 
ATOM   1955 O OG  . SER B 2 135 ? 38.272  3.394   18.548  1.00 44.44 ? 135  SER U OG  1 
ATOM   1956 N N   . LEU B 2 136 ? 34.741  0.385   18.693  1.00 42.94 ? 136  LEU U N   1 
ATOM   1957 C CA  . LEU B 2 136 ? 33.328  0.076   18.407  1.00 42.25 ? 136  LEU U CA  1 
ATOM   1958 C C   . LEU B 2 136 ? 32.781  -1.144  19.151  1.00 41.61 ? 136  LEU U C   1 
ATOM   1959 O O   . LEU B 2 136 ? 33.433  -2.183  19.238  1.00 41.47 ? 136  LEU U O   1 
ATOM   1960 C CB  . LEU B 2 136 ? 33.109  -0.153  16.902  1.00 42.60 ? 136  LEU U CB  1 
ATOM   1961 C CG  . LEU B 2 136 ? 33.783  0.639   15.769  1.00 42.86 ? 136  LEU U CG  1 
ATOM   1962 C CD1 . LEU B 2 136 ? 33.187  0.227   14.418  1.00 42.31 ? 136  LEU U CD1 1 
ATOM   1963 C CD2 . LEU B 2 136 ? 33.672  2.154   15.957  1.00 43.59 ? 136  LEU U CD2 1 
ATOM   1964 N N   . LYS B 2 137 ? 31.555  -1.025  19.640  1.00 40.90 ? 137  LYS U N   1 
ATOM   1965 C CA  . LYS B 2 137 ? 30.929  -2.104  20.392  1.00 40.28 ? 137  LYS U CA  1 
ATOM   1966 C C   . LYS B 2 137 ? 29.993  -2.945  19.526  1.00 39.25 ? 137  LYS U C   1 
ATOM   1967 O O   . LYS B 2 137 ? 28.867  -3.236  19.910  1.00 38.54 ? 137  LYS U O   1 
ATOM   1968 C CB  . LYS B 2 137 ? 30.206  -1.530  21.631  1.00 40.96 ? 137  LYS U CB  1 
ATOM   1969 C CG  . LYS B 2 137 ? 31.147  -1.104  22.806  1.00 42.02 ? 137  LYS U CG  1 
ATOM   1970 C CD  . LYS B 2 137 ? 31.869  -2.324  23.440  1.00 43.84 ? 137  LYS U CD  1 
ATOM   1971 C CE  . LYS B 2 137 ? 33.228  -1.951  24.056  1.00 44.63 ? 137  LYS U CE  1 
ATOM   1972 N NZ  . LYS B 2 137 ? 34.179  -1.266  23.103  1.00 44.71 ? 137  LYS U NZ  1 
ATOM   1973 N N   . ASP B 2 138 ? 30.494  -3.349  18.361  1.00 38.79 ? 138  ASP U N   1 
ATOM   1974 C CA  . ASP B 2 138 ? 29.705  -4.052  17.315  1.00 38.24 ? 138  ASP U CA  1 
ATOM   1975 C C   . ASP B 2 138 ? 30.114  -5.521  17.143  1.00 37.23 ? 138  ASP U C   1 
ATOM   1976 O O   . ASP B 2 138 ? 31.309  -5.830  17.062  1.00 37.37 ? 138  ASP U O   1 
ATOM   1977 C CB  . ASP B 2 138 ? 29.885  -3.347  15.958  1.00 38.60 ? 138  ASP U CB  1 
ATOM   1978 C CG  . ASP B 2 138 ? 28.780  -2.329  15.643  1.00 39.90 ? 138  ASP U CG  1 
ATOM   1979 O OD1 . ASP B 2 138 ? 28.409  -2.230  14.448  1.00 41.57 ? 138  ASP U OD1 1 
ATOM   1980 O OD2 . ASP B 2 138 ? 28.291  -1.620  16.557  1.00 41.08 ? 138  ASP U OD2 1 
ATOM   1981 N N   . GLU B 2 139 ? 29.134  -6.417  17.056  1.00 35.68 ? 139  GLU U N   1 
ATOM   1982 C CA  . GLU B 2 139 ? 29.416  -7.825  16.832  1.00 34.81 ? 139  GLU U CA  1 
ATOM   1983 C C   . GLU B 2 139 ? 30.415  -8.019  15.682  1.00 34.25 ? 139  GLU U C   1 
ATOM   1984 O O   . GLU B 2 139 ? 30.526  -7.185  14.783  1.00 34.79 ? 139  GLU U O   1 
ATOM   1985 C CB  . GLU B 2 139 ? 28.122  -8.569  16.552  1.00 34.54 ? 139  GLU U CB  1 
ATOM   1986 C CG  . GLU B 2 139 ? 27.307  -8.750  17.795  1.00 36.42 ? 139  GLU U CG  1 
ATOM   1987 C CD  . GLU B 2 139 ? 25.804  -8.591  17.574  1.00 39.69 ? 139  GLU U CD  1 
ATOM   1988 O OE1 . GLU B 2 139 ? 25.227  -7.527  17.941  1.00 39.39 ? 139  GLU U OE1 1 
ATOM   1989 O OE2 . GLU B 2 139 ? 25.190  -9.540  17.038  1.00 41.84 ? 139  GLU U OE2 1 
ATOM   1990 N N   . ASP B 2 140 ? 31.169  -9.103  15.706  1.00 33.12 ? 140  ASP U N   1 
ATOM   1991 C CA  . ASP B 2 140 ? 32.093  -9.334  14.632  1.00 31.79 ? 140  ASP U CA  1 
ATOM   1992 C C   . ASP B 2 140 ? 31.314  -9.795  13.433  1.00 30.93 ? 140  ASP U C   1 
ATOM   1993 O O   . ASP B 2 140 ? 31.418  -9.220  12.367  1.00 31.11 ? 140  ASP U O   1 
ATOM   1994 C CB  . ASP B 2 140 ? 33.160  -10.324 15.052  1.00 31.99 ? 140  ASP U CB  1 
ATOM   1995 C CG  . ASP B 2 140 ? 34.169  -9.707  16.002  1.00 32.78 ? 140  ASP U CG  1 
ATOM   1996 O OD1 . ASP B 2 140 ? 33.768  -8.873  16.852  1.00 34.59 ? 140  ASP U OD1 1 
ATOM   1997 O OD2 . ASP B 2 140 ? 35.366  -10.049 15.903  1.00 32.55 ? 140  ASP U OD2 1 
ATOM   1998 N N   . TYR B 2 141 ? 30.494  -10.809 13.613  1.00 29.77 ? 141  TYR U N   1 
ATOM   1999 C CA  . TYR B 2 141 ? 29.723  -11.307 12.511  1.00 28.90 ? 141  TYR U CA  1 
ATOM   2000 C C   . TYR B 2 141 ? 28.277  -11.263 12.911  1.00 28.66 ? 141  TYR U C   1 
ATOM   2001 O O   . TYR B 2 141 ? 27.936  -11.568 14.059  1.00 28.44 ? 141  TYR U O   1 
ATOM   2002 C CB  . TYR B 2 141 ? 30.135  -12.733 12.169  1.00 28.69 ? 141  TYR U CB  1 
ATOM   2003 C CG  . TYR B 2 141 ? 31.584  -12.902 11.733  1.00 28.92 ? 141  TYR U CG  1 
ATOM   2004 C CD1 . TYR B 2 141 ? 32.441  -13.774 12.407  1.00 28.78 ? 141  TYR U CD1 1 
ATOM   2005 C CD2 . TYR B 2 141 ? 32.097  -12.209 10.629  1.00 30.40 ? 141  TYR U CD2 1 
ATOM   2006 C CE1 . TYR B 2 141 ? 33.776  -13.949 11.998  1.00 28.67 ? 141  TYR U CE1 1 
ATOM   2007 C CE2 . TYR B 2 141 ? 33.435  -12.378 10.210  1.00 29.61 ? 141  TYR U CE2 1 
ATOM   2008 C CZ  . TYR B 2 141 ? 34.261  -13.246 10.902  1.00 29.04 ? 141  TYR U CZ  1 
ATOM   2009 O OH  . TYR B 2 141 ? 35.568  -13.408 10.499  1.00 28.66 ? 141  TYR U OH  1 
ATOM   2010 N N   . THR B 2 142 ? 27.436  -10.849 11.968  1.00 28.35 ? 142  THR U N   1 
ATOM   2011 C CA  . THR B 2 142 ? 25.992  -10.821 12.156  1.00 28.30 ? 142  THR U CA  1 
ATOM   2012 C C   . THR B 2 142 ? 25.323  -11.197 10.858  1.00 28.30 ? 142  THR U C   1 
ATOM   2013 O O   . THR B 2 142 ? 25.684  -10.679 9.810   1.00 28.63 ? 142  THR U O   1 
ATOM   2014 C CB  . THR B 2 142 ? 25.480  -9.428  12.595  1.00 28.27 ? 142  THR U CB  1 
ATOM   2015 O OG1 . THR B 2 142 ? 25.749  -9.225  13.983  1.00 29.07 ? 142  THR U OG1 1 
ATOM   2016 C CG2 . THR B 2 142 ? 23.979  -9.303  12.405  1.00 28.48 ? 142  THR U CG2 1 
ATOM   2017 N N   . ARG B 2 143 ? 24.347  -12.097 10.940  1.00 28.33 ? 143  ARG U N   1 
ATOM   2018 C CA  . ARG B 2 143 ? 23.540  -12.499 9.799   1.00 28.51 ? 143  ARG U CA  1 
ATOM   2019 C C   . ARG B 2 143 ? 22.081  -12.276 10.137  1.00 28.62 ? 143  ARG U C   1 
ATOM   2020 O O   . ARG B 2 143 ? 21.649  -12.687 11.197  1.00 28.80 ? 143  ARG U O   1 
ATOM   2021 C CB  . ARG B 2 143 ? 23.749  -13.977 9.510   1.00 28.59 ? 143  ARG U CB  1 
ATOM   2022 C CG  . ARG B 2 143 ? 25.103  -14.335 8.950   1.00 28.92 ? 143  ARG U CG  1 
ATOM   2023 C CD  . ARG B 2 143 ? 25.042  -15.705 8.328   1.00 28.92 ? 143  ARG U CD  1 
ATOM   2024 N NE  . ARG B 2 143 ? 26.200  -15.999 7.492   1.00 28.23 ? 143  ARG U NE  1 
ATOM   2025 C CZ  . ARG B 2 143 ? 27.247  -16.691 7.910   1.00 29.34 ? 143  ARG U CZ  1 
ATOM   2026 N NH1 . ARG B 2 143 ? 27.271  -17.129 9.167   1.00 30.85 ? 143  ARG U NH1 1 
ATOM   2027 N NH2 . ARG B 2 143 ? 28.268  -16.930 7.090   1.00 28.70 ? 143  ARG U NH2 1 
ATOM   2028 N N   . GLY B 2 144 ? 21.320  -11.644 9.245   1.00 28.77 ? 144  GLY U N   1 
ATOM   2029 C CA  . GLY B 2 144 ? 19.918  -11.344 9.521   1.00 28.99 ? 144  GLY U CA  1 
ATOM   2030 C C   . GLY B 2 144 ? 19.147  -10.879 8.312   1.00 29.62 ? 144  GLY U C   1 
ATOM   2031 O O   . GLY B 2 144 ? 19.640  -10.974 7.189   1.00 29.84 ? 144  GLY U O   1 
ATOM   2032 N N   . CYS B 2 145 ? 17.930  -10.392 8.541   1.00 30.27 ? 145  CYS U N   1 
ATOM   2033 C CA  . CYS B 2 145 ? 17.095  -9.830  7.486   1.00 31.47 ? 145  CYS U CA  1 
ATOM   2034 C C   . CYS B 2 145 ? 17.104  -8.315  7.537   1.00 31.37 ? 145  CYS U C   1 
ATOM   2035 O O   . CYS B 2 145 ? 17.155  -7.745  8.616   1.00 31.65 ? 145  CYS U O   1 
ATOM   2036 C CB  . CYS B 2 145 ? 15.659  -10.312 7.626   1.00 31.48 ? 145  CYS U CB  1 
ATOM   2037 S SG  . CYS B 2 145 ? 15.236  -11.761 6.595   1.00 36.78 ? 145  CYS U SG  1 
ATOM   2038 N N   . GLY B 2 146 ? 17.055  -7.666  6.374   1.00 31.58 ? 146  GLY U N   1 
ATOM   2039 C CA  . GLY B 2 146 ? 16.820  -6.217  6.303   1.00 31.97 ? 146  GLY U CA  1 
ATOM   2040 C C   . GLY B 2 146 ? 17.464  -5.425  5.178   1.00 32.10 ? 146  GLY U C   1 
ATOM   2041 O O   . GLY B 2 146 ? 18.187  -5.979  4.364   1.00 32.60 ? 146  GLY U O   1 
ATOM   2042 N N   . SER B 2 147 ? 17.211  -4.118  5.147   1.00 32.18 ? 147  SER U N   1 
ATOM   2043 C CA  . SER B 2 147 ? 17.746  -3.242  4.100   1.00 32.41 ? 147  SER U CA  1 
ATOM   2044 C C   . SER B 2 147 ? 18.694  -2.164  4.623   1.00 32.51 ? 147  SER U C   1 
ATOM   2045 O O   . SER B 2 147 ? 18.380  -1.462  5.570   1.00 32.35 ? 147  SER U O   1 
ATOM   2046 C CB  . SER B 2 147 ? 16.598  -2.574  3.333   1.00 32.70 ? 147  SER U CB  1 
ATOM   2047 O OG  . SER B 2 147 ? 15.969  -1.578  4.127   1.00 32.05 ? 147  SER U OG  1 
ATOM   2048 N N   . LEU B 2 148 ? 19.850  -2.024  3.986   1.00 32.91 ? 148  LEU U N   1 
ATOM   2049 C CA  . LEU B 2 148 ? 20.806  -0.990  4.355   1.00 33.21 ? 148  LEU U CA  1 
ATOM   2050 C C   . LEU B 2 148 ? 21.305  -0.259  3.112   1.00 33.86 ? 148  LEU U C   1 
ATOM   2051 O O   . LEU B 2 148 ? 20.947  -0.626  1.985   1.00 33.62 ? 148  LEU U O   1 
ATOM   2052 C CB  . LEU B 2 148 ? 21.984  -1.602  5.105   1.00 33.04 ? 148  LEU U CB  1 
ATOM   2053 C CG  . LEU B 2 148 ? 21.704  -2.671  6.161   1.00 32.90 ? 148  LEU U CG  1 
ATOM   2054 C CD1 . LEU B 2 148 ? 22.991  -3.296  6.651   1.00 32.74 ? 148  LEU U CD1 1 
ATOM   2055 C CD2 . LEU B 2 148 ? 20.920  -2.130  7.320   1.00 33.48 ? 148  LEU U CD2 1 
ATOM   2056 N N   . PRO B 2 149 ? 22.145  0.779   3.307   1.00 34.56 ? 149  PRO U N   1 
ATOM   2057 C CA  . PRO B 2 149 ? 22.602  1.564   2.165   1.00 34.97 ? 149  PRO U CA  1 
ATOM   2058 C C   . PRO B 2 149 ? 23.197  0.670   1.115   1.00 35.45 ? 149  PRO U C   1 
ATOM   2059 O O   . PRO B 2 149 ? 23.954  -0.252  1.432   1.00 35.33 ? 149  PRO U O   1 
ATOM   2060 C CB  . PRO B 2 149 ? 23.682  2.483   2.749   1.00 35.12 ? 149  PRO U CB  1 
ATOM   2061 C CG  . PRO B 2 149 ? 23.975  1.960   4.123   1.00 34.86 ? 149  PRO U CG  1 
ATOM   2062 C CD  . PRO B 2 149 ? 22.723  1.273   4.570   1.00 34.65 ? 149  PRO U CD  1 
ATOM   2063 N N   . GLY B 2 150 ? 22.812  0.944   -0.126  1.00 36.23 ? 150  GLY U N   1 
ATOM   2064 C CA  . GLY B 2 150 ? 23.270  0.205   -1.296  1.00 36.67 ? 150  GLY U CA  1 
ATOM   2065 C C   . GLY B 2 150 ? 23.093  -1.267  -1.066  1.00 36.93 ? 150  GLY U C   1 
ATOM   2066 O O   . GLY B 2 150 ? 24.075  -1.993  -0.903  1.00 36.48 ? 150  GLY U O   1 
ATOM   2067 N N   . CYS B 2 151 ? 21.843  -1.711  -1.035  1.00 37.81 ? 151  CYS U N   1 
ATOM   2068 C CA  . CYS B 2 151 ? 21.617  -3.085  -0.622  1.00 38.91 ? 151  CYS U CA  1 
ATOM   2069 C C   . CYS B 2 151 ? 21.945  -4.130  -1.702  1.00 38.83 ? 151  CYS U C   1 
ATOM   2070 O O   . CYS B 2 151 ? 23.117  -4.527  -1.806  1.00 39.14 ? 151  CYS U O   1 
ATOM   2071 C CB  . CYS B 2 151 ? 20.283  -3.305  0.112   1.00 39.20 ? 151  CYS U CB  1 
ATOM   2072 S SG  . CYS B 2 151 ? 20.554  -4.338  1.612   1.00 40.49 ? 151  CYS U SG  1 
ATOM   2073 N N   . PRO B 2 152 ? 20.960  -4.553  -2.521  1.00 38.49 ? 152  PRO U N   1 
ATOM   2074 C CA  . PRO B 2 152 ? 21.323  -5.716  -3.337  1.00 38.02 ? 152  PRO U CA  1 
ATOM   2075 C C   . PRO B 2 152 ? 22.741  -5.507  -3.836  1.00 37.63 ? 152  PRO U C   1 
ATOM   2076 O O   . PRO B 2 152 ? 23.004  -4.566  -4.585  1.00 37.56 ? 152  PRO U O   1 
ATOM   2077 C CB  . PRO B 2 152 ? 20.310  -5.691  -4.489  1.00 37.87 ? 152  PRO U CB  1 
ATOM   2078 C CG  . PRO B 2 152 ? 19.803  -4.298  -4.539  1.00 38.65 ? 152  PRO U CG  1 
ATOM   2079 C CD  . PRO B 2 152 ? 19.853  -3.781  -3.110  1.00 38.69 ? 152  PRO U CD  1 
ATOM   2080 N N   . GLY B 2 153 ? 23.656  -6.341  -3.358  1.00 37.41 ? 153  GLY U N   1 
ATOM   2081 C CA  . GLY B 2 153 ? 25.074  -6.161  -3.633  1.00 37.48 ? 153  GLY U CA  1 
ATOM   2082 C C   . GLY B 2 153 ? 25.877  -6.193  -2.352  1.00 37.47 ? 153  GLY U C   1 
ATOM   2083 O O   . GLY B 2 153 ? 25.529  -6.920  -1.428  1.00 37.49 ? 153  GLY U O   1 
ATOM   2084 N N   . THR B 2 154 ? 26.936  -5.381  -2.291  1.00 37.57 ? 154  THR U N   1 
ATOM   2085 C CA  . THR B 2 154 ? 27.990  -5.503  -1.262  1.00 37.19 ? 154  THR U CA  1 
ATOM   2086 C C   . THR B 2 154 ? 28.753  -4.204  -0.985  1.00 36.96 ? 154  THR U C   1 
ATOM   2087 O O   . THR B 2 154 ? 28.962  -3.402  -1.887  1.00 37.01 ? 154  THR U O   1 
ATOM   2088 C CB  . THR B 2 154 ? 29.069  -6.532  -1.709  1.00 37.21 ? 154  THR U CB  1 
ATOM   2089 O OG1 . THR B 2 154 ? 29.293  -6.412  -3.127  1.00 36.75 ? 154  THR U OG1 1 
ATOM   2090 C CG2 . THR B 2 154 ? 28.659  -7.966  -1.356  1.00 36.68 ? 154  THR U CG2 1 
ATOM   2091 N N   . ALA B 2 155 ? 29.202  -4.026  0.254   1.00 36.70 ? 155  ALA U N   1 
ATOM   2092 C CA  . ALA B 2 155 ? 30.172  -2.973  0.584   1.00 36.47 ? 155  ALA U CA  1 
ATOM   2093 C C   . ALA B 2 155 ? 31.272  -3.474  1.525   1.00 36.27 ? 155  ALA U C   1 
ATOM   2094 O O   . ALA B 2 155 ? 31.102  -4.489  2.208   1.00 36.49 ? 155  ALA U O   1 
ATOM   2095 C CB  . ALA B 2 155 ? 29.468  -1.776  1.183   1.00 36.53 ? 155  ALA U CB  1 
ATOM   2096 N N   . GLY B 2 156 ? 32.392  -2.761  1.576   1.00 35.87 ? 156  GLY U N   1 
ATOM   2097 C CA  . GLY B 2 156 ? 33.504  -3.195  2.403   1.00 35.66 ? 156  GLY U CA  1 
ATOM   2098 C C   . GLY B 2 156 ? 34.787  -2.418  2.243   1.00 35.69 ? 156  GLY U C   1 
ATOM   2099 O O   . GLY B 2 156 ? 35.043  -1.773  1.225   1.00 35.63 ? 156  GLY U O   1 
ATOM   2100 N N   . PHE B 2 157 ? 35.606  -2.499  3.273   1.00 35.88 ? 157  PHE U N   1 
ATOM   2101 C CA  . PHE B 2 157 ? 36.842  -1.777  3.324   1.00 36.25 ? 157  PHE U CA  1 
ATOM   2102 C C   . PHE B 2 157 ? 37.694  -2.391  4.396   1.00 36.39 ? 157  PHE U C   1 
ATOM   2103 O O   . PHE B 2 157 ? 37.215  -2.678  5.493   1.00 36.24 ? 157  PHE U O   1 
ATOM   2104 C CB  . PHE B 2 157 ? 36.578  -0.319  3.678   1.00 36.52 ? 157  PHE U CB  1 
ATOM   2105 C CG  . PHE B 2 157 ? 37.667  0.315   4.504   1.00 37.49 ? 157  PHE U CG  1 
ATOM   2106 C CD1 . PHE B 2 157 ? 38.936  0.569   3.953   1.00 37.57 ? 157  PHE U CD1 1 
ATOM   2107 C CD2 . PHE B 2 157 ? 37.427  0.663   5.831   1.00 37.33 ? 157  PHE U CD2 1 
ATOM   2108 C CE1 . PHE B 2 157 ? 39.944  1.146   4.710   1.00 37.18 ? 157  PHE U CE1 1 
ATOM   2109 C CE2 . PHE B 2 157 ? 38.437  1.245   6.598   1.00 37.69 ? 157  PHE U CE2 1 
ATOM   2110 C CZ  . PHE B 2 157 ? 39.696  1.488   6.035   1.00 37.48 ? 157  PHE U CZ  1 
ATOM   2111 N N   . HIS B 2 158 ? 38.969  -2.563  4.090   1.00 36.77 ? 158  HIS U N   1 
ATOM   2112 C CA  . HIS B 2 158 ? 39.880  -3.061  5.081   1.00 37.40 ? 158  HIS U CA  1 
ATOM   2113 C C   . HIS B 2 158 ? 41.056  -2.135  5.302   1.00 38.07 ? 158  HIS U C   1 
ATOM   2114 O O   . HIS B 2 158 ? 41.474  -1.407  4.401   1.00 37.98 ? 158  HIS U O   1 
ATOM   2115 C CB  . HIS B 2 158 ? 40.350  -4.470  4.728   1.00 37.43 ? 158  HIS U CB  1 
ATOM   2116 C CG  . HIS B 2 158 ? 41.509  -4.511  3.783   1.00 36.93 ? 158  HIS U CG  1 
ATOM   2117 N ND1 . HIS B 2 158 ? 41.359  -4.410  2.418   1.00 36.54 ? 158  HIS U ND1 1 
ATOM   2118 C CD2 . HIS B 2 158 ? 42.835  -4.665  4.008   1.00 36.18 ? 158  HIS U CD2 1 
ATOM   2119 C CE1 . HIS B 2 158 ? 42.545  -4.491  1.843   1.00 36.81 ? 158  HIS U CE1 1 
ATOM   2120 N NE2 . HIS B 2 158 ? 43.456  -4.650  2.785   1.00 36.60 ? 158  HIS U NE2 1 
ATOM   2121 N N   . SER B 2 159 ? 41.558  -2.179  6.533   1.00 38.98 ? 159  SER U N   1 
ATOM   2122 C CA  . SER B 2 159 ? 42.721  -1.441  6.978   1.00 39.66 ? 159  SER U CA  1 
ATOM   2123 C C   . SER B 2 159 ? 43.685  -2.434  7.602   1.00 40.23 ? 159  SER U C   1 
ATOM   2124 O O   . SER B 2 159 ? 43.349  -3.611  7.757   1.00 40.05 ? 159  SER U O   1 
ATOM   2125 C CB  . SER B 2 159 ? 42.298  -0.413  8.019   1.00 39.47 ? 159  SER U CB  1 
ATOM   2126 O OG  . SER B 2 159 ? 43.431  0.169   8.624   1.00 39.97 ? 159  SER U OG  1 
ATOM   2127 N N   . ASN B 2 160 ? 44.878  -1.959  7.960   1.00 41.17 ? 160  ASN U N   1 
ATOM   2128 C CA  . ASN B 2 160 ? 45.844  -2.777  8.678   1.00 42.29 ? 160  ASN U CA  1 
ATOM   2129 C C   . ASN B 2 160 ? 45.206  -3.408  9.916   1.00 41.57 ? 160  ASN U C   1 
ATOM   2130 O O   . ASN B 2 160 ? 45.376  -4.599  10.149  1.00 41.72 ? 160  ASN U O   1 
ATOM   2131 C CB  . ASN B 2 160 ? 47.091  -1.961  9.039   1.00 43.26 ? 160  ASN U CB  1 
ATOM   2132 C CG  . ASN B 2 160 ? 48.013  -2.682  10.012  1.00 48.93 ? 160  ASN U CG  1 
ATOM   2133 O OD1 . ASN B 2 160 ? 49.137  -3.057  9.668   1.00 49.60 ? 160  ASN U OD1 1 
ATOM   2134 N ND2 . ASN B 2 160 ? 47.532  -2.876  11.240  1.00 59.15 ? 160  ASN U ND2 1 
ATOM   2135 N N   . GLN B 2 161 ? 44.453  -2.620  10.686  1.00 40.93 ? 161  GLN U N   1 
ATOM   2136 C CA  . GLN B 2 161 ? 43.873  -3.089  11.958  1.00 39.94 ? 161  GLN U CA  1 
ATOM   2137 C C   . GLN B 2 161 ? 42.363  -3.247  11.916  1.00 39.07 ? 161  GLN U C   1 
ATOM   2138 O O   . GLN B 2 161 ? 41.740  -3.526  12.940  1.00 39.12 ? 161  GLN U O   1 
ATOM   2139 C CB  . GLN B 2 161 ? 44.211  -2.156  13.139  1.00 40.07 ? 161  GLN U CB  1 
ATOM   2140 C CG  . GLN B 2 161 ? 45.398  -1.221  12.964  1.00 40.44 ? 161  GLN U CG  1 
ATOM   2141 C CD  . GLN B 2 161 ? 45.017  0.090   12.295  1.00 40.56 ? 161  GLN U CD  1 
ATOM   2142 O OE1 . GLN B 2 161 ? 43.858  0.518   12.358  1.00 39.37 ? 161  GLN U OE1 1 
ATOM   2143 N NE2 . GLN B 2 161 ? 45.998  0.737   11.648  1.00 40.41 ? 161  GLN U NE2 1 
ATOM   2144 N N   . THR B 2 162 ? 41.761  -3.060  10.752  1.00 37.97 ? 162  THR U N   1 
ATOM   2145 C CA  . THR B 2 162 ? 40.308  -3.035  10.705  1.00 36.87 ? 162  THR U CA  1 
ATOM   2146 C C   . THR B 2 162 ? 39.735  -3.595  9.418   1.00 36.14 ? 162  THR U C   1 
ATOM   2147 O O   . THR B 2 162 ? 40.318  -3.451  8.350   1.00 36.26 ? 162  THR U O   1 
ATOM   2148 C CB  . THR B 2 162 ? 39.793  -1.619  10.905  1.00 36.86 ? 162  THR U CB  1 
ATOM   2149 O OG1 . THR B 2 162 ? 40.801  -0.849  11.572  1.00 36.59 ? 162  THR U OG1 1 
ATOM   2150 C CG2 . THR B 2 162 ? 38.525  -1.643  11.735  1.00 36.70 ? 162  THR U CG2 1 
ATOM   2151 N N   . PHE B 2 163 ? 38.586  -4.242  9.529   1.00 34.97 ? 163  PHE U N   1 
ATOM   2152 C CA  . PHE B 2 163 ? 37.919  -4.762  8.355   1.00 33.94 ? 163  PHE U CA  1 
ATOM   2153 C C   . PHE B 2 163 ? 36.397  -4.785  8.495   1.00 32.98 ? 163  PHE U C   1 
ATOM   2154 O O   . PHE B 2 163 ? 35.832  -5.480  9.350   1.00 32.79 ? 163  PHE U O   1 
ATOM   2155 C CB  . PHE B 2 163 ? 38.462  -6.139  8.003   1.00 34.13 ? 163  PHE U CB  1 
ATOM   2156 C CG  . PHE B 2 163 ? 37.612  -6.893  7.017   1.00 35.43 ? 163  PHE U CG  1 
ATOM   2157 C CD1 . PHE B 2 163 ? 37.409  -6.405  5.726   1.00 35.89 ? 163  PHE U CD1 1 
ATOM   2158 C CD2 . PHE B 2 163 ? 37.021  -8.107  7.374   1.00 36.55 ? 163  PHE U CD2 1 
ATOM   2159 C CE1 . PHE B 2 163 ? 36.619  -7.100  4.811   1.00 35.34 ? 163  PHE U CE1 1 
ATOM   2160 C CE2 . PHE B 2 163 ? 36.237  -8.815  6.458   1.00 36.44 ? 163  PHE U CE2 1 
ATOM   2161 C CZ  . PHE B 2 163 ? 36.038  -8.301  5.176   1.00 35.96 ? 163  PHE U CZ  1 
ATOM   2162 N N   . HIS B 2 164 ? 35.746  -4.018  7.632   1.00 31.68 ? 164  HIS U N   1 
ATOM   2163 C CA  . HIS B 2 164 ? 34.311  -3.998  7.585   1.00 30.59 ? 164  HIS U CA  1 
ATOM   2164 C C   . HIS B 2 164 ? 33.865  -4.569  6.274   1.00 29.63 ? 164  HIS U C   1 
ATOM   2165 O O   . HIS B 2 164 ? 34.593  -4.544  5.299   1.00 29.28 ? 164  HIS U O   1 
ATOM   2166 C CB  . HIS B 2 164 ? 33.775  -2.583  7.716   1.00 30.81 ? 164  HIS U CB  1 
ATOM   2167 C CG  . HIS B 2 164 ? 34.234  -1.874  8.946   1.00 31.28 ? 164  HIS U CG  1 
ATOM   2168 N ND1 . HIS B 2 164 ? 35.268  -0.964  8.936   1.00 32.39 ? 164  HIS U ND1 1 
ATOM   2169 C CD2 . HIS B 2 164 ? 33.799  -1.935  10.223  1.00 32.53 ? 164  HIS U CD2 1 
ATOM   2170 C CE1 . HIS B 2 164 ? 35.452  -0.491  10.154  1.00 32.67 ? 164  HIS U CE1 1 
ATOM   2171 N NE2 . HIS B 2 164 ? 34.575  -1.068  10.955  1.00 33.78 ? 164  HIS U NE2 1 
ATOM   2172 N N   . PHE B 2 165 ? 32.642  -5.071  6.265   1.00 28.82 ? 165  PHE U N   1 
ATOM   2173 C CA  . PHE B 2 165 ? 32.057  -5.606  5.079   1.00 27.95 ? 165  PHE U CA  1 
ATOM   2174 C C   . PHE B 2 165 ? 30.591  -5.917  5.310   1.00 27.80 ? 165  PHE U C   1 
ATOM   2175 O O   . PHE B 2 165 ? 30.207  -6.484  6.333   1.00 27.48 ? 165  PHE U O   1 
ATOM   2176 C CB  . PHE B 2 165 ? 32.811  -6.855  4.683   1.00 27.72 ? 165  PHE U CB  1 
ATOM   2177 C CG  . PHE B 2 165 ? 32.392  -7.418  3.384   1.00 26.98 ? 165  PHE U CG  1 
ATOM   2178 C CD1 . PHE B 2 165 ? 31.369  -8.352  3.323   1.00 26.22 ? 165  PHE U CD1 1 
ATOM   2179 C CD2 . PHE B 2 165 ? 33.035  -7.039  2.223   1.00 26.64 ? 165  PHE U CD2 1 
ATOM   2180 C CE1 . PHE B 2 165 ? 30.980  -8.887  2.132   1.00 26.76 ? 165  PHE U CE1 1 
ATOM   2181 C CE2 . PHE B 2 165 ? 32.659  -7.572  1.015   1.00 26.89 ? 165  PHE U CE2 1 
ATOM   2182 C CZ  . PHE B 2 165 ? 31.625  -8.499  0.962   1.00 27.23 ? 165  PHE U CZ  1 
ATOM   2183 N N   . LEU B 2 166 ? 29.787  -5.538  4.331   1.00 27.81 ? 166  LEU U N   1 
ATOM   2184 C CA  . LEU B 2 166 ? 28.378  -5.838  4.295   1.00 28.18 ? 166  LEU U CA  1 
ATOM   2185 C C   . LEU B 2 166 ? 28.161  -6.713  3.070   1.00 29.33 ? 166  LEU U C   1 
ATOM   2186 O O   . LEU B 2 166 ? 28.904  -6.628  2.109   1.00 29.35 ? 166  LEU U O   1 
ATOM   2187 C CB  . LEU B 2 166 ? 27.598  -4.536  4.117   1.00 27.68 ? 166  LEU U CB  1 
ATOM   2188 C CG  . LEU B 2 166 ? 26.166  -4.296  4.603   1.00 25.43 ? 166  LEU U CG  1 
ATOM   2189 C CD1 . LEU B 2 166 ? 25.550  -3.098  3.879   1.00 21.72 ? 166  LEU U CD1 1 
ATOM   2190 C CD2 . LEU B 2 166 ? 25.300  -5.519  4.428   1.00 24.54 ? 166  LEU U CD2 1 
ATOM   2191 N N   . LYS B 2 167 ? 27.146  -7.560  3.114   1.00 30.84 ? 167  LYS U N   1 
ATOM   2192 C CA  . LYS B 2 167 ? 26.673  -8.295  1.942   1.00 32.43 ? 167  LYS U CA  1 
ATOM   2193 C C   . LYS B 2 167 ? 25.153  -8.409  2.047   1.00 33.90 ? 167  LYS U C   1 
ATOM   2194 O O   . LYS B 2 167 ? 24.609  -8.718  3.110   1.00 34.36 ? 167  LYS U O   1 
ATOM   2195 C CB  . LYS B 2 167 ? 27.325  -9.683  1.850   1.00 32.20 ? 167  LYS U CB  1 
ATOM   2196 C CG  . LYS B 2 167 ? 26.523  -10.723 1.058   1.00 31.74 ? 167  LYS U CG  1 
ATOM   2197 C CD  . LYS B 2 167 ? 27.339  -11.990 0.753   1.00 32.12 ? 167  LYS U CD  1 
ATOM   2198 C CE  . LYS B 2 167 ? 26.441  -13.236 0.532   1.00 32.01 ? 167  LYS U CE  1 
ATOM   2199 N NZ  . LYS B 2 167 ? 27.118  -14.374 -0.171  1.00 30.74 ? 167  LYS U NZ  1 
ATOM   2200 N N   . CYS B 2 168 ? 24.468  -8.164  0.940   1.00 35.39 ? 168  CYS U N   1 
ATOM   2201 C CA  . CYS B 2 168 ? 23.020  -8.054  0.958   1.00 36.73 ? 168  CYS U CA  1 
ATOM   2202 C C   . CYS B 2 168 ? 22.417  -8.695  -0.304  1.00 36.84 ? 168  CYS U C   1 
ATOM   2203 O O   . CYS B 2 168 ? 22.734  -8.272  -1.414  1.00 36.72 ? 168  CYS U O   1 
ATOM   2204 C CB  . CYS B 2 168 ? 22.638  -6.566  1.119   1.00 36.71 ? 168  CYS U CB  1 
ATOM   2205 S SG  . CYS B 2 168 ? 20.893  -6.205  0.827   1.00 40.09 ? 168  CYS U SG  1 
ATOM   2206 N N   . CYS B 2 169 ? 21.571  -9.716  -0.135  1.00 37.61 ? 169  CYS U N   1 
ATOM   2207 C CA  . CYS B 2 169 ? 20.940  -10.398 -1.297  1.00 38.69 ? 169  CYS U CA  1 
ATOM   2208 C C   . CYS B 2 169 ? 19.452  -10.810 -1.210  1.00 39.00 ? 169  CYS U C   1 
ATOM   2209 O O   . CYS B 2 169 ? 18.937  -11.148 -0.132  1.00 39.05 ? 169  CYS U O   1 
ATOM   2210 C CB  . CYS B 2 169 ? 21.792  -11.571 -1.799  1.00 38.71 ? 169  CYS U CB  1 
ATOM   2211 S SG  . CYS B 2 169 ? 22.596  -12.525 -0.524  1.00 40.02 ? 169  CYS U SG  1 
ATOM   2212 N N   . ASN B 2 170 ? 18.797  -10.806 -2.379  1.00 39.28 ? 170  ASN U N   1 
ATOM   2213 C CA  . ASN B 2 170 ? 17.367  -11.079 -2.506  1.00 39.69 ? 170  ASN U CA  1 
ATOM   2214 C C   . ASN B 2 170 ? 17.082  -12.548 -2.842  1.00 38.75 ? 170  ASN U C   1 
ATOM   2215 O O   . ASN B 2 170 ? 16.203  -12.847 -3.646  1.00 38.82 ? 170  ASN U O   1 
ATOM   2216 C CB  . ASN B 2 170 ? 16.744  -10.106 -3.532  1.00 40.34 ? 170  ASN U CB  1 
ATOM   2217 C CG  . ASN B 2 170 ? 15.275  -10.424 -3.875  1.00 44.29 ? 170  ASN U CG  1 
ATOM   2218 O OD1 . ASN B 2 170 ? 14.574  -11.160 -3.158  1.00 44.32 ? 170  ASN U OD1 1 
ATOM   2219 N ND2 . ASN B 2 170 ? 14.811  -9.835  -4.988  1.00 50.76 ? 170  ASN U ND2 1 
ATOM   2220 N N   . TYR B 2 171 ? 17.811  -13.473 -2.220  1.00 37.76 ? 171  TYR U N   1 
ATOM   2221 C CA  . TYR B 2 171 ? 17.564  -14.889 -2.489  1.00 36.69 ? 171  TYR U CA  1 
ATOM   2222 C C   . TYR B 2 171 ? 17.678  -15.833 -1.303  1.00 36.59 ? 171  TYR U C   1 
ATOM   2223 O O   . TYR B 2 171 ? 18.504  -15.654 -0.421  1.00 36.73 ? 171  TYR U O   1 
ATOM   2224 C CB  . TYR B 2 171 ? 18.363  -15.366 -3.701  1.00 36.42 ? 171  TYR U CB  1 
ATOM   2225 C CG  . TYR B 2 171 ? 19.732  -15.972 -3.488  1.00 34.92 ? 171  TYR U CG  1 
ATOM   2226 C CD1 . TYR B 2 171 ? 20.874  -15.333 -3.984  1.00 33.76 ? 171  TYR U CD1 1 
ATOM   2227 C CD2 . TYR B 2 171 ? 19.880  -17.229 -2.885  1.00 33.43 ? 171  TYR U CD2 1 
ATOM   2228 C CE1 . TYR B 2 171 ? 22.133  -15.901 -3.843  1.00 33.22 ? 171  TYR U CE1 1 
ATOM   2229 C CE2 . TYR B 2 171 ? 21.131  -17.809 -2.738  1.00 33.06 ? 171  TYR U CE2 1 
ATOM   2230 C CZ  . TYR B 2 171 ? 22.253  -17.138 -3.218  1.00 33.46 ? 171  TYR U CZ  1 
ATOM   2231 O OH  . TYR B 2 171 ? 23.493  -17.706 -3.074  1.00 34.01 ? 171  TYR U OH  1 
ATOM   2232 N N   . THR B 2 172 ? 16.827  -16.846 -1.302  1.00 36.33 ? 172  THR U N   1 
ATOM   2233 C CA  . THR B 2 172 ? 16.662  -17.722 -0.153  1.00 36.38 ? 172  THR U CA  1 
ATOM   2234 C C   . THR B 2 172 ? 17.981  -18.258 0.414   1.00 36.41 ? 172  THR U C   1 
ATOM   2235 O O   . THR B 2 172 ? 18.824  -18.785 -0.325  1.00 36.50 ? 172  THR U O   1 
ATOM   2236 C CB  . THR B 2 172 ? 15.678  -18.854 -0.471  1.00 36.35 ? 172  THR U CB  1 
ATOM   2237 O OG1 . THR B 2 172 ? 14.466  -18.276 -0.964  1.00 36.27 ? 172  THR U OG1 1 
ATOM   2238 C CG2 . THR B 2 172 ? 15.365  -19.683 0.779   1.00 36.69 ? 172  THR U CG2 1 
ATOM   2239 N N   . HIS B 2 173 ? 18.126  -18.091 1.734   1.00 36.18 ? 173  HIS U N   1 
ATOM   2240 C CA  . HIS B 2 173 ? 19.317  -18.442 2.500   1.00 36.02 ? 173  HIS U CA  1 
ATOM   2241 C C   . HIS B 2 173 ? 20.607  -18.004 1.870   1.00 36.13 ? 173  HIS U C   1 
ATOM   2242 O O   . HIS B 2 173 ? 21.632  -18.630 2.111   1.00 36.13 ? 173  HIS U O   1 
ATOM   2243 C CB  . HIS B 2 173 ? 19.392  -19.941 2.775   1.00 35.82 ? 173  HIS U CB  1 
ATOM   2244 C CG  . HIS B 2 173 ? 19.029  -20.306 4.174   1.00 36.39 ? 173  HIS U CG  1 
ATOM   2245 N ND1 . HIS B 2 173 ? 18.031  -21.208 4.476   1.00 36.85 ? 173  HIS U ND1 1 
ATOM   2246 C CD2 . HIS B 2 173 ? 19.513  -19.870 5.359   1.00 36.97 ? 173  HIS U CD2 1 
ATOM   2247 C CE1 . HIS B 2 173 ? 17.918  -21.316 5.786   1.00 36.78 ? 173  HIS U CE1 1 
ATOM   2248 N NE2 . HIS B 2 173 ? 18.806  -20.513 6.346   1.00 37.35 ? 173  HIS U NE2 1 
ATOM   2249 N N   . CYS B 2 174 ? 20.568  -16.923 1.095   1.00 36.44 ? 174  CYS U N   1 
ATOM   2250 C CA  . CYS B 2 174 ? 21.719  -16.525 0.278   1.00 37.25 ? 174  CYS U CA  1 
ATOM   2251 C C   . CYS B 2 174 ? 23.007  -16.276 1.045   1.00 37.33 ? 174  CYS U C   1 
ATOM   2252 O O   . CYS B 2 174 ? 24.051  -16.023 0.426   1.00 37.38 ? 174  CYS U O   1 
ATOM   2253 C CB  . CYS B 2 174 ? 21.403  -15.313 -0.602  1.00 37.53 ? 174  CYS U CB  1 
ATOM   2254 S SG  . CYS B 2 174 ? 21.120  -13.722 0.202   1.00 39.77 ? 174  CYS U SG  1 
ATOM   2255 N N   . ASN B 2 175 ? 22.922  -16.370 2.377   1.00 37.42 ? 175  ASN U N   1 
ATOM   2256 C CA  . ASN B 2 175 ? 24.011  -16.026 3.293   1.00 37.23 ? 175  ASN U CA  1 
ATOM   2257 C C   . ASN B 2 175 ? 24.392  -17.114 4.320   1.00 37.45 ? 175  ASN U C   1 
ATOM   2258 O O   . ASN B 2 175 ? 24.840  -16.810 5.418   1.00 37.75 ? 175  ASN U O   1 
ATOM   2259 C CB  . ASN B 2 175 ? 23.646  -14.736 4.021   1.00 36.73 ? 175  ASN U CB  1 
ATOM   2260 C CG  . ASN B 2 175 ? 22.357  -14.858 4.821   1.00 36.39 ? 175  ASN U CG  1 
ATOM   2261 O OD1 . ASN B 2 175 ? 21.439  -14.086 4.613   1.00 36.53 ? 175  ASN U OD1 1 
ATOM   2262 N ND2 . ASN B 2 175 ? 22.285  -15.826 5.738   1.00 35.55 ? 175  ASN U ND2 1 
ATOM   2263 N N   . GLY B 2 176 ? 24.212  -18.380 3.986   1.00 37.66 ? 176  GLY U N   1 
ATOM   2264 C CA  . GLY B 2 176 ? 24.604  -19.432 4.917   1.00 38.04 ? 176  GLY U CA  1 
ATOM   2265 C C   . GLY B 2 176 ? 26.090  -19.693 4.787   1.00 38.31 ? 176  GLY U C   1 
ATOM   2266 O O   . GLY B 2 176 ? 26.876  -18.760 4.597   1.00 38.08 ? 176  GLY U O   1 
ATOM   2267 N N   . GLY B 2 177 ? 26.463  -20.971 4.881   1.00 38.60 ? 177  GLY U N   1 
ATOM   2268 C CA  . GLY B 2 177 ? 27.842  -21.436 4.663   1.00 38.80 ? 177  GLY U CA  1 
ATOM   2269 C C   . GLY B 2 177 ? 28.976  -20.693 5.366   1.00 38.85 ? 177  GLY U C   1 
ATOM   2270 O O   . GLY B 2 177 ? 28.745  -20.000 6.361   1.00 38.80 ? 177  GLY U O   1 
ATOM   2271 N N   . PRO B 2 178 ? 30.214  -20.833 4.843   1.00 38.99 ? 178  PRO U N   1 
ATOM   2272 C CA  . PRO B 2 178 ? 31.412  -20.222 5.408   1.00 39.09 ? 178  PRO U CA  1 
ATOM   2273 C C   . PRO B 2 178 ? 31.159  -18.802 5.848   1.00 39.26 ? 178  PRO U C   1 
ATOM   2274 O O   . PRO B 2 178 ? 30.366  -18.091 5.237   1.00 39.48 ? 178  PRO U O   1 
ATOM   2275 C CB  . PRO B 2 178 ? 32.383  -20.197 4.228   1.00 39.08 ? 178  PRO U CB  1 
ATOM   2276 C CG  . PRO B 2 178 ? 31.998  -21.370 3.396   1.00 39.39 ? 178  PRO U CG  1 
ATOM   2277 C CD  . PRO B 2 178 ? 30.524  -21.620 3.631   1.00 39.24 ? 178  PRO U CD  1 
ATOM   2278 N N   . VAL B 2 179 ? 31.830  -18.391 6.910   1.00 39.36 ? 179  VAL U N   1 
ATOM   2279 C CA  . VAL B 2 179 ? 31.813  -16.998 7.308   1.00 39.25 ? 179  VAL U CA  1 
ATOM   2280 C C   . VAL B 2 179 ? 32.843  -16.274 6.411   1.00 39.37 ? 179  VAL U C   1 
ATOM   2281 O O   . VAL B 2 179 ? 33.236  -16.819 5.371   1.00 39.44 ? 179  VAL U O   1 
ATOM   2282 C CB  . VAL B 2 179 ? 32.127  -16.861 8.805   1.00 39.26 ? 179  VAL U CB  1 
ATOM   2283 C CG1 . VAL B 2 179 ? 31.386  -15.680 9.372   1.00 38.74 ? 179  VAL U CG1 1 
ATOM   2284 C CG2 . VAL B 2 179 ? 31.751  -18.152 9.558   1.00 38.88 ? 179  VAL U CG2 1 
ATOM   2285 N N   . LEU B 2 180 ? 33.281  -15.068 6.787   1.00 39.20 ? 180  LEU U N   1 
ATOM   2286 C CA  . LEU B 2 180 ? 34.246  -14.323 5.968   1.00 38.98 ? 180  LEU U CA  1 
ATOM   2287 C C   . LEU B 2 180 ? 35.397  -13.725 6.758   1.00 38.88 ? 180  LEU U C   1 
ATOM   2288 O O   . LEU B 2 180 ? 35.236  -12.706 7.414   1.00 38.95 ? 180  LEU U O   1 
ATOM   2289 C CB  . LEU B 2 180 ? 33.531  -13.217 5.205   1.00 39.05 ? 180  LEU U CB  1 
ATOM   2290 C CG  . LEU B 2 180 ? 32.321  -13.648 4.377   1.00 39.57 ? 180  LEU U CG  1 
ATOM   2291 C CD1 . LEU B 2 180 ? 31.278  -12.527 4.314   1.00 38.81 ? 180  LEU U CD1 1 
ATOM   2292 C CD2 . LEU B 2 180 ? 32.763  -14.137 2.976   1.00 39.64 ? 180  LEU U CD2 1 
ATOM   2293 N N   . ASP B 2 181 ? 36.561  -14.353 6.683   1.00 38.95 ? 181  ASP U N   1 
ATOM   2294 C CA  . ASP B 2 181 ? 37.748  -13.836 7.343   1.00 39.37 ? 181  ASP U CA  1 
ATOM   2295 C C   . ASP B 2 181 ? 38.602  -12.995 6.385   1.00 39.52 ? 181  ASP U C   1 
ATOM   2296 O O   . ASP B 2 181 ? 38.160  -12.623 5.298   1.00 39.45 ? 181  ASP U O   1 
ATOM   2297 C CB  . ASP B 2 181 ? 38.570  -14.995 7.909   1.00 39.58 ? 181  ASP U CB  1 
ATOM   2298 C CG  . ASP B 2 181 ? 39.231  -15.839 6.817   1.00 40.90 ? 181  ASP U CG  1 
ATOM   2299 O OD1 . ASP B 2 181 ? 38.501  -16.374 5.953   1.00 42.05 ? 181  ASP U OD1 1 
ATOM   2300 O OD2 . ASP B 2 181 ? 40.481  -15.972 6.825   1.00 41.56 ? 181  ASP U OD2 1 
ATOM   2301 N N   . LEU B 2 182 ? 39.832  -12.697 6.795   1.00 39.88 ? 182  LEU U N   1 
ATOM   2302 C CA  . LEU B 2 182 ? 40.795  -12.043 5.914   1.00 40.26 ? 182  LEU U CA  1 
ATOM   2303 C C   . LEU B 2 182 ? 41.241  -12.991 4.785   1.00 40.22 ? 182  LEU U C   1 
ATOM   2304 O O   . LEU B 2 182 ? 41.069  -12.676 3.606   1.00 40.43 ? 182  LEU U O   1 
ATOM   2305 C CB  . LEU B 2 182 ? 42.016  -11.513 6.707   1.00 40.48 ? 182  LEU U CB  1 
ATOM   2306 C CG  . LEU B 2 182 ? 43.288  -12.375 6.911   1.00 40.73 ? 182  LEU U CG  1 
ATOM   2307 C CD1 . LEU B 2 182 ? 44.562  -11.533 6.980   1.00 40.40 ? 182  LEU U CD1 1 
ATOM   2308 C CD2 . LEU B 2 182 ? 43.184  -13.305 8.128   1.00 41.09 ? 182  LEU U CD2 1 
ATOM   2309 N N   . GLN B 2 183 ? 41.782  -14.154 5.166   1.00 39.88 ? 183  GLN U N   1 
ATOM   2310 C CA  . GLN B 2 183 ? 42.462  -15.079 4.257   1.00 39.43 ? 183  GLN U CA  1 
ATOM   2311 C C   . GLN B 2 183 ? 41.592  -15.596 3.129   1.00 39.26 ? 183  GLN U C   1 
ATOM   2312 O O   . GLN B 2 183 ? 42.098  -16.105 2.124   1.00 39.25 ? 183  GLN U O   1 
ATOM   2313 C CB  . GLN B 2 183 ? 43.000  -16.263 5.037   1.00 39.41 ? 183  GLN U CB  1 
ATOM   2314 C CG  . GLN B 2 183 ? 44.224  -15.956 5.845   1.00 39.22 ? 183  GLN U CG  1 
ATOM   2315 C CD  . GLN B 2 183 ? 44.623  -17.129 6.696   1.00 39.19 ? 183  GLN U CD  1 
ATOM   2316 O OE1 . GLN B 2 183 ? 43.818  -17.658 7.466   1.00 39.08 ? 183  GLN U OE1 1 
ATOM   2317 N NE2 . GLN B 2 183 ? 45.870  -17.557 6.558   1.00 39.13 ? 183  GLN U NE2 1 
ATOM   2318 N N   . SER B 2 184 ? 40.282  -15.472 3.305   1.00 38.88 ? 184  SER U N   1 
ATOM   2319 C CA  . SER B 2 184 ? 39.330  -15.839 2.272   1.00 38.53 ? 184  SER U CA  1 
ATOM   2320 C C   . SER B 2 184 ? 39.342  -14.856 1.095   1.00 38.36 ? 184  SER U C   1 
ATOM   2321 O O   . SER B 2 184 ? 38.551  -14.998 0.164   1.00 38.53 ? 184  SER U O   1 
ATOM   2322 C CB  . SER B 2 184 ? 37.934  -15.931 2.870   1.00 38.29 ? 184  SER U CB  1 
ATOM   2323 O OG  . SER B 2 184 ? 37.725  -14.838 3.735   1.00 38.12 ? 184  SER U OG  1 
ATOM   2324 N N   . PHE B 2 185 ? 40.238  -13.872 1.124   1.00 38.08 ? 185  PHE U N   1 
ATOM   2325 C CA  . PHE B 2 185 ? 40.308  -12.892 0.039   1.00 37.87 ? 185  PHE U CA  1 
ATOM   2326 C C   . PHE B 2 185 ? 41.625  -12.902 -0.710  1.00 37.59 ? 185  PHE U C   1 
ATOM   2327 O O   . PHE B 2 185 ? 42.690  -12.943 -0.090  1.00 37.47 ? 185  PHE U O   1 
ATOM   2328 C CB  . PHE B 2 185 ? 39.953  -11.490 0.526   1.00 37.92 ? 185  PHE U CB  1 
ATOM   2329 C CG  . PHE B 2 185 ? 38.514  -11.347 0.881   1.00 38.22 ? 185  PHE U CG  1 
ATOM   2330 C CD1 . PHE B 2 185 ? 37.593  -10.946 -0.077  1.00 38.14 ? 185  PHE U CD1 1 
ATOM   2331 C CD2 . PHE B 2 185 ? 38.065  -11.659 2.170   1.00 38.71 ? 185  PHE U CD2 1 
ATOM   2332 C CE1 . PHE B 2 185 ? 36.240  -10.830 0.246   1.00 38.90 ? 185  PHE U CE1 1 
ATOM   2333 C CE2 . PHE B 2 185 ? 36.713  -11.550 2.508   1.00 38.76 ? 185  PHE U CE2 1 
ATOM   2334 C CZ  . PHE B 2 185 ? 35.797  -11.133 1.546   1.00 38.81 ? 185  PHE U CZ  1 
ATOM   2335 N N   . PRO B 2 186 ? 41.541  -12.853 -2.054  1.00 37.34 ? 186  PRO U N   1 
ATOM   2336 C CA  . PRO B 2 186 ? 42.696  -12.945 -2.938  1.00 37.15 ? 186  PRO U CA  1 
ATOM   2337 C C   . PRO B 2 186 ? 43.503  -11.653 -2.960  1.00 36.94 ? 186  PRO U C   1 
ATOM   2338 O O   . PRO B 2 186 ? 43.059  -10.672 -3.562  1.00 36.77 ? 186  PRO U O   1 
ATOM   2339 C CB  . PRO B 2 186 ? 42.062  -13.195 -4.311  1.00 37.27 ? 186  PRO U CB  1 
ATOM   2340 C CG  . PRO B 2 186 ? 40.705  -12.564 -4.228  1.00 37.22 ? 186  PRO U CG  1 
ATOM   2341 C CD  . PRO B 2 186 ? 40.276  -12.674 -2.800  1.00 37.23 ? 186  PRO U CD  1 
ATOM   2342 N N   . PRO B 2 187 ? 44.691  -11.649 -2.321  1.00 36.84 ? 187  PRO U N   1 
ATOM   2343 C CA  . PRO B 2 187 ? 45.506  -10.433 -2.364  1.00 36.76 ? 187  PRO U CA  1 
ATOM   2344 C C   . PRO B 2 187 ? 45.559  -9.971  -3.808  1.00 36.63 ? 187  PRO U C   1 
ATOM   2345 O O   . PRO B 2 187 ? 46.388  -10.454 -4.581  1.00 36.63 ? 187  PRO U O   1 
ATOM   2346 C CB  . PRO B 2 187 ? 46.893  -10.904 -1.905  1.00 36.80 ? 187  PRO U CB  1 
ATOM   2347 C CG  . PRO B 2 187 ? 46.660  -12.189 -1.186  1.00 36.96 ? 187  PRO U CG  1 
ATOM   2348 C CD  . PRO B 2 187 ? 45.421  -12.802 -1.758  1.00 36.85 ? 187  PRO U CD  1 
ATOM   2349 N N   . ASN B 2 188 ? 44.645  -9.071  -4.166  1.00 36.45 ? 188  ASN U N   1 
ATOM   2350 C CA  . ASN B 2 188 ? 44.454  -8.661  -5.552  1.00 36.42 ? 188  ASN U CA  1 
ATOM   2351 C C   . ASN B 2 188 ? 45.714  -8.121  -6.230  1.00 36.63 ? 188  ASN U C   1 
ATOM   2352 O O   . ASN B 2 188 ? 45.834  -8.183  -7.455  1.00 36.84 ? 188  ASN U O   1 
ATOM   2353 C CB  . ASN B 2 188 ? 43.316  -7.652  -5.654  1.00 36.25 ? 188  ASN U CB  1 
ATOM   2354 C CG  . ASN B 2 188 ? 43.551  -6.412  -4.813  1.00 35.60 ? 188  ASN U CG  1 
ATOM   2355 O OD1 . ASN B 2 188 ? 44.688  -5.990  -4.587  1.00 34.47 ? 188  ASN U OD1 1 
ATOM   2356 N ND2 . ASN B 2 188 ? 42.466  -5.810  -4.360  1.00 34.99 ? 188  ASN U ND2 1 
ATOM   2357 N N   . GLY B 2 189 ? 46.641  -7.595  -5.426  1.00 36.66 ? 189  GLY U N   1 
ATOM   2358 C CA  . GLY B 2 189 ? 47.939  -7.126  -5.916  1.00 36.56 ? 189  GLY U CA  1 
ATOM   2359 C C   . GLY B 2 189 ? 48.101  -5.623  -5.799  1.00 36.55 ? 189  GLY U C   1 
ATOM   2360 O O   . GLY B 2 189 ? 49.224  -5.106  -5.739  1.00 36.54 ? 189  GLY U O   1 
ATOM   2361 N N   . PHE B 2 190 ? 46.967  -4.926  -5.776  1.00 36.54 ? 190  PHE U N   1 
ATOM   2362 C CA  . PHE B 2 190 ? 46.940  -3.469  -5.651  1.00 36.37 ? 190  PHE U CA  1 
ATOM   2363 C C   . PHE B 2 190 ? 47.140  -3.102  -4.184  1.00 36.13 ? 190  PHE U C   1 
ATOM   2364 O O   . PHE B 2 190 ? 46.936  -3.935  -3.282  1.00 36.07 ? 190  PHE U O   1 
ATOM   2365 C CB  . PHE B 2 190 ? 45.626  -2.893  -6.208  1.00 36.38 ? 190  PHE U CB  1 
ATOM   2366 C CG  . PHE B 2 190 ? 45.180  -3.530  -7.509  1.00 36.76 ? 190  PHE U CG  1 
ATOM   2367 C CD1 . PHE B 2 190 ? 45.690  -3.092  -8.731  1.00 37.03 ? 190  PHE U CD1 1 
ATOM   2368 C CD2 . PHE B 2 190 ? 44.254  -4.579  -7.508  1.00 36.90 ? 190  PHE U CD2 1 
ATOM   2369 C CE1 . PHE B 2 190 ? 45.284  -3.690  -9.932  1.00 37.46 ? 190  PHE U CE1 1 
ATOM   2370 C CE2 . PHE B 2 190 ? 43.838  -5.182  -8.702  1.00 36.73 ? 190  PHE U CE2 1 
ATOM   2371 C CZ  . PHE B 2 190 ? 44.352  -4.736  -9.916  1.00 37.22 ? 190  PHE U CZ  1 
ATOM   2372 N N   . GLN B 2 191 ? 47.563  -1.867  -3.942  1.00 35.63 ? 191  GLN U N   1 
ATOM   2373 C CA  . GLN B 2 191 ? 47.910  -1.463  -2.588  1.00 35.17 ? 191  GLN U CA  1 
ATOM   2374 C C   . GLN B 2 191 ? 47.163  -0.214  -2.124  1.00 34.93 ? 191  GLN U C   1 
ATOM   2375 O O   . GLN B 2 191 ? 46.580  0.499   -2.939  1.00 34.96 ? 191  GLN U O   1 
ATOM   2376 C CB  . GLN B 2 191 ? 49.424  -1.278  -2.479  1.00 35.04 ? 191  GLN U CB  1 
ATOM   2377 C CG  . GLN B 2 191 ? 50.204  -2.502  -2.920  1.00 34.64 ? 191  GLN U CG  1 
ATOM   2378 C CD  . GLN B 2 191 ? 51.374  -2.808  -2.019  1.00 34.40 ? 191  GLN U CD  1 
ATOM   2379 O OE1 . GLN B 2 191 ? 52.522  -2.755  -2.448  1.00 34.61 ? 191  GLN U OE1 1 
ATOM   2380 N NE2 . GLN B 2 191 ? 51.092  -3.135  -0.762  1.00 34.11 ? 191  GLN U NE2 1 
ATOM   2381 N N   . CYS B 2 192 ? 47.166  0.022   -0.810  1.00 34.52 ? 192  CYS U N   1 
ATOM   2382 C CA  . CYS B 2 192 ? 46.699  1.288   -0.223  1.00 34.02 ? 192  CYS U CA  1 
ATOM   2383 C C   . CYS B 2 192 ? 47.551  1.715   0.993   1.00 33.96 ? 192  CYS U C   1 
ATOM   2384 O O   . CYS B 2 192 ? 48.625  1.156   1.233   1.00 33.79 ? 192  CYS U O   1 
ATOM   2385 C CB  . CYS B 2 192 ? 45.201  1.219   0.122   1.00 33.77 ? 192  CYS U CB  1 
ATOM   2386 S SG  . CYS B 2 192 ? 44.058  1.511   -1.280  1.00 32.74 ? 192  CYS U SG  1 
ATOM   2387 N N   . TYR B 2 193 ? 47.078  2.716   1.735   1.00 33.96 ? 193  TYR U N   1 
ATOM   2388 C CA  . TYR B 2 193 ? 47.719  3.147   2.982   1.00 34.02 ? 193  TYR U CA  1 
ATOM   2389 C C   . TYR B 2 193 ? 46.793  2.958   4.188   1.00 34.09 ? 193  TYR U C   1 
ATOM   2390 O O   . TYR B 2 193 ? 45.573  2.960   4.042   1.00 34.11 ? 193  TYR U O   1 
ATOM   2391 C CB  . TYR B 2 193 ? 48.133  4.613   2.887   1.00 34.06 ? 193  TYR U CB  1 
ATOM   2392 C CG  . TYR B 2 193 ? 49.245  4.894   1.905   1.00 33.92 ? 193  TYR U CG  1 
ATOM   2393 C CD1 . TYR B 2 193 ? 50.532  5.200   2.351   1.00 33.46 ? 193  TYR U CD1 1 
ATOM   2394 C CD2 . TYR B 2 193 ? 49.009  4.868   0.532   1.00 33.60 ? 193  TYR U CD2 1 
ATOM   2395 C CE1 . TYR B 2 193 ? 51.552  5.469   1.453   1.00 33.46 ? 193  TYR U CE1 1 
ATOM   2396 C CE2 . TYR B 2 193 ? 50.022  5.128   -0.375  1.00 33.80 ? 193  TYR U CE2 1 
ATOM   2397 C CZ  . TYR B 2 193 ? 51.291  5.428   0.089   1.00 33.56 ? 193  TYR U CZ  1 
ATOM   2398 O OH  . TYR B 2 193 ? 52.291  5.694   -0.817  1.00 33.27 ? 193  TYR U OH  1 
ATOM   2399 N N   . SER B 2 194 ? 47.381  2.798   5.374   1.00 34.16 ? 194  SER U N   1 
ATOM   2400 C CA  . SER B 2 194 ? 46.622  2.662   6.623   1.00 34.11 ? 194  SER U CA  1 
ATOM   2401 C C   . SER B 2 194 ? 47.149  3.656   7.666   1.00 34.21 ? 194  SER U C   1 
ATOM   2402 O O   . SER B 2 194 ? 48.321  3.604   8.044   1.00 34.24 ? 194  SER U O   1 
ATOM   2403 C CB  . SER B 2 194 ? 46.714  1.222   7.133   1.00 33.96 ? 194  SER U CB  1 
ATOM   2404 O OG  . SER B 2 194 ? 45.895  1.011   8.265   1.00 33.75 ? 194  SER U OG  1 
ATOM   2405 N N   . CYS B 2 195 ? 46.295  4.570   8.117   1.00 34.32 ? 195  CYS U N   1 
ATOM   2406 C CA  . CYS B 2 195 ? 46.733  5.610   9.047   1.00 34.76 ? 195  CYS U CA  1 
ATOM   2407 C C   . CYS B 2 195 ? 45.742  5.918   10.171  1.00 35.03 ? 195  CYS U C   1 
ATOM   2408 O O   . CYS B 2 195 ? 44.561  6.191   9.906   1.00 35.18 ? 195  CYS U O   1 
ATOM   2409 C CB  . CYS B 2 195 ? 47.081  6.902   8.299   1.00 34.71 ? 195  CYS U CB  1 
ATOM   2410 S SG  . CYS B 2 195 ? 46.893  8.397   9.326   1.00 35.12 ? 195  CYS U SG  1 
ATOM   2411 N N   . GLU B 2 196 ? 46.244  5.863   11.416  1.00 35.23 ? 196  GLU U N   1 
ATOM   2412 C CA  . GLU B 2 196 ? 45.503  6.256   12.649  1.00 35.21 ? 196  GLU U CA  1 
ATOM   2413 C C   . GLU B 2 196 ? 46.409  6.612   13.866  1.00 35.11 ? 196  GLU U C   1 
ATOM   2414 O O   . GLU B 2 196 ? 46.692  5.771   14.734  1.00 34.88 ? 196  GLU U O   1 
ATOM   2415 C CB  . GLU B 2 196 ? 44.389  5.247   13.034  1.00 35.09 ? 196  GLU U CB  1 
ATOM   2416 C CG  . GLU B 2 196 ? 44.652  3.769   12.699  1.00 35.20 ? 196  GLU U CG  1 
ATOM   2417 C CD  . GLU B 2 196 ? 44.190  3.369   11.291  1.00 35.04 ? 196  GLU U CD  1 
ATOM   2418 O OE1 . GLU B 2 196 ? 42.981  3.465   11.005  1.00 34.72 ? 196  GLU U OE1 1 
ATOM   2419 O OE2 . GLU B 2 196 ? 45.036  2.943   10.471  1.00 34.74 ? 196  GLU U OE2 1 
ATOM   2420 N N   . GLY B 2 197 ? 46.851  7.873   13.894  1.00 35.05 ? 197  GLY U N   1 
ATOM   2421 C CA  . GLY B 2 197 ? 47.608  8.468   15.006  1.00 34.90 ? 197  GLY U CA  1 
ATOM   2422 C C   . GLY B 2 197 ? 46.796  9.566   15.683  1.00 34.88 ? 197  GLY U C   1 
ATOM   2423 O O   . GLY B 2 197 ? 46.090  9.286   16.653  1.00 34.92 ? 197  GLY U O   1 
ATOM   2424 N N   . ASN B 2 198 ? 46.892  10.805  15.170  1.00 34.85 ? 198  ASN U N   1 
ATOM   2425 C CA  . ASN B 2 198 ? 46.045  11.964  15.603  1.00 34.57 ? 198  ASN U CA  1 
ATOM   2426 C C   . ASN B 2 198 ? 45.668  13.024  14.528  1.00 34.51 ? 198  ASN U C   1 
ATOM   2427 O O   . ASN B 2 198 ? 44.524  13.050  14.045  1.00 34.49 ? 198  ASN U O   1 
ATOM   2428 C CB  . ASN B 2 198 ? 46.639  12.651  16.838  1.00 34.32 ? 198  ASN U CB  1 
ATOM   2429 C CG  . ASN B 2 198 ? 46.362  11.886  18.101  1.00 33.68 ? 198  ASN U CG  1 
ATOM   2430 O OD1 . ASN B 2 198 ? 45.260  11.941  18.643  1.00 32.80 ? 198  ASN U OD1 1 
ATOM   2431 N ND2 . ASN B 2 198 ? 47.354  11.139  18.567  1.00 33.00 ? 198  ASN U ND2 1 
ATOM   2432 N N   . ASN B 2 199 ? 46.624  13.895  14.187  1.00 34.35 ? 199  ASN U N   1 
ATOM   2433 C CA  . ASN B 2 199 ? 46.466  14.933  13.156  1.00 34.15 ? 199  ASN U CA  1 
ATOM   2434 C C   . ASN B 2 199 ? 47.756  15.167  12.349  1.00 34.43 ? 199  ASN U C   1 
ATOM   2435 O O   . ASN B 2 199 ? 48.709  15.756  12.871  1.00 34.55 ? 199  ASN U O   1 
ATOM   2436 C CB  . ASN B 2 199 ? 46.049  16.264  13.795  1.00 33.83 ? 199  ASN U CB  1 
ATOM   2437 C CG  . ASN B 2 199 ? 44.555  16.392  13.993  1.00 32.89 ? 199  ASN U CG  1 
ATOM   2438 O OD1 . ASN B 2 199 ? 43.924  17.270  13.409  1.00 31.27 ? 199  ASN U OD1 1 
ATOM   2439 N ND2 . ASN B 2 199 ? 43.984  15.539  14.838  1.00 32.25 ? 199  ASN U ND2 1 
ATOM   2440 N N   . THR B 2 200 ? 47.782  14.699  11.093  1.00 34.62 ? 200  THR U N   1 
ATOM   2441 C CA  . THR B 2 200 ? 48.894  14.921  10.114  1.00 34.72 ? 200  THR U CA  1 
ATOM   2442 C C   . THR B 2 200 ? 50.271  14.260  10.417  1.00 34.87 ? 200  THR U C   1 
ATOM   2443 O O   . THR B 2 200 ? 50.909  13.719  9.504   1.00 34.83 ? 200  THR U O   1 
ATOM   2444 C CB  . THR B 2 200 ? 49.095  16.437  9.738   1.00 34.66 ? 200  THR U CB  1 
ATOM   2445 O OG1 . THR B 2 200 ? 47.831  17.113  9.708   1.00 34.36 ? 200  THR U OG1 1 
ATOM   2446 C CG2 . THR B 2 200 ? 49.770  16.579  8.375   1.00 34.49 ? 200  THR U CG2 1 
ATOM   2447 N N   . LEU B 2 201 ? 50.725  14.330  11.675  1.00 35.01 ? 201  LEU U N   1 
ATOM   2448 C CA  . LEU B 2 201 ? 52.025  13.759  12.102  1.00 35.05 ? 201  LEU U CA  1 
ATOM   2449 C C   . LEU B 2 201 ? 51.940  12.593  13.122  1.00 35.07 ? 201  LEU U C   1 
ATOM   2450 O O   . LEU B 2 201 ? 52.918  12.309  13.835  1.00 35.04 ? 201  LEU U O   1 
ATOM   2451 C CB  . LEU B 2 201 ? 52.984  14.857  12.618  1.00 34.99 ? 201  LEU U CB  1 
ATOM   2452 C CG  . LEU B 2 201 ? 53.995  15.531  11.672  1.00 34.93 ? 201  LEU U CG  1 
ATOM   2453 C CD1 . LEU B 2 201 ? 54.733  16.681  12.367  1.00 34.76 ? 201  LEU U CD1 1 
ATOM   2454 C CD2 . LEU B 2 201 ? 54.997  14.531  11.101  1.00 34.76 ? 201  LEU U CD2 1 
ATOM   2455 N N   . GLY B 2 202 ? 50.778  11.936  13.193  1.00 34.94 ? 202  GLY U N   1 
ATOM   2456 C CA  . GLY B 2 202 ? 50.646  10.654  13.895  1.00 34.65 ? 202  GLY U CA  1 
ATOM   2457 C C   . GLY B 2 202 ? 51.048  9.574   12.912  1.00 34.48 ? 202  GLY U C   1 
ATOM   2458 O O   . GLY B 2 202 ? 51.628  8.549   13.274  1.00 34.36 ? 202  GLY U O   1 
ATOM   2459 N N   . CYS B 2 203 ? 50.734  9.844   11.650  1.00 34.39 ? 203  CYS U N   1 
ATOM   2460 C CA  . CYS B 2 203 ? 51.098  9.009   10.525  1.00 34.33 ? 203  CYS U CA  1 
ATOM   2461 C C   . CYS B 2 203 ? 51.652  9.913   9.425   1.00 34.14 ? 203  CYS U C   1 
ATOM   2462 O O   . CYS B 2 203 ? 51.319  11.098  9.361   1.00 34.12 ? 203  CYS U O   1 
ATOM   2463 C CB  . CYS B 2 203 ? 49.858  8.283   10.012  1.00 34.43 ? 203  CYS U CB  1 
ATOM   2464 S SG  . CYS B 2 203 ? 48.671  9.367   9.160   1.00 34.88 ? 203  CYS U SG  1 
ATOM   2465 N N   . SER B 2 204 ? 52.495  9.354   8.564   1.00 33.90 ? 204  SER U N   1 
ATOM   2466 C CA  . SER B 2 204 ? 53.028  10.076  7.411   1.00 33.67 ? 204  SER U CA  1 
ATOM   2467 C C   . SER B 2 204 ? 53.574  9.057   6.421   1.00 33.65 ? 204  SER U C   1 
ATOM   2468 O O   . SER B 2 204 ? 53.092  7.927   6.364   1.00 33.55 ? 204  SER U O   1 
ATOM   2469 C CB  . SER B 2 204 ? 54.130  11.057  7.841   1.00 33.65 ? 204  SER U CB  1 
ATOM   2470 O OG  . SER B 2 204 ? 53.605  12.142  8.587   1.00 33.22 ? 204  SER U OG  1 
ATOM   2471 N N   . SER B 2 205 ? 54.575  9.465   5.640   1.00 33.73 ? 205  SER U N   1 
ATOM   2472 C CA  . SER B 2 205 ? 55.420  8.535   4.884   1.00 33.74 ? 205  SER U CA  1 
ATOM   2473 C C   . SER B 2 205 ? 56.348  7.802   5.859   1.00 33.70 ? 205  SER U C   1 
ATOM   2474 O O   . SER B 2 205 ? 57.248  7.059   5.442   1.00 33.71 ? 205  SER U O   1 
ATOM   2475 C CB  . SER B 2 205 ? 56.262  9.286   3.842   1.00 33.75 ? 205  SER U CB  1 
ATOM   2476 O OG  . SER B 2 205 ? 55.454  9.993   2.917   1.00 33.80 ? 205  SER U OG  1 
ATOM   2477 N N   . GLU B 2 206 ? 56.115  8.025   7.156   1.00 33.59 ? 206  GLU U N   1 
ATOM   2478 C CA  . GLU B 2 206 ? 56.973  7.514   8.233   1.00 33.33 ? 206  GLU U CA  1 
ATOM   2479 C C   . GLU B 2 206 ? 56.238  6.580   9.226   1.00 33.11 ? 206  GLU U C   1 
ATOM   2480 O O   . GLU B 2 206 ? 56.724  5.481   9.517   1.00 33.23 ? 206  GLU U O   1 
ATOM   2481 C CB  . GLU B 2 206 ? 57.697  8.673   8.963   1.00 33.35 ? 206  GLU U CB  1 
ATOM   2482 C CG  . GLU B 2 206 ? 58.766  9.413   8.119   1.00 32.81 ? 206  GLU U CG  1 
ATOM   2483 C CD  . GLU B 2 206 ? 59.595  10.432  8.913   1.00 32.06 ? 206  GLU U CD  1 
ATOM   2484 O OE1 . GLU B 2 206 ? 59.224  10.764  10.059  1.00 31.71 ? 206  GLU U OE1 1 
ATOM   2485 O OE2 . GLU B 2 206 ? 60.622  10.910  8.381   1.00 31.52 ? 206  GLU U OE2 1 
ATOM   2486 N N   . GLU B 2 207 ? 55.083  7.002   9.743   1.00 32.63 ? 207  GLU U N   1 
ATOM   2487 C CA  . GLU B 2 207 ? 54.310  6.149   10.657  1.00 32.24 ? 207  GLU U CA  1 
ATOM   2488 C C   . GLU B 2 207 ? 52.942  5.754   10.094  1.00 32.05 ? 207  GLU U C   1 
ATOM   2489 O O   . GLU B 2 207 ? 51.923  5.790   10.787  1.00 31.92 ? 207  GLU U O   1 
ATOM   2490 C CB  . GLU B 2 207 ? 54.219  6.756   12.067  1.00 32.25 ? 207  GLU U CB  1 
ATOM   2491 C CG  . GLU B 2 207 ? 54.929  5.936   13.163  1.00 31.97 ? 207  GLU U CG  1 
ATOM   2492 C CD  . GLU B 2 207 ? 56.449  5.853   13.008  1.00 31.85 ? 207  GLU U CD  1 
ATOM   2493 O OE1 . GLU B 2 207 ? 56.983  4.724   12.940  1.00 31.78 ? 207  GLU U OE1 1 
ATOM   2494 O OE2 . GLU B 2 207 ? 57.115  6.909   12.967  1.00 31.85 ? 207  GLU U OE2 1 
ATOM   2495 N N   . ALA B 2 208 ? 52.963  5.384   8.815   1.00 31.90 ? 208  ALA U N   1 
ATOM   2496 C CA  . ALA B 2 208 ? 51.871  4.707   8.105   1.00 31.67 ? 208  ALA U CA  1 
ATOM   2497 C C   . ALA B 2 208 ? 52.498  4.007   6.897   1.00 31.53 ? 208  ALA U C   1 
ATOM   2498 O O   . ALA B 2 208 ? 53.343  4.593   6.203   1.00 31.70 ? 208  ALA U O   1 
ATOM   2499 C CB  . ALA B 2 208 ? 50.813  5.700   7.652   1.00 31.62 ? 208  ALA U CB  1 
ATOM   2500 N N   . SER B 2 209 ? 52.106  2.755   6.653   1.00 31.14 ? 209  SER U N   1 
ATOM   2501 C CA  . SER B 2 209 ? 52.702  1.958   5.566   1.00 30.67 ? 209  SER U CA  1 
ATOM   2502 C C   . SER B 2 209 ? 51.686  1.484   4.520   1.00 30.27 ? 209  SER U C   1 
ATOM   2503 O O   . SER B 2 209 ? 50.475  1.634   4.698   1.00 30.22 ? 209  SER U O   1 
ATOM   2504 C CB  . SER B 2 209 ? 53.494  0.770   6.132   1.00 30.72 ? 209  SER U CB  1 
ATOM   2505 O OG  . SER B 2 209 ? 54.754  1.180   6.641   1.00 30.61 ? 209  SER U OG  1 
ATOM   2506 N N   . LEU B 2 210 ? 52.201  0.916   3.430   1.00 29.76 ? 210  LEU U N   1 
ATOM   2507 C CA  . LEU B 2 210 ? 51.381  0.382   2.349   1.00 29.31 ? 210  LEU U CA  1 
ATOM   2508 C C   . LEU B 2 210 ? 50.775  -0.948  2.735   1.00 28.96 ? 210  LEU U C   1 
ATOM   2509 O O   . LEU B 2 210 ? 51.497  -1.892  3.055   1.00 28.95 ? 210  LEU U O   1 
ATOM   2510 C CB  . LEU B 2 210 ? 52.221  0.169   1.087   1.00 29.42 ? 210  LEU U CB  1 
ATOM   2511 C CG  . LEU B 2 210 ? 52.510  1.297   0.089   1.00 29.68 ? 210  LEU U CG  1 
ATOM   2512 C CD1 . LEU B 2 210 ? 51.236  1.785   -0.603  1.00 29.70 ? 210  LEU U CD1 1 
ATOM   2513 C CD2 . LEU B 2 210 ? 53.278  2.448   0.735   1.00 30.24 ? 210  LEU U CD2 1 
ATOM   2514 N N   . ILE B 2 211 ? 49.450  -1.026  2.704   1.00 28.62 ? 211  ILE U N   1 
ATOM   2515 C CA  . ILE B 2 211 ? 48.769  -2.304  2.900   1.00 28.21 ? 211  ILE U CA  1 
ATOM   2516 C C   . ILE B 2 211 ? 48.755  -3.010  1.568   1.00 27.99 ? 211  ILE U C   1 
ATOM   2517 O O   . ILE B 2 211 ? 48.854  -2.364  0.523   1.00 27.89 ? 211  ILE U O   1 
ATOM   2518 C CB  . ILE B 2 211 ? 47.300  -2.176  3.454   1.00 28.17 ? 211  ILE U CB  1 
ATOM   2519 C CG1 . ILE B 2 211 ? 46.382  -1.419  2.483   1.00 28.00 ? 211  ILE U CG1 1 
ATOM   2520 C CG2 . ILE B 2 211 ? 47.285  -1.556  4.856   1.00 28.08 ? 211  ILE U CG2 1 
ATOM   2521 C CD1 . ILE B 2 211 ? 44.930  -1.357  2.925   1.00 27.46 ? 211  ILE U CD1 1 
ATOM   2522 N N   . ASN B 2 212 ? 48.661  -4.333  1.602   1.00 27.77 ? 212  ASN U N   1 
ATOM   2523 C CA  . ASN B 2 212 ? 48.447  -5.071  0.378   1.00 27.52 ? 212  ASN U CA  1 
ATOM   2524 C C   . ASN B 2 212 ? 46.969  -5.334  0.263   1.00 27.53 ? 212  ASN U C   1 
ATOM   2525 O O   . ASN B 2 212 ? 46.405  -6.100  1.049   1.00 27.36 ? 212  ASN U O   1 
ATOM   2526 C CB  . ASN B 2 212 ? 49.252  -6.363  0.344   1.00 27.35 ? 212  ASN U CB  1 
ATOM   2527 C CG  . ASN B 2 212 ? 49.751  -6.680  -1.039  1.00 26.64 ? 212  ASN U CG  1 
ATOM   2528 O OD1 . ASN B 2 212 ? 48.973  -6.780  -1.989  1.00 26.00 ? 212  ASN U OD1 1 
ATOM   2529 N ND2 . ASN B 2 212 ? 51.057  -6.817  -1.169  1.00 25.88 ? 212  ASN U ND2 1 
ATOM   2530 N N   . CYS B 2 213 ? 46.344  -4.662  -0.702  1.00 27.65 ? 213  CYS U N   1 
ATOM   2531 C CA  . CYS B 2 213 ? 44.888  -4.674  -0.834  1.00 27.91 ? 213  CYS U CA  1 
ATOM   2532 C C   . CYS B 2 213 ? 44.396  -6.085  -1.106  1.00 27.76 ? 213  CYS U C   1 
ATOM   2533 O O   . CYS B 2 213 ? 45.083  -6.865  -1.782  1.00 28.08 ? 213  CYS U O   1 
ATOM   2534 C CB  . CYS B 2 213 ? 44.430  -3.718  -1.943  1.00 28.04 ? 213  CYS U CB  1 
ATOM   2535 S SG  . CYS B 2 213 ? 44.205  -1.969  -1.453  1.00 28.75 ? 213  CYS U SG  1 
ATOM   2536 N N   . ARG B 2 214 ? 43.220  -6.415  -0.578  1.00 27.33 ? 214  ARG U N   1 
ATOM   2537 C CA  . ARG B 2 214 ? 42.701  -7.779  -0.694  1.00 27.10 ? 214  ARG U CA  1 
ATOM   2538 C C   . ARG B 2 214 ? 41.409  -7.933  -1.503  1.00 27.14 ? 214  ARG U C   1 
ATOM   2539 O O   . ARG B 2 214 ? 40.323  -7.550  -1.069  1.00 27.12 ? 214  ARG U O   1 
ATOM   2540 C CB  . ARG B 2 214 ? 42.578  -8.450  0.681   1.00 26.84 ? 214  ARG U CB  1 
ATOM   2541 C CG  . ARG B 2 214 ? 43.912  -8.867  1.282   1.00 26.15 ? 214  ARG U CG  1 
ATOM   2542 C CD  . ARG B 2 214 ? 43.797  -10.238 1.913   1.00 24.96 ? 214  ARG U CD  1 
ATOM   2543 N NE  . ARG B 2 214 ? 44.975  -10.588 2.698   1.00 23.62 ? 214  ARG U NE  1 
ATOM   2544 C CZ  . ARG B 2 214 ? 45.082  -11.693 3.427   1.00 23.40 ? 214  ARG U CZ  1 
ATOM   2545 N NH1 . ARG B 2 214 ? 44.089  -12.573 3.470   1.00 22.22 ? 214  ARG U NH1 1 
ATOM   2546 N NH2 . ARG B 2 214 ? 46.193  -11.920 4.114   1.00 23.90 ? 214  ARG U NH2 1 
ATOM   2547 N N   . GLY B 2 215 ? 41.553  -8.506  -2.693  1.00 27.32 ? 215  GLY U N   1 
ATOM   2548 C CA  . GLY B 2 215 ? 40.412  -8.898  -3.514  1.00 27.34 ? 215  GLY U CA  1 
ATOM   2549 C C   . GLY B 2 215 ? 39.485  -7.761  -3.894  1.00 27.06 ? 215  GLY U C   1 
ATOM   2550 O O   . GLY B 2 215 ? 39.922  -6.785  -4.516  1.00 27.10 ? 215  GLY U O   1 
ATOM   2551 N N   . PRO B 2 216 ? 38.198  -7.880  -3.520  1.00 26.70 ? 216  PRO U N   1 
ATOM   2552 C CA  . PRO B 2 216 ? 37.199  -6.900  -3.932  1.00 26.67 ? 216  PRO U CA  1 
ATOM   2553 C C   . PRO B 2 216 ? 37.563  -5.449  -3.591  1.00 26.74 ? 216  PRO U C   1 
ATOM   2554 O O   . PRO B 2 216 ? 37.099  -4.530  -4.271  1.00 27.09 ? 216  PRO U O   1 
ATOM   2555 C CB  . PRO B 2 216 ? 35.941  -7.365  -3.202  1.00 26.46 ? 216  PRO U CB  1 
ATOM   2556 C CG  . PRO B 2 216 ? 36.133  -8.844  -3.109  1.00 26.40 ? 216  PRO U CG  1 
ATOM   2557 C CD  . PRO B 2 216 ? 37.586  -9.013  -2.805  1.00 26.38 ? 216  PRO U CD  1 
ATOM   2558 N N   . MET B 2 217 ? 38.395  -5.243  -2.572  1.00 26.47 ? 217  MET U N   1 
ATOM   2559 C CA  . MET B 2 217 ? 38.895  -3.907  -2.257  1.00 26.18 ? 217  MET U CA  1 
ATOM   2560 C C   . MET B 2 217 ? 39.929  -3.475  -3.291  1.00 25.98 ? 217  MET U C   1 
ATOM   2561 O O   . MET B 2 217 ? 40.929  -4.162  -3.510  1.00 26.00 ? 217  MET U O   1 
ATOM   2562 C CB  . MET B 2 217 ? 39.513  -3.877  -0.859  1.00 26.34 ? 217  MET U CB  1 
ATOM   2563 C CG  . MET B 2 217 ? 38.557  -3.577  0.274   1.00 26.69 ? 217  MET U CG  1 
ATOM   2564 S SD  . MET B 2 217 ? 37.332  -4.862  0.583   1.00 26.95 ? 217  MET U SD  1 
ATOM   2565 C CE  . MET B 2 217 ? 36.067  -4.416  -0.601  1.00 26.38 ? 217  MET U CE  1 
ATOM   2566 N N   . ASN B 2 218 ? 39.680  -2.338  -3.930  1.00 25.64 ? 218  ASN U N   1 
ATOM   2567 C CA  . ASN B 2 218 ? 40.600  -1.806  -4.932  1.00 25.39 ? 218  ASN U CA  1 
ATOM   2568 C C   . ASN B 2 218 ? 40.604  -0.281  -4.989  1.00 25.21 ? 218  ASN U C   1 
ATOM   2569 O O   . ASN B 2 218 ? 41.345  0.314   -5.763  1.00 25.32 ? 218  ASN U O   1 
ATOM   2570 C CB  . ASN B 2 218 ? 40.296  -2.398  -6.316  1.00 25.50 ? 218  ASN U CB  1 
ATOM   2571 C CG  . ASN B 2 218 ? 38.821  -2.295  -6.693  1.00 25.86 ? 218  ASN U CG  1 
ATOM   2572 O OD1 . ASN B 2 218 ? 38.166  -1.278  -6.452  1.00 26.54 ? 218  ASN U OD1 1 
ATOM   2573 N ND2 . ASN B 2 218 ? 38.296  -3.355  -7.292  1.00 25.74 ? 218  ASN U ND2 1 
ATOM   2574 N N   . GLN B 2 219 ? 39.766  0.343   -4.167  1.00 25.21 ? 219  GLN U N   1 
ATOM   2575 C CA  . GLN B 2 219 ? 39.684  1.797   -4.084  1.00 24.84 ? 219  GLN U CA  1 
ATOM   2576 C C   . GLN B 2 219 ? 40.500  2.299   -2.913  1.00 24.58 ? 219  GLN U C   1 
ATOM   2577 O O   . GLN B 2 219 ? 40.257  1.911   -1.773  1.00 24.35 ? 219  GLN U O   1 
ATOM   2578 C CB  . GLN B 2 219 ? 38.231  2.245   -3.913  1.00 24.95 ? 219  GLN U CB  1 
ATOM   2579 C CG  . GLN B 2 219 ? 37.316  1.987   -5.108  1.00 24.75 ? 219  GLN U CG  1 
ATOM   2580 C CD  . GLN B 2 219 ? 37.470  3.026   -6.181  1.00 24.30 ? 219  GLN U CD  1 
ATOM   2581 O OE1 . GLN B 2 219 ? 38.407  2.969   -6.967  1.00 25.25 ? 219  GLN U OE1 1 
ATOM   2582 N NE2 . GLN B 2 219 ? 36.551  3.990   -6.223  1.00 23.82 ? 219  GLN U NE2 1 
ATOM   2583 N N   . CYS B 2 220 ? 41.473  3.153   -3.201  1.00 24.58 ? 220  CYS U N   1 
ATOM   2584 C CA  . CYS B 2 220 ? 42.218  3.817   -2.156  1.00 25.07 ? 220  CYS U CA  1 
ATOM   2585 C C   . CYS B 2 220 ? 41.440  5.015   -1.658  1.00 24.60 ? 220  CYS U C   1 
ATOM   2586 O O   . CYS B 2 220 ? 40.952  5.822   -2.456  1.00 24.68 ? 220  CYS U O   1 
ATOM   2587 C CB  . CYS B 2 220 ? 43.594  4.230   -2.635  1.00 25.47 ? 220  CYS U CB  1 
ATOM   2588 S SG  . CYS B 2 220 ? 44.922  3.043   -2.319  1.00 28.73 ? 220  CYS U SG  1 
ATOM   2589 N N   . LEU B 2 221 ? 41.357  5.119   -0.330  1.00 24.04 ? 221  LEU U N   1 
ATOM   2590 C CA  . LEU B 2 221 ? 40.398  5.969   0.354   1.00 23.22 ? 221  LEU U CA  1 
ATOM   2591 C C   . LEU B 2 221 ? 40.973  6.700   1.582   1.00 22.79 ? 221  LEU U C   1 
ATOM   2592 O O   . LEU B 2 221 ? 41.850  6.159   2.256   1.00 22.86 ? 221  LEU U O   1 
ATOM   2593 C CB  . LEU B 2 221 ? 39.213  5.099   0.762   1.00 23.11 ? 221  LEU U CB  1 
ATOM   2594 C CG  . LEU B 2 221 ? 38.609  5.279   2.151   1.00 23.43 ? 221  LEU U CG  1 
ATOM   2595 C CD1 . LEU B 2 221 ? 37.131  4.966   2.112   1.00 23.77 ? 221  LEU U CD1 1 
ATOM   2596 C CD2 . LEU B 2 221 ? 39.337  4.431   3.191   1.00 23.64 ? 221  LEU U CD2 1 
ATOM   2597 N N   . VAL B 2 222 ? 40.456  7.914   1.849   1.00 21.93 ? 222  VAL U N   1 
ATOM   2598 C CA  . VAL B 2 222 ? 40.757  8.741   3.044   1.00 20.61 ? 222  VAL U CA  1 
ATOM   2599 C C   . VAL B 2 222 ? 39.470  9.162   3.749   1.00 19.96 ? 222  VAL U C   1 
ATOM   2600 O O   . VAL B 2 222 ? 38.411  9.188   3.129   1.00 20.05 ? 222  VAL U O   1 
ATOM   2601 C CB  . VAL B 2 222 ? 41.485  10.059  2.689   1.00 20.54 ? 222  VAL U CB  1 
ATOM   2602 C CG1 . VAL B 2 222 ? 42.919  9.802   2.229   1.00 20.60 ? 222  VAL U CG1 1 
ATOM   2603 C CG2 . VAL B 2 222 ? 40.687  10.854  1.661   1.00 19.99 ? 222  VAL U CG2 1 
ATOM   2604 N N   . ALA B 2 223 ? 39.576  9.536   5.027   1.00 18.89 ? 223  ALA U N   1 
ATOM   2605 C CA  . ALA B 2 223 ? 38.420  9.920   5.844   1.00 17.62 ? 223  ALA U CA  1 
ATOM   2606 C C   . ALA B 2 223 ? 38.806  10.920  6.925   1.00 16.86 ? 223  ALA U C   1 
ATOM   2607 O O   . ALA B 2 223 ? 39.947  10.929  7.375   1.00 16.60 ? 223  ALA U O   1 
ATOM   2608 C CB  . ALA B 2 223 ? 37.809  8.690   6.472   1.00 17.45 ? 223  ALA U CB  1 
ATOM   2609 N N   . THR B 2 224 ? 37.857  11.751  7.354   1.00 16.11 ? 224  THR U N   1 
ATOM   2610 C CA  . THR B 2 224 ? 38.164  12.804  8.329   1.00 15.70 ? 224  THR U CA  1 
ATOM   2611 C C   . THR B 2 224 ? 36.923  13.332  9.078   1.00 15.14 ? 224  THR U C   1 
ATOM   2612 O O   . THR B 2 224 ? 35.808  12.928  8.775   1.00 15.28 ? 224  THR U O   1 
ATOM   2613 C CB  . THR B 2 224 ? 38.911  13.968  7.645   1.00 15.95 ? 224  THR U CB  1 
ATOM   2614 O OG1 . THR B 2 224 ? 39.401  13.539  6.365   1.00 16.33 ? 224  THR U OG1 1 
ATOM   2615 C CG2 . THR B 2 224 ? 40.078  14.451  8.511   1.00 15.99 ? 224  THR U CG2 1 
ATOM   2616 N N   . GLY B 2 225 ? 37.127  14.209  10.066  1.00 14.36 ? 225  GLY U N   1 
ATOM   2617 C CA  . GLY B 2 225 ? 36.033  14.815  10.832  1.00 13.31 ? 225  GLY U CA  1 
ATOM   2618 C C   . GLY B 2 225 ? 36.525  15.537  12.081  1.00 12.89 ? 225  GLY U C   1 
ATOM   2619 O O   . GLY B 2 225 ? 37.509  15.114  12.697  1.00 12.71 ? 225  GLY U O   1 
ATOM   2620 N N   . LEU B 2 226 ? 35.843  16.633  12.438  1.00 12.41 ? 226  LEU U N   1 
ATOM   2621 C CA  . LEU B 2 226 ? 36.099  17.399  13.671  1.00 11.82 ? 226  LEU U CA  1 
ATOM   2622 C C   . LEU B 2 226 ? 34.988  17.168  14.676  1.00 11.72 ? 226  LEU U C   1 
ATOM   2623 O O   . LEU B 2 226 ? 35.251  16.803  15.821  1.00 11.69 ? 226  LEU U O   1 
ATOM   2624 C CB  . LEU B 2 226 ? 36.209  18.911  13.400  1.00 11.67 ? 226  LEU U CB  1 
ATOM   2625 C CG  . LEU B 2 226 ? 37.497  19.751  13.577  1.00 10.80 ? 226  LEU U CG  1 
ATOM   2626 C CD1 . LEU B 2 226 ? 37.973  19.907  15.042  1.00 9.08  ? 226  LEU U CD1 1 
ATOM   2627 C CD2 . LEU B 2 226 ? 38.616  19.240  12.680  1.00 10.17 ? 226  LEU U CD2 1 
ATOM   2628 N N   . ARG B 2 232 ? 39.875  14.891  18.703  1.00 19.55 ? 232  ARG U N   1 
ATOM   2629 C CA  . ARG B 2 232 ? 39.037  15.943  18.137  1.00 19.67 ? 232  ARG U CA  1 
ATOM   2630 C C   . ARG B 2 232 ? 38.862  15.768  16.624  1.00 20.09 ? 232  ARG U C   1 
ATOM   2631 O O   . ARG B 2 232 ? 37.732  15.637  16.132  1.00 19.95 ? 232  ARG U O   1 
ATOM   2632 C CB  . ARG B 2 232 ? 39.589  17.327  18.507  1.00 19.36 ? 232  ARG U CB  1 
ATOM   2633 C CG  . ARG B 2 232 ? 39.420  17.659  19.987  1.00 18.25 ? 232  ARG U CG  1 
ATOM   2634 C CD  . ARG B 2 232 ? 40.334  18.758  20.399  1.00 17.20 ? 232  ARG U CD  1 
ATOM   2635 N NE  . ARG B 2 232 ? 40.185  19.922  19.533  1.00 17.55 ? 232  ARG U NE  1 
ATOM   2636 C CZ  . ARG B 2 232 ? 40.734  21.114  19.764  1.00 17.41 ? 232  ARG U CZ  1 
ATOM   2637 N NH1 . ARG B 2 232 ? 41.476  21.312  20.845  1.00 17.56 ? 232  ARG U NH1 1 
ATOM   2638 N NH2 . ARG B 2 232 ? 40.537  22.116  18.914  1.00 16.98 ? 232  ARG U NH2 1 
ATOM   2639 N N   . SER B 2 233 ? 39.982  15.743  15.900  1.00 20.57 ? 233  SER U N   1 
ATOM   2640 C CA  . SER B 2 233 ? 39.967  15.500  14.463  1.00 20.96 ? 233  SER U CA  1 
ATOM   2641 C C   . SER B 2 233 ? 40.588  14.151  14.126  1.00 21.45 ? 233  SER U C   1 
ATOM   2642 O O   . SER B 2 233 ? 41.812  14.009  14.044  1.00 21.26 ? 233  SER U O   1 
ATOM   2643 C CB  . SER B 2 233 ? 40.672  16.622  13.708  1.00 20.87 ? 233  SER U CB  1 
ATOM   2644 O OG  . SER B 2 233 ? 40.386  16.535  12.326  1.00 20.45 ? 233  SER U OG  1 
ATOM   2645 N N   . TYR B 2 234 ? 39.727  13.159  13.940  1.00 22.27 ? 234  TYR U N   1 
ATOM   2646 C CA  . TYR B 2 234 ? 40.180  11.809  13.617  1.00 23.17 ? 234  TYR U CA  1 
ATOM   2647 C C   . TYR B 2 234 ? 40.163  11.556  12.116  1.00 22.84 ? 234  TYR U C   1 
ATOM   2648 O O   . TYR B 2 234 ? 39.318  12.103  11.407  1.00 22.72 ? 234  TYR U O   1 
ATOM   2649 C CB  . TYR B 2 234 ? 39.364  10.742  14.368  1.00 23.74 ? 234  TYR U CB  1 
ATOM   2650 C CG  . TYR B 2 234 ? 39.984  9.350   14.306  1.00 25.77 ? 234  TYR U CG  1 
ATOM   2651 C CD1 . TYR B 2 234 ? 39.206  8.223   14.012  1.00 26.53 ? 234  TYR U CD1 1 
ATOM   2652 C CD2 . TYR B 2 234 ? 41.362  9.167   14.533  1.00 27.86 ? 234  TYR U CD2 1 
ATOM   2653 C CE1 . TYR B 2 234 ? 39.783  6.951   13.958  1.00 28.19 ? 234  TYR U CE1 1 
ATOM   2654 C CE2 . TYR B 2 234 ? 41.949  7.907   14.474  1.00 28.95 ? 234  TYR U CE2 1 
ATOM   2655 C CZ  . TYR B 2 234 ? 41.160  6.806   14.185  1.00 29.47 ? 234  TYR U CZ  1 
ATOM   2656 O OH  . TYR B 2 234 ? 41.762  5.569   14.125  1.00 30.80 ? 234  TYR U OH  1 
ATOM   2657 N N   . THR B 2 235 ? 41.106  10.727  11.657  1.00 22.72 ? 235  THR U N   1 
ATOM   2658 C CA  . THR B 2 235 ? 41.362  10.481  10.227  1.00 22.54 ? 235  THR U CA  1 
ATOM   2659 C C   . THR B 2 235 ? 41.859  9.056   9.932   1.00 22.60 ? 235  THR U C   1 
ATOM   2660 O O   . THR B 2 235 ? 42.608  8.478   10.718  1.00 22.67 ? 235  THR U O   1 
ATOM   2661 C CB  . THR B 2 235 ? 42.360  11.513  9.626   1.00 22.40 ? 235  THR U CB  1 
ATOM   2662 O OG1 . THR B 2 235 ? 43.037  10.916  8.518   1.00 21.51 ? 235  THR U OG1 1 
ATOM   2663 C CG2 . THR B 2 235 ? 43.405  11.977  10.669  1.00 22.19 ? 235  THR U CG2 1 
ATOM   2664 N N   . VAL B 2 236 ? 41.448  8.511   8.787   1.00 22.63 ? 236  VAL U N   1 
ATOM   2665 C CA  . VAL B 2 236 ? 41.711  7.108   8.429   1.00 22.79 ? 236  VAL U CA  1 
ATOM   2666 C C   . VAL B 2 236 ? 41.764  6.855   6.916   1.00 22.96 ? 236  VAL U C   1 
ATOM   2667 O O   . VAL B 2 236 ? 40.905  7.321   6.158   1.00 23.04 ? 236  VAL U O   1 
ATOM   2668 C CB  . VAL B 2 236 ? 40.655  6.163   9.061   1.00 22.76 ? 236  VAL U CB  1 
ATOM   2669 C CG1 . VAL B 2 236 ? 40.496  4.855   8.263   1.00 22.12 ? 236  VAL U CG1 1 
ATOM   2670 C CG2 . VAL B 2 236 ? 41.002  5.876   10.514  1.00 23.26 ? 236  VAL U CG2 1 
ATOM   2671 N N   . ARG B 2 237 ? 42.765  6.095   6.485   1.00 22.98 ? 237  ARG U N   1 
ATOM   2672 C CA  . ARG B 2 237 ? 42.909  5.778   5.075   1.00 23.06 ? 237  ARG U CA  1 
ATOM   2673 C C   . ARG B 2 237 ? 43.056  4.289   4.766   1.00 23.10 ? 237  ARG U C   1 
ATOM   2674 O O   . ARG B 2 237 ? 43.456  3.492   5.615   1.00 22.78 ? 237  ARG U O   1 
ATOM   2675 C CB  . ARG B 2 237 ? 44.056  6.586   4.444   1.00 23.17 ? 237  ARG U CB  1 
ATOM   2676 C CG  . ARG B 2 237 ? 45.454  6.329   4.999   1.00 23.08 ? 237  ARG U CG  1 
ATOM   2677 C CD  . ARG B 2 237 ? 46.384  7.448   4.567   1.00 23.05 ? 237  ARG U CD  1 
ATOM   2678 N NE  . ARG B 2 237 ? 45.796  8.749   4.879   1.00 23.08 ? 237  ARG U NE  1 
ATOM   2679 C CZ  . ARG B 2 237 ? 45.923  9.842   4.136   1.00 22.69 ? 237  ARG U CZ  1 
ATOM   2680 N NH1 . ARG B 2 237 ? 46.622  9.818   3.014   1.00 22.75 ? 237  ARG U NH1 1 
ATOM   2681 N NH2 . ARG B 2 237 ? 45.338  10.964  4.520   1.00 22.38 ? 237  ARG U NH2 1 
ATOM   2682 N N   . GLY B 2 238 ? 42.738  3.929   3.528   1.00 23.35 ? 238  GLY U N   1 
ATOM   2683 C CA  . GLY B 2 238 ? 42.852  2.556   3.101   1.00 23.55 ? 238  GLY U CA  1 
ATOM   2684 C C   . GLY B 2 238 ? 42.003  2.154   1.919   1.00 23.72 ? 238  GLY U C   1 
ATOM   2685 O O   . GLY B 2 238 ? 41.584  2.982   1.112   1.00 23.28 ? 238  GLY U O   1 
ATOM   2686 N N   . CYS B 2 239 ? 41.721  0.855   1.888   1.00 24.14 ? 239  CYS U N   1 
ATOM   2687 C CA  . CYS B 2 239 ? 41.311  0.120   0.708   1.00 24.46 ? 239  CYS U CA  1 
ATOM   2688 C C   . CYS B 2 239 ? 39.847  -0.270  0.810   1.00 24.26 ? 239  CYS U C   1 
ATOM   2689 O O   . CYS B 2 239 ? 39.434  -0.898  1.783   1.00 24.18 ? 239  CYS U O   1 
ATOM   2690 C CB  . CYS B 2 239 ? 42.179  -1.125  0.622   1.00 24.58 ? 239  CYS U CB  1 
ATOM   2691 S SG  . CYS B 2 239 ? 42.222  -1.875  -0.959  1.00 26.70 ? 239  CYS U SG  1 
ATOM   2692 N N   . ALA B 2 240 ? 39.062  0.113   -0.189  1.00 24.22 ? 240  ALA U N   1 
ATOM   2693 C CA  . ALA B 2 240 ? 37.608  0.043   -0.076  1.00 24.30 ? 240  ALA U CA  1 
ATOM   2694 C C   . ALA B 2 240 ? 36.938  -0.314  -1.389  1.00 24.41 ? 240  ALA U C   1 
ATOM   2695 O O   . ALA B 2 240 ? 37.605  -0.468  -2.415  1.00 24.42 ? 240  ALA U O   1 
ATOM   2696 C CB  . ALA B 2 240 ? 37.068  1.366   0.428   1.00 24.34 ? 240  ALA U CB  1 
ATOM   2697 N N   . THR B 2 241 ? 35.612  -0.442  -1.352  1.00 24.27 ? 241  THR U N   1 
ATOM   2698 C CA  . THR B 2 241 ? 34.837  -0.640  -2.574  1.00 24.10 ? 241  THR U CA  1 
ATOM   2699 C C   . THR B 2 241 ? 34.510  0.690   -3.276  1.00 24.42 ? 241  THR U C   1 
ATOM   2700 O O   . THR B 2 241 ? 35.202  1.695   -3.084  1.00 24.48 ? 241  THR U O   1 
ATOM   2701 C CB  . THR B 2 241 ? 33.526  -1.342  -2.284  1.00 23.80 ? 241  THR U CB  1 
ATOM   2702 O OG1 . THR B 2 241 ? 32.593  -0.394  -1.770  1.00 22.67 ? 241  THR U OG1 1 
ATOM   2703 C CG2 . THR B 2 241 ? 33.733  -2.425  -1.297  1.00 23.28 ? 241  THR U CG2 1 
ATOM   2704 N N   . ALA B 2 242 ? 33.459  0.673   -4.099  1.00 24.44 ? 242  ALA U N   1 
ATOM   2705 C CA  . ALA B 2 242 ? 32.863  1.891   -4.642  1.00 24.37 ? 242  ALA U CA  1 
ATOM   2706 C C   . ALA B 2 242 ? 31.470  2.075   -4.043  1.00 24.45 ? 242  ALA U C   1 
ATOM   2707 O O   . ALA B 2 242 ? 30.870  3.143   -4.143  1.00 24.52 ? 242  ALA U O   1 
ATOM   2708 C CB  . ALA B 2 242 ? 32.797  1.837   -6.159  1.00 24.21 ? 242  ALA U CB  1 
ATOM   2709 N N   . SER B 2 243 ? 30.953  1.029   -3.418  1.00 24.42 ? 243  SER U N   1 
ATOM   2710 C CA  . SER B 2 243 ? 29.678  1.136   -2.742  1.00 24.80 ? 243  SER U CA  1 
ATOM   2711 C C   . SER B 2 243 ? 29.909  1.646   -1.329  1.00 25.13 ? 243  SER U C   1 
ATOM   2712 O O   . SER B 2 243 ? 29.045  2.319   -0.754  1.00 25.54 ? 243  SER U O   1 
ATOM   2713 C CB  . SER B 2 243 ? 29.001  -0.220  -2.687  1.00 24.71 ? 243  SER U CB  1 
ATOM   2714 O OG  . SER B 2 243 ? 29.938  -1.198  -2.284  1.00 24.99 ? 243  SER U OG  1 
ATOM   2715 N N   . TRP B 2 244 ? 31.078  1.310   -0.778  1.00 25.11 ? 244  TRP U N   1 
ATOM   2716 C CA  . TRP B 2 244 ? 31.443  1.647   0.599   1.00 24.60 ? 244  TRP U CA  1 
ATOM   2717 C C   . TRP B 2 244 ? 31.742  3.093   0.592   1.00 24.51 ? 244  TRP U C   1 
ATOM   2718 O O   . TRP B 2 244 ? 31.233  3.866   1.401   1.00 24.69 ? 244  TRP U O   1 
ATOM   2719 C CB  . TRP B 2 244 ? 32.715  0.915   1.019   1.00 24.58 ? 244  TRP U CB  1 
ATOM   2720 C CG  . TRP B 2 244 ? 33.153  1.216   2.411   1.00 23.08 ? 244  TRP U CG  1 
ATOM   2721 C CD1 . TRP B 2 244 ? 34.146  2.050   2.783   1.00 21.91 ? 244  TRP U CD1 1 
ATOM   2722 C CD2 . TRP B 2 244 ? 32.613  0.667   3.611   1.00 22.29 ? 244  TRP U CD2 1 
ATOM   2723 N NE1 . TRP B 2 244 ? 34.268  2.056   4.143   1.00 22.07 ? 244  TRP U NE1 1 
ATOM   2724 C CE2 . TRP B 2 244 ? 33.331  1.218   4.675   1.00 21.95 ? 244  TRP U CE2 1 
ATOM   2725 C CE3 . TRP B 2 244 ? 31.585  -0.240  3.888   1.00 23.26 ? 244  TRP U CE3 1 
ATOM   2726 C CZ2 . TRP B 2 244 ? 33.054  0.910   5.997   1.00 23.38 ? 244  TRP U CZ2 1 
ATOM   2727 C CZ3 . TRP B 2 244 ? 31.312  -0.558  5.206   1.00 22.89 ? 244  TRP U CZ3 1 
ATOM   2728 C CH2 . TRP B 2 244 ? 32.041  0.017   6.244   1.00 23.58 ? 244  TRP U CH2 1 
ATOM   2729 N N   . CYS B 2 245 ? 32.586  3.430   -0.364  1.00 24.51 ? 245  CYS U N   1 
ATOM   2730 C CA  . CYS B 2 245 ? 33.033  4.762   -0.568  1.00 24.97 ? 245  CYS U CA  1 
ATOM   2731 C C   . CYS B 2 245 ? 31.865  5.659   -0.899  1.00 24.85 ? 245  CYS U C   1 
ATOM   2732 O O   . CYS B 2 245 ? 32.005  6.868   -0.943  1.00 24.72 ? 245  CYS U O   1 
ATOM   2733 C CB  . CYS B 2 245 ? 34.009  4.758   -1.704  1.00 25.08 ? 245  CYS U CB  1 
ATOM   2734 S SG  . CYS B 2 245 ? 34.887  6.243   -1.760  1.00 27.86 ? 245  CYS U SG  1 
ATOM   2735 N N   . GLN B 2 246 ? 30.702  5.057   -1.102  1.00 25.07 ? 246  GLN U N   1 
ATOM   2736 C CA  . GLN B 2 246 ? 29.513  5.808   -1.421  1.00 25.40 ? 246  GLN U CA  1 
ATOM   2737 C C   . GLN B 2 246 ? 28.422  5.559   -0.386  1.00 25.38 ? 246  GLN U C   1 
ATOM   2738 O O   . GLN B 2 246 ? 28.321  4.476   0.192   1.00 24.95 ? 246  GLN U O   1 
ATOM   2739 C CB  . GLN B 2 246 ? 29.038  5.418   -2.815  1.00 25.70 ? 246  GLN U CB  1 
ATOM   2740 C CG  . GLN B 2 246 ? 27.997  6.339   -3.423  1.00 26.94 ? 246  GLN U CG  1 
ATOM   2741 C CD  . GLN B 2 246 ? 27.203  5.661   -4.532  1.00 28.26 ? 246  GLN U CD  1 
ATOM   2742 O OE1 . GLN B 2 246 ? 27.182  4.425   -4.646  1.00 28.20 ? 246  GLN U OE1 1 
ATOM   2743 N NE2 . GLN B 2 246 ? 26.539  6.469   -5.356  1.00 28.99 ? 246  GLN U NE2 1 
ATOM   2744 N N   . GLY B 2 247 ? 27.609  6.582   -0.155  1.00 25.63 ? 247  GLY U N   1 
ATOM   2745 C CA  . GLY B 2 247 ? 26.491  6.485   0.772   1.00 25.75 ? 247  GLY U CA  1 
ATOM   2746 C C   . GLY B 2 247 ? 26.869  6.599   2.237   1.00 25.83 ? 247  GLY U C   1 
ATOM   2747 O O   . GLY B 2 247 ? 27.956  7.079   2.605   1.00 25.92 ? 247  GLY U O   1 
ATOM   2748 N N   . SER B 2 248 ? 25.957  6.121   3.070   1.00 25.82 ? 248  SER U N   1 
ATOM   2749 C CA  . SER B 2 248 ? 26.028  6.302   4.513   1.00 25.74 ? 248  SER U CA  1 
ATOM   2750 C C   . SER B 2 248 ? 27.208  5.622   5.212   1.00 25.50 ? 248  SER U C   1 
ATOM   2751 O O   . SER B 2 248 ? 27.636  6.077   6.265   1.00 25.17 ? 248  SER U O   1 
ATOM   2752 C CB  . SER B 2 248 ? 24.728  5.816   5.136   1.00 25.68 ? 248  SER U CB  1 
ATOM   2753 O OG  . SER B 2 248 ? 24.398  6.630   6.238   1.00 26.20 ? 248  SER U OG  1 
ATOM   2754 N N   . HIS B 2 249 ? 27.724  4.548   4.609   1.00 25.46 ? 249  HIS U N   1 
ATOM   2755 C CA  . HIS B 2 249 ? 28.700  3.631   5.236   1.00 25.10 ? 249  HIS U CA  1 
ATOM   2756 C C   . HIS B 2 249 ? 29.858  4.300   5.933   1.00 24.74 ? 249  HIS U C   1 
ATOM   2757 O O   . HIS B 2 249 ? 29.764  4.691   7.078   1.00 24.41 ? 249  HIS U O   1 
ATOM   2758 C CB  . HIS B 2 249 ? 29.261  2.650   4.203   1.00 25.10 ? 249  HIS U CB  1 
ATOM   2759 C CG  . HIS B 2 249 ? 28.213  1.853   3.502   1.00 24.87 ? 249  HIS U CG  1 
ATOM   2760 N ND1 . HIS B 2 249 ? 27.834  2.108   2.203   1.00 25.79 ? 249  HIS U ND1 1 
ATOM   2761 C CD2 . HIS B 2 249 ? 27.451  0.819   3.923   1.00 24.39 ? 249  HIS U CD2 1 
ATOM   2762 C CE1 . HIS B 2 249 ? 26.892  1.254   1.846   1.00 25.67 ? 249  HIS U CE1 1 
ATOM   2763 N NE2 . HIS B 2 249 ? 26.637  0.466   2.875   1.00 25.56 ? 249  HIS U NE2 1 
ATOM   2764 N N   . VAL B 2 250 ? 30.969  4.395   5.227   1.00 24.73 ? 250  VAL U N   1 
ATOM   2765 C CA  . VAL B 2 250 ? 32.107  5.181   5.669   1.00 24.68 ? 250  VAL U CA  1 
ATOM   2766 C C   . VAL B 2 250 ? 31.798  6.070   6.880   1.00 24.64 ? 250  VAL U C   1 
ATOM   2767 O O   . VAL B 2 250 ? 32.430  5.940   7.911   1.00 24.55 ? 250  VAL U O   1 
ATOM   2768 C CB  . VAL B 2 250 ? 32.647  6.018   4.495   1.00 24.59 ? 250  VAL U CB  1 
ATOM   2769 C CG1 . VAL B 2 250 ? 31.470  6.601   3.649   1.00 24.52 ? 250  VAL U CG1 1 
ATOM   2770 C CG2 . VAL B 2 250 ? 33.621  7.068   4.989   1.00 23.72 ? 250  VAL U CG2 1 
ATOM   2771 N N   . ALA B 2 251 ? 30.813  6.951   6.752   1.00 24.93 ? 251  ALA U N   1 
ATOM   2772 C CA  . ALA B 2 251 ? 30.429  7.855   7.836   1.00 25.27 ? 251  ALA U CA  1 
ATOM   2773 C C   . ALA B 2 251 ? 30.374  7.148   9.174   1.00 25.37 ? 251  ALA U C   1 
ATOM   2774 O O   . ALA B 2 251 ? 31.101  7.499   10.098  1.00 25.73 ? 251  ALA U O   1 
ATOM   2775 C CB  . ALA B 2 251 ? 29.089  8.515   7.544   1.00 25.41 ? 251  ALA U CB  1 
ATOM   2776 N N   . ASP B 2 252 ? 29.518  6.143   9.270   1.00 25.39 ? 252  ASP U N   1 
ATOM   2777 C CA  . ASP B 2 252 ? 29.356  5.410   10.503  1.00 25.36 ? 252  ASP U CA  1 
ATOM   2778 C C   . ASP B 2 252 ? 30.533  4.476   10.768  1.00 24.81 ? 252  ASP U C   1 
ATOM   2779 O O   . ASP B 2 252 ? 30.598  3.865   11.819  1.00 25.17 ? 252  ASP U O   1 
ATOM   2780 C CB  . ASP B 2 252 ? 28.032  4.647   10.494  1.00 25.74 ? 252  ASP U CB  1 
ATOM   2781 C CG  . ASP B 2 252 ? 28.048  3.429   9.557   1.00 28.09 ? 252  ASP U CG  1 
ATOM   2782 O OD1 . ASP B 2 252 ? 27.291  2.464   9.824   1.00 30.94 ? 252  ASP U OD1 1 
ATOM   2783 O OD2 . ASP B 2 252 ? 28.812  3.412   8.562   1.00 29.95 ? 252  ASP U OD2 1 
ATOM   2784 N N   . SER B 2 253 ? 31.463  4.375   9.829   1.00 24.29 ? 253  SER U N   1 
ATOM   2785 C CA  . SER B 2 253 ? 32.612  3.509   9.993   1.00 24.28 ? 253  SER U CA  1 
ATOM   2786 C C   . SER B 2 253 ? 33.340  3.826   11.296  1.00 24.39 ? 253  SER U C   1 
ATOM   2787 O O   . SER B 2 253 ? 34.176  3.045   11.755  1.00 24.23 ? 253  SER U O   1 
ATOM   2788 C CB  . SER B 2 253 ? 33.536  3.642   8.773   1.00 24.52 ? 253  SER U CB  1 
ATOM   2789 O OG  . SER B 2 253 ? 34.816  3.051   8.951   1.00 24.93 ? 253  SER U OG  1 
ATOM   2790 N N   . PHE B 2 254 ? 33.002  4.966   11.898  1.00 24.85 ? 254  PHE U N   1 
ATOM   2791 C CA  . PHE B 2 254 ? 33.589  5.399   13.179  1.00 25.64 ? 254  PHE U CA  1 
ATOM   2792 C C   . PHE B 2 254 ? 32.611  6.202   14.062  1.00 26.58 ? 254  PHE U C   1 
ATOM   2793 O O   . PHE B 2 254 ? 31.770  6.913   13.514  1.00 26.99 ? 254  PHE U O   1 
ATOM   2794 C CB  . PHE B 2 254 ? 34.873  6.207   12.932  1.00 25.45 ? 254  PHE U CB  1 
ATOM   2795 C CG  . PHE B 2 254 ? 34.811  7.149   11.742  1.00 24.18 ? 254  PHE U CG  1 
ATOM   2796 C CD1 . PHE B 2 254 ? 33.943  8.234   11.724  1.00 22.79 ? 254  PHE U CD1 1 
ATOM   2797 C CD2 . PHE B 2 254 ? 35.664  6.968   10.661  1.00 22.65 ? 254  PHE U CD2 1 
ATOM   2798 C CE1 . PHE B 2 254 ? 33.912  9.100   10.644  1.00 21.54 ? 254  PHE U CE1 1 
ATOM   2799 C CE2 . PHE B 2 254 ? 35.631  7.829   9.589   1.00 21.30 ? 254  PHE U CE2 1 
ATOM   2800 C CZ  . PHE B 2 254 ? 34.757  8.899   9.584   1.00 21.03 ? 254  PHE U CZ  1 
ATOM   2801 N N   . PRO B 2 255 ? 32.746  6.132   15.418  1.00 27.28 ? 255  PRO U N   1 
ATOM   2802 C CA  . PRO B 2 255 ? 31.812  6.746   16.397  1.00 28.02 ? 255  PRO U CA  1 
ATOM   2803 C C   . PRO B 2 255 ? 30.847  7.820   15.831  1.00 28.96 ? 255  PRO U C   1 
ATOM   2804 O O   . PRO B 2 255 ? 29.745  7.466   15.381  1.00 29.02 ? 255  PRO U O   1 
ATOM   2805 C CB  . PRO B 2 255 ? 32.756  7.352   17.446  1.00 27.78 ? 255  PRO U CB  1 
ATOM   2806 C CG  . PRO B 2 255 ? 34.138  6.763   17.140  1.00 27.38 ? 255  PRO U CG  1 
ATOM   2807 C CD  . PRO B 2 255 ? 33.974  5.702   16.103  1.00 26.99 ? 255  PRO U CD  1 
ATOM   2808 N N   . THR B 2 256 ? 31.249  9.098   15.863  1.00 29.81 ? 256  THR U N   1 
ATOM   2809 C CA  . THR B 2 256 ? 30.523  10.185  15.176  1.00 30.58 ? 256  THR U CA  1 
ATOM   2810 C C   . THR B 2 256 ? 31.508  11.139  14.522  1.00 31.63 ? 256  THR U C   1 
ATOM   2811 O O   . THR B 2 256 ? 32.681  11.138  14.881  1.00 31.73 ? 256  THR U O   1 
ATOM   2812 C CB  . THR B 2 256 ? 29.692  11.044  16.144  1.00 30.26 ? 256  THR U CB  1 
ATOM   2813 O OG1 . THR B 2 256 ? 29.161  10.219  17.185  1.00 30.30 ? 256  THR U OG1 1 
ATOM   2814 C CG2 . THR B 2 256 ? 28.556  11.771  15.400  1.00 29.18 ? 256  THR U CG2 1 
ATOM   2815 N N   . HIS B 2 257 ? 31.029  11.937  13.562  1.00 32.84 ? 257  HIS U N   1 
ATOM   2816 C CA  . HIS B 2 257 ? 31.738  13.137  13.099  1.00 33.94 ? 257  HIS U CA  1 
ATOM   2817 C C   . HIS B 2 257 ? 31.060  13.986  12.025  1.00 34.85 ? 257  HIS U C   1 
ATOM   2818 O O   . HIS B 2 257 ? 29.878  13.807  11.746  1.00 34.89 ? 257  HIS U O   1 
ATOM   2819 C CB  . HIS B 2 257 ? 33.178  12.843  12.712  1.00 33.98 ? 257  HIS U CB  1 
ATOM   2820 C CG  . HIS B 2 257 ? 34.159  13.273  13.748  1.00 34.77 ? 257  HIS U CG  1 
ATOM   2821 N ND1 . HIS B 2 257 ? 35.112  12.429  14.269  1.00 35.96 ? 257  HIS U ND1 1 
ATOM   2822 C CD2 . HIS B 2 257 ? 34.308  14.454  14.392  1.00 35.78 ? 257  HIS U CD2 1 
ATOM   2823 C CE1 . HIS B 2 257 ? 35.827  13.080  15.172  1.00 36.74 ? 257  HIS U CE1 1 
ATOM   2824 N NE2 . HIS B 2 257 ? 35.359  14.312  15.265  1.00 36.28 ? 257  HIS U NE2 1 
ATOM   2825 N N   . LEU B 2 258 ? 31.857  14.879  11.425  1.00 36.25 ? 258  LEU U N   1 
ATOM   2826 C CA  . LEU B 2 258 ? 31.431  16.048  10.627  1.00 37.41 ? 258  LEU U CA  1 
ATOM   2827 C C   . LEU B 2 258 ? 30.582  15.744  9.390   1.00 38.18 ? 258  LEU U C   1 
ATOM   2828 O O   . LEU B 2 258 ? 29.611  14.992  9.442   1.00 38.25 ? 258  LEU U O   1 
ATOM   2829 C CB  . LEU B 2 258 ? 32.687  16.818  10.181  1.00 37.39 ? 258  LEU U CB  1 
ATOM   2830 C CG  . LEU B 2 258 ? 32.863  18.334  10.383  1.00 37.86 ? 258  LEU U CG  1 
ATOM   2831 C CD1 . LEU B 2 258 ? 34.053  18.838  9.550   1.00 37.30 ? 258  LEU U CD1 1 
ATOM   2832 C CD2 . LEU B 2 258 ? 31.600  19.157  10.088  1.00 37.87 ? 258  LEU U CD2 1 
ATOM   2833 N N   . ASN B 2 259 ? 30.939  16.379  8.281   1.00 39.31 ? 259  ASN U N   1 
ATOM   2834 C CA  . ASN B 2 259 ? 30.463  15.977  6.962   1.00 40.54 ? 259  ASN U CA  1 
ATOM   2835 C C   . ASN B 2 259 ? 31.368  14.828  6.504   1.00 39.51 ? 259  ASN U C   1 
ATOM   2836 O O   . ASN B 2 259 ? 31.233  14.293  5.391   1.00 39.48 ? 259  ASN U O   1 
ATOM   2837 C CB  . ASN B 2 259 ? 30.540  17.158  5.981   1.00 41.75 ? 259  ASN U CB  1 
ATOM   2838 C CG  . ASN B 2 259 ? 30.436  18.513  6.677   1.00 47.06 ? 259  ASN U CG  1 
ATOM   2839 O OD1 . ASN B 2 259 ? 29.521  18.753  7.474   1.00 47.41 ? 259  ASN U OD1 1 
ATOM   2840 N ND2 . ASN B 2 259 ? 31.384  19.404  6.374   1.00 56.64 ? 259  ASN U ND2 1 
ATOM   2841 N N   . VAL B 2 260 ? 32.286  14.464  7.404   1.00 38.26 ? 260  VAL U N   1 
ATOM   2842 C CA  . VAL B 2 260 ? 33.322  13.453  7.194   1.00 36.94 ? 260  VAL U CA  1 
ATOM   2843 C C   . VAL B 2 260 ? 33.859  13.357  5.763   1.00 36.03 ? 260  VAL U C   1 
ATOM   2844 O O   . VAL B 2 260 ? 33.794  12.301  5.142   1.00 35.85 ? 260  VAL U O   1 
ATOM   2845 C CB  . VAL B 2 260 ? 32.890  12.072  7.717   1.00 36.90 ? 260  VAL U CB  1 
ATOM   2846 C CG1 . VAL B 2 260 ? 32.552  12.158  9.191   1.00 36.70 ? 260  VAL U CG1 1 
ATOM   2847 C CG2 . VAL B 2 260 ? 31.712  11.533  6.921   1.00 37.22 ? 260  VAL U CG2 1 
ATOM   2848 N N   . SER B 2 261 ? 34.399  14.461  5.253   1.00 34.84 ? 261  SER U N   1 
ATOM   2849 C CA  . SER B 2 261 ? 34.984  14.462  3.929   1.00 33.82 ? 261  SER U CA  1 
ATOM   2850 C C   . SER B 2 261 ? 35.707  13.143  3.699   1.00 33.10 ? 261  SER U C   1 
ATOM   2851 O O   . SER B 2 261 ? 36.480  12.674  4.544   1.00 32.84 ? 261  SER U O   1 
ATOM   2852 C CB  . SER B 2 261 ? 35.962  15.613  3.765   1.00 34.02 ? 261  SER U CB  1 
ATOM   2853 O OG  . SER B 2 261 ? 37.297  15.155  3.897   1.00 34.41 ? 261  SER U OG  1 
ATOM   2854 N N   . VAL B 2 262 ? 35.446  12.565  2.536   1.00 32.32 ? 262  VAL U N   1 
ATOM   2855 C CA  . VAL B 2 262 ? 35.889  11.224  2.202   1.00 31.59 ? 262  VAL U CA  1 
ATOM   2856 C C   . VAL B 2 262 ? 36.345  11.206  0.732   1.00 31.27 ? 262  VAL U C   1 
ATOM   2857 O O   . VAL B 2 262 ? 35.746  11.893  -0.092  1.00 31.17 ? 262  VAL U O   1 
ATOM   2858 C CB  . VAL B 2 262 ? 34.736  10.214  2.514   1.00 31.38 ? 262  VAL U CB  1 
ATOM   2859 C CG1 . VAL B 2 262 ? 33.390  10.770  2.074   1.00 30.67 ? 262  VAL U CG1 1 
ATOM   2860 C CG2 . VAL B 2 262 ? 34.997  8.835   1.923   1.00 31.44 ? 262  VAL U CG2 1 
ATOM   2861 N N   . SER B 2 263 ? 37.406  10.462  0.407   1.00 30.91 ? 263  SER U N   1 
ATOM   2862 C CA  . SER B 2 263 ? 37.882  10.410  -0.988  1.00 30.97 ? 263  SER U CA  1 
ATOM   2863 C C   . SER B 2 263 ? 38.332  9.064   -1.577  1.00 30.77 ? 263  SER U C   1 
ATOM   2864 O O   . SER B 2 263 ? 38.956  8.254   -0.900  1.00 30.47 ? 263  SER U O   1 
ATOM   2865 C CB  . SER B 2 263 ? 38.953  11.473  -1.248  1.00 31.02 ? 263  SER U CB  1 
ATOM   2866 O OG  . SER B 2 263 ? 38.377  12.624  -1.841  1.00 31.31 ? 263  SER U OG  1 
ATOM   2867 N N   . CYS B 2 264 ? 38.031  8.879   -2.868  1.00 30.67 ? 264  CYS U N   1 
ATOM   2868 C CA  . CYS B 2 264 ? 38.316  7.647   -3.605  1.00 30.57 ? 264  CYS U CA  1 
ATOM   2869 C C   . CYS B 2 264 ? 39.001  7.858   -4.941  1.00 30.51 ? 264  CYS U C   1 
ATOM   2870 O O   . CYS B 2 264 ? 38.688  8.807   -5.660  1.00 30.37 ? 264  CYS U O   1 
ATOM   2871 C CB  . CYS B 2 264 ? 37.020  6.898   -3.859  1.00 30.33 ? 264  CYS U CB  1 
ATOM   2872 S SG  . CYS B 2 264 ? 36.679  5.686   -2.576  1.00 31.33 ? 264  CYS U SG  1 
ATOM   2873 N N   . CYS B 2 265 ? 39.927  6.964   -5.275  1.00 30.57 ? 265  CYS U N   1 
ATOM   2874 C CA  . CYS B 2 265 ? 40.433  6.900   -6.642  1.00 31.28 ? 265  CYS U CA  1 
ATOM   2875 C C   . CYS B 2 265 ? 41.153  5.585   -6.968  1.00 31.02 ? 265  CYS U C   1 
ATOM   2876 O O   . CYS B 2 265 ? 41.475  4.817   -6.057  1.00 31.01 ? 265  CYS U O   1 
ATOM   2877 C CB  . CYS B 2 265 ? 41.323  8.114   -6.956  1.00 31.58 ? 265  CYS U CB  1 
ATOM   2878 S SG  . CYS B 2 265 ? 43.089  7.939   -6.559  1.00 33.78 ? 265  CYS U SG  1 
ATOM   2879 N N   . HIS B 2 266 ? 41.392  5.339   -8.264  1.00 30.76 ? 266  HIS U N   1 
ATOM   2880 C CA  . HIS B 2 266 ? 42.242  4.225   -8.706  1.00 30.40 ? 266  HIS U CA  1 
ATOM   2881 C C   . HIS B 2 266 ? 43.738  4.553   -8.556  1.00 30.27 ? 266  HIS U C   1 
ATOM   2882 O O   . HIS B 2 266 ? 44.158  5.721   -8.641  1.00 30.04 ? 266  HIS U O   1 
ATOM   2883 C CB  . HIS B 2 266 ? 41.881  3.742   -10.136 1.00 30.42 ? 266  HIS U CB  1 
ATOM   2884 C CG  . HIS B 2 266 ? 42.821  4.204   -11.227 1.00 30.19 ? 266  HIS U CG  1 
ATOM   2885 N ND1 . HIS B 2 266 ? 44.040  3.602   -11.474 1.00 29.54 ? 266  HIS U ND1 1 
ATOM   2886 C CD2 . HIS B 2 266 ? 42.686  5.168   -12.173 1.00 29.32 ? 266  HIS U CD2 1 
ATOM   2887 C CE1 . HIS B 2 266 ? 44.628  4.196   -12.497 1.00 28.53 ? 266  HIS U CE1 1 
ATOM   2888 N NE2 . HIS B 2 266 ? 43.827  5.149   -12.939 1.00 28.61 ? 266  HIS U NE2 1 
ATOM   2889 N N   . GLY B 2 267 ? 44.526  3.504   -8.323  1.00 30.08 ? 267  GLY U N   1 
ATOM   2890 C CA  . GLY B 2 267 ? 45.968  3.622   -8.131  1.00 29.71 ? 267  GLY U CA  1 
ATOM   2891 C C   . GLY B 2 267 ? 46.396  2.989   -6.824  1.00 29.48 ? 267  GLY U C   1 
ATOM   2892 O O   . GLY B 2 267 ? 45.612  2.915   -5.872  1.00 29.32 ? 267  GLY U O   1 
ATOM   2893 N N   . SER B 2 268 ? 47.640  2.526   -6.783  1.00 29.28 ? 268  SER U N   1 
ATOM   2894 C CA  . SER B 2 268 ? 48.216  2.001   -5.556  1.00 29.29 ? 268  SER U CA  1 
ATOM   2895 C C   . SER B 2 268 ? 48.353  3.119   -4.504  1.00 29.35 ? 268  SER U C   1 
ATOM   2896 O O   . SER B 2 268 ? 47.708  3.076   -3.449  1.00 29.21 ? 268  SER U O   1 
ATOM   2897 C CB  . SER B 2 268 ? 49.564  1.332   -5.841  1.00 29.24 ? 268  SER U CB  1 
ATOM   2898 O OG  . SER B 2 268 ? 49.414  0.240   -6.729  1.00 29.22 ? 268  SER U OG  1 
ATOM   2899 N N   . GLY B 2 269 ? 49.168  4.129   -4.809  1.00 29.23 ? 269  GLY U N   1 
ATOM   2900 C CA  . GLY B 2 269 ? 49.394  5.248   -3.895  1.00 28.89 ? 269  GLY U CA  1 
ATOM   2901 C C   . GLY B 2 269 ? 48.329  6.319   -3.980  1.00 28.74 ? 269  GLY U C   1 
ATOM   2902 O O   . GLY B 2 269 ? 48.554  7.441   -3.558  1.00 28.56 ? 269  GLY U O   1 
ATOM   2903 N N   . CYS B 2 270 ? 47.174  5.960   -4.533  1.00 28.94 ? 270  CYS U N   1 
ATOM   2904 C CA  . CYS B 2 270 ? 46.014  6.841   -4.658  1.00 29.42 ? 270  CYS U CA  1 
ATOM   2905 C C   . CYS B 2 270 ? 45.738  7.648   -3.388  1.00 29.50 ? 270  CYS U C   1 
ATOM   2906 O O   . CYS B 2 270 ? 45.432  8.842   -3.463  1.00 29.47 ? 270  CYS U O   1 
ATOM   2907 C CB  . CYS B 2 270 ? 44.770  6.001   -5.006  1.00 29.80 ? 270  CYS U CB  1 
ATOM   2908 S SG  . CYS B 2 270 ? 43.116  6.822   -4.849  1.00 30.67 ? 270  CYS U SG  1 
ATOM   2909 N N   . ASN B 2 271 ? 45.844  6.981   -2.232  1.00 29.54 ? 271  ASN U N   1 
ATOM   2910 C CA  . ASN B 2 271 ? 45.458  7.553   -0.934  1.00 29.30 ? 271  ASN U CA  1 
ATOM   2911 C C   . ASN B 2 271 ? 46.609  7.956   0.005   1.00 29.46 ? 271  ASN U C   1 
ATOM   2912 O O   . ASN B 2 271 ? 46.374  8.303   1.163   1.00 29.63 ? 271  ASN U O   1 
ATOM   2913 C CB  . ASN B 2 271 ? 44.436  6.647   -0.217  1.00 29.02 ? 271  ASN U CB  1 
ATOM   2914 C CG  . ASN B 2 271 ? 45.055  5.384   0.382   1.00 28.30 ? 271  ASN U CG  1 
ATOM   2915 O OD1 . ASN B 2 271 ? 44.513  4.824   1.338   1.00 27.50 ? 271  ASN U OD1 1 
ATOM   2916 N ND2 . ASN B 2 271 ? 46.173  4.927   -0.177  1.00 26.73 ? 271  ASN U ND2 1 
ATOM   2917 N N   . SER B 2 272 ? 47.841  7.911   -0.497  1.00 29.56 ? 272  SER U N   1 
ATOM   2918 C CA  . SER B 2 272 ? 48.983  8.500   0.197   1.00 29.61 ? 272  SER U CA  1 
ATOM   2919 C C   . SER B 2 272 ? 48.649  9.951   0.487   1.00 29.67 ? 272  SER U C   1 
ATOM   2920 O O   . SER B 2 272 ? 47.941  10.566  -0.306  1.00 29.54 ? 272  SER U O   1 
ATOM   2921 C CB  . SER B 2 272 ? 50.223  8.444   -0.689  1.00 29.58 ? 272  SER U CB  1 
ATOM   2922 O OG  . SER B 2 272 ? 51.375  8.835   0.034   1.00 29.72 ? 272  SER U OG  1 
ATOM   2923 N N   . PRO B 2 273 ? 49.136  10.496  1.620   1.00 29.85 ? 273  PRO U N   1 
ATOM   2924 C CA  . PRO B 2 273 ? 48.899  11.888  2.026   1.00 30.18 ? 273  PRO U CA  1 
ATOM   2925 C C   . PRO B 2 273 ? 48.850  12.909  0.868   1.00 30.56 ? 273  PRO U C   1 
ATOM   2926 O O   . PRO B 2 273 ? 49.706  13.801  0.784   1.00 30.60 ? 273  PRO U O   1 
ATOM   2927 C CB  . PRO B 2 273 ? 50.075  12.160  2.960   1.00 30.19 ? 273  PRO U CB  1 
ATOM   2928 C CG  . PRO B 2 273 ? 50.318  10.835  3.618   1.00 29.92 ? 273  PRO U CG  1 
ATOM   2929 C CD  . PRO B 2 273 ? 49.865  9.755   2.667   1.00 29.75 ? 273  PRO U CD  1 
ATOM   2930 N N   . THR B 2 274 ? 47.812  12.777  0.029   1.00 30.92 ? 274  THR U N   1 
ATOM   2931 C CA  . THR B 2 274 ? 47.620  13.500  -1.254  1.00 31.20 ? 274  THR U CA  1 
ATOM   2932 C C   . THR B 2 274 ? 48.866  13.479  -2.160  1.00 31.41 ? 274  THR U C   1 
ATOM   2933 O O   . THR B 2 274 ? 48.961  12.652  -3.069  1.00 31.64 ? 274  THR U O   1 
ATOM   2934 C CB  . THR B 2 274 ? 47.022  14.927  -1.063  1.00 31.25 ? 274  THR U CB  1 
ATOM   2935 O OG1 . THR B 2 274 ? 45.691  14.812  -0.538  1.00 31.31 ? 274  THR U OG1 1 
ATOM   2936 C CG2 . THR B 2 274 ? 46.957  15.687  -2.392  1.00 31.23 ? 274  THR U CG2 1 
ATOM   2937 N N   . ASP C 1 8   ? 18.505  26.476  42.009  1.00 76.29 ? 8    ASP B N   1 
ATOM   2938 C CA  . ASP C 1 8   ? 19.556  25.755  42.781  1.00 76.71 ? 8    ASP B CA  1 
ATOM   2939 C C   . ASP C 1 8   ? 20.429  26.688  43.660  1.00 76.86 ? 8    ASP B C   1 
ATOM   2940 O O   . ASP C 1 8   ? 19.987  27.106  44.739  1.00 77.18 ? 8    ASP B O   1 
ATOM   2941 C CB  . ASP C 1 8   ? 20.418  24.890  41.842  1.00 76.76 ? 8    ASP B CB  1 
ATOM   2942 C CG  . ASP C 1 8   ? 21.240  23.832  42.591  1.00 77.09 ? 8    ASP B CG  1 
ATOM   2943 O OD1 . ASP C 1 8   ? 20.656  23.044  43.372  1.00 77.98 ? 8    ASP B OD1 1 
ATOM   2944 O OD2 . ASP C 1 8   ? 22.473  23.778  42.391  1.00 76.80 ? 8    ASP B OD2 1 
ATOM   2945 N N   . GLU C 1 9   ? 21.650  27.010  43.202  1.00 76.61 ? 9    GLU B N   1 
ATOM   2946 C CA  . GLU C 1 9   ? 22.655  27.737  44.017  1.00 76.00 ? 9    GLU B CA  1 
ATOM   2947 C C   . GLU C 1 9   ? 23.592  28.637  43.186  1.00 75.08 ? 9    GLU B C   1 
ATOM   2948 O O   . GLU C 1 9   ? 24.794  28.344  43.020  1.00 75.03 ? 9    GLU B O   1 
ATOM   2949 C CB  . GLU C 1 9   ? 23.486  26.749  44.849  1.00 76.37 ? 9    GLU B CB  1 
ATOM   2950 C CG  . GLU C 1 9   ? 24.309  27.396  45.970  1.00 77.61 ? 9    GLU B CG  1 
ATOM   2951 C CD  . GLU C 1 9   ? 25.593  26.640  46.267  1.00 79.29 ? 9    GLU B CD  1 
ATOM   2952 O OE1 . GLU C 1 9   ? 25.818  25.567  45.645  1.00 80.45 ? 9    GLU B OE1 1 
ATOM   2953 O OE2 . GLU C 1 9   ? 26.377  27.126  47.119  1.00 79.32 ? 9    GLU B OE2 1 
ATOM   2954 N N   . SER C 1 10  ? 23.029  29.743  42.692  1.00 73.78 ? 10   SER B N   1 
ATOM   2955 C CA  . SER C 1 10  ? 23.726  30.683  41.796  1.00 72.07 ? 10   SER B CA  1 
ATOM   2956 C C   . SER C 1 10  ? 23.507  32.148  42.210  1.00 70.41 ? 10   SER B C   1 
ATOM   2957 O O   . SER C 1 10  ? 24.413  32.778  42.788  1.00 70.76 ? 10   SER B O   1 
ATOM   2958 C CB  . SER C 1 10  ? 23.253  30.473  40.358  1.00 72.30 ? 10   SER B CB  1 
ATOM   2959 O OG  . SER C 1 10  ? 21.835  30.383  40.301  1.00 72.95 ? 10   SER B OG  1 
ATOM   2960 N N   . ASN C 1 11  ? 22.300  32.658  41.927  1.00 67.42 ? 11   ASN B N   1 
ATOM   2961 C CA  . ASN C 1 11  ? 21.892  34.056  42.156  1.00 64.68 ? 11   ASN B CA  1 
ATOM   2962 C C   . ASN C 1 11  ? 21.942  34.881  40.850  1.00 62.69 ? 11   ASN B C   1 
ATOM   2963 O O   . ASN C 1 11  ? 20.890  35.164  40.245  1.00 62.30 ? 11   ASN B O   1 
ATOM   2964 C CB  . ASN C 1 11  ? 22.679  34.715  43.316  1.00 64.64 ? 11   ASN B CB  1 
ATOM   2965 C CG  . ASN C 1 11  ? 22.027  35.984  43.820  1.00 64.15 ? 11   ASN B CG  1 
ATOM   2966 O OD1 . ASN C 1 11  ? 21.318  35.972  44.826  1.00 63.56 ? 11   ASN B OD1 1 
ATOM   2967 N ND2 . ASN C 1 11  ? 22.253  37.086  43.115  1.00 63.54 ? 11   ASN B ND2 1 
ATOM   2968 N N   . CYS C 1 12  ? 23.159  35.243  40.426  1.00 59.88 ? 12   CYS B N   1 
ATOM   2969 C CA  . CYS C 1 12  ? 23.404  35.969  39.171  1.00 57.01 ? 12   CYS B CA  1 
ATOM   2970 C C   . CYS C 1 12  ? 22.511  35.412  38.113  1.00 55.57 ? 12   CYS B C   1 
ATOM   2971 O O   . CYS C 1 12  ? 22.467  34.201  37.945  1.00 55.55 ? 12   CYS B O   1 
ATOM   2972 C CB  . CYS C 1 12  ? 24.853  35.797  38.732  1.00 56.47 ? 12   CYS B CB  1 
ATOM   2973 S SG  . CYS C 1 12  ? 25.667  34.441  39.622  1.00 54.37 ? 12   CYS B SG  1 
ATOM   2974 N N   . GLY C 1 13  ? 21.783  36.296  37.435  1.00 53.74 ? 13   GLY B N   1 
ATOM   2975 C CA  . GLY C 1 13  ? 20.837  35.929  36.373  1.00 51.95 ? 13   GLY B CA  1 
ATOM   2976 C C   . GLY C 1 13  ? 20.289  34.503  36.371  1.00 50.34 ? 13   GLY B C   1 
ATOM   2977 O O   . GLY C 1 13  ? 19.138  34.276  36.749  1.00 50.18 ? 13   GLY B O   1 
ATOM   2978 N N   . CYS C 1 14  ? 21.127  33.563  35.922  1.00 48.50 ? 14   CYS B N   1 
ATOM   2979 C CA  . CYS C 1 14  ? 20.867  32.121  35.934  1.00 46.60 ? 14   CYS B CA  1 
ATOM   2980 C C   . CYS C 1 14  ? 19.486  31.771  36.409  1.00 45.74 ? 14   CYS B C   1 
ATOM   2981 O O   . CYS C 1 14  ? 19.132  32.085  37.547  1.00 45.91 ? 14   CYS B O   1 
ATOM   2982 C CB  . CYS C 1 14  ? 21.913  31.395  36.783  1.00 46.29 ? 14   CYS B CB  1 
ATOM   2983 S SG  . CYS C 1 14  ? 23.524  31.158  35.930  1.00 46.16 ? 14   CYS B SG  1 
ATOM   2984 N N   . GLN C 1 15  ? 18.708  31.125  35.534  1.00 44.55 ? 15   GLN B N   1 
ATOM   2985 C CA  . GLN C 1 15  ? 17.297  30.812  35.825  1.00 43.03 ? 15   GLN B CA  1 
ATOM   2986 C C   . GLN C 1 15  ? 16.957  29.323  35.811  1.00 41.72 ? 15   GLN B C   1 
ATOM   2987 O O   . GLN C 1 15  ? 17.767  28.482  35.417  1.00 41.36 ? 15   GLN B O   1 
ATOM   2988 C CB  . GLN C 1 15  ? 16.350  31.613  34.919  1.00 43.12 ? 15   GLN B CB  1 
ATOM   2989 C CG  . GLN C 1 15  ? 16.568  33.140  35.004  1.00 44.11 ? 15   GLN B CG  1 
ATOM   2990 C CD  . GLN C 1 15  ? 15.413  33.972  34.432  1.00 44.97 ? 15   GLN B CD  1 
ATOM   2991 O OE1 . GLN C 1 15  ? 15.604  34.741  33.481  1.00 44.94 ? 15   GLN B OE1 1 
ATOM   2992 N NE2 . GLN C 1 15  ? 14.215  33.825  35.013  1.00 44.33 ? 15   GLN B NE2 1 
ATOM   2993 N N   . ASN C 1 16  ? 15.748  29.020  36.270  1.00 40.48 ? 16   ASN B N   1 
ATOM   2994 C CA  . ASN C 1 16  ? 15.247  27.656  36.382  1.00 39.44 ? 16   ASN B CA  1 
ATOM   2995 C C   . ASN C 1 16  ? 16.205  26.765  37.184  1.00 39.21 ? 16   ASN B C   1 
ATOM   2996 O O   . ASN C 1 16  ? 16.364  26.993  38.389  1.00 39.59 ? 16   ASN B O   1 
ATOM   2997 C CB  . ASN C 1 16  ? 14.845  27.098  35.010  1.00 38.99 ? 16   ASN B CB  1 
ATOM   2998 C CG  . ASN C 1 16  ? 13.768  27.962  34.317  1.00 38.24 ? 16   ASN B CG  1 
ATOM   2999 O OD1 . ASN C 1 16  ? 12.591  27.937  34.688  1.00 35.92 ? 16   ASN B OD1 1 
ATOM   3000 N ND2 . ASN C 1 16  ? 14.181  28.727  33.302  1.00 37.69 ? 16   ASN B ND2 1 
ATOM   3001 N N   . GLY C 1 17  ? 16.845  25.774  36.561  1.00 38.56 ? 17   GLY B N   1 
ATOM   3002 C CA  . GLY C 1 17  ? 17.814  24.932  37.285  1.00 37.53 ? 17   GLY B CA  1 
ATOM   3003 C C   . GLY C 1 17  ? 19.086  25.734  37.411  1.00 36.85 ? 17   GLY B C   1 
ATOM   3004 O O   . GLY C 1 17  ? 19.065  26.826  37.936  1.00 37.13 ? 17   GLY B O   1 
ATOM   3005 N N   . GLY C 1 18  ? 20.196  25.192  36.939  1.00 36.29 ? 18   GLY B N   1 
ATOM   3006 C CA  . GLY C 1 18  ? 21.343  26.005  36.544  1.00 35.89 ? 18   GLY B CA  1 
ATOM   3007 C C   . GLY C 1 18  ? 22.068  26.888  37.533  1.00 35.59 ? 18   GLY B C   1 
ATOM   3008 O O   . GLY C 1 18  ? 21.487  27.733  38.190  1.00 35.33 ? 18   GLY B O   1 
ATOM   3009 N N   . VAL C 1 19  ? 23.373  26.721  37.602  1.00 35.78 ? 19   VAL B N   1 
ATOM   3010 C CA  . VAL C 1 19  ? 24.132  27.468  38.570  1.00 36.15 ? 19   VAL B CA  1 
ATOM   3011 C C   . VAL C 1 19  ? 25.292  28.236  37.964  1.00 36.56 ? 19   VAL B C   1 
ATOM   3012 O O   . VAL C 1 19  ? 25.941  27.807  37.014  1.00 36.09 ? 19   VAL B O   1 
ATOM   3013 C CB  . VAL C 1 19  ? 24.597  26.583  39.744  1.00 36.18 ? 19   VAL B CB  1 
ATOM   3014 C CG1 . VAL C 1 19  ? 23.550  25.515  40.032  1.00 36.28 ? 19   VAL B CG1 1 
ATOM   3015 C CG2 . VAL C 1 19  ? 25.956  25.947  39.463  1.00 35.57 ? 19   VAL B CG2 1 
ATOM   3016 N N   . CYS C 1 20  ? 25.529  29.390  38.566  1.00 37.46 ? 20   CYS B N   1 
ATOM   3017 C CA  . CYS C 1 20  ? 26.530  30.338  38.150  1.00 38.30 ? 20   CYS B CA  1 
ATOM   3018 C C   . CYS C 1 20  ? 27.914  29.753  38.319  1.00 36.93 ? 20   CYS B C   1 
ATOM   3019 O O   . CYS C 1 20  ? 28.157  28.926  39.199  1.00 36.77 ? 20   CYS B O   1 
ATOM   3020 C CB  . CYS C 1 20  ? 26.410  31.560  39.041  1.00 39.48 ? 20   CYS B CB  1 
ATOM   3021 S SG  . CYS C 1 20  ? 26.343  33.128  38.185  1.00 46.42 ? 20   CYS B SG  1 
ATOM   3022 N N   . VAL C 1 21  ? 28.821  30.200  37.467  1.00 35.64 ? 21   VAL B N   1 
ATOM   3023 C CA  . VAL C 1 21  ? 30.218  29.787  37.522  1.00 34.28 ? 21   VAL B CA  1 
ATOM   3024 C C   . VAL C 1 21  ? 31.102  30.855  36.853  1.00 33.54 ? 21   VAL B C   1 
ATOM   3025 O O   . VAL C 1 21  ? 31.091  30.994  35.626  1.00 33.86 ? 21   VAL B O   1 
ATOM   3026 C CB  . VAL C 1 21  ? 30.413  28.373  36.914  1.00 34.20 ? 21   VAL B CB  1 
ATOM   3027 C CG1 . VAL C 1 21  ? 29.229  27.981  36.034  1.00 33.69 ? 21   VAL B CG1 1 
ATOM   3028 C CG2 . VAL C 1 21  ? 31.735  28.258  36.167  1.00 34.01 ? 21   VAL B CG2 1 
ATOM   3029 N N   . SER C 1 22  ? 31.835  31.621  37.668  1.00 32.05 ? 22   SER B N   1 
ATOM   3030 C CA  . SER C 1 22  ? 32.710  32.701  37.190  1.00 30.54 ? 22   SER B CA  1 
ATOM   3031 C C   . SER C 1 22  ? 34.117  32.176  36.879  1.00 29.63 ? 22   SER B C   1 
ATOM   3032 O O   . SER C 1 22  ? 34.415  31.019  37.131  1.00 29.92 ? 22   SER B O   1 
ATOM   3033 C CB  . SER C 1 22  ? 32.797  33.789  38.247  1.00 30.54 ? 22   SER B CB  1 
ATOM   3034 O OG  . SER C 1 22  ? 33.405  33.270  39.410  1.00 30.39 ? 22   SER B OG  1 
ATOM   3035 N N   . TYR C 1 23  ? 34.986  33.004  36.318  1.00 28.17 ? 23   TYR B N   1 
ATOM   3036 C CA  . TYR C 1 23  ? 36.327  32.544  36.006  1.00 26.96 ? 23   TYR B CA  1 
ATOM   3037 C C   . TYR C 1 23  ? 37.401  33.548  36.386  1.00 26.31 ? 23   TYR B C   1 
ATOM   3038 O O   . TYR C 1 23  ? 37.810  34.390  35.601  1.00 25.65 ? 23   TYR B O   1 
ATOM   3039 C CB  . TYR C 1 23  ? 36.453  32.116  34.548  1.00 27.07 ? 23   TYR B CB  1 
ATOM   3040 C CG  . TYR C 1 23  ? 35.551  30.983  34.173  1.00 27.09 ? 23   TYR B CG  1 
ATOM   3041 C CD1 . TYR C 1 23  ? 36.051  29.712  33.941  1.00 28.03 ? 23   TYR B CD1 1 
ATOM   3042 C CD2 . TYR C 1 23  ? 34.189  31.190  34.030  1.00 28.84 ? 23   TYR B CD2 1 
ATOM   3043 C CE1 . TYR C 1 23  ? 35.195  28.659  33.601  1.00 30.20 ? 23   TYR B CE1 1 
ATOM   3044 C CE2 . TYR C 1 23  ? 33.327  30.163  33.687  1.00 30.69 ? 23   TYR B CE2 1 
ATOM   3045 C CZ  . TYR C 1 23  ? 33.827  28.902  33.476  1.00 31.19 ? 23   TYR B CZ  1 
ATOM   3046 O OH  . TYR C 1 23  ? 32.936  27.916  33.129  1.00 32.42 ? 23   TYR B OH  1 
ATOM   3047 N N   . LYS C 1 24  ? 37.810  33.428  37.642  1.00 26.16 ? 24   LYS B N   1 
ATOM   3048 C CA  . LYS C 1 24  ? 39.031  34.006  38.220  1.00 25.76 ? 24   LYS B CA  1 
ATOM   3049 C C   . LYS C 1 24  ? 39.979  34.700  37.224  1.00 25.49 ? 24   LYS B C   1 
ATOM   3050 O O   . LYS C 1 24  ? 40.133  35.922  37.295  1.00 25.93 ? 24   LYS B O   1 
ATOM   3051 C CB  . LYS C 1 24  ? 39.770  32.934  39.048  1.00 25.34 ? 24   LYS B CB  1 
ATOM   3052 C CG  . LYS C 1 24  ? 40.714  33.481  40.071  1.00 24.34 ? 24   LYS B CG  1 
ATOM   3053 C CD  . LYS C 1 24  ? 41.911  32.574  40.265  1.00 23.82 ? 24   LYS B CD  1 
ATOM   3054 C CE  . LYS C 1 24  ? 41.523  31.191  40.768  1.00 24.58 ? 24   LYS B CE  1 
ATOM   3055 N NZ  . LYS C 1 24  ? 42.635  30.449  41.472  1.00 23.54 ? 24   LYS B NZ  1 
ATOM   3056 N N   . TYR C 1 25  ? 40.573  33.950  36.296  1.00 24.75 ? 25   TYR B N   1 
ATOM   3057 C CA  . TYR C 1 25  ? 41.586  34.507  35.383  1.00 24.63 ? 25   TYR B CA  1 
ATOM   3058 C C   . TYR C 1 25  ? 41.111  35.326  34.142  1.00 24.95 ? 25   TYR B C   1 
ATOM   3059 O O   . TYR C 1 25  ? 41.922  35.725  33.284  1.00 24.76 ? 25   TYR B O   1 
ATOM   3060 C CB  . TYR C 1 25  ? 42.509  33.396  34.946  1.00 24.19 ? 25   TYR B CB  1 
ATOM   3061 C CG  . TYR C 1 25  ? 43.347  32.938  36.075  1.00 24.22 ? 25   TYR B CG  1 
ATOM   3062 C CD1 . TYR C 1 25  ? 44.530  33.586  36.372  1.00 24.29 ? 25   TYR B CD1 1 
ATOM   3063 C CD2 . TYR C 1 25  ? 42.954  31.869  36.878  1.00 25.06 ? 25   TYR B CD2 1 
ATOM   3064 C CE1 . TYR C 1 25  ? 45.316  33.183  37.434  1.00 24.22 ? 25   TYR B CE1 1 
ATOM   3065 C CE2 . TYR C 1 25  ? 43.741  31.449  37.941  1.00 24.15 ? 25   TYR B CE2 1 
ATOM   3066 C CZ  . TYR C 1 25  ? 44.920  32.123  38.209  1.00 23.97 ? 25   TYR B CZ  1 
ATOM   3067 O OH  . TYR C 1 25  ? 45.731  31.750  39.237  1.00 24.78 ? 25   TYR B OH  1 
ATOM   3068 N N   . PHE C 1 26  ? 39.806  35.581  34.076  1.00 24.97 ? 26   PHE B N   1 
ATOM   3069 C CA  . PHE C 1 26  ? 39.157  36.061  32.884  1.00 24.74 ? 26   PHE B CA  1 
ATOM   3070 C C   . PHE C 1 26  ? 38.160  37.122  33.267  1.00 25.66 ? 26   PHE B C   1 
ATOM   3071 O O   . PHE C 1 26  ? 36.968  36.999  33.039  1.00 26.06 ? 26   PHE B O   1 
ATOM   3072 C CB  . PHE C 1 26  ? 38.472  34.877  32.214  1.00 24.18 ? 26   PHE B CB  1 
ATOM   3073 C CG  . PHE C 1 26  ? 39.418  33.987  31.510  1.00 22.43 ? 26   PHE B CG  1 
ATOM   3074 C CD1 . PHE C 1 26  ? 40.060  32.978  32.180  1.00 22.62 ? 26   PHE B CD1 1 
ATOM   3075 C CD2 . PHE C 1 26  ? 39.699  34.188  30.183  1.00 22.13 ? 26   PHE B CD2 1 
ATOM   3076 C CE1 . PHE C 1 26  ? 40.962  32.172  31.547  1.00 23.22 ? 26   PHE B CE1 1 
ATOM   3077 C CE2 . PHE C 1 26  ? 40.593  33.402  29.533  1.00 23.43 ? 26   PHE B CE2 1 
ATOM   3078 C CZ  . PHE C 1 26  ? 41.233  32.384  30.210  1.00 24.54 ? 26   PHE B CZ  1 
ATOM   3079 N N   . SER C 1 27  ? 38.657  38.161  33.905  1.00 26.79 ? 27   SER B N   1 
ATOM   3080 C CA  . SER C 1 27  ? 37.801  39.215  34.439  1.00 27.74 ? 27   SER B CA  1 
ATOM   3081 C C   . SER C 1 27  ? 36.500  38.693  35.081  1.00 28.37 ? 27   SER B C   1 
ATOM   3082 O O   . SER C 1 27  ? 35.402  39.142  34.752  1.00 28.41 ? 27   SER B O   1 
ATOM   3083 C CB  . SER C 1 27  ? 37.541  40.244  33.346  1.00 27.73 ? 27   SER B CB  1 
ATOM   3084 O OG  . SER C 1 27  ? 38.735  40.462  32.611  1.00 27.57 ? 27   SER B OG  1 
ATOM   3085 N N   . ARG C 1 28  ? 36.657  37.757  36.022  1.00 29.46 ? 28   ARG B N   1 
ATOM   3086 C CA  . ARG C 1 28  ? 35.548  37.113  36.756  1.00 30.32 ? 28   ARG B CA  1 
ATOM   3087 C C   . ARG C 1 28  ? 34.277  36.981  35.900  1.00 30.42 ? 28   ARG B C   1 
ATOM   3088 O O   . ARG C 1 28  ? 33.245  37.569  36.213  1.00 30.61 ? 28   ARG B O   1 
ATOM   3089 C CB  . ARG C 1 28  ? 35.287  37.780  38.135  1.00 30.04 ? 28   ARG B CB  1 
ATOM   3090 C CG  . ARG C 1 28  ? 35.717  39.272  38.251  1.00 32.56 ? 28   ARG B CG  1 
ATOM   3091 C CD  . ARG C 1 28  ? 36.964  39.584  39.141  1.00 36.05 ? 28   ARG B CD  1 
ATOM   3092 N NE  . ARG C 1 28  ? 37.658  38.377  39.586  1.00 40.94 ? 28   ARG B NE  1 
ATOM   3093 C CZ  . ARG C 1 28  ? 37.358  37.701  40.704  1.00 43.93 ? 28   ARG B CZ  1 
ATOM   3094 N NH1 . ARG C 1 28  ? 36.384  38.125  41.517  1.00 44.27 ? 28   ARG B NH1 1 
ATOM   3095 N NH2 . ARG C 1 28  ? 38.030  36.593  41.020  1.00 44.62 ? 28   ARG B NH2 1 
ATOM   3096 N N   . ILE C 1 29  ? 34.372  36.205  34.816  1.00 30.72 ? 29   ILE B N   1 
ATOM   3097 C CA  . ILE C 1 29  ? 33.267  36.066  33.846  1.00 31.26 ? 29   ILE B CA  1 
ATOM   3098 C C   . ILE C 1 29  ? 32.270  34.906  34.115  1.00 32.05 ? 29   ILE B C   1 
ATOM   3099 O O   . ILE C 1 29  ? 32.609  33.728  34.040  1.00 32.15 ? 29   ILE B O   1 
ATOM   3100 C CB  . ILE C 1 29  ? 33.776  36.093  32.364  1.00 31.00 ? 29   ILE B CB  1 
ATOM   3101 C CG1 . ILE C 1 29  ? 32.591  36.123  31.394  1.00 31.36 ? 29   ILE B CG1 1 
ATOM   3102 C CG2 . ILE C 1 29  ? 34.780  34.971  32.074  1.00 29.48 ? 29   ILE B CG2 1 
ATOM   3103 C CD1 . ILE C 1 29  ? 32.978  36.323  29.944  1.00 32.23 ? 29   ILE B CD1 1 
ATOM   3104 N N   . ARG C 1 30  ? 31.029  35.257  34.420  1.00 32.95 ? 30   ARG B N   1 
ATOM   3105 C CA  . ARG C 1 30  ? 30.042  34.267  34.845  1.00 33.93 ? 30   ARG B CA  1 
ATOM   3106 C C   . ARG C 1 30  ? 29.574  33.418  33.687  1.00 33.95 ? 30   ARG B C   1 
ATOM   3107 O O   . ARG C 1 30  ? 29.736  33.787  32.520  1.00 34.21 ? 30   ARG B O   1 
ATOM   3108 C CB  . ARG C 1 30  ? 28.855  34.939  35.551  1.00 34.36 ? 30   ARG B CB  1 
ATOM   3109 C CG  . ARG C 1 30  ? 29.097  35.192  37.054  1.00 37.02 ? 30   ARG B CG  1 
ATOM   3110 C CD  . ARG C 1 30  ? 28.988  36.672  37.457  1.00 40.73 ? 30   ARG B CD  1 
ATOM   3111 N NE  . ARG C 1 30  ? 27.916  37.356  36.738  1.00 44.25 ? 30   ARG B NE  1 
ATOM   3112 C CZ  . ARG C 1 30  ? 27.074  38.236  37.278  1.00 47.61 ? 30   ARG B CZ  1 
ATOM   3113 N NH1 . ARG C 1 30  ? 27.131  38.558  38.572  1.00 48.72 ? 30   ARG B NH1 1 
ATOM   3114 N NH2 . ARG C 1 30  ? 26.148  38.790  36.515  1.00 49.45 ? 30   ARG B NH2 1 
ATOM   3115 N N   . ARG C 1 31  ? 29.027  32.257  34.032  1.00 34.02 ? 31   ARG B N   1 
ATOM   3116 C CA  . ARG C 1 31  ? 28.464  31.324  33.075  1.00 33.89 ? 31   ARG B CA  1 
ATOM   3117 C C   . ARG C 1 31  ? 27.283  30.655  33.733  1.00 33.77 ? 31   ARG B C   1 
ATOM   3118 O O   . ARG C 1 31  ? 26.902  31.043  34.832  1.00 34.13 ? 31   ARG B O   1 
ATOM   3119 C CB  . ARG C 1 31  ? 29.490  30.295  32.654  1.00 33.83 ? 31   ARG B CB  1 
ATOM   3120 C CG  . ARG C 1 31  ? 28.913  29.292  31.720  1.00 34.75 ? 31   ARG B CG  1 
ATOM   3121 C CD  . ARG C 1 31  ? 29.877  28.202  31.461  1.00 37.13 ? 31   ARG B CD  1 
ATOM   3122 N NE  . ARG C 1 31  ? 29.231  26.925  31.693  1.00 38.27 ? 31   ARG B NE  1 
ATOM   3123 C CZ  . ARG C 1 31  ? 29.698  26.011  32.529  1.00 39.79 ? 31   ARG B CZ  1 
ATOM   3124 N NH1 . ARG C 1 31  ? 30.824  26.224  33.203  1.00 40.06 ? 31   ARG B NH1 1 
ATOM   3125 N NH2 . ARG C 1 31  ? 29.044  24.873  32.678  1.00 41.66 ? 31   ARG B NH2 1 
ATOM   3126 N N   . CYS C 1 32  ? 26.693  29.662  33.081  1.00 33.67 ? 32   CYS B N   1 
ATOM   3127 C CA  . CYS C 1 32  ? 25.452  29.129  33.593  1.00 34.23 ? 32   CYS B CA  1 
ATOM   3128 C C   . CYS C 1 32  ? 25.084  27.698  33.201  1.00 33.55 ? 32   CYS B C   1 
ATOM   3129 O O   . CYS C 1 32  ? 24.171  27.477  32.405  1.00 34.01 ? 32   CYS B O   1 
ATOM   3130 C CB  . CYS C 1 32  ? 24.325  30.063  33.225  1.00 34.57 ? 32   CYS B CB  1 
ATOM   3131 S SG  . CYS C 1 32  ? 23.021  29.870  34.375  1.00 40.40 ? 32   CYS B SG  1 
ATOM   3132 N N   . SER C 1 33  ? 25.778  26.722  33.777  1.00 32.53 ? 33   SER B N   1 
ATOM   3133 C CA  . SER C 1 33  ? 25.478  25.310  33.523  1.00 31.21 ? 33   SER B CA  1 
ATOM   3134 C C   . SER C 1 33  ? 24.028  25.003  33.841  1.00 30.05 ? 33   SER B C   1 
ATOM   3135 O O   . SER C 1 33  ? 23.652  24.950  35.004  1.00 30.21 ? 33   SER B O   1 
ATOM   3136 C CB  . SER C 1 33  ? 26.392  24.439  34.355  1.00 31.00 ? 33   SER B CB  1 
ATOM   3137 O OG  . SER C 1 33  ? 27.062  25.289  35.261  1.00 32.02 ? 33   SER B OG  1 
ATOM   3138 N N   . CYS C 1 34  ? 23.233  24.805  32.793  1.00 28.32 ? 34   CYS B N   1 
ATOM   3139 C CA  . CYS C 1 34  ? 21.807  24.640  32.924  1.00 26.81 ? 34   CYS B CA  1 
ATOM   3140 C C   . CYS C 1 34  ? 21.474  23.189  33.061  1.00 25.04 ? 34   CYS B C   1 
ATOM   3141 O O   . CYS C 1 34  ? 22.258  22.346  32.656  1.00 24.60 ? 34   CYS B O   1 
ATOM   3142 C CB  . CYS C 1 34  ? 21.133  25.164  31.669  1.00 27.28 ? 34   CYS B CB  1 
ATOM   3143 S SG  . CYS C 1 34  ? 21.486  26.897  31.286  1.00 31.04 ? 34   CYS B SG  1 
ATOM   3144 N N   . PRO C 1 35  ? 20.281  22.887  33.594  1.00 23.79 ? 35   PRO B N   1 
ATOM   3145 C CA  . PRO C 1 35  ? 19.778  21.547  33.503  1.00 22.92 ? 35   PRO B CA  1 
ATOM   3146 C C   . PRO C 1 35  ? 19.438  21.300  32.048  1.00 22.49 ? 35   PRO B C   1 
ATOM   3147 O O   . PRO C 1 35  ? 19.531  22.207  31.235  1.00 22.68 ? 35   PRO B O   1 
ATOM   3148 C CB  . PRO C 1 35  ? 18.502  21.611  34.337  1.00 22.49 ? 35   PRO B CB  1 
ATOM   3149 C CG  . PRO C 1 35  ? 18.014  22.932  34.171  1.00 22.44 ? 35   PRO B CG  1 
ATOM   3150 C CD  . PRO C 1 35  ? 19.246  23.801  34.102  1.00 24.00 ? 35   PRO B CD  1 
ATOM   3151 N N   . ARG C 1 36  ? 19.016  20.092  31.719  1.00 22.20 ? 36   ARG B N   1 
ATOM   3152 C CA  . ARG C 1 36  ? 18.741  19.734  30.323  1.00 21.35 ? 36   ARG B CA  1 
ATOM   3153 C C   . ARG C 1 36  ? 17.652  20.508  29.561  1.00 20.87 ? 36   ARG B C   1 
ATOM   3154 O O   . ARG C 1 36  ? 17.878  20.869  28.415  1.00 21.12 ? 36   ARG B O   1 
ATOM   3155 C CB  . ARG C 1 36  ? 18.444  18.246  30.209  1.00 21.34 ? 36   ARG B CB  1 
ATOM   3156 C CG  . ARG C 1 36  ? 18.703  17.756  28.836  1.00 19.37 ? 36   ARG B CG  1 
ATOM   3157 C CD  . ARG C 1 36  ? 18.102  16.443  28.601  1.00 16.61 ? 36   ARG B CD  1 
ATOM   3158 N NE  . ARG C 1 36  ? 18.658  15.965  27.360  1.00 16.40 ? 36   ARG B NE  1 
ATOM   3159 C CZ  . ARG C 1 36  ? 17.939  15.642  26.304  1.00 16.18 ? 36   ARG B CZ  1 
ATOM   3160 N NH1 . ARG C 1 36  ? 16.619  15.702  26.346  1.00 16.01 ? 36   ARG B NH1 1 
ATOM   3161 N NH2 . ARG C 1 36  ? 18.553  15.238  25.215  1.00 16.91 ? 36   ARG B NH2 1 
ATOM   3162 N N   . LYS C 1 37  ? 16.479  20.708  30.158  1.00 20.33 ? 37   LYS B N   1 
ATOM   3163 C CA  . LYS C 1 37  ? 15.343  21.303  29.442  1.00 20.42 ? 37   LYS B CA  1 
ATOM   3164 C C   . LYS C 1 37  ? 15.513  22.782  29.184  1.00 20.32 ? 37   LYS B C   1 
ATOM   3165 O O   . LYS C 1 37  ? 14.644  23.408  28.585  1.00 20.91 ? 37   LYS B O   1 
ATOM   3166 C CB  . LYS C 1 37  ? 14.011  21.116  30.192  1.00 20.65 ? 37   LYS B CB  1 
ATOM   3167 C CG  . LYS C 1 37  ? 13.523  19.671  30.290  1.00 22.51 ? 37   LYS B CG  1 
ATOM   3168 C CD  . LYS C 1 37  ? 12.020  19.548  30.534  1.00 23.47 ? 37   LYS B CD  1 
ATOM   3169 C CE  . LYS C 1 37  ? 11.587  18.082  30.479  1.00 24.14 ? 37   LYS B CE  1 
ATOM   3170 N NZ  . LYS C 1 37  ? 10.200  17.877  29.925  1.00 25.06 ? 37   LYS B NZ  1 
ATOM   3171 N N   . PHE C 1 38  ? 16.602  23.368  29.655  1.00 19.89 ? 38   PHE B N   1 
ATOM   3172 C CA  . PHE C 1 38  ? 16.743  24.798  29.540  1.00 19.39 ? 38   PHE B CA  1 
ATOM   3173 C C   . PHE C 1 38  ? 18.101  25.131  29.028  1.00 20.08 ? 38   PHE B C   1 
ATOM   3174 O O   . PHE C 1 38  ? 19.080  24.526  29.434  1.00 20.25 ? 38   PHE B O   1 
ATOM   3175 C CB  . PHE C 1 38  ? 16.485  25.477  30.889  1.00 19.05 ? 38   PHE B CB  1 
ATOM   3176 C CG  . PHE C 1 38  ? 15.163  25.155  31.463  1.00 16.28 ? 38   PHE B CG  1 
ATOM   3177 C CD1 . PHE C 1 38  ? 14.031  25.756  30.977  1.00 14.44 ? 38   PHE B CD1 1 
ATOM   3178 C CD2 . PHE C 1 38  ? 15.047  24.217  32.467  1.00 15.88 ? 38   PHE B CD2 1 
ATOM   3179 C CE1 . PHE C 1 38  ? 12.793  25.436  31.482  1.00 15.31 ? 38   PHE B CE1 1 
ATOM   3180 C CE2 . PHE C 1 38  ? 13.814  23.883  32.988  1.00 15.97 ? 38   PHE B CE2 1 
ATOM   3181 C CZ  . PHE C 1 38  ? 12.680  24.492  32.494  1.00 16.01 ? 38   PHE B CZ  1 
ATOM   3182 N N   . GLN C 1 39  ? 18.163  26.097  28.131  1.00 21.03 ? 39   GLN B N   1 
ATOM   3183 C CA  . GLN C 1 39  ? 19.429  26.506  27.566  1.00 22.55 ? 39   GLN B CA  1 
ATOM   3184 C C   . GLN C 1 39  ? 19.486  28.014  27.620  1.00 23.79 ? 39   GLN B C   1 
ATOM   3185 O O   . GLN C 1 39  ? 18.607  28.649  28.220  1.00 23.88 ? 39   GLN B O   1 
ATOM   3186 C CB  . GLN C 1 39  ? 19.562  25.984  26.140  1.00 22.36 ? 39   GLN B CB  1 
ATOM   3187 C CG  . GLN C 1 39  ? 19.043  24.548  25.997  1.00 23.43 ? 39   GLN B CG  1 
ATOM   3188 C CD  . GLN C 1 39  ? 18.935  24.060  24.575  1.00 23.81 ? 39   GLN B CD  1 
ATOM   3189 O OE1 . GLN C 1 39  ? 19.387  22.968  24.245  1.00 23.75 ? 39   GLN B OE1 1 
ATOM   3190 N NE2 . GLN C 1 39  ? 18.323  24.859  23.729  1.00 26.23 ? 39   GLN B NE2 1 
ATOM   3191 N N   . GLY C 1 40  ? 20.530  28.576  27.015  1.00 25.20 ? 40   GLY B N   1 
ATOM   3192 C CA  . GLY C 1 40  ? 20.744  30.016  27.000  1.00 27.10 ? 40   GLY B CA  1 
ATOM   3193 C C   . GLY C 1 40  ? 21.723  30.504  28.045  1.00 28.61 ? 40   GLY B C   1 
ATOM   3194 O O   . GLY C 1 40  ? 21.991  29.815  29.033  1.00 28.76 ? 40   GLY B O   1 
ATOM   3195 N N   . GLU C 1 41  ? 22.236  31.712  27.811  1.00 30.30 ? 41   GLU B N   1 
ATOM   3196 C CA  . GLU C 1 41  ? 23.150  32.453  28.697  1.00 32.11 ? 41   GLU B CA  1 
ATOM   3197 C C   . GLU C 1 41  ? 22.675  32.471  30.161  1.00 32.58 ? 41   GLU B C   1 
ATOM   3198 O O   . GLU C 1 41  ? 23.473  32.693  31.070  1.00 32.99 ? 41   GLU B O   1 
ATOM   3199 C CB  . GLU C 1 41  ? 23.272  33.881  28.154  1.00 32.36 ? 41   GLU B CB  1 
ATOM   3200 C CG  . GLU C 1 41  ? 24.490  34.735  28.545  1.00 35.96 ? 41   GLU B CG  1 
ATOM   3201 C CD  . GLU C 1 41  ? 24.524  36.094  27.757  1.00 42.89 ? 41   GLU B CD  1 
ATOM   3202 O OE1 . GLU C 1 41  ? 24.404  37.193  28.380  1.00 44.04 ? 41   GLU B OE1 1 
ATOM   3203 O OE2 . GLU C 1 41  ? 24.629  36.066  26.495  1.00 45.37 ? 41   GLU B OE2 1 
ATOM   3204 N N   . HIS C 1 42  ? 21.384  32.213  30.376  1.00 32.96 ? 42   HIS B N   1 
ATOM   3205 C CA  . HIS C 1 42  ? 20.771  32.268  31.692  1.00 33.39 ? 42   HIS B CA  1 
ATOM   3206 C C   . HIS C 1 42  ? 19.794  31.127  31.905  1.00 32.55 ? 42   HIS B C   1 
ATOM   3207 O O   . HIS C 1 42  ? 18.973  31.180  32.822  1.00 32.58 ? 42   HIS B O   1 
ATOM   3208 C CB  . HIS C 1 42  ? 20.012  33.593  31.836  1.00 34.50 ? 42   HIS B CB  1 
ATOM   3209 C CG  . HIS C 1 42  ? 20.901  34.798  31.786  1.00 39.23 ? 42   HIS B CG  1 
ATOM   3210 N ND1 . HIS C 1 42  ? 21.550  35.198  30.632  1.00 41.90 ? 42   HIS B ND1 1 
ATOM   3211 C CD2 . HIS C 1 42  ? 21.272  35.676  32.753  1.00 42.55 ? 42   HIS B CD2 1 
ATOM   3212 C CE1 . HIS C 1 42  ? 22.283  36.268  30.891  1.00 43.24 ? 42   HIS B CE1 1 
ATOM   3213 N NE2 . HIS C 1 42  ? 22.134  36.577  32.171  1.00 44.49 ? 42   HIS B NE2 1 
ATOM   3214 N N   . CYS C 1 43  ? 19.849  30.110  31.049  1.00 31.62 ? 43   CYS B N   1 
ATOM   3215 C CA  . CYS C 1 43  ? 18.835  29.058  31.061  1.00 30.85 ? 43   CYS B CA  1 
ATOM   3216 C C   . CYS C 1 43  ? 17.453  29.679  30.963  1.00 29.71 ? 43   CYS B C   1 
ATOM   3217 O O   . CYS C 1 43  ? 16.544  29.355  31.716  1.00 29.18 ? 43   CYS B O   1 
ATOM   3218 C CB  . CYS C 1 43  ? 18.939  28.223  32.340  1.00 31.42 ? 43   CYS B CB  1 
ATOM   3219 S SG  . CYS C 1 43  ? 20.640  27.884  32.893  1.00 34.17 ? 43   CYS B SG  1 
ATOM   3220 N N   . GLU C 1 44  ? 17.309  30.604  30.033  1.00 28.97 ? 44   GLU B N   1 
ATOM   3221 C CA  . GLU C 1 44  ? 16.059  31.308  29.871  1.00 28.40 ? 44   GLU B CA  1 
ATOM   3222 C C   . GLU C 1 44  ? 15.209  30.580  28.857  1.00 27.84 ? 44   GLU B C   1 
ATOM   3223 O O   . GLU C 1 44  ? 13.998  30.784  28.783  1.00 27.85 ? 44   GLU B O   1 
ATOM   3224 C CB  . GLU C 1 44  ? 16.309  32.750  29.445  1.00 28.44 ? 44   GLU B CB  1 
ATOM   3225 C CG  . GLU C 1 44  ? 16.986  32.945  28.078  1.00 30.66 ? 44   GLU B CG  1 
ATOM   3226 C CD  . GLU C 1 44  ? 18.520  32.952  28.127  1.00 33.89 ? 44   GLU B CD  1 
ATOM   3227 O OE1 . GLU C 1 44  ? 19.120  31.990  28.664  1.00 34.43 ? 44   GLU B OE1 1 
ATOM   3228 O OE2 . GLU C 1 44  ? 19.126  33.922  27.606  1.00 35.35 ? 44   GLU B OE2 1 
ATOM   3229 N N   . ILE C 1 45  ? 15.851  29.705  28.092  1.00 27.33 ? 45   ILE B N   1 
ATOM   3230 C CA  . ILE C 1 45  ? 15.198  29.045  26.983  1.00 26.92 ? 45   ILE B CA  1 
ATOM   3231 C C   . ILE C 1 45  ? 14.814  27.639  27.370  1.00 26.90 ? 45   ILE B C   1 
ATOM   3232 O O   . ILE C 1 45  ? 15.672  26.863  27.753  1.00 27.06 ? 45   ILE B O   1 
ATOM   3233 C CB  . ILE C 1 45  ? 16.095  28.993  25.746  1.00 26.64 ? 45   ILE B CB  1 
ATOM   3234 C CG1 . ILE C 1 45  ? 17.033  30.188  25.720  1.00 26.49 ? 45   ILE B CG1 1 
ATOM   3235 C CG2 . ILE C 1 45  ? 15.244  28.990  24.494  1.00 27.13 ? 45   ILE B CG2 1 
ATOM   3236 C CD1 . ILE C 1 45  ? 18.040  30.138  24.647  1.00 27.52 ? 45   ILE B CD1 1 
ATOM   3237 N N   . ASP C 1 46  ? 13.518  27.333  27.271  1.00 27.14 ? 46   ASP B N   1 
ATOM   3238 C CA  . ASP C 1 46  ? 12.955  25.999  27.534  1.00 26.98 ? 46   ASP B CA  1 
ATOM   3239 C C   . ASP C 1 46  ? 12.935  25.203  26.254  1.00 27.49 ? 46   ASP B C   1 
ATOM   3240 O O   . ASP C 1 46  ? 12.064  25.365  25.410  1.00 28.28 ? 46   ASP B O   1 
ATOM   3241 C CB  . ASP C 1 46  ? 11.524  26.102  28.081  1.00 26.47 ? 46   ASP B CB  1 
ATOM   3242 C CG  . ASP C 1 46  ? 10.854  24.747  28.246  1.00 25.53 ? 46   ASP B CG  1 
ATOM   3243 O OD1 . ASP C 1 46  ? 11.414  23.717  27.800  1.00 23.35 ? 46   ASP B OD1 1 
ATOM   3244 O OD2 . ASP C 1 46  ? 9.752   24.722  28.830  1.00 25.16 ? 46   ASP B OD2 1 
ATOM   3245 N N   . ALA C 1 47  ? 13.890  24.322  26.101  1.00 27.84 ? 47   ALA B N   1 
ATOM   3246 C CA  . ALA C 1 47  ? 13.997  23.621  24.856  1.00 28.50 ? 47   ALA B CA  1 
ATOM   3247 C C   . ALA C 1 47  ? 12.982  22.467  24.715  1.00 29.10 ? 47   ALA B C   1 
ATOM   3248 O O   . ALA C 1 47  ? 13.045  21.697  23.759  1.00 29.03 ? 47   ALA B O   1 
ATOM   3249 C CB  . ALA C 1 47  ? 15.438  23.152  24.659  1.00 28.47 ? 47   ALA B CB  1 
ATOM   3250 N N   . SER C 1 48  ? 12.037  22.337  25.639  1.00 30.21 ? 48   SER B N   1 
ATOM   3251 C CA  . SER C 1 48  ? 11.116  21.201  25.551  1.00 31.66 ? 48   SER B CA  1 
ATOM   3252 C C   . SER C 1 48  ? 9.736   21.630  25.099  1.00 32.94 ? 48   SER B C   1 
ATOM   3253 O O   . SER C 1 48  ? 8.883   20.785  24.818  1.00 33.23 ? 48   SER B O   1 
ATOM   3254 C CB  . SER C 1 48  ? 10.999  20.477  26.876  1.00 31.34 ? 48   SER B CB  1 
ATOM   3255 O OG  . SER C 1 48  ? 10.115  21.187  27.717  1.00 32.08 ? 48   SER B OG  1 
ATOM   3256 N N   . LYS C 1 49  ? 9.514   22.937  25.030  1.00 34.25 ? 49   LYS B N   1 
ATOM   3257 C CA  . LYS C 1 49  ? 8.224   23.443  24.626  1.00 35.55 ? 49   LYS B CA  1 
ATOM   3258 C C   . LYS C 1 49  ? 7.964   23.310  23.125  1.00 36.76 ? 49   LYS B C   1 
ATOM   3259 O O   . LYS C 1 49  ? 8.882   23.408  22.314  1.00 36.91 ? 49   LYS B O   1 
ATOM   3260 C CB  . LYS C 1 49  ? 8.046   24.875  25.095  1.00 35.38 ? 49   LYS B CB  1 
ATOM   3261 C CG  . LYS C 1 49  ? 7.394   24.953  26.458  1.00 35.61 ? 49   LYS B CG  1 
ATOM   3262 C CD  . LYS C 1 49  ? 6.290   26.016  26.486  1.00 35.34 ? 49   LYS B CD  1 
ATOM   3263 C CE  . LYS C 1 49  ? 5.037   25.576  25.704  1.00 33.61 ? 49   LYS B CE  1 
ATOM   3264 N NZ  . LYS C 1 49  ? 4.024   26.668  25.584  1.00 32.24 ? 49   LYS B NZ  1 
ATOM   3265 N N   . THR C 1 50  ? 6.691   23.099  22.789  1.00 38.23 ? 50   THR B N   1 
ATOM   3266 C CA  . THR C 1 50  ? 6.209   22.814  21.431  1.00 39.48 ? 50   THR B CA  1 
ATOM   3267 C C   . THR C 1 50  ? 4.984   23.706  21.071  1.00 40.17 ? 50   THR B C   1 
ATOM   3268 O O   . THR C 1 50  ? 5.006   24.389  20.058  1.00 40.14 ? 50   THR B O   1 
ATOM   3269 C CB  . THR C 1 50  ? 5.946   21.261  21.224  1.00 39.67 ? 50   THR B CB  1 
ATOM   3270 O OG1 . THR C 1 50  ? 4.796   21.041  20.396  1.00 40.72 ? 50   THR B OG1 1 
ATOM   3271 C CG2 . THR C 1 50  ? 5.704   20.521  22.565  1.00 40.15 ? 50   THR B CG2 1 
ATOM   3272 N N   . CYS C 1 51  ? 3.936   23.703  21.903  1.00 41.25 ? 51   CYS B N   1 
ATOM   3273 C CA  . CYS C 1 51  ? 2.801   24.635  21.779  1.00 42.44 ? 51   CYS B CA  1 
ATOM   3274 C C   . CYS C 1 51  ? 3.135   26.036  22.336  1.00 42.00 ? 51   CYS B C   1 
ATOM   3275 O O   . CYS C 1 51  ? 4.214   26.244  22.889  1.00 41.98 ? 51   CYS B O   1 
ATOM   3276 C CB  . CYS C 1 51  ? 1.575   24.071  22.516  1.00 43.21 ? 51   CYS B CB  1 
ATOM   3277 S SG  . CYS C 1 51  ? 0.057   25.128  22.416  1.00 48.48 ? 51   CYS B SG  1 
ATOM   3278 N N   . TYR C 1 52  ? 2.213   26.990  22.188  1.00 41.69 ? 52   TYR B N   1 
ATOM   3279 C CA  . TYR C 1 52  ? 2.285   28.269  22.919  1.00 41.54 ? 52   TYR B CA  1 
ATOM   3280 C C   . TYR C 1 52  ? 1.044   28.537  23.821  1.00 41.16 ? 52   TYR B C   1 
ATOM   3281 O O   . TYR C 1 52  ? -0.074  28.679  23.331  1.00 40.92 ? 52   TYR B O   1 
ATOM   3282 C CB  . TYR C 1 52  ? 2.617   29.447  21.973  1.00 41.82 ? 52   TYR B CB  1 
ATOM   3283 C CG  . TYR C 1 52  ? 1.505   29.892  21.037  1.00 42.85 ? 52   TYR B CG  1 
ATOM   3284 C CD1 . TYR C 1 52  ? 0.822   31.089  21.261  1.00 43.41 ? 52   TYR B CD1 1 
ATOM   3285 C CD2 . TYR C 1 52  ? 1.136   29.121  19.927  1.00 43.92 ? 52   TYR B CD2 1 
ATOM   3286 C CE1 . TYR C 1 52  ? -0.208  31.502  20.417  1.00 43.38 ? 52   TYR B CE1 1 
ATOM   3287 C CE2 . TYR C 1 52  ? 0.107   29.526  19.075  1.00 43.47 ? 52   TYR B CE2 1 
ATOM   3288 C CZ  . TYR C 1 52  ? -0.557  30.716  19.331  1.00 43.47 ? 52   TYR B CZ  1 
ATOM   3289 O OH  . TYR C 1 52  ? -1.570  31.131  18.502  1.00 43.17 ? 52   TYR B OH  1 
ATOM   3290 N N   . HIS C 1 53  ? 1.274   28.577  25.140  1.00 40.83 ? 53   HIS B N   1 
ATOM   3291 C CA  . HIS C 1 53  ? 0.234   28.677  26.187  1.00 40.22 ? 53   HIS B CA  1 
ATOM   3292 C C   . HIS C 1 53  ? -0.788  29.777  25.932  1.00 39.29 ? 53   HIS B C   1 
ATOM   3293 O O   . HIS C 1 53  ? -0.499  30.944  26.181  1.00 39.27 ? 53   HIS B O   1 
ATOM   3294 C CB  . HIS C 1 53  ? 0.887   28.943  27.562  1.00 40.69 ? 53   HIS B CB  1 
ATOM   3295 C CG  . HIS C 1 53  ? 0.812   27.794  28.532  1.00 42.60 ? 53   HIS B CG  1 
ATOM   3296 N ND1 . HIS C 1 53  ? 1.903   27.368  29.266  1.00 44.31 ? 53   HIS B ND1 1 
ATOM   3297 C CD2 . HIS C 1 53  ? -0.226  27.010  28.918  1.00 43.88 ? 53   HIS B CD2 1 
ATOM   3298 C CE1 . HIS C 1 53  ? 1.546   26.360  30.044  1.00 44.52 ? 53   HIS B CE1 1 
ATOM   3299 N NE2 . HIS C 1 53  ? 0.259   26.123  29.851  1.00 44.74 ? 53   HIS B NE2 1 
ATOM   3300 N N   . GLY C 1 54  ? -1.980  29.395  25.466  1.00 38.37 ? 54   GLY B N   1 
ATOM   3301 C CA  . GLY C 1 54  ? -3.104  30.322  25.234  1.00 37.05 ? 54   GLY B CA  1 
ATOM   3302 C C   . GLY C 1 54  ? -2.721  31.504  24.369  1.00 36.33 ? 54   GLY B C   1 
ATOM   3303 O O   . GLY C 1 54  ? -2.830  31.463  23.145  1.00 36.33 ? 54   GLY B O   1 
ATOM   3304 N N   . ASN C 1 55  ? -2.263  32.563  25.018  1.00 35.55 ? 55   ASN B N   1 
ATOM   3305 C CA  . ASN C 1 55  ? -1.620  33.657  24.325  1.00 34.80 ? 55   ASN B CA  1 
ATOM   3306 C C   . ASN C 1 55  ? -0.147  33.340  24.079  1.00 34.36 ? 55   ASN B C   1 
ATOM   3307 O O   . ASN C 1 55  ? 0.292   32.204  24.254  1.00 34.37 ? 55   ASN B O   1 
ATOM   3308 C CB  . ASN C 1 55  ? -1.734  34.923  25.156  1.00 34.87 ? 55   ASN B CB  1 
ATOM   3309 C CG  . ASN C 1 55  ? -1.284  36.134  24.402  1.00 35.14 ? 55   ASN B CG  1 
ATOM   3310 O OD1 . ASN C 1 55  ? -1.780  36.404  23.311  1.00 36.78 ? 55   ASN B OD1 1 
ATOM   3311 N ND2 . ASN C 1 55  ? -0.331  36.869  24.962  1.00 34.62 ? 55   ASN B ND2 1 
ATOM   3312 N N   . GLY C 1 56  ? 0.625   34.341  23.682  1.00 33.75 ? 56   GLY B N   1 
ATOM   3313 C CA  . GLY C 1 56  ? 2.047   34.137  23.475  1.00 33.17 ? 56   GLY B CA  1 
ATOM   3314 C C   . GLY C 1 56  ? 2.886   34.606  24.638  1.00 32.77 ? 56   GLY B C   1 
ATOM   3315 O O   . GLY C 1 56  ? 4.038   34.188  24.776  1.00 32.92 ? 56   GLY B O   1 
ATOM   3316 N N   . ASP C 1 57  ? 2.294   35.466  25.472  1.00 32.25 ? 57   ASP B N   1 
ATOM   3317 C CA  . ASP C 1 57  ? 2.978   36.210  26.545  1.00 31.67 ? 57   ASP B CA  1 
ATOM   3318 C C   . ASP C 1 57  ? 4.031   35.398  27.288  1.00 31.44 ? 57   ASP B C   1 
ATOM   3319 O O   . ASP C 1 57  ? 5.178   35.834  27.457  1.00 31.39 ? 57   ASP B O   1 
ATOM   3320 C CB  . ASP C 1 57  ? 1.948   36.733  27.547  1.00 31.63 ? 57   ASP B CB  1 
ATOM   3321 C CG  . ASP C 1 57  ? 0.974   35.650  28.008  1.00 32.29 ? 57   ASP B CG  1 
ATOM   3322 O OD1 . ASP C 1 57  ? -0.180  35.980  28.377  1.00 33.17 ? 57   ASP B OD1 1 
ATOM   3323 O OD2 . ASP C 1 57  ? 1.353   34.459  27.986  1.00 32.05 ? 57   ASP B OD2 1 
ATOM   3324 N N   . SER C 1 58  ? 3.622   34.208  27.717  1.00 30.92 ? 58   SER B N   1 
ATOM   3325 C CA  . SER C 1 58  ? 4.454   33.342  28.523  1.00 30.27 ? 58   SER B CA  1 
ATOM   3326 C C   . SER C 1 58  ? 5.433   32.617  27.653  1.00 29.42 ? 58   SER B C   1 
ATOM   3327 O O   . SER C 1 58  ? 6.557   32.412  28.073  1.00 30.16 ? 58   SER B O   1 
ATOM   3328 C CB  . SER C 1 58  ? 3.607   32.331  29.281  1.00 30.51 ? 58   SER B CB  1 
ATOM   3329 O OG  . SER C 1 58  ? 2.501   32.975  29.905  1.00 32.22 ? 58   SER B OG  1 
ATOM   3330 N N   . TYR C 1 59  ? 5.022   32.238  26.443  1.00 28.27 ? 59   TYR B N   1 
ATOM   3331 C CA  . TYR C 1 59  ? 5.853   31.404  25.568  1.00 26.90 ? 59   TYR B CA  1 
ATOM   3332 C C   . TYR C 1 59  ? 7.320   31.833  25.645  1.00 26.53 ? 59   TYR B C   1 
ATOM   3333 O O   . TYR C 1 59  ? 7.622   33.033  25.629  1.00 26.35 ? 59   TYR B O   1 
ATOM   3334 C CB  . TYR C 1 59  ? 5.339   31.414  24.116  1.00 26.46 ? 59   TYR B CB  1 
ATOM   3335 C CG  . TYR C 1 59  ? 6.232   30.634  23.165  1.00 25.02 ? 59   TYR B CG  1 
ATOM   3336 C CD1 . TYR C 1 59  ? 6.208   29.249  23.147  1.00 24.66 ? 59   TYR B CD1 1 
ATOM   3337 C CD2 . TYR C 1 59  ? 7.115   31.275  22.296  1.00 22.97 ? 59   TYR B CD2 1 
ATOM   3338 C CE1 . TYR C 1 59  ? 7.030   28.521  22.289  1.00 22.50 ? 59   TYR B CE1 1 
ATOM   3339 C CE2 . TYR C 1 59  ? 7.940   30.547  21.451  1.00 21.02 ? 59   TYR B CE2 1 
ATOM   3340 C CZ  . TYR C 1 59  ? 7.882   29.175  21.458  1.00 20.73 ? 59   TYR B CZ  1 
ATOM   3341 O OH  . TYR C 1 59  ? 8.674   28.422  20.649  1.00 20.78 ? 59   TYR B OH  1 
ATOM   3342 N N   . ARG C 1 60  ? 8.214   30.853  25.748  1.00 25.91 ? 60   ARG B N   1 
ATOM   3343 C CA  . ARG C 1 60  ? 9.643   31.116  25.890  1.00 25.77 ? 60   ARG B CA  1 
ATOM   3344 C C   . ARG C 1 60  ? 10.491  30.077  25.138  1.00 25.73 ? 60   ARG B C   1 
ATOM   3345 O O   . ARG C 1 60  ? 11.662  29.818  25.480  1.00 25.44 ? 60   ARG B O   1 
ATOM   3346 C CB  . ARG C 1 60  ? 10.003  31.120  27.374  1.00 25.74 ? 60   ARG B CB  1 
ATOM   3347 C CG  . ARG C 1 60  ? 11.059  32.140  27.739  1.00 26.11 ? 60   ARG B CG  1 
ATOM   3348 C CD  . ARG C 1 60  ? 10.544  33.581  27.586  1.00 24.80 ? 60   ARG B CD  1 
ATOM   3349 N NE  . ARG C 1 60  ? 9.193   33.773  28.119  1.00 22.57 ? 60   ARG B NE  1 
ATOM   3350 C CZ  . ARG C 1 60  ? 8.539   34.928  28.083  1.00 22.81 ? 60   ARG B CZ  1 
ATOM   3351 N NH1 . ARG C 1 60  ? 9.108   35.996  27.553  1.00 24.51 ? 60   ARG B NH1 1 
ATOM   3352 N NH2 . ARG C 1 60  ? 7.315   35.029  28.571  1.00 23.13 ? 60   ARG B NH2 1 
ATOM   3353 N N   . GLY C 1 61  ? 9.883   29.505  24.100  1.00 25.56 ? 61   GLY B N   1 
ATOM   3354 C CA  . GLY C 1 61  ? 10.421  28.338  23.409  1.00 25.60 ? 61   GLY B CA  1 
ATOM   3355 C C   . GLY C 1 61  ? 11.506  28.590  22.377  1.00 25.58 ? 61   GLY B C   1 
ATOM   3356 O O   . GLY C 1 61  ? 12.262  29.581  22.477  1.00 25.58 ? 61   GLY B O   1 
ATOM   3357 N N   . LYS C 1 62  ? 11.576  27.690  21.388  1.00 24.93 ? 62   LYS B N   1 
ATOM   3358 C CA  . LYS C 1 62  ? 12.697  27.665  20.450  1.00 24.64 ? 62   LYS B CA  1 
ATOM   3359 C C   . LYS C 1 62  ? 12.342  27.828  18.964  1.00 25.14 ? 62   LYS B C   1 
ATOM   3360 O O   . LYS C 1 62  ? 13.225  27.708  18.100  1.00 24.96 ? 62   LYS B O   1 
ATOM   3361 C CB  . LYS C 1 62  ? 13.546  26.416  20.654  1.00 24.28 ? 62   LYS B CB  1 
ATOM   3362 C CG  . LYS C 1 62  ? 14.373  26.414  21.921  1.00 23.08 ? 62   LYS B CG  1 
ATOM   3363 C CD  . LYS C 1 62  ? 15.859  26.140  21.628  1.00 20.38 ? 62   LYS B CD  1 
ATOM   3364 C CE  . LYS C 1 62  ? 16.186  24.666  21.441  1.00 15.99 ? 62   LYS B CE  1 
ATOM   3365 N NZ  . LYS C 1 62  ? 17.548  24.556  20.854  1.00 14.44 ? 62   LYS B NZ  1 
ATOM   3366 N N   . ALA C 1 63  ? 11.066  28.105  18.681  1.00 25.63 ? 63   ALA B N   1 
ATOM   3367 C CA  . ALA C 1 63  ? 10.575  28.372  17.325  1.00 26.13 ? 63   ALA B CA  1 
ATOM   3368 C C   . ALA C 1 63  ? 11.396  29.424  16.614  1.00 26.79 ? 63   ALA B C   1 
ATOM   3369 O O   . ALA C 1 63  ? 11.639  30.509  17.112  1.00 27.04 ? 63   ALA B O   1 
ATOM   3370 C CB  . ALA C 1 63  ? 9.142   28.798  17.355  1.00 26.11 ? 63   ALA B CB  1 
ATOM   3371 N N   . ASN C 1 64  ? 11.801  29.099  15.412  1.00 27.67 ? 64   ASN B N   1 
ATOM   3372 C CA  . ASN C 1 64  ? 12.753  29.908  14.736  1.00 28.16 ? 64   ASN B CA  1 
ATOM   3373 C C   . ASN C 1 64  ? 12.169  30.792  13.626  1.00 28.03 ? 64   ASN B C   1 
ATOM   3374 O O   . ASN C 1 64  ? 12.714  31.852  13.350  1.00 28.44 ? 64   ASN B O   1 
ATOM   3375 C CB  . ASN C 1 64  ? 13.841  29.000  14.181  1.00 28.48 ? 64   ASN B CB  1 
ATOM   3376 C CG  . ASN C 1 64  ? 15.095  29.751  13.898  1.00 31.63 ? 64   ASN B CG  1 
ATOM   3377 O OD1 . ASN C 1 64  ? 15.566  30.505  14.763  1.00 33.74 ? 64   ASN B OD1 1 
ATOM   3378 N ND2 . ASN C 1 64  ? 15.635  29.609  12.667  1.00 33.92 ? 64   ASN B ND2 1 
ATOM   3379 N N   . THR C 1 65  ? 11.076  30.367  12.986  1.00 27.70 ? 65   THR B N   1 
ATOM   3380 C CA  . THR C 1 65  ? 10.667  30.953  11.689  1.00 27.23 ? 65   THR B CA  1 
ATOM   3381 C C   . THR C 1 65  ? 9.219   31.412  11.561  1.00 26.90 ? 65   THR B C   1 
ATOM   3382 O O   . THR C 1 65  ? 8.341   30.908  12.243  1.00 26.89 ? 65   THR B O   1 
ATOM   3383 C CB  . THR C 1 65  ? 10.901  29.977  10.547  1.00 27.17 ? 65   THR B CB  1 
ATOM   3384 O OG1 . THR C 1 65  ? 10.016  28.865  10.705  1.00 26.83 ? 65   THR B OG1 1 
ATOM   3385 C CG2 . THR C 1 65  ? 12.371  29.510  10.513  1.00 27.36 ? 65   THR B CG2 1 
ATOM   3386 N N   . ASP C 1 66  ? 8.975   32.334  10.636  1.00 26.53 ? 66   ASP B N   1 
ATOM   3387 C CA  . ASP C 1 66  ? 7.658   32.965  10.503  1.00 26.34 ? 66   ASP B CA  1 
ATOM   3388 C C   . ASP C 1 66  ? 6.602   32.033  9.929   1.00 25.90 ? 66   ASP B C   1 
ATOM   3389 O O   . ASP C 1 66  ? 6.895   30.883  9.607   1.00 25.52 ? 66   ASP B O   1 
ATOM   3390 C CB  . ASP C 1 66  ? 7.749   34.205  9.620   1.00 26.59 ? 66   ASP B CB  1 
ATOM   3391 C CG  . ASP C 1 66  ? 8.054   33.864  8.172   1.00 26.78 ? 66   ASP B CG  1 
ATOM   3392 O OD1 . ASP C 1 66  ? 8.199   34.797  7.357   1.00 26.46 ? 66   ASP B OD1 1 
ATOM   3393 O OD2 . ASP C 1 66  ? 8.161   32.661  7.856   1.00 27.18 ? 66   ASP B OD2 1 
ATOM   3394 N N   . THR C 1 67  ? 5.388   32.565  9.767   1.00 25.68 ? 67   THR B N   1 
ATOM   3395 C CA  . THR C 1 67  ? 4.229   31.775  9.342   1.00 25.48 ? 67   THR B CA  1 
ATOM   3396 C C   . THR C 1 67  ? 4.604   31.036  8.107   1.00 25.11 ? 67   THR B C   1 
ATOM   3397 O O   . THR C 1 67  ? 4.320   29.849  7.990   1.00 25.29 ? 67   THR B O   1 
ATOM   3398 C CB  . THR C 1 67  ? 3.014   32.633  8.953   1.00 25.48 ? 67   THR B CB  1 
ATOM   3399 O OG1 . THR C 1 67  ? 3.046   33.878  9.657   1.00 26.77 ? 67   THR B OG1 1 
ATOM   3400 C CG2 . THR C 1 67  ? 1.714   31.894  9.255   1.00 25.19 ? 67   THR B CG2 1 
ATOM   3401 N N   . LYS C 1 68  ? 5.281   31.759  7.213   1.00 24.62 ? 68   LYS B N   1 
ATOM   3402 C CA  . LYS C 1 68  ? 5.538   31.324  5.849   1.00 23.79 ? 68   LYS B CA  1 
ATOM   3403 C C   . LYS C 1 68  ? 7.016   31.069  5.568   1.00 23.16 ? 68   LYS B C   1 
ATOM   3404 O O   . LYS C 1 68  ? 7.501   31.379  4.483   1.00 22.75 ? 68   LYS B O   1 
ATOM   3405 C CB  . LYS C 1 68  ? 5.005   32.380  4.899   1.00 23.82 ? 68   LYS B CB  1 
ATOM   3406 C CG  . LYS C 1 68  ? 3.648   32.952  5.319   1.00 25.05 ? 68   LYS B CG  1 
ATOM   3407 C CD  . LYS C 1 68  ? 3.231   34.121  4.445   1.00 26.67 ? 68   LYS B CD  1 
ATOM   3408 C CE  . LYS C 1 68  ? 4.263   35.237  4.518   1.00 28.66 ? 68   LYS B CE  1 
ATOM   3409 N NZ  . LYS C 1 68  ? 5.617   34.761  4.080   1.00 29.44 ? 68   LYS B NZ  1 
ATOM   3410 N N   . GLY C 1 69  ? 7.728   30.548  6.573   1.00 22.71 ? 69   GLY B N   1 
ATOM   3411 C CA  . GLY C 1 69  ? 9.065   29.976  6.396   1.00 22.15 ? 69   GLY B CA  1 
ATOM   3412 C C   . GLY C 1 69  ? 10.314  30.841  6.504   1.00 21.77 ? 69   GLY B C   1 
ATOM   3413 O O   . GLY C 1 69  ? 11.424  30.330  6.570   1.00 21.86 ? 69   GLY B O   1 
ATOM   3414 N N   . ARG C 1 70  ? 10.183  32.149  6.496   1.00 21.41 ? 70   ARG B N   1 
ATOM   3415 C CA  . ARG C 1 70  ? 11.392  32.932  6.657   1.00 21.32 ? 70   ARG B CA  1 
ATOM   3416 C C   . ARG C 1 70  ? 11.976  32.816  8.079   1.00 21.14 ? 70   ARG B C   1 
ATOM   3417 O O   . ARG C 1 70  ? 11.237  32.782  9.071   1.00 20.70 ? 70   ARG B O   1 
ATOM   3418 C CB  . ARG C 1 70  ? 11.182  34.403  6.274   1.00 21.43 ? 70   ARG B CB  1 
ATOM   3419 C CG  . ARG C 1 70  ? 11.395  34.750  4.785   1.00 21.44 ? 70   ARG B CG  1 
ATOM   3420 C CD  . ARG C 1 70  ? 10.089  35.174  4.053   1.00 18.84 ? 70   ARG B CD  1 
ATOM   3421 N NE  . ARG C 1 70  ? 9.164   35.868  4.954   1.00 17.37 ? 70   ARG B NE  1 
ATOM   3422 C CZ  . ARG C 1 70  ? 8.152   36.635  4.572   1.00 16.35 ? 70   ARG B CZ  1 
ATOM   3423 N NH1 . ARG C 1 70  ? 7.922   36.827  3.286   1.00 18.54 ? 70   ARG B NH1 1 
ATOM   3424 N NH2 . ARG C 1 70  ? 7.367   37.211  5.476   1.00 15.28 ? 70   ARG B NH2 1 
ATOM   3425 N N   . PRO C 1 71  ? 13.307  32.710  8.157   1.00 20.98 ? 71   PRO B N   1 
ATOM   3426 C CA  . PRO C 1 71  ? 14.156  32.895  9.302   1.00 20.94 ? 71   PRO B CA  1 
ATOM   3427 C C   . PRO C 1 71  ? 13.853  34.185  9.988   1.00 21.11 ? 71   PRO B C   1 
ATOM   3428 O O   . PRO C 1 71  ? 13.778  35.205  9.308   1.00 20.78 ? 71   PRO B O   1 
ATOM   3429 C CB  . PRO C 1 71  ? 15.523  33.060  8.661   1.00 20.58 ? 71   PRO B CB  1 
ATOM   3430 C CG  . PRO C 1 71  ? 15.489  32.160  7.534   1.00 21.45 ? 71   PRO B CG  1 
ATOM   3431 C CD  . PRO C 1 71  ? 14.047  32.046  7.075   1.00 21.41 ? 71   PRO B CD  1 
ATOM   3432 N N   . CYS C 1 72  ? 13.713  34.146  11.318  1.00 21.64 ? 72   CYS B N   1 
ATOM   3433 C CA  . CYS C 1 72  ? 13.694  35.369  12.112  1.00 22.37 ? 72   CYS B CA  1 
ATOM   3434 C C   . CYS C 1 72  ? 15.108  35.895  12.286  1.00 22.39 ? 72   CYS B C   1 
ATOM   3435 O O   . CYS C 1 72  ? 16.097  35.269  11.870  1.00 22.05 ? 72   CYS B O   1 
ATOM   3436 C CB  . CYS C 1 72  ? 13.101  35.139  13.480  1.00 22.65 ? 72   CYS B CB  1 
ATOM   3437 S SG  . CYS C 1 72  ? 11.475  34.389  13.507  1.00 26.15 ? 72   CYS B SG  1 
ATOM   3438 N N   . LEU C 1 73  ? 15.196  37.056  12.923  1.00 22.76 ? 73   LEU B N   1 
ATOM   3439 C CA  . LEU C 1 73  ? 16.483  37.741  13.123  1.00 22.76 ? 73   LEU B CA  1 
ATOM   3440 C C   . LEU C 1 73  ? 16.826  37.861  14.619  1.00 22.54 ? 73   LEU B C   1 
ATOM   3441 O O   . LEU C 1 73  ? 15.986  38.270  15.438  1.00 22.25 ? 73   LEU B O   1 
ATOM   3442 C CB  . LEU C 1 73  ? 16.452  39.127  12.454  1.00 22.78 ? 73   LEU B CB  1 
ATOM   3443 C CG  . LEU C 1 73  ? 15.812  39.268  11.068  1.00 20.94 ? 73   LEU B CG  1 
ATOM   3444 C CD1 . LEU C 1 73  ? 15.133  40.633  10.935  1.00 18.49 ? 73   LEU B CD1 1 
ATOM   3445 C CD2 . LEU C 1 73  ? 16.852  39.009  9.963   1.00 19.81 ? 73   LEU B CD2 1 
ATOM   3446 N N   . ALA C 1 74  ? 18.053  37.489  14.960  1.00 22.27 ? 74   ALA B N   1 
ATOM   3447 C CA  . ALA C 1 74  ? 18.489  37.511  16.344  1.00 22.40 ? 74   ALA B CA  1 
ATOM   3448 C C   . ALA C 1 74  ? 18.105  38.850  16.924  1.00 22.58 ? 74   ALA B C   1 
ATOM   3449 O O   . ALA C 1 74  ? 18.452  39.883  16.358  1.00 23.16 ? 74   ALA B O   1 
ATOM   3450 C CB  . ALA C 1 74  ? 20.014  37.316  16.440  1.00 22.34 ? 74   ALA B CB  1 
ATOM   3451 N N   . TRP C 1 75  ? 17.382  38.844  18.038  1.00 22.50 ? 75   TRP B N   1 
ATOM   3452 C CA  . TRP C 1 75  ? 17.045  40.088  18.734  1.00 22.36 ? 75   TRP B CA  1 
ATOM   3453 C C   . TRP C 1 75  ? 18.286  40.871  19.114  1.00 22.37 ? 75   TRP B C   1 
ATOM   3454 O O   . TRP C 1 75  ? 18.196  41.896  19.766  1.00 22.13 ? 75   TRP B O   1 
ATOM   3455 C CB  . TRP C 1 75  ? 16.256  39.802  19.993  1.00 22.33 ? 75   TRP B CB  1 
ATOM   3456 C CG  . TRP C 1 75  ? 15.187  38.820  19.807  1.00 22.17 ? 75   TRP B CG  1 
ATOM   3457 C CD1 . TRP C 1 75  ? 15.304  37.469  19.904  1.00 23.04 ? 75   TRP B CD1 1 
ATOM   3458 C CD2 . TRP C 1 75  ? 13.818  39.090  19.506  1.00 21.15 ? 75   TRP B CD2 1 
ATOM   3459 N NE1 . TRP C 1 75  ? 14.088  36.878  19.685  1.00 23.64 ? 75   TRP B NE1 1 
ATOM   3460 C CE2 . TRP C 1 75  ? 13.158  37.856  19.438  1.00 22.68 ? 75   TRP B CE2 1 
ATOM   3461 C CE3 . TRP C 1 75  ? 13.086  40.253  19.296  1.00 21.30 ? 75   TRP B CE3 1 
ATOM   3462 C CZ2 . TRP C 1 75  ? 11.790  37.751  19.163  1.00 23.27 ? 75   TRP B CZ2 1 
ATOM   3463 C CZ3 . TRP C 1 75  ? 11.731  40.152  19.018  1.00 21.70 ? 75   TRP B CZ3 1 
ATOM   3464 C CH2 . TRP C 1 75  ? 11.099  38.911  18.954  1.00 22.89 ? 75   TRP B CH2 1 
ATOM   3465 N N   . ASN C 1 76  ? 19.438  40.373  18.699  1.00 22.68 ? 76   ASN B N   1 
ATOM   3466 C CA  . ASN C 1 76  ? 20.676  41.017  18.985  1.00 23.58 ? 76   ASN B CA  1 
ATOM   3467 C C   . ASN C 1 76  ? 21.408  41.403  17.698  1.00 24.05 ? 76   ASN B C   1 
ATOM   3468 O O   . ASN C 1 76  ? 22.490  42.022  17.714  1.00 24.15 ? 76   ASN B O   1 
ATOM   3469 C CB  . ASN C 1 76  ? 21.499  40.123  19.901  1.00 23.74 ? 76   ASN B CB  1 
ATOM   3470 C CG  . ASN C 1 76  ? 22.208  39.037  19.163  1.00 25.05 ? 76   ASN B CG  1 
ATOM   3471 O OD1 . ASN C 1 76  ? 23.313  39.236  18.649  1.00 26.59 ? 76   ASN B OD1 1 
ATOM   3472 N ND2 . ASN C 1 76  ? 21.601  37.863  19.123  1.00 26.65 ? 76   ASN B ND2 1 
ATOM   3473 N N   . ALA C 1 77  ? 20.783  41.060  16.579  1.00 24.72 ? 77   ALA B N   1 
ATOM   3474 C CA  . ALA C 1 77  ? 21.267  41.449  15.260  1.00 25.30 ? 77   ALA B CA  1 
ATOM   3475 C C   . ALA C 1 77  ? 21.123  42.954  15.060  1.00 25.76 ? 77   ALA B C   1 
ATOM   3476 O O   . ALA C 1 77  ? 20.093  43.539  15.414  1.00 25.43 ? 77   ALA B O   1 
ATOM   3477 C CB  . ALA C 1 77  ? 20.513  40.698  14.187  1.00 25.64 ? 77   ALA B CB  1 
ATOM   3478 N N   . PRO C 1 78  ? 22.155  43.586  14.475  1.00 26.28 ? 78   PRO B N   1 
ATOM   3479 C CA  . PRO C 1 78  ? 22.226  45.046  14.431  1.00 26.80 ? 78   PRO B CA  1 
ATOM   3480 C C   . PRO C 1 78  ? 20.962  45.690  13.866  1.00 27.52 ? 78   PRO B C   1 
ATOM   3481 O O   . PRO C 1 78  ? 20.447  46.643  14.462  1.00 27.47 ? 78   PRO B O   1 
ATOM   3482 C CB  . PRO C 1 78  ? 23.446  45.323  13.537  1.00 26.58 ? 78   PRO B CB  1 
ATOM   3483 C CG  . PRO C 1 78  ? 23.665  44.060  12.785  1.00 26.35 ? 78   PRO B CG  1 
ATOM   3484 C CD  . PRO C 1 78  ? 23.245  42.963  13.706  1.00 26.18 ? 78   PRO B CD  1 
ATOM   3485 N N   . ALA C 1 79  ? 20.454  45.165  12.746  1.00 28.41 ? 79   ALA B N   1 
ATOM   3486 C CA  . ALA C 1 79  ? 19.277  45.758  12.103  1.00 29.12 ? 79   ALA B CA  1 
ATOM   3487 C C   . ALA C 1 79  ? 18.028  45.599  12.980  1.00 29.67 ? 79   ALA B C   1 
ATOM   3488 O O   . ALA C 1 79  ? 16.981  46.210  12.716  1.00 29.53 ? 79   ALA B O   1 
ATOM   3489 C CB  . ALA C 1 79  ? 19.064  45.184  10.730  1.00 28.94 ? 79   ALA B CB  1 
ATOM   3490 N N   . VAL C 1 80  ? 18.164  44.795  14.038  1.00 30.25 ? 80   VAL B N   1 
ATOM   3491 C CA  . VAL C 1 80  ? 17.131  44.674  15.069  1.00 30.62 ? 80   VAL B CA  1 
ATOM   3492 C C   . VAL C 1 80  ? 17.413  45.623  16.226  1.00 30.95 ? 80   VAL B C   1 
ATOM   3493 O O   . VAL C 1 80  ? 16.495  46.154  16.859  1.00 30.78 ? 80   VAL B O   1 
ATOM   3494 C CB  . VAL C 1 80  ? 17.042  43.251  15.617  1.00 30.41 ? 80   VAL B CB  1 
ATOM   3495 C CG1 . VAL C 1 80  ? 15.748  43.068  16.429  1.00 29.55 ? 80   VAL B CG1 1 
ATOM   3496 C CG2 . VAL C 1 80  ? 17.131  42.263  14.479  1.00 30.45 ? 80   VAL B CG2 1 
ATOM   3497 N N   . LEU C 1 81  ? 18.689  45.841  16.500  1.00 31.46 ? 81   LEU B N   1 
ATOM   3498 C CA  . LEU C 1 81  ? 19.039  46.704  17.601  1.00 32.36 ? 81   LEU B CA  1 
ATOM   3499 C C   . LEU C 1 81  ? 18.298  48.041  17.546  1.00 32.90 ? 81   LEU B C   1 
ATOM   3500 O O   . LEU C 1 81  ? 17.951  48.568  18.598  1.00 33.21 ? 81   LEU B O   1 
ATOM   3501 C CB  . LEU C 1 81  ? 20.562  46.875  17.724  1.00 32.43 ? 81   LEU B CB  1 
ATOM   3502 C CG  . LEU C 1 81  ? 21.296  45.674  18.352  1.00 33.42 ? 81   LEU B CG  1 
ATOM   3503 C CD1 . LEU C 1 81  ? 22.808  45.688  18.110  1.00 33.37 ? 81   LEU B CD1 1 
ATOM   3504 C CD2 . LEU C 1 81  ? 20.990  45.551  19.857  1.00 34.12 ? 81   LEU B CD2 1 
ATOM   3505 N N   . GLN C 1 82  ? 18.017  48.568  16.342  1.00 33.60 ? 82   GLN B N   1 
ATOM   3506 C CA  . GLN C 1 82  ? 17.393  49.914  16.186  1.00 34.02 ? 82   GLN B CA  1 
ATOM   3507 C C   . GLN C 1 82  ? 15.865  49.949  16.294  1.00 34.22 ? 82   GLN B C   1 
ATOM   3508 O O   . GLN C 1 82  ? 15.258  51.026  16.362  1.00 34.12 ? 82   GLN B O   1 
ATOM   3509 C CB  . GLN C 1 82  ? 17.808  50.554  14.873  1.00 33.97 ? 82   GLN B CB  1 
ATOM   3510 C CG  . GLN C 1 82  ? 19.277  50.848  14.777  1.00 35.17 ? 82   GLN B CG  1 
ATOM   3511 C CD  . GLN C 1 82  ? 19.779  50.733  13.350  1.00 37.45 ? 82   GLN B CD  1 
ATOM   3512 O OE1 . GLN C 1 82  ? 19.718  49.651  12.744  1.00 38.74 ? 82   GLN B OE1 1 
ATOM   3513 N NE2 . GLN C 1 82  ? 20.285  51.844  12.801  1.00 36.42 ? 82   GLN B NE2 1 
ATOM   3514 N N   . LYS C 1 83  ? 15.263  48.761  16.296  1.00 34.44 ? 83   LYS B N   1 
ATOM   3515 C CA  . LYS C 1 83  ? 13.829  48.585  16.467  1.00 34.51 ? 83   LYS B CA  1 
ATOM   3516 C C   . LYS C 1 83  ? 13.486  48.741  17.949  1.00 34.89 ? 83   LYS B C   1 
ATOM   3517 O O   . LYS C 1 83  ? 14.390  48.725  18.784  1.00 34.78 ? 83   LYS B O   1 
ATOM   3518 C CB  . LYS C 1 83  ? 13.441  47.188  15.984  1.00 34.40 ? 83   LYS B CB  1 
ATOM   3519 C CG  . LYS C 1 83  ? 13.892  46.854  14.570  1.00 33.97 ? 83   LYS B CG  1 
ATOM   3520 C CD  . LYS C 1 83  ? 12.872  47.324  13.537  1.00 33.60 ? 83   LYS B CD  1 
ATOM   3521 C CE  . LYS C 1 83  ? 13.344  47.033  12.130  1.00 32.64 ? 83   LYS B CE  1 
ATOM   3522 N NZ  . LYS C 1 83  ? 12.280  47.313  11.154  1.00 32.27 ? 83   LYS B NZ  1 
ATOM   3523 N N   . PRO C 1 84  ? 12.184  48.886  18.288  1.00 35.25 ? 84   PRO B N   1 
ATOM   3524 C CA  . PRO C 1 84  ? 11.758  49.006  19.691  1.00 35.58 ? 84   PRO B CA  1 
ATOM   3525 C C   . PRO C 1 84  ? 12.179  47.886  20.670  1.00 36.01 ? 84   PRO B C   1 
ATOM   3526 O O   . PRO C 1 84  ? 12.148  48.103  21.885  1.00 36.18 ? 84   PRO B O   1 
ATOM   3527 C CB  . PRO C 1 84  ? 10.231  49.071  19.584  1.00 35.34 ? 84   PRO B CB  1 
ATOM   3528 C CG  . PRO C 1 84  ? 9.986   49.702  18.291  1.00 35.33 ? 84   PRO B CG  1 
ATOM   3529 C CD  . PRO C 1 84  ? 11.072  49.196  17.369  1.00 35.30 ? 84   PRO B CD  1 
ATOM   3530 N N   . TYR C 1 85  ? 12.575  46.714  20.172  1.00 36.53 ? 85   TYR B N   1 
ATOM   3531 C CA  . TYR C 1 85  ? 12.813  45.560  21.061  1.00 36.95 ? 85   TYR B CA  1 
ATOM   3532 C C   . TYR C 1 85  ? 14.080  44.780  20.749  1.00 37.02 ? 85   TYR B C   1 
ATOM   3533 O O   . TYR C 1 85  ? 14.200  44.178  19.685  1.00 37.25 ? 85   TYR B O   1 
ATOM   3534 C CB  . TYR C 1 85  ? 11.597  44.622  21.055  1.00 36.95 ? 85   TYR B CB  1 
ATOM   3535 C CG  . TYR C 1 85  ? 10.321  45.277  21.561  1.00 37.67 ? 85   TYR B CG  1 
ATOM   3536 C CD1 . TYR C 1 85  ? 10.089  45.439  22.933  1.00 37.92 ? 85   TYR B CD1 1 
ATOM   3537 C CD2 . TYR C 1 85  ? 9.354   45.748  20.674  1.00 37.58 ? 85   TYR B CD2 1 
ATOM   3538 C CE1 . TYR C 1 85  ? 8.930   46.038  23.400  1.00 37.08 ? 85   TYR B CE1 1 
ATOM   3539 C CE2 . TYR C 1 85  ? 8.198   46.351  21.136  1.00 37.02 ? 85   TYR B CE2 1 
ATOM   3540 C CZ  . TYR C 1 85  ? 7.992   46.485  22.497  1.00 37.02 ? 85   TYR B CZ  1 
ATOM   3541 O OH  . TYR C 1 85  ? 6.846   47.077  22.961  1.00 37.77 ? 85   TYR B OH  1 
ATOM   3542 N N   . ASN C 1 86  ? 15.029  44.795  21.678  1.00 37.15 ? 86   ASN B N   1 
ATOM   3543 C CA  . ASN C 1 86  ? 16.310  44.130  21.455  1.00 37.39 ? 86   ASN B CA  1 
ATOM   3544 C C   . ASN C 1 86  ? 16.733  43.246  22.598  1.00 37.38 ? 86   ASN B C   1 
ATOM   3545 O O   . ASN C 1 86  ? 16.014  43.071  23.569  1.00 37.58 ? 86   ASN B O   1 
ATOM   3546 C CB  . ASN C 1 86  ? 17.433  45.144  21.236  1.00 37.27 ? 86   ASN B CB  1 
ATOM   3547 C CG  . ASN C 1 86  ? 16.940  46.451  20.713  1.00 37.84 ? 86   ASN B CG  1 
ATOM   3548 O OD1 . ASN C 1 86  ? 16.112  46.507  19.793  1.00 37.57 ? 86   ASN B OD1 1 
ATOM   3549 N ND2 . ASN C 1 86  ? 17.451  47.534  21.293  1.00 39.01 ? 86   ASN B ND2 1 
ATOM   3550 N N   . ALA C 1 87  ? 17.919  42.679  22.451  1.00 37.43 ? 87   ALA B N   1 
ATOM   3551 C CA  . ALA C 1 87  ? 18.647  42.150  23.570  1.00 37.49 ? 87   ALA B CA  1 
ATOM   3552 C C   . ALA C 1 87  ? 19.157  43.342  24.382  1.00 37.42 ? 87   ALA B C   1 
ATOM   3553 O O   . ALA C 1 87  ? 18.804  43.470  25.553  1.00 37.84 ? 87   ALA B O   1 
ATOM   3554 C CB  . ALA C 1 87  ? 19.791  41.273  23.098  1.00 37.82 ? 87   ALA B CB  1 
ATOM   3555 N N   . HIS C 1 88  ? 19.943  44.227  23.758  1.00 37.09 ? 88   HIS B N   1 
ATOM   3556 C CA  . HIS C 1 88  ? 20.462  45.444  24.423  1.00 36.81 ? 88   HIS B CA  1 
ATOM   3557 C C   . HIS C 1 88  ? 19.346  46.355  24.958  1.00 36.65 ? 88   HIS B C   1 
ATOM   3558 O O   . HIS C 1 88  ? 19.607  47.457  25.425  1.00 36.52 ? 88   HIS B O   1 
ATOM   3559 C CB  . HIS C 1 88  ? 21.369  46.235  23.481  1.00 36.74 ? 88   HIS B CB  1 
ATOM   3560 C CG  . HIS C 1 88  ? 22.522  45.449  22.939  1.00 36.76 ? 88   HIS B CG  1 
ATOM   3561 N ND1 . HIS C 1 88  ? 23.561  46.037  22.253  1.00 36.64 ? 88   HIS B ND1 1 
ATOM   3562 C CD2 . HIS C 1 88  ? 22.797  44.123  22.971  1.00 36.72 ? 88   HIS B CD2 1 
ATOM   3563 C CE1 . HIS C 1 88  ? 24.432  45.112  21.894  1.00 36.72 ? 88   HIS B CE1 1 
ATOM   3564 N NE2 . HIS C 1 88  ? 23.990  43.941  22.315  1.00 37.04 ? 88   HIS B NE2 1 
ATOM   3565 N N   . ARG C 1 89  ? 18.104  45.884  24.855  1.00 36.61 ? 89   ARG B N   1 
ATOM   3566 C CA  . ARG C 1 89  ? 16.956  46.441  25.569  1.00 36.37 ? 89   ARG B CA  1 
ATOM   3567 C C   . ARG C 1 89  ? 17.171  46.363  27.081  1.00 36.14 ? 89   ARG B C   1 
ATOM   3568 O O   . ARG C 1 89  ? 17.881  45.473  27.569  1.00 35.81 ? 89   ARG B O   1 
ATOM   3569 C CB  . ARG C 1 89  ? 15.703  45.638  25.219  1.00 36.46 ? 89   ARG B CB  1 
ATOM   3570 C CG  . ARG C 1 89  ? 14.829  46.219  24.135  1.00 36.57 ? 89   ARG B CG  1 
ATOM   3571 C CD  . ARG C 1 89  ? 13.837  47.205  24.697  1.00 37.48 ? 89   ARG B CD  1 
ATOM   3572 N NE  . ARG C 1 89  ? 13.360  46.812  26.021  1.00 38.23 ? 89   ARG B NE  1 
ATOM   3573 C CZ  . ARG C 1 89  ? 12.083  46.758  26.379  1.00 38.68 ? 89   ARG B CZ  1 
ATOM   3574 N NH1 . ARG C 1 89  ? 11.136  47.079  25.511  1.00 38.56 ? 89   ARG B NH1 1 
ATOM   3575 N NH2 . ARG C 1 89  ? 11.756  46.404  27.615  1.00 39.21 ? 89   ARG B NH2 1 
ATOM   3576 N N   . PRO C 1 90  ? 16.543  47.281  27.836  1.00 35.99 ? 90   PRO B N   1 
ATOM   3577 C CA  . PRO C 1 90  ? 16.765  47.268  29.276  1.00 35.78 ? 90   PRO B CA  1 
ATOM   3578 C C   . PRO C 1 90  ? 16.173  46.016  29.904  1.00 35.42 ? 90   PRO B C   1 
ATOM   3579 O O   . PRO C 1 90  ? 16.876  45.324  30.646  1.00 35.57 ? 90   PRO B O   1 
ATOM   3580 C CB  . PRO C 1 90  ? 16.048  48.536  29.769  1.00 35.75 ? 90   PRO B CB  1 
ATOM   3581 C CG  . PRO C 1 90  ? 15.006  48.804  28.729  1.00 36.41 ? 90   PRO B CG  1 
ATOM   3582 C CD  . PRO C 1 90  ? 15.638  48.371  27.426  1.00 36.17 ? 90   PRO B CD  1 
ATOM   3583 N N   . ASP C 1 91  ? 14.912  45.713  29.605  1.00 34.86 ? 91   ASP B N   1 
ATOM   3584 C CA  . ASP C 1 91  ? 14.282  44.531  30.192  1.00 34.64 ? 91   ASP B CA  1 
ATOM   3585 C C   . ASP C 1 91  ? 14.938  43.219  29.726  1.00 34.29 ? 91   ASP B C   1 
ATOM   3586 O O   . ASP C 1 91  ? 15.446  42.457  30.562  1.00 33.84 ? 91   ASP B O   1 
ATOM   3587 C CB  . ASP C 1 91  ? 12.771  44.509  29.917  1.00 34.74 ? 91   ASP B CB  1 
ATOM   3588 C CG  . ASP C 1 91  ? 12.112  43.155  30.277  1.00 35.23 ? 91   ASP B CG  1 
ATOM   3589 O OD1 . ASP C 1 91  ? 12.692  42.057  30.022  1.00 33.07 ? 91   ASP B OD1 1 
ATOM   3590 O OD2 . ASP C 1 91  ? 10.975  43.208  30.803  1.00 36.20 ? 91   ASP B OD2 1 
ATOM   3591 N N   . ALA C 1 92  ? 14.921  42.990  28.402  1.00 33.67 ? 92   ALA B N   1 
ATOM   3592 C CA  . ALA C 1 92  ? 15.304  41.721  27.773  1.00 32.90 ? 92   ALA B CA  1 
ATOM   3593 C C   . ALA C 1 92  ? 14.887  40.563  28.657  1.00 32.39 ? 92   ALA B C   1 
ATOM   3594 O O   . ALA C 1 92  ? 13.737  40.171  28.641  1.00 32.19 ? 92   ALA B O   1 
ATOM   3595 C CB  . ALA C 1 92  ? 16.797  41.680  27.461  1.00 32.76 ? 92   ALA B CB  1 
ATOM   3596 N N   . ILE C 1 93  ? 15.829  40.067  29.454  1.00 32.13 ? 93   ILE B N   1 
ATOM   3597 C CA  . ILE C 1 93  ? 15.616  39.015  30.478  1.00 31.58 ? 93   ILE B CA  1 
ATOM   3598 C C   . ILE C 1 93  ? 14.173  38.729  30.921  1.00 31.29 ? 93   ILE B C   1 
ATOM   3599 O O   . ILE C 1 93  ? 13.685  37.617  30.727  1.00 31.23 ? 93   ILE B O   1 
ATOM   3600 C CB  . ILE C 1 93  ? 16.550  39.174  31.743  1.00 31.35 ? 93   ILE B CB  1 
ATOM   3601 C CG1 . ILE C 1 93  ? 17.009  40.642  31.962  1.00 30.83 ? 93   ILE B CG1 1 
ATOM   3602 C CG2 . ILE C 1 93  ? 17.718  38.175  31.669  1.00 30.87 ? 93   ILE B CG2 1 
ATOM   3603 C CD1 . ILE C 1 93  ? 18.209  41.147  31.087  1.00 29.09 ? 93   ILE B CD1 1 
ATOM   3604 N N   . SER C 1 94  ? 13.483  39.711  31.494  1.00 30.83 ? 94   SER B N   1 
ATOM   3605 C CA  . SER C 1 94  ? 12.140  39.423  31.990  1.00 30.50 ? 94   SER B CA  1 
ATOM   3606 C C   . SER C 1 94  ? 11.103  39.430  30.856  1.00 29.93 ? 94   SER B C   1 
ATOM   3607 O O   . SER C 1 94  ? 10.005  38.905  31.007  1.00 29.90 ? 94   SER B O   1 
ATOM   3608 C CB  . SER C 1 94  ? 11.763  40.302  33.193  1.00 30.71 ? 94   SER B CB  1 
ATOM   3609 O OG  . SER C 1 94  ? 10.994  41.428  32.817  1.00 31.73 ? 94   SER B OG  1 
ATOM   3610 N N   . LEU C 1 95  ? 11.468  39.988  29.705  1.00 29.40 ? 95   LEU B N   1 
ATOM   3611 C CA  . LEU C 1 95  ? 10.770  39.646  28.457  1.00 28.70 ? 95   LEU B CA  1 
ATOM   3612 C C   . LEU C 1 95  ? 11.170  38.220  28.055  1.00 28.52 ? 95   LEU B C   1 
ATOM   3613 O O   . LEU C 1 95  ? 10.884  37.270  28.790  1.00 28.89 ? 95   LEU B O   1 
ATOM   3614 C CB  . LEU C 1 95  ? 11.106  40.636  27.353  1.00 28.18 ? 95   LEU B CB  1 
ATOM   3615 C CG  . LEU C 1 95  ? 10.383  41.957  27.510  1.00 27.78 ? 95   LEU B CG  1 
ATOM   3616 C CD1 . LEU C 1 95  ? 10.883  42.931  26.478  1.00 28.21 ? 95   LEU B CD1 1 
ATOM   3617 C CD2 . LEU C 1 95  ? 8.872   41.788  27.420  1.00 27.14 ? 95   LEU B CD2 1 
ATOM   3618 N N   . GLY C 1 96  ? 11.846  38.065  26.921  1.00 27.62 ? 96   GLY B N   1 
ATOM   3619 C CA  . GLY C 1 96  ? 12.401  36.778  26.569  1.00 26.84 ? 96   GLY B CA  1 
ATOM   3620 C C   . GLY C 1 96  ? 13.499  36.923  25.541  1.00 26.56 ? 96   GLY B C   1 
ATOM   3621 O O   . GLY C 1 96  ? 14.020  35.934  25.014  1.00 27.20 ? 96   GLY B O   1 
ATOM   3622 N N   . LEU C 1 97  ? 13.883  38.153  25.262  1.00 25.56 ? 97   LEU B N   1 
ATOM   3623 C CA  . LEU C 1 97  ? 14.720  38.395  24.117  1.00 24.80 ? 97   LEU B CA  1 
ATOM   3624 C C   . LEU C 1 97  ? 16.176  38.377  24.487  1.00 24.71 ? 97   LEU B C   1 
ATOM   3625 O O   . LEU C 1 97  ? 16.608  39.139  25.350  1.00 24.85 ? 97   LEU B O   1 
ATOM   3626 C CB  . LEU C 1 97  ? 14.355  39.737  23.526  1.00 24.80 ? 97   LEU B CB  1 
ATOM   3627 C CG  . LEU C 1 97  ? 12.942  40.201  23.841  1.00 23.91 ? 97   LEU B CG  1 
ATOM   3628 C CD1 . LEU C 1 97  ? 12.935  41.703  23.702  1.00 23.16 ? 97   LEU B CD1 1 
ATOM   3629 C CD2 . LEU C 1 97  ? 11.883  39.513  22.952  1.00 22.78 ? 97   LEU B CD2 1 
ATOM   3630 N N   . GLY C 1 98  ? 16.937  37.525  23.816  1.00 24.65 ? 98   GLY B N   1 
ATOM   3631 C CA  . GLY C 1 98  ? 18.360  37.352  24.131  1.00 25.48 ? 98   GLY B CA  1 
ATOM   3632 C C   . GLY C 1 98  ? 19.239  37.133  22.919  1.00 25.72 ? 98   GLY B C   1 
ATOM   3633 O O   . GLY C 1 98  ? 18.884  37.567  21.833  1.00 26.22 ? 98   GLY B O   1 
ATOM   3634 N N   . LYS C 1 99  ? 20.382  36.472  23.101  1.00 25.77 ? 99   LYS B N   1 
ATOM   3635 C CA  . LYS C 1 99  ? 21.288  36.172  21.987  1.00 26.43 ? 99   LYS B CA  1 
ATOM   3636 C C   . LYS C 1 99  ? 20.748  35.046  21.082  1.00 27.00 ? 99   LYS B C   1 
ATOM   3637 O O   . LYS C 1 99  ? 21.463  34.090  20.755  1.00 27.98 ? 99   LYS B O   1 
ATOM   3638 C CB  . LYS C 1 99  ? 22.704  35.815  22.486  1.00 26.31 ? 99   LYS B CB  1 
ATOM   3639 C CG  . LYS C 1 99  ? 23.747  36.934  22.418  1.00 26.50 ? 99   LYS B CG  1 
ATOM   3640 C CD  . LYS C 1 99  ? 24.974  36.575  23.287  1.00 26.77 ? 99   LYS B CD  1 
ATOM   3641 C CE  . LYS C 1 99  ? 26.114  37.617  23.215  1.00 26.16 ? 99   LYS B CE  1 
ATOM   3642 N NZ  . LYS C 1 99  ? 25.909  38.788  24.107  1.00 25.61 ? 99   LYS B NZ  1 
ATOM   3643 N N   . HIS C 1 100 ? 19.509  35.159  20.641  1.00 26.80 ? 100  HIS B N   1 
ATOM   3644 C CA  . HIS C 1 100 ? 18.926  34.080  19.901  1.00 26.98 ? 100  HIS B CA  1 
ATOM   3645 C C   . HIS C 1 100 ? 17.973  34.597  18.820  1.00 27.45 ? 100  HIS B C   1 
ATOM   3646 O O   . HIS C 1 100 ? 17.851  35.796  18.635  1.00 27.55 ? 100  HIS B O   1 
ATOM   3647 C CB  . HIS C 1 100 ? 18.196  33.202  20.912  1.00 26.95 ? 100  HIS B CB  1 
ATOM   3648 C CG  . HIS C 1 100 ? 16.996  33.855  21.508  1.00 26.35 ? 100  HIS B CG  1 
ATOM   3649 N ND1 . HIS C 1 100 ? 17.073  34.704  22.584  1.00 26.88 ? 100  HIS B ND1 1 
ATOM   3650 C CD2 . HIS C 1 100 ? 15.691  33.817  21.154  1.00 26.33 ? 100  HIS B CD2 1 
ATOM   3651 C CE1 . HIS C 1 100 ? 15.862  35.130  22.895  1.00 26.87 ? 100  HIS B CE1 1 
ATOM   3652 N NE2 . HIS C 1 100 ? 15.004  34.609  22.039  1.00 25.57 ? 100  HIS B NE2 1 
ATOM   3653 N N   . ASN C 1 101 ? 17.280  33.707  18.113  1.00 28.01 ? 101  ASN B N   1 
ATOM   3654 C CA  . ASN C 1 101 ? 16.211  34.148  17.201  1.00 28.53 ? 101  ASN B CA  1 
ATOM   3655 C C   . ASN C 1 101 ? 14.946  33.309  17.302  1.00 28.93 ? 101  ASN B C   1 
ATOM   3656 O O   . ASN C 1 101 ? 14.467  32.743  16.314  1.00 28.96 ? 101  ASN B O   1 
ATOM   3657 C CB  . ASN C 1 101 ? 16.686  34.224  15.743  1.00 28.49 ? 101  ASN B CB  1 
ATOM   3658 C CG  . ASN C 1 101 ? 17.048  32.879  15.189  1.00 27.71 ? 101  ASN B CG  1 
ATOM   3659 O OD1 . ASN C 1 101 ? 17.525  32.026  15.924  1.00 29.17 ? 101  ASN B OD1 1 
ATOM   3660 N ND2 . ASN C 1 101 ? 16.824  32.672  13.899  1.00 26.46 ? 101  ASN B ND2 1 
ATOM   3661 N N   . TYR C 1 102 ? 14.418  33.235  18.511  1.00 29.37 ? 102  TYR B N   1 
ATOM   3662 C CA  . TYR C 1 102 ? 13.156  32.570  18.757  1.00 29.89 ? 102  TYR B CA  1 
ATOM   3663 C C   . TYR C 1 102 ? 12.076  33.595  19.046  1.00 30.63 ? 102  TYR B C   1 
ATOM   3664 O O   . TYR C 1 102 ? 12.258  34.529  19.828  1.00 30.94 ? 102  TYR B O   1 
ATOM   3665 C CB  . TYR C 1 102 ? 13.280  31.601  19.922  1.00 29.38 ? 102  TYR B CB  1 
ATOM   3666 C CG  . TYR C 1 102 ? 14.565  30.826  19.925  1.00 29.35 ? 102  TYR B CG  1 
ATOM   3667 C CD1 . TYR C 1 102 ? 14.923  30.051  18.835  1.00 29.65 ? 102  TYR B CD1 1 
ATOM   3668 C CD2 . TYR C 1 102 ? 15.417  30.842  21.035  1.00 29.31 ? 102  TYR B CD2 1 
ATOM   3669 C CE1 . TYR C 1 102 ? 16.081  29.319  18.843  1.00 29.46 ? 102  TYR B CE1 1 
ATOM   3670 C CE2 . TYR C 1 102 ? 16.580  30.115  21.053  1.00 28.23 ? 102  TYR B CE2 1 
ATOM   3671 C CZ  . TYR C 1 102 ? 16.901  29.360  19.946  1.00 29.19 ? 102  TYR B CZ  1 
ATOM   3672 O OH  . TYR C 1 102 ? 18.050  28.636  19.908  1.00 31.01 ? 102  TYR B OH  1 
ATOM   3673 N N   . CYS C 1 103 ? 10.936  33.408  18.422  1.00 31.58 ? 103  CYS B N   1 
ATOM   3674 C CA  . CYS C 1 103 ? 9.866   34.371  18.532  1.00 33.21 ? 103  CYS B CA  1 
ATOM   3675 C C   . CYS C 1 103 ? 9.314   34.484  19.936  1.00 32.93 ? 103  CYS B C   1 
ATOM   3676 O O   . CYS C 1 103 ? 9.336   33.531  20.714  1.00 32.84 ? 103  CYS B O   1 
ATOM   3677 C CB  . CYS C 1 103 ? 8.754   33.991  17.580  1.00 33.85 ? 103  CYS B CB  1 
ATOM   3678 S SG  . CYS C 1 103 ? 8.833   32.244  17.298  1.00 38.36 ? 103  CYS B SG  1 
ATOM   3679 N N   . ARG C 1 104 ? 8.822   35.680  20.232  1.00 32.78 ? 104  ARG B N   1 
ATOM   3680 C CA  . ARG C 1 104 ? 8.239   36.006  21.501  1.00 32.48 ? 104  ARG B CA  1 
ATOM   3681 C C   . ARG C 1 104 ? 7.146   37.022  21.215  1.00 32.08 ? 104  ARG B C   1 
ATOM   3682 O O   . ARG C 1 104 ? 7.215   37.764  20.238  1.00 31.85 ? 104  ARG B O   1 
ATOM   3683 C CB  . ARG C 1 104 ? 9.292   36.638  22.417  1.00 32.82 ? 104  ARG B CB  1 
ATOM   3684 C CG  . ARG C 1 104 ? 10.625  35.892  22.528  1.00 33.59 ? 104  ARG B CG  1 
ATOM   3685 C CD  . ARG C 1 104 ? 10.655  34.959  23.737  1.00 34.87 ? 104  ARG B CD  1 
ATOM   3686 N NE  . ARG C 1 104 ? 11.850  34.113  23.753  1.00 35.62 ? 104  ARG B NE  1 
ATOM   3687 C CZ  . ARG C 1 104 ? 11.893  32.863  23.294  1.00 36.53 ? 104  ARG B CZ  1 
ATOM   3688 N NH1 . ARG C 1 104 ? 10.818  32.286  22.775  1.00 37.16 ? 104  ARG B NH1 1 
ATOM   3689 N NH2 . ARG C 1 104 ? 13.014  32.178  23.351  1.00 36.97 ? 104  ARG B NH2 1 
ATOM   3690 N N   . ASN C 1 105 ? 6.140   37.036  22.082  1.00 31.82 ? 105  ASN B N   1 
ATOM   3691 C CA  . ASN C 1 105 ? 5.042   37.997  22.076  1.00 31.28 ? 105  ASN B CA  1 
ATOM   3692 C C   . ASN C 1 105 ? 5.248   38.925  23.273  1.00 31.05 ? 105  ASN B C   1 
ATOM   3693 O O   . ASN C 1 105 ? 4.456   38.908  24.212  1.00 30.70 ? 105  ASN B O   1 
ATOM   3694 C CB  . ASN C 1 105 ? 3.710   37.219  22.173  1.00 31.26 ? 105  ASN B CB  1 
ATOM   3695 C CG  . ASN C 1 105 ? 2.462   38.115  22.262  1.00 31.26 ? 105  ASN B CG  1 
ATOM   3696 O OD1 . ASN C 1 105 ? 2.522   39.340  22.124  1.00 31.63 ? 105  ASN B OD1 1 
ATOM   3697 N ND2 . ASN C 1 105 ? 1.317   37.482  22.495  1.00 29.98 ? 105  ASN B ND2 1 
ATOM   3698 N N   . PRO C 1 106 ? 6.331   39.731  23.254  1.00 31.18 ? 106  PRO B N   1 
ATOM   3699 C CA  . PRO C 1 106 ? 6.642   40.582  24.407  1.00 31.36 ? 106  PRO B CA  1 
ATOM   3700 C C   . PRO C 1 106 ? 5.796   41.846  24.405  1.00 31.45 ? 106  PRO B C   1 
ATOM   3701 O O   . PRO C 1 106 ? 5.559   42.447  25.458  1.00 31.40 ? 106  PRO B O   1 
ATOM   3702 C CB  . PRO C 1 106 ? 8.100   40.969  24.154  1.00 31.42 ? 106  PRO B CB  1 
ATOM   3703 C CG  . PRO C 1 106 ? 8.197   41.072  22.677  1.00 31.29 ? 106  PRO B CG  1 
ATOM   3704 C CD  . PRO C 1 106 ? 7.241   40.012  22.125  1.00 31.19 ? 106  PRO B CD  1 
ATOM   3705 N N   . ASP C 1 107 ? 5.325   42.193  23.203  1.00 31.52 ? 107  ASP B N   1 
ATOM   3706 C CA  . ASP C 1 107 ? 4.821   43.511  22.843  1.00 31.07 ? 107  ASP B CA  1 
ATOM   3707 C C   . ASP C 1 107 ? 3.331   43.669  23.073  1.00 30.43 ? 107  ASP B C   1 
ATOM   3708 O O   . ASP C 1 107 ? 2.684   44.479  22.423  1.00 30.17 ? 107  ASP B O   1 
ATOM   3709 C CB  . ASP C 1 107 ? 5.147   43.769  21.371  1.00 31.16 ? 107  ASP B CB  1 
ATOM   3710 C CG  . ASP C 1 107 ? 5.193   45.238  21.037  1.00 31.55 ? 107  ASP B CG  1 
ATOM   3711 O OD1 . ASP C 1 107 ? 4.821   46.069  21.897  1.00 32.01 ? 107  ASP B OD1 1 
ATOM   3712 O OD2 . ASP C 1 107 ? 5.613   45.563  19.908  1.00 31.66 ? 107  ASP B OD2 1 
ATOM   3713 N N   . ASN C 1 108 ? 2.799   42.897  24.011  1.00 30.16 ? 108  ASN B N   1 
ATOM   3714 C CA  . ASN C 1 108 ? 1.395   42.986  24.405  1.00 30.28 ? 108  ASN B CA  1 
ATOM   3715 C C   . ASN C 1 108 ? 0.450   42.765  23.201  1.00 29.95 ? 108  ASN B C   1 
ATOM   3716 O O   . ASN C 1 108 ? -0.539  43.475  23.008  1.00 29.48 ? 108  ASN B O   1 
ATOM   3717 C CB  . ASN C 1 108 ? 1.112   44.328  25.115  1.00 30.68 ? 108  ASN B CB  1 
ATOM   3718 C CG  . ASN C 1 108 ? 2.377   44.983  25.740  1.00 31.38 ? 108  ASN B CG  1 
ATOM   3719 O OD1 . ASN C 1 108 ? 3.471   44.399  25.783  1.00 31.14 ? 108  ASN B OD1 1 
ATOM   3720 N ND2 . ASN C 1 108 ? 2.207   46.218  26.222  1.00 31.63 ? 108  ASN B ND2 1 
ATOM   3721 N N   . GLN C 1 109 ? 0.775   41.751  22.406  1.00 29.85 ? 109  GLN B N   1 
ATOM   3722 C CA  . GLN C 1 109 ? 0.166   41.538  21.106  1.00 29.55 ? 109  GLN B CA  1 
ATOM   3723 C C   . GLN C 1 109 ? -0.502  40.184  21.030  1.00 29.44 ? 109  GLN B C   1 
ATOM   3724 O O   . GLN C 1 109 ? -0.455  39.415  21.977  1.00 29.66 ? 109  GLN B O   1 
ATOM   3725 C CB  . GLN C 1 109 ? 1.252   41.593  20.050  1.00 29.69 ? 109  GLN B CB  1 
ATOM   3726 C CG  . GLN C 1 109 ? 0.794   42.050  18.695  1.00 29.53 ? 109  GLN B CG  1 
ATOM   3727 C CD  . GLN C 1 109 ? 1.893   41.911  17.676  1.00 29.51 ? 109  GLN B CD  1 
ATOM   3728 O OE1 . GLN C 1 109 ? 2.378   40.805  17.412  1.00 29.17 ? 109  GLN B OE1 1 
ATOM   3729 N NE2 . GLN C 1 109 ? 2.308   43.034  17.103  1.00 28.96 ? 109  GLN B NE2 1 
ATOM   3730 N N   . LYS C 1 110 ? -1.086  39.895  19.873  1.00 29.34 ? 110  LYS B N   1 
ATOM   3731 C CA  . LYS C 1 110 ? -1.961  38.741  19.667  1.00 29.12 ? 110  LYS B CA  1 
ATOM   3732 C C   . LYS C 1 110 ? -1.282  37.386  19.800  1.00 29.18 ? 110  LYS B C   1 
ATOM   3733 O O   . LYS C 1 110 ? -1.895  36.450  20.306  1.00 29.25 ? 110  LYS B O   1 
ATOM   3734 C CB  . LYS C 1 110 ? -2.654  38.838  18.298  1.00 29.06 ? 110  LYS B CB  1 
ATOM   3735 C CG  . LYS C 1 110 ? -4.100  39.282  18.342  1.00 27.95 ? 110  LYS B CG  1 
ATOM   3736 C CD  . LYS C 1 110 ? -4.985  38.150  18.825  1.00 27.13 ? 110  LYS B CD  1 
ATOM   3737 C CE  . LYS C 1 110 ? -6.437  38.415  18.514  1.00 26.55 ? 110  LYS B CE  1 
ATOM   3738 N NZ  . LYS C 1 110 ? -7.227  37.174  18.677  1.00 26.63 ? 110  LYS B NZ  1 
ATOM   3739 N N   . ARG C 1 111 ? -0.035  37.283  19.341  1.00 29.22 ? 111  ARG B N   1 
ATOM   3740 C CA  . ARG C 1 111 ? 0.716   36.022  19.380  1.00 29.50 ? 111  ARG B CA  1 
ATOM   3741 C C   . ARG C 1 111 ? 2.186   36.201  18.958  1.00 29.54 ? 111  ARG B C   1 
ATOM   3742 O O   . ARG C 1 111 ? 2.486   37.073  18.139  1.00 29.57 ? 111  ARG B O   1 
ATOM   3743 C CB  . ARG C 1 111 ? 0.045   34.992  18.478  1.00 29.59 ? 111  ARG B CB  1 
ATOM   3744 C CG  . ARG C 1 111 ? -0.023  35.405  17.027  1.00 30.33 ? 111  ARG B CG  1 
ATOM   3745 C CD  . ARG C 1 111 ? 0.328   34.233  16.131  1.00 31.73 ? 111  ARG B CD  1 
ATOM   3746 N NE  . ARG C 1 111 ? -0.830  33.382  15.861  1.00 32.47 ? 111  ARG B NE  1 
ATOM   3747 C CZ  . ARG C 1 111 ? -0.759  32.122  15.433  1.00 32.74 ? 111  ARG B CZ  1 
ATOM   3748 N NH1 . ARG C 1 111 ? 0.420   31.533  15.233  1.00 32.63 ? 111  ARG B NH1 1 
ATOM   3749 N NH2 . ARG C 1 111 ? -1.877  31.442  15.216  1.00 32.79 ? 111  ARG B NH2 1 
ATOM   3750 N N   . PRO C 1 112 ? 3.102   35.351  19.471  1.00 29.67 ? 112  PRO B N   1 
ATOM   3751 C CA  . PRO C 1 112 ? 4.522   35.637  19.240  1.00 29.91 ? 112  PRO B CA  1 
ATOM   3752 C C   . PRO C 1 112 ? 4.845   35.848  17.773  1.00 29.86 ? 112  PRO B C   1 
ATOM   3753 O O   . PRO C 1 112 ? 4.174   35.326  16.886  1.00 30.07 ? 112  PRO B O   1 
ATOM   3754 C CB  . PRO C 1 112 ? 5.258   34.397  19.788  1.00 29.75 ? 112  PRO B CB  1 
ATOM   3755 C CG  . PRO C 1 112 ? 4.262   33.328  19.763  1.00 30.17 ? 112  PRO B CG  1 
ATOM   3756 C CD  . PRO C 1 112 ? 2.910   33.989  19.996  1.00 30.05 ? 112  PRO B CD  1 
ATOM   3757 N N   . TRP C 1 113 ? 5.898   36.605  17.544  1.00 29.55 ? 113  TRP B N   1 
ATOM   3758 C CA  . TRP C 1 113 ? 6.178   37.151  16.264  1.00 29.16 ? 113  TRP B CA  1 
ATOM   3759 C C   . TRP C 1 113 ? 7.617   37.530  16.372  1.00 29.16 ? 113  TRP B C   1 
ATOM   3760 O O   . TRP C 1 113 ? 8.160   37.578  17.474  1.00 29.34 ? 113  TRP B O   1 
ATOM   3761 C CB  . TRP C 1 113 ? 5.355   38.410  16.111  1.00 29.28 ? 113  TRP B CB  1 
ATOM   3762 C CG  . TRP C 1 113 ? 5.554   39.353  17.253  1.00 29.46 ? 113  TRP B CG  1 
ATOM   3763 C CD1 . TRP C 1 113 ? 4.747   39.510  18.349  1.00 29.64 ? 113  TRP B CD1 1 
ATOM   3764 C CD2 . TRP C 1 113 ? 6.640   40.260  17.423  1.00 29.02 ? 113  TRP B CD2 1 
ATOM   3765 N NE1 . TRP C 1 113 ? 5.260   40.476  19.181  1.00 29.12 ? 113  TRP B NE1 1 
ATOM   3766 C CE2 . TRP C 1 113 ? 6.427   40.945  18.637  1.00 29.19 ? 113  TRP B CE2 1 
ATOM   3767 C CE3 . TRP C 1 113 ? 7.768   40.572  16.658  1.00 28.71 ? 113  TRP B CE3 1 
ATOM   3768 C CZ2 . TRP C 1 113 ? 7.307   41.915  19.104  1.00 29.79 ? 113  TRP B CZ2 1 
ATOM   3769 C CZ3 . TRP C 1 113 ? 8.645   41.525  17.125  1.00 29.13 ? 113  TRP B CZ3 1 
ATOM   3770 C CH2 . TRP C 1 113 ? 8.411   42.188  18.336  1.00 29.87 ? 113  TRP B CH2 1 
ATOM   3771 N N   . CYS C 1 114 ? 8.244   37.810  15.244  1.00 28.95 ? 114  CYS B N   1 
ATOM   3772 C CA  . CYS C 1 114 ? 9.655   38.146  15.246  1.00 28.94 ? 114  CYS B CA  1 
ATOM   3773 C C   . CYS C 1 114 ? 9.861   39.044  14.066  1.00 28.47 ? 114  CYS B C   1 
ATOM   3774 O O   . CYS C 1 114 ? 9.018   39.106  13.182  1.00 28.09 ? 114  CYS B O   1 
ATOM   3775 C CB  . CYS C 1 114 ? 10.525  36.889  15.123  1.00 28.87 ? 114  CYS B CB  1 
ATOM   3776 S SG  . CYS C 1 114 ? 10.200  35.990  13.562  1.00 31.29 ? 114  CYS B SG  1 
ATOM   3777 N N   . TYR C 1 115 ? 10.979  39.749  14.067  1.00 28.64 ? 115  TYR B N   1 
ATOM   3778 C CA  . TYR C 1 115 ? 11.358  40.551  12.935  1.00 29.17 ? 115  TYR B CA  1 
ATOM   3779 C C   . TYR C 1 115 ? 11.868  39.631  11.837  1.00 29.99 ? 115  TYR B C   1 
ATOM   3780 O O   . TYR C 1 115 ? 12.633  38.682  12.098  1.00 30.34 ? 115  TYR B O   1 
ATOM   3781 C CB  . TYR C 1 115 ? 12.401  41.574  13.335  1.00 28.77 ? 115  TYR B CB  1 
ATOM   3782 C CG  . TYR C 1 115 ? 11.904  42.513  14.407  1.00 28.86 ? 115  TYR B CG  1 
ATOM   3783 C CD1 . TYR C 1 115 ? 11.006  43.547  14.106  1.00 29.00 ? 115  TYR B CD1 1 
ATOM   3784 C CD2 . TYR C 1 115 ? 12.313  42.362  15.729  1.00 28.04 ? 115  TYR B CD2 1 
ATOM   3785 C CE1 . TYR C 1 115 ? 10.544  44.408  15.103  1.00 28.40 ? 115  TYR B CE1 1 
ATOM   3786 C CE2 . TYR C 1 115 ? 11.866  43.210  16.721  1.00 27.62 ? 115  TYR B CE2 1 
ATOM   3787 C CZ  . TYR C 1 115 ? 10.984  44.228  16.408  1.00 28.06 ? 115  TYR B CZ  1 
ATOM   3788 O OH  . TYR C 1 115 ? 10.558  45.066  17.409  1.00 27.78 ? 115  TYR B OH  1 
ATOM   3789 N N   . VAL C 1 116 ? 11.398  39.895  10.615  1.00 30.46 ? 116  VAL B N   1 
ATOM   3790 C CA  . VAL C 1 116 ? 11.726  39.076  9.452   1.00 30.34 ? 116  VAL B CA  1 
ATOM   3791 C C   . VAL C 1 116 ? 12.301  39.956  8.381   1.00 30.51 ? 116  VAL B C   1 
ATOM   3792 O O   . VAL C 1 116 ? 11.922  41.128  8.285   1.00 30.52 ? 116  VAL B O   1 
ATOM   3793 C CB  . VAL C 1 116 ? 10.510  38.362  8.909   1.00 30.15 ? 116  VAL B CB  1 
ATOM   3794 C CG1 . VAL C 1 116 ? 10.900  37.563  7.697   1.00 29.73 ? 116  VAL B CG1 1 
ATOM   3795 C CG2 . VAL C 1 116 ? 9.956   37.439  9.970   1.00 30.55 ? 116  VAL B CG2 1 
ATOM   3796 N N   . GLN C 1 117 ? 13.214  39.387  7.587   1.00 30.62 ? 117  GLN B N   1 
ATOM   3797 C CA  . GLN C 1 117 ? 13.995  40.158  6.625   1.00 30.93 ? 117  GLN B CA  1 
ATOM   3798 C C   . GLN C 1 117 ? 13.353  40.212  5.244   1.00 31.14 ? 117  GLN B C   1 
ATOM   3799 O O   . GLN C 1 117 ? 13.879  39.585  4.316   1.00 32.05 ? 117  GLN B O   1 
ATOM   3800 C CB  . GLN C 1 117 ? 15.405  39.573  6.492   1.00 30.77 ? 117  GLN B CB  1 
ATOM   3801 C CG  . GLN C 1 117 ? 16.307  40.357  5.543   1.00 31.59 ? 117  GLN B CG  1 
ATOM   3802 C CD  . GLN C 1 117 ? 16.206  41.857  5.776   1.00 33.76 ? 117  GLN B CD  1 
ATOM   3803 O OE1 . GLN C 1 117 ? 16.630  42.364  6.823   1.00 36.05 ? 117  GLN B OE1 1 
ATOM   3804 N NE2 . GLN C 1 117 ? 15.632  42.572  4.814   1.00 32.56 ? 117  GLN B NE2 1 
ATOM   3805 N N   . ILE C 1 118 ? 12.245  40.947  5.075   1.00 30.47 ? 118  ILE B N   1 
ATOM   3806 C CA  . ILE C 1 118 ? 11.556  40.928  3.770   1.00 29.44 ? 118  ILE B CA  1 
ATOM   3807 C C   . ILE C 1 118 ? 12.242  41.799  2.703   1.00 29.14 ? 118  ILE B C   1 
ATOM   3808 O O   . ILE C 1 118 ? 11.848  42.936  2.424   1.00 28.63 ? 118  ILE B O   1 
ATOM   3809 C CB  . ILE C 1 118 ? 9.975   40.973  3.857   1.00 29.31 ? 118  ILE B CB  1 
ATOM   3810 C CG1 . ILE C 1 118 ? 9.350   41.628  2.607   1.00 30.26 ? 118  ILE B CG1 1 
ATOM   3811 C CG2 . ILE C 1 118 ? 9.498   41.594  5.143   1.00 27.99 ? 118  ILE B CG2 1 
ATOM   3812 C CD1 . ILE C 1 118 ? 8.038   40.953  2.072   1.00 30.16 ? 118  ILE B CD1 1 
ATOM   3813 N N   . GLY C 1 119 ? 13.315  41.239  2.151   1.00 28.89 ? 119  GLY B N   1 
ATOM   3814 C CA  . GLY C 1 119 ? 14.113  41.888  1.120   1.00 29.01 ? 119  GLY B CA  1 
ATOM   3815 C C   . GLY C 1 119 ? 14.995  43.053  1.549   1.00 28.91 ? 119  GLY B C   1 
ATOM   3816 O O   . GLY C 1 119 ? 16.231  42.941  1.521   1.00 28.90 ? 119  GLY B O   1 
ATOM   3817 N N   . LEU C 1 120 ? 14.370  44.175  1.920   1.00 28.61 ? 120  LEU B N   1 
ATOM   3818 C CA  . LEU C 1 120 ? 15.110  45.405  2.219   1.00 28.45 ? 120  LEU B CA  1 
ATOM   3819 C C   . LEU C 1 120 ? 14.652  46.190  3.450   1.00 28.31 ? 120  LEU B C   1 
ATOM   3820 O O   . LEU C 1 120 ? 15.297  47.155  3.843   1.00 28.03 ? 120  LEU B O   1 
ATOM   3821 C CB  . LEU C 1 120 ? 15.134  46.319  0.999   1.00 28.68 ? 120  LEU B CB  1 
ATOM   3822 C CG  . LEU C 1 120 ? 16.166  45.978  -0.077  1.00 29.12 ? 120  LEU B CG  1 
ATOM   3823 C CD1 . LEU C 1 120 ? 15.998  46.923  -1.270  1.00 29.30 ? 120  LEU B CD1 1 
ATOM   3824 C CD2 . LEU C 1 120 ? 17.605  45.997  0.465   1.00 28.63 ? 120  LEU B CD2 1 
ATOM   3825 N N   . ARG C 1 121 ? 13.538  45.778  4.044   1.00 28.36 ? 121  ARG B N   1 
ATOM   3826 C CA  . ARG C 1 121 ? 13.123  46.270  5.353   1.00 28.20 ? 121  ARG B CA  1 
ATOM   3827 C C   . ARG C 1 121 ? 12.870  45.111  6.316   1.00 28.11 ? 121  ARG B C   1 
ATOM   3828 O O   . ARG C 1 121 ? 13.103  43.947  5.979   1.00 27.71 ? 121  ARG B O   1 
ATOM   3829 C CB  . ARG C 1 121 ? 11.883  47.147  5.220   1.00 28.23 ? 121  ARG B CB  1 
ATOM   3830 C CG  . ARG C 1 121 ? 12.160  48.636  5.163   1.00 28.47 ? 121  ARG B CG  1 
ATOM   3831 C CD  . ARG C 1 121 ? 10.866  49.425  5.196   1.00 28.44 ? 121  ARG B CD  1 
ATOM   3832 N NE  . ARG C 1 121 ? 10.234  49.435  3.878   1.00 29.70 ? 121  ARG B NE  1 
ATOM   3833 C CZ  . ARG C 1 121 ? 8.936   49.631  3.653   1.00 29.89 ? 121  ARG B CZ  1 
ATOM   3834 N NH1 . ARG C 1 121 ? 8.103   49.817  4.669   1.00 29.87 ? 121  ARG B NH1 1 
ATOM   3835 N NH2 . ARG C 1 121 ? 8.469   49.637  2.405   1.00 29.73 ? 121  ARG B NH2 1 
ATOM   3836 N N   . GLN C 1 122 ? 12.419  45.430  7.522   1.00 28.53 ? 122  GLN B N   1 
ATOM   3837 C CA  . GLN C 1 122 ? 12.151  44.397  8.525   1.00 29.28 ? 122  GLN B CA  1 
ATOM   3838 C C   . GLN C 1 122 ? 10.779  44.550  9.118   1.00 29.56 ? 122  GLN B C   1 
ATOM   3839 O O   . GLN C 1 122 ? 10.537  45.454  9.906   1.00 29.80 ? 122  GLN B O   1 
ATOM   3840 C CB  . GLN C 1 122 ? 13.170  44.419  9.666   1.00 29.16 ? 122  GLN B CB  1 
ATOM   3841 C CG  . GLN C 1 122 ? 14.577  44.097  9.273   1.00 29.70 ? 122  GLN B CG  1 
ATOM   3842 C CD  . GLN C 1 122 ? 15.237  45.289  8.681   1.00 31.18 ? 122  GLN B CD  1 
ATOM   3843 O OE1 . GLN C 1 122 ? 15.743  45.240  7.561   1.00 32.58 ? 122  GLN B OE1 1 
ATOM   3844 N NE2 . GLN C 1 122 ? 15.188  46.401  9.402   1.00 32.09 ? 122  GLN B NE2 1 
ATOM   3845 N N   . PHE C 1 123 ? 9.885   43.652  8.754   1.00 29.98 ? 123  PHE B N   1 
ATOM   3846 C CA  . PHE C 1 123 ? 8.536   43.706  9.261   1.00 30.57 ? 123  PHE B CA  1 
ATOM   3847 C C   . PHE C 1 123 ? 8.390   42.706  10.389  1.00 31.17 ? 123  PHE B C   1 
ATOM   3848 O O   . PHE C 1 123 ? 9.202   41.785  10.550  1.00 31.21 ? 123  PHE B O   1 
ATOM   3849 C CB  . PHE C 1 123 ? 7.535   43.380  8.161   1.00 30.46 ? 123  PHE B CB  1 
ATOM   3850 C CG  . PHE C 1 123 ? 7.705   44.200  6.926   1.00 30.71 ? 123  PHE B CG  1 
ATOM   3851 C CD1 . PHE C 1 123 ? 8.939   44.291  6.295   1.00 30.44 ? 123  PHE B CD1 1 
ATOM   3852 C CD2 . PHE C 1 123 ? 6.618   44.866  6.375   1.00 31.64 ? 123  PHE B CD2 1 
ATOM   3853 C CE1 . PHE C 1 123 ? 9.094   45.041  5.156   1.00 31.28 ? 123  PHE B CE1 1 
ATOM   3854 C CE2 . PHE C 1 123 ? 6.758   45.631  5.231   1.00 31.63 ? 123  PHE B CE2 1 
ATOM   3855 C CZ  . PHE C 1 123 ? 8.002   45.722  4.617   1.00 31.94 ? 123  PHE B CZ  1 
ATOM   3856 N N   . VAL C 1 124 ? 7.332   42.905  11.157  1.00 31.74 ? 124  VAL B N   1 
ATOM   3857 C CA  . VAL C 1 124 ? 6.968   42.027  12.235  1.00 32.42 ? 124  VAL B CA  1 
ATOM   3858 C C   . VAL C 1 124 ? 6.135   40.900  11.664  1.00 32.96 ? 124  VAL B C   1 
ATOM   3859 O O   . VAL C 1 124 ? 5.002   41.111  11.257  1.00 33.12 ? 124  VAL B O   1 
ATOM   3860 C CB  . VAL C 1 124 ? 6.212   42.825  13.327  1.00 32.31 ? 124  VAL B CB  1 
ATOM   3861 C CG1 . VAL C 1 124 ? 5.177   41.978  14.073  1.00 32.21 ? 124  VAL B CG1 1 
ATOM   3862 C CG2 . VAL C 1 124 ? 7.215   43.430  14.291  1.00 32.84 ? 124  VAL B CG2 1 
ATOM   3863 N N   . GLN C 1 125 ? 6.705   39.704  11.615  1.00 33.91 ? 125  GLN B N   1 
ATOM   3864 C CA  . GLN C 1 125 ? 5.954   38.546  11.153  1.00 35.13 ? 125  GLN B CA  1 
ATOM   3865 C C   . GLN C 1 125 ? 5.509   37.642  12.301  1.00 35.79 ? 125  GLN B C   1 
ATOM   3866 O O   . GLN C 1 125 ? 6.190   37.560  13.323  1.00 35.92 ? 125  GLN B O   1 
ATOM   3867 C CB  . GLN C 1 125 ? 6.767   37.755  10.128  1.00 35.22 ? 125  GLN B CB  1 
ATOM   3868 C CG  . GLN C 1 125 ? 6.964   38.462  8.791   1.00 35.75 ? 125  GLN B CG  1 
ATOM   3869 C CD  . GLN C 1 125 ? 5.668   38.648  8.022   1.00 36.92 ? 125  GLN B CD  1 
ATOM   3870 O OE1 . GLN C 1 125 ? 5.044   37.680  7.575   1.00 37.59 ? 125  GLN B OE1 1 
ATOM   3871 N NE2 . GLN C 1 125 ? 5.257   39.904  7.860   1.00 37.04 ? 125  GLN B NE2 1 
ATOM   3872 N N   . GLU C 1 126 ? 4.364   36.981  12.126  1.00 36.75 ? 126  GLU B N   1 
ATOM   3873 C CA  . GLU C 1 126 ? 3.875   35.994  13.084  1.00 37.89 ? 126  GLU B CA  1 
ATOM   3874 C C   . GLU C 1 126 ? 4.644   34.713  12.924  1.00 38.57 ? 126  GLU B C   1 
ATOM   3875 O O   . GLU C 1 126 ? 5.028   34.350  11.814  1.00 38.27 ? 126  GLU B O   1 
ATOM   3876 C CB  . GLU C 1 126 ? 2.399   35.700  12.888  1.00 37.88 ? 126  GLU B CB  1 
ATOM   3877 C CG  . GLU C 1 126 ? 1.481   36.642  13.614  1.00 39.26 ? 126  GLU B CG  1 
ATOM   3878 C CD  . GLU C 1 126 ? 0.038   36.463  13.183  1.00 42.32 ? 126  GLU B CD  1 
ATOM   3879 O OE1 . GLU C 1 126 ? -0.225  36.379  11.954  1.00 43.56 ? 126  GLU B OE1 1 
ATOM   3880 O OE2 . GLU C 1 126 ? -0.845  36.407  14.069  1.00 43.65 ? 126  GLU B OE2 1 
ATOM   3881 N N   . CYS C 1 127 ? 4.839   34.027  14.047  1.00 39.80 ? 127  CYS B N   1 
ATOM   3882 C CA  . CYS C 1 127 ? 5.754   32.903  14.126  1.00 41.10 ? 127  CYS B CA  1 
ATOM   3883 C C   . CYS C 1 127 ? 5.096   31.554  13.868  1.00 41.79 ? 127  CYS B C   1 
ATOM   3884 O O   . CYS C 1 127 ? 3.891   31.405  14.034  1.00 42.14 ? 127  CYS B O   1 
ATOM   3885 C CB  . CYS C 1 127 ? 6.450   32.893  15.480  1.00 40.91 ? 127  CYS B CB  1 
ATOM   3886 S SG  . CYS C 1 127 ? 8.028   31.987  15.430  1.00 43.03 ? 127  CYS B SG  1 
ATOM   3887 N N   . MET C 1 128 ? 5.912   30.585  13.454  1.00 42.85 ? 128  MET B N   1 
ATOM   3888 C CA  . MET C 1 128 ? 5.497   29.200  13.192  1.00 43.64 ? 128  MET B CA  1 
ATOM   3889 C C   . MET C 1 128 ? 4.592   28.667  14.315  1.00 43.92 ? 128  MET B C   1 
ATOM   3890 O O   . MET C 1 128 ? 3.378   28.826  14.235  1.00 43.71 ? 128  MET B O   1 
ATOM   3891 C CB  . MET C 1 128 ? 6.748   28.316  12.979  1.00 43.75 ? 128  MET B CB  1 
ATOM   3892 C CG  . MET C 1 128 ? 6.583   27.028  12.152  1.00 45.05 ? 128  MET B CG  1 
ATOM   3893 S SD  . MET C 1 128 ? 5.731   27.107  10.533  1.00 48.00 ? 128  MET B SD  1 
ATOM   3894 C CE  . MET C 1 128 ? 4.192   26.238  10.884  1.00 46.28 ? 128  MET B CE  1 
ATOM   3895 N N   . VAL C 1 129 ? 5.191   28.095  15.365  1.00 44.68 ? 129  VAL B N   1 
ATOM   3896 C CA  . VAL C 1 129 ? 4.478   27.376  16.462  1.00 45.43 ? 129  VAL B CA  1 
ATOM   3897 C C   . VAL C 1 129 ? 2.954   27.432  16.490  1.00 45.93 ? 129  VAL B C   1 
ATOM   3898 O O   . VAL C 1 129 ? 2.345   28.491  16.666  1.00 45.70 ? 129  VAL B O   1 
ATOM   3899 C CB  . VAL C 1 129 ? 5.016   27.701  17.910  1.00 45.44 ? 129  VAL B CB  1 
ATOM   3900 C CG1 . VAL C 1 129 ? 6.113   26.713  18.329  1.00 45.44 ? 129  VAL B CG1 1 
ATOM   3901 C CG2 . VAL C 1 129 ? 5.476   29.156  18.046  1.00 45.26 ? 129  VAL B CG2 1 
ATOM   3902 N N   . HIS C 1 130 ? 2.357   26.258  16.337  1.00 46.91 ? 130  HIS B N   1 
ATOM   3903 C CA  . HIS C 1 130 ? 0.916   26.097  16.415  1.00 48.09 ? 130  HIS B CA  1 
ATOM   3904 C C   . HIS C 1 130 ? 0.451   26.314  17.858  1.00 48.71 ? 130  HIS B C   1 
ATOM   3905 O O   . HIS C 1 130 ? 1.254   26.502  18.761  1.00 48.65 ? 130  HIS B O   1 
ATOM   3906 C CB  . HIS C 1 130 ? 0.503   24.705  15.888  1.00 48.22 ? 130  HIS B CB  1 
ATOM   3907 C CG  . HIS C 1 130 ? 0.557   24.560  14.385  1.00 48.69 ? 130  HIS B CG  1 
ATOM   3908 N ND1 . HIS C 1 130 ? -0.537  24.174  13.632  1.00 48.36 ? 130  HIS B ND1 1 
ATOM   3909 C CD2 . HIS C 1 130 ? 1.575   24.723  13.501  1.00 48.54 ? 130  HIS B CD2 1 
ATOM   3910 C CE1 . HIS C 1 130 ? -0.197  24.114  12.356  1.00 48.48 ? 130  HIS B CE1 1 
ATOM   3911 N NE2 . HIS C 1 130 ? 1.079   24.445  12.249  1.00 48.38 ? 130  HIS B NE2 1 
ATOM   3912 N N   . ASP C 1 131 ? -0.852  26.307  18.066  1.00 49.95 ? 131  ASP B N   1 
ATOM   3913 C CA  . ASP C 1 131 ? -1.400  26.479  19.391  1.00 51.33 ? 131  ASP B CA  1 
ATOM   3914 C C   . ASP C 1 131 ? -1.711  25.123  20.024  1.00 52.46 ? 131  ASP B C   1 
ATOM   3915 O O   . ASP C 1 131 ? -1.246  24.086  19.556  1.00 52.39 ? 131  ASP B O   1 
ATOM   3916 C CB  . ASP C 1 131 ? -2.672  27.319  19.304  1.00 51.30 ? 131  ASP B CB  1 
ATOM   3917 C CG  . ASP C 1 131 ? -3.071  27.912  20.636  1.00 51.15 ? 131  ASP B CG  1 
ATOM   3918 O OD1 . ASP C 1 131 ? -2.303  28.754  21.153  1.00 50.88 ? 131  ASP B OD1 1 
ATOM   3919 O OD2 . ASP C 1 131 ? -4.152  27.538  21.153  1.00 50.31 ? 131  ASP B OD2 1 
ATOM   3920 N N   . CYS C 1 132 ? -2.480  25.162  21.110  1.00 54.35 ? 132  CYS B N   1 
ATOM   3921 C CA  . CYS C 1 132 ? -3.047  23.987  21.762  1.00 55.79 ? 132  CYS B CA  1 
ATOM   3922 C C   . CYS C 1 132 ? -4.567  23.899  21.429  1.00 56.57 ? 132  CYS B C   1 
ATOM   3923 O O   . CYS C 1 132 ? -5.022  23.325  20.406  1.00 57.19 ? 132  CYS B O   1 
ATOM   3924 C CB  . CYS C 1 132 ? -2.853  24.120  23.267  1.00 55.51 ? 132  CYS B CB  1 
ATOM   3925 S SG  . CYS C 1 132 ? -1.140  24.487  23.941  1.00 58.09 ? 132  CYS B SG  1 
ATOM   3926 N N   . LEU D 2 1   ? 43.676  56.621  27.786  1.00 33.65 ? 1    LEU V N   1 
ATOM   3927 C CA  . LEU D 2 1   ? 43.426  55.562  26.759  1.00 33.64 ? 1    LEU V CA  1 
ATOM   3928 C C   . LEU D 2 1   ? 41.938  55.281  26.655  1.00 33.11 ? 1    LEU V C   1 
ATOM   3929 O O   . LEU D 2 1   ? 41.224  55.306  27.652  1.00 32.97 ? 1    LEU V O   1 
ATOM   3930 C CB  . LEU D 2 1   ? 44.154  54.262  27.156  1.00 34.12 ? 1    LEU V CB  1 
ATOM   3931 C CG  . LEU D 2 1   ? 44.734  53.188  26.202  1.00 34.25 ? 1    LEU V CG  1 
ATOM   3932 C CD1 . LEU D 2 1   ? 44.376  51.798  26.737  1.00 33.97 ? 1    LEU V CD1 1 
ATOM   3933 C CD2 . LEU D 2 1   ? 44.315  53.314  24.730  1.00 34.52 ? 1    LEU V CD2 1 
ATOM   3934 N N   . GLN D 2 2   ? 41.464  54.991  25.459  1.00 32.72 ? 2    GLN V N   1 
ATOM   3935 C CA  . GLN D 2 2   ? 40.057  54.705  25.326  1.00 33.04 ? 2    GLN V CA  1 
ATOM   3936 C C   . GLN D 2 2   ? 39.787  53.260  24.966  1.00 33.31 ? 2    GLN V C   1 
ATOM   3937 O O   . GLN D 2 2   ? 40.175  52.805  23.901  1.00 33.60 ? 2    GLN V O   1 
ATOM   3938 C CB  . GLN D 2 2   ? 39.423  55.640  24.319  1.00 32.84 ? 2    GLN V CB  1 
ATOM   3939 C CG  . GLN D 2 2   ? 39.586  57.077  24.697  1.00 33.52 ? 2    GLN V CG  1 
ATOM   3940 C CD  . GLN D 2 2   ? 38.341  57.877  24.435  1.00 34.24 ? 2    GLN V CD  1 
ATOM   3941 O OE1 . GLN D 2 2   ? 37.910  58.022  23.291  1.00 34.98 ? 2    GLN V OE1 1 
ATOM   3942 N NE2 . GLN D 2 2   ? 37.750  58.411  25.498  1.00 33.90 ? 2    GLN V NE2 1 
ATOM   3943 N N   . CYS D 2 3   ? 39.139  52.539  25.874  1.00 33.54 ? 3    CYS V N   1 
ATOM   3944 C CA  . CYS D 2 3   ? 38.719  51.175  25.621  1.00 34.11 ? 3    CYS V CA  1 
ATOM   3945 C C   . CYS D 2 3   ? 37.233  51.147  25.415  1.00 34.50 ? 3    CYS V C   1 
ATOM   3946 O O   . CYS D 2 3   ? 36.549  52.122  25.692  1.00 34.89 ? 3    CYS V O   1 
ATOM   3947 C CB  . CYS D 2 3   ? 39.083  50.259  26.778  1.00 33.69 ? 3    CYS V CB  1 
ATOM   3948 S SG  . CYS D 2 3   ? 40.828  49.718  26.811  1.00 35.64 ? 3    CYS V SG  1 
ATOM   3949 N N   . MET D 2 4   ? 36.723  50.028  24.932  1.00 34.98 ? 4    MET V N   1 
ATOM   3950 C CA  . MET D 2 4   ? 35.317  49.954  24.647  1.00 35.80 ? 4    MET V CA  1 
ATOM   3951 C C   . MET D 2 4   ? 34.693  49.140  25.718  1.00 35.92 ? 4    MET V C   1 
ATOM   3952 O O   . MET D 2 4   ? 34.614  47.944  25.583  1.00 37.00 ? 4    MET V O   1 
ATOM   3953 C CB  . MET D 2 4   ? 35.081  49.248  23.315  1.00 36.15 ? 4    MET V CB  1 
ATOM   3954 C CG  . MET D 2 4   ? 35.214  50.119  22.113  1.00 37.06 ? 4    MET V CG  1 
ATOM   3955 S SD  . MET D 2 4   ? 33.646  50.904  21.899  1.00 41.28 ? 4    MET V SD  1 
ATOM   3956 C CE  . MET D 2 4   ? 34.050  51.994  20.536  1.00 41.24 ? 4    MET V CE  1 
ATOM   3957 N N   . GLN D 2 5   ? 34.248  49.737  26.801  1.00 35.86 ? 5    GLN V N   1 
ATOM   3958 C CA  . GLN D 2 5   ? 33.602  48.890  27.787  1.00 35.87 ? 5    GLN V CA  1 
ATOM   3959 C C   . GLN D 2 5   ? 32.213  48.510  27.325  1.00 36.09 ? 5    GLN V C   1 
ATOM   3960 O O   . GLN D 2 5   ? 31.458  49.339  26.842  1.00 35.83 ? 5    GLN V O   1 
ATOM   3961 C CB  . GLN D 2 5   ? 33.567  49.511  29.189  1.00 35.68 ? 5    GLN V CB  1 
ATOM   3962 C CG  . GLN D 2 5   ? 32.836  48.647  30.207  1.00 34.63 ? 5    GLN V CG  1 
ATOM   3963 C CD  . GLN D 2 5   ? 31.363  48.941  30.232  1.00 33.97 ? 5    GLN V CD  1 
ATOM   3964 O OE1 . GLN D 2 5   ? 30.970  50.091  30.176  1.00 36.45 ? 5    GLN V OE1 1 
ATOM   3965 N NE2 . GLN D 2 5   ? 30.542  47.916  30.337  1.00 33.68 ? 5    GLN V NE2 1 
ATOM   3966 N N   . CYS D 2 6   ? 31.918  47.226  27.446  1.00 36.91 ? 6    CYS V N   1 
ATOM   3967 C CA  . CYS D 2 6   ? 30.553  46.721  27.409  1.00 38.08 ? 6    CYS V CA  1 
ATOM   3968 C C   . CYS D 2 6   ? 30.551  45.340  28.071  1.00 37.73 ? 6    CYS V C   1 
ATOM   3969 O O   . CYS D 2 6   ? 31.456  44.542  27.849  1.00 37.09 ? 6    CYS V O   1 
ATOM   3970 C CB  . CYS D 2 6   ? 29.949  46.739  25.990  1.00 37.98 ? 6    CYS V CB  1 
ATOM   3971 S SG  . CYS D 2 6   ? 30.818  45.754  24.670  1.00 42.94 ? 6    CYS V SG  1 
ATOM   3972 N N   . GLU D 2 7   ? 29.581  45.127  28.960  1.00 38.10 ? 7    GLU V N   1 
ATOM   3973 C CA  . GLU D 2 7   ? 29.301  43.824  29.530  1.00 38.80 ? 7    GLU V CA  1 
ATOM   3974 C C   . GLU D 2 7   ? 28.553  43.060  28.439  1.00 39.14 ? 7    GLU V C   1 
ATOM   3975 O O   . GLU D 2 7   ? 28.403  43.583  27.330  1.00 39.84 ? 7    GLU V O   1 
ATOM   3976 C CB  . GLU D 2 7   ? 28.439  43.974  30.776  1.00 38.89 ? 7    GLU V CB  1 
ATOM   3977 C CG  . GLU D 2 7   ? 28.556  42.847  31.770  1.00 40.70 ? 7    GLU V CG  1 
ATOM   3978 C CD  . GLU D 2 7   ? 29.990  42.629  32.208  1.00 43.52 ? 7    GLU V CD  1 
ATOM   3979 O OE1 . GLU D 2 7   ? 30.691  43.624  32.508  1.00 44.92 ? 7    GLU V OE1 1 
ATOM   3980 O OE2 . GLU D 2 7   ? 30.424  41.462  32.246  1.00 45.20 ? 7    GLU V OE2 1 
ATOM   3981 N N   . SER D 2 8   ? 28.088  41.842  28.713  1.00 38.78 ? 8    SER V N   1 
ATOM   3982 C CA  . SER D 2 8   ? 27.425  41.081  27.678  1.00 38.30 ? 8    SER V CA  1 
ATOM   3983 C C   . SER D 2 8   ? 26.025  41.587  27.440  1.00 38.31 ? 8    SER V C   1 
ATOM   3984 O O   . SER D 2 8   ? 25.349  42.060  28.353  1.00 37.83 ? 8    SER V O   1 
ATOM   3985 C CB  . SER D 2 8   ? 27.371  39.615  28.031  1.00 38.52 ? 8    SER V CB  1 
ATOM   3986 O OG  . SER D 2 8   ? 26.426  38.954  27.210  1.00 39.20 ? 8    SER V OG  1 
ATOM   3987 N N   . ASN D 2 9   ? 25.600  41.433  26.192  1.00 38.82 ? 9    ASN V N   1 
ATOM   3988 C CA  . ASN D 2 9   ? 24.319  41.947  25.676  1.00 39.53 ? 9    ASN V CA  1 
ATOM   3989 C C   . ASN D 2 9   ? 23.785  43.239  26.343  1.00 38.93 ? 9    ASN V C   1 
ATOM   3990 O O   . ASN D 2 9   ? 22.579  43.457  26.507  1.00 38.81 ? 9    ASN V O   1 
ATOM   3991 C CB  . ASN D 2 9   ? 23.261  40.826  25.463  1.00 40.13 ? 9    ASN V CB  1 
ATOM   3992 C CG  . ASN D 2 9   ? 22.562  40.395  26.757  1.00 42.36 ? 9    ASN V CG  1 
ATOM   3993 O OD1 . ASN D 2 9   ? 23.192  39.854  27.692  1.00 44.52 ? 9    ASN V OD1 1 
ATOM   3994 N ND2 . ASN D 2 9   ? 21.234  40.604  26.799  1.00 42.50 ? 9    ASN V ND2 1 
ATOM   3995 N N   . GLN D 2 10  ? 24.742  44.077  26.725  1.00 38.37 ? 10   GLN V N   1 
ATOM   3996 C CA  . GLN D 2 10  ? 24.555  45.512  26.834  1.00 37.67 ? 10   GLN V CA  1 
ATOM   3997 C C   . GLN D 2 10  ? 25.563  46.071  25.851  1.00 37.05 ? 10   GLN V C   1 
ATOM   3998 O O   . GLN D 2 10  ? 26.712  45.639  25.833  1.00 37.40 ? 10   GLN V O   1 
ATOM   3999 C CB  . GLN D 2 10  ? 24.791  46.030  28.273  1.00 37.84 ? 10   GLN V CB  1 
ATOM   4000 C CG  . GLN D 2 10  ? 26.075  45.612  28.940  1.00 37.91 ? 10   GLN V CG  1 
ATOM   4001 C CD  . GLN D 2 10  ? 26.755  46.740  29.684  1.00 40.82 ? 10   GLN V CD  1 
ATOM   4002 O OE1 . GLN D 2 10  ? 27.415  46.503  30.694  1.00 41.86 ? 10   GLN V OE1 1 
ATOM   4003 N NE2 . GLN D 2 10  ? 26.629  47.983  29.177  1.00 43.41 ? 10   GLN V NE2 1 
ATOM   4004 N N   . SER D 2 11  ? 25.144  46.995  25.003  1.00 36.16 ? 11   SER V N   1 
ATOM   4005 C CA  . SER D 2 11  ? 26.027  47.501  23.940  1.00 35.40 ? 11   SER V CA  1 
ATOM   4006 C C   . SER D 2 11  ? 27.288  48.167  24.452  1.00 34.25 ? 11   SER V C   1 
ATOM   4007 O O   . SER D 2 11  ? 27.303  48.702  25.537  1.00 34.87 ? 11   SER V O   1 
ATOM   4008 C CB  . SER D 2 11  ? 25.286  48.552  23.148  1.00 35.84 ? 11   SER V CB  1 
ATOM   4009 O OG  . SER D 2 11  ? 25.028  49.633  24.018  1.00 36.86 ? 11   SER V OG  1 
ATOM   4010 N N   . CYS D 2 12  ? 28.330  48.177  23.644  1.00 32.87 ? 12   CYS V N   1 
ATOM   4011 C CA  . CYS D 2 12  ? 29.555  48.851  24.002  1.00 32.31 ? 12   CYS V CA  1 
ATOM   4012 C C   . CYS D 2 12  ? 29.420  50.329  24.188  1.00 30.90 ? 12   CYS V C   1 
ATOM   4013 O O   . CYS D 2 12  ? 28.504  50.941  23.674  1.00 30.81 ? 12   CYS V O   1 
ATOM   4014 C CB  . CYS D 2 12  ? 30.616  48.614  22.964  1.00 32.31 ? 12   CYS V CB  1 
ATOM   4015 S SG  . CYS D 2 12  ? 31.399  46.977  22.990  1.00 38.68 ? 12   CYS V SG  1 
ATOM   4016 N N   . LEU D 2 13  ? 30.362  50.878  24.945  1.00 29.80 ? 13   LEU V N   1 
ATOM   4017 C CA  . LEU D 2 13  ? 30.488  52.295  25.224  1.00 28.51 ? 13   LEU V CA  1 
ATOM   4018 C C   . LEU D 2 13  ? 31.958  52.568  25.226  1.00 28.03 ? 13   LEU V C   1 
ATOM   4019 O O   . LEU D 2 13  ? 32.741  51.659  25.484  1.00 28.08 ? 13   LEU V O   1 
ATOM   4020 C CB  . LEU D 2 13  ? 29.946  52.596  26.608  1.00 28.21 ? 13   LEU V CB  1 
ATOM   4021 C CG  . LEU D 2 13  ? 28.615  53.331  26.761  1.00 27.93 ? 13   LEU V CG  1 
ATOM   4022 C CD1 . LEU D 2 13  ? 27.491  52.777  25.903  1.00 28.63 ? 13   LEU V CD1 1 
ATOM   4023 C CD2 . LEU D 2 13  ? 28.206  53.319  28.206  1.00 27.65 ? 13   LEU V CD2 1 
ATOM   4024 N N   . VAL D 2 14  ? 32.344  53.805  24.938  1.00 27.55 ? 14   VAL V N   1 
ATOM   4025 C CA  . VAL D 2 14  ? 33.746  54.187  24.980  1.00 27.47 ? 14   VAL V CA  1 
ATOM   4026 C C   . VAL D 2 14  ? 34.010  54.607  26.394  1.00 28.03 ? 14   VAL V C   1 
ATOM   4027 O O   . VAL D 2 14  ? 33.231  55.335  26.965  1.00 28.23 ? 14   VAL V O   1 
ATOM   4028 C CB  . VAL D 2 14  ? 34.055  55.345  24.040  1.00 27.12 ? 14   VAL V CB  1 
ATOM   4029 C CG1 . VAL D 2 14  ? 35.538  55.551  23.916  1.00 26.50 ? 14   VAL V CG1 1 
ATOM   4030 C CG2 . VAL D 2 14  ? 33.503  55.058  22.685  1.00 27.43 ? 14   VAL V CG2 1 
ATOM   4031 N N   . GLU D 2 15  ? 35.096  54.130  26.969  1.00 28.80 ? 15   GLU V N   1 
ATOM   4032 C CA  . GLU D 2 15  ? 35.396  54.382  28.354  1.00 30.23 ? 15   GLU V CA  1 
ATOM   4033 C C   . GLU D 2 15  ? 36.816  54.907  28.374  1.00 30.54 ? 15   GLU V C   1 
ATOM   4034 O O   . GLU D 2 15  ? 37.687  54.321  27.745  1.00 30.97 ? 15   GLU V O   1 
ATOM   4035 C CB  . GLU D 2 15  ? 35.253  53.063  29.138  1.00 30.91 ? 15   GLU V CB  1 
ATOM   4036 C CG  . GLU D 2 15  ? 36.111  52.877  30.427  1.00 34.68 ? 15   GLU V CG  1 
ATOM   4037 C CD  . GLU D 2 15  ? 36.130  51.411  30.957  1.00 40.18 ? 15   GLU V CD  1 
ATOM   4038 O OE1 . GLU D 2 15  ? 36.546  50.491  30.204  1.00 42.29 ? 15   GLU V OE1 1 
ATOM   4039 O OE2 . GLU D 2 15  ? 35.758  51.172  32.139  1.00 42.36 ? 15   GLU V OE2 1 
ATOM   4040 N N   . GLU D 2 16  ? 37.053  56.026  29.056  1.00 31.06 ? 16   GLU V N   1 
ATOM   4041 C CA  . GLU D 2 16  ? 38.422  56.499  29.284  1.00 31.31 ? 16   GLU V CA  1 
ATOM   4042 C C   . GLU D 2 16  ? 39.022  55.650  30.395  1.00 31.43 ? 16   GLU V C   1 
ATOM   4043 O O   . GLU D 2 16  ? 38.331  55.274  31.338  1.00 31.59 ? 16   GLU V O   1 
ATOM   4044 C CB  . GLU D 2 16  ? 38.427  57.972  29.684  1.00 31.31 ? 16   GLU V CB  1 
ATOM   4045 C CG  . GLU D 2 16  ? 39.353  58.867  28.850  1.00 32.20 ? 16   GLU V CG  1 
ATOM   4046 C CD  . GLU D 2 16  ? 40.823  58.811  29.267  1.00 34.07 ? 16   GLU V CD  1 
ATOM   4047 O OE1 . GLU D 2 16  ? 41.560  59.796  28.990  1.00 34.13 ? 16   GLU V OE1 1 
ATOM   4048 O OE2 . GLU D 2 16  ? 41.246  57.791  29.866  1.00 35.41 ? 16   GLU V OE2 1 
ATOM   4049 N N   . CYS D 2 17  ? 40.297  55.320  30.287  1.00 31.66 ? 17   CYS V N   1 
ATOM   4050 C CA  . CYS D 2 17  ? 40.885  54.473  31.298  1.00 32.12 ? 17   CYS V CA  1 
ATOM   4051 C C   . CYS D 2 17  ? 41.684  55.255  32.310  1.00 32.23 ? 17   CYS V C   1 
ATOM   4052 O O   . CYS D 2 17  ? 42.482  56.125  31.958  1.00 32.12 ? 17   CYS V O   1 
ATOM   4053 C CB  . CYS D 2 17  ? 41.778  53.400  30.684  1.00 32.28 ? 17   CYS V CB  1 
ATOM   4054 S SG  . CYS D 2 17  ? 41.093  52.405  29.347  1.00 33.49 ? 17   CYS V SG  1 
ATOM   4055 N N   . ALA D 2 18  ? 41.472  54.902  33.571  1.00 32.62 ? 18   ALA V N   1 
ATOM   4056 C CA  . ALA D 2 18  ? 42.270  55.386  34.685  1.00 33.48 ? 18   ALA V CA  1 
ATOM   4057 C C   . ALA D 2 18  ? 43.780  55.295  34.451  1.00 33.97 ? 18   ALA V C   1 
ATOM   4058 O O   . ALA D 2 18  ? 44.260  54.347  33.854  1.00 33.82 ? 18   ALA V O   1 
ATOM   4059 C CB  . ALA D 2 18  ? 41.909  54.596  35.930  1.00 33.52 ? 18   ALA V CB  1 
ATOM   4060 N N   . LEU D 2 19  ? 44.528  56.276  34.949  1.00 34.90 ? 19   LEU V N   1 
ATOM   4061 C CA  . LEU D 2 19  ? 45.976  56.132  35.066  1.00 35.72 ? 19   LEU V CA  1 
ATOM   4062 C C   . LEU D 2 19  ? 46.247  54.801  35.777  1.00 36.08 ? 19   LEU V C   1 
ATOM   4063 O O   . LEU D 2 19  ? 45.542  54.449  36.726  1.00 36.34 ? 19   LEU V O   1 
ATOM   4064 C CB  . LEU D 2 19  ? 46.579  57.319  35.841  1.00 35.84 ? 19   LEU V CB  1 
ATOM   4065 C CG  . LEU D 2 19  ? 46.686  57.336  37.380  1.00 36.42 ? 19   LEU V CG  1 
ATOM   4066 C CD1 . LEU D 2 19  ? 48.099  56.953  37.879  1.00 36.48 ? 19   LEU V CD1 1 
ATOM   4067 C CD2 . LEU D 2 19  ? 46.301  58.708  37.926  1.00 36.96 ? 19   LEU V CD2 1 
ATOM   4068 N N   . GLY D 2 20  ? 47.240  54.050  35.310  1.00 36.39 ? 20   GLY V N   1 
ATOM   4069 C CA  . GLY D 2 20  ? 47.552  52.753  35.921  1.00 36.91 ? 20   GLY V CA  1 
ATOM   4070 C C   . GLY D 2 20  ? 47.025  51.596  35.086  1.00 37.11 ? 20   GLY V C   1 
ATOM   4071 O O   . GLY D 2 20  ? 47.798  50.712  34.672  1.00 37.42 ? 20   GLY V O   1 
ATOM   4072 N N   . GLN D 2 21  ? 45.711  51.583  34.844  1.00 36.76 ? 21   GLN V N   1 
ATOM   4073 C CA  . GLN D 2 21  ? 45.183  50.816  33.707  1.00 36.36 ? 21   GLN V CA  1 
ATOM   4074 C C   . GLN D 2 21  ? 45.755  51.412  32.411  1.00 35.83 ? 21   GLN V C   1 
ATOM   4075 O O   . GLN D 2 21  ? 46.215  52.561  32.394  1.00 35.97 ? 21   GLN V O   1 
ATOM   4076 C CB  . GLN D 2 21  ? 43.652  50.818  33.676  1.00 36.30 ? 21   GLN V CB  1 
ATOM   4077 C CG  . GLN D 2 21  ? 43.023  49.572  34.259  1.00 36.23 ? 21   GLN V CG  1 
ATOM   4078 C CD  . GLN D 2 21  ? 41.635  49.804  34.833  1.00 37.24 ? 21   GLN V CD  1 
ATOM   4079 O OE1 . GLN D 2 21  ? 41.218  50.946  35.054  1.00 38.27 ? 21   GLN V OE1 1 
ATOM   4080 N NE2 . GLN D 2 21  ? 40.914  48.715  35.095  1.00 37.24 ? 21   GLN V NE2 1 
ATOM   4081 N N   . ASP D 2 22  ? 45.768  50.618  31.348  1.00 35.12 ? 22   ASP V N   1 
ATOM   4082 C CA  . ASP D 2 22  ? 46.212  51.083  30.038  1.00 34.60 ? 22   ASP V CA  1 
ATOM   4083 C C   . ASP D 2 22  ? 46.460  49.917  29.084  1.00 33.77 ? 22   ASP V C   1 
ATOM   4084 O O   . ASP D 2 22  ? 47.398  49.933  28.280  1.00 34.03 ? 22   ASP V O   1 
ATOM   4085 C CB  . ASP D 2 22  ? 47.429  52.044  30.118  1.00 34.98 ? 22   ASP V CB  1 
ATOM   4086 C CG  . ASP D 2 22  ? 48.658  51.411  30.777  1.00 35.96 ? 22   ASP V CG  1 
ATOM   4087 O OD1 . ASP D 2 22  ? 49.765  52.005  30.648  1.00 37.13 ? 22   ASP V OD1 1 
ATOM   4088 O OD2 . ASP D 2 22  ? 48.518  50.337  31.416  1.00 35.33 ? 22   ASP V OD2 1 
ATOM   4089 N N   . LEU D 2 23  ? 45.621  48.900  29.190  1.00 32.36 ? 23   LEU V N   1 
ATOM   4090 C CA  . LEU D 2 23  ? 45.463  47.981  28.091  1.00 31.39 ? 23   LEU V CA  1 
ATOM   4091 C C   . LEU D 2 23  ? 43.987  47.919  27.778  1.00 30.60 ? 23   LEU V C   1 
ATOM   4092 O O   . LEU D 2 23  ? 43.170  48.334  28.595  1.00 30.78 ? 23   LEU V O   1 
ATOM   4093 C CB  . LEU D 2 23  ? 46.003  46.607  28.449  1.00 31.43 ? 23   LEU V CB  1 
ATOM   4094 C CG  . LEU D 2 23  ? 47.518  46.427  28.541  1.00 32.06 ? 23   LEU V CG  1 
ATOM   4095 C CD1 . LEU D 2 23  ? 47.826  44.944  28.712  1.00 31.10 ? 23   LEU V CD1 1 
ATOM   4096 C CD2 . LEU D 2 23  ? 48.274  47.016  27.328  1.00 31.84 ? 23   LEU V CD2 1 
ATOM   4097 N N   . CYS D 2 24  ? 43.636  47.435  26.598  1.00 29.45 ? 24   CYS V N   1 
ATOM   4098 C CA  . CYS D 2 24  ? 42.244  47.195  26.294  1.00 28.93 ? 24   CYS V CA  1 
ATOM   4099 C C   . CYS D 2 24  ? 41.960  45.726  26.435  1.00 28.35 ? 24   CYS V C   1 
ATOM   4100 O O   . CYS D 2 24  ? 42.826  44.914  26.183  1.00 28.99 ? 24   CYS V O   1 
ATOM   4101 C CB  . CYS D 2 24  ? 41.936  47.668  24.892  1.00 29.17 ? 24   CYS V CB  1 
ATOM   4102 S SG  . CYS D 2 24  ? 41.467  49.367  24.875  1.00 30.86 ? 24   CYS V SG  1 
ATOM   4103 N N   . ARG D 2 25  ? 40.759  45.350  26.830  1.00 27.43 ? 25   ARG V N   1 
ATOM   4104 C CA  . ARG D 2 25  ? 40.507  43.931  27.046  1.00 26.73 ? 25   ARG V CA  1 
ATOM   4105 C C   . ARG D 2 25  ? 39.275  43.413  26.289  1.00 27.22 ? 25   ARG V C   1 
ATOM   4106 O O   . ARG D 2 25  ? 38.234  44.077  26.226  1.00 27.23 ? 25   ARG V O   1 
ATOM   4107 C CB  . ARG D 2 25  ? 40.424  43.641  28.561  1.00 26.31 ? 25   ARG V CB  1 
ATOM   4108 C CG  . ARG D 2 25  ? 39.598  42.434  28.961  1.00 23.53 ? 25   ARG V CG  1 
ATOM   4109 C CD  . ARG D 2 25  ? 39.357  42.358  30.450  1.00 19.21 ? 25   ARG V CD  1 
ATOM   4110 N NE  . ARG D 2 25  ? 38.140  43.014  30.969  1.00 15.57 ? 25   ARG V NE  1 
ATOM   4111 C CZ  . ARG D 2 25  ? 36.877  42.625  30.763  1.00 14.12 ? 25   ARG V CZ  1 
ATOM   4112 N NH1 . ARG D 2 25  ? 36.572  41.608  29.977  1.00 15.57 ? 25   ARG V NH1 1 
ATOM   4113 N NH2 . ARG D 2 25  ? 35.887  43.277  31.325  1.00 13.25 ? 25   ARG V NH2 1 
ATOM   4114 N N   . THR D 2 26  ? 39.407  42.226  25.709  1.00 27.32 ? 26   THR V N   1 
ATOM   4115 C CA  . THR D 2 26  ? 38.250  41.479  25.260  1.00 27.64 ? 26   THR V CA  1 
ATOM   4116 C C   . THR D 2 26  ? 38.317  40.149  25.958  1.00 27.52 ? 26   THR V C   1 
ATOM   4117 O O   . THR D 2 26  ? 39.317  39.450  25.836  1.00 27.47 ? 26   THR V O   1 
ATOM   4118 C CB  . THR D 2 26  ? 38.312  41.217  23.761  1.00 27.94 ? 26   THR V CB  1 
ATOM   4119 O OG1 . THR D 2 26  ? 38.866  42.362  23.093  1.00 29.76 ? 26   THR V OG1 1 
ATOM   4120 C CG2 . THR D 2 26  ? 36.934  40.911  23.209  1.00 27.40 ? 26   THR V CG2 1 
ATOM   4121 N N   . THR D 2 27  ? 37.277  39.812  26.709  1.00 27.49 ? 27   THR V N   1 
ATOM   4122 C CA  . THR D 2 27  ? 37.166  38.495  27.302  1.00 27.77 ? 27   THR V CA  1 
ATOM   4123 C C   . THR D 2 27  ? 35.950  37.806  26.720  1.00 28.53 ? 27   THR V C   1 
ATOM   4124 O O   . THR D 2 27  ? 34.818  38.249  26.918  1.00 28.71 ? 27   THR V O   1 
ATOM   4125 C CB  . THR D 2 27  ? 36.985  38.588  28.799  1.00 27.56 ? 27   THR V CB  1 
ATOM   4126 O OG1 . THR D 2 27  ? 38.171  39.114  29.374  1.00 28.74 ? 27   THR V OG1 1 
ATOM   4127 C CG2 . THR D 2 27  ? 36.768  37.249  29.390  1.00 27.33 ? 27   THR V CG2 1 
ATOM   4128 N N   . VAL D 2 28  ? 36.184  36.714  26.000  1.00 29.34 ? 28   VAL V N   1 
ATOM   4129 C CA  . VAL D 2 28  ? 35.099  35.908  25.446  1.00 29.52 ? 28   VAL V CA  1 
ATOM   4130 C C   . VAL D 2 28  ? 35.118  34.462  25.979  1.00 30.12 ? 28   VAL V C   1 
ATOM   4131 O O   . VAL D 2 28  ? 36.175  33.835  26.091  1.00 30.06 ? 28   VAL V O   1 
ATOM   4132 C CB  . VAL D 2 28  ? 35.157  35.932  23.914  1.00 29.29 ? 28   VAL V CB  1 
ATOM   4133 C CG1 . VAL D 2 28  ? 36.563  35.632  23.433  1.00 28.38 ? 28   VAL V CG1 1 
ATOM   4134 C CG2 . VAL D 2 28  ? 34.124  34.976  23.309  1.00 29.41 ? 28   VAL V CG2 1 
ATOM   4135 N N   . LEU D 2 29  ? 33.946  33.947  26.319  1.00 30.71 ? 29   LEU V N   1 
ATOM   4136 C CA  . LEU D 2 29  ? 33.813  32.545  26.644  1.00 31.59 ? 29   LEU V CA  1 
ATOM   4137 C C   . LEU D 2 29  ? 32.673  31.901  25.841  1.00 32.48 ? 29   LEU V C   1 
ATOM   4138 O O   . LEU D 2 29  ? 31.581  32.456  25.755  1.00 32.16 ? 29   LEU V O   1 
ATOM   4139 C CB  . LEU D 2 29  ? 33.626  32.378  28.143  1.00 31.37 ? 29   LEU V CB  1 
ATOM   4140 C CG  . LEU D 2 29  ? 32.356  31.658  28.612  1.00 32.33 ? 29   LEU V CG  1 
ATOM   4141 C CD1 . LEU D 2 29  ? 32.626  30.623  29.708  1.00 33.24 ? 29   LEU V CD1 1 
ATOM   4142 C CD2 . LEU D 2 29  ? 31.282  32.664  29.059  1.00 32.91 ? 29   LEU V CD2 1 
ATOM   4143 N N   . ARG D 2 30  ? 32.956  30.725  25.266  1.00 34.17 ? 30   ARG V N   1 
ATOM   4144 C CA  . ARG D 2 30  ? 32.036  29.952  24.393  1.00 35.33 ? 30   ARG V CA  1 
ATOM   4145 C C   . ARG D 2 30  ? 31.676  28.551  24.925  1.00 36.35 ? 30   ARG V C   1 
ATOM   4146 O O   . ARG D 2 30  ? 32.476  27.890  25.587  1.00 36.43 ? 30   ARG V O   1 
ATOM   4147 C CB  . ARG D 2 30  ? 32.659  29.750  23.015  1.00 34.89 ? 30   ARG V CB  1 
ATOM   4148 C CG  . ARG D 2 30  ? 32.914  30.991  22.266  1.00 35.73 ? 30   ARG V CG  1 
ATOM   4149 C CD  . ARG D 2 30  ? 33.926  30.739  21.203  1.00 37.80 ? 30   ARG V CD  1 
ATOM   4150 N NE  . ARG D 2 30  ? 33.886  31.779  20.178  1.00 40.40 ? 30   ARG V NE  1 
ATOM   4151 C CZ  . ARG D 2 30  ? 34.661  32.865  20.161  1.00 42.22 ? 30   ARG V CZ  1 
ATOM   4152 N NH1 . ARG D 2 30  ? 35.564  33.095  21.112  1.00 42.85 ? 30   ARG V NH1 1 
ATOM   4153 N NH2 . ARG D 2 30  ? 34.535  33.731  19.170  1.00 44.05 ? 30   ARG V NH2 1 
ATOM   4154 N N   . GLU D 2 31  ? 30.480  28.086  24.583  1.00 37.68 ? 31   GLU V N   1 
ATOM   4155 C CA  . GLU D 2 31  ? 30.080  26.713  24.856  1.00 38.65 ? 31   GLU V CA  1 
ATOM   4156 C C   . GLU D 2 31  ? 29.789  25.993  23.545  1.00 38.85 ? 31   GLU V C   1 
ATOM   4157 O O   . GLU D 2 31  ? 29.879  26.583  22.479  1.00 38.89 ? 31   GLU V O   1 
ATOM   4158 C CB  . GLU D 2 31  ? 28.852  26.712  25.747  1.00 39.08 ? 31   GLU V CB  1 
ATOM   4159 C CG  . GLU D 2 31  ? 29.101  27.312  27.119  1.00 40.84 ? 31   GLU V CG  1 
ATOM   4160 C CD  . GLU D 2 31  ? 28.015  28.307  27.516  1.00 44.36 ? 31   GLU V CD  1 
ATOM   4161 O OE1 . GLU D 2 31  ? 27.125  27.951  28.334  1.00 46.09 ? 31   GLU V OE1 1 
ATOM   4162 O OE2 . GLU D 2 31  ? 28.040  29.446  26.992  1.00 45.50 ? 31   GLU V OE2 1 
ATOM   4163 N N   . TRP D 2 32  ? 29.465  24.713  23.625  1.00 39.37 ? 32   TRP V N   1 
ATOM   4164 C CA  . TRP D 2 32  ? 29.145  23.933  22.449  1.00 40.11 ? 32   TRP V CA  1 
ATOM   4165 C C   . TRP D 2 32  ? 28.426  22.676  22.863  1.00 39.97 ? 32   TRP V C   1 
ATOM   4166 O O   . TRP D 2 32  ? 28.769  22.082  23.867  1.00 39.87 ? 32   TRP V O   1 
ATOM   4167 C CB  . TRP D 2 32  ? 30.407  23.554  21.683  1.00 40.32 ? 32   TRP V CB  1 
ATOM   4168 C CG  . TRP D 2 32  ? 30.187  22.393  20.703  1.00 43.38 ? 32   TRP V CG  1 
ATOM   4169 C CD1 . TRP D 2 32  ? 30.244  21.045  20.990  1.00 44.93 ? 32   TRP V CD1 1 
ATOM   4170 C CD2 . TRP D 2 32  ? 29.869  22.481  19.296  1.00 44.60 ? 32   TRP V CD2 1 
ATOM   4171 N NE1 . TRP D 2 32  ? 29.995  20.305  19.855  1.00 44.29 ? 32   TRP V NE1 1 
ATOM   4172 C CE2 . TRP D 2 32  ? 29.768  21.154  18.803  1.00 44.19 ? 32   TRP V CE2 1 
ATOM   4173 C CE3 . TRP D 2 32  ? 29.674  23.546  18.408  1.00 45.53 ? 32   TRP V CE3 1 
ATOM   4174 C CZ2 . TRP D 2 32  ? 29.477  20.866  17.464  1.00 44.79 ? 32   TRP V CZ2 1 
ATOM   4175 C CZ3 . TRP D 2 32  ? 29.383  23.254  17.069  1.00 47.12 ? 32   TRP V CZ3 1 
ATOM   4176 C CH2 . TRP D 2 32  ? 29.289  21.919  16.614  1.00 46.26 ? 32   TRP V CH2 1 
ATOM   4177 N N   . GLN D 2 33  ? 27.441  22.269  22.072  1.00 40.18 ? 33   GLN V N   1 
ATOM   4178 C CA  . GLN D 2 33  ? 26.798  20.985  22.254  1.00 40.35 ? 33   GLN V CA  1 
ATOM   4179 C C   . GLN D 2 33  ? 26.057  20.582  20.983  1.00 40.64 ? 33   GLN V C   1 
ATOM   4180 O O   . GLN D 2 33  ? 24.839  20.699  20.904  1.00 40.76 ? 33   GLN V O   1 
ATOM   4181 C CB  . GLN D 2 33  ? 25.842  21.049  23.440  1.00 40.27 ? 33   GLN V CB  1 
ATOM   4182 C CG  . GLN D 2 33  ? 26.444  20.530  24.723  1.00 40.23 ? 33   GLN V CG  1 
ATOM   4183 C CD  . GLN D 2 33  ? 25.455  20.506  25.878  1.00 40.78 ? 33   GLN V CD  1 
ATOM   4184 O OE1 . GLN D 2 33  ? 24.910  21.541  26.275  1.00 41.36 ? 33   GLN V OE1 1 
ATOM   4185 N NE2 . GLN D 2 33  ? 25.224  19.319  26.433  1.00 40.06 ? 33   GLN V NE2 1 
ATOM   4186 N N   . ASP D 2 34  ? 26.794  20.106  19.986  1.00 40.85 ? 34   ASP V N   1 
ATOM   4187 C CA  . ASP D 2 34  ? 26.210  19.789  18.672  1.00 41.24 ? 34   ASP V CA  1 
ATOM   4188 C C   . ASP D 2 34  ? 25.551  21.018  18.060  1.00 41.11 ? 34   ASP V C   1 
ATOM   4189 O O   . ASP D 2 34  ? 24.408  21.305  18.394  1.00 41.10 ? 34   ASP V O   1 
ATOM   4190 C CB  . ASP D 2 34  ? 25.168  18.648  18.780  1.00 41.48 ? 34   ASP V CB  1 
ATOM   4191 C CG  . ASP D 2 34  ? 25.777  17.228  18.600  1.00 42.50 ? 34   ASP V CG  1 
ATOM   4192 O OD1 . ASP D 2 34  ? 26.699  17.027  17.763  1.00 42.67 ? 34   ASP V OD1 1 
ATOM   4193 O OD2 . ASP D 2 34  ? 25.298  16.295  19.295  1.00 43.02 ? 34   ASP V OD2 1 
ATOM   4194 N N   . ASP D 2 35  ? 26.255  21.731  17.176  1.00 41.36 ? 35   ASP V N   1 
ATOM   4195 C CA  . ASP D 2 35  ? 25.742  22.983  16.541  1.00 42.00 ? 35   ASP V CA  1 
ATOM   4196 C C   . ASP D 2 35  ? 25.183  24.018  17.543  1.00 41.92 ? 35   ASP V C   1 
ATOM   4197 O O   . ASP D 2 35  ? 24.209  24.730  17.255  1.00 41.96 ? 35   ASP V O   1 
ATOM   4198 C CB  . ASP D 2 35  ? 24.715  22.662  15.404  1.00 42.49 ? 35   ASP V CB  1 
ATOM   4199 C CG  . ASP D 2 35  ? 23.817  23.882  14.996  1.00 43.05 ? 35   ASP V CG  1 
ATOM   4200 O OD1 . ASP D 2 35  ? 24.304  24.855  14.343  1.00 43.77 ? 35   ASP V OD1 1 
ATOM   4201 O OD2 . ASP D 2 35  ? 22.604  23.838  15.314  1.00 42.01 ? 35   ASP V OD2 1 
ATOM   4202 N N   . ARG D 2 36  ? 25.796  24.121  18.723  1.00 41.88 ? 36   ARG V N   1 
ATOM   4203 C CA  . ARG D 2 36  ? 25.216  24.996  19.745  1.00 41.15 ? 36   ARG V CA  1 
ATOM   4204 C C   . ARG D 2 36  ? 26.131  26.068  20.335  1.00 41.05 ? 36   ARG V C   1 
ATOM   4205 O O   . ARG D 2 36  ? 25.934  26.473  21.480  1.00 41.55 ? 36   ARG V O   1 
ATOM   4206 C CB  . ARG D 2 36  ? 24.507  24.170  20.825  1.00 40.77 ? 36   ARG V CB  1 
ATOM   4207 C CG  . ARG D 2 36  ? 23.002  24.088  20.603  1.00 39.52 ? 36   ARG V CG  1 
ATOM   4208 C CD  . ARG D 2 36  ? 22.220  24.755  21.721  1.00 39.17 ? 36   ARG V CD  1 
ATOM   4209 N NE  . ARG D 2 36  ? 22.334  24.026  22.985  1.00 40.25 ? 36   ARG V NE  1 
ATOM   4210 C CZ  . ARG D 2 36  ? 22.438  22.701  23.087  1.00 41.43 ? 36   ARG V CZ  1 
ATOM   4211 N NH1 . ARG D 2 36  ? 22.410  21.958  21.992  1.00 42.73 ? 36   ARG V NH1 1 
ATOM   4212 N NH2 . ARG D 2 36  ? 22.552  22.103  24.273  1.00 40.51 ? 36   ARG V NH2 1 
ATOM   4213 N N   . GLU D 2 37  ? 27.081  26.577  19.551  1.00 40.52 ? 37   GLU V N   1 
ATOM   4214 C CA  . GLU D 2 37  ? 27.931  27.639  20.061  1.00 40.38 ? 37   GLU V CA  1 
ATOM   4215 C C   . GLU D 2 37  ? 27.108  28.786  20.669  1.00 39.64 ? 37   GLU V C   1 
ATOM   4216 O O   . GLU D 2 37  ? 26.447  29.537  19.968  1.00 39.42 ? 37   GLU V O   1 
ATOM   4217 C CB  . GLU D 2 37  ? 29.003  28.105  19.049  1.00 40.79 ? 37   GLU V CB  1 
ATOM   4218 C CG  . GLU D 2 37  ? 28.530  28.981  17.861  1.00 43.67 ? 37   GLU V CG  1 
ATOM   4219 C CD  . GLU D 2 37  ? 29.661  29.854  17.246  1.00 46.68 ? 37   GLU V CD  1 
ATOM   4220 O OE1 . GLU D 2 37  ? 29.953  29.702  16.016  1.00 45.43 ? 37   GLU V OE1 1 
ATOM   4221 O OE2 . GLU D 2 37  ? 30.245  30.690  18.003  1.00 47.48 ? 37   GLU V OE2 1 
ATOM   4222 N N   . LEU D 2 38  ? 27.099  28.827  22.002  1.00 39.19 ? 38   LEU V N   1 
ATOM   4223 C CA  . LEU D 2 38  ? 26.749  30.012  22.781  1.00 38.33 ? 38   LEU V CA  1 
ATOM   4224 C C   . LEU D 2 38  ? 28.056  30.745  22.998  1.00 37.75 ? 38   LEU V C   1 
ATOM   4225 O O   . LEU D 2 38  ? 29.110  30.094  23.146  1.00 37.44 ? 38   LEU V O   1 
ATOM   4226 C CB  . LEU D 2 38  ? 26.194  29.618  24.142  1.00 38.46 ? 38   LEU V CB  1 
ATOM   4227 C CG  . LEU D 2 38  ? 25.638  30.725  25.037  1.00 38.40 ? 38   LEU V CG  1 
ATOM   4228 C CD1 . LEU D 2 38  ? 24.504  31.461  24.337  1.00 39.30 ? 38   LEU V CD1 1 
ATOM   4229 C CD2 . LEU D 2 38  ? 25.136  30.130  26.343  1.00 38.90 ? 38   LEU V CD2 1 
ATOM   4230 N N   . GLU D 2 39  ? 27.995  32.081  23.015  1.00 36.71 ? 39   GLU V N   1 
ATOM   4231 C CA  . GLU D 2 39  ? 29.211  32.902  23.065  1.00 35.92 ? 39   GLU V CA  1 
ATOM   4232 C C   . GLU D 2 39  ? 29.043  34.261  23.760  1.00 34.81 ? 39   GLU V C   1 
ATOM   4233 O O   . GLU D 2 39  ? 28.355  35.131  23.246  1.00 35.14 ? 39   GLU V O   1 
ATOM   4234 C CB  . GLU D 2 39  ? 29.757  33.084  21.649  1.00 35.93 ? 39   GLU V CB  1 
ATOM   4235 C CG  . GLU D 2 39  ? 30.935  34.018  21.537  1.00 38.13 ? 39   GLU V CG  1 
ATOM   4236 C CD  . GLU D 2 39  ? 31.182  34.430  20.096  1.00 42.31 ? 39   GLU V CD  1 
ATOM   4237 O OE1 . GLU D 2 39  ? 30.849  35.597  19.729  1.00 42.35 ? 39   GLU V OE1 1 
ATOM   4238 O OE2 . GLU D 2 39  ? 31.686  33.572  19.325  1.00 44.49 ? 39   GLU V OE2 1 
ATOM   4239 N N   . VAL D 2 40  ? 29.671  34.455  24.921  1.00 33.51 ? 40   VAL V N   1 
ATOM   4240 C CA  . VAL D 2 40  ? 29.624  35.785  25.535  1.00 32.14 ? 40   VAL V CA  1 
ATOM   4241 C C   . VAL D 2 40  ? 30.948  36.504  25.664  1.00 31.32 ? 40   VAL V C   1 
ATOM   4242 O O   . VAL D 2 40  ? 31.943  35.979  26.176  1.00 31.06 ? 40   VAL V O   1 
ATOM   4243 C CB  . VAL D 2 40  ? 28.861  35.856  26.860  1.00 31.95 ? 40   VAL V CB  1 
ATOM   4244 C CG1 . VAL D 2 40  ? 27.851  34.717  26.948  1.00 32.73 ? 40   VAL V CG1 1 
ATOM   4245 C CG2 . VAL D 2 40  ? 29.815  35.861  28.016  1.00 31.47 ? 40   VAL V CG2 1 
ATOM   4246 N N   . VAL D 2 41  ? 30.921  37.732  25.166  1.00 30.46 ? 41   VAL V N   1 
ATOM   4247 C CA  . VAL D 2 41  ? 32.042  38.634  25.243  1.00 29.50 ? 41   VAL V CA  1 
ATOM   4248 C C   . VAL D 2 41  ? 31.759  39.759  26.239  1.00 29.35 ? 41   VAL V C   1 
ATOM   4249 O O   . VAL D 2 41  ? 30.596  40.194  26.391  1.00 29.35 ? 41   VAL V O   1 
ATOM   4250 C CB  . VAL D 2 41  ? 32.340  39.241  23.906  1.00 28.80 ? 41   VAL V CB  1 
ATOM   4251 C CG1 . VAL D 2 41  ? 33.790  39.574  23.845  1.00 28.94 ? 41   VAL V CG1 1 
ATOM   4252 C CG2 . VAL D 2 41  ? 31.997  38.273  22.831  1.00 28.41 ? 41   VAL V CG2 1 
ATOM   4253 N N   . THR D 2 42  ? 32.820  40.182  26.936  1.00 28.52 ? 42   THR V N   1 
ATOM   4254 C CA  . THR D 2 42  ? 32.806  41.347  27.791  1.00 27.91 ? 42   THR V CA  1 
ATOM   4255 C C   . THR D 2 42  ? 34.127  42.018  27.577  1.00 27.81 ? 42   THR V C   1 
ATOM   4256 O O   . THR D 2 42  ? 35.077  41.385  27.130  1.00 27.77 ? 42   THR V O   1 
ATOM   4257 C CB  . THR D 2 42  ? 32.671  40.995  29.256  1.00 27.90 ? 42   THR V CB  1 
ATOM   4258 O OG1 . THR D 2 42  ? 33.752  40.141  29.635  1.00 29.31 ? 42   THR V OG1 1 
ATOM   4259 C CG2 . THR D 2 42  ? 31.342  40.324  29.544  1.00 27.12 ? 42   THR V CG2 1 
ATOM   4260 N N   . ARG D 2 43  ? 34.187  43.307  27.878  1.00 28.19 ? 43   ARG V N   1 
ATOM   4261 C CA  . ARG D 2 43  ? 35.365  44.109  27.530  1.00 29.02 ? 43   ARG V CA  1 
ATOM   4262 C C   . ARG D 2 43  ? 35.411  45.412  28.308  1.00 29.64 ? 43   ARG V C   1 
ATOM   4263 O O   . ARG D 2 43  ? 34.366  45.849  28.816  1.00 30.20 ? 43   ARG V O   1 
ATOM   4264 C CB  . ARG D 2 43  ? 35.411  44.391  26.026  1.00 28.87 ? 43   ARG V CB  1 
ATOM   4265 C CG  . ARG D 2 43  ? 34.041  44.573  25.341  1.00 28.11 ? 43   ARG V CG  1 
ATOM   4266 C CD  . ARG D 2 43  ? 34.250  44.701  23.864  1.00 26.38 ? 43   ARG V CD  1 
ATOM   4267 N NE  . ARG D 2 43  ? 33.163  44.159  23.075  1.00 26.09 ? 43   ARG V NE  1 
ATOM   4268 C CZ  . ARG D 2 43  ? 33.345  43.387  22.006  1.00 26.52 ? 43   ARG V CZ  1 
ATOM   4269 N NH1 . ARG D 2 43  ? 34.576  43.022  21.624  1.00 23.87 ? 43   ARG V NH1 1 
ATOM   4270 N NH2 . ARG D 2 43  ? 32.283  42.948  21.344  1.00 27.29 ? 43   ARG V NH2 1 
ATOM   4271 N N   . GLY D 2 44  ? 36.606  46.012  28.398  1.00 29.80 ? 44   GLY V N   1 
ATOM   4272 C CA  . GLY D 2 44  ? 36.848  47.191  29.237  1.00 30.58 ? 44   GLY V CA  1 
ATOM   4273 C C   . GLY D 2 44  ? 38.326  47.482  29.451  1.00 31.30 ? 44   GLY V C   1 
ATOM   4274 O O   . GLY D 2 44  ? 39.164  46.995  28.688  1.00 31.27 ? 44   GLY V O   1 
ATOM   4275 N N   . CYS D 2 45  ? 38.661  48.262  30.485  1.00 31.76 ? 45   CYS V N   1 
ATOM   4276 C CA  . CYS D 2 45  ? 40.057  48.641  30.711  1.00 32.38 ? 45   CYS V CA  1 
ATOM   4277 C C   . CYS D 2 45  ? 40.876  47.590  31.500  1.00 32.37 ? 45   CYS V C   1 
ATOM   4278 O O   . CYS D 2 45  ? 40.306  46.748  32.193  1.00 32.22 ? 45   CYS V O   1 
ATOM   4279 C CB  . CYS D 2 45  ? 40.121  50.048  31.294  1.00 32.59 ? 45   CYS V CB  1 
ATOM   4280 S SG  . CYS D 2 45  ? 39.470  51.359  30.114  1.00 35.85 ? 45   CYS V SG  1 
ATOM   4281 N N   . ALA D 2 46  ? 42.203  47.631  31.394  1.00 32.90 ? 46   ALA V N   1 
ATOM   4282 C CA  . ALA D 2 46  ? 43.022  46.437  31.666  1.00 34.02 ? 46   ALA V CA  1 
ATOM   4283 C C   . ALA D 2 46  ? 43.808  46.279  32.971  1.00 35.04 ? 46   ALA V C   1 
ATOM   4284 O O   . ALA D 2 46  ? 43.571  45.328  33.739  1.00 35.24 ? 46   ALA V O   1 
ATOM   4285 C CB  . ALA D 2 46  ? 43.962  46.202  30.533  1.00 33.98 ? 46   ALA V CB  1 
ATOM   4286 N N   . HIS D 2 47  ? 44.768  47.180  33.188  1.00 36.03 ? 47   HIS V N   1 
ATOM   4287 C CA  . HIS D 2 47  ? 45.891  46.996  34.143  1.00 36.90 ? 47   HIS V CA  1 
ATOM   4288 C C   . HIS D 2 47  ? 46.936  46.239  33.375  1.00 36.45 ? 47   HIS V C   1 
ATOM   4289 O O   . HIS D 2 47  ? 46.670  45.162  32.848  1.00 36.58 ? 47   HIS V O   1 
ATOM   4290 C CB  . HIS D 2 47  ? 45.502  46.258  35.435  1.00 37.43 ? 47   HIS V CB  1 
ATOM   4291 C CG  . HIS D 2 47  ? 44.412  46.941  36.204  1.00 40.80 ? 47   HIS V CG  1 
ATOM   4292 N ND1 . HIS D 2 47  ? 44.604  48.144  36.860  1.00 42.88 ? 47   HIS V ND1 1 
ATOM   4293 C CD2 . HIS D 2 47  ? 43.106  46.614  36.386  1.00 42.16 ? 47   HIS V CD2 1 
ATOM   4294 C CE1 . HIS D 2 47  ? 43.468  48.516  37.428  1.00 43.17 ? 47   HIS V CE1 1 
ATOM   4295 N NE2 . HIS D 2 47  ? 42.544  47.609  37.151  1.00 43.37 ? 47   HIS V NE2 1 
ATOM   4296 N N   . SER D 2 48  ? 48.116  46.817  33.274  1.00 36.03 ? 48   SER V N   1 
ATOM   4297 C CA  . SER D 2 48  ? 49.041  46.337  32.293  1.00 36.19 ? 48   SER V CA  1 
ATOM   4298 C C   . SER D 2 48  ? 49.828  45.184  32.820  1.00 36.14 ? 48   SER V C   1 
ATOM   4299 O O   . SER D 2 48  ? 50.820  44.799  32.219  1.00 36.10 ? 48   SER V O   1 
ATOM   4300 C CB  . SER D 2 48  ? 49.970  47.445  31.876  1.00 36.45 ? 48   SER V CB  1 
ATOM   4301 O OG  . SER D 2 48  ? 50.486  48.039  33.040  1.00 37.86 ? 48   SER V OG  1 
ATOM   4302 N N   . GLU D 2 49  ? 49.380  44.625  33.939  1.00 36.64 ? 49   GLU V N   1 
ATOM   4303 C CA  . GLU D 2 49  ? 49.940  43.365  34.454  1.00 37.19 ? 49   GLU V CA  1 
ATOM   4304 C C   . GLU D 2 49  ? 49.085  42.182  34.003  1.00 37.15 ? 49   GLU V C   1 
ATOM   4305 O O   . GLU D 2 49  ? 48.807  41.251  34.746  1.00 37.22 ? 49   GLU V O   1 
ATOM   4306 C CB  . GLU D 2 49  ? 50.120  43.415  35.977  1.00 37.17 ? 49   GLU V CB  1 
ATOM   4307 C CG  . GLU D 2 49  ? 50.996  44.589  36.456  1.00 38.44 ? 49   GLU V CG  1 
ATOM   4308 C CD  . GLU D 2 49  ? 52.324  44.740  35.679  1.00 39.35 ? 49   GLU V CD  1 
ATOM   4309 O OE1 . GLU D 2 49  ? 52.445  45.669  34.842  1.00 38.49 ? 49   GLU V OE1 1 
ATOM   4310 O OE2 . GLU D 2 49  ? 53.245  43.928  35.909  1.00 39.91 ? 49   GLU V OE2 1 
ATOM   4311 N N   . LYS D 2 50  ? 48.680  42.245  32.746  1.00 37.39 ? 50   LYS V N   1 
ATOM   4312 C CA  . LYS D 2 50  ? 47.734  41.310  32.187  1.00 37.49 ? 50   LYS V CA  1 
ATOM   4313 C C   . LYS D 2 50  ? 48.177  40.915  30.790  1.00 37.80 ? 50   LYS V C   1 
ATOM   4314 O O   . LYS D 2 50  ? 48.784  41.725  30.078  1.00 37.78 ? 50   LYS V O   1 
ATOM   4315 C CB  . LYS D 2 50  ? 46.348  41.935  32.157  1.00 37.07 ? 50   LYS V CB  1 
ATOM   4316 C CG  . LYS D 2 50  ? 45.678  41.907  33.493  1.00 36.75 ? 50   LYS V CG  1 
ATOM   4317 C CD  . LYS D 2 50  ? 44.194  41.923  33.313  1.00 37.69 ? 50   LYS V CD  1 
ATOM   4318 C CE  . LYS D 2 50  ? 43.726  40.663  32.609  1.00 37.79 ? 50   LYS V CE  1 
ATOM   4319 N NZ  . LYS D 2 50  ? 42.673  40.955  31.619  1.00 37.62 ? 50   LYS V NZ  1 
ATOM   4320 N N   . THR D 2 51  ? 47.874  39.669  30.415  1.00 38.17 ? 51   THR V N   1 
ATOM   4321 C CA  . THR D 2 51  ? 48.338  39.078  29.148  1.00 38.55 ? 51   THR V CA  1 
ATOM   4322 C C   . THR D 2 51  ? 47.199  38.436  28.356  1.00 39.19 ? 51   THR V C   1 
ATOM   4323 O O   . THR D 2 51  ? 46.048  38.450  28.799  1.00 39.32 ? 51   THR V O   1 
ATOM   4324 C CB  . THR D 2 51  ? 49.409  38.015  29.396  1.00 38.16 ? 51   THR V CB  1 
ATOM   4325 O OG1 . THR D 2 51  ? 49.039  37.252  30.551  1.00 37.38 ? 51   THR V OG1 1 
ATOM   4326 C CG2 . THR D 2 51  ? 50.764  38.658  29.602  1.00 37.38 ? 51   THR V CG2 1 
ATOM   4327 N N   . ASN D 2 52  ? 47.515  37.902  27.179  1.00 39.67 ? 52   ASN V N   1 
ATOM   4328 C CA  . ASN D 2 52  ? 46.560  37.089  26.466  1.00 41.02 ? 52   ASN V CA  1 
ATOM   4329 C C   . ASN D 2 52  ? 46.476  35.732  27.173  1.00 40.95 ? 52   ASN V C   1 
ATOM   4330 O O   . ASN D 2 52  ? 47.499  35.224  27.603  1.00 41.39 ? 52   ASN V O   1 
ATOM   4331 C CB  . ASN D 2 52  ? 47.019  36.916  25.024  1.00 41.72 ? 52   ASN V CB  1 
ATOM   4332 C CG  . ASN D 2 52  ? 46.927  38.202  24.202  1.00 45.32 ? 52   ASN V CG  1 
ATOM   4333 O OD1 . ASN D 2 52  ? 46.266  39.173  24.587  1.00 46.04 ? 52   ASN V OD1 1 
ATOM   4334 N ND2 . ASN D 2 52  ? 47.597  38.200  23.053  1.00 50.56 ? 52   ASN V ND2 1 
ATOM   4335 N N   . ARG D 2 53  ? 45.287  35.144  27.313  1.00 41.00 ? 53   ARG V N   1 
ATOM   4336 C CA  . ARG D 2 53  ? 45.158  33.829  27.969  1.00 41.11 ? 53   ARG V CA  1 
ATOM   4337 C C   . ARG D 2 53  ? 43.968  32.961  27.537  1.00 41.53 ? 53   ARG V C   1 
ATOM   4338 O O   . ARG D 2 53  ? 42.904  33.459  27.209  1.00 42.02 ? 53   ARG V O   1 
ATOM   4339 C CB  . ARG D 2 53  ? 45.174  33.981  29.492  1.00 41.09 ? 53   ARG V CB  1 
ATOM   4340 C CG  . ARG D 2 53  ? 43.925  34.573  30.130  1.00 40.64 ? 53   ARG V CG  1 
ATOM   4341 C CD  . ARG D 2 53  ? 44.114  36.019  30.515  1.00 40.15 ? 53   ARG V CD  1 
ATOM   4342 N NE  . ARG D 2 53  ? 45.263  36.264  31.397  1.00 39.45 ? 53   ARG V NE  1 
ATOM   4343 C CZ  . ARG D 2 53  ? 45.186  36.864  32.585  1.00 38.74 ? 53   ARG V CZ  1 
ATOM   4344 N NH1 . ARG D 2 53  ? 44.013  37.274  33.061  1.00 37.67 ? 53   ARG V NH1 1 
ATOM   4345 N NH2 . ARG D 2 53  ? 46.286  37.061  33.298  1.00 37.56 ? 53   ARG V NH2 1 
ATOM   4346 N N   . THR D 2 54  ? 44.155  31.653  27.545  1.00 41.91 ? 54   THR V N   1 
ATOM   4347 C CA  . THR D 2 54  ? 43.096  30.729  27.162  1.00 42.51 ? 54   THR V CA  1 
ATOM   4348 C C   . THR D 2 54  ? 42.868  29.773  28.299  1.00 42.64 ? 54   THR V C   1 
ATOM   4349 O O   . THR D 2 54  ? 43.739  29.595  29.139  1.00 43.60 ? 54   THR V O   1 
ATOM   4350 C CB  . THR D 2 54  ? 43.532  29.806  26.015  1.00 42.78 ? 54   THR V CB  1 
ATOM   4351 O OG1 . THR D 2 54  ? 44.772  30.257  25.454  1.00 43.26 ? 54   THR V OG1 1 
ATOM   4352 C CG2 . THR D 2 54  ? 42.425  29.669  24.944  1.00 43.16 ? 54   THR V CG2 1 
ATOM   4353 N N   . MET D 2 55  ? 41.717  29.123  28.308  1.00 42.41 ? 55   MET V N   1 
ATOM   4354 C CA  . MET D 2 55  ? 41.466  27.994  29.194  1.00 42.39 ? 55   MET V CA  1 
ATOM   4355 C C   . MET D 2 55  ? 40.389  27.243  28.447  1.00 41.46 ? 55   MET V C   1 
ATOM   4356 O O   . MET D 2 55  ? 39.765  27.818  27.548  1.00 42.14 ? 55   MET V O   1 
ATOM   4357 C CB  . MET D 2 55  ? 40.964  28.477  30.551  1.00 43.09 ? 55   MET V CB  1 
ATOM   4358 C CG  . MET D 2 55  ? 41.044  27.458  31.694  1.00 46.55 ? 55   MET V CG  1 
ATOM   4359 S SD  . MET D 2 55  ? 40.174  27.979  33.234  1.00 53.86 ? 55   MET V SD  1 
ATOM   4360 C CE  . MET D 2 55  ? 41.279  29.265  33.866  1.00 51.91 ? 55   MET V CE  1 
ATOM   4361 N N   . SER D 2 56  ? 40.182  25.968  28.760  1.00 39.76 ? 56   SER V N   1 
ATOM   4362 C CA  . SER D 2 56  ? 39.208  25.158  28.024  1.00 38.08 ? 56   SER V CA  1 
ATOM   4363 C C   . SER D 2 56  ? 39.096  23.837  28.722  1.00 37.15 ? 56   SER V C   1 
ATOM   4364 O O   . SER D 2 56  ? 40.099  23.153  28.947  1.00 37.51 ? 56   SER V O   1 
ATOM   4365 C CB  . SER D 2 56  ? 39.644  24.907  26.580  1.00 37.78 ? 56   SER V CB  1 
ATOM   4366 O OG  . SER D 2 56  ? 40.524  25.916  26.111  1.00 37.46 ? 56   SER V OG  1 
ATOM   4367 N N   . TYR D 2 57  ? 37.883  23.478  29.088  1.00 35.47 ? 57   TYR V N   1 
ATOM   4368 C CA  . TYR D 2 57  ? 37.663  22.196  29.707  1.00 34.04 ? 57   TYR V CA  1 
ATOM   4369 C C   . TYR D 2 57  ? 36.328  21.710  29.206  1.00 33.82 ? 57   TYR V C   1 
ATOM   4370 O O   . TYR D 2 57  ? 35.640  22.447  28.481  1.00 33.83 ? 57   TYR V O   1 
ATOM   4371 C CB  . TYR D 2 57  ? 37.703  22.303  31.234  1.00 33.42 ? 57   TYR V CB  1 
ATOM   4372 C CG  . TYR D 2 57  ? 36.619  23.168  31.831  1.00 31.69 ? 57   TYR V CG  1 
ATOM   4373 C CD1 . TYR D 2 57  ? 35.448  22.608  32.331  1.00 30.33 ? 57   TYR V CD1 1 
ATOM   4374 C CD2 . TYR D 2 57  ? 36.763  24.549  31.903  1.00 30.33 ? 57   TYR V CD2 1 
ATOM   4375 C CE1 . TYR D 2 57  ? 34.448  23.413  32.876  1.00 29.13 ? 57   TYR V CE1 1 
ATOM   4376 C CE2 . TYR D 2 57  ? 35.764  25.355  32.446  1.00 27.84 ? 57   TYR V CE2 1 
ATOM   4377 C CZ  . TYR D 2 57  ? 34.622  24.783  32.923  1.00 27.15 ? 57   TYR V CZ  1 
ATOM   4378 O OH  . TYR D 2 57  ? 33.653  25.573  33.460  1.00 26.40 ? 57   TYR V OH  1 
ATOM   4379 N N   . ARG D 2 58  ? 35.963  20.480  29.573  1.00 33.12 ? 58   ARG V N   1 
ATOM   4380 C CA  . ARG D 2 58  ? 34.688  19.936  29.140  1.00 32.45 ? 58   ARG V CA  1 
ATOM   4381 C C   . ARG D 2 58  ? 33.826  19.320  30.238  1.00 31.66 ? 58   ARG V C   1 
ATOM   4382 O O   . ARG D 2 58  ? 34.349  18.742  31.182  1.00 31.47 ? 58   ARG V O   1 
ATOM   4383 C CB  . ARG D 2 58  ? 34.855  19.010  27.917  1.00 32.89 ? 58   ARG V CB  1 
ATOM   4384 C CG  . ARG D 2 58  ? 35.717  17.763  28.068  1.00 33.06 ? 58   ARG V CG  1 
ATOM   4385 C CD  . ARG D 2 58  ? 35.061  16.619  27.258  1.00 33.66 ? 58   ARG V CD  1 
ATOM   4386 N NE  . ARG D 2 58  ? 35.807  16.173  26.080  1.00 32.84 ? 58   ARG V NE  1 
ATOM   4387 C CZ  . ARG D 2 58  ? 35.250  15.606  25.010  1.00 32.21 ? 58   ARG V CZ  1 
ATOM   4388 N NH1 . ARG D 2 58  ? 33.935  15.434  24.941  1.00 31.68 ? 58   ARG V NH1 1 
ATOM   4389 N NH2 . ARG D 2 58  ? 36.010  15.228  23.996  1.00 31.96 ? 58   ARG V NH2 1 
ATOM   4390 N N   . MET D 2 59  ? 32.507  19.468  30.075  1.00 30.86 ? 59   MET V N   1 
ATOM   4391 C CA  . MET D 2 59  ? 31.482  18.949  30.972  1.00 30.14 ? 59   MET V CA  1 
ATOM   4392 C C   . MET D 2 59  ? 30.551  17.998  30.247  1.00 29.26 ? 59   MET V C   1 
ATOM   4393 O O   . MET D 2 59  ? 29.421  18.340  29.914  1.00 29.00 ? 59   MET V O   1 
ATOM   4394 C CB  . MET D 2 59  ? 30.637  20.088  31.498  1.00 30.53 ? 59   MET V CB  1 
ATOM   4395 C CG  . MET D 2 59  ? 31.161  20.814  32.714  1.00 32.76 ? 59   MET V CG  1 
ATOM   4396 S SD  . MET D 2 59  ? 29.775  21.777  33.416  1.00 37.53 ? 59   MET V SD  1 
ATOM   4397 C CE  . MET D 2 59  ? 28.944  20.521  34.397  1.00 37.36 ? 59   MET V CE  1 
ATOM   4398 N N   . GLY D 2 60  ? 31.037  16.786  30.001  1.00 28.91 ? 60   GLY V N   1 
ATOM   4399 C CA  . GLY D 2 60  ? 30.254  15.775  29.315  1.00 28.89 ? 60   GLY V CA  1 
ATOM   4400 C C   . GLY D 2 60  ? 30.278  15.944  27.809  1.00 28.90 ? 60   GLY V C   1 
ATOM   4401 O O   . GLY D 2 60  ? 31.283  15.660  27.158  1.00 29.18 ? 60   GLY V O   1 
ATOM   4402 N N   . SER D 2 61  ? 29.163  16.409  27.254  1.00 28.33 ? 61   SER V N   1 
ATOM   4403 C CA  . SER D 2 61  ? 29.053  16.617  25.815  1.00 27.75 ? 61   SER V CA  1 
ATOM   4404 C C   . SER D 2 61  ? 29.361  18.062  25.440  1.00 27.58 ? 61   SER V C   1 
ATOM   4405 O O   . SER D 2 61  ? 29.540  18.384  24.265  1.00 27.43 ? 61   SER V O   1 
ATOM   4406 C CB  . SER D 2 61  ? 27.656  16.232  25.324  1.00 28.01 ? 61   SER V CB  1 
ATOM   4407 O OG  . SER D 2 61  ? 26.711  17.241  25.635  1.00 27.40 ? 61   SER V OG  1 
ATOM   4408 N N   . MET D 2 62  ? 29.421  18.930  26.445  1.00 27.71 ? 62   MET V N   1 
ATOM   4409 C CA  . MET D 2 62  ? 29.707  20.342  26.222  1.00 28.07 ? 62   MET V CA  1 
ATOM   4410 C C   . MET D 2 62  ? 31.179  20.652  26.466  1.00 28.02 ? 62   MET V C   1 
ATOM   4411 O O   . MET D 2 62  ? 31.784  20.140  27.408  1.00 28.55 ? 62   MET V O   1 
ATOM   4412 C CB  . MET D 2 62  ? 28.829  21.215  27.122  1.00 27.95 ? 62   MET V CB  1 
ATOM   4413 C CG  . MET D 2 62  ? 29.300  22.655  27.239  1.00 29.02 ? 62   MET V CG  1 
ATOM   4414 S SD  . MET D 2 62  ? 28.118  23.705  28.106  1.00 33.55 ? 62   MET V SD  1 
ATOM   4415 C CE  . MET D 2 62  ? 26.922  24.011  26.809  1.00 32.57 ? 62   MET V CE  1 
ATOM   4416 N N   . ILE D 2 63  ? 31.751  21.495  25.612  1.00 27.79 ? 63   ILE V N   1 
ATOM   4417 C CA  . ILE D 2 63  ? 33.154  21.876  25.734  1.00 27.67 ? 63   ILE V CA  1 
ATOM   4418 C C   . ILE D 2 63  ? 33.105  23.353  25.954  1.00 27.74 ? 63   ILE V C   1 
ATOM   4419 O O   . ILE D 2 63  ? 32.444  24.065  25.198  1.00 27.97 ? 63   ILE V O   1 
ATOM   4420 C CB  . ILE D 2 63  ? 33.964  21.634  24.468  1.00 27.67 ? 63   ILE V CB  1 
ATOM   4421 C CG1 . ILE D 2 63  ? 33.982  20.147  24.083  1.00 29.10 ? 63   ILE V CG1 1 
ATOM   4422 C CG2 . ILE D 2 63  ? 35.369  22.131  24.654  1.00 27.15 ? 63   ILE V CG2 1 
ATOM   4423 C CD1 . ILE D 2 63  ? 33.036  19.736  22.895  1.00 30.33 ? 63   ILE V CD1 1 
ATOM   4424 N N   . ILE D 2 64  ? 33.766  23.830  27.001  1.00 27.72 ? 64   ILE V N   1 
ATOM   4425 C CA  . ILE D 2 64  ? 33.686  25.251  27.291  1.00 27.47 ? 64   ILE V CA  1 
ATOM   4426 C C   . ILE D 2 64  ? 35.033  25.929  27.035  1.00 27.51 ? 64   ILE V C   1 
ATOM   4427 O O   . ILE D 2 64  ? 36.082  25.381  27.392  1.00 27.78 ? 64   ILE V O   1 
ATOM   4428 C CB  . ILE D 2 64  ? 33.080  25.535  28.675  1.00 27.14 ? 64   ILE V CB  1 
ATOM   4429 C CG1 . ILE D 2 64  ? 34.163  25.822  29.681  1.00 28.33 ? 64   ILE V CG1 1 
ATOM   4430 C CG2 . ILE D 2 64  ? 32.158  24.417  29.131  1.00 26.40 ? 64   ILE V CG2 1 
ATOM   4431 C CD1 . ILE D 2 64  ? 34.488  27.289  29.766  1.00 30.23 ? 64   ILE V CD1 1 
ATOM   4432 N N   . SER D 2 65  ? 35.002  27.093  26.381  1.00 27.37 ? 65   SER V N   1 
ATOM   4433 C CA  . SER D 2 65  ? 36.225  27.668  25.848  1.00 27.32 ? 65   SER V CA  1 
ATOM   4434 C C   . SER D 2 65  ? 36.425  29.162  26.035  1.00 27.43 ? 65   SER V C   1 
ATOM   4435 O O   . SER D 2 65  ? 35.871  29.980  25.301  1.00 26.70 ? 65   SER V O   1 
ATOM   4436 C CB  . SER D 2 65  ? 36.402  27.293  24.393  1.00 27.30 ? 65   SER V CB  1 
ATOM   4437 O OG  . SER D 2 65  ? 37.700  27.652  23.973  1.00 27.92 ? 65   SER V OG  1 
ATOM   4438 N N   . LEU D 2 66  ? 37.282  29.465  27.017  1.00 28.17 ? 66   LEU V N   1 
ATOM   4439 C CA  . LEU D 2 66  ? 37.630  30.810  27.455  1.00 28.72 ? 66   LEU V CA  1 
ATOM   4440 C C   . LEU D 2 66  ? 38.867  31.319  26.816  1.00 29.08 ? 66   LEU V C   1 
ATOM   4441 O O   . LEU D 2 66  ? 39.874  30.624  26.756  1.00 29.34 ? 66   LEU V O   1 
ATOM   4442 C CB  . LEU D 2 66  ? 37.870  30.849  28.947  1.00 28.45 ? 66   LEU V CB  1 
ATOM   4443 C CG  . LEU D 2 66  ? 36.576  31.241  29.624  1.00 30.03 ? 66   LEU V CG  1 
ATOM   4444 C CD1 . LEU D 2 66  ? 35.908  30.022  30.201  1.00 31.21 ? 66   LEU V CD1 1 
ATOM   4445 C CD2 . LEU D 2 66  ? 36.839  32.230  30.712  1.00 32.13 ? 66   LEU V CD2 1 
ATOM   4446 N N   . THR D 2 67  ? 38.778  32.558  26.358  1.00 29.72 ? 67   THR V N   1 
ATOM   4447 C CA  . THR D 2 67  ? 39.901  33.275  25.790  1.00 30.46 ? 67   THR V CA  1 
ATOM   4448 C C   . THR D 2 67  ? 39.755  34.722  26.183  1.00 30.72 ? 67   THR V C   1 
ATOM   4449 O O   . THR D 2 67  ? 38.641  35.253  26.205  1.00 30.85 ? 67   THR V O   1 
ATOM   4450 C CB  . THR D 2 67  ? 39.967  33.175  24.244  1.00 30.77 ? 67   THR V CB  1 
ATOM   4451 O OG1 . THR D 2 67  ? 40.274  34.472  23.700  1.00 31.60 ? 67   THR V OG1 1 
ATOM   4452 C CG2 . THR D 2 67  ? 38.629  32.647  23.634  1.00 30.89 ? 67   THR V CG2 1 
ATOM   4453 N N   . GLU D 2 68  ? 40.880  35.353  26.497  1.00 30.98 ? 68   GLU V N   1 
ATOM   4454 C CA  . GLU D 2 68  ? 40.898  36.761  26.852  1.00 31.56 ? 68   GLU V CA  1 
ATOM   4455 C C   . GLU D 2 68  ? 42.115  37.353  26.219  1.00 31.87 ? 68   GLU V C   1 
ATOM   4456 O O   . GLU D 2 68  ? 43.119  36.669  26.104  1.00 32.16 ? 68   GLU V O   1 
ATOM   4457 C CB  . GLU D 2 68  ? 40.999  36.941  28.345  1.00 31.53 ? 68   GLU V CB  1 
ATOM   4458 C CG  . GLU D 2 68  ? 40.856  38.366  28.762  1.00 32.34 ? 68   GLU V CG  1 
ATOM   4459 C CD  . GLU D 2 68  ? 41.101  38.554  30.231  1.00 34.60 ? 68   GLU V CD  1 
ATOM   4460 O OE1 . GLU D 2 68  ? 40.096  38.745  30.980  1.00 34.85 ? 68   GLU V OE1 1 
ATOM   4461 O OE2 . GLU D 2 68  ? 42.299  38.494  30.629  1.00 34.93 ? 68   GLU V OE2 1 
ATOM   4462 N N   . THR D 2 69  ? 42.037  38.614  25.798  1.00 32.37 ? 69   THR V N   1 
ATOM   4463 C CA  . THR D 2 69  ? 43.145  39.210  25.053  1.00 32.74 ? 69   THR V CA  1 
ATOM   4464 C C   . THR D 2 69  ? 43.278  40.688  25.233  1.00 33.04 ? 69   THR V C   1 
ATOM   4465 O O   . THR D 2 69  ? 42.294  41.431  25.094  1.00 33.51 ? 69   THR V O   1 
ATOM   4466 C CB  . THR D 2 69  ? 43.030  38.979  23.558  1.00 32.86 ? 69   THR V CB  1 
ATOM   4467 O OG1 . THR D 2 69  ? 44.181  39.558  22.933  1.00 32.66 ? 69   THR V OG1 1 
ATOM   4468 C CG2 . THR D 2 69  ? 41.734  39.611  23.012  1.00 32.38 ? 69   THR V CG2 1 
ATOM   4469 N N   . VAL D 2 70  ? 44.505  41.115  25.507  1.00 33.05 ? 70   VAL V N   1 
ATOM   4470 C CA  . VAL D 2 70  ? 44.729  42.508  25.817  1.00 33.33 ? 70   VAL V CA  1 
ATOM   4471 C C   . VAL D 2 70  ? 45.576  43.213  24.791  1.00 34.09 ? 70   VAL V C   1 
ATOM   4472 O O   . VAL D 2 70  ? 46.710  42.829  24.528  1.00 34.42 ? 70   VAL V O   1 
ATOM   4473 C CB  . VAL D 2 70  ? 45.259  42.750  27.249  1.00 32.79 ? 70   VAL V CB  1 
ATOM   4474 C CG1 . VAL D 2 70  ? 44.143  42.580  28.238  1.00 32.91 ? 70   VAL V CG1 1 
ATOM   4475 C CG2 . VAL D 2 70  ? 46.385  41.850  27.574  1.00 32.13 ? 70   VAL V CG2 1 
ATOM   4476 N N   . CYS D 2 71  ? 44.991  44.251  24.214  1.00 34.87 ? 71   CYS V N   1 
ATOM   4477 C CA  . CYS D 2 71  ? 45.652  45.082  23.244  1.00 36.12 ? 71   CYS V CA  1 
ATOM   4478 C C   . CYS D 2 71  ? 46.062  46.420  23.880  1.00 36.10 ? 71   CYS V C   1 
ATOM   4479 O O   . CYS D 2 71  ? 45.486  46.818  24.907  1.00 36.30 ? 71   CYS V O   1 
ATOM   4480 C CB  . CYS D 2 71  ? 44.685  45.330  22.106  1.00 36.39 ? 71   CYS V CB  1 
ATOM   4481 S SG  . CYS D 2 71  ? 44.743  47.029  21.642  1.00 40.44 ? 71   CYS V SG  1 
ATOM   4482 N N   . ALA D 2 72  ? 47.029  47.119  23.264  1.00 36.03 ? 72   ALA V N   1 
ATOM   4483 C CA  . ALA D 2 72  ? 47.517  48.420  23.787  1.00 35.80 ? 72   ALA V CA  1 
ATOM   4484 C C   . ALA D 2 72  ? 46.975  49.653  23.058  1.00 35.53 ? 72   ALA V C   1 
ATOM   4485 O O   . ALA D 2 72  ? 46.835  50.713  23.648  1.00 35.70 ? 72   ALA V O   1 
ATOM   4486 C CB  . ALA D 2 72  ? 49.066  48.462  23.863  1.00 35.54 ? 72   ALA V CB  1 
ATOM   4487 N N   . THR D 2 73  ? 46.671  49.520  21.779  1.00 35.38 ? 73   THR V N   1 
ATOM   4488 C CA  . THR D 2 73  ? 46.196  50.652  21.002  1.00 35.42 ? 73   THR V CA  1 
ATOM   4489 C C   . THR D 2 73  ? 44.850  51.188  21.486  1.00 35.49 ? 73   THR V C   1 
ATOM   4490 O O   . THR D 2 73  ? 44.162  50.535  22.260  1.00 35.47 ? 73   THR V O   1 
ATOM   4491 C CB  . THR D 2 73  ? 46.095  50.309  19.502  1.00 35.50 ? 73   THR V CB  1 
ATOM   4492 O OG1 . THR D 2 73  ? 44.794  50.685  19.014  1.00 36.31 ? 73   THR V OG1 1 
ATOM   4493 C CG2 . THR D 2 73  ? 46.322  48.808  19.238  1.00 35.28 ? 73   THR V CG2 1 
ATOM   4494 N N   . ASN D 2 74  ? 44.500  52.381  21.002  1.00 35.79 ? 74   ASN V N   1 
ATOM   4495 C CA  . ASN D 2 74  ? 43.207  53.042  21.240  1.00 36.07 ? 74   ASN V CA  1 
ATOM   4496 C C   . ASN D 2 74  ? 42.006  52.370  20.630  1.00 35.94 ? 74   ASN V C   1 
ATOM   4497 O O   . ASN D 2 74  ? 42.090  51.849  19.520  1.00 36.31 ? 74   ASN V O   1 
ATOM   4498 C CB  . ASN D 2 74  ? 43.233  54.474  20.704  1.00 36.20 ? 74   ASN V CB  1 
ATOM   4499 C CG  . ASN D 2 74  ? 43.104  55.500  21.801  1.00 37.36 ? 74   ASN V CG  1 
ATOM   4500 O OD1 . ASN D 2 74  ? 42.485  55.245  22.846  1.00 39.20 ? 74   ASN V OD1 1 
ATOM   4501 N ND2 . ASN D 2 74  ? 43.689  56.671  21.580  1.00 37.54 ? 74   ASN V ND2 1 
ATOM   4502 N N   . LEU D 2 75  ? 40.886  52.449  21.348  1.00 35.72 ? 75   LEU V N   1 
ATOM   4503 C CA  . LEU D 2 75  ? 39.602  51.854  20.967  1.00 35.75 ? 75   LEU V CA  1 
ATOM   4504 C C   . LEU D 2 75  ? 39.726  50.534  20.253  1.00 36.40 ? 75   LEU V C   1 
ATOM   4505 O O   . LEU D 2 75  ? 38.965  50.235  19.340  1.00 36.57 ? 75   LEU V O   1 
ATOM   4506 C CB  . LEU D 2 75  ? 38.770  52.812  20.131  1.00 35.09 ? 75   LEU V CB  1 
ATOM   4507 C CG  . LEU D 2 75  ? 37.880  53.729  20.950  1.00 34.94 ? 75   LEU V CG  1 
ATOM   4508 C CD1 . LEU D 2 75  ? 36.778  54.252  20.089  1.00 35.17 ? 75   LEU V CD1 1 
ATOM   4509 C CD2 . LEU D 2 75  ? 37.285  52.996  22.126  1.00 36.21 ? 75   LEU V CD2 1 
ATOM   4510 N N   . CYS D 2 76  ? 40.675  49.729  20.690  1.00 37.23 ? 76   CYS V N   1 
ATOM   4511 C CA  . CYS D 2 76  ? 41.114  48.634  19.869  1.00 38.58 ? 76   CYS V CA  1 
ATOM   4512 C C   . CYS D 2 76  ? 40.325  47.355  20.107  1.00 39.10 ? 76   CYS V C   1 
ATOM   4513 O O   . CYS D 2 76  ? 40.617  46.323  19.480  1.00 39.55 ? 76   CYS V O   1 
ATOM   4514 C CB  . CYS D 2 76  ? 42.582  48.380  20.141  1.00 38.53 ? 76   CYS V CB  1 
ATOM   4515 S SG  . CYS D 2 76  ? 42.820  47.634  21.757  1.00 40.92 ? 76   CYS V SG  1 
ATOM   4516 N N   . ASN D 2 77  ? 39.341  47.401  21.002  1.00 39.51 ? 77   ASN V N   1 
ATOM   4517 C CA  . ASN D 2 77  ? 38.700  46.165  21.421  1.00 39.89 ? 77   ASN V CA  1 
ATOM   4518 C C   . ASN D 2 77  ? 37.209  46.026  21.108  1.00 40.75 ? 77   ASN V C   1 
ATOM   4519 O O   . ASN D 2 77  ? 36.390  45.900  22.007  1.00 40.56 ? 77   ASN V O   1 
ATOM   4520 C CB  . ASN D 2 77  ? 39.048  45.843  22.885  1.00 39.60 ? 77   ASN V CB  1 
ATOM   4521 C CG  . ASN D 2 77  ? 38.566  46.901  23.876  1.00 38.25 ? 77   ASN V CG  1 
ATOM   4522 O OD1 . ASN D 2 77  ? 37.898  47.855  23.535  1.00 35.91 ? 77   ASN V OD1 1 
ATOM   4523 N ND2 . ASN D 2 77  ? 38.897  46.697  25.126  1.00 38.52 ? 77   ASN V ND2 1 
ATOM   4524 N N   . ARG D 2 78  ? 36.873  46.013  19.818  1.00 42.17 ? 78   ARG V N   1 
ATOM   4525 C CA  . ARG D 2 78  ? 35.478  45.849  19.379  1.00 43.45 ? 78   ARG V CA  1 
ATOM   4526 C C   . ARG D 2 78  ? 35.146  44.448  18.777  1.00 45.29 ? 78   ARG V C   1 
ATOM   4527 O O   . ARG D 2 78  ? 35.411  43.418  19.423  1.00 46.00 ? 78   ARG V O   1 
ATOM   4528 C CB  . ARG D 2 78  ? 35.123  46.974  18.443  1.00 42.61 ? 78   ARG V CB  1 
ATOM   4529 C CG  . ARG D 2 78  ? 36.150  48.053  18.498  1.00 40.80 ? 78   ARG V CG  1 
ATOM   4530 C CD  . ARG D 2 78  ? 36.059  48.943  17.291  1.00 39.18 ? 78   ARG V CD  1 
ATOM   4531 N NE  . ARG D 2 78  ? 37.378  49.441  16.924  1.00 37.42 ? 78   ARG V NE  1 
ATOM   4532 C CZ  . ARG D 2 78  ? 37.597  50.349  15.986  1.00 35.96 ? 78   ARG V CZ  1 
ATOM   4533 N NH1 . ARG D 2 78  ? 36.570  50.861  15.327  1.00 35.59 ? 78   ARG V NH1 1 
ATOM   4534 N NH2 . ARG D 2 78  ? 38.838  50.741  15.713  1.00 35.24 ? 78   ARG V NH2 1 
ATOM   4535 N N   . PRO D 2 79  ? 34.726  44.394  17.500  1.00 46.59 ? 79   PRO V N   1 
ATOM   4536 C CA  . PRO D 2 79  ? 33.637  43.582  16.917  1.00 47.61 ? 79   PRO V CA  1 
ATOM   4537 C C   . PRO D 2 79  ? 33.650  42.052  17.235  1.00 48.56 ? 79   PRO V C   1 
ATOM   4538 O O   . PRO D 2 79  ? 33.379  41.651  18.391  1.00 48.82 ? 79   PRO V O   1 
ATOM   4539 C CB  . PRO D 2 79  ? 33.829  43.817  15.413  1.00 47.83 ? 79   PRO V CB  1 
ATOM   4540 C CG  . PRO D 2 79  ? 35.375  43.831  15.270  1.00 47.69 ? 79   PRO V CG  1 
ATOM   4541 C CD  . PRO D 2 79  ? 35.915  44.372  16.610  1.00 46.74 ? 79   PRO V CD  1 
ATOM   4542 N N   . ARG D 2 80  ? 33.924  41.220  16.211  1.00 49.09 ? 80   ARG V N   1 
ATOM   4543 C CA  . ARG D 2 80  ? 34.097  39.763  16.366  1.00 49.37 ? 80   ARG V CA  1 
ATOM   4544 C C   . ARG D 2 80  ? 34.884  39.500  17.659  1.00 49.75 ? 80   ARG V C   1 
ATOM   4545 O O   . ARG D 2 80  ? 35.895  40.161  17.900  1.00 49.81 ? 80   ARG V O   1 
ATOM   4546 C CB  . ARG D 2 80  ? 34.821  39.140  15.147  1.00 49.39 ? 80   ARG V CB  1 
ATOM   4547 C CG  . ARG D 2 80  ? 33.919  38.414  14.115  1.00 48.62 ? 80   ARG V CG  1 
ATOM   4548 C CD  . ARG D 2 80  ? 34.729  37.728  13.009  1.00 46.91 ? 80   ARG V CD  1 
ATOM   4549 N NE  . ARG D 2 80  ? 33.933  37.525  11.792  1.00 46.85 ? 80   ARG V NE  1 
ATOM   4550 C CZ  . ARG D 2 80  ? 34.430  37.292  10.569  1.00 46.48 ? 80   ARG V CZ  1 
ATOM   4551 N NH1 . ARG D 2 80  ? 35.740  37.223  10.356  1.00 45.62 ? 80   ARG V NH1 1 
ATOM   4552 N NH2 . ARG D 2 80  ? 33.611  37.131  9.538   1.00 46.21 ? 80   ARG V NH2 1 
ATOM   4553 N N   . PRO D 2 81  ? 34.410  38.547  18.497  1.00 49.97 ? 81   PRO V N   1 
ATOM   4554 C CA  . PRO D 2 81  ? 34.855  38.356  19.884  1.00 49.67 ? 81   PRO V CA  1 
ATOM   4555 C C   . PRO D 2 81  ? 36.341  38.058  20.026  1.00 49.58 ? 81   PRO V C   1 
ATOM   4556 O O   . PRO D 2 81  ? 36.935  37.473  19.125  1.00 49.70 ? 81   PRO V O   1 
ATOM   4557 C CB  . PRO D 2 81  ? 34.041  37.142  20.332  1.00 49.66 ? 81   PRO V CB  1 
ATOM   4558 C CG  . PRO D 2 81  ? 32.844  37.149  19.454  1.00 49.55 ? 81   PRO V CG  1 
ATOM   4559 C CD  . PRO D 2 81  ? 33.389  37.542  18.131  1.00 50.15 ? 81   PRO V CD  1 
ATOM   4560 N N   . TYR D 2 93  ? 50.513  19.712  20.416  1.00 37.60 ? 93   TYR V N   1 
ATOM   4561 C CA  . TYR D 2 93  ? 49.081  19.519  20.258  1.00 37.49 ? 93   TYR V CA  1 
ATOM   4562 C C   . TYR D 2 93  ? 48.474  18.967  21.550  1.00 37.02 ? 93   TYR V C   1 
ATOM   4563 O O   . TYR D 2 93  ? 47.310  19.244  21.858  1.00 36.98 ? 93   TYR V O   1 
ATOM   4564 C CB  . TYR D 2 93  ? 48.793  18.594  19.076  1.00 37.86 ? 93   TYR V CB  1 
ATOM   4565 C CG  . TYR D 2 93  ? 47.655  19.062  18.194  1.00 39.66 ? 93   TYR V CG  1 
ATOM   4566 C CD1 . TYR D 2 93  ? 46.738  20.019  18.657  1.00 40.71 ? 93   TYR V CD1 1 
ATOM   4567 C CD2 . TYR D 2 93  ? 47.478  18.540  16.897  1.00 40.93 ? 93   TYR V CD2 1 
ATOM   4568 C CE1 . TYR D 2 93  ? 45.671  20.458  17.863  1.00 41.60 ? 93   TYR V CE1 1 
ATOM   4569 C CE2 . TYR D 2 93  ? 46.406  18.976  16.085  1.00 41.96 ? 93   TYR V CE2 1 
ATOM   4570 C CZ  . TYR D 2 93  ? 45.506  19.938  16.586  1.00 42.48 ? 93   TYR V CZ  1 
ATOM   4571 O OH  . TYR D 2 93  ? 44.447  20.393  15.826  1.00 42.93 ? 93   TYR V OH  1 
ATOM   4572 N N   . LEU D 2 94  ? 49.274  18.170  22.266  1.00 36.38 ? 94   LEU V N   1 
ATOM   4573 C CA  . LEU D 2 94  ? 49.082  17.789  23.681  1.00 35.85 ? 94   LEU V CA  1 
ATOM   4574 C C   . LEU D 2 94  ? 47.673  17.435  24.174  1.00 36.02 ? 94   LEU V C   1 
ATOM   4575 O O   . LEU D 2 94  ? 46.748  18.254  24.113  1.00 36.10 ? 94   LEU V O   1 
ATOM   4576 C CB  . LEU D 2 94  ? 49.690  18.858  24.596  1.00 35.47 ? 94   LEU V CB  1 
ATOM   4577 C CG  . LEU D 2 94  ? 50.112  18.411  25.989  1.00 34.52 ? 94   LEU V CG  1 
ATOM   4578 C CD1 . LEU D 2 94  ? 51.241  17.418  25.873  1.00 34.08 ? 94   LEU V CD1 1 
ATOM   4579 C CD2 . LEU D 2 94  ? 50.547  19.594  26.797  1.00 33.16 ? 94   LEU V CD2 1 
ATOM   4580 N N   . GLU D 2 95  ? 47.539  16.216  24.698  1.00 36.15 ? 95   GLU V N   1 
ATOM   4581 C CA  . GLU D 2 95  ? 46.285  15.731  25.298  1.00 36.24 ? 95   GLU V CA  1 
ATOM   4582 C C   . GLU D 2 95  ? 46.303  15.783  26.830  1.00 36.01 ? 95   GLU V C   1 
ATOM   4583 O O   . GLU D 2 95  ? 47.260  15.331  27.454  1.00 35.98 ? 95   GLU V O   1 
ATOM   4584 C CB  . GLU D 2 95  ? 45.993  14.295  24.855  1.00 36.35 ? 95   GLU V CB  1 
ATOM   4585 C CG  . GLU D 2 95  ? 44.716  13.709  25.484  1.00 36.99 ? 95   GLU V CG  1 
ATOM   4586 C CD  . GLU D 2 95  ? 44.593  12.199  25.329  1.00 37.50 ? 95   GLU V CD  1 
ATOM   4587 O OE1 . GLU D 2 95  ? 43.500  11.677  25.646  1.00 37.39 ? 95   GLU V OE1 1 
ATOM   4588 O OE2 . GLU D 2 95  ? 45.575  11.541  24.901  1.00 37.19 ? 95   GLU V OE2 1 
ATOM   4589 N N   . CYS D 2 96  ? 45.232  16.308  27.425  1.00 35.76 ? 96   CYS V N   1 
ATOM   4590 C CA  . CYS D 2 96  ? 45.137  16.424  28.875  1.00 35.54 ? 96   CYS V CA  1 
ATOM   4591 C C   . CYS D 2 96  ? 43.908  15.770  29.430  1.00 35.42 ? 96   CYS V C   1 
ATOM   4592 O O   . CYS D 2 96  ? 42.966  15.466  28.709  1.00 35.37 ? 96   CYS V O   1 
ATOM   4593 C CB  . CYS D 2 96  ? 45.106  17.882  29.288  1.00 35.36 ? 96   CYS V CB  1 
ATOM   4594 S SG  . CYS D 2 96  ? 46.335  18.814  28.445  1.00 36.16 ? 96   CYS V SG  1 
ATOM   4595 N N   . ALA D 2 97  ? 43.929  15.571  30.740  1.00 35.34 ? 97   ALA V N   1 
ATOM   4596 C CA  . ALA D 2 97  ? 42.739  15.207  31.471  1.00 35.28 ? 97   ALA V CA  1 
ATOM   4597 C C   . ALA D 2 97  ? 41.888  16.447  31.533  1.00 35.09 ? 97   ALA V C   1 
ATOM   4598 O O   . ALA D 2 97  ? 42.411  17.552  31.443  1.00 35.09 ? 97   ALA V O   1 
ATOM   4599 C CB  . ALA D 2 97  ? 43.100  14.770  32.859  1.00 35.32 ? 97   ALA V CB  1 
ATOM   4600 N N   . SER D 2 98  ? 40.584  16.268  31.668  1.00 34.85 ? 98   SER V N   1 
ATOM   4601 C CA  . SER D 2 98  ? 39.724  17.392  31.891  1.00 35.13 ? 98   SER V CA  1 
ATOM   4602 C C   . SER D 2 98  ? 38.568  17.045  32.793  1.00 35.59 ? 98   SER V C   1 
ATOM   4603 O O   . SER D 2 98  ? 37.839  16.102  32.535  1.00 35.75 ? 98   SER V O   1 
ATOM   4604 C CB  . SER D 2 98  ? 39.208  17.937  30.576  1.00 35.05 ? 98   SER V CB  1 
ATOM   4605 O OG  . SER D 2 98  ? 38.084  18.774  30.798  1.00 35.60 ? 98   SER V OG  1 
ATOM   4606 N N   . CYS D 2 99  ? 38.390  17.828  33.851  1.00 36.26 ? 99   CYS V N   1 
ATOM   4607 C CA  . CYS D 2 99  ? 37.285  17.612  34.776  1.00 36.72 ? 99   CYS V CA  1 
ATOM   4608 C C   . CYS D 2 99  ? 36.841  18.923  35.372  1.00 35.70 ? 99   CYS V C   1 
ATOM   4609 O O   . CYS D 2 99  ? 37.494  19.945  35.217  1.00 35.12 ? 99   CYS V O   1 
ATOM   4610 C CB  . CYS D 2 99  ? 37.696  16.645  35.903  1.00 37.49 ? 99   CYS V CB  1 
ATOM   4611 S SG  . CYS D 2 99  ? 38.321  17.447  37.446  1.00 41.98 ? 99   CYS V SG  1 
ATOM   4612 N N   . THR D 2 100 ? 35.740  18.865  36.090  1.00 35.34 ? 100  THR V N   1 
ATOM   4613 C CA  . THR D 2 100 ? 35.250  20.004  36.805  1.00 35.84 ? 100  THR V CA  1 
ATOM   4614 C C   . THR D 2 100 ? 34.645  19.540  38.124  1.00 36.13 ? 100  THR V C   1 
ATOM   4615 O O   . THR D 2 100 ? 33.778  18.681  38.146  1.00 36.54 ? 100  THR V O   1 
ATOM   4616 C CB  . THR D 2 100 ? 34.264  20.824  35.899  1.00 36.02 ? 100  THR V CB  1 
ATOM   4617 O OG1 . THR D 2 100 ? 34.896  22.044  35.516  1.00 37.09 ? 100  THR V OG1 1 
ATOM   4618 C CG2 . THR D 2 100 ? 32.946  21.176  36.569  1.00 35.43 ? 100  THR V CG2 1 
ATOM   4619 N N   . SER D 2 101 ? 35.117  20.085  39.233  1.00 36.23 ? 101  SER V N   1 
ATOM   4620 C CA  . SER D 2 101 ? 34.420  19.899  40.490  1.00 36.27 ? 101  SER V CA  1 
ATOM   4621 C C   . SER D 2 101 ? 32.910  20.052  40.344  1.00 36.52 ? 101  SER V C   1 
ATOM   4622 O O   . SER D 2 101 ? 32.173  19.460  41.097  1.00 36.83 ? 101  SER V O   1 
ATOM   4623 C CB  . SER D 2 101 ? 34.924  20.903  41.523  1.00 36.29 ? 101  SER V CB  1 
ATOM   4624 O OG  . SER D 2 101 ? 33.850  21.576  42.170  1.00 36.37 ? 101  SER V OG  1 
ATOM   4625 N N   . LEU D 2 102 ? 32.448  20.840  39.381  1.00 37.18 ? 102  LEU V N   1 
ATOM   4626 C CA  . LEU D 2 102 ? 31.056  21.276  39.364  1.00 38.18 ? 102  LEU V CA  1 
ATOM   4627 C C   . LEU D 2 102 ? 30.058  20.166  39.180  1.00 39.18 ? 102  LEU V C   1 
ATOM   4628 O O   . LEU D 2 102 ? 28.965  20.212  39.740  1.00 39.31 ? 102  LEU V O   1 
ATOM   4629 C CB  . LEU D 2 102 ? 30.825  22.339  38.295  1.00 37.97 ? 102  LEU V CB  1 
ATOM   4630 C CG  . LEU D 2 102 ? 29.377  22.807  38.056  1.00 37.93 ? 102  LEU V CG  1 
ATOM   4631 C CD1 . LEU D 2 102 ? 28.533  23.004  39.350  1.00 37.16 ? 102  LEU V CD1 1 
ATOM   4632 C CD2 . LEU D 2 102 ? 29.385  24.072  37.207  1.00 37.10 ? 102  LEU V CD2 1 
ATOM   4633 N N   . ASP D 2 103 ? 30.434  19.187  38.371  1.00 40.80 ? 103  ASP V N   1 
ATOM   4634 C CA  . ASP D 2 103 ? 29.583  18.042  38.048  1.00 42.24 ? 103  ASP V CA  1 
ATOM   4635 C C   . ASP D 2 103 ? 29.685  16.915  39.108  1.00 42.86 ? 103  ASP V C   1 
ATOM   4636 O O   . ASP D 2 103 ? 28.836  16.011  39.147  1.00 43.12 ? 103  ASP V O   1 
ATOM   4637 C CB  . ASP D 2 103 ? 29.943  17.558  36.632  1.00 42.33 ? 103  ASP V CB  1 
ATOM   4638 C CG  . ASP D 2 103 ? 30.107  16.036  36.527  1.00 44.13 ? 103  ASP V CG  1 
ATOM   4639 O OD1 . ASP D 2 103 ? 30.607  15.377  37.474  1.00 43.37 ? 103  ASP V OD1 1 
ATOM   4640 O OD2 . ASP D 2 103 ? 29.752  15.488  35.457  1.00 47.13 ? 103  ASP V OD2 1 
ATOM   4641 N N   . GLN D 2 104 ? 30.680  17.041  39.999  1.00 43.46 ? 104  GLN V N   1 
ATOM   4642 C CA  . GLN D 2 104 ? 31.265  15.949  40.809  1.00 43.65 ? 104  GLN V CA  1 
ATOM   4643 C C   . GLN D 2 104 ? 32.145  15.124  39.864  1.00 44.04 ? 104  GLN V C   1 
ATOM   4644 O O   . GLN D 2 104 ? 32.202  13.902  39.943  1.00 44.29 ? 104  GLN V O   1 
ATOM   4645 C CB  . GLN D 2 104 ? 30.204  15.091  41.527  1.00 43.56 ? 104  GLN V CB  1 
ATOM   4646 C CG  . GLN D 2 104 ? 29.341  15.835  42.558  1.00 43.37 ? 104  GLN V CG  1 
ATOM   4647 C CD  . GLN D 2 104 ? 28.358  16.824  41.924  1.00 42.42 ? 104  GLN V CD  1 
ATOM   4648 O OE1 . GLN D 2 104 ? 28.551  18.040  41.987  1.00 40.90 ? 104  GLN V OE1 1 
ATOM   4649 N NE2 . GLN D 2 104 ? 27.315  16.299  41.291  1.00 41.98 ? 104  GLN V NE2 1 
ATOM   4650 N N   . SER D 2 105 ? 32.844  15.836  38.980  1.00 44.50 ? 105  SER V N   1 
ATOM   4651 C CA  . SER D 2 105 ? 33.414  15.291  37.744  1.00 44.86 ? 105  SER V CA  1 
ATOM   4652 C C   . SER D 2 105 ? 34.793  14.671  37.859  1.00 44.95 ? 105  SER V C   1 
ATOM   4653 O O   . SER D 2 105 ? 35.135  13.812  37.061  1.00 44.59 ? 105  SER V O   1 
ATOM   4654 C CB  . SER D 2 105 ? 33.400  16.372  36.641  1.00 45.07 ? 105  SER V CB  1 
ATOM   4655 O OG  . SER D 2 105 ? 34.458  16.238  35.704  1.00 45.74 ? 105  SER V OG  1 
ATOM   4656 N N   . CYS D 2 106 ? 35.595  15.114  38.820  1.00 45.52 ? 106  CYS V N   1 
ATOM   4657 C CA  . CYS D 2 106 ? 36.918  14.518  38.981  1.00 46.21 ? 106  CYS V CA  1 
ATOM   4658 C C   . CYS D 2 106 ? 36.888  13.180  39.678  1.00 46.72 ? 106  CYS V C   1 
ATOM   4659 O O   . CYS D 2 106 ? 37.036  12.141  39.027  1.00 46.72 ? 106  CYS V O   1 
ATOM   4660 C CB  . CYS D 2 106 ? 37.893  15.456  39.666  1.00 45.88 ? 106  CYS V CB  1 
ATOM   4661 S SG  . CYS D 2 106 ? 39.180  15.922  38.502  1.00 46.47 ? 106  CYS V SG  1 
ATOM   4662 N N   . GLU D 2 107 ? 36.699  13.227  40.997  1.00 47.53 ? 107  GLU V N   1 
ATOM   4663 C CA  . GLU D 2 107 ? 36.526  12.046  41.866  1.00 48.24 ? 107  GLU V CA  1 
ATOM   4664 C C   . GLU D 2 107 ? 36.540  10.673  41.139  1.00 48.12 ? 107  GLU V C   1 
ATOM   4665 O O   . GLU D 2 107 ? 37.475  9.868   41.343  1.00 48.12 ? 107  GLU V O   1 
ATOM   4666 C CB  . GLU D 2 107 ? 35.279  12.212  42.767  1.00 48.46 ? 107  GLU V CB  1 
ATOM   4667 C CG  . GLU D 2 107 ? 35.241  13.525  43.578  1.00 50.08 ? 107  GLU V CG  1 
ATOM   4668 C CD  . GLU D 2 107 ? 34.600  14.691  42.798  1.00 53.21 ? 107  GLU V CD  1 
ATOM   4669 O OE1 . GLU D 2 107 ? 33.352  14.797  42.815  1.00 54.78 ? 107  GLU V OE1 1 
ATOM   4670 O OE2 . GLU D 2 107 ? 35.332  15.506  42.173  1.00 53.44 ? 107  GLU V OE2 1 
ATOM   4671 N N   . ARG D 2 108 ? 35.537  10.434  40.281  1.00 47.68 ? 108  ARG V N   1 
ATOM   4672 C CA  . ARG D 2 108 ? 35.341  9.138   39.594  1.00 47.35 ? 108  ARG V CA  1 
ATOM   4673 C C   . ARG D 2 108 ? 36.606  8.537   38.969  1.00 46.95 ? 108  ARG V C   1 
ATOM   4674 O O   . ARG D 2 108 ? 37.071  7.466   39.389  1.00 47.00 ? 108  ARG V O   1 
ATOM   4675 C CB  . ARG D 2 108 ? 34.247  9.238   38.527  1.00 47.41 ? 108  ARG V CB  1 
ATOM   4676 C CG  . ARG D 2 108 ? 33.110  10.203  38.840  1.00 47.85 ? 108  ARG V CG  1 
ATOM   4677 C CD  . ARG D 2 108 ? 32.264  9.724   39.993  1.00 48.71 ? 108  ARG V CD  1 
ATOM   4678 N NE  . ARG D 2 108 ? 31.217  10.685  40.309  1.00 49.22 ? 108  ARG V NE  1 
ATOM   4679 C CZ  . ARG D 2 108 ? 30.346  10.551  41.307  1.00 49.90 ? 108  ARG V CZ  1 
ATOM   4680 N NH1 . ARG D 2 108 ? 30.380  9.488   42.109  1.00 49.18 ? 108  ARG V NH1 1 
ATOM   4681 N NH2 . ARG D 2 108 ? 29.432  11.492  41.504  1.00 50.26 ? 108  ARG V NH2 1 
ATOM   4682 N N   . GLY D 2 109 ? 37.159  9.229   37.975  1.00 46.32 ? 109  GLY V N   1 
ATOM   4683 C CA  . GLY D 2 109 ? 38.369  8.764   37.303  1.00 45.69 ? 109  GLY V CA  1 
ATOM   4684 C C   . GLY D 2 109 ? 38.072  8.083   35.981  1.00 45.14 ? 109  GLY V C   1 
ATOM   4685 O O   . GLY D 2 109 ? 38.909  7.341   35.449  1.00 45.22 ? 109  GLY V O   1 
ATOM   4686 N N   . ARG D 2 110 ? 36.859  8.314   35.479  1.00 44.41 ? 110  ARG V N   1 
ATOM   4687 C CA  . ARG D 2 110 ? 36.496  8.042   34.081  1.00 43.50 ? 110  ARG V CA  1 
ATOM   4688 C C   . ARG D 2 110 ? 36.439  9.356   33.281  1.00 42.68 ? 110  ARG V C   1 
ATOM   4689 O O   . ARG D 2 110 ? 35.584  9.501   32.405  1.00 42.43 ? 110  ARG V O   1 
ATOM   4690 C CB  . ARG D 2 110 ? 35.154  7.275   33.968  1.00 43.67 ? 110  ARG V CB  1 
ATOM   4691 C CG  . ARG D 2 110 ? 34.046  7.610   35.004  1.00 43.88 ? 110  ARG V CG  1 
ATOM   4692 C CD  . ARG D 2 110 ? 33.478  9.052   34.912  1.00 44.18 ? 110  ARG V CD  1 
ATOM   4693 N NE  . ARG D 2 110 ? 34.363  10.039  35.546  1.00 44.17 ? 110  ARG V NE  1 
ATOM   4694 C CZ  . ARG D 2 110 ? 34.774  11.183  34.997  1.00 43.83 ? 110  ARG V CZ  1 
ATOM   4695 N NH1 . ARG D 2 110 ? 34.375  11.547  33.791  1.00 44.46 ? 110  ARG V NH1 1 
ATOM   4696 N NH2 . ARG D 2 110 ? 35.594  11.975  35.661  1.00 43.99 ? 110  ARG V NH2 1 
ATOM   4697 N N   . GLU D 2 111 ? 37.361  10.279  33.610  1.00 41.71 ? 111  GLU V N   1 
ATOM   4698 C CA  . GLU D 2 111 ? 37.477  11.681  33.119  1.00 40.59 ? 111  GLU V CA  1 
ATOM   4699 C C   . GLU D 2 111 ? 37.118  12.000  31.670  1.00 39.58 ? 111  GLU V C   1 
ATOM   4700 O O   . GLU D 2 111 ? 36.415  11.248  31.017  1.00 39.85 ? 111  GLU V O   1 
ATOM   4701 C CB  . GLU D 2 111 ? 38.876  12.214  33.422  1.00 40.73 ? 111  GLU V CB  1 
ATOM   4702 C CG  . GLU D 2 111 ? 39.010  12.675  34.849  1.00 42.58 ? 111  GLU V CG  1 
ATOM   4703 C CD  . GLU D 2 111 ? 40.307  13.416  35.133  1.00 44.47 ? 111  GLU V CD  1 
ATOM   4704 O OE1 . GLU D 2 111 ? 40.246  14.658  35.285  1.00 43.71 ? 111  GLU V OE1 1 
ATOM   4705 O OE2 . GLU D 2 111 ? 41.374  12.754  35.221  1.00 45.95 ? 111  GLU V OE2 1 
ATOM   4706 N N   . GLN D 2 112 ? 37.605  13.118  31.155  1.00 38.28 ? 112  GLN V N   1 
ATOM   4707 C CA  . GLN D 2 112 ? 37.112  13.595  29.872  1.00 37.15 ? 112  GLN V CA  1 
ATOM   4708 C C   . GLN D 2 112 ? 38.167  14.166  28.939  1.00 36.85 ? 112  GLN V C   1 
ATOM   4709 O O   . GLN D 2 112 ? 37.817  14.895  28.006  1.00 36.56 ? 112  GLN V O   1 
ATOM   4710 C CB  . GLN D 2 112 ? 36.002  14.632  30.092  1.00 37.12 ? 112  GLN V CB  1 
ATOM   4711 C CG  . GLN D 2 112 ? 34.605  14.078  30.335  1.00 35.77 ? 112  GLN V CG  1 
ATOM   4712 C CD  . GLN D 2 112 ? 33.847  13.853  29.053  1.00 34.14 ? 112  GLN V CD  1 
ATOM   4713 O OE1 . GLN D 2 112 ? 34.234  13.032  28.228  1.00 35.04 ? 112  GLN V OE1 1 
ATOM   4714 N NE2 . GLN D 2 112 ? 32.761  14.576  28.878  1.00 32.62 ? 112  GLN V NE2 1 
ATOM   4715 N N   . SER D 2 113 ? 39.437  13.859  29.204  1.00 36.50 ? 113  SER V N   1 
ATOM   4716 C CA  . SER D 2 113 ? 40.565  14.159  28.301  1.00 36.63 ? 113  SER V CA  1 
ATOM   4717 C C   . SER D 2 113 ? 40.245  14.851  26.961  1.00 36.83 ? 113  SER V C   1 
ATOM   4718 O O   . SER D 2 113 ? 39.487  14.309  26.149  1.00 37.02 ? 113  SER V O   1 
ATOM   4719 C CB  . SER D 2 113 ? 41.291  12.857  27.960  1.00 36.66 ? 113  SER V CB  1 
ATOM   4720 O OG  . SER D 2 113 ? 40.569  12.109  26.990  1.00 35.77 ? 113  SER V OG  1 
ATOM   4721 N N   . LEU D 2 114 ? 40.845  16.016  26.706  1.00 36.78 ? 114  LEU V N   1 
ATOM   4722 C CA  . LEU D 2 114 ? 40.716  16.669  25.388  1.00 36.58 ? 114  LEU V CA  1 
ATOM   4723 C C   . LEU D 2 114 ? 42.048  17.179  24.840  1.00 36.61 ? 114  LEU V C   1 
ATOM   4724 O O   . LEU D 2 114 ? 42.990  17.428  25.594  1.00 36.68 ? 114  LEU V O   1 
ATOM   4725 C CB  . LEU D 2 114 ? 39.667  17.790  25.414  1.00 36.60 ? 114  LEU V CB  1 
ATOM   4726 C CG  . LEU D 2 114 ? 40.019  19.251  25.735  1.00 36.16 ? 114  LEU V CG  1 
ATOM   4727 C CD1 . LEU D 2 114 ? 38.828  20.170  25.427  1.00 35.59 ? 114  LEU V CD1 1 
ATOM   4728 C CD2 . LEU D 2 114 ? 40.470  19.427  27.172  1.00 35.62 ? 114  LEU V CD2 1 
ATOM   4729 N N   . GLN D 2 115 ? 42.118  17.336  23.525  1.00 36.52 ? 115  GLN V N   1 
ATOM   4730 C CA  . GLN D 2 115 ? 43.335  17.819  22.893  1.00 36.52 ? 115  GLN V CA  1 
ATOM   4731 C C   . GLN D 2 115 ? 43.425  19.330  22.983  1.00 36.67 ? 115  GLN V C   1 
ATOM   4732 O O   . GLN D 2 115 ? 42.412  20.016  22.926  1.00 36.48 ? 115  GLN V O   1 
ATOM   4733 C CB  . GLN D 2 115 ? 43.382  17.367  21.440  1.00 36.48 ? 115  GLN V CB  1 
ATOM   4734 C CG  . GLN D 2 115 ? 44.492  17.994  20.630  1.00 35.90 ? 115  GLN V CG  1 
ATOM   4735 C CD  . GLN D 2 115 ? 45.172  16.996  19.736  1.00 34.89 ? 115  GLN V CD  1 
ATOM   4736 O OE1 . GLN D 2 115 ? 45.844  16.078  20.211  1.00 34.19 ? 115  GLN V OE1 1 
ATOM   4737 N NE2 . GLN D 2 115 ? 45.005  17.163  18.431  1.00 34.38 ? 115  GLN V NE2 1 
ATOM   4738 N N   . CYS D 2 116 ? 44.642  19.842  23.122  1.00 37.07 ? 116  CYS V N   1 
ATOM   4739 C CA  . CYS D 2 116 ? 44.859  21.283  23.192  1.00 37.85 ? 116  CYS V CA  1 
ATOM   4740 C C   . CYS D 2 116 ? 44.776  21.930  21.821  1.00 38.42 ? 116  CYS V C   1 
ATOM   4741 O O   . CYS D 2 116 ? 45.214  21.323  20.853  1.00 38.99 ? 116  CYS V O   1 
ATOM   4742 C CB  . CYS D 2 116 ? 46.228  21.566  23.784  1.00 37.50 ? 116  CYS V CB  1 
ATOM   4743 S SG  . CYS D 2 116 ? 46.279  21.829  25.583  1.00 38.33 ? 116  CYS V SG  1 
ATOM   4744 N N   . ARG D 2 117 ? 44.217  23.143  21.731  1.00 39.00 ? 117  ARG V N   1 
ATOM   4745 C CA  . ARG D 2 117 ? 44.217  23.899  20.472  1.00 39.59 ? 117  ARG V CA  1 
ATOM   4746 C C   . ARG D 2 117 ? 45.652  24.227  20.076  1.00 39.85 ? 117  ARG V C   1 
ATOM   4747 O O   . ARG D 2 117 ? 46.232  23.542  19.221  1.00 40.32 ? 117  ARG V O   1 
ATOM   4748 C CB  . ARG D 2 117 ? 43.359  25.181  20.522  1.00 39.57 ? 117  ARG V CB  1 
ATOM   4749 C CG  . ARG D 2 117 ? 41.846  24.977  20.231  1.00 41.69 ? 117  ARG V CG  1 
ATOM   4750 C CD  . ARG D 2 117 ? 41.240  25.957  19.137  1.00 43.99 ? 117  ARG V CD  1 
ATOM   4751 N NE  . ARG D 2 117 ? 41.172  25.379  17.771  1.00 43.70 ? 117  ARG V NE  1 
ATOM   4752 C CZ  . ARG D 2 117 ? 41.346  26.056  16.628  1.00 42.43 ? 117  ARG V CZ  1 
ATOM   4753 N NH1 . ARG D 2 117 ? 41.606  27.361  16.636  1.00 40.89 ? 117  ARG V NH1 1 
ATOM   4754 N NH2 . ARG D 2 117 ? 41.270  25.417  15.465  1.00 41.61 ? 117  ARG V NH2 1 
ATOM   4755 N N   . TYR D 2 118 ? 46.235  25.236  20.723  1.00 39.91 ? 118  TYR V N   1 
ATOM   4756 C CA  . TYR D 2 118 ? 47.501  25.819  20.272  1.00 40.07 ? 118  TYR V CA  1 
ATOM   4757 C C   . TYR D 2 118 ? 48.721  25.170  20.884  1.00 39.79 ? 118  TYR V C   1 
ATOM   4758 O O   . TYR D 2 118 ? 48.862  25.197  22.098  1.00 40.12 ? 118  TYR V O   1 
ATOM   4759 C CB  . TYR D 2 118 ? 47.518  27.303  20.605  1.00 40.18 ? 118  TYR V CB  1 
ATOM   4760 C CG  . TYR D 2 118 ? 46.235  27.995  20.230  1.00 41.61 ? 118  TYR V CG  1 
ATOM   4761 C CD1 . TYR D 2 118 ? 45.848  28.108  18.891  1.00 42.49 ? 118  TYR V CD1 1 
ATOM   4762 C CD2 . TYR D 2 118 ? 45.397  28.533  21.213  1.00 42.92 ? 118  TYR V CD2 1 
ATOM   4763 C CE1 . TYR D 2 118 ? 44.665  28.741  18.536  1.00 43.34 ? 118  TYR V CE1 1 
ATOM   4764 C CE2 . TYR D 2 118 ? 44.213  29.176  20.873  1.00 43.14 ? 118  TYR V CE2 1 
ATOM   4765 C CZ  . TYR D 2 118 ? 43.858  29.275  19.532  1.00 44.08 ? 118  TYR V CZ  1 
ATOM   4766 O OH  . TYR D 2 118 ? 42.694  29.906  19.177  1.00 45.68 ? 118  TYR V OH  1 
ATOM   4767 N N   . PRO D 2 119 ? 49.606  24.570  20.059  1.00 39.52 ? 119  PRO V N   1 
ATOM   4768 C CA  . PRO D 2 119 ? 50.898  24.212  20.667  1.00 39.32 ? 119  PRO V CA  1 
ATOM   4769 C C   . PRO D 2 119 ? 51.578  25.416  21.369  1.00 38.84 ? 119  PRO V C   1 
ATOM   4770 O O   . PRO D 2 119 ? 52.223  26.233  20.714  1.00 38.53 ? 119  PRO V O   1 
ATOM   4771 C CB  . PRO D 2 119 ? 51.706  23.656  19.475  1.00 39.28 ? 119  PRO V CB  1 
ATOM   4772 C CG  . PRO D 2 119 ? 50.640  22.981  18.619  1.00 39.18 ? 119  PRO V CG  1 
ATOM   4773 C CD  . PRO D 2 119 ? 49.382  23.850  18.781  1.00 39.58 ? 119  PRO V CD  1 
ATOM   4774 N N   . THR D 2 120 ? 51.403  25.482  22.699  1.00 38.39 ? 120  THR V N   1 
ATOM   4775 C CA  . THR D 2 120 ? 51.712  26.631  23.596  1.00 37.97 ? 120  THR V CA  1 
ATOM   4776 C C   . THR D 2 120 ? 50.597  26.739  24.655  1.00 37.53 ? 120  THR V C   1 
ATOM   4777 O O   . THR D 2 120 ? 50.411  27.756  25.333  1.00 37.23 ? 120  THR V O   1 
ATOM   4778 C CB  . THR D 2 120 ? 51.847  27.999  22.867  1.00 38.11 ? 120  THR V CB  1 
ATOM   4779 O OG1 . THR D 2 120 ? 50.789  28.149  21.901  1.00 38.32 ? 120  THR V OG1 1 
ATOM   4780 C CG2 . THR D 2 120 ? 53.246  28.157  22.213  1.00 37.53 ? 120  THR V CG2 1 
ATOM   4781 N N   . GLU D 2 121 ? 49.837  25.665  24.766  1.00 37.10 ? 121  GLU V N   1 
ATOM   4782 C CA  . GLU D 2 121 ? 48.744  25.576  25.708  1.00 36.45 ? 121  GLU V CA  1 
ATOM   4783 C C   . GLU D 2 121 ? 49.083  24.339  26.540  1.00 36.30 ? 121  GLU V C   1 
ATOM   4784 O O   . GLU D 2 121 ? 49.340  23.258  26.004  1.00 36.29 ? 121  GLU V O   1 
ATOM   4785 C CB  . GLU D 2 121 ? 47.434  25.406  24.940  1.00 36.21 ? 121  GLU V CB  1 
ATOM   4786 C CG  . GLU D 2 121 ? 46.162  25.650  25.695  1.00 35.36 ? 121  GLU V CG  1 
ATOM   4787 C CD  . GLU D 2 121 ? 44.943  25.517  24.804  1.00 34.64 ? 121  GLU V CD  1 
ATOM   4788 O OE1 . GLU D 2 121 ? 43.868  26.068  25.124  1.00 34.16 ? 121  GLU V OE1 1 
ATOM   4789 O OE2 . GLU D 2 121 ? 45.067  24.858  23.760  1.00 35.40 ? 121  GLU V OE2 1 
ATOM   4790 N N   . HIS D 2 122 ? 49.138  24.524  27.851  1.00 35.79 ? 122  HIS V N   1 
ATOM   4791 C CA  . HIS D 2 122 ? 49.545  23.477  28.770  1.00 34.96 ? 122  HIS V CA  1 
ATOM   4792 C C   . HIS D 2 122 ? 48.347  22.752  29.369  1.00 34.95 ? 122  HIS V C   1 
ATOM   4793 O O   . HIS D 2 122 ? 47.240  23.313  29.477  1.00 35.39 ? 122  HIS V O   1 
ATOM   4794 C CB  . HIS D 2 122 ? 50.347  24.097  29.899  1.00 34.61 ? 122  HIS V CB  1 
ATOM   4795 C CG  . HIS D 2 122 ? 51.488  24.940  29.434  1.00 34.12 ? 122  HIS V CG  1 
ATOM   4796 N ND1 . HIS D 2 122 ? 52.178  24.681  28.272  1.00 34.68 ? 122  HIS V ND1 1 
ATOM   4797 C CD2 . HIS D 2 122 ? 52.084  26.017  29.993  1.00 33.93 ? 122  HIS V CD2 1 
ATOM   4798 C CE1 . HIS D 2 122 ? 53.143  25.574  28.128  1.00 35.21 ? 122  HIS V CE1 1 
ATOM   4799 N NE2 . HIS D 2 122 ? 53.105  26.399  29.159  1.00 34.08 ? 122  HIS V NE2 1 
ATOM   4800 N N   . CYS D 2 123 ? 48.552  21.499  29.756  1.00 34.30 ? 123  CYS V N   1 
ATOM   4801 C CA  . CYS D 2 123 ? 47.580  20.867  30.614  1.00 33.71 ? 123  CYS V CA  1 
ATOM   4802 C C   . CYS D 2 123 ? 47.665  21.688  31.872  1.00 33.10 ? 123  CYS V C   1 
ATOM   4803 O O   . CYS D 2 123 ? 48.754  21.940  32.386  1.00 32.88 ? 123  CYS V O   1 
ATOM   4804 C CB  . CYS D 2 123 ? 47.931  19.413  30.900  1.00 33.89 ? 123  CYS V CB  1 
ATOM   4805 S SG  . CYS D 2 123 ? 48.054  18.391  29.452  1.00 34.35 ? 123  CYS V SG  1 
ATOM   4806 N N   . ILE D 2 124 ? 46.518  22.147  32.341  1.00 32.53 ? 124  ILE V N   1 
ATOM   4807 C CA  . ILE D 2 124 ? 46.497  22.950  33.539  1.00 31.82 ? 124  ILE V CA  1 
ATOM   4808 C C   . ILE D 2 124 ? 45.488  22.469  34.558  1.00 31.76 ? 124  ILE V C   1 
ATOM   4809 O O   . ILE D 2 124 ? 44.452  21.912  34.207  1.00 31.55 ? 124  ILE V O   1 
ATOM   4810 C CB  . ILE D 2 124 ? 46.214  24.406  33.218  1.00 31.57 ? 124  ILE V CB  1 
ATOM   4811 C CG1 . ILE D 2 124 ? 44.861  24.530  32.524  1.00 30.85 ? 124  ILE V CG1 1 
ATOM   4812 C CG2 . ILE D 2 124 ? 47.352  24.987  32.393  1.00 30.86 ? 124  ILE V CG2 1 
ATOM   4813 C CD1 . ILE D 2 124 ? 43.903  25.466  33.225  1.00 29.61 ? 124  ILE V CD1 1 
ATOM   4814 N N   . GLU D 2 125 ? 45.817  22.668  35.825  1.00 31.92 ? 125  GLU V N   1 
ATOM   4815 C CA  . GLU D 2 125 ? 44.832  22.496  36.878  1.00 32.61 ? 125  GLU V CA  1 
ATOM   4816 C C   . GLU D 2 125 ? 44.716  23.762  37.715  1.00 32.03 ? 125  GLU V C   1 
ATOM   4817 O O   . GLU D 2 125 ? 45.713  24.421  38.017  1.00 31.97 ? 125  GLU V O   1 
ATOM   4818 C CB  . GLU D 2 125 ? 45.153  21.287  37.762  1.00 32.98 ? 125  GLU V CB  1 
ATOM   4819 C CG  . GLU D 2 125 ? 43.941  20.785  38.582  1.00 35.86 ? 125  GLU V CG  1 
ATOM   4820 C CD  . GLU D 2 125 ? 44.163  19.397  39.235  1.00 40.35 ? 125  GLU V CD  1 
ATOM   4821 O OE1 . GLU D 2 125 ? 43.170  18.745  39.685  1.00 41.79 ? 125  GLU V OE1 1 
ATOM   4822 O OE2 . GLU D 2 125 ? 45.331  18.943  39.290  1.00 41.65 ? 125  GLU V OE2 1 
ATOM   4823 N N   . VAL D 2 126 ? 43.487  24.100  38.073  1.00 31.49 ? 126  VAL V N   1 
ATOM   4824 C CA  . VAL D 2 126 ? 43.232  25.255  38.895  1.00 31.16 ? 126  VAL V CA  1 
ATOM   4825 C C   . VAL D 2 126 ? 42.254  24.922  39.994  1.00 31.38 ? 126  VAL V C   1 
ATOM   4826 O O   . VAL D 2 126 ? 41.074  24.638  39.754  1.00 31.50 ? 126  VAL V O   1 
ATOM   4827 C CB  . VAL D 2 126 ? 42.689  26.441  38.092  1.00 31.01 ? 126  VAL V CB  1 
ATOM   4828 C CG1 . VAL D 2 126 ? 43.634  26.791  36.975  1.00 30.89 ? 126  VAL V CG1 1 
ATOM   4829 C CG2 . VAL D 2 126 ? 41.304  26.154  37.555  1.00 30.94 ? 126  VAL V CG2 1 
ATOM   4830 N N   . VAL D 2 127 ? 42.747  24.963  41.217  1.00 31.40 ? 127  VAL V N   1 
ATOM   4831 C CA  . VAL D 2 127 ? 41.877  24.710  42.333  1.00 31.47 ? 127  VAL V CA  1 
ATOM   4832 C C   . VAL D 2 127 ? 41.512  26.026  43.025  1.00 31.69 ? 127  VAL V C   1 
ATOM   4833 O O   . VAL D 2 127 ? 42.276  26.991  42.988  1.00 31.59 ? 127  VAL V O   1 
ATOM   4834 C CB  . VAL D 2 127 ? 42.487  23.655  43.253  1.00 31.22 ? 127  VAL V CB  1 
ATOM   4835 C CG1 . VAL D 2 127 ? 43.826  24.122  43.770  1.00 30.92 ? 127  VAL V CG1 1 
ATOM   4836 C CG2 . VAL D 2 127 ? 41.515  23.264  44.371  1.00 31.21 ? 127  VAL V CG2 1 
ATOM   4837 N N   . THR D 2 128 ? 40.318  26.063  43.607  1.00 32.13 ? 128  THR V N   1 
ATOM   4838 C CA  . THR D 2 128 ? 39.789  27.257  44.243  1.00 32.62 ? 128  THR V CA  1 
ATOM   4839 C C   . THR D 2 128 ? 38.901  26.877  45.422  1.00 33.12 ? 128  THR V C   1 
ATOM   4840 O O   . THR D 2 128 ? 37.695  26.707  45.302  1.00 33.21 ? 128  THR V O   1 
ATOM   4841 C CB  . THR D 2 128 ? 39.074  28.162  43.197  1.00 32.62 ? 128  THR V CB  1 
ATOM   4842 O OG1 . THR D 2 128 ? 40.057  28.953  42.516  1.00 32.28 ? 128  THR V OG1 1 
ATOM   4843 C CG2 . THR D 2 128 ? 38.043  29.091  43.839  1.00 32.26 ? 128  THR V CG2 1 
ATOM   4844 N N   . LEU D 2 129 ? 39.522  26.712  46.568  1.00 34.04 ? 129  LEU V N   1 
ATOM   4845 C CA  . LEU D 2 129 ? 38.775  26.361  47.743  1.00 35.34 ? 129  LEU V CA  1 
ATOM   4846 C C   . LEU D 2 129 ? 38.602  27.579  48.629  1.00 36.32 ? 129  LEU V C   1 
ATOM   4847 O O   . LEU D 2 129 ? 39.546  28.346  48.854  1.00 36.61 ? 129  LEU V O   1 
ATOM   4848 C CB  . LEU D 2 129 ? 39.493  25.266  48.517  1.00 35.48 ? 129  LEU V CB  1 
ATOM   4849 C CG  . LEU D 2 129 ? 39.494  23.824  48.012  1.00 35.96 ? 129  LEU V CG  1 
ATOM   4850 C CD1 . LEU D 2 129 ? 39.732  22.857  49.196  1.00 36.29 ? 129  LEU V CD1 1 
ATOM   4851 C CD2 . LEU D 2 129 ? 38.191  23.489  47.304  1.00 36.94 ? 129  LEU V CD2 1 
ATOM   4852 N N   . GLN D 2 130 ? 37.394  27.745  49.149  1.00 37.20 ? 130  GLN V N   1 
ATOM   4853 C CA  . GLN D 2 130 ? 37.101  28.885  49.997  1.00 38.10 ? 130  GLN V CA  1 
ATOM   4854 C C   . GLN D 2 130 ? 36.449  28.475  51.326  1.00 38.69 ? 130  GLN V C   1 
ATOM   4855 O O   . GLN D 2 130 ? 36.843  27.468  51.926  1.00 38.65 ? 130  GLN V O   1 
ATOM   4856 C CB  . GLN D 2 130 ? 36.268  29.910  49.217  1.00 38.05 ? 130  GLN V CB  1 
ATOM   4857 C CG  . GLN D 2 130 ? 35.326  29.315  48.189  1.00 38.31 ? 130  GLN V CG  1 
ATOM   4858 C CD  . GLN D 2 130 ? 34.835  30.335  47.155  1.00 39.01 ? 130  GLN V CD  1 
ATOM   4859 O OE1 . GLN D 2 130 ? 34.682  31.528  47.452  1.00 38.61 ? 130  GLN V OE1 1 
ATOM   4860 N NE2 . GLN D 2 130 ? 34.563  29.854  45.935  1.00 38.32 ? 130  GLN V NE2 1 
ATOM   4861 N N   . SER D 2 131 ? 35.483  29.270  51.788  1.00 39.33 ? 131  SER V N   1 
ATOM   4862 C CA  . SER D 2 131 ? 34.675  28.934  52.955  1.00 39.98 ? 131  SER V CA  1 
ATOM   4863 C C   . SER D 2 131 ? 33.256  29.495  52.840  1.00 40.52 ? 131  SER V C   1 
ATOM   4864 O O   . SER D 2 131 ? 33.074  30.689  52.599  1.00 40.49 ? 131  SER V O   1 
ATOM   4865 C CB  . SER D 2 131 ? 35.350  29.400  54.250  1.00 40.00 ? 131  SER V CB  1 
ATOM   4866 O OG  . SER D 2 131 ? 36.374  28.496  54.637  1.00 39.65 ? 131  SER V OG  1 
ATOM   4867 N N   . THR D 2 132 ? 32.277  28.600  53.008  1.00 41.24 ? 132  THR V N   1 
ATOM   4868 C CA  . THR D 2 132 ? 30.820  28.864  52.942  1.00 42.04 ? 132  THR V CA  1 
ATOM   4869 C C   . THR D 2 132 ? 30.349  30.166  52.303  1.00 42.51 ? 132  THR V C   1 
ATOM   4870 O O   . THR D 2 132 ? 29.829  30.145  51.180  1.00 43.04 ? 132  THR V O   1 
ATOM   4871 C CB  . THR D 2 132 ? 30.155  28.686  54.296  1.00 42.01 ? 132  THR V CB  1 
ATOM   4872 O OG1 . THR D 2 132 ? 31.177  28.486  55.281  1.00 42.97 ? 132  THR V OG1 1 
ATOM   4873 C CG2 . THR D 2 132 ? 29.237  27.465  54.272  1.00 42.58 ? 132  THR V CG2 1 
ATOM   4874 N N   . GLU D 2 133 ? 30.520  31.288  53.000  1.00 42.75 ? 133  GLU V N   1 
ATOM   4875 C CA  . GLU D 2 133 ? 30.187  32.599  52.436  1.00 42.94 ? 133  GLU V CA  1 
ATOM   4876 C C   . GLU D 2 133 ? 30.429  32.639  50.903  1.00 42.93 ? 133  GLU V C   1 
ATOM   4877 O O   . GLU D 2 133 ? 29.519  32.999  50.143  1.00 43.01 ? 133  GLU V O   1 
ATOM   4878 C CB  . GLU D 2 133 ? 30.935  33.720  53.182  1.00 43.08 ? 133  GLU V CB  1 
ATOM   4879 C CG  . GLU D 2 133 ? 30.482  33.937  54.651  1.00 43.81 ? 133  GLU V CG  1 
ATOM   4880 C CD  . GLU D 2 133 ? 31.355  34.938  55.437  1.00 44.78 ? 133  GLU V CD  1 
ATOM   4881 O OE1 . GLU D 2 133 ? 30.981  35.286  56.578  1.00 44.27 ? 133  GLU V OE1 1 
ATOM   4882 O OE2 . GLU D 2 133 ? 32.408  35.383  54.925  1.00 45.61 ? 133  GLU V OE2 1 
ATOM   4883 N N   . ARG D 2 134 ? 31.633  32.235  50.467  1.00 42.77 ? 134  ARG V N   1 
ATOM   4884 C CA  . ARG D 2 134 ? 31.975  32.066  49.044  1.00 42.49 ? 134  ARG V CA  1 
ATOM   4885 C C   . ARG D 2 134 ? 31.890  33.366  48.277  1.00 42.00 ? 134  ARG V C   1 
ATOM   4886 O O   . ARG D 2 134 ? 30.903  33.613  47.573  1.00 42.04 ? 134  ARG V O   1 
ATOM   4887 C CB  . ARG D 2 134 ? 31.060  31.033  48.368  1.00 42.91 ? 134  ARG V CB  1 
ATOM   4888 C CG  . ARG D 2 134 ? 31.729  29.752  47.922  1.00 44.07 ? 134  ARG V CG  1 
ATOM   4889 C CD  . ARG D 2 134 ? 30.743  28.589  47.907  1.00 46.13 ? 134  ARG V CD  1 
ATOM   4890 N NE  . ARG D 2 134 ? 31.428  27.295  47.847  1.00 47.95 ? 134  ARG V NE  1 
ATOM   4891 C CZ  . ARG D 2 134 ? 31.976  26.661  48.891  1.00 48.01 ? 134  ARG V CZ  1 
ATOM   4892 N NH1 . ARG D 2 134 ? 31.944  27.186  50.112  1.00 47.27 ? 134  ARG V NH1 1 
ATOM   4893 N NH2 . ARG D 2 134 ? 32.575  25.491  48.707  1.00 47.94 ? 134  ARG V NH2 1 
ATOM   4894 N N   . SER D 2 135 ? 32.923  34.192  48.404  1.00 41.40 ? 135  SER V N   1 
ATOM   4895 C CA  . SER D 2 135 ? 32.929  35.497  47.725  1.00 40.64 ? 135  SER V CA  1 
ATOM   4896 C C   . SER D 2 135 ? 33.167  35.393  46.208  1.00 39.91 ? 135  SER V C   1 
ATOM   4897 O O   . SER D 2 135 ? 32.687  36.229  45.451  1.00 39.77 ? 135  SER V O   1 
ATOM   4898 C CB  . SER D 2 135 ? 33.877  36.502  48.410  1.00 40.62 ? 135  SER V CB  1 
ATOM   4899 O OG  . SER D 2 135 ? 35.240  36.133  48.278  1.00 40.89 ? 135  SER V OG  1 
ATOM   4900 N N   . LEU D 2 136 ? 33.884  34.369  45.763  1.00 39.20 ? 136  LEU V N   1 
ATOM   4901 C CA  . LEU D 2 136 ? 33.934  34.077  44.334  1.00 38.92 ? 136  LEU V CA  1 
ATOM   4902 C C   . LEU D 2 136 ? 32.879  33.038  43.986  1.00 38.42 ? 136  LEU V C   1 
ATOM   4903 O O   . LEU D 2 136 ? 32.505  32.221  44.836  1.00 38.86 ? 136  LEU V O   1 
ATOM   4904 C CB  . LEU D 2 136 ? 35.313  33.584  43.914  1.00 39.23 ? 136  LEU V CB  1 
ATOM   4905 C CG  . LEU D 2 136 ? 36.538  34.428  44.315  1.00 40.75 ? 136  LEU V CG  1 
ATOM   4906 C CD1 . LEU D 2 136 ? 37.794  33.923  43.598  1.00 41.21 ? 136  LEU V CD1 1 
ATOM   4907 C CD2 . LEU D 2 136 ? 36.357  35.936  44.066  1.00 42.18 ? 136  LEU V CD2 1 
ATOM   4908 N N   . LYS D 2 137 ? 32.367  33.087  42.757  1.00 37.41 ? 137  LYS V N   1 
ATOM   4909 C CA  . LYS D 2 137 ? 31.411  32.089  42.305  1.00 36.34 ? 137  LYS V CA  1 
ATOM   4910 C C   . LYS D 2 137 ? 32.115  31.123  41.388  1.00 35.85 ? 137  LYS V C   1 
ATOM   4911 O O   . LYS D 2 137 ? 31.516  30.616  40.456  1.00 36.25 ? 137  LYS V O   1 
ATOM   4912 C CB  . LYS D 2 137 ? 30.214  32.725  41.594  1.00 36.18 ? 137  LYS V CB  1 
ATOM   4913 C CG  . LYS D 2 137 ? 29.163  33.407  42.495  1.00 36.45 ? 137  LYS V CG  1 
ATOM   4914 C CD  . LYS D 2 137 ? 28.520  32.497  43.557  1.00 36.44 ? 137  LYS V CD  1 
ATOM   4915 C CE  . LYS D 2 137 ? 29.337  32.514  44.863  1.00 36.14 ? 137  LYS V CE  1 
ATOM   4916 N NZ  . LYS D 2 137 ? 28.543  32.179  46.072  1.00 36.13 ? 137  LYS V NZ  1 
ATOM   4917 N N   . ASP D 2 138 ? 33.397  30.886  41.648  1.00 35.02 ? 138  ASP V N   1 
ATOM   4918 C CA  . ASP D 2 138 ? 34.173  29.906  40.905  1.00 34.37 ? 138  ASP V CA  1 
ATOM   4919 C C   . ASP D 2 138 ? 33.861  28.488  41.354  1.00 33.80 ? 138  ASP V C   1 
ATOM   4920 O O   . ASP D 2 138 ? 32.916  28.252  42.097  1.00 33.08 ? 138  ASP V O   1 
ATOM   4921 C CB  . ASP D 2 138 ? 35.667  30.163  41.080  1.00 34.77 ? 138  ASP V CB  1 
ATOM   4922 C CG  . ASP D 2 138 ? 36.257  31.067  39.996  1.00 35.87 ? 138  ASP V CG  1 
ATOM   4923 O OD1 . ASP D 2 138 ? 37.217  30.614  39.296  1.00 35.26 ? 138  ASP V OD1 1 
ATOM   4924 O OD2 . ASP D 2 138 ? 35.775  32.228  39.866  1.00 37.50 ? 138  ASP V OD2 1 
ATOM   4925 N N   . GLU D 2 139 ? 34.677  27.546  40.895  1.00 33.89 ? 139  GLU V N   1 
ATOM   4926 C CA  . GLU D 2 139 ? 34.476  26.126  41.183  1.00 34.44 ? 139  GLU V CA  1 
ATOM   4927 C C   . GLU D 2 139 ? 35.697  25.511  41.808  1.00 33.82 ? 139  GLU V C   1 
ATOM   4928 O O   . GLU D 2 139 ? 36.820  25.849  41.450  1.00 33.91 ? 139  GLU V O   1 
ATOM   4929 C CB  . GLU D 2 139 ? 34.150  25.365  39.907  1.00 34.86 ? 139  GLU V CB  1 
ATOM   4930 C CG  . GLU D 2 139 ? 35.044  25.750  38.756  1.00 37.29 ? 139  GLU V CG  1 
ATOM   4931 C CD  . GLU D 2 139 ? 34.454  25.355  37.421  1.00 40.88 ? 139  GLU V CD  1 
ATOM   4932 O OE1 . GLU D 2 139 ? 34.724  26.075  36.419  1.00 40.84 ? 139  GLU V OE1 1 
ATOM   4933 O OE2 . GLU D 2 139 ? 33.721  24.326  37.390  1.00 41.98 ? 139  GLU V OE2 1 
ATOM   4934 N N   . ASP D 2 140 ? 35.469  24.587  42.722  1.00 33.25 ? 140  ASP V N   1 
ATOM   4935 C CA  . ASP D 2 140 ? 36.544  24.047  43.507  1.00 33.40 ? 140  ASP V CA  1 
ATOM   4936 C C   . ASP D 2 140 ? 37.714  23.566  42.658  1.00 33.26 ? 140  ASP V C   1 
ATOM   4937 O O   . ASP D 2 140 ? 38.829  24.053  42.815  1.00 33.27 ? 140  ASP V O   1 
ATOM   4938 C CB  . ASP D 2 140 ? 36.028  22.917  44.386  1.00 33.89 ? 140  ASP V CB  1 
ATOM   4939 C CG  . ASP D 2 140 ? 35.177  23.410  45.549  1.00 35.11 ? 140  ASP V CG  1 
ATOM   4940 O OD1 . ASP D 2 140 ? 34.585  22.535  46.224  1.00 36.06 ? 140  ASP V OD1 1 
ATOM   4941 O OD2 . ASP D 2 140 ? 35.107  24.644  45.798  1.00 35.89 ? 140  ASP V OD2 1 
ATOM   4942 N N   . TYR D 2 141 ? 37.454  22.624  41.753  1.00 33.03 ? 141  TYR V N   1 
ATOM   4943 C CA  . TYR D 2 141 ? 38.507  21.988  40.955  1.00 32.58 ? 141  TYR V CA  1 
ATOM   4944 C C   . TYR D 2 141 ? 38.127  22.007  39.485  1.00 31.91 ? 141  TYR V C   1 
ATOM   4945 O O   . TYR D 2 141 ? 36.960  21.823  39.139  1.00 31.64 ? 141  TYR V O   1 
ATOM   4946 C CB  . TYR D 2 141 ? 38.658  20.528  41.356  1.00 33.27 ? 141  TYR V CB  1 
ATOM   4947 C CG  . TYR D 2 141 ? 39.105  20.239  42.774  1.00 34.23 ? 141  TYR V CG  1 
ATOM   4948 C CD1 . TYR D 2 141 ? 38.281  20.522  43.865  1.00 35.38 ? 141  TYR V CD1 1 
ATOM   4949 C CD2 . TYR D 2 141 ? 40.324  19.609  43.016  1.00 35.14 ? 141  TYR V CD2 1 
ATOM   4950 C CE1 . TYR D 2 141 ? 38.686  20.244  45.169  1.00 35.81 ? 141  TYR V CE1 1 
ATOM   4951 C CE2 . TYR D 2 141 ? 40.738  19.320  44.320  1.00 36.04 ? 141  TYR V CE2 1 
ATOM   4952 C CZ  . TYR D 2 141 ? 39.915  19.643  45.387  1.00 35.77 ? 141  TYR V CZ  1 
ATOM   4953 O OH  . TYR D 2 141 ? 40.323  19.359  46.666  1.00 35.65 ? 141  TYR V OH  1 
ATOM   4954 N N   . THR D 2 142 ? 39.123  22.210  38.625  1.00 31.18 ? 142  THR V N   1 
ATOM   4955 C CA  . THR D 2 142 ? 38.907  22.373  37.178  1.00 30.50 ? 142  THR V CA  1 
ATOM   4956 C C   . THR D 2 142 ? 40.177  22.049  36.429  1.00 30.03 ? 142  THR V C   1 
ATOM   4957 O O   . THR D 2 142 ? 41.182  22.733  36.595  1.00 30.02 ? 142  THR V O   1 
ATOM   4958 C CB  . THR D 2 142 ? 38.515  23.836  36.804  1.00 30.39 ? 142  THR V CB  1 
ATOM   4959 O OG1 . THR D 2 142 ? 37.219  24.147  37.320  1.00 30.32 ? 142  THR V OG1 1 
ATOM   4960 C CG2 . THR D 2 142 ? 38.489  24.035  35.297  1.00 30.40 ? 142  THR V CG2 1 
ATOM   4961 N N   . ARG D 2 143 ? 40.147  21.004  35.608  1.00 29.61 ? 143  ARG V N   1 
ATOM   4962 C CA  . ARG D 2 143 ? 41.324  20.682  34.792  1.00 29.25 ? 143  ARG V CA  1 
ATOM   4963 C C   . ARG D 2 143 ? 40.980  20.643  33.325  1.00 28.92 ? 143  ARG V C   1 
ATOM   4964 O O   . ARG D 2 143 ? 39.853  20.319  32.963  1.00 28.82 ? 143  ARG V O   1 
ATOM   4965 C CB  . ARG D 2 143 ? 42.043  19.411  35.249  1.00 29.12 ? 143  ARG V CB  1 
ATOM   4966 C CG  . ARG D 2 143 ? 41.152  18.393  35.900  1.00 28.99 ? 143  ARG V CG  1 
ATOM   4967 C CD  . ARG D 2 143 ? 41.916  17.128  36.237  1.00 29.15 ? 143  ARG V CD  1 
ATOM   4968 N NE  . ARG D 2 143 ? 42.767  17.232  37.420  1.00 27.62 ? 143  ARG V NE  1 
ATOM   4969 C CZ  . ARG D 2 143 ? 43.337  16.191  38.018  1.00 27.65 ? 143  ARG V CZ  1 
ATOM   4970 N NH1 . ARG D 2 143 ? 43.144  14.960  37.551  1.00 28.72 ? 143  ARG V NH1 1 
ATOM   4971 N NH2 . ARG D 2 143 ? 44.096  16.372  39.085  1.00 27.09 ? 143  ARG V NH2 1 
ATOM   4972 N N   . GLY D 2 144 ? 41.956  21.002  32.497  1.00 28.66 ? 144  GLY V N   1 
ATOM   4973 C CA  . GLY D 2 144 ? 41.738  21.191  31.076  1.00 28.69 ? 144  GLY V CA  1 
ATOM   4974 C C   . GLY D 2 144 ? 42.971  21.778  30.435  1.00 28.97 ? 144  GLY V C   1 
ATOM   4975 O O   . GLY D 2 144 ? 44.037  21.822  31.049  1.00 29.01 ? 144  GLY V O   1 
ATOM   4976 N N   . CYS D 2 145 ? 42.826  22.213  29.187  1.00 29.23 ? 145  CYS V N   1 
ATOM   4977 C CA  . CYS D 2 145 ? 43.905  22.853  28.455  1.00 29.56 ? 145  CYS V CA  1 
ATOM   4978 C C   . CYS D 2 145 ? 43.852  24.312  28.758  1.00 29.06 ? 145  CYS V C   1 
ATOM   4979 O O   . CYS D 2 145 ? 42.764  24.866  28.879  1.00 29.24 ? 145  CYS V O   1 
ATOM   4980 C CB  . CYS D 2 145 ? 43.710  22.663  26.965  1.00 29.81 ? 145  CYS V CB  1 
ATOM   4981 S SG  . CYS D 2 145 ? 44.500  21.164  26.346  1.00 33.60 ? 145  CYS V SG  1 
ATOM   4982 N N   . GLY D 2 146 ? 45.010  24.948  28.881  1.00 28.64 ? 146  GLY V N   1 
ATOM   4983 C CA  . GLY D 2 146 ? 45.042  26.393  29.099  1.00 28.54 ? 146  GLY V CA  1 
ATOM   4984 C C   . GLY D 2 146 ? 46.357  27.043  28.723  1.00 28.80 ? 146  GLY V C   1 
ATOM   4985 O O   . GLY D 2 146 ? 47.288  26.365  28.286  1.00 28.88 ? 146  GLY V O   1 
ATOM   4986 N N   . SER D 2 147 ? 46.420  28.366  28.864  1.00 28.99 ? 147  SER V N   1 
ATOM   4987 C CA  . SER D 2 147 ? 47.679  29.118  28.824  1.00 29.13 ? 147  SER V CA  1 
ATOM   4988 C C   . SER D 2 147 ? 47.449  30.331  29.661  1.00 29.11 ? 147  SER V C   1 
ATOM   4989 O O   . SER D 2 147 ? 46.656  31.190  29.302  1.00 28.77 ? 147  SER V O   1 
ATOM   4990 C CB  . SER D 2 147 ? 48.067  29.548  27.406  1.00 29.52 ? 147  SER V CB  1 
ATOM   4991 O OG  . SER D 2 147 ? 49.070  30.553  27.445  1.00 28.93 ? 147  SER V OG  1 
ATOM   4992 N N   . LEU D 2 148 ? 48.138  30.388  30.787  1.00 29.58 ? 148  LEU V N   1 
ATOM   4993 C CA  . LEU D 2 148 ? 47.900  31.425  31.768  1.00 30.01 ? 148  LEU V CA  1 
ATOM   4994 C C   . LEU D 2 148 ? 49.215  31.893  32.347  1.00 30.69 ? 148  LEU V C   1 
ATOM   4995 O O   . LEU D 2 148 ? 50.275  31.480  31.887  1.00 30.38 ? 148  LEU V O   1 
ATOM   4996 C CB  . LEU D 2 148 ? 46.988  30.902  32.884  1.00 29.79 ? 148  LEU V CB  1 
ATOM   4997 C CG  . LEU D 2 148 ? 45.648  30.278  32.531  1.00 28.28 ? 148  LEU V CG  1 
ATOM   4998 C CD1 . LEU D 2 148 ? 45.031  29.756  33.757  1.00 27.82 ? 148  LEU V CD1 1 
ATOM   4999 C CD2 . LEU D 2 148 ? 44.768  31.303  31.961  1.00 28.46 ? 148  LEU V CD2 1 
ATOM   5000 N N   . PRO D 2 149 ? 49.143  32.763  33.362  1.00 31.69 ? 149  PRO V N   1 
ATOM   5001 C CA  . PRO D 2 149 ? 50.287  33.386  33.994  1.00 32.83 ? 149  PRO V CA  1 
ATOM   5002 C C   . PRO D 2 149 ? 51.358  32.426  34.504  1.00 34.11 ? 149  PRO V C   1 
ATOM   5003 O O   . PRO D 2 149 ? 51.036  31.417  35.149  1.00 34.21 ? 149  PRO V O   1 
ATOM   5004 C CB  . PRO D 2 149 ? 49.654  34.134  35.158  1.00 32.55 ? 149  PRO V CB  1 
ATOM   5005 C CG  . PRO D 2 149 ? 48.370  34.549  34.634  1.00 31.99 ? 149  PRO V CG  1 
ATOM   5006 C CD  . PRO D 2 149 ? 47.892  33.380  33.828  1.00 31.73 ? 149  PRO V CD  1 
ATOM   5007 N N   . GLY D 2 150 ? 52.616  32.769  34.193  1.00 35.34 ? 150  GLY V N   1 
ATOM   5008 C CA  . GLY D 2 150 ? 53.812  32.050  34.636  1.00 36.95 ? 150  GLY V CA  1 
ATOM   5009 C C   . GLY D 2 150 ? 53.725  30.577  34.305  1.00 38.13 ? 150  GLY V C   1 
ATOM   5010 O O   . GLY D 2 150 ? 54.023  29.716  35.148  1.00 38.06 ? 150  GLY V O   1 
ATOM   5011 N N   . CYS D 2 151 ? 53.332  30.297  33.062  1.00 39.03 ? 151  CYS V N   1 
ATOM   5012 C CA  . CYS D 2 151 ? 52.847  28.980  32.712  1.00 39.92 ? 151  CYS V CA  1 
ATOM   5013 C C   . CYS D 2 151 ? 53.866  27.817  32.804  1.00 40.22 ? 151  CYS V C   1 
ATOM   5014 O O   . CYS D 2 151 ? 53.644  26.878  33.578  1.00 40.58 ? 151  CYS V O   1 
ATOM   5015 C CB  . CYS D 2 151 ? 52.125  29.016  31.389  1.00 39.64 ? 151  CYS V CB  1 
ATOM   5016 S SG  . CYS D 2 151 ? 50.585  28.043  31.375  1.00 42.83 ? 151  CYS V SG  1 
ATOM   5017 N N   . PRO D 2 152 ? 54.984  27.855  32.048  1.00 40.21 ? 152  PRO V N   1 
ATOM   5018 C CA  . PRO D 2 152 ? 55.847  26.707  32.341  1.00 39.90 ? 152  PRO V CA  1 
ATOM   5019 C C   . PRO D 2 152 ? 56.236  26.779  33.821  1.00 39.74 ? 152  PRO V C   1 
ATOM   5020 O O   . PRO D 2 152 ? 57.158  27.518  34.183  1.00 40.26 ? 152  PRO V O   1 
ATOM   5021 C CB  . PRO D 2 152 ? 57.056  26.922  31.420  1.00 40.04 ? 152  PRO V CB  1 
ATOM   5022 C CG  . PRO D 2 152 ? 56.573  27.869  30.347  1.00 40.25 ? 152  PRO V CG  1 
ATOM   5023 C CD  . PRO D 2 152 ? 55.554  28.747  31.022  1.00 40.15 ? 152  PRO V CD  1 
ATOM   5024 N N   . GLY D 2 153 ? 55.505  26.051  34.668  1.00 39.10 ? 153  GLY V N   1 
ATOM   5025 C CA  . GLY D 2 153 ? 55.665  26.136  36.128  1.00 38.49 ? 153  GLY V CA  1 
ATOM   5026 C C   . GLY D 2 153 ? 54.329  26.190  36.846  1.00 38.02 ? 153  GLY V C   1 
ATOM   5027 O O   . GLY D 2 153 ? 53.291  25.961  36.227  1.00 38.18 ? 153  GLY V O   1 
ATOM   5028 N N   . THR D 2 154 ? 54.337  26.472  38.153  1.00 37.41 ? 154  THR V N   1 
ATOM   5029 C CA  . THR D 2 154 ? 53.073  26.630  38.912  1.00 36.90 ? 154  THR V CA  1 
ATOM   5030 C C   . THR D 2 154 ? 53.174  27.702  40.004  1.00 35.92 ? 154  THR V C   1 
ATOM   5031 O O   . THR D 2 154 ? 54.256  28.244  40.231  1.00 35.73 ? 154  THR V O   1 
ATOM   5032 C CB  . THR D 2 154 ? 52.590  25.311  39.571  1.00 37.23 ? 154  THR V CB  1 
ATOM   5033 O OG1 . THR D 2 154 ? 53.145  25.201  40.888  1.00 37.83 ? 154  THR V OG1 1 
ATOM   5034 C CG2 . THR D 2 154 ? 52.957  24.068  38.732  1.00 37.78 ? 154  THR V CG2 1 
ATOM   5035 N N   . ALA D 2 155 ? 52.046  27.994  40.667  1.00 34.93 ? 155  ALA V N   1 
ATOM   5036 C CA  . ALA D 2 155 ? 51.969  29.008  41.751  1.00 33.85 ? 155  ALA V CA  1 
ATOM   5037 C C   . ALA D 2 155 ? 50.623  29.046  42.503  1.00 32.85 ? 155  ALA V C   1 
ATOM   5038 O O   . ALA D 2 155 ? 49.564  28.877  41.905  1.00 32.88 ? 155  ALA V O   1 
ATOM   5039 C CB  . ALA D 2 155 ? 52.304  30.402  41.225  1.00 33.94 ? 155  ALA V CB  1 
ATOM   5040 N N   . GLY D 2 156 ? 50.675  29.301  43.809  1.00 31.35 ? 156  GLY V N   1 
ATOM   5041 C CA  . GLY D 2 156 ? 49.488  29.226  44.642  1.00 29.68 ? 156  GLY V CA  1 
ATOM   5042 C C   . GLY D 2 156 ? 49.583  29.981  45.947  1.00 28.69 ? 156  GLY V C   1 
ATOM   5043 O O   . GLY D 2 156 ? 50.658  30.435  46.338  1.00 28.67 ? 156  GLY V O   1 
ATOM   5044 N N   . PHE D 2 157 ? 48.442  30.085  46.623  1.00 27.71 ? 157  PHE V N   1 
ATOM   5045 C CA  . PHE D 2 157 ? 48.287  30.907  47.808  1.00 27.18 ? 157  PHE V CA  1 
ATOM   5046 C C   . PHE D 2 157 ? 47.306  30.241  48.759  1.00 27.50 ? 157  PHE V C   1 
ATOM   5047 O O   . PHE D 2 157 ? 46.296  29.684  48.301  1.00 27.62 ? 157  PHE V O   1 
ATOM   5048 C CB  . PHE D 2 157 ? 47.756  32.290  47.400  1.00 26.61 ? 157  PHE V CB  1 
ATOM   5049 C CG  . PHE D 2 157 ? 47.210  33.115  48.549  1.00 25.54 ? 157  PHE V CG  1 
ATOM   5050 C CD1 . PHE D 2 157 ? 48.072  33.799  49.413  1.00 24.63 ? 157  PHE V CD1 1 
ATOM   5051 C CD2 . PHE D 2 157 ? 45.839  33.213  48.767  1.00 24.14 ? 157  PHE V CD2 1 
ATOM   5052 C CE1 . PHE D 2 157 ? 47.576  34.554  50.479  1.00 22.91 ? 157  PHE V CE1 1 
ATOM   5053 C CE2 . PHE D 2 157 ? 45.338  33.969  49.839  1.00 23.82 ? 157  PHE V CE2 1 
ATOM   5054 C CZ  . PHE D 2 157 ? 46.210  34.637  50.692  1.00 22.51 ? 157  PHE V CZ  1 
ATOM   5055 N N   . HIS D 2 158 ? 47.578  30.302  50.070  1.00 27.53 ? 158  HIS V N   1 
ATOM   5056 C CA  . HIS D 2 158 ? 46.545  29.947  51.047  1.00 27.74 ? 158  HIS V CA  1 
ATOM   5057 C C   . HIS D 2 158 ? 46.514  30.741  52.330  1.00 27.86 ? 158  HIS V C   1 
ATOM   5058 O O   . HIS D 2 158 ? 47.529  31.221  52.812  1.00 27.73 ? 158  HIS V O   1 
ATOM   5059 C CB  . HIS D 2 158 ? 46.578  28.454  51.363  1.00 28.11 ? 158  HIS V CB  1 
ATOM   5060 C CG  . HIS D 2 158 ? 47.412  28.091  52.551  1.00 28.45 ? 158  HIS V CG  1 
ATOM   5061 N ND1 . HIS D 2 158 ? 48.789  28.105  52.527  1.00 29.44 ? 158  HIS V ND1 1 
ATOM   5062 C CD2 . HIS D 2 158 ? 47.061  27.678  53.793  1.00 28.41 ? 158  HIS V CD2 1 
ATOM   5063 C CE1 . HIS D 2 158 ? 49.252  27.735  53.708  1.00 29.18 ? 158  HIS V CE1 1 
ATOM   5064 N NE2 . HIS D 2 158 ? 48.223  27.468  54.493  1.00 29.05 ? 158  HIS V NE2 1 
ATOM   5065 N N   . SER D 2 159 ? 45.309  30.718  52.707  1.00 29.63 ? 159  SER V N   1 
ATOM   5066 C CA  . SER D 2 159 ? 44.982  31.321  53.955  1.00 30.73 ? 159  SER V CA  1 
ATOM   5067 C C   . SER D 2 159 ? 44.247  30.262  54.769  1.00 31.37 ? 159  SER V C   1 
ATOM   5068 O O   . SER D 2 159 ? 43.946  29.200  54.253  1.00 31.86 ? 159  SER V O   1 
ATOM   5069 C CB  . SER D 2 159 ? 44.064  32.482  53.670  1.00 30.72 ? 159  SER V CB  1 
ATOM   5070 O OG  . SER D 2 159 ? 43.300  32.770  54.816  1.00 32.88 ? 159  SER V OG  1 
ATOM   5071 N N   . ASN D 2 160 ? 43.941  30.542  56.031  1.00 32.26 ? 160  ASN V N   1 
ATOM   5072 C CA  . ASN D 2 160 ? 43.104  29.638  56.824  1.00 33.47 ? 160  ASN V CA  1 
ATOM   5073 C C   . ASN D 2 160 ? 41.761  29.413  56.108  1.00 32.77 ? 160  ASN V C   1 
ATOM   5074 O O   . ASN D 2 160 ? 41.246  28.297  56.054  1.00 32.71 ? 160  ASN V O   1 
ATOM   5075 C CB  . ASN D 2 160 ? 42.918  30.177  58.269  1.00 34.57 ? 160  ASN V CB  1 
ATOM   5076 C CG  . ASN D 2 160 ? 42.280  29.152  59.227  1.00 39.25 ? 160  ASN V CG  1 
ATOM   5077 O OD1 . ASN D 2 160 ? 42.707  27.978  59.277  1.00 40.47 ? 160  ASN V OD1 1 
ATOM   5078 N ND2 . ASN D 2 160 ? 41.256  29.616  60.004  1.00 47.99 ? 160  ASN V ND2 1 
ATOM   5079 N N   . GLN D 2 161 ? 41.220  30.473  55.517  1.00 32.29 ? 161  GLN V N   1 
ATOM   5080 C CA  . GLN D 2 161 ? 39.921  30.392  54.846  1.00 31.85 ? 161  GLN V CA  1 
ATOM   5081 C C   . GLN D 2 161 ? 40.004  30.003  53.371  1.00 31.05 ? 161  GLN V C   1 
ATOM   5082 O O   . GLN D 2 161 ? 39.202  29.188  52.893  1.00 31.04 ? 161  GLN V O   1 
ATOM   5083 C CB  . GLN D 2 161 ? 39.139  31.705  55.000  1.00 32.10 ? 161  GLN V CB  1 
ATOM   5084 C CG  . GLN D 2 161 ? 39.012  32.203  56.443  1.00 33.43 ? 161  GLN V CG  1 
ATOM   5085 C CD  . GLN D 2 161 ? 38.162  31.308  57.372  1.00 35.17 ? 161  GLN V CD  1 
ATOM   5086 O OE1 . GLN D 2 161 ? 37.659  31.791  58.388  1.00 35.96 ? 161  GLN V OE1 1 
ATOM   5087 N NE2 . GLN D 2 161 ? 38.008  30.018  57.036  1.00 35.33 ? 161  GLN V NE2 1 
ATOM   5088 N N   . THR D 2 162 ? 41.031  30.702  52.720  1.00 24.28 ? 162  THR V N   1 
ATOM   5089 C CA  . THR D 2 162 ? 41.026  30.417  51.291  1.00 23.73 ? 162  THR V CA  1 
ATOM   5090 C C   . THR D 2 162 ? 42.229  29.598  50.793  1.00 23.41 ? 162  THR V C   1 
ATOM   5091 O O   . THR D 2 162 ? 43.272  29.495  51.450  1.00 22.93 ? 162  THR V O   1 
ATOM   5092 C CB  . THR D 2 162 ? 40.852  31.729  50.410  1.00 23.95 ? 162  THR V CB  1 
ATOM   5093 O OG1 . THR D 2 162 ? 42.122  32.218  49.945  1.00 23.44 ? 162  THR V OG1 1 
ATOM   5094 C CG2 . THR D 2 162 ? 40.082  32.844  51.152  1.00 23.54 ? 162  THR V CG2 1 
ATOM   5095 N N   . PHE D 2 163 ? 42.057  29.034  49.602  1.00 23.16 ? 163  PHE V N   1 
ATOM   5096 C CA  . PHE D 2 163 ? 43.142  28.401  48.870  1.00 22.80 ? 163  PHE V CA  1 
ATOM   5097 C C   . PHE D 2 163 ? 43.006  28.620  47.353  1.00 23.04 ? 163  PHE V C   1 
ATOM   5098 O O   . PHE D 2 163 ? 41.892  28.666  46.805  1.00 22.68 ? 163  PHE V O   1 
ATOM   5099 C CB  . PHE D 2 163 ? 43.188  26.913  49.206  1.00 22.57 ? 163  PHE V CB  1 
ATOM   5100 C CG  . PHE D 2 163 ? 44.287  26.162  48.522  1.00 20.74 ? 163  PHE V CG  1 
ATOM   5101 C CD1 . PHE D 2 163 ? 45.588  26.651  48.513  1.00 18.94 ? 163  PHE V CD1 1 
ATOM   5102 C CD2 . PHE D 2 163 ? 44.022  24.950  47.903  1.00 19.63 ? 163  PHE V CD2 1 
ATOM   5103 C CE1 . PHE D 2 163 ? 46.623  25.952  47.884  1.00 18.36 ? 163  PHE V CE1 1 
ATOM   5104 C CE2 . PHE D 2 163 ? 45.041  24.237  47.276  1.00 19.80 ? 163  PHE V CE2 1 
ATOM   5105 C CZ  . PHE D 2 163 ? 46.357  24.744  47.269  1.00 19.13 ? 163  PHE V CZ  1 
ATOM   5106 N N   . HIS D 2 164 ? 44.162  28.779  46.705  1.00 23.19 ? 164  HIS V N   1 
ATOM   5107 C CA  . HIS D 2 164 ? 44.272  28.911  45.262  1.00 23.51 ? 164  HIS V CA  1 
ATOM   5108 C C   . HIS D 2 164 ? 45.519  28.225  44.806  1.00 23.54 ? 164  HIS V C   1 
ATOM   5109 O O   . HIS D 2 164 ? 46.571  28.406  45.393  1.00 23.33 ? 164  HIS V O   1 
ATOM   5110 C CB  . HIS D 2 164 ? 44.359  30.376  44.858  1.00 23.70 ? 164  HIS V CB  1 
ATOM   5111 C CG  . HIS D 2 164 ? 43.147  31.168  45.223  1.00 25.07 ? 164  HIS V CG  1 
ATOM   5112 N ND1 . HIS D 2 164 ? 42.014  31.197  44.438  1.00 26.30 ? 164  HIS V ND1 1 
ATOM   5113 C CD2 . HIS D 2 164 ? 42.878  31.939  46.301  1.00 26.32 ? 164  HIS V CD2 1 
ATOM   5114 C CE1 . HIS D 2 164 ? 41.107  31.967  45.009  1.00 26.77 ? 164  HIS V CE1 1 
ATOM   5115 N NE2 . HIS D 2 164 ? 41.603  32.424  46.145  1.00 26.87 ? 164  HIS V NE2 1 
ATOM   5116 N N   . PHE D 2 165 ? 45.399  27.436  43.753  1.00 24.47 ? 165  PHE V N   1 
ATOM   5117 C CA  . PHE D 2 165 ? 46.550  26.789  43.148  1.00 25.78 ? 165  PHE V CA  1 
ATOM   5118 C C   . PHE D 2 165 ? 46.362  26.598  41.644  1.00 26.51 ? 165  PHE V C   1 
ATOM   5119 O O   . PHE D 2 165 ? 45.255  26.342  41.164  1.00 26.52 ? 165  PHE V O   1 
ATOM   5120 C CB  . PHE D 2 165 ? 46.788  25.449  43.815  1.00 26.05 ? 165  PHE V CB  1 
ATOM   5121 C CG  . PHE D 2 165 ? 48.033  24.755  43.377  1.00 27.05 ? 165  PHE V CG  1 
ATOM   5122 C CD1 . PHE D 2 165 ? 47.983  23.784  42.384  1.00 28.19 ? 165  PHE V CD1 1 
ATOM   5123 C CD2 . PHE D 2 165 ? 49.250  25.036  43.987  1.00 27.84 ? 165  PHE V CD2 1 
ATOM   5124 C CE1 . PHE D 2 165 ? 49.141  23.125  41.984  1.00 30.29 ? 165  PHE V CE1 1 
ATOM   5125 C CE2 . PHE D 2 165 ? 50.419  24.383  43.607  1.00 28.53 ? 165  PHE V CE2 1 
ATOM   5126 C CZ  . PHE D 2 165 ? 50.375  23.426  42.610  1.00 29.80 ? 165  PHE V CZ  1 
ATOM   5127 N N   . LEU D 2 166 ? 47.463  26.729  40.915  1.00 27.33 ? 166  LEU V N   1 
ATOM   5128 C CA  . LEU D 2 166 ? 47.469  26.561  39.483  1.00 28.15 ? 166  LEU V CA  1 
ATOM   5129 C C   . LEU D 2 166 ? 48.683  25.744  39.096  1.00 29.16 ? 166  LEU V C   1 
ATOM   5130 O O   . LEU D 2 166 ? 49.793  25.972  39.594  1.00 28.71 ? 166  LEU V O   1 
ATOM   5131 C CB  . LEU D 2 166 ? 47.529  27.916  38.792  1.00 28.03 ? 166  LEU V CB  1 
ATOM   5132 C CG  . LEU D 2 166 ? 47.760  27.912  37.277  1.00 27.77 ? 166  LEU V CG  1 
ATOM   5133 C CD1 . LEU D 2 166 ? 46.576  28.517  36.594  1.00 27.38 ? 166  LEU V CD1 1 
ATOM   5134 C CD2 . LEU D 2 166 ? 49.026  28.673  36.884  1.00 27.97 ? 166  LEU V CD2 1 
ATOM   5135 N N   . LYS D 2 167 ? 48.451  24.803  38.184  1.00 30.73 ? 167  LYS V N   1 
ATOM   5136 C CA  . LYS D 2 167 ? 49.498  23.948  37.639  1.00 32.34 ? 167  LYS V CA  1 
ATOM   5137 C C   . LYS D 2 167 ? 49.425  23.898  36.098  1.00 33.40 ? 167  LYS V C   1 
ATOM   5138 O O   . LYS D 2 167 ? 48.400  23.479  35.551  1.00 33.15 ? 167  LYS V O   1 
ATOM   5139 C CB  . LYS D 2 167 ? 49.348  22.560  38.258  1.00 32.17 ? 167  LYS V CB  1 
ATOM   5140 C CG  . LYS D 2 167 ? 50.376  21.527  37.860  1.00 32.26 ? 167  LYS V CG  1 
ATOM   5141 C CD  . LYS D 2 167 ? 50.142  20.295  38.706  1.00 32.12 ? 167  LYS V CD  1 
ATOM   5142 C CE  . LYS D 2 167 ? 50.596  19.029  38.031  1.00 31.86 ? 167  LYS V CE  1 
ATOM   5143 N NZ  . LYS D 2 167 ? 49.864  17.888  38.655  1.00 32.56 ? 167  LYS V NZ  1 
ATOM   5144 N N   . CYS D 2 168 ? 50.489  24.371  35.425  1.00 34.89 ? 168  CYS V N   1 
ATOM   5145 C CA  . CYS D 2 168 ? 50.664  24.243  33.957  1.00 36.76 ? 168  CYS V CA  1 
ATOM   5146 C C   . CYS D 2 168 ? 51.703  23.159  33.711  1.00 37.07 ? 168  CYS V C   1 
ATOM   5147 O O   . CYS D 2 168 ? 52.826  23.277  34.182  1.00 37.32 ? 168  CYS V O   1 
ATOM   5148 C CB  . CYS D 2 168 ? 51.196  25.532  33.256  1.00 37.06 ? 168  CYS V CB  1 
ATOM   5149 S SG  . CYS D 2 168 ? 50.266  27.166  33.216  1.00 40.48 ? 168  CYS V SG  1 
ATOM   5150 N N   . CYS D 2 169 ? 51.345  22.121  32.964  1.00 37.79 ? 169  CYS V N   1 
ATOM   5151 C CA  . CYS D 2 169 ? 52.304  21.092  32.591  1.00 38.81 ? 169  CYS V CA  1 
ATOM   5152 C C   . CYS D 2 169 ? 52.407  21.004  31.077  1.00 39.12 ? 169  CYS V C   1 
ATOM   5153 O O   . CYS D 2 169 ? 51.544  21.501  30.382  1.00 39.44 ? 169  CYS V O   1 
ATOM   5154 C CB  . CYS D 2 169 ? 51.876  19.749  33.161  1.00 39.13 ? 169  CYS V CB  1 
ATOM   5155 S SG  . CYS D 2 169 ? 50.683  18.851  32.122  1.00 40.59 ? 169  CYS V SG  1 
ATOM   5156 N N   . ASN D 2 170 ? 53.434  20.338  30.570  1.00 39.67 ? 170  ASN V N   1 
ATOM   5157 C CA  . ASN D 2 170 ? 53.713  20.347  29.142  1.00 40.50 ? 170  ASN V CA  1 
ATOM   5158 C C   . ASN D 2 170 ? 54.053  18.963  28.592  1.00 40.45 ? 170  ASN V C   1 
ATOM   5159 O O   . ASN D 2 170 ? 54.967  18.833  27.764  1.00 40.71 ? 170  ASN V O   1 
ATOM   5160 C CB  . ASN D 2 170 ? 54.854  21.334  28.857  1.00 41.07 ? 170  ASN V CB  1 
ATOM   5161 C CG  . ASN D 2 170 ? 55.982  21.236  29.882  1.00 44.37 ? 170  ASN V CG  1 
ATOM   5162 O OD1 . ASN D 2 170 ? 56.059  20.264  30.638  1.00 45.63 ? 170  ASN V OD1 1 
ATOM   5163 N ND2 . ASN D 2 170 ? 56.857  22.237  29.917  1.00 49.60 ? 170  ASN V ND2 1 
ATOM   5164 N N   . TYR D 2 171 ? 53.338  17.931  29.060  1.00 40.36 ? 171  TYR V N   1 
ATOM   5165 C CA  . TYR D 2 171 ? 53.552  16.543  28.590  1.00 39.96 ? 171  TYR V CA  1 
ATOM   5166 C C   . TYR D 2 171 ? 52.366  15.626  28.806  1.00 39.45 ? 171  TYR V C   1 
ATOM   5167 O O   . TYR D 2 171 ? 51.898  15.471  29.919  1.00 39.10 ? 171  TYR V O   1 
ATOM   5168 C CB  . TYR D 2 171 ? 54.792  15.927  29.221  1.00 40.15 ? 171  TYR V CB  1 
ATOM   5169 C CG  . TYR D 2 171 ? 54.747  15.749  30.719  1.00 41.08 ? 171  TYR V CG  1 
ATOM   5170 C CD1 . TYR D 2 171 ? 55.358  16.672  31.560  1.00 42.26 ? 171  TYR V CD1 1 
ATOM   5171 C CD2 . TYR D 2 171 ? 54.139  14.630  31.296  1.00 42.05 ? 171  TYR V CD2 1 
ATOM   5172 C CE1 . TYR D 2 171 ? 55.352  16.501  32.940  1.00 43.34 ? 171  TYR V CE1 1 
ATOM   5173 C CE2 . TYR D 2 171 ? 54.124  14.445  32.675  1.00 42.77 ? 171  TYR V CE2 1 
ATOM   5174 C CZ  . TYR D 2 171 ? 54.736  15.386  33.493  1.00 43.53 ? 171  TYR V CZ  1 
ATOM   5175 O OH  . TYR D 2 171 ? 54.736  15.218  34.863  1.00 44.28 ? 171  TYR V OH  1 
ATOM   5176 N N   . THR D 2 172 ? 51.918  14.988  27.730  1.00 39.30 ? 172  THR V N   1 
ATOM   5177 C CA  . THR D 2 172 ? 50.638  14.266  27.698  1.00 39.10 ? 172  THR V CA  1 
ATOM   5178 C C   . THR D 2 172 ? 50.109  13.874  29.057  1.00 38.81 ? 172  THR V C   1 
ATOM   5179 O O   . THR D 2 172 ? 50.769  13.187  29.824  1.00 38.97 ? 172  THR V O   1 
ATOM   5180 C CB  . THR D 2 172 ? 50.695  12.980  26.858  1.00 39.08 ? 172  THR V CB  1 
ATOM   5181 O OG1 . THR D 2 172 ? 51.465  13.205  25.671  1.00 39.90 ? 172  THR V OG1 1 
ATOM   5182 C CG2 . THR D 2 172 ? 49.286  12.527  26.488  1.00 38.70 ? 172  THR V CG2 1 
ATOM   5183 N N   . HIS D 2 173 ? 48.906  14.335  29.336  1.00 38.58 ? 173  HIS V N   1 
ATOM   5184 C CA  . HIS D 2 173 ? 48.132  13.871  30.462  1.00 38.43 ? 173  HIS V CA  1 
ATOM   5185 C C   . HIS D 2 173 ? 48.725  14.066  31.831  1.00 38.07 ? 173  HIS V C   1 
ATOM   5186 O O   . HIS D 2 173 ? 48.528  13.227  32.693  1.00 38.21 ? 173  HIS V O   1 
ATOM   5187 C CB  . HIS D 2 173 ? 47.754  12.412  30.267  1.00 38.50 ? 173  HIS V CB  1 
ATOM   5188 C CG  . HIS D 2 173 ? 46.310  12.232  29.982  1.00 40.12 ? 173  HIS V CG  1 
ATOM   5189 N ND1 . HIS D 2 173 ? 45.781  12.397  28.722  1.00 41.44 ? 173  HIS V ND1 1 
ATOM   5190 C CD2 . HIS D 2 173 ? 45.266  11.976  30.805  1.00 41.50 ? 173  HIS V CD2 1 
ATOM   5191 C CE1 . HIS D 2 173 ? 44.473  12.218  28.774  1.00 42.60 ? 173  HIS V CE1 1 
ATOM   5192 N NE2 . HIS D 2 173 ? 44.135  11.961  30.026  1.00 42.89 ? 173  HIS V NE2 1 
ATOM   5193 N N   . CYS D 2 174 ? 49.414  15.180  32.051  1.00 37.86 ? 174  CYS V N   1 
ATOM   5194 C CA  . CYS D 2 174 ? 50.027  15.424  33.366  1.00 37.72 ? 174  CYS V CA  1 
ATOM   5195 C C   . CYS D 2 174 ? 49.111  16.106  34.380  1.00 36.81 ? 174  CYS V C   1 
ATOM   5196 O O   . CYS D 2 174 ? 49.401  17.196  34.850  1.00 36.72 ? 174  CYS V O   1 
ATOM   5197 C CB  . CYS D 2 174 ? 51.382  16.147  33.255  1.00 38.12 ? 174  CYS V CB  1 
ATOM   5198 S SG  . CYS D 2 174 ? 51.660  17.115  31.745  1.00 40.23 ? 174  CYS V SG  1 
ATOM   5199 N N   . ASN D 2 175 ? 48.002  15.452  34.705  1.00 36.00 ? 175  ASN V N   1 
ATOM   5200 C CA  . ASN D 2 175 ? 47.134  15.885  35.798  1.00 35.43 ? 175  ASN V CA  1 
ATOM   5201 C C   . ASN D 2 175 ? 46.098  14.824  36.206  1.00 34.84 ? 175  ASN V C   1 
ATOM   5202 O O   . ASN D 2 175 ? 44.930  14.901  35.832  1.00 34.87 ? 175  ASN V O   1 
ATOM   5203 C CB  . ASN D 2 175 ? 46.492  17.257  35.505  1.00 35.57 ? 175  ASN V CB  1 
ATOM   5204 C CG  . ASN D 2 175 ? 45.915  17.369  34.099  1.00 35.99 ? 175  ASN V CG  1 
ATOM   5205 O OD1 . ASN D 2 175 ? 44.743  17.699  33.932  1.00 37.63 ? 175  ASN V OD1 1 
ATOM   5206 N ND2 . ASN D 2 175 ? 46.735  17.123  33.088  1.00 36.30 ? 175  ASN V ND2 1 
ATOM   5207 N N   . GLY D 2 176 ? 46.532  13.838  36.985  1.00 33.92 ? 176  GLY V N   1 
ATOM   5208 C CA  . GLY D 2 176 ? 45.720  12.659  37.213  1.00 32.98 ? 176  GLY V CA  1 
ATOM   5209 C C   . GLY D 2 176 ? 45.026  12.580  38.551  1.00 32.45 ? 176  GLY V C   1 
ATOM   5210 O O   . GLY D 2 176 ? 45.303  13.380  39.446  1.00 32.11 ? 176  GLY V O   1 
ATOM   5211 N N   . GLY D 2 177 ? 44.121  11.595  38.651  1.00 32.16 ? 177  GLY V N   1 
ATOM   5212 C CA  . GLY D 2 177 ? 43.350  11.239  39.857  1.00 31.24 ? 177  GLY V CA  1 
ATOM   5213 C C   . GLY D 2 177 ? 43.545  12.170  41.039  1.00 30.51 ? 177  GLY V C   1 
ATOM   5214 O O   . GLY D 2 177 ? 42.697  13.019  41.299  1.00 30.33 ? 177  GLY V O   1 
ATOM   5215 N N   . PRO D 2 178 ? 44.663  12.007  41.768  1.00 29.84 ? 178  PRO V N   1 
ATOM   5216 C CA  . PRO D 2 178 ? 45.075  12.997  42.726  1.00 29.35 ? 178  PRO V CA  1 
ATOM   5217 C C   . PRO D 2 178 ? 44.508  14.389  42.390  1.00 28.91 ? 178  PRO V C   1 
ATOM   5218 O O   . PRO D 2 178 ? 45.132  15.179  41.684  1.00 28.34 ? 178  PRO V O   1 
ATOM   5219 C CB  . PRO D 2 178 ? 46.606  12.976  42.587  1.00 29.50 ? 178  PRO V CB  1 
ATOM   5220 C CG  . PRO D 2 178 ? 46.946  11.665  41.882  1.00 29.25 ? 178  PRO V CG  1 
ATOM   5221 C CD  . PRO D 2 178 ? 45.659  10.930  41.678  1.00 29.68 ? 178  PRO V CD  1 
ATOM   5222 N N   . VAL D 2 179 ? 43.303  14.640  42.888  1.00 28.66 ? 179  VAL V N   1 
ATOM   5223 C CA  . VAL D 2 179 ? 42.669  15.956  42.887  1.00 28.54 ? 179  VAL V CA  1 
ATOM   5224 C C   . VAL D 2 179 ? 43.301  16.825  43.964  1.00 28.34 ? 179  VAL V C   1 
ATOM   5225 O O   . VAL D 2 179 ? 42.930  16.728  45.143  1.00 28.73 ? 179  VAL V O   1 
ATOM   5226 C CB  . VAL D 2 179 ? 41.174  15.832  43.205  1.00 28.63 ? 179  VAL V CB  1 
ATOM   5227 C CG1 . VAL D 2 179 ? 40.426  15.336  41.995  1.00 29.60 ? 179  VAL V CG1 1 
ATOM   5228 C CG2 . VAL D 2 179 ? 40.937  14.893  44.414  1.00 28.54 ? 179  VAL V CG2 1 
ATOM   5229 N N   . LEU D 2 180 ? 44.235  17.683  43.558  1.00 27.79 ? 180  LEU V N   1 
ATOM   5230 C CA  . LEU D 2 180 ? 45.196  18.324  44.480  1.00 27.31 ? 180  LEU V CA  1 
ATOM   5231 C C   . LEU D 2 180 ? 44.622  19.227  45.590  1.00 27.04 ? 180  LEU V C   1 
ATOM   5232 O O   . LEU D 2 180 ? 44.605  20.452  45.436  1.00 26.64 ? 180  LEU V O   1 
ATOM   5233 C CB  . LEU D 2 180 ? 46.278  19.080  43.687  1.00 27.05 ? 180  LEU V CB  1 
ATOM   5234 C CG  . LEU D 2 180 ? 46.817  18.460  42.383  1.00 27.29 ? 180  LEU V CG  1 
ATOM   5235 C CD1 . LEU D 2 180 ? 47.926  19.337  41.786  1.00 26.40 ? 180  LEU V CD1 1 
ATOM   5236 C CD2 . LEU D 2 180 ? 47.283  16.983  42.513  1.00 27.68 ? 180  LEU V CD2 1 
ATOM   5237 N N   . ASP D 2 181 ? 44.202  18.623  46.716  1.00 26.90 ? 181  ASP V N   1 
ATOM   5238 C CA  . ASP D 2 181 ? 43.695  19.392  47.881  1.00 26.38 ? 181  ASP V CA  1 
ATOM   5239 C C   . ASP D 2 181 ? 44.765  19.706  48.919  1.00 25.96 ? 181  ASP V C   1 
ATOM   5240 O O   . ASP D 2 181 ? 45.923  19.331  48.744  1.00 26.18 ? 181  ASP V O   1 
ATOM   5241 C CB  . ASP D 2 181 ? 42.465  18.748  48.532  1.00 26.33 ? 181  ASP V CB  1 
ATOM   5242 C CG  . ASP D 2 181 ? 42.772  17.453  49.241  1.00 26.28 ? 181  ASP V CG  1 
ATOM   5243 O OD1 . ASP D 2 181 ? 41.898  16.563  49.176  1.00 27.31 ? 181  ASP V OD1 1 
ATOM   5244 O OD2 . ASP D 2 181 ? 43.844  17.327  49.876  1.00 25.40 ? 181  ASP V OD2 1 
ATOM   5245 N N   . LEU D 2 182 ? 44.377  20.385  49.995  1.00 25.37 ? 182  LEU V N   1 
ATOM   5246 C CA  . LEU D 2 182 ? 45.359  20.929  50.934  1.00 25.02 ? 182  LEU V CA  1 
ATOM   5247 C C   . LEU D 2 182 ? 46.084  19.900  51.817  1.00 25.00 ? 182  LEU V C   1 
ATOM   5248 O O   . LEU D 2 182 ? 47.321  19.851  51.836  1.00 24.44 ? 182  LEU V O   1 
ATOM   5249 C CB  . LEU D 2 182 ? 44.738  22.042  51.772  1.00 24.75 ? 182  LEU V CB  1 
ATOM   5250 C CG  . LEU D 2 182 ? 45.730  23.133  52.166  1.00 23.73 ? 182  LEU V CG  1 
ATOM   5251 C CD1 . LEU D 2 182 ? 46.841  23.263  51.128  1.00 22.52 ? 182  LEU V CD1 1 
ATOM   5252 C CD2 . LEU D 2 182 ? 44.999  24.453  52.354  1.00 23.04 ? 182  LEU V CD2 1 
ATOM   5253 N N   . GLN D 2 183 ? 45.311  19.092  52.539  1.00 25.22 ? 183  GLN V N   1 
ATOM   5254 C CA  . GLN D 2 183 ? 45.831  17.941  53.265  1.00 25.73 ? 183  GLN V CA  1 
ATOM   5255 C C   . GLN D 2 183 ? 47.043  17.329  52.533  1.00 25.93 ? 183  GLN V C   1 
ATOM   5256 O O   . GLN D 2 183 ? 47.999  16.843  53.166  1.00 25.85 ? 183  GLN V O   1 
ATOM   5257 C CB  . GLN D 2 183 ? 44.689  16.923  53.460  1.00 25.88 ? 183  GLN V CB  1 
ATOM   5258 C CG  . GLN D 2 183 ? 45.062  15.424  53.470  1.00 26.49 ? 183  GLN V CG  1 
ATOM   5259 C CD  . GLN D 2 183 ? 45.756  14.984  54.745  1.00 27.57 ? 183  GLN V CD  1 
ATOM   5260 O OE1 . GLN D 2 183 ? 45.121  14.455  55.663  1.00 28.34 ? 183  GLN V OE1 1 
ATOM   5261 N NE2 . GLN D 2 183 ? 47.067  15.202  54.812  1.00 27.68 ? 183  GLN V NE2 1 
ATOM   5262 N N   . SER D 2 184 ? 46.996  17.406  51.200  1.00 26.03 ? 184  SER V N   1 
ATOM   5263 C CA  . SER D 2 184 ? 47.975  16.790  50.294  1.00 26.15 ? 184  SER V CA  1 
ATOM   5264 C C   . SER D 2 184 ? 49.380  17.414  50.300  1.00 25.79 ? 184  SER V C   1 
ATOM   5265 O O   . SER D 2 184 ? 50.298  16.867  49.699  1.00 25.60 ? 184  SER V O   1 
ATOM   5266 C CB  . SER D 2 184 ? 47.442  16.797  48.850  1.00 26.52 ? 184  SER V CB  1 
ATOM   5267 O OG  . SER D 2 184 ? 46.025  16.915  48.786  1.00 27.27 ? 184  SER V OG  1 
ATOM   5268 N N   . PHE D 2 185 ? 49.555  18.556  50.950  1.00 25.59 ? 185  PHE V N   1 
ATOM   5269 C CA  . PHE D 2 185 ? 50.873  19.187  50.970  1.00 25.56 ? 185  PHE V CA  1 
ATOM   5270 C C   . PHE D 2 185 ? 51.567  19.130  52.340  1.00 25.39 ? 185  PHE V C   1 
ATOM   5271 O O   . PHE D 2 185 ? 50.954  19.456  53.367  1.00 25.81 ? 185  PHE V O   1 
ATOM   5272 C CB  . PHE D 2 185 ? 50.786  20.635  50.489  1.00 25.74 ? 185  PHE V CB  1 
ATOM   5273 C CG  . PHE D 2 185 ? 50.623  20.775  49.002  1.00 25.82 ? 185  PHE V CG  1 
ATOM   5274 C CD1 . PHE D 2 185 ? 51.708  20.564  48.148  1.00 25.45 ? 185  PHE V CD1 1 
ATOM   5275 C CD2 . PHE D 2 185 ? 49.384  21.127  48.456  1.00 24.93 ? 185  PHE V CD2 1 
ATOM   5276 C CE1 . PHE D 2 185 ? 51.563  20.702  46.781  1.00 25.39 ? 185  PHE V CE1 1 
ATOM   5277 C CE2 . PHE D 2 185 ? 49.225  21.266  47.088  1.00 24.20 ? 185  PHE V CE2 1 
ATOM   5278 C CZ  . PHE D 2 185 ? 50.314  21.058  46.244  1.00 24.65 ? 185  PHE V CZ  1 
ATOM   5279 N N   . PRO D 2 186 ? 52.860  18.744  52.356  1.00 24.68 ? 186  PRO V N   1 
ATOM   5280 C CA  . PRO D 2 186 ? 53.598  18.696  53.606  1.00 24.15 ? 186  PRO V CA  1 
ATOM   5281 C C   . PRO D 2 186 ? 53.856  20.122  54.144  1.00 23.84 ? 186  PRO V C   1 
ATOM   5282 O O   . PRO D 2 186 ? 54.403  20.953  53.418  1.00 24.00 ? 186  PRO V O   1 
ATOM   5283 C CB  . PRO D 2 186 ? 54.913  18.046  53.185  1.00 24.11 ? 186  PRO V CB  1 
ATOM   5284 C CG  . PRO D 2 186 ? 55.118  18.502  51.779  1.00 23.97 ? 186  PRO V CG  1 
ATOM   5285 C CD  . PRO D 2 186 ? 53.747  18.574  51.185  1.00 24.47 ? 186  PRO V CD  1 
ATOM   5286 N N   . PRO D 2 187 ? 53.458  20.415  55.399  1.00 23.36 ? 187  PRO V N   1 
ATOM   5287 C CA  . PRO D 2 187 ? 53.793  21.736  55.930  1.00 22.97 ? 187  PRO V CA  1 
ATOM   5288 C C   . PRO D 2 187 ? 55.293  21.971  55.827  1.00 22.56 ? 187  PRO V C   1 
ATOM   5289 O O   . PRO D 2 187 ? 56.068  21.153  56.308  1.00 22.47 ? 187  PRO V O   1 
ATOM   5290 C CB  . PRO D 2 187 ? 53.361  21.648  57.397  1.00 23.07 ? 187  PRO V CB  1 
ATOM   5291 C CG  . PRO D 2 187 ? 52.330  20.581  57.436  1.00 23.01 ? 187  PRO V CG  1 
ATOM   5292 C CD  . PRO D 2 187 ? 52.733  19.591  56.384  1.00 23.42 ? 187  PRO V CD  1 
ATOM   5293 N N   . ASN D 2 188 ? 55.689  23.070  55.189  1.00 22.35 ? 188  ASN V N   1 
ATOM   5294 C CA  . ASN D 2 188 ? 57.106  23.315  54.863  1.00 22.15 ? 188  ASN V CA  1 
ATOM   5295 C C   . ASN D 2 188 ? 57.985  23.893  55.979  1.00 22.15 ? 188  ASN V C   1 
ATOM   5296 O O   . ASN D 2 188 ? 59.215  23.885  55.858  1.00 22.06 ? 188  ASN V O   1 
ATOM   5297 C CB  . ASN D 2 188 ? 57.254  24.142  53.573  1.00 22.01 ? 188  ASN V CB  1 
ATOM   5298 C CG  . ASN D 2 188 ? 56.360  25.371  53.552  1.00 20.94 ? 188  ASN V CG  1 
ATOM   5299 O OD1 . ASN D 2 188 ? 55.244  25.351  54.053  1.00 17.63 ? 188  ASN V OD1 1 
ATOM   5300 N ND2 . ASN D 2 188 ? 56.852  26.444  52.948  1.00 21.17 ? 188  ASN V ND2 1 
ATOM   5301 N N   . GLY D 2 189 ? 57.356  24.385  57.050  1.00 22.18 ? 189  GLY V N   1 
ATOM   5302 C CA  . GLY D 2 189 ? 58.078  24.816  58.255  1.00 22.25 ? 189  GLY V CA  1 
ATOM   5303 C C   . GLY D 2 189 ? 58.109  26.313  58.462  1.00 22.16 ? 189  GLY V C   1 
ATOM   5304 O O   . GLY D 2 189 ? 58.462  26.807  59.533  1.00 21.89 ? 189  GLY V O   1 
ATOM   5305 N N   . PHE D 2 190 ? 57.752  27.033  57.412  1.00 22.42 ? 190  PHE V N   1 
ATOM   5306 C CA  . PHE D 2 190 ? 57.559  28.457  57.498  1.00 22.83 ? 190  PHE V CA  1 
ATOM   5307 C C   . PHE D 2 190 ? 56.188  28.669  58.132  1.00 23.33 ? 190  PHE V C   1 
ATOM   5308 O O   . PHE D 2 190 ? 55.406  27.716  58.298  1.00 23.33 ? 190  PHE V O   1 
ATOM   5309 C CB  . PHE D 2 190 ? 57.625  29.084  56.100  1.00 22.48 ? 190  PHE V CB  1 
ATOM   5310 C CG  . PHE D 2 190 ? 58.910  28.798  55.357  1.00 22.80 ? 190  PHE V CG  1 
ATOM   5311 C CD1 . PHE D 2 190 ? 59.803  29.823  55.066  1.00 23.29 ? 190  PHE V CD1 1 
ATOM   5312 C CD2 . PHE D 2 190 ? 59.228  27.506  54.935  1.00 23.51 ? 190  PHE V CD2 1 
ATOM   5313 C CE1 . PHE D 2 190 ? 61.006  29.567  54.371  1.00 23.22 ? 190  PHE V CE1 1 
ATOM   5314 C CE2 . PHE D 2 190 ? 60.425  27.237  54.241  1.00 23.39 ? 190  PHE V CE2 1 
ATOM   5315 C CZ  . PHE D 2 190 ? 61.314  28.273  53.960  1.00 22.97 ? 190  PHE V CZ  1 
ATOM   5316 N N   . GLN D 2 191 ? 55.913  29.909  58.522  1.00 23.92 ? 191  GLN V N   1 
ATOM   5317 C CA  . GLN D 2 191 ? 54.568  30.323  58.928  1.00 24.65 ? 191  GLN V CA  1 
ATOM   5318 C C   . GLN D 2 191 ? 54.348  31.774  58.522  1.00 25.22 ? 191  GLN V C   1 
ATOM   5319 O O   . GLN D 2 191 ? 55.301  32.540  58.456  1.00 25.62 ? 191  GLN V O   1 
ATOM   5320 C CB  . GLN D 2 191 ? 54.375  30.214  60.431  1.00 24.62 ? 191  GLN V CB  1 
ATOM   5321 C CG  . GLN D 2 191 ? 55.288  29.256  61.152  1.00 24.66 ? 191  GLN V CG  1 
ATOM   5322 C CD  . GLN D 2 191 ? 55.445  29.639  62.600  1.00 24.32 ? 191  GLN V CD  1 
ATOM   5323 O OE1 . GLN D 2 191 ? 56.561  29.799  63.098  1.00 23.74 ? 191  GLN V OE1 1 
ATOM   5324 N NE2 . GLN D 2 191 ? 54.319  29.815  63.285  1.00 24.15 ? 191  GLN V NE2 1 
ATOM   5325 N N   . CYS D 2 192 ? 53.105  32.154  58.236  1.00 25.92 ? 192  CYS V N   1 
ATOM   5326 C CA  . CYS D 2 192 ? 52.782  33.549  57.907  1.00 26.56 ? 192  CYS V CA  1 
ATOM   5327 C C   . CYS D 2 192 ? 51.447  33.898  58.532  1.00 26.88 ? 192  CYS V C   1 
ATOM   5328 O O   . CYS D 2 192 ? 50.674  33.003  58.889  1.00 27.17 ? 192  CYS V O   1 
ATOM   5329 C CB  . CYS D 2 192 ? 52.730  33.775  56.397  1.00 26.57 ? 192  CYS V CB  1 
ATOM   5330 S SG  . CYS D 2 192 ? 54.199  33.220  55.473  1.00 27.82 ? 192  CYS V SG  1 
ATOM   5331 N N   . TYR D 2 193 ? 51.182  35.189  58.688  1.00 27.13 ? 193  TYR V N   1 
ATOM   5332 C CA  . TYR D 2 193 ? 49.960  35.614  59.330  1.00 27.60 ? 193  TYR V CA  1 
ATOM   5333 C C   . TYR D 2 193 ? 48.884  35.534  58.301  1.00 28.12 ? 193  TYR V C   1 
ATOM   5334 O O   . TYR D 2 193 ? 48.827  36.346  57.393  1.00 27.84 ? 193  TYR V O   1 
ATOM   5335 C CB  . TYR D 2 193 ? 50.075  37.038  59.850  1.00 27.47 ? 193  TYR V CB  1 
ATOM   5336 C CG  . TYR D 2 193 ? 51.079  37.183  60.938  1.00 27.83 ? 193  TYR V CG  1 
ATOM   5337 C CD1 . TYR D 2 193 ? 50.722  36.977  62.269  1.00 28.75 ? 193  TYR V CD1 1 
ATOM   5338 C CD2 . TYR D 2 193 ? 52.400  37.508  60.649  1.00 28.57 ? 193  TYR V CD2 1 
ATOM   5339 C CE1 . TYR D 2 193 ? 51.654  37.108  63.293  1.00 28.35 ? 193  TYR V CE1 1 
ATOM   5340 C CE2 . TYR D 2 193 ? 53.343  37.627  61.661  1.00 28.97 ? 193  TYR V CE2 1 
ATOM   5341 C CZ  . TYR D 2 193 ? 52.962  37.430  62.980  1.00 28.94 ? 193  TYR V CZ  1 
ATOM   5342 O OH  . TYR D 2 193 ? 53.898  37.559  63.982  1.00 30.19 ? 193  TYR V OH  1 
ATOM   5343 N N   . SER D 2 194 ? 48.047  34.524  58.427  1.00 29.37 ? 194  SER V N   1 
ATOM   5344 C CA  . SER D 2 194 ? 46.916  34.409  57.547  1.00 30.87 ? 194  SER V CA  1 
ATOM   5345 C C   . SER D 2 194 ? 45.795  35.278  58.059  1.00 32.02 ? 194  SER V C   1 
ATOM   5346 O O   . SER D 2 194 ? 45.666  35.501  59.269  1.00 32.02 ? 194  SER V O   1 
ATOM   5347 C CB  . SER D 2 194 ? 46.426  32.983  57.464  1.00 30.74 ? 194  SER V CB  1 
ATOM   5348 O OG  . SER D 2 194 ? 45.065  32.985  57.077  1.00 31.18 ? 194  SER V OG  1 
ATOM   5349 N N   . CYS D 2 195 ? 44.971  35.746  57.122  1.00 33.58 ? 195  CYS V N   1 
ATOM   5350 C CA  . CYS D 2 195 ? 43.850  36.612  57.445  1.00 34.92 ? 195  CYS V CA  1 
ATOM   5351 C C   . CYS D 2 195 ? 43.027  37.028  56.219  1.00 35.05 ? 195  CYS V C   1 
ATOM   5352 O O   . CYS D 2 195 ? 43.570  37.218  55.131  1.00 34.77 ? 195  CYS V O   1 
ATOM   5353 C CB  . CYS D 2 195 ? 44.367  37.829  58.212  1.00 35.12 ? 195  CYS V CB  1 
ATOM   5354 S SG  . CYS D 2 195 ? 43.495  39.345  57.924  1.00 38.19 ? 195  CYS V SG  1 
ATOM   5355 N N   . GLU D 2 196 ? 41.708  37.099  56.430  1.00 35.75 ? 196  GLU V N   1 
ATOM   5356 C CA  . GLU D 2 196 ? 40.728  37.782  55.561  1.00 36.39 ? 196  GLU V CA  1 
ATOM   5357 C C   . GLU D 2 196 ? 39.352  37.812  56.251  1.00 37.02 ? 196  GLU V C   1 
ATOM   5358 O O   . GLU D 2 196 ? 38.568  36.859  56.133  1.00 37.00 ? 196  GLU V O   1 
ATOM   5359 C CB  . GLU D 2 196 ? 40.630  37.161  54.151  1.00 36.27 ? 196  GLU V CB  1 
ATOM   5360 C CG  . GLU D 2 196 ? 39.404  37.621  53.299  1.00 35.39 ? 196  GLU V CG  1 
ATOM   5361 C CD  . GLU D 2 196 ? 39.097  39.117  53.388  1.00 34.30 ? 196  GLU V CD  1 
ATOM   5362 O OE1 . GLU D 2 196 ? 37.947  39.487  53.703  1.00 33.98 ? 196  GLU V OE1 1 
ATOM   5363 O OE2 . GLU D 2 196 ? 40.004  39.928  53.146  1.00 34.64 ? 196  GLU V OE2 1 
ATOM   5364 N N   . GLY D 2 197 ? 39.068  38.907  56.968  1.00 37.70 ? 197  GLY V N   1 
ATOM   5365 C CA  . GLY D 2 197 ? 37.791  39.057  57.691  1.00 38.14 ? 197  GLY V CA  1 
ATOM   5366 C C   . GLY D 2 197 ? 37.494  40.396  58.343  1.00 38.38 ? 197  GLY V C   1 
ATOM   5367 O O   . GLY D 2 197 ? 36.438  40.546  58.955  1.00 38.18 ? 197  GLY V O   1 
ATOM   5368 N N   . ASN D 2 198 ? 38.416  41.358  58.206  1.00 38.91 ? 198  ASN V N   1 
ATOM   5369 C CA  . ASN D 2 198 ? 38.302  42.694  58.833  1.00 39.48 ? 198  ASN V CA  1 
ATOM   5370 C C   . ASN D 2 198 ? 39.026  43.873  58.123  1.00 39.94 ? 198  ASN V C   1 
ATOM   5371 O O   . ASN D 2 198 ? 38.582  44.328  57.066  1.00 39.78 ? 198  ASN V O   1 
ATOM   5372 C CB  . ASN D 2 198 ? 38.701  42.630  60.318  1.00 39.36 ? 198  ASN V CB  1 
ATOM   5373 C CG  . ASN D 2 198 ? 37.522  42.808  61.253  1.00 39.29 ? 198  ASN V CG  1 
ATOM   5374 O OD1 . ASN D 2 198 ? 37.676  42.759  62.468  1.00 39.42 ? 198  ASN V OD1 1 
ATOM   5375 N ND2 . ASN D 2 198 ? 36.339  43.034  60.692  1.00 39.15 ? 198  ASN V ND2 1 
ATOM   5376 N N   . ASN D 2 199 ? 40.111  44.371  58.736  1.00 40.67 ? 199  ASN V N   1 
ATOM   5377 C CA  . ASN D 2 199 ? 40.919  45.520  58.237  1.00 41.17 ? 199  ASN V CA  1 
ATOM   5378 C C   . ASN D 2 199 ? 42.151  45.894  59.136  1.00 41.30 ? 199  ASN V C   1 
ATOM   5379 O O   . ASN D 2 199 ? 43.072  45.069  59.323  1.00 41.43 ? 199  ASN V O   1 
ATOM   5380 C CB  . ASN D 2 199 ? 40.029  46.755  57.957  1.00 41.24 ? 199  ASN V CB  1 
ATOM   5381 C CG  . ASN D 2 199 ? 40.781  47.892  57.248  1.00 41.79 ? 199  ASN V CG  1 
ATOM   5382 O OD1 . ASN D 2 199 ? 40.439  49.072  57.412  1.00 42.54 ? 199  ASN V OD1 1 
ATOM   5383 N ND2 . ASN D 2 199 ? 41.807  47.542  56.466  1.00 41.65 ? 199  ASN V ND2 1 
ATOM   5384 N N   . THR D 2 200 ? 42.159  47.127  59.666  1.00 40.99 ? 200  THR V N   1 
ATOM   5385 C CA  . THR D 2 200 ? 43.287  47.671  60.447  1.00 40.69 ? 200  THR V CA  1 
ATOM   5386 C C   . THR D 2 200 ? 43.020  47.642  61.962  1.00 40.45 ? 200  THR V C   1 
ATOM   5387 O O   . THR D 2 200 ? 43.770  48.226  62.765  1.00 40.51 ? 200  THR V O   1 
ATOM   5388 C CB  . THR D 2 200 ? 43.699  49.101  59.987  1.00 40.74 ? 200  THR V CB  1 
ATOM   5389 O OG1 . THR D 2 200 ? 42.526  49.879  59.718  1.00 40.80 ? 200  THR V OG1 1 
ATOM   5390 C CG2 . THR D 2 200 ? 44.578  49.045  58.734  1.00 40.63 ? 200  THR V CG2 1 
ATOM   5391 N N   . LEU D 2 201 ? 41.924  46.981  62.327  1.00 39.85 ? 201  LEU V N   1 
ATOM   5392 C CA  . LEU D 2 201 ? 41.729  46.406  63.661  1.00 39.06 ? 201  LEU V CA  1 
ATOM   5393 C C   . LEU D 2 201 ? 40.779  45.212  63.491  1.00 38.80 ? 201  LEU V C   1 
ATOM   5394 O O   . LEU D 2 201 ? 39.872  45.230  62.651  1.00 38.71 ? 201  LEU V O   1 
ATOM   5395 C CB  . LEU D 2 201 ? 41.290  47.442  64.723  1.00 38.69 ? 201  LEU V CB  1 
ATOM   5396 C CG  . LEU D 2 201 ? 39.881  48.003  64.922  1.00 37.91 ? 201  LEU V CG  1 
ATOM   5397 C CD1 . LEU D 2 201 ? 39.821  48.672  66.283  1.00 37.19 ? 201  LEU V CD1 1 
ATOM   5398 C CD2 . LEU D 2 201 ? 39.481  48.977  63.820  1.00 37.10 ? 201  LEU V CD2 1 
ATOM   5399 N N   . GLY D 2 202 ? 41.034  44.154  64.252  1.00 38.42 ? 202  GLY V N   1 
ATOM   5400 C CA  . GLY D 2 202 ? 40.416  42.860  63.995  1.00 37.96 ? 202  GLY V CA  1 
ATOM   5401 C C   . GLY D 2 202 ? 41.381  41.965  63.232  1.00 37.59 ? 202  GLY V C   1 
ATOM   5402 O O   . GLY D 2 202 ? 41.954  41.025  63.796  1.00 37.56 ? 202  GLY V O   1 
ATOM   5403 N N   . CYS D 2 203 ? 41.567  42.262  61.948  1.00 37.03 ? 203  CYS V N   1 
ATOM   5404 C CA  . CYS D 2 203 ? 42.527  41.533  61.125  1.00 36.53 ? 203  CYS V CA  1 
ATOM   5405 C C   . CYS D 2 203 ? 43.808  42.371  60.945  1.00 35.58 ? 203  CYS V C   1 
ATOM   5406 O O   . CYS D 2 203 ? 44.471  42.343  59.897  1.00 35.40 ? 203  CYS V O   1 
ATOM   5407 C CB  . CYS D 2 203 ? 41.884  41.138  59.790  1.00 36.83 ? 203  CYS V CB  1 
ATOM   5408 S SG  . CYS D 2 203 ? 42.027  39.354  59.355  1.00 38.98 ? 203  CYS V SG  1 
ATOM   5409 N N   . SER D 2 204 ? 44.132  43.121  61.998  1.00 34.52 ? 204  SER V N   1 
ATOM   5410 C CA  . SER D 2 204 ? 45.356  43.908  62.079  1.00 33.59 ? 204  SER V CA  1 
ATOM   5411 C C   . SER D 2 204 ? 46.404  43.099  62.831  1.00 33.16 ? 204  SER V C   1 
ATOM   5412 O O   . SER D 2 204 ? 46.587  41.909  62.549  1.00 33.34 ? 204  SER V O   1 
ATOM   5413 C CB  . SER D 2 204 ? 45.097  45.227  62.812  1.00 33.52 ? 204  SER V CB  1 
ATOM   5414 O OG  . SER D 2 204 ? 44.768  45.015  64.175  1.00 32.36 ? 204  SER V OG  1 
ATOM   5415 N N   . SER D 2 205 ? 47.090  43.750  63.779  1.00 32.28 ? 205  SER V N   1 
ATOM   5416 C CA  . SER D 2 205 ? 47.922  43.057  64.771  1.00 31.12 ? 205  SER V CA  1 
ATOM   5417 C C   . SER D 2 205 ? 47.018  42.566  65.906  1.00 30.62 ? 205  SER V C   1 
ATOM   5418 O O   . SER D 2 205 ? 47.485  42.045  66.915  1.00 30.09 ? 205  SER V O   1 
ATOM   5419 C CB  . SER D 2 205 ? 49.019  43.979  65.297  1.00 31.03 ? 205  SER V CB  1 
ATOM   5420 O OG  . SER D 2 205 ? 49.876  44.416  64.261  1.00 29.71 ? 205  SER V OG  1 
ATOM   5421 N N   . GLU D 2 206 ? 45.713  42.762  65.706  1.00 30.20 ? 206  GLU V N   1 
ATOM   5422 C CA  . GLU D 2 206 ? 44.654  42.220  66.546  1.00 29.80 ? 206  GLU V CA  1 
ATOM   5423 C C   . GLU D 2 206 ? 44.470  40.727  66.252  1.00 29.61 ? 206  GLU V C   1 
ATOM   5424 O O   . GLU D 2 206 ? 43.355  40.220  66.091  1.00 29.45 ? 206  GLU V O   1 
ATOM   5425 C CB  . GLU D 2 206 ? 43.353  43.015  66.345  1.00 29.76 ? 206  GLU V CB  1 
ATOM   5426 C CG  . GLU D 2 206 ? 42.130  42.538  67.153  1.00 29.57 ? 206  GLU V CG  1 
ATOM   5427 C CD  . GLU D 2 206 ? 42.167  42.898  68.633  1.00 29.30 ? 206  GLU V CD  1 
ATOM   5428 O OE1 . GLU D 2 206 ? 43.260  43.181  69.174  1.00 29.58 ? 206  GLU V OE1 1 
ATOM   5429 O OE2 . GLU D 2 206 ? 41.086  42.884  69.262  1.00 28.82 ? 206  GLU V OE2 1 
ATOM   5430 N N   . GLU D 2 207 ? 45.601  40.036  66.169  1.00 29.47 ? 207  GLU V N   1 
ATOM   5431 C CA  . GLU D 2 207 ? 45.654  38.579  66.251  1.00 29.21 ? 207  GLU V CA  1 
ATOM   5432 C C   . GLU D 2 207 ? 44.904  37.878  65.133  1.00 28.72 ? 207  GLU V C   1 
ATOM   5433 O O   . GLU D 2 207 ? 44.095  36.984  65.387  1.00 28.65 ? 207  GLU V O   1 
ATOM   5434 C CB  . GLU D 2 207 ? 45.155  38.094  67.628  1.00 29.44 ? 207  GLU V CB  1 
ATOM   5435 C CG  . GLU D 2 207 ? 45.922  38.663  68.824  1.00 29.42 ? 207  GLU V CG  1 
ATOM   5436 C CD  . GLU D 2 207 ? 45.844  40.184  68.899  1.00 29.54 ? 207  GLU V CD  1 
ATOM   5437 O OE1 . GLU D 2 207 ? 46.828  40.850  68.524  1.00 29.63 ? 207  GLU V OE1 1 
ATOM   5438 O OE2 . GLU D 2 207 ? 44.786  40.720  69.287  1.00 29.41 ? 207  GLU V OE2 1 
ATOM   5439 N N   . ALA D 2 208 ? 45.172  38.288  63.898  1.00 28.26 ? 208  ALA V N   1 
ATOM   5440 C CA  . ALA D 2 208 ? 44.686  37.528  62.745  1.00 27.98 ? 208  ALA V CA  1 
ATOM   5441 C C   . ALA D 2 208 ? 45.598  36.317  62.547  1.00 27.56 ? 208  ALA V C   1 
ATOM   5442 O O   . ALA D 2 208 ? 46.746  36.436  62.105  1.00 27.69 ? 208  ALA V O   1 
ATOM   5443 C CB  . ALA D 2 208 ? 44.624  38.385  61.501  1.00 27.99 ? 208  ALA V CB  1 
ATOM   5444 N N   . SER D 2 209 ? 45.067  35.157  62.903  1.00 26.74 ? 209  SER V N   1 
ATOM   5445 C CA  . SER D 2 209 ? 45.830  33.926  63.045  1.00 26.02 ? 209  SER V CA  1 
ATOM   5446 C C   . SER D 2 209 ? 47.244  33.858  62.450  1.00 25.59 ? 209  SER V C   1 
ATOM   5447 O O   . SER D 2 209 ? 47.594  34.543  61.485  1.00 25.05 ? 209  SER V O   1 
ATOM   5448 C CB  . SER D 2 209 ? 44.988  32.754  62.539  1.00 26.11 ? 209  SER V CB  1 
ATOM   5449 O OG  . SER D 2 209 ? 43.715  32.771  63.158  1.00 25.75 ? 209  SER V OG  1 
ATOM   5450 N N   . LEU D 2 210 ? 48.050  33.016  63.078  1.00 25.40 ? 210  LEU V N   1 
ATOM   5451 C CA  . LEU D 2 210 ? 49.268  32.510  62.492  1.00 25.31 ? 210  LEU V CA  1 
ATOM   5452 C C   . LEU D 2 210 ? 48.895  31.241  61.750  1.00 25.31 ? 210  LEU V C   1 
ATOM   5453 O O   . LEU D 2 210 ? 47.982  30.540  62.169  1.00 25.47 ? 210  LEU V O   1 
ATOM   5454 C CB  . LEU D 2 210 ? 50.227  32.123  63.601  1.00 25.19 ? 210  LEU V CB  1 
ATOM   5455 C CG  . LEU D 2 210 ? 51.703  32.432  63.414  1.00 25.26 ? 210  LEU V CG  1 
ATOM   5456 C CD1 . LEU D 2 210 ? 52.148  32.444  61.951  1.00 24.77 ? 210  LEU V CD1 1 
ATOM   5457 C CD2 . LEU D 2 210 ? 51.943  33.771  64.055  1.00 26.23 ? 210  LEU V CD2 1 
ATOM   5458 N N   . ILE D 2 211 ? 49.575  30.936  60.651  1.00 25.26 ? 211  ILE V N   1 
ATOM   5459 C CA  . ILE D 2 211 ? 49.388  29.632  60.012  1.00 25.48 ? 211  ILE V CA  1 
ATOM   5460 C C   . ILE D 2 211 ? 50.710  29.159  59.468  1.00 25.65 ? 211  ILE V C   1 
ATOM   5461 O O   . ILE D 2 211 ? 51.492  29.969  58.959  1.00 25.56 ? 211  ILE V O   1 
ATOM   5462 C CB  . ILE D 2 211 ? 48.333  29.620  58.851  1.00 25.59 ? 211  ILE V CB  1 
ATOM   5463 C CG1 . ILE D 2 211 ? 48.846  30.381  57.621  1.00 25.17 ? 211  ILE V CG1 1 
ATOM   5464 C CG2 . ILE D 2 211 ? 46.943  30.121  59.322  1.00 25.98 ? 211  ILE V CG2 1 
ATOM   5465 C CD1 . ILE D 2 211 ? 48.244  29.936  56.328  1.00 24.20 ? 211  ILE V CD1 1 
ATOM   5466 N N   . ASN D 2 212 ? 50.955  27.852  59.598  1.00 25.83 ? 212  ASN V N   1 
ATOM   5467 C CA  . ASN D 2 212 ? 52.118  27.199  58.990  1.00 25.70 ? 212  ASN V CA  1 
ATOM   5468 C C   . ASN D 2 212 ? 51.776  26.992  57.547  1.00 25.56 ? 212  ASN V C   1 
ATOM   5469 O O   . ASN D 2 212 ? 50.652  26.589  57.220  1.00 25.38 ? 212  ASN V O   1 
ATOM   5470 C CB  . ASN D 2 212 ? 52.417  25.841  59.629  1.00 25.68 ? 212  ASN V CB  1 
ATOM   5471 C CG  . ASN D 2 212 ? 52.502  25.915  61.131  1.00 25.97 ? 212  ASN V CG  1 
ATOM   5472 O OD1 . ASN D 2 212 ? 53.362  26.603  61.673  1.00 26.98 ? 212  ASN V OD1 1 
ATOM   5473 N ND2 . ASN D 2 212 ? 51.601  25.217  61.819  1.00 25.87 ? 212  ASN V ND2 1 
ATOM   5474 N N   . CYS D 2 213 ? 52.740  27.282  56.686  1.00 25.34 ? 213  CYS V N   1 
ATOM   5475 C CA  . CYS D 2 213 ? 52.515  27.192  55.259  1.00 25.46 ? 213  CYS V CA  1 
ATOM   5476 C C   . CYS D 2 213 ? 52.766  25.769  54.746  1.00 24.96 ? 213  CYS V C   1 
ATOM   5477 O O   . CYS D 2 213 ? 53.484  24.993  55.388  1.00 24.78 ? 213  CYS V O   1 
ATOM   5478 C CB  . CYS D 2 213 ? 53.381  28.221  54.539  1.00 25.66 ? 213  CYS V CB  1 
ATOM   5479 S SG  . CYS D 2 213 ? 53.178  29.939  55.157  1.00 27.59 ? 213  CYS V SG  1 
ATOM   5480 N N   . ARG D 2 214 ? 52.158  25.428  53.605  1.00 24.42 ? 214  ARG V N   1 
ATOM   5481 C CA  . ARG D 2 214 ? 52.310  24.094  53.002  1.00 23.85 ? 214  ARG V CA  1 
ATOM   5482 C C   . ARG D 2 214 ? 52.862  24.124  51.571  1.00 23.71 ? 214  ARG V C   1 
ATOM   5483 O O   . ARG D 2 214 ? 53.013  25.190  50.973  1.00 23.49 ? 214  ARG V O   1 
ATOM   5484 C CB  . ARG D 2 214 ? 50.994  23.319  53.049  1.00 23.53 ? 214  ARG V CB  1 
ATOM   5485 C CG  . ARG D 2 214 ? 50.129  23.666  54.241  1.00 22.78 ? 214  ARG V CG  1 
ATOM   5486 C CD  . ARG D 2 214 ? 49.109  22.600  54.516  1.00 21.82 ? 214  ARG V CD  1 
ATOM   5487 N NE  . ARG D 2 214 ? 49.706  21.444  55.170  1.00 22.31 ? 214  ARG V NE  1 
ATOM   5488 C CZ  . ARG D 2 214 ? 49.016  20.550  55.867  1.00 23.54 ? 214  ARG V CZ  1 
ATOM   5489 N NH1 . ARG D 2 214 ? 47.703  20.673  56.002  1.00 24.26 ? 214  ARG V NH1 1 
ATOM   5490 N NH2 . ARG D 2 214 ? 49.634  19.528  56.435  1.00 25.04 ? 214  ARG V NH2 1 
ATOM   5491 N N   . GLY D 2 215 ? 53.179  22.945  51.043  1.00 23.60 ? 215  GLY V N   1 
ATOM   5492 C CA  . GLY D 2 215 ? 53.695  22.803  49.682  1.00 23.66 ? 215  GLY V CA  1 
ATOM   5493 C C   . GLY D 2 215 ? 54.826  23.745  49.306  1.00 23.64 ? 215  GLY V C   1 
ATOM   5494 O O   . GLY D 2 215 ? 55.750  23.931  50.089  1.00 23.67 ? 215  GLY V O   1 
ATOM   5495 N N   . PRO D 2 216 ? 54.744  24.366  48.107  1.00 23.77 ? 216  PRO V N   1 
ATOM   5496 C CA  . PRO D 2 216 ? 55.809  25.182  47.549  1.00 23.66 ? 216  PRO V CA  1 
ATOM   5497 C C   . PRO D 2 216 ? 55.667  26.614  48.007  1.00 23.71 ? 216  PRO V C   1 
ATOM   5498 O O   . PRO D 2 216 ? 56.236  27.516  47.393  1.00 23.66 ? 216  PRO V O   1 
ATOM   5499 C CB  . PRO D 2 216 ? 55.512  25.120  46.059  1.00 23.55 ? 216  PRO V CB  1 
ATOM   5500 C CG  . PRO D 2 216 ? 54.021  25.149  46.014  1.00 23.60 ? 216  PRO V CG  1 
ATOM   5501 C CD  . PRO D 2 216 ? 53.540  24.427  47.251  1.00 24.01 ? 216  PRO V CD  1 
ATOM   5502 N N   . MET D 2 217 ? 54.907  26.808  49.082  1.00 23.89 ? 217  MET V N   1 
ATOM   5503 C CA  . MET D 2 217 ? 54.509  28.141  49.532  1.00 24.10 ? 217  MET V CA  1 
ATOM   5504 C C   . MET D 2 217 ? 55.268  28.604  50.775  1.00 23.52 ? 217  MET V C   1 
ATOM   5505 O O   . MET D 2 217 ? 54.908  28.300  51.904  1.00 23.28 ? 217  MET V O   1 
ATOM   5506 C CB  . MET D 2 217 ? 52.985  28.205  49.719  1.00 24.49 ? 217  MET V CB  1 
ATOM   5507 C CG  . MET D 2 217 ? 52.225  27.597  48.531  1.00 25.74 ? 217  MET V CG  1 
ATOM   5508 S SD  . MET D 2 217 ? 50.423  27.548  48.647  1.00 28.60 ? 217  MET V SD  1 
ATOM   5509 C CE  . MET D 2 217 ? 50.111  26.084  47.638  1.00 26.04 ? 217  MET V CE  1 
ATOM   5510 N N   . ASN D 2 218 ? 56.328  29.353  50.539  1.00 23.06 ? 218  ASN V N   1 
ATOM   5511 C CA  . ASN D 2 218 ? 57.196  29.766  51.601  1.00 22.97 ? 218  ASN V CA  1 
ATOM   5512 C C   . ASN D 2 218 ? 57.444  31.267  51.584  1.00 23.29 ? 218  ASN V C   1 
ATOM   5513 O O   . ASN D 2 218 ? 58.385  31.755  52.224  1.00 23.80 ? 218  ASN V O   1 
ATOM   5514 C CB  . ASN D 2 218 ? 58.508  28.990  51.533  1.00 22.81 ? 218  ASN V CB  1 
ATOM   5515 C CG  . ASN D 2 218 ? 58.965  28.729  50.109  1.00 22.30 ? 218  ASN V CG  1 
ATOM   5516 O OD1 . ASN D 2 218 ? 59.915  29.353  49.615  1.00 20.79 ? 218  ASN V OD1 1 
ATOM   5517 N ND2 . ASN D 2 218 ? 58.297  27.790  49.442  1.00 21.87 ? 218  ASN V ND2 1 
ATOM   5518 N N   . GLN D 2 219 ? 56.607  32.000  50.851  1.00 23.20 ? 219  GLN V N   1 
ATOM   5519 C CA  . GLN D 2 219 ? 56.623  33.460  50.909  1.00 22.96 ? 219  GLN V CA  1 
ATOM   5520 C C   . GLN D 2 219 ? 55.426  33.907  51.694  1.00 22.98 ? 219  GLN V C   1 
ATOM   5521 O O   . GLN D 2 219 ? 54.344  33.320  51.587  1.00 22.70 ? 219  GLN V O   1 
ATOM   5522 C CB  . GLN D 2 219 ? 56.537  34.078  49.522  1.00 22.95 ? 219  GLN V CB  1 
ATOM   5523 C CG  . GLN D 2 219 ? 57.334  33.366  48.479  1.00 22.82 ? 219  GLN V CG  1 
ATOM   5524 C CD  . GLN D 2 219 ? 58.794  33.532  48.697  1.00 22.62 ? 219  GLN V CD  1 
ATOM   5525 O OE1 . GLN D 2 219 ? 59.331  34.624  48.534  1.00 23.28 ? 219  GLN V OE1 1 
ATOM   5526 N NE2 . GLN D 2 219 ? 59.460  32.450  49.071  1.00 22.72 ? 219  GLN V NE2 1 
ATOM   5527 N N   . CYS D 2 220 ? 55.616  34.947  52.489  1.00 23.37 ? 220  CYS V N   1 
ATOM   5528 C CA  . CYS D 2 220 ? 54.493  35.580  53.159  1.00 24.06 ? 220  CYS V CA  1 
ATOM   5529 C C   . CYS D 2 220 ? 53.986  36.709  52.287  1.00 24.24 ? 220  CYS V C   1 
ATOM   5530 O O   . CYS D 2 220 ? 54.753  37.316  51.538  1.00 24.83 ? 220  CYS V O   1 
ATOM   5531 C CB  . CYS D 2 220 ? 54.898  36.079  54.529  1.00 23.83 ? 220  CYS V CB  1 
ATOM   5532 S SG  . CYS D 2 220 ? 55.544  34.772  55.589  1.00 25.70 ? 220  CYS V SG  1 
ATOM   5533 N N   . LEU D 2 221 ? 52.689  36.974  52.347  1.00 24.14 ? 221  LEU V N   1 
ATOM   5534 C CA  . LEU D 2 221 ? 52.103  37.939  51.434  1.00 23.98 ? 221  LEU V CA  1 
ATOM   5535 C C   . LEU D 2 221 ? 51.034  38.834  52.081  1.00 24.21 ? 221  LEU V C   1 
ATOM   5536 O O   . LEU D 2 221 ? 50.158  38.354  52.826  1.00 24.38 ? 221  LEU V O   1 
ATOM   5537 C CB  . LEU D 2 221 ? 51.548  37.217  50.194  1.00 23.75 ? 221  LEU V CB  1 
ATOM   5538 C CG  . LEU D 2 221 ? 50.939  38.007  49.020  1.00 23.64 ? 221  LEU V CG  1 
ATOM   5539 C CD1 . LEU D 2 221 ? 51.239  37.344  47.673  1.00 23.36 ? 221  LEU V CD1 1 
ATOM   5540 C CD2 . LEU D 2 221 ? 49.434  38.253  49.189  1.00 22.27 ? 221  LEU V CD2 1 
ATOM   5541 N N   . VAL D 2 222 ? 51.129  40.135  51.779  1.00 23.89 ? 222  VAL V N   1 
ATOM   5542 C CA  . VAL D 2 222 ? 50.075  41.114  52.060  1.00 23.24 ? 222  VAL V CA  1 
ATOM   5543 C C   . VAL D 2 222 ? 49.360  41.555  50.762  1.00 23.04 ? 222  VAL V C   1 
ATOM   5544 O O   . VAL D 2 222 ? 49.927  41.464  49.667  1.00 23.22 ? 222  VAL V O   1 
ATOM   5545 C CB  . VAL D 2 222 ? 50.660  42.335  52.764  1.00 22.95 ? 222  VAL V CB  1 
ATOM   5546 C CG1 . VAL D 2 222 ? 49.553  43.217  53.282  1.00 22.73 ? 222  VAL V CG1 1 
ATOM   5547 C CG2 . VAL D 2 222 ? 51.542  41.893  53.908  1.00 23.16 ? 222  VAL V CG2 1 
ATOM   5548 N N   . ALA D 2 223 ? 48.116  42.018  50.891  1.00 22.53 ? 223  ALA V N   1 
ATOM   5549 C CA  . ALA D 2 223 ? 47.375  42.623  49.777  1.00 22.16 ? 223  ALA V CA  1 
ATOM   5550 C C   . ALA D 2 223 ? 46.386  43.691  50.280  1.00 21.93 ? 223  ALA V C   1 
ATOM   5551 O O   . ALA D 2 223 ? 45.866  43.584  51.384  1.00 22.02 ? 223  ALA V O   1 
ATOM   5552 C CB  . ALA D 2 223 ? 46.660  41.547  48.973  1.00 22.08 ? 223  ALA V CB  1 
ATOM   5553 N N   . THR D 2 224 ? 46.143  44.727  49.486  1.00 21.45 ? 224  THR V N   1 
ATOM   5554 C CA  . THR D 2 224 ? 45.253  45.799  49.910  1.00 21.46 ? 224  THR V CA  1 
ATOM   5555 C C   . THR D 2 224 ? 44.528  46.362  48.714  1.00 21.22 ? 224  THR V C   1 
ATOM   5556 O O   . THR D 2 224 ? 45.130  46.545  47.650  1.00 21.23 ? 224  THR V O   1 
ATOM   5557 C CB  . THR D 2 224 ? 46.027  46.973  50.529  1.00 21.74 ? 224  THR V CB  1 
ATOM   5558 O OG1 . THR D 2 224 ? 47.155  46.482  51.256  1.00 22.85 ? 224  THR V OG1 1 
ATOM   5559 C CG2 . THR D 2 224 ? 45.127  47.828  51.446  1.00 21.76 ? 224  THR V CG2 1 
ATOM   5560 N N   . GLY D 2 225 ? 43.248  46.678  48.912  1.00 20.73 ? 225  GLY V N   1 
ATOM   5561 C CA  . GLY D 2 225 ? 42.411  47.211  47.855  1.00 19.92 ? 225  GLY V CA  1 
ATOM   5562 C C   . GLY D 2 225 ? 41.380  48.190  48.354  1.00 19.56 ? 225  GLY V C   1 
ATOM   5563 O O   . GLY D 2 225 ? 40.424  47.797  49.030  1.00 19.48 ? 225  GLY V O   1 
ATOM   5564 N N   . LEU D 2 226 ? 41.585  49.467  48.020  1.00 19.18 ? 226  LEU V N   1 
ATOM   5565 C CA  . LEU D 2 226 ? 40.623  50.520  48.324  1.00 18.61 ? 226  LEU V CA  1 
ATOM   5566 C C   . LEU D 2 226 ? 39.432  50.278  47.419  1.00 18.40 ? 226  LEU V C   1 
ATOM   5567 O O   . LEU D 2 226 ? 39.583  49.759  46.303  1.00 18.44 ? 226  LEU V O   1 
ATOM   5568 C CB  . LEU D 2 226 ? 41.236  51.903  48.095  1.00 18.48 ? 226  LEU V CB  1 
ATOM   5569 C CG  . LEU D 2 226 ? 40.505  53.248  48.332  1.00 19.28 ? 226  LEU V CG  1 
ATOM   5570 C CD1 . LEU D 2 226 ? 39.791  53.736  47.064  1.00 19.97 ? 226  LEU V CD1 1 
ATOM   5571 C CD2 . LEU D 2 226 ? 39.564  53.300  49.550  1.00 18.96 ? 226  LEU V CD2 1 
ATOM   5572 N N   . ASP D 2 227 ? 38.247  50.628  47.910  1.00 17.99 ? 227  ASP V N   1 
ATOM   5573 C CA  . ASP D 2 227 ? 37.005  50.320  47.205  1.00 17.23 ? 227  ASP V CA  1 
ATOM   5574 C C   . ASP D 2 227 ? 36.352  51.554  46.586  1.00 16.76 ? 227  ASP V C   1 
ATOM   5575 O O   . ASP D 2 227 ? 36.546  51.822  45.401  1.00 16.80 ? 227  ASP V O   1 
ATOM   5576 C CB  . ASP D 2 227 ? 36.024  49.596  48.132  1.00 17.10 ? 227  ASP V CB  1 
ATOM   5577 C CG  . ASP D 2 227 ? 34.715  49.301  47.463  1.00 16.79 ? 227  ASP V CG  1 
ATOM   5578 O OD1 . ASP D 2 227 ? 34.713  48.478  46.527  1.00 16.93 ? 227  ASP V OD1 1 
ATOM   5579 O OD2 . ASP D 2 227 ? 33.696  49.902  47.864  1.00 16.81 ? 227  ASP V OD2 1 
ATOM   5580 N N   . VAL D 2 228 ? 35.595  52.300  47.390  1.00 15.96 ? 228  VAL V N   1 
ATOM   5581 C CA  . VAL D 2 228 ? 34.772  53.392  46.893  1.00 15.35 ? 228  VAL V CA  1 
ATOM   5582 C C   . VAL D 2 228 ? 33.383  52.842  46.565  1.00 14.86 ? 228  VAL V C   1 
ATOM   5583 O O   . VAL D 2 228 ? 32.638  52.430  47.457  1.00 14.20 ? 228  VAL V O   1 
ATOM   5584 C CB  . VAL D 2 228 ? 35.427  54.107  45.662  1.00 15.32 ? 228  VAL V CB  1 
ATOM   5585 C CG1 . VAL D 2 228 ? 34.522  55.151  45.091  1.00 15.33 ? 228  VAL V CG1 1 
ATOM   5586 C CG2 . VAL D 2 228 ? 36.745  54.764  46.046  1.00 15.75 ? 228  VAL V CG2 1 
ATOM   5587 N N   . ARG D 2 232 ? 34.958  48.928  53.141  1.00 2.00  ? 232  ARG V N   1 
ATOM   5588 C CA  . ARG D 2 232 ? 35.575  49.592  51.997  1.00 2.00  ? 232  ARG V CA  1 
ATOM   5589 C C   . ARG D 2 232 ? 37.089  49.355  51.846  1.00 2.00  ? 232  ARG V C   1 
ATOM   5590 O O   . ARG D 2 232 ? 37.600  49.218  50.746  1.00 2.00  ? 232  ARG V O   1 
ATOM   5591 C CB  . ARG D 2 232 ? 35.224  51.090  51.975  1.00 2.00  ? 232  ARG V CB  1 
ATOM   5592 C CG  . ARG D 2 232 ? 33.740  51.370  51.651  1.00 2.00  ? 232  ARG V CG  1 
ATOM   5593 C CD  . ARG D 2 232 ? 33.533  52.662  50.934  1.00 2.00  ? 232  ARG V CD  1 
ATOM   5594 N NE  . ARG D 2 232 ? 33.706  53.790  51.837  1.00 2.00  ? 232  ARG V NE  1 
ATOM   5595 C CZ  . ARG D 2 232 ? 34.826  54.499  51.968  1.00 2.00  ? 232  ARG V CZ  1 
ATOM   5596 N NH1 . ARG D 2 232 ? 35.900  54.202  51.251  1.00 2.00  ? 232  ARG V NH1 1 
ATOM   5597 N NH2 . ARG D 2 232 ? 34.869  55.515  52.816  1.00 2.00  ? 232  ARG V NH2 1 
ATOM   5598 N N   . SER D 2 233 ? 37.811  49.325  52.953  1.00 3.44  ? 233  SER V N   1 
ATOM   5599 C CA  . SER D 2 233 ? 39.226  48.943  52.949  1.00 5.14  ? 233  SER V CA  1 
ATOM   5600 C C   . SER D 2 233 ? 39.321  47.419  53.053  1.00 6.25  ? 233  SER V C   1 
ATOM   5601 O O   . SER D 2 233 ? 38.740  46.816  53.953  1.00 6.59  ? 233  SER V O   1 
ATOM   5602 C CB  . SER D 2 233 ? 39.947  49.604  54.129  1.00 5.01  ? 233  SER V CB  1 
ATOM   5603 O OG  . SER D 2 233 ? 41.298  49.186  54.194  1.00 5.48  ? 233  SER V OG  1 
ATOM   5604 N N   . TYR D 2 234 ? 40.042  46.781  52.150  1.00 7.65  ? 234  TYR V N   1 
ATOM   5605 C CA  . TYR D 2 234 ? 39.958  45.329  52.087  1.00 9.40  ? 234  TYR V CA  1 
ATOM   5606 C C   . TYR D 2 234 ? 41.358  44.718  51.909  1.00 9.87  ? 234  TYR V C   1 
ATOM   5607 O O   . TYR D 2 234 ? 42.133  45.169  51.065  1.00 10.43 ? 234  TYR V O   1 
ATOM   5608 C CB  . TYR D 2 234 ? 38.957  44.936  50.980  1.00 9.64  ? 234  TYR V CB  1 
ATOM   5609 C CG  . TYR D 2 234 ? 38.717  43.452  50.811  1.00 12.46 ? 234  TYR V CG  1 
ATOM   5610 C CD1 . TYR D 2 234 ? 37.491  42.868  51.178  1.00 14.78 ? 234  TYR V CD1 1 
ATOM   5611 C CD2 . TYR D 2 234 ? 39.719  42.608  50.260  1.00 13.80 ? 234  TYR V CD2 1 
ATOM   5612 C CE1 . TYR D 2 234 ? 37.272  41.454  51.005  1.00 14.67 ? 234  TYR V CE1 1 
ATOM   5613 C CE2 . TYR D 2 234 ? 39.509  41.220  50.093  1.00 13.11 ? 234  TYR V CE2 1 
ATOM   5614 C CZ  . TYR D 2 234 ? 38.296  40.657  50.465  1.00 13.40 ? 234  TYR V CZ  1 
ATOM   5615 O OH  . TYR D 2 234 ? 38.123  39.310  50.290  1.00 13.45 ? 234  TYR V OH  1 
ATOM   5616 N N   . THR D 2 235 ? 41.703  43.722  52.723  1.00 10.44 ? 235  THR V N   1 
ATOM   5617 C CA  . THR D 2 235 ? 43.091  43.202  52.724  1.00 11.16 ? 235  THR V CA  1 
ATOM   5618 C C   . THR D 2 235 ? 43.271  41.708  52.996  1.00 11.20 ? 235  THR V C   1 
ATOM   5619 O O   . THR D 2 235 ? 42.672  41.130  53.914  1.00 10.96 ? 235  THR V O   1 
ATOM   5620 C CB  . THR D 2 235 ? 44.039  43.935  53.731  1.00 11.18 ? 235  THR V CB  1 
ATOM   5621 O OG1 . THR D 2 235 ? 43.925  43.324  55.025  1.00 11.93 ? 235  THR V OG1 1 
ATOM   5622 C CG2 . THR D 2 235 ? 43.761  45.436  53.814  1.00 11.44 ? 235  THR V CG2 1 
ATOM   5623 N N   . VAL D 2 236 ? 44.169  41.121  52.219  1.00 11.48 ? 236  VAL V N   1 
ATOM   5624 C CA  . VAL D 2 236 ? 44.433  39.711  52.283  1.00 12.27 ? 236  VAL V CA  1 
ATOM   5625 C C   . VAL D 2 236 ? 45.894  39.466  52.582  1.00 12.85 ? 236  VAL V C   1 
ATOM   5626 O O   . VAL D 2 236 ? 46.767  40.099  51.995  1.00 13.14 ? 236  VAL V O   1 
ATOM   5627 C CB  . VAL D 2 236 ? 44.064  39.023  50.966  1.00 12.30 ? 236  VAL V CB  1 
ATOM   5628 C CG1 . VAL D 2 236 ? 44.636  37.620  50.911  1.00 12.33 ? 236  VAL V CG1 1 
ATOM   5629 C CG2 . VAL D 2 236 ? 42.552  38.968  50.803  1.00 13.23 ? 236  VAL V CG2 1 
ATOM   5630 N N   . ARG D 2 237 ? 46.136  38.536  53.504  1.00 13.56 ? 237  ARG V N   1 
ATOM   5631 C CA  . ARG D 2 237 ? 47.460  38.082  53.862  1.00 14.25 ? 237  ARG V CA  1 
ATOM   5632 C C   . ARG D 2 237 ? 47.413  36.571  54.009  1.00 15.19 ? 237  ARG V C   1 
ATOM   5633 O O   . ARG D 2 237 ? 46.425  36.038  54.535  1.00 15.07 ? 237  ARG V O   1 
ATOM   5634 C CB  . ARG D 2 237 ? 47.869  38.735  55.162  1.00 14.38 ? 237  ARG V CB  1 
ATOM   5635 C CG  . ARG D 2 237 ? 46.680  39.144  56.034  1.00 14.53 ? 237  ARG V CG  1 
ATOM   5636 C CD  . ARG D 2 237 ? 47.107  39.858  57.304  1.00 13.83 ? 237  ARG V CD  1 
ATOM   5637 N NE  . ARG D 2 237 ? 47.711  41.163  57.040  1.00 13.73 ? 237  ARG V NE  1 
ATOM   5638 C CZ  . ARG D 2 237 ? 48.986  41.359  56.698  1.00 13.75 ? 237  ARG V CZ  1 
ATOM   5639 N NH1 . ARG D 2 237 ? 49.826  40.333  56.557  1.00 13.15 ? 237  ARG V NH1 1 
ATOM   5640 N NH2 . ARG D 2 237 ? 49.428  42.593  56.503  1.00 13.63 ? 237  ARG V NH2 1 
ATOM   5641 N N   . GLY D 2 238 ? 48.462  35.890  53.521  1.00 16.40 ? 238  GLY V N   1 
ATOM   5642 C CA  . GLY D 2 238 ? 48.561  34.408  53.520  1.00 18.11 ? 238  GLY V CA  1 
ATOM   5643 C C   . GLY D 2 238 ? 49.914  33.876  53.046  1.00 19.38 ? 238  GLY V C   1 
ATOM   5644 O O   . GLY D 2 238 ? 50.904  34.619  53.028  1.00 19.60 ? 238  GLY V O   1 
ATOM   5645 N N   . CYS D 2 239 ? 49.967  32.597  52.665  1.00 20.40 ? 239  CYS V N   1 
ATOM   5646 C CA  . CYS D 2 239 ? 51.222  31.949  52.203  1.00 21.62 ? 239  CYS V CA  1 
ATOM   5647 C C   . CYS D 2 239 ? 51.312  31.778  50.677  1.00 21.19 ? 239  CYS V C   1 
ATOM   5648 O O   . CYS D 2 239 ? 50.372  31.290  50.036  1.00 21.58 ? 239  CYS V O   1 
ATOM   5649 C CB  . CYS D 2 239 ? 51.363  30.560  52.828  1.00 22.18 ? 239  CYS V CB  1 
ATOM   5650 S SG  . CYS D 2 239 ? 51.263  30.467  54.625  1.00 26.73 ? 239  CYS V SG  1 
ATOM   5651 N N   . ALA D 2 240 ? 52.451  32.114  50.090  1.00 20.56 ? 240  ALA V N   1 
ATOM   5652 C CA  . ALA D 2 240 ? 52.511  32.118  48.640  1.00 20.21 ? 240  ALA V CA  1 
ATOM   5653 C C   . ALA D 2 240 ? 53.717  31.444  48.012  1.00 20.11 ? 240  ALA V C   1 
ATOM   5654 O O   . ALA D 2 240 ? 54.790  31.315  48.612  1.00 19.96 ? 240  ALA V O   1 
ATOM   5655 C CB  . ALA D 2 240 ? 52.385  33.537  48.111  1.00 20.34 ? 240  ALA V CB  1 
ATOM   5656 N N   . THR D 2 241 ? 53.503  31.028  46.770  1.00 19.82 ? 241  THR V N   1 
ATOM   5657 C CA  . THR D 2 241 ? 54.569  30.696  45.860  1.00 19.46 ? 241  THR V CA  1 
ATOM   5658 C C   . THR D 2 241 ? 55.093  32.028  45.385  1.00 19.63 ? 241  THR V C   1 
ATOM   5659 O O   . THR D 2 241 ? 54.355  33.016  45.349  1.00 19.40 ? 241  THR V O   1 
ATOM   5660 C CB  . THR D 2 241 ? 54.027  29.961  44.647  1.00 19.44 ? 241  THR V CB  1 
ATOM   5661 O OG1 . THR D 2 241 ? 52.742  29.416  44.966  1.00 19.00 ? 241  THR V OG1 1 
ATOM   5662 C CG2 . THR D 2 241 ? 54.983  28.854  44.202  1.00 18.84 ? 241  THR V CG2 1 
ATOM   5663 N N   . ALA D 2 242 ? 56.367  32.048  45.010  1.00 19.90 ? 242  ALA V N   1 
ATOM   5664 C CA  . ALA D 2 242 ? 57.047  33.281  44.639  1.00 19.95 ? 242  ALA V CA  1 
ATOM   5665 C C   . ALA D 2 242 ? 56.462  33.903  43.385  1.00 20.14 ? 242  ALA V C   1 
ATOM   5666 O O   . ALA D 2 242 ? 56.597  35.104  43.175  1.00 20.15 ? 242  ALA V O   1 
ATOM   5667 C CB  . ALA D 2 242 ? 58.520  33.029  44.463  1.00 19.78 ? 242  ALA V CB  1 
ATOM   5668 N N   . SER D 2 243 ? 55.812  33.085  42.563  1.00 20.58 ? 243  SER V N   1 
ATOM   5669 C CA  . SER D 2 243 ? 55.304  33.540  41.280  1.00 21.04 ? 243  SER V CA  1 
ATOM   5670 C C   . SER D 2 243 ? 53.808  33.685  41.340  1.00 21.51 ? 243  SER V C   1 
ATOM   5671 O O   . SER D 2 243 ? 53.177  33.988  40.342  1.00 21.21 ? 243  SER V O   1 
ATOM   5672 C CB  . SER D 2 243 ? 55.677  32.564  40.184  1.00 20.91 ? 243  SER V CB  1 
ATOM   5673 O OG  . SER D 2 243 ? 55.122  31.313  40.501  1.00 21.01 ? 243  SER V OG  1 
ATOM   5674 N N   . TRP D 2 244 ? 53.237  33.458  42.514  1.00 22.59 ? 244  TRP V N   1 
ATOM   5675 C CA  . TRP D 2 244 ? 51.867  33.887  42.756  1.00 23.65 ? 244  TRP V CA  1 
ATOM   5676 C C   . TRP D 2 244 ? 51.894  35.291  43.296  1.00 24.55 ? 244  TRP V C   1 
ATOM   5677 O O   . TRP D 2 244 ? 50.858  35.837  43.639  1.00 24.71 ? 244  TRP V O   1 
ATOM   5678 C CB  . TRP D 2 244 ? 51.142  32.974  43.737  1.00 23.58 ? 244  TRP V CB  1 
ATOM   5679 C CG  . TRP D 2 244 ? 49.646  32.969  43.539  1.00 23.44 ? 244  TRP V CG  1 
ATOM   5680 C CD1 . TRP D 2 244 ? 48.913  32.201  42.645  1.00 23.49 ? 244  TRP V CD1 1 
ATOM   5681 C CD2 . TRP D 2 244 ? 48.703  33.757  44.242  1.00 22.37 ? 244  TRP V CD2 1 
ATOM   5682 N NE1 . TRP D 2 244 ? 47.569  32.481  42.759  1.00 21.70 ? 244  TRP V NE1 1 
ATOM   5683 C CE2 . TRP D 2 244 ? 47.413  33.430  43.734  1.00 22.55 ? 244  TRP V CE2 1 
ATOM   5684 C CE3 . TRP D 2 244 ? 48.814  34.708  45.254  1.00 22.47 ? 244  TRP V CE3 1 
ATOM   5685 C CZ2 . TRP D 2 244 ? 46.254  34.019  44.215  1.00 23.80 ? 244  TRP V CZ2 1 
ATOM   5686 C CZ3 . TRP D 2 244 ? 47.662  35.305  45.731  1.00 24.35 ? 244  TRP V CZ3 1 
ATOM   5687 C CH2 . TRP D 2 244 ? 46.394  34.956  45.215  1.00 25.69 ? 244  TRP V CH2 1 
ATOM   5688 N N   . CYS D 2 245 ? 53.095  35.864  43.360  1.00 25.93 ? 245  CYS V N   1 
ATOM   5689 C CA  . CYS D 2 245 ? 53.311  37.234  43.828  1.00 27.48 ? 245  CYS V CA  1 
ATOM   5690 C C   . CYS D 2 245 ? 53.402  38.248  42.666  1.00 27.27 ? 245  CYS V C   1 
ATOM   5691 O O   . CYS D 2 245 ? 53.422  39.454  42.901  1.00 27.75 ? 245  CYS V O   1 
ATOM   5692 C CB  . CYS D 2 245 ? 54.568  37.325  44.731  1.00 28.19 ? 245  CYS V CB  1 
ATOM   5693 S SG  . CYS D 2 245 ? 54.570  36.427  46.403  1.00 33.19 ? 245  CYS V SG  1 
ATOM   5694 N N   . GLN D 2 246 ? 53.465  37.781  41.417  1.00 27.18 ? 246  GLN V N   1 
ATOM   5695 C CA  . GLN D 2 246 ? 53.442  38.714  40.268  1.00 26.87 ? 246  GLN V CA  1 
ATOM   5696 C C   . GLN D 2 246 ? 52.579  38.349  39.060  1.00 26.79 ? 246  GLN V C   1 
ATOM   5697 O O   . GLN D 2 246 ? 52.200  37.197  38.866  1.00 26.76 ? 246  GLN V O   1 
ATOM   5698 C CB  . GLN D 2 246 ? 54.838  39.110  39.809  1.00 26.67 ? 246  GLN V CB  1 
ATOM   5699 C CG  . GLN D 2 246 ? 55.923  38.234  40.284  1.00 26.17 ? 246  GLN V CG  1 
ATOM   5700 C CD  . GLN D 2 246 ? 56.933  39.040  41.037  1.00 26.52 ? 246  GLN V CD  1 
ATOM   5701 O OE1 . GLN D 2 246 ? 58.132  38.854  40.869  1.00 27.80 ? 246  GLN V OE1 1 
ATOM   5702 N NE2 . GLN D 2 246 ? 56.456  39.969  41.863  1.00 25.87 ? 246  GLN V NE2 1 
ATOM   5703 N N   . GLY D 2 247 ? 52.294  39.354  38.238  1.00 26.50 ? 247  GLY V N   1 
ATOM   5704 C CA  . GLY D 2 247 ? 51.267  39.231  37.231  1.00 26.37 ? 247  GLY V CA  1 
ATOM   5705 C C   . GLY D 2 247 ? 49.943  39.362  37.947  1.00 26.44 ? 247  GLY V C   1 
ATOM   5706 O O   . GLY D 2 247 ? 49.894  39.838  39.084  1.00 26.53 ? 247  GLY V O   1 
ATOM   5707 N N   . SER D 2 248 ? 48.875  38.913  37.293  1.00 26.49 ? 248  SER V N   1 
ATOM   5708 C CA  . SER D 2 248 ? 47.511  39.088  37.792  1.00 26.59 ? 248  SER V CA  1 
ATOM   5709 C C   . SER D 2 248 ? 47.236  38.354  39.109  1.00 26.44 ? 248  SER V C   1 
ATOM   5710 O O   . SER D 2 248 ? 47.038  38.986  40.140  1.00 26.76 ? 248  SER V O   1 
ATOM   5711 C CB  . SER D 2 248 ? 46.507  38.665  36.719  1.00 26.83 ? 248  SER V CB  1 
ATOM   5712 O OG  . SER D 2 248 ? 45.189  39.013  37.099  1.00 27.73 ? 248  SER V OG  1 
ATOM   5713 N N   . HIS D 2 249 ? 47.240  37.025  39.059  1.00 26.17 ? 249  HIS V N   1 
ATOM   5714 C CA  . HIS D 2 249 ? 46.915  36.156  40.194  1.00 25.82 ? 249  HIS V CA  1 
ATOM   5715 C C   . HIS D 2 249 ? 46.166  36.802  41.342  1.00 26.11 ? 249  HIS V C   1 
ATOM   5716 O O   . HIS D 2 249 ? 44.934  36.820  41.402  1.00 25.87 ? 249  HIS V O   1 
ATOM   5717 C CB  . HIS D 2 249 ? 48.185  35.539  40.750  1.00 25.49 ? 249  HIS V CB  1 
ATOM   5718 C CG  . HIS D 2 249 ? 48.754  34.471  39.886  1.00 24.46 ? 249  HIS V CG  1 
ATOM   5719 N ND1 . HIS D 2 249 ? 50.000  34.567  39.312  1.00 24.26 ? 249  HIS V ND1 1 
ATOM   5720 C CD2 . HIS D 2 249 ? 48.245  33.284  39.489  1.00 23.63 ? 249  HIS V CD2 1 
ATOM   5721 C CE1 . HIS D 2 249 ? 50.241  33.480  38.601  1.00 23.56 ? 249  HIS V CE1 1 
ATOM   5722 N NE2 . HIS D 2 249 ? 49.190  32.687  38.690  1.00 23.61 ? 249  HIS V NE2 1 
ATOM   5723 N N   . VAL D 2 250 ? 46.942  37.330  42.269  1.00 26.63 ? 250  VAL V N   1 
ATOM   5724 C CA  . VAL D 2 250 ? 46.383  37.875  43.475  1.00 27.25 ? 250  VAL V CA  1 
ATOM   5725 C C   . VAL D 2 250 ? 45.270  38.851  43.133  1.00 27.67 ? 250  VAL V C   1 
ATOM   5726 O O   . VAL D 2 250 ? 44.184  38.752  43.689  1.00 27.93 ? 250  VAL V O   1 
ATOM   5727 C CB  . VAL D 2 250 ? 47.481  38.473  44.383  1.00 27.14 ? 250  VAL V CB  1 
ATOM   5728 C CG1 . VAL D 2 250 ? 48.608  39.071  43.539  1.00 27.37 ? 250  VAL V CG1 1 
ATOM   5729 C CG2 . VAL D 2 250 ? 46.887  39.456  45.384  1.00 27.13 ? 250  VAL V CG2 1 
ATOM   5730 N N   . ALA D 2 251 ? 45.531  39.752  42.184  1.00 28.18 ? 251  ALA V N   1 
ATOM   5731 C CA  . ALA D 2 251 ? 44.563  40.774  41.780  1.00 28.51 ? 251  ALA V CA  1 
ATOM   5732 C C   . ALA D 2 251 ? 43.160  40.195  41.700  1.00 28.96 ? 251  ALA V C   1 
ATOM   5733 O O   . ALA D 2 251 ? 42.297  40.518  42.511  1.00 28.98 ? 251  ALA V O   1 
ATOM   5734 C CB  . ALA D 2 251 ? 44.963  41.394  40.461  1.00 28.37 ? 251  ALA V CB  1 
ATOM   5735 N N   . ASP D 2 252 ? 42.949  39.304  40.746  1.00 29.57 ? 252  ASP V N   1 
ATOM   5736 C CA  . ASP D 2 252 ? 41.664  38.664  40.582  1.00 30.46 ? 252  ASP V CA  1 
ATOM   5737 C C   . ASP D 2 252 ? 41.516  37.521  41.584  1.00 31.51 ? 252  ASP V C   1 
ATOM   5738 O O   . ASP D 2 252 ? 41.054  36.423  41.233  1.00 31.76 ? 252  ASP V O   1 
ATOM   5739 C CB  . ASP D 2 252 ? 41.579  38.121  39.182  1.00 30.33 ? 252  ASP V CB  1 
ATOM   5740 C CG  . ASP D 2 252 ? 42.816  37.377  38.808  1.00 29.95 ? 252  ASP V CG  1 
ATOM   5741 O OD1 . ASP D 2 252 ? 42.697  36.178  38.493  1.00 30.33 ? 252  ASP V OD1 1 
ATOM   5742 O OD2 . ASP D 2 252 ? 43.909  37.982  38.886  1.00 28.97 ? 252  ASP V OD2 1 
ATOM   5743 N N   . SER D 2 253 ? 41.929  37.784  42.822  1.00 32.35 ? 253  SER V N   1 
ATOM   5744 C CA  . SER D 2 253 ? 41.639  36.920  43.944  1.00 33.15 ? 253  SER V CA  1 
ATOM   5745 C C   . SER D 2 253 ? 40.231  37.248  44.462  1.00 33.65 ? 253  SER V C   1 
ATOM   5746 O O   . SER D 2 253 ? 39.578  36.390  45.051  1.00 34.02 ? 253  SER V O   1 
ATOM   5747 C CB  . SER D 2 253 ? 42.681  37.151  45.033  1.00 33.36 ? 253  SER V CB  1 
ATOM   5748 O OG  . SER D 2 253 ? 42.831  36.045  45.901  1.00 34.34 ? 253  SER V OG  1 
ATOM   5749 N N   . PHE D 2 254 ? 39.761  38.474  44.216  1.00 34.09 ? 254  PHE V N   1 
ATOM   5750 C CA  . PHE D 2 254 ? 38.442  38.949  44.670  1.00 34.76 ? 254  PHE V CA  1 
ATOM   5751 C C   . PHE D 2 254 ? 37.784  39.830  43.595  1.00 35.57 ? 254  PHE V C   1 
ATOM   5752 O O   . PHE D 2 254 ? 38.245  39.822  42.448  1.00 35.67 ? 254  PHE V O   1 
ATOM   5753 C CB  . PHE D 2 254 ? 38.628  39.731  45.953  1.00 34.66 ? 254  PHE V CB  1 
ATOM   5754 C CG  . PHE D 2 254 ? 40.049  40.144  46.201  1.00 35.06 ? 254  PHE V CG  1 
ATOM   5755 C CD1 . PHE D 2 254 ? 40.786  40.787  45.222  1.00 34.52 ? 254  PHE V CD1 1 
ATOM   5756 C CD2 . PHE D 2 254 ? 40.662  39.874  47.423  1.00 36.35 ? 254  PHE V CD2 1 
ATOM   5757 C CE1 . PHE D 2 254 ? 42.113  41.156  45.459  1.00 35.13 ? 254  PHE V CE1 1 
ATOM   5758 C CE2 . PHE D 2 254 ? 41.995  40.252  47.670  1.00 36.12 ? 254  PHE V CE2 1 
ATOM   5759 C CZ  . PHE D 2 254 ? 42.717  40.892  46.686  1.00 35.13 ? 254  PHE V CZ  1 
ATOM   5760 N N   . PRO D 2 255 ? 36.684  40.564  43.935  1.00 36.35 ? 255  PRO V N   1 
ATOM   5761 C CA  . PRO D 2 255 ? 36.076  41.652  43.073  1.00 36.68 ? 255  PRO V CA  1 
ATOM   5762 C C   . PRO D 2 255 ? 37.002  42.818  42.620  1.00 36.98 ? 255  PRO V C   1 
ATOM   5763 O O   . PRO D 2 255 ? 38.026  43.076  43.257  1.00 36.93 ? 255  PRO V O   1 
ATOM   5764 C CB  . PRO D 2 255 ? 34.927  42.188  43.935  1.00 36.39 ? 255  PRO V CB  1 
ATOM   5765 C CG  . PRO D 2 255 ? 34.506  41.012  44.746  1.00 36.56 ? 255  PRO V CG  1 
ATOM   5766 C CD  . PRO D 2 255 ? 35.732  40.116  44.974  1.00 36.26 ? 255  PRO V CD  1 
ATOM   5767 N N   . THR D 2 256 ? 36.616  43.517  41.546  1.00 37.39 ? 256  THR V N   1 
ATOM   5768 C CA  . THR D 2 256 ? 37.514  44.446  40.804  1.00 38.03 ? 256  THR V CA  1 
ATOM   5769 C C   . THR D 2 256 ? 38.125  45.616  41.610  1.00 38.84 ? 256  THR V C   1 
ATOM   5770 O O   . THR D 2 256 ? 37.472  46.151  42.509  1.00 38.84 ? 256  THR V O   1 
ATOM   5771 C CB  . THR D 2 256 ? 36.858  44.969  39.468  1.00 37.88 ? 256  THR V CB  1 
ATOM   5772 O OG1 . THR D 2 256 ? 37.620  46.065  38.936  1.00 36.88 ? 256  THR V OG1 1 
ATOM   5773 C CG2 . THR D 2 256 ? 35.396  45.400  39.679  1.00 37.41 ? 256  THR V CG2 1 
ATOM   5774 N N   . HIS D 2 257 ? 39.363  46.010  41.268  1.00 39.70 ? 257  HIS V N   1 
ATOM   5775 C CA  . HIS D 2 257 ? 40.123  47.032  42.026  1.00 40.48 ? 257  HIS V CA  1 
ATOM   5776 C C   . HIS D 2 257 ? 41.151  47.883  41.276  1.00 41.08 ? 257  HIS V C   1 
ATOM   5777 O O   . HIS D 2 257 ? 41.531  47.557  40.154  1.00 41.17 ? 257  HIS V O   1 
ATOM   5778 C CB  . HIS D 2 257 ? 40.797  46.396  43.221  1.00 40.33 ? 257  HIS V CB  1 
ATOM   5779 C CG  . HIS D 2 257 ? 39.867  46.181  44.363  1.00 41.23 ? 257  HIS V CG  1 
ATOM   5780 N ND1 . HIS D 2 257 ? 39.535  47.186  45.246  1.00 42.53 ? 257  HIS V ND1 1 
ATOM   5781 C CD2 . HIS D 2 257 ? 39.167  45.089  44.747  1.00 41.80 ? 257  HIS V CD2 1 
ATOM   5782 C CE1 . HIS D 2 257 ? 38.683  46.714  46.140  1.00 43.04 ? 257  HIS V CE1 1 
ATOM   5783 N NE2 . HIS D 2 257 ? 38.440  45.445  45.856  1.00 42.77 ? 257  HIS V NE2 1 
ATOM   5784 N N   . LEU D 2 258 ? 41.598  48.970  41.929  1.00 41.92 ? 258  LEU V N   1 
ATOM   5785 C CA  . LEU D 2 258 ? 42.469  49.997  41.303  1.00 42.33 ? 258  LEU V CA  1 
ATOM   5786 C C   . LEU D 2 258 ? 43.934  49.893  41.744  1.00 42.49 ? 258  LEU V C   1 
ATOM   5787 O O   . LEU D 2 258 ? 44.248  50.077  42.918  1.00 42.09 ? 258  LEU V O   1 
ATOM   5788 C CB  . LEU D 2 258 ? 41.912  51.435  41.480  1.00 42.16 ? 258  LEU V CB  1 
ATOM   5789 C CG  . LEU D 2 258 ? 40.572  51.779  40.792  1.00 41.88 ? 258  LEU V CG  1 
ATOM   5790 C CD1 . LEU D 2 258 ? 40.040  53.171  41.147  1.00 41.18 ? 258  LEU V CD1 1 
ATOM   5791 C CD2 . LEU D 2 258 ? 40.671  51.593  39.272  1.00 42.19 ? 258  LEU V CD2 1 
ATOM   5792 N N   . ASN D 2 259 ? 44.801  49.649  40.753  1.00 42.99 ? 259  ASN V N   1 
ATOM   5793 C CA  . ASN D 2 259 ? 46.205  49.242  40.920  1.00 43.60 ? 259  ASN V CA  1 
ATOM   5794 C C   . ASN D 2 259 ? 46.637  48.951  42.365  1.00 42.28 ? 259  ASN V C   1 
ATOM   5795 O O   . ASN D 2 259 ? 47.711  49.363  42.820  1.00 42.14 ? 259  ASN V O   1 
ATOM   5796 C CB  . ASN D 2 259 ? 47.178  50.157  40.129  1.00 44.82 ? 259  ASN V CB  1 
ATOM   5797 C CG  . ASN D 2 259 ? 47.256  51.591  40.670  1.00 50.14 ? 259  ASN V CG  1 
ATOM   5798 O OD1 . ASN D 2 259 ? 46.642  51.932  41.690  1.00 51.09 ? 259  ASN V OD1 1 
ATOM   5799 N ND2 . ASN D 2 259 ? 48.035  52.438  39.966  1.00 58.92 ? 259  ASN V ND2 1 
ATOM   5800 N N   . VAL D 2 260 ? 45.765  48.217  43.060  1.00 40.84 ? 260  VAL V N   1 
ATOM   5801 C CA  . VAL D 2 260 ? 45.964  47.808  44.447  1.00 39.32 ? 260  VAL V CA  1 
ATOM   5802 C C   . VAL D 2 260 ? 47.023  46.713  44.497  1.00 38.37 ? 260  VAL V C   1 
ATOM   5803 O O   . VAL D 2 260 ? 47.135  45.902  43.581  1.00 38.20 ? 260  VAL V O   1 
ATOM   5804 C CB  . VAL D 2 260 ? 44.647  47.346  45.108  1.00 39.36 ? 260  VAL V CB  1 
ATOM   5805 C CG1 . VAL D 2 260 ? 43.532  48.400  44.919  1.00 38.76 ? 260  VAL V CG1 1 
ATOM   5806 C CG2 . VAL D 2 260 ? 44.225  45.965  44.592  1.00 39.13 ? 260  VAL V CG2 1 
ATOM   5807 N N   . SER D 2 261 ? 47.800  46.689  45.567  1.00 37.09 ? 261  SER V N   1 
ATOM   5808 C CA  . SER D 2 261 ? 49.104  46.082  45.469  1.00 36.11 ? 261  SER V CA  1 
ATOM   5809 C C   . SER D 2 261 ? 49.359  44.992  46.455  1.00 35.33 ? 261  SER V C   1 
ATOM   5810 O O   . SER D 2 261 ? 48.595  44.771  47.384  1.00 35.19 ? 261  SER V O   1 
ATOM   5811 C CB  . SER D 2 261 ? 50.179  47.139  45.629  1.00 36.39 ? 261  SER V CB  1 
ATOM   5812 O OG  . SER D 2 261 ? 50.166  47.629  46.954  1.00 37.23 ? 261  SER V OG  1 
ATOM   5813 N N   . VAL D 2 262 ? 50.494  44.351  46.242  1.00 34.57 ? 262  VAL V N   1 
ATOM   5814 C CA  . VAL D 2 262 ? 50.835  43.111  46.868  1.00 33.92 ? 262  VAL V CA  1 
ATOM   5815 C C   . VAL D 2 262 ? 52.247  43.217  47.372  1.00 34.07 ? 262  VAL V C   1 
ATOM   5816 O O   . VAL D 2 262 ? 53.149  43.588  46.626  1.00 34.11 ? 262  VAL V O   1 
ATOM   5817 C CB  . VAL D 2 262 ? 50.746  41.955  45.843  1.00 33.77 ? 262  VAL V CB  1 
ATOM   5818 C CG1 . VAL D 2 262 ? 49.323  41.736  45.447  1.00 33.26 ? 262  VAL V CG1 1 
ATOM   5819 C CG2 . VAL D 2 262 ? 51.583  42.235  44.590  1.00 32.97 ? 262  VAL V CG2 1 
ATOM   5820 N N   . SER D 2 263 ? 52.448  42.900  48.640  1.00 34.37 ? 263  SER V N   1 
ATOM   5821 C CA  . SER D 2 263 ? 53.808  42.834  49.172  1.00 34.79 ? 263  SER V CA  1 
ATOM   5822 C C   . SER D 2 263 ? 54.232  41.385  49.464  1.00 34.92 ? 263  SER V C   1 
ATOM   5823 O O   . SER D 2 263 ? 53.566  40.672  50.215  1.00 34.90 ? 263  SER V O   1 
ATOM   5824 C CB  . SER D 2 263 ? 53.971  43.734  50.398  1.00 34.78 ? 263  SER V CB  1 
ATOM   5825 O OG  . SER D 2 263 ? 55.341  43.992  50.645  1.00 34.69 ? 263  SER V OG  1 
ATOM   5826 N N   . CYS D 2 264 ? 55.337  40.969  48.845  1.00 35.08 ? 264  CYS V N   1 
ATOM   5827 C CA  . CYS D 2 264 ? 55.847  39.603  48.927  1.00 35.21 ? 264  CYS V CA  1 
ATOM   5828 C C   . CYS D 2 264 ? 57.243  39.637  49.507  1.00 35.33 ? 264  CYS V C   1 
ATOM   5829 O O   . CYS D 2 264 ? 58.177  40.157  48.888  1.00 35.48 ? 264  CYS V O   1 
ATOM   5830 C CB  . CYS D 2 264 ? 55.899  38.976  47.529  1.00 35.34 ? 264  CYS V CB  1 
ATOM   5831 S SG  . CYS D 2 264 ? 56.229  37.161  47.422  1.00 36.02 ? 264  CYS V SG  1 
ATOM   5832 N N   . CYS D 2 265 ? 57.380  39.086  50.703  1.00 35.42 ? 265  CYS V N   1 
ATOM   5833 C CA  . CYS D 2 265 ? 58.662  39.006  51.364  1.00 35.62 ? 265  CYS V CA  1 
ATOM   5834 C C   . CYS D 2 265 ? 59.204  37.596  51.189  1.00 35.55 ? 265  CYS V C   1 
ATOM   5835 O O   . CYS D 2 265 ? 58.530  36.720  50.628  1.00 36.01 ? 265  CYS V O   1 
ATOM   5836 C CB  . CYS D 2 265 ? 58.470  39.250  52.854  1.00 35.60 ? 265  CYS V CB  1 
ATOM   5837 S SG  . CYS D 2 265 ? 58.094  37.705  53.755  1.00 37.11 ? 265  CYS V SG  1 
ATOM   5838 N N   . HIS D 2 266 ? 60.420  37.377  51.674  1.00 35.24 ? 266  HIS V N   1 
ATOM   5839 C CA  . HIS D 2 266 ? 60.794  36.050  52.141  1.00 34.93 ? 266  HIS V CA  1 
ATOM   5840 C C   . HIS D 2 266 ? 61.342  36.186  53.563  1.00 34.65 ? 266  HIS V C   1 
ATOM   5841 O O   . HIS D 2 266 ? 62.101  37.116  53.860  1.00 34.75 ? 266  HIS V O   1 
ATOM   5842 C CB  . HIS D 2 266 ? 61.771  35.344  51.195  1.00 35.01 ? 266  HIS V CB  1 
ATOM   5843 C CG  . HIS D 2 266 ? 61.972  33.893  51.517  1.00 34.53 ? 266  HIS V CG  1 
ATOM   5844 N ND1 . HIS D 2 266 ? 63.170  33.241  51.306  1.00 34.15 ? 266  HIS V ND1 1 
ATOM   5845 C CD2 . HIS D 2 266 ? 61.135  32.977  52.058  1.00 33.62 ? 266  HIS V CD2 1 
ATOM   5846 C CE1 . HIS D 2 266 ? 63.055  31.982  51.689  1.00 34.06 ? 266  HIS V CE1 1 
ATOM   5847 N NE2 . HIS D 2 266 ? 61.831  31.797  52.151  1.00 34.07 ? 266  HIS V NE2 1 
ATOM   5848 N N   . GLY D 2 267 ? 60.927  35.276  54.440  1.00 34.03 ? 267  GLY V N   1 
ATOM   5849 C CA  . GLY D 2 267 ? 61.282  35.349  55.850  1.00 33.00 ? 267  GLY V CA  1 
ATOM   5850 C C   . GLY D 2 267 ? 60.046  35.079  56.668  1.00 32.34 ? 267  GLY V C   1 
ATOM   5851 O O   . GLY D 2 267 ? 59.075  35.834  56.605  1.00 32.17 ? 267  GLY V O   1 
ATOM   5852 N N   . SER D 2 268 ? 60.090  33.989  57.424  1.00 31.61 ? 268  SER V N   1 
ATOM   5853 C CA  . SER D 2 268 ? 58.946  33.514  58.189  1.00 31.06 ? 268  SER V CA  1 
ATOM   5854 C C   . SER D 2 268 ? 58.356  34.550  59.139  1.00 30.80 ? 268  SER V C   1 
ATOM   5855 O O   . SER D 2 268 ? 59.076  35.226  59.854  1.00 31.12 ? 268  SER V O   1 
ATOM   5856 C CB  . SER D 2 268 ? 59.344  32.272  58.974  1.00 30.99 ? 268  SER V CB  1 
ATOM   5857 O OG  . SER D 2 268 ? 58.201  31.674  59.547  1.00 30.82 ? 268  SER V OG  1 
ATOM   5858 N N   . GLY D 2 269 ? 57.039  34.669  59.144  1.00 30.60 ? 269  GLY V N   1 
ATOM   5859 C CA  . GLY D 2 269 ? 56.356  35.586  60.041  1.00 30.79 ? 269  GLY V CA  1 
ATOM   5860 C C   . GLY D 2 269 ? 56.488  37.024  59.600  1.00 31.26 ? 269  GLY V C   1 
ATOM   5861 O O   . GLY D 2 269 ? 55.898  37.917  60.203  1.00 31.28 ? 269  GLY V O   1 
ATOM   5862 N N   . CYS D 2 270 ? 57.254  37.244  58.533  1.00 31.77 ? 270  CYS V N   1 
ATOM   5863 C CA  . CYS D 2 270 ? 57.610  38.587  58.060  1.00 32.41 ? 270  CYS V CA  1 
ATOM   5864 C C   . CYS D 2 270 ? 56.410  39.518  57.931  1.00 31.94 ? 270  CYS V C   1 
ATOM   5865 O O   . CYS D 2 270 ? 56.480  40.670  58.332  1.00 32.10 ? 270  CYS V O   1 
ATOM   5866 C CB  . CYS D 2 270 ? 58.288  38.501  56.697  1.00 32.72 ? 270  CYS V CB  1 
ATOM   5867 S SG  . CYS D 2 270 ? 57.051  38.318  55.380  1.00 35.99 ? 270  CYS V SG  1 
ATOM   5868 N N   . ASN D 2 271 ? 55.319  39.014  57.360  1.00 31.65 ? 271  ASN V N   1 
ATOM   5869 C CA  . ASN D 2 271 ? 54.162  39.837  57.025  1.00 31.51 ? 271  ASN V CA  1 
ATOM   5870 C C   . ASN D 2 271 ? 53.303  40.179  58.240  1.00 31.74 ? 271  ASN V C   1 
ATOM   5871 O O   . ASN D 2 271 ? 52.072  40.146  58.190  1.00 31.97 ? 271  ASN V O   1 
ATOM   5872 C CB  . ASN D 2 271 ? 53.332  39.199  55.897  1.00 31.32 ? 271  ASN V CB  1 
ATOM   5873 C CG  . ASN D 2 271 ? 52.797  37.826  56.252  1.00 30.32 ? 271  ASN V CG  1 
ATOM   5874 O OD1 . ASN D 2 271 ? 52.792  37.417  57.405  1.00 30.11 ? 271  ASN V OD1 1 
ATOM   5875 N ND2 . ASN D 2 271 ? 52.340  37.110  55.251  1.00 29.54 ? 271  ASN V ND2 1 
ATOM   5876 N N   . SER D 2 272 ? 53.978  40.505  59.334  1.00 31.76 ? 272  SER V N   1 
ATOM   5877 C CA  . SER D 2 272 ? 53.333  41.015  60.528  1.00 31.61 ? 272  SER V CA  1 
ATOM   5878 C C   . SER D 2 272 ? 52.672  42.352  60.202  1.00 31.58 ? 272  SER V C   1 
ATOM   5879 O O   . SER D 2 272 ? 53.263  43.196  59.524  1.00 31.33 ? 272  SER V O   1 
ATOM   5880 C CB  . SER D 2 272 ? 54.359  41.192  61.654  1.00 31.66 ? 272  SER V CB  1 
ATOM   5881 O OG  . SER D 2 272 ? 55.456  40.296  61.515  1.00 31.34 ? 272  SER V OG  1 
ATOM   5882 N N   . PRO D 2 273 ? 51.430  42.531  60.657  1.00 31.73 ? 273  PRO V N   1 
ATOM   5883 C CA  . PRO D 2 273 ? 50.724  43.802  60.565  1.00 32.37 ? 273  PRO V CA  1 
ATOM   5884 C C   . PRO D 2 273 ? 51.358  44.928  61.420  1.00 33.27 ? 273  PRO V C   1 
ATOM   5885 O O   . PRO D 2 273 ? 51.280  46.111  61.038  1.00 33.18 ? 273  PRO V O   1 
ATOM   5886 C CB  . PRO D 2 273 ? 49.320  43.446  61.058  1.00 32.16 ? 273  PRO V CB  1 
ATOM   5887 C CG  . PRO D 2 273 ? 49.199  41.993  60.834  1.00 31.53 ? 273  PRO V CG  1 
ATOM   5888 C CD  . PRO D 2 273 ? 50.544  41.447  61.105  1.00 31.57 ? 273  PRO V CD  1 
ATOM   5889 N N   . THR D 2 274 ? 51.957  44.551  62.562  1.00 34.27 ? 274  THR V N   1 
ATOM   5890 C CA  . THR D 2 274 ? 52.883  45.400  63.371  1.00 35.30 ? 274  THR V CA  1 
ATOM   5891 C C   . THR D 2 274 ? 52.419  46.786  63.873  1.00 35.35 ? 274  THR V C   1 
ATOM   5892 O O   . THR D 2 274 ? 52.040  47.696  63.115  1.00 35.50 ? 274  THR V O   1 
ATOM   5893 C CB  . THR D 2 274 ? 54.287  45.556  62.694  1.00 35.61 ? 274  THR V CB  1 
ATOM   5894 O OG1 . THR D 2 274 ? 54.156  45.527  61.261  1.00 37.09 ? 274  THR V OG1 1 
ATOM   5895 C CG2 . THR D 2 274 ? 55.199  44.438  63.117  1.00 35.80 ? 274  THR V CG2 1 
HETATM 5896 C C1  . NAG E 3 .   ? 11.180  7.427   4.776   1.00 60.14 ? 1052 NAG U C1  1 
HETATM 5897 C C2  . NAG E 3 .   ? 10.890  7.404   3.251   1.00 65.66 ? 1052 NAG U C2  1 
HETATM 5898 C C3  . NAG E 3 .   ? 9.591   8.121   2.873   1.00 66.05 ? 1052 NAG U C3  1 
HETATM 5899 C C4  . NAG E 3 .   ? 8.452   7.756   3.806   1.00 67.79 ? 1052 NAG U C4  1 
HETATM 5900 C C5  . NAG E 3 .   ? 8.976   8.278   5.147   1.00 66.59 ? 1052 NAG U C5  1 
HETATM 5901 C C6  . NAG E 3 .   ? 7.974   8.481   6.281   1.00 66.86 ? 1052 NAG U C6  1 
HETATM 5902 C C7  . NAG E 3 .   ? 12.247  7.757   1.200   1.00 66.99 ? 1052 NAG U C7  1 
HETATM 5903 C C8  . NAG E 3 .   ? 13.405  8.509   0.603   1.00 65.90 ? 1052 NAG U C8  1 
HETATM 5904 N N2  . NAG E 3 .   ? 11.970  8.020   2.481   1.00 66.89 ? 1052 NAG U N2  1 
HETATM 5905 O O3  . NAG E 3 .   ? 9.284   7.817   1.543   1.00 66.48 ? 1052 NAG U O3  1 
HETATM 5906 O O4  . NAG E 3 .   ? 7.309   8.421   3.321   1.00 72.52 ? 1052 NAG U O4  1 
HETATM 5907 O O5  . NAG E 3 .   ? 9.984   7.363   5.545   1.00 63.93 ? 1052 NAG U O5  1 
HETATM 5908 O O6  . NAG E 3 .   ? 8.134   7.441   7.224   1.00 67.00 ? 1052 NAG U O6  1 
HETATM 5909 O O7  . NAG E 3 .   ? 11.601  6.953   0.525   1.00 67.64 ? 1052 NAG U O7  1 
HETATM 5910 C C1  . NAG F 3 .   ? 6.852   9.877   3.749   1.00 78.23 ? 1053 NAG U C1  1 
HETATM 5911 C C2  . NAG F 3 .   ? 6.561   9.817   2.218   1.00 80.87 ? 1053 NAG U C2  1 
HETATM 5912 C C3  . NAG F 3 .   ? 5.128   10.375  1.984   1.00 81.45 ? 1053 NAG U C3  1 
HETATM 5913 C C4  . NAG F 3 .   ? 4.062   9.775   2.917   1.00 81.24 ? 1053 NAG U C4  1 
HETATM 5914 C C5  . NAG F 3 .   ? 4.555   9.698   4.374   1.00 81.50 ? 1053 NAG U C5  1 
HETATM 5915 C C6  . NAG F 3 .   ? 3.572   8.921   5.253   1.00 80.74 ? 1053 NAG U C6  1 
HETATM 5916 C C7  . NAG F 3 .   ? 8.175   10.104  0.263   1.00 82.86 ? 1053 NAG U C7  1 
HETATM 5917 C C8  . NAG F 3 .   ? 9.149   11.060  -0.374  1.00 82.01 ? 1053 NAG U C8  1 
HETATM 5918 N N2  . NAG F 3 .   ? 7.553   10.535  1.389   1.00 82.63 ? 1053 NAG U N2  1 
HETATM 5919 O O3  . NAG F 3 .   ? 4.681   10.220  0.649   1.00 81.98 ? 1053 NAG U O3  1 
HETATM 5920 O O4  . NAG F 3 .   ? 2.881   10.548  2.843   1.00 80.59 ? 1053 NAG U O4  1 
HETATM 5921 O O5  . NAG F 3 .   ? 5.868   9.130   4.459   1.00 80.60 ? 1053 NAG U O5  1 
HETATM 5922 O O6  . NAG F 3 .   ? 3.853   9.213   6.601   1.00 79.85 ? 1053 NAG U O6  1 
HETATM 5923 O O7  . NAG F 3 .   ? 8.008   8.993   -0.255  1.00 83.20 ? 1053 NAG U O7  1 
HETATM 5924 C C1  . NAG G 3 .   ? 48.313  -3.783  12.353  1.00 70.47 ? 1160 NAG U C1  1 
HETATM 5925 C C2  . NAG G 3 .   ? 48.774  -5.254  12.510  1.00 76.53 ? 1160 NAG U C2  1 
HETATM 5926 C C3  . NAG G 3 .   ? 48.557  -5.780  13.943  1.00 77.23 ? 1160 NAG U C3  1 
HETATM 5927 C C4  . NAG G 3 .   ? 49.352  -4.860  14.877  1.00 77.60 ? 1160 NAG U C4  1 
HETATM 5928 C C5  . NAG G 3 .   ? 48.728  -3.453  14.801  1.00 77.07 ? 1160 NAG U C5  1 
HETATM 5929 C C6  . NAG G 3 .   ? 49.489  -2.469  15.698  1.00 77.73 ? 1160 NAG U C6  1 
HETATM 5930 C C7  . NAG G 3 .   ? 48.675  -6.361  10.319  1.00 79.76 ? 1160 NAG U C7  1 
HETATM 5931 C C8  . NAG G 3 .   ? 47.895  -7.290  9.415   1.00 79.52 ? 1160 NAG U C8  1 
HETATM 5932 N N2  . NAG G 3 .   ? 48.141  -6.125  11.523  1.00 77.91 ? 1160 NAG U N2  1 
HETATM 5933 O O3  . NAG G 3 .   ? 48.902  -7.155  14.080  1.00 77.22 ? 1160 NAG U O3  1 
HETATM 5934 O O4  . NAG G 3 .   ? 49.383  -5.346  16.206  1.00 78.23 ? 1160 NAG U O4  1 
HETATM 5935 O O5  . NAG G 3 .   ? 48.684  -2.935  13.457  1.00 74.74 ? 1160 NAG U O5  1 
HETATM 5936 O O6  . NAG G 3 .   ? 48.601  -1.953  16.667  1.00 78.39 ? 1160 NAG U O6  1 
HETATM 5937 O O7  . NAG G 3 .   ? 49.747  -5.853  9.952   1.00 80.71 ? 1160 NAG U O7  1 
HETATM 5938 C C1  . NAG H 3 .   ? 13.856  -10.006 -5.921  1.00 61.00 ? 1170 NAG U C1  1 
HETATM 5939 C C2  . NAG H 3 .   ? 13.807  -10.590 -7.344  1.00 66.11 ? 1170 NAG U C2  1 
HETATM 5940 C C3  . NAG H 3 .   ? 12.371  -10.683 -7.938  1.00 66.87 ? 1170 NAG U C3  1 
HETATM 5941 C C4  . NAG H 3 .   ? 11.275  -11.042 -6.920  1.00 67.60 ? 1170 NAG U C4  1 
HETATM 5942 C C5  . NAG H 3 .   ? 11.543  -10.420 -5.543  1.00 67.26 ? 1170 NAG U C5  1 
HETATM 5943 C C6  . NAG H 3 .   ? 10.664  -11.074 -4.485  1.00 69.13 ? 1170 NAG U C6  1 
HETATM 5944 C C7  . NAG H 3 .   ? 16.038  -9.844  -8.193  1.00 67.45 ? 1170 NAG U C7  1 
HETATM 5945 C C8  . NAG H 3 .   ? 16.762  -9.093  -9.279  1.00 67.23 ? 1170 NAG U C8  1 
HETATM 5946 N N2  . NAG H 3 .   ? 14.698  -9.894  -8.276  1.00 67.06 ? 1170 NAG U N2  1 
HETATM 5947 O O3  . NAG H 3 .   ? 12.307  -11.652 -8.971  1.00 66.25 ? 1170 NAG U O3  1 
HETATM 5948 O O4  . NAG H 3 .   ? 9.998   -10.677 -7.417  1.00 67.36 ? 1170 NAG U O4  1 
HETATM 5949 O O5  . NAG H 3 .   ? 12.884  -10.684 -5.156  1.00 64.81 ? 1170 NAG U O5  1 
HETATM 5950 O O6  . NAG H 3 .   ? 11.316  -10.978 -3.226  1.00 71.10 ? 1170 NAG U O6  1 
HETATM 5951 O O7  . NAG H 3 .   ? 16.689  -10.363 -7.287  1.00 67.34 ? 1170 NAG U O7  1 
HETATM 5952 C C1  . NAG I 3 .   ? 31.434  20.733  6.942   1.00 69.60 ? 1259 NAG U C1  1 
HETATM 5953 C C2  . NAG I 3 .   ? 32.576  21.376  6.118   1.00 75.87 ? 1259 NAG U C2  1 
HETATM 5954 C C3  . NAG I 3 .   ? 32.287  22.836  5.774   1.00 77.02 ? 1259 NAG U C3  1 
HETATM 5955 C C4  . NAG I 3 .   ? 30.922  22.869  5.095   1.00 77.53 ? 1259 NAG U C4  1 
HETATM 5956 C C5  . NAG I 3 .   ? 29.878  22.553  6.179   1.00 76.34 ? 1259 NAG U C5  1 
HETATM 5957 C C6  . NAG I 3 .   ? 28.467  22.523  5.587   1.00 76.30 ? 1259 NAG U C6  1 
HETATM 5958 C C7  . NAG I 3 .   ? 35.018  20.865  6.186   1.00 78.34 ? 1259 NAG U C7  1 
HETATM 5959 C C8  . NAG I 3 .   ? 34.968  20.337  4.768   1.00 77.60 ? 1259 NAG U C8  1 
HETATM 5960 N N2  . NAG I 3 .   ? 33.887  21.322  6.768   1.00 77.10 ? 1259 NAG U N2  1 
HETATM 5961 O O3  . NAG I 3 .   ? 33.302  23.369  4.943   1.00 78.10 ? 1259 NAG U O3  1 
HETATM 5962 O O4  . NAG I 3 .   ? 30.688  24.119  4.468   1.00 78.58 ? 1259 NAG U O4  1 
HETATM 5963 O O5  . NAG I 3 .   ? 30.128  21.330  6.882   1.00 73.41 ? 1259 NAG U O5  1 
HETATM 5964 O O6  . NAG I 3 .   ? 27.851  23.737  5.954   1.00 76.02 ? 1259 NAG U O6  1 
HETATM 5965 O O7  . NAG I 3 .   ? 36.099  20.867  6.789   1.00 78.87 ? 1259 NAG U O7  1 
HETATM 5966 C C1  . NAG J 3 .   ? 47.606  39.301  22.140  1.00 59.72 ? 1052 NAG V C1  1 
HETATM 5967 C C2  . NAG J 3 .   ? 48.922  39.910  21.665  1.00 65.32 ? 1052 NAG V C2  1 
HETATM 5968 C C3  . NAG J 3 .   ? 48.644  41.127  20.781  1.00 67.00 ? 1052 NAG V C3  1 
HETATM 5969 C C4  . NAG J 3 .   ? 47.905  40.554  19.571  1.00 68.66 ? 1052 NAG V C4  1 
HETATM 5970 C C5  . NAG J 3 .   ? 46.578  39.967  20.056  1.00 66.40 ? 1052 NAG V C5  1 
HETATM 5971 C C6  . NAG J 3 .   ? 45.751  39.350  18.936  1.00 65.77 ? 1052 NAG V C6  1 
HETATM 5972 C C7  . NAG J 3 .   ? 51.112  39.691  22.744  1.00 66.41 ? 1052 NAG V C7  1 
HETATM 5973 C C8  . NAG J 3 .   ? 51.623  38.945  21.541  1.00 66.56 ? 1052 NAG V C8  1 
HETATM 5974 N N2  . NAG J 3 .   ? 49.844  40.140  22.768  1.00 66.00 ? 1052 NAG V N2  1 
HETATM 5975 O O3  . NAG J 3 .   ? 49.848  41.771  20.411  1.00 67.05 ? 1052 NAG V O3  1 
HETATM 5976 O O4  . NAG J 3 .   ? 47.729  41.501  18.542  1.00 73.88 ? 1052 NAG V O4  1 
HETATM 5977 O O5  . NAG J 3 .   ? 46.842  38.935  21.002  1.00 63.36 ? 1052 NAG V O5  1 
HETATM 5978 O O6  . NAG J 3 .   ? 46.488  38.301  18.354  1.00 64.31 ? 1052 NAG V O6  1 
HETATM 5979 O O7  . NAG J 3 .   ? 51.888  39.858  23.675  1.00 66.65 ? 1052 NAG V O7  1 
HETATM 5980 C C1  . NAG K 3 .   ? 48.576  41.388  17.181  1.00 78.73 ? 1053 NAG V C1  1 
HETATM 5981 C C2  . NAG K 3 .   ? 47.502  42.195  16.438  1.00 80.62 ? 1053 NAG V C2  1 
HETATM 5982 C C3  . NAG K 3 .   ? 48.204  43.146  15.449  1.00 82.27 ? 1053 NAG V C3  1 
HETATM 5983 C C4  . NAG K 3 .   ? 49.322  43.965  16.139  1.00 83.09 ? 1053 NAG V C4  1 
HETATM 5984 C C5  . NAG K 3 .   ? 50.145  43.153  17.159  1.00 81.78 ? 1053 NAG V C5  1 
HETATM 5985 C C6  . NAG K 3 .   ? 51.005  44.047  18.041  1.00 81.16 ? 1053 NAG V C6  1 
HETATM 5986 C C7  . NAG K 3 .   ? 45.154  41.508  15.914  1.00 79.49 ? 1053 NAG V C7  1 
HETATM 5987 C C8  . NAG K 3 .   ? 44.600  42.714  16.632  1.00 79.47 ? 1053 NAG V C8  1 
HETATM 5988 N N2  . NAG K 3 .   ? 46.486  41.320  15.843  1.00 80.08 ? 1053 NAG V N2  1 
HETATM 5989 O O3  . NAG K 3 .   ? 47.275  44.019  14.835  1.00 82.51 ? 1053 NAG V O3  1 
HETATM 5990 O O4  . NAG K 3 .   ? 50.210  44.495  15.166  1.00 84.90 ? 1053 NAG V O4  1 
HETATM 5991 O O5  . NAG K 3 .   ? 49.327  42.309  17.961  1.00 80.30 ? 1053 NAG V O5  1 
HETATM 5992 O O6  . NAG K 3 .   ? 52.347  43.899  17.637  1.00 80.71 ? 1053 NAG V O6  1 
HETATM 5993 O O7  . NAG K 3 .   ? 44.364  40.723  15.398  1.00 78.42 ? 1053 NAG V O7  1 
HETATM 5994 C C1  . NAG L 3 .   ? 58.221  21.798  30.526  1.00 58.07 ? 1170 NAG V C1  1 
HETATM 5995 C C2  . NAG L 3 .   ? 59.435  22.594  30.052  1.00 62.67 ? 1170 NAG V C2  1 
HETATM 5996 C C3  . NAG L 3 .   ? 60.532  22.648  31.113  1.00 63.38 ? 1170 NAG V C3  1 
HETATM 5997 C C4  . NAG L 3 .   ? 59.986  23.033  32.496  1.00 63.68 ? 1170 NAG V C4  1 
HETATM 5998 C C5  . NAG L 3 .   ? 58.834  22.093  32.881  1.00 63.22 ? 1170 NAG V C5  1 
HETATM 5999 C C6  . NAG L 3 .   ? 58.250  22.423  34.271  1.00 63.25 ? 1170 NAG V C6  1 
HETATM 6000 C C7  . NAG L 3 .   ? 59.960  22.650  27.647  1.00 65.44 ? 1170 NAG V C7  1 
HETATM 6001 C C8  . NAG L 3 .   ? 60.537  21.883  26.488  1.00 64.49 ? 1170 NAG V C8  1 
HETATM 6002 N N2  . NAG L 3 .   ? 59.958  22.012  28.827  1.00 64.50 ? 1170 NAG V N2  1 
HETATM 6003 O O3  . NAG L 3 .   ? 61.486  23.591  30.685  1.00 64.47 ? 1170 NAG V O3  1 
HETATM 6004 O O4  . NAG L 3 .   ? 61.015  23.003  33.466  1.00 64.65 ? 1170 NAG V O4  1 
HETATM 6005 O O5  . NAG L 3 .   ? 57.839  22.172  31.854  1.00 61.41 ? 1170 NAG V O5  1 
HETATM 6006 O O6  . NAG L 3 .   ? 57.377  21.416  34.756  1.00 62.45 ? 1170 NAG V O6  1 
HETATM 6007 O O7  . NAG L 3 .   ? 59.522  23.797  27.486  1.00 65.71 ? 1170 NAG V O7  1 
HETATM 6008 C C1  . NAG M 3 .   ? 40.724  28.427  60.613  1.00 62.06 ? 1160 NAG V C1  1 
HETATM 6009 C C2  . NAG M 3 .   ? 39.573  29.424  60.956  1.00 68.26 ? 1160 NAG V C2  1 
HETATM 6010 C C3  . NAG M 3 .   ? 38.377  28.604  61.445  1.00 67.79 ? 1160 NAG V C3  1 
HETATM 6011 C C4  . NAG M 3 .   ? 37.933  27.757  60.251  1.00 68.09 ? 1160 NAG V C4  1 
HETATM 6012 C C5  . NAG M 3 .   ? 39.102  26.835  59.834  1.00 66.63 ? 1160 NAG V C5  1 
HETATM 6013 C C6  . NAG M 3 .   ? 38.727  25.887  58.694  1.00 65.98 ? 1160 NAG V C6  1 
HETATM 6014 C C7  . NAG M 3 .   ? 39.358  31.712  62.044  1.00 73.48 ? 1160 NAG V C7  1 
HETATM 6015 C C8  . NAG M 3 .   ? 38.291  32.208  61.089  1.00 72.96 ? 1160 NAG V C8  1 
HETATM 6016 N N2  . NAG M 3 .   ? 39.891  30.471  61.932  1.00 71.46 ? 1160 NAG V N2  1 
HETATM 6017 O O3  . NAG M 3 .   ? 37.348  29.413  61.987  1.00 67.20 ? 1160 NAG V O3  1 
HETATM 6018 O O4  . NAG M 3 .   ? 36.780  27.022  60.602  1.00 70.38 ? 1160 NAG V O4  1 
HETATM 6019 O O5  . NAG M 3 .   ? 40.278  27.596  59.523  1.00 64.80 ? 1160 NAG V O5  1 
HETATM 6020 O O6  . NAG M 3 .   ? 38.098  24.741  59.232  1.00 63.65 ? 1160 NAG V O6  1 
HETATM 6021 O O7  . NAG M 3 .   ? 39.746  32.470  62.940  1.00 74.54 ? 1160 NAG V O7  1 
HETATM 6022 C C1  . NAG N 3 .   ? 48.317  53.838  40.237  1.00 71.21 ? 1259 NAG V C1  1 
HETATM 6023 C C2  . NAG N 3 .   ? 47.700  53.581  41.638  1.00 78.81 ? 1259 NAG V C2  1 
HETATM 6024 C C3  . NAG N 3 .   ? 48.414  54.478  42.682  1.00 78.60 ? 1259 NAG V C3  1 
HETATM 6025 C C4  . NAG N 3 .   ? 49.919  54.143  42.691  1.00 78.17 ? 1259 NAG V C4  1 
HETATM 6026 C C5  . NAG N 3 .   ? 50.535  54.148  41.249  1.00 77.34 ? 1259 NAG V C5  1 
HETATM 6027 C C6  . NAG N 3 .   ? 51.949  53.547  41.121  1.00 78.36 ? 1259 NAG V C6  1 
HETATM 6028 C C7  . NAG N 3 .   ? 45.345  53.061  42.475  1.00 85.40 ? 1259 NAG V C7  1 
HETATM 6029 C C8  . NAG N 3 .   ? 45.849  52.012  43.447  1.00 85.27 ? 1259 NAG V C8  1 
HETATM 6030 N N2  . NAG N 3 .   ? 46.233  53.729  41.681  1.00 82.81 ? 1259 NAG V N2  1 
HETATM 6031 O O3  . NAG N 3 .   ? 47.848  54.393  43.987  1.00 78.10 ? 1259 NAG V O3  1 
HETATM 6032 O O4  . NAG N 3 .   ? 50.578  55.023  43.590  1.00 77.28 ? 1259 NAG V O4  1 
HETATM 6033 O O5  . NAG N 3 .   ? 49.718  53.526  40.237  1.00 73.72 ? 1259 NAG V O5  1 
HETATM 6034 O O6  . NAG N 3 .   ? 52.190  52.447  41.989  1.00 79.97 ? 1259 NAG V O6  1 
HETATM 6035 O O7  . NAG N 3 .   ? 44.116  53.280  42.427  1.00 85.86 ? 1259 NAG V O7  1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   ?   ?   ?   A . n 
A 1 4   LEU 4   4   ?   ?   ?   A . n 
A 1 5   GLY 5   5   ?   ?   ?   A . n 
A 1 6   ALA 6   6   ?   ?   ?   A . n 
A 1 7   PRO 7   7   ?   ?   ?   A . n 
A 1 8   ASP 8   8   ?   ?   ?   A . n 
A 1 9   GLU 9   9   9   GLU GLU A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  CYS 12  12  12  CYS CYS A . n 
A 1 13  GLY 13  13  13  GLY GLY A . n 
A 1 14  CYS 14  14  14  CYS CYS A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  ASN 16  16  16  ASN ASN A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  CYS 20  20  20  CYS CYS A . n 
A 1 21  VAL 21  21  21  VAL VAL A . n 
A 1 22  SER 22  22  22  SER SER A . n 
A 1 23  TYR 23  23  23  TYR TYR A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  ARG 30  30  30  ARG ARG A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  CYS 32  32  32  CYS CYS A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  CYS 34  34  34  CYS CYS A . n 
A 1 35  PRO 35  35  35  PRO PRO A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  GLN 39  39  39  GLN GLN A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  GLU 41  41  41  GLU GLU A . n 
A 1 42  HIS 42  42  42  HIS HIS A . n 
A 1 43  CYS 43  43  43  CYS CYS A . n 
A 1 44  GLU 44  44  44  GLU GLU A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  LYS 49  49  49  LYS LYS A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  CYS 51  51  51  CYS CYS A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  GLY 54  54  54  GLY GLY A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  TYR 59  59  59  TYR TYR A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  PRO 71  71  71  PRO PRO A . n 
A 1 72  CYS 72  72  72  CYS CYS A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  ALA 74  74  74  ALA ALA A . n 
A 1 75  TRP 75  75  75  TRP TRP A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  PRO 78  78  78  PRO PRO A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  VAL 80  80  80  VAL VAL A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  HIS 88  88  88  HIS HIS A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 HIS 100 100 100 HIS HIS A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 TYR 102 102 102 TYR TYR A . n 
A 1 103 CYS 103 103 103 CYS CYS A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 ASN 105 105 105 ASN ASN A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ASP 107 107 107 ASP ASP A . n 
A 1 108 ASN 108 108 108 ASN ASN A . n 
A 1 109 GLN 109 109 109 GLN GLN A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 TRP 113 113 113 TRP TRP A . n 
A 1 114 CYS 114 114 114 CYS CYS A . n 
A 1 115 TYR 115 115 115 TYR TYR A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 GLN 117 117 117 GLN GLN A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 GLN 122 122 122 GLN GLN A . n 
A 1 123 PHE 123 123 123 PHE PHE A . n 
A 1 124 VAL 124 124 124 VAL VAL A . n 
A 1 125 GLN 125 125 125 GLN GLN A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 CYS 127 127 127 CYS CYS A . n 
A 1 128 MET 128 128 128 MET MET A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 CYS 132 132 132 CYS CYS A . n 
A 1 133 SER 133 133 ?   ?   ?   A . n 
A 1 134 LEU 134 134 ?   ?   ?   A . n 
B 2 1   LEU 1   1   1   LEU LEU U . n 
B 2 2   GLN 2   2   2   GLN GLN U . n 
B 2 3   CYS 3   3   3   CYS CYS U . n 
B 2 4   MET 4   4   4   MET MET U . n 
B 2 5   GLN 5   5   5   GLN GLN U . n 
B 2 6   CYS 6   6   6   CYS CYS U . n 
B 2 7   GLU 7   7   7   GLU GLU U . n 
B 2 8   SER 8   8   8   SER SER U . n 
B 2 9   ASN 9   9   9   ASN ASN U . n 
B 2 10  GLN 10  10  10  GLN GLN U . n 
B 2 11  SER 11  11  11  SER SER U . n 
B 2 12  CYS 12  12  12  CYS CYS U . n 
B 2 13  LEU 13  13  13  LEU LEU U . n 
B 2 14  VAL 14  14  14  VAL VAL U . n 
B 2 15  GLU 15  15  15  GLU GLU U . n 
B 2 16  GLU 16  16  16  GLU GLU U . n 
B 2 17  CYS 17  17  17  CYS CYS U . n 
B 2 18  ALA 18  18  18  ALA ALA U . n 
B 2 19  LEU 19  19  19  LEU LEU U . n 
B 2 20  GLY 20  20  20  GLY GLY U . n 
B 2 21  GLN 21  21  21  GLN GLN U . n 
B 2 22  ASP 22  22  22  ASP ASP U . n 
B 2 23  LEU 23  23  23  LEU LEU U . n 
B 2 24  CYS 24  24  24  CYS CYS U . n 
B 2 25  ARG 25  25  25  ARG ARG U . n 
B 2 26  THR 26  26  26  THR THR U . n 
B 2 27  THR 27  27  27  THR THR U . n 
B 2 28  VAL 28  28  28  VAL VAL U . n 
B 2 29  LEU 29  29  29  LEU LEU U . n 
B 2 30  ARG 30  30  30  ARG ARG U . n 
B 2 31  GLU 31  31  31  GLU GLU U . n 
B 2 32  TRP 32  32  32  TRP TRP U . n 
B 2 33  GLN 33  33  33  GLN GLN U . n 
B 2 34  ASP 34  34  34  ASP ASP U . n 
B 2 35  ASP 35  35  35  ASP ASP U . n 
B 2 36  ARG 36  36  36  ARG ARG U . n 
B 2 37  GLU 37  37  37  GLU GLU U . n 
B 2 38  LEU 38  38  38  LEU LEU U . n 
B 2 39  GLU 39  39  39  GLU GLU U . n 
B 2 40  VAL 40  40  40  VAL VAL U . n 
B 2 41  VAL 41  41  41  VAL VAL U . n 
B 2 42  THR 42  42  42  THR THR U . n 
B 2 43  ARG 43  43  43  ARG ARG U . n 
B 2 44  GLY 44  44  44  GLY GLY U . n 
B 2 45  CYS 45  45  45  CYS CYS U . n 
B 2 46  ALA 46  46  46  ALA ALA U . n 
B 2 47  HIS 47  47  47  HIS HIS U . n 
B 2 48  SER 48  48  48  SER SER U . n 
B 2 49  GLU 49  49  49  GLU GLU U . n 
B 2 50  LYS 50  50  50  LYS LYS U . n 
B 2 51  THR 51  51  51  THR THR U . n 
B 2 52  ASN 52  52  52  ASN ASN U . n 
B 2 53  ARG 53  53  53  ARG ARG U . n 
B 2 54  THR 54  54  54  THR THR U . n 
B 2 55  MET 55  55  55  MET MET U . n 
B 2 56  SER 56  56  56  SER SER U . n 
B 2 57  TYR 57  57  57  TYR TYR U . n 
B 2 58  ARG 58  58  58  ARG ARG U . n 
B 2 59  MET 59  59  59  MET MET U . n 
B 2 60  GLY 60  60  60  GLY GLY U . n 
B 2 61  SER 61  61  61  SER SER U . n 
B 2 62  MET 62  62  62  MET MET U . n 
B 2 63  ILE 63  63  63  ILE ILE U . n 
B 2 64  ILE 64  64  64  ILE ILE U . n 
B 2 65  SER 65  65  65  SER SER U . n 
B 2 66  LEU 66  66  66  LEU LEU U . n 
B 2 67  THR 67  67  67  THR THR U . n 
B 2 68  GLU 68  68  68  GLU GLU U . n 
B 2 69  THR 69  69  69  THR THR U . n 
B 2 70  VAL 70  70  70  VAL VAL U . n 
B 2 71  CYS 71  71  71  CYS CYS U . n 
B 2 72  ALA 72  72  72  ALA ALA U . n 
B 2 73  THR 73  73  73  THR THR U . n 
B 2 74  ASN 74  74  74  ASN ASN U . n 
B 2 75  LEU 75  75  75  LEU LEU U . n 
B 2 76  CYS 76  76  76  CYS CYS U . n 
B 2 77  ASN 77  77  77  ASN ASN U . n 
B 2 78  ARG 78  78  78  ARG ARG U . n 
B 2 79  PRO 79  79  79  PRO PRO U . n 
B 2 80  ARG 80  80  80  ARG ARG U . n 
B 2 81  PRO 81  81  81  PRO PRO U . n 
B 2 82  GLY 82  82  ?   ?   ?   U . n 
B 2 83  ALA 83  83  ?   ?   ?   U . n 
B 2 84  ARG 84  84  ?   ?   ?   U . n 
B 2 85  GLY 85  85  ?   ?   ?   U . n 
B 2 86  ARG 86  86  ?   ?   ?   U . n 
B 2 87  ALA 87  87  ?   ?   ?   U . n 
B 2 88  PHE 88  88  ?   ?   ?   U . n 
B 2 89  PRO 89  89  ?   ?   ?   U . n 
B 2 90  GLN 90  90  ?   ?   ?   U . n 
B 2 91  GLY 91  91  ?   ?   ?   U . n 
B 2 92  ARG 92  92  ?   ?   ?   U . n 
B 2 93  TYR 93  93  93  TYR TYR U . n 
B 2 94  LEU 94  94  94  LEU LEU U . n 
B 2 95  GLU 95  95  95  GLU GLU U . n 
B 2 96  CYS 96  96  96  CYS CYS U . n 
B 2 97  ALA 97  97  97  ALA ALA U . n 
B 2 98  SER 98  98  98  SER SER U . n 
B 2 99  CYS 99  99  99  CYS CYS U . n 
B 2 100 THR 100 100 100 THR THR U . n 
B 2 101 SER 101 101 101 SER SER U . n 
B 2 102 LEU 102 102 102 LEU LEU U . n 
B 2 103 ASP 103 103 103 ASP ASP U . n 
B 2 104 GLN 104 104 104 GLN GLN U . n 
B 2 105 SER 105 105 105 SER SER U . n 
B 2 106 CYS 106 106 106 CYS CYS U . n 
B 2 107 GLU 107 107 107 GLU GLU U . n 
B 2 108 ARG 108 108 108 ARG ARG U . n 
B 2 109 GLY 109 109 109 GLY GLY U . n 
B 2 110 ARG 110 110 110 ARG ARG U . n 
B 2 111 GLU 111 111 111 GLU GLU U . n 
B 2 112 GLN 112 112 112 GLN GLN U . n 
B 2 113 SER 113 113 113 SER SER U . n 
B 2 114 LEU 114 114 114 LEU LEU U . n 
B 2 115 GLN 115 115 115 GLN GLN U . n 
B 2 116 CYS 116 116 116 CYS CYS U . n 
B 2 117 ARG 117 117 117 ARG ARG U . n 
B 2 118 TYR 118 118 118 TYR TYR U . n 
B 2 119 PRO 119 119 119 PRO PRO U . n 
B 2 120 THR 120 120 120 THR THR U . n 
B 2 121 GLU 121 121 121 GLU GLU U . n 
B 2 122 HIS 122 122 122 HIS HIS U . n 
B 2 123 CYS 123 123 123 CYS CYS U . n 
B 2 124 ILE 124 124 124 ILE ILE U . n 
B 2 125 GLU 125 125 125 GLU GLU U . n 
B 2 126 VAL 126 126 126 VAL VAL U . n 
B 2 127 VAL 127 127 127 VAL VAL U . n 
B 2 128 THR 128 128 128 THR THR U . n 
B 2 129 LEU 129 129 129 LEU LEU U . n 
B 2 130 GLN 130 130 130 GLN GLN U . n 
B 2 131 SER 131 131 131 SER SER U . n 
B 2 132 THR 132 132 132 THR THR U . n 
B 2 133 GLU 133 133 133 GLU GLU U . n 
B 2 134 ARG 134 134 134 ARG ARG U . n 
B 2 135 SER 135 135 135 SER SER U . n 
B 2 136 LEU 136 136 136 LEU LEU U . n 
B 2 137 LYS 137 137 137 LYS LYS U . n 
B 2 138 ASP 138 138 138 ASP ASP U . n 
B 2 139 GLU 139 139 139 GLU GLU U . n 
B 2 140 ASP 140 140 140 ASP ASP U . n 
B 2 141 TYR 141 141 141 TYR TYR U . n 
B 2 142 THR 142 142 142 THR THR U . n 
B 2 143 ARG 143 143 143 ARG ARG U . n 
B 2 144 GLY 144 144 144 GLY GLY U . n 
B 2 145 CYS 145 145 145 CYS CYS U . n 
B 2 146 GLY 146 146 146 GLY GLY U . n 
B 2 147 SER 147 147 147 SER SER U . n 
B 2 148 LEU 148 148 148 LEU LEU U . n 
B 2 149 PRO 149 149 149 PRO PRO U . n 
B 2 150 GLY 150 150 150 GLY GLY U . n 
B 2 151 CYS 151 151 151 CYS CYS U . n 
B 2 152 PRO 152 152 152 PRO PRO U . n 
B 2 153 GLY 153 153 153 GLY GLY U . n 
B 2 154 THR 154 154 154 THR THR U . n 
B 2 155 ALA 155 155 155 ALA ALA U . n 
B 2 156 GLY 156 156 156 GLY GLY U . n 
B 2 157 PHE 157 157 157 PHE PHE U . n 
B 2 158 HIS 158 158 158 HIS HIS U . n 
B 2 159 SER 159 159 159 SER SER U . n 
B 2 160 ASN 160 160 160 ASN ASN U . n 
B 2 161 GLN 161 161 161 GLN GLN U . n 
B 2 162 THR 162 162 162 THR THR U . n 
B 2 163 PHE 163 163 163 PHE PHE U . n 
B 2 164 HIS 164 164 164 HIS HIS U . n 
B 2 165 PHE 165 165 165 PHE PHE U . n 
B 2 166 LEU 166 166 166 LEU LEU U . n 
B 2 167 LYS 167 167 167 LYS LYS U . n 
B 2 168 CYS 168 168 168 CYS CYS U . n 
B 2 169 CYS 169 169 169 CYS CYS U . n 
B 2 170 ASN 170 170 170 ASN ASN U . n 
B 2 171 TYR 171 171 171 TYR TYR U . n 
B 2 172 THR 172 172 172 THR THR U . n 
B 2 173 HIS 173 173 173 HIS HIS U . n 
B 2 174 CYS 174 174 174 CYS CYS U . n 
B 2 175 ASN 175 175 175 ASN ASN U . n 
B 2 176 GLY 176 176 176 GLY GLY U . n 
B 2 177 GLY 177 177 177 GLY GLY U . n 
B 2 178 PRO 178 178 178 PRO PRO U . n 
B 2 179 VAL 179 179 179 VAL VAL U . n 
B 2 180 LEU 180 180 180 LEU LEU U . n 
B 2 181 ASP 181 181 181 ASP ASP U . n 
B 2 182 LEU 182 182 182 LEU LEU U . n 
B 2 183 GLN 183 183 183 GLN GLN U . n 
B 2 184 SER 184 184 184 SER SER U . n 
B 2 185 PHE 185 185 185 PHE PHE U . n 
B 2 186 PRO 186 186 186 PRO PRO U . n 
B 2 187 PRO 187 187 187 PRO PRO U . n 
B 2 188 ASN 188 188 188 ASN ASN U . n 
B 2 189 GLY 189 189 189 GLY GLY U . n 
B 2 190 PHE 190 190 190 PHE PHE U . n 
B 2 191 GLN 191 191 191 GLN GLN U . n 
B 2 192 CYS 192 192 192 CYS CYS U . n 
B 2 193 TYR 193 193 193 TYR TYR U . n 
B 2 194 SER 194 194 194 SER SER U . n 
B 2 195 CYS 195 195 195 CYS CYS U . n 
B 2 196 GLU 196 196 196 GLU GLU U . n 
B 2 197 GLY 197 197 197 GLY GLY U . n 
B 2 198 ASN 198 198 198 ASN ASN U . n 
B 2 199 ASN 199 199 199 ASN ASN U . n 
B 2 200 THR 200 200 200 THR THR U . n 
B 2 201 LEU 201 201 201 LEU LEU U . n 
B 2 202 GLY 202 202 202 GLY GLY U . n 
B 2 203 CYS 203 203 203 CYS CYS U . n 
B 2 204 SER 204 204 204 SER SER U . n 
B 2 205 SER 205 205 205 SER SER U . n 
B 2 206 GLU 206 206 206 GLU GLU U . n 
B 2 207 GLU 207 207 207 GLU GLU U . n 
B 2 208 ALA 208 208 208 ALA ALA U . n 
B 2 209 SER 209 209 209 SER SER U . n 
B 2 210 LEU 210 210 210 LEU LEU U . n 
B 2 211 ILE 211 211 211 ILE ILE U . n 
B 2 212 ASN 212 212 212 ASN ASN U . n 
B 2 213 CYS 213 213 213 CYS CYS U . n 
B 2 214 ARG 214 214 214 ARG ARG U . n 
B 2 215 GLY 215 215 215 GLY GLY U . n 
B 2 216 PRO 216 216 216 PRO PRO U . n 
B 2 217 MET 217 217 217 MET MET U . n 
B 2 218 ASN 218 218 218 ASN ASN U . n 
B 2 219 GLN 219 219 219 GLN GLN U . n 
B 2 220 CYS 220 220 220 CYS CYS U . n 
B 2 221 LEU 221 221 221 LEU LEU U . n 
B 2 222 VAL 222 222 222 VAL VAL U . n 
B 2 223 ALA 223 223 223 ALA ALA U . n 
B 2 224 THR 224 224 224 THR THR U . n 
B 2 225 GLY 225 225 225 GLY GLY U . n 
B 2 226 LEU 226 226 226 LEU LEU U . n 
B 2 227 ASP 227 227 ?   ?   ?   U . n 
B 2 228 VAL 228 228 ?   ?   ?   U . n 
B 2 229 LEU 229 229 ?   ?   ?   U . n 
B 2 230 GLY 230 230 ?   ?   ?   U . n 
B 2 231 ASN 231 231 ?   ?   ?   U . n 
B 2 232 ARG 232 232 232 ARG ARG U . n 
B 2 233 SER 233 233 233 SER SER U . n 
B 2 234 TYR 234 234 234 TYR TYR U . n 
B 2 235 THR 235 235 235 THR THR U . n 
B 2 236 VAL 236 236 236 VAL VAL U . n 
B 2 237 ARG 237 237 237 ARG ARG U . n 
B 2 238 GLY 238 238 238 GLY GLY U . n 
B 2 239 CYS 239 239 239 CYS CYS U . n 
B 2 240 ALA 240 240 240 ALA ALA U . n 
B 2 241 THR 241 241 241 THR THR U . n 
B 2 242 ALA 242 242 242 ALA ALA U . n 
B 2 243 SER 243 243 243 SER SER U . n 
B 2 244 TRP 244 244 244 TRP TRP U . n 
B 2 245 CYS 245 245 245 CYS CYS U . n 
B 2 246 GLN 246 246 246 GLN GLN U . n 
B 2 247 GLY 247 247 247 GLY GLY U . n 
B 2 248 SER 248 248 248 SER SER U . n 
B 2 249 HIS 249 249 249 HIS HIS U . n 
B 2 250 VAL 250 250 250 VAL VAL U . n 
B 2 251 ALA 251 251 251 ALA ALA U . n 
B 2 252 ASP 252 252 252 ASP ASP U . n 
B 2 253 SER 253 253 253 SER SER U . n 
B 2 254 PHE 254 254 254 PHE PHE U . n 
B 2 255 PRO 255 255 255 PRO PRO U . n 
B 2 256 THR 256 256 256 THR THR U . n 
B 2 257 HIS 257 257 257 HIS HIS U . n 
B 2 258 LEU 258 258 258 LEU LEU U . n 
B 2 259 ASN 259 259 259 ASN ASN U . n 
B 2 260 VAL 260 260 260 VAL VAL U . n 
B 2 261 SER 261 261 261 SER SER U . n 
B 2 262 VAL 262 262 262 VAL VAL U . n 
B 2 263 SER 263 263 263 SER SER U . n 
B 2 264 CYS 264 264 264 CYS CYS U . n 
B 2 265 CYS 265 265 265 CYS CYS U . n 
B 2 266 HIS 266 266 266 HIS HIS U . n 
B 2 267 GLY 267 267 267 GLY GLY U . n 
B 2 268 SER 268 268 268 SER SER U . n 
B 2 269 GLY 269 269 269 GLY GLY U . n 
B 2 270 CYS 270 270 270 CYS CYS U . n 
B 2 271 ASN 271 271 271 ASN ASN U . n 
B 2 272 SER 272 272 272 SER SER U . n 
B 2 273 PRO 273 273 273 PRO PRO U . n 
B 2 274 THR 274 274 274 THR THR U . n 
B 2 275 GLY 275 275 ?   ?   ?   U . n 
B 2 276 GLY 276 276 ?   ?   ?   U . n 
B 2 277 ALA 277 277 ?   ?   ?   U . n 
C 1 1   GLY 1   1   ?   ?   ?   B . n 
C 1 2   SER 2   2   ?   ?   ?   B . n 
C 1 3   VAL 3   3   ?   ?   ?   B . n 
C 1 4   LEU 4   4   ?   ?   ?   B . n 
C 1 5   GLY 5   5   ?   ?   ?   B . n 
C 1 6   ALA 6   6   ?   ?   ?   B . n 
C 1 7   PRO 7   7   ?   ?   ?   B . n 
C 1 8   ASP 8   8   8   ASP ASP B . n 
C 1 9   GLU 9   9   9   GLU GLU B . n 
C 1 10  SER 10  10  10  SER SER B . n 
C 1 11  ASN 11  11  11  ASN ASN B . n 
C 1 12  CYS 12  12  12  CYS CYS B . n 
C 1 13  GLY 13  13  13  GLY GLY B . n 
C 1 14  CYS 14  14  14  CYS CYS B . n 
C 1 15  GLN 15  15  15  GLN GLN B . n 
C 1 16  ASN 16  16  16  ASN ASN B . n 
C 1 17  GLY 17  17  17  GLY GLY B . n 
C 1 18  GLY 18  18  18  GLY GLY B . n 
C 1 19  VAL 19  19  19  VAL VAL B . n 
C 1 20  CYS 20  20  20  CYS CYS B . n 
C 1 21  VAL 21  21  21  VAL VAL B . n 
C 1 22  SER 22  22  22  SER SER B . n 
C 1 23  TYR 23  23  23  TYR TYR B . n 
C 1 24  LYS 24  24  24  LYS LYS B . n 
C 1 25  TYR 25  25  25  TYR TYR B . n 
C 1 26  PHE 26  26  26  PHE PHE B . n 
C 1 27  SER 27  27  27  SER SER B . n 
C 1 28  ARG 28  28  28  ARG ARG B . n 
C 1 29  ILE 29  29  29  ILE ILE B . n 
C 1 30  ARG 30  30  30  ARG ARG B . n 
C 1 31  ARG 31  31  31  ARG ARG B . n 
C 1 32  CYS 32  32  32  CYS CYS B . n 
C 1 33  SER 33  33  33  SER SER B . n 
C 1 34  CYS 34  34  34  CYS CYS B . n 
C 1 35  PRO 35  35  35  PRO PRO B . n 
C 1 36  ARG 36  36  36  ARG ARG B . n 
C 1 37  LYS 37  37  37  LYS LYS B . n 
C 1 38  PHE 38  38  38  PHE PHE B . n 
C 1 39  GLN 39  39  39  GLN GLN B . n 
C 1 40  GLY 40  40  40  GLY GLY B . n 
C 1 41  GLU 41  41  41  GLU GLU B . n 
C 1 42  HIS 42  42  42  HIS HIS B . n 
C 1 43  CYS 43  43  43  CYS CYS B . n 
C 1 44  GLU 44  44  44  GLU GLU B . n 
C 1 45  ILE 45  45  45  ILE ILE B . n 
C 1 46  ASP 46  46  46  ASP ASP B . n 
C 1 47  ALA 47  47  47  ALA ALA B . n 
C 1 48  SER 48  48  48  SER SER B . n 
C 1 49  LYS 49  49  49  LYS LYS B . n 
C 1 50  THR 50  50  50  THR THR B . n 
C 1 51  CYS 51  51  51  CYS CYS B . n 
C 1 52  TYR 52  52  52  TYR TYR B . n 
C 1 53  HIS 53  53  53  HIS HIS B . n 
C 1 54  GLY 54  54  54  GLY GLY B . n 
C 1 55  ASN 55  55  55  ASN ASN B . n 
C 1 56  GLY 56  56  56  GLY GLY B . n 
C 1 57  ASP 57  57  57  ASP ASP B . n 
C 1 58  SER 58  58  58  SER SER B . n 
C 1 59  TYR 59  59  59  TYR TYR B . n 
C 1 60  ARG 60  60  60  ARG ARG B . n 
C 1 61  GLY 61  61  61  GLY GLY B . n 
C 1 62  LYS 62  62  62  LYS LYS B . n 
C 1 63  ALA 63  63  63  ALA ALA B . n 
C 1 64  ASN 64  64  64  ASN ASN B . n 
C 1 65  THR 65  65  65  THR THR B . n 
C 1 66  ASP 66  66  66  ASP ASP B . n 
C 1 67  THR 67  67  67  THR THR B . n 
C 1 68  LYS 68  68  68  LYS LYS B . n 
C 1 69  GLY 69  69  69  GLY GLY B . n 
C 1 70  ARG 70  70  70  ARG ARG B . n 
C 1 71  PRO 71  71  71  PRO PRO B . n 
C 1 72  CYS 72  72  72  CYS CYS B . n 
C 1 73  LEU 73  73  73  LEU LEU B . n 
C 1 74  ALA 74  74  74  ALA ALA B . n 
C 1 75  TRP 75  75  75  TRP TRP B . n 
C 1 76  ASN 76  76  76  ASN ASN B . n 
C 1 77  ALA 77  77  77  ALA ALA B . n 
C 1 78  PRO 78  78  78  PRO PRO B . n 
C 1 79  ALA 79  79  79  ALA ALA B . n 
C 1 80  VAL 80  80  80  VAL VAL B . n 
C 1 81  LEU 81  81  81  LEU LEU B . n 
C 1 82  GLN 82  82  82  GLN GLN B . n 
C 1 83  LYS 83  83  83  LYS LYS B . n 
C 1 84  PRO 84  84  84  PRO PRO B . n 
C 1 85  TYR 85  85  85  TYR TYR B . n 
C 1 86  ASN 86  86  86  ASN ASN B . n 
C 1 87  ALA 87  87  87  ALA ALA B . n 
C 1 88  HIS 88  88  88  HIS HIS B . n 
C 1 89  ARG 89  89  89  ARG ARG B . n 
C 1 90  PRO 90  90  90  PRO PRO B . n 
C 1 91  ASP 91  91  91  ASP ASP B . n 
C 1 92  ALA 92  92  92  ALA ALA B . n 
C 1 93  ILE 93  93  93  ILE ILE B . n 
C 1 94  SER 94  94  94  SER SER B . n 
C 1 95  LEU 95  95  95  LEU LEU B . n 
C 1 96  GLY 96  96  96  GLY GLY B . n 
C 1 97  LEU 97  97  97  LEU LEU B . n 
C 1 98  GLY 98  98  98  GLY GLY B . n 
C 1 99  LYS 99  99  99  LYS LYS B . n 
C 1 100 HIS 100 100 100 HIS HIS B . n 
C 1 101 ASN 101 101 101 ASN ASN B . n 
C 1 102 TYR 102 102 102 TYR TYR B . n 
C 1 103 CYS 103 103 103 CYS CYS B . n 
C 1 104 ARG 104 104 104 ARG ARG B . n 
C 1 105 ASN 105 105 105 ASN ASN B . n 
C 1 106 PRO 106 106 106 PRO PRO B . n 
C 1 107 ASP 107 107 107 ASP ASP B . n 
C 1 108 ASN 108 108 108 ASN ASN B . n 
C 1 109 GLN 109 109 109 GLN GLN B . n 
C 1 110 LYS 110 110 110 LYS LYS B . n 
C 1 111 ARG 111 111 111 ARG ARG B . n 
C 1 112 PRO 112 112 112 PRO PRO B . n 
C 1 113 TRP 113 113 113 TRP TRP B . n 
C 1 114 CYS 114 114 114 CYS CYS B . n 
C 1 115 TYR 115 115 115 TYR TYR B . n 
C 1 116 VAL 116 116 116 VAL VAL B . n 
C 1 117 GLN 117 117 117 GLN GLN B . n 
C 1 118 ILE 118 118 118 ILE ILE B . n 
C 1 119 GLY 119 119 119 GLY GLY B . n 
C 1 120 LEU 120 120 120 LEU LEU B . n 
C 1 121 ARG 121 121 121 ARG ARG B . n 
C 1 122 GLN 122 122 122 GLN GLN B . n 
C 1 123 PHE 123 123 123 PHE PHE B . n 
C 1 124 VAL 124 124 124 VAL VAL B . n 
C 1 125 GLN 125 125 125 GLN GLN B . n 
C 1 126 GLU 126 126 126 GLU GLU B . n 
C 1 127 CYS 127 127 127 CYS CYS B . n 
C 1 128 MET 128 128 128 MET MET B . n 
C 1 129 VAL 129 129 129 VAL VAL B . n 
C 1 130 HIS 130 130 130 HIS HIS B . n 
C 1 131 ASP 131 131 131 ASP ASP B . n 
C 1 132 CYS 132 132 132 CYS CYS B . n 
C 1 133 SER 133 133 ?   ?   ?   B . n 
C 1 134 LEU 134 134 ?   ?   ?   B . n 
D 2 1   LEU 1   1   1   LEU LEU V . n 
D 2 2   GLN 2   2   2   GLN GLN V . n 
D 2 3   CYS 3   3   3   CYS CYS V . n 
D 2 4   MET 4   4   4   MET MET V . n 
D 2 5   GLN 5   5   5   GLN GLN V . n 
D 2 6   CYS 6   6   6   CYS CYS V . n 
D 2 7   GLU 7   7   7   GLU GLU V . n 
D 2 8   SER 8   8   8   SER SER V . n 
D 2 9   ASN 9   9   9   ASN ASN V . n 
D 2 10  GLN 10  10  10  GLN GLN V . n 
D 2 11  SER 11  11  11  SER SER V . n 
D 2 12  CYS 12  12  12  CYS CYS V . n 
D 2 13  LEU 13  13  13  LEU LEU V . n 
D 2 14  VAL 14  14  14  VAL VAL V . n 
D 2 15  GLU 15  15  15  GLU GLU V . n 
D 2 16  GLU 16  16  16  GLU GLU V . n 
D 2 17  CYS 17  17  17  CYS CYS V . n 
D 2 18  ALA 18  18  18  ALA ALA V . n 
D 2 19  LEU 19  19  19  LEU LEU V . n 
D 2 20  GLY 20  20  20  GLY GLY V . n 
D 2 21  GLN 21  21  21  GLN GLN V . n 
D 2 22  ASP 22  22  22  ASP ASP V . n 
D 2 23  LEU 23  23  23  LEU LEU V . n 
D 2 24  CYS 24  24  24  CYS CYS V . n 
D 2 25  ARG 25  25  25  ARG ARG V . n 
D 2 26  THR 26  26  26  THR THR V . n 
D 2 27  THR 27  27  27  THR THR V . n 
D 2 28  VAL 28  28  28  VAL VAL V . n 
D 2 29  LEU 29  29  29  LEU LEU V . n 
D 2 30  ARG 30  30  30  ARG ARG V . n 
D 2 31  GLU 31  31  31  GLU GLU V . n 
D 2 32  TRP 32  32  32  TRP TRP V . n 
D 2 33  GLN 33  33  33  GLN GLN V . n 
D 2 34  ASP 34  34  34  ASP ASP V . n 
D 2 35  ASP 35  35  35  ASP ASP V . n 
D 2 36  ARG 36  36  36  ARG ARG V . n 
D 2 37  GLU 37  37  37  GLU GLU V . n 
D 2 38  LEU 38  38  38  LEU LEU V . n 
D 2 39  GLU 39  39  39  GLU GLU V . n 
D 2 40  VAL 40  40  40  VAL VAL V . n 
D 2 41  VAL 41  41  41  VAL VAL V . n 
D 2 42  THR 42  42  42  THR THR V . n 
D 2 43  ARG 43  43  43  ARG ARG V . n 
D 2 44  GLY 44  44  44  GLY GLY V . n 
D 2 45  CYS 45  45  45  CYS CYS V . n 
D 2 46  ALA 46  46  46  ALA ALA V . n 
D 2 47  HIS 47  47  47  HIS HIS V . n 
D 2 48  SER 48  48  48  SER SER V . n 
D 2 49  GLU 49  49  49  GLU GLU V . n 
D 2 50  LYS 50  50  50  LYS LYS V . n 
D 2 51  THR 51  51  51  THR THR V . n 
D 2 52  ASN 52  52  52  ASN ASN V . n 
D 2 53  ARG 53  53  53  ARG ARG V . n 
D 2 54  THR 54  54  54  THR THR V . n 
D 2 55  MET 55  55  55  MET MET V . n 
D 2 56  SER 56  56  56  SER SER V . n 
D 2 57  TYR 57  57  57  TYR TYR V . n 
D 2 58  ARG 58  58  58  ARG ARG V . n 
D 2 59  MET 59  59  59  MET MET V . n 
D 2 60  GLY 60  60  60  GLY GLY V . n 
D 2 61  SER 61  61  61  SER SER V . n 
D 2 62  MET 62  62  62  MET MET V . n 
D 2 63  ILE 63  63  63  ILE ILE V . n 
D 2 64  ILE 64  64  64  ILE ILE V . n 
D 2 65  SER 65  65  65  SER SER V . n 
D 2 66  LEU 66  66  66  LEU LEU V . n 
D 2 67  THR 67  67  67  THR THR V . n 
D 2 68  GLU 68  68  68  GLU GLU V . n 
D 2 69  THR 69  69  69  THR THR V . n 
D 2 70  VAL 70  70  70  VAL VAL V . n 
D 2 71  CYS 71  71  71  CYS CYS V . n 
D 2 72  ALA 72  72  72  ALA ALA V . n 
D 2 73  THR 73  73  73  THR THR V . n 
D 2 74  ASN 74  74  74  ASN ASN V . n 
D 2 75  LEU 75  75  75  LEU LEU V . n 
D 2 76  CYS 76  76  76  CYS CYS V . n 
D 2 77  ASN 77  77  77  ASN ASN V . n 
D 2 78  ARG 78  78  78  ARG ARG V . n 
D 2 79  PRO 79  79  79  PRO PRO V . n 
D 2 80  ARG 80  80  80  ARG ARG V . n 
D 2 81  PRO 81  81  81  PRO PRO V . n 
D 2 82  GLY 82  82  ?   ?   ?   V . n 
D 2 83  ALA 83  83  ?   ?   ?   V . n 
D 2 84  ARG 84  84  ?   ?   ?   V . n 
D 2 85  GLY 85  85  ?   ?   ?   V . n 
D 2 86  ARG 86  86  ?   ?   ?   V . n 
D 2 87  ALA 87  87  ?   ?   ?   V . n 
D 2 88  PHE 88  88  ?   ?   ?   V . n 
D 2 89  PRO 89  89  ?   ?   ?   V . n 
D 2 90  GLN 90  90  ?   ?   ?   V . n 
D 2 91  GLY 91  91  ?   ?   ?   V . n 
D 2 92  ARG 92  92  ?   ?   ?   V . n 
D 2 93  TYR 93  93  93  TYR TYR V . n 
D 2 94  LEU 94  94  94  LEU LEU V . n 
D 2 95  GLU 95  95  95  GLU GLU V . n 
D 2 96  CYS 96  96  96  CYS CYS V . n 
D 2 97  ALA 97  97  97  ALA ALA V . n 
D 2 98  SER 98  98  98  SER SER V . n 
D 2 99  CYS 99  99  99  CYS CYS V . n 
D 2 100 THR 100 100 100 THR THR V . n 
D 2 101 SER 101 101 101 SER SER V . n 
D 2 102 LEU 102 102 102 LEU LEU V . n 
D 2 103 ASP 103 103 103 ASP ASP V . n 
D 2 104 GLN 104 104 104 GLN GLN V . n 
D 2 105 SER 105 105 105 SER SER V . n 
D 2 106 CYS 106 106 106 CYS CYS V . n 
D 2 107 GLU 107 107 107 GLU GLU V . n 
D 2 108 ARG 108 108 108 ARG ARG V . n 
D 2 109 GLY 109 109 109 GLY GLY V . n 
D 2 110 ARG 110 110 110 ARG ARG V . n 
D 2 111 GLU 111 111 111 GLU GLU V . n 
D 2 112 GLN 112 112 112 GLN GLN V . n 
D 2 113 SER 113 113 113 SER SER V . n 
D 2 114 LEU 114 114 114 LEU LEU V . n 
D 2 115 GLN 115 115 115 GLN GLN V . n 
D 2 116 CYS 116 116 116 CYS CYS V . n 
D 2 117 ARG 117 117 117 ARG ARG V . n 
D 2 118 TYR 118 118 118 TYR TYR V . n 
D 2 119 PRO 119 119 119 PRO PRO V . n 
D 2 120 THR 120 120 120 THR THR V . n 
D 2 121 GLU 121 121 121 GLU GLU V . n 
D 2 122 HIS 122 122 122 HIS HIS V . n 
D 2 123 CYS 123 123 123 CYS CYS V . n 
D 2 124 ILE 124 124 124 ILE ILE V . n 
D 2 125 GLU 125 125 125 GLU GLU V . n 
D 2 126 VAL 126 126 126 VAL VAL V . n 
D 2 127 VAL 127 127 127 VAL VAL V . n 
D 2 128 THR 128 128 128 THR THR V . n 
D 2 129 LEU 129 129 129 LEU LEU V . n 
D 2 130 GLN 130 130 130 GLN GLN V . n 
D 2 131 SER 131 131 131 SER SER V . n 
D 2 132 THR 132 132 132 THR THR V . n 
D 2 133 GLU 133 133 133 GLU GLU V . n 
D 2 134 ARG 134 134 134 ARG ARG V . n 
D 2 135 SER 135 135 135 SER SER V . n 
D 2 136 LEU 136 136 136 LEU LEU V . n 
D 2 137 LYS 137 137 137 LYS LYS V . n 
D 2 138 ASP 138 138 138 ASP ASP V . n 
D 2 139 GLU 139 139 139 GLU GLU V . n 
D 2 140 ASP 140 140 140 ASP ASP V . n 
D 2 141 TYR 141 141 141 TYR TYR V . n 
D 2 142 THR 142 142 142 THR THR V . n 
D 2 143 ARG 143 143 143 ARG ARG V . n 
D 2 144 GLY 144 144 144 GLY GLY V . n 
D 2 145 CYS 145 145 145 CYS CYS V . n 
D 2 146 GLY 146 146 146 GLY GLY V . n 
D 2 147 SER 147 147 147 SER SER V . n 
D 2 148 LEU 148 148 148 LEU LEU V . n 
D 2 149 PRO 149 149 149 PRO PRO V . n 
D 2 150 GLY 150 150 150 GLY GLY V . n 
D 2 151 CYS 151 151 151 CYS CYS V . n 
D 2 152 PRO 152 152 152 PRO PRO V . n 
D 2 153 GLY 153 153 153 GLY GLY V . n 
D 2 154 THR 154 154 154 THR THR V . n 
D 2 155 ALA 155 155 155 ALA ALA V . n 
D 2 156 GLY 156 156 156 GLY GLY V . n 
D 2 157 PHE 157 157 157 PHE PHE V . n 
D 2 158 HIS 158 158 158 HIS HIS V . n 
D 2 159 SER 159 159 159 SER SER V . n 
D 2 160 ASN 160 160 160 ASN ASN V . n 
D 2 161 GLN 161 161 161 GLN GLN V . n 
D 2 162 THR 162 162 162 THR THR V . n 
D 2 163 PHE 163 163 163 PHE PHE V . n 
D 2 164 HIS 164 164 164 HIS HIS V . n 
D 2 165 PHE 165 165 165 PHE PHE V . n 
D 2 166 LEU 166 166 166 LEU LEU V . n 
D 2 167 LYS 167 167 167 LYS LYS V . n 
D 2 168 CYS 168 168 168 CYS CYS V . n 
D 2 169 CYS 169 169 169 CYS CYS V . n 
D 2 170 ASN 170 170 170 ASN ASN V . n 
D 2 171 TYR 171 171 171 TYR TYR V . n 
D 2 172 THR 172 172 172 THR THR V . n 
D 2 173 HIS 173 173 173 HIS HIS V . n 
D 2 174 CYS 174 174 174 CYS CYS V . n 
D 2 175 ASN 175 175 175 ASN ASN V . n 
D 2 176 GLY 176 176 176 GLY GLY V . n 
D 2 177 GLY 177 177 177 GLY GLY V . n 
D 2 178 PRO 178 178 178 PRO PRO V . n 
D 2 179 VAL 179 179 179 VAL VAL V . n 
D 2 180 LEU 180 180 180 LEU LEU V . n 
D 2 181 ASP 181 181 181 ASP ASP V . n 
D 2 182 LEU 182 182 182 LEU LEU V . n 
D 2 183 GLN 183 183 183 GLN GLN V . n 
D 2 184 SER 184 184 184 SER SER V . n 
D 2 185 PHE 185 185 185 PHE PHE V . n 
D 2 186 PRO 186 186 186 PRO PRO V . n 
D 2 187 PRO 187 187 187 PRO PRO V . n 
D 2 188 ASN 188 188 188 ASN ASN V . n 
D 2 189 GLY 189 189 189 GLY GLY V . n 
D 2 190 PHE 190 190 190 PHE PHE V . n 
D 2 191 GLN 191 191 191 GLN GLN V . n 
D 2 192 CYS 192 192 192 CYS CYS V . n 
D 2 193 TYR 193 193 193 TYR TYR V . n 
D 2 194 SER 194 194 194 SER SER V . n 
D 2 195 CYS 195 195 195 CYS CYS V . n 
D 2 196 GLU 196 196 196 GLU GLU V . n 
D 2 197 GLY 197 197 197 GLY GLY V . n 
D 2 198 ASN 198 198 198 ASN ASN V . n 
D 2 199 ASN 199 199 199 ASN ASN V . n 
D 2 200 THR 200 200 200 THR THR V . n 
D 2 201 LEU 201 201 201 LEU LEU V . n 
D 2 202 GLY 202 202 202 GLY GLY V . n 
D 2 203 CYS 203 203 203 CYS CYS V . n 
D 2 204 SER 204 204 204 SER SER V . n 
D 2 205 SER 205 205 205 SER SER V . n 
D 2 206 GLU 206 206 206 GLU GLU V . n 
D 2 207 GLU 207 207 207 GLU GLU V . n 
D 2 208 ALA 208 208 208 ALA ALA V . n 
D 2 209 SER 209 209 209 SER SER V . n 
D 2 210 LEU 210 210 210 LEU LEU V . n 
D 2 211 ILE 211 211 211 ILE ILE V . n 
D 2 212 ASN 212 212 212 ASN ASN V . n 
D 2 213 CYS 213 213 213 CYS CYS V . n 
D 2 214 ARG 214 214 214 ARG ARG V . n 
D 2 215 GLY 215 215 215 GLY GLY V . n 
D 2 216 PRO 216 216 216 PRO PRO V . n 
D 2 217 MET 217 217 217 MET MET V . n 
D 2 218 ASN 218 218 218 ASN ASN V . n 
D 2 219 GLN 219 219 219 GLN GLN V . n 
D 2 220 CYS 220 220 220 CYS CYS V . n 
D 2 221 LEU 221 221 221 LEU LEU V . n 
D 2 222 VAL 222 222 222 VAL VAL V . n 
D 2 223 ALA 223 223 223 ALA ALA V . n 
D 2 224 THR 224 224 224 THR THR V . n 
D 2 225 GLY 225 225 225 GLY GLY V . n 
D 2 226 LEU 226 226 226 LEU LEU V . n 
D 2 227 ASP 227 227 227 ASP ASP V . n 
D 2 228 VAL 228 228 228 VAL VAL V . n 
D 2 229 LEU 229 229 ?   ?   ?   V . n 
D 2 230 GLY 230 230 ?   ?   ?   V . n 
D 2 231 ASN 231 231 ?   ?   ?   V . n 
D 2 232 ARG 232 232 232 ARG ARG V . n 
D 2 233 SER 233 233 233 SER SER V . n 
D 2 234 TYR 234 234 234 TYR TYR V . n 
D 2 235 THR 235 235 235 THR THR V . n 
D 2 236 VAL 236 236 236 VAL VAL V . n 
D 2 237 ARG 237 237 237 ARG ARG V . n 
D 2 238 GLY 238 238 238 GLY GLY V . n 
D 2 239 CYS 239 239 239 CYS CYS V . n 
D 2 240 ALA 240 240 240 ALA ALA V . n 
D 2 241 THR 241 241 241 THR THR V . n 
D 2 242 ALA 242 242 242 ALA ALA V . n 
D 2 243 SER 243 243 243 SER SER V . n 
D 2 244 TRP 244 244 244 TRP TRP V . n 
D 2 245 CYS 245 245 245 CYS CYS V . n 
D 2 246 GLN 246 246 246 GLN GLN V . n 
D 2 247 GLY 247 247 247 GLY GLY V . n 
D 2 248 SER 248 248 248 SER SER V . n 
D 2 249 HIS 249 249 249 HIS HIS V . n 
D 2 250 VAL 250 250 250 VAL VAL V . n 
D 2 251 ALA 251 251 251 ALA ALA V . n 
D 2 252 ASP 252 252 252 ASP ASP V . n 
D 2 253 SER 253 253 253 SER SER V . n 
D 2 254 PHE 254 254 254 PHE PHE V . n 
D 2 255 PRO 255 255 255 PRO PRO V . n 
D 2 256 THR 256 256 256 THR THR V . n 
D 2 257 HIS 257 257 257 HIS HIS V . n 
D 2 258 LEU 258 258 258 LEU LEU V . n 
D 2 259 ASN 259 259 259 ASN ASN V . n 
D 2 260 VAL 260 260 260 VAL VAL V . n 
D 2 261 SER 261 261 261 SER SER V . n 
D 2 262 VAL 262 262 262 VAL VAL V . n 
D 2 263 SER 263 263 263 SER SER V . n 
D 2 264 CYS 264 264 264 CYS CYS V . n 
D 2 265 CYS 265 265 265 CYS CYS V . n 
D 2 266 HIS 266 266 266 HIS HIS V . n 
D 2 267 GLY 267 267 267 GLY GLY V . n 
D 2 268 SER 268 268 268 SER SER V . n 
D 2 269 GLY 269 269 269 GLY GLY V . n 
D 2 270 CYS 270 270 270 CYS CYS V . n 
D 2 271 ASN 271 271 271 ASN ASN V . n 
D 2 272 SER 272 272 272 SER SER V . n 
D 2 273 PRO 273 273 273 PRO PRO V . n 
D 2 274 THR 274 274 274 THR THR V . n 
D 2 275 GLY 275 275 ?   ?   ?   V . n 
D 2 276 GLY 276 276 ?   ?   ?   V . n 
D 2 277 ALA 277 277 ?   ?   ?   V . n 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 B ASN 52  U ASN 52  ? ASN 'GLYCOSYLATION SITE' 
2 B ASN 170 U ASN 170 ? ASN 'GLYCOSYLATION SITE' 
3 D ASN 52  V ASN 52  ? ASN 'GLYCOSYLATION SITE' 
4 D ASN 160 V ASN 160 ? ASN 'GLYCOSYLATION SITE' 
5 B ASN 259 U ASN 259 ? ASN 'GLYCOSYLATION SITE' 
6 D ASN 259 V ASN 259 ? ASN 'GLYCOSYLATION SITE' 
7 D ASN 170 V ASN 170 ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I 
2 1 C,D,J,K,L,M,N 
# 
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)' 3750  ? 
1 MORE         1     ? 
1 'SSA (A^2)'  20340 ? 
2 'ABSA (A^2)' 3600  ? 
2 MORE         -1    ? 
2 'SSA (A^2)'  19940 ? 
# 
_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 2010-02-02 
2 'Structure model' 1 1 2011-07-13 
# 
_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' Advisory                    
2 2 'Structure model' 'Refinement description'    
3 2 'Structure model' 'Version format compliance' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 21.3220 -3.0670 14.9170 0.1706 0.1635 0.0618 -0.0146 0.0515  -0.0824 1.4104 3.9989  3.6870  0.1777 
-0.3156 -0.5502 -0.0879 0.0181  0.0698  0.1515  -0.1565 -0.2343 -0.3706 0.2697  0.1155  
'X-RAY DIFFRACTION' 2 ? refined 6.5640  1.9870  42.2730 0.1585 0.0829 0.1411 0.0120  0.0983  -0.0686 5.4312 5.4130  7.0463  
-0.7627 1.6768  0.1041  0.0236  0.1342  -0.1578 -0.6408 0.6719  0.2690  0.6028  -0.6398 -0.1852 
'X-RAY DIFFRACTION' 3 ? refined 37.1640 30.2580 32.4060 0.1815 0.1117 0.1254 0.1020  -0.0217 0.0032  3.0315 3.3545  2.3165  0.7674 
0.7112  -0.8733 0.2566  -0.1850 -0.0716 -0.0129 -0.3642 -0.3909 0.2050  0.1574  0.2630  
'X-RAY DIFFRACTION' 4 ? refined 9.9440  37.3650 17.9420 0.2175 0.1676 0.3508 0.0648  -0.1062 -0.0342 3.2279 5.8826  10.1037 
-0.8602 0.1298  -3.9270 -0.1535 0.2941  -0.1406 -0.0056 0.4157  1.0512  -0.0946 -0.7888 -1.1924 
'X-RAY DIFFRACTION' 5 ? refined 41.2280 5.0530  3.9560  0.7211 0.7776 0.5425 -0.2960 0.3203  0.0172  7.8211 11.0619 5.0973  
-1.1741 -2.2019 2.6207  -0.5267 0.2665  0.2602  0.0851  0.3743  -1.2302 0.2199  -0.2805 1.3371  
'X-RAY DIFFRACTION' 6 ? refined 48.4090 37.9830 52.2530 0.6272 0.2154 0.4145 -0.1070 -0.2094 0.0230  5.5129 10.4136 8.4932  
-1.8222 2.0412  -0.1608 -0.2303 -0.3199 0.5501  -0.3984 0.0233  0.1398  0.2414  -1.2601 0.4078  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 11  A 47  ? . . . . ? 
'X-RAY DIFFRACTION' 2 1 U 1   U 184 ? . . . . ? 
'X-RAY DIFFRACTION' 3 2 A 48  A 131 ? . . . . ? 
'X-RAY DIFFRACTION' 4 3 B 11  B 47  ? . . . . ? 
'X-RAY DIFFRACTION' 5 3 V 1   V 184 ? . . . . ? 
'X-RAY DIFFRACTION' 6 4 B 48  B 131 ? . . . . ? 
'X-RAY DIFFRACTION' 7 5 U 185 U 274 ? . . . . ? 
'X-RAY DIFFRACTION' 8 6 V 185 V 274 ? . . . . ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .        ? 1 
AMoRE    phasing           .        ? 2 
REFMAC   refinement        5.5.0102 ? 3 
HKL-2000 'data reduction'  .        ? 4 
HKL-2000 'data scaling'    .        ? 5 
# 
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 O4  U NAG 1052 ? ? C1  U NAG 1053 ? ? 1.58 
2  1 O4  V NAG 1052 ? ? C1  V NAG 1053 ? ? 1.61 
3  1 ND2 U ASN 160  ? ? C1  U NAG 1160 ? ? 1.63 
4  1 OD1 V ASN 259  ? ? N2  V NAG 1259 ? ? 1.84 
5  1 O4  V NAG 1052 ? ? O5  V NAG 1053 ? ? 1.88 
6  1 OD1 V ASN 259  ? ? C7  V NAG 1259 ? ? 1.89 
7  1 OD1 V ASN 259  ? ? C8  V NAG 1259 ? ? 1.93 
8  1 O4  U NAG 1052 ? ? C2  U NAG 1053 ? ? 1.93 
9  1 ND2 V ASN 160  ? ? C2  V NAG 1160 ? ? 1.94 
10 1 OD1 V ASN 259  ? ? C2  V NAG 1259 ? ? 1.96 
11 1 O4  U NAG 1052 ? ? O5  U NAG 1053 ? ? 1.97 
12 1 ND2 V ASN 259  ? ? O5  V NAG 1259 ? ? 2.02 
13 1 ND2 V ASN 259  ? ? C2  V NAG 1259 ? ? 2.05 
14 1 O   V SER 205  ? ? OE1 V GLU 207  ? ? 2.11 
15 1 ND2 U ASN 170  ? ? O5  U NAG 1170 ? ? 2.11 
16 1 N   A SER 22   ? ? O   U LYS 137  ? ? 2.15 
17 1 ND2 V ASN 170  ? ? O5  V NAG 1170 ? ? 2.17 
18 1 O   U HIS 249  ? ? OD2 U ASP 252  ? ? 2.18 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A CYS 51  ? ? CB A CYS 51  ? ? SG A CYS 51  ? ? 121.72 114.20 7.52   1.10 N 
2 1 CA A CYS 103 ? ? CB A CYS 103 ? ? SG A CYS 103 ? ? 101.50 114.00 -12.50 1.80 N 
3 1 CA U CYS 24  ? ? CB U CYS 24  ? ? SG U CYS 24  ? ? 102.29 114.00 -11.71 1.80 N 
4 1 C  B ARG 70  ? ? N  B PRO 71  ? ? CA B PRO 71  ? ? 128.61 119.30 9.31   1.50 Y 
5 1 C  V ARG 78  ? ? N  V PRO 79  ? ? CA V PRO 79  ? ? 128.78 119.30 9.48   1.50 Y 
6 1 C  V ARG 78  ? ? N  V PRO 79  ? ? CD V PRO 79  ? ? 108.63 128.40 -19.77 2.10 Y 
7 1 O  V HIS 158 ? ? C  V HIS 158 ? ? N  V SER 159 ? ? 133.00 122.70 10.30  1.60 Y 
8 1 CA V CYS 168 ? ? CB V CYS 168 ? ? SG V CYS 168 ? ? 123.96 114.20 9.76   1.10 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1   1 SER A 10  ? ? -131.71 -68.68  
2   1 ASN A 11  ? ? 2.13    60.82   
3   1 CYS A 12  ? ? -145.62 -2.67   
4   1 ASN A 16  ? ? 55.66   -132.70 
5   1 SER A 22  ? ? -105.99 -167.45 
6   1 PHE A 26  ? ? -108.15 55.91   
7   1 ARG A 28  ? ? 44.64   18.80   
8   1 ASP A 57  ? ? -37.40  -29.24  
9   1 THR A 67  ? ? -65.78  10.08   
10  1 ARG A 70  ? ? -34.08  144.25  
11  1 ALA A 77  ? ? -21.32  136.01  
12  1 ARG A 89  ? ? -31.65  136.65  
13  1 LYS A 99  ? ? -57.83  9.74    
14  1 HIS A 100 ? ? -103.44 -163.36 
15  1 ASN A 105 ? ? -155.04 73.92   
16  1 ASP A 107 ? ? -71.73  -166.71 
17  1 GLN A 109 ? ? 159.57  128.12  
18  1 LYS A 110 ? ? -25.18  -68.41  
19  1 VAL A 129 ? ? -1.36   107.99  
20  1 CYS U 6   ? ? 172.61  116.52  
21  1 GLU U 7   ? ? -62.50  -177.78 
22  1 SER U 8   ? ? -41.28  -79.57  
23  1 LEU U 19  ? ? -47.01  109.33  
24  1 ASP U 22  ? ? -142.40 24.42   
25  1 THR U 26  ? ? -150.89 74.65   
26  1 GLN U 33  ? ? -172.46 142.46  
27  1 ASP U 34  ? ? 33.61   60.38   
28  1 ASP U 35  ? ? 32.00   51.18   
29  1 ALA U 46  ? ? -92.69  -118.45 
30  1 ASN U 52  ? ? -46.37  104.83  
31  1 ARG U 78  ? ? -147.22 -117.01 
32  1 PRO U 79  ? ? -94.23  -61.42  
33  1 CYS U 99  ? ? 152.61  161.21  
34  1 ARG U 110 ? ? -172.23 147.05  
35  1 GLU U 111 ? ? -173.65 100.34  
36  1 THR U 120 ? ? 96.19   -20.55  
37  1 THR U 132 ? ? 35.85   -120.93 
38  1 GLU U 133 ? ? -96.49  30.93   
39  1 ARG U 134 ? ? 10.91   119.65  
40  1 LYS U 137 ? ? -98.07  48.53   
41  1 GLU U 139 ? ? -47.84  152.84  
42  1 CYS U 151 ? ? -76.90  -92.83  
43  1 PHE U 165 ? ? -171.60 135.96  
44  1 ASN U 170 ? ? -95.13  40.77   
45  1 HIS U 173 ? ? 45.60   28.52   
46  1 CYS U 174 ? ? -57.92  -3.84   
47  1 PRO U 187 ? ? -47.76  93.72   
48  1 GLU U 196 ? ? -158.28 84.76   
49  1 ASN U 198 ? ? -146.83 -76.79  
50  1 THR U 200 ? ? 66.81   -43.55  
51  1 SER U 204 ? ? -162.08 -151.55 
52  1 ASN U 218 ? ? -148.48 -1.72   
53  1 THR U 241 ? ? -84.24  -157.65 
54  1 HIS U 249 ? ? -47.06  -97.03  
55  1 VAL U 250 ? ? -10.33  -57.96  
56  1 PRO U 255 ? ? -16.07  -91.30  
57  1 HIS U 257 ? ? -178.16 -165.56 
58  1 LEU U 258 ? ? -59.74  -133.98 
59  1 VAL U 260 ? ? 33.21   58.55   
60  1 SER U 261 ? ? -37.92  133.04  
61  1 PRO U 273 ? ? -35.74  66.75   
62  1 SER B 10  ? ? -134.49 -74.85  
63  1 ASN B 11  ? ? 100.70  -75.72  
64  1 CYS B 14  ? ? 4.74    118.95  
65  1 ASN B 16  ? ? 53.63   -112.82 
66  1 LYS B 24  ? ? -6.20   -65.50  
67  1 ARG B 28  ? ? 32.15   63.35   
68  1 CYS B 32  ? ? -156.26 72.97   
69  1 SER B 33  ? ? -55.88  107.11  
70  1 GLU B 41  ? ? -47.57  -19.87  
71  1 THR B 50  ? ? -132.07 -53.69  
72  1 HIS B 53  ? ? -48.89  102.72  
73  1 ARG B 60  ? ? -143.64 26.37   
74  1 TRP B 75  ? ? -57.21  4.05    
75  1 HIS B 88  ? ? -58.34  5.39    
76  1 ALA B 92  ? ? 35.25   -96.90  
77  1 ILE B 93  ? ? -16.94  -61.43  
78  1 LEU B 95  ? ? -72.13  -115.63 
79  1 ASN B 105 ? ? -108.33 65.94   
80  1 MET B 128 ? ? -45.13  -87.96  
81  1 VAL B 129 ? ? -7.72   116.71  
82  1 ASN V 9   ? ? 29.98   33.76   
83  1 ASP V 22  ? ? 165.86  37.00   
84  1 GLN V 33  ? ? -161.43 77.69   
85  1 ASP V 34  ? ? 58.44   96.93   
86  1 GLU V 37  ? ? -50.85  104.64  
87  1 ALA V 46  ? ? -103.46 -62.93  
88  1 HIS V 47  ? ? 84.99   121.96  
89  1 GLU V 49  ? ? -96.00  42.02   
90  1 SER V 56  ? ? -173.27 124.94  
91  1 LEU V 75  ? ? 35.55   38.08   
92  1 ASN V 77  ? ? -117.53 63.40   
93  1 ARG V 78  ? ? -106.20 -118.91 
94  1 PRO V 79  ? ? -50.85  -110.99 
95  1 ARG V 80  ? ? -39.93  132.85  
96  1 LEU V 94  ? ? 41.84   121.82  
97  1 GLN V 104 ? ? 74.85   39.41   
98  1 CYS V 106 ? ? -77.93  -75.85  
99  1 GLU V 107 ? ? -1.47   -65.05  
100 1 GLU V 111 ? ? -36.05  -159.75 
101 1 SER V 113 ? ? -0.96   122.56  
102 1 ARG V 117 ? ? -63.72  -77.94  
103 1 PRO V 119 ? ? -53.22  98.15   
104 1 THR V 120 ? ? 140.95  16.00   
105 1 GLN V 130 ? ? -128.79 -141.45 
106 1 THR V 132 ? ? 15.98   -73.82  
107 1 ARG V 134 ? ? 62.53   79.55   
108 1 ASP V 138 ? ? -77.44  -169.14 
109 1 PRO V 152 ? ? -60.58  96.37   
110 1 ALA V 155 ? ? -172.10 143.94  
111 1 THR V 172 ? ? -20.96  122.57  
112 1 ASN V 175 ? ? -166.85 79.37   
113 1 PRO V 178 ? ? -24.17  87.47   
114 1 LEU V 180 ? ? -61.52  83.76   
115 1 GLN V 183 ? ? -31.78  -33.40  
116 1 CYS V 195 ? ? -179.68 142.50  
117 1 GLU V 196 ? ? -171.80 93.61   
118 1 ASN V 198 ? ? -152.81 -109.21 
119 1 ASN V 199 ? ? -179.34 -118.84 
120 1 SER V 204 ? ? -96.01  -134.06 
121 1 GLU V 206 ? ? -75.75  45.16   
122 1 SER V 209 ? ? -14.86  152.14  
123 1 ASP V 227 ? ? -107.84 -82.92  
124 1 HIS V 249 ? ? 17.82   -89.55  
125 1 ASP V 252 ? ? -80.45  43.22   
126 1 ASN V 259 ? ? 6.21    44.55   
127 1 ASN V 271 ? ? -77.10  41.92   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ARG 
_pdbx_validate_peptide_omega.auth_asym_id_1   V 
_pdbx_validate_peptide_omega.auth_seq_id_1    78 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_2   V 
_pdbx_validate_peptide_omega.auth_seq_id_2    79 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -137.59 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 N 1 U NAG 1053 ? O1 ? F NAG 1 O1 
2 1 N 1 U NAG 1160 ? O1 ? G NAG 1 O1 
3 1 N 1 V NAG 1053 ? O1 ? K NAG 1 O1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 1   ? A GLY 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A VAL 3   ? A VAL 3   
4  1 Y 1 A LEU 4   ? A LEU 4   
5  1 Y 1 A GLY 5   ? A GLY 5   
6  1 Y 1 A ALA 6   ? A ALA 6   
7  1 Y 1 A PRO 7   ? A PRO 7   
8  1 Y 1 A ASP 8   ? A ASP 8   
9  1 Y 1 A SER 133 ? A SER 133 
10 1 Y 1 A LEU 134 ? A LEU 134 
11 1 Y 1 U GLY 82  ? B GLY 82  
12 1 Y 1 U ALA 83  ? B ALA 83  
13 1 Y 1 U ARG 84  ? B ARG 84  
14 1 Y 1 U GLY 85  ? B GLY 85  
15 1 Y 1 U ARG 86  ? B ARG 86  
16 1 Y 1 U ALA 87  ? B ALA 87  
17 1 Y 1 U PHE 88  ? B PHE 88  
18 1 Y 1 U PRO 89  ? B PRO 89  
19 1 Y 1 U GLN 90  ? B GLN 90  
20 1 Y 1 U GLY 91  ? B GLY 91  
21 1 Y 1 U ARG 92  ? B ARG 92  
22 1 Y 1 U ASP 227 ? B ASP 227 
23 1 Y 1 U VAL 228 ? B VAL 228 
24 1 Y 1 U LEU 229 ? B LEU 229 
25 1 Y 1 U GLY 230 ? B GLY 230 
26 1 Y 1 U ASN 231 ? B ASN 231 
27 1 Y 1 U GLY 275 ? B GLY 275 
28 1 Y 1 U GLY 276 ? B GLY 276 
29 1 Y 1 U ALA 277 ? B ALA 277 
30 1 Y 1 B GLY 1   ? C GLY 1   
31 1 Y 1 B SER 2   ? C SER 2   
32 1 Y 1 B VAL 3   ? C VAL 3   
33 1 Y 1 B LEU 4   ? C LEU 4   
34 1 Y 1 B GLY 5   ? C GLY 5   
35 1 Y 1 B ALA 6   ? C ALA 6   
36 1 Y 1 B PRO 7   ? C PRO 7   
37 1 Y 1 B SER 133 ? C SER 133 
38 1 Y 1 B LEU 134 ? C LEU 134 
39 1 Y 1 V GLY 82  ? D GLY 82  
40 1 Y 1 V ALA 83  ? D ALA 83  
41 1 Y 1 V ARG 84  ? D ARG 84  
42 1 Y 1 V GLY 85  ? D GLY 85  
43 1 Y 1 V ARG 86  ? D ARG 86  
44 1 Y 1 V ALA 87  ? D ALA 87  
45 1 Y 1 V PHE 88  ? D PHE 88  
46 1 Y 1 V PRO 89  ? D PRO 89  
47 1 Y 1 V GLN 90  ? D GLN 90  
48 1 Y 1 V GLY 91  ? D GLY 91  
49 1 Y 1 V ARG 92  ? D ARG 92  
50 1 Y 1 V LEU 229 ? D LEU 229 
51 1 Y 1 V GLY 230 ? D GLY 230 
52 1 Y 1 V ASN 231 ? D ASN 231 
53 1 Y 1 V GLY 275 ? D GLY 275 
54 1 Y 1 V GLY 276 ? D GLY 276 
55 1 Y 1 V ALA 277 ? D ALA 277 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        N-ACETYL-D-GLUCOSAMINE 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
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 
E 3 NAG 1 1052 1052 NAG NAG U . 
F 3 NAG 1 1053 1053 NAG NAG U . 
G 3 NAG 1 1160 1160 NAG NAG U . 
H 3 NAG 1 1170 1170 NAG NAG U . 
I 3 NAG 1 1259 1259 NAG NAG U . 
J 3 NAG 1 1052 1052 NAG NAG V . 
K 3 NAG 1 1053 1053 NAG NAG V . 
L 3 NAG 1 1170 1170 NAG NAG V . 
M 3 NAG 1 1160 1160 NAG NAG V . 
N 3 NAG 1 1259 1259 NAG NAG V . 
# 
