data_9MUV
# 
_entry.id   9MUV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9MUV         pdb_00009muv 10.2210/pdb9muv/pdb 
WWPDB D_1000291604 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-18 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9MUV 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gary_yellen@hms.harvard.edu 
_pdbx_contact_author.name_first         Gary 
_pdbx_contact_author.name_last          Yellen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4228-7866 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rosen, P.'  1 0000-0001-7414-454X 
'Yellen, G.' 2 0000-0003-4228-7866 
'Lim, D.C.'  3 0000-0002-8861-4837 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                e2503978122 
_citation.page_last                 e2503978122 
_citation.title                     
'Mechanism and application of thiol-disulfide redox biosensors with a fluorescence-lifetime readout.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2503978122 
_citation.pdbx_database_id_PubMed   40327692 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Rosen, P.C.'             1 0000-0001-7414-454X 
primary 'Glaser, A.'              2 ?                   
primary 'Martinez-Francois, J.R.' 3 ?                   
primary 'Lim, D.C.'               4 ?                   
primary 'Brooks, D.J.'            5 0009-0004-7527-242X 
primary 'Fu, P.'                  6 ?                   
primary 'Kim, E.'                 7 0009-0003-8025-6152 
primary 'Kern, D.'                8 0000-0002-7631-8328 
primary 'Yellen, G.'              9 0000-0003-4228-7866 
# 
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 'Fluorescent thiol-disulfide redox biosensor' 28457.117 2   ? 
'Engineered, based on GFP, with numerous mutations relative to GFP' ? ? 
2 non-polymer syn 'ACETIC ACID'                                 60.052    2   ? ? ? ? 
3 non-polymer syn 'TRIETHYLENE GLYCOL'                          150.173   1   ? ? ? ? 
4 non-polymer syn GLYCEROL                                      92.094    4   ? ? ? ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                       106.120   1   ? ? ? ? 
6 water       nat water                                         18.015    253 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MKHHHHHHHGGASMVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFISTTGKLPVPWPTLVTTL
(SWG)VQCFARYPDHMKRHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLE
YNGWCGDNVYITADKQKNGIKANFKIRHNIEDGGVQLADHYQQNTPIGDGPVLLPDNHYLSTCSKLSKDPNEKRDHMVFL
EFVTAAGITLGMDELYK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKHHHHHHHGGASMVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFISTTGKLPVPWPTLVTTL
SWGVQCFARYPDHMKRHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYN
GWCGDNVYITADKQKNGIKANFKIRHNIEDGGVQLADHYQQNTPIGDGPVLLPDNHYLSTCSKLSKDPNEKRDHMVFLEF
VTAAGITLGMDELYK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ACETIC ACID'           ACY 
3 'TRIETHYLENE GLYCOL'    PGE 
4 GLYCEROL                GOL 
5 'DI(HYDROXYETHYL)ETHER' PEG 
6 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  GLY n 
1 11  GLY n 
1 12  ALA n 
1 13  SER n 
1 14  MET n 
1 15  VAL n 
1 16  SER n 
1 17  LYS n 
1 18  GLY n 
1 19  GLU n 
1 20  GLU n 
1 21  LEU n 
1 22  PHE n 
1 23  THR n 
1 24  GLY n 
1 25  VAL n 
1 26  VAL n 
1 27  PRO n 
1 28  ILE n 
1 29  LEU n 
1 30  VAL n 
1 31  GLU n 
1 32  LEU n 
1 33  ASP n 
1 34  GLY n 
1 35  ASP n 
1 36  VAL n 
1 37  ASN n 
1 38  GLY n 
1 39  HIS n 
1 40  LYS n 
1 41  PHE n 
1 42  SER n 
1 43  VAL n 
1 44  SER n 
1 45  GLY n 
1 46  GLU n 
1 47  GLY n 
1 48  GLU n 
1 49  GLY n 
1 50  ASP n 
1 51  ALA n 
1 52  THR n 
1 53  TYR n 
1 54  GLY n 
1 55  LYS n 
1 56  LEU n 
1 57  THR n 
1 58  LEU n 
1 59  LYS n 
1 60  PHE n 
1 61  ILE n 
1 62  SER n 
1 63  THR n 
1 64  THR n 
1 65  GLY n 
1 66  LYS n 
1 67  LEU n 
1 68  PRO n 
1 69  VAL n 
1 70  PRO n 
1 71  TRP n 
1 72  PRO n 
1 73  THR n 
1 74  LEU n 
1 75  VAL n 
1 76  THR n 
1 77  THR n 
1 78  LEU n 
1 79  SWG n 
1 80  VAL n 
1 81  GLN n 
1 82  CYS n 
1 83  PHE n 
1 84  ALA n 
1 85  ARG n 
1 86  TYR n 
1 87  PRO n 
1 88  ASP n 
1 89  HIS n 
1 90  MET n 
1 91  LYS n 
1 92  ARG n 
1 93  HIS n 
1 94  ASP n 
1 95  PHE n 
1 96  PHE n 
1 97  LYS n 
1 98  SER n 
1 99  ALA n 
1 100 MET n 
1 101 PRO n 
1 102 GLU n 
1 103 GLY n 
1 104 TYR n 
1 105 VAL n 
1 106 GLN n 
1 107 GLU n 
1 108 ARG n 
1 109 THR n 
1 110 ILE n 
1 111 PHE n 
1 112 PHE n 
1 113 LYS n 
1 114 ASP n 
1 115 ASP n 
1 116 GLY n 
1 117 ASN n 
1 118 TYR n 
1 119 LYS n 
1 120 THR n 
1 121 ARG n 
1 122 ALA n 
1 123 GLU n 
1 124 VAL n 
1 125 LYS n 
1 126 PHE n 
1 127 GLU n 
1 128 GLY n 
1 129 ASP n 
1 130 THR n 
1 131 LEU n 
1 132 VAL n 
1 133 ASN n 
1 134 ARG n 
1 135 ILE n 
1 136 GLU n 
1 137 LEU n 
1 138 LYS n 
1 139 GLY n 
1 140 ILE n 
1 141 ASP n 
1 142 PHE n 
1 143 LYS n 
1 144 GLU n 
1 145 ASP n 
1 146 GLY n 
1 147 ASN n 
1 148 ILE n 
1 149 LEU n 
1 150 GLY n 
1 151 HIS n 
1 152 LYS n 
1 153 LEU n 
1 154 GLU n 
1 155 TYR n 
1 156 ASN n 
1 157 GLY n 
1 158 TRP n 
1 159 CYS n 
1 160 GLY n 
1 161 ASP n 
1 162 ASN n 
1 163 VAL n 
1 164 TYR n 
1 165 ILE n 
1 166 THR n 
1 167 ALA n 
1 168 ASP n 
1 169 LYS n 
1 170 GLN n 
1 171 LYS n 
1 172 ASN n 
1 173 GLY n 
1 174 ILE n 
1 175 LYS n 
1 176 ALA n 
1 177 ASN n 
1 178 PHE n 
1 179 LYS n 
1 180 ILE n 
1 181 ARG n 
1 182 HIS n 
1 183 ASN n 
1 184 ILE n 
1 185 GLU n 
1 186 ASP n 
1 187 GLY n 
1 188 GLY n 
1 189 VAL n 
1 190 GLN n 
1 191 LEU n 
1 192 ALA n 
1 193 ASP n 
1 194 HIS n 
1 195 TYR n 
1 196 GLN n 
1 197 GLN n 
1 198 ASN n 
1 199 THR n 
1 200 PRO n 
1 201 ILE n 
1 202 GLY n 
1 203 ASP n 
1 204 GLY n 
1 205 PRO n 
1 206 VAL n 
1 207 LEU n 
1 208 LEU n 
1 209 PRO n 
1 210 ASP n 
1 211 ASN n 
1 212 HIS n 
1 213 TYR n 
1 214 LEU n 
1 215 SER n 
1 216 THR n 
1 217 CYS n 
1 218 SER n 
1 219 LYS n 
1 220 LEU n 
1 221 SER n 
1 222 LYS n 
1 223 ASP n 
1 224 PRO n 
1 225 ASN n 
1 226 GLU n 
1 227 LYS n 
1 228 ARG n 
1 229 ASP n 
1 230 HIS n 
1 231 MET n 
1 232 VAL n 
1 233 PHE n 
1 234 LEU n 
1 235 GLU n 
1 236 PHE n 
1 237 VAL n 
1 238 THR n 
1 239 ALA n 
1 240 ALA n 
1 241 GLY n 
1 242 ILE n 
1 243 THR n 
1 244 LEU n 
1 245 GLY n 
1 246 MET n 
1 247 ASP n 
1 248 GLU n 
1 249 LEU n 
1 250 TYR n 
1 251 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   251 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GFP 
_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      'Aequorea victoria' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     6100 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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                   ? 
# 
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 
ACY non-polymer         . 'ACETIC ACID' ?                               'C2 H4 O2'       60.052  
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  
GOL non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'  149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                               'C4 H10 O3'      106.120 
PGE non-polymer         . 'TRIETHYLENE GLYCOL' ?                               'C6 H14 O4'      150.173 
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 
SWG 'L-peptide linking' n 
'2-[(4Z)-2-[(1R)-1-amino-2-hydroxy-ethyl]-4-(1H-indol-3-ylmethylidene)-5-oxo-imidazol-1-yl]ethanoic acid' ? 'C16 H16 N4 O4'  
328.323 
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 
# 
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   MET 1   -13 ?   ?   ?   A . n 
A 1 2   LYS 2   -12 ?   ?   ?   A . n 
A 1 3   HIS 3   -11 ?   ?   ?   A . n 
A 1 4   HIS 4   -10 ?   ?   ?   A . n 
A 1 5   HIS 5   -9  ?   ?   ?   A . n 
A 1 6   HIS 6   -8  ?   ?   ?   A . n 
A 1 7   HIS 7   -7  ?   ?   ?   A . n 
A 1 8   HIS 8   -6  ?   ?   ?   A . n 
A 1 9   HIS 9   -5  ?   ?   ?   A . n 
A 1 10  GLY 10  -4  ?   ?   ?   A . n 
A 1 11  GLY 11  -3  ?   ?   ?   A . n 
A 1 12  ALA 12  -2  ?   ?   ?   A . n 
A 1 13  SER 13  -1  ?   ?   ?   A . n 
A 1 14  MET 14  0   ?   ?   ?   A . n 
A 1 15  VAL 15  1   ?   ?   ?   A . n 
A 1 16  SER 16  2   ?   ?   ?   A . n 
A 1 17  LYS 17  3   3   LYS LYS A . n 
A 1 18  GLY 18  4   4   GLY GLY A . n 
A 1 19  GLU 19  5   5   GLU GLU A . n 
A 1 20  GLU 20  6   6   GLU GLU A . n 
A 1 21  LEU 21  7   7   LEU LEU A . n 
A 1 22  PHE 22  8   8   PHE PHE A . n 
A 1 23  THR 23  9   9   THR THR A . n 
A 1 24  GLY 24  10  10  GLY GLY A . n 
A 1 25  VAL 25  11  11  VAL VAL A . n 
A 1 26  VAL 26  12  12  VAL VAL A . n 
A 1 27  PRO 27  13  13  PRO PRO A . n 
A 1 28  ILE 28  14  14  ILE ILE A . n 
A 1 29  LEU 29  15  15  LEU LEU A . n 
A 1 30  VAL 30  16  16  VAL VAL A . n 
A 1 31  GLU 31  17  17  GLU GLU A . n 
A 1 32  LEU 32  18  18  LEU LEU A . n 
A 1 33  ASP 33  19  19  ASP ASP A . n 
A 1 34  GLY 34  20  20  GLY GLY A . n 
A 1 35  ASP 35  21  21  ASP ASP A . n 
A 1 36  VAL 36  22  22  VAL VAL A . n 
A 1 37  ASN 37  23  23  ASN ASN A . n 
A 1 38  GLY 38  24  24  GLY GLY A . n 
A 1 39  HIS 39  25  25  HIS HIS A . n 
A 1 40  LYS 40  26  26  LYS LYS A . n 
A 1 41  PHE 41  27  27  PHE PHE A . n 
A 1 42  SER 42  28  28  SER SER A . n 
A 1 43  VAL 43  29  29  VAL VAL A . n 
A 1 44  SER 44  30  30  SER SER A . n 
A 1 45  GLY 45  31  31  GLY GLY A . n 
A 1 46  GLU 46  32  32  GLU GLU A . n 
A 1 47  GLY 47  33  33  GLY GLY A . n 
A 1 48  GLU 48  34  34  GLU GLU A . n 
A 1 49  GLY 49  35  35  GLY GLY A . n 
A 1 50  ASP 50  36  36  ASP ASP A . n 
A 1 51  ALA 51  37  37  ALA ALA A . n 
A 1 52  THR 52  38  38  THR THR A . n 
A 1 53  TYR 53  39  39  TYR TYR A . n 
A 1 54  GLY 54  40  40  GLY GLY A . n 
A 1 55  LYS 55  41  41  LYS LYS A . n 
A 1 56  LEU 56  42  42  LEU LEU A . n 
A 1 57  THR 57  43  43  THR THR A . n 
A 1 58  LEU 58  44  44  LEU LEU A . n 
A 1 59  LYS 59  45  45  LYS LYS A . n 
A 1 60  PHE 60  46  46  PHE PHE A . n 
A 1 61  ILE 61  47  47  ILE ILE A . n 
A 1 62  SER 62  48  48  SER SER A . n 
A 1 63  THR 63  49  49  THR THR A . n 
A 1 64  THR 64  50  50  THR THR A . n 
A 1 65  GLY 65  51  51  GLY GLY A . n 
A 1 66  LYS 66  52  52  LYS LYS A . n 
A 1 67  LEU 67  53  53  LEU LEU A . n 
A 1 68  PRO 68  54  54  PRO PRO A . n 
A 1 69  VAL 69  55  55  VAL VAL A . n 
A 1 70  PRO 70  56  56  PRO PRO A . n 
A 1 71  TRP 71  57  57  TRP TRP A . n 
A 1 72  PRO 72  58  58  PRO PRO A . n 
A 1 73  THR 73  59  59  THR THR A . n 
A 1 74  LEU 74  60  60  LEU LEU A . n 
A 1 75  VAL 75  61  61  VAL VAL A . n 
A 1 76  THR 76  62  62  THR THR A . n 
A 1 77  THR 77  63  63  THR THR A . n 
A 1 78  LEU 78  64  64  LEU LEU A . n 
A 1 79  SWG 79  65  66  SWG SWG A . n 
A 1 80  VAL 80  66  68  VAL VAL A . n 
A 1 81  GLN 81  67  69  GLN GLN A . n 
A 1 82  CYS 82  68  70  CYS CYS A . n 
A 1 83  PHE 83  69  71  PHE PHE A . n 
A 1 84  ALA 84  70  72  ALA ALA A . n 
A 1 85  ARG 85  71  73  ARG ARG A . n 
A 1 86  TYR 86  72  74  TYR TYR A . n 
A 1 87  PRO 87  73  75  PRO PRO A . n 
A 1 88  ASP 88  74  76  ASP ASP A . n 
A 1 89  HIS 89  75  77  HIS HIS A . n 
A 1 90  MET 90  76  78  MET MET A . n 
A 1 91  LYS 91  77  79  LYS LYS A . n 
A 1 92  ARG 92  78  80  ARG ARG A . n 
A 1 93  HIS 93  79  81  HIS HIS A . n 
A 1 94  ASP 94  80  82  ASP ASP A . n 
A 1 95  PHE 95  81  83  PHE PHE A . n 
A 1 96  PHE 96  82  84  PHE PHE A . n 
A 1 97  LYS 97  83  85  LYS LYS A . n 
A 1 98  SER 98  84  86  SER SER A . n 
A 1 99  ALA 99  85  87  ALA ALA A . n 
A 1 100 MET 100 86  88  MET MET A . n 
A 1 101 PRO 101 87  89  PRO PRO A . n 
A 1 102 GLU 102 88  90  GLU GLU A . n 
A 1 103 GLY 103 89  91  GLY GLY A . n 
A 1 104 TYR 104 90  92  TYR TYR A . n 
A 1 105 VAL 105 91  93  VAL VAL A . n 
A 1 106 GLN 106 92  94  GLN GLN A . n 
A 1 107 GLU 107 93  95  GLU GLU A . n 
A 1 108 ARG 108 94  96  ARG ARG A . n 
A 1 109 THR 109 95  97  THR THR A . n 
A 1 110 ILE 110 96  98  ILE ILE A . n 
A 1 111 PHE 111 97  99  PHE PHE A . n 
A 1 112 PHE 112 98  100 PHE PHE A . n 
A 1 113 LYS 113 99  101 LYS LYS A . n 
A 1 114 ASP 114 100 102 ASP ASP A . n 
A 1 115 ASP 115 101 103 ASP ASP A . n 
A 1 116 GLY 116 102 104 GLY GLY A . n 
A 1 117 ASN 117 103 105 ASN ASN A . n 
A 1 118 TYR 118 104 106 TYR TYR A . n 
A 1 119 LYS 119 105 107 LYS LYS A . n 
A 1 120 THR 120 106 108 THR THR A . n 
A 1 121 ARG 121 107 109 ARG ARG A . n 
A 1 122 ALA 122 108 110 ALA ALA A . n 
A 1 123 GLU 123 109 111 GLU GLU A . n 
A 1 124 VAL 124 110 112 VAL VAL A . n 
A 1 125 LYS 125 111 113 LYS LYS A . n 
A 1 126 PHE 126 112 114 PHE PHE A . n 
A 1 127 GLU 127 113 115 GLU GLU A . n 
A 1 128 GLY 128 114 116 GLY GLY A . n 
A 1 129 ASP 129 115 117 ASP ASP A . n 
A 1 130 THR 130 116 118 THR THR A . n 
A 1 131 LEU 131 117 119 LEU LEU A . n 
A 1 132 VAL 132 118 120 VAL VAL A . n 
A 1 133 ASN 133 119 121 ASN ASN A . n 
A 1 134 ARG 134 120 122 ARG ARG A . n 
A 1 135 ILE 135 121 123 ILE ILE A . n 
A 1 136 GLU 136 122 124 GLU GLU A . n 
A 1 137 LEU 137 123 125 LEU LEU A . n 
A 1 138 LYS 138 124 126 LYS LYS A . n 
A 1 139 GLY 139 125 127 GLY GLY A . n 
A 1 140 ILE 140 126 128 ILE ILE A . n 
A 1 141 ASP 141 127 129 ASP ASP A . n 
A 1 142 PHE 142 128 130 PHE PHE A . n 
A 1 143 LYS 143 129 131 LYS LYS A . n 
A 1 144 GLU 144 130 132 GLU GLU A . n 
A 1 145 ASP 145 131 133 ASP ASP A . n 
A 1 146 GLY 146 132 134 GLY GLY A . n 
A 1 147 ASN 147 133 135 ASN ASN A . n 
A 1 148 ILE 148 134 136 ILE ILE A . n 
A 1 149 LEU 149 135 137 LEU LEU A . n 
A 1 150 GLY 150 136 138 GLY GLY A . n 
A 1 151 HIS 151 137 139 HIS HIS A . n 
A 1 152 LYS 152 138 140 LYS LYS A . n 
A 1 153 LEU 153 139 141 LEU LEU A . n 
A 1 154 GLU 154 140 142 GLU GLU A . n 
A 1 155 TYR 155 141 143 TYR TYR A . n 
A 1 156 ASN 156 142 144 ASN ASN A . n 
A 1 157 GLY 157 143 145 GLY GLY A . n 
A 1 158 TRP 158 144 146 TRP TRP A . n 
A 1 159 CYS 159 145 147 CYS CYS A . n 
A 1 160 GLY 160 146 148 GLY GLY A . n 
A 1 161 ASP 161 147 149 ASP ASP A . n 
A 1 162 ASN 162 148 150 ASN ASN A . n 
A 1 163 VAL 163 149 151 VAL VAL A . n 
A 1 164 TYR 164 150 152 TYR TYR A . n 
A 1 165 ILE 165 151 153 ILE ILE A . n 
A 1 166 THR 166 152 154 THR THR A . n 
A 1 167 ALA 167 153 155 ALA ALA A . n 
A 1 168 ASP 168 154 156 ASP ASP A . n 
A 1 169 LYS 169 155 157 LYS LYS A . n 
A 1 170 GLN 170 156 158 GLN GLN A . n 
A 1 171 LYS 171 157 159 LYS LYS A . n 
A 1 172 ASN 172 158 160 ASN ASN A . n 
A 1 173 GLY 173 159 161 GLY GLY A . n 
A 1 174 ILE 174 160 162 ILE ILE A . n 
A 1 175 LYS 175 161 163 LYS LYS A . n 
A 1 176 ALA 176 162 164 ALA ALA A . n 
A 1 177 ASN 177 163 165 ASN ASN A . n 
A 1 178 PHE 178 164 166 PHE PHE A . n 
A 1 179 LYS 179 165 167 LYS LYS A . n 
A 1 180 ILE 180 166 168 ILE ILE A . n 
A 1 181 ARG 181 167 169 ARG ARG A . n 
A 1 182 HIS 182 168 170 HIS HIS A . n 
A 1 183 ASN 183 169 171 ASN ASN A . n 
A 1 184 ILE 184 170 172 ILE ILE A . n 
A 1 185 GLU 185 171 173 GLU GLU A . n 
A 1 186 ASP 186 172 174 ASP ASP A . n 
A 1 187 GLY 187 173 175 GLY GLY A . n 
A 1 188 GLY 188 174 176 GLY GLY A . n 
A 1 189 VAL 189 175 177 VAL VAL A . n 
A 1 190 GLN 190 176 178 GLN GLN A . n 
A 1 191 LEU 191 177 179 LEU LEU A . n 
A 1 192 ALA 192 178 180 ALA ALA A . n 
A 1 193 ASP 193 179 181 ASP ASP A . n 
A 1 194 HIS 194 180 182 HIS HIS A . n 
A 1 195 TYR 195 181 183 TYR TYR A . n 
A 1 196 GLN 196 182 184 GLN GLN A . n 
A 1 197 GLN 197 183 185 GLN GLN A . n 
A 1 198 ASN 198 184 186 ASN ASN A . n 
A 1 199 THR 199 185 187 THR THR A . n 
A 1 200 PRO 200 186 188 PRO PRO A . n 
A 1 201 ILE 201 187 189 ILE ILE A . n 
A 1 202 GLY 202 188 190 GLY GLY A . n 
A 1 203 ASP 203 189 191 ASP ASP A . n 
A 1 204 GLY 204 190 192 GLY GLY A . n 
A 1 205 PRO 205 191 193 PRO PRO A . n 
A 1 206 VAL 206 192 194 VAL VAL A . n 
A 1 207 LEU 207 193 195 LEU LEU A . n 
A 1 208 LEU 208 194 196 LEU LEU A . n 
A 1 209 PRO 209 195 197 PRO PRO A . n 
A 1 210 ASP 210 196 198 ASP ASP A . n 
A 1 211 ASN 211 197 199 ASN ASN A . n 
A 1 212 HIS 212 198 200 HIS HIS A . n 
A 1 213 TYR 213 199 201 TYR TYR A . n 
A 1 214 LEU 214 200 202 LEU LEU A . n 
A 1 215 SER 215 201 203 SER SER A . n 
A 1 216 THR 216 202 204 THR THR A . n 
A 1 217 CYS 217 203 205 CYS CYS A . n 
A 1 218 SER 218 204 206 SER SER A . n 
A 1 219 LYS 219 205 207 LYS LYS A . n 
A 1 220 LEU 220 206 208 LEU LEU A . n 
A 1 221 SER 221 207 209 SER SER A . n 
A 1 222 LYS 222 208 210 LYS LYS A . n 
A 1 223 ASP 223 209 211 ASP ASP A . n 
A 1 224 PRO 224 210 212 PRO PRO A . n 
A 1 225 ASN 225 211 213 ASN ASN A . n 
A 1 226 GLU 226 212 214 GLU GLU A . n 
A 1 227 LYS 227 213 215 LYS LYS A . n 
A 1 228 ARG 228 214 216 ARG ARG A . n 
A 1 229 ASP 229 215 217 ASP ASP A . n 
A 1 230 HIS 230 216 218 HIS HIS A . n 
A 1 231 MET 231 217 219 MET MET A . n 
A 1 232 VAL 232 218 220 VAL VAL A . n 
A 1 233 PHE 233 219 221 PHE PHE A . n 
A 1 234 LEU 234 220 222 LEU LEU A . n 
A 1 235 GLU 235 221 223 GLU GLU A . n 
A 1 236 PHE 236 222 224 PHE PHE A . n 
A 1 237 VAL 237 223 225 VAL VAL A . n 
A 1 238 THR 238 224 226 THR THR A . n 
A 1 239 ALA 239 225 227 ALA ALA A . n 
A 1 240 ALA 240 226 228 ALA ALA A . n 
A 1 241 GLY 241 227 229 GLY GLY A . n 
A 1 242 ILE 242 228 230 ILE ILE A . n 
A 1 243 THR 243 229 231 THR THR A . n 
A 1 244 LEU 244 230 232 LEU LEU A . n 
A 1 245 GLY 245 231 ?   ?   ?   A . n 
A 1 246 MET 246 232 ?   ?   ?   A . n 
A 1 247 ASP 247 233 ?   ?   ?   A . n 
A 1 248 GLU 248 234 ?   ?   ?   A . n 
A 1 249 LEU 249 235 ?   ?   ?   A . n 
A 1 250 TYR 250 236 ?   ?   ?   A . n 
A 1 251 LYS 251 237 ?   ?   ?   A . n 
B 1 1   MET 1   -13 ?   ?   ?   B . n 
B 1 2   LYS 2   -12 ?   ?   ?   B . n 
B 1 3   HIS 3   -11 ?   ?   ?   B . n 
B 1 4   HIS 4   -10 ?   ?   ?   B . n 
B 1 5   HIS 5   -9  ?   ?   ?   B . n 
B 1 6   HIS 6   -8  ?   ?   ?   B . n 
B 1 7   HIS 7   -7  ?   ?   ?   B . n 
B 1 8   HIS 8   -6  ?   ?   ?   B . n 
B 1 9   HIS 9   -5  ?   ?   ?   B . n 
B 1 10  GLY 10  -4  ?   ?   ?   B . n 
B 1 11  GLY 11  -3  ?   ?   ?   B . n 
B 1 12  ALA 12  -2  ?   ?   ?   B . n 
B 1 13  SER 13  -1  ?   ?   ?   B . n 
B 1 14  MET 14  0   ?   ?   ?   B . n 
B 1 15  VAL 15  1   ?   ?   ?   B . n 
B 1 16  SER 16  2   ?   ?   ?   B . n 
B 1 17  LYS 17  3   3   LYS LYS B . n 
B 1 18  GLY 18  4   4   GLY GLY B . n 
B 1 19  GLU 19  5   5   GLU GLU B . n 
B 1 20  GLU 20  6   6   GLU GLU B . n 
B 1 21  LEU 21  7   7   LEU LEU B . n 
B 1 22  PHE 22  8   8   PHE PHE B . n 
B 1 23  THR 23  9   9   THR THR B . n 
B 1 24  GLY 24  10  10  GLY GLY B . n 
B 1 25  VAL 25  11  11  VAL VAL B . n 
B 1 26  VAL 26  12  12  VAL VAL B . n 
B 1 27  PRO 27  13  13  PRO PRO B . n 
B 1 28  ILE 28  14  14  ILE ILE B . n 
B 1 29  LEU 29  15  15  LEU LEU B . n 
B 1 30  VAL 30  16  16  VAL VAL B . n 
B 1 31  GLU 31  17  17  GLU GLU B . n 
B 1 32  LEU 32  18  18  LEU LEU B . n 
B 1 33  ASP 33  19  19  ASP ASP B . n 
B 1 34  GLY 34  20  20  GLY GLY B . n 
B 1 35  ASP 35  21  21  ASP ASP B . n 
B 1 36  VAL 36  22  22  VAL VAL B . n 
B 1 37  ASN 37  23  23  ASN ASN B . n 
B 1 38  GLY 38  24  24  GLY GLY B . n 
B 1 39  HIS 39  25  25  HIS HIS B . n 
B 1 40  LYS 40  26  26  LYS LYS B . n 
B 1 41  PHE 41  27  27  PHE PHE B . n 
B 1 42  SER 42  28  28  SER SER B . n 
B 1 43  VAL 43  29  29  VAL VAL B . n 
B 1 44  SER 44  30  30  SER SER B . n 
B 1 45  GLY 45  31  31  GLY GLY B . n 
B 1 46  GLU 46  32  32  GLU GLU B . n 
B 1 47  GLY 47  33  33  GLY GLY B . n 
B 1 48  GLU 48  34  34  GLU GLU B . n 
B 1 49  GLY 49  35  35  GLY GLY B . n 
B 1 50  ASP 50  36  36  ASP ASP B . n 
B 1 51  ALA 51  37  37  ALA ALA B . n 
B 1 52  THR 52  38  38  THR THR B . n 
B 1 53  TYR 53  39  39  TYR TYR B . n 
B 1 54  GLY 54  40  40  GLY GLY B . n 
B 1 55  LYS 55  41  41  LYS LYS B . n 
B 1 56  LEU 56  42  42  LEU LEU B . n 
B 1 57  THR 57  43  43  THR THR B . n 
B 1 58  LEU 58  44  44  LEU LEU B . n 
B 1 59  LYS 59  45  45  LYS LYS B . n 
B 1 60  PHE 60  46  46  PHE PHE B . n 
B 1 61  ILE 61  47  47  ILE ILE B . n 
B 1 62  SER 62  48  48  SER SER B . n 
B 1 63  THR 63  49  49  THR THR B . n 
B 1 64  THR 64  50  50  THR THR B . n 
B 1 65  GLY 65  51  51  GLY GLY B . n 
B 1 66  LYS 66  52  52  LYS LYS B . n 
B 1 67  LEU 67  53  53  LEU LEU B . n 
B 1 68  PRO 68  54  54  PRO PRO B . n 
B 1 69  VAL 69  55  55  VAL VAL B . n 
B 1 70  PRO 70  56  56  PRO PRO B . n 
B 1 71  TRP 71  57  57  TRP TRP B . n 
B 1 72  PRO 72  58  58  PRO PRO B . n 
B 1 73  THR 73  59  59  THR THR B . n 
B 1 74  LEU 74  60  60  LEU LEU B . n 
B 1 75  VAL 75  61  61  VAL VAL B . n 
B 1 76  THR 76  62  62  THR THR B . n 
B 1 77  THR 77  63  63  THR THR B . n 
B 1 78  LEU 78  64  64  LEU LEU B . n 
B 1 79  SWG 79  65  66  SWG SWG B . n 
B 1 80  VAL 80  66  68  VAL VAL B . n 
B 1 81  GLN 81  67  69  GLN GLN B . n 
B 1 82  CYS 82  68  70  CYS CYS B . n 
B 1 83  PHE 83  69  71  PHE PHE B . n 
B 1 84  ALA 84  70  72  ALA ALA B . n 
B 1 85  ARG 85  71  73  ARG ARG B . n 
B 1 86  TYR 86  72  74  TYR TYR B . n 
B 1 87  PRO 87  73  75  PRO PRO B . n 
B 1 88  ASP 88  74  76  ASP ASP B . n 
B 1 89  HIS 89  75  77  HIS HIS B . n 
B 1 90  MET 90  76  78  MET MET B . n 
B 1 91  LYS 91  77  79  LYS LYS B . n 
B 1 92  ARG 92  78  80  ARG ARG B . n 
B 1 93  HIS 93  79  81  HIS HIS B . n 
B 1 94  ASP 94  80  82  ASP ASP B . n 
B 1 95  PHE 95  81  83  PHE PHE B . n 
B 1 96  PHE 96  82  84  PHE PHE B . n 
B 1 97  LYS 97  83  85  LYS LYS B . n 
B 1 98  SER 98  84  86  SER SER B . n 
B 1 99  ALA 99  85  87  ALA ALA B . n 
B 1 100 MET 100 86  88  MET MET B . n 
B 1 101 PRO 101 87  89  PRO PRO B . n 
B 1 102 GLU 102 88  90  GLU GLU B . n 
B 1 103 GLY 103 89  91  GLY GLY B . n 
B 1 104 TYR 104 90  92  TYR TYR B . n 
B 1 105 VAL 105 91  93  VAL VAL B . n 
B 1 106 GLN 106 92  94  GLN GLN B . n 
B 1 107 GLU 107 93  95  GLU GLU B . n 
B 1 108 ARG 108 94  96  ARG ARG B . n 
B 1 109 THR 109 95  97  THR THR B . n 
B 1 110 ILE 110 96  98  ILE ILE B . n 
B 1 111 PHE 111 97  99  PHE PHE B . n 
B 1 112 PHE 112 98  100 PHE PHE B . n 
B 1 113 LYS 113 99  101 LYS LYS B . n 
B 1 114 ASP 114 100 102 ASP ASP B . n 
B 1 115 ASP 115 101 103 ASP ASP B . n 
B 1 116 GLY 116 102 104 GLY GLY B . n 
B 1 117 ASN 117 103 105 ASN ASN B . n 
B 1 118 TYR 118 104 106 TYR TYR B . n 
B 1 119 LYS 119 105 107 LYS LYS B . n 
B 1 120 THR 120 106 108 THR THR B . n 
B 1 121 ARG 121 107 109 ARG ARG B . n 
B 1 122 ALA 122 108 110 ALA ALA B . n 
B 1 123 GLU 123 109 111 GLU GLU B . n 
B 1 124 VAL 124 110 112 VAL VAL B . n 
B 1 125 LYS 125 111 113 LYS LYS B . n 
B 1 126 PHE 126 112 114 PHE PHE B . n 
B 1 127 GLU 127 113 115 GLU GLU B . n 
B 1 128 GLY 128 114 116 GLY GLY B . n 
B 1 129 ASP 129 115 117 ASP ASP B . n 
B 1 130 THR 130 116 118 THR THR B . n 
B 1 131 LEU 131 117 119 LEU LEU B . n 
B 1 132 VAL 132 118 120 VAL VAL B . n 
B 1 133 ASN 133 119 121 ASN ASN B . n 
B 1 134 ARG 134 120 122 ARG ARG B . n 
B 1 135 ILE 135 121 123 ILE ILE B . n 
B 1 136 GLU 136 122 124 GLU GLU B . n 
B 1 137 LEU 137 123 125 LEU LEU B . n 
B 1 138 LYS 138 124 126 LYS LYS B . n 
B 1 139 GLY 139 125 127 GLY GLY B . n 
B 1 140 ILE 140 126 128 ILE ILE B . n 
B 1 141 ASP 141 127 129 ASP ASP B . n 
B 1 142 PHE 142 128 130 PHE PHE B . n 
B 1 143 LYS 143 129 131 LYS LYS B . n 
B 1 144 GLU 144 130 132 GLU GLU B . n 
B 1 145 ASP 145 131 133 ASP ASP B . n 
B 1 146 GLY 146 132 134 GLY GLY B . n 
B 1 147 ASN 147 133 135 ASN ASN B . n 
B 1 148 ILE 148 134 136 ILE ILE B . n 
B 1 149 LEU 149 135 137 LEU LEU B . n 
B 1 150 GLY 150 136 138 GLY GLY B . n 
B 1 151 HIS 151 137 139 HIS HIS B . n 
B 1 152 LYS 152 138 140 LYS LYS B . n 
B 1 153 LEU 153 139 141 LEU LEU B . n 
B 1 154 GLU 154 140 142 GLU GLU B . n 
B 1 155 TYR 155 141 143 TYR TYR B . n 
B 1 156 ASN 156 142 144 ASN ASN B . n 
B 1 157 GLY 157 143 145 GLY GLY B . n 
B 1 158 TRP 158 144 146 TRP TRP B . n 
B 1 159 CYS 159 145 147 CYS CYS B . n 
B 1 160 GLY 160 146 148 GLY GLY B . n 
B 1 161 ASP 161 147 149 ASP ASP B . n 
B 1 162 ASN 162 148 150 ASN ASN B . n 
B 1 163 VAL 163 149 151 VAL VAL B . n 
B 1 164 TYR 164 150 152 TYR TYR B . n 
B 1 165 ILE 165 151 153 ILE ILE B . n 
B 1 166 THR 166 152 154 THR THR B . n 
B 1 167 ALA 167 153 155 ALA ALA B . n 
B 1 168 ASP 168 154 156 ASP ASP B . n 
B 1 169 LYS 169 155 157 LYS LYS B . n 
B 1 170 GLN 170 156 158 GLN GLN B . n 
B 1 171 LYS 171 157 159 LYS LYS B . n 
B 1 172 ASN 172 158 160 ASN ASN B . n 
B 1 173 GLY 173 159 161 GLY GLY B . n 
B 1 174 ILE 174 160 162 ILE ILE B . n 
B 1 175 LYS 175 161 163 LYS LYS B . n 
B 1 176 ALA 176 162 164 ALA ALA B . n 
B 1 177 ASN 177 163 165 ASN ASN B . n 
B 1 178 PHE 178 164 166 PHE PHE B . n 
B 1 179 LYS 179 165 167 LYS LYS B . n 
B 1 180 ILE 180 166 168 ILE ILE B . n 
B 1 181 ARG 181 167 169 ARG ARG B . n 
B 1 182 HIS 182 168 170 HIS HIS B . n 
B 1 183 ASN 183 169 171 ASN ASN B . n 
B 1 184 ILE 184 170 172 ILE ILE B . n 
B 1 185 GLU 185 171 173 GLU GLU B . n 
B 1 186 ASP 186 172 174 ASP ASP B . n 
B 1 187 GLY 187 173 175 GLY GLY B . n 
B 1 188 GLY 188 174 176 GLY GLY B . n 
B 1 189 VAL 189 175 177 VAL VAL B . n 
B 1 190 GLN 190 176 178 GLN GLN B . n 
B 1 191 LEU 191 177 179 LEU LEU B . n 
B 1 192 ALA 192 178 180 ALA ALA B . n 
B 1 193 ASP 193 179 181 ASP ASP B . n 
B 1 194 HIS 194 180 182 HIS HIS B . n 
B 1 195 TYR 195 181 183 TYR TYR B . n 
B 1 196 GLN 196 182 184 GLN GLN B . n 
B 1 197 GLN 197 183 185 GLN GLN B . n 
B 1 198 ASN 198 184 186 ASN ASN B . n 
B 1 199 THR 199 185 187 THR THR B . n 
B 1 200 PRO 200 186 188 PRO PRO B . n 
B 1 201 ILE 201 187 189 ILE ILE B . n 
B 1 202 GLY 202 188 190 GLY GLY B . n 
B 1 203 ASP 203 189 191 ASP ASP B . n 
B 1 204 GLY 204 190 192 GLY GLY B . n 
B 1 205 PRO 205 191 193 PRO PRO B . n 
B 1 206 VAL 206 192 194 VAL VAL B . n 
B 1 207 LEU 207 193 195 LEU LEU B . n 
B 1 208 LEU 208 194 196 LEU LEU B . n 
B 1 209 PRO 209 195 197 PRO PRO B . n 
B 1 210 ASP 210 196 198 ASP ASP B . n 
B 1 211 ASN 211 197 199 ASN ASN B . n 
B 1 212 HIS 212 198 200 HIS HIS B . n 
B 1 213 TYR 213 199 201 TYR TYR B . n 
B 1 214 LEU 214 200 202 LEU LEU B . n 
B 1 215 SER 215 201 203 SER SER B . n 
B 1 216 THR 216 202 204 THR THR B . n 
B 1 217 CYS 217 203 205 CYS CYS B . n 
B 1 218 SER 218 204 206 SER SER B . n 
B 1 219 LYS 219 205 207 LYS LYS B . n 
B 1 220 LEU 220 206 208 LEU LEU B . n 
B 1 221 SER 221 207 209 SER SER B . n 
B 1 222 LYS 222 208 210 LYS LYS B . n 
B 1 223 ASP 223 209 211 ASP ASP B . n 
B 1 224 PRO 224 210 212 PRO PRO B . n 
B 1 225 ASN 225 211 213 ASN ASN B . n 
B 1 226 GLU 226 212 214 GLU GLU B . n 
B 1 227 LYS 227 213 215 LYS LYS B . n 
B 1 228 ARG 228 214 216 ARG ARG B . n 
B 1 229 ASP 229 215 217 ASP ASP B . n 
B 1 230 HIS 230 216 218 HIS HIS B . n 
B 1 231 MET 231 217 219 MET MET B . n 
B 1 232 VAL 232 218 220 VAL VAL B . n 
B 1 233 PHE 233 219 221 PHE PHE B . n 
B 1 234 LEU 234 220 222 LEU LEU B . n 
B 1 235 GLU 235 221 223 GLU GLU B . n 
B 1 236 PHE 236 222 224 PHE PHE B . n 
B 1 237 VAL 237 223 225 VAL VAL B . n 
B 1 238 THR 238 224 226 THR THR B . n 
B 1 239 ALA 239 225 227 ALA ALA B . n 
B 1 240 ALA 240 226 228 ALA ALA B . n 
B 1 241 GLY 241 227 229 GLY GLY B . n 
B 1 242 ILE 242 228 230 ILE ILE B . n 
B 1 243 THR 243 229 ?   ?   ?   B . n 
B 1 244 LEU 244 230 ?   ?   ?   B . n 
B 1 245 GLY 245 231 ?   ?   ?   B . n 
B 1 246 MET 246 232 ?   ?   ?   B . n 
B 1 247 ASP 247 233 ?   ?   ?   B . n 
B 1 248 GLU 248 234 ?   ?   ?   B . n 
B 1 249 LEU 249 235 ?   ?   ?   B . n 
B 1 250 TYR 250 236 ?   ?   ?   B . n 
B 1 251 LYS 251 237 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        SWG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   SWG 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
C 2 ACY 1   301 301 ACY ACY A . 
D 3 PGE 1   302 302 PGE PGE A . 
E 4 GOL 1   303 307 GOL GOL A . 
F 5 PEG 1   304 308 PEG PEG A . 
G 4 GOL 1   301 321 GOL GOL B . 
H 4 GOL 1   302 323 GOL GOL B . 
I 4 GOL 1   303 324 GOL GOL B . 
J 2 ACY 1   304 311 ACY ACY B . 
K 6 HOH 1   401 73  HOH HOH A . 
K 6 HOH 2   402 175 HOH HOH A . 
K 6 HOH 3   403 72  HOH HOH A . 
K 6 HOH 4   404 177 HOH HOH A . 
K 6 HOH 5   405 138 HOH HOH A . 
K 6 HOH 6   406 100 HOH HOH A . 
K 6 HOH 7   407 1   HOH HOH A . 
K 6 HOH 8   408 7   HOH HOH A . 
K 6 HOH 9   409 58  HOH HOH A . 
K 6 HOH 10  410 158 HOH HOH A . 
K 6 HOH 11  411 2   HOH HOH A . 
K 6 HOH 12  412 15  HOH HOH A . 
K 6 HOH 13  413 118 HOH HOH A . 
K 6 HOH 14  414 200 HOH HOH A . 
K 6 HOH 15  415 144 HOH HOH A . 
K 6 HOH 16  416 49  HOH HOH A . 
K 6 HOH 17  417 169 HOH HOH A . 
K 6 HOH 18  418 106 HOH HOH A . 
K 6 HOH 19  419 154 HOH HOH A . 
K 6 HOH 20  420 99  HOH HOH A . 
K 6 HOH 21  421 116 HOH HOH A . 
K 6 HOH 22  422 115 HOH HOH A . 
K 6 HOH 23  423 137 HOH HOH A . 
K 6 HOH 24  424 185 HOH HOH A . 
K 6 HOH 25  425 77  HOH HOH A . 
K 6 HOH 26  426 94  HOH HOH A . 
K 6 HOH 27  427 206 HOH HOH A . 
K 6 HOH 28  428 52  HOH HOH A . 
K 6 HOH 29  429 11  HOH HOH A . 
K 6 HOH 30  430 105 HOH HOH A . 
K 6 HOH 31  431 9   HOH HOH A . 
K 6 HOH 32  432 278 HOH HOH A . 
K 6 HOH 33  433 191 HOH HOH A . 
K 6 HOH 34  434 88  HOH HOH A . 
K 6 HOH 35  435 107 HOH HOH A . 
K 6 HOH 36  436 53  HOH HOH A . 
K 6 HOH 37  437 218 HOH HOH A . 
K 6 HOH 38  438 188 HOH HOH A . 
K 6 HOH 39  439 135 HOH HOH A . 
K 6 HOH 40  440 97  HOH HOH A . 
K 6 HOH 41  441 102 HOH HOH A . 
K 6 HOH 42  442 75  HOH HOH A . 
K 6 HOH 43  443 4   HOH HOH A . 
K 6 HOH 44  444 20  HOH HOH A . 
K 6 HOH 45  445 151 HOH HOH A . 
K 6 HOH 46  446 124 HOH HOH A . 
K 6 HOH 47  447 57  HOH HOH A . 
K 6 HOH 48  448 10  HOH HOH A . 
K 6 HOH 49  449 126 HOH HOH A . 
K 6 HOH 50  450 31  HOH HOH A . 
K 6 HOH 51  451 189 HOH HOH A . 
K 6 HOH 52  452 85  HOH HOH A . 
K 6 HOH 53  453 41  HOH HOH A . 
K 6 HOH 54  454 47  HOH HOH A . 
K 6 HOH 55  455 80  HOH HOH A . 
K 6 HOH 56  456 13  HOH HOH A . 
K 6 HOH 57  457 279 HOH HOH A . 
K 6 HOH 58  458 131 HOH HOH A . 
K 6 HOH 59  459 280 HOH HOH A . 
K 6 HOH 60  460 180 HOH HOH A . 
K 6 HOH 61  461 101 HOH HOH A . 
K 6 HOH 62  462 24  HOH HOH A . 
K 6 HOH 63  463 74  HOH HOH A . 
K 6 HOH 64  464 50  HOH HOH A . 
K 6 HOH 65  465 86  HOH HOH A . 
K 6 HOH 66  466 40  HOH HOH A . 
K 6 HOH 67  467 70  HOH HOH A . 
K 6 HOH 68  468 113 HOH HOH A . 
K 6 HOH 69  469 220 HOH HOH A . 
K 6 HOH 70  470 176 HOH HOH A . 
K 6 HOH 71  471 204 HOH HOH A . 
K 6 HOH 72  472 78  HOH HOH A . 
K 6 HOH 73  473 267 HOH HOH A . 
K 6 HOH 74  474 37  HOH HOH A . 
K 6 HOH 75  475 239 HOH HOH A . 
K 6 HOH 76  476 128 HOH HOH A . 
K 6 HOH 77  477 79  HOH HOH A . 
K 6 HOH 78  478 67  HOH HOH A . 
K 6 HOH 79  479 43  HOH HOH A . 
K 6 HOH 80  480 96  HOH HOH A . 
K 6 HOH 81  481 29  HOH HOH A . 
K 6 HOH 82  482 197 HOH HOH A . 
K 6 HOH 83  483 108 HOH HOH A . 
K 6 HOH 84  484 21  HOH HOH A . 
K 6 HOH 85  485 147 HOH HOH A . 
K 6 HOH 86  486 242 HOH HOH A . 
K 6 HOH 87  487 212 HOH HOH A . 
K 6 HOH 88  488 38  HOH HOH A . 
K 6 HOH 89  489 84  HOH HOH A . 
K 6 HOH 90  490 145 HOH HOH A . 
K 6 HOH 91  491 157 HOH HOH A . 
K 6 HOH 92  492 103 HOH HOH A . 
K 6 HOH 93  493 265 HOH HOH A . 
K 6 HOH 94  494 54  HOH HOH A . 
K 6 HOH 95  495 39  HOH HOH A . 
K 6 HOH 96  496 83  HOH HOH A . 
K 6 HOH 97  497 209 HOH HOH A . 
K 6 HOH 98  498 276 HOH HOH A . 
K 6 HOH 99  499 283 HOH HOH A . 
K 6 HOH 100 500 104 HOH HOH A . 
K 6 HOH 101 501 235 HOH HOH A . 
K 6 HOH 102 502 130 HOH HOH A . 
K 6 HOH 103 503 120 HOH HOH A . 
K 6 HOH 104 504 95  HOH HOH A . 
K 6 HOH 105 505 263 HOH HOH A . 
K 6 HOH 106 506 87  HOH HOH A . 
K 6 HOH 107 507 237 HOH HOH A . 
K 6 HOH 108 508 253 HOH HOH A . 
K 6 HOH 109 509 240 HOH HOH A . 
K 6 HOH 110 510 245 HOH HOH A . 
K 6 HOH 111 511 224 HOH HOH A . 
K 6 HOH 112 512 241 HOH HOH A . 
K 6 HOH 113 513 199 HOH HOH A . 
K 6 HOH 114 514 222 HOH HOH A . 
K 6 HOH 115 515 98  HOH HOH A . 
K 6 HOH 116 516 178 HOH HOH A . 
K 6 HOH 117 517 167 HOH HOH A . 
K 6 HOH 118 518 257 HOH HOH A . 
K 6 HOH 119 519 187 HOH HOH A . 
K 6 HOH 120 520 255 HOH HOH A . 
K 6 HOH 121 521 216 HOH HOH A . 
K 6 HOH 122 522 258 HOH HOH A . 
K 6 HOH 123 523 143 HOH HOH A . 
K 6 HOH 124 524 264 HOH HOH A . 
K 6 HOH 125 525 247 HOH HOH A . 
K 6 HOH 126 526 246 HOH HOH A . 
K 6 HOH 127 527 256 HOH HOH A . 
K 6 HOH 128 528 61  HOH HOH A . 
K 6 HOH 129 529 238 HOH HOH A . 
K 6 HOH 130 530 252 HOH HOH A . 
K 6 HOH 131 531 159 HOH HOH A . 
K 6 HOH 132 532 59  HOH HOH A . 
K 6 HOH 133 533 248 HOH HOH A . 
L 6 HOH 1   401 152 HOH HOH B . 
L 6 HOH 2   402 203 HOH HOH B . 
L 6 HOH 3   403 17  HOH HOH B . 
L 6 HOH 4   404 110 HOH HOH B . 
L 6 HOH 5   405 25  HOH HOH B . 
L 6 HOH 6   406 3   HOH HOH B . 
L 6 HOH 7   407 42  HOH HOH B . 
L 6 HOH 8   408 271 HOH HOH B . 
L 6 HOH 9   409 146 HOH HOH B . 
L 6 HOH 10  410 51  HOH HOH B . 
L 6 HOH 11  411 160 HOH HOH B . 
L 6 HOH 12  412 26  HOH HOH B . 
L 6 HOH 13  413 201 HOH HOH B . 
L 6 HOH 14  414 196 HOH HOH B . 
L 6 HOH 15  415 68  HOH HOH B . 
L 6 HOH 16  416 119 HOH HOH B . 
L 6 HOH 17  417 69  HOH HOH B . 
L 6 HOH 18  418 141 HOH HOH B . 
L 6 HOH 19  419 149 HOH HOH B . 
L 6 HOH 20  420 27  HOH HOH B . 
L 6 HOH 21  421 194 HOH HOH B . 
L 6 HOH 22  422 14  HOH HOH B . 
L 6 HOH 23  423 28  HOH HOH B . 
L 6 HOH 24  424 134 HOH HOH B . 
L 6 HOH 25  425 213 HOH HOH B . 
L 6 HOH 26  426 190 HOH HOH B . 
L 6 HOH 27  427 30  HOH HOH B . 
L 6 HOH 28  428 5   HOH HOH B . 
L 6 HOH 29  429 55  HOH HOH B . 
L 6 HOH 30  430 6   HOH HOH B . 
L 6 HOH 31  431 133 HOH HOH B . 
L 6 HOH 32  432 8   HOH HOH B . 
L 6 HOH 33  433 122 HOH HOH B . 
L 6 HOH 34  434 16  HOH HOH B . 
L 6 HOH 35  435 259 HOH HOH B . 
L 6 HOH 36  436 33  HOH HOH B . 
L 6 HOH 37  437 81  HOH HOH B . 
L 6 HOH 38  438 32  HOH HOH B . 
L 6 HOH 39  439 60  HOH HOH B . 
L 6 HOH 40  440 170 HOH HOH B . 
L 6 HOH 41  441 44  HOH HOH B . 
L 6 HOH 42  442 12  HOH HOH B . 
L 6 HOH 43  443 123 HOH HOH B . 
L 6 HOH 44  444 262 HOH HOH B . 
L 6 HOH 45  445 45  HOH HOH B . 
L 6 HOH 46  446 34  HOH HOH B . 
L 6 HOH 47  447 56  HOH HOH B . 
L 6 HOH 48  448 270 HOH HOH B . 
L 6 HOH 49  449 91  HOH HOH B . 
L 6 HOH 50  450 112 HOH HOH B . 
L 6 HOH 51  451 82  HOH HOH B . 
L 6 HOH 52  452 192 HOH HOH B . 
L 6 HOH 53  453 140 HOH HOH B . 
L 6 HOH 54  454 18  HOH HOH B . 
L 6 HOH 55  455 195 HOH HOH B . 
L 6 HOH 56  456 166 HOH HOH B . 
L 6 HOH 57  457 161 HOH HOH B . 
L 6 HOH 58  458 125 HOH HOH B . 
L 6 HOH 59  459 208 HOH HOH B . 
L 6 HOH 60  460 121 HOH HOH B . 
L 6 HOH 61  461 172 HOH HOH B . 
L 6 HOH 62  462 136 HOH HOH B . 
L 6 HOH 63  463 210 HOH HOH B . 
L 6 HOH 64  464 90  HOH HOH B . 
L 6 HOH 65  465 22  HOH HOH B . 
L 6 HOH 66  466 46  HOH HOH B . 
L 6 HOH 67  467 236 HOH HOH B . 
L 6 HOH 68  468 184 HOH HOH B . 
L 6 HOH 69  469 109 HOH HOH B . 
L 6 HOH 70  470 168 HOH HOH B . 
L 6 HOH 71  471 65  HOH HOH B . 
L 6 HOH 72  472 282 HOH HOH B . 
L 6 HOH 73  473 111 HOH HOH B . 
L 6 HOH 74  474 186 HOH HOH B . 
L 6 HOH 75  475 23  HOH HOH B . 
L 6 HOH 76  476 19  HOH HOH B . 
L 6 HOH 77  477 174 HOH HOH B . 
L 6 HOH 78  478 76  HOH HOH B . 
L 6 HOH 79  479 219 HOH HOH B . 
L 6 HOH 80  480 155 HOH HOH B . 
L 6 HOH 81  481 277 HOH HOH B . 
L 6 HOH 82  482 162 HOH HOH B . 
L 6 HOH 83  483 150 HOH HOH B . 
L 6 HOH 84  484 62  HOH HOH B . 
L 6 HOH 85  485 273 HOH HOH B . 
L 6 HOH 86  486 202 HOH HOH B . 
L 6 HOH 87  487 117 HOH HOH B . 
L 6 HOH 88  488 275 HOH HOH B . 
L 6 HOH 89  489 132 HOH HOH B . 
L 6 HOH 90  490 139 HOH HOH B . 
L 6 HOH 91  491 156 HOH HOH B . 
L 6 HOH 92  492 230 HOH HOH B . 
L 6 HOH 93  493 226 HOH HOH B . 
L 6 HOH 94  494 254 HOH HOH B . 
L 6 HOH 95  495 63  HOH HOH B . 
L 6 HOH 96  496 217 HOH HOH B . 
L 6 HOH 97  497 173 HOH HOH B . 
L 6 HOH 98  498 129 HOH HOH B . 
L 6 HOH 99  499 268 HOH HOH B . 
L 6 HOH 100 500 66  HOH HOH B . 
L 6 HOH 101 501 193 HOH HOH B . 
L 6 HOH 102 502 231 HOH HOH B . 
L 6 HOH 103 503 228 HOH HOH B . 
L 6 HOH 104 504 227 HOH HOH B . 
L 6 HOH 105 505 89  HOH HOH B . 
L 6 HOH 106 506 221 HOH HOH B . 
L 6 HOH 107 507 232 HOH HOH B . 
L 6 HOH 108 508 142 HOH HOH B . 
L 6 HOH 109 509 64  HOH HOH B . 
L 6 HOH 110 510 281 HOH HOH B . 
L 6 HOH 111 511 165 HOH HOH B . 
L 6 HOH 112 512 205 HOH HOH B . 
L 6 HOH 113 513 153 HOH HOH B . 
L 6 HOH 114 514 198 HOH HOH B . 
L 6 HOH 115 515 223 HOH HOH B . 
L 6 HOH 116 516 171 HOH HOH B . 
L 6 HOH 117 517 127 HOH HOH B . 
L 6 HOH 118 518 163 HOH HOH B . 
L 6 HOH 119 519 182 HOH HOH B . 
L 6 HOH 120 520 179 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 5  ? CG  ? A GLU 19 CG  
2  1 Y 1 A GLU 5  ? CD  ? A GLU 19 CD  
3  1 Y 1 A GLU 5  ? OE1 ? A GLU 19 OE1 
4  1 Y 1 A GLU 5  ? OE2 ? A GLU 19 OE2 
5  1 Y 1 A GLU 6  ? CG  ? A GLU 20 CG  
6  1 Y 1 A GLU 6  ? CD  ? A GLU 20 CD  
7  1 Y 1 A GLU 6  ? OE1 ? A GLU 20 OE1 
8  1 Y 1 A GLU 6  ? OE2 ? A GLU 20 OE2 
9  1 Y 1 A LYS 52 ? CG  ? A LYS 66 CG  
10 1 Y 1 A LYS 52 ? CD  ? A LYS 66 CD  
11 1 Y 1 A LYS 52 ? CE  ? A LYS 66 CE  
12 1 Y 1 A LYS 52 ? NZ  ? A LYS 66 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.20.1_4487 1 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MUV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.550 
_cell.length_a_esd                 ? 
_cell.length_b                     140.430 
_cell.length_b_esd                 ? 
_cell.length_c                     130.960 
_cell.length_c_esd                 ? 
_cell.volume                       966431.958 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9MUV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9MUV 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.05 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '5% Tacsimate (pH 4.0), 16% PEG 3350, 0.1 M sodium acetate (pH 4.8), 10 mM oxidized DTT' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RIGAKU SATURN 944' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-02 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          29.61 
_reflns.entry_id                                       9MUV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.2 
_reflns.d_resolution_low                               35.11 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     24648 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.26 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.81 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.2 
_reflns_shell.d_res_low                                     2.279 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2164 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.904 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               36.24 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9MUV 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.20 
_refine.ls_d_res_low                             35.11 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     24632 
_refine.ls_number_reflns_R_free                  3793 
_refine.ls_number_reflns_R_work                  42823 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.11 
_refine.ls_percent_reflns_R_free                 8.14 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1924 
_refine.ls_R_factor_R_free                       0.2343 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1887 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.9702 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2557 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        35.11 
_refine_hist.number_atoms_solvent             253 
_refine_hist.number_atoms_total               3913 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3565 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         95 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0020  ? 3772 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4664  ? 5089 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0454  ? 539  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0026  ? 658  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.4470 ? 1382 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.20 2.23  . . 114 1273 80.92  . . . . 0.2677 . . . . . . . . . . . 0.2726 
'X-RAY DIFFRACTION' 2.23 2.26  . . 128 1442 87.86  . . . . 0.2447 . . . . . . . . . . . 0.3021 
'X-RAY DIFFRACTION' 2.26 2.29  . . 136 1521 93.51  . . . . 0.2526 . . . . . . . . . . . 0.2931 
'X-RAY DIFFRACTION' 2.29 2.32  . . 138 1587 98.97  . . . . 0.2272 . . . . . . . . . . . 0.3003 
'X-RAY DIFFRACTION' 2.32 2.36  . . 143 1602 99.54  . . . . 0.2259 . . . . . . . . . . . 0.2835 
'X-RAY DIFFRACTION' 2.36 2.39  . . 146 1639 99.44  . . . . 0.2216 . . . . . . . . . . . 0.3023 
'X-RAY DIFFRACTION' 2.39 2.43  . . 140 1610 99.21  . . . . 0.2240 . . . . . . . . . . . 0.2562 
'X-RAY DIFFRACTION' 2.43 2.47  . . 135 1576 99.07  . . . . 0.2187 . . . . . . . . . . . 0.2627 
'X-RAY DIFFRACTION' 2.47 2.52  . . 149 1648 99.23  . . . . 0.2192 . . . . . . . . . . . 0.2683 
'X-RAY DIFFRACTION' 2.52 2.57  . . 136 1541 99.05  . . . . 0.2192 . . . . . . . . . . . 0.2486 
'X-RAY DIFFRACTION' 2.57 2.62  . . 145 1628 99.33  . . . . 0.2195 . . . . . . . . . . . 0.2861 
'X-RAY DIFFRACTION' 2.62 2.68  . . 139 1594 99.54  . . . . 0.2133 . . . . . . . . . . . 0.3001 
'X-RAY DIFFRACTION' 2.68 2.74  . . 144 1606 99.09  . . . . 0.2159 . . . . . . . . . . . 0.2691 
'X-RAY DIFFRACTION' 2.74 2.81  . . 141 1607 98.42  . . . . 0.2233 . . . . . . . . . . . 0.2538 
'X-RAY DIFFRACTION' 2.81 2.88  . . 143 1602 98.81  . . . . 0.2152 . . . . . . . . . . . 0.3004 
'X-RAY DIFFRACTION' 2.88 2.97  . . 142 1592 99.43  . . . . 0.2190 . . . . . . . . . . . 0.2496 
'X-RAY DIFFRACTION' 2.97 3.06  . . 140 1613 99.66  . . . . 0.2151 . . . . . . . . . . . 0.2853 
'X-RAY DIFFRACTION' 3.06 3.17  . . 144 1609 99.83  . . . . 0.2041 . . . . . . . . . . . 0.2284 
'X-RAY DIFFRACTION' 3.17 3.30  . . 138 1639 99.89  . . . . 0.1929 . . . . . . . . . . . 0.2470 
'X-RAY DIFFRACTION' 3.30 3.45  . . 146 1595 99.89  . . . . 0.1802 . . . . . . . . . . . 0.2822 
'X-RAY DIFFRACTION' 3.45 3.63  . . 142 1620 100.00 . . . . 0.1656 . . . . . . . . . . . 0.2216 
'X-RAY DIFFRACTION' 3.63 3.86  . . 143 1598 99.89  . . . . 0.1617 . . . . . . . . . . . 0.2037 
'X-RAY DIFFRACTION' 3.86 4.15  . . 144 1635 99.94  . . . . 0.1470 . . . . . . . . . . . 0.1754 
'X-RAY DIFFRACTION' 4.16 4.57  . . 142 1615 99.83  . . . . 0.1355 . . . . . . . . . . . 0.1995 
'X-RAY DIFFRACTION' 4.57 5.23  . . 143 1619 99.77  . . . . 0.1367 . . . . . . . . . . . 0.1496 
'X-RAY DIFFRACTION' 5.23 6.59  . . 142 1622 99.94  . . . . 0.1867 . . . . . . . . . . . 0.1880 
'X-RAY DIFFRACTION' 6.59 35.11 . . 150 1590 98.75  . . . . 0.2067 . . . . . . . . . . . 0.2297 
# 
_struct.entry_id                     9MUV 
_struct.title                        
'Oxidized state of a turn-on thiol-disulfide redox biosensor with a fluorescence-lifetime readout' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9MUV 
_struct_keywords.text            'Fluorescence lifetime, thiol-disulfide redox, FLUORESCENT PROTEIN' 
_struct_keywords.pdbx_keywords   'FLUORESCENT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 2 ? 
K N N 6 ? 
L N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    9MUV 
_struct_ref.pdbx_db_accession          9MUV 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9MUV A 1 ? 251 ? 9MUV -13 ? 237 ? -13 237 
2 1 9MUV B 1 ? 251 ? 9MUV -13 ? 237 ? -13 237 
# 
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_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,K 
2 1 B,G,H,I,J,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 17 ? THR A 23 ? LYS A 3  THR A 9  5 ? 7 
HELX_P HELX_P2  AA2 PRO A 70 ? VAL A 75 ? PRO A 56 VAL A 61 1 ? 6 
HELX_P HELX_P3  AA3 VAL A 80 ? ALA A 84 ? VAL A 66 ALA A 70 5 ? 5 
HELX_P HELX_P4  AA4 PRO A 87 ? HIS A 93 ? PRO A 73 HIS A 79 5 ? 7 
HELX_P HELX_P5  AA5 ASP A 94 ? ALA A 99 ? ASP A 80 ALA A 85 1 ? 6 
HELX_P HELX_P6  AA6 GLY B 18 ? THR B 23 ? GLY B 4  THR B 9  5 ? 6 
HELX_P HELX_P7  AA7 PRO B 70 ? VAL B 75 ? PRO B 56 VAL B 61 5 ? 6 
HELX_P HELX_P8  AA8 VAL B 80 ? ALA B 84 ? VAL B 66 ALA B 70 5 ? 5 
HELX_P HELX_P9  AA9 PRO B 87 ? HIS B 93 ? PRO B 73 HIS B 79 5 ? 7 
HELX_P HELX_P10 AB1 ASP B 94 ? ALA B 99 ? ASP B 80 ALA B 85 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ?    ? A CYS 159 SG ? ? ? 1_555 A CYS 217 SG ? ? A CYS 145 A CYS 203 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf2 disulf ?    ? B CYS 159 SG ? ? ? 1_555 B CYS 217 SG ? ? B CYS 145 B CYS 203 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
covale1 covale both ? A LEU 78  C  ? ? ? 1_555 A SWG 79  N1 ? ? A LEU 64  A SWG 65  1_555 ? ? ? ? ? ? ? 1.429 ? ? 
covale2 covale both ? A SWG 79  C3 ? ? ? 1_555 A VAL 80  N  ? ? A SWG 65  A VAL 66  1_555 ? ? ? ? ? ? ? 1.429 ? ? 
covale3 covale both ? B LEU 78  C  ? ? ? 1_555 B SWG 79  N1 ? ? B LEU 64  B SWG 65  1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale4 covale both ? B SWG 79  C3 ? ? ? 1_555 B VAL 80  N  ? ? B SWG 65  B VAL 66  1_555 ? ? ? ? ? ? ? 1.430 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 SWG A 79  ? .   . .   . SWG A 65  ? 1_555 .   . .   . .     .  .  'SER, TRP, GLY' 1 SWG None Chromophore/chromophore-like 
2 SWG B 79  ? .   . .   . SWG B 65  ? 1_555 .   . .   . .     .  .  'SER, TRP, GLY' 1 SWG None Chromophore/chromophore-like 
3 CYS A 159 ? CYS A 217 ? CYS A 145 ? 1_555 CYS A 203 ? 1_555 SG SG .               . .   None 'Disulfide bridge'           
4 CYS B 159 ? CYS B 217 ? CYS B 145 ? 1_555 CYS B 203 ? 1_555 SG SG .               . .   None 'Disulfide bridge'           
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 MET 100 A . ? MET 86  A PRO 101 A ? PRO 87  A 1 2.52  
2 GLY 160 A . ? GLY 146 A ASP 161 A ? ASP 147 A 1 -0.28 
3 MET 100 B . ? MET 86  B PRO 101 B ? PRO 87  B 1 3.92  
4 GLY 160 B . ? GLY 146 B ASP 161 B ? ASP 147 B 1 -1.09 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 12 ? 
AA2 ? 12 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? anti-parallel 
AA1 11 12 ? parallel      
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? anti-parallel 
AA2 8  9  ? anti-parallel 
AA2 9  10 ? anti-parallel 
AA2 10 11 ? anti-parallel 
AA2 11 12 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  VAL A 25  ? VAL A 36  ? VAL A 11  VAL A 22  
AA1 2  HIS A 39  ? ASP A 50  ? HIS A 25  ASP A 36  
AA1 3  LYS A 55  ? SER A 62  ? LYS A 41  SER A 48  
AA1 4  HIS A 230 ? ALA A 240 ? HIS A 216 ALA A 226 
AA1 5  HIS A 212 ? SER A 221 ? HIS A 198 SER A 207 
AA1 6  VAL A 163 ? ASP A 168 ? VAL A 149 ASP A 154 
AA1 7  GLY A 173 ? ASN A 183 ? GLY A 159 ASN A 169 
AA1 8  VAL A 189 ? PRO A 200 ? VAL A 175 PRO A 186 
AA1 9  TYR A 104 ? PHE A 112 ? TYR A 90  PHE A 98  
AA1 10 ASN A 117 ? GLU A 127 ? ASN A 103 GLU A 113 
AA1 11 THR A 130 ? ILE A 140 ? THR A 116 ILE A 126 
AA1 12 VAL A 25  ? VAL A 36  ? VAL A 11  VAL A 22  
AA2 1  VAL B 26  ? VAL B 36  ? VAL B 12  VAL B 22  
AA2 2  HIS B 39  ? ASP B 50  ? HIS B 25  ASP B 36  
AA2 3  LYS B 55  ? SER B 62  ? LYS B 41  SER B 48  
AA2 4  HIS B 230 ? ALA B 240 ? HIS B 216 ALA B 226 
AA2 5  HIS B 212 ? SER B 221 ? HIS B 198 SER B 207 
AA2 6  VAL B 163 ? ASP B 168 ? VAL B 149 ASP B 154 
AA2 7  GLY B 173 ? ASN B 183 ? GLY B 159 ASN B 169 
AA2 8  VAL B 189 ? PRO B 200 ? VAL B 175 PRO B 186 
AA2 9  TYR B 104 ? PHE B 112 ? TYR B 90  PHE B 98  
AA2 10 ASN B 117 ? GLU B 127 ? ASN B 103 GLU B 113 
AA2 11 THR B 130 ? ILE B 140 ? THR B 116 ILE B 126 
AA2 12 VAL B 26  ? VAL B 36  ? VAL B 12  VAL B 22  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N GLY A 34  ? N GLY A 20  O PHE A 41  ? O PHE A 27  
AA1 2  3  N ASP A 50  ? N ASP A 36  O LYS A 55  ? O LYS A 41  
AA1 3  4  N LEU A 58  ? N LEU A 44  O PHE A 233 ? O PHE A 219 
AA1 4  5  O THR A 238 ? O THR A 224 N SER A 215 ? N SER A 201 
AA1 5  6  O HIS A 212 ? O HIS A 198 N ILE A 165 ? N ILE A 151 
AA1 6  7  N THR A 166 ? N THR A 152 O LYS A 175 ? O LYS A 161 
AA1 7  8  N ALA A 176 ? N ALA A 162 O GLN A 196 ? O GLN A 182 
AA1 8  9  O THR A 199 ? O THR A 185 N VAL A 105 ? N VAL A 91  
AA1 9  10 N ILE A 110 ? N ILE A 96  O TYR A 118 ? O TYR A 104 
AA1 10 11 N LYS A 125 ? N LYS A 111 O VAL A 132 ? O VAL A 118 
AA1 11 12 O GLY A 139 ? O GLY A 125 N ASP A 35  ? N ASP A 21  
AA2 1  2  N GLY B 34  ? N GLY B 20  O PHE B 41  ? O PHE B 27  
AA2 2  3  N ASP B 50  ? N ASP B 36  O LYS B 55  ? O LYS B 41  
AA2 3  4  N LEU B 58  ? N LEU B 44  O PHE B 233 ? O PHE B 219 
AA2 4  5  O LEU B 234 ? O LEU B 220 N LYS B 219 ? N LYS B 205 
AA2 5  6  O HIS B 212 ? O HIS B 198 N ILE B 165 ? N ILE B 151 
AA2 6  7  N THR B 166 ? N THR B 152 O LYS B 175 ? O LYS B 161 
AA2 7  8  N HIS B 182 ? N HIS B 168 O GLN B 190 ? O GLN B 176 
AA2 8  9  O THR B 199 ? O THR B 185 N VAL B 105 ? N VAL B 91  
AA2 9  10 N GLN B 106 ? N GLN B 92  O ALA B 122 ? O ALA B 108 
AA2 10 11 N LYS B 125 ? N LYS B 111 O VAL B 132 ? O VAL B 118 
AA2 11 12 O ILE B 135 ? O ILE B 121 N GLU B 31  ? N GLU B 17  
# 
_pdbx_entry_details.entry_id                   9MUV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           'Chromophore SWG 65 formed from Ser-Trp-Gly in the translated sequence' 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ASP A 172 ? ? -96.34  49.01   
2 1 ASP B 101 ? ? -163.65 -164.66 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A SWG 79 A SWG 65 ? SER chromophore 
2 A SWG 79 A SWG 65 ? TYR chromophore 
3 A SWG 79 A SWG 65 ? GLY chromophore 
4 B SWG 79 B SWG 65 ? SER chromophore 
5 B SWG 79 B SWG 65 ? TYR chromophore 
6 B SWG 79 B SWG 65 ? GLY chromophore 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 519 ? K HOH . 
2 1 A HOH 533 ? K HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_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[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 3.30695393393  12.4738910106   16.0524413226 0.182349365113 ? 0.021410894878    ? 0.107958929445 
? 0.242634384983 ? -0.0155489557821  ? 0.22595865193  ? 8.24594034544 ? -2.684985592     ? 5.64200932576    ? 2.79428519829 ? 
-1.72644900369   ? 5.40574005068 ? -0.272333775331  ? -0.211232371626  ? 0.626870940554  ? 0.0988220180431  ? -0.0745040653217  ? 
0.145273078778    ? -0.608630139016  ? -0.176321596707  ? 0.30230383107    ? 
2  'X-RAY DIFFRACTION' ? refined 13.4200618186  12.1281164032   14.607342341  0.242273377224 ? -0.0131955757596  ? 0.0620966835334 
? 0.201844528648 ? 0.0160239291757   ? 0.202601508467 ? 5.74755442003 ? 2.45818263658    ? 3.55398807859    ? 3.60055341121 ? 
1.3219410319     ? 3.07765818077 ? -0.115236679406  ? 0.103852781768   ? 0.206294553043  ? 0.0841866461964  ? -0.069020067861   ? 
-0.173849004409   ? -0.385017355577  ? 0.00623216137354 ? 0.16581273846    ? 
3  'X-RAY DIFFRACTION' ? refined -4.96344611485 -0.872743781502 8.685110495   0.189578526016 ? -0.0261901261799  ? 0.0169229510603 
? 0.224964479681 ? 0.0230108024758   ? 0.248111157024 ? 6.09108566287 ? 1.24552924227    ? 3.36636363894    ? 5.1738154346  ? 
1.27653970237    ? 6.23267037779 ? 0.261849120411   ? 0.139981684299   ? -0.344574505647 ? 0.347997257529   ? -0.165649087669   ? 
-0.00985380124782 ? 0.227722015656   ? -0.0615248433531 ? -0.228135814509  ? 
4  'X-RAY DIFFRACTION' ? refined 4.60060766844  5.47186896308   22.4259205485 0.323497826373 ? -0.0237256477656  ? 
0.00508905402031 ? 0.266529900086 ? 0.0150716178132   ? 0.243851805353 ? 2.59418807672 ? 0.511355924657   ? 0.670636423469   ? 
1.0481571154  ? -0.114488707362  ? 1.49001377281 ? 0.0826942848198  ? -0.351930848254  ? -0.124983943798 ? 0.259423327456   ? 
-0.0261575135059  ? 0.195668762605    ? 0.0230043758299  ? -0.235541726678  ? -0.0436040764062 ? 
5  'X-RAY DIFFRACTION' ? refined 17.4613384627  5.4854586165    19.5827022858 0.268308963289 ? -0.0165250627474  ? -0.010043428865 
? 0.198576959966 ? 0.0143978720909   ? 0.280922119842 ? 2.38344459308 ? 0.145286680384   ? 0.585105058613   ? 1.19241207777 ? 
0.0131848219844  ? 1.11844056541 ? 0.0753047338722  ? -0.0864423199338 ? 0.0135782695281 ? 0.139577459199   ? -0.0266251372742  ? 
-0.2068993817     ? 0.0673694438926  ? 0.0351417378281  ? -0.0575567432531 ? 
6  'X-RAY DIFFRACTION' ? refined 8.88330858879  -3.87308066733  20.4335033808 0.333218848324 ? -0.0431308525279  ? 
-0.0129906373255 ? 0.286849761959 ? 0.0323171564473   ? 0.27703716678  ? 2.91003872907 ? -0.0915727822425 ? 1.06726567282    ? 
2.04373213517 ? 0.0223352473648  ? 1.21646027328 ? -0.0259878581377 ? -0.127080635111  ? -0.256509749016 ? 0.204367941275   ? 
0.0886004507808   ? 0.0506712248923   ? 0.102156840809   ? -0.196823385493  ? -0.105800443574  ? 
7  'X-RAY DIFFRACTION' ? refined 6.73073969025  4.4106200773    10.9201909476 0.210961315333 ? 0.0151877390972   ? 
-0.0253364652654 ? 0.214631433199 ? 0.0281513102872   ? 0.227101356263 ? 2.32546280668 ? 1.85589959431    ? 0.420801033088   ? 
2.32496548369 ? 0.316520805257   ? 1.51704343055 ? 0.0389649280225  ? 0.00481784275356 ? -0.167678235876 ? -0.0498744909965 ? 
0.0188498372298   ? -0.0952104677286  ? -0.0291592904191 ? -0.062287929706  ? -0.050172842779  ? 
8  'X-RAY DIFFRACTION' ? refined -2.73354357691 -33.7532462098  14.3363179762 0.29626342532  ? -0.0192526844714  ? 
-0.0208155091133 ? 0.18214081163  ? -0.00466574322646 ? 0.19067588449  ? 4.36542740241 ? 0.978952170159   ? -0.977150389996  ? 
2.56575865844 ? -0.319062501149  ? 2.27741096178 ? -0.0664886879465 ? 0.200827468846   ? -0.166354620921 ? -0.335795687412  ? 
0.0453430616428   ? -0.0704064024533  ? -0.0212322428897 ? -0.0125488815275 ? 0.0377490836117  ? 
9  'X-RAY DIFFRACTION' ? refined -6.40132857999 -25.8724466066  20.8608283282 0.32860635562  ? -0.0268541806407  ? 
-0.0116061143267 ? 0.18807346591  ? 0.0170592029355   ? 0.201266531067 ? 3.73849869195 ? -0.523003011048  ? -0.0903574558398 ? 
2.48919608055 ? -0.0765593010147 ? 1.49711746229 ? -0.0164020002128 ? -0.12719772568   ? 0.128842355103  ? 0.194008891657   ? 
-0.00230645837779 ? 0.198411712998    ? -0.23491932988   ? -0.0196314551655 ? 0.0211827968028  ? 
10 'X-RAY DIFFRACTION' ? refined -2.90533589011 -29.5384251926  11.4935951686 0.3129996613   ? 0.000820855640891 ? 0.0301949737143 
? 0.258553421778 ? 0.00393260920738  ? 0.231460879346 ? 2.37136446779 ? 1.99086847828    ? 0.962383122281   ? 3.14030182971 ? 
0.147003740137   ? 1.49063198035 ? -0.31136786194   ? 0.295799795683   ? 0.257997744917  ? -0.440739981009  ? 0.185071380272    ? 
0.161777858849    ? -0.2660546178    ? 0.176994955942   ? 0.137478426587   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1   A 3   ? A 22  A 24  ? ? 
;chain 'A' and (resid 3 through 24 )
;
2  'X-RAY DIFFRACTION' 2  A 23  A 25  ? A 63  A 68  ? ? 
;chain 'A' and (resid 25 through 68 )
;
3  'X-RAY DIFFRACTION' 3  A 64  A 69  ? A 76  A 81  ? ? 
;chain 'A' and (resid 69 through 81 )
;
4  'X-RAY DIFFRACTION' 4  A 77  A 82  ? A 110 A 115 ? ? 
;chain 'A' and (resid 82 through 115 )
;
5  'X-RAY DIFFRACTION' 5  A 111 A 116 ? A 145 A 150 ? ? 
;chain 'A' and (resid 116 through 150 )
;
6  'X-RAY DIFFRACTION' 6  A 146 A 151 ? A 183 A 188 ? ? 
;chain 'A' and (resid 151 through 188 )
;
7  'X-RAY DIFFRACTION' 7  A 184 A 189 ? A 227 A 232 ? ? 
;chain 'A' and (resid 189 through 232 )
;
8  'X-RAY DIFFRACTION' 8  J 1   B 3   ? J 76  B 81  ? ? 
;chain 'B' and (resid 3 through 81 )
;
9  'X-RAY DIFFRACTION' 9  J 77  B 82  ? J 183 B 188 ? ? 
;chain 'B' and (resid 82 through 188 )
;
10 'X-RAY DIFFRACTION' 10 J 184 B 189 ? J 225 B 230 ? ? 
;chain 'B' and (resid 189 through 230 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 533 ? 6.36 . 
2 1 O ? B HOH 520 ? 6.72 . 
# 
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 MET -13 ? A MET 1   
2  1 Y 1 A LYS -12 ? A LYS 2   
3  1 Y 1 A HIS -11 ? A HIS 3   
4  1 Y 1 A HIS -10 ? A HIS 4   
5  1 Y 1 A HIS -9  ? A HIS 5   
6  1 Y 1 A HIS -8  ? A HIS 6   
7  1 Y 1 A HIS -7  ? A HIS 7   
8  1 Y 1 A HIS -6  ? A HIS 8   
9  1 Y 1 A HIS -5  ? A HIS 9   
10 1 Y 1 A GLY -4  ? A GLY 10  
11 1 Y 1 A GLY -3  ? A GLY 11  
12 1 Y 1 A ALA -2  ? A ALA 12  
13 1 Y 1 A SER -1  ? A SER 13  
14 1 Y 1 A MET 0   ? A MET 14  
15 1 Y 1 A VAL 1   ? A VAL 15  
16 1 Y 1 A SER 2   ? A SER 16  
17 1 Y 1 A GLY 231 ? A GLY 245 
18 1 Y 1 A MET 232 ? A MET 246 
19 1 Y 1 A ASP 233 ? A ASP 247 
20 1 Y 1 A GLU 234 ? A GLU 248 
21 1 Y 1 A LEU 235 ? A LEU 249 
22 1 Y 1 A TYR 236 ? A TYR 250 
23 1 Y 1 A LYS 237 ? A LYS 251 
24 1 Y 1 B MET -13 ? B MET 1   
25 1 Y 1 B LYS -12 ? B LYS 2   
26 1 Y 1 B HIS -11 ? B HIS 3   
27 1 Y 1 B HIS -10 ? B HIS 4   
28 1 Y 1 B HIS -9  ? B HIS 5   
29 1 Y 1 B HIS -8  ? B HIS 6   
30 1 Y 1 B HIS -7  ? B HIS 7   
31 1 Y 1 B HIS -6  ? B HIS 8   
32 1 Y 1 B HIS -5  ? B HIS 9   
33 1 Y 1 B GLY -4  ? B GLY 10  
34 1 Y 1 B GLY -3  ? B GLY 11  
35 1 Y 1 B ALA -2  ? B ALA 12  
36 1 Y 1 B SER -1  ? B SER 13  
37 1 Y 1 B MET 0   ? B MET 14  
38 1 Y 1 B VAL 1   ? B VAL 15  
39 1 Y 1 B SER 2   ? B SER 16  
40 1 Y 1 B THR 229 ? B THR 243 
41 1 Y 1 B LEU 230 ? B LEU 244 
42 1 Y 1 B GLY 231 ? B GLY 245 
43 1 Y 1 B MET 232 ? B MET 246 
44 1 Y 1 B ASP 233 ? B ASP 247 
45 1 Y 1 B GLU 234 ? B GLU 248 
46 1 Y 1 B LEU 235 ? B LEU 249 
47 1 Y 1 B TYR 236 ? B TYR 250 
48 1 Y 1 B LYS 237 ? B LYS 251 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ACY C    C N N 1   
ACY O    O N N 2   
ACY OXT  O N N 3   
ACY CH3  C N N 4   
ACY HXT  H N N 5   
ACY H1   H N N 6   
ACY H2   H N N 7   
ACY H3   H N N 8   
ALA N    N N N 9   
ALA CA   C N S 10  
ALA C    C N N 11  
ALA O    O N N 12  
ALA CB   C N N 13  
ALA OXT  O N N 14  
ALA H    H N N 15  
ALA H2   H N N 16  
ALA HA   H N N 17  
ALA HB1  H N N 18  
ALA HB2  H N N 19  
ALA HB3  H N N 20  
ALA HXT  H N N 21  
ARG N    N N N 22  
ARG CA   C N S 23  
ARG C    C N N 24  
ARG O    O N N 25  
ARG CB   C N N 26  
ARG CG   C N N 27  
ARG CD   C N N 28  
ARG NE   N N N 29  
ARG CZ   C N N 30  
ARG NH1  N N N 31  
ARG NH2  N N N 32  
ARG OXT  O N N 33  
ARG H    H N N 34  
ARG H2   H N N 35  
ARG HA   H N N 36  
ARG HB2  H N N 37  
ARG HB3  H N N 38  
ARG HG2  H N N 39  
ARG HG3  H N N 40  
ARG HD2  H N N 41  
ARG HD3  H N N 42  
ARG HE   H N N 43  
ARG HH11 H N N 44  
ARG HH12 H N N 45  
ARG HH21 H N N 46  
ARG HH22 H N N 47  
ARG HXT  H N N 48  
ASN N    N N N 49  
ASN CA   C N S 50  
ASN C    C N N 51  
ASN O    O N N 52  
ASN CB   C N N 53  
ASN CG   C N N 54  
ASN OD1  O N N 55  
ASN ND2  N N N 56  
ASN OXT  O N N 57  
ASN H    H N N 58  
ASN H2   H N N 59  
ASN HA   H N N 60  
ASN HB2  H N N 61  
ASN HB3  H N N 62  
ASN HD21 H N N 63  
ASN HD22 H N N 64  
ASN HXT  H N N 65  
ASP N    N N N 66  
ASP CA   C N S 67  
ASP C    C N N 68  
ASP O    O N N 69  
ASP CB   C N N 70  
ASP CG   C N N 71  
ASP OD1  O N N 72  
ASP OD2  O N N 73  
ASP OXT  O N N 74  
ASP H    H N N 75  
ASP H2   H N N 76  
ASP HA   H N N 77  
ASP HB2  H N N 78  
ASP HB3  H N N 79  
ASP HD2  H N N 80  
ASP HXT  H N N 81  
CYS N    N N N 82  
CYS CA   C N R 83  
CYS C    C N N 84  
CYS O    O N N 85  
CYS CB   C N N 86  
CYS SG   S N N 87  
CYS OXT  O N N 88  
CYS H    H N N 89  
CYS H2   H N N 90  
CYS HA   H N N 91  
CYS HB2  H N N 92  
CYS HB3  H N N 93  
CYS HG   H N N 94  
CYS HXT  H N N 95  
GLN N    N N N 96  
GLN CA   C N S 97  
GLN C    C N N 98  
GLN O    O N N 99  
GLN CB   C N N 100 
GLN CG   C N N 101 
GLN CD   C N N 102 
GLN OE1  O N N 103 
GLN NE2  N N N 104 
GLN OXT  O N N 105 
GLN H    H N N 106 
GLN H2   H N N 107 
GLN HA   H N N 108 
GLN HB2  H N N 109 
GLN HB3  H N N 110 
GLN HG2  H N N 111 
GLN HG3  H N N 112 
GLN HE21 H N N 113 
GLN HE22 H N N 114 
GLN HXT  H N N 115 
GLU N    N N N 116 
GLU CA   C N S 117 
GLU C    C N N 118 
GLU O    O N N 119 
GLU CB   C N N 120 
GLU CG   C N N 121 
GLU CD   C N N 122 
GLU OE1  O N N 123 
GLU OE2  O N N 124 
GLU OXT  O N N 125 
GLU H    H N N 126 
GLU H2   H N N 127 
GLU HA   H N N 128 
GLU HB2  H N N 129 
GLU HB3  H N N 130 
GLU HG2  H N N 131 
GLU HG3  H N N 132 
GLU HE2  H N N 133 
GLU HXT  H N N 134 
GLY N    N N N 135 
GLY CA   C N N 136 
GLY C    C N N 137 
GLY O    O N N 138 
GLY OXT  O N N 139 
GLY H    H N N 140 
GLY H2   H N N 141 
GLY HA2  H N N 142 
GLY HA3  H N N 143 
GLY HXT  H N N 144 
GOL C1   C N N 145 
GOL O1   O N N 146 
GOL C2   C N N 147 
GOL O2   O N N 148 
GOL C3   C N N 149 
GOL O3   O N N 150 
GOL H11  H N N 151 
GOL H12  H N N 152 
GOL HO1  H N N 153 
GOL H2   H N N 154 
GOL HO2  H N N 155 
GOL H31  H N N 156 
GOL H32  H N N 157 
GOL HO3  H N N 158 
HIS N    N N N 159 
HIS CA   C N S 160 
HIS C    C N N 161 
HIS O    O N N 162 
HIS CB   C N N 163 
HIS CG   C Y N 164 
HIS ND1  N Y N 165 
HIS CD2  C Y N 166 
HIS CE1  C Y N 167 
HIS NE2  N Y N 168 
HIS OXT  O N N 169 
HIS H    H N N 170 
HIS H2   H N N 171 
HIS HA   H N N 172 
HIS HB2  H N N 173 
HIS HB3  H N N 174 
HIS HD1  H N N 175 
HIS HD2  H N N 176 
HIS HE1  H N N 177 
HIS HE2  H N N 178 
HIS HXT  H N N 179 
HOH O    O N N 180 
HOH H1   H N N 181 
HOH H2   H N N 182 
ILE N    N N N 183 
ILE CA   C N S 184 
ILE C    C N N 185 
ILE O    O N N 186 
ILE CB   C N S 187 
ILE CG1  C N N 188 
ILE CG2  C N N 189 
ILE CD1  C N N 190 
ILE OXT  O N N 191 
ILE H    H N N 192 
ILE H2   H N N 193 
ILE HA   H N N 194 
ILE HB   H N N 195 
ILE HG12 H N N 196 
ILE HG13 H N N 197 
ILE HG21 H N N 198 
ILE HG22 H N N 199 
ILE HG23 H N N 200 
ILE HD11 H N N 201 
ILE HD12 H N N 202 
ILE HD13 H N N 203 
ILE HXT  H N N 204 
LEU N    N N N 205 
LEU CA   C N S 206 
LEU C    C N N 207 
LEU O    O N N 208 
LEU CB   C N N 209 
LEU CG   C N N 210 
LEU CD1  C N N 211 
LEU CD2  C N N 212 
LEU OXT  O N N 213 
LEU H    H N N 214 
LEU H2   H N N 215 
LEU HA   H N N 216 
LEU HB2  H N N 217 
LEU HB3  H N N 218 
LEU HG   H N N 219 
LEU HD11 H N N 220 
LEU HD12 H N N 221 
LEU HD13 H N N 222 
LEU HD21 H N N 223 
LEU HD22 H N N 224 
LEU HD23 H N N 225 
LEU HXT  H N N 226 
LYS N    N N N 227 
LYS CA   C N S 228 
LYS C    C N N 229 
LYS O    O N N 230 
LYS CB   C N N 231 
LYS CG   C N N 232 
LYS CD   C N N 233 
LYS CE   C N N 234 
LYS NZ   N N N 235 
LYS OXT  O N N 236 
LYS H    H N N 237 
LYS H2   H N N 238 
LYS HA   H N N 239 
LYS HB2  H N N 240 
LYS HB3  H N N 241 
LYS HG2  H N N 242 
LYS HG3  H N N 243 
LYS HD2  H N N 244 
LYS HD3  H N N 245 
LYS HE2  H N N 246 
LYS HE3  H N N 247 
LYS HZ1  H N N 248 
LYS HZ2  H N N 249 
LYS HZ3  H N N 250 
LYS HXT  H N N 251 
MET N    N N N 252 
MET CA   C N S 253 
MET C    C N N 254 
MET O    O N N 255 
MET CB   C N N 256 
MET CG   C N N 257 
MET SD   S N N 258 
MET CE   C N N 259 
MET OXT  O N N 260 
MET H    H N N 261 
MET H2   H N N 262 
MET HA   H N N 263 
MET HB2  H N N 264 
MET HB3  H N N 265 
MET HG2  H N N 266 
MET HG3  H N N 267 
MET HE1  H N N 268 
MET HE2  H N N 269 
MET HE3  H N N 270 
MET HXT  H N N 271 
PEG C1   C N N 272 
PEG O1   O N N 273 
PEG C2   C N N 274 
PEG O2   O N N 275 
PEG C3   C N N 276 
PEG C4   C N N 277 
PEG O4   O N N 278 
PEG H11  H N N 279 
PEG H12  H N N 280 
PEG HO1  H N N 281 
PEG H21  H N N 282 
PEG H22  H N N 283 
PEG H31  H N N 284 
PEG H32  H N N 285 
PEG H41  H N N 286 
PEG H42  H N N 287 
PEG HO4  H N N 288 
PGE C1   C N N 289 
PGE O1   O N N 290 
PGE C2   C N N 291 
PGE O2   O N N 292 
PGE C3   C N N 293 
PGE C4   C N N 294 
PGE O4   O N N 295 
PGE C6   C N N 296 
PGE C5   C N N 297 
PGE O3   O N N 298 
PGE H1   H N N 299 
PGE H12  H N N 300 
PGE HO1  H N N 301 
PGE H2   H N N 302 
PGE H22  H N N 303 
PGE H3   H N N 304 
PGE H32  H N N 305 
PGE H4   H N N 306 
PGE H42  H N N 307 
PGE HO4  H N N 308 
PGE H6   H N N 309 
PGE H62  H N N 310 
PGE H5   H N N 311 
PGE H52  H N N 312 
PHE N    N N N 313 
PHE CA   C N S 314 
PHE C    C N N 315 
PHE O    O N N 316 
PHE CB   C N N 317 
PHE CG   C Y N 318 
PHE CD1  C Y N 319 
PHE CD2  C Y N 320 
PHE CE1  C Y N 321 
PHE CE2  C Y N 322 
PHE CZ   C Y N 323 
PHE OXT  O N N 324 
PHE H    H N N 325 
PHE H2   H N N 326 
PHE HA   H N N 327 
PHE HB2  H N N 328 
PHE HB3  H N N 329 
PHE HD1  H N N 330 
PHE HD2  H N N 331 
PHE HE1  H N N 332 
PHE HE2  H N N 333 
PHE HZ   H N N 334 
PHE HXT  H N N 335 
PRO N    N N N 336 
PRO CA   C N S 337 
PRO C    C N N 338 
PRO O    O N N 339 
PRO CB   C N N 340 
PRO CG   C N N 341 
PRO CD   C N N 342 
PRO OXT  O N N 343 
PRO H    H N N 344 
PRO HA   H N N 345 
PRO HB2  H N N 346 
PRO HB3  H N N 347 
PRO HG2  H N N 348 
PRO HG3  H N N 349 
PRO HD2  H N N 350 
PRO HD3  H N N 351 
PRO HXT  H N N 352 
SER N    N N N 353 
SER CA   C N S 354 
SER C    C N N 355 
SER O    O N N 356 
SER CB   C N N 357 
SER OG   O N N 358 
SER OXT  O N N 359 
SER H    H N N 360 
SER H2   H N N 361 
SER HA   H N N 362 
SER HB2  H N N 363 
SER HB3  H N N 364 
SER HG   H N N 365 
SER HXT  H N N 366 
SWG CD2  C Y N 367 
SWG CE3  C Y N 368 
SWG CZ3  C Y N 369 
SWG CH2  C Y N 370 
SWG CZ2  C Y N 371 
SWG CE2  C Y N 372 
SWG NE1  N Y N 373 
SWG CD1  C Y N 374 
SWG CG   C Y N 375 
SWG CB2  C N N 376 
SWG CA2  C N N 377 
SWG N2   N N N 378 
SWG C2   C N N 379 
SWG O2   O N N 380 
SWG N3   N N N 381 
SWG CA3  C N N 382 
SWG C3   C N N 383 
SWG O3   O N N 384 
SWG OXT  O N N 385 
SWG C1   C N N 386 
SWG CA1  C N R 387 
SWG N1   N N N 388 
SWG CB1  C N N 389 
SWG OG1  O N N 390 
SWG HE3  H N N 391 
SWG HZ3  H N N 392 
SWG HH2  H N N 393 
SWG HZ2  H N N 394 
SWG HE1  H N N 395 
SWG HD1  H N N 396 
SWG HB2  H N N 397 
SWG HA31 H N N 398 
SWG HA32 H N N 399 
SWG HXT  H N N 400 
SWG HA1  H N N 401 
SWG H    H N N 402 
SWG H2   H N N 403 
SWG HB11 H N N 404 
SWG HB12 H N N 405 
SWG HG1  H N N 406 
THR N    N N N 407 
THR CA   C N S 408 
THR C    C N N 409 
THR O    O N N 410 
THR CB   C N R 411 
THR OG1  O N N 412 
THR CG2  C N N 413 
THR OXT  O N N 414 
THR H    H N N 415 
THR H2   H N N 416 
THR HA   H N N 417 
THR HB   H N N 418 
THR HG1  H N N 419 
THR HG21 H N N 420 
THR HG22 H N N 421 
THR HG23 H N N 422 
THR HXT  H N N 423 
TRP N    N N N 424 
TRP CA   C N S 425 
TRP C    C N N 426 
TRP O    O N N 427 
TRP CB   C N N 428 
TRP CG   C Y N 429 
TRP CD1  C Y N 430 
TRP CD2  C Y N 431 
TRP NE1  N Y N 432 
TRP CE2  C Y N 433 
TRP CE3  C Y N 434 
TRP CZ2  C Y N 435 
TRP CZ3  C Y N 436 
TRP CH2  C Y N 437 
TRP OXT  O N N 438 
TRP H    H N N 439 
TRP H2   H N N 440 
TRP HA   H N N 441 
TRP HB2  H N N 442 
TRP HB3  H N N 443 
TRP HD1  H N N 444 
TRP HE1  H N N 445 
TRP HE3  H N N 446 
TRP HZ2  H N N 447 
TRP HZ3  H N N 448 
TRP HH2  H N N 449 
TRP HXT  H N N 450 
TYR N    N N N 451 
TYR CA   C N S 452 
TYR C    C N N 453 
TYR O    O N N 454 
TYR CB   C N N 455 
TYR CG   C Y N 456 
TYR CD1  C Y N 457 
TYR CD2  C Y N 458 
TYR CE1  C Y N 459 
TYR CE2  C Y N 460 
TYR CZ   C Y N 461 
TYR OH   O N N 462 
TYR OXT  O N N 463 
TYR H    H N N 464 
TYR H2   H N N 465 
TYR HA   H N N 466 
TYR HB2  H N N 467 
TYR HB3  H N N 468 
TYR HD1  H N N 469 
TYR HD2  H N N 470 
TYR HE1  H N N 471 
TYR HE2  H N N 472 
TYR HH   H N N 473 
TYR HXT  H N N 474 
VAL N    N N N 475 
VAL CA   C N S 476 
VAL C    C N N 477 
VAL O    O N N 478 
VAL CB   C N N 479 
VAL CG1  C N N 480 
VAL CG2  C N N 481 
VAL OXT  O N N 482 
VAL H    H N N 483 
VAL H2   H N N 484 
VAL HA   H N N 485 
VAL HB   H N N 486 
VAL HG11 H N N 487 
VAL HG12 H N N 488 
VAL HG13 H N N 489 
VAL HG21 H N N 490 
VAL HG22 H N N 491 
VAL HG23 H N N 492 
VAL HXT  H N N 493 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ACY C   O    doub N N 1   
ACY C   OXT  sing N N 2   
ACY C   CH3  sing N N 3   
ACY OXT HXT  sing N N 4   
ACY CH3 H1   sing N N 5   
ACY CH3 H2   sing N N 6   
ACY CH3 H3   sing N N 7   
ALA N   CA   sing N N 8   
ALA N   H    sing N N 9   
ALA N   H2   sing N N 10  
ALA CA  C    sing N N 11  
ALA CA  CB   sing N N 12  
ALA CA  HA   sing N N 13  
ALA C   O    doub N N 14  
ALA C   OXT  sing N N 15  
ALA CB  HB1  sing N N 16  
ALA CB  HB2  sing N N 17  
ALA CB  HB3  sing N N 18  
ALA OXT HXT  sing N N 19  
ARG N   CA   sing N N 20  
ARG N   H    sing N N 21  
ARG N   H2   sing N N 22  
ARG CA  C    sing N N 23  
ARG CA  CB   sing N N 24  
ARG CA  HA   sing N N 25  
ARG C   O    doub N N 26  
ARG C   OXT  sing N N 27  
ARG CB  CG   sing N N 28  
ARG CB  HB2  sing N N 29  
ARG CB  HB3  sing N N 30  
ARG CG  CD   sing N N 31  
ARG CG  HG2  sing N N 32  
ARG CG  HG3  sing N N 33  
ARG CD  NE   sing N N 34  
ARG CD  HD2  sing N N 35  
ARG CD  HD3  sing N N 36  
ARG NE  CZ   sing N N 37  
ARG NE  HE   sing N N 38  
ARG CZ  NH1  sing N N 39  
ARG CZ  NH2  doub N N 40  
ARG NH1 HH11 sing N N 41  
ARG NH1 HH12 sing N N 42  
ARG NH2 HH21 sing N N 43  
ARG NH2 HH22 sing N N 44  
ARG OXT HXT  sing N N 45  
ASN N   CA   sing N N 46  
ASN N   H    sing N N 47  
ASN N   H2   sing N N 48  
ASN CA  C    sing N N 49  
ASN CA  CB   sing N N 50  
ASN CA  HA   sing N N 51  
ASN C   O    doub N N 52  
ASN C   OXT  sing N N 53  
ASN CB  CG   sing N N 54  
ASN CB  HB2  sing N N 55  
ASN CB  HB3  sing N N 56  
ASN CG  OD1  doub N N 57  
ASN CG  ND2  sing N N 58  
ASN ND2 HD21 sing N N 59  
ASN ND2 HD22 sing N N 60  
ASN OXT HXT  sing N N 61  
ASP N   CA   sing N N 62  
ASP N   H    sing N N 63  
ASP N   H2   sing N N 64  
ASP CA  C    sing N N 65  
ASP CA  CB   sing N N 66  
ASP CA  HA   sing N N 67  
ASP C   O    doub N N 68  
ASP C   OXT  sing N N 69  
ASP CB  CG   sing N N 70  
ASP CB  HB2  sing N N 71  
ASP CB  HB3  sing N N 72  
ASP CG  OD1  doub N N 73  
ASP CG  OD2  sing N N 74  
ASP OD2 HD2  sing N N 75  
ASP OXT HXT  sing N N 76  
CYS N   CA   sing N N 77  
CYS N   H    sing N N 78  
CYS N   H2   sing N N 79  
CYS CA  C    sing N N 80  
CYS CA  CB   sing N N 81  
CYS CA  HA   sing N N 82  
CYS C   O    doub N N 83  
CYS C   OXT  sing N N 84  
CYS CB  SG   sing N N 85  
CYS CB  HB2  sing N N 86  
CYS CB  HB3  sing N N 87  
CYS SG  HG   sing N N 88  
CYS OXT HXT  sing N N 89  
GLN N   CA   sing N N 90  
GLN N   H    sing N N 91  
GLN N   H2   sing N N 92  
GLN CA  C    sing N N 93  
GLN CA  CB   sing N N 94  
GLN CA  HA   sing N N 95  
GLN C   O    doub N N 96  
GLN C   OXT  sing N N 97  
GLN CB  CG   sing N N 98  
GLN CB  HB2  sing N N 99  
GLN CB  HB3  sing N N 100 
GLN CG  CD   sing N N 101 
GLN CG  HG2  sing N N 102 
GLN CG  HG3  sing N N 103 
GLN CD  OE1  doub N N 104 
GLN CD  NE2  sing N N 105 
GLN NE2 HE21 sing N N 106 
GLN NE2 HE22 sing N N 107 
GLN OXT HXT  sing N N 108 
GLU N   CA   sing N N 109 
GLU N   H    sing N N 110 
GLU N   H2   sing N N 111 
GLU CA  C    sing N N 112 
GLU CA  CB   sing N N 113 
GLU CA  HA   sing N N 114 
GLU C   O    doub N N 115 
GLU C   OXT  sing N N 116 
GLU CB  CG   sing N N 117 
GLU CB  HB2  sing N N 118 
GLU CB  HB3  sing N N 119 
GLU CG  CD   sing N N 120 
GLU CG  HG2  sing N N 121 
GLU CG  HG3  sing N N 122 
GLU CD  OE1  doub N N 123 
GLU CD  OE2  sing N N 124 
GLU OE2 HE2  sing N N 125 
GLU OXT HXT  sing N N 126 
GLY N   CA   sing N N 127 
GLY N   H    sing N N 128 
GLY N   H2   sing N N 129 
GLY CA  C    sing N N 130 
GLY CA  HA2  sing N N 131 
GLY CA  HA3  sing N N 132 
GLY C   O    doub N N 133 
GLY C   OXT  sing N N 134 
GLY OXT HXT  sing N N 135 
GOL C1  O1   sing N N 136 
GOL C1  C2   sing N N 137 
GOL C1  H11  sing N N 138 
GOL C1  H12  sing N N 139 
GOL O1  HO1  sing N N 140 
GOL C2  O2   sing N N 141 
GOL C2  C3   sing N N 142 
GOL C2  H2   sing N N 143 
GOL O2  HO2  sing N N 144 
GOL C3  O3   sing N N 145 
GOL C3  H31  sing N N 146 
GOL C3  H32  sing N N 147 
GOL O3  HO3  sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
LEU N   CA   sing N N 193 
LEU N   H    sing N N 194 
LEU N   H2   sing N N 195 
LEU CA  C    sing N N 196 
LEU CA  CB   sing N N 197 
LEU CA  HA   sing N N 198 
LEU C   O    doub N N 199 
LEU C   OXT  sing N N 200 
LEU CB  CG   sing N N 201 
LEU CB  HB2  sing N N 202 
LEU CB  HB3  sing N N 203 
LEU CG  CD1  sing N N 204 
LEU CG  CD2  sing N N 205 
LEU CG  HG   sing N N 206 
LEU CD1 HD11 sing N N 207 
LEU CD1 HD12 sing N N 208 
LEU CD1 HD13 sing N N 209 
LEU CD2 HD21 sing N N 210 
LEU CD2 HD22 sing N N 211 
LEU CD2 HD23 sing N N 212 
LEU OXT HXT  sing N N 213 
LYS N   CA   sing N N 214 
LYS N   H    sing N N 215 
LYS N   H2   sing N N 216 
LYS CA  C    sing N N 217 
LYS CA  CB   sing N N 218 
LYS CA  HA   sing N N 219 
LYS C   O    doub N N 220 
LYS C   OXT  sing N N 221 
LYS CB  CG   sing N N 222 
LYS CB  HB2  sing N N 223 
LYS CB  HB3  sing N N 224 
LYS CG  CD   sing N N 225 
LYS CG  HG2  sing N N 226 
LYS CG  HG3  sing N N 227 
LYS CD  CE   sing N N 228 
LYS CD  HD2  sing N N 229 
LYS CD  HD3  sing N N 230 
LYS CE  NZ   sing N N 231 
LYS CE  HE2  sing N N 232 
LYS CE  HE3  sing N N 233 
LYS NZ  HZ1  sing N N 234 
LYS NZ  HZ2  sing N N 235 
LYS NZ  HZ3  sing N N 236 
LYS OXT HXT  sing N N 237 
MET N   CA   sing N N 238 
MET N   H    sing N N 239 
MET N   H2   sing N N 240 
MET CA  C    sing N N 241 
MET CA  CB   sing N N 242 
MET CA  HA   sing N N 243 
MET C   O    doub N N 244 
MET C   OXT  sing N N 245 
MET CB  CG   sing N N 246 
MET CB  HB2  sing N N 247 
MET CB  HB3  sing N N 248 
MET CG  SD   sing N N 249 
MET CG  HG2  sing N N 250 
MET CG  HG3  sing N N 251 
MET SD  CE   sing N N 252 
MET CE  HE1  sing N N 253 
MET CE  HE2  sing N N 254 
MET CE  HE3  sing N N 255 
MET OXT HXT  sing N N 256 
PEG C1  O1   sing N N 257 
PEG C1  C2   sing N N 258 
PEG C1  H11  sing N N 259 
PEG C1  H12  sing N N 260 
PEG O1  HO1  sing N N 261 
PEG C2  O2   sing N N 262 
PEG C2  H21  sing N N 263 
PEG C2  H22  sing N N 264 
PEG O2  C3   sing N N 265 
PEG C3  C4   sing N N 266 
PEG C3  H31  sing N N 267 
PEG C3  H32  sing N N 268 
PEG C4  O4   sing N N 269 
PEG C4  H41  sing N N 270 
PEG C4  H42  sing N N 271 
PEG O4  HO4  sing N N 272 
PGE C1  O1   sing N N 273 
PGE C1  C2   sing N N 274 
PGE C1  H1   sing N N 275 
PGE C1  H12  sing N N 276 
PGE O1  HO1  sing N N 277 
PGE C2  O2   sing N N 278 
PGE C2  H2   sing N N 279 
PGE C2  H22  sing N N 280 
PGE O2  C3   sing N N 281 
PGE C3  C4   sing N N 282 
PGE C3  H3   sing N N 283 
PGE C3  H32  sing N N 284 
PGE C4  O3   sing N N 285 
PGE C4  H4   sing N N 286 
PGE C4  H42  sing N N 287 
PGE O4  C6   sing N N 288 
PGE O4  HO4  sing N N 289 
PGE C6  C5   sing N N 290 
PGE C6  H6   sing N N 291 
PGE C6  H62  sing N N 292 
PGE C5  O3   sing N N 293 
PGE C5  H5   sing N N 294 
PGE C5  H52  sing N N 295 
PHE N   CA   sing N N 296 
PHE N   H    sing N N 297 
PHE N   H2   sing N N 298 
PHE CA  C    sing N N 299 
PHE CA  CB   sing N N 300 
PHE CA  HA   sing N N 301 
PHE C   O    doub N N 302 
PHE C   OXT  sing N N 303 
PHE CB  CG   sing N N 304 
PHE CB  HB2  sing N N 305 
PHE CB  HB3  sing N N 306 
PHE CG  CD1  doub Y N 307 
PHE CG  CD2  sing Y N 308 
PHE CD1 CE1  sing Y N 309 
PHE CD1 HD1  sing N N 310 
PHE CD2 CE2  doub Y N 311 
PHE CD2 HD2  sing N N 312 
PHE CE1 CZ   doub Y N 313 
PHE CE1 HE1  sing N N 314 
PHE CE2 CZ   sing Y N 315 
PHE CE2 HE2  sing N N 316 
PHE CZ  HZ   sing N N 317 
PHE OXT HXT  sing N N 318 
PRO N   CA   sing N N 319 
PRO N   CD   sing N N 320 
PRO N   H    sing N N 321 
PRO CA  C    sing N N 322 
PRO CA  CB   sing N N 323 
PRO CA  HA   sing N N 324 
PRO C   O    doub N N 325 
PRO C   OXT  sing N N 326 
PRO CB  CG   sing N N 327 
PRO CB  HB2  sing N N 328 
PRO CB  HB3  sing N N 329 
PRO CG  CD   sing N N 330 
PRO CG  HG2  sing N N 331 
PRO CG  HG3  sing N N 332 
PRO CD  HD2  sing N N 333 
PRO CD  HD3  sing N N 334 
PRO OXT HXT  sing N N 335 
SER N   CA   sing N N 336 
SER N   H    sing N N 337 
SER N   H2   sing N N 338 
SER CA  C    sing N N 339 
SER CA  CB   sing N N 340 
SER CA  HA   sing N N 341 
SER C   O    doub N N 342 
SER C   OXT  sing N N 343 
SER CB  OG   sing N N 344 
SER CB  HB2  sing N N 345 
SER CB  HB3  sing N N 346 
SER OG  HG   sing N N 347 
SER OXT HXT  sing N N 348 
SWG CD2 CE3  sing Y N 349 
SWG CD2 CE2  doub Y N 350 
SWG CD2 CG   sing Y N 351 
SWG CE3 CZ3  doub Y N 352 
SWG CZ3 CH2  sing Y N 353 
SWG CH2 CZ2  doub Y N 354 
SWG CZ2 CE2  sing Y N 355 
SWG CE2 NE1  sing Y N 356 
SWG NE1 CD1  sing Y N 357 
SWG CD1 CG   doub Y N 358 
SWG CG  CB2  sing N N 359 
SWG CB2 CA2  doub N N 360 
SWG CA2 N2   sing N N 361 
SWG CA2 C2   sing N N 362 
SWG N2  C1   doub N N 363 
SWG C2  O2   doub N N 364 
SWG C2  N3   sing N N 365 
SWG N3  CA3  sing N Z 366 
SWG N3  C1   sing N N 367 
SWG CA3 C3   sing N N 368 
SWG C3  O3   doub N N 369 
SWG C3  OXT  sing N N 370 
SWG C1  CA1  sing N N 371 
SWG CA1 N1   sing N N 372 
SWG CA1 CB1  sing N N 373 
SWG CB1 OG1  sing N N 374 
SWG CE3 HE3  sing N N 375 
SWG CZ3 HZ3  sing N N 376 
SWG CH2 HH2  sing N N 377 
SWG CZ2 HZ2  sing N N 378 
SWG NE1 HE1  sing N N 379 
SWG CD1 HD1  sing N N 380 
SWG CB2 HB2  sing N N 381 
SWG CA3 HA31 sing N N 382 
SWG CA3 HA32 sing N N 383 
SWG CA1 HA1  sing N N 384 
SWG N1  H    sing N N 385 
SWG N1  H2   sing N N 386 
SWG CB1 HB11 sing N N 387 
SWG CB1 HB12 sing N N 388 
SWG OG1 HG1  sing N N 389 
SWG OXT HXT  sing N N 390 
THR N   CA   sing N N 391 
THR N   H    sing N N 392 
THR N   H2   sing N N 393 
THR CA  C    sing N N 394 
THR CA  CB   sing N N 395 
THR CA  HA   sing N N 396 
THR C   O    doub N N 397 
THR C   OXT  sing N N 398 
THR CB  OG1  sing N N 399 
THR CB  CG2  sing N N 400 
THR CB  HB   sing N N 401 
THR OG1 HG1  sing N N 402 
THR CG2 HG21 sing N N 403 
THR CG2 HG22 sing N N 404 
THR CG2 HG23 sing N N 405 
THR OXT HXT  sing N N 406 
TRP N   CA   sing N N 407 
TRP N   H    sing N N 408 
TRP N   H2   sing N N 409 
TRP CA  C    sing N N 410 
TRP CA  CB   sing N N 411 
TRP CA  HA   sing N N 412 
TRP C   O    doub N N 413 
TRP C   OXT  sing N N 414 
TRP CB  CG   sing N N 415 
TRP CB  HB2  sing N N 416 
TRP CB  HB3  sing N N 417 
TRP CG  CD1  doub Y N 418 
TRP CG  CD2  sing Y N 419 
TRP CD1 NE1  sing Y N 420 
TRP CD1 HD1  sing N N 421 
TRP CD2 CE2  doub Y N 422 
TRP CD2 CE3  sing Y N 423 
TRP NE1 CE2  sing Y N 424 
TRP NE1 HE1  sing N N 425 
TRP CE2 CZ2  sing Y N 426 
TRP CE3 CZ3  doub Y N 427 
TRP CE3 HE3  sing N N 428 
TRP CZ2 CH2  doub Y N 429 
TRP CZ2 HZ2  sing N N 430 
TRP CZ3 CH2  sing Y N 431 
TRP CZ3 HZ3  sing N N 432 
TRP CH2 HH2  sing N N 433 
TRP OXT HXT  sing N N 434 
TYR N   CA   sing N N 435 
TYR N   H    sing N N 436 
TYR N   H2   sing N N 437 
TYR CA  C    sing N N 438 
TYR CA  CB   sing N N 439 
TYR CA  HA   sing N N 440 
TYR C   O    doub N N 441 
TYR C   OXT  sing N N 442 
TYR CB  CG   sing N N 443 
TYR CB  HB2  sing N N 444 
TYR CB  HB3  sing N N 445 
TYR CG  CD1  doub Y N 446 
TYR CG  CD2  sing Y N 447 
TYR CD1 CE1  sing Y N 448 
TYR CD1 HD1  sing N N 449 
TYR CD2 CE2  doub Y N 450 
TYR CD2 HD2  sing N N 451 
TYR CE1 CZ   doub Y N 452 
TYR CE1 HE1  sing N N 453 
TYR CE2 CZ   sing Y N 454 
TYR CE2 HE2  sing N N 455 
TYR CZ  OH   sing N N 456 
TYR OH  HH   sing N N 457 
TYR OXT HXT  sing N N 458 
VAL N   CA   sing N N 459 
VAL N   H    sing N N 460 
VAL N   H2   sing N N 461 
VAL CA  C    sing N N 462 
VAL CA  CB   sing N N 463 
VAL CA  HA   sing N N 464 
VAL C   O    doub N N 465 
VAL C   OXT  sing N N 466 
VAL CB  CG1  sing N N 467 
VAL CB  CG2  sing N N 468 
VAL CB  HB   sing N N 469 
VAL CG1 HG11 sing N N 470 
VAL CG1 HG12 sing N N 471 
VAL CG1 HG13 sing N N 472 
VAL CG2 HG21 sing N N 473 
VAL CG2 HG22 sing N N 474 
VAL CG2 HG23 sing N N 475 
VAL OXT HXT  sing N N 476 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R01GM124038 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9MUS 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9MUV 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.019029 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007121 
_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]   0.007636 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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    . LYS A 1 17  ? -15.13904 9.16648   12.83072 1.000 58.93440  ? 3   LYS A N    1 
ATOM   2    C CA   A LYS A 1 17  ? -14.15328 8.11237   12.61921 0.853 51.84138  ? 3   LYS A CA   1 
ATOM   3    C CA   B LYS A 1 17  ? -14.15462 8.11394   12.61502 0.147 52.12812  ? 3   LYS A CA   1 
ATOM   4    C C    . LYS A 1 17  ? -12.75069 8.70438   12.53352 1.000 49.91347  ? 3   LYS A C    1 
ATOM   5    O O    . LYS A 1 17  ? -12.45181 9.50061   11.64159 1.000 45.40768  ? 3   LYS A O    1 
ATOM   6    C CB   A LYS A 1 17  ? -14.47540 7.31805   11.34993 0.853 55.43432  ? 3   LYS A CB   1 
ATOM   7    C CB   B LYS A 1 17  ? -14.48379 7.33533   11.33757 0.147 55.32542  ? 3   LYS A CB   1 
ATOM   8    C CG   A LYS A 1 17  ? -13.54897 6.12844   11.09540 0.853 53.97321  ? 3   LYS A CG   1 
ATOM   9    C CG   B LYS A 1 17  ? -13.47824 6.25256   10.97127 0.147 53.74234  ? 3   LYS A CG   1 
ATOM   10   C CD   A LYS A 1 17  ? -13.46934 5.20235   12.30324 0.853 53.69926  ? 3   LYS A CD   1 
ATOM   11   C CD   B LYS A 1 17  ? -13.33472 5.21825   12.07389 0.147 53.59313  ? 3   LYS A CD   1 
ATOM   12   C CE   A LYS A 1 17  ? -12.72234 3.91645   11.97925 0.853 55.33234  ? 3   LYS A CE   1 
ATOM   13   C CE   B LYS A 1 17  ? -12.43565 4.07454   11.63773 0.147 54.35360  ? 3   LYS A CE   1 
ATOM   14   N NZ   A LYS A 1 17  ? -13.48135 3.05148   11.03009 0.853 57.45006  ? 3   LYS A NZ   1 
ATOM   15   N NZ   B LYS A 1 17  ? -12.17745 3.11278   12.74023 0.147 52.30829  ? 3   LYS A NZ   1 
ATOM   16   H HA   . LYS A 1 17  ? -14.17813 7.49374   13.36593 1.000 62.60969  ? 3   LYS A HA   1 
ATOM   17   H HB2  A LYS A 1 17  ? -15.37998 6.97518   11.42110 0.853 66.57712  ? 3   LYS A HB2  1 
ATOM   18   H HB2  B LYS A 1 17  ? -15.34577 6.90566   11.45278 0.147 66.44644  ? 3   LYS A HB2  1 
ATOM   19   H HB3  A LYS A 1 17  ? -14.40513 7.91284   10.58692 0.853 66.57712  ? 3   LYS A HB3  1 
ATOM   20   H HB3  B LYS A 1 17  ? -14.52122 7.96086   10.59717 0.147 66.44644  ? 3   LYS A HB3  1 
ATOM   21   H HG2  A LYS A 1 17  ? -13.88457 5.61695   10.34264 0.853 64.82380  ? 3   LYS A HG2  1 
ATOM   22   H HG2  B LYS A 1 17  ? -13.77508 5.79917   10.16676 0.147 64.54674  ? 3   LYS A HG2  1 
ATOM   23   H HG3  A LYS A 1 17  ? -12.65564 6.45401   10.90342 0.853 64.82380  ? 3   LYS A HG3  1 
ATOM   24   H HG3  B LYS A 1 17  ? -12.61035 6.65919   10.82189 0.147 64.54674  ? 3   LYS A HG3  1 
ATOM   25   H HD2  A LYS A 1 17  ? -13.00007 5.65340   13.02244 0.853 64.49506  ? 3   LYS A HD2  1 
ATOM   26   H HD2  B LYS A 1 17  ? -12.94291 5.63429   12.85766 0.147 64.36770  ? 3   LYS A HD2  1 
ATOM   27   H HD3  A LYS A 1 17  ? -14.36682 4.96895   12.58776 0.853 64.49506  ? 3   LYS A HD3  1 
ATOM   28   H HD3  B LYS A 1 17  ? -14.20761 4.85582   12.29204 0.147 64.36770  ? 3   LYS A HD3  1 
ATOM   29   H HE2  A LYS A 1 17  ? -11.86976 4.13669   11.57244 0.853 66.45475  ? 3   LYS A HE2  1 
ATOM   30   H HE2  B LYS A 1 17  ? -12.86164 3.59380   10.91087 0.147 65.28026  ? 3   LYS A HE2  1 
ATOM   31   H HE3  A LYS A 1 17  ? -12.57992 3.41547   12.79756 0.853 66.45475  ? 3   LYS A HE3  1 
ATOM   32   H HE3  B LYS A 1 17  ? -11.58367 4.43328   11.34389 0.147 65.28026  ? 3   LYS A HE3  1 
ATOM   33   H HZ1  A LYS A 1 17  ? -13.03223 2.29809   10.87912 0.853 68.99601  ? 3   LYS A HZ1  1 
ATOM   34   H HZ1  B LYS A 1 17  ? -11.61523 2.47954   12.46634 0.147 62.82589  ? 3   LYS A HZ1  1 
ATOM   35   H HZ2  A LYS A 1 17  ? -14.27758 2.84942   11.37255 0.853 68.99601  ? 3   LYS A HZ2  1 
ATOM   36   H HZ2  B LYS A 1 17  ? -11.81868 3.53636   13.43590 0.147 62.82589  ? 3   LYS A HZ2  1 
ATOM   37   H HZ3  A LYS A 1 17  ? -13.59888 3.47743   10.25752 0.853 68.99601  ? 3   LYS A HZ3  1 
ATOM   38   H HZ3  B LYS A 1 17  ? -12.93973 2.73127   12.99612 0.147 62.82589  ? 3   LYS A HZ3  1 
ATOM   39   N N    . GLY A 1 18  ? -11.89236 8.30651   13.47474 1.000 41.68103  ? 4   GLY A N    1 
ATOM   40   C CA   . GLY A 1 18  ? -10.53618 8.82422   13.49703 1.000 36.38208  ? 4   GLY A CA   1 
ATOM   41   C C    . GLY A 1 18  ? -9.76125  8.52475   12.23046 1.000 38.86445  ? 4   GLY A C    1 
ATOM   42   O O    . GLY A 1 18  ? -8.82271  9.24856   11.88682 1.000 35.37782  ? 4   GLY A O    1 
ATOM   43   H H    . GLY A 1 18  ? -12.07243 7.74534   14.10105 1.000 50.07318  ? 4   GLY A H    1 
ATOM   44   H HA2  . GLY A 1 18  ? -10.56566 9.78683   13.61285 1.000 43.71444  ? 4   GLY A HA2  1 
ATOM   45   H HA3  . GLY A 1 18  ? -10.05836 8.43077   14.24387 1.000 43.71444  ? 4   GLY A HA3  1 
ATOM   46   N N    . GLU A 1 19  ? -10.13000 7.45433   11.52372 1.000 36.99908  ? 5   GLU A N    1 
ATOM   47   C CA   . GLU A 1 19  ? -9.46315  7.14775   10.26396 1.000 37.69920  ? 5   GLU A CA   1 
ATOM   48   C C    . GLU A 1 19  ? -9.69287  8.24581   9.23488  1.000 33.93409  ? 5   GLU A C    1 
ATOM   49   O O    . GLU A 1 19  ? -8.81031  8.52158   8.41511  1.000 36.85744  ? 5   GLU A O    1 
ATOM   50   C CB   . GLU A 1 19  ? -9.94958  5.80269   9.72353  1.000 40.43949  ? 5   GLU A CB   1 
ATOM   51   H H    . GLU A 1 19  ? -10.75031 6.90269   11.74845 1.000 44.45483  ? 5   GLU A H    1 
ATOM   52   H HA   . GLU A 1 19  ? -8.50899  7.07649   10.42329 1.000 45.29498  ? 5   GLU A HA   1 
ATOM   53   N N    . GLU A 1 20  ? -10.86164 8.89075   9.26678  1.000 36.31557  ? 6   GLU A N    1 
ATOM   54   C CA   . GLU A 1 20  ? -11.14348 9.96245   8.31926  1.000 36.41933  ? 6   GLU A CA   1 
ATOM   55   C C    . GLU A 1 20  ? -10.14153 11.10510  8.42591  1.000 36.31163  ? 6   GLU A C    1 
ATOM   56   O O    . GLU A 1 20  ? -9.96841  11.85579  7.45956  1.000 33.93517  ? 6   GLU A O    1 
ATOM   57   C CB   . GLU A 1 20  ? -12.56103 10.49420  8.53744  1.000 34.53680  ? 6   GLU A CB   1 
ATOM   58   H H    . GLU A 1 20  ? -11.49841 8.72707   9.82116  1.000 43.63462  ? 6   GLU A H    1 
ATOM   59   H HA   . GLU A 1 20  ? -11.09101 9.60251   7.42004  1.000 43.75913  ? 6   GLU A HA   1 
ATOM   60   N N    . LEU A 1 21  ? -9.47838  11.25385  9.57375  1.000 32.97361  ? 7   LEU A N    1 
ATOM   61   C CA   . LEU A 1 21  ? -8.50775  12.32495  9.75701  1.000 32.03303  ? 7   LEU A CA   1 
ATOM   62   C C    . LEU A 1 21  ? -7.21670  12.09209  8.98381  1.000 31.11168  ? 7   LEU A C    1 
ATOM   63   O O    . LEU A 1 21  ? -6.41778  13.02627  8.85768  1.000 32.70132  ? 7   LEU A O    1 
ATOM   64   C CB   . LEU A 1 21  ? -8.18927  12.48343  11.24596 1.000 27.22986  ? 7   LEU A CB   1 
ATOM   65   C CG   . LEU A 1 21  ? -9.38484  12.77138  12.15430 1.000 31.04304  ? 7   LEU A CG   1 
ATOM   66   C CD1  . LEU A 1 21  ? -9.01020  12.58348  13.61602 1.000 34.89947  ? 7   LEU A CD1  1 
ATOM   67   C CD2  . LEU A 1 21  ? -9.91542  14.17808  11.91454 1.000 35.42092  ? 7   LEU A CD2  1 
ATOM   68   H H    . LEU A 1 21  ? -9.57462  10.74559  10.26078 1.000 39.62427  ? 7   LEU A H    1 
ATOM   69   H HA   . LEU A 1 21  ? -8.89767  13.15394  9.43822  1.000 38.49558  ? 7   LEU A HA   1 
ATOM   70   H HB2  . LEU A 1 21  ? -7.78169  11.66047  11.55823 1.000 32.73177  ? 7   LEU A HB2  1 
ATOM   71   H HB3  . LEU A 1 21  ? -7.56697  13.22071  11.34624 1.000 32.73177  ? 7   LEU A HB3  1 
ATOM   72   H HG   . LEU A 1 21  ? -10.09333 12.14291  11.94460 1.000 37.30759  ? 7   LEU A HG   1 
ATOM   73   H HD11 . LEU A 1 21  ? -9.74140  12.89511  14.17201 1.000 41.93530  ? 7   LEU A HD11 1 
ATOM   74   H HD12 . LEU A 1 21  ? -8.84681  11.64179  13.78162 1.000 41.93530  ? 7   LEU A HD12 1 
ATOM   75   H HD13 . LEU A 1 21  ? -8.20896  13.09647  13.80513 1.000 41.93530  ? 7   LEU A HD13 1 
ATOM   76   H HD21 . LEU A 1 21  ? -9.20437  14.81646  12.08120 1.000 42.56105  ? 7   LEU A HD21 1 
ATOM   77   H HD22 . LEU A 1 21  ? -10.21560 14.24990  10.99495 1.000 42.56105  ? 7   LEU A HD22 1 
ATOM   78   H HD23 . LEU A 1 21  ? -10.65646 14.34326  12.51825 1.000 42.56105  ? 7   LEU A HD23 1 
ATOM   79   N N    . PHE A 1 22  ? -6.99784  10.88466  8.46124  1.000 29.98165  ? 8   PHE A N    1 
ATOM   80   C CA   . PHE A 1 22  ? -5.74988  10.52266  7.80109  1.000 28.56267  ? 8   PHE A CA   1 
ATOM   81   C C    . PHE A 1 22  ? -5.91558  10.31842  6.29869  1.000 28.86543  ? 8   PHE A C    1 
ATOM   82   O O    . PHE A 1 22  ? -5.01412  9.77392   5.65250  1.000 29.98233  ? 8   PHE A O    1 
ATOM   83   C CB   . PHE A 1 22  ? -5.17393  9.25524   8.43929  1.000 32.63628  ? 8   PHE A CB   1 
ATOM   84   C CG   . PHE A 1 22  ? -4.71704  9.44268   9.85784  1.000 29.44776  ? 8   PHE A CG   1 
ATOM   85   C CD1  . PHE A 1 22  ? -5.63212  9.47452   10.89731 1.000 31.03286  ? 8   PHE A CD1  1 
ATOM   86   C CD2  . PHE A 1 22  ? -3.37132  9.58049   10.15230 1.000 28.17185  ? 8   PHE A CD2  1 
ATOM   87   C CE1  . PHE A 1 22  ? -5.21321  9.64570   12.20184 1.000 26.87936  ? 8   PHE A CE1  1 
ATOM   88   C CE2  . PHE A 1 22  ? -2.94642  9.75072   11.45805 1.000 31.39597  ? 8   PHE A CE2  1 
ATOM   89   C CZ   . PHE A 1 22  ? -3.86864  9.78339   12.48253 1.000 25.13066  ? 8   PHE A CZ   1 
ATOM   90   H H    . PHE A 1 22  ? -7.57270  10.24527  8.47866  1.000 36.03392  ? 8   PHE A H    1 
ATOM   91   H HA   . PHE A 1 22  ? -5.11443  11.24435  7.92862  1.000 34.33115  ? 8   PHE A HA   1 
ATOM   92   H HB2  . PHE A 1 22  ? -5.85773  8.56726   8.43748  1.000 39.21947  ? 8   PHE A HB2  1 
ATOM   93   H HB3  . PHE A 1 22  ? -4.40912  8.96420   7.91846  1.000 39.21947  ? 8   PHE A HB3  1 
ATOM   94   H HD1  . PHE A 1 22  ? -6.53900  9.37951   10.71444 1.000 37.29538  ? 8   PHE A HD1  1 
ATOM   95   H HD2  . PHE A 1 22  ? -2.74571  9.55839   9.46454  1.000 33.86216  ? 8   PHE A HD2  1 
ATOM   96   H HE1  . PHE A 1 22  ? -5.83688  9.66824   12.89135 1.000 32.31117  ? 8   PHE A HE1  1 
ATOM   97   H HE2  . PHE A 1 22  ? -2.03997  9.84299   11.64443 1.000 37.73111  ? 8   PHE A HE2  1 
ATOM   98   H HZ   . PHE A 1 22  ? -3.58540  9.89796   13.36091 1.000 30.21273  ? 8   PHE A HZ   1 
ATOM   99   N N    . THR A 1 23  ? -7.03724  10.75729  5.72334  1.000 35.19684  ? 9   THR A N    1 
ATOM   100  C CA   . THR A 1 23  ? -7.32050  10.44480  4.32522  1.000 38.58464  ? 9   THR A CA   1 
ATOM   101  C C    . THR A 1 23  ? -6.26410  11.02369  3.39093  1.000 36.31641  ? 9   THR A C    1 
ATOM   102  O O    . THR A 1 23  ? -5.91442  10.40210  2.38033  1.000 50.08805  ? 9   THR A O    1 
ATOM   103  C CB   . THR A 1 23  ? -8.70734  10.96043  3.94094  1.000 38.63248  ? 9   THR A CB   1 
ATOM   104  O OG1  . THR A 1 23  ? -8.87074  12.30668  4.40659  1.000 40.59346  ? 9   THR A OG1  1 
ATOM   105  C CG2  . THR A 1 23  ? -9.78744  10.07536  4.54002  1.000 41.53043  ? 9   THR A CG2  1 
ATOM   106  H H    . THR A 1 23  ? -7.63988  11.22978  6.11472  1.000 42.29215  ? 9   THR A H    1 
ATOM   107  H HA   . THR A 1 23  ? -7.31316  9.48034   4.22195  1.000 46.35751  ? 9   THR A HA   1 
ATOM   108  H HB   . THR A 1 23  ? -8.80323  10.94563  2.97581  1.000 46.41491  ? 9   THR A HB   1 
ATOM   109  H HG1  . THR A 1 23  ? -9.66614  12.55381  4.29765  1.000 48.76809  ? 9   THR A HG1  1 
ATOM   110  H HG21 . THR A 1 23  ? -9.74852  9.19054   4.14444  1.000 49.89246  ? 9   THR A HG21 1 
ATOM   111  H HG22 . THR A 1 23  ? -9.65898  9.99767   5.49834  1.000 49.89246  ? 9   THR A HG22 1 
ATOM   112  H HG23 . THR A 1 23  ? -10.66230 10.45813  4.36969  1.000 49.89246  ? 9   THR A HG23 1 
ATOM   113  N N    . GLY A 1 24  ? -5.75182  12.21104  3.70181  1.000 38.25356  ? 10  GLY A N    1 
ATOM   114  C CA   . GLY A 1 24  ? -4.75479  12.84405  2.86009  1.000 35.46009  ? 10  GLY A CA   1 
ATOM   115  C C    . GLY A 1 24  ? -3.40150  12.93761  3.53146  1.000 41.04311  ? 10  GLY A C    1 
ATOM   116  O O    . GLY A 1 24  ? -3.05862  12.09812  4.36982  1.000 41.90395  ? 10  GLY A O    1 
ATOM   117  H H    . GLY A 1 24  ? -5.96842  12.66811  4.39735  1.000 45.96021  ? 10  GLY A H    1 
ATOM   118  H HA2  . GLY A 1 24  ? -4.65476  12.33220  2.04222  1.000 42.60805  ? 10  GLY A HA2  1 
ATOM   119  H HA3  . GLY A 1 24  ? -5.04734  13.74160  2.63713  1.000 42.60805  ? 10  GLY A HA3  1 
ATOM   120  N N    . VAL A 1 25  ? -2.62196  13.95133  3.17117  1.000 30.60057  ? 11  VAL A N    1 
ATOM   121  C CA   . VAL A 1 25  ? -1.31638  14.18232  3.77751  1.000 31.60750  ? 11  VAL A CA   1 
ATOM   122  C C    . VAL A 1 25  ? -1.51158  15.02405  5.03137  1.000 34.12129  ? 11  VAL A C    1 
ATOM   123  O O    . VAL A 1 25  ? -2.18812  16.05934  4.99750  1.000 37.00359  ? 11  VAL A O    1 
ATOM   124  C CB   . VAL A 1 25  ? -0.36209  14.86749  2.78559  1.000 34.82502  ? 11  VAL A CB   1 
ATOM   125  C CG1  . VAL A 1 25  ? 0.98400   15.13225  3.43863  1.000 37.28521  ? 11  VAL A CG1  1 
ATOM   126  C CG2  . VAL A 1 25  ? -0.18631  14.00713  1.53943  1.000 36.28454  ? 11  VAL A CG2  1 
ATOM   127  H H    . VAL A 1 25  ? -2.83060  14.52798  2.56823  1.000 36.77662  ? 11  VAL A H    1 
ATOM   128  H HA   . VAL A 1 25  ? -0.92206  13.33441  4.03531  1.000 37.98494  ? 11  VAL A HA   1 
ATOM   129  H HB   . VAL A 1 25  ? -0.74400  15.71862  2.51983  1.000 41.84597  ? 11  VAL A HB   1 
ATOM   130  H HG11 . VAL A 1 25  ? 1.64699   15.28116  2.74641  1.000 44.79819  ? 11  VAL A HG11 1 
ATOM   131  H HG12 . VAL A 1 25  ? 0.91229   15.91823  4.00255  1.000 44.79819  ? 11  VAL A HG12 1 
ATOM   132  H HG13 . VAL A 1 25  ? 1.23207   14.36245  3.97414  1.000 44.79819  ? 11  VAL A HG13 1 
ATOM   133  H HG21 . VAL A 1 25  ? 0.30241   14.51390  0.87216  1.000 43.59739  ? 11  VAL A HG21 1 
ATOM   134  H HG22 . VAL A 1 25  ? 0.30884   13.20708  1.77531  1.000 43.59739  ? 11  VAL A HG22 1 
ATOM   135  H HG23 . VAL A 1 25  ? -1.06092  13.76575  1.19638  1.000 43.59739  ? 11  VAL A HG23 1 
ATOM   136  N N    . VAL A 1 26  ? -0.92542  14.57973  6.13833  1.000 29.53251  ? 12  VAL A N    1 
ATOM   137  C CA   . VAL A 1 26  ? -1.12510  15.18599  7.44857  1.000 31.10163  ? 12  VAL A CA   1 
ATOM   138  C C    . VAL A 1 26  ? 0.22397   15.68226  7.94862  1.000 28.96087  ? 12  VAL A C    1 
ATOM   139  O O    . VAL A 1 26  ? 1.18302   14.90866  7.97610  1.000 26.02290  ? 12  VAL A O    1 
ATOM   140  C CB   . VAL A 1 26  ? -1.73807  14.20221  8.46272  1.000 28.49086  ? 12  VAL A CB   1 
ATOM   141  C CG1  . VAL A 1 26  ? -1.89339  14.86492  9.81587  1.000 30.74836  ? 12  VAL A CG1  1 
ATOM   142  C CG2  . VAL A 1 26  ? -3.08116  13.67919  7.96572  1.000 29.50752  ? 12  VAL A CG2  1 
ATOM   143  H H    . VAL A 1 26  ? -0.39061  13.90644  6.15464  1.000 35.49495  ? 12  VAL A H    1 
ATOM   144  H HA   . VAL A 1 26  ? -1.71618  15.95008  7.36089  1.000 37.37790  ? 12  VAL A HA   1 
ATOM   145  H HB   . VAL A 1 26  ? -1.13981  13.44501  8.56088  1.000 34.24497  ? 12  VAL A HB   1 
ATOM   146  H HG11 . VAL A 1 26  ? -2.44720  14.30356  10.38073 1.000 36.95398  ? 12  VAL A HG11 1 
ATOM   147  H HG12 . VAL A 1 26  ? -1.01673  14.97456  10.21630 1.000 36.95398  ? 12  VAL A HG12 1 
ATOM   148  H HG13 . VAL A 1 26  ? -2.31340  15.73114  9.69692  1.000 36.95398  ? 12  VAL A HG13 1 
ATOM   149  H HG21 . VAL A 1 26  ? -3.05834  13.61980  6.99781  1.000 35.46497  ? 12  VAL A HG21 1 
ATOM   150  H HG22 . VAL A 1 26  ? -3.23908  12.80151  8.34734  1.000 35.46497  ? 12  VAL A HG22 1 
ATOM   151  H HG23 . VAL A 1 26  ? -3.78066  14.29126  8.24316  1.000 35.46497  ? 12  VAL A HG23 1 
ATOM   152  N N    . PRO A 1 27  ? 0.34804   16.94382  8.35949  1.000 26.10975  ? 13  PRO A N    1 
ATOM   153  C CA   . PRO A 1 27  ? 1.63083   17.41386  8.89125  1.000 27.07426  ? 13  PRO A CA   1 
ATOM   154  C C    . PRO A 1 27  ? 1.90746   16.82687  10.26502 1.000 28.91886  ? 13  PRO A C    1 
ATOM   155  O O    . PRO A 1 27  ? 0.99337   16.54110  11.04307 1.000 27.62799  ? 13  PRO A O    1 
ATOM   156  C CB   . PRO A 1 27  ? 1.45555   18.93539  8.95583  1.000 29.49658  ? 13  PRO A CB   1 
ATOM   157  C CG   . PRO A 1 27  ? -0.00630  19.13592  9.11207  1.000 33.14513  ? 13  PRO A CG   1 
ATOM   158  C CD   . PRO A 1 27  ? -0.67108  18.01058  8.35810  1.000 31.77062  ? 13  PRO A CD   1 
ATOM   159  H HA   . PRO A 1 27  ? 2.35972   17.19725  8.28899  1.000 32.54505  ? 13  PRO A HA   1 
ATOM   160  H HB2  . PRO A 1 27  ? 1.93992   19.29337  9.71618  1.000 35.45183  ? 13  PRO A HB2  1 
ATOM   161  H HB3  . PRO A 1 27  ? 1.77768   19.34175  8.13607  1.000 35.45183  ? 13  PRO A HB3  1 
ATOM   162  H HG2  . PRO A 1 27  ? -0.24056  19.10248  10.05276 1.000 39.83010  ? 13  PRO A HG2  1 
ATOM   163  H HG3  . PRO A 1 27  ? -0.25877  19.99437  8.73761  1.000 39.83010  ? 13  PRO A HG3  1 
ATOM   164  H HD2  . PRO A 1 27  ? -1.47566  17.71857  8.81447  1.000 38.18069  ? 13  PRO A HD2  1 
ATOM   165  H HD3  . PRO A 1 27  ? -0.88389  18.28215  7.45153  1.000 38.18069  ? 13  PRO A HD3  1 
ATOM   166  N N    . ILE A 1 28  ? 3.19401   16.64981  10.55666 1.000 27.14020  ? 14  ILE A N    1 
ATOM   167  C CA   . ILE A 1 28  ? 3.64605   16.00585  11.78225 1.000 24.70477  ? 14  ILE A CA   1 
ATOM   168  C C    . ILE A 1 28  ? 4.65550   16.90946  12.47347 1.000 28.12730  ? 14  ILE A C    1 
ATOM   169  O O    . ILE A 1 28  ? 5.48814   17.54430  11.81703 1.000 26.46831  ? 14  ILE A O    1 
ATOM   170  C CB   . ILE A 1 28  ? 4.27441   14.62400  11.50244 1.000 26.23667  ? 14  ILE A CB   1 
ATOM   171  C CG1  . ILE A 1 28  ? 3.27127   13.71481  10.78780 1.000 29.42381  ? 14  ILE A CG1  1 
ATOM   172  C CG2  . ILE A 1 28  ? 4.74981   13.99022  12.80354 1.000 23.50594  ? 14  ILE A CG2  1 
ATOM   173  C CD1  . ILE A 1 28  ? 3.88546   12.44739  10.22860 1.000 29.47496  ? 14  ILE A CD1  1 
ATOM   174  H H    . ILE A 1 28  ? 3.83813   16.90157  10.04546 1.000 32.62418  ? 14  ILE A H    1 
ATOM   175  H HA   . ILE A 1 28  ? 2.88502   15.88844  12.37213 1.000 29.70166  ? 14  ILE A HA   1 
ATOM   176  H HB   . ILE A 1 28  ? 5.04074   14.74412  10.92002 1.000 31.53995  ? 14  ILE A HB   1 
ATOM   177  H HG12 . ILE A 1 28  ? 2.58101   13.45595  11.41822 1.000 35.36451  ? 14  ILE A HG12 1 
ATOM   178  H HG13 . ILE A 1 28  ? 2.87847   14.20451  10.04834 1.000 35.36451  ? 14  ILE A HG13 1 
ATOM   179  H HG21 . ILE A 1 28  ? 4.98201   13.06328  12.63692 1.000 28.26307  ? 14  ILE A HG21 1 
ATOM   180  H HG22 . ILE A 1 28  ? 5.52723   14.47339  13.12459 1.000 28.26307  ? 14  ILE A HG22 1 
ATOM   181  H HG23 . ILE A 1 28  ? 4.03587   14.03982  13.45831 1.000 28.26307  ? 14  ILE A HG23 1 
ATOM   182  H HD11 . ILE A 1 28  ? 4.11672   11.85774  10.96327 1.000 35.42589  ? 14  ILE A HD11 1 
ATOM   183  H HD12 . ILE A 1 28  ? 3.24124   12.01424  9.64700  1.000 35.42589  ? 14  ILE A HD12 1 
ATOM   184  H HD13 . ILE A 1 28  ? 4.68241   12.67780  9.72593  1.000 35.42589  ? 14  ILE A HD13 1 
ATOM   185  N N    . LEU A 1 29  ? 4.57659   16.96444  13.80124 1.000 31.11368  ? 15  LEU A N    1 
ATOM   186  C CA   . LEU A 1 29  ? 5.57962   17.60908  14.63803 1.000 27.06523  ? 15  LEU A CA   1 
ATOM   187  C C    . LEU A 1 29  ? 5.95499   16.63949  15.74769 1.000 26.90683  ? 15  LEU A C    1 
ATOM   188  O O    . LEU A 1 29  ? 5.07535   16.03030  16.36440 1.000 26.55297  ? 15  LEU A O    1 
ATOM   189  C CB   . LEU A 1 29  ? 5.06294   18.92674  15.22611 1.000 28.99437  ? 15  LEU A CB   1 
ATOM   190  C CG   . LEU A 1 29  ? 4.85229   20.07137  14.23320 1.000 31.92567  ? 15  LEU A CG   1 
ATOM   191  C CD1  . LEU A 1 29  ? 4.15089   21.23985  14.90983 1.000 36.19465  ? 15  LEU A CD1  1 
ATOM   192  C CD2  . LEU A 1 29  ? 6.17451   20.52242  13.63441 1.000 33.96196  ? 15  LEU A CD2  1 
ATOM   193  H H    . LEU A 1 29  ? 3.92910   16.62354  14.25307 1.000 37.39236  ? 15  LEU A H    1 
ATOM   194  H HA   . LEU A 1 29  ? 6.36985   17.81505  14.11457 1.000 32.53421  ? 15  LEU A HA   1 
ATOM   195  H HB2  . LEU A 1 29  ? 4.20753   18.75348  15.64938 1.000 34.51354  ? 15  LEU A HB2  1 
ATOM   196  H HB3  . LEU A 1 29  ? 5.70354   19.23434  15.88635 1.000 34.51354  ? 15  LEU A HB3  1 
ATOM   197  H HG   . LEU A 1 29  ? 4.29030   19.75462  13.50881 1.000 38.03110  ? 15  LEU A HG   1 
ATOM   198  H HD11 . LEU A 1 29  ? 3.33444   20.92056  15.32501 1.000 43.48953  ? 15  LEU A HD11 1 
ATOM   199  H HD12 . LEU A 1 29  ? 4.73982   21.61458  15.58335 1.000 43.48953  ? 15  LEU A HD12 1 
ATOM   200  H HD13 . LEU A 1 29  ? 3.94166   21.91195  14.24245 1.000 43.48953  ? 15  LEU A HD13 1 
ATOM   201  H HD21 . LEU A 1 29  ? 6.88703   19.96722  13.98793 1.000 40.47465  ? 15  LEU A HD21 1 
ATOM   202  H HD22 . LEU A 1 29  ? 6.13176   20.43117  12.66966 1.000 40.47465  ? 15  LEU A HD22 1 
ATOM   203  H HD23 . LEU A 1 29  ? 6.32889   21.45001  13.87241 1.000 40.47465  ? 15  LEU A HD23 1 
ATOM   204  N N    . VAL A 1 30  ? 7.25333   16.48481  15.98995 1.000 23.98285  ? 16  VAL A N    1 
ATOM   205  C CA   . VAL A 1 30  ? 7.76472   15.56304  16.99719 1.000 31.44700  ? 16  VAL A CA   1 
ATOM   206  C C    . VAL A 1 30  ? 8.65199   16.33809  17.96164 1.000 30.67902  ? 16  VAL A C    1 
ATOM   207  O O    . VAL A 1 30  ? 9.49217   17.13924  17.53470 1.000 29.21313  ? 16  VAL A O    1 
ATOM   208  C CB   . VAL A 1 30  ? 8.54165   14.39776  16.35626 1.000 26.98629  ? 16  VAL A CB   1 
ATOM   209  C CG1  . VAL A 1 30  ? 9.06700   13.45399  17.42787 1.000 26.99642  ? 16  VAL A CG1  1 
ATOM   210  C CG2  . VAL A 1 30  ? 7.65457   13.64890  15.36999 1.000 23.32961  ? 16  VAL A CG2  1 
ATOM   211  H H    . VAL A 1 30  ? 7.87111   16.91379  15.57289 1.000 28.49972  ? 16  VAL A H    1 
ATOM   212  H HA   . VAL A 1 30  ? 7.02007   15.19753  17.49998 1.000 37.79233  ? 16  VAL A HA   1 
ATOM   213  H HB   . VAL A 1 30  ? 9.30167   14.75500  15.87082 1.000 32.43949  ? 16  VAL A HB   1 
ATOM   214  H HG11 . VAL A 1 30  ? 9.44710   12.67075  17.00012 1.000 32.45164  ? 16  VAL A HG11 1 
ATOM   215  H HG12 . VAL A 1 30  ? 9.74800   13.91152  17.94536 1.000 32.45164  ? 16  VAL A HG12 1 
ATOM   216  H HG13 . VAL A 1 30  ? 8.33300   13.19203  18.00539 1.000 32.45164  ? 16  VAL A HG13 1 
ATOM   217  H HG21 . VAL A 1 30  ? 6.72622   13.77551  15.62108 1.000 28.05147  ? 16  VAL A HG21 1 
ATOM   218  H HG22 . VAL A 1 30  ? 7.80698   13.99988  14.47865 1.000 28.05147  ? 16  VAL A HG22 1 
ATOM   219  H HG23 . VAL A 1 30  ? 7.87878   12.70555  15.39683 1.000 28.05147  ? 16  VAL A HG23 1 
ATOM   220  N N    . GLU A 1 31  ? 8.46152   16.09691  19.25827 1.000 25.19500  ? 17  GLU A N    1 
ATOM   221  C CA   . GLU A 1 31  ? 9.28987   16.67533  20.30790 1.000 30.00094  ? 17  GLU A CA   1 
ATOM   222  C C    . GLU A 1 31  ? 9.78447   15.55911  21.21489 1.000 30.33674  ? 17  GLU A C    1 
ATOM   223  O O    . GLU A 1 31  ? 8.98816   14.74116  21.68740 1.000 26.95261  ? 17  GLU A O    1 
ATOM   224  C CB   . GLU A 1 31  ? 8.51794   17.71268  21.13235 1.000 34.02066  ? 17  GLU A CB   1 
ATOM   225  C CG   . GLU A 1 31  ? 8.37432   19.07029  20.46430 1.000 41.99079  ? 17  GLU A CG   1 
ATOM   226  C CD   . GLU A 1 31  ? 7.27606   19.10068  19.42013 1.000 44.06101  ? 17  GLU A CD   1 
ATOM   227  O OE1  . GLU A 1 31  ? 6.32750   18.29490  19.52396 1.000 50.60542  ? 17  GLU A OE1  1 
ATOM   228  O OE2  . GLU A 1 31  ? 7.36040   19.93292  18.49512 1.000 39.02853  ? 17  GLU A OE2  1 
ATOM   229  H H    . GLU A 1 31  ? 7.83952   15.58585  19.56081 1.000 30.28994  ? 17  GLU A H    1 
ATOM   230  H HA   . GLU A 1 31  ? 10.05396  17.11678  19.90518 1.000 36.05707  ? 17  GLU A HA   1 
ATOM   231  H HB2  . GLU A 1 31  ? 7.62497   17.37234  21.29873 1.000 40.88073  ? 17  GLU A HB2  1 
ATOM   232  H HB3  . GLU A 1 31  ? 8.98343   17.84765  21.97259 1.000 40.88073  ? 17  GLU A HB3  1 
ATOM   233  H HG2  . GLU A 1 31  ? 8.16347   19.73366  21.13986 1.000 50.44489  ? 17  GLU A HG2  1 
ATOM   234  H HG3  . GLU A 1 31  ? 9.20984   19.29653  20.02656 1.000 50.44489  ? 17  GLU A HG3  1 
ATOM   235  N N    . LEU A 1 32  ? 11.09291  15.53175  21.46052 1.000 28.03096  ? 18  LEU A N    1 
ATOM   236  C CA   . LEU A 1 32  ? 11.71465  14.52279  22.30910 1.000 29.98348  ? 18  LEU A CA   1 
ATOM   237  C C    . LEU A 1 32  ? 12.60091  15.21037  23.33466 1.000 31.30865  ? 18  LEU A C    1 
ATOM   238  O O    . LEU A 1 32  ? 13.53438  15.93184  22.96766 1.000 28.20951  ? 18  LEU A O    1 
ATOM   239  C CB   . LEU A 1 32  ? 12.53570  13.52926  21.48002 1.000 33.90468  ? 18  LEU A CB   1 
ATOM   240  C CG   . LEU A 1 32  ? 13.47668  12.61073  22.26558 1.000 29.30178  ? 18  LEU A CG   1 
ATOM   241  C CD1  . LEU A 1 32  ? 12.72283  11.84701  23.32207 1.000 30.76084  ? 18  LEU A CD1  1 
ATOM   242  C CD2  . LEU A 1 32  ? 14.18744  11.64603  21.32879 1.000 36.44923  ? 18  LEU A CD2  1 
ATOM   243  H H    . LEU A 1 32  ? 11.65181  16.10069  21.13876 1.000 33.69309  ? 18  LEU A H    1 
ATOM   244  H HA   . LEU A 1 32  ? 11.02109  14.03635  22.78160 1.000 36.03611  ? 18  LEU A HA   1 
ATOM   245  H HB2  . LEU A 1 32  ? 11.91910  12.95976  20.99384 1.000 40.74156  ? 18  LEU A HB2  1 
ATOM   246  H HB3  . LEU A 1 32  ? 13.08186  14.03439  20.85756 1.000 40.74156  ? 18  LEU A HB3  1 
ATOM   247  H HG   . LEU A 1 32  ? 14.14472  13.15796  22.70736 1.000 35.21808  ? 18  LEU A HG   1 
ATOM   248  H HD11 . LEU A 1 32  ? 11.99930  11.35663  22.90145 1.000 36.96895  ? 18  LEU A HD11 1 
ATOM   249  H HD12 . LEU A 1 32  ? 13.33015  11.23002  23.75954 1.000 36.96895  ? 18  LEU A HD12 1 
ATOM   250  H HD13 . LEU A 1 32  ? 12.36478  12.47393  23.96990 1.000 36.96895  ? 18  LEU A HD13 1 
ATOM   251  H HD21 . LEU A 1 32  ? 14.75116  11.05516  21.85222 1.000 43.79501  ? 18  LEU A HD21 1 
ATOM   252  H HD22 . LEU A 1 32  ? 13.52426  11.12851  20.84582 1.000 43.79501  ? 18  LEU A HD22 1 
ATOM   253  H HD23 . LEU A 1 32  ? 14.72963  12.15354  20.70480 1.000 43.79501  ? 18  LEU A HD23 1 
ATOM   254  N N    . ASP A 1 33  ? 12.30452  14.98899  24.61229 1.000 36.59601  ? 19  ASP A N    1 
ATOM   255  C CA   . ASP A 1 33  ? 13.18452  15.36984  25.70914 1.000 34.76379  ? 19  ASP A CA   1 
ATOM   256  C C    . ASP A 1 33  ? 13.86115  14.10655  26.22539 1.000 37.21585  ? 19  ASP A C    1 
ATOM   257  O O    . ASP A 1 33  ? 13.18738  13.19637  26.72140 1.000 33.68788  ? 19  ASP A O    1 
ATOM   258  C CB   . ASP A 1 33  ? 12.40893  16.07046  26.82321 1.000 45.85970  ? 19  ASP A CB   1 
ATOM   259  C CG   . ASP A 1 33  ? 12.25736  17.56104  26.57900 1.000 59.88615  ? 19  ASP A CG   1 
ATOM   260  O OD1  . ASP A 1 33  ? 12.82586  18.06627  25.58732 1.000 52.09117  ? 19  ASP A OD1  1 
ATOM   261  O OD2  . ASP A 1 33  ? 11.57050  18.22903  27.38019 1.000 77.45775  ? 19  ASP A OD2  1 
ATOM   262  H H    . ASP A 1 33  ? 11.57890  14.60902  24.87440 1.000 43.97116  ? 19  ASP A H    1 
ATOM   263  H HA   . ASP A 1 33  ? 13.86262  15.98785  25.39427 1.000 41.77249  ? 19  ASP A HA   1 
ATOM   264  H HB2  . ASP A 1 33  ? 11.52137  15.68371  26.88298 1.000 55.08758  ? 19  ASP A HB2  1 
ATOM   265  H HB3  . ASP A 1 33  ? 12.88067  15.94957  27.66210 1.000 55.08758  ? 19  ASP A HB3  1 
ATOM   266  N N    . GLY A 1 34  ? 15.18400  14.04796  26.09566 1.000 33.02735  ? 20  GLY A N    1 
ATOM   267  C CA   . GLY A 1 34  ? 15.91661  12.83792  26.41053 1.000 29.69327  ? 20  GLY A CA   1 
ATOM   268  C C    . GLY A 1 34  ? 16.84118  12.96696  27.60110 1.000 32.32571  ? 20  GLY A C    1 
ATOM   269  O O    . GLY A 1 34  ? 17.27113  14.06859  27.95343 1.000 30.91900  ? 20  GLY A O    1 
ATOM   270  H H    . GLY A 1 34  ? 15.67664  14.69937  25.82627 1.000 39.68875  ? 20  GLY A H    1 
ATOM   271  H HA2  . GLY A 1 34  ? 15.28355  12.12780  26.59990 1.000 35.68787  ? 20  GLY A HA2  1 
ATOM   272  H HA3  . GLY A 1 34  ? 16.45273  12.58648  25.64224 1.000 35.68787  ? 20  GLY A HA3  1 
ATOM   273  N N    . ASP A 1 35  ? 17.15286  11.83347  28.22886 1.000 37.62857  ? 21  ASP A N    1 
ATOM   274  C CA   . ASP A 1 35  ? 18.06586  11.80286  29.36947 1.000 35.22603  ? 21  ASP A CA   1 
ATOM   275  C C    . ASP A 1 35  ? 18.69072  10.41023  29.39613 1.000 35.66530  ? 21  ASP A C    1 
ATOM   276  O O    . ASP A 1 35  ? 18.05053  9.44868   29.83172 1.000 35.03313  ? 21  ASP A O    1 
ATOM   277  C CB   . ASP A 1 35  ? 17.33445  12.12195  30.66624 1.000 36.13501  ? 21  ASP A CB   1 
ATOM   278  C CG   . ASP A 1 35  ? 18.27556  12.30162  31.84142 1.000 39.37002  ? 21  ASP A CG   1 
ATOM   279  O OD1  . ASP A 1 35  ? 19.49480  12.09819  31.66960 1.000 44.68043  ? 21  ASP A OD1  1 
ATOM   280  O OD2  . ASP A 1 35  ? 17.79488  12.65400  32.93895 1.000 43.12020  ? 21  ASP A OD2  1 
ATOM   281  H H    . ASP A 1 35  ? 16.84514  11.06063  28.01065 1.000 45.21023  ? 21  ASP A H    1 
ATOM   282  H HA   . ASP A 1 35  ? 18.76898  12.46034  29.25015 1.000 42.32717  ? 21  ASP A HA   1 
ATOM   283  H HB2  . ASP A 1 35  ? 16.83520  12.94588  30.55308 1.000 43.41795  ? 21  ASP A HB2  1 
ATOM   284  H HB3  . ASP A 1 35  ? 16.72920  11.39335  30.87533 1.000 43.41795  ? 21  ASP A HB3  1 
ATOM   285  N N    . VAL A 1 36  ? 19.92642  10.30968  28.91487 1.000 32.94185  ? 22  VAL A N    1 
ATOM   286  C CA   . VAL A 1 36  ? 20.66149  9.05159   28.86096 1.000 30.74425  ? 22  VAL A CA   1 
ATOM   287  C C    . VAL A 1 36  ? 21.84927  9.15547   29.80623 1.000 33.37876  ? 22  VAL A C    1 
ATOM   288  O O    . VAL A 1 36  ? 22.74907  9.97835   29.59624 1.000 30.34124  ? 22  VAL A O    1 
ATOM   289  C CB   . VAL A 1 36  ? 21.12300  8.72855   27.43291 1.000 30.10072  ? 22  VAL A CB   1 
ATOM   290  C CG1  . VAL A 1 36  ? 22.05581  7.52864   27.43846 1.000 32.62359  ? 22  VAL A CG1  1 
ATOM   291  C CG2  . VAL A 1 36  ? 19.92255  8.47070   26.54108 1.000 30.21054  ? 22  VAL A CG2  1 
ATOM   292  H H    . VAL A 1 36  ? 20.37185  10.97688  28.60498 1.000 39.58617  ? 22  VAL A H    1 
ATOM   293  H HA   . VAL A 1 36  ? 20.08753  8.33343   29.17033 1.000 36.94904  ? 22  VAL A HA   1 
ATOM   294  H HB   . VAL A 1 36  ? 21.61013  9.48722   27.07511 1.000 36.17680  ? 22  VAL A HB   1 
ATOM   295  H HG11 . VAL A 1 36  ? 21.82794  6.95494   28.18669 1.000 39.20425  ? 22  VAL A HG11 1 
ATOM   296  H HG12 . VAL A 1 36  ? 21.95072  7.04308   26.60534 1.000 39.20425  ? 22  VAL A HG12 1 
ATOM   297  H HG13 . VAL A 1 36  ? 22.97025  7.83992   27.52681 1.000 39.20425  ? 22  VAL A HG13 1 
ATOM   298  H HG21 . VAL A 1 36  ? 20.22741  8.35052   25.62811 1.000 36.30859  ? 22  VAL A HG21 1 
ATOM   299  H HG22 . VAL A 1 36  ? 19.46857  7.66970   26.84637 1.000 36.30859  ? 22  VAL A HG22 1 
ATOM   300  H HG23 . VAL A 1 36  ? 19.32223  9.23091   26.59198 1.000 36.30859  ? 22  VAL A HG23 1 
ATOM   301  N N    . ASN A 1 37  ? 21.85657  8.31477   30.84127 1.000 32.90525  ? 23  ASN A N    1 
ATOM   302  C CA   . ASN A 1 37  ? 22.92028  8.32301   31.84389 1.000 31.90411  ? 23  ASN A CA   1 
ATOM   303  C C    . ASN A 1 37  ? 23.08334  9.71356   32.45312 1.000 36.40123  ? 23  ASN A C    1 
ATOM   304  O O    . ASN A 1 37  ? 24.19222  10.16136  32.75174 1.000 36.86442  ? 23  ASN A O    1 
ATOM   305  C CB   . ASN A 1 37  ? 24.24115  7.83185   31.24782 1.000 30.19839  ? 23  ASN A CB   1 
ATOM   306  C CG   . ASN A 1 37  ? 24.32348  6.31797   31.17259 1.000 31.74499  ? 23  ASN A CG   1 
ATOM   307  O OD1  . ASN A 1 37  ? 23.30486  5.62837   31.13284 1.000 28.84905  ? 23  ASN A OD1  1 
ATOM   308  N ND2  . ASN A 1 37  ? 25.54463  5.79314   31.16192 1.000 31.88543  ? 23  ASN A ND2  1 
ATOM   309  H H    . ASN A 1 37  ? 21.24903  7.72352   30.98592 1.000 39.54224  ? 23  ASN A H    1 
ATOM   310  H HA   . ASN A 1 37  ? 22.67187  7.71518   32.55785 1.000 38.34087  ? 23  ASN A HA   1 
ATOM   311  H HB2  . ASN A 1 37  ? 24.33174  8.18240   30.34793 1.000 36.29401  ? 23  ASN A HB2  1 
ATOM   312  H HB3  . ASN A 1 37  ? 24.97366  8.14509   31.80118 1.000 36.29401  ? 23  ASN A HB3  1 
ATOM   313  H HD21 . ASN A 1 37  ? 25.64570  4.94012   31.12023 1.000 38.31846  ? 23  ASN A HD21 1 
ATOM   314  H HD22 . ASN A 1 37  ? 26.23366  6.30660   31.19670 1.000 38.31846  ? 23  ASN A HD22 1 
ATOM   315  N N    . GLY A 1 38  ? 21.96095  10.40408  32.63986 1.000 35.32554  ? 24  GLY A N    1 
ATOM   316  C CA   . GLY A 1 38  ? 21.97505  11.72738  33.22463 1.000 38.05999  ? 24  GLY A CA   1 
ATOM   317  C C    . GLY A 1 38  ? 22.38998  12.83615  32.28694 1.000 42.13785  ? 24  GLY A C    1 
ATOM   318  O O    . GLY A 1 38  ? 22.53375  13.98081  32.73218 1.000 46.50727  ? 24  GLY A O    1 
ATOM   319  H H    . GLY A 1 38  ? 21.17601  10.12038  32.43255 1.000 42.44659  ? 24  GLY A H    1 
ATOM   320  H HA2  . GLY A 1 38  ? 21.08395  11.93261  33.54825 1.000 45.72793  ? 24  GLY A HA2  1 
ATOM   321  H HA3  . GLY A 1 38  ? 22.59116  11.72850  33.97384 1.000 45.72793  ? 24  GLY A HA3  1 
ATOM   322  N N    . HIS A 1 39  ? 22.58900  12.53847  31.00752 1.000 39.66506  ? 25  HIS A N    1 
ATOM   323  C CA   . HIS A 1 39  ? 22.98094  13.53215  30.01745 1.000 45.25942  ? 25  HIS A CA   1 
ATOM   324  C C    . HIS A 1 39  ? 21.76828  13.87310  29.16051 1.000 42.10951  ? 25  HIS A C    1 
ATOM   325  O O    . HIS A 1 39  ? 21.24298  13.01118  28.44558 1.000 33.53200  ? 25  HIS A O    1 
ATOM   326  C CB   . HIS A 1 39  ? 24.13719  13.01384  29.16420 1.000 41.68686  ? 25  HIS A CB   1 
ATOM   327  C CG   . HIS A 1 39  ? 25.38716  12.75654  29.94735 1.000 47.86592  ? 25  HIS A CG   1 
ATOM   328  N ND1  . HIS A 1 39  ? 26.27041  13.75834  30.28813 1.000 51.16448  ? 25  HIS A ND1  1 
ATOM   329  C CD2  . HIS A 1 39  ? 25.89494  11.61444  30.46835 1.000 47.43712  ? 25  HIS A CD2  1 
ATOM   330  C CE1  . HIS A 1 39  ? 27.27124  13.24369  30.98018 1.000 54.54671  ? 25  HIS A CE1  1 
ATOM   331  N NE2  . HIS A 1 39  ? 27.06741  11.94449  31.10400 1.000 45.00798  ? 25  HIS A NE2  1 
ATOM   332  H H    . HIS A 1 39  ? 22.50066  11.74748  30.68176 1.000 47.65401  ? 25  HIS A H    1 
ATOM   333  H HA   . HIS A 1 39  ? 23.27614  14.34418  30.45832 1.000 54.36724  ? 25  HIS A HA   1 
ATOM   334  H HB2  . HIS A 1 39  ? 23.86980  12.17931  28.74831 1.000 50.08017  ? 25  HIS A HB2  1 
ATOM   335  H HB3  . HIS A 1 39  ? 24.34348  13.67284  28.48297 1.000 50.08017  ? 25  HIS A HB3  1 
ATOM   336  H HD2  . HIS A 1 39  ? 25.52016  10.76549  30.40731 1.000 56.98049  ? 25  HIS A HD2  1 
ATOM   337  H HE1  . HIS A 1 39  ? 27.99594  13.71579  31.32199 1.000 65.51199  ? 25  HIS A HE1  1 
ATOM   338  H HE2  . HIS A 1 39  ? 27.58468  11.39445  31.51570 1.000 54.06552  ? 25  HIS A HE2  1 
ATOM   339  N N    . LYS A 1 40  ? 21.32845  15.12568  29.24020 1.000 41.62258  ? 26  LYS A N    1 
ATOM   340  C CA   . LYS A 1 40  ? 20.09260  15.55783  28.60881 1.000 42.41440  ? 26  LYS A CA   1 
ATOM   341  C C    . LYS A 1 40  ? 20.32759  15.98889  27.16800 1.000 32.75490  ? 26  LYS A C    1 
ATOM   342  O O    . LYS A 1 40  ? 21.40266  16.47451  26.80570 1.000 36.04353  ? 26  LYS A O    1 
ATOM   343  C CB   . LYS A 1 40  ? 19.46481  16.71773  29.38361 1.000 40.40318  ? 26  LYS A CB   1 
ATOM   344  C CG   . LYS A 1 40  ? 19.06586  16.38362  30.80783 1.000 46.46341  ? 26  LYS A CG   1 
ATOM   345  C CD   . LYS A 1 40  ? 18.39356  17.57731  31.47042 1.000 48.44198  ? 26  LYS A CD   1 
ATOM   346  C CE   . LYS A 1 40  ? 18.22749  17.37637  32.96527 1.000 59.80774  ? 26  LYS A CE   1 
ATOM   347  N NZ   . LYS A 1 40  ? 18.36766  18.66581  33.70383 1.000 66.26946  ? 26  LYS A NZ   1 
ATOM   348  H H    . LYS A 1 40  ? 21.73762  15.75312  29.66270 1.000 50.00303  ? 26  LYS A H    1 
ATOM   349  H HA   . LYS A 1 40  ? 19.47298  14.81153  28.60401 1.000 50.95323  ? 26  LYS A HA   1 
ATOM   350  H HB2  . LYS A 1 40  ? 20.10524  17.44524  29.42232 1.000 48.53976  ? 26  LYS A HB2  1 
ATOM   351  H HB3  . LYS A 1 40  ? 18.66506  17.00433  28.91546 1.000 48.53976  ? 26  LYS A HB3  1 
ATOM   352  H HG2  . LYS A 1 40  ? 18.44201  15.64085  30.80442 1.000 55.81203  ? 26  LYS A HG2  1 
ATOM   353  H HG3  . LYS A 1 40  ? 19.85596  16.15092  31.32016 1.000 55.81203  ? 26  LYS A HG3  1 
ATOM   354  H HD2  . LYS A 1 40  ? 18.93634  18.36879  31.32949 1.000 58.18632  ? 26  LYS A HD2  1 
ATOM   355  H HD3  . LYS A 1 40  ? 17.51384  17.70489  31.08220 1.000 58.18632  ? 26  LYS A HD3  1 
ATOM   356  H HE2  . LYS A 1 40  ? 17.34564  17.01477  33.14554 1.000 71.82523  ? 26  LYS A HE2  1 
ATOM   357  H HE3  . LYS A 1 40  ? 18.90873  16.76464  33.28558 1.000 71.82523  ? 26  LYS A HE3  1 
ATOM   358  H HZ1  . LYS A 1 40  ? 19.15735  19.03504  33.52448 1.000 79.57929  ? 26  LYS A HZ1  1 
ATOM   359  H HZ2  . LYS A 1 40  ? 17.72329  19.22864  33.45865 1.000 79.57929  ? 26  LYS A HZ2  1 
ATOM   360  H HZ3  . LYS A 1 40  ? 18.30810  18.52266  34.58022 1.000 79.57929  ? 26  LYS A HZ3  1 
ATOM   361  N N    . PHE A 1 41  ? 19.29380  15.81204  26.35016 1.000 31.71757  ? 27  PHE A N    1 
ATOM   362  C CA   . PHE A 1 41  ? 19.30123  16.26670  24.96790 1.000 31.33924  ? 27  PHE A CA   1 
ATOM   363  C C    . PHE A 1 41  ? 17.85871  16.47134  24.53334 1.000 28.73330  ? 27  PHE A C    1 
ATOM   364  O O    . PHE A 1 41  ? 16.92536  15.96149  25.15861 1.000 32.22881  ? 27  PHE A O    1 
ATOM   365  C CB   . PHE A 1 41  ? 20.01668  15.27343  24.04545 1.000 30.72287  ? 27  PHE A CB   1 
ATOM   366  C CG   . PHE A 1 41  ? 19.40994  13.89909  24.03983 1.000 28.63687  ? 27  PHE A CG   1 
ATOM   367  C CD1  . PHE A 1 41  ? 19.71331  12.99036  25.03847 1.000 32.48711  ? 27  PHE A CD1  1 
ATOM   368  C CD2  . PHE A 1 41  ? 18.54832  13.51067  23.02767 1.000 26.67006  ? 27  PHE A CD2  1 
ATOM   369  C CE1  . PHE A 1 41  ? 19.16087  11.72528  25.03276 1.000 34.75927  ? 27  PHE A CE1  1 
ATOM   370  C CE2  . PHE A 1 41  ? 17.99349  12.24706  23.01770 1.000 25.58918  ? 27  PHE A CE2  1 
ATOM   371  C CZ   . PHE A 1 41  ? 18.30080  11.35309  24.01757 1.000 32.40363  ? 27  PHE A CZ   1 
ATOM   372  H H    . PHE A 1 41  ? 18.56163  15.42300  26.57857 1.000 38.11702  ? 27  PHE A H    1 
ATOM   373  H HA   . PHE A 1 41  ? 19.76819  17.11453  24.90440 1.000 37.66303  ? 27  PHE A HA   1 
ATOM   374  H HB2  . PHE A 1 41  ? 19.98489  15.61371  23.13765 1.000 36.92338  ? 27  PHE A HB2  1 
ATOM   375  H HB3  . PHE A 1 41  ? 20.93831  15.18790  24.33561 1.000 36.92338  ? 27  PHE A HB3  1 
ATOM   376  H HD1  . PHE A 1 41  ? 20.29583  13.23466  25.72102 1.000 39.04048  ? 27  PHE A HD1  1 
ATOM   377  H HD2  . PHE A 1 41  ? 18.34102  14.10868  22.34627 1.000 32.06002  ? 27  PHE A HD2  1 
ATOM   378  H HE1  . PHE A 1 41  ? 19.36743  11.12412  25.71161 1.000 41.76706  ? 27  PHE A HE1  1 
ATOM   379  H HE2  . PHE A 1 41  ? 17.41200  11.99981  22.33532 1.000 30.76296  ? 27  PHE A HE2  1 
ATOM   380  H HZ   . PHE A 1 41  ? 17.93034  10.50010  24.01002 1.000 38.94029  ? 27  PHE A HZ   1 
ATOM   381  N N    . SER A 1 42  ? 17.68766  17.23320  23.45653 1.000 28.38889  ? 28  SER A N    1 
ATOM   382  C CA   . SER A 1 42  ? 16.36422  17.54477  22.93547 1.000 29.97428  ? 28  SER A CA   1 
ATOM   383  C C    . SER A 1 42  ? 16.39464  17.45855  21.41901 1.000 28.02838  ? 28  SER A C    1 
ATOM   384  O O    . SER A 1 42  ? 17.32431  17.96681  20.78520 1.000 32.17032  ? 28  SER A O    1 
ATOM   385  C CB   . SER A 1 42  ? 15.90785  18.93947  23.37718 1.000 32.30101  ? 28  SER A CB   1 
ATOM   386  O OG   . SER A 1 42  ? 15.93705  19.06622  24.78839 1.000 44.56182  ? 28  SER A OG   1 
ATOM   387  H H    . SER A 1 42  ? 18.33101  17.58437  23.00668 1.000 34.12261  ? 28  SER A H    1 
ATOM   388  H HA   . SER A 1 42  ? 15.72429  16.89503  23.26597 1.000 36.02508  ? 28  SER A HA   1 
ATOM   389  H HB2  . SER A 1 42  ? 16.50157  19.60161  22.98992 1.000 38.81715  ? 28  SER A HB2  1 
ATOM   390  H HB3  . SER A 1 42  ? 15.00042  19.08590  23.06730 1.000 38.81715  ? 28  SER A HB3  1 
ATOM   391  H HG   . SER A 1 42  ? 15.69405  19.83841  25.01258 1.000 53.53013  ? 28  SER A HG   1 
ATOM   392  N N    . VAL A 1 43  ? 15.38044  16.81548  20.84485 1.000 26.74474  ? 29  VAL A N    1 
ATOM   393  C CA   . VAL A 1 43  ? 15.24680  16.66758  19.40111 1.000 29.76437  ? 29  VAL A CA   1 
ATOM   394  C C    . VAL A 1 43  ? 13.90924  17.25660  18.97614 1.000 30.61098  ? 29  VAL A C    1 
ATOM   395  O O    . VAL A 1 43  ? 12.88574  17.03904  19.63443 1.000 27.33756  ? 29  VAL A O    1 
ATOM   396  C CB   . VAL A 1 43  ? 15.35365  15.19019  18.96355 1.000 31.52125  ? 29  VAL A CB   1 
ATOM   397  C CG1  . VAL A 1 43  ? 15.19320  15.05949  17.45265 1.000 29.02253  ? 29  VAL A CG1  1 
ATOM   398  C CG2  . VAL A 1 43  ? 16.68155  14.59235  19.41024 1.000 26.18945  ? 29  VAL A CG2  1 
ATOM   399  H H    . VAL A 1 43  ? 14.74036  16.44668  21.28517 1.000 32.14963  ? 29  VAL A H    1 
ATOM   400  H HA   . VAL A 1 43  ? 15.95588  17.16488  18.96430 1.000 35.77318  ? 29  VAL A HA   1 
ATOM   401  H HB   . VAL A 1 43  ? 14.63741  14.69183  19.38727 1.000 37.88144  ? 29  VAL A HB   1 
ATOM   402  H HG11 . VAL A 1 43  ? 15.27673  14.12514  17.20586 1.000 34.88298  ? 29  VAL A HG11 1 
ATOM   403  H HG12 . VAL A 1 43  ? 14.31822  15.39191  17.19807 1.000 34.88298  ? 29  VAL A HG12 1 
ATOM   404  H HG13 . VAL A 1 43  ? 15.88496  15.58023  17.01540 1.000 34.88298  ? 29  VAL A HG13 1 
ATOM   405  H HG21 . VAL A 1 43  ? 17.12790  15.21986  20.00008 1.000 31.48328  ? 29  VAL A HG21 1 
ATOM   406  H HG22 . VAL A 1 43  ? 16.51148  13.76073  19.87969 1.000 31.48328  ? 29  VAL A HG22 1 
ATOM   407  H HG23 . VAL A 1 43  ? 17.23117  14.42464  18.62878 1.000 31.48328  ? 29  VAL A HG23 1 
ATOM   408  N N    . SER A 1 44  ? 13.92446  18.00873  17.87830 1.000 29.22992  ? 30  SER A N    1 
ATOM   409  C CA   . SER A 1 44  ? 12.71800  18.53574  17.25517 1.000 30.99197  ? 30  SER A CA   1 
ATOM   410  C C    . SER A 1 44  ? 12.57999  17.91618  15.87251 1.000 33.01211  ? 30  SER A C    1 
ATOM   411  O O    . SER A 1 44  ? 13.55861  17.84034  15.12149 1.000 28.24313  ? 30  SER A O    1 
ATOM   412  C CB   . SER A 1 44  ? 12.76012  20.06416  17.15311 1.000 32.55848  ? 30  SER A CB   1 
ATOM   413  O OG   . SER A 1 44  ? 12.73235  20.66708  18.43753 1.000 33.83698  ? 30  SER A OG   1 
ATOM   414  H H    . SER A 1 44  ? 14.64482  18.23274  17.46538 1.000 35.13185  ? 30  SER A H    1 
ATOM   415  H HA   . SER A 1 44  ? 11.94238  18.29716  17.78658 1.000 37.24631  ? 30  SER A HA   1 
ATOM   416  H HB2  . SER A 1 44  ? 13.57719  20.32627  16.70079 1.000 39.12612  ? 30  SER A HB2  1 
ATOM   417  H HB3  . SER A 1 44  ? 11.98943  20.36647  16.64759 1.000 39.12612  ? 30  SER A HB3  1 
ATOM   418  H HG   . SER A 1 44  ? 12.00835  20.48733  18.82369 1.000 40.66031  ? 30  SER A HG   1 
ATOM   419  N N    . GLY A 1 45  ? 11.37576  17.46963  15.54413 1.000 28.24306  ? 31  GLY A N    1 
ATOM   420  C CA   . GLY A 1 45  ? 11.12400  16.84370  14.26311 1.000 29.28746  ? 31  GLY A CA   1 
ATOM   421  C C    . GLY A 1 45  ? 9.86474   17.38579  13.62332 1.000 25.20960  ? 31  GLY A C    1 
ATOM   422  O O    . GLY A 1 45  ? 8.93257   17.81774  14.30043 1.000 25.42800  ? 31  GLY A O    1 
ATOM   423  H H    . GLY A 1 45  ? 10.68402  17.51938  16.05267 1.000 33.94761  ? 31  GLY A H    1 
ATOM   424  H HA2  . GLY A 1 45  ? 11.87084  17.01050  13.66704 1.000 35.20089  ? 31  GLY A HA2  1 
ATOM   425  H HA3  . GLY A 1 45  ? 11.02323  15.88641  14.38288 1.000 35.20089  ? 31  GLY A HA3  1 
ATOM   426  N N    . GLU A 1 46  ? 9.85506   17.36633  12.29307 1.000 25.69953  ? 32  GLU A N    1 
ATOM   427  C CA   . GLU A 1 46  ? 8.67784   17.77124  11.54157 1.000 28.20638  ? 32  GLU A CA   1 
ATOM   428  C C    . GLU A 1 46  ? 8.65721   17.02350  10.21671 1.000 26.83164  ? 32  GLU A C    1 
ATOM   429  O O    . GLU A 1 46  ? 9.65243   16.43130  9.79285  1.000 23.29374  ? 32  GLU A O    1 
ATOM   430  C CB   . GLU A 1 46  ? 8.64265   19.28902  11.31728 1.000 26.79371  ? 32  GLU A CB   1 
ATOM   431  C CG   . GLU A 1 46  ? 9.57468   19.80393  10.22855 1.000 28.41963  ? 32  GLU A CG   1 
ATOM   432  C CD   . GLU A 1 46  ? 9.51029   21.31289  10.08009 1.000 33.52935  ? 32  GLU A CD   1 
ATOM   433  O OE1  . GLU A 1 46  ? 9.75391   22.01894  11.07908 1.000 34.94837  ? 32  GLU A OE1  1 
ATOM   434  O OE2  . GLU A 1 46  ? 9.20134   21.79583  8.97105  1.000 40.94476  ? 32  GLU A OE2  1 
ATOM   435  H H    . GLU A 1 46  ? 10.51970  17.12202  11.80505 1.000 30.89538  ? 32  GLU A H    1 
ATOM   436  H HA   . GLU A 1 46  ? 7.88458   17.52333  12.04176 1.000 33.90360  ? 32  GLU A HA   1 
ATOM   437  H HB2  . GLU A 1 46  ? 7.73944   19.54126  11.06931 1.000 31.87275  ? 32  GLU A HB2  1 
ATOM   438  H HB3  . GLU A 1 46  ? 8.89390   19.72706  12.14547 1.000 31.87275  ? 32  GLU A HB3  1 
ATOM   439  H HG2  . GLU A 1 46  ? 10.48721  19.56130  10.45062 1.000 34.15949  ? 32  GLU A HG2  1 
ATOM   440  H HG3  . GLU A 1 46  ? 9.32271   19.40631  9.38042  1.000 34.15949  ? 32  GLU A HG3  1 
ATOM   441  N N    . GLY A 1 47  ? 7.50655   17.06496  9.56498  1.000 25.34011  ? 33  GLY A N    1 
ATOM   442  C CA   . GLY A 1 47  ? 7.32586   16.38644  8.29385  1.000 26.64963  ? 33  GLY A CA   1 
ATOM   443  C C    . GLY A 1 47  ? 5.84976   16.13422  8.04543  1.000 26.08589  ? 33  GLY A C    1 
ATOM   444  O O    . GLY A 1 47  ? 4.99616   16.90947  8.47327  1.000 27.70504  ? 33  GLY A O    1 
ATOM   445  H H    . GLY A 1 47  ? 6.80756   17.48354  9.84029  1.000 30.46407  ? 33  GLY A H    1 
ATOM   446  H HA2  . GLY A 1 47  ? 7.67782   16.93312  7.57401  1.000 32.03550  ? 33  GLY A HA2  1 
ATOM   447  H HA3  . GLY A 1 47  ? 7.79374   15.53678  8.30289  1.000 32.03550  ? 33  GLY A HA3  1 
ATOM   448  N N    . GLU A 1 48  ? 5.57318   15.03043  7.35923  1.000 25.43354  ? 34  GLU A N    1 
ATOM   449  C CA   . GLU A 1 48  ? 4.20246   14.69984  7.00983  1.000 29.35160  ? 34  GLU A CA   1 
ATOM   450  C C    . GLU A 1 48  ? 4.06382   13.19405  6.86574  1.000 31.21582  ? 34  GLU A C    1 
ATOM   451  O O    . GLU A 1 48  ? 5.03614   12.47662  6.61419  1.000 26.60946  ? 34  GLU A O    1 
ATOM   452  C CB   . GLU A 1 48  ? 3.77094   15.40576  5.72040  1.000 34.79179  ? 34  GLU A CB   1 
ATOM   453  C CG   . GLU A 1 48  ? 4.76271   15.27321  4.58216  1.000 37.16115  ? 34  GLU A CG   1 
ATOM   454  C CD   . GLU A 1 48  ? 4.30612   15.99707  3.33584  1.000 49.42046  ? 34  GLU A CD   1 
ATOM   455  O OE1  . GLU A 1 48  ? 3.68438   17.07191  3.46986  1.000 52.10862  ? 34  GLU A OE1  1 
ATOM   456  O OE2  . GLU A 1 48  ? 4.55965   15.48652  2.22398  1.000 53.62457  ? 34  GLU A OE2  1 
ATOM   457  H H    . GLU A 1 48  ? 6.15936   14.46275  7.08769  1.000 30.57618  ? 34  GLU A H    1 
ATOM   458  H HA   . GLU A 1 48  ? 3.61446   14.98230  7.72773  1.000 35.27785  ? 34  GLU A HA   1 
ATOM   459  H HB2  . GLU A 1 48  ? 2.92951   15.02471  5.42427  1.000 41.80609  ? 34  GLU A HB2  1 
ATOM   460  H HB3  . GLU A 1 48  ? 3.65983   16.35130  5.90613  1.000 41.80609  ? 34  GLU A HB3  1 
ATOM   461  H HG2  . GLU A 1 48  ? 5.61317   15.65085  4.85606  1.000 44.64932  ? 34  GLU A HG2  1 
ATOM   462  H HG3  . GLU A 1 48  ? 4.87163   14.33455  4.36322  1.000 44.64932  ? 34  GLU A HG3  1 
ATOM   463  N N    . GLY A 1 49  ? 2.83972   12.73012  7.04029  1.000 29.03292  ? 35  GLY A N    1 
ATOM   464  C CA   . GLY A 1 49  ? 2.52791   11.31975  6.88564  1.000 24.92065  ? 35  GLY A CA   1 
ATOM   465  C C    . GLY A 1 49  ? 1.35857   11.12788  5.94751  1.000 26.12091  ? 35  GLY A C    1 
ATOM   466  O O    . GLY A 1 49  ? 0.41154   11.91415  5.94597  1.000 26.84460  ? 35  GLY A O    1 
ATOM   467  H H    . GLY A 1 49  ? 2.16267   13.21660  7.25133  1.000 34.89545  ? 35  GLY A H    1 
ATOM   468  H HA2  . GLY A 1 49  ? 3.29732   10.85194  6.52500  1.000 29.96072  ? 35  GLY A HA2  1 
ATOM   469  H HA3  . GLY A 1 49  ? 2.30189   10.93789  7.74819  1.000 29.96072  ? 35  GLY A HA3  1 
ATOM   470  N N    . ASP A 1 50  ? 1.43488   10.06468  5.14910  1.000 27.07437  ? 36  ASP A N    1 
ATOM   471  C CA   . ASP A 1 50  ? 0.44371   9.74820   4.12096  1.000 25.67443  ? 36  ASP A CA   1 
ATOM   472  C C    . ASP A 1 50  ? 0.00313   8.30808   4.36640  1.000 29.16789  ? 36  ASP A C    1 
ATOM   473  O O    . ASP A 1 50  ? 0.62505   7.36559   3.86789  1.000 26.79783  ? 36  ASP A O    1 
ATOM   474  C CB   . ASP A 1 50  ? 1.03324   9.94504   2.72932  1.000 27.46754  ? 36  ASP A CB   1 
ATOM   475  C CG   . ASP A 1 50  ? -0.00024  9.81734   1.63293  1.000 32.55527  ? 36  ASP A CG   1 
ATOM   476  O OD1  . ASP A 1 50  ? -1.14971  9.43355   1.93336  1.000 40.08958  ? 36  ASP A OD1  1 
ATOM   477  O OD2  . ASP A 1 50  ? 0.33984   10.10742  0.46785  1.000 39.40423  ? 36  ASP A OD2  1 
ATOM   478  H H    . ASP A 1 50  ? 2.07483   9.49131   5.18538  1.000 32.54518  ? 36  ASP A H    1 
ATOM   479  H HA   . ASP A 1 50  ? -0.32945  10.32789  4.20513  1.000 30.86525  ? 36  ASP A HA   1 
ATOM   480  H HB2  . ASP A 1 50  ? 1.42200   10.83196  2.67325  1.000 33.01698  ? 36  ASP A HB2  1 
ATOM   481  H HB3  . ASP A 1 50  ? 1.71625   9.27323   2.57743  1.000 33.01698  ? 36  ASP A HB3  1 
ATOM   482  N N    . ALA A 1 51  ? -1.07240  8.14497   5.14208  1.000 31.82207  ? 37  ALA A N    1 
ATOM   483  C CA   . ALA A 1 51  ? -1.47570  6.81377   5.58351  1.000 34.17930  ? 37  ALA A CA   1 
ATOM   484  C C    . ALA A 1 51  ? -1.98157  5.95806   4.42970  1.000 30.34145  ? 37  ALA A C    1 
ATOM   485  O O    . ALA A 1 51  ? -1.83330  4.73145   4.46253  1.000 32.82887  ? 37  ALA A O    1 
ATOM   486  C CB   . ALA A 1 51  ? -2.54635  6.92417   6.66884  1.000 34.84921  ? 37  ALA A CB   1 
ATOM   487  H H    . ALA A 1 51  ? -1.57786  8.78195   5.42203  1.000 38.24243  ? 37  ALA A H    1 
ATOM   488  H HA   . ALA A 1 51  ? -0.70228  6.36901   5.96419  1.000 41.07110  ? 37  ALA A HA   1 
ATOM   489  H HB1  . ALA A 1 51  ? -3.30729  7.40962   6.31358  1.000 41.87500  ? 37  ALA A HB1  1 
ATOM   490  H HB2  . ALA A 1 51  ? -2.81841  6.03224   6.93595  1.000 41.87500  ? 37  ALA A HB2  1 
ATOM   491  H HB3  . ALA A 1 51  ? -2.17695  7.39907   7.42970  1.000 41.87500  ? 37  ALA A HB3  1 
ATOM   492  N N    . THR A 1 52  ? -2.58397  6.57492   3.41076  1.000 29.72662  ? 38  THR A N    1 
ATOM   493  C CA   . THR A 1 52  ? -3.01302  5.81480   2.24205  1.000 28.64936  ? 38  THR A CA   1 
ATOM   494  C C    . THR A 1 52  ? -1.86058  5.02150   1.64405  1.000 27.55734  ? 38  THR A C    1 
ATOM   495  O O    . THR A 1 52  ? -2.07521  3.95217   1.06229  1.000 27.25680  ? 38  THR A O    1 
ATOM   496  C CB   . THR A 1 52  ? -3.60303  6.75535   1.18945  1.000 34.44172  ? 38  THR A CB   1 
ATOM   497  O OG1  . THR A 1 52  ? -4.79243  7.36780   1.70308  1.000 39.14770  ? 38  THR A OG1  1 
ATOM   498  C CG2  . THR A 1 52  ? -3.93409  5.99497   -0.08753 1.000 36.98026  ? 38  THR A CG2  1 
ATOM   499  H H    . THR A 1 52  ? -2.75217  7.41750   3.37384  1.000 35.72788  ? 38  THR A H    1 
ATOM   500  H HA   . THR A 1 52  ? -3.70692  5.19229   2.51015  1.000 34.43517  ? 38  THR A HA   1 
ATOM   501  H HB   . THR A 1 52  ? -2.95422  7.44309   0.97277  1.000 41.38600  ? 38  THR A HB   1 
ATOM   502  H HG1  . THR A 1 52  ? -4.62163  7.77018   2.42037  1.000 47.03318  ? 38  THR A HG1  1 
ATOM   503  H HG21 . THR A 1 52  ? -4.34241  5.14250   0.13034  1.000 44.43225  ? 38  THR A HG21 1 
ATOM   504  H HG22 . THR A 1 52  ? -4.55151  6.51028   -0.62989 1.000 44.43225  ? 38  THR A HG22 1 
ATOM   505  H HG23 . THR A 1 52  ? -3.12476  5.83511   -0.59775 1.000 44.43225  ? 38  THR A HG23 1 
ATOM   506  N N    . TYR A 1 53  ? -0.63539  5.52754   1.77456  1.000 27.55272  ? 39  TYR A N    1 
ATOM   507  C CA   . TYR A 1 53  ? 0.55762   4.84129   1.30083  1.000 27.09191  ? 39  TYR A CA   1 
ATOM   508  C C    . TYR A 1 53  ? 1.46750   4.40792   2.44340  1.000 24.33303  ? 39  TYR A C    1 
ATOM   509  O O    . TYR A 1 53  ? 2.56660   3.90505   2.19125  1.000 26.65830  ? 39  TYR A O    1 
ATOM   510  C CB   . TYR A 1 53  ? 1.32710   5.73927   0.32865  1.000 29.37447  ? 39  TYR A CB   1 
ATOM   511  C CG   . TYR A 1 53  ? 0.59085   6.01286   -0.96622 1.000 32.48199  ? 39  TYR A CG   1 
ATOM   512  C CD1  . TYR A 1 53  ? 0.69523   5.14244   -2.04282 1.000 27.82825  ? 39  TYR A CD1  1 
ATOM   513  C CD2  . TYR A 1 53  ? -0.20683  7.14061   -1.11181 1.000 34.45574  ? 39  TYR A CD2  1 
ATOM   514  C CE1  . TYR A 1 53  ? 0.02772   5.38491   -3.22474 1.000 30.34288  ? 39  TYR A CE1  1 
ATOM   515  C CE2  . TYR A 1 53  ? -0.87897  7.39244   -2.29313 1.000 37.48896  ? 39  TYR A CE2  1 
ATOM   516  C CZ   . TYR A 1 53  ? -0.75833  6.50925   -3.34619 1.000 32.02480  ? 39  TYR A CZ   1 
ATOM   517  O OH   . TYR A 1 53  ? -1.42282  6.74705   -4.52670 1.000 31.75587  ? 39  TYR A OH   1 
ATOM   518  H H    . TYR A 1 53  ? -0.46876  6.28614   2.14382  1.000 33.11921  ? 39  TYR A H    1 
ATOM   519  H HA   . TYR A 1 53  ? 0.28660   4.04369   0.81991  1.000 32.56623  ? 39  TYR A HA   1 
ATOM   520  H HB2  . TYR A 1 53  ? 1.49516   6.59216   0.75905  1.000 35.30530  ? 39  TYR A HB2  1 
ATOM   521  H HB3  . TYR A 1 53  ? 2.16732   5.30889   0.10573  1.000 35.30530  ? 39  TYR A HB3  1 
ATOM   522  H HD1  . TYR A 1 53  ? 1.22500   4.38202   -1.96540 1.000 33.44984  ? 39  TYR A HD1  1 
ATOM   523  H HD2  . TYR A 1 53  ? -0.29011  7.73633   -0.40252 1.000 41.40283  ? 39  TYR A HD2  1 
ATOM   524  H HE1  . TYR A 1 53  ? 0.10795   4.79191   -3.93666 1.000 36.46739  ? 39  TYR A HE1  1 
ATOM   525  H HE2  . TYR A 1 53  ? -1.40889  8.15202   -2.37751 1.000 45.04270  ? 39  TYR A HE2  1 
ATOM   526  H HH   . TYR A 1 53  ? -1.92482  7.41547   -4.44421 1.000 37.82734  ? 39  TYR A HH   1 
ATOM   527  N N    . GLY A 1 54  ? 1.03657   4.58436   3.68971  1.000 25.45542  ? 40  GLY A N    1 
ATOM   528  C CA   . GLY A 1 54  ? 1.87689   4.24015   4.82240  1.000 25.92544  ? 40  GLY A CA   1 
ATOM   529  C C    . GLY A 1 54  ? 3.22603   4.91805   4.79860  1.000 27.68321  ? 40  GLY A C    1 
ATOM   530  O O    . GLY A 1 54  ? 4.20034   4.36338   5.31576  1.000 24.27819  ? 40  GLY A O    1 
ATOM   531  H H    . GLY A 1 54  ? 0.26528   4.90025   3.90167  1.000 30.60245  ? 40  GLY A H    1 
ATOM   532  H HA2  . GLY A 1 54  ? 1.42483   4.49706   5.64127  1.000 31.16646  ? 40  GLY A HA2  1 
ATOM   533  H HA3  . GLY A 1 54  ? 2.02152   3.28102   4.82907  1.000 31.16646  ? 40  GLY A HA3  1 
ATOM   534  N N    . LYS A 1 55  ? 3.30792   6.11207   4.21629  1.000 26.67443  ? 41  LYS A N    1 
ATOM   535  C CA   . LYS A 1 55  ? 4.57324   6.79298   3.98271  1.000 25.68039  ? 41  LYS A CA   1 
ATOM   536  C C    . LYS A 1 55  ? 4.80030   7.88537   5.01725  1.000 28.04214  ? 41  LYS A C    1 
ATOM   537  O O    . LYS A 1 55  ? 3.88386   8.64048   5.35425  1.000 30.08037  ? 41  LYS A O    1 
ATOM   538  C CB   . LYS A 1 55  ? 4.60372   7.40402   2.58055  1.000 33.09976  ? 41  LYS A CB   1 
ATOM   539  C CG   . LYS A 1 55  ? 5.95182   7.97769   2.17500  1.000 31.27747  ? 41  LYS A CG   1 
ATOM   540  C CD   . LYS A 1 55  ? 5.91111   8.51638   0.75142  1.000 40.89241  ? 41  LYS A CD   1 
ATOM   541  C CE   . LYS A 1 55  ? 7.30257   8.84355   0.23546  1.000 53.84325  ? 41  LYS A CE   1 
ATOM   542  N NZ   . LYS A 1 55  ? 7.29149   9.20892   -1.21149 1.000 56.35171  ? 41  LYS A NZ   1 
ATOM   543  H H    . LYS A 1 55  ? 2.62525   6.55715   3.94158  1.000 32.06526  ? 41  LYS A H    1 
ATOM   544  H HA   . LYS A 1 55  ? 5.29541   6.15048   4.06377  1.000 30.87240  ? 41  LYS A HA   1 
ATOM   545  H HB2  . LYS A 1 55  ? 4.37258   6.71524   1.93786  1.000 39.77566  ? 41  LYS A HB2  1 
ATOM   546  H HB3  . LYS A 1 55  ? 3.95499   8.12418   2.54278  1.000 39.77566  ? 41  LYS A HB3  1 
ATOM   547  H HG2  . LYS A 1 55  ? 6.18583   8.70565   2.77184  1.000 37.58890  ? 41  LYS A HG2  1 
ATOM   548  H HG3  . LYS A 1 55  ? 6.62591   7.28168   2.22043  1.000 37.58890  ? 41  LYS A HG3  1 
ATOM   549  H HD2  . LYS A 1 55  ? 5.51919   7.84874   0.16699  1.000 49.12683  ? 41  LYS A HD2  1 
ATOM   550  H HD3  . LYS A 1 55  ? 5.38039   9.32805   0.73073  1.000 49.12683  ? 41  LYS A HD3  1 
ATOM   551  H HE2  . LYS A 1 55  ? 7.65958   9.59468   0.73471  1.000 64.66784  ? 41  LYS A HE2  1 
ATOM   552  H HE3  . LYS A 1 55  ? 7.87492   8.06849   0.34768  1.000 64.66784  ? 41  LYS A HE3  1 
ATOM   553  H HZ1  . LYS A 1 55  ? 8.11065   9.43723   -1.47407 1.000 67.67799  ? 41  LYS A HZ1  1 
ATOM   554  H HZ2  . LYS A 1 55  ? 7.01454   8.51706   -1.69804 1.000 67.67799  ? 41  LYS A HZ2  1 
ATOM   555  H HZ3  . LYS A 1 55  ? 6.74250   9.89605   -1.34774 1.000 67.67799  ? 41  LYS A HZ3  1 
ATOM   556  N N    . LEU A 1 56  ? 6.03433   7.97283   5.50506  1.000 27.86672  ? 42  LEU A N    1 
ATOM   557  C CA   . LEU A 1 56  ? 6.43948   9.00522   6.44762  1.000 25.67913  ? 42  LEU A CA   1 
ATOM   558  C C    . LEU A 1 56  ? 7.70738   9.66840   5.93310  1.000 30.41700  ? 42  LEU A C    1 
ATOM   559  O O    . LEU A 1 56  ? 8.68769   8.98378   5.62288  1.000 26.62060  ? 42  LEU A O    1 
ATOM   560  C CB   . LEU A 1 56  ? 6.66886   8.41928   7.84480  1.000 27.38567  ? 42  LEU A CB   1 
ATOM   561  C CG   . LEU A 1 56  ? 5.39916   8.06561   8.62171  1.000 28.05111  ? 42  LEU A CG   1 
ATOM   562  C CD1  . LEU A 1 56  ? 5.69523   7.01643   9.68060  1.000 33.02310  ? 42  LEU A CD1  1 
ATOM   563  C CD2  . LEU A 1 56  ? 4.79786   9.30836   9.25898  1.000 27.02759  ? 42  LEU A CD2  1 
ATOM   564  H H    . LEU A 1 56  ? 6.66915   7.43073   5.29833  1.000 33.49601  ? 42  LEU A H    1 
ATOM   565  H HA   . LEU A 1 56  ? 5.74660   9.68075   6.51458  1.000 30.87089  ? 42  LEU A HA   1 
ATOM   566  H HB2  . LEU A 1 56  ? 7.18901   7.60571   7.75292  1.000 32.91875  ? 42  LEU A HB2  1 
ATOM   567  H HB3  . LEU A 1 56  ? 7.15983   9.06925   8.37148  1.000 32.91875  ? 42  LEU A HB3  1 
ATOM   568  H HG   . LEU A 1 56  ? 4.74716   7.69707   8.00529  1.000 33.71727  ? 42  LEU A HG   1 
ATOM   569  H HD11 . LEU A 1 56  ? 6.03240   6.21678   9.24726  1.000 39.68366  ? 42  LEU A HD11 1 
ATOM   570  H HD12 . LEU A 1 56  ? 6.36051   7.36578   10.29400 1.000 39.68366  ? 42  LEU A HD12 1 
ATOM   571  H HD13 . LEU A 1 56  ? 4.87734   6.81267   10.16065 1.000 39.68366  ? 42  LEU A HD13 1 
ATOM   572  H HD21 . LEU A 1 56  ? 3.91741   9.09195   9.60375  1.000 32.48905  ? 42  LEU A HD21 1 
ATOM   573  H HD22 . LEU A 1 56  ? 5.37334   9.60222   9.98242  1.000 32.48905  ? 42  LEU A HD22 1 
ATOM   574  H HD23 . LEU A 1 56  ? 4.72819   10.00521  8.58783  1.000 32.48905  ? 42  LEU A HD23 1 
ATOM   575  N N    . THR A 1 57  ? 7.67550   10.99464  5.81942  1.000 25.50687  ? 43  THR A N    1 
ATOM   576  C CA   . THR A 1 57  ? 8.85280   11.79492  5.50370  1.000 26.37369  ? 43  THR A CA   1 
ATOM   577  C C    . THR A 1 57  ? 9.05844   12.78569  6.64005  1.000 28.18001  ? 43  THR A C    1 
ATOM   578  O O    . THR A 1 57  ? 8.21256   13.65753  6.86689  1.000 30.55722  ? 43  THR A O    1 
ATOM   579  C CB   . THR A 1 57  ? 8.70042   12.52260  4.16470  1.000 25.90556  ? 43  THR A CB   1 
ATOM   580  O OG1  . THR A 1 57  ? 7.41308   13.14748  4.09115  1.000 35.60710  ? 43  THR A OG1  1 
ATOM   581  C CG2  . THR A 1 57  ? 8.85463   11.55260  3.00890  1.000 25.44802  ? 43  THR A CG2  1 
ATOM   582  H H    . THR A 1 57  ? 6.96283   11.46449  5.92401  1.000 30.66418  ? 43  THR A H    1 
ATOM   583  H HA   . THR A 1 57  ? 9.63244   11.22182  5.43584  1.000 31.70436  ? 43  THR A HA   1 
ATOM   584  H HB   . THR A 1 57  ? 9.38986   13.20089  4.09057  1.000 31.14261  ? 43  THR A HB   1 
ATOM   585  H HG1  . THR A 1 57  ? 7.35232   13.74966  4.67363  1.000 42.78446  ? 43  THR A HG1  1 
ATOM   586  H HG21 . THR A 1 57  ? 8.94694   12.04101  2.17594  1.000 30.59356  ? 43  THR A HG21 1 
ATOM   587  H HG22 . THR A 1 57  ? 9.64272   11.00256  3.14030  1.000 30.59356  ? 43  THR A HG22 1 
ATOM   588  H HG23 . THR A 1 57  ? 8.07542   10.97771  2.95205  1.000 30.59356  ? 43  THR A HG23 1 
ATOM   589  N N    . LEU A 1 58  ? 10.17364  12.64581  7.35391  1.000 27.00608  ? 44  LEU A N    1 
ATOM   590  C CA   . LEU A 1 58  ? 10.42224  13.41209  8.56484  1.000 26.64564  ? 44  LEU A CA   1 
ATOM   591  C C    . LEU A 1 58  ? 11.87458  13.86144  8.60298  1.000 29.44228  ? 44  LEU A C    1 
ATOM   592  O O    . LEU A 1 58  ? 12.76514  13.18472  8.08280  1.000 30.42815  ? 44  LEU A O    1 
ATOM   593  C CB   . LEU A 1 58  ? 10.10117  12.58480  9.81853  1.000 26.78371  ? 44  LEU A CB   1 
ATOM   594  C CG   . LEU A 1 58  ? 8.62640   12.25568  10.05151 1.000 25.66995  ? 44  LEU A CG   1 
ATOM   595  C CD1  . LEU A 1 58  ? 8.48648   11.05687  10.96190 1.000 27.71385  ? 44  LEU A CD1  1 
ATOM   596  C CD2  . LEU A 1 58  ? 7.90453   13.45476  10.64331 1.000 30.70963  ? 44  LEU A CD2  1 
ATOM   597  H H    . LEU A 1 58  ? 10.80967  12.10363  7.15115  1.000 32.46324  ? 44  LEU A H    1 
ATOM   598  H HA   . LEU A 1 58  ? 9.86661   14.20718  8.56298  1.000 32.03071  ? 44  LEU A HA   1 
ATOM   599  H HB2  . LEU A 1 58  ? 10.57574  11.74137  9.75289  1.000 32.19639  ? 44  LEU A HB2  1 
ATOM   600  H HB3  . LEU A 1 58  ? 10.40987  13.07972  10.59355 1.000 32.19639  ? 44  LEU A HB3  1 
ATOM   601  H HG   . LEU A 1 58  ? 8.21339   12.03885  9.20103  1.000 30.85988  ? 44  LEU A HG   1 
ATOM   602  H HD11 . LEU A 1 58  ? 8.68958   10.25282  10.45876 1.000 33.31256  ? 44  LEU A HD11 1 
ATOM   603  H HD12 . LEU A 1 58  ? 9.10594   11.14885  11.70265 1.000 33.31256  ? 44  LEU A HD12 1 
ATOM   604  H HD13 . LEU A 1 58  ? 7.57624   11.01767  11.29481 1.000 33.31256  ? 44  LEU A HD13 1 
ATOM   605  H HD21 . LEU A 1 58  ? 6.96603   13.23565  10.75337 1.000 36.90750  ? 44  LEU A HD21 1 
ATOM   606  H HD22 . LEU A 1 58  ? 8.29786   13.66685  11.50425 1.000 36.90750  ? 44  LEU A HD22 1 
ATOM   607  H HD23 . LEU A 1 58  ? 7.99963   14.20935  10.04128 1.000 36.90750  ? 44  LEU A HD23 1 
ATOM   608  N N    . LYS A 1 59  ? 12.10214  15.01789  9.22354  1.000 26.82417  ? 45  LYS A N    1 
ATOM   609  C CA   . LYS A 1 59  ? 13.44318  15.52407  9.48209  1.000 28.83556  ? 45  LYS A CA   1 
ATOM   610  C C    . LYS A 1 59  ? 13.57069  15.82263  10.96708 1.000 30.28621  ? 45  LYS A C    1 
ATOM   611  O O    . LYS A 1 59  ? 12.70900  16.49499  11.54276 1.000 30.89535  ? 45  LYS A O    1 
ATOM   612  C CB   . LYS A 1 59  ? 13.74178  16.78538  8.66632  1.000 29.49462  ? 45  LYS A CB   1 
ATOM   613  C CG   . LYS A 1 59  ? 15.17129  17.28375  8.83429  1.000 32.59537  ? 45  LYS A CG   1 
ATOM   614  C CD   . LYS A 1 59  ? 15.39485  18.62084  8.15886  1.000 34.18028  ? 45  LYS A CD   1 
ATOM   615  C CE   . LYS A 1 59  ? 16.80286  19.13852  8.42354  1.000 34.34245  ? 45  LYS A CE   1 
ATOM   616  N NZ   . LYS A 1 59  ? 17.08196  20.40660  7.69419  1.000 40.78013  ? 45  LYS A NZ   1 
ATOM   617  H H    . LYS A 1 59  ? 11.47931  15.53723  9.50984  1.000 32.24494  ? 45  LYS A H    1 
ATOM   618  H HA   . LYS A 1 59  ? 14.09524  14.84901  9.23712  1.000 34.65861  ? 45  LYS A HA   1 
ATOM   619  H HB2  . LYS A 1 59  ? 13.60160  16.59181  7.72622  1.000 35.44948  ? 45  LYS A HB2  1 
ATOM   620  H HB3  . LYS A 1 59  ? 13.14329  17.49320  8.95214  1.000 35.44948  ? 45  LYS A HB3  1 
ATOM   621  H HG2  . LYS A 1 59  ? 15.36360  17.38715  9.77940  1.000 39.17038  ? 45  LYS A HG2  1 
ATOM   622  H HG3  . LYS A 1 59  ? 15.78121  16.64074  8.44003  1.000 39.17038  ? 45  LYS A HG3  1 
ATOM   623  H HD2  . LYS A 1 59  ? 15.27929  18.52218  7.20084  1.000 41.07228  ? 45  LYS A HD2  1 
ATOM   624  H HD3  . LYS A 1 59  ? 14.76010  19.26765  8.50473  1.000 41.07228  ? 45  LYS A HD3  1 
ATOM   625  H HE2  . LYS A 1 59  ? 16.90708  19.30687  9.37311  1.000 41.26687  ? 45  LYS A HE2  1 
ATOM   626  H HE3  . LYS A 1 59  ? 17.44659  18.47415  8.13177  1.000 41.26687  ? 45  LYS A HE3  1 
ATOM   627  H HZ1  . LYS A 1 59  ? 17.87595  20.72817  7.93558  1.000 48.99209  ? 45  LYS A HZ1  1 
ATOM   628  H HZ2  . LYS A 1 59  ? 17.08492  20.25867  6.81657  1.000 48.99209  ? 45  LYS A HZ2  1 
ATOM   629  H HZ3  . LYS A 1 59  ? 16.45615  21.01053  7.88319  1.000 48.99209  ? 45  LYS A HZ3  1 
ATOM   630  N N    . PHE A 1 60  ? 14.64221  15.32754  11.58010 1.000 31.44944  ? 46  PHE A N    1 
ATOM   631  C CA   . PHE A 1 60  ? 14.89930  15.51625  12.99999 1.000 25.43373  ? 46  PHE A CA   1 
ATOM   632  C C    . PHE A 1 60  ? 16.22467  16.23809  13.19159 1.000 25.72796  ? 46  PHE A C    1 
ATOM   633  O O    . PHE A 1 60  ? 17.18270  16.00303  12.44947 1.000 29.83630  ? 46  PHE A O    1 
ATOM   634  C CB   . PHE A 1 60  ? 14.93539  14.17610  13.73892 1.000 24.44477  ? 46  PHE A CB   1 
ATOM   635  C CG   . PHE A 1 60  ? 13.68095  13.36588  13.58996 1.000 27.89298  ? 46  PHE A CG   1 
ATOM   636  C CD1  . PHE A 1 60  ? 12.60750  13.56824  14.44141 1.000 23.55466  ? 46  PHE A CD1  1 
ATOM   637  C CD2  . PHE A 1 60  ? 13.57718  12.39441  12.60403 1.000 23.14532  ? 46  PHE A CD2  1 
ATOM   638  C CE1  . PHE A 1 60  ? 11.45072  12.82330  14.31131 1.000 25.85152  ? 46  PHE A CE1  1 
ATOM   639  C CE2  . PHE A 1 60  ? 12.42312  11.64277  12.46879 1.000 17.40769  ? 46  PHE A CE2  1 
ATOM   640  C CZ   . PHE A 1 60  ? 11.35743  11.85824  13.32362 1.000 23.60809  ? 46  PHE A CZ   1 
ATOM   641  H H    . PHE A 1 60  ? 15.24931  14.86686  11.18161 1.000 37.79527  ? 46  PHE A H    1 
ATOM   642  H HA   . PHE A 1 60  ? 14.19405  16.06061  13.38365 1.000 30.57641  ? 46  PHE A HA   1 
ATOM   643  H HB2  . PHE A 1 60  ? 15.67108  13.64835  13.39086 1.000 29.38967  ? 46  PHE A HB2  1 
ATOM   644  H HB3  . PHE A 1 60  ? 15.06708  14.34558  14.68487 1.000 29.38967  ? 46  PHE A HB3  1 
ATOM   645  H HD1  . PHE A 1 60  ? 12.66583  14.21327  15.10881 1.000 28.32153  ? 46  PHE A HD1  1 
ATOM   646  H HD2  . PHE A 1 60  ? 14.29177  12.24685  12.02741 1.000 27.83033  ? 46  PHE A HD2  1 
ATOM   647  H HE1  . PHE A 1 60  ? 10.73539  12.97039  14.88712 1.000 31.07777  ? 46  PHE A HE1  1 
ATOM   648  H HE2  . PHE A 1 60  ? 12.36430  10.99435  11.80472 1.000 20.94517  ? 46  PHE A HE2  1 
ATOM   649  H HZ   . PHE A 1 60  ? 10.57989  11.35578  13.23494 1.000 28.38564  ? 46  PHE A HZ   1 
ATOM   650  N N    . ILE A 1 61  ? 16.27785  17.11604  14.19138 1.000 28.60683  ? 47  ILE A N    1 
ATOM   651  C CA   A ILE A 1 61  ? 17.49405  17.84456  14.52473 0.692 30.13643  ? 47  ILE A CA   1 
ATOM   652  C CA   B ILE A 1 61  ? 17.49526  17.84174  14.52398 0.308 28.84837  ? 47  ILE A CA   1 
ATOM   653  C C    . ILE A 1 61  ? 17.65113  17.87142  16.03717 1.000 31.06607  ? 47  ILE A C    1 
ATOM   654  O O    . ILE A 1 61  ? 16.66815  17.85773  16.78460 1.000 30.75254  ? 47  ILE A O    1 
ATOM   655  C CB   A ILE A 1 61  ? 17.48944  19.28624  13.96528 0.692 31.16546  ? 47  ILE A CB   1 
ATOM   656  C CB   B ILE A 1 61  ? 17.49204  19.27664  13.94944 0.308 32.09641  ? 47  ILE A CB   1 
ATOM   657  C CG1  A ILE A 1 61  ? 16.34688  20.10146  14.57998 0.692 33.12064  ? 47  ILE A CG1  1 
ATOM   658  C CG1  B ILE A 1 61  ? 16.36923  20.10734  14.57414 0.308 33.07354  ? 47  ILE A CG1  1 
ATOM   659  C CG2  A ILE A 1 61  ? 17.37606  19.26811  12.44769 0.692 32.19347  ? 47  ILE A CG2  1 
ATOM   660  C CG2  B ILE A 1 61  ? 17.34647  19.24356  12.43551 0.308 32.43899  ? 47  ILE A CG2  1 
ATOM   661  C CD1  A ILE A 1 61  ? 16.38243  21.57143  14.21298 0.692 35.86897  ? 47  ILE A CD1  1 
ATOM   662  C CD1  B ILE A 1 61  ? 16.83705  21.02814  15.67974 0.308 33.00866  ? 47  ILE A CD1  1 
ATOM   663  H H    . ILE A 1 61  ? 15.60872  17.30680  14.69683 1.000 34.38414  ? 47  ILE A H    1 
ATOM   664  H HA   . ILE A 1 61  ? 18.25028  17.37311  14.14164 1.000 34.67399  ? 47  ILE A HA   1 
ATOM   665  H HB   A ILE A 1 61  ? 18.32891  19.70728  14.20799 0.692 37.45449  ? 47  ILE A HB   1 
ATOM   666  H HB   B ILE A 1 61  ? 18.34007  19.69159  14.17208 0.308 38.57163  ? 47  ILE A HB   1 
ATOM   667  H HG12 A ILE A 1 61  ? 15.50244  19.73879  14.26968 0.692 39.80071  ? 47  ILE A HG12 1 
ATOM   668  H HG12 B ILE A 1 61  ? 15.96497  20.65530  13.88334 0.308 39.74419  ? 47  ILE A HG12 1 
ATOM   669  H HG13 A ILE A 1 61  ? 16.40113  20.03577  15.54623 0.692 39.80071  ? 47  ILE A HG13 1 
ATOM   670  H HG13 B ILE A 1 61  ? 15.70768  19.50555  14.94977 0.308 39.74419  ? 47  ILE A HG13 1 
ATOM   671  H HG21 A ILE A 1 61  ? 17.52888  20.16407  12.10886 0.692 38.68810  ? 47  ILE A HG21 1 
ATOM   672  H HG21 B ILE A 1 61  ? 17.48180  20.13808  12.08562 0.308 38.98273  ? 47  ILE A HG21 1 
ATOM   673  H HG22 A ILE A 1 61  ? 18.04157  18.66066  12.08852 0.692 38.68810  ? 47  ILE A HG22 1 
ATOM   674  H HG22 B ILE A 1 61  ? 18.01101  18.64038  12.06746 0.308 38.98273  ? 47  ILE A HG22 1 
ATOM   675  H HG23 A ILE A 1 61  ? 16.48715  18.96832  12.20097 0.692 38.68810  ? 47  ILE A HG23 1 
ATOM   676  H HG23 B ILE A 1 61  ? 16.45596  18.93162  12.21062 0.308 38.98273  ? 47  ILE A HG23 1 
ATOM   677  H HD11 A ILE A 1 61  ? 15.68171  22.03499  14.69776 0.692 43.09871  ? 47  ILE A HD11 1 
ATOM   678  H HD11 B ILE A 1 61  ? 16.06901  21.48649  16.05515 0.308 39.66633  ? 47  ILE A HD11 1 
ATOM   679  H HD12 A ILE A 1 61  ? 17.24833  21.93622  14.45389 0.692 43.09871  ? 47  ILE A HD12 1 
ATOM   680  H HD12 B ILE A 1 61  ? 17.27534  20.50068  16.36574 0.308 39.66633  ? 47  ILE A HD12 1 
ATOM   681  H HD13 A ILE A 1 61  ? 16.23946  21.66201  13.25786 0.692 43.09871  ? 47  ILE A HD13 1 
ATOM   682  H HD13 B ILE A 1 61  ? 17.45974  21.67384  15.31065 0.308 39.66633  ? 47  ILE A HD13 1 
ATOM   683  N N    . SER A 1 62  ? 18.90069  17.90617  16.48336 1.000 29.36471  ? 48  SER A N    1 
ATOM   684  C CA   . SER A 1 62  ? 19.21291  18.11006  17.88747 1.000 30.15751  ? 48  SER A CA   1 
ATOM   685  C C    . SER A 1 62  ? 19.34309  19.60527  18.14085 1.000 27.82182  ? 48  SER A C    1 
ATOM   686  O O    . SER A 1 62  ? 20.02600  20.30902  17.39080 1.000 28.84623  ? 48  SER A O    1 
ATOM   687  C CB   . SER A 1 62  ? 20.50778  17.40244  18.27432 1.000 30.81393  ? 48  SER A CB   1 
ATOM   688  O OG   . SER A 1 62  ? 20.90901  17.79713  19.57303 1.000 32.38426  ? 48  SER A OG   1 
ATOM   689  H H    . SER A 1 62  ? 19.59406  17.81253  15.98328 1.000 35.29359  ? 48  SER A H    1 
ATOM   690  H HA   . SER A 1 62  ? 18.50246  17.74493  18.43777 1.000 36.24495  ? 48  SER A HA   1 
ATOM   691  H HB2  . SER A 1 62  ? 20.36237  16.44346  18.26340 1.000 37.03266  ? 48  SER A HB2  1 
ATOM   692  H HB3  . SER A 1 62  ? 21.20238  17.63991  17.64026 1.000 37.03266  ? 48  SER A HB3  1 
ATOM   693  H HG   . SER A 1 62  ? 20.30621  17.61305  20.12832 1.000 38.91705  ? 48  SER A HG   1 
ATOM   694  N N    . THR A 1 63  ? 18.68050  20.08750  19.18667 1.000 31.68535  ? 49  THR A N    1 
ATOM   695  C CA   . THR A 1 63  ? 18.76927  21.48313  19.58712 1.000 32.83822  ? 49  THR A CA   1 
ATOM   696  C C    . THR A 1 63  ? 19.73921  21.69261  20.74280 1.000 34.22886  ? 49  THR A C    1 
ATOM   697  O O    . THR A 1 63  ? 19.82353  22.80414  21.27389 1.000 32.06948  ? 49  THR A O    1 
ATOM   698  C CB   . THR A 1 63  ? 17.38345  22.00970  19.96633 1.000 32.49341  ? 49  THR A CB   1 
ATOM   699  O OG1  . THR A 1 63  ? 16.84818  21.23227  21.04489 1.000 35.17192  ? 49  THR A OG1  1 
ATOM   700  C CG2  . THR A 1 63  ? 16.44033  21.92700  18.77861 1.000 31.84608  ? 49  THR A CG2  1 
ATOM   701  H H    . THR A 1 63  ? 18.16447  19.61585  19.68753 1.000 38.07836  ? 49  THR A H    1 
ATOM   702  H HA   . THR A 1 63  ? 19.08784  22.00280  18.83257 1.000 39.46181  ? 49  THR A HA   1 
ATOM   703  H HB   . THR A 1 63  ? 17.45659  22.93720  20.24072 1.000 39.04803  ? 49  THR A HB   1 
ATOM   704  H HG1  . THR A 1 63  ? 17.31570  21.33779  21.73474 1.000 42.26224  ? 49  THR A HG1  1 
ATOM   705  H HG21 . THR A 1 63  ? 16.39208  21.01340  18.45627 1.000 38.27123  ? 49  THR A HG21 1 
ATOM   706  H HG22 . THR A 1 63  ? 15.55195  22.21605  19.03964 1.000 38.27123  ? 49  THR A HG22 1 
ATOM   707  H HG23 . THR A 1 63  ? 16.75895  22.49737  18.06163 1.000 38.27123  ? 49  THR A HG23 1 
ATOM   708  N N    . THR A 1 64  ? 20.48387  20.65163  21.13106 1.000 27.74505  ? 50  THR A N    1 
ATOM   709  C CA   . THR A 1 64  ? 21.38048  20.70998  22.27959 1.000 35.31100  ? 50  THR A CA   1 
ATOM   710  C C    . THR A 1 64  ? 22.76609  20.16273  21.94933 1.000 38.92802  ? 50  THR A C    1 
ATOM   711  O O    . THR A 1 64  ? 23.50411  19.77299  22.86050 1.000 37.75873  ? 50  THR A O    1 
ATOM   712  C CB   . THR A 1 64  ? 20.78306  19.94032  23.46201 1.000 36.12625  ? 50  THR A CB   1 
ATOM   713  O OG1  . THR A 1 64  ? 20.44302  18.61238  23.04232 1.000 33.61171  ? 50  THR A OG1  1 
ATOM   714  C CG2  . THR A 1 64  ? 19.53345  20.64028  23.98395 1.000 33.77547  ? 50  THR A CG2  1 
ATOM   715  H H    . THR A 1 64  ? 20.48409  19.88825  20.73502 1.000 33.35000  ? 50  THR A H    1 
ATOM   716  H HA   . THR A 1 64  ? 21.48746  21.63775  22.54168 1.000 42.42913  ? 50  THR A HA   1 
ATOM   717  H HB   . THR A 1 64  ? 21.43115  19.89911  24.18255 1.000 43.40744  ? 50  THR A HB   1 
ATOM   718  H HG1  . THR A 1 64  ? 21.10897  18.24411  22.68666 1.000 40.38999  ? 50  THR A HG1  1 
ATOM   719  H HG21 . THR A 1 64  ? 19.71879  21.58015  24.13624 1.000 40.58650  ? 50  THR A HG21 1 
ATOM   720  H HG22 . THR A 1 64  ? 18.81472  20.56190  23.33728 1.000 40.58650  ? 50  THR A HG22 1 
ATOM   721  H HG23 . THR A 1 64  ? 19.25098  20.23578  24.81911 1.000 40.58650  ? 50  THR A HG23 1 
ATOM   722  N N    . GLY A 1 65  ? 23.13173  20.11818  20.67240 1.000 32.68358  ? 51  GLY A N    1 
ATOM   723  C CA   . GLY A 1 65  ? 24.44545  19.65972  20.26151 1.000 30.99045  ? 51  GLY A CA   1 
ATOM   724  C C    . GLY A 1 65  ? 24.43468  18.22649  19.76792 1.000 29.08698  ? 51  GLY A C    1 
ATOM   725  O O    . GLY A 1 65  ? 23.39145  17.58370  19.61736 1.000 32.40005  ? 51  GLY A O    1 
ATOM   726  H H    . GLY A 1 65  ? 22.62596  20.35277  20.01760 1.000 39.27624  ? 51  GLY A H    1 
ATOM   727  H HA2  . GLY A 1 65  ? 24.77271  20.22616  19.54531 1.000 37.24447  ? 51  GLY A HA2  1 
ATOM   728  H HA3  . GLY A 1 65  ? 25.05480  19.71825  21.01395 1.000 37.24447  ? 51  GLY A HA3  1 
ATOM   729  N N    . LYS A 1 66  ? 25.64036  17.72196  19.50883 1.000 32.49659  ? 52  LYS A N    1 
ATOM   730  C CA   . LYS A 1 66  ? 25.79762  16.33554  19.08760 1.000 38.75847  ? 52  LYS A CA   1 
ATOM   731  C C    . LYS A 1 66  ? 25.13315  15.40498  20.09270 1.000 33.64953  ? 52  LYS A C    1 
ATOM   732  O O    . LYS A 1 66  ? 25.35063  15.51900  21.30229 1.000 38.40185  ? 52  LYS A O    1 
ATOM   733  C CB   . LYS A 1 66  ? 27.28149  15.99117  18.94664 1.000 35.78252  ? 52  LYS A CB   1 
ATOM   734  H H    . LYS A 1 66  ? 26.37761  18.16055  19.56958 1.000 39.05185  ? 52  LYS A H    1 
ATOM   735  H HA   . LYS A 1 66  ? 25.37903  16.21057  18.22153 1.000 46.56611  ? 52  LYS A HA   1 
ATOM   736  N N    . LEU A 1 67  ? 24.31359  14.48878  19.58660 1.000 28.98802  ? 53  LEU A N    1 
ATOM   737  C CA   . LEU A 1 67  ? 23.57127  13.60319  20.46435 1.000 25.78480  ? 53  LEU A CA   1 
ATOM   738  C C    . LEU A 1 67  ? 24.53012  12.68680  21.22391 1.000 30.39138  ? 53  LEU A C    1 
ATOM   739  O O    . LEU A 1 67  ? 25.57627  12.29618  20.69925 1.000 31.51715  ? 53  LEU A O    1 
ATOM   740  C CB   . LEU A 1 67  ? 22.57971  12.75850  19.66948 1.000 26.65805  ? 53  LEU A CB   1 
ATOM   741  C CG   . LEU A 1 67  ? 21.37402  13.45762  19.04576 1.000 28.18461  ? 53  LEU A CG   1 
ATOM   742  C CD1  . LEU A 1 67  ? 20.47287  12.41849  18.39224 1.000 31.19916  ? 53  LEU A CD1  1 
ATOM   743  C CD2  . LEU A 1 67  ? 20.60162  14.25961  20.07456 1.000 29.31308  ? 53  LEU A CD2  1 
ATOM   744  H H    . LEU A 1 67  ? 24.17330  14.36335  18.74744 1.000 34.84157  ? 53  LEU A H    1 
ATOM   745  H HA   . LEU A 1 67  ? 23.07167  14.13195  21.10600 1.000 30.99770  ? 53  LEU A HA   1 
ATOM   746  H HB2  . LEU A 1 67  ? 23.06645  12.34176  18.94126 1.000 32.04560  ? 53  LEU A HB2  1 
ATOM   747  H HB3  . LEU A 1 67  ? 22.22872  12.07873  20.26581 1.000 32.04560  ? 53  LEU A HB3  1 
ATOM   748  H HG   . LEU A 1 67  ? 21.68275  14.08390  18.37244 1.000 33.87747  ? 53  LEU A HG   1 
ATOM   749  H HD11 . LEU A 1 67  ? 20.97458  11.95283  17.70497 1.000 37.49493  ? 53  LEU A HD11 1 
ATOM   750  H HD12 . LEU A 1 67  ? 20.17477  11.78939  19.06772 1.000 37.49493  ? 53  LEU A HD12 1 
ATOM   751  H HD13 . LEU A 1 67  ? 19.70861  12.86676  17.99745 1.000 37.49493  ? 53  LEU A HD13 1 
ATOM   752  H HD21 . LEU A 1 67  ? 19.76627  14.55674  19.68112 1.000 35.23163  ? 53  LEU A HD21 1 
ATOM   753  H HD22 . LEU A 1 67  ? 20.42306  13.69709  20.84436 1.000 35.23163  ? 53  LEU A HD22 1 
ATOM   754  H HD23 . LEU A 1 67  ? 21.13283  15.02619  20.34114 1.000 35.23163  ? 53  LEU A HD23 1 
ATOM   755  N N    . PRO A 1 68  ? 24.19818  12.33155  22.46880 1.000 30.53583  ? 54  PRO A N    1 
ATOM   756  C CA   . PRO A 1 68  ? 25.00015  11.33185  23.18581 1.000 32.53743  ? 54  PRO A CA   1 
ATOM   757  C C    . PRO A 1 68  ? 24.74792  9.90680   22.72369 1.000 31.72517  ? 54  PRO A C    1 
ATOM   758  O O    . PRO A 1 68  ? 25.47915  9.00058   23.14452 1.000 28.10059  ? 54  PRO A O    1 
ATOM   759  C CB   . PRO A 1 68  ? 24.56624  11.52529  24.64533 1.000 34.88914  ? 54  PRO A CB   1 
ATOM   760  C CG   . PRO A 1 68  ? 23.17098  12.02571  24.54865 1.000 31.58973  ? 54  PRO A CG   1 
ATOM   761  C CD   . PRO A 1 68  ? 23.11635  12.87591  23.30986 1.000 31.46140  ? 54  PRO A CD   1 
ATOM   762  H HA   . PRO A 1 68  ? 25.94626  11.53190  23.10995 1.000 39.10086  ? 54  PRO A HA   1 
ATOM   763  H HB2  . PRO A 1 68  ? 24.60253  10.67937  25.11862 1.000 41.92291  ? 54  PRO A HB2  1 
ATOM   764  H HB3  . PRO A 1 68  ? 25.14121  12.17396  25.08068 1.000 41.92291  ? 54  PRO A HB3  1 
ATOM   765  H HG2  . PRO A 1 68  ? 22.56003  11.27576  24.47647 1.000 37.96361  ? 54  PRO A HG2  1 
ATOM   766  H HG3  . PRO A 1 68  ? 22.95839  12.55232  25.33502 1.000 37.96361  ? 54  PRO A HG3  1 
ATOM   767  H HD2  . PRO A 1 68  ? 22.25779  12.78513  22.86768 1.000 37.80962  ? 54  PRO A HD2  1 
ATOM   768  H HD3  . PRO A 1 68  ? 23.28239  13.80729  23.52402 1.000 37.80962  ? 54  PRO A HD3  1 
ATOM   769  N N    . VAL A 1 69  ? 23.75204  9.68434   21.87115 1.000 40.08988  ? 55  VAL A N    1 
ATOM   770  C CA   . VAL A 1 69  ? 23.41689  8.34426   21.39389 1.000 31.32653  ? 55  VAL A CA   1 
ATOM   771  C C    . VAL A 1 69  ? 23.24435  8.40051   19.88198 1.000 35.85079  ? 55  VAL A C    1 
ATOM   772  O O    . VAL A 1 69  ? 22.96730  9.46779   19.31207 1.000 31.51267  ? 55  VAL A O    1 
ATOM   773  C CB   . VAL A 1 69  ? 22.13933  7.79970   22.07470 1.000 33.70894  ? 55  VAL A CB   1 
ATOM   774  C CG1  . VAL A 1 69  ? 22.28657  7.83993   23.58633 1.000 38.34515  ? 55  VAL A CG1  1 
ATOM   775  C CG2  . VAL A 1 69  ? 20.91727  8.58938   21.63417 1.000 34.65426  ? 55  VAL A CG2  1 
ATOM   776  H H    . VAL A 1 69  ? 23.24730  10.30156  21.54887 1.000 48.16380  ? 55  VAL A H    1 
ATOM   777  H HA   . VAL A 1 69  ? 24.14996  7.74153   21.59445 1.000 37.64778  ? 55  VAL A HA   1 
ATOM   778  H HB   . VAL A 1 69  ? 22.01148  6.87645   21.80609 1.000 40.50667  ? 55  VAL A HB   1 
ATOM   779  H HG11 . VAL A 1 69  ? 23.22420  7.94932   23.80950 1.000 46.07012  ? 55  VAL A HG11 1 
ATOM   780  H HG12 . VAL A 1 69  ? 21.77454  8.58695   23.93373 1.000 46.07012  ? 55  VAL A HG12 1 
ATOM   781  H HG13 . VAL A 1 69  ? 21.95281  7.00862   23.95838 1.000 46.07012  ? 55  VAL A HG13 1 
ATOM   782  H HG21 . VAL A 1 69  ? 20.17679  8.38107   22.22509 1.000 41.64106  ? 55  VAL A HG21 1 
ATOM   783  H HG22 . VAL A 1 69  ? 21.12027  9.53681   21.67957 1.000 41.64106  ? 55  VAL A HG22 1 
ATOM   784  H HG23 . VAL A 1 69  ? 20.69317  8.34239   20.72331 1.000 41.64106  ? 55  VAL A HG23 1 
ATOM   785  N N    . PRO A 1 70  ? 23.39536  7.26350   19.20022 1.000 34.36061  ? 56  PRO A N    1 
ATOM   786  C CA   . PRO A 1 70  ? 23.24637  7.26330   17.73944 1.000 26.25060  ? 56  PRO A CA   1 
ATOM   787  C C    . PRO A 1 70  ? 21.79693  7.44381   17.31776 1.000 30.97115  ? 56  PRO A C    1 
ATOM   788  O O    . PRO A 1 70  ? 20.87566  6.91443   17.94459 1.000 25.86079  ? 56  PRO A O    1 
ATOM   789  C CB   . PRO A 1 70  ? 23.77658  5.88389   17.32252 1.000 33.56664  ? 56  PRO A CB   1 
ATOM   790  C CG   . PRO A 1 70  ? 24.53111  5.36511   18.51358 1.000 37.32978  ? 56  PRO A CG   1 
ATOM   791  C CD   . PRO A 1 70  ? 23.83498  5.95080   19.70045 1.000 32.85446  ? 56  PRO A CD   1 
ATOM   792  H HA   . PRO A 1 70  ? 23.79076  7.96236   17.34464 1.000 31.55666  ? 56  PRO A HA   1 
ATOM   793  H HB2  . PRO A 1 70  ? 23.03386  5.29974   17.10335 1.000 40.33591  ? 56  PRO A HB2  1 
ATOM   794  H HB3  . PRO A 1 70  ? 24.36344  5.97630   16.55574 1.000 40.33591  ? 56  PRO A HB3  1 
ATOM   795  H HG2  . PRO A 1 70  ? 24.49239  4.39607   18.53265 1.000 44.85168  ? 56  PRO A HG2  1 
ATOM   796  H HG3  . PRO A 1 70  ? 25.45449  5.65951   18.47347 1.000 44.85168  ? 56  PRO A HG3  1 
ATOM   797  H HD2  . PRO A 1 70  ? 23.07601  5.40638   19.96213 1.000 39.48129  ? 56  PRO A HD2  1 
ATOM   798  H HD3  . PRO A 1 70  ? 24.44544  6.05004   20.44771 1.000 39.48129  ? 56  PRO A HD3  1 
ATOM   799  N N    . TRP A 1 71  ? 21.60645  8.18667   16.22929 1.000 25.29267  ? 57  TRP A N    1 
ATOM   800  C CA   . TRP A 1 71  ? 20.26409  8.40637   15.70073 1.000 24.46229  ? 57  TRP A CA   1 
ATOM   801  C C    . TRP A 1 71  ? 19.47528  7.12124   15.48199 1.000 23.34991  ? 57  TRP A C    1 
ATOM   802  O O    . TRP A 1 71  ? 18.28131  7.09987   15.82555 1.000 25.77094  ? 57  TRP A O    1 
ATOM   803  C CB   . TRP A 1 71  ? 20.34818  9.18984   14.38162 1.000 26.15425  ? 57  TRP A CB   1 
ATOM   804  C CG   . TRP A 1 71  ? 20.60992  10.65574  14.55306 1.000 26.01557  ? 57  TRP A CG   1 
ATOM   805  C CD1  . TRP A 1 71  ? 21.78692  11.30951  14.33881 1.000 24.62634  ? 57  TRP A CD1  1 
ATOM   806  C CD2  . TRP A 1 71  ? 19.66826  11.65117  14.97113 1.000 23.84674  ? 57  TRP A CD2  1 
ATOM   807  N NE1  . TRP A 1 71  ? 21.63737  12.65108  14.59744 1.000 23.73867  ? 57  TRP A NE1  1 
ATOM   808  C CE2  . TRP A 1 71  ? 20.34529  12.88598  14.98704 1.000 22.59448  ? 57  TRP A CE2  1 
ATOM   809  C CE3  . TRP A 1 71  ? 18.31861  11.61695  15.33363 1.000 26.03084  ? 57  TRP A CE3  1 
ATOM   810  C CZ2  . TRP A 1 71  ? 19.72003  14.07540  15.35318 1.000 25.44385  ? 57  TRP A CZ2  1 
ATOM   811  C CZ3  . TRP A 1 71  ? 17.69866  12.79860  15.69523 1.000 28.26565  ? 57  TRP A CZ3  1 
ATOM   812  C CH2  . TRP A 1 71  ? 18.39971  14.01173  15.70186 1.000 28.61181  ? 57  TRP A CH2  1 
ATOM   813  H H    . TRP A 1 71  ? 22.23231  8.57131   15.78212 1.000 30.40715  ? 57  TRP A H    1 
ATOM   814  H HA   . TRP A 1 71  ? 19.78588  8.94169   16.35314 1.000 29.41068  ? 57  TRP A HA   1 
ATOM   815  H HB2  . TRP A 1 71  ? 21.07033  8.82259   13.84821 1.000 31.44104  ? 57  TRP A HB2  1 
ATOM   816  H HB3  . TRP A 1 71  ? 19.50586  9.09469   13.91008 1.000 31.44104  ? 57  TRP A HB3  1 
ATOM   817  H HD1  . TRP A 1 71  ? 22.57657  10.90617  14.05831 1.000 29.60755  ? 57  TRP A HD1  1 
ATOM   818  H HE1  . TRP A 1 71  ? 22.25432  13.24598  14.52629 1.000 28.54235  ? 57  TRP A HE1  1 
ATOM   819  H HE3  . TRP A 1 71  ? 17.84715  10.81531  15.33160 1.000 31.29295  ? 57  TRP A HE3  1 
ATOM   820  H HZ2  . TRP A 1 71  ? 20.18294  14.88197  15.36021 1.000 30.58857  ? 57  TRP A HZ2  1 
ATOM   821  H HZ3  . TRP A 1 71  ? 16.80103  12.78808  15.93822 1.000 33.97473  ? 57  TRP A HZ3  1 
ATOM   822  H HH2  . TRP A 1 71  ? 17.95681  14.79125  15.94904 1.000 34.39011  ? 57  TRP A HH2  1 
ATOM   823  N N    . PRO A 1 72  ? 20.04225  6.04810   14.92118 1.000 22.87291  ? 58  PRO A N    1 
ATOM   824  C CA   . PRO A 1 72  ? 19.22685  4.84861   14.66187 1.000 23.75290  ? 58  PRO A CA   1 
ATOM   825  C C    . PRO A 1 72  ? 18.55756  4.28535   15.90175 1.000 26.76580  ? 58  PRO A C    1 
ATOM   826  O O    . PRO A 1 72  ? 17.51691  3.62419   15.78613 1.000 26.83187  ? 58  PRO A O    1 
ATOM   827  C CB   . PRO A 1 72  ? 20.24000  3.85726   14.07060 1.000 25.34858  ? 58  PRO A CB   1 
ATOM   828  C CG   . PRO A 1 72  ? 21.32607  4.70965   13.50822 1.000 27.45271  ? 58  PRO A CG   1 
ATOM   829  C CD   . PRO A 1 72  ? 21.41758  5.90285   14.41389 1.000 23.48534  ? 58  PRO A CD   1 
ATOM   830  H HA   . PRO A 1 72  ? 18.54863  5.05290   13.99916 1.000 28.55942  ? 58  PRO A HA   1 
ATOM   831  H HB2  . PRO A 1 72  ? 20.58038  3.27639   14.76891 1.000 30.47423  ? 58  PRO A HB2  1 
ATOM   832  H HB3  . PRO A 1 72  ? 19.81807  3.32838   13.37550 1.000 30.47423  ? 58  PRO A HB3  1 
ATOM   833  H HG2  . PRO A 1 72  ? 22.16108  4.21605   13.50425 1.000 32.99919  ? 58  PRO A HG2  1 
ATOM   834  H HG3  . PRO A 1 72  ? 21.09615  4.97993   12.60546 1.000 32.99919  ? 58  PRO A HG3  1 
ATOM   835  H HD2  . PRO A 1 72  ? 22.03823  5.73787   15.14086 1.000 28.23835  ? 58  PRO A HD2  1 
ATOM   836  H HD3  . PRO A 1 72  ? 21.68836  6.69202   13.91914 1.000 28.23835  ? 58  PRO A HD3  1 
ATOM   837  N N    . THR A 1 73  ? 19.12619  4.52181   17.08695 1.000 27.13664  ? 59  THR A N    1 
ATOM   838  C CA   . THR A 1 73  ? 18.53719  4.00851   18.31782 1.000 25.37928  ? 59  THR A CA   1 
ATOM   839  C C    . THR A 1 73  ? 17.29809  4.78905   18.73661 1.000 28.66732  ? 59  THR A C    1 
ATOM   840  O O    . THR A 1 73  ? 16.50411  4.28244   19.53612 1.000 30.14435  ? 59  THR A O    1 
ATOM   841  C CB   . THR A 1 73  ? 19.56616  4.04190   19.45031 1.000 26.47961  ? 59  THR A CB   1 
ATOM   842  O OG1  . THR A 1 73  ? 19.84485  5.40082   19.81173 1.000 25.66618  ? 59  THR A OG1  1 
ATOM   843  C CG2  . THR A 1 73  ? 20.85652  3.36337   19.02137 1.000 29.33405  ? 59  THR A CG2  1 
ATOM   844  H H    . THR A 1 73  ? 19.84862  4.97408   17.20163 1.000 32.61991  ? 59  THR A H    1 
ATOM   845  H HA   . THR A 1 73  ? 18.27818  3.08541   18.17049 1.000 30.51107  ? 59  THR A HA   1 
ATOM   846  H HB   . THR A 1 73  ? 19.21133  3.56908   20.21936 1.000 31.83147  ? 59  THR A HB   1 
ATOM   847  H HG1  . THR A 1 73  ? 20.53576  5.43546   20.28821 1.000 30.85536  ? 59  THR A HG1  1 
ATOM   848  H HG21 . THR A 1 73  ? 21.36371  3.09128   19.80216 1.000 35.25680  ? 59  THR A HG21 1 
ATOM   849  H HG22 . THR A 1 73  ? 20.65705  2.57909   18.48656 1.000 35.25680  ? 59  THR A HG22 1 
ATOM   850  H HG23 . THR A 1 73  ? 21.39390  3.97534   18.49448 1.000 35.25680  ? 59  THR A HG23 1 
ATOM   851  N N    . LEU A 1 74  ? 17.11993  6.00533   18.22412 1.000 27.10485  ? 60  LEU A N    1 
ATOM   852  C CA   . LEU A 1 74  ? 15.95666  6.82669   18.52606 1.000 25.05633  ? 60  LEU A CA   1 
ATOM   853  C C    . LEU A 1 74  ? 14.87036  6.73296   17.46176 1.000 26.55172  ? 60  LEU A C    1 
ATOM   854  O O    . LEU A 1 74  ? 13.80824  7.34182   17.62651 1.000 25.16758  ? 60  LEU A O    1 
ATOM   855  C CB   . LEU A 1 74  ? 16.37781  8.29120   18.68747 1.000 25.05813  ? 60  LEU A CB   1 
ATOM   856  C CG   . LEU A 1 74  ? 17.50229  8.58047   19.68286 1.000 24.27436  ? 60  LEU A CG   1 
ATOM   857  C CD1  . LEU A 1 74  ? 17.89489  10.04797  19.62966 1.000 30.15484  ? 60  LEU A CD1  1 
ATOM   858  C CD2  . LEU A 1 74  ? 17.08694  8.18830   21.08339 1.000 26.47098  ? 60  LEU A CD2  1 
ATOM   859  H H    . LEU A 1 74  ? 17.67434  6.38313   17.68608 1.000 32.58176  ? 60  LEU A H    1 
ATOM   860  H HA   . LEU A 1 74  ? 15.57824  6.52414   19.36639 1.000 30.12354  ? 60  LEU A HA   1 
ATOM   861  H HB2  . LEU A 1 74  ? 16.67483  8.61411   17.82236 1.000 30.12569  ? 60  LEU A HB2  1 
ATOM   862  H HB3  . LEU A 1 74  ? 15.60254  8.79475   18.98122 1.000 30.12569  ? 60  LEU A HB3  1 
ATOM   863  H HG   . LEU A 1 74  ? 18.28014  8.05263   19.44363 1.000 29.18517  ? 60  LEU A HG   1 
ATOM   864  H HD11 . LEU A 1 74  ? 17.18259  10.57972  20.01795 1.000 36.24175  ? 60  LEU A HD11 1 
ATOM   865  H HD12 . LEU A 1 74  ? 18.71415  10.17416  20.13343 1.000 36.24175  ? 60  LEU A HD12 1 
ATOM   866  H HD13 . LEU A 1 74  ? 18.03263  10.30468  18.70444 1.000 36.24175  ? 60  LEU A HD13 1 
ATOM   867  H HD21 . LEU A 1 74  ? 17.12678  7.22264   21.16586 1.000 31.82112  ? 60  LEU A HD21 1 
ATOM   868  H HD22 . LEU A 1 74  ? 17.69278  8.59987   21.71936 1.000 31.82112  ? 60  LEU A HD22 1 
ATOM   869  H HD23 . LEU A 1 74  ? 16.18110  8.49675   21.24218 1.000 31.82112  ? 60  LEU A HD23 1 
ATOM   870  N N    . VAL A 1 75  ? 15.10590  5.98418   16.38214 1.000 24.85143  ? 61  VAL A N    1 
ATOM   871  C CA   . VAL A 1 75  ? 14.16591  5.96491   15.26249 1.000 23.58553  ? 61  VAL A CA   1 
ATOM   872  C C    . VAL A 1 75  ? 12.78891  5.50153   15.72357 1.000 23.10351  ? 61  VAL A C    1 
ATOM   873  O O    . VAL A 1 75  ? 11.77403  6.16030   15.46502 1.000 22.98780  ? 61  VAL A O    1 
ATOM   874  C CB   . VAL A 1 75  ? 14.71087  5.07806   14.12785 1.000 21.14068  ? 61  VAL A CB   1 
ATOM   875  C CG1  . VAL A 1 75  ? 13.59659  4.67780   13.16908 1.000 26.44229  ? 61  VAL A CG1  1 
ATOM   876  C CG2  . VAL A 1 75  ? 15.81967  5.80362   13.38586 1.000 20.39776  ? 61  VAL A CG2  1 
ATOM   877  H H    . VAL A 1 75  ? 15.79642  5.48299   16.27447 1.000 29.87766  ? 61  VAL A H    1 
ATOM   878  H HA   . VAL A 1 75  ? 14.07243  6.86901   14.92372 1.000 28.35857  ? 61  VAL A HA   1 
ATOM   879  H HB   . VAL A 1 75  ? 15.07631  4.26580   14.51202 1.000 25.42476  ? 61  VAL A HB   1 
ATOM   880  H HG11 . VAL A 1 75  ? 13.99073  4.36466   12.33993 1.000 31.78669  ? 61  VAL A HG11 1 
ATOM   881  H HG12 . VAL A 1 75  ? 13.07105  3.96992   13.57358 1.000 31.78669  ? 61  VAL A HG12 1 
ATOM   882  H HG13 . VAL A 1 75  ? 13.03507  5.44991   12.99753 1.000 31.78669  ? 61  VAL A HG13 1 
ATOM   883  H HG21 . VAL A 1 75  ? 16.50383  6.06817   14.02056 1.000 24.53325  ? 61  VAL A HG21 1 
ATOM   884  H HG22 . VAL A 1 75  ? 15.44891  6.58844   12.95287 1.000 24.53325  ? 61  VAL A HG22 1 
ATOM   885  H HG23 . VAL A 1 75  ? 16.19799  5.20686   12.72129 1.000 24.53325  ? 61  VAL A HG23 1 
ATOM   886  N N    . THR A 1 76  ? 12.73089  4.35763   16.41039 1.000 23.16547  ? 62  THR A N    1 
ATOM   887  C CA   . THR A 1 76  ? 11.43969  3.81818   16.82362 1.000 24.67536  ? 62  THR A CA   1 
ATOM   888  C C    . THR A 1 76  ? 10.74787  4.72608   17.83149 1.000 24.95212  ? 62  THR A C    1 
ATOM   889  O O    . THR A 1 76  ? 9.51469   4.79890   17.85457 1.000 25.88245  ? 62  THR A O    1 
ATOM   890  C CB   . THR A 1 76  ? 11.61252  2.41712   17.41083 1.000 25.07684  ? 62  THR A CB   1 
ATOM   891  O OG1  . THR A 1 76  ? 12.45401  2.47583   18.57102 1.000 26.96795  ? 62  THR A OG1  1 
ATOM   892  C CG2  . THR A 1 76  ? 12.22799  1.47814   16.37829 1.000 28.09678  ? 62  THR A CG2  1 
ATOM   893  H H    . THR A 1 76  ? 13.41108  3.88597   16.64380 1.000 27.85450  ? 62  THR A H    1 
ATOM   894  H HA   . THR A 1 76  ? 10.87187  3.74672   16.04044 1.000 29.66637  ? 62  THR A HA   1 
ATOM   895  H HB   . THR A 1 76  ? 10.74556  2.06432   17.66543 1.000 30.14815  ? 62  THR A HB   1 
ATOM   896  H HG1  . THR A 1 76  ? 12.03204  2.20727   19.24587 1.000 32.41748  ? 62  THR A HG1  1 
ATOM   897  H HG21 . THR A 1 76  ? 12.16803  0.56051   16.68693 1.000 33.77208  ? 62  THR A HG21 1 
ATOM   898  H HG22 . THR A 1 76  ? 11.75629  1.55792   15.53447 1.000 33.77208  ? 62  THR A HG22 1 
ATOM   899  H HG23 . THR A 1 76  ? 13.16127  1.70331   16.23973 1.000 33.77208  ? 62  THR A HG23 1 
ATOM   900  N N    . THR A 1 77  ? 11.51444  5.42403   18.66747 1.000 25.76627  ? 63  THR A N    1 
ATOM   901  C CA   . THR A 1 77  ? 10.90087  6.32247   19.63801 1.000 26.92276  ? 63  THR A CA   1 
ATOM   902  C C    . THR A 1 77  ? 10.33930  7.56338   18.95424 1.000 24.07274  ? 63  THR A C    1 
ATOM   903  O O    . THR A 1 77  ? 9.21232   7.98325   19.24299 1.000 24.82088  ? 63  THR A O    1 
ATOM   904  C CB   . THR A 1 77  ? 11.92306  6.70190   20.70843 1.000 28.33852  ? 63  THR A CB   1 
ATOM   905  O OG1  . THR A 1 77  ? 12.32668  5.52483   21.42308 1.000 28.63087  ? 63  THR A OG1  1 
ATOM   906  C CG2  . THR A 1 77  ? 11.33545  7.70915   21.68278 1.000 27.14388  ? 63  THR A CG2  1 
ATOM   907  H H    . THR A 1 77  ? 12.37362  5.39566   18.69222 1.000 30.97546  ? 63  THR A H    1 
ATOM   908  H HA   . THR A 1 77  ? 10.16547  5.86715   20.07707 1.000 32.36325  ? 63  THR A HA   1 
ATOM   909  H HB   . THR A 1 77  ? 12.69681  7.10699   20.28639 1.000 34.06217  ? 63  THR A HB   1 
ATOM   910  H HG1  . THR A 1 77  ? 11.67593  5.21212   21.85243 1.000 34.41299  ? 63  THR A HG1  1 
ATOM   911  H HG21 . THR A 1 77  ? 10.43006  7.45324   21.91872 1.000 32.62860  ? 63  THR A HG21 1 
ATOM   912  H HG22 . THR A 1 77  ? 11.87326  7.74322   22.48931 1.000 32.62860  ? 63  THR A HG22 1 
ATOM   913  H HG23 . THR A 1 77  ? 11.31818  8.59070   21.27846 1.000 32.62860  ? 63  THR A HG23 1 
ATOM   914  N N    . LEU A 1 78  ? 11.09964  8.14992   18.03629 1.000 23.52586  ? 64  LEU A N    1 
ATOM   915  C CA   . LEU A 1 78  ? 10.66470  9.34005   17.31623 1.000 29.27756  ? 64  LEU A CA   1 
ATOM   916  C C    . LEU A 1 78  ? 9.58345   9.01095   16.29238 1.000 27.43896  ? 64  LEU A C    1 
ATOM   917  O O    . LEU A 1 78  ? 8.67828   9.80905   16.05262 1.000 28.89130  ? 64  LEU A O    1 
ATOM   918  C CB   . LEU A 1 78  ? 11.85644  9.99603   16.62108 1.000 23.48950  ? 64  LEU A CB   1 
ATOM   919  C CG   . LEU A 1 78  ? 12.91560  10.58082  17.55361 1.000 21.60580  ? 64  LEU A CG   1 
ATOM   920  C CD1  . LEU A 1 78  ? 14.24024  10.74264  16.82386 1.000 24.61447  ? 64  LEU A CD1  1 
ATOM   921  C CD2  . LEU A 1 78  ? 12.44800  11.91137  18.11487 1.000 23.40771  ? 64  LEU A CD2  1 
ATOM   922  H H    . LEU A 1 78  ? 11.88198  7.87411   17.80943 1.000 28.28697  ? 64  LEU A H    1 
ATOM   923  H HA   . LEU A 1 78  ? 10.28817  9.97050   17.94999 1.000 35.18901  ? 64  LEU A HA   1 
ATOM   924  H HB2  . LEU A 1 78  ? 12.29275  9.32860   16.06875 1.000 28.24334  ? 64  LEU A HB2  1 
ATOM   925  H HB3  . LEU A 1 78  ? 11.52572  10.72039  16.06715 1.000 28.24334  ? 64  LEU A HB3  1 
ATOM   926  H HG   . LEU A 1 78  ? 13.05608  9.97205   18.29560 1.000 25.98290  ? 64  LEU A HG   1 
ATOM   927  H HD11 . LEU A 1 78  ? 14.53243  9.87490   16.50361 1.000 29.59331  ? 64  LEU A HD11 1 
ATOM   928  H HD12 . LEU A 1 78  ? 14.11663  11.34704  16.07531 1.000 29.59331  ? 64  LEU A HD12 1 
ATOM   929  H HD13 . LEU A 1 78  ? 14.89675  11.10678  17.43810 1.000 29.59331  ? 64  LEU A HD13 1 
ATOM   930  H HD21 . LEU A 1 78  ? 13.18924  12.33980  18.57085 1.000 28.14519  ? 64  LEU A HD21 1 
ATOM   931  H HD22 . LEU A 1 78  ? 12.14040  12.47140  17.38504 1.000 28.14519  ? 64  LEU A HD22 1 
ATOM   932  H HD23 . LEU A 1 78  ? 11.72250  11.75338  18.73904 1.000 28.14519  ? 64  LEU A HD23 1 
HETATM 933  C CD2  . SWG A 1 79  ? 9.82053   0.66386   13.73985 1.000 30.45716  ? 65  SWG A CD2  1 
HETATM 934  C CE3  . SWG A 1 79  ? 9.39805   -0.54957  14.30496 1.000 28.38388  ? 65  SWG A CE3  1 
HETATM 935  C CZ3  . SWG A 1 79  ? 9.99693   -1.73741  13.92871 1.000 35.27024  ? 65  SWG A CZ3  1 
HETATM 936  C CH2  . SWG A 1 79  ? 11.00276  -1.70092  12.99479 1.000 28.16452  ? 65  SWG A CH2  1 
HETATM 937  C CZ2  . SWG A 1 79  ? 11.46053  -0.51529  12.40051 1.000 34.22810  ? 65  SWG A CZ2  1 
HETATM 938  C CE2  . SWG A 1 79  ? 10.84414  0.66225   12.79933 1.000 29.10571  ? 65  SWG A CE2  1 
HETATM 939  N NE1  . SWG A 1 79  ? 11.09593  1.97009   12.37384 1.000 29.90809  ? 65  SWG A NE1  1 
HETATM 940  C CD1  . SWG A 1 79  ? 10.21827  2.77937   13.06295 1.000 28.47601  ? 65  SWG A CD1  1 
HETATM 941  C CG   . SWG A 1 79  ? 9.41558   2.06757   13.90818 1.000 29.22941  ? 65  SWG A CG   1 
HETATM 942  C CB2  . SWG A 1 79  ? 8.33734   2.54334   14.83012 1.000 28.49696  ? 65  SWG A CB2  1 
HETATM 943  C CA2  . SWG A 1 79  ? 8.12004   3.87664   15.09313 1.000 26.67051  ? 65  SWG A CA2  1 
HETATM 944  N N2   . SWG A 1 79  ? 8.67579   4.95438   14.43942 1.000 27.65987  ? 65  SWG A N2   1 
HETATM 945  C C2   . SWG A 1 79  ? 7.25098   4.42250   16.12510 1.000 27.71622  ? 65  SWG A C2   1 
HETATM 946  O O2   . SWG A 1 79  ? 6.54296   3.84549   16.96441 1.000 30.21239  ? 65  SWG A O2   1 
HETATM 947  N N3   . SWG A 1 79  ? 7.35414   5.76180   16.01498 1.000 26.23575  ? 65  SWG A N3   1 
HETATM 948  C CA3  . SWG A 1 79  ? 6.65233   6.67846   16.85064 1.000 23.31912  ? 65  SWG A CA3  1 
HETATM 949  C C3   . SWG A 1 79  ? 5.23241   7.03855   16.67732 1.000 27.70006  ? 65  SWG A C3   1 
HETATM 950  O O3   . SWG A 1 79  ? 4.62450   7.61262   17.59560 1.000 26.27648  ? 65  SWG A O3   1 
HETATM 951  C C1   . SWG A 1 79  ? 8.19098   6.07600   15.02537 1.000 29.29327  ? 65  SWG A C1   1 
HETATM 952  C CA1  . SWG A 1 79  ? 8.57842   7.46145   14.57352 1.000 27.51581  ? 65  SWG A CA1  1 
HETATM 953  N N1   . SWG A 1 79  ? 9.67480   7.83671   15.48235 1.000 29.97506  ? 65  SWG A N1   1 
HETATM 954  C CB1  . SWG A 1 79  ? 9.17619   7.56021   13.16042 1.000 26.52214  ? 65  SWG A CB1  1 
HETATM 955  O OG1  . SWG A 1 79  ? 8.14401   7.14526   12.25748 1.000 26.37053  ? 65  SWG A OG1  1 
ATOM   956  N N    . VAL A 1 80  ? 4.94657   7.13550   15.28029 1.000 26.30760  ? 66  VAL A N    1 
ATOM   957  C CA   . VAL A 1 80  ? 3.63881   7.57474   14.80918 1.000 32.13547  ? 66  VAL A CA   1 
ATOM   958  C C    . VAL A 1 80  ? 3.00720   6.47148   13.96063 1.000 31.28847  ? 66  VAL A C    1 
ATOM   959  O O    . VAL A 1 80  ? 2.79292   6.63310   12.75907 1.000 26.62035  ? 66  VAL A O    1 
ATOM   960  C CB   . VAL A 1 80  ? 3.75023   8.89462   14.02724 1.000 28.91676  ? 66  VAL A CB   1 
ATOM   961  C CG1  . VAL A 1 80  ? 4.07009   10.04935  14.97830 1.000 27.42684  ? 66  VAL A CG1  1 
ATOM   962  C CG2  . VAL A 1 80  ? 4.81230   8.78449   12.94490 1.000 28.40283  ? 66  VAL A CG2  1 
ATOM   963  H HA   . VAL A 1 80  ? 3.05771   7.74212   15.56760 1.000 38.61851  ? 66  VAL A HA   1 
ATOM   964  H HB   . VAL A 1 80  ? 2.90029   9.07949   13.59790 1.000 34.75605  ? 66  VAL A HB   1 
ATOM   965  H HG11 . VAL A 1 80  ? 4.14803   10.86879  14.46513 1.000 32.96815  ? 66  VAL A HG11 1 
ATOM   966  H HG12 . VAL A 1 80  ? 3.35351   10.13208  15.62681 1.000 32.96815  ? 66  VAL A HG12 1 
ATOM   967  H HG13 . VAL A 1 80  ? 4.90681   9.86231   15.43196 1.000 32.96815  ? 66  VAL A HG13 1 
ATOM   968  H HG21 . VAL A 1 80  ? 4.85531   7.86567   12.63698 1.000 34.13934  ? 66  VAL A HG21 1 
ATOM   969  H HG22 . VAL A 1 80  ? 4.57455   9.36935   12.20848 1.000 34.13934  ? 66  VAL A HG22 1 
ATOM   970  H HG23 . VAL A 1 80  ? 5.66885   9.04983   13.31480 1.000 34.13934  ? 66  VAL A HG23 1 
ATOM   971  N N    . GLN A 1 81  ? 2.70960   5.34144   14.60348 1.000 33.00423  ? 67  GLN A N    1 
ATOM   972  C CA   . GLN A 1 81  ? 2.16100   4.18969   13.89820 1.000 28.67844  ? 67  GLN A CA   1 
ATOM   973  C C    . GLN A 1 81  ? 0.72861   4.40892   13.43206 1.000 30.20073  ? 67  GLN A C    1 
ATOM   974  O O    . GLN A 1 81  ? 0.19161   3.55570   12.71691 1.000 26.53634  ? 67  GLN A O    1 
ATOM   975  C CB   . GLN A 1 81  ? 2.24930   2.95699   14.79688 1.000 27.80606  ? 67  GLN A CB   1 
ATOM   976  C CG   . GLN A 1 81  ? 3.68386   2.50361   15.04072 1.000 24.09300  ? 67  GLN A CG   1 
ATOM   977  C CD   . GLN A 1 81  ? 3.81190   1.56395   16.21705 1.000 31.10894  ? 67  GLN A CD   1 
ATOM   978  O OE1  . GLN A 1 81  ? 3.04774   1.64601   17.17836 1.000 32.16103  ? 67  GLN A OE1  1 
ATOM   979  N NE2  . GLN A 1 81  ? 4.78492   0.66392   16.15026 1.000 32.49766  ? 67  GLN A NE2  1 
ATOM   980  H H    . GLN A 1 81  ? 2.81694   5.21871   15.44788 1.000 39.66102  ? 67  GLN A H    1 
ATOM   981  H HA   . GLN A 1 81  ? 2.69213   4.01798   13.10491 1.000 34.47007  ? 67  GLN A HA   1 
ATOM   982  H HB2  . GLN A 1 81  ? 1.84999   3.16410   15.65628 1.000 33.42322  ? 67  GLN A HB2  1 
ATOM   983  H HB3  . GLN A 1 81  ? 1.77086   2.22540   14.37644 1.000 33.42322  ? 67  GLN A HB3  1 
ATOM   984  H HG2  . GLN A 1 81  ? 4.00702   2.04113   14.25169 1.000 28.76173  ? 67  GLN A HG2  1 
ATOM   985  H HG3  . GLN A 1 81  ? 4.23491   3.28194   15.21805 1.000 28.76173  ? 67  GLN A HG3  1 
ATOM   986  H HE21 . GLN A 1 81  ? 5.30082   0.63864   15.46265 1.000 39.05313  ? 67  GLN A HE21 1 
ATOM   987  H HE22 . GLN A 1 81  ? 4.89954   0.10596   16.79458 1.000 39.05313  ? 67  GLN A HE22 1 
ATOM   988  N N    . CYS A 1 82  ? 0.10330   5.52672   13.80443 1.000 29.75755  ? 68  CYS A N    1 
ATOM   989  C CA   . CYS A 1 82  ? -1.19262  5.87780   13.23958 1.000 31.34441  ? 68  CYS A CA   1 
ATOM   990  C C    . CYS A 1 82  ? -1.12300  6.14781   11.74127 1.000 26.89127  ? 68  CYS A C    1 
ATOM   991  O O    . CYS A 1 82  ? -2.17450  6.25987   11.10111 1.000 24.49539  ? 68  CYS A O    1 
ATOM   992  C CB   . CYS A 1 82  ? -1.75431  7.10169   13.96208 1.000 26.81855  ? 68  CYS A CB   1 
ATOM   993  S SG   . CYS A 1 82  ? -0.58508  8.47065   14.07719 1.000 31.53179  ? 68  CYS A SG   1 
ATOM   994  H H    . CYS A 1 82  ? 0.40777   6.09137   14.37720 1.000 35.76501  ? 68  CYS A H    1 
ATOM   995  H HA   . CYS A 1 82  ? -1.80602  5.13923   13.37797 1.000 37.66923  ? 68  CYS A HA   1 
ATOM   996  H HB2  . CYS A 1 82  ? -2.53511  7.41754   13.48096 1.000 32.23820  ? 68  CYS A HB2  1 
ATOM   997  H HB3  . CYS A 1 82  ? -2.00172  6.84566   14.86438 1.000 32.23820  ? 68  CYS A HB3  1 
ATOM   998  H HG   . CYS A 1 82  ? -1.11050  9.38626   14.64781 1.000 37.89408  ? 68  CYS A HG   1 
ATOM   999  N N    . PHE A 1 83  ? 0.07589   6.25508   11.16892 1.000 26.75949  ? 69  PHE A N    1 
ATOM   1000 C CA   . PHE A 1 83  ? 0.24669   6.45982   9.73695  1.000 29.66281  ? 69  PHE A CA   1 
ATOM   1001 C C    . PHE A 1 83  ? 0.50602   5.16098   8.98553  1.000 27.73440  ? 69  PHE A C    1 
ATOM   1002 O O    . PHE A 1 83  ? 0.79874   5.19890   7.78763  1.000 25.36880  ? 69  PHE A O    1 
ATOM   1003 C CB   . PHE A 1 83  ? 1.38472   7.44857   9.47667  1.000 27.19656  ? 69  PHE A CB   1 
ATOM   1004 C CG   . PHE A 1 83  ? 1.03510   8.86492   9.81281  1.000 27.80993  ? 69  PHE A CG   1 
ATOM   1005 C CD1  . PHE A 1 83  ? 0.24917   9.61569   8.95482  1.000 26.37582  ? 69  PHE A CD1  1 
ATOM   1006 C CD2  . PHE A 1 83  ? 1.48194   9.44501   10.98801 1.000 30.53708  ? 69  PHE A CD2  1 
ATOM   1007 C CE1  . PHE A 1 83  ? -0.08202  10.91927  9.25889  1.000 30.72490  ? 69  PHE A CE1  1 
ATOM   1008 C CE2  . PHE A 1 83  ? 1.15421   10.75244  11.29908 1.000 33.28142  ? 69  PHE A CE2  1 
ATOM   1009 C CZ   . PHE A 1 83  ? 0.37047   11.49016  10.43292 1.000 33.93398  ? 69  PHE A CZ   1 
ATOM   1010 H H    . PHE A 1 83  ? 0.81835   6.21121   11.60070 1.000 32.16733  ? 69  PHE A H    1 
ATOM   1011 H HA   . PHE A 1 83  ? -0.57008  6.84689   9.38485  1.000 35.65132  ? 69  PHE A HA   1 
ATOM   1012 H HB2  . PHE A 1 83  ? 2.14904   7.19504   10.01745 1.000 32.69181  ? 69  PHE A HB2  1 
ATOM   1013 H HB3  . PHE A 1 83  ? 1.61846   7.41569   8.53582  1.000 32.69181  ? 69  PHE A HB3  1 
ATOM   1014 H HD1  . PHE A 1 83  ? -0.05909  9.23607   8.16377  1.000 31.70693  ? 69  PHE A HD1  1 
ATOM   1015 H HD2  . PHE A 1 83  ? 2.00787   8.95049   11.57431 1.000 36.70044  ? 69  PHE A HD2  1 
ATOM   1016 H HE1  . PHE A 1 83  ? -0.60960  11.41384  8.67413  1.000 36.92581  ? 69  PHE A HE1  1 
ATOM   1017 H HE2  . PHE A 1 83  ? 1.46087   11.13411  12.08977 1.000 39.99365  ? 69  PHE A HE2  1 
ATOM   1018 H HZ   . PHE A 1 83  ? 0.14794   12.36916  10.63966 1.000 40.77672  ? 69  PHE A HZ   1 
ATOM   1019 N N    . ALA A 1 84  ? 0.41019   4.01822   9.65715  1.000 26.48173  ? 70  ALA A N    1 
ATOM   1020 C CA   . ALA A 1 84  ? 0.52217   2.74109   8.96934  1.000 28.41046  ? 70  ALA A CA   1 
ATOM   1021 C C    . ALA A 1 84  ? -0.66174  2.54883   8.03241  1.000 25.66195  ? 70  ALA A C    1 
ATOM   1022 O O    . ALA A 1 84  ? -1.78970  2.93989   8.34304  1.000 25.99627  ? 70  ALA A O    1 
ATOM   1023 C CB   . ALA A 1 84  ? 0.58199   1.59451   9.97731  1.000 28.34555  ? 70  ALA A CB   1 
ATOM   1024 H H    . ALA A 1 84  ? 0.28137   3.95685   10.50523 1.000 31.83401  ? 70  ALA A H    1 
ATOM   1025 H HA   . ALA A 1 84  ? 1.33956   2.72342   8.44737  1.000 34.14850  ? 70  ALA A HA   1 
ATOM   1026 H HB1  . ALA A 1 84  ? -0.23622  1.58900   10.49827 1.000 34.07060  ? 70  ALA A HB1  1 
ATOM   1027 H HB2  . ALA A 1 84  ? 0.67421   0.75661   9.49739  1.000 34.07060  ? 70  ALA A HB2  1 
ATOM   1028 H HB3  . ALA A 1 84  ? 1.34508   1.72692   10.56132 1.000 34.07060  ? 70  ALA A HB3  1 
ATOM   1029 N N    . ARG A 1 85  ? -0.39968  1.94907   6.87492  1.000 26.90855  ? 71  ARG A N    1 
ATOM   1030 C CA   . ARG A 1 85  ? -1.45973  1.61843   5.92959  1.000 25.28504  ? 71  ARG A CA   1 
ATOM   1031 C C    . ARG A 1 85  ? -2.05394  0.27458   6.32816  1.000 23.30848  ? 71  ARG A C    1 
ATOM   1032 O O    . ARG A 1 85  ? -1.39284  -0.76455  6.21704  1.000 24.74876  ? 71  ARG A O    1 
ATOM   1033 C CB   . ARG A 1 85  ? -0.92720  1.57808   4.49999  1.000 28.10374  ? 71  ARG A CB   1 
ATOM   1034 C CG   . ARG A 1 85  ? -1.99622  1.25402   3.45368  1.000 29.23595  ? 71  ARG A CG   1 
ATOM   1035 C CD   . ARG A 1 85  ? -1.49009  0.26857   2.41269  1.000 34.74977  ? 71  ARG A CD   1 
ATOM   1036 N NE   . ARG A 1 85  ? -2.58101  -0.39179  1.70387  1.000 32.05746  ? 71  ARG A NE   1 
ATOM   1037 C CZ   . ARG A 1 85  ? -2.43691  -1.47931  0.95918  1.000 28.36909  ? 71  ARG A CZ   1 
ATOM   1038 N NH1  . ARG A 1 85  ? -1.25903  -2.06330  0.80973  1.000 29.80795  ? 71  ARG A NH1  1 
ATOM   1039 N NH2  . ARG A 1 85  ? -3.50192  -1.99734  0.35384  1.000 35.30698  ? 71  ARG A NH2  1 
ATOM   1040 H H    . ARG A 1 85  ? 0.38766   1.72258   6.61338  1.000 32.34620  ? 71  ARG A H    1 
ATOM   1041 H HA   . ARG A 1 85  ? -2.14993  2.29882   5.96956  1.000 30.39798  ? 71  ARG A HA   1 
ATOM   1042 H HB2  . ARG A 1 85  ? -0.55270  2.44591   4.28201  1.000 33.78043  ? 71  ARG A HB2  1 
ATOM   1043 H HB3  . ARG A 1 85  ? -0.23979  0.89614   4.44231  1.000 33.78043  ? 71  ARG A HB3  1 
ATOM   1044 H HG2  . ARG A 1 85  ? -2.76605  0.86116   3.89406  1.000 35.13909  ? 71  ARG A HG2  1 
ATOM   1045 H HG3  . ARG A 1 85  ? -2.25540  2.07010   2.99789  1.000 35.13909  ? 71  ARG A HG3  1 
ATOM   1046 H HD2  . ARG A 1 85  ? -0.94963  0.74261   1.76147  1.000 41.75566  ? 71  ARG A HD2  1 
ATOM   1047 H HD3  . ARG A 1 85  ? -0.95821  -0.41351  2.85174  1.000 41.75566  ? 71  ARG A HD3  1 
ATOM   1048 H HE   . ARG A 1 85  ? -3.36868  -0.05370  1.77360  1.000 38.52490  ? 71  ARG A HE   1 
ATOM   1049 H HH11 . ARG A 1 85  ? -1.18729  -2.76811  0.32219  1.000 35.82548  ? 71  ARG A HH11 1 
ATOM   1050 H HH12 . ARG A 1 85  ? -0.56520  -1.73807  1.20015  1.000 35.82548  ? 71  ARG A HH12 1 
ATOM   1051 H HH21 . ARG A 1 85  ? -3.42003  -2.70251  -0.13158 1.000 42.42432  ? 71  ARG A HH21 1 
ATOM   1052 H HH22 . ARG A 1 85  ? -4.27244  -1.62713  0.44785  1.000 42.42432  ? 71  ARG A HH22 1 
ATOM   1053 N N    . TYR A 1 86  ? -3.29314  0.29743   6.81536  1.000 23.27596  ? 72  TYR A N    1 
ATOM   1054 C CA   . TYR A 1 86  ? -4.05182  -0.92563  7.03946  1.000 24.72199  ? 72  TYR A CA   1 
ATOM   1055 C C    . TYR A 1 86  ? -4.88123  -1.23005  5.80067  1.000 27.64747  ? 72  TYR A C    1 
ATOM   1056 O O    . TYR A 1 86  ? -5.77969  -0.44262  5.46530  1.000 30.77679  ? 72  TYR A O    1 
ATOM   1057 C CB   . TYR A 1 86  ? -4.95965  -0.78451  8.25038  1.000 26.04296  ? 72  TYR A CB   1 
ATOM   1058 C CG   . TYR A 1 86  ? -4.26758  -1.03285  9.57296  1.000 25.57715  ? 72  TYR A CG   1 
ATOM   1059 C CD1  . TYR A 1 86  ? -3.34868  -0.12456  10.07558 1.000 24.74674  ? 72  TYR A CD1  1 
ATOM   1060 C CD2  . TYR A 1 86  ? -4.53632  -2.17456  10.32107 1.000 27.73765  ? 72  TYR A CD2  1 
ATOM   1061 C CE1  . TYR A 1 86  ? -2.71185  -0.34264  11.27801 1.000 25.70602  ? 72  TYR A CE1  1 
ATOM   1062 C CE2  . TYR A 1 86  ? -3.90180  -2.40123  11.53055 1.000 25.59779  ? 72  TYR A CE2  1 
ATOM   1063 C CZ   . TYR A 1 86  ? -2.99115  -1.47887  12.00264 1.000 27.73126  ? 72  TYR A CZ   1 
ATOM   1064 O OH   . TYR A 1 86  ? -2.35189  -1.68667  13.20210 1.000 27.63953  ? 72  TYR A OH   1 
ATOM   1065 H H    . TYR A 1 86  ? -3.71790  1.01524   7.02492  1.000 27.98709  ? 72  TYR A H    1 
ATOM   1066 H HA   . TYR A 1 86  ? -3.43562  -1.65878  7.19340  1.000 29.72232  ? 72  TYR A HA   1 
ATOM   1067 H HB2  . TYR A 1 86  ? -5.31515  0.11782   8.26862  1.000 31.30749  ? 72  TYR A HB2  1 
ATOM   1068 H HB3  . TYR A 1 86  ? -5.68396  -1.42492  8.17192  1.000 31.30749  ? 72  TYR A HB3  1 
ATOM   1069 H HD1  . TYR A 1 86  ? -3.15839  0.64669   9.59199  1.000 29.75203  ? 72  TYR A HD1  1 
ATOM   1070 H HD2  . TYR A 1 86  ? -5.15188  -2.79528  10.00376 1.000 33.34111  ? 72  TYR A HD2  1 
ATOM   1071 H HE1  . TYR A 1 86  ? -2.09562  0.27569   11.59866 1.000 30.90316  ? 72  TYR A HE1  1 
ATOM   1072 H HE2  . TYR A 1 86  ? -4.08804  -3.16924  12.02083 1.000 30.77328  ? 72  TYR A HE2  1 
ATOM   1073 H HH   . TYR A 1 86  ? -2.83753  -2.14618  13.71065 1.000 33.22338  ? 72  TYR A HH   1 
ATOM   1074 N N    . PRO A 1 87  ? -4.62426  -2.33353  5.08678  1.000 26.58182  ? 73  PRO A N    1 
ATOM   1075 C CA   . PRO A 1 87  ? -5.47583  -2.67424  3.93882  1.000 26.43517  ? 73  PRO A CA   1 
ATOM   1076 C C    . PRO A 1 87  ? -6.95096  -2.70289  4.30489  1.000 32.09304  ? 73  PRO A C    1 
ATOM   1077 O O    . PRO A 1 87  ? -7.30357  -2.79645  5.48551  1.000 30.40704  ? 73  PRO A O    1 
ATOM   1078 C CB   . PRO A 1 87  ? -4.96586  -4.05957  3.52342  1.000 31.44875  ? 73  PRO A CB   1 
ATOM   1079 C CG   . PRO A 1 87  ? -3.54468  -4.07802  3.96663  1.000 26.32093  ? 73  PRO A CG   1 
ATOM   1080 C CD   . PRO A 1 87  ? -3.50263  -3.27902  5.23923  1.000 27.57372  ? 73  PRO A CD   1 
ATOM   1081 H HA   . PRO A 1 87  ? -5.33591  -2.04974  3.20990  1.000 31.77814  ? 73  PRO A HA   1 
ATOM   1082 H HB2  . PRO A 1 87  ? -5.47995  -4.75084  3.96925  1.000 37.79444  ? 73  PRO A HB2  1 
ATOM   1083 H HB3  . PRO A 1 87  ? -5.03331  -4.16429  2.56146  1.000 37.79444  ? 73  PRO A HB3  1 
ATOM   1084 H HG2  . PRO A 1 87  ? -3.26310  -4.99256  4.12545  1.000 31.64105  ? 73  PRO A HG2  1 
ATOM   1085 H HG3  . PRO A 1 87  ? -2.98447  -3.67169  3.28695  1.000 31.64105  ? 73  PRO A HG3  1 
ATOM   1086 H HD2  . PRO A 1 87  ? -3.63688  -3.85175  6.01050  1.000 33.14441  ? 73  PRO A HD2  1 
ATOM   1087 H HD3  . PRO A 1 87  ? -2.66048  -2.80465  5.32083  1.000 33.14441  ? 73  PRO A HD3  1 
ATOM   1088 N N    . ASP A 1 88  ? -7.81893  -2.61764  3.29281  1.000 36.14754  ? 74  ASP A N    1 
ATOM   1089 C CA   . ASP A 1 88  ? -9.25666  -2.56807  3.54188  1.000 36.69126  ? 74  ASP A CA   1 
ATOM   1090 C C    . ASP A 1 88  ? -9.71544  -3.71176  4.44039  1.000 37.48018  ? 74  ASP A C    1 
ATOM   1091 O O    . ASP A 1 88  ? -10.54733 -3.51332  5.33292  1.000 37.17268  ? 74  ASP A O    1 
ATOM   1092 C CB   . ASP A 1 88  ? -10.01874 -2.60367  2.21497  1.000 33.64411  ? 74  ASP A CB   1 
ATOM   1093 C CG   . ASP A 1 88  ? -9.95803  -1.28374  1.46305  1.000 40.44496  ? 74  ASP A CG   1 
ATOM   1094 O OD1  . ASP A 1 88  ? -9.54660  -0.26426  2.05714  1.000 37.48826  ? 74  ASP A OD1  1 
ATOM   1095 O OD2  . ASP A 1 88  ? -10.32586 -1.26904  0.26985  1.000 47.14696  ? 74  ASP A OD2  1 
ATOM   1096 H H    . ASP A 1 88  ? -7.60145  -2.58735  2.46132  1.000 43.43299  ? 74  ASP A H    1 
ATOM   1097 H HA   . ASP A 1 88  ? -9.46036  -1.73354  3.99240  1.000 44.08545  ? 74  ASP A HA   1 
ATOM   1098 H HB2  . ASP A 1 88  ? -9.63298  -3.28946  1.64771  1.000 40.42887  ? 74  ASP A HB2  1 
ATOM   1099 H HB3  . ASP A 1 88  ? -10.95101 -2.80501  2.39170  1.000 40.42887  ? 74  ASP A HB3  1 
ATOM   1100 N N    . HIS A 1 89  ? -9.18657  -4.91725  4.22253  1.000 35.54209  ? 75  HIS A N    1 
ATOM   1101 C CA   . HIS A 1 89  ? -9.63874  -6.07861  4.98178  1.000 39.39672  ? 75  HIS A CA   1 
ATOM   1102 C C    . HIS A 1 89  ? -9.12177  -6.09379  6.41535  1.000 37.76530  ? 75  HIS A C    1 
ATOM   1103 O O    . HIS A 1 89  ? -9.47275  -7.01120  7.16519  1.000 36.19352  ? 75  HIS A O    1 
ATOM   1104 C CB   . HIS A 1 89  ? -9.22105  -7.36812  4.26646  1.000 38.24915  ? 75  HIS A CB   1 
ATOM   1105 C CG   . HIS A 1 89  ? -7.77720  -7.72583  4.44410  1.000 43.05371  ? 75  HIS A CG   1 
ATOM   1106 N ND1  . HIS A 1 89  ? -6.75674  -7.04893  3.81124  1.000 48.35270  ? 75  HIS A ND1  1 
ATOM   1107 C CD2  . HIS A 1 89  ? -7.18454  -8.70083  5.17381  1.000 45.40617  ? 75  HIS A CD2  1 
ATOM   1108 C CE1  . HIS A 1 89  ? -5.59769  -7.58598  4.14943  1.000 40.31790  ? 75  HIS A CE1  1 
ATOM   1109 N NE2  . HIS A 1 89  ? -5.82949  -8.59024  4.97524  1.000 43.58091  ? 75  HIS A NE2  1 
ATOM   1110 H H    . HIS A 1 89  ? -8.57092  -5.08480  3.64590  1.000 42.70645  ? 75  HIS A H    1 
ATOM   1111 H HA   . HIS A 1 89  ? -10.60778 -6.05946  5.02042  1.000 47.33201  ? 75  HIS A HA   1 
ATOM   1112 H HB2  . HIS A 1 89  ? -9.75136  -8.10203  4.61437  1.000 45.95492  ? 75  HIS A HB2  1 
ATOM   1113 H HB3  . HIS A 1 89  ? -9.38367  -7.26269  3.31602  1.000 45.95492  ? 75  HIS A HB3  1 
ATOM   1114 H HD2  . HIS A 1 89  ? -7.61446  -9.32802  5.70926  1.000 54.54334  ? 75  HIS A HD2  1 
ATOM   1115 H HE1  . HIS A 1 89  ? -4.76125  -7.30469  3.85592  1.000 48.43742  ? 75  HIS A HE1  1 
ATOM   1116 H HE2  . HIS A 1 89  ? -5.22957  -9.09336  5.33100  1.000 52.35303  ? 75  HIS A HE2  1 
ATOM   1117 N N    . MET A 1 90  ? -8.31773  -5.10913  6.81823  1.000 31.96490  ? 76  MET A N    1 
ATOM   1118 C CA   . MET A 1 90  ? -7.77178  -5.05126  8.16512  1.000 33.69385  ? 76  MET A CA   1 
ATOM   1119 C C    . MET A 1 90  ? -8.15253  -3.79028  8.92714  1.000 31.98556  ? 76  MET A C    1 
ATOM   1120 O O    . MET A 1 90  ? -7.78824  -3.66620  10.10229 1.000 31.55536  ? 76  MET A O    1 
ATOM   1121 C CB   . MET A 1 90  ? -6.24148  -5.14321  8.12306  1.000 32.42129  ? 76  MET A CB   1 
ATOM   1122 C CG   . MET A 1 90  ? -5.69614  -6.49996  7.76350  1.000 34.53933  ? 76  MET A CG   1 
ATOM   1123 S SD   . MET A 1 90  ? -3.89569  -6.47953  7.75577  1.000 32.75345  ? 76  MET A SD   1 
ATOM   1124 C CE   . MET A 1 90  ? -3.53365  -6.14040  9.47965  1.000 30.84849  ? 76  MET A CE   1 
ATOM   1125 H H    . MET A 1 90  ? -8.07233  -4.45402  6.31801  1.000 38.41382  ? 76  MET A H    1 
ATOM   1126 H HA   . MET A 1 90  ? -8.11355  -5.81970  8.64844  1.000 40.48856  ? 76  MET A HA   1 
ATOM   1127 H HB2  . MET A 1 90  ? -5.91401  -4.51341  7.46198  1.000 38.96149  ? 76  MET A HB2  1 
ATOM   1128 H HB3  . MET A 1 90  ? -5.89579  -4.91364  8.99981  1.000 38.96149  ? 76  MET A HB3  1 
ATOM   1129 H HG2  . MET A 1 90  ? -5.99473  -7.15258  8.41605  1.000 41.50314  ? 76  MET A HG2  1 
ATOM   1130 H HG3  . MET A 1 90  ? -6.00590  -6.74968  6.87886  1.000 41.50314  ? 76  MET A HG3  1 
ATOM   1131 H HE1  . MET A 1 90  ? -3.99647  -6.78884  10.03303 1.000 37.07413  ? 76  MET A HE1  1 
ATOM   1132 H HE2  . MET A 1 90  ? -2.57637  -6.20854  9.62063  1.000 37.07413  ? 76  MET A HE2  1 
ATOM   1133 H HE3  . MET A 1 90  ? -3.83690  -5.24472  9.69575  1.000 37.07413  ? 76  MET A HE3  1 
ATOM   1134 N N    . LYS A 1 91  ? -8.86871  -2.85222  8.30484  1.000 33.24418  ? 77  LYS A N    1 
ATOM   1135 C CA   . LYS A 1 91  ? -9.09472  -1.56085  8.94470  1.000 35.24784  ? 77  LYS A CA   1 
ATOM   1136 C C    . LYS A 1 91  ? -9.86670  -1.68419  10.25113 1.000 33.25740  ? 77  LYS A C    1 
ATOM   1137 O O    . LYS A 1 91  ? -9.84147  -0.75007  11.06039 1.000 34.34904  ? 77  LYS A O    1 
ATOM   1138 C CB   . LYS A 1 91  ? -9.82353  -0.61890  7.98637  1.000 38.45518  ? 77  LYS A CB   1 
ATOM   1139 C CG   . LYS A 1 91  ? -8.93085  -0.09274  6.86854  1.000 38.86721  ? 77  LYS A CG   1 
ATOM   1140 C CD   . LYS A 1 91  ? -9.45688  1.20875   6.28841  1.000 42.16124  ? 77  LYS A CD   1 
ATOM   1141 C CE   . LYS A 1 91  ? -8.46000  1.82618   5.31637  1.000 39.11992  ? 77  LYS A CE   1 
ATOM   1142 N NZ   . LYS A 1 91  ? -8.25406  0.97703   4.11105  1.000 49.08884  ? 77  LYS A NZ   1 
ATOM   1143 H H    . LYS A 1 91  ? -9.22661  -2.93838  7.52761  1.000 39.94896  ? 77  LYS A H    1 
ATOM   1144 H HA   . LYS A 1 91  ? -8.23358  -1.16534  9.15185  1.000 42.35335  ? 77  LYS A HA   1 
ATOM   1145 H HB2  . LYS A 1 91  ? -10.56295 -1.09620  7.57851  1.000 46.20216  ? 77  LYS A HB2  1 
ATOM   1146 H HB3  . LYS A 1 91  ? -10.15593 0.14272   8.48670  1.000 46.20216  ? 77  LYS A HB3  1 
ATOM   1147 H HG2  . LYS A 1 91  ? -8.04116  0.06943   7.21934  1.000 46.69659  ? 77  LYS A HG2  1 
ATOM   1148 H HG3  . LYS A 1 91  ? -8.89165  -0.74872  6.15505  1.000 46.69659  ? 77  LYS A HG3  1 
ATOM   1149 H HD2  . LYS A 1 91  ? -10.28332 1.03721   5.81041  1.000 50.64942  ? 77  LYS A HD2  1 
ATOM   1150 H HD3  . LYS A 1 91  ? -9.61435  1.84097   7.00702  1.000 50.64942  ? 77  LYS A HD3  1 
ATOM   1151 H HE2  . LYS A 1 91  ? -8.79186  2.68979   5.02493  1.000 46.99984  ? 77  LYS A HE2  1 
ATOM   1152 H HE3  . LYS A 1 91  ? -7.60467  1.93240   5.76137  1.000 46.99984  ? 77  LYS A HE3  1 
ATOM   1153 H HZ1  . LYS A 1 91  ? -7.97347  0.16784   4.35311  1.000 58.96255  ? 77  LYS A HZ1  1 
ATOM   1154 H HZ2  . LYS A 1 91  ? -9.01813  0.89544   3.66202  1.000 58.96255  ? 77  LYS A HZ2  1 
ATOM   1155 H HZ3  . LYS A 1 91  ? -7.64425  1.34692   3.57869  1.000 58.96255  ? 77  LYS A HZ3  1 
ATOM   1156 N N    . ARG A 1 92  ? -10.54619 -2.81059  10.47925 1.000 28.64397  ? 78  ARG A N    1 
ATOM   1157 C CA   . ARG A 1 92  ? -11.17790 -3.04660  11.77089 1.000 35.26537  ? 78  ARG A CA   1 
ATOM   1158 C C    . ARG A 1 92  ? -10.15858 -3.14643  12.89684 1.000 29.11832  ? 78  ARG A C    1 
ATOM   1159 O O    . ARG A 1 92  ? -10.53512 -3.05667  14.06989 1.000 30.57023  ? 78  ARG A O    1 
ATOM   1160 C CB   . ARG A 1 92  ? -11.99747 -4.33899  11.74298 1.000 37.08496  ? 78  ARG A CB   1 
ATOM   1161 C CG   . ARG A 1 92  ? -13.29241 -4.28132  10.95758 1.000 55.26126  ? 78  ARG A CG   1 
ATOM   1162 C CD   . ARG A 1 92  ? -14.09562 -5.56509  11.16471 1.000 76.16620  ? 78  ARG A CD   1 
ATOM   1163 N NE   . ARG A 1 92  ? -13.24736 -6.75110  11.09340 1.000 77.55855  ? 78  ARG A NE   1 
ATOM   1164 C CZ   . ARG A 1 92  ? -13.03117 -7.46643  9.99644  1.000 76.82802  ? 78  ARG A CZ   1 
ATOM   1165 N NH1  . ARG A 1 92  ? -13.62601 -7.17707  8.85013  1.000 74.12493  ? 78  ARG A NH1  1 
ATOM   1166 N NH2  . ARG A 1 92  ? -12.19443 -8.49901  10.05103 1.000 73.23213  ? 78  ARG A NH2  1 
ATOM   1167 H H    . ARG A 1 92  ? -10.65321 -3.44435  9.90785  1.000 34.42870  ? 78  ARG A H    1 
ATOM   1168 H HA   . ARG A 1 92  ? -11.77704 -2.30469  11.94838 1.000 42.37438  ? 78  ARG A HA   1 
ATOM   1169 H HB2  . ARG A 1 92  ? -11.45186 -5.03640  11.34696 1.000 44.55790  ? 78  ARG A HB2  1 
ATOM   1170 H HB3  . ARG A 1 92  ? -12.22525 -4.57423  12.65604 1.000 44.55790  ? 78  ARG A HB3  1 
ATOM   1171 H HG2  . ARG A 1 92  ? -13.82503 -3.52997  11.26203 1.000 66.36945  ? 78  ARG A HG2  1 
ATOM   1172 H HG3  . ARG A 1 92  ? -13.09630 -4.18755  10.01225 1.000 66.36945  ? 78  ARG A HG3  1 
ATOM   1173 H HD2  . ARG A 1 92  ? -14.51458 -5.54305  12.03929 1.000 91.45538  ? 78  ARG A HD2  1 
ATOM   1174 H HD3  . ARG A 1 92  ? -14.77312 -5.63385  10.47394 1.000 91.45538  ? 78  ARG A HD3  1 
ATOM   1175 H HE   . ARG A 1 92  ? -12.85828 -7.00554  11.81692 1.000 93.12620  ? 78  ARG A HE   1 
ATOM   1176 H HH11 . ARG A 1 92  ? -14.16815 -6.51114  8.80310  1.000 89.00586  ? 78  ARG A HH11 1 
ATOM   1177 H HH12 . ARG A 1 92  ? -13.47039 -7.65498  8.15229  1.000 89.00586  ? 78  ARG A HH12 1 
ATOM   1178 H HH21 . ARG A 1 92  ? -11.80167 -8.69557  10.79042 1.000 87.93449  ? 78  ARG A HH21 1 
ATOM   1179 H HH22 . ARG A 1 92  ? -12.04622 -8.97005  9.34693  1.000 87.93449  ? 78  ARG A HH22 1 
ATOM   1180 N N    . HIS A 1 93  ? -8.88174  -3.34260  12.56797 1.000 32.68044  ? 79  HIS A N    1 
ATOM   1181 C CA   . HIS A 1 93  ? -7.85142  -3.64266  13.55278 1.000 35.76483  ? 79  HIS A CA   1 
ATOM   1182 C C    . HIS A 1 93  ? -6.85831  -2.50044  13.73138 1.000 29.95411  ? 79  HIS A C    1 
ATOM   1183 O O    . HIS A 1 93  ? -5.78317  -2.70415  14.30351 1.000 33.83112  ? 79  HIS A O    1 
ATOM   1184 C CB   . HIS A 1 93  ? -7.12515  -4.92618  13.15186 1.000 33.29991  ? 79  HIS A CB   1 
ATOM   1185 C CG   . HIS A 1 93  ? -8.04945  -6.06830  12.86678 1.000 35.88953  ? 79  HIS A CG   1 
ATOM   1186 N ND1  . HIS A 1 93  ? -8.52202  -6.90625  13.85313 1.000 33.75314  ? 79  HIS A ND1  1 
ATOM   1187 C CD2  . HIS A 1 93  ? -8.60558  -6.49844  11.70987 1.000 36.49374  ? 79  HIS A CD2  1 
ATOM   1188 C CE1  . HIS A 1 93  ? -9.32111  -7.80981  13.31538 1.000 35.44874  ? 79  HIS A CE1  1 
ATOM   1189 N NE2  . HIS A 1 93  ? -9.38859  -7.58468  12.01564 1.000 40.95517  ? 79  HIS A NE2  1 
ATOM   1190 H H    . HIS A 1 93  ? -8.58447  -3.30554  11.76184 1.000 39.27247  ? 79  HIS A H    1 
ATOM   1191 H HA   . HIS A 1 93  ? -8.27486  -3.78333  14.41407 1.000 42.97374  ? 79  HIS A HA   1 
ATOM   1192 H HB2  . HIS A 1 93  ? -6.60704  -4.75541  12.34981 1.000 40.01583  ? 79  HIS A HB2  1 
ATOM   1193 H HB3  . HIS A 1 93  ? -6.53739  -5.19273  13.87602 1.000 40.01583  ? 79  HIS A HB3  1 
ATOM   1194 H HD2  . HIS A 1 93  ? -8.48081  -6.12783  10.86608 1.000 43.84843  ? 79  HIS A HD2  1 
ATOM   1195 H HE1  . HIS A 1 93  ? -9.76126  -8.48884  13.77371 1.000 42.59443  ? 79  HIS A HE1  1 
ATOM   1196 H HE2  . HIS A 1 93  ? -9.84828  -8.04379  11.45217 1.000 49.20215  ? 79  HIS A HE2  1 
ATOM   1197 N N    . ASP A 1 94  ? -7.19884  -1.30080  13.26434 1.000 27.47878  ? 80  ASP A N    1 
ATOM   1198 C CA   . ASP A 1 94  ? -6.32426  -0.13509  13.39435 1.000 28.39681  ? 80  ASP A CA   1 
ATOM   1199 C C    . ASP A 1 94  ? -6.71039  0.59862   14.67320 1.000 28.86884  ? 80  ASP A C    1 
ATOM   1200 O O    . ASP A 1 94  ? -7.58371  1.46659   14.68113 1.000 26.90833  ? 80  ASP A O    1 
ATOM   1201 C CB   . ASP A 1 94  ? -6.43792  0.76182   12.16754 1.000 27.08921  ? 80  ASP A CB   1 
ATOM   1202 C CG   . ASP A 1 94  ? -5.41284  1.88697   12.16125 1.000 30.80320  ? 80  ASP A CG   1 
ATOM   1203 O OD1  . ASP A 1 94  ? -4.72837  2.08831   13.18615 1.000 27.53197  ? 80  ASP A OD1  1 
ATOM   1204 O OD2  . ASP A 1 94  ? -5.28788  2.56672   11.12068 1.000 28.36838  ? 80  ASP A OD2  1 
ATOM   1205 H H    . ASP A 1 94  ? -7.94083  -1.13371  12.86292 1.000 32.69484  ? 80  ASP A H    1 
ATOM   1206 H HA   . ASP A 1 94  ? -5.40261  -0.42720  13.47271 1.000 34.13211  ? 80  ASP A HA   1 
ATOM   1207 H HB2  . ASP A 1 94  ? -6.29963  0.22610   11.37080 1.000 32.56299  ? 80  ASP A HB2  1 
ATOM   1208 H HB3  . ASP A 1 94  ? -7.32156  1.16149   12.14934 1.000 32.56299  ? 80  ASP A HB3  1 
ATOM   1209 N N    . PHE A 1 95  ? -6.05366  0.23296   15.77572 1.000 27.96434  ? 81  PHE A N    1 
ATOM   1210 C CA   . PHE A 1 95  ? -6.29258  0.91707   17.04240 1.000 31.12889  ? 81  PHE A CA   1 
ATOM   1211 C C    . PHE A 1 95  ? -5.78634  2.35280   16.99961 1.000 33.73302  ? 81  PHE A C    1 
ATOM   1212 O O    . PHE A 1 95  ? -6.40717  3.25543   17.57424 1.000 32.81322  ? 81  PHE A O    1 
ATOM   1213 C CB   . PHE A 1 95  ? -5.61530  0.15349   18.18085 1.000 33.08364  ? 81  PHE A CB   1 
ATOM   1214 C CG   . PHE A 1 95  ? -5.42560  0.96752   19.43003 1.000 32.24685  ? 81  PHE A CG   1 
ATOM   1215 C CD1  . PHE A 1 95  ? -6.41833  1.02498   20.39393 1.000 35.95973  ? 81  PHE A CD1  1 
ATOM   1216 C CD2  . PHE A 1 95  ? -4.25072  1.67233   19.64128 1.000 31.02189  ? 81  PHE A CD2  1 
ATOM   1217 C CE1  . PHE A 1 95  ? -6.24484  1.77416   21.54442 1.000 37.45873  ? 81  PHE A CE1  1 
ATOM   1218 C CE2  . PHE A 1 95  ? -4.07097  2.42236   20.78654 1.000 34.40356  ? 81  PHE A CE2  1 
ATOM   1219 C CZ   . PHE A 1 95  ? -5.06856  2.47332   21.74073 1.000 35.78474  ? 81  PHE A CZ   1 
ATOM   1220 H H    . PHE A 1 95  ? -5.47260  -0.39981  15.81535 1.000 33.61315  ? 81  PHE A H    1 
ATOM   1221 H HA   . PHE A 1 95  ? -7.24767  0.93688   17.21066 1.000 37.41061  ? 81  PHE A HA   1 
ATOM   1222 H HB2  . PHE A 1 95  ? -6.16155  -0.61498  18.40881 1.000 39.75631  ? 81  PHE A HB2  1 
ATOM   1223 H HB3  . PHE A 1 95  ? -4.73977  -0.13861  17.88248 1.000 39.75631  ? 81  PHE A HB3  1 
ATOM   1224 H HD1  . PHE A 1 95  ? -7.21054  0.55476   20.26661 1.000 43.20762  ? 81  PHE A HD1  1 
ATOM   1225 H HD2  . PHE A 1 95  ? -3.57482  1.63957   19.00332 1.000 37.28221  ? 81  PHE A HD2  1 
ATOM   1226 H HE1  . PHE A 1 95  ? -6.91861  1.80724   22.18461 1.000 45.00642  ? 81  PHE A HE1  1 
ATOM   1227 H HE2  . PHE A 1 95  ? -3.27911  2.89275   20.91541 1.000 41.34022  ? 81  PHE A HE2  1 
ATOM   1228 H HZ   . PHE A 1 95  ? -4.94909  2.97685   22.51344 1.000 42.99763  ? 81  PHE A HZ   1 
ATOM   1229 N N    . PHE A 1 96  ? -4.66218  2.58094   16.31924 1.000 30.40292  ? 82  PHE A N    1 
ATOM   1230 C CA   . PHE A 1 96  ? -3.99579  3.87694   16.38762 1.000 30.93701  ? 82  PHE A CA   1 
ATOM   1231 C C    . PHE A 1 96  ? -4.90342  4.99454   15.88903 1.000 34.06284  ? 82  PHE A C    1 
ATOM   1232 O O    . PHE A 1 96  ? -5.06938  6.02125   16.55844 1.000 31.99436  ? 82  PHE A O    1 
ATOM   1233 C CB   . PHE A 1 96  ? -2.70018  3.83072   15.57871 1.000 30.17604  ? 82  PHE A CB   1 
ATOM   1234 C CG   . PHE A 1 96  ? -1.78476  2.70638   15.96763 1.000 29.09824  ? 82  PHE A CG   1 
ATOM   1235 C CD1  . PHE A 1 96  ? -0.96569  2.81558   17.07746 1.000 30.40741  ? 82  PHE A CD1  1 
ATOM   1236 C CD2  . PHE A 1 96  ? -1.74386  1.53919   15.22251 1.000 31.96039  ? 82  PHE A CD2  1 
ATOM   1237 C CE1  . PHE A 1 96  ? -0.12285  1.78078   17.43926 1.000 32.55123  ? 82  PHE A CE1  1 
ATOM   1238 C CE2  . PHE A 1 96  ? -0.90219  0.50247   15.57818 1.000 29.59297  ? 82  PHE A CE2  1 
ATOM   1239 C CZ   . PHE A 1 96  ? -0.08978  0.62447   16.68713 1.000 32.02083  ? 82  PHE A CZ   1 
ATOM   1240 H H    . PHE A 1 96  ? -4.26889  2.00583   15.81508 1.000 36.53944  ? 82  PHE A H    1 
ATOM   1241 H HA   . PHE A 1 96  ? -3.77342  4.06775   17.31230 1.000 37.18036  ? 82  PHE A HA   1 
ATOM   1242 H HB2  . PHE A 1 96  ? -2.92178  3.72122   14.64073 1.000 36.26718  ? 82  PHE A HB2  1 
ATOM   1243 H HB3  . PHE A 1 96  ? -2.21987  4.66298   15.71115 1.000 36.26718  ? 82  PHE A HB3  1 
ATOM   1244 H HD1  . PHE A 1 96  ? -0.98222  3.59404   17.58602 1.000 36.54483  ? 82  PHE A HD1  1 
ATOM   1245 H HD2  . PHE A 1 96  ? -2.28921  1.45232   14.47421 1.000 38.40841  ? 82  PHE A HD2  1 
ATOM   1246 H HE1  . PHE A 1 96  ? 0.42124   1.86411   18.18888 1.000 39.11742  ? 82  PHE A HE1  1 
ATOM   1247 H HE2  . PHE A 1 96  ? -0.88324  -0.27667  15.07075 1.000 35.56751  ? 82  PHE A HE2  1 
ATOM   1248 H HZ   . PHE A 1 96  ? 0.47882   -0.07127  16.92698 1.000 38.48094  ? 82  PHE A HZ   1 
ATOM   1249 N N    . LYS A 1 97  ? -5.49875  4.81520   14.70839 1.000 28.24828  ? 83  LYS A N    1 
ATOM   1250 C CA   . LYS A 1 97  ? -6.36686  5.85307   14.16448 1.000 34.17334  ? 83  LYS A CA   1 
ATOM   1251 C C    . LYS A 1 97  ? -7.68327  5.94422   14.92498 1.000 32.15210  ? 83  LYS A C    1 
ATOM   1252 O O    . LYS A 1 97  ? -8.25998  7.03225   15.02909 1.000 36.01260  ? 83  LYS A O    1 
ATOM   1253 C CB   . LYS A 1 97  ? -6.63871  5.59394   12.68305 1.000 30.81588  ? 83  LYS A CB   1 
ATOM   1254 C CG   . LYS A 1 97  ? -5.39941  5.61437   11.80624 1.000 28.78684  ? 83  LYS A CG   1 
ATOM   1255 C CD   . LYS A 1 97  ? -5.76732  5.46349   10.33492 1.000 28.94724  ? 83  LYS A CD   1 
ATOM   1256 C CE   . LYS A 1 97  ? -4.53952  5.44757   9.44545  1.000 26.30638  ? 83  LYS A CE   1 
ATOM   1257 N NZ   . LYS A 1 97  ? -3.67020  4.27433   9.70960  1.000 28.87520  ? 83  LYS A NZ   1 
ATOM   1258 H H    . LYS A 1 97  ? -5.41715  4.11605   14.21428 1.000 33.95387  ? 83  LYS A H    1 
ATOM   1259 H HA   . LYS A 1 97  ? -5.91063  6.70537   14.24407 1.000 41.06395  ? 83  LYS A HA   1 
ATOM   1260 H HB2  . LYS A 1 97  ? -7.04846  4.71946   12.59192 1.000 37.03500  ? 83  LYS A HB2  1 
ATOM   1261 H HB3  . LYS A 1 97  ? -7.24202  6.27884   12.35468 1.000 37.03500  ? 83  LYS A HB3  1 
ATOM   1262 H HG2  . LYS A 1 97  ? -4.93601  6.45868   11.92155 1.000 34.60015  ? 83  LYS A HG2  1 
ATOM   1263 H HG3  . LYS A 1 97  ? -4.81654  4.87954   12.05361 1.000 34.60015  ? 83  LYS A HG3  1 
ATOM   1264 H HD2  . LYS A 1 97  ? -6.24457  4.62856   10.20835 1.000 34.79262  ? 83  LYS A HD2  1 
ATOM   1265 H HD3  . LYS A 1 97  ? -6.32663  6.20927   10.06678 1.000 34.79262  ? 83  LYS A HD3  1 
ATOM   1266 H HE2  . LYS A 1 97  ? -4.81923  5.41326   8.51729  1.000 31.62360  ? 83  LYS A HE2  1 
ATOM   1267 H HE3  . LYS A 1 97  ? -4.01978  6.25071   9.60585  1.000 31.62360  ? 83  LYS A HE3  1 
ATOM   1268 H HZ1  . LYS A 1 97  ? -3.64826  4.10211   10.58250 1.000 34.70617  ? 83  LYS A HZ1  1 
ATOM   1269 H HZ2  . LYS A 1 97  ? -3.98482  3.55995   9.28207  1.000 34.70617  ? 83  LYS A HZ2  1 
ATOM   1270 H HZ3  . LYS A 1 97  ? -2.84254  4.43891   9.42677  1.000 34.70617  ? 83  LYS A HZ3  1 
ATOM   1271 N N    . SER A 1 98  ? -8.17750  4.82265   15.45605 1.000 31.49020  ? 84  SER A N    1 
ATOM   1272 C CA   . SER A 1 98  ? -9.44556  4.84514   16.17644 1.000 31.06127  ? 84  SER A CA   1 
ATOM   1273 C C    . SER A 1 98  ? -9.38107  5.71151   17.42659 1.000 30.73387  ? 84  SER A C    1 
ATOM   1274 O O    . SER A 1 98  ? -10.41953 6.20560   17.87863 1.000 33.30250  ? 84  SER A O    1 
ATOM   1275 C CB   . SER A 1 98  ? -9.86385  3.42315   16.55665 1.000 32.56286  ? 84  SER A CB   1 
ATOM   1276 O OG   . SER A 1 98  ? -9.01776  2.89302   17.56152 1.000 36.07338  ? 84  SER A OG   1 
ATOM   1277 H H    . SER A 1 98  ? -7.80241  4.04998   15.41259 1.000 37.84418  ? 84  SER A H    1 
ATOM   1278 H HA   . SER A 1 98  ? -10.12550 5.21150   15.58960 1.000 37.32946  ? 84  SER A HA   1 
ATOM   1279 H HB2  . SER A 1 98  ? -10.77463 3.44167   16.88988 1.000 39.13137  ? 84  SER A HB2  1 
ATOM   1280 H HB3  . SER A 1 98  ? -9.80987  2.85841   15.76985 1.000 39.13137  ? 84  SER A HB3  1 
ATOM   1281 H HG   . SER A 1 98  ? -8.21423  3.04708   17.37124 1.000 43.34399  ? 84  SER A HG   1 
ATOM   1282 N N    . ALA A 1 99  ? -8.19280  5.90845   17.99181 1.000 30.93556  ? 85  ALA A N    1 
ATOM   1283 C CA   . ALA A 1 99  ? -8.02407  6.70808   19.19668 1.000 32.80452  ? 85  ALA A CA   1 
ATOM   1284 C C    . ALA A 1 99  ? -7.88011  8.19723   18.90715 1.000 35.41858  ? 85  ALA A C    1 
ATOM   1285 O O    . ALA A 1 99  ? -7.75773  8.98776   19.84873 1.000 32.07827  ? 85  ALA A O    1 
ATOM   1286 C CB   . ALA A 1 99  ? -6.80274  6.21816   19.98119 1.000 29.68900  ? 85  ALA A CB   1 
ATOM   1287 H H    . ALA A 1 99  ? -7.45700  5.58231   17.68877 1.000 37.17861  ? 85  ALA A H    1 
ATOM   1288 H HA   . ALA A 1 99  ? -8.80733  6.59199   19.75697 1.000 39.42137  ? 85  ALA A HA   1 
ATOM   1289 H HB1  . ALA A 1 99  ? -6.01212  6.31516   19.42764 1.000 35.68274  ? 85  ALA A HB1  1 
ATOM   1290 H HB2  . ALA A 1 99  ? -6.71013  6.75095   20.78646 1.000 35.68274  ? 85  ALA A HB2  1 
ATOM   1291 H HB3  . ALA A 1 99  ? -6.93070  5.28540   20.21461 1.000 35.68274  ? 85  ALA A HB3  1 
ATOM   1292 N N    . MET A 1 100 ? -7.89523  8.59652   17.64248 1.000 34.09908  ? 86  MET A N    1 
ATOM   1293 C CA   . MET A 1 100 ? -7.74808  9.99245   17.26608 1.000 36.19543  ? 86  MET A CA   1 
ATOM   1294 C C    . MET A 1 100 ? -9.10502  10.67960  17.22964 1.000 35.15806  ? 86  MET A C    1 
ATOM   1295 O O    . MET A 1 100 ? -10.13922 10.02814  17.05586 1.000 37.11133  ? 86  MET A O    1 
ATOM   1296 C CB   . MET A 1 100 ? -7.06929  10.09193  15.90283 1.000 33.95013  ? 86  MET A CB   1 
ATOM   1297 C CG   . MET A 1 100 ? -5.64589  9.55929   15.89638 1.000 30.35728  ? 86  MET A CG   1 
ATOM   1298 S SD   . MET A 1 100 ? -4.57266  10.49301  17.00302 1.000 35.84190  ? 86  MET A SD   1 
ATOM   1299 C CE   . MET A 1 100 ? -3.15412  9.40485   17.08695 1.000 32.56732  ? 86  MET A CE   1 
ATOM   1300 H H    . MET A 1 100 ? -7.99129  8.06681   16.97182 1.000 40.97484  ? 86  MET A H    1 
ATOM   1301 H HA   . MET A 1 100 ? -7.18490  10.44633  17.91239 1.000 43.49045  ? 86  MET A HA   1 
ATOM   1302 H HB2  . MET A 1 100 ? -7.58217  9.57817   15.25947 1.000 40.79609  ? 86  MET A HB2  1 
ATOM   1303 H HB3  . MET A 1 100 ? -7.03952  11.02379  15.63515 1.000 40.79609  ? 86  MET A HB3  1 
ATOM   1304 H HG2  . MET A 1 100 ? -5.65002  8.63386   16.18701 1.000 36.48467  ? 86  MET A HG2  1 
ATOM   1305 H HG3  . MET A 1 100 ? -5.28513  9.62336   14.99825 1.000 36.48467  ? 86  MET A HG3  1 
ATOM   1306 H HE1  . MET A 1 100 ? -2.88600  9.16545   16.18601 1.000 39.13672  ? 86  MET A HE1  1 
ATOM   1307 H HE2  . MET A 1 100 ? -2.42865  9.86583   17.53649 1.000 39.13672  ? 86  MET A HE2  1 
ATOM   1308 H HE3  . MET A 1 100 ? -3.39683  8.60727   17.58278 1.000 39.13672  ? 86  MET A HE3  1 
ATOM   1309 N N    . PRO A 1 101 ? -9.14015  12.01273  17.38078 1.000 34.55855  ? 87  PRO A N    1 
ATOM   1310 C CA   . PRO A 1 101 ? -8.00823  12.94054  17.53332 1.000 34.00818  ? 87  PRO A CA   1 
ATOM   1311 C C    . PRO A 1 101 ? -7.46041  13.03725  18.95476 1.000 36.42481  ? 87  PRO A C    1 
ATOM   1312 O O    . PRO A 1 101 ? -6.37222  13.57302  19.15033 1.000 34.64895  ? 87  PRO A O    1 
ATOM   1313 C CB   . PRO A 1 101 ? -8.61124  14.27724  17.08108 1.000 34.58317  ? 87  PRO A CB   1 
ATOM   1314 C CG   . PRO A 1 101 ? -10.04694 14.18196  17.51161 1.000 37.61416  ? 87  PRO A CG   1 
ATOM   1315 C CD   . PRO A 1 101 ? -10.42599 12.73229  17.30491 1.000 35.64952  ? 87  PRO A CD   1 
ATOM   1316 H HA   . PRO A 1 101 ? -7.29216  12.66210  16.94118 1.000 40.86575  ? 87  PRO A HA   1 
ATOM   1317 H HB2  . PRO A 1 101 ? -8.15990  15.01473  17.52075 1.000 41.55574  ? 87  PRO A HB2  1 
ATOM   1318 H HB3  . PRO A 1 101 ? -8.53766  14.36983  16.11831 1.000 41.55574  ? 87  PRO A HB3  1 
ATOM   1319 H HG2  . PRO A 1 101 ? -10.12853 14.43154  18.44539 1.000 45.19294  ? 87  PRO A HG2  1 
ATOM   1320 H HG3  . PRO A 1 101 ? -10.59510 14.76486  16.96329 1.000 45.19294  ? 87  PRO A HG3  1 
ATOM   1321 H HD2  . PRO A 1 101 ? -11.02796 12.43262  18.00401 1.000 42.83537  ? 87  PRO A HD2  1 
ATOM   1322 H HD3  . PRO A 1 101 ? -10.83810 12.60656  16.43585 1.000 42.83537  ? 87  PRO A HD3  1 
ATOM   1323 N N    . GLU A 1 102 ? -8.17727  12.53972  19.96690 1.000 40.40561  ? 88  GLU A N    1 
ATOM   1324 C CA   . GLU A 1 102 ? -7.69112  12.66539  21.33798 1.000 40.08829  ? 88  GLU A CA   1 
ATOM   1325 C C    . GLU A 1 102 ? -6.30847  12.04797  21.50077 1.000 37.35546  ? 88  GLU A C    1 
ATOM   1326 O O    . GLU A 1 102 ? -5.49445  12.54868  22.28498 1.000 34.74460  ? 88  GLU A O    1 
ATOM   1327 C CB   . GLU A 1 102 ? -8.67414  12.01678  22.31249 1.000 49.01189  ? 88  GLU A CB   1 
ATOM   1328 C CG   . GLU A 1 102 ? -10.07618 12.60919  22.27858 1.000 52.52227  ? 88  GLU A CG   1 
ATOM   1329 C CD   . GLU A 1 102 ? -11.08541 11.68405  21.61809 1.000 63.48312  ? 88  GLU A CD   1 
ATOM   1330 O OE1  . GLU A 1 102 ? -10.79292 11.16369  20.51900 1.000 50.67205  ? 88  GLU A OE1  1 
ATOM   1331 O OE2  . GLU A 1 102 ? -12.16751 11.46893  22.20539 1.000 72.04918  ? 88  GLU A OE2  1 
ATOM   1332 H H    . GLU A 1 102 ? -8.93138  12.13418  19.88647 1.000 48.54267  ? 88  GLU A H    1 
ATOM   1333 H HA   . GLU A 1 102 ? -7.63050  13.60831  21.55734 1.000 48.16189  ? 88  GLU A HA   1 
ATOM   1334 H HB2  . GLU A 1 102 ? -8.74848  11.07430  22.09545 1.000 58.87021  ? 88  GLU A HB2  1 
ATOM   1335 H HB3  . GLU A 1 102 ? -8.33212  12.12367  23.21388 1.000 58.87021  ? 88  GLU A HB3  1 
ATOM   1336 H HG2  . GLU A 1 102 ? -10.37141 12.77641  23.18731 1.000 63.08266  ? 88  GLU A HG2  1 
ATOM   1337 H HG3  . GLU A 1 102 ? -10.05704 13.43973  21.77785 1.000 63.08266  ? 88  GLU A HG3  1 
ATOM   1338 N N    . GLY A 1 103 ? -6.02710  10.96946  20.78185 1.000 30.43377  ? 89  GLY A N    1 
ATOM   1339 C CA   . GLY A 1 103 ? -4.70291  10.38414  20.76853 1.000 32.53099  ? 89  GLY A CA   1 
ATOM   1340 C C    . GLY A 1 103 ? -4.57416  9.19014   21.69091 1.000 30.89598  ? 89  GLY A C    1 
ATOM   1341 O O    . GLY A 1 103 ? -5.54175  8.67852   22.26213 1.000 32.90950  ? 89  GLY A O    1 
ATOM   1342 H H    . GLY A 1 103 ? -6.59659  10.55550  20.28798 1.000 36.57647  ? 89  GLY A H    1 
ATOM   1343 H HA2  . GLY A 1 103 ? -4.49147  10.09485  19.86714 1.000 39.09313  ? 89  GLY A HA2  1 
ATOM   1344 H HA3  . GLY A 1 103 ? -4.05646  11.05214  21.04562 1.000 39.09313  ? 89  GLY A HA3  1 
ATOM   1345 N N    . TYR A 1 104 ? -3.33016  8.73840   21.82473 1.000 31.71561  ? 90  TYR A N    1 
ATOM   1346 C CA   . TYR A 1 104 ? -3.00337  7.60869   22.67810 1.000 33.28629  ? 90  TYR A CA   1 
ATOM   1347 C C    . TYR A 1 104 ? -1.64330  7.84120   23.31694 1.000 31.46657  ? 90  TYR A C    1 
ATOM   1348 O O    . TYR A 1 104 ? -0.82571  8.62296   22.82516 1.000 31.47433  ? 90  TYR A O    1 
ATOM   1349 C CB   . TYR A 1 104 ? -3.00396  6.28673   21.89588 1.000 31.10944  ? 90  TYR A CB   1 
ATOM   1350 C CG   . TYR A 1 104 ? -2.14361  6.29236   20.64968 1.000 29.38027  ? 90  TYR A CG   1 
ATOM   1351 C CD1  . TYR A 1 104 ? -0.76101  6.19639   20.73389 1.000 29.62432  ? 90  TYR A CD1  1 
ATOM   1352 C CD2  . TYR A 1 104 ? -2.71709  6.37460   19.38691 1.000 34.44119  ? 90  TYR A CD2  1 
ATOM   1353 C CE1  . TYR A 1 104 ? 0.02852   6.19398   19.59636 1.000 28.17525  ? 90  TYR A CE1  1 
ATOM   1354 C CE2  . TYR A 1 104 ? -1.93602  6.37070   18.24329 1.000 33.60527  ? 90  TYR A CE2  1 
ATOM   1355 C CZ   . TYR A 1 104 ? -0.56491  6.28159   18.35359 1.000 32.03192  ? 90  TYR A CZ   1 
ATOM   1356 O OH   . TYR A 1 104 ? 0.21139   6.27862   17.21591 1.000 29.02165  ? 90  TYR A OH   1 
ATOM   1357 H H    . TYR A 1 104 ? -2.64920  9.07741   21.42352 1.000 38.11467  ? 90  TYR A H    1 
ATOM   1358 H HA   . TYR A 1 104 ? -3.66274  7.54069   23.38626 1.000 39.99949  ? 90  TYR A HA   1 
ATOM   1359 H HB2  . TYR A 1 104 ? -2.67289  5.58407   22.47688 1.000 37.38726  ? 90  TYR A HB2  1 
ATOM   1360 H HB3  . TYR A 1 104 ? -3.91365  6.09012   21.62258 1.000 37.38726  ? 90  TYR A HB3  1 
ATOM   1361 H HD1  . TYR A 1 104 ? -0.35788  6.13257   21.56954 1.000 35.60512  ? 90  TYR A HD1  1 
ATOM   1362 H HD2  . TYR A 1 104 ? -3.64189  6.43331   19.30820 1.000 41.38537  ? 90  TYR A HD2  1 
ATOM   1363 H HE1  . TYR A 1 104 ? 0.95367   6.13364   19.66949 1.000 33.86624  ? 90  TYR A HE1  1 
ATOM   1364 H HE2  . TYR A 1 104 ? -2.33463  6.42792   17.40499 1.000 40.38226  ? 90  TYR A HE2  1 
ATOM   1365 H HH   . TYR A 1 104 ? 1.02306   6.21330   17.42213 1.000 34.88192  ? 90  TYR A HH   1 
ATOM   1366 N N    . VAL A 1 105 ? -1.41548  7.15132   24.42862 1.000 30.41379  ? 91  VAL A N    1 
ATOM   1367 C CA   . VAL A 1 105 ? -0.13348  7.16042   25.11936 1.000 29.82329  ? 91  VAL A CA   1 
ATOM   1368 C C    . VAL A 1 105 ? 0.64033   5.92866   24.67491 1.000 32.04228  ? 91  VAL A C    1 
ATOM   1369 O O    . VAL A 1 105 ? 0.18667   4.79717   24.87890 1.000 32.87547  ? 91  VAL A O    1 
ATOM   1370 C CB   . VAL A 1 105 ? -0.31693  7.17358   26.64478 1.000 27.44474  ? 91  VAL A CB   1 
ATOM   1371 C CG1  . VAL A 1 105 ? 1.02394   6.99886   27.34101 1.000 32.06368  ? 91  VAL A CG1  1 
ATOM   1372 C CG2  . VAL A 1 105 ? -0.99345  8.45861   27.08661 1.000 36.27382  ? 91  VAL A CG2  1 
ATOM   1373 H H    . VAL A 1 105 ? -2.00545  6.65678   24.81199 1.000 36.55249  ? 91  VAL A H    1 
ATOM   1374 H HA   . VAL A 1 105 ? 0.36591   7.95240   24.86585 1.000 35.84388  ? 91  VAL A HA   1 
ATOM   1375 H HB   . VAL A 1 105 ? -0.88717  6.43222   26.90189 1.000 32.65476  ? 91  VAL A HB   1 
ATOM   1376 H HG11 . VAL A 1 105 ? 1.33507   6.09043   27.20370 1.000 38.53235  ? 91  VAL A HG11 1 
ATOM   1377 H HG12 . VAL A 1 105 ? 1.65980   7.62684   26.96388 1.000 38.53235  ? 91  VAL A HG12 1 
ATOM   1378 H HG13 . VAL A 1 105 ? 0.91220   7.17047   28.28915 1.000 38.53235  ? 91  VAL A HG13 1 
ATOM   1379 H HG21 . VAL A 1 105 ? -0.85338  9.13838   26.40897 1.000 43.58452  ? 91  VAL A HG21 1 
ATOM   1380 H HG22 . VAL A 1 105 ? -1.94276  8.29350   27.19823 1.000 43.58452  ? 91  VAL A HG22 1 
ATOM   1381 H HG23 . VAL A 1 105 ? -0.60646  8.74597   27.92837 1.000 43.58452  ? 91  VAL A HG23 1 
ATOM   1382 N N    . GLN A 1 106 ? 1.80302   6.14265   24.06838 1.000 30.00217  ? 92  GLN A N    1 
ATOM   1383 C CA   . GLN A 1 106 ? 2.68955   5.06031   23.66058 1.000 26.46198  ? 92  GLN A CA   1 
ATOM   1384 C C    . GLN A 1 106 ? 3.85641   4.99224   24.63908 1.000 27.31893  ? 92  GLN A C    1 
ATOM   1385 O O    . GLN A 1 106 ? 4.58892   5.97344   24.80757 1.000 28.03061  ? 92  GLN A O    1 
ATOM   1386 C CB   . GLN A 1 106 ? 3.18612   5.27108   22.22879 1.000 26.87896  ? 92  GLN A CB   1 
ATOM   1387 C CG   . GLN A 1 106 ? 4.24033   4.26812   21.77766 1.000 27.34126  ? 92  GLN A CG   1 
ATOM   1388 C CD   . GLN A 1 106 ? 4.42136   4.23909   20.26885 1.000 29.37282  ? 92  GLN A CD   1 
ATOM   1389 O OE1  . GLN A 1 106 ? 3.46015   4.06478   19.52035 1.000 24.98518  ? 92  GLN A OE1  1 
ATOM   1390 N NE2  . GLN A 1 106 ? 5.65848   4.41389   19.81623 1.000 31.28350  ? 92  GLN A NE2  1 
ATOM   1391 H H    . GLN A 1 106 ? 2.10647   6.92454   23.87821 1.000 36.05855  ? 92  GLN A H    1 
ATOM   1392 H HA   . GLN A 1 106 ? 2.21337   4.21574   23.68981 1.000 31.81032  ? 92  GLN A HA   1 
ATOM   1393 H HB2  . GLN A 1 106 ? 2.43096   5.19556   21.62470 1.000 32.31069  ? 92  GLN A HB2  1 
ATOM   1394 H HB3  . GLN A 1 106 ? 3.57604   6.15685   22.16335 1.000 32.31069  ? 92  GLN A HB3  1 
ATOM   1395 H HG2  . GLN A 1 106 ? 5.09216   4.50455   22.17689 1.000 32.86545  ? 92  GLN A HG2  1 
ATOM   1396 H HG3  . GLN A 1 106 ? 3.97453   3.38042   22.06442 1.000 32.86545  ? 92  GLN A HG3  1 
ATOM   1397 H HE21 . GLN A 1 106 ? 6.30564   4.53523   20.36946 1.000 37.59614  ? 92  GLN A HE21 1 
ATOM   1398 H HE22 . GLN A 1 106 ? 5.81195   4.40567   18.97008 1.000 37.59614  ? 92  GLN A HE22 1 
ATOM   1399 N N    . GLU A 1 107 ? 4.01459   3.84416   25.29291 1.000 29.29143  ? 93  GLU A N    1 
ATOM   1400 C CA   . GLU A 1 107 ? 5.10141   3.60985   26.23235 1.000 30.16558  ? 93  GLU A CA   1 
ATOM   1401 C C    . GLU A 1 107 ? 5.93741   2.43135   25.75749 1.000 34.25409  ? 93  GLU A C    1 
ATOM   1402 O O    . GLU A 1 107 ? 5.40406   1.46175   25.20824 1.000 29.80902  ? 93  GLU A O    1 
ATOM   1403 C CB   . GLU A 1 107 ? 4.56895   3.33082   27.64090 1.000 27.70007  ? 93  GLU A CB   1 
ATOM   1404 C CG   . GLU A 1 107 ? 3.73855   4.45792   28.22197 1.000 34.47993  ? 93  GLU A CG   1 
ATOM   1405 C CD   . GLU A 1 107 ? 3.31733   4.19064   29.65278 1.000 44.31584  ? 93  GLU A CD   1 
ATOM   1406 O OE1  . GLU A 1 107 ? 2.63349   3.17464   29.89321 1.000 48.76799  ? 93  GLU A OE1  1 
ATOM   1407 O OE2  . GLU A 1 107 ? 3.68041   4.99176   30.53878 1.000 51.23021  ? 93  GLU A OE2  1 
ATOM   1408 H H    . GLU A 1 107 ? 3.48910   3.16913   25.20462 1.000 35.20566  ? 93  GLU A H    1 
ATOM   1409 H HA   . GLU A 1 107 ? 5.66880   4.39556   26.27274 1.000 36.25464  ? 93  GLU A HA   1 
ATOM   1410 H HB2  . GLU A 1 107 ? 4.01038   2.53837   27.61052 1.000 33.29602  ? 93  GLU A HB2  1 
ATOM   1411 H HB3  . GLU A 1 107 ? 5.32209   3.18330   28.23413 1.000 33.29602  ? 93  GLU A HB3  1 
ATOM   1412 H HG2  . GLU A 1 107 ? 4.26074   5.27527   28.20970 1.000 41.43185  ? 93  GLU A HG2  1 
ATOM   1413 H HG3  . GLU A 1 107 ? 2.93645   4.56863   27.68784 1.000 41.43185  ? 93  GLU A HG3  1 
ATOM   1414 N N    . ARG A 1 108 ? 7.24850   2.51514   25.97234 1.000 32.62241  ? 94  ARG A N    1 
ATOM   1415 C CA   . ARG A 1 108 ? 8.14641   1.43447   25.60345 1.000 30.55328  ? 94  ARG A CA   1 
ATOM   1416 C C    . ARG A 1 108 ? 9.24393   1.28017   26.64277 1.000 30.29264  ? 94  ARG A C    1 
ATOM   1417 O O    . ARG A 1 108 ? 9.61222   2.23185   27.33469 1.000 28.58283  ? 94  ARG A O    1 
ATOM   1418 C CB   . ARG A 1 108 ? 8.80839   1.66295   24.23883 1.000 25.76824  ? 94  ARG A CB   1 
ATOM   1419 C CG   . ARG A 1 108 ? 7.90229   1.47213   23.04429 1.000 31.06707  ? 94  ARG A CG   1 
ATOM   1420 C CD   . ARG A 1 108 ? 8.72071   1.03384   21.83850 1.000 29.27578  ? 94  ARG A CD   1 
ATOM   1421 N NE   . ARG A 1 108 ? 7.93645   0.98068   20.61054 1.000 27.28223  ? 94  ARG A NE   1 
ATOM   1422 C CZ   . ARG A 1 108 ? 7.91824   1.93081   19.68486 1.000 22.21993  ? 94  ARG A CZ   1 
ATOM   1423 N NH1  . ARG A 1 108 ? 8.61672   3.04613   19.82213 1.000 27.08722  ? 94  ARG A NH1  1 
ATOM   1424 N NH2  . ARG A 1 108 ? 7.18492   1.75413   18.58994 1.000 24.85548  ? 94  ARG A NH2  1 
ATOM   1425 H H    . ARG A 1 108 ? 7.63916   3.19171   26.33182 1.000 39.20283  ? 94  ARG A H    1 
ATOM   1426 H HA   . ARG A 1 108 ? 7.62462   0.61737   25.57203 1.000 36.71988  ? 94  ARG A HA   1 
ATOM   1427 H HB2  . ARG A 1 108 ? 9.14057   2.57378   24.20829 1.000 30.97783  ? 94  ARG A HB2  1 
ATOM   1428 H HB3  . ARG A 1 108 ? 9.54460   1.03806   24.14715 1.000 30.97783  ? 94  ARG A HB3  1 
ATOM   1429 H HG2  . ARG A 1 108 ? 7.24337   0.78748   23.23919 1.000 37.33643  ? 94  ARG A HG2  1 
ATOM   1430 H HG3  . ARG A 1 108 ? 7.45899   2.30855   22.83265 1.000 37.33643  ? 94  ARG A HG3  1 
ATOM   1431 H HD2  . ARG A 1 108 ? 9.44609   1.66348   21.70333 1.000 35.18687  ? 94  ARG A HD2  1 
ATOM   1432 H HD3  . ARG A 1 108 ? 9.07756   0.14724   22.00433 1.000 35.18687  ? 94  ARG A HD3  1 
ATOM   1433 H HE   . ARG A 1 108 ? 7.45094   0.28356   20.47674 1.000 32.79462  ? 94  ARG A HE   1 
ATOM   1434 H HH11 . ARG A 1 108 ? 9.09766   3.16862   20.52449 1.000 32.56060  ? 94  ARG A HH11 1 
ATOM   1435 H HH12 . ARG A 1 108 ? 8.58978   3.64858   19.20900 1.000 32.56060  ? 94  ARG A HH12 1 
ATOM   1436 H HH21 . ARG A 1 108 ? 6.73042   1.03107   18.48885 1.000 29.88252  ? 94  ARG A HH21 1 
ATOM   1437 H HH22 . ARG A 1 108 ? 7.16511   2.36290   17.98281 1.000 29.88252  ? 94  ARG A HH22 1 
ATOM   1438 N N    . THR A 1 109 ? 9.75549   0.05858   26.74233 1.000 34.53826  ? 95  THR A N    1 
ATOM   1439 C CA   . THR A 1 109 ? 11.05244  -0.21741  27.34225 1.000 30.12428  ? 95  THR A CA   1 
ATOM   1440 C C    . THR A 1 109 ? 11.88673  -0.90367  26.27104 1.000 27.69491  ? 95  THR A C    1 
ATOM   1441 O O    . THR A 1 109 ? 11.45863  -1.91396  25.70320 1.000 25.81278  ? 95  THR A O    1 
ATOM   1442 C CB   . THR A 1 109 ? 10.92732  -1.09293  28.58878 1.000 31.24586  ? 95  THR A CB   1 
ATOM   1443 O OG1  . THR A 1 109 ? 10.01218  -0.48990  29.51261 1.000 34.41906  ? 95  THR A OG1  1 
ATOM   1444 C CG2  . THR A 1 109 ? 12.27904  -1.24905  29.25819 1.000 36.05344  ? 95  THR A CG2  1 
ATOM   1445 H H    . THR A 1 109 ? 9.35572   -0.64851  26.45983 1.000 41.50185  ? 95  THR A H    1 
ATOM   1446 H HA   . THR A 1 109 ? 11.48370  0.60585   27.62004 1.000 36.20508  ? 95  THR A HA   1 
ATOM   1447 H HB   . THR A 1 109 ? 10.60044  -1.97084  28.33712 1.000 37.55097  ? 95  THR A HB   1 
ATOM   1448 H HG1  . THR A 1 109 ? 9.24070   -0.46964  29.18092 1.000 41.35881  ? 95  THR A HG1  1 
ATOM   1449 H HG21 . THR A 1 109 ? 12.64286  -0.37725  29.47842 1.000 43.32007  ? 95  THR A HG21 1 
ATOM   1450 H HG22 . THR A 1 109 ? 12.18780  -1.76710  30.07317 1.000 43.32007  ? 95  THR A HG22 1 
ATOM   1451 H HG23 . THR A 1 109 ? 12.89363  -1.70525  28.66232 1.000 43.32007  ? 95  THR A HG23 1 
ATOM   1452 N N    . ILE A 1 110 ? 13.04894  -0.33891  25.96839 1.000 27.18386  ? 96  ILE A N    1 
ATOM   1453 C CA   . ILE A 1 110 ? 13.92218  -0.85047  24.91978 1.000 30.26245  ? 96  ILE A CA   1 
ATOM   1454 C C    . ILE A 1 110 ? 15.18790  -1.35967  25.59134 1.000 31.63255  ? 96  ILE A C    1 
ATOM   1455 O O    . ILE A 1 110 ? 16.00487  -0.56816  26.07609 1.000 30.96904  ? 96  ILE A O    1 
ATOM   1456 C CB   . ILE A 1 110 ? 14.24032  0.22007   23.86754 1.000 28.49042  ? 96  ILE A CB   1 
ATOM   1457 C CG1  . ILE A 1 110 ? 12.94389  0.83604   23.32952 1.000 24.79952  ? 96  ILE A CG1  1 
ATOM   1458 C CG2  . ILE A 1 110 ? 15.05471  -0.38537  22.73279 1.000 32.33885  ? 96  ILE A CG2  1 
ATOM   1459 C CD1  . ILE A 1 110 ? 13.15813  1.96535   22.33645 1.000 32.00971  ? 96  ILE A CD1  1 
ATOM   1460 H H    . ILE A 1 110 ? 13.36003  0.35745   26.36577 1.000 32.67657  ? 96  ILE A H    1 
ATOM   1461 H HA   . ILE A 1 110 ? 13.48899  -1.59548  24.47459 1.000 36.37088  ? 96  ILE A HA   1 
ATOM   1462 H HB   . ILE A 1 110 ? 14.76390  0.92123   24.28603 1.000 34.24444  ? 96  ILE A HB   1 
ATOM   1463 H HG12 . ILE A 1 110 ? 12.43347  0.14322   22.88189 1.000 29.81536  ? 96  ILE A HG12 1 
ATOM   1464 H HG13 . ILE A 1 110 ? 12.43654  1.19229   24.07556 1.000 29.81536  ? 96  ILE A HG13 1 
ATOM   1465 H HG21 . ILE A 1 110 ? 15.27296  0.31127   22.09407 1.000 38.86256  ? 96  ILE A HG21 1 
ATOM   1466 H HG22 . ILE A 1 110 ? 15.86871  -0.76705  23.09697 1.000 38.86256  ? 96  ILE A HG22 1 
ATOM   1467 H HG23 . ILE A 1 110 ? 14.52931  -1.07712  22.30113 1.000 38.86256  ? 96  ILE A HG23 1 
ATOM   1468 H HD11 . ILE A 1 110 ? 13.75637  2.62090   22.72794 1.000 38.46760  ? 96  ILE A HD11 1 
ATOM   1469 H HD12 . ILE A 1 110 ? 13.54902  1.60323   21.52592 1.000 38.46760  ? 96  ILE A HD12 1 
ATOM   1470 H HD13 . ILE A 1 110 ? 12.30260  2.37627   22.13613 1.000 38.46760  ? 96  ILE A HD13 1 
ATOM   1471 N N    . PHE A 1 111 ? 15.35240  -2.67966  25.62312 1.000 29.71244  ? 97  PHE A N    1 
ATOM   1472 C CA   . PHE A 1 111 ? 16.52114  -3.30683  26.22918 1.000 32.98480  ? 97  PHE A CA   1 
ATOM   1473 C C    . PHE A 1 111 ? 17.58577  -3.49429  25.15518 1.000 33.42081  ? 97  PHE A C    1 
ATOM   1474 O O    . PHE A 1 111 ? 17.40541  -4.28550  24.22447 1.000 30.73290  ? 97  PHE A O    1 
ATOM   1475 C CB   . PHE A 1 111 ? 16.15323  -4.64607  26.86280 1.000 36.24370  ? 97  PHE A CB   1 
ATOM   1476 C CG   . PHE A 1 111 ? 15.18277  -4.53534  28.00515 1.000 40.81890  ? 97  PHE A CG   1 
ATOM   1477 C CD1  . PHE A 1 111 ? 13.81678  -4.57146  27.77768 1.000 37.11861  ? 97  PHE A CD1  1 
ATOM   1478 C CD2  . PHE A 1 111 ? 15.63694  -4.40573  29.30812 1.000 38.32703  ? 97  PHE A CD2  1 
ATOM   1479 C CE1  . PHE A 1 111 ? 12.92023  -4.47419  28.82690 1.000 36.90593  ? 97  PHE A CE1  1 
ATOM   1480 C CE2  . PHE A 1 111 ? 14.74492  -4.30749  30.36343 1.000 36.55654  ? 97  PHE A CE2  1 
ATOM   1481 C CZ   . PHE A 1 111 ? 13.38459  -4.34268  30.12164 1.000 35.81501  ? 97  PHE A CZ   1 
ATOM   1482 H H    . PHE A 1 111 ? 14.79067  -3.24175  25.29430 1.000 35.71087  ? 97  PHE A H    1 
ATOM   1483 H HA   . PHE A 1 111 ? 16.87097  -2.72430  26.92141 1.000 39.63770  ? 97  PHE A HA   1 
ATOM   1484 H HB2  . PHE A 1 111 ? 15.74837  -5.20991  26.18526 1.000 43.54838  ? 97  PHE A HB2  1 
ATOM   1485 H HB3  . PHE A 1 111 ? 16.96129  -5.06238  27.20137 1.000 43.54838  ? 97  PHE A HB3  1 
ATOM   1486 H HD1  . PHE A 1 111 ? 13.49833  -4.66225  26.90863 1.000 44.59828  ? 97  PHE A HD1  1 
ATOM   1487 H HD2  . PHE A 1 111 ? 16.55142  -4.38446  29.47598 1.000 46.04837  ? 97  PHE A HD2  1 
ATOM   1488 H HE1  . PHE A 1 111 ? 12.00546  -4.49731  28.66084 1.000 44.34305  ? 97  PHE A HE1  1 
ATOM   1489 H HE2  . PHE A 1 111 ? 15.06101  -4.21797  31.23348 1.000 43.92378  ? 97  PHE A HE2  1 
ATOM   1490 H HZ   . PHE A 1 111 ? 12.78351  -4.27803  30.82833 1.000 43.03395  ? 97  PHE A HZ   1 
ATOM   1491 N N    . PHE A 1 112 ? 18.69236  -2.76897  25.28006 1.000 29.66072  ? 98  PHE A N    1 
ATOM   1492 C CA   . PHE A 1 112 ? 19.83986  -2.96094  24.40404 1.000 30.59154  ? 98  PHE A CA   1 
ATOM   1493 C C    . PHE A 1 112 ? 20.70240  -4.07372  24.98654 1.000 30.70055  ? 98  PHE A C    1 
ATOM   1494 O O    . PHE A 1 112 ? 21.14673  -3.98541  26.13680 1.000 31.79227  ? 98  PHE A O    1 
ATOM   1495 C CB   . PHE A 1 112 ? 20.63581  -1.66687  24.25124 1.000 29.39590  ? 98  PHE A CB   1 
ATOM   1496 C CG   . PHE A 1 112 ? 19.91393  -0.59947  23.47427 1.000 30.86537  ? 98  PHE A CG   1 
ATOM   1497 C CD1  . PHE A 1 112 ? 19.07571  0.29927   24.11485 1.000 28.46352  ? 98  PHE A CD1  1 
ATOM   1498 C CD2  . PHE A 1 112 ? 20.07356  -0.49532  22.10233 1.000 29.79988  ? 98  PHE A CD2  1 
ATOM   1499 C CE1  . PHE A 1 112 ? 18.41214  1.28176   23.40025 1.000 27.47428  ? 98  PHE A CE1  1 
ATOM   1500 C CE2  . PHE A 1 112 ? 19.41207  0.48476   21.38495 1.000 29.42943  ? 98  PHE A CE2  1 
ATOM   1501 C CZ   . PHE A 1 112 ? 18.58118  1.37370   22.03587 1.000 25.34557  ? 98  PHE A CZ   1 
ATOM   1502 H H    . PHE A 1 112 ? 18.80269  -2.15374  25.87075 1.000 35.64881  ? 98  PHE A H    1 
ATOM   1503 H HA   . PHE A 1 112 ? 19.54299  -3.22302  23.51856 1.000 36.76578  ? 98  PHE A HA   1 
ATOM   1504 H HB2  . PHE A 1 112 ? 20.82729  -1.31244  25.13363 1.000 35.33103  ? 98  PHE A HB2  1 
ATOM   1505 H HB3  . PHE A 1 112 ? 21.46384  -1.86313  23.78568 1.000 35.33103  ? 98  PHE A HB3  1 
ATOM   1506 H HD1  . PHE A 1 112 ? 18.95766  0.24164   25.03553 1.000 34.21216  ? 98  PHE A HD1  1 
ATOM   1507 H HD2  . PHE A 1 112 ? 20.63226  -1.09160  21.65824 1.000 35.81580  ? 98  PHE A HD2  1 
ATOM   1508 H HE1  . PHE A 1 112 ? 17.85240  1.87959   23.84092 1.000 33.02508  ? 98  PHE A HE1  1 
ATOM   1509 H HE2  . PHE A 1 112 ? 19.52720  0.54471   20.46406 1.000 35.37126  ? 98  PHE A HE2  1 
ATOM   1510 H HZ   . PHE A 1 112 ? 18.13623  2.03349   21.55464 1.000 30.47063  ? 98  PHE A HZ   1 
ATOM   1511 N N    . LYS A 1 113 ? 20.92321  -5.12231  24.19904 1.000 33.64820  ? 99  LYS A N    1 
ATOM   1512 C CA   . LYS A 1 113 ? 21.62204  -6.29917  24.69695 1.000 34.72906  ? 99  LYS A CA   1 
ATOM   1513 C C    . LYS A 1 113 ? 23.01288  -5.92655  25.19225 1.000 37.11119  ? 99  LYS A C    1 
ATOM   1514 O O    . LYS A 1 113 ? 23.74331  -5.17990  24.53369 1.000 36.63400  ? 99  LYS A O    1 
ATOM   1515 C CB   . LYS A 1 113 ? 21.71440  -7.35438  23.59553 1.000 39.67941  ? 99  LYS A CB   1 
ATOM   1516 C CG   . LYS A 1 113 ? 22.24026  -8.70588  24.05398 1.000 38.88454  ? 99  LYS A CG   1 
ATOM   1517 C CD   . LYS A 1 113 ? 21.31672  -9.33737  25.08416 1.000 52.71817  ? 99  LYS A CD   1 
ATOM   1518 C CE   . LYS A 1 113 ? 21.16969  -10.83660 24.86516 1.000 69.61247  ? 99  LYS A CE   1 
ATOM   1519 N NZ   . LYS A 1 113 ? 22.45546  -11.56709 25.03801 1.000 67.99011  ? 99  LYS A NZ   1 
ATOM   1520 H H    . LYS A 1 113 ? 20.67924  -5.17637  23.37615 1.000 40.43378  ? 99  LYS A H    1 
ATOM   1521 H HA   . LYS A 1 113 ? 21.12767  -6.67624  25.44148 1.000 41.73081  ? 99  LYS A HA   1 
ATOM   1522 H HB2  . LYS A 1 113 ? 20.82772  -7.49505  23.22823 1.000 47.67123  ? 99  LYS A HB2  1 
ATOM   1523 H HB3  . LYS A 1 113 ? 22.31165  -7.02742  22.90466 1.000 47.67123  ? 99  LYS A HB3  1 
ATOM   1524 H HG2  . LYS A 1 113 ? 22.30187  -9.30287  23.29193 1.000 46.71739  ? 99  LYS A HG2  1 
ATOM   1525 H HG3  . LYS A 1 113 ? 23.11502  -8.59121  24.45716 1.000 46.71739  ? 99  LYS A HG3  1 
ATOM   1526 H HD2  . LYS A 1 113 ? 21.68106  -9.19417  25.97165 1.000 63.31774  ? 99  LYS A HD2  1 
ATOM   1527 H HD3  . LYS A 1 113 ? 20.43766  -8.93281  25.01716 1.000 63.31774  ? 99  LYS A HD3  1 
ATOM   1528 H HE2  . LYS A 1 113 ? 20.53433  -11.19015 25.50720 1.000 83.59090  ? 99  LYS A HE2  1 
ATOM   1529 H HE3  . LYS A 1 113 ? 20.85248  -10.99569 23.96241 1.000 83.59090  ? 99  LYS A HE3  1 
ATOM   1530 H HZ1  . LYS A 1 113 ? 22.33833  -12.43330 24.87050 1.000 81.64407  ? 99  LYS A HZ1  1 
ATOM   1531 H HZ2  . LYS A 1 113 ? 23.06660  -11.24451 24.47717 1.000 81.64407  ? 99  LYS A HZ2  1 
ATOM   1532 H HZ3  . LYS A 1 113 ? 22.75007  -11.47152 25.87238 1.000 81.64407  ? 99  LYS A HZ3  1 
ATOM   1533 N N    . ASP A 1 114 ? 23.37405  -6.45094  26.36293 1.000 36.70498  ? 100 ASP A N    1 
ATOM   1534 C CA   . ASP A 1 114 ? 24.67189  -6.20747  26.98466 1.000 33.14139  ? 100 ASP A CA   1 
ATOM   1535 C C    . ASP A 1 114 ? 24.92669  -4.72494  27.22819 1.000 33.82848  ? 100 ASP A C    1 
ATOM   1536 O O    . ASP A 1 114 ? 26.07983  -4.30611  27.36917 1.000 34.36281  ? 100 ASP A O    1 
ATOM   1537 C CB   . ASP A 1 114 ? 25.80711  -6.79539  26.13792 1.000 43.76869  ? 100 ASP A CB   1 
ATOM   1538 C CG   . ASP A 1 114 ? 25.62447  -8.27389  25.86070 1.000 47.68003  ? 100 ASP A CG   1 
ATOM   1539 O OD1  . ASP A 1 114 ? 25.10912  -8.99032  26.74544 1.000 47.69625  ? 100 ASP A OD1  1 
ATOM   1540 O OD2  . ASP A 1 114 ? 25.99656  -8.71917  24.75389 1.000 54.59663  ? 100 ASP A OD2  1 
ATOM   1541 H H    . ASP A 1 114 ? 22.86738  -6.96655  26.82880 1.000 44.10192  ? 100 ASP A H    1 
ATOM   1542 H HA   . ASP A 1 114 ? 24.67644  -6.64888  27.84840 1.000 39.82561  ? 100 ASP A HA   1 
ATOM   1543 H HB2  . ASP A 1 114 ? 25.83919  -6.33203  25.28636 1.000 52.57837  ? 100 ASP A HB2  1 
ATOM   1544 H HB3  . ASP A 1 114 ? 26.64645  -6.67998  26.61025 1.000 52.57837  ? 100 ASP A HB3  1 
ATOM   1545 N N    . ASP A 1 115 ? 23.87430  -3.91858  27.28662 1.000 34.85171  ? 101 ASP A N    1 
ATOM   1546 C CA   . ASP A 1 115 ? 24.02226  -2.47663  27.43619 1.000 29.48346  ? 101 ASP A CA   1 
ATOM   1547 C C    . ASP A 1 115 ? 22.80357  -1.95692  28.19546 1.000 32.70494  ? 101 ASP A C    1 
ATOM   1548 O O    . ASP A 1 115 ? 22.08473  -2.72844  28.83876 1.000 31.40044  ? 101 ASP A O    1 
ATOM   1549 C CB   . ASP A 1 115 ? 24.21201  -1.82198  26.05545 1.000 28.95957  ? 101 ASP A CB   1 
ATOM   1550 C CG   . ASP A 1 115 ? 25.06992  -0.57097  26.11421 1.000 34.89313  ? 101 ASP A CG   1 
ATOM   1551 O OD1  . ASP A 1 115 ? 24.99006  0.15761   27.12313 1.000 32.48916  ? 101 ASP A OD1  1 
ATOM   1552 O OD2  . ASP A 1 115 ? 25.82697  -0.31663  25.15298 1.000 37.23739  ? 101 ASP A OD2  1 
ATOM   1553 H H    . ASP A 1 115 ? 23.05761  -4.18428  27.24153 1.000 41.87800  ? 101 ASP A H    1 
ATOM   1554 H HA   . ASP A 1 115 ? 24.81034  -2.29336  27.97120 1.000 35.43609  ? 101 ASP A HA   1 
ATOM   1555 H HB2  . ASP A 1 115 ? 24.64477  -2.45531  25.46172 1.000 34.80743  ? 101 ASP A HB2  1 
ATOM   1556 H HB3  . ASP A 1 115 ? 23.34386  -1.57441  25.70059 1.000 34.80743  ? 101 ASP A HB3  1 
ATOM   1557 N N    . GLY A 1 116 ? 22.56899  -0.64855  28.12339 1.000 36.58626  ? 102 GLY A N    1 
ATOM   1558 C CA   . GLY A 1 116 ? 21.50308  -0.01362  28.86957 1.000 34.91986  ? 102 GLY A CA   1 
ATOM   1559 C C    . GLY A 1 116 ? 20.14104  -0.23744  28.24355 1.000 29.67236  ? 102 GLY A C    1 
ATOM   1560 O O    . GLY A 1 116 ? 19.94740  -1.09309  27.38004 1.000 28.94438  ? 102 GLY A O    1 
ATOM   1561 H H    . GLY A 1 116 ? 23.02481  -0.10326  27.63915 1.000 43.95946  ? 102 GLY A H    1 
ATOM   1562 H HA2  . GLY A 1 116 ? 21.48648  -0.37072  29.77129 1.000 41.95977  ? 102 GLY A HA2  1 
ATOM   1563 H HA3  . GLY A 1 116 ? 21.66613  0.94168   28.91118 1.000 41.95977  ? 102 GLY A HA3  1 
ATOM   1564 N N    . ASN A 1 117 ? 19.17586  0.56362   28.69618 1.000 30.12434  ? 103 ASN A N    1 
ATOM   1565 C CA   . ASN A 1 117 ? 17.80457  0.44466   28.22396 1.000 33.01016  ? 103 ASN A CA   1 
ATOM   1566 C C    . ASN A 1 117 ? 17.14776  1.81565   28.19925 1.000 28.38231  ? 103 ASN A C    1 
ATOM   1567 O O    . ASN A 1 117 ? 17.41587  2.65574   29.06276 1.000 30.72153  ? 103 ASN A O    1 
ATOM   1568 C CB   . ASN A 1 117 ? 16.98492  -0.50079  29.11307 1.000 31.34559  ? 103 ASN A CB   1 
ATOM   1569 C CG   . ASN A 1 117 ? 16.76119  0.05660   30.51315 1.000 35.04388  ? 103 ASN A CG   1 
ATOM   1570 O OD1  . ASN A 1 117 ? 15.90845  0.92077   30.72248 1.000 33.49351  ? 103 ASN A OD1  1 
ATOM   1571 N ND2  . ASN A 1 117 ? 17.52265  -0.44518  31.47931 1.000 32.53044  ? 103 ASN A ND2  1 
ATOM   1572 H H    . ASN A 1 117 ? 19.29441  1.18480   29.27900 1.000 36.20515  ? 103 ASN A H    1 
ATOM   1573 H HA   . ASN A 1 117 ? 17.81515  0.09679   27.31854 1.000 39.66813  ? 103 ASN A HA   1 
ATOM   1574 H HB2  . ASN A 1 117 ? 16.11682  -0.64553  28.70519 1.000 37.67065  ? 103 ASN A HB2  1 
ATOM   1575 H HB3  . ASN A 1 117 ? 17.45661  -1.34417  29.19741 1.000 37.67065  ? 103 ASN A HB3  1 
ATOM   1576 H HD21 . ASN A 1 117 ? 17.43420  -0.16298  32.28686 1.000 39.09247  ? 103 ASN A HD21 1 
ATOM   1577 H HD22 . ASN A 1 117 ? 18.10399  -1.05219  31.29718 1.000 39.09247  ? 103 ASN A HD22 1 
ATOM   1578 N N    . TYR A 1 118 ? 16.28488  2.03040   27.20989 1.000 27.51339  ? 104 TYR A N    1 
ATOM   1579 C CA   . TYR A 1 118 ? 15.44400  3.21559   27.15182 1.000 27.51392  ? 104 TYR A CA   1 
ATOM   1580 C C    . TYR A 1 118 ? 14.07786  2.91339   27.75250 1.000 28.07933  ? 104 TYR A C    1 
ATOM   1581 O O    . TYR A 1 118 ? 13.52750  1.82590   27.55487 1.000 28.67020  ? 104 TYR A O    1 
ATOM   1582 C CB   . TYR A 1 118 ? 15.23773  3.69664   25.71374 1.000 25.97941  ? 104 TYR A CB   1 
ATOM   1583 C CG   . TYR A 1 118 ? 16.46609  4.18804   24.97983 1.000 25.45195  ? 104 TYR A CG   1 
ATOM   1584 C CD1  . TYR A 1 118 ? 17.57807  4.66201   25.66089 1.000 25.97119  ? 104 TYR A CD1  1 
ATOM   1585 C CD2  . TYR A 1 118 ? 16.50009  4.18792   23.59029 1.000 26.44698  ? 104 TYR A CD2  1 
ATOM   1586 C CE1  . TYR A 1 118 ? 18.69491  5.11454   24.97537 1.000 28.08080  ? 104 TYR A CE1  1 
ATOM   1587 C CE2  . TYR A 1 118 ? 17.60530  4.63519   22.89914 1.000 23.32303  ? 104 TYR A CE2  1 
ATOM   1588 C CZ   . TYR A 1 118 ? 18.69964  5.09814   23.59085 1.000 28.36221  ? 104 TYR A CZ   1 
ATOM   1589 O OH   . TYR A 1 118 ? 19.79345  5.54215   22.88177 1.000 24.35606  ? 104 TYR A OH   1 
ATOM   1590 H H    . TYR A 1 118 ? 16.16840  1.49195   26.54951 1.000 33.07201  ? 104 TYR A H    1 
ATOM   1591 H HA   . TYR A 1 118 ? 15.87791  3.92077   27.65714 1.000 33.07265  ? 104 TYR A HA   1 
ATOM   1592 H HB2  . TYR A 1 118 ? 14.87604  2.95845   25.19881 1.000 31.23123  ? 104 TYR A HB2  1 
ATOM   1593 H HB3  . TYR A 1 118 ? 14.60448  4.43122   25.73042 1.000 31.23123  ? 104 TYR A HB3  1 
ATOM   1594 H HD1  . TYR A 1 118 ? 17.57418  4.67637   26.59078 1.000 31.22137  ? 104 TYR A HD1  1 
ATOM   1595 H HD2  . TYR A 1 118 ? 15.76136  3.87948   23.11696 1.000 31.79232  ? 104 TYR A HD2  1 
ATOM   1596 H HE1  . TYR A 1 118 ? 19.43598  5.42703   25.44233 1.000 33.75290  ? 104 TYR A HE1  1 
ATOM   1597 H HE2  . TYR A 1 118 ? 17.61088  4.62394   21.96922 1.000 28.04358  ? 104 TYR A HE2  1 
ATOM   1598 H HH   . TYR A 1 118 ? 19.67606  5.41075   22.06045 1.000 29.28321  ? 104 TYR A HH   1 
ATOM   1599 N N    . LYS A 1 119 ? 13.52287  3.88895   28.46279 1.000 25.98747  ? 105 LYS A N    1 
ATOM   1600 C CA   . LYS A 1 119 ? 12.12236  3.86879   28.86724 1.000 32.34909  ? 105 LYS A CA   1 
ATOM   1601 C C    . LYS A 1 119 ? 11.48241  5.15351   28.36434 1.000 28.66390  ? 105 LYS A C    1 
ATOM   1602 O O    . LYS A 1 119 ? 11.89428  6.24878   28.75931 1.000 31.45000  ? 105 LYS A O    1 
ATOM   1603 C CB   . LYS A 1 119 ? 11.97626  3.73215   30.38428 1.000 29.63089  ? 105 LYS A CB   1 
ATOM   1604 C CG   . LYS A 1 119 ? 12.23978  2.32036   30.89075 1.000 40.19822  ? 105 LYS A CG   1 
ATOM   1605 C CD   . LYS A 1 119 ? 11.74719  2.12517   32.31532 1.000 44.74960  ? 105 LYS A CD   1 
ATOM   1606 C CE   . LYS A 1 119 ? 11.54444  0.64731   32.62933 1.000 46.86286  ? 105 LYS A CE   1 
ATOM   1607 N NZ   . LYS A 1 119 ? 11.07183  0.42792   34.02635 1.000 66.57737  ? 105 LYS A NZ   1 
ATOM   1608 H H    . LYS A 1 119 ? 13.94720  4.58839   28.72798 1.000 31.24091  ? 105 LYS A H    1 
ATOM   1609 H HA   . LYS A 1 119 ? 11.66830  3.11113   28.46639 1.000 38.87484  ? 105 LYS A HA   1 
ATOM   1610 H HB2  . LYS A 1 119 ? 12.61040  4.32646   30.81504 1.000 35.61300  ? 105 LYS A HB2  1 
ATOM   1611 H HB3  . LYS A 1 119 ? 11.07117  3.97461   30.63511 1.000 35.61300  ? 105 LYS A HB3  1 
ATOM   1612 H HG2  . LYS A 1 119 ? 11.77809  1.68533   30.32112 1.000 48.29381  ? 105 LYS A HG2  1 
ATOM   1613 H HG3  . LYS A 1 119 ? 13.19421  2.14806   30.87419 1.000 48.29381  ? 105 LYS A HG3  1 
ATOM   1614 H HD2  . LYS A 1 119 ? 12.40201  2.48302   32.93504 1.000 53.75546  ? 105 LYS A HD2  1 
ATOM   1615 H HD3  . LYS A 1 119 ? 10.89887  2.58166   32.42880 1.000 53.75546  ? 105 LYS A HD3  1 
ATOM   1616 H HE2  . LYS A 1 119 ? 10.88000  0.28151   32.02468 1.000 56.29137  ? 105 LYS A HE2  1 
ATOM   1617 H HE3  . LYS A 1 119 ? 12.38703  0.17970   32.51853 1.000 56.29137  ? 105 LYS A HE3  1 
ATOM   1618 H HZ1  . LYS A 1 119 ? 11.67544  0.73521   34.60369 1.000 79.94878  ? 105 LYS A HZ1  1 
ATOM   1619 H HZ2  . LYS A 1 119 ? 10.30238  0.85536   34.15805 1.000 79.94878  ? 105 LYS A HZ2  1 
ATOM   1620 H HZ3  . LYS A 1 119 ? 10.94821  -0.44118  34.17292 1.000 79.94878  ? 105 LYS A HZ3  1 
ATOM   1621 N N    . THR A 1 120 ? 10.49421  5.02182   27.48439 1.000 29.26251  ? 106 THR A N    1 
ATOM   1622 C CA   . THR A 1 120 ? 9.90202   6.16255   26.80215 1.000 29.15082  ? 106 THR A CA   1 
ATOM   1623 C C    . THR A 1 120 ? 8.41618   6.26192   27.11339 1.000 29.39721  ? 106 THR A C    1 
ATOM   1624 O O    . THR A 1 120 ? 7.71926   5.24767   27.21173 1.000 26.29508  ? 106 THR A O    1 
ATOM   1625 C CB   . THR A 1 120 ? 10.09646  6.06162   25.28359 1.000 25.45168  ? 106 THR A CB   1 
ATOM   1626 O OG1  . THR A 1 120 ? 9.38612   4.92127   24.78251 1.000 23.38672  ? 106 THR A OG1  1 
ATOM   1627 C CG2  . THR A 1 120 ? 11.56966  5.92960   24.94143 1.000 21.85390  ? 106 THR A CG2  1 
ATOM   1628 H H    . THR A 1 120 ? 10.14551  4.26726   27.26383 1.000 35.17095  ? 106 THR A H    1 
ATOM   1629 H HA   . THR A 1 120 ? 10.33028  6.97194   27.12212 1.000 35.03692  ? 106 THR A HA   1 
ATOM   1630 H HB   . THR A 1 120 ? 9.75633   6.86522   24.85999 1.000 30.59796  ? 106 THR A HB   1 
ATOM   1631 H HG1  . THR A 1 120 ? 9.53275   4.25396   25.27118 1.000 28.12000  ? 106 THR A HG1  1 
ATOM   1632 H HG21 . THR A 1 120 ? 11.92125  5.10098   25.30291 1.000 26.28062  ? 106 THR A HG21 1 
ATOM   1633 H HG22 . THR A 1 120 ? 11.68781  5.92823   23.97865 1.000 26.28062  ? 106 THR A HG22 1 
ATOM   1634 H HG23 . THR A 1 120 ? 12.06572  6.67305   25.31841 1.000 26.28062  ? 106 THR A HG23 1 
ATOM   1635 N N    . ARG A 1 121 ? 7.94371   7.49446   27.27321 1.000 29.48175  ? 107 ARG A N    1 
ATOM   1636 C CA   . ARG A 1 121 ? 6.52302   7.79781   27.35275 1.000 31.01958  ? 107 ARG A CA   1 
ATOM   1637 C C    . ARG A 1 121 ? 6.22449   8.88271   26.33069 1.000 29.72336  ? 107 ARG A C    1 
ATOM   1638 O O    . ARG A 1 121 ? 6.89478   9.92068   26.31198 1.000 30.12044  ? 107 ARG A O    1 
ATOM   1639 C CB   . ARG A 1 121 ? 6.11885   8.26294   28.75307 1.000 26.01029  ? 107 ARG A CB   1 
ATOM   1640 C CG   . ARG A 1 121 ? 4.61492   8.29035   28.97490 1.000 34.47937  ? 107 ARG A CG   1 
ATOM   1641 C CD   . ARG A 1 121 ? 4.25018   9.01007   30.25976 1.000 33.44566  ? 107 ARG A CD   1 
ATOM   1642 N NE   . ARG A 1 121 ? 2.89504   8.69415   30.69535 1.000 41.16715  ? 107 ARG A NE   1 
ATOM   1643 C CZ   . ARG A 1 121 ? 1.80126   9.32173   30.28257 1.000 46.86536  ? 107 ARG A CZ   1 
ATOM   1644 N NH1  . ARG A 1 121 ? 1.85858   10.31243  29.40657 1.000 34.35688  ? 107 ARG A NH1  1 
ATOM   1645 N NH2  . ARG A 1 121 ? 0.61859   8.94530   30.76207 1.000 51.62795  ? 107 ARG A NH2  1 
ATOM   1646 H H    . ARG A 1 121 ? 8.44357   8.19109   27.33990 1.000 35.43404  ? 107 ARG A H    1 
ATOM   1647 H HA   . ARG A 1 121 ? 6.00130   7.00623   27.14756 1.000 37.27944  ? 107 ARG A HA   1 
ATOM   1648 H HB2  . ARG A 1 121 ? 6.50428   7.65841   29.40643 1.000 31.26829  ? 107 ARG A HB2  1 
ATOM   1649 H HB3  . ARG A 1 121 ? 6.45596   9.16162   28.89317 1.000 31.26829  ? 107 ARG A HB3  1 
ATOM   1650 H HG2  . ARG A 1 121 ? 4.19034   8.75359   28.23595 1.000 41.43118  ? 107 ARG A HG2  1 
ATOM   1651 H HG3  . ARG A 1 121 ? 4.28262   7.38079   29.03113 1.000 41.43118  ? 107 ARG A HG3  1 
ATOM   1652 H HD2  . ARG A 1 121 ? 4.86431   8.74234   30.96124 1.000 40.19073  ? 107 ARG A HD2  1 
ATOM   1653 H HD3  . ARG A 1 121 ? 4.30714   9.96776   30.11665 1.000 40.19073  ? 107 ARG A HD3  1 
ATOM   1654 H HE   . ARG A 1 121 ? 2.79751   8.05405   31.26136 1.000 49.45652  ? 107 ARG A HE   1 
ATOM   1655 H HH11 . ARG A 1 121 ? 2.61798   10.56372  29.09069 1.000 41.28419  ? 107 ARG A HH11 1 
ATOM   1656 H HH12 . ARG A 1 121 ? 1.13643   10.70481  29.15331 1.000 41.28419  ? 107 ARG A HH12 1 
ATOM   1657 H HH21 . ARG A 1 121 ? 0.57029   8.30295   31.33185 1.000 62.00948  ? 107 ARG A HH21 1 
ATOM   1658 H HH22 . ARG A 1 121 ? -0.09754  9.34435   30.50221 1.000 62.00948  ? 107 ARG A HH22 1 
ATOM   1659 N N    . ALA A 1 122 ? 5.23234   8.64268   25.48046 1.000 24.31025  ? 108 ALA A N    1 
ATOM   1660 C CA   . ALA A 1 122 ? 4.87663   9.58320   24.43214 1.000 28.86098  ? 108 ALA A CA   1 
ATOM   1661 C C    . ALA A 1 122 ? 3.36889   9.76971   24.38779 1.000 31.86346  ? 108 ALA A C    1 
ATOM   1662 O O    . ALA A 1 122 ? 2.60088   8.87597   24.75524 1.000 29.71667  ? 108 ALA A O    1 
ATOM   1663 C CB   . ALA A 1 122 ? 5.38049   9.11421   23.05984 1.000 29.01804  ? 108 ALA A CB   1 
ATOM   1664 H H    . ALA A 1 122 ? 4.74678   7.93299   25.49326 1.000 29.22824  ? 108 ALA A H    1 
ATOM   1665 H HA   . ALA A 1 122 ? 5.27846   10.44405  24.62802 1.000 34.68912  ? 108 ALA A HA   1 
ATOM   1666 H HB1  . ALA A 1 122 ? 4.97961   8.25553   22.85281 1.000 34.87759  ? 108 ALA A HB1  1 
ATOM   1667 H HB2  . ALA A 1 122 ? 5.12646   9.76800   22.38983 1.000 34.87759  ? 108 ALA A HB2  1 
ATOM   1668 H HB3  . ALA A 1 122 ? 6.34633   9.02968   23.09005 1.000 34.87759  ? 108 ALA A HB3  1 
ATOM   1669 N N    . GLU A 1 123 ? 2.95849   10.95463  23.94466 1.000 25.85340  ? 109 GLU A N    1 
ATOM   1670 C CA   . GLU A 1 123 ? 1.56550   11.25924  23.64677 1.000 31.27881  ? 109 GLU A CA   1 
ATOM   1671 C C    . GLU A 1 123 ? 1.46605   11.56901  22.16059 1.000 28.34669  ? 109 GLU A C    1 
ATOM   1672 O O    . GLU A 1 123 ? 2.12304   12.49477  21.67210 1.000 30.63958  ? 109 GLU A O    1 
ATOM   1673 C CB   . GLU A 1 123 ? 1.06021   12.43685  24.48311 1.000 29.05989  ? 109 GLU A CB   1 
ATOM   1674 C CG   . GLU A 1 123 ? 1.10480   12.19462  25.98007 1.000 32.91994  ? 109 GLU A CG   1 
ATOM   1675 C CD   . GLU A 1 123 ? 0.46994   13.32208  26.77410 1.000 48.95243  ? 109 GLU A CD   1 
ATOM   1676 O OE1  . GLU A 1 123 ? -0.41720  14.01104  26.22671 1.000 46.77036  ? 109 GLU A OE1  1 
ATOM   1677 O OE2  . GLU A 1 123 ? 0.85999   13.52127  27.94503 1.000 50.30178  ? 109 GLU A OE2  1 
ATOM   1678 H H    . GLU A 1 123 ? 3.48707   11.61844  23.80479 1.000 31.08002  ? 109 GLU A H    1 
ATOM   1679 H HA   . GLU A 1 123 ? 1.00701   10.49252  23.84956 1.000 37.59051  ? 109 GLU A HA   1 
ATOM   1680 H HB2  . GLU A 1 123 ? 1.61124   13.21218  24.29308 1.000 34.92781  ? 109 GLU A HB2  1 
ATOM   1681 H HB3  . GLU A 1 123 ? 0.13851   12.61744  24.24071 1.000 34.92781  ? 109 GLU A HB3  1 
ATOM   1682 H HG2  . GLU A 1 123 ? 0.62420   11.37680  26.18279 1.000 39.55987  ? 109 GLU A HG2  1 
ATOM   1683 H HG3  . GLU A 1 123 ? 2.02996   12.11387  26.26017 1.000 39.55987  ? 109 GLU A HG3  1 
ATOM   1684 N N    . VAL A 1 124 ? 0.66282   10.78757  21.44666 1.000 31.33437  ? 110 VAL A N    1 
ATOM   1685 C CA   . VAL A 1 124 ? 0.46296   10.94111  20.01016 1.000 28.92597  ? 110 VAL A CA   1 
ATOM   1686 C C    . VAL A 1 124 ? -0.97920  11.38367  19.80610 1.000 32.79487  ? 110 VAL A C    1 
ATOM   1687 O O    . VAL A 1 124 ? -1.91417  10.60244  20.02262 1.000 30.04375  ? 110 VAL A O    1 
ATOM   1688 C CB   . VAL A 1 124 ? 0.76230   9.64126   19.25070 1.000 34.11642  ? 110 VAL A CB   1 
ATOM   1689 C CG1  . VAL A 1 124 ? 0.61456   9.85322   17.75156 1.000 36.79928  ? 110 VAL A CG1  1 
ATOM   1690 C CG2  . VAL A 1 124 ? 2.16233   9.13380   19.58725 1.000 29.98346  ? 110 VAL A CG2  1 
ATOM   1691 H H    . VAL A 1 124 ? 0.20803   10.14017  21.78376 1.000 37.65718  ? 110 VAL A H    1 
ATOM   1692 H HA   . VAL A 1 124 ? 1.05155   11.63300  19.66992 1.000 34.76710  ? 110 VAL A HA   1 
ATOM   1693 H HB   . VAL A 1 124 ? 0.12298   8.96500   19.52431 1.000 40.99565  ? 110 VAL A HB   1 
ATOM   1694 H HG11 . VAL A 1 124 ? 0.49766   10.80010  17.57650 1.000 44.21507  ? 110 VAL A HG11 1 
ATOM   1695 H HG12 . VAL A 1 124 ? 1.41399   9.53082   17.30673 1.000 44.21507  ? 110 VAL A HG12 1 
ATOM   1696 H HG13 . VAL A 1 124 ? -0.15999  9.36074   17.43780 1.000 44.21507  ? 110 VAL A HG13 1 
ATOM   1697 H HG21 . VAL A 1 124 ? 2.30885   8.28816   19.13524 1.000 36.03609  ? 110 VAL A HG21 1 
ATOM   1698 H HG22 . VAL A 1 124 ? 2.81501   9.78612   19.28828 1.000 36.03609  ? 110 VAL A HG22 1 
ATOM   1699 H HG23 . VAL A 1 124 ? 2.23191   9.01223   20.54708 1.000 36.03609  ? 110 VAL A HG23 1 
ATOM   1700 N N    . LYS A 1 125 ? -1.16466  12.63166  19.38440 1.000 27.56367  ? 111 LYS A N    1 
ATOM   1701 C CA   . LYS A 1 125 ? -2.49313  13.22466  19.32974 1.000 34.41983  ? 111 LYS A CA   1 
ATOM   1702 C C    . LYS A 1 125 ? -2.49602  14.35091  18.30740 1.000 31.42071  ? 111 LYS A C    1 
ATOM   1703 O O    . LYS A 1 125 ? -1.44644  14.80676  17.84781 1.000 32.11300  ? 111 LYS A O    1 
ATOM   1704 C CB   . LYS A 1 125 ? -2.91703  13.75015  20.70436 1.000 31.35138  ? 111 LYS A CB   1 
ATOM   1705 C CG   . LYS A 1 125 ? -2.00419  14.84318  21.23732 1.000 34.62991  ? 111 LYS A CG   1 
ATOM   1706 C CD   . LYS A 1 125 ? -2.32178  15.18866  22.67901 1.000 42.26851  ? 111 LYS A CD   1 
ATOM   1707 C CE   . LYS A 1 125 ? -1.39097  16.27113  23.20286 1.000 42.88275  ? 111 LYS A CE   1 
ATOM   1708 N NZ   . LYS A 1 125 ? -1.62654  16.56282  24.64437 1.000 46.63727  ? 111 LYS A NZ   1 
ATOM   1709 H H    . LYS A 1 125 ? -0.53411  13.15539  19.12420 1.000 33.13234  ? 111 LYS A H    1 
ATOM   1710 H HA   . LYS A 1 125 ? -3.12506  12.54921  19.03760 1.000 41.35974  ? 111 LYS A HA   1 
ATOM   1711 H HB2  . LYS A 1 125 ? -3.81291  14.11600  20.63770 1.000 37.67760  ? 111 LYS A HB2  1 
ATOM   1712 H HB3  . LYS A 1 125 ? -2.90479  13.01601  21.33824 1.000 37.67760  ? 111 LYS A HB3  1 
ATOM   1713 H HG2  . LYS A 1 125 ? -1.08347  14.54113  21.19326 1.000 41.61183  ? 111 LYS A HG2  1 
ATOM   1714 H HG3  . LYS A 1 125 ? -2.11669  15.64383  20.70141 1.000 41.61183  ? 111 LYS A HG3  1 
ATOM   1715 H HD2  . LYS A 1 125 ? -3.23375  15.51357  22.73937 1.000 50.77815  ? 111 LYS A HD2  1 
ATOM   1716 H HD3  . LYS A 1 125 ? -2.21385  14.39854  23.23124 1.000 50.77815  ? 111 LYS A HD3  1 
ATOM   1717 H HE2  . LYS A 1 125 ? -0.47186  15.97878  23.09958 1.000 51.51524  ? 111 LYS A HE2  1 
ATOM   1718 H HE3  . LYS A 1 125 ? -1.53762  17.08813  22.70095 1.000 51.51524  ? 111 LYS A HE3  1 
ATOM   1719 H HZ1  . LYS A 1 125 ? -2.49213  16.71274  24.78710 1.000 56.02067  ? 111 LYS A HZ1  1 
ATOM   1720 H HZ2  . LYS A 1 125 ? -1.36741  15.87133  25.14116 1.000 56.02067  ? 111 LYS A HZ2  1 
ATOM   1721 H HZ3  . LYS A 1 125 ? -1.16451  17.28321  24.88863 1.000 56.02067  ? 111 LYS A HZ3  1 
ATOM   1722 N N    . PHE A 1 126 ? -3.69975  14.80278  17.96814 1.000 30.03983  ? 112 PHE A N    1 
ATOM   1723 C CA   . PHE A 1 126 ? -3.88193  15.92745  17.06274 1.000 32.95444  ? 112 PHE A CA   1 
ATOM   1724 C C    . PHE A 1 126 ? -3.95027  17.22564  17.85882 1.000 36.79374  ? 112 PHE A C    1 
ATOM   1725 O O    . PHE A 1 126 ? -4.76111  17.35253  18.78282 1.000 34.36056  ? 112 PHE A O    1 
ATOM   1726 C CB   . PHE A 1 126 ? -5.15867  15.75914  16.23717 1.000 31.75640  ? 112 PHE A CB   1 
ATOM   1727 C CG   . PHE A 1 126 ? -4.96104  15.01223  14.94754 1.000 34.01901  ? 112 PHE A CG   1 
ATOM   1728 C CD1  . PHE A 1 126 ? -5.02503  13.62916  14.91205 1.000 30.45011  ? 112 PHE A CD1  1 
ATOM   1729 C CD2  . PHE A 1 126 ? -4.72664  15.69765  13.76661 1.000 31.71888  ? 112 PHE A CD2  1 
ATOM   1730 C CE1  . PHE A 1 126 ? -4.84900  12.94268  13.72361 1.000 31.32075  ? 112 PHE A CE1  1 
ATOM   1731 C CE2  . PHE A 1 126 ? -4.54934  15.01857  12.57709 1.000 31.77159  ? 112 PHE A CE2  1 
ATOM   1732 C CZ   . PHE A 1 126 ? -4.61311  13.63886  12.55453 1.000 34.95127  ? 112 PHE A CZ   1 
ATOM   1733 H H    . PHE A 1 126 ? -4.43773  14.46737  18.25532 1.000 36.10374  ? 112 PHE A H    1 
ATOM   1734 H HA   . PHE A 1 126 ? -3.12484  15.97270  16.45804 1.000 39.60127  ? 112 PHE A HA   1 
ATOM   1735 H HB2  . PHE A 1 126 ? -5.80774  15.26859  16.76535 1.000 38.16362  ? 112 PHE A HB2  1 
ATOM   1736 H HB3  . PHE A 1 126 ? -5.50531  16.63828  16.01842 1.000 38.16362  ? 112 PHE A HB3  1 
ATOM   1737 H HD1  . PHE A 1 126 ? -5.18821  13.15635  15.69609 1.000 36.59607  ? 112 PHE A HD1  1 
ATOM   1738 H HD2  . PHE A 1 126 ? -4.68819  16.62682  13.77495 1.000 38.11860  ? 112 PHE A HD2  1 
ATOM   1739 H HE1  . PHE A 1 126 ? -4.88949  12.01363  13.71216 1.000 37.64084  ? 112 PHE A HE1  1 
ATOM   1740 H HE2  . PHE A 1 126 ? -4.38716  15.48983  11.79191 1.000 38.18185  ? 112 PHE A HE2  1 
ATOM   1741 H HZ   . PHE A 1 126 ? -4.49746  13.17993  11.75396 1.000 41.99746  ? 112 PHE A HZ   1 
ATOM   1742 N N    A GLU A 1 127 ? -3.08928  18.17792  17.51560 0.459 36.56935  ? 113 GLU A N    1 
ATOM   1743 N N    B GLU A 1 127 ? -3.09525  18.17840  17.49774 0.541 36.43324  ? 113 GLU A N    1 
ATOM   1744 C CA   A GLU A 1 127 ? -3.16439  19.54419  18.03111 0.459 35.62553  ? 113 GLU A CA   1 
ATOM   1745 C CA   B GLU A 1 127 ? -3.13401  19.54482  18.01515 0.541 36.98242  ? 113 GLU A CA   1 
ATOM   1746 C C    A GLU A 1 127 ? -3.48665  20.43278  16.83261 0.459 36.56726  ? 113 GLU A C    1 
ATOM   1747 C C    B GLU A 1 127 ? -3.48211  20.43995  16.82676 0.541 36.52856  ? 113 GLU A C    1 
ATOM   1748 O O    A GLU A 1 127 ? -2.59565  20.90544  16.12519 0.459 36.55602  ? 113 GLU A O    1 
ATOM   1749 O O    B GLU A 1 127 ? -2.60129  20.92652  16.11712 0.541 36.58336  ? 113 GLU A O    1 
ATOM   1750 C CB   A GLU A 1 127 ? -1.87303  19.96268  18.72897 0.459 36.09364  ? 113 GLU A CB   1 
ATOM   1751 C CB   B GLU A 1 127 ? -1.80266  19.94128  18.65171 0.541 35.77718  ? 113 GLU A CB   1 
ATOM   1752 C CG   A GLU A 1 127 ? -1.77013  19.48906  20.17931 0.459 37.50051  ? 113 GLU A CG   1 
ATOM   1753 C CG   B GLU A 1 127 ? -1.38335  19.06657  19.82544 0.541 38.22536  ? 113 GLU A CG   1 
ATOM   1754 C CD   A GLU A 1 127 ? -2.85136  20.07451  21.07598 0.459 35.55782  ? 113 GLU A CD   1 
ATOM   1755 C CD   B GLU A 1 127 ? -0.06751  19.50604  20.44277 0.541 36.98384  ? 113 GLU A CD   1 
ATOM   1756 O OE1  A GLU A 1 127 ? -3.56420  21.00074  20.63383 0.459 37.59149  ? 113 GLU A OE1  1 
ATOM   1757 O OE1  B GLU A 1 127 ? 0.52402   20.48969  19.95064 0.541 38.11520  ? 113 GLU A OE1  1 
ATOM   1758 O OE2  A GLU A 1 127 ? -2.98905  19.60721  22.22674 0.459 37.68935  ? 113 GLU A OE2  1 
ATOM   1759 O OE2  B GLU A 1 127 ? 0.37663   18.86648  21.41932 0.541 36.55327  ? 113 GLU A OE2  1 
ATOM   1760 H H    A GLU A 1 127 ? -2.43513  18.05453  16.97110 0.459 43.93916  ? 113 GLU A H    1 
ATOM   1761 H H    B GLU A 1 127 ? -2.45928  18.05277  16.93263 0.541 43.77583  ? 113 GLU A H    1 
ATOM   1762 H HA   A GLU A 1 127 ? -3.87526  19.61236  18.68755 0.459 42.80657  ? 113 GLU A HA   1 
ATOM   1763 H HA   B GLU A 1 127 ? -3.81931  19.62379  18.69708 0.541 44.43484  ? 113 GLU A HA   1 
ATOM   1764 H HB2  A GLU A 1 127 ? -1.12142  19.58960  18.24235 0.459 43.36831  ? 113 GLU A HB2  1 
ATOM   1765 H HB2  B GLU A 1 127 ? -1.10744  19.88166  17.97790 0.541 42.98856  ? 113 GLU A HB2  1 
ATOM   1766 H HB3  A GLU A 1 127 ? -1.81974  20.93122  18.73002 0.459 43.36831  ? 113 GLU A HB3  1 
ATOM   1767 H HB3  B GLU A 1 127 ? -1.87361  20.85291  18.97543 0.541 42.98856  ? 113 GLU A HB3  1 
ATOM   1768 H HG2  A GLU A 1 127 ? -1.85431  18.52298  20.20181 0.459 45.05655  ? 113 GLU A HG2  1 
ATOM   1769 H HG2  B GLU A 1 127 ? -2.06670  19.11021  20.51249 0.541 45.92637  ? 113 GLU A HG2  1 
ATOM   1770 H HG3  A GLU A 1 127 ? -0.90882  19.75545  20.53721 0.459 45.05655  ? 113 GLU A HG3  1 
ATOM   1771 H HG3  B GLU A 1 127 ? -1.28015  18.15247  19.51776 0.541 45.92637  ? 113 GLU A HG3  1 
ATOM   1772 N N    . GLY A 1 128 ? -4.77663  20.64947  16.60837 1.000 37.56067  ? 114 GLY A N    1 
ATOM   1773 C CA   . GLY A 1 128 ? -5.23145  21.33852  15.41913 1.000 31.69485  ? 114 GLY A CA   1 
ATOM   1774 C C    . GLY A 1 128 ? -5.35196  20.35738  14.27291 1.000 40.65000  ? 114 GLY A C    1 
ATOM   1775 O O    . GLY A 1 128 ? -6.04005  19.33967  14.39157 1.000 42.08856  ? 114 GLY A O    1 
ATOM   1776 H H    . GLY A 1 128 ? -5.40720  20.40007  17.13732 1.000 45.12874  ? 114 GLY A H    1 
ATOM   1777 H HA2  . GLY A 1 128 ? -6.09774  21.74333  15.58213 1.000 38.08976  ? 114 GLY A HA2  1 
ATOM   1778 H HA3  . GLY A 1 128 ? -4.59899  22.03288  15.17670 1.000 38.08976  ? 114 GLY A HA3  1 
ATOM   1779 N N    . ASP A 1 129 ? -4.67877  20.64913  13.16220 1.000 41.91045  ? 115 ASP A N    1 
ATOM   1780 C CA   . ASP A 1 129 ? -4.59471  19.73766  12.03071 1.000 41.73818  ? 115 ASP A CA   1 
ATOM   1781 C C    . ASP A 1 129 ? -3.24511  19.03764  11.94978 1.000 36.57653  ? 115 ASP A C    1 
ATOM   1782 O O    . ASP A 1 129 ? -2.94857  18.40020  10.93413 1.000 35.14977  ? 115 ASP A O    1 
ATOM   1783 C CB   . ASP A 1 129 ? -4.87093  20.48723  10.72573 1.000 42.09612  ? 115 ASP A CB   1 
ATOM   1784 C CG   . ASP A 1 129 ? -6.32946  20.86943  10.57315 1.000 52.81097  ? 115 ASP A CG   1 
ATOM   1785 O OD1  . ASP A 1 129 ? -7.19684  20.10773  11.05284 1.000 54.39805  ? 115 ASP A OD1  1 
ATOM   1786 O OD2  . ASP A 1 129 ? -6.60938  21.92776  9.97279  1.000 59.86638  ? 115 ASP A OD2  1 
ATOM   1787 H H    . ASP A 1 129 ? -4.25366  21.38671  13.04032 1.000 50.34848  ? 115 ASP A H    1 
ATOM   1788 H HA   . ASP A 1 129 ? -5.27910  19.05779  12.13209 1.000 50.14176  ? 115 ASP A HA   1 
ATOM   1789 H HB2  . ASP A 1 129 ? -4.34336  21.30106  10.70988 1.000 50.57128  ? 115 ASP A HB2  1 
ATOM   1790 H HB3  . ASP A 1 129 ? -4.62857  19.92011  9.97704  1.000 50.57128  ? 115 ASP A HB3  1 
ATOM   1791 N N    . THR A 1 130 ? -2.42597  19.14136  12.99275 1.000 33.81989  ? 116 THR A N    1 
ATOM   1792 C CA   . THR A 1 130 ? -1.09372  18.55550  13.01975 1.000 28.62908  ? 116 THR A CA   1 
ATOM   1793 C C    . THR A 1 130 ? -1.08012  17.36760  13.97011 1.000 32.02814  ? 116 THR A C    1 
ATOM   1794 O O    . THR A 1 130 ? -1.57054  17.46384  15.10070 1.000 33.98165  ? 116 THR A O    1 
ATOM   1795 C CB   . THR A 1 130 ? -0.04588  19.58430  13.45559 1.000 28.27612  ? 116 THR A CB   1 
ATOM   1796 O OG1  . THR A 1 130 ? -0.04776  20.68974  12.54649 1.000 30.43436  ? 116 THR A OG1  1 
ATOM   1797 C CG2  . THR A 1 130 ? 1.34467   18.96045  13.47773 1.000 32.53708  ? 116 THR A CG2  1 
ATOM   1798 H H    . THR A 1 130 ? -2.62796  19.55929  13.71672 1.000 40.63981  ? 116 THR A H    1 
ATOM   1799 H HA   . THR A 1 130 ? -0.86500  18.24258  12.13056 1.000 34.41084  ? 116 THR A HA   1 
ATOM   1800 H HB   . THR A 1 130 ? -0.25773  19.89667  14.34915 1.000 33.98728  ? 116 THR A HB   1 
ATOM   1801 H HG1  . THR A 1 130 ? 0.24036   20.44524  11.79629 1.000 36.57717  ? 116 THR A HG1  1 
ATOM   1802 H HG21 . THR A 1 130 ? 2.02032   19.65632  13.49030 1.000 39.10043  ? 116 THR A HG21 1 
ATOM   1803 H HG22 . THR A 1 130 ? 1.44763   18.40740  14.26795 1.000 39.10043  ? 116 THR A HG22 1 
ATOM   1804 H HG23 . THR A 1 130 ? 1.47405   18.41027  12.68940 1.000 39.10043  ? 116 THR A HG23 1 
ATOM   1805 N N    . LEU A 1 131 ? -0.52663  16.25163  13.50470 1.000 31.66447  ? 117 LEU A N    1 
ATOM   1806 C CA   . LEU A 1 131 ? -0.31566  15.08583  14.35236 1.000 25.30979  ? 117 LEU A CA   1 
ATOM   1807 C C    . LEU A 1 131 ? 0.98540   15.27638  15.12254 1.000 26.14308  ? 117 LEU A C    1 
ATOM   1808 O O    . LEU A 1 131 ? 2.05901   15.37861  14.52002 1.000 27.57494  ? 117 LEU A O    1 
ATOM   1809 C CB   . LEU A 1 131 ? -0.27600  13.81592  13.50458 1.000 29.70048  ? 117 LEU A CB   1 
ATOM   1810 C CG   . LEU A 1 131 ? -0.22449  12.46628  14.22624 1.000 26.38762  ? 117 LEU A CG   1 
ATOM   1811 C CD1  . LEU A 1 131 ? 1.12887   12.23094  14.88813 1.000 29.22015  ? 117 LEU A CD1  1 
ATOM   1812 C CD2  . LEU A 1 131 ? -1.34533  12.36944  15.25406 1.000 26.93512  ? 117 LEU A CD2  1 
ATOM   1813 H H    . LEU A 1 131 ? -0.26248  16.14466  12.69330 1.000 38.05330  ? 117 LEU A H    1 
ATOM   1814 H HA   . LEU A 1 131 ? -1.04362  14.99353  14.98676 1.000 30.42769  ? 117 LEU A HA   1 
ATOM   1815 H HB2  . LEU A 1 131 ? -1.07390  13.80576  12.95308 1.000 35.69651  ? 117 LEU A HB2  1 
ATOM   1816 H HB3  . LEU A 1 131 ? 0.51425   13.86147  12.94392 1.000 35.69651  ? 117 LEU A HB3  1 
ATOM   1817 H HG   . LEU A 1 131 ? -0.34752  11.76544  13.56702 1.000 31.72108  ? 117 LEU A HG   1 
ATOM   1818 H HD11 . LEU A 1 131 ? 1.11812   12.62084  15.77625 1.000 35.12012  ? 117 LEU A HD11 1 
ATOM   1819 H HD12 . LEU A 1 131 ? 1.28940   11.27619  14.94794 1.000 35.12012  ? 117 LEU A HD12 1 
ATOM   1820 H HD13 . LEU A 1 131 ? 1.81996   12.64958  14.35143 1.000 35.12012  ? 117 LEU A HD13 1 
ATOM   1821 H HD21 . LEU A 1 131 ? -1.16103  12.98444  15.98118 1.000 32.37808  ? 117 LEU A HD21 1 
ATOM   1822 H HD22 . LEU A 1 131 ? -2.18516  12.60268  14.82839 1.000 32.37808  ? 117 LEU A HD22 1 
ATOM   1823 H HD23 . LEU A 1 131 ? -1.38665  11.46101  15.59161 1.000 32.37808  ? 117 LEU A HD23 1 
ATOM   1824 N N    . VAL A 1 132 ? 0.89381   15.32221  16.44848 1.000 31.64056  ? 118 VAL A N    1 
ATOM   1825 C CA   . VAL A 1 132 ? 2.02327   15.65756  17.30766 1.000 34.43931  ? 118 VAL A CA   1 
ATOM   1826 C C    . VAL A 1 132 ? 2.44347   14.42367  18.09232 1.000 30.10711  ? 118 VAL A C    1 
ATOM   1827 O O    . VAL A 1 132 ? 1.59798   13.65343  18.56144 1.000 30.52361  ? 118 VAL A O    1 
ATOM   1828 C CB   . VAL A 1 132 ? 1.67043   16.81868  18.25748 1.000 34.78188  ? 118 VAL A CB   1 
ATOM   1829 C CG1  . VAL A 1 132 ? 2.88513   17.22959  19.07930 1.000 38.73595  ? 118 VAL A CG1  1 
ATOM   1830 C CG2  . VAL A 1 132 ? 1.13526   17.99840  17.46083 1.000 33.66499  ? 118 VAL A CG2  1 
ATOM   1831 H H    . VAL A 1 132 ? 0.16977   15.15878  16.88282 1.000 38.02461  ? 118 VAL A H    1 
ATOM   1832 H HA   . VAL A 1 132 ? 2.77301   15.92472  16.75321 1.000 41.38311  ? 118 VAL A HA   1 
ATOM   1833 H HB   . VAL A 1 132 ? 0.98110   16.52618  18.87407 1.000 41.79420  ? 118 VAL A HB   1 
ATOM   1834 H HG11 . VAL A 1 132 ? 2.61438   17.89315  19.73297 1.000 46.53908  ? 118 VAL A HG11 1 
ATOM   1835 H HG12 . VAL A 1 132 ? 3.24095   16.44762  19.52963 1.000 46.53908  ? 118 VAL A HG12 1 
ATOM   1836 H HG13 . VAL A 1 132 ? 3.55564   17.60362  18.48649 1.000 46.53908  ? 118 VAL A HG13 1 
ATOM   1837 H HG21 . VAL A 1 132 ? 1.02297   18.75629  18.05573 1.000 40.45393  ? 118 VAL A HG21 1 
ATOM   1838 H HG22 . VAL A 1 132 ? 1.76818   18.21916  16.75971 1.000 40.45393  ? 118 VAL A HG22 1 
ATOM   1839 H HG23 . VAL A 1 132 ? 0.28123   17.75468  17.07078 1.000 40.45393  ? 118 VAL A HG23 1 
ATOM   1840 N N    . ASN A 1 133 ? 3.75658   14.24545  18.23823 1.000 31.03872  ? 119 ASN A N    1 
ATOM   1841 C CA   . ASN A 1 133 ? 4.34148   13.15112  19.01286 1.000 27.84276  ? 119 ASN A CA   1 
ATOM   1842 C C    . ASN A 1 133 ? 5.28404   13.77068  20.04145 1.000 29.59075  ? 119 ASN A C    1 
ATOM   1843 O O    . ASN A 1 133 ? 6.42017   14.12504  19.71259 1.000 28.18850  ? 119 ASN A O    1 
ATOM   1844 C CB   . ASN A 1 133 ? 5.07600   12.16342  18.10930 1.000 24.92181  ? 119 ASN A CB   1 
ATOM   1845 C CG   . ASN A 1 133 ? 5.66593   10.99149  18.87874 1.000 24.99305  ? 119 ASN A CG   1 
ATOM   1846 O OD1  . ASN A 1 133 ? 5.22092   10.67037  19.97964 1.000 26.30799  ? 119 ASN A OD1  1 
ATOM   1847 N ND2  . ASN A 1 133 ? 6.67328   10.34837  18.29935 1.000 24.85502  ? 119 ASN A ND2  1 
ATOM   1848 H H    . ASN A 1 133 ? 4.34723   14.76219  17.88651 1.000 37.30240  ? 119 ASN A H    1 
ATOM   1849 H HA   . ASN A 1 133 ? 3.63972   12.67099  19.47967 1.000 33.46725  ? 119 ASN A HA   1 
ATOM   1850 H HB2  . ASN A 1 133 ? 4.45337   11.81000  17.45484 1.000 29.96211  ? 119 ASN A HB2  1 
ATOM   1851 H HB3  . ASN A 1 133 ? 5.80228   12.62444  17.66110 1.000 29.96211  ? 119 ASN A HB3  1 
ATOM   1852 H HD21 . ASN A 1 133 ? 7.04033   9.67880   18.69502 1.000 29.88197  ? 119 ASN A HD21 1 
ATOM   1853 H HD22 . ASN A 1 133 ? 6.95851   10.60152  17.52853 1.000 29.88197  ? 119 ASN A HD22 1 
ATOM   1854 N N    . ARG A 1 134 ? 4.80925   13.90461  21.27936 1.000 31.86453  ? 120 ARG A N    1 
ATOM   1855 C CA   . ARG A 1 134 ? 5.58537   14.47782  22.37483 1.000 35.01996  ? 120 ARG A CA   1 
ATOM   1856 C C    . ARG A 1 134 ? 6.13391   13.34917  23.23842 1.000 28.30305  ? 120 ARG A C    1 
ATOM   1857 O O    . ARG A 1 134 ? 5.36433   12.53987  23.76595 1.000 30.09945  ? 120 ARG A O    1 
ATOM   1858 C CB   . ARG A 1 134 ? 4.72313   15.42303  23.20930 1.000 34.63650  ? 120 ARG A CB   1 
ATOM   1859 C CG   . ARG A 1 134 ? 4.18285   16.59872  22.41839 1.000 47.16040  ? 120 ARG A CG   1 
ATOM   1860 C CD   . ARG A 1 134 ? 3.21138   17.43930  23.22512 1.000 49.47510  ? 120 ARG A CD   1 
ATOM   1861 N NE   . ARG A 1 134 ? 2.79677   18.62651  22.48654 1.000 43.39834  ? 120 ARG A NE   1 
ATOM   1862 C CZ   . ARG A 1 134 ? 3.51533   19.73714  22.39029 1.000 49.40076  ? 120 ARG A CZ   1 
ATOM   1863 N NH1  . ARG A 1 134 ? 4.69621   19.85040  22.97698 1.000 46.23813  ? 120 ARG A NH1  1 
ATOM   1864 N NH2  . ARG A 1 134 ? 3.03878   20.75897  21.68467 1.000 52.50931  ? 120 ARG A NH2  1 
ATOM   1865 H H    . ARG A 1 134 ? 4.01789   13.66349  21.51433 1.000 38.29338  ? 120 ARG A H    1 
ATOM   1866 H HA   . ARG A 1 134 ? 6.33341   14.98026  22.01581 1.000 42.07989  ? 120 ARG A HA   1 
ATOM   1867 H HB2  . ARG A 1 134 ? 3.96690   14.92841  23.56197 1.000 41.61975  ? 120 ARG A HB2  1 
ATOM   1868 H HB3  . ARG A 1 134 ? 5.25838   15.77472  23.93780 1.000 41.61975  ? 120 ARG A HB3  1 
ATOM   1869 H HG2  . ARG A 1 134 ? 4.92131   17.16708  22.14903 1.000 56.64842  ? 120 ARG A HG2  1 
ATOM   1870 H HG3  . ARG A 1 134 ? 3.71623   16.26758  21.63512 1.000 56.64842  ? 120 ARG A HG3  1 
ATOM   1871 H HD2  . ARG A 1 134 ? 2.42166   16.91347  23.42696 1.000 59.42606  ? 120 ARG A HD2  1 
ATOM   1872 H HD3  . ARG A 1 134 ? 3.63904   17.72474  24.04763 1.000 59.42606  ? 120 ARG A HD3  1 
ATOM   1873 H HE   . ARG A 1 134 ? 2.03563   18.60502  22.08679 1.000 52.13394  ? 120 ARG A HE   1 
ATOM   1874 H HH11 . ARG A 1 134 ? 5.14559   20.57976  22.90165 1.000 55.54169  ? 120 ARG A HH11 1 
ATOM   1875 H HH12 . ARG A 1 134 ? 5.01417   19.19463  23.43356 1.000 55.54169  ? 120 ARG A HH12 1 
ATOM   1876 H HH21 . ARG A 1 134 ? 2.27345   20.69456  21.29774 1.000 63.06711  ? 120 ARG A HH21 1 
ATOM   1877 H HH22 . ARG A 1 134 ? 3.49599   21.48406  21.61536 1.000 63.06711  ? 120 ARG A HH22 1 
ATOM   1878 N N    . ILE A 1 135 ? 7.45580   13.31050  23.39961 1.000 28.93333  ? 121 ILE A N    1 
ATOM   1879 C CA   . ILE A 1 135 ? 8.14625   12.15447  23.95609 1.000 25.32224  ? 121 ILE A CA   1 
ATOM   1880 C C    . ILE A 1 135 ? 8.98276   12.56934  25.15609 1.000 28.21576  ? 121 ILE A C    1 
ATOM   1881 O O    . ILE A 1 135 ? 9.64979   13.60983  25.13653 1.000 30.04751  ? 121 ILE A O    1 
ATOM   1882 C CB   . ILE A 1 135 ? 9.05782   11.47860  22.91177 1.000 24.72411  ? 121 ILE A CB   1 
ATOM   1883 C CG1  . ILE A 1 135 ? 8.28140   11.12190  21.64575 1.000 27.66150  ? 121 ILE A CG1  1 
ATOM   1884 C CG2  . ILE A 1 135 ? 9.69380   10.23445  23.50765 1.000 26.31263  ? 121 ILE A CG2  1 
ATOM   1885 C CD1  . ILE A 1 135 ? 9.16123   11.03116  20.42327 1.000 27.24353  ? 121 ILE A CD1  1 
ATOM   1886 H H    . ILE A 1 135 ? 7.98238   13.95688  23.18864 1.000 34.77594  ? 121 ILE A H    1 
ATOM   1887 H HA   . ILE A 1 135 ? 7.47047   11.52732  24.25759 1.000 30.44263  ? 121 ILE A HA   1 
ATOM   1888 H HB   . ILE A 1 135 ? 9.75266   12.10953  22.66674 1.000 29.72488  ? 121 ILE A HB   1 
ATOM   1889 H HG12 . ILE A 1 135 ? 7.85270   10.26084  21.77103 1.000 33.24974  ? 121 ILE A HG12 1 
ATOM   1890 H HG13 . ILE A 1 135 ? 7.61229   11.80514  21.48336 1.000 33.24974  ? 121 ILE A HG13 1 
ATOM   1891 H HG21 . ILE A 1 135 ? 10.31668  10.49994  24.20223 1.000 31.63110  ? 121 ILE A HG21 1 
ATOM   1892 H HG22 . ILE A 1 135 ? 8.99782   9.67349   23.88426 1.000 31.63110  ? 121 ILE A HG22 1 
ATOM   1893 H HG23 . ILE A 1 135 ? 10.16354  9.75396   22.80811 1.000 31.63110  ? 121 ILE A HG23 1 
ATOM   1894 H HD11 . ILE A 1 135 ? 8.74223   10.44308  19.77558 1.000 32.74818  ? 121 ILE A HD11 1 
ATOM   1895 H HD12 . ILE A 1 135 ? 9.26807   11.91776  20.04455 1.000 32.74818  ? 121 ILE A HD12 1 
ATOM   1896 H HD13 . ILE A 1 135 ? 10.02582  10.67565  20.68212 1.000 32.74818  ? 121 ILE A HD13 1 
ATOM   1897 N N    . GLU A 1 136 ? 8.96383   11.72887  26.18689 1.000 27.18046  ? 122 GLU A N    1 
ATOM   1898 C CA   . GLU A 1 136 ? 9.93846   11.75259  27.26820 1.000 28.24850  ? 122 GLU A CA   1 
ATOM   1899 C C    . GLU A 1 136 ? 10.71073  10.44240  27.21341 1.000 27.06172  ? 122 GLU A C    1 
ATOM   1900 O O    . GLU A 1 136 ? 10.10445  9.36755   27.15511 1.000 29.87745  ? 122 GLU A O    1 
ATOM   1901 C CB   . GLU A 1 136 ? 9.26493   11.91542  28.63393 1.000 32.90702  ? 122 GLU A CB   1 
ATOM   1902 C CG   . GLU A 1 136 ? 8.47963   13.21156  28.80728 1.000 47.76315  ? 122 GLU A CG   1 
ATOM   1903 C CD   . GLU A 1 136 ? 9.37048   14.42243  29.03448 1.000 58.05575  ? 122 GLU A CD   1 
ATOM   1904 O OE1  . GLU A 1 136 ? 10.53931  14.24180  29.43754 1.000 55.63634  ? 122 GLU A OE1  1 
ATOM   1905 O OE2  . GLU A 1 136 ? 8.89954   15.55858  28.81135 1.000 62.59414  ? 122 GLU A OE2  1 
ATOM   1906 H H    . GLU A 1 136 ? 8.37184   11.11261  26.28368 1.000 32.67249  ? 122 GLU A H    1 
ATOM   1907 H HA   . GLU A 1 136 ? 10.54803  12.49885  27.15681 1.000 33.95414  ? 122 GLU A HA   1 
ATOM   1908 H HB2  . GLU A 1 136 ? 8.64598   11.17961  28.76188 1.000 39.54436  ? 122 GLU A HB2  1 
ATOM   1909 H HB3  . GLU A 1 136 ? 9.95049   11.89536  29.31987 1.000 39.54436  ? 122 GLU A HB3  1 
ATOM   1910 H HG2  . GLU A 1 136 ? 7.95620   13.37204  28.00655 1.000 57.37172  ? 122 GLU A HG2  1 
ATOM   1911 H HG3  . GLU A 1 136 ? 7.89320   13.12411  29.57498 1.000 57.37172  ? 122 GLU A HG3  1 
ATOM   1912 N N    . LEU A 1 137 ? 12.03753  10.52788  27.21272 1.000 24.41055  ? 123 LEU A N    1 
ATOM   1913 C CA   . LEU A 1 137 ? 12.88949  9.34845   27.16056 1.000 29.06552  ? 123 LEU A CA   1 
ATOM   1914 C C    . LEU A 1 137 ? 13.88725  9.38682   28.30695 1.000 25.64372  ? 123 LEU A C    1 
ATOM   1915 O O    . LEU A 1 137 ? 14.44482  10.44141  28.62372 1.000 30.39999  ? 123 LEU A O    1 
ATOM   1916 C CB   . LEU A 1 137 ? 13.63193  9.25066   25.81675 1.000 30.52495  ? 123 LEU A CB   1 
ATOM   1917 C CG   . LEU A 1 137 ? 14.63283  8.09823   25.67982 1.000 22.88767  ? 123 LEU A CG   1 
ATOM   1918 C CD1  . LEU A 1 137 ? 14.76165  7.68263   24.22396 1.000 21.57003  ? 123 LEU A CD1  1 
ATOM   1919 C CD2  . LEU A 1 137 ? 16.00155  8.46374   26.23768 1.000 25.78016  ? 123 LEU A CD2  1 
ATOM   1920 H H    . LEU A 1 137 ? 12.47192  11.26952  27.24240 1.000 29.34860  ? 123 LEU A H    1 
ATOM   1921 H HA   . LEU A 1 137 ? 12.34487  8.55226   27.26244 1.000 34.93457  ? 123 LEU A HA   1 
ATOM   1922 H HB2  . LEU A 1 137 ? 12.97172  9.14162   25.11452 1.000 36.68588  ? 123 LEU A HB2  1 
ATOM   1923 H HB3  . LEU A 1 137 ? 14.12477  10.07545  25.68360 1.000 36.68588  ? 123 LEU A HB3  1 
ATOM   1924 H HG   . LEU A 1 137 ? 14.29855  7.34894   26.19724 1.000 27.52114  ? 123 LEU A HG   1 
ATOM   1925 H HD11 . LEU A 1 137 ? 14.98254  8.46258   23.69125 1.000 25.93998  ? 123 LEU A HD11 1 
ATOM   1926 H HD12 . LEU A 1 137 ? 15.46473  7.01892   24.14604 1.000 25.93998  ? 123 LEU A HD12 1 
ATOM   1927 H HD13 . LEU A 1 137 ? 13.91801  7.30726   23.92686 1.000 25.93998  ? 123 LEU A HD13 1 
ATOM   1928 H HD21 . LEU A 1 137 ? 16.22949  7.84281   26.94718 1.000 30.99213  ? 123 LEU A HD21 1 
ATOM   1929 H HD22 . LEU A 1 137 ? 16.65795  8.40790   25.52570 1.000 30.99213  ? 123 LEU A HD22 1 
ATOM   1930 H HD23 . LEU A 1 137 ? 15.96888  9.36796   26.58729 1.000 30.99213  ? 123 LEU A HD23 1 
ATOM   1931 N N    . LYS A 1 138 ? 14.11033  8.22510   28.91905 1.000 30.31974  ? 124 LYS A N    1 
ATOM   1932 C CA   . LYS A 1 138 ? 15.05271  8.07956   30.02216 1.000 31.62403  ? 124 LYS A CA   1 
ATOM   1933 C C    . LYS A 1 138 ? 15.86850  6.82011   29.78125 1.000 28.57025  ? 124 LYS A C    1 
ATOM   1934 O O    . LYS A 1 138 ? 15.30351  5.72810   29.66920 1.000 29.79650  ? 124 LYS A O    1 
ATOM   1935 C CB   . LYS A 1 138 ? 14.32049  8.00263   31.36579 1.000 34.36343  ? 124 LYS A CB   1 
ATOM   1936 C CG   . LYS A 1 138 ? 15.23064  7.95239   32.58549 1.000 45.81269  ? 124 LYS A CG   1 
ATOM   1937 C CD   . LYS A 1 138 ? 15.99463  9.25612   32.77174 1.000 45.89878  ? 124 LYS A CD   1 
ATOM   1938 C CE   . LYS A 1 138 ? 16.28730  9.52145   34.24211 1.000 52.12889  ? 124 LYS A CE   1 
ATOM   1939 N NZ   . LYS A 1 138 ? 17.12659  8.45843   34.85759 1.000 55.57850  ? 124 LYS A NZ   1 
ATOM   1940 H H    . LYS A 1 138 ? 13.71754  7.49001   28.70700 1.000 36.43962  ? 124 LYS A H    1 
ATOM   1941 H HA   . LYS A 1 138 ? 15.65417  8.84014   30.04773 1.000 38.00478  ? 124 LYS A HA   1 
ATOM   1942 H HB2  . LYS A 1 138 ? 13.75647  8.78679   31.45451 1.000 41.29205  ? 124 LYS A HB2  1 
ATOM   1943 H HB3  . LYS A 1 138 ? 13.77620  7.19978   31.37440 1.000 41.29205  ? 124 LYS A HB3  1 
ATOM   1944 H HG2  . LYS A 1 138 ? 14.69480  7.79797   33.37917 1.000 55.03117  ? 124 LYS A HG2  1 
ATOM   1945 H HG3  . LYS A 1 138 ? 15.87482  7.23557   32.47546 1.000 55.03117  ? 124 LYS A HG3  1 
ATOM   1946 H HD2  . LYS A 1 138 ? 16.83872  9.20533   32.29652 1.000 55.13447  ? 124 LYS A HD2  1 
ATOM   1947 H HD3  . LYS A 1 138 ? 15.46422  9.99199   32.42814 1.000 55.13447  ? 124 LYS A HD3  1 
ATOM   1948 H HE2  . LYS A 1 138 ? 16.76121  10.36381  34.32413 1.000 62.61061  ? 124 LYS A HE2  1 
ATOM   1949 H HE3  . LYS A 1 138 ? 15.44976  9.56315   34.72964 1.000 62.61061  ? 124 LYS A HE3  1 
ATOM   1950 H HZ1  . LYS A 1 138 ? 16.75053  7.66187   34.73041 1.000 66.75014  ? 124 LYS A HZ1  1 
ATOM   1951 H HZ2  . LYS A 1 138 ? 17.93631  8.45785   34.48819 1.000 66.75014  ? 124 LYS A HZ2  1 
ATOM   1952 H HZ3  . LYS A 1 138 ? 17.20812  8.60305   35.73197 1.000 66.75014  ? 124 LYS A HZ3  1 
ATOM   1953 N N    . GLY A 1 139 ? 17.18146  6.97257   29.69242 1.000 30.29054  ? 125 GLY A N    1 
ATOM   1954 C CA   . GLY A 1 139 ? 18.08540  5.84810   29.49598 1.000 28.89629  ? 125 GLY A CA   1 
ATOM   1955 C C    . GLY A 1 139 ? 19.07631  5.74479   30.63843 1.000 28.48937  ? 125 GLY A C    1 
ATOM   1956 O O    . GLY A 1 139 ? 19.59445  6.75832   31.11270 1.000 28.45770  ? 125 GLY A O    1 
ATOM   1957 H H    . GLY A 1 139 ? 17.58156  7.73209   29.74381 1.000 36.40459  ? 125 GLY A H    1 
ATOM   1958 H HA2  . GLY A 1 139 ? 17.57665  5.02355   29.44930 1.000 34.73149  ? 125 GLY A HA2  1 
ATOM   1959 H HA3  . GLY A 1 139 ? 18.57621  5.96368   28.66734 1.000 34.73149  ? 125 GLY A HA3  1 
ATOM   1960 N N    . ILE A 1 140 ? 19.33744  4.51128   31.07393 1.000 30.42019  ? 126 ILE A N    1 
ATOM   1961 C CA   . ILE A 1 140 ? 20.24878  4.23328   32.17565 1.000 27.39459  ? 126 ILE A CA   1 
ATOM   1962 C C    . ILE A 1 140 ? 21.05684  2.98488   31.84351 1.000 31.98556  ? 126 ILE A C    1 
ATOM   1963 O O    . ILE A 1 140 ? 20.74362  2.24004   30.91316 1.000 33.46366  ? 126 ILE A O    1 
ATOM   1964 C CB   . ILE A 1 140 ? 19.50501  4.04463   33.51618 1.000 32.11529  ? 126 ILE A CB   1 
ATOM   1965 C CG1  . ILE A 1 140 ? 18.59260  2.81362   33.46059 1.000 34.03459  ? 126 ILE A CG1  1 
ATOM   1966 C CG2  . ILE A 1 140 ? 18.69414  5.28670   33.85033 1.000 34.31402  ? 126 ILE A CG2  1 
ATOM   1967 C CD1  . ILE A 1 140 ? 17.87193  2.52866   34.76475 1.000 35.72771  ? 126 ILE A CD1  1 
ATOM   1968 H H    . ILE A 1 140 ? 18.98715  3.80268   30.73514 1.000 36.56017  ? 126 ILE A H    1 
ATOM   1969 H HA   . ILE A 1 140 ? 20.86496  4.97675   32.26773 1.000 32.60688  ? 126 ILE A HA   1 
ATOM   1970 H HB   . ILE A 1 140 ? 20.16654  3.90505   34.21174 1.000 38.59429  ? 126 ILE A HB   1 
ATOM   1971 H HG12 . ILE A 1 140 ? 17.92055  2.95406   32.77537 1.000 40.89744  ? 126 ILE A HG12 1 
ATOM   1972 H HG13 . ILE A 1 140 ? 19.13044  2.03616   33.24338 1.000 40.89744  ? 126 ILE A HG13 1 
ATOM   1973 H HG21 . ILE A 1 140 ? 18.37618  5.21984   34.76429 1.000 41.23277  ? 126 ILE A HG21 1 
ATOM   1974 H HG22 . ILE A 1 140 ? 19.25981  6.06869   33.75328 1.000 41.23277  ? 126 ILE A HG22 1 
ATOM   1975 H HG23 . ILE A 1 140 ? 17.94120  5.34550   33.24162 1.000 41.23277  ? 126 ILE A HG23 1 
ATOM   1976 H HD11 . ILE A 1 140 ? 17.43858  1.66301   34.70349 1.000 42.92919  ? 126 ILE A HD11 1 
ATOM   1977 H HD12 . ILE A 1 140 ? 18.51802  2.52468   35.48825 1.000 42.92919  ? 126 ILE A HD12 1 
ATOM   1978 H HD13 . ILE A 1 140 ? 17.20912  3.22034   34.91697 1.000 42.92919  ? 126 ILE A HD13 1 
ATOM   1979 N N    . ASP A 1 141 ? 22.10924  2.76349   32.63284 1.000 28.51801  ? 127 ASP A N    1 
ATOM   1980 C CA   . ASP A 1 141 ? 22.92327  1.54950   32.56262 1.000 33.29283  ? 127 ASP A CA   1 
ATOM   1981 C C    . ASP A 1 141 ? 23.62404  1.40006   31.21517 1.000 33.76974  ? 127 ASP A C    1 
ATOM   1982 O O    . ASP A 1 141 ? 23.87196  0.28273   30.75493 1.000 30.41854  ? 127 ASP A O    1 
ATOM   1983 C CB   . ASP A 1 141 ? 22.08258  0.30201   32.85790 1.000 33.94379  ? 127 ASP A CB   1 
ATOM   1984 C CG   . ASP A 1 141 ? 21.53009  0.28966   34.26883 1.000 34.67756  ? 127 ASP A CG   1 
ATOM   1985 O OD1  . ASP A 1 141 ? 21.78453  1.25589   35.01982 1.000 31.79641  ? 127 ASP A OD1  1 
ATOM   1986 O OD2  . ASP A 1 141 ? 20.84162  -0.69004  34.62610 1.000 36.44562  ? 127 ASP A OD2  1 
ATOM   1987 H H    . ASP A 1 141 ? 22.37884  3.31691   33.23338 1.000 33.94191  ? 127 ASP A H    1 
ATOM   1988 H HA   . ASP A 1 141 ? 23.61507  1.62058   33.23883 1.000 40.00734  ? 127 ASP A HA   1 
ATOM   1989 H HB2  . ASP A 1 141 ? 21.33376  0.27215   32.24204 1.000 40.78849  ? 127 ASP A HB2  1 
ATOM   1990 H HB3  . ASP A 1 141 ? 22.63627  -0.48646  32.74543 1.000 40.78849  ? 127 ASP A HB3  1 
ATOM   1991 N N    . PHE A 1 142 ? 23.96693  2.51421   30.57660 1.000 32.16148  ? 128 PHE A N    1 
ATOM   1992 C CA   . PHE A 1 142 ? 24.64388  2.47411   29.28890 1.000 31.15944  ? 128 PHE A CA   1 
ATOM   1993 C C    . PHE A 1 142 ? 26.15155  2.55606   29.48041 1.000 31.69718  ? 128 PHE A C    1 
ATOM   1994 O O    . PHE A 1 142 ? 26.64302  3.24390   30.37984 1.000 31.61368  ? 128 PHE A O    1 
ATOM   1995 C CB   . PHE A 1 142 ? 24.15547  3.60563   28.38405 1.000 29.28979  ? 128 PHE A CB   1 
ATOM   1996 C CG   . PHE A 1 142 ? 22.88615  3.27682   27.65098 1.000 33.83690  ? 128 PHE A CG   1 
ATOM   1997 C CD1  . PHE A 1 142 ? 22.91781  2.50294   26.50111 1.000 33.16711  ? 128 PHE A CD1  1 
ATOM   1998 C CD2  . PHE A 1 142 ? 21.66243  3.72457   28.11700 1.000 32.96312  ? 128 PHE A CD2  1 
ATOM   1999 C CE1  . PHE A 1 142 ? 21.75501  2.18909   25.82708 1.000 30.09980  ? 128 PHE A CE1  1 
ATOM   2000 C CE2  . PHE A 1 142 ? 20.49446  3.41308   27.44602 1.000 31.75323  ? 128 PHE A CE2  1 
ATOM   2001 C CZ   . PHE A 1 142 ? 20.54226  2.64376   26.29921 1.000 30.52905  ? 128 PHE A CZ   1 
ATOM   2002 H H    . PHE A 1 142 ? 23.81701  3.30814   30.87123 1.000 38.64972  ? 128 PHE A H    1 
ATOM   2003 H HA   . PHE A 1 142 ? 24.44490  1.63441   28.84594 1.000 37.44727  ? 128 PHE A HA   1 
ATOM   2004 H HB2  . PHE A 1 142 ? 23.99034  4.39213   28.92723 1.000 35.20369  ? 128 PHE A HB2  1 
ATOM   2005 H HB3  . PHE A 1 142 ? 24.83983  3.79628   27.72359 1.000 35.20369  ? 128 PHE A HB3  1 
ATOM   2006 H HD1  . PHE A 1 142 ? 23.73301  2.19130   26.17983 1.000 39.85647  ? 128 PHE A HD1  1 
ATOM   2007 H HD2  . PHE A 1 142 ? 21.62533  4.24055   28.88985 1.000 39.61168  ? 128 PHE A HD2  1 
ATOM   2008 H HE1  . PHE A 1 142 ? 21.78961  1.67145   25.05523 1.000 36.17570  ? 128 PHE A HE1  1 
ATOM   2009 H HE2  . PHE A 1 142 ? 19.67742  3.72103   27.76621 1.000 38.15982  ? 128 PHE A HE2  1 
ATOM   2010 H HZ   . PHE A 1 142 ? 19.75761  2.43306   25.84663 1.000 36.69080  ? 128 PHE A HZ   1 
ATOM   2011 N N    . LYS A 1 143 ? 26.87912  1.84294   28.62649 1.000 31.17411  ? 129 LYS A N    1 
ATOM   2012 C CA   . LYS A 1 143 ? 28.32040  1.68245   28.75529 1.000 32.34254  ? 129 LYS A CA   1 
ATOM   2013 C C    . LYS A 1 143 ? 29.03781  2.63828   27.81112 1.000 38.14224  ? 129 LYS A C    1 
ATOM   2014 O O    . LYS A 1 143 ? 28.74057  2.67651   26.61220 1.000 32.64388  ? 129 LYS A O    1 
ATOM   2015 C CB   . LYS A 1 143 ? 28.72148  0.23539   28.46226 1.000 34.18708  ? 129 LYS A CB   1 
ATOM   2016 C CG   . LYS A 1 143 ? 28.08916  -0.77396  29.41644 1.000 35.08851  ? 129 LYS A CG   1 
ATOM   2017 C CD   . LYS A 1 143 ? 28.33774  -2.20336  28.98083 1.000 33.36864  ? 129 LYS A CD   1 
ATOM   2018 C CE   . LYS A 1 143 ? 27.82863  -3.18856  30.02304 1.000 38.73610  ? 129 LYS A CE   1 
ATOM   2019 N NZ   . LYS A 1 143 ? 27.82915  -4.59409  29.52639 1.000 43.36859  ? 129 LYS A NZ   1 
ATOM   2020 H H    . LYS A 1 143 ? 26.54995  1.43207   27.94647 1.000 37.46487  ? 129 LYS A H    1 
ATOM   2021 H HA   . LYS A 1 143 ? 28.59370  1.90223   29.65967 1.000 38.86699  ? 129 LYS A HA   1 
ATOM   2022 H HB2  . LYS A 1 143 ? 28.44168  0.00915   27.56147 1.000 41.08044  ? 129 LYS A HB2  1 
ATOM   2023 H HB3  . LYS A 1 143 ? 29.68503  0.15555   28.54027 1.000 41.08044  ? 129 LYS A HB3  1 
ATOM   2024 H HG2  . LYS A 1 143 ? 28.46862  -0.65733  30.30149 1.000 42.16215  ? 129 LYS A HG2  1 
ATOM   2025 H HG3  . LYS A 1 143 ? 27.13048  -0.62895  29.44476 1.000 42.16215  ? 129 LYS A HG3  1 
ATOM   2026 H HD2  . LYS A 1 143 ? 27.87308  -2.37219  28.14627 1.000 40.09831  ? 129 LYS A HD2  1 
ATOM   2027 H HD3  . LYS A 1 143 ? 29.29034  -2.34464  28.86464 1.000 40.09831  ? 129 LYS A HD3  1 
ATOM   2028 H HE2  . LYS A 1 143 ? 28.39970  -3.14579  30.80595 1.000 46.53926  ? 129 LYS A HE2  1 
ATOM   2029 H HE3  . LYS A 1 143 ? 26.91842  -2.95454  30.26314 1.000 46.53926  ? 129 LYS A HE3  1 
ATOM   2030 H HZ1  . LYS A 1 143 ? 28.64044  -4.81302  29.23317 1.000 52.09825  ? 129 LYS A HZ1  1 
ATOM   2031 H HZ2  . LYS A 1 143 ? 27.59992  -5.14912  30.18326 1.000 52.09825  ? 129 LYS A HZ2  1 
ATOM   2032 H HZ3  . LYS A 1 143 ? 27.24741  -4.68114  28.85848 1.000 52.09825  ? 129 LYS A HZ3  1 
ATOM   2033 N N    . GLU A 1 144 ? 29.97723  3.41264   28.36274 1.000 34.81578  ? 130 GLU A N    1 
ATOM   2034 C CA   . GLU A 1 144 ? 30.75078  4.34608   27.54961 1.000 37.18863  ? 130 GLU A CA   1 
ATOM   2035 C C    . GLU A 1 144 ? 31.52558  3.61398   26.46256 1.000 37.35331  ? 130 GLU A C    1 
ATOM   2036 O O    . GLU A 1 144 ? 31.65648  4.11214   25.33781 1.000 34.59723  ? 130 GLU A O    1 
ATOM   2037 C CB   . GLU A 1 144 ? 31.70503  5.14432   28.44103 1.000 33.23771  ? 130 GLU A CB   1 
ATOM   2038 C CG   . GLU A 1 144 ? 32.58062  6.14904   27.69873 1.000 48.45393  ? 130 GLU A CG   1 
ATOM   2039 C CD   . GLU A 1 144 ? 31.77887  7.27784   27.07628 1.000 51.75153  ? 130 GLU A CD   1 
ATOM   2040 O OE1  . GLU A 1 144 ? 30.58542  7.41817   27.41637 1.000 49.69800  ? 130 GLU A OE1  1 
ATOM   2041 O OE2  . GLU A 1 144 ? 32.34155  8.02422   26.24742 1.000 51.90667  ? 130 GLU A OE2  1 
ATOM   2042 H H    . GLU A 1 144 ? 30.18266  3.41522   29.19784 1.000 41.83488  ? 130 GLU A H    1 
ATOM   2043 H HA   . GLU A 1 144 ? 30.14367  4.96902   27.12035 1.000 44.68230  ? 130 GLU A HA   1 
ATOM   2044 H HB2  . GLU A 1 144 ? 31.17984  5.63806   29.09010 1.000 39.94119  ? 130 GLU A HB2  1 
ATOM   2045 H HB3  . GLU A 1 144 ? 32.29482  4.52256   28.89543 1.000 39.94119  ? 130 GLU A HB3  1 
ATOM   2046 H HG2  . GLU A 1 144 ? 33.21325  6.53865   28.32234 1.000 58.20065  ? 130 GLU A HG2  1 
ATOM   2047 H HG3  . GLU A 1 144 ? 33.05516  5.69045   26.98781 1.000 58.20065  ? 130 GLU A HG3  1 
ATOM   2048 N N    . ASP A 1 145 ? 32.05293  2.43263   26.78247 1.000 37.18353  ? 131 ASP A N    1 
ATOM   2049 C CA   . ASP A 1 145 ? 32.78336  1.61006   25.82997 1.000 41.69183  ? 131 ASP A CA   1 
ATOM   2050 C C    . ASP A 1 145 ? 31.87332  0.65099   25.06808 1.000 35.90112  ? 131 ASP A C    1 
ATOM   2051 O O    . ASP A 1 145 ? 32.34784  -0.37587  24.56872 1.000 37.75811  ? 131 ASP A O    1 
ATOM   2052 C CB   . ASP A 1 145 ? 33.89431  0.83308   26.54759 1.000 48.39906  ? 131 ASP A CB   1 
ATOM   2053 C CG   . ASP A 1 145 ? 33.39980  0.09726   27.78688 1.000 47.15060  ? 131 ASP A CG   1 
ATOM   2054 O OD1  . ASP A 1 145 ? 32.17225  0.06170   28.02069 1.000 43.38590  ? 131 ASP A OD1  1 
ATOM   2055 O OD2  . ASP A 1 145 ? 34.24663  -0.43942  28.53303 1.000 42.86064  ? 131 ASP A OD2  1 
ATOM   2056 H H    . ASP A 1 145 ? 31.99740  2.08095   27.56531 1.000 44.67618  ? 131 ASP A H    1 
ATOM   2057 H HA   . ASP A 1 145 ? 33.20474  2.19382   25.17992 1.000 50.08614  ? 131 ASP A HA   1 
ATOM   2058 H HB2  . ASP A 1 145 ? 34.26432  0.17607   25.93741 1.000 58.13481  ? 131 ASP A HB2  1 
ATOM   2059 H HB3  . ASP A 1 145 ? 34.58543  1.45473   26.82473 1.000 58.13481  ? 131 ASP A HB3  1 
ATOM   2060 N N    . GLY A 1 146 ? 30.57990  0.96612   24.96848 1.000 36.07620  ? 132 GLY A N    1 
ATOM   2061 C CA   . GLY A 1 146 ? 29.63805  0.15719   24.22947 1.000 40.66650  ? 132 GLY A CA   1 
ATOM   2062 C C    . GLY A 1 146 ? 29.27576  0.77863   22.88703 1.000 34.00995  ? 132 GLY A C    1 
ATOM   2063 O O    . GLY A 1 146 ? 29.79380  1.81465   22.48114 1.000 35.85342  ? 132 GLY A O    1 
ATOM   2064 H H    . GLY A 1 146 ? 30.22590  1.66067   25.33165 1.000 43.34738  ? 132 GLY A H    1 
ATOM   2065 H HA2  . GLY A 1 146 ? 30.02298  -0.71842  24.06809 1.000 48.85574  ? 132 GLY A HA2  1 
ATOM   2066 H HA3  . GLY A 1 146 ? 28.82536  0.05404   24.74888 1.000 48.85574  ? 132 GLY A HA3  1 
ATOM   2067 N N    . ASN A 1 147 ? 28.34588  0.11524   22.19648 1.000 36.76794  ? 133 ASN A N    1 
ATOM   2068 C CA   . ASN A 1 147 ? 27.98579  0.52195   20.84321 1.000 32.21467  ? 133 ASN A CA   1 
ATOM   2069 C C    . ASN A 1 147 ? 27.11544  1.76851   20.80194 1.000 32.19339  ? 133 ASN A C    1 
ATOM   2070 O O    . ASN A 1 147 ? 27.08203  2.44501   19.76866 1.000 35.64059  ? 133 ASN A O    1 
ATOM   2071 C CB   . ASN A 1 147 ? 27.25570  -0.61347  20.12739 1.000 32.52032  ? 133 ASN A CB   1 
ATOM   2072 C CG   . ASN A 1 147 ? 28.07862  -1.87179  20.05526 1.000 29.41100  ? 133 ASN A CG   1 
ATOM   2073 O OD1  . ASN A 1 147 ? 29.28349  -1.82852  19.80263 1.000 29.90076  ? 133 ASN A OD1  1 
ATOM   2074 N ND2  . ASN A 1 147 ? 27.43714  -3.00617  20.29182 1.000 33.32891  ? 133 ASN A ND2  1 
ATOM   2075 H H    . ASN A 1 147 ? 27.91369  -0.56819  22.48928 1.000 44.17747  ? 133 ASN A H    1 
ATOM   2076 H HA   . ASN A 1 147 ? 28.80596  0.71398   20.36224 1.000 38.71355  ? 133 ASN A HA   1 
ATOM   2077 H HB2  . ASN A 1 147 ? 26.43712  -0.81610  20.60674 1.000 39.08033  ? 133 ASN A HB2  1 
ATOM   2078 H HB3  . ASN A 1 147 ? 27.04944  -0.33621  19.22103 1.000 39.08033  ? 133 ASN A HB3  1 
ATOM   2079 H HD21 . ASN A 1 147 ? 27.86101  -3.75390  20.26315 1.000 40.05063  ? 133 ASN A HD21 1 
ATOM   2080 H HD22 . ASN A 1 147 ? 26.59675  -2.99499  20.47409 1.000 40.05063  ? 133 ASN A HD22 1 
ATOM   2081 N N    . ILE A 1 148 ? 26.40705  2.08230   21.88485 1.000 29.62950  ? 134 ILE A N    1 
ATOM   2082 C CA   . ILE A 1 148 ? 25.50244  3.22576   21.90131 1.000 30.80405  ? 134 ILE A CA   1 
ATOM   2083 C C    . ILE A 1 148 ? 26.28431  4.48129   22.26716 1.000 34.97899  ? 134 ILE A C    1 
ATOM   2084 O O    . ILE A 1 148 ? 26.46876  5.37119   21.43012 1.000 34.56939  ? 134 ILE A O    1 
ATOM   2085 C CB   . ILE A 1 148 ? 24.32475  2.99291   22.86580 1.000 32.75536  ? 134 ILE A CB   1 
ATOM   2086 C CG1  . ILE A 1 148 ? 23.40502  1.89269   22.32384 1.000 35.62798  ? 134 ILE A CG1  1 
ATOM   2087 C CG2  . ILE A 1 148 ? 23.54093  4.28086   23.07665 1.000 37.23586  ? 134 ILE A CG2  1 
ATOM   2088 C CD1  . ILE A 1 148 ? 23.74496  0.50597   22.81293 1.000 40.10703  ? 134 ILE A CD1  1 
ATOM   2089 H H    . ILE A 1 148 ? 26.43408  1.64546   22.62515 1.000 35.61134  ? 134 ILE A H    1 
ATOM   2090 H HA   . ILE A 1 148 ? 25.13648  3.35161   21.01186 1.000 37.02080  ? 134 ILE A HA   1 
ATOM   2091 H HB   . ILE A 1 148 ? 24.68364  2.70766   23.72063 1.000 39.36237  ? 134 ILE A HB   1 
ATOM   2092 H HG12 . ILE A 1 148 ? 22.49487  2.08638   22.59773 1.000 42.80951  ? 134 ILE A HG12 1 
ATOM   2093 H HG13 . ILE A 1 148 ? 23.46593  1.88639   21.35578 1.000 42.80951  ? 134 ILE A HG13 1 
ATOM   2094 H HG21 . ILE A 1 148 ? 24.03997  4.86012   23.67357 1.000 44.73897  ? 134 ILE A HG21 1 
ATOM   2095 H HG22 . ILE A 1 148 ? 23.41539  4.71799   22.21988 1.000 44.73897  ? 134 ILE A HG22 1 
ATOM   2096 H HG23 . ILE A 1 148 ? 22.67966  4.06597   23.46770 1.000 44.73897  ? 134 ILE A HG23 1 
ATOM   2097 H HD11 . ILE A 1 148 ? 24.66210  0.30203   22.57175 1.000 48.18438  ? 134 ILE A HD11 1 
ATOM   2098 H HD12 . ILE A 1 148 ? 23.64224  0.47713   23.77705 1.000 48.18438  ? 134 ILE A HD12 1 
ATOM   2099 H HD13 . ILE A 1 148 ? 23.14394  -0.13176  22.39702 1.000 48.18438  ? 134 ILE A HD13 1 
ATOM   2100 N N    . LEU A 1 149 ? 26.75544  4.56558   23.51480 1.000 34.56250  ? 135 LEU A N    1 
ATOM   2101 C CA   . LEU A 1 149 ? 27.52258  5.73904   23.92291 1.000 30.28399  ? 135 LEU A CA   1 
ATOM   2102 C C    . LEU A 1 149 ? 28.80994  5.86934   23.11983 1.000 30.62227  ? 135 LEU A C    1 
ATOM   2103 O O    . LEU A 1 149 ? 29.31746  6.98113   22.93640 1.000 34.24201  ? 135 LEU A O    1 
ATOM   2104 C CB   . LEU A 1 149 ? 27.83990  5.67744   25.41852 1.000 32.93261  ? 135 LEU A CB   1 
ATOM   2105 C CG   . LEU A 1 149 ? 26.64429  5.52709   26.36317 1.000 32.00193  ? 135 LEU A CG   1 
ATOM   2106 C CD1  . LEU A 1 149 ? 27.07623  5.68529   27.81200 1.000 32.37318  ? 135 LEU A CD1  1 
ATOM   2107 C CD2  . LEU A 1 149 ? 25.54245  6.51823   26.02098 1.000 35.33052  ? 135 LEU A CD2  1 
ATOM   2108 H H    . LEU A 1 149 ? 26.64667  3.97147   24.12701 1.000 41.53094  ? 135 LEU A H    1 
ATOM   2109 H HA   . LEU A 1 149 ? 26.98262  6.52941   23.76592 1.000 36.39673  ? 135 LEU A HA   1 
ATOM   2110 H HB2  . LEU A 1 149 ? 28.42179  4.91656   25.57138 1.000 39.57507  ? 135 LEU A HB2  1 
ATOM   2111 H HB3  . LEU A 1 149 ? 28.29555  6.49803   25.66330 1.000 39.57507  ? 135 LEU A HB3  1 
ATOM   2112 H HG   . LEU A 1 149 ? 26.28043  4.63461   26.25366 1.000 38.45825  ? 135 LEU A HG   1 
ATOM   2113 H HD11 . LEU A 1 149 ? 26.28719  5.77933   28.36831 1.000 38.90376  ? 135 LEU A HD11 1 
ATOM   2114 H HD12 . LEU A 1 149 ? 27.57787  4.89939   28.07960 1.000 38.90376  ? 135 LEU A HD12 1 
ATOM   2115 H HD13 . LEU A 1 149 ? 27.63283  6.47576   27.89109 1.000 38.90376  ? 135 LEU A HD13 1 
ATOM   2116 H HD21 . LEU A 1 149 ? 25.10376  6.23316   25.20417 1.000 42.45256  ? 135 LEU A HD21 1 
ATOM   2117 H HD22 . LEU A 1 149 ? 24.90216  6.54248   26.74922 1.000 42.45256  ? 135 LEU A HD22 1 
ATOM   2118 H HD23 . LEU A 1 149 ? 25.93514  7.39640   25.89641 1.000 42.45256  ? 135 LEU A HD23 1 
ATOM   2119 N N    . GLY A 1 150 ? 29.35244  4.75473   22.63869 1.000 36.15490  ? 136 GLY A N    1 
ATOM   2120 C CA   . GLY A 1 150 ? 30.54254  4.77871   21.81785 1.000 38.09745  ? 136 GLY A CA   1 
ATOM   2121 C C    . GLY A 1 150 ? 30.31674  5.11282   20.36277 1.000 34.13896  ? 136 GLY A C    1 
ATOM   2122 O O    . GLY A 1 150 ? 31.28504  5.20908   19.60438 1.000 35.88612  ? 136 GLY A O    1 
ATOM   2123 H H    . GLY A 1 150 ? 29.04087  3.96556   22.77918 1.000 43.44182  ? 136 GLY A H    1 
ATOM   2124 H HA2  . GLY A 1 150 ? 31.15378  5.43926   22.17974 1.000 45.77289  ? 136 GLY A HA2  1 
ATOM   2125 H HA3  . GLY A 1 150 ? 30.96221  3.90508   21.85718 1.000 45.77289  ? 136 GLY A HA3  1 
ATOM   2126 N N    . HIS A 1 151 ? 29.06569  5.28747   19.94549 1.000 32.87723  ? 137 HIS A N    1 
ATOM   2127 C CA   . HIS A 1 151 ? 28.73118  5.64376   18.56940 1.000 35.06013  ? 137 HIS A CA   1 
ATOM   2128 C C    . HIS A 1 151 ? 29.39595  4.68188   17.58496 1.000 31.02515  ? 137 HIS A C    1 
ATOM   2129 O O    . HIS A 1 151 ? 30.20674  5.06615   16.74050 1.000 29.20914  ? 137 HIS A O    1 
ATOM   2130 C CB   . HIS A 1 151 ? 29.12781  7.09287   18.27322 1.000 34.28525  ? 137 HIS A CB   1 
ATOM   2131 C CG   . HIS A 1 151 ? 28.38523  8.10178   19.09171 1.000 37.12999  ? 137 HIS A CG   1 
ATOM   2132 N ND1  . HIS A 1 151 ? 27.13758  8.57102   18.74127 1.000 34.86271  ? 137 HIS A ND1  1 
ATOM   2133 C CD2  . HIS A 1 151 ? 28.71538  8.73383   20.24276 1.000 37.83572  ? 137 HIS A CD2  1 
ATOM   2134 C CE1  . HIS A 1 151 ? 26.72987  9.44642   19.64244 1.000 38.75077  ? 137 HIS A CE1  1 
ATOM   2135 N NE2  . HIS A 1 151 ? 27.66925  9.56432   20.56362 1.000 41.46080  ? 137 HIS A NE2  1 
ATOM   2136 H H    . HIS A 1 151 ? 28.37677  5.20306   20.45329 1.000 39.50862  ? 137 HIS A H    1 
ATOM   2137 H HA   . HIS A 1 151 ? 27.77096  5.56429   18.45733 1.000 42.12810  ? 137 HIS A HA   1 
ATOM   2138 H HB2  . HIS A 1 151 ? 30.07398  7.20094   18.45758 1.000 41.19824  ? 137 HIS A HB2  1 
ATOM   2139 H HB3  . HIS A 1 151 ? 28.94840  7.28030   17.33857 1.000 41.19824  ? 137 HIS A HB3  1 
ATOM   2140 H HD1  . HIS A 1 151 ? 26.69385  8.33129   18.04468 1.000 41.89120  ? 137 HIS A HD1  1 
ATOM   2141 H HD2  . HIS A 1 151 ? 29.50283  8.62592   20.72565 1.000 45.45881  ? 137 HIS A HD2  1 
ATOM   2142 H HE1  . HIS A 1 151 ? 25.91932  9.90224   19.63045 1.000 46.55687  ? 137 HIS A HE1  1 
ATOM   2143 N N    . LYS A 1 152 ? 29.03398  3.40609   17.71140 1.000 30.92579  ? 138 LYS A N    1 
ATOM   2144 C CA   . LYS A 1 152 ? 29.59753  2.34913   16.88265 1.000 27.95172  ? 138 LYS A CA   1 
ATOM   2145 C C    . LYS A 1 152 ? 28.57823  1.76070   15.91708 1.000 31.81096  ? 138 LYS A C    1 
ATOM   2146 O O    . LYS A 1 152 ? 28.85525  0.73330   15.28848 1.000 32.27088  ? 138 LYS A O    1 
ATOM   2147 C CB   . LYS A 1 152 ? 30.17853  1.24095   17.76328 1.000 26.93560  ? 138 LYS A CB   1 
ATOM   2148 C CG   . LYS A 1 152 ? 31.22930  1.72005   18.75195 1.000 33.78577  ? 138 LYS A CG   1 
ATOM   2149 C CD   . LYS A 1 152 ? 31.84246  0.55777   19.52137 1.000 28.57870  ? 138 LYS A CD   1 
ATOM   2150 C CE   . LYS A 1 152 ? 32.93142  1.03322   20.46801 1.000 40.18398  ? 138 LYS A CE   1 
ATOM   2151 N NZ   . LYS A 1 152 ? 33.67442  -0.10209  21.08742 1.000 38.46675  ? 138 LYS A NZ   1 
ATOM   2152 H H    . LYS A 1 152 ? 28.45353  3.12598   18.28079 1.000 37.16688  ? 138 LYS A H    1 
ATOM   2153 H HA   . LYS A 1 152 ? 30.32110  2.72571   16.35774 1.000 33.59801  ? 138 LYS A HA   1 
ATOM   2154 H HB2  . LYS A 1 152 ? 29.45730  0.83837   18.27186 1.000 32.37866  ? 138 LYS A HB2  1 
ATOM   2155 H HB3  . LYS A 1 152 ? 30.59317  0.57571   17.19193 1.000 32.37866  ? 138 LYS A HB3  1 
ATOM   2156 H HG2  . LYS A 1 152 ? 31.93832  2.17564   18.27172 1.000 40.59886  ? 138 LYS A HG2  1 
ATOM   2157 H HG3  . LYS A 1 152 ? 30.81859  2.32486   19.38946 1.000 40.59886  ? 138 LYS A HG3  1 
ATOM   2158 H HD2  . LYS A 1 152 ? 31.15341  0.11894   20.04438 1.000 34.35038  ? 138 LYS A HD2  1 
ATOM   2159 H HD3  . LYS A 1 152 ? 32.23494  -0.07096  18.89563 1.000 34.35038  ? 138 LYS A HD3  1 
ATOM   2160 H HE2  . LYS A 1 152 ? 33.56617  1.57705   19.97583 1.000 48.27671  ? 138 LYS A HE2  1 
ATOM   2161 H HE3  . LYS A 1 152 ? 32.52912  1.55520   21.17977 1.000 48.27671  ? 138 LYS A HE3  1 
ATOM   2162 H HZ1  . LYS A 1 152 ? 33.10768  -0.64137  21.51179 1.000 46.21604  ? 138 LYS A HZ1  1 
ATOM   2163 H HZ2  . LYS A 1 152 ? 34.09946  -0.56690  20.45862 1.000 46.21604  ? 138 LYS A HZ2  1 
ATOM   2164 H HZ3  . LYS A 1 152 ? 34.27103  0.20691   21.67110 1.000 46.21604  ? 138 LYS A HZ3  1 
ATOM   2165 N N    . LEU A 1 153 ? 27.41450  2.38715   15.77709 1.000 34.00756  ? 139 LEU A N    1 
ATOM   2166 C CA   . LEU A 1 153 ? 26.35187  1.88271   14.92100 1.000 36.24298  ? 139 LEU A CA   1 
ATOM   2167 C C    . LEU A 1 153 ? 26.40463  2.55476   13.55659 1.000 35.14773  ? 139 LEU A C    1 
ATOM   2168 O O    . LEU A 1 153 ? 26.58670  3.77185   13.45695 1.000 29.06593  ? 139 LEU A O    1 
ATOM   2169 C CB   . LEU A 1 153 ? 24.98087  2.12122   15.55549 1.000 30.21230  ? 139 LEU A CB   1 
ATOM   2170 C CG   . LEU A 1 153 ? 24.75708  1.49721   16.93193 1.000 28.07292  ? 139 LEU A CG   1 
ATOM   2171 C CD1  . LEU A 1 153 ? 23.32318  1.72514   17.38154 1.000 32.55436  ? 139 LEU A CD1  1 
ATOM   2172 C CD2  . LEU A 1 153 ? 25.08792  0.01466   16.91484 1.000 33.62916  ? 139 LEU A CD2  1 
ATOM   2173 H H    . LEU A 1 153 ? 27.21453  3.12169   16.17717 1.000 40.86501  ? 139 LEU A H    1 
ATOM   2174 H HA   . LEU A 1 153 ? 26.47363  0.92857   14.79569 1.000 43.54751  ? 139 LEU A HA   1 
ATOM   2175 H HB2  . LEU A 1 153 ? 24.85510  3.07827   15.65106 1.000 36.31070  ? 139 LEU A HB2  1 
ATOM   2176 H HB3  . LEU A 1 153 ? 24.30619  1.75556   14.96218 1.000 36.31070  ? 139 LEU A HB3  1 
ATOM   2177 H HG   . LEU A 1 153 ? 25.34906  1.92084   17.57303 1.000 33.74344  ? 139 LEU A HG   1 
ATOM   2178 H HD11 . LEU A 1 153 ? 23.16997  2.67816   17.47735 1.000 39.12118  ? 139 LEU A HD11 1 
ATOM   2179 H HD12 . LEU A 1 153 ? 22.72120  1.35870   16.71503 1.000 39.12118  ? 139 LEU A HD12 1 
ATOM   2180 H HD13 . LEU A 1 153 ? 23.18460  1.28064   18.23249 1.000 39.12118  ? 139 LEU A HD13 1 
ATOM   2181 H HD21 . LEU A 1 153 ? 26.04735  -0.09375  16.82186 1.000 40.41094  ? 139 LEU A HD21 1 
ATOM   2182 H HD22 . LEU A 1 153 ? 24.78890  -0.38525  17.74643 1.000 40.41094  ? 139 LEU A HD22 1 
ATOM   2183 H HD23 . LEU A 1 153 ? 24.63385  -0.40161  16.16555 1.000 40.41094  ? 139 LEU A HD23 1 
ATOM   2184 N N    . GLU A 1 154 ? 26.24233  1.75274   12.50723 1.000 35.30191  ? 140 GLU A N    1 
ATOM   2185 C CA   . GLU A 1 154 ? 26.14121  2.30361   11.16476 1.000 39.04723  ? 140 GLU A CA   1 
ATOM   2186 C C    . GLU A 1 154 ? 24.95443  3.25305   11.08000 1.000 32.15170  ? 140 GLU A C    1 
ATOM   2187 O O    . GLU A 1 154 ? 23.91329  3.03038   11.70410 1.000 30.77538  ? 140 GLU A O    1 
ATOM   2188 C CB   . GLU A 1 154 ? 25.98214  1.18522   10.13448 1.000 36.49140  ? 140 GLU A CB   1 
ATOM   2189 C CG   . GLU A 1 154 ? 27.19355  0.28674   9.98756  1.000 45.46446  ? 140 GLU A CG   1 
ATOM   2190 C CD   . GLU A 1 154 ? 27.03048  -0.73671  8.87632  1.000 52.27885  ? 140 GLU A CD   1 
ATOM   2191 O OE1  . GLU A 1 154 ? 25.96015  -0.75027  8.23006  1.000 44.42149  ? 140 GLU A OE1  1 
ATOM   2192 O OE2  . GLU A 1 154 ? 27.97296  -1.52657  8.64993  1.000 53.72411  ? 140 GLU A OE2  1 
ATOM   2193 H H    . GLU A 1 154 ? 26.18856  0.89536   12.54741 1.000 42.41824  ? 140 GLU A H    1 
ATOM   2194 H HA   . GLU A 1 154 ? 26.95344  2.79110   10.95608 1.000 46.91262  ? 140 GLU A HA   1 
ATOM   2195 H HB2  . GLU A 1 154 ? 25.23396  0.62694   10.39802 1.000 43.84562  ? 140 GLU A HB2  1 
ATOM   2196 H HB3  . GLU A 1 154 ? 25.80820  1.58590   9.26840  1.000 43.84562  ? 140 GLU A HB3  1 
ATOM   2197 H HG2  . GLU A 1 154 ? 27.96919  0.83196   9.78257  1.000 54.61329  ? 140 GLU A HG2  1 
ATOM   2198 H HG3  . GLU A 1 154 ? 27.33517  -0.19236  10.81901 1.000 54.61329  ? 140 GLU A HG3  1 
ATOM   2199 N N    . TYR A 1 155 ? 25.11586  4.31872   10.30001 1.000 31.79284  ? 141 TYR A N    1 
ATOM   2200 C CA   . TYR A 1 155 ? 24.02582  5.25415   10.03431 1.000 29.04997  ? 141 TYR A CA   1 
ATOM   2201 C C    . TYR A 1 155 ? 23.29264  4.75872   8.79561  1.000 32.31379  ? 141 TYR A C    1 
ATOM   2202 O O    . TYR A 1 155 ? 23.64369  5.08973   7.66224  1.000 31.97308  ? 141 TYR A O    1 
ATOM   2203 C CB   . TYR A 1 155 ? 24.54833  6.67178   9.84652  1.000 23.49499  ? 141 TYR A CB   1 
ATOM   2204 C CG   . TYR A 1 155 ? 23.43673  7.68263   9.70884  1.000 24.19418  ? 141 TYR A CG   1 
ATOM   2205 C CD1  . TYR A 1 155 ? 22.81240  8.20586   10.83068 1.000 24.68162  ? 141 TYR A CD1  1 
ATOM   2206 C CD2  . TYR A 1 155 ? 22.99892  8.10046   8.45830  1.000 26.30315  ? 141 TYR A CD2  1 
ATOM   2207 C CE1  . TYR A 1 155 ? 21.78895  9.12256   10.71632 1.000 26.01409  ? 141 TYR A CE1  1 
ATOM   2208 C CE2  . TYR A 1 155 ? 21.97496  9.01835   8.33201  1.000 25.65894  ? 141 TYR A CE2  1 
ATOM   2209 C CZ   . TYR A 1 155 ? 21.37469  9.52648   9.46617  1.000 27.70794  ? 141 TYR A CZ   1 
ATOM   2210 O OH   . TYR A 1 155 ? 20.35523  10.43992  9.35835  1.000 28.85524  ? 141 TYR A OH   1 
ATOM   2211 H H    . TYR A 1 155 ? 25.85419  4.52359   9.90949  1.000 38.20735  ? 141 TYR A H    1 
ATOM   2212 H HA   . TYR A 1 155 ? 23.41495  5.25872   10.78778 1.000 34.91590  ? 141 TYR A HA   1 
ATOM   2213 H HB2  . TYR A 1 155 ? 25.08464  6.91640   10.61687 1.000 28.24381  ? 141 TYR A HB2  1 
ATOM   2214 H HB3  . TYR A 1 155 ? 25.08864  6.70626   9.04167  1.000 28.24381  ? 141 TYR A HB3  1 
ATOM   2215 H HD1  . TYR A 1 155 ? 23.08900  7.93352   11.67579 1.000 29.67389  ? 141 TYR A HD1  1 
ATOM   2216 H HD2  . TYR A 1 155 ? 23.40189  7.75648   7.69398  1.000 31.61972  ? 141 TYR A HD2  1 
ATOM   2217 H HE1  . TYR A 1 155 ? 21.38093  9.46599   11.47821 1.000 31.27284  ? 141 TYR A HE1  1 
ATOM   2218 H HE2  . TYR A 1 155 ? 21.69209  9.29196   7.48938  1.000 30.84666  ? 141 TYR A HE2  1 
ATOM   2219 H HH   . TYR A 1 155 ? 20.06430  10.63712  10.12128 1.000 34.68223  ? 141 TYR A HH   1 
ATOM   2220 N N    . ASN A 1 156 ? 22.26346  3.94641   9.01277  1.000 36.65719  ? 142 ASN A N    1 
ATOM   2221 C CA   . ASN A 1 156 ? 21.49181  3.40196   7.90667  1.000 45.74656  ? 142 ASN A CA   1 
ATOM   2222 C C    . ASN A 1 156 ? 20.15887  2.90535   8.44057  1.000 41.28059  ? 142 ASN A C    1 
ATOM   2223 O O    . ASN A 1 156 ? 20.05273  2.49461   9.59962  1.000 38.34098  ? 142 ASN A O    1 
ATOM   2224 C CB   . ASN A 1 156 ? 22.24457  2.26724   7.19798  1.000 43.12210  ? 142 ASN A CB   1 
ATOM   2225 C CG   . ASN A 1 156 ? 22.47774  1.06907   8.09768  1.000 49.25599  ? 142 ASN A CG   1 
ATOM   2226 O OD1  . ASN A 1 156 ? 22.41041  1.17412   9.32270  1.000 53.43507  ? 142 ASN A OD1  1 
ATOM   2227 N ND2  . ASN A 1 156 ? 22.75964  -0.07897  7.49233  1.000 55.15218  ? 142 ASN A ND2  1 
ATOM   2228 H H    . ASN A 1 156 ? 21.99412  3.69713   9.79053  1.000 44.04456  ? 142 ASN A H    1 
ATOM   2229 H HA   . ASN A 1 156 ? 21.31900  4.10100   7.25676  1.000 54.95182  ? 142 ASN A HA   1 
ATOM   2230 H HB2  . ASN A 1 156 ? 21.72542  1.97222   6.43356  1.000 51.80246  ? 142 ASN A HB2  1 
ATOM   2231 H HB3  . ASN A 1 156 ? 23.10905  2.59559   6.90513  1.000 51.80246  ? 142 ASN A HB3  1 
ATOM   2232 H HD21 . ASN A 1 156 ? 22.90021  -0.78778  7.95862  1.000 66.23856  ? 142 ASN A HD21 1 
ATOM   2233 H HD22 . ASN A 1 156 ? 22.80161  -0.11355  6.63405  1.000 66.23856  ? 142 ASN A HD22 1 
ATOM   2234 N N    . GLY A 1 157 ? 19.14303  2.96960   7.58773  1.000 47.24136  ? 143 GLY A N    1 
ATOM   2235 C CA   . GLY A 1 157 ? 17.85664  2.39424   7.90353  1.000 50.76437  ? 143 GLY A CA   1 
ATOM   2236 C C    . GLY A 1 157 ? 17.89589  0.87980   7.81617  1.000 49.06008  ? 143 GLY A C    1 
ATOM   2237 O O    . GLY A 1 157 ? 18.92577  0.25532   7.56006  1.000 52.37537  ? 143 GLY A O    1 
ATOM   2238 H H    . GLY A 1 157 ? 19.18006  3.34541   6.81508  1.000 56.74558  ? 143 GLY A H    1 
ATOM   2239 H HA2  . GLY A 1 157 ? 17.59915  2.64683   8.80397  1.000 60.97318  ? 143 GLY A HA2  1 
ATOM   2240 H HA3  . GLY A 1 157 ? 17.19054  2.72412   7.28032  1.000 60.97318  ? 143 GLY A HA3  1 
ATOM   2241 N N    . TRP A 1 158 ? 16.73229  0.27853   8.03073  1.000 38.80014  ? 144 TRP A N    1 
ATOM   2242 C CA   . TRP A 1 158 ? 16.61485  -1.17169  8.03304  1.000 39.93661  ? 144 TRP A CA   1 
ATOM   2243 C C    . TRP A 1 158 ? 15.14719  -1.53195  7.84792  1.000 40.32848  ? 144 TRP A C    1 
ATOM   2244 O O    . TRP A 1 158 ? 14.28274  -0.66109  7.71887  1.000 36.78188  ? 144 TRP A O    1 
ATOM   2245 C CB   . TRP A 1 158 ? 17.17151  -1.76232  9.33066  1.000 39.35205  ? 144 TRP A CB   1 
ATOM   2246 C CG   . TRP A 1 158 ? 16.34580  -1.39089  10.51118 1.000 35.93623  ? 144 TRP A CG   1 
ATOM   2247 C CD1  . TRP A 1 158 ? 15.32277  -2.10811  11.04619 1.000 34.38687  ? 144 TRP A CD1  1 
ATOM   2248 C CD2  . TRP A 1 158 ? 16.45443  -0.19686  11.29493 1.000 29.74120  ? 144 TRP A CD2  1 
ATOM   2249 N NE1  . TRP A 1 158 ? 14.78696  -1.44156  12.12072 1.000 40.72621  ? 144 TRP A NE1  1 
ATOM   2250 C CE2  . TRP A 1 158 ? 15.46544  -0.26399  12.29443 1.000 37.83930  ? 144 TRP A CE2  1 
ATOM   2251 C CE3  . TRP A 1 158 ? 17.29358  0.91982   11.25023 1.000 39.38538  ? 144 TRP A CE3  1 
ATOM   2252 C CZ2  . TRP A 1 158 ? 15.29232  0.74200   13.24245 1.000 34.68660  ? 144 TRP A CZ2  1 
ATOM   2253 C CZ3  . TRP A 1 158 ? 17.12093  1.91772   12.19298 1.000 36.91083  ? 144 TRP A CZ3  1 
ATOM   2254 C CH2  . TRP A 1 158 ? 16.12805  1.82176   13.17494 1.000 32.42520  ? 144 TRP A CH2  1 
ATOM   2255 H H    . TRP A 1 158 ? 15.99265  0.69180   8.17818  1.000 46.61611  ? 144 TRP A H    1 
ATOM   2256 H HA   . TRP A 1 158 ? 17.11731  -1.53241  7.28584  1.000 47.97987  ? 144 TRP A HA   1 
ATOM   2257 H HB2  . TRP A 1 158 ? 17.18359  -2.72975  9.26108  1.000 47.27840  ? 144 TRP A HB2  1 
ATOM   2258 H HB3  . TRP A 1 158 ? 18.07119  -1.42865  9.47253  1.000 47.27840  ? 144 TRP A HB3  1 
ATOM   2259 H HD1  . TRP A 1 158 ? 15.02806  -2.93161  10.73014 1.000 41.32019  ? 144 TRP A HD1  1 
ATOM   2260 H HE1  . TRP A 1 158 ? 14.13254  -1.71809  12.60535 1.000 48.92739  ? 144 TRP A HE1  1 
ATOM   2261 H HE3  . TRP A 1 158 ? 17.95467  0.99074   10.59997 1.000 47.31839  ? 144 TRP A HE3  1 
ATOM   2262 H HZ2  . TRP A 1 158 ? 14.63356  0.68136   13.89609 1.000 41.67986  ? 144 TRP A HZ2  1 
ATOM   2263 H HZ3  . TRP A 1 158 ? 17.67408  2.66509   12.17390 1.000 44.34894  ? 144 TRP A HZ3  1 
ATOM   2264 H HH2  . TRP A 1 158 ? 16.03479  2.50811   13.79552 1.000 38.96617  ? 144 TRP A HH2  1 
ATOM   2265 N N    . CYS A 1 159 ? 14.87388  -2.83297  7.84109  1.000 41.33896  ? 145 CYS A N    1 
ATOM   2266 C CA   . CYS A 1 159 ? 13.52013  -3.36100  7.75925  1.000 42.15440  ? 145 CYS A CA   1 
ATOM   2267 C C    . CYS A 1 159 ? 13.30964  -4.32341  8.91728  1.000 41.40500  ? 145 CYS A C    1 
ATOM   2268 O O    . CYS A 1 159 ? 14.17602  -5.15820  9.19557  1.000 38.75074  ? 145 CYS A O    1 
ATOM   2269 C CB   . CYS A 1 159 ? 13.28235  -4.07641  6.42343  1.000 40.44854  ? 145 CYS A CB   1 
ATOM   2270 S SG   . CYS A 1 159 ? 13.34489  -3.02534  4.94276  1.000 44.17913  ? 145 CYS A SG   1 
ATOM   2271 N N    . GLY A 1 160 ? 12.17379  -4.20377  9.59439  1.000 38.54161  ? 146 GLY A N    1 
ATOM   2272 C CA   . GLY A 1 160 ? 11.84494  -5.12927  10.65972 1.000 38.50503  ? 146 GLY A CA   1 
ATOM   2273 C C    . GLY A 1 160 ? 12.68544  -4.93100  11.91184 1.000 33.94953  ? 146 GLY A C    1 
ATOM   2274 O O    . GLY A 1 160 ? 13.49522  -4.01224  12.03073 1.000 32.24055  ? 146 GLY A O    1 
ATOM   2275 N N    . ASP A 1 161 ? 12.47057  -5.83079  12.86932 1.000 37.99803  ? 147 ASP A N    1 
ATOM   2276 C CA   . ASP A 1 161 ? 11.50808  -6.92048  12.74879 1.000 33.11334  ? 147 ASP A CA   1 
ATOM   2277 C C    . ASP A 1 161 ? 10.07842  -6.39395  12.78442 1.000 35.39976  ? 147 ASP A C    1 
ATOM   2278 O O    . ASP A 1 161 ? 9.81788   -5.30762  13.30359 1.000 33.92610  ? 147 ASP A O    1 
ATOM   2279 C CB   . ASP A 1 161 ? 11.70808  -7.95139  13.86443 1.000 38.25467  ? 147 ASP A CB   1 
ATOM   2280 C CG   . ASP A 1 161 ? 13.04506  -8.66372  13.77589 1.000 42.27392  ? 147 ASP A CG   1 
ATOM   2281 O OD1  . ASP A 1 161 ? 13.83951  -8.34367  12.86686 1.000 40.77952  ? 147 ASP A OD1  1 
ATOM   2282 O OD2  . ASP A 1 161 ? 13.29843  -9.54912  14.62151 1.000 44.28663  ? 147 ASP A OD2  1 
ATOM   2283 N N    . ASN A 1 162 ? 9.16056   -7.17741  12.22216 1.000 33.81994  ? 148 ASN A N    1 
ATOM   2284 C CA   . ASN A 1 162 ? 7.75319   -6.80611  12.20689 1.000 30.76513  ? 148 ASN A CA   1 
ATOM   2285 C C    . ASN A 1 162 ? 7.26774   -6.47358  13.61131 1.000 33.14824  ? 148 ASN A C    1 
ATOM   2286 O O    . ASN A 1 162 ? 7.64900   -7.12101  14.59011 1.000 30.68958  ? 148 ASN A O    1 
ATOM   2287 C CB   . ASN A 1 162 ? 6.92182   -7.94737  11.61832 1.000 33.01713  ? 148 ASN A CB   1 
ATOM   2288 C CG   . ASN A 1 162 ? 7.24496   -8.20854  10.16065 1.000 33.81311  ? 148 ASN A CG   1 
ATOM   2289 O OD1  . ASN A 1 162 ? 7.46968   -7.27693  9.38697  1.000 30.69263  ? 148 ASN A OD1  1 
ATOM   2290 N ND2  . ASN A 1 162 ? 7.27635   -9.48004  9.77942  1.000 33.23005  ? 148 ASN A ND2  1 
ATOM   2291 H H    . ASN A 1 162 ? 9.32924   -7.93040  11.84248 1.000 40.63987  ? 148 ASN A H    1 
ATOM   2292 H HA   . ASN A 1 162 ? 7.63269   -6.01968  11.65201 1.000 36.97410  ? 148 ASN A HA   1 
ATOM   2293 H HB2  . ASN A 1 162 ? 7.10113   -8.76001  12.11668 1.000 39.67650  ? 148 ASN A HB2  1 
ATOM   2294 H HB3  . ASN A 1 162 ? 5.98103   -7.71989  11.68201 1.000 39.67650  ? 148 ASN A HB3  1 
ATOM   2295 H HD21 . ASN A 1 162 ? 7.45516   -9.67965  8.96224  1.000 39.93200  ? 148 ASN A HD21 1 
ATOM   2296 H HD22 . ASN A 1 162 ? 7.11788   -10.10397 10.34968 1.000 39.93200  ? 148 ASN A HD22 1 
ATOM   2297 N N    . VAL A 1 163 ? 6.41969   -5.45239  13.70247 1.000 28.76831  ? 149 VAL A N    1 
ATOM   2298 C CA   . VAL A 1 163 ? 5.85662   -5.01305  14.97397 1.000 33.30429  ? 149 VAL A CA   1 
ATOM   2299 C C    . VAL A 1 163 ? 4.62007   -5.86595  15.24015 1.000 32.51619  ? 149 VAL A C    1 
ATOM   2300 O O    . VAL A 1 163 ? 3.53230   -5.57875  14.74104 1.000 28.64025  ? 149 VAL A O    1 
ATOM   2301 C CB   . VAL A 1 163 ? 5.52187   -3.52148  14.95851 1.000 31.41500  ? 149 VAL A CB   1 
ATOM   2302 C CG1  . VAL A 1 163 ? 4.91643   -3.10693  16.28790 1.000 28.34403  ? 149 VAL A CG1  1 
ATOM   2303 C CG2  . VAL A 1 163 ? 6.77059   -2.70081  14.64486 1.000 29.38915  ? 149 VAL A CG2  1 
ATOM   2304 H H    . VAL A 1 163 ? 6.15096   -4.99031  13.02878 1.000 34.57791  ? 149 VAL A H    1 
ATOM   2305 H HA   . VAL A 1 163 ? 6.50022   -5.17678  15.68098 1.000 40.02109  ? 149 VAL A HA   1 
ATOM   2306 H HB   . VAL A 1 163 ? 4.86838   -3.34592  14.26351 1.000 37.75394  ? 149 VAL A HB   1 
ATOM   2307 H HG11 . VAL A 1 163 ? 5.27644   -3.67249  16.98893 1.000 34.06877  ? 149 VAL A HG11 1 
ATOM   2308 H HG12 . VAL A 1 163 ? 5.14211   -2.17981  16.46228 1.000 34.06877  ? 149 VAL A HG12 1 
ATOM   2309 H HG13 . VAL A 1 163 ? 3.95300   -3.20985  16.24193 1.000 34.06877  ? 149 VAL A HG13 1 
ATOM   2310 H HG21 . VAL A 1 163 ? 6.56003   -1.75828  14.73540 1.000 35.32292  ? 149 VAL A HG21 1 
ATOM   2311 H HG22 . VAL A 1 163 ? 7.47312   -2.94414  15.26787 1.000 35.32292  ? 149 VAL A HG22 1 
ATOM   2312 H HG23 . VAL A 1 163 ? 7.05346   -2.89079  13.73668 1.000 35.32292  ? 149 VAL A HG23 1 
ATOM   2313 N N    . TYR A 1 164 ? 4.78705   -6.91786  16.03665 1.000 28.24299  ? 150 TYR A N    1 
ATOM   2314 C CA   . TYR A 1 164 ? 3.68093   -7.80720  16.36738 1.000 28.67374  ? 150 TYR A CA   1 
ATOM   2315 C C    . TYR A 1 164 ? 2.79208   -7.14199  17.40949 1.000 26.54922  ? 150 TYR A C    1 
ATOM   2316 O O    . TYR A 1 164 ? 3.25067   -6.81494  18.50828 1.000 26.37431  ? 150 TYR A O    1 
ATOM   2317 C CB   . TYR A 1 164 ? 4.21030   -9.15067  16.86343 1.000 31.09140  ? 150 TYR A CB   1 
ATOM   2318 C CG   . TYR A 1 164 ? 4.53849   -10.09399 15.73128 1.000 29.02404  ? 150 TYR A CG   1 
ATOM   2319 C CD1  . TYR A 1 164 ? 5.65824   -9.89074  14.93754 1.000 33.58098  ? 150 TYR A CD1  1 
ATOM   2320 C CD2  . TYR A 1 164 ? 3.71825   -11.17729 15.44302 1.000 29.12462  ? 150 TYR A CD2  1 
ATOM   2321 C CE1  . TYR A 1 164 ? 5.95800   -10.74355 13.89208 1.000 31.40939  ? 150 TYR A CE1  1 
ATOM   2322 C CE2  . TYR A 1 164 ? 4.00994   -12.03645 14.40069 1.000 31.66521  ? 150 TYR A CE2  1 
ATOM   2323 C CZ   . TYR A 1 164 ? 5.13095   -11.81330 13.62799 1.000 32.36318  ? 150 TYR A CZ   1 
ATOM   2324 O OH   . TYR A 1 164 ? 5.42943   -12.66123 12.58682 1.000 37.68809  ? 150 TYR A OH   1 
ATOM   2325 H H    . TYR A 1 164 ? 5.53508   -7.13812  16.39933 1.000 33.94753  ? 150 TYR A H    1 
ATOM   2326 H HA   . TYR A 1 164 ? 3.14548   -7.97366  15.57587 1.000 34.46443  ? 150 TYR A HA   1 
ATOM   2327 H HB2  . TYR A 1 164 ? 5.01980   -9.00236  17.37687 1.000 37.36562  ? 150 TYR A HB2  1 
ATOM   2328 H HB3  . TYR A 1 164 ? 3.53642   -9.57077  17.42047 1.000 37.36562  ? 150 TYR A HB3  1 
ATOM   2329 H HD1  . TYR A 1 164 ? 6.21686   -9.16798  15.11208 1.000 40.35312  ? 150 TYR A HD1  1 
ATOM   2330 H HD2  . TYR A 1 164 ? 2.95996   -11.32692 15.96023 1.000 35.00548  ? 150 TYR A HD2  1 
ATOM   2331 H HE1  . TYR A 1 164 ? 6.71341   -10.59619 13.37002 1.000 37.74721  ? 150 TYR A HE1  1 
ATOM   2332 H HE2  . TYR A 1 164 ? 3.45428   -12.76029 14.22126 1.000 38.05420  ? 150 TYR A HE2  1 
ATOM   2333 H HH   . TYR A 1 164 ? 6.16204   -12.44234 12.23901 1.000 45.28165  ? 150 TYR A HH   1 
ATOM   2334 N N    . ILE A 1 165 ? 1.52329   -6.94174  17.06080 1.000 29.95495  ? 151 ILE A N    1 
ATOM   2335 C CA   . ILE A 1 165 ? 0.57112   -6.21367  17.88937 1.000 29.69471  ? 151 ILE A CA   1 
ATOM   2336 C C    . ILE A 1 165 ? -0.44484  -7.19701  18.45110 1.000 31.86895  ? 151 ILE A C    1 
ATOM   2337 O O    . ILE A 1 165 ? -0.89754  -8.11064  17.75060 1.000 29.45005  ? 151 ILE A O    1 
ATOM   2338 C CB   . ILE A 1 165 ? -0.12152  -5.09354  17.08474 1.000 31.34525  ? 151 ILE A CB   1 
ATOM   2339 C CG1  . ILE A 1 165 ? 0.92886   -4.11090  16.55303 1.000 29.38563  ? 151 ILE A CG1  1 
ATOM   2340 C CG2  . ILE A 1 165 ? -1.15942  -4.37483  17.94357 1.000 33.72360  ? 151 ILE A CG2  1 
ATOM   2341 C CD1  . ILE A 1 165 ? 0.35741   -2.92211  15.80247 1.000 31.15411  ? 151 ILE A CD1  1 
ATOM   2342 H H    . ILE A 1 165 ? 1.18209   -7.22807  16.32514 1.000 36.00189  ? 151 ILE A H    1 
ATOM   2343 H HA   . ILE A 1 165 ? 1.03800   -5.80889  18.63709 1.000 35.68959  ? 151 ILE A HA   1 
ATOM   2344 H HB   . ILE A 1 165 ? -0.58445  -5.49087  16.33059 1.000 37.67024  ? 151 ILE A HB   1 
ATOM   2345 H HG12 . ILE A 1 165 ? 1.43719   -3.76613  17.30379 1.000 35.31870  ? 151 ILE A HG12 1 
ATOM   2346 H HG13 . ILE A 1 165 ? 1.51636   -4.58610  15.94482 1.000 35.31870  ? 151 ILE A HG13 1 
ATOM   2347 H HG21 . ILE A 1 165 ? -0.71485  -3.97401  18.70685 1.000 40.52426  ? 151 ILE A HG21 1 
ATOM   2348 H HG22 . ILE A 1 165 ? -1.58780  -3.68638  17.41119 1.000 40.52426  ? 151 ILE A HG22 1 
ATOM   2349 H HG23 . ILE A 1 165 ? -1.81960  -5.01815  18.24556 1.000 40.52426  ? 151 ILE A HG23 1 
ATOM   2350 H HD11 . ILE A 1 165 ? -0.07710  -2.32860  16.43479 1.000 37.44087  ? 151 ILE A HD11 1 
ATOM   2351 H HD12 . ILE A 1 165 ? 1.07947   -2.45550  15.35324 1.000 37.44087  ? 151 ILE A HD12 1 
ATOM   2352 H HD13 . ILE A 1 165 ? -0.28687  -3.24011  15.15080 1.000 37.44087  ? 151 ILE A HD13 1 
ATOM   2353 N N    . THR A 1 166 ? -0.79461  -7.00916  19.72239 1.000 29.90189  ? 152 THR A N    1 
ATOM   2354 C CA   . THR A 1 166 ? -1.80111  -7.81322  20.39747 1.000 30.88028  ? 152 THR A CA   1 
ATOM   2355 C C    . THR A 1 166 ? -2.73814  -6.89838  21.17198 1.000 31.52895  ? 152 THR A C    1 
ATOM   2356 O O    . THR A 1 166 ? -2.34384  -5.82292  21.63069 1.000 33.19606  ? 152 THR A O    1 
ATOM   2357 C CB   . THR A 1 166 ? -1.17130  -8.83351  21.36133 1.000 34.46920  ? 152 THR A CB   1 
ATOM   2358 O OG1  . THR A 1 166 ? -0.23879  -8.16900  22.22512 1.000 39.80731  ? 152 THR A OG1  1 
ATOM   2359 C CG2  . THR A 1 166 ? -0.46144  -9.93403  20.59047 1.000 31.82096  ? 152 THR A CG2  1 
ATOM   2360 H H    . THR A 1 166 ? -0.45067  -6.40320  20.22648 1.000 35.93821  ? 152 THR A H    1 
ATOM   2361 H HA   . THR A 1 166 ? -2.31549  -8.30261  19.73655 1.000 36.82838  ? 152 THR A HA   1 
ATOM   2362 H HB   . THR A 1 166 ? -1.86768  -9.24370  21.89772 1.000 41.41898  ? 152 THR A HB   1 
ATOM   2363 H HG1  . THR A 1 166 ? 0.09566   -8.71931  22.76447 1.000 47.82471  ? 152 THR A HG1  1 
ATOM   2364 H HG21 . THR A 1 166 ? -1.09128  -10.39497 20.01451 1.000 38.24109  ? 152 THR A HG21 1 
ATOM   2365 H HG22 . THR A 1 166 ? 0.24468   -9.55425  20.04452 1.000 38.24109  ? 152 THR A HG22 1 
ATOM   2366 H HG23 . THR A 1 166 ? -0.07279  -10.57365 21.20751 1.000 38.24109  ? 152 THR A HG23 1 
ATOM   2367 N N    . ALA A 1 167 ? -3.98341  -7.33876  21.31685 1.000 36.93434  ? 153 ALA A N    1 
ATOM   2368 C CA   . ALA A 1 167 ? -4.97763  -6.56304  22.03957 1.000 37.30790  ? 153 ALA A CA   1 
ATOM   2369 C C    . ALA A 1 167 ? -4.76708  -6.68925  23.54303 1.000 38.14181  ? 153 ALA A C    1 
ATOM   2370 O O    . ALA A 1 167 ? -4.35930  -7.73716  24.05097 1.000 42.05387  ? 153 ALA A O    1 
ATOM   2371 C CB   . ALA A 1 167 ? -6.38875  -7.02196  21.67302 1.000 35.99038  ? 153 ALA A CB   1 
ATOM   2372 H H    . ALA A 1 167 ? -4.27591  -8.08486  21.00480 1.000 44.37715  ? 153 ALA A H    1 
ATOM   2373 H HA   . ALA A 1 167 ? -4.89296  -5.62746  21.79786 1.000 44.82542  ? 153 ALA A HA   1 
ATOM   2374 H HB1  . ALA A 1 167 ? -6.58674  -6.74058  20.76609 1.000 43.24440  ? 153 ALA A HB1  1 
ATOM   2375 H HB2  . ALA A 1 167 ? -6.43282  -7.98888  21.73643 1.000 43.24440  ? 153 ALA A HB2  1 
ATOM   2376 H HB3  . ALA A 1 167 ? -7.02134  -6.62087  22.28934 1.000 43.24440  ? 153 ALA A HB3  1 
ATOM   2377 N N    . ASP A 1 168 ? -5.04947  -5.59816  24.25427 1.000 38.94966  ? 154 ASP A N    1 
ATOM   2378 C CA   . ASP A 1 168 ? -4.96348  -5.53698  25.71445 1.000 43.21809  ? 154 ASP A CA   1 
ATOM   2379 C C    . ASP A 1 168 ? -6.28941  -4.96084  26.20383 1.000 44.20710  ? 154 ASP A C    1 
ATOM   2380 O O    . ASP A 1 168 ? -6.41859  -3.74820  26.39435 1.000 42.20175  ? 154 ASP A O    1 
ATOM   2381 C CB   . ASP A 1 168 ? -3.77157  -4.69636  26.15996 1.000 44.60758  ? 154 ASP A CB   1 
ATOM   2382 C CG   . ASP A 1 168 ? -3.57254  -4.70961  27.66381 1.000 50.17804  ? 154 ASP A CG   1 
ATOM   2383 O OD1  . ASP A 1 168 ? -4.38598  -5.33622  28.37592 1.000 54.73662  ? 154 ASP A OD1  1 
ATOM   2384 O OD2  . ASP A 1 168 ? -2.59440  -4.09154  28.13342 1.000 51.17271  ? 154 ASP A OD2  1 
ATOM   2385 H H    . ASP A 1 168 ? -5.30167  -4.85557  23.90135 1.000 46.79553  ? 154 ASP A H    1 
ATOM   2386 H HA   . ASP A 1 168 ? -4.85117  -6.42842  26.07998 1.000 51.91764  ? 154 ASP A HA   1 
ATOM   2387 H HB2  . ASP A 1 168 ? -2.96629  -5.04652  25.74787 1.000 53.58504  ? 154 ASP A HB2  1 
ATOM   2388 H HB3  . ASP A 1 168 ? -3.91255  -3.77711  25.88429 1.000 53.58504  ? 154 ASP A HB3  1 
ATOM   2389 N N    . LYS A 1 169 ? -7.27578  -5.83835  26.40125 1.000 42.16580  ? 155 LYS A N    1 
ATOM   2390 C CA   . LYS A 1 169 ? -8.61328  -5.38082  26.76183 1.000 48.67412  ? 155 LYS A CA   1 
ATOM   2391 C C    . LYS A 1 169 ? -8.63845  -4.73724  28.14299 1.000 48.91078  ? 155 LYS A C    1 
ATOM   2392 O O    . LYS A 1 169 ? -9.45431  -3.84161  28.38964 1.000 51.68880  ? 155 LYS A O    1 
ATOM   2393 C CB   . LYS A 1 169 ? -9.59514  -6.55245  26.69669 1.000 45.69751  ? 155 LYS A CB   1 
ATOM   2394 C CG   . LYS A 1 169 ? -10.98605 -6.17324  26.21384 1.000 56.53604  ? 155 LYS A CG   1 
ATOM   2395 C CD   . LYS A 1 169 ? -11.84680 -5.62861  27.33957 1.000 63.43877  ? 155 LYS A CD   1 
ATOM   2396 C CE   . LYS A 1 169 ? -12.38493 -6.75430  28.20662 1.000 67.93287  ? 155 LYS A CE   1 
ATOM   2397 N NZ   . LYS A 1 169 ? -13.20780 -7.70655  27.40884 1.000 66.48945  ? 155 LYS A NZ   1 
ATOM   2398 H H    . LYS A 1 169 ? -7.19612  -6.69194  26.33319 1.000 50.65489  ? 155 LYS A H    1 
ATOM   2399 H HA   . LYS A 1 169 ? -8.89996  -4.71085  26.12163 1.000 58.46488  ? 155 LYS A HA   1 
ATOM   2400 N N    . GLN A 1 170 ? -7.76187  -5.17379  29.05176 1.000 53.70027  ? 156 GLN A N    1 
ATOM   2401 C CA   . GLN A 1 170 ? -7.70291  -4.56455  30.37792 1.000 57.35665  ? 156 GLN A CA   1 
ATOM   2402 C C    . GLN A 1 170 ? -7.45691  -3.06490  30.27851 1.000 57.82817  ? 156 GLN A C    1 
ATOM   2403 O O    . GLN A 1 170 ? -8.14468  -2.26391  30.92246 1.000 54.85441  ? 156 GLN A O    1 
ATOM   2404 C CB   . GLN A 1 170 ? -6.60490  -5.22340  31.21345 1.000 62.60872  ? 156 GLN A CB   1 
ATOM   2405 C CG   . GLN A 1 170 ? -7.11290  -6.08307  32.35683 1.000 67.80725  ? 156 GLN A CG   1 
ATOM   2406 C CD   . GLN A 1 170 ? -6.01192  -6.45264  33.33394 1.000 75.00431  ? 156 GLN A CD   1 
ATOM   2407 O OE1  . GLN A 1 170 ? -5.46440  -5.59120  34.02225 1.000 70.60425  ? 156 GLN A OE1  1 
ATOM   2408 N NE2  . GLN A 1 170 ? -5.67670  -7.73657  33.39343 1.000 75.71646  ? 156 GLN A NE2  1 
ATOM   2409 H H    . GLN A 1 170 ? -7.19927  -5.81195  28.92587 1.000 64.49627  ? 156 GLN A H    1 
ATOM   2410 H HA   . GLN A 1 170 ? -8.55276  -4.70996  30.82235 1.000 68.88393  ? 156 GLN A HA   1 
ATOM   2411 H HB2  . GLN A 1 170 ? -6.07435  -5.79154  30.63325 1.000 75.18640  ? 156 GLN A HB2  1 
ATOM   2412 H HB3  . GLN A 1 170 ? -6.04800  -4.52718  31.59560 1.000 75.18640  ? 156 GLN A HB3  1 
ATOM   2413 H HG2  . GLN A 1 170 ? -7.79587  -5.59460  32.84248 1.000 81.42464  ? 156 GLN A HG2  1 
ATOM   2414 H HG3  . GLN A 1 170 ? -7.48457  -6.90347  31.99668 1.000 81.42464  ? 156 GLN A HG3  1 
ATOM   2415 H HE21 . GLN A 1 170 ? -6.07825  -8.30945  32.89327 1.000 90.91570  ? 156 GLN A HE21 1 
ATOM   2416 H HE22 . GLN A 1 170 ? -5.05811  -7.99497  33.93212 1.000 90.91570  ? 156 GLN A HE22 1 
ATOM   2417 N N    . LYS A 1 171 ? -6.46946  -2.66938  29.47999 1.000 51.60960  ? 157 LYS A N    1 
ATOM   2418 C CA   . LYS A 1 171 ? -6.12662  -1.26903  29.28392 1.000 48.79174  ? 157 LYS A CA   1 
ATOM   2419 C C    . LYS A 1 171 ? -6.93110  -0.61536  28.16841 1.000 46.05942  ? 157 LYS A C    1 
ATOM   2420 O O    . LYS A 1 171 ? -6.69880  0.55921   27.86553 1.000 43.16862  ? 157 LYS A O    1 
ATOM   2421 C CB   . LYS A 1 171 ? -4.63237  -1.13262  28.96669 1.000 49.44218  ? 157 LYS A CB   1 
ATOM   2422 C CG   . LYS A 1 171 ? -3.68808  -1.78081  29.97869 1.000 53.03781  ? 157 LYS A CG   1 
ATOM   2423 C CD   . LYS A 1 171 ? -3.26723  -0.82200  31.08630 1.000 52.75370  ? 157 LYS A CD   1 
ATOM   2424 C CE   . LYS A 1 171 ? -4.19360  -0.89902  32.28831 1.000 57.89286  ? 157 LYS A CE   1 
ATOM   2425 N NZ   . LYS A 1 171 ? -3.82071  0.09197   33.33836 1.000 60.26415  ? 157 LYS A NZ   1 
ATOM   2426 H H    . LYS A 1 171 ? -5.97258  -3.20868  29.03072 1.000 61.98746  ? 157 LYS A H    1 
ATOM   2427 H HA   . LYS A 1 171 ? -6.30737  -0.79105  30.10840 1.000 58.60602  ? 157 LYS A HA   1 
ATOM   2428 H HB2  . LYS A 1 171 ? -4.46335  -1.54714  28.10617 1.000 59.38656  ? 157 LYS A HB2  1 
ATOM   2429 H HB3  . LYS A 1 171 ? -4.41268  -0.18857  28.92906 1.000 59.38656  ? 157 LYS A HB3  1 
ATOM   2430 H HG2  . LYS A 1 171 ? -4.13514  -2.53691  30.39021 1.000 63.70131  ? 157 LYS A HG2  1 
ATOM   2431 H HG3  . LYS A 1 171 ? -2.88731  -2.07865  29.51939 1.000 63.70131  ? 157 LYS A HG3  1 
ATOM   2432 H HD2  . LYS A 1 171 ? -2.37066  -1.04723  31.38013 1.000 63.36037  ? 157 LYS A HD2  1 
ATOM   2433 H HD3  . LYS A 1 171 ? -3.28669  0.08645   30.74681 1.000 63.36037  ? 157 LYS A HD3  1 
ATOM   2434 H HE2  . LYS A 1 171 ? -5.10240  -0.71356  32.00444 1.000 69.52737  ? 157 LYS A HE2  1 
ATOM   2435 H HE3  . LYS A 1 171 ? -4.14175  -1.78665  32.67603 1.000 69.52737  ? 157 LYS A HE3  1 
ATOM   2436 H HZ1  . LYS A 1 171 ? -2.94629  0.05077   33.49901 1.000 72.37291  ? 157 LYS A HZ1  1 
ATOM   2437 H HZ2  . LYS A 1 171 ? -4.02615  0.91444   33.06739 1.000 72.37291  ? 157 LYS A HZ2  1 
ATOM   2438 H HZ3  . LYS A 1 171 ? -4.26132  -0.08244  34.09171 1.000 72.37291  ? 157 LYS A HZ3  1 
ATOM   2439 N N    . ASN A 1 172 ? -7.86178  -1.34103  27.54898 1.000 51.29116  ? 158 ASN A N    1 
ATOM   2440 C CA   . ASN A 1 172 ? -8.58784  -0.83681  26.38502 1.000 47.89529  ? 158 ASN A CA   1 
ATOM   2441 C C    . ASN A 1 172 ? -7.61129  -0.32995  25.32621 1.000 43.79087  ? 158 ASN A C    1 
ATOM   2442 O O    . ASN A 1 172 ? -7.84436  0.68142   24.66227 1.000 47.27989  ? 158 ASN A O    1 
ATOM   2443 C CB   . ASN A 1 172 ? -9.57398  0.26099   26.78645 1.000 49.49003  ? 158 ASN A CB   1 
ATOM   2444 C CG   . ASN A 1 172 ? -10.52664 0.62856   25.66390 1.000 52.62725  ? 158 ASN A CG   1 
ATOM   2445 O OD1  . ASN A 1 172 ? -11.04590 -0.24214  24.96445 1.000 47.42100  ? 158 ASN A OD1  1 
ATOM   2446 N ND2  . ASN A 1 172 ? -10.75149 1.92522   25.47862 1.000 53.79128  ? 158 ASN A ND2  1 
ATOM   2447 H H    . ASN A 1 172 ? -8.09227  -2.13489  27.78618 1.000 61.60533  ? 158 ASN A H    1 
ATOM   2448 H HA   . ASN A 1 172 ? -9.09882  -1.56478  25.99790 1.000 57.53029  ? 158 ASN A HA   1 
ATOM   2449 H HB2  . ASN A 1 172 ? -10.10173 -0.04739  27.53963 1.000 59.44397  ? 158 ASN A HB2  1 
ATOM   2450 H HB3  . ASN A 1 172 ? -9.07813  1.05746   27.03272 1.000 59.44397  ? 158 ASN A HB3  1 
ATOM   2451 H HD21 . ASN A 1 172 ? -11.28381 2.18452   24.85493 1.000 64.60548  ? 158 ASN A HD21 1 
ATOM   2452 H HD22 . ASN A 1 172 ? -10.36467 2.50501   25.98243 1.000 64.60548  ? 158 ASN A HD22 1 
ATOM   2453 N N    . GLY A 1 173 ? -6.49813  -1.04142  25.17395 1.000 36.32185  ? 159 GLY A N    1 
ATOM   2454 C CA   . GLY A 1 173 ? -5.45009  -0.64448  24.25391 1.000 38.83502  ? 159 GLY A CA   1 
ATOM   2455 C C    . GLY A 1 173 ? -4.79417  -1.84549  23.61880 1.000 36.76054  ? 159 GLY A C    1 
ATOM   2456 O O    . GLY A 1 173 ? -5.46039  -2.85032  23.34553 1.000 35.31658  ? 159 GLY A O    1 
ATOM   2457 H H    . GLY A 1 173 ? -6.32731  -1.76844  25.60040 1.000 43.64216  ? 159 GLY A H    1 
ATOM   2458 H HA2  . GLY A 1 173 ? -5.82599  -0.08917  23.55303 1.000 46.65797  ? 159 GLY A HA2  1 
ATOM   2459 H HA3  . GLY A 1 173 ? -4.77426  -0.13734  24.73031 1.000 46.65797  ? 159 GLY A HA3  1 
ATOM   2460 N N    . ILE A 1 174 ? -3.48447  -1.75278  23.38911 1.000 34.90341  ? 160 ILE A N    1 
ATOM   2461 C CA   . ILE A 1 174 ? -2.72767  -2.78687  22.69955 1.000 35.48667  ? 160 ILE A CA   1 
ATOM   2462 C C    . ILE A 1 174 ? -1.34421  -2.89686  23.32634 1.000 34.26567  ? 160 ILE A C    1 
ATOM   2463 O O    . ILE A 1 174 ? -0.89583  -2.02141  24.06873 1.000 32.19300  ? 160 ILE A O    1 
ATOM   2464 C CB   . ILE A 1 174 ? -2.59322  -2.50132  21.18865 1.000 32.17331  ? 160 ILE A CB   1 
ATOM   2465 C CG1  . ILE A 1 174 ? -2.01134  -1.10280  20.97262 1.000 34.36731  ? 160 ILE A CG1  1 
ATOM   2466 C CG2  . ILE A 1 174 ? -3.93748  -2.63397  20.50184 1.000 33.62739  ? 160 ILE A CG2  1 
ATOM   2467 C CD1  . ILE A 1 174 ? -1.12846  -0.98326  19.75354 1.000 35.69787  ? 160 ILE A CD1  1 
ATOM   2468 H H    . ILE A 1 174 ? -3.00411  -1.08171  23.63102 1.000 41.94003  ? 160 ILE A H    1 
ATOM   2469 H HA   . ILE A 1 174 ? -3.18388  -3.63433  22.82033 1.000 42.63994  ? 160 ILE A HA   1 
ATOM   2470 H HB   . ILE A 1 174 ? -1.98886  -3.15351  20.80096 1.000 38.66392  ? 160 ILE A HB   1 
ATOM   2471 H HG12 . ILE A 1 174 ? -2.74318  -0.47467  20.86895 1.000 41.29671  ? 160 ILE A HG12 1 
ATOM   2472 H HG13 . ILE A 1 174 ? -1.47769  -0.86554  21.74711 1.000 41.29671  ? 160 ILE A HG13 1 
ATOM   2473 H HG21 . ILE A 1 174 ? -3.83528  -2.41428  19.56259 1.000 40.40881  ? 160 ILE A HG21 1 
ATOM   2474 H HG22 . ILE A 1 174 ? -4.25136  -3.54697  20.59574 1.000 40.40881  ? 160 ILE A HG22 1 
ATOM   2475 H HG23 . ILE A 1 174 ? -4.56623  -2.02360  20.91780 1.000 40.40881  ? 160 ILE A HG23 1 
ATOM   2476 H HD11 . ILE A 1 174 ? -0.59031  -0.17994  19.83091 1.000 42.89339  ? 160 ILE A HD11 1 
ATOM   2477 H HD12 . ILE A 1 174 ? -0.55357  -1.76286  19.70229 1.000 42.89339  ? 160 ILE A HD12 1 
ATOM   2478 H HD13 . ILE A 1 174 ? -1.68753  -0.93196  18.96253 1.000 42.89339  ? 160 ILE A HD13 1 
ATOM   2479 N N    . LYS A 1 175 ? -0.66922  -3.99598  23.00617 1.000 30.98660  ? 161 LYS A N    1 
ATOM   2480 C CA   . LYS A 1 175 ? 0.73994   -4.18492  23.30686 1.000 31.11406  ? 161 LYS A CA   1 
ATOM   2481 C C    . LYS A 1 175 ? 1.43506   -4.62310  22.02619 1.000 32.41775  ? 161 LYS A C    1 
ATOM   2482 O O    . LYS A 1 175 ? 0.80575   -5.15332  21.10688 1.000 30.36246  ? 161 LYS A O    1 
ATOM   2483 C CB   . LYS A 1 175 ? 0.95512   -5.22255  24.42031 1.000 31.28482  ? 161 LYS A CB   1 
ATOM   2484 C CG   . LYS A 1 175 ? 0.36639   -4.82061  25.76998 1.000 33.18419  ? 161 LYS A CG   1 
ATOM   2485 C CD   . LYS A 1 175 ? 0.37485   -5.98405  26.75787 1.000 48.06310  ? 161 LYS A CD   1 
ATOM   2486 C CE   . LYS A 1 175 ? 1.49043   -5.85493  27.78373 1.000 56.82424  ? 161 LYS A CE   1 
ATOM   2487 N NZ   . LYS A 1 175 ? 1.27805   -4.69936  28.70241 1.000 56.34032  ? 161 LYS A NZ   1 
ATOM   2488 H H    . LYS A 1 175 ? -1.02033  -4.66799  22.60031 1.000 37.23986  ? 161 LYS A H    1 
ATOM   2489 H HA   . LYS A 1 175 ? 1.13486   -3.35388  23.61398 1.000 37.39281  ? 161 LYS A HA   1 
ATOM   2490 H HB2  . LYS A 1 175 ? 0.53691   -6.05593  24.15295 1.000 37.59773  ? 161 LYS A HB2  1 
ATOM   2491 H HB3  . LYS A 1 175 ? 1.90844   -5.35388  24.54214 1.000 37.59773  ? 161 LYS A HB3  1 
ATOM   2492 H HG2  . LYS A 1 175 ? 0.89236   -4.09792  26.14678 1.000 39.87696  ? 161 LYS A HG2  1 
ATOM   2493 H HG3  . LYS A 1 175 ? -0.55180  -4.53324  25.64647 1.000 39.87696  ? 161 LYS A HG3  1 
ATOM   2494 H HD2  . LYS A 1 175 ? -0.47102  -6.00612  27.23213 1.000 57.73166  ? 161 LYS A HD2  1 
ATOM   2495 H HD3  . LYS A 1 175 ? 0.50485   -6.81380  26.27257 1.000 57.73166  ? 161 LYS A HD3  1 
ATOM   2496 H HE2  . LYS A 1 175 ? 1.52694   -6.66348  28.31834 1.000 68.24502  ? 161 LYS A HE2  1 
ATOM   2497 H HE3  . LYS A 1 175 ? 2.33372   -5.72367  27.32271 1.000 68.24502  ? 161 LYS A HE3  1 
ATOM   2498 H HZ1  . LYS A 1 175 ? 1.93333   -4.66402  29.30363 1.000 67.66432  ? 161 LYS A HZ1  1 
ATOM   2499 H HZ2  . LYS A 1 175 ? 1.26995   -3.93956  28.23901 1.000 67.66432  ? 161 LYS A HZ2  1 
ATOM   2500 H HZ3  . LYS A 1 175 ? 0.50084   -4.78696  29.12710 1.000 67.66432  ? 161 LYS A HZ3  1 
ATOM   2501 N N    . ALA A 1 176 ? 2.74016   -4.37955  21.96027 1.000 31.15782  ? 162 ALA A N    1 
ATOM   2502 C CA   . ALA A 1 176 ? 3.52522   -4.78874  20.80794 1.000 32.26397  ? 162 ALA A CA   1 
ATOM   2503 C C    . ALA A 1 176 ? 4.90716   -5.22503  21.26590 1.000 33.76721  ? 162 ALA A C    1 
ATOM   2504 O O    . ALA A 1 176 ? 5.42751   -4.74855  22.27844 1.000 28.32877  ? 162 ALA A O    1 
ATOM   2505 C CB   . ALA A 1 176 ? 3.63838   -3.66697  19.76480 1.000 27.91781  ? 162 ALA A CB   1 
ATOM   2506 H H    . ALA A 1 176 ? 3.19147   -3.97818  22.57250 1.000 37.44532  ? 162 ALA A H    1 
ATOM   2507 H HA   . ALA A 1 176 ? 3.09854   -5.54840  20.38162 1.000 38.77270  ? 162 ALA A HA   1 
ATOM   2508 H HB1  . ALA A 1 176 ? 4.07622   -2.90204  20.16987 1.000 33.55732  ? 162 ALA A HB1  1 
ATOM   2509 H HB2  . ALA A 1 176 ? 4.16043   -3.98683  19.01244 1.000 33.55732  ? 162 ALA A HB2  1 
ATOM   2510 H HB3  . ALA A 1 176 ? 2.74827   -3.42013  19.46869 1.000 33.55732  ? 162 ALA A HB3  1 
ATOM   2511 N N    . ASN A 1 177 ? 5.48651   -6.15243  20.50720 1.000 33.89616  ? 163 ASN A N    1 
ATOM   2512 C CA   . ASN A 1 177 ? 6.81093   -6.68615  20.77726 1.000 31.91914  ? 163 ASN A CA   1 
ATOM   2513 C C    . ASN A 1 177 ? 7.54021   -6.88094  19.45898 1.000 29.33098  ? 163 ASN A C    1 
ATOM   2514 O O    . ASN A 1 177 ? 6.96254   -7.38087  18.48918 1.000 34.47823  ? 163 ASN A O    1 
ATOM   2515 C CB   . ASN A 1 177 ? 6.74043   -8.01850  21.52984 1.000 35.73978  ? 163 ASN A CB   1 
ATOM   2516 C CG   . ASN A 1 177 ? 8.09425   -8.69023  21.64586 1.000 36.85152  ? 163 ASN A CG   1 
ATOM   2517 O OD1  . ASN A 1 177 ? 8.49426   -9.46153  20.77431 1.000 27.72036  ? 163 ASN A OD1  1 
ATOM   2518 N ND2  . ASN A 1 177 ? 8.81343   -8.39021  22.72087 1.000 42.16832  ? 163 ASN A ND2  1 
ATOM   2519 H H    . ASN A 1 177 ? 5.11838   -6.49628  19.81018 1.000 40.73133  ? 163 ASN A H    1 
ATOM   2520 H HA   . ASN A 1 177 ? 7.31060   -6.05799  21.32192 1.000 38.35891  ? 163 ASN A HA   1 
ATOM   2521 H HB2  . ASN A 1 177 ? 6.40537   -7.85928  22.42611 1.000 42.94367  ? 163 ASN A HB2  1 
ATOM   2522 H HB3  . ASN A 1 177 ? 6.14547   -8.61988  21.05521 1.000 42.94367  ? 163 ASN A HB3  1 
ATOM   2523 H HD21 . ASN A 1 177 ? 9.58861   -8.74552  22.83253 1.000 50.65792  ? 163 ASN A HD21 1 
ATOM   2524 H HD22 . ASN A 1 177 ? 8.50409   -7.84058  23.30552 1.000 50.65792  ? 163 ASN A HD22 1 
ATOM   2525 N N    . PHE A 1 178 ? 8.80706   -6.48282  19.42839 1.000 27.10793  ? 164 PHE A N    1 
ATOM   2526 C CA   . PHE A 1 178 ? 9.62851   -6.65525  18.23957 1.000 28.94896  ? 164 PHE A CA   1 
ATOM   2527 C C    . PHE A 1 178 ? 11.07754  -6.39236  18.61293 1.000 27.58962  ? 164 PHE A C    1 
ATOM   2528 O O    . PHE A 1 178 ? 11.36932  -5.69932  19.59149 1.000 30.80706  ? 164 PHE A O    1 
ATOM   2529 C CB   . PHE A 1 178 ? 9.18126   -5.73031  17.10105 1.000 31.35075  ? 164 PHE A CB   1 
ATOM   2530 C CG   . PHE A 1 178 ? 9.13563   -4.27398  17.47339 1.000 28.08596  ? 164 PHE A CG   1 
ATOM   2531 C CD1  . PHE A 1 178 ? 8.01464   -3.73456  18.08243 1.000 27.46067  ? 164 PHE A CD1  1 
ATOM   2532 C CD2  . PHE A 1 178 ? 10.20553  -3.44118  17.19646 1.000 31.65520  ? 164 PHE A CD2  1 
ATOM   2533 C CE1  . PHE A 1 178 ? 7.96664   -2.39539  18.41640 1.000 30.18731  ? 164 PHE A CE1  1 
ATOM   2534 C CE2  . PHE A 1 178 ? 10.16281  -2.09918  17.52884 1.000 29.01762  ? 164 PHE A CE2  1 
ATOM   2535 C CZ   . PHE A 1 178 ? 9.04173   -1.57663  18.13875 1.000 26.36176  ? 164 PHE A CZ   1 
ATOM   2536 H H    . PHE A 1 178 ? 9.21453   -6.10861  20.08683 1.000 32.58545  ? 164 PHE A H    1 
ATOM   2537 H HA   . PHE A 1 178 ? 9.55768   -7.57131  17.92854 1.000 34.79470  ? 164 PHE A HA   1 
ATOM   2538 H HB2  . PHE A 1 178 ? 9.80180   -5.82581  16.36165 1.000 37.67683  ? 164 PHE A HB2  1 
ATOM   2539 H HB3  . PHE A 1 178 ? 8.28965   -5.99079  16.82164 1.000 37.67683  ? 164 PHE A HB3  1 
ATOM   2540 H HD1  . PHE A 1 178 ? 7.28542   -4.28084  18.26872 1.000 33.00874  ? 164 PHE A HD1  1 
ATOM   2541 H HD2  . PHE A 1 178 ? 10.96236  -3.78794  16.78190 1.000 38.04218  ? 164 PHE A HD2  1 
ATOM   2542 H HE1  . PHE A 1 178 ? 7.20979   -2.04560  18.82837 1.000 36.28072  ? 164 PHE A HE1  1 
ATOM   2543 H HE2  . PHE A 1 178 ? 10.88938  -1.54983  17.34122 1.000 34.87708  ? 164 PHE A HE2  1 
ATOM   2544 H HZ   . PHE A 1 178 ? 9.01052   -0.67444  18.36234 1.000 31.69006  ? 164 PHE A HZ   1 
ATOM   2545 N N    . LYS A 1 179 ? 11.97907  -6.96849  17.82512 1.000 26.47868  ? 165 LYS A N    1 
ATOM   2546 C CA   . LYS A 1 179 ? 13.41255  -6.80099  18.00242 1.000 30.92539  ? 165 LYS A CA   1 
ATOM   2547 C C    . LYS A 1 179 ? 13.96671  -5.92747  16.88554 1.000 23.91082  ? 165 LYS A C    1 
ATOM   2548 O O    . LYS A 1 179 ? 13.53250  -6.02749  15.73454 1.000 28.53173  ? 165 LYS A O    1 
ATOM   2549 C CB   . LYS A 1 179 ? 14.12826  -8.15536  18.00511 1.000 34.52241  ? 165 LYS A CB   1 
ATOM   2550 C CG   . LYS A 1 179 ? 13.75916  -9.06331  19.16968 1.000 32.55291  ? 165 LYS A CG   1 
ATOM   2551 C CD   . LYS A 1 179 ? 14.57986  -10.34574 19.13813 1.000 39.28219  ? 165 LYS A CD   1 
ATOM   2552 C CE   . LYS A 1 179 ? 14.51479  -11.09586 20.45861 1.000 35.87462  ? 165 LYS A CE   1 
ATOM   2553 N NZ   . LYS A 1 179 ? 15.67052  -12.02149 20.61968 1.000 44.97616  ? 165 LYS A NZ   1 
ATOM   2554 H H    . LYS A 1 179 ? 11.77602  -7.47619  17.16134 1.000 31.83035  ? 165 LYS A H    1 
ATOM   2555 H HA   . LYS A 1 179 ? 13.58681  -6.36440  18.85091 1.000 37.16641  ? 165 LYS A HA   1 
ATOM   2556 H HB2  . LYS A 1 179 ? 13.90468  -8.62431  17.18597 1.000 41.48283  ? 165 LYS A HB2  1 
ATOM   2557 H HB3  . LYS A 1 179 ? 15.08465  -7.99906  18.04744 1.000 41.48283  ? 165 LYS A HB3  1 
ATOM   2558 H HG2  . LYS A 1 179 ? 13.93627  -8.60524  20.00616 1.000 39.11943  ? 165 LYS A HG2  1 
ATOM   2559 H HG3  . LYS A 1 179 ? 12.81968  -9.29782  19.11230 1.000 39.11943  ? 165 LYS A HG3  1 
ATOM   2560 H HD2  . LYS A 1 179 ? 14.23654  -10.92764 18.44213 1.000 47.19457  ? 165 LYS A HD2  1 
ATOM   2561 H HD3  . LYS A 1 179 ? 15.50783  -10.12680 18.95970 1.000 47.19457  ? 165 LYS A HD3  1 
ATOM   2562 H HE2  . LYS A 1 179 ? 14.52981  -10.45930 21.19037 1.000 43.10548  ? 165 LYS A HE2  1 
ATOM   2563 H HE3  . LYS A 1 179 ? 13.69855  -11.61896 20.49064 1.000 43.10548  ? 165 LYS A HE3  1 
ATOM   2564 H HZ1  . LYS A 1 179 ? 15.68030  -12.61455 19.95614 1.000 54.02733  ? 165 LYS A HZ1  1 
ATOM   2565 H HZ2  . LYS A 1 179 ? 16.43258  -11.56191 20.60756 1.000 54.02733  ? 165 LYS A HZ2  1 
ATOM   2566 H HZ3  . LYS A 1 179 ? 15.60726  -12.45553 21.39409 1.000 54.02733  ? 165 LYS A HZ3  1 
ATOM   2567 N N    . ILE A 1 180 ? 14.91855  -5.06590  17.23344 1.000 29.71575  ? 166 ILE A N    1 
ATOM   2568 C CA   . ILE A 1 180 ? 15.65186  -4.25440  16.26931 1.000 33.08454  ? 166 ILE A CA   1 
ATOM   2569 C C    . ILE A 1 180 ? 17.10879  -4.69259  16.29569 1.000 33.11361  ? 166 ILE A C    1 
ATOM   2570 O O    . ILE A 1 180 ? 17.67840  -4.92575  17.36859 1.000 29.25746  ? 166 ILE A O    1 
ATOM   2571 C CB   . ILE A 1 180 ? 15.53302  -2.74764  16.57052 1.000 34.45988  ? 166 ILE A CB   1 
ATOM   2572 C CG1  . ILE A 1 180 ? 14.06650  -2.30651  16.57356 1.000 31.81852  ? 166 ILE A CG1  1 
ATOM   2573 C CG2  . ILE A 1 180 ? 16.33591  -1.94050  15.55555 1.000 35.72333  ? 166 ILE A CG2  1 
ATOM   2574 C CD1  . ILE A 1 180 ? 13.37372  -2.43056  15.23320 1.000 34.64870  ? 166 ILE A CD1  1 
ATOM   2575 H H    . ILE A 1 180 ? 15.16356  -4.93090  18.04667 1.000 35.71484  ? 166 ILE A H    1 
ATOM   2576 H HA   . ILE A 1 180 ? 15.28799  -4.40929  15.38359 1.000 39.75739  ? 166 ILE A HA   1 
ATOM   2577 H HB   . ILE A 1 180 ? 15.89701  -2.58561  17.45491 1.000 41.40779  ? 166 ILE A HB   1 
ATOM   2578 H HG12 . ILE A 1 180 ? 13.57943  -2.85586  17.20750 1.000 38.23816  ? 166 ILE A HG12 1 
ATOM   2579 H HG13 . ILE A 1 180 ? 14.02412  -1.37496  16.84061 1.000 38.23816  ? 166 ILE A HG13 1 
ATOM   2580 H HG21 . ILE A 1 180 ? 16.19303  -2.31328  14.67152 1.000 42.92394  ? 166 ILE A HG21 1 
ATOM   2581 H HG22 . ILE A 1 180 ? 16.03673  -1.01806  15.57788 1.000 42.92394  ? 166 ILE A HG22 1 
ATOM   2582 H HG23 . ILE A 1 180 ? 17.27670  -1.98879  15.78681 1.000 42.92394  ? 166 ILE A HG23 1 
ATOM   2583 H HD11 . ILE A 1 180 ? 12.44703  -2.16099  15.33053 1.000 41.63438  ? 166 ILE A HD11 1 
ATOM   2584 H HD12 . ILE A 1 180 ? 13.82008  -1.85504  14.59254 1.000 41.63438  ? 166 ILE A HD12 1 
ATOM   2585 H HD13 . ILE A 1 180 ? 13.42051  -3.35327  14.93772 1.000 41.63438  ? 166 ILE A HD13 1 
ATOM   2586 N N    . ARG A 1 181 ? 17.71023  -4.80012  15.11475 1.000 36.93840  ? 167 ARG A N    1 
ATOM   2587 C CA   . ARG A 1 181 ? 19.08775  -5.26016  14.95394 1.000 40.73270  ? 167 ARG A CA   1 
ATOM   2588 C C    . ARG A 1 181 ? 19.87425  -4.14312  14.27622 1.000 37.93703  ? 167 ARG A C    1 
ATOM   2589 O O    . ARG A 1 181 ? 19.88207  -4.03119  13.04829 1.000 40.62071  ? 167 ARG A O    1 
ATOM   2590 C CB   . ARG A 1 181 ? 19.13361  -6.55501  14.14723 1.000 41.31205  ? 167 ARG A CB   1 
ATOM   2591 C CG   . ARG A 1 181 ? 18.29155  -7.66878  14.74825 1.000 45.46989  ? 167 ARG A CG   1 
ATOM   2592 C CD   . ARG A 1 181 ? 17.88138  -8.70278  13.71365 1.000 51.59377  ? 167 ARG A CD   1 
ATOM   2593 N NE   . ARG A 1 181 ? 16.75491  -9.50046  14.18442 1.000 51.12405  ? 167 ARG A NE   1 
ATOM   2594 C CZ   . ARG A 1 181 ? 16.85185  -10.49117 15.06030 1.000 42.76126  ? 167 ARG A CZ   1 
ATOM   2595 N NH1  . ARG A 1 181 ? 18.01776  -10.84921 15.57314 1.000 44.45483  ? 167 ARG A NH1  1 
ATOM   2596 N NH2  . ARG A 1 181 ? 15.75028  -11.13413 15.43669 1.000 43.17522  ? 167 ARG A NH2  1 
ATOM   2597 H H    . ARG A 1 181 ? 17.32882  -4.60633  14.36871 1.000 44.38202  ? 167 ARG A H    1 
ATOM   2598 H HA   . ARG A 1 181 ? 19.47962  -5.42508  15.82580 1.000 48.93518  ? 167 ARG A HA   1 
ATOM   2599 H HB2  . ARG A 1 181 ? 18.80093  -6.37926  13.25317 1.000 49.63040  ? 167 ARG A HB2  1 
ATOM   2600 H HB3  . ARG A 1 181 ? 20.05161  -6.86540  14.10456 1.000 49.63040  ? 167 ARG A HB3  1 
ATOM   2601 H HG2  . ARG A 1 181 ? 18.80432  -8.11893  15.43769 1.000 54.61981  ? 167 ARG A HG2  1 
ATOM   2602 H HG3  . ARG A 1 181 ? 17.48529  -7.28776  15.12992 1.000 54.61981  ? 167 ARG A HG3  1 
ATOM   2603 H HD2  . ARG A 1 181 ? 17.61793  -8.25327  12.89547 1.000 61.96847  ? 167 ARG A HD2  1 
ATOM   2604 H HD3  . ARG A 1 181 ? 18.62711  -9.29821  13.53972 1.000 61.96847  ? 167 ARG A HD3  1 
ATOM   2605 H HE   . ARG A 1 181 ? 15.97492  -9.31576  13.87282 1.000 61.40480  ? 167 ARG A HE   1 
ATOM   2606 H HH11 . ARG A 1 181 ? 18.73518  -10.43639 15.33972 1.000 53.40174  ? 167 ARG A HH11 1 
ATOM   2607 H HH12 . ARG A 1 181 ? 18.05817  -11.49476 16.13992 1.000 53.40174  ? 167 ARG A HH12 1 
ATOM   2608 H HH21 . ARG A 1 181 ? 14.98712  -10.90574 15.11260 1.000 51.86620  ? 167 ARG A HH21 1 
ATOM   2609 H HH22 . ARG A 1 181 ? 15.80107  -11.77831 16.00418 1.000 51.86620  ? 167 ARG A HH22 1 
ATOM   2610 N N    . HIS A 1 182 ? 20.53359  -3.31519  15.08222 1.000 35.20783  ? 168 HIS A N    1 
ATOM   2611 C CA   . HIS A 1 182 ? 21.32464  -2.20949  14.55888 1.000 34.68877  ? 168 HIS A CA   1 
ATOM   2612 C C    . HIS A 1 182 ? 22.67417  -2.73138  14.08256 1.000 37.02206  ? 168 HIS A C    1 
ATOM   2613 O O    . HIS A 1 182 ? 23.43443  -3.30857  14.86782 1.000 33.40388  ? 168 HIS A O    1 
ATOM   2614 C CB   . HIS A 1 182 ? 21.51772  -1.13451  15.62537 1.000 27.70635  ? 168 HIS A CB   1 
ATOM   2615 C CG   . HIS A 1 182 ? 20.23988  -0.53588  16.12300 1.000 29.52397  ? 168 HIS A CG   1 
ATOM   2616 N ND1  . HIS A 1 182 ? 19.43535  0.26153   15.33784 1.000 31.46726  ? 168 HIS A ND1  1 
ATOM   2617 C CD2  . HIS A 1 182 ? 19.63398  -0.60733  17.33172 1.000 32.17676  ? 168 HIS A CD2  1 
ATOM   2618 C CE1  . HIS A 1 182 ? 18.38600  0.65093   16.03994 1.000 33.14874  ? 168 HIS A CE1  1 
ATOM   2619 N NE2  . HIS A 1 182 ? 18.48177  0.13650   17.25271 1.000 31.84886  ? 168 HIS A NE2  1 
ATOM   2620 H H    . HIS A 1 182 ? 20.53780  -3.37423  15.94018 1.000 42.30534  ? 168 HIS A H    1 
ATOM   2621 H HA   . HIS A 1 182 ? 20.85843  -1.81259  13.80654 1.000 41.68247  ? 168 HIS A HA   1 
ATOM   2622 H HB2  . HIS A 1 182 ? 21.97466  -1.52839  16.38495 1.000 33.30356  ? 168 HIS A HB2  1 
ATOM   2623 H HB3  . HIS A 1 182 ? 22.05345  -0.41768  15.25113 1.000 33.30356  ? 168 HIS A HB3  1 
ATOM   2624 H HD1  . HIS A 1 182 ? 19.59189  0.47263   14.51898 1.000 37.81665  ? 168 HIS A HD1  1 
ATOM   2625 H HD2  . HIS A 1 182 ? 19.94049  -1.07288  18.07617 1.000 38.66805  ? 168 HIS A HD2  1 
ATOM   2626 H HE1  . HIS A 1 182 ? 17.69708  1.19477   15.73250 1.000 39.83443  ? 168 HIS A HE1  1 
ATOM   2627 N N    . ASN A 1 183 ? 22.97218  -2.52736  12.80147 1.000 31.85013  ? 169 ASN A N    1 
ATOM   2628 C CA   . ASN A 1 183 ? 24.26835  -2.92032  12.26853 1.000 32.55070  ? 169 ASN A CA   1 
ATOM   2629 C C    . ASN A 1 183 ? 25.38299  -2.17170  12.98620 1.000 36.54716  ? 169 ASN A C    1 
ATOM   2630 O O    . ASN A 1 183 ? 25.33456  -0.94666  13.13106 1.000 33.08584  ? 169 ASN A O    1 
ATOM   2631 C CB   . ASN A 1 183 ? 24.33162  -2.64250  10.76736 1.000 39.74584  ? 169 ASN A CB   1 
ATOM   2632 C CG   . ASN A 1 183 ? 23.75601  -3.77194  9.93956  1.000 38.41898  ? 169 ASN A CG   1 
ATOM   2633 O OD1  . ASN A 1 183 ? 23.02162  -4.61877  10.44615 1.000 39.47174  ? 169 ASN A OD1  1 
ATOM   2634 N ND2  . ASN A 1 183 ? 24.09140  -3.79139  8.65523  1.000 47.75577  ? 169 ASN A ND2  1 
ATOM   2635 H H    . ASN A 1 183 ? 22.44450  -2.16615  12.22641 1.000 38.27610  ? 169 ASN A H    1 
ATOM   2636 H HA   . ASN A 1 183 ? 24.39470  -3.87217  12.40604 1.000 39.11678  ? 169 ASN A HA   1 
ATOM   2637 H HB2  . ASN A 1 183 ? 23.82442  -1.83891  10.57271 1.000 47.75094  ? 169 ASN A HB2  1 
ATOM   2638 H HB3  . ASN A 1 183 ? 25.25809  -2.52130  10.50685 1.000 47.75094  ? 169 ASN A HB3  1 
ATOM   2639 H HD21 . ASN A 1 183 ? 23.79085  -4.41231  8.14168  1.000 57.36287  ? 169 ASN A HD21 1 
ATOM   2640 H HD22 . ASN A 1 183 ? 24.60922  -3.18308  8.33677  1.000 57.36287  ? 169 ASN A HD22 1 
ATOM   2641 N N    . ILE A 1 184 ? 26.38366  -2.91244  13.43702 1.000 35.33666  ? 170 ILE A N    1 
ATOM   2642 C CA   . ILE A 1 184 ? 27.55918  -2.33562  14.07606 1.000 35.21841  ? 170 ILE A CA   1 
ATOM   2643 C C    . ILE A 1 184 ? 28.59256  -2.03845  13.00140 1.000 42.02082  ? 170 ILE A C    1 
ATOM   2644 O O    . ILE A 1 184 ? 28.83949  -2.86271  12.11284 1.000 40.88665  ? 170 ILE A O    1 
ATOM   2645 C CB   . ILE A 1 184 ? 28.11646  -3.28282  15.15437 1.000 30.26547  ? 170 ILE A CB   1 
ATOM   2646 C CG1  . ILE A 1 184 ? 27.09284  -3.43760  16.28279 1.000 33.69649  ? 170 ILE A CG1  1 
ATOM   2647 C CG2  . ILE A 1 184 ? 29.44066  -2.75898  15.69062 1.000 34.43965  ? 170 ILE A CG2  1 
ATOM   2648 C CD1  . ILE A 1 184 ? 27.45736  -4.48873  17.31840 1.000 33.73607  ? 170 ILE A CD1  1 
ATOM   2649 H H    . ILE A 1 184 ? 26.40699  -3.77048  13.38394 1.000 42.45994  ? 170 ILE A H    1 
ATOM   2650 H HA   . ILE A 1 184 ? 27.31863  -1.50230  14.51036 1.000 42.31803  ? 170 ILE A HA   1 
ATOM   2651 H HB   . ILE A 1 184 ? 28.27710  -4.15317  14.75739 1.000 36.37450  ? 170 ILE A HB   1 
ATOM   2652 H HG12 . ILE A 1 184 ? 27.00889  -2.58813  16.74350 1.000 40.49173  ? 170 ILE A HG12 1 
ATOM   2653 H HG13 . ILE A 1 184 ? 26.24037  -3.69044  15.89516 1.000 40.49173  ? 170 ILE A HG13 1 
ATOM   2654 H HG21 . ILE A 1 184 ? 30.12155  -2.86377  15.00775 1.000 41.38352  ? 170 ILE A HG21 1 
ATOM   2655 H HG22 . ILE A 1 184 ? 29.34085  -1.82107  15.91702 1.000 41.38352  ? 170 ILE A HG22 1 
ATOM   2656 H HG23 . ILE A 1 184 ? 29.68405  -3.26595  16.48096 1.000 41.38352  ? 170 ILE A HG23 1 
ATOM   2657 H HD11 . ILE A 1 184 ? 28.16893  -4.14464  17.88069 1.000 40.53923  ? 170 ILE A HD11 1 
ATOM   2658 H HD12 . ILE A 1 184 ? 26.67538  -4.68529  17.85763 1.000 40.53923  ? 170 ILE A HD12 1 
ATOM   2659 H HD13 . ILE A 1 184 ? 27.75498  -5.29146  16.86237 1.000 40.53923  ? 170 ILE A HD13 1 
ATOM   2660 N N    . GLU A 1 185 ? 29.20564  -0.85483  13.09016 1.000 44.98684  ? 171 GLU A N    1 
ATOM   2661 C CA   . GLU A 1 185 ? 30.04433  -0.35703  12.00358 1.000 52.91398  ? 171 GLU A CA   1 
ATOM   2662 C C    . GLU A 1 185 ? 31.05738  -1.40171  11.55107 1.000 56.99062  ? 171 GLU A C    1 
ATOM   2663 O O    . GLU A 1 185 ? 31.15467  -1.71236  10.35872 1.000 65.12734  ? 171 GLU A O    1 
ATOM   2664 C CB   . GLU A 1 185 ? 30.75368  0.92752   12.43945 1.000 54.59495  ? 171 GLU A CB   1 
ATOM   2665 C CG   . GLU A 1 185 ? 31.56022  1.59497   11.33234 1.000 66.76727  ? 171 GLU A CG   1 
ATOM   2666 C CD   . GLU A 1 185 ? 30.70582  1.99577   10.14193 1.000 69.40765  ? 171 GLU A CD   1 
ATOM   2667 O OE1  . GLU A 1 185 ? 29.66894  2.66145   10.34763 1.000 64.06341  ? 171 GLU A OE1  1 
ATOM   2668 O OE2  . GLU A 1 185 ? 31.06763  1.63769   9.00060  1.000 69.47146  ? 171 GLU A OE2  1 
ATOM   2669 H H    . GLU A 1 185 ? 29.15140  -0.32527  13.76560 1.000 54.04014  ? 171 GLU A H    1 
ATOM   2670 H HA   . GLU A 1 185 ? 29.47529  -0.14969  11.24589 1.000 63.55272  ? 171 GLU A HA   1 
ATOM   2671 H HB2  . GLU A 1 185 ? 30.08701  1.56318   12.74342 1.000 65.56987  ? 171 GLU A HB2  1 
ATOM   2672 H HB3  . GLU A 1 185 ? 31.36416  0.71559   13.16285 1.000 65.56987  ? 171 GLU A HB3  1 
ATOM   2673 H HG2  . GLU A 1 185 ? 31.97802  2.39626   11.68488 1.000 80.17667  ? 171 GLU A HG2  1 
ATOM   2674 H HG3  . GLU A 1 185 ? 32.23925  0.97695   11.01952 1.000 80.17667  ? 171 GLU A HG3  1 
ATOM   2675 N N    . ASP A 1 186 ? 31.81741  -1.95748  12.48576 1.000 54.58737  ? 172 ASP A N    1 
ATOM   2676 C CA   . ASP A 1 186 ? 32.86652  -2.92126  12.14976 1.000 65.17859  ? 172 ASP A CA   1 
ATOM   2677 C C    . ASP A 1 186 ? 32.36867  -4.35358  12.30289 1.000 61.18234  ? 172 ASP A C    1 
ATOM   2678 O O    . ASP A 1 186 ? 33.01562  -5.19522  12.92413 1.000 66.91398  ? 172 ASP A O    1 
ATOM   2679 C CB   . ASP A 1 186 ? 34.09802  -2.67259  13.01222 1.000 80.80810  ? 172 ASP A CB   1 
ATOM   2680 C CG   . ASP A 1 186 ? 35.36826  -3.22895  12.39233 1.000 93.22146  ? 172 ASP A CG   1 
ATOM   2681 O OD1  . ASP A 1 186 ? 35.28303  -3.86993  11.32277 1.000 84.79942  ? 172 ASP A OD1  1 
ATOM   2682 O OD2  . ASP A 1 186 ? 36.45458  -3.01858  12.97300 1.000 93.75915  ? 172 ASP A OD2  1 
ATOM   2683 H H    . ASP A 1 186 ? 31.74688  -1.79370  13.32707 1.000 65.56078  ? 172 ASP A H    1 
ATOM   2684 H HA   . ASP A 1 186 ? 33.12242  -2.79464  11.22273 1.000 78.27024  ? 172 ASP A HA   1 
ATOM   2685 H HB2  . ASP A 1 186 ? 34.21462  -1.71678  13.12941 1.000 97.02566  ? 172 ASP A HB2  1 
ATOM   2686 H HB3  . ASP A 1 186 ? 33.97234  -3.09961  13.87405 1.000 97.02566  ? 172 ASP A HB3  1 
ATOM   2687 N N    . GLY A 1 187 ? 31.20374  -4.64515  11.72975 1.000 47.97974  ? 173 GLY A N    1 
ATOM   2688 C CA   . GLY A 1 187 ? 30.64768  -5.98187  11.78861 1.000 47.98692  ? 173 GLY A CA   1 
ATOM   2689 C C    . GLY A 1 187 ? 29.88392  -6.25055  13.06775 1.000 41.91396  ? 173 GLY A C    1 
ATOM   2690 O O    . GLY A 1 187 ? 30.22243  -5.71292  14.12597 1.000 47.00763  ? 173 GLY A O    1 
ATOM   2691 H H    . GLY A 1 187 ? 30.71790  -4.08033  11.30017 1.000 57.63163  ? 173 GLY A H    1 
ATOM   2692 H HA2  . GLY A 1 187 ? 30.04163  -6.10760  11.04175 1.000 57.64024  ? 173 GLY A HA2  1 
ATOM   2693 H HA3  . GLY A 1 187 ? 31.36731  -6.62904  11.72376 1.000 57.64024  ? 173 GLY A HA3  1 
ATOM   2694 N N    . GLY A 1 188 ? 28.85206  -7.08342  12.98065 1.000 36.16832  ? 174 GLY A N    1 
ATOM   2695 C CA   . GLY A 1 188 ? 28.02980  -7.42840  14.12416 1.000 33.71873  ? 174 GLY A CA   1 
ATOM   2696 C C    . GLY A 1 188 ? 26.72999  -6.64783  14.14633 1.000 35.20315  ? 174 GLY A C    1 
ATOM   2697 O O    . GLY A 1 188 ? 26.47537  -5.75932  13.32742 1.000 36.98110  ? 174 GLY A O    1 
ATOM   2698 H H    . GLY A 1 188 ? 28.60599  -7.46807  12.25188 1.000 43.45792  ? 174 GLY A H    1 
ATOM   2699 H HA2  . GLY A 1 188 ? 27.81921  -8.37485  14.09620 1.000 40.51841  ? 174 GLY A HA2  1 
ATOM   2700 H HA3  . GLY A 1 188 ? 28.51678  -7.23724  14.94099 1.000 40.51841  ? 174 GLY A HA3  1 
ATOM   2701 N N    . VAL A 1 189 ? 25.89061  -7.00115  15.11859 1.000 34.79197  ? 175 VAL A N    1 
ATOM   2702 C CA   . VAL A 1 189 ? 24.60073  -6.35511  15.31626 1.000 34.75638  ? 175 VAL A CA   1 
ATOM   2703 C C    . VAL A 1 189 ? 24.41959  -6.05171  16.79656 1.000 33.52783  ? 175 VAL A C    1 
ATOM   2704 O O    . VAL A 1 189 ? 24.87097  -6.80294  17.66718 1.000 30.76185  ? 175 VAL A O    1 
ATOM   2705 C CB   . VAL A 1 189 ? 23.42921  -7.22048  14.79658 1.000 37.21124  ? 175 VAL A CB   1 
ATOM   2706 C CG1  . VAL A 1 189 ? 23.44722  -7.28954  13.27061 1.000 38.68009  ? 175 VAL A CG1  1 
ATOM   2707 C CG2  . VAL A 1 189 ? 23.48208  -8.61789  15.41486 1.000 38.15868  ? 175 VAL A CG2  1 
ATOM   2708 H H    . VAL A 1 189 ? 26.05226  -7.62605  15.68690 1.000 41.80631  ? 175 VAL A H    1 
ATOM   2709 H HA   . VAL A 1 189 ? 24.59614  -5.51546  14.83059 1.000 41.76360  ? 175 VAL A HA   1 
ATOM   2710 H HB   . VAL A 1 189 ? 22.59108  -6.81057  15.06194 1.000 44.70943  ? 175 VAL A HB   1 
ATOM   2711 H HG11 . VAL A 1 189 ? 24.35107  -7.12792  12.95781 1.000 46.47205  ? 175 VAL A HG11 1 
ATOM   2712 H HG12 . VAL A 1 189 ? 23.15293  -8.17047  12.99085 1.000 46.47205  ? 175 VAL A HG12 1 
ATOM   2713 H HG13 . VAL A 1 189 ? 22.84882  -6.61305  12.91678 1.000 46.47205  ? 175 VAL A HG13 1 
ATOM   2714 H HG21 . VAL A 1 189 ? 24.14830  -8.62631  16.11983 1.000 45.84636  ? 175 VAL A HG21 1 
ATOM   2715 H HG22 . VAL A 1 189 ? 22.61032  -8.83442  15.78099 1.000 45.84636  ? 175 VAL A HG22 1 
ATOM   2716 H HG23 . VAL A 1 189 ? 23.72038  -9.25882  14.72687 1.000 45.84636  ? 175 VAL A HG23 1 
ATOM   2717 N N    . GLN A 1 190 ? 23.75612  -4.93116  17.07346 1.000 32.34403  ? 176 GLN A N    1 
ATOM   2718 C CA   . GLN A 1 190 ? 23.38667  -4.52042  18.42372 1.000 30.04683  ? 176 GLN A CA   1 
ATOM   2719 C C    . GLN A 1 190 ? 21.88964  -4.75229  18.57323 1.000 31.57999  ? 176 GLN A C    1 
ATOM   2720 O O    . GLN A 1 190 ? 21.08111  -4.04095  17.96527 1.000 32.17352  ? 176 GLN A O    1 
ATOM   2721 C CB   . GLN A 1 190 ? 23.74847  -3.05699  18.67614 1.000 31.71114  ? 176 GLN A CB   1 
ATOM   2722 C CG   . GLN A 1 190 ? 23.24749  -2.50114  20.00966 1.000 28.50447  ? 176 GLN A CG   1 
ATOM   2723 C CD   . GLN A 1 190 ? 23.83101  -3.22731  21.20520 1.000 33.15356  ? 176 GLN A CD   1 
ATOM   2724 O OE1  . GLN A 1 190 ? 25.01345  -3.08104  21.51811 1.000 30.60138  ? 176 GLN A OE1  1 
ATOM   2725 N NE2  . GLN A 1 190 ? 23.00307  -4.01865  21.88020 1.000 31.14422  ? 176 GLN A NE2  1 
ATOM   2726 H H    . GLN A 1 190 ? 23.50010  -4.37248  16.47185 1.000 38.86877  ? 176 GLN A H    1 
ATOM   2727 H HA   . GLN A 1 190 ? 23.86125  -5.05985  19.07540 1.000 36.11213  ? 176 GLN A HA   1 
ATOM   2728 H HB2  . GLN A 1 190 ? 24.71468  -2.97170  18.66757 1.000 38.10931  ? 176 GLN A HB2  1 
ATOM   2729 H HB3  . GLN A 1 190 ? 23.36146  -2.51675  17.96956 1.000 38.10931  ? 176 GLN A HB3  1 
ATOM   2730 H HG2  . GLN A 1 190 ? 23.49694  -1.56610  20.07588 1.000 34.26130  ? 176 GLN A HG2  1 
ATOM   2731 H HG3  . GLN A 1 190 ? 22.28231  -2.59042  20.04653 1.000 34.26130  ? 176 GLN A HG3  1 
ATOM   2732 H HE21 . GLN A 1 190 ? 22.18382  -4.09681  21.63056 1.000 37.42901  ? 176 GLN A HE21 1 
ATOM   2733 H HE22 . GLN A 1 190 ? 23.28672  -4.45241  22.56648 1.000 37.42901  ? 176 GLN A HE22 1 
ATOM   2734 N N    . LEU A 1 191 ? 21.52536  -5.74583  19.37549 1.000 30.16835  ? 177 LEU A N    1 
ATOM   2735 C CA   . LEU A 1 191 ? 20.12650  -6.09707  19.56018 1.000 27.29369  ? 177 LEU A CA   1 
ATOM   2736 C C    . LEU A 1 191 ? 19.43128  -5.07956  20.45710 1.000 28.50391  ? 177 LEU A C    1 
ATOM   2737 O O    . LEU A 1 191 ? 19.99641  -4.61449  21.45084 1.000 30.70737  ? 177 LEU A O    1 
ATOM   2738 C CB   . LEU A 1 191 ? 20.01648  -7.49483  20.16777 1.000 33.54458  ? 177 LEU A CB   1 
ATOM   2739 C CG   . LEU A 1 191 ? 18.62000  -8.10845  20.25659 1.000 40.76018  ? 177 LEU A CG   1 
ATOM   2740 C CD1  . LEU A 1 191 ? 18.14600  -8.52350  18.87321 1.000 41.35774  ? 177 LEU A CD1  1 
ATOM   2741 C CD2  . LEU A 1 191 ? 18.59922  -9.29368  21.22113 1.000 41.95861  ? 177 LEU A CD2  1 
ATOM   2742 H H    . LEU A 1 191 ? 22.07269  -6.23315  19.82554 1.000 36.25797  ? 177 LEU A H    1 
ATOM   2743 H HA   . LEU A 1 191 ? 19.67388  -6.09751  18.70225 1.000 32.80837  ? 177 LEU A HA   1 
ATOM   2744 H HB2  . LEU A 1 191 ? 20.55544  -8.09639  19.63061 1.000 40.30943  ? 177 LEU A HB2  1 
ATOM   2745 H HB3  . LEU A 1 191 ? 20.36523  -7.45486  21.07202 1.000 40.30943  ? 177 LEU A HB3  1 
ATOM   2746 H HG   . LEU A 1 191 ? 18.00346  -7.44547  20.60478 1.000 48.96815  ? 177 LEU A HG   1 
ATOM   2747 H HD11 . LEU A 1 191 ? 18.68398  -9.26980  18.56578 1.000 49.68523  ? 177 LEU A HD11 1 
ATOM   2748 H HD12 . LEU A 1 191 ? 17.21381  -8.78671  18.92458 1.000 49.68523  ? 177 LEU A HD12 1 
ATOM   2749 H HD13 . LEU A 1 191 ? 18.24479  -7.77267  18.26709 1.000 49.68523  ? 177 LEU A HD13 1 
ATOM   2750 H HD21 . LEU A 1 191 ? 18.30813  -10.08545 20.74230 1.000 50.40628  ? 177 LEU A HD21 1 
ATOM   2751 H HD22 . LEU A 1 191 ? 19.49270  -9.42992  21.57333 1.000 50.40628  ? 177 LEU A HD22 1 
ATOM   2752 H HD23 . LEU A 1 191 ? 17.98396  -9.10044  21.94570 1.000 50.40628  ? 177 LEU A HD23 1 
ATOM   2753 N N    . ALA A 1 192 ? 18.19437  -4.73760  20.10068 1.000 29.19774  ? 178 ALA A N    1 
ATOM   2754 C CA   . ALA A 1 192 ? 17.36242  -3.82510  20.88448 1.000 28.45387  ? 178 ALA A CA   1 
ATOM   2755 C C    . ALA A 1 192 ? 15.96957  -4.43929  20.98760 1.000 31.57524  ? 178 ALA A C    1 
ATOM   2756 O O    . ALA A 1 192 ? 15.19373  -4.39858  20.02759 1.000 28.74702  ? 178 ALA A O    1 
ATOM   2757 C CB   . ALA A 1 192 ? 17.31438  -2.43601  20.25407 1.000 31.00944  ? 178 ALA A CB   1 
ATOM   2758 H H    . ALA A 1 192 ? 17.80537  -5.02854  19.39101 1.000 35.09322  ? 178 ALA A H    1 
ATOM   2759 H HA   . ALA A 1 192 ? 17.73083  -3.73958  21.77771 1.000 34.20058  ? 178 ALA A HA   1 
ATOM   2760 H HB1  . ALA A 1 192 ? 16.72430  -1.87175  20.77782 1.000 37.26727  ? 178 ALA A HB1  1 
ATOM   2761 H HB2  . ALA A 1 192 ? 18.20919  -2.06163  20.24626 1.000 37.26727  ? 178 ALA A HB2  1 
ATOM   2762 H HB3  . ALA A 1 192 ? 16.97984  -2.51235  19.34679 1.000 37.26727  ? 178 ALA A HB3  1 
ATOM   2763 N N    . ASP A 1 193 ? 15.66018  -5.01030  22.15066 1.000 33.10626  ? 179 ASP A N    1 
ATOM   2764 C CA   . ASP A 1 193 ? 14.37150  -5.65283  22.37890 1.000 30.90174  ? 179 ASP A CA   1 
ATOM   2765 C C    . ASP A 1 193 ? 13.34175  -4.60424  22.78485 1.000 29.04769  ? 179 ASP A C    1 
ATOM   2766 O O    . ASP A 1 193 ? 13.46616  -3.98530  23.84754 1.000 24.67708  ? 179 ASP A O    1 
ATOM   2767 C CB   . ASP A 1 193 ? 14.49684  -6.72391  23.46160 1.000 33.04728  ? 179 ASP A CB   1 
ATOM   2768 C CG   . ASP A 1 193 ? 15.45103  -7.84256  23.07667 1.000 31.87318  ? 179 ASP A CG   1 
ATOM   2769 O OD1  . ASP A 1 193 ? 15.42413  -8.27956  21.91045 1.000 38.87947  ? 179 ASP A OD1  1 
ATOM   2770 O OD2  . ASP A 1 193 ? 16.22869  -8.29051  23.94506 1.000 46.79399  ? 179 ASP A OD2  1 
ATOM   2771 H H    . ASP A 1 193 ? 16.18678  -5.03826  22.83000 1.000 39.78345  ? 179 ASP A H    1 
ATOM   2772 H HA   . ASP A 1 193 ? 14.07502  -6.07697  21.55847 1.000 37.13803  ? 179 ASP A HA   1 
ATOM   2773 H HB2  . ASP A 1 193 ? 14.82916  -6.31327  24.27513 1.000 39.71268  ? 179 ASP A HB2  1 
ATOM   2774 H HB3  . ASP A 1 193 ? 13.62397  -7.11602  23.62051 1.000 39.71268  ? 179 ASP A HB3  1 
ATOM   2775 N N    . HIS A 1 194 ? 12.32323  -4.41366  21.94826 1.000 26.02121  ? 180 HIS A N    1 
ATOM   2776 C CA   . HIS A 1 194 ? 11.27761  -3.42676  22.18733 1.000 28.26013  ? 180 HIS A CA   1 
ATOM   2777 C C    . HIS A 1 194 ? 10.05622  -4.09268  22.80971 1.000 28.22187  ? 180 HIS A C    1 
ATOM   2778 O O    . HIS A 1 194 ? 9.54795   -5.08732  22.28205 1.000 28.03405  ? 180 HIS A O    1 
ATOM   2779 C CB   . HIS A 1 194 ? 10.86517  -2.73147  20.88623 1.000 24.95698  ? 180 HIS A CB   1 
ATOM   2780 C CG   . HIS A 1 194 ? 11.88177  -1.76975  20.35377 1.000 28.30580  ? 180 HIS A CG   1 
ATOM   2781 N ND1  . HIS A 1 194 ? 13.17125  -2.14281  20.04334 1.000 26.79617  ? 180 HIS A ND1  1 
ATOM   2782 C CD2  . HIS A 1 194 ? 11.78880  -0.45249  20.05259 1.000 27.89665  ? 180 HIS A CD2  1 
ATOM   2783 C CE1  . HIS A 1 194 ? 13.83319  -1.09431  19.58743 1.000 28.29847  ? 180 HIS A CE1  1 
ATOM   2784 N NE2  . HIS A 1 194 ? 13.01651  -0.05631  19.58070 1.000 29.30945  ? 180 HIS A NE2  1 
ATOM   2785 H H    . HIS A 1 194 ? 12.21546  -4.85565  21.21844 1.000 31.28139  ? 180 HIS A H    1 
ATOM   2786 H HA   . HIS A 1 194 ? 11.61872  -2.76203  22.80595 1.000 33.96809  ? 180 HIS A HA   1 
ATOM   2787 H HB2  . HIS A 1 194 ? 10.71638  -3.40784  20.20704 1.000 30.00432  ? 180 HIS A HB2  1 
ATOM   2788 H HB3  . HIS A 1 194 ? 10.04679  -2.23575  21.04564 1.000 30.00432  ? 180 HIS A HB3  1 
ATOM   2789 H HD1  . HIS A 1 194 ? 13.49475  -2.93464  20.13245 1.000 32.21134  ? 180 HIS A HD1  1 
ATOM   2790 H HD2  . HIS A 1 194 ? 11.03476  0.08353   20.14753 1.000 33.53192  ? 180 HIS A HD2  1 
ATOM   2791 H HE1  . HIS A 1 194 ? 14.72303  -1.08815  19.31715 1.000 34.01410  ? 180 HIS A HE1  1 
ATOM   2792 N N    . TYR A 1 195 ? 9.58588   -3.53568  23.92228 1.000 24.86043  ? 181 TYR A N    1 
ATOM   2793 C CA   . TYR A 1 195 ? 8.30467   -3.89296  24.51708 1.000 26.98048  ? 181 TYR A CA   1 
ATOM   2794 C C    . TYR A 1 195 ? 7.44846   -2.63704  24.56966 1.000 30.10551  ? 181 TYR A C    1 
ATOM   2795 O O    . TYR A 1 195 ? 7.88661   -1.60961  25.09713 1.000 33.16127  ? 181 TYR A O    1 
ATOM   2796 C CB   . TYR A 1 195 ? 8.48040   -4.48013  25.91781 1.000 28.88018  ? 181 TYR A CB   1 
ATOM   2797 C CG   . TYR A 1 195 ? 9.28245   -5.75827  25.94862 1.000 28.49732  ? 181 TYR A CG   1 
ATOM   2798 C CD1  . TYR A 1 195 ? 10.66798  -5.72785  26.01737 1.000 31.83983  ? 181 TYR A CD1  1 
ATOM   2799 C CD2  . TYR A 1 195 ? 8.65492   -6.99564  25.91251 1.000 32.61728  ? 181 TYR A CD2  1 
ATOM   2800 C CE1  . TYR A 1 195 ? 11.40760  -6.89221  26.04674 1.000 33.66810  ? 181 TYR A CE1  1 
ATOM   2801 C CE2  . TYR A 1 195 ? 9.38590   -8.16848  25.94389 1.000 33.82326  ? 181 TYR A CE2  1 
ATOM   2802 C CZ   . TYR A 1 195 ? 10.76220  -8.11068  26.01022 1.000 36.87390  ? 181 TYR A CZ   1 
ATOM   2803 O OH   . TYR A 1 195 ? 11.49764  -9.27284  26.04029 1.000 40.76133  ? 181 TYR A OH   1 
ATOM   2804 H H    . TYR A 1 195 ? 10.00589  -2.92878  24.36372 1.000 29.57254  ? 181 TYR A H    1 
ATOM   2805 H HA   . TYR A 1 195 ? 7.85870   -4.56299  23.97572 1.000 32.43252  ? 181 TYR A HA   1 
ATOM   2806 H HB2  . TYR A 1 195 ? 8.93907   -3.82999  26.47263 1.000 34.71216  ? 181 TYR A HB2  1 
ATOM   2807 H HB3  . TYR A 1 195 ? 7.60422   -4.67211  26.28708 1.000 34.71216  ? 181 TYR A HB3  1 
ATOM   2808 H HD1  . TYR A 1 195 ? 11.10596  -4.90787  26.04412 1.000 38.26373  ? 181 TYR A HD1  1 
ATOM   2809 H HD2  . TYR A 1 195 ? 7.72696   -7.03643  25.86641 1.000 39.19667  ? 181 TYR A HD2  1 
ATOM   2810 H HE1  . TYR A 1 195 ? 12.33583  -6.85572  26.09091 1.000 40.45765  ? 181 TYR A HE1  1 
ATOM   2811 H HE2  . TYR A 1 195 ? 8.95249   -8.99098  25.92043 1.000 40.64385  ? 181 TYR A HE2  1 
ATOM   2812 H HH   . TYR A 1 195 ? 10.98466  -9.93788  26.02720 1.000 48.96954  ? 181 TYR A HH   1 
ATOM   2813 N N    . GLN A 1 196 ? 6.23358   -2.72054  24.03083 1.000 30.18810  ? 182 GLN A N    1 
ATOM   2814 C CA   . GLN A 1 196 ? 5.40956   -1.54678  23.78396 1.000 30.17834  ? 182 GLN A CA   1 
ATOM   2815 C C    . GLN A 1 196 ? 4.01399   -1.72961  24.36382 1.000 31.34999  ? 182 GLN A C    1 
ATOM   2816 O O    . GLN A 1 196 ? 3.51678   -2.85059  24.50114 1.000 30.93523  ? 182 GLN A O    1 
ATOM   2817 C CB   . GLN A 1 196 ? 5.31619   -1.26574  22.27699 1.000 27.60100  ? 182 GLN A CB   1 
ATOM   2818 C CG   . GLN A 1 196 ? 4.52160   -0.02785  21.90222 1.000 31.65946  ? 182 GLN A CG   1 
ATOM   2819 C CD   . GLN A 1 196 ? 4.54097   0.24731   20.40648 1.000 31.22739  ? 182 GLN A CD   1 
ATOM   2820 O OE1  . GLN A 1 196 ? 5.37648   -0.28402  19.67455 1.000 25.21048  ? 182 GLN A OE1  1 
ATOM   2821 N NE2  . GLN A 1 196 ? 3.61472   1.08016   19.94705 1.000 31.84561  ? 182 GLN A NE2  1 
ATOM   2822 H H    . GLN A 1 196 ? 5.86155   -3.45981  23.79703 1.000 36.28166  ? 182 GLN A H    1 
ATOM   2823 H HA   . GLN A 1 196 ? 5.80046   -0.77959  24.23063 1.000 36.26995  ? 182 GLN A HA   1 
ATOM   2824 H HB2  . GLN A 1 196 ? 6.21469   -1.15039  21.93017 1.000 33.17714  ? 182 GLN A HB2  1 
ATOM   2825 H HB3  . GLN A 1 196 ? 4.89035   -2.02501  21.84911 1.000 33.17714  ? 182 GLN A HB3  1 
ATOM   2826 H HG2  . GLN A 1 196 ? 3.59837   -0.14975  22.17367 1.000 38.04730  ? 182 GLN A HG2  1 
ATOM   2827 H HG3  . GLN A 1 196 ? 4.90157   0.74152   22.35452 1.000 38.04730  ? 182 GLN A HG3  1 
ATOM   2828 H HE21 . GLN A 1 196 ? 3.04600   1.43155   20.48804 1.000 38.27067  ? 182 GLN A HE21 1 
ATOM   2829 H HE22 . GLN A 1 196 ? 3.58346   1.26825   19.10845 1.000 38.27067  ? 182 GLN A HE22 1 
ATOM   2830 N N    . GLN A 1 197 ? 3.38737   -0.60223  24.69751 1.000 34.54163  ? 183 GLN A N    1 
ATOM   2831 C CA   . GLN A 1 197 ? 2.01492   -0.57008  25.18638 1.000 40.02577  ? 183 GLN A CA   1 
ATOM   2832 C C    . GLN A 1 197 ? 1.39987   0.76246   24.78790 1.000 37.09803  ? 183 GLN A C    1 
ATOM   2833 O O    . GLN A 1 197 ? 1.99797   1.81494   25.02936 1.000 36.46488  ? 183 GLN A O    1 
ATOM   2834 C CB   . GLN A 1 197 ? 1.96179   -0.74622  26.70828 1.000 41.91390  ? 183 GLN A CB   1 
ATOM   2835 C CG   . GLN A 1 197 ? 0.67374   -0.24888  27.35539 1.000 51.53368  ? 183 GLN A CG   1 
ATOM   2836 C CD   . GLN A 1 197 ? -0.40329  -1.31535  27.43193 1.000 60.35442  ? 183 GLN A CD   1 
ATOM   2837 O OE1  . GLN A 1 197 ? -0.30927  -2.25234  28.22634 1.000 67.97535  ? 183 GLN A OE1  1 
ATOM   2838 N NE2  . GLN A 1 197 ? -1.43690  -1.17557  26.60802 1.000 57.01712  ? 183 GLN A NE2  1 
ATOM   2839 H H    . GLN A 1 197 ? 3.74738   0.17718   24.64750 1.000 41.50590  ? 183 GLN A H    1 
ATOM   2840 H HA   . GLN A 1 197 ? 1.50315   -1.28773  24.78144 1.000 48.08687  ? 183 GLN A HA   1 
ATOM   2841 N N    . ASN A 1 198 ? 0.22004   0.71748   24.17511 1.000 30.99534  ? 184 ASN A N    1 
ATOM   2842 C CA   . ASN A 1 198 ? -0.51409  1.91854   23.80337 1.000 32.38189  ? 184 ASN A CA   1 
ATOM   2843 C C    . ASN A 1 198 ? -1.88467  1.90963   24.46736 1.000 35.54917  ? 184 ASN A C    1 
ATOM   2844 O O    . ASN A 1 198 ? -2.57922  0.88829   24.46797 1.000 32.74083  ? 184 ASN A O    1 
ATOM   2845 C CB   . ASN A 1 198 ? -0.67771  2.03536   22.28170 1.000 33.90731  ? 184 ASN A CB   1 
ATOM   2846 C CG   . ASN A 1 198 ? 0.65067   2.15491   21.55318 1.000 32.15555  ? 184 ASN A CG   1 
ATOM   2847 O OD1  . ASN A 1 198 ? 1.59754   1.41930   21.83250 1.000 33.07370  ? 184 ASN A OD1  1 
ATOM   2848 N ND2  . ASN A 1 198 ? 0.72524   3.09168   20.61371 1.000 32.08141  ? 184 ASN A ND2  1 
ATOM   2849 H H    . ASN A 1 198 ? -0.18127  -0.01242  23.96112 1.000 37.25035  ? 184 ASN A H    1 
ATOM   2850 H HA   . ASN A 1 198 ? -0.02528  2.69682   24.11361 1.000 38.91421  ? 184 ASN A HA   1 
ATOM   2851 H HB2  . ASN A 1 198 ? -1.13058  1.24384   21.95108 1.000 40.74471  ? 184 ASN A HB2  1 
ATOM   2852 H HB3  . ASN A 1 198 ? -1.20214  2.82612   22.08025 1.000 40.74471  ? 184 ASN A HB3  1 
ATOM   2853 H HD21 . ASN A 1 198 ? 1.45501   3.20043   20.17187 1.000 38.55363  ? 184 ASN A HD21 1 
ATOM   2854 H HD22 . ASN A 1 198 ? 0.04374   3.58921   20.44752 1.000 38.55363  ? 184 ASN A HD22 1 
ATOM   2855 N N    . THR A 1 199 ? -2.26925  3.05741   25.02846 1.000 33.80017  ? 185 THR A N    1 
ATOM   2856 C CA   . THR A 1 199 ? -3.54810  3.23182   25.69895 1.000 33.52850  ? 185 THR A CA   1 
ATOM   2857 C C    . THR A 1 199 ? -4.16577  4.55146   25.25511 1.000 33.89294  ? 185 THR A C    1 
ATOM   2858 O O    . THR A 1 199 ? -3.44975  5.55546   25.12256 1.000 33.32917  ? 185 THR A O    1 
ATOM   2859 C CB   . THR A 1 199 ? -3.39121  3.22659   27.22541 1.000 37.06878  ? 185 THR A CB   1 
ATOM   2860 O OG1  . THR A 1 199 ? -2.37750  4.16460   27.60537 1.000 46.22988  ? 185 THR A OG1  1 
ATOM   2861 C CG2  . THR A 1 199 ? -3.00590  1.84458   27.71944 1.000 42.98750  ? 185 THR A CG2  1 
ATOM   2862 H H    . THR A 1 199 ? -1.78739  3.76973   25.03117 1.000 40.61615  ? 185 THR A H    1 
ATOM   2863 H HA   . THR A 1 199 ? -4.14462  2.50987   25.44627 1.000 40.29014  ? 185 THR A HA   1 
ATOM   2864 H HB   . THR A 1 199 ? -4.23402  3.47353   27.63723 1.000 44.53848  ? 185 THR A HB   1 
ATOM   2865 H HG1  . THR A 1 199 ? -2.53885  4.91549   27.26517 1.000 55.53180  ? 185 THR A HG1  1 
ATOM   2866 H HG21 . THR A 1 199 ? -2.08042  1.65858   27.49631 1.000 51.64094  ? 185 THR A HG21 1 
ATOM   2867 H HG22 . THR A 1 199 ? -3.11385  1.79434   28.68210 1.000 51.64094  ? 185 THR A HG22 1 
ATOM   2868 H HG23 . THR A 1 199 ? -3.57072  1.17432   27.30393 1.000 51.64094  ? 185 THR A HG23 1 
ATOM   2869 N N    . PRO A 1 200 ? -5.47888  4.59024   25.03270 1.000 35.45872  ? 186 PRO A N    1 
ATOM   2870 C CA   . PRO A 1 200 ? -6.09820  5.81597   24.51672 1.000 36.78536  ? 186 PRO A CA   1 
ATOM   2871 C C    . PRO A 1 200 ? -6.12073  6.93078   25.54902 1.000 36.86088  ? 186 PRO A C    1 
ATOM   2872 O O    . PRO A 1 200 ? -6.21197  6.69608   26.75597 1.000 38.64627  ? 186 PRO A O    1 
ATOM   2873 C CB   . PRO A 1 200 ? -7.52000  5.36940   24.15488 1.000 38.86945  ? 186 PRO A CB   1 
ATOM   2874 C CG   . PRO A 1 200 ? -7.78509  4.21135   25.04208 1.000 37.51146  ? 186 PRO A CG   1 
ATOM   2875 C CD   . PRO A 1 200 ? -6.46690  3.51262   25.22274 1.000 40.66003  ? 186 PRO A CD   1 
ATOM   2876 H HA   . PRO A 1 200 ? -5.63156  6.12261   23.72355 1.000 44.19838  ? 186 PRO A HA   1 
ATOM   2877 H HB2  . PRO A 1 200 ? -8.14727  6.08951   24.32480 1.000 46.69928  ? 186 PRO A HB2  1 
ATOM   2878 H HB3  . PRO A 1 200 ? -7.55853  5.10926   23.22121 1.000 46.69928  ? 186 PRO A HB3  1 
ATOM   2879 H HG2  . PRO A 1 200 ? -8.12602  4.52500   25.89431 1.000 44.73405  ? 186 PRO A HG2  1 
ATOM   2880 H HG3  . PRO A 1 200 ? -8.43096  3.62109   24.62334 1.000 44.73405  ? 186 PRO A HG3  1 
ATOM   2881 H HD2  . PRO A 1 200 ? -6.39678  3.13379   26.11295 1.000 48.84798  ? 186 PRO A HD2  1 
ATOM   2882 H HD3  . PRO A 1 200 ? -6.35113  2.81741   24.55627 1.000 48.84798  ? 186 PRO A HD3  1 
ATOM   2883 N N    . ILE A 1 201 ? -6.04035  8.16560   25.05152 1.000 39.42892  ? 187 ILE A N    1 
ATOM   2884 C CA   . ILE A 1 201 ? -6.11828  9.32568   25.93269 1.000 41.70908  ? 187 ILE A CA   1 
ATOM   2885 C C    . ILE A 1 201 ? -7.57001  9.66815   26.23925 1.000 42.60550  ? 187 ILE A C    1 
ATOM   2886 O O    . ILE A 1 201 ? -7.90309  10.05543  27.36422 1.000 51.53783  ? 187 ILE A O    1 
ATOM   2887 C CB   . ILE A 1 201 ? -5.37625  10.51975  25.30384 1.000 42.60849  ? 187 ILE A CB   1 
ATOM   2888 C CG1  . ILE A 1 201 ? -3.89618  10.17992  25.10945 1.000 38.27992  ? 187 ILE A CG1  1 
ATOM   2889 C CG2  . ILE A 1 201 ? -5.53191  11.76513  26.17316 1.000 42.61658  ? 187 ILE A CG2  1 
ATOM   2890 C CD1  . ILE A 1 201 ? -3.09989  11.25661  24.39538 1.000 42.14589  ? 187 ILE A CD1  1 
ATOM   2891 H H    . ILE A 1 201 ? -5.94190  8.35486   24.21840 1.000 47.37064  ? 187 ILE A H    1 
ATOM   2892 H HA   . ILE A 1 201 ? -5.67922  9.10780   26.76974 1.000 50.10684  ? 187 ILE A HA   1 
ATOM   2893 H HB   . ILE A 1 201 ? -5.76832  10.70221  24.43558 1.000 51.18613  ? 187 ILE A HB   1 
ATOM   2894 H HG12 . ILE A 1 201 ? -3.49201  10.04405  25.98070 1.000 45.99184  ? 187 ILE A HG12 1 
ATOM   2895 H HG13 . ILE A 1 201 ? -3.83085  9.36775   24.58312 1.000 45.99184  ? 187 ILE A HG13 1 
ATOM   2896 H HG21 . ILE A 1 201 ? -6.46941  12.01185  26.20648 1.000 51.19583  ? 187 ILE A HG21 1 
ATOM   2897 H HG22 . ILE A 1 201 ? -5.20957  11.56883  27.06673 1.000 51.19583  ? 187 ILE A HG22 1 
ATOM   2898 H HG23 . ILE A 1 201 ? -5.01332  12.48754  25.78573 1.000 51.19583  ? 187 ILE A HG23 1 
ATOM   2899 H HD11 . ILE A 1 201 ? -2.97631  12.00846  24.99567 1.000 50.63101  ? 187 ILE A HD11 1 
ATOM   2900 H HD12 . ILE A 1 201 ? -2.23796  10.89362  24.13806 1.000 50.63101  ? 187 ILE A HD12 1 
ATOM   2901 H HD13 . ILE A 1 201 ? -3.58832  11.53987  23.60664 1.000 50.63101  ? 187 ILE A HD13 1 
ATOM   2902 N N    . GLY A 1 202 ? -8.45449  9.53413   25.24892 1.000 47.04296  ? 188 GLY A N    1 
ATOM   2903 C CA   . GLY A 1 202 ? -9.85398  9.85305   25.42578 1.000 51.81835  ? 188 GLY A CA   1 
ATOM   2904 C C    . GLY A 1 202 ? -10.66194 8.67621   25.94425 1.000 53.56948  ? 188 GLY A C    1 
ATOM   2905 O O    . GLY A 1 202 ? -10.15605 7.57832   26.17182 1.000 49.90757  ? 188 GLY A O    1 
ATOM   2906 H H    . GLY A 1 202 ? -8.25764  9.25638   24.45918 1.000 56.50749  ? 188 GLY A H    1 
ATOM   2907 H HA2  . GLY A 1 202 ? -9.93816  10.58280  26.05925 1.000 62.23796  ? 188 GLY A HA2  1 
ATOM   2908 H HA3  . GLY A 1 202 ? -10.22924 10.12867  24.57483 1.000 62.23796  ? 188 GLY A HA3  1 
ATOM   2909 N N    . ASP A 1 203 ? -11.95569 8.92856   26.13301 1.000 62.66622  ? 189 ASP A N    1 
ATOM   2910 C CA   . ASP A 1 203 ? -12.88692 7.92777   26.63209 1.000 65.58775  ? 189 ASP A CA   1 
ATOM   2911 C C    . ASP A 1 203 ? -13.76704 7.34906   25.53171 1.000 66.40944  ? 189 ASP A C    1 
ATOM   2912 O O    . ASP A 1 203 ? -14.69735 6.59369   25.82981 1.000 69.81784  ? 189 ASP A O    1 
ATOM   2913 C CB   . ASP A 1 203 ? -13.76237 8.52988   27.73414 1.000 65.40813  ? 189 ASP A CB   1 
ATOM   2914 C CG   . ASP A 1 203 ? -12.94717 9.15270   28.85214 1.000 69.52232  ? 189 ASP A CG   1 
ATOM   2915 O OD1  . ASP A 1 203 ? -11.82095 8.67531   29.10754 1.000 72.43042  ? 189 ASP A OD1  1 
ATOM   2916 O OD2  . ASP A 1 203 ? -13.43247 10.12075  29.47542 1.000 67.61660  ? 189 ASP A OD2  1 
ATOM   2917 H H    . ASP A 1 203 ? -12.32282 9.68997   25.97468 1.000 75.25541  ? 189 ASP A H    1 
ATOM   2918 H HA   . ASP A 1 203 ? -12.37695 7.19878   27.01862 1.000 78.76124  ? 189 ASP A HA   1 
ATOM   2919 H HB2  . ASP A 1 203 ? -14.32363 9.22159   27.35019 1.000 78.54569  ? 189 ASP A HB2  1 
ATOM   2920 H HB3  . ASP A 1 203 ? -14.31383 7.83032   28.11809 1.000 78.54569  ? 189 ASP A HB3  1 
ATOM   2921 N N    . GLY A 1 204 ? -13.49740 7.68274   24.27213 1.000 63.50799  ? 190 GLY A N    1 
ATOM   2922 C CA   . GLY A 1 204 ? -14.29027 7.19311   23.17070 1.000 64.31117  ? 190 GLY A CA   1 
ATOM   2923 C C    . GLY A 1 204 ? -13.99237 5.74258   22.85177 1.000 64.66007  ? 190 GLY A C    1 
ATOM   2924 O O    . GLY A 1 204 ? -12.95637 5.19647   23.24450 1.000 65.66258  ? 190 GLY A O    1 
ATOM   2925 H H    . GLY A 1 204 ? -12.85083 8.19810   24.03558 1.000 76.26553  ? 190 GLY A H    1 
ATOM   2926 H HA2  . GLY A 1 204 ? -15.23148 7.27122   23.39190 1.000 77.22935  ? 190 GLY A HA2  1 
ATOM   2927 H HA3  . GLY A 1 204 ? -14.10642 7.72468   22.38043 1.000 77.22935  ? 190 GLY A HA3  1 
ATOM   2928 N N    . PRO A 1 205 ? -14.90010 5.08529   22.12984 1.000 68.39165  ? 191 PRO A N    1 
ATOM   2929 C CA   . PRO A 1 205 ? -14.67224 3.67822   21.77281 1.000 66.81167  ? 191 PRO A CA   1 
ATOM   2930 C C    . PRO A 1 205 ? -13.54797 3.55041   20.75546 1.000 61.27923  ? 191 PRO A C    1 
ATOM   2931 O O    . PRO A 1 205 ? -13.51508 4.26463   19.75078 1.000 56.72629  ? 191 PRO A O    1 
ATOM   2932 C CB   . PRO A 1 205 ? -16.02013 3.23350   21.19246 1.000 60.11244  ? 191 PRO A CB   1 
ATOM   2933 C CG   . PRO A 1 205 ? -16.64429 4.48978   20.68724 1.000 65.45973  ? 191 PRO A CG   1 
ATOM   2934 C CD   . PRO A 1 205 ? -16.18668 5.58708   21.61342 1.000 71.88318  ? 191 PRO A CD   1 
ATOM   2935 H HA   . PRO A 1 205 ? -14.46421 3.14930   22.55885 1.000 80.22994  ? 191 PRO A HA   1 
ATOM   2936 H HB2  . PRO A 1 205 ? -15.87827 2.60027   20.47149 1.000 72.19087  ? 191 PRO A HB2  1 
ATOM   2937 H HB3  . PRO A 1 205 ? -16.56328 2.82920   21.88704 1.000 72.19087  ? 191 PRO A HB3  1 
ATOM   2938 H HG2  . PRO A 1 205 ? -16.34550 4.66034   19.78030 1.000 78.60762  ? 191 PRO A HG2  1 
ATOM   2939 H HG3  . PRO A 1 205 ? -17.61036 4.40494   20.70784 1.000 78.60762  ? 191 PRO A HG3  1 
ATOM   2940 H HD2  . PRO A 1 205 ? -16.06296 6.41808   21.12862 1.000 86.31575  ? 191 PRO A HD2  1 
ATOM   2941 H HD3  . PRO A 1 205 ? -16.82139 5.71563   22.33558 1.000 86.31575  ? 191 PRO A HD3  1 
ATOM   2942 N N    . VAL A 1 206 ? -12.62278 2.63623   21.02845 1.000 52.83112  ? 192 VAL A N    1 
ATOM   2943 C CA   . VAL A 1 206 ? -11.48995 2.38586   20.15357 1.000 41.86945  ? 192 VAL A CA   1 
ATOM   2944 C C    . VAL A 1 206 ? -11.62459 0.98442   19.56500 1.000 42.04333  ? 192 VAL A C    1 
ATOM   2945 O O    . VAL A 1 206 ? -12.49068 0.19959   19.95190 1.000 36.62706  ? 192 VAL A O    1 
ATOM   2946 C CB   . VAL A 1 206 ? -10.14426 2.55163   20.88742 1.000 42.82302  ? 192 VAL A CB   1 
ATOM   2947 C CG1  . VAL A 1 206 ? -9.98633  3.97843   21.38872 1.000 43.11331  ? 192 VAL A CG1  1 
ATOM   2948 C CG2  . VAL A 1 206 ? -10.03449 1.56027   22.04041 1.000 42.00647  ? 192 VAL A CG2  1 
ATOM   2949 H H    . VAL A 1 206 ? -12.63209 2.13914   21.73018 1.000 63.45328  ? 192 VAL A H    1 
ATOM   2950 H HA   . VAL A 1 206 ? -11.51292 3.02458   19.42391 1.000 50.29928  ? 192 VAL A HA   1 
ATOM   2951 H HB   . VAL A 1 206 ? -9.42334  2.36720   20.26520 1.000 51.44356  ? 192 VAL A HB   1 
ATOM   2952 H HG11 . VAL A 1 206 ? -10.67643 4.53141   20.99011 1.000 51.79192  ? 192 VAL A HG11 1 
ATOM   2953 H HG12 . VAL A 1 206 ? -10.07389 3.98527   22.35474 1.000 51.79192  ? 192 VAL A HG12 1 
ATOM   2954 H HG13 . VAL A 1 206 ? -9.11028  4.30763   21.13366 1.000 51.79192  ? 192 VAL A HG13 1 
ATOM   2955 H HG21 . VAL A 1 206 ? -9.20320  1.71822   22.51465 1.000 50.46370  ? 192 VAL A HG21 1 
ATOM   2956 H HG22 . VAL A 1 206 ? -10.78655 1.68816   22.63954 1.000 50.46370  ? 192 VAL A HG22 1 
ATOM   2957 H HG23 . VAL A 1 206 ? -10.04551 0.65837   21.68356 1.000 50.46370  ? 192 VAL A HG23 1 
ATOM   2958 N N    . LEU A 1 207 ? -10.74801 0.67584   18.61509 1.000 37.55396  ? 193 LEU A N    1 
ATOM   2959 C CA   . LEU A 1 207 ? -10.70636 -0.63161  17.97677 1.000 34.30970  ? 193 LEU A CA   1 
ATOM   2960 C C    . LEU A 1 207 ? -9.64209  -1.48234  18.65806 1.000 33.07525  ? 193 LEU A C    1 
ATOM   2961 O O    . LEU A 1 207 ? -8.45579  -1.14116  18.62238 1.000 33.91161  ? 193 LEU A O    1 
ATOM   2962 C CB   . LEU A 1 207 ? -10.40253 -0.50449  16.48433 1.000 34.97062  ? 193 LEU A CB   1 
ATOM   2963 C CG   . LEU A 1 207 ? -11.42760 0.20840   15.60307 1.000 34.25501  ? 193 LEU A CG   1 
ATOM   2964 C CD1  . LEU A 1 207 ? -10.94270 0.22945   14.15821 1.000 35.75131  ? 193 LEU A CD1  1 
ATOM   2965 C CD2  . LEU A 1 207 ? -12.78949 -0.45864  15.70341 1.000 37.47140  ? 193 LEU A CD2  1 
ATOM   2966 H H    . LEU A 1 207 ? -10.15369 1.22154   18.31744 1.000 45.12069  ? 193 LEU A H    1 
ATOM   2967 H HA   . LEU A 1 207 ? -11.56820 -1.06460  18.08001 1.000 41.22759  ? 193 LEU A HA   1 
ATOM   2968 H HB2  . LEU A 1 207 ? -9.56935  -0.01611  16.39372 1.000 42.02069  ? 193 LEU A HB2  1 
ATOM   2969 H HB3  . LEU A 1 207 ? -10.30245 -1.40052  16.12655 1.000 42.02069  ? 193 LEU A HB3  1 
ATOM   2970 H HG   . LEU A 1 207 ? -11.52927 1.12336   15.90871 1.000 41.16195  ? 193 LEU A HG   1 
ATOM   2971 H HD11 . LEU A 1 207 ? -10.03052 0.55860   14.13599 1.000 42.95751  ? 193 LEU A HD11 1 
ATOM   2972 H HD12 . LEU A 1 207 ? -10.97815 -0.67131  13.80005 1.000 42.95751  ? 193 LEU A HD12 1 
ATOM   2973 H HD13 . LEU A 1 207 ? -11.51804 0.81415   13.64051 1.000 42.95751  ? 193 LEU A HD13 1 
ATOM   2974 H HD21 . LEU A 1 207 ? -12.68466 -1.41300  15.56518 1.000 45.02162  ? 193 LEU A HD21 1 
ATOM   2975 H HD22 . LEU A 1 207 ? -13.15929 -0.29065  16.58428 1.000 45.02162  ? 193 LEU A HD22 1 
ATOM   2976 H HD23 . LEU A 1 207 ? -13.37351 -0.08809  15.02332 1.000 45.02162  ? 193 LEU A HD23 1 
ATOM   2977 N N    . LEU A 1 208 ? -10.06485 -2.58309  19.27482 1.000 35.22128  ? 194 LEU A N    1 
ATOM   2978 C CA   . LEU A 1 208 ? -9.12763  -3.55493  19.82290 1.000 32.85797  ? 194 LEU A CA   1 
ATOM   2979 C C    . LEU A 1 208 ? -8.86549  -4.63083  18.77842 1.000 33.45210  ? 194 LEU A C    1 
ATOM   2980 O O    . LEU A 1 208 ? -9.80454  -5.33685  18.38712 1.000 38.71667  ? 194 LEU A O    1 
ATOM   2981 C CB   . LEU A 1 208 ? -9.67377  -4.18058  21.09535 1.000 32.44616  ? 194 LEU A CB   1 
ATOM   2982 C CG   . LEU A 1 208 ? -9.78104  -3.25035  22.30779 1.000 35.15444  ? 194 LEU A CG   1 
ATOM   2983 C CD1  . LEU A 1 208 ? -10.16537 -4.03685  23.55065 1.000 48.69417  ? 194 LEU A CD1  1 
ATOM   2984 C CD2  . LEU A 1 208 ? -8.48462  -2.48629  22.54311 1.000 41.35318  ? 194 LEU A CD2  1 
ATOM   2985 H H    . LEU A 1 208 ? -10.89200 -2.78933  19.38834 1.000 42.32147  ? 194 LEU A H    1 
ATOM   2986 H HA   . LEU A 1 208 ? -8.28927  -3.11947  20.04299 1.000 39.48551  ? 194 LEU A HA   1 
ATOM   2987 H HB2  . LEU A 1 208 ? -10.56533 -4.51459  20.90969 1.000 38.99134  ? 194 LEU A HB2  1 
ATOM   2988 H HB3  . LEU A 1 208 ? -9.09044  -4.91377  21.34645 1.000 38.99134  ? 194 LEU A HB3  1 
ATOM   2989 H HG   . LEU A 1 208 ? -10.47555 -2.59730  22.12868 1.000 42.24126  ? 194 LEU A HG   1 
ATOM   2990 H HD11 . LEU A 1 208 ? -9.48702  -4.70883  23.72145 1.000 58.48895  ? 194 LEU A HD11 1 
ATOM   2991 H HD12 . LEU A 1 208 ? -10.22505 -3.42824  24.30360 1.000 58.48895  ? 194 LEU A HD12 1 
ATOM   2992 H HD13 . LEU A 1 208 ? -11.02357 -4.46363  23.40147 1.000 58.48895  ? 194 LEU A HD13 1 
ATOM   2993 H HD21 . LEU A 1 208 ? -8.48659  -2.13143  23.44586 1.000 49.67975  ? 194 LEU A HD21 1 
ATOM   2994 H HD22 . LEU A 1 208 ? -7.73572  -3.09181  22.42735 1.000 49.67975  ? 194 LEU A HD22 1 
ATOM   2995 H HD23 . LEU A 1 208 ? -8.42514  -1.76038  21.90247 1.000 49.67975  ? 194 LEU A HD23 1 
ATOM   2996 N N    . PRO A 1 209 ? -7.63307  -4.79519  18.30454 1.000 31.83638  ? 195 PRO A N    1 
ATOM   2997 C CA   . PRO A 1 209 ? -7.39380  -5.65153  17.14338 1.000 31.85075  ? 195 PRO A CA   1 
ATOM   2998 C C    . PRO A 1 209 ? -7.11883  -7.10458  17.48782 1.000 31.60883  ? 195 PRO A C    1 
ATOM   2999 O O    . PRO A 1 209 ? -6.59053  -7.44287  18.54754 1.000 32.21037  ? 195 PRO A O    1 
ATOM   3000 C CB   . PRO A 1 209 ? -6.14479  -5.01182  16.52143 1.000 30.47624  ? 195 PRO A CB   1 
ATOM   3001 C CG   . PRO A 1 209 ? -5.36946  -4.55924  17.70825 1.000 33.19530  ? 195 PRO A CG   1 
ATOM   3002 C CD   . PRO A 1 209 ? -6.39041  -4.13463  18.74797 1.000 35.20360  ? 195 PRO A CD   1 
ATOM   3003 H HA   . PRO A 1 209 ? -8.15060  -5.61194  16.53791 1.000 38.27684  ? 195 PRO A HA   1 
ATOM   3004 H HB2  . PRO A 1 209 ? -5.65085  -5.66798  16.00532 1.000 36.62743  ? 195 PRO A HB2  1 
ATOM   3005 H HB3  . PRO A 1 209 ? -6.39438  -4.26437  15.95581 1.000 36.62743  ? 195 PRO A HB3  1 
ATOM   3006 H HG2  . PRO A 1 209 ? -4.82701  -5.29136  18.04090 1.000 39.89030  ? 195 PRO A HG2  1 
ATOM   3007 H HG3  . PRO A 1 209 ? -4.80254  -3.81207  17.46080 1.000 39.89030  ? 195 PRO A HG3  1 
ATOM   3008 H HD2  . PRO A 1 209 ? -6.13216  -4.44427  19.63019 1.000 42.30026  ? 195 PRO A HD2  1 
ATOM   3009 H HD3  . PRO A 1 209 ? -6.49613  -3.17042  18.75256 1.000 42.30026  ? 195 PRO A HD3  1 
ATOM   3010 N N    . ASP A 1 210 ? -7.48850  -7.97214  16.55150 1.000 27.98954  ? 196 ASP A N    1 
ATOM   3011 C CA   . ASP A 1 210 ? -6.94264  -9.31642  16.54382 1.000 32.79561  ? 196 ASP A CA   1 
ATOM   3012 C C    . ASP A 1 210 ? -5.44188  -9.24890  16.26292 1.000 31.12755  ? 196 ASP A C    1 
ATOM   3013 O O    . ASP A 1 210 ? -4.90280  -8.21321  15.86027 1.000 28.61732  ? 196 ASP A O    1 
ATOM   3014 C CB   . ASP A 1 210 ? -7.64463  -10.17785 15.49650 1.000 32.05501  ? 196 ASP A CB   1 
ATOM   3015 C CG   . ASP A 1 210 ? -9.13397  -10.30427 15.74553 1.000 33.98753  ? 196 ASP A CG   1 
ATOM   3016 O OD1  . ASP A 1 210 ? -9.61627  -9.78809  16.77412 1.000 37.40523  ? 196 ASP A OD1  1 
ATOM   3017 O OD2  . ASP A 1 210 ? -9.82434  -10.92204 14.90856 1.000 38.80572  ? 196 ASP A OD2  1 
ATOM   3018 H H    . ASP A 1 210 ? -8.04699  -7.80594  15.91899 1.000 33.64339  ? 196 ASP A H    1 
ATOM   3019 H HA   . ASP A 1 210 ? -7.08362  -9.73547  17.40720 1.000 39.41067  ? 196 ASP A HA   1 
ATOM   3020 H HB2  . ASP A 1 210 ? -7.51952  -9.77719  14.62202 1.000 38.52195  ? 196 ASP A HB2  1 
ATOM   3021 H HB3  . ASP A 1 210 ? -7.26121  -11.06873 15.51117 1.000 38.52195  ? 196 ASP A HB3  1 
ATOM   3022 N N    . ASN A 1 211 ? -4.76198  -10.37136 16.47667 1.000 29.79463  ? 197 ASN A N    1 
ATOM   3023 C CA   . ASN A 1 211 ? -3.31761  -10.40302 16.29203 1.000 30.17697  ? 197 ASN A CA   1 
ATOM   3024 C C    . ASN A 1 211 ? -2.95490  -10.05127 14.85368 1.000 29.39198  ? 197 ASN A C    1 
ATOM   3025 O O    . ASN A 1 211 ? -3.61146  -10.48573 13.90390 1.000 29.07350  ? 197 ASN A O    1 
ATOM   3026 C CB   . ASN A 1 211 ? -2.76944  -11.78286 16.65231 1.000 30.02224  ? 197 ASN A CB   1 
ATOM   3027 C CG   . ASN A 1 211 ? -3.14881  -12.21125 18.05457 1.000 31.46451  ? 197 ASN A CG   1 
ATOM   3028 O OD1  . ASN A 1 211 ? -3.23293  -11.38960 18.96757 1.000 35.22386  ? 197 ASN A OD1  1 
ATOM   3029 N ND2  . ASN A 1 211 ? -3.38542  -13.50430 18.23163 1.000 30.03112  ? 197 ASN A ND2  1 
ATOM   3030 H H    . ASN A 1 211 ? -5.10916  -11.11770 16.72574 1.000 35.80950  ? 197 ASN A H    1 
ATOM   3031 H HA   . ASN A 1 211 ? -2.90365  -9.75053  16.87837 1.000 36.26831  ? 197 ASN A HA   1 
ATOM   3032 H HB2  . ASN A 1 211 ? -3.12563  -12.43730 16.03124 1.000 36.08263  ? 197 ASN A HB2  1 
ATOM   3033 H HB3  . ASN A 1 211 ? -1.80130  -11.76391 16.59524 1.000 36.08263  ? 197 ASN A HB3  1 
ATOM   3034 H HD21 . ASN A 1 211 ? -3.60450  -13.79881 19.00936 1.000 36.09328  ? 197 ASN A HD21 1 
ATOM   3035 H HD22 . ASN A 1 211 ? -3.31976  -14.04818 17.56869 1.000 36.09328  ? 197 ASN A HD22 1 
ATOM   3036 N N    . HIS A 1 212 ? -1.90713  -9.25427  14.69946 1.000 28.41533  ? 198 HIS A N    1 
ATOM   3037 C CA   . HIS A 1 212 ? -1.40669  -8.83648  13.39119 1.000 31.36751  ? 198 HIS A CA   1 
ATOM   3038 C C    . HIS A 1 212 ? -0.03772  -8.20125  13.61295 1.000 28.27913  ? 198 HIS A C    1 
ATOM   3039 O O    . HIS A 1 212 ? 0.49859   -8.22553  14.72777 1.000 28.36355  ? 198 HIS A O    1 
ATOM   3040 C CB   . HIS A 1 212 ? -2.38594  -7.88773  12.69647 1.000 27.39133  ? 198 HIS A CB   1 
ATOM   3041 C CG   . HIS A 1 212 ? -2.48247  -6.53796  13.33527 1.000 31.04853  ? 198 HIS A CG   1 
ATOM   3042 N ND1  . HIS A 1 212 ? -3.21310  -6.30562  14.48066 1.000 32.10926  ? 198 HIS A ND1  1 
ATOM   3043 C CD2  . HIS A 1 212 ? -1.95054  -5.34461  12.97961 1.000 29.22536  ? 198 HIS A CD2  1 
ATOM   3044 C CE1  . HIS A 1 212 ? -3.12154  -5.02859  14.80676 1.000 33.84683  ? 198 HIS A CE1  1 
ATOM   3045 N NE2  . HIS A 1 212 ? -2.36162  -4.42335  13.91184 1.000 29.03446  ? 198 HIS A NE2  1 
ATOM   3046 H H    . HIS A 1 212 ? -1.45401  -8.93133  15.35520 1.000 34.15434  ? 198 HIS A H    1 
ATOM   3047 H HA   . HIS A 1 212 ? -1.29677  -9.61896  12.82856 1.000 37.69695  ? 198 HIS A HA   1 
ATOM   3048 H HB2  . HIS A 1 212 ? -2.09741  -7.76006  11.77922 1.000 32.92553  ? 198 HIS A HB2  1 
ATOM   3049 H HB3  . HIS A 1 212 ? -3.27014  -8.28620  12.71372 1.000 32.92553  ? 198 HIS A HB3  1 
ATOM   3050 H HD1  . HIS A 1 212 ? -3.65884  -6.89906  14.91510 1.000 38.58705  ? 198 HIS A HD1  1 
ATOM   3051 H HD2  . HIS A 1 212 ? -1.40838  -5.17963  12.24222 1.000 35.12637  ? 198 HIS A HD2  1 
ATOM   3052 H HE1  . HIS A 1 212 ? -3.52376  -4.62451  15.54150 1.000 40.67214  ? 198 HIS A HE1  1 
ATOM   3053 N N    . TYR A 1 213 ? 0.53658   -7.63380  12.55404 1.000 28.01667  ? 199 TYR A N    1 
ATOM   3054 C CA   . TYR A 1 213 ? 1.84050   -6.99867  12.66900 1.000 29.35225  ? 199 TYR A CA   1 
ATOM   3055 C C    . TYR A 1 213 ? 1.96261   -5.88062  11.64438 1.000 32.21389  ? 199 TYR A C    1 
ATOM   3056 O O    . TYR A 1 213 ? 1.22448   -5.82803  10.65701 1.000 25.44490  ? 199 TYR A O    1 
ATOM   3057 C CB   . TYR A 1 213 ? 2.97919   -8.01246  12.48565 1.000 26.67518  ? 199 TYR A CB   1 
ATOM   3058 C CG   . TYR A 1 213 ? 3.07992   -8.58247  11.08833 1.000 30.86764  ? 199 TYR A CG   1 
ATOM   3059 C CD1  . TYR A 1 213 ? 3.76158   -7.90155  10.08642 1.000 32.35221  ? 199 TYR A CD1  1 
ATOM   3060 C CD2  . TYR A 1 213 ? 2.50092   -9.80316  10.77190 1.000 31.73283  ? 199 TYR A CD2  1 
ATOM   3061 C CE1  . TYR A 1 213 ? 3.85765   -8.41533  8.81033  1.000 32.53072  ? 199 TYR A CE1  1 
ATOM   3062 C CE2  . TYR A 1 213 ? 2.59139   -10.32684 9.49389  1.000 35.77487  ? 199 TYR A CE2  1 
ATOM   3063 C CZ   . TYR A 1 213 ? 3.27252   -9.62851  8.51820  1.000 36.15289  ? 199 TYR A CZ   1 
ATOM   3064 O OH   . TYR A 1 213 ? 3.36883   -10.14126 7.24476  1.000 36.62071  ? 199 TYR A OH   1 
ATOM   3065 H H    . TYR A 1 213 ? 0.19203   -7.60530  11.76659 1.000 33.67595  ? 199 TYR A H    1 
ATOM   3066 H HA   . TYR A 1 213 ? 1.91547   -6.60191  13.55096 1.000 35.27864  ? 199 TYR A HA   1 
ATOM   3067 H HB2  . TYR A 1 213 ? 3.82075   -7.57377  12.68620 1.000 32.06616  ? 199 TYR A HB2  1 
ATOM   3068 H HB3  . TYR A 1 213 ? 2.83716   -8.75269  13.09622 1.000 32.06616  ? 199 TYR A HB3  1 
ATOM   3069 H HD1  . TYR A 1 213 ? 4.16037   -7.08408  10.28034 1.000 38.87859  ? 199 TYR A HD1  1 
ATOM   3070 H HD2  . TYR A 1 213 ? 2.04464   -10.27712 11.42922 1.000 38.13533  ? 199 TYR A HD2  1 
ATOM   3071 H HE1  . TYR A 1 213 ? 4.31477   -7.94576  8.15045  1.000 39.09281  ? 199 TYR A HE1  1 
ATOM   3072 H HE2  . TYR A 1 213 ? 2.19554   -11.14433 9.29410  1.000 42.98579  ? 199 TYR A HE2  1 
ATOM   3073 H HH   . TYR A 1 213 ? 2.94701   -10.86591 7.19417  1.000 44.00080  ? 199 TYR A HH   1 
ATOM   3074 N N    . LEU A 1 214 ? 2.91518   -4.98533  11.89672 1.000 29.67287  ? 200 LEU A N    1 
ATOM   3075 C CA   . LEU A 1 214 ? 3.26636   -3.91175  10.97795 1.000 32.47940  ? 200 LEU A CA   1 
ATOM   3076 C C    . LEU A 1 214 ? 4.62144   -4.21680  10.35515 1.000 29.39070  ? 200 LEU A C    1 
ATOM   3077 O O    . LEU A 1 214 ? 5.58566   -4.50957  11.07085 1.000 28.20049  ? 200 LEU A O    1 
ATOM   3078 C CB   . LEU A 1 214 ? 3.31941   -2.55883  11.69190 1.000 31.84753  ? 200 LEU A CB   1 
ATOM   3079 C CG   . LEU A 1 214 ? 2.11144   -2.15660  12.53649 1.000 31.97398  ? 200 LEU A CG   1 
ATOM   3080 C CD1  . LEU A 1 214 ? 2.33839   -0.77988  13.14831 1.000 31.66828  ? 200 LEU A CD1  1 
ATOM   3081 C CD2  . LEU A 1 214 ? 0.84103   -2.17339  11.71110 1.000 28.22675  ? 200 LEU A CD2  1 
ATOM   3082 H H    . LEU A 1 214 ? 3.38499   -4.98163  12.61705 1.000 35.66338  ? 200 LEU A H    1 
ATOM   3083 H HA   . LEU A 1 214 ? 2.59785   -3.85845  10.27713 1.000 39.03122  ? 200 LEU A HA   1 
ATOM   3084 H HB2  . LEU A 1 214 ? 4.08634   -2.56724  12.28573 1.000 38.27298  ? 200 LEU A HB2  1 
ATOM   3085 H HB3  . LEU A 1 214 ? 3.43042   -1.87166  11.01634 1.000 38.27298  ? 200 LEU A HB3  1 
ATOM   3086 H HG   . LEU A 1 214 ? 1.99964   -2.79841  13.25515 1.000 38.42472  ? 200 LEU A HG   1 
ATOM   3087 H HD11 . LEU A 1 214 ? 1.79944   -0.69812  13.95066 1.000 38.05788  ? 200 LEU A HD11 1 
ATOM   3088 H HD12 . LEU A 1 214 ? 3.27787   -0.68365  13.36968 1.000 38.05788  ? 200 LEU A HD12 1 
ATOM   3089 H HD13 . LEU A 1 214 ? 2.07897   -0.10177  12.50506 1.000 38.05788  ? 200 LEU A HD13 1 
ATOM   3090 H HD21 . LEU A 1 214 ? 0.67911   -3.07743  11.39903 1.000 33.92803  ? 200 LEU A HD21 1 
ATOM   3091 H HD22 . LEU A 1 214 ? 0.10126   -1.87684  12.26401 1.000 33.92803  ? 200 LEU A HD22 1 
ATOM   3092 H HD23 . LEU A 1 214 ? 0.94831   -1.57639  10.95415 1.000 33.92803  ? 200 LEU A HD23 1 
ATOM   3093 N N    . SER A 1 215 ? 4.68868   -4.15295  9.02853  1.000 29.96120  ? 201 SER A N    1 
ATOM   3094 C CA   . SER A 1 215 ? 5.94465   -4.29118  8.30298  1.000 30.81022  ? 201 SER A CA   1 
ATOM   3095 C C    . SER A 1 215 ? 6.53975   -2.90633  8.08242  1.000 30.14965  ? 201 SER A C    1 
ATOM   3096 O O    . SER A 1 215 ? 5.86411   -2.01305  7.56304  1.000 30.34964  ? 201 SER A O    1 
ATOM   3097 C CB   . SER A 1 215 ? 5.71997   -4.99906  6.96642  1.000 27.32149  ? 201 SER A CB   1 
ATOM   3098 O OG   . SER A 1 215 ? 6.89899   -4.99546  6.18256  1.000 37.32815  ? 201 SER A OG   1 
ATOM   3099 H H    . SER A 1 215 ? 4.00777   -4.02801  8.51828  1.000 36.00938  ? 201 SER A H    1 
ATOM   3100 H HA   . SER A 1 215 ? 6.57136   -4.82362  8.81741  1.000 37.02820  ? 201 SER A HA   1 
ATOM   3101 H HB2  . SER A 1 215 ? 5.45827   -5.91741  7.13686  1.000 32.84173  ? 201 SER A HB2  1 
ATOM   3102 H HB3  . SER A 1 215 ? 5.01780   -4.53869  6.48070  1.000 32.84173  ? 201 SER A HB3  1 
ATOM   3103 H HG   . SER A 1 215 ? 6.74919   -5.35160  5.43668  1.000 44.84973  ? 201 SER A HG   1 
ATOM   3104 N N    . THR A 1 216 ? 7.79795   -2.72784  8.48170  1.000 35.89402  ? 202 THR A N    1 
ATOM   3105 C CA   . THR A 1 216 ? 8.43824   -1.41923  8.46523  1.000 35.45529  ? 202 THR A CA   1 
ATOM   3106 C C    . THR A 1 216 ? 9.76469   -1.48290  7.72467  1.000 35.22319  ? 202 THR A C    1 
ATOM   3107 O O    . THR A 1 216 ? 10.57337  -2.38472  7.96493  1.000 39.80805  ? 202 THR A O    1 
ATOM   3108 C CB   . THR A 1 216 ? 8.67791   -0.90317  9.88820  1.000 37.72567  ? 202 THR A CB   1 
ATOM   3109 O OG1  . THR A 1 216 ? 7.44151   -0.87984  10.61085 1.000 41.77338  ? 202 THR A OG1  1 
ATOM   3110 C CG2  . THR A 1 216 ? 9.27045   0.49743   9.84953  1.000 37.79265  ? 202 THR A CG2  1 
ATOM   3111 H H    . THR A 1 216 ? 8.30549   -3.35955  8.76970  1.000 43.12876  ? 202 THR A H    1 
ATOM   3112 H HA   . THR A 1 216 ? 7.85878   -0.80329  7.99012  1.000 42.60229  ? 202 THR A HA   1 
ATOM   3113 H HB   . THR A 1 216 ? 9.30197   -1.48887  10.34473 1.000 45.32675  ? 202 THR A HB   1 
ATOM   3114 H HG1  . THR A 1 216 ? 7.56815   -0.58579  11.38745 1.000 50.18399  ? 202 THR A HG1  1 
ATOM   3115 H HG21 . THR A 1 216 ? 10.21820  0.45126   9.64817  1.000 45.40712  ? 202 THR A HG21 1 
ATOM   3116 H HG22 . THR A 1 216 ? 8.82884   1.02574   9.16633  1.000 45.40712  ? 202 THR A HG22 1 
ATOM   3117 H HG23 . THR A 1 216 ? 9.15198   0.93161   10.70880 1.000 45.40712  ? 202 THR A HG23 1 
ATOM   3118 N N    . CYS A 1 217 ? 9.98442   -0.51666  6.83536  1.000 32.96606  ? 203 CYS A N    1 
ATOM   3119 C CA   . CYS A 1 217 ? 11.26845  -0.30789  6.17941  1.000 37.92078  ? 203 CYS A CA   1 
ATOM   3120 C C    . CYS A 1 217 ? 11.58066  1.17976   6.20935  1.000 36.76227  ? 203 CYS A C    1 
ATOM   3121 O O    . CYS A 1 217 ? 10.76397  1.99515   5.76935  1.000 31.09081  ? 203 CYS A O    1 
ATOM   3122 C CB   . CYS A 1 217 ? 11.25841  -0.81146  4.73463  1.000 40.88192  ? 203 CYS A CB   1 
ATOM   3123 S SG   . CYS A 1 217 ? 11.39599  -2.60261  4.54035  1.000 45.89453  ? 203 CYS A SG   1 
ATOM   3124 H H    . CYS A 1 217 ? 9.38413   0.04781   6.58913  1.000 39.61521  ? 203 CYS A H    1 
ATOM   3125 H HA   . CYS A 1 217 ? 11.96048  -0.79197  6.65655  1.000 45.56088  ? 203 CYS A HA   1 
ATOM   3126 H HB2  . CYS A 1 217 ? 10.42428  -0.53853  4.32153  1.000 49.11424  ? 203 CYS A HB2  1 
ATOM   3127 H HB3  . CYS A 1 217 ? 12.00733  -0.41091  4.26604  1.000 49.11424  ? 203 CYS A HB3  1 
ATOM   3128 N N    . SER A 1 218 ? 12.75447  1.53093   6.72350  1.000 37.74136  ? 204 SER A N    1 
ATOM   3129 C CA   . SER A 1 218 ? 13.14057  2.92032   6.89591  1.000 33.53439  ? 204 SER A CA   1 
ATOM   3130 C C    . SER A 1 218 ? 14.40161  3.22308   6.09829  1.000 40.15709  ? 204 SER A C    1 
ATOM   3131 O O    . SER A 1 218 ? 15.17661  2.32840   5.74841  1.000 38.89727  ? 204 SER A O    1 
ATOM   3132 C CB   . SER A 1 218 ? 13.37238  3.24817   8.37502  1.000 39.59707  ? 204 SER A CB   1 
ATOM   3133 O OG   . SER A 1 218 ? 14.44649  2.48650   8.89711  1.000 50.60152  ? 204 SER A OG   1 
ATOM   3134 H H    . SER A 1 218 ? 13.35230  0.97001   6.98344  1.000 45.34557  ? 204 SER A H    1 
ATOM   3135 H HA   . SER A 1 218 ? 12.43153  3.49080   6.56019  1.000 40.29721  ? 204 SER A HA   1 
ATOM   3136 H HB2  . SER A 1 218 ? 13.58308  4.19116   8.46028  1.000 47.57242  ? 204 SER A HB2  1 
ATOM   3137 H HB3  . SER A 1 218 ? 12.56678  3.04176   8.87432  1.000 47.57242  ? 204 SER A HB3  1 
ATOM   3138 H HG   . SER A 1 218 ? 14.54901  2.65629   9.71336  1.000 60.77777  ? 204 SER A HG   1 
ATOM   3139 N N    . LYS A 1 219 ? 14.59445  4.50878   5.81294  1.000 29.86900  ? 205 LYS A N    1 
ATOM   3140 C CA   . LYS A 1 219 ? 15.78354  4.99811   5.12815  1.000 29.23321  ? 205 LYS A CA   1 
ATOM   3141 C C    . LYS A 1 219 ? 16.28149  6.23033   5.86463  1.000 28.56441  ? 205 LYS A C    1 
ATOM   3142 O O    . LYS A 1 219 ? 15.53166  7.19716   6.03736  1.000 27.39679  ? 205 LYS A O    1 
ATOM   3143 C CB   . LYS A 1 219 ? 15.48459  5.33498   3.66562  1.000 31.66044  ? 205 LYS A CB   1 
ATOM   3144 C CG   . LYS A 1 219 ? 16.71728  5.67259   2.83562  1.000 32.24645  ? 205 LYS A CG   1 
ATOM   3145 C CD   . LYS A 1 219 ? 16.42369  6.77730   1.83144  1.000 47.73633  ? 205 LYS A CD   1 
ATOM   3146 C CE   . LYS A 1 219 ? 17.11375  6.52806   0.50072  1.000 57.49932  ? 205 LYS A CE   1 
ATOM   3147 N NZ   . LYS A 1 219 ? 16.80006  7.59344   -0.49279 1.000 66.22657  ? 205 LYS A NZ   1 
ATOM   3148 H H    . LYS A 1 219 ? 14.03503  5.13091   6.01194  1.000 35.89874  ? 205 LYS A H    1 
ATOM   3149 H HA   . LYS A 1 219 ? 16.47493  4.31804   5.14800  1.000 35.13579  ? 205 LYS A HA   1 
ATOM   3150 H HB2  . LYS A 1 219 ? 15.05326  4.57012   3.25351  1.000 38.04847  ? 205 LYS A HB2  1 
ATOM   3151 H HB3  . LYS A 1 219 ? 14.89316  6.10337   3.63940  1.000 38.04847  ? 205 LYS A HB3  1 
ATOM   3152 H HG2  . LYS A 1 219 ? 17.42785  5.97452   3.42283  1.000 38.75168  ? 205 LYS A HG2  1 
ATOM   3153 H HG3  . LYS A 1 219 ? 17.00256  4.88424   2.34774  1.000 38.75168  ? 205 LYS A HG3  1 
ATOM   3154 H HD2  . LYS A 1 219 ? 15.46754  6.82117   1.67410  1.000 57.33953  ? 205 LYS A HD2  1 
ATOM   3155 H HD3  . LYS A 1 219 ? 16.74102  7.62332   2.18423  1.000 57.33953  ? 205 LYS A HD3  1 
ATOM   3156 H HE2  . LYS A 1 219 ? 18.07411  6.51216   0.63621  1.000 69.05513  ? 205 LYS A HE2  1 
ATOM   3157 H HE3  . LYS A 1 219 ? 16.81553  5.67857   0.13970  1.000 69.05513  ? 205 LYS A HE3  1 
ATOM   3158 H HZ1  . LYS A 1 219 ? 17.24845  7.44735   -1.24758 1.000 79.52783  ? 205 LYS A HZ1  1 
ATOM   3159 H HZ2  . LYS A 1 219 ? 15.92805  7.59642   -0.67082 1.000 79.52783  ? 205 LYS A HZ2  1 
ATOM   3160 H HZ3  . LYS A 1 219 ? 17.03144  8.38944   -0.16882 1.000 79.52783  ? 205 LYS A HZ3  1 
ATOM   3161 N N    . LEU A 1 220 ? 17.53582  6.19500   6.29837  1.000 27.86348  ? 206 LEU A N    1 
ATOM   3162 C CA   . LEU A 1 220 ? 18.16639  7.31952   6.97077  1.000 28.62970  ? 206 LEU A CA   1 
ATOM   3163 C C    . LEU A 1 220 ? 19.14228  8.00293   6.02329  1.000 29.84557  ? 206 LEU A C    1 
ATOM   3164 O O    . LEU A 1 220 ? 19.87004  7.33885   5.27937  1.000 27.52636  ? 206 LEU A O    1 
ATOM   3165 C CB   . LEU A 1 220 ? 18.89395  6.86200   8.23595  1.000 29.43473  ? 206 LEU A CB   1 
ATOM   3166 C CG   . LEU A 1 220 ? 18.03221  6.71124   9.49293  1.000 29.43011  ? 206 LEU A CG   1 
ATOM   3167 C CD1  . LEU A 1 220 ? 16.84994  5.79150   9.24174  1.000 29.91295  ? 206 LEU A CD1  1 
ATOM   3168 C CD2  . LEU A 1 220 ? 18.86993  6.20310   10.66042 1.000 28.72870  ? 206 LEU A CD2  1 
ATOM   3169 H H    . LEU A 1 220 ? 18.05268  5.51313   6.21168  1.000 33.49211  ? 206 LEU A H    1 
ATOM   3170 H HA   . LEU A 1 220 ? 17.49156  7.96667   7.22904  1.000 34.41158  ? 206 LEU A HA   1 
ATOM   3171 H HB2  . LEU A 1 220 ? 19.29442  5.99672   8.05760  1.000 35.37761  ? 206 LEU A HB2  1 
ATOM   3172 H HB3  . LEU A 1 220 ? 19.58492  7.51196   8.43849  1.000 35.37761  ? 206 LEU A HB3  1 
ATOM   3173 H HG   . LEU A 1 220 ? 17.67948  7.58311   9.73025  1.000 35.37207  ? 206 LEU A HG   1 
ATOM   3174 H HD11 . LEU A 1 220 ? 16.45710  5.54251   10.09297 1.000 35.95149  ? 206 LEU A HD11 1 
ATOM   3175 H HD12 . LEU A 1 220 ? 16.19555  6.25923   8.69962  1.000 35.95149  ? 206 LEU A HD12 1 
ATOM   3176 H HD13 . LEU A 1 220 ? 17.15970  4.99904   8.77596  1.000 35.95149  ? 206 LEU A HD13 1 
ATOM   3177 H HD21 . LEU A 1 220 ? 19.59298  6.82816   10.82593 1.000 34.53038  ? 206 LEU A HD21 1 
ATOM   3178 H HD22 . LEU A 1 220 ? 18.30632  6.13352   11.44681 1.000 34.53038  ? 206 LEU A HD22 1 
ATOM   3179 H HD23 . LEU A 1 220 ? 19.23120  5.33177   10.43423 1.000 34.53038  ? 206 LEU A HD23 1 
ATOM   3180 N N    . SER A 1 221 ? 19.15098  9.33226   6.05166  1.000 24.90312  ? 207 SER A N    1 
ATOM   3181 C CA   . SER A 1 221 ? 20.03308  10.11137  5.19686  1.000 27.82338  ? 207 SER A CA   1 
ATOM   3182 C C    . SER A 1 221 ? 20.36619  11.41779  5.90542  1.000 29.64261  ? 207 SER A C    1 
ATOM   3183 O O    . SER A 1 221 ? 19.94821  11.65718  7.04267  1.000 27.97514  ? 207 SER A O    1 
ATOM   3184 C CB   . SER A 1 221 ? 19.39054  10.35744  3.82708  1.000 26.86721  ? 207 SER A CB   1 
ATOM   3185 O OG   . SER A 1 221 ? 18.12828  10.98542  3.96368  1.000 30.54314  ? 207 SER A OG   1 
ATOM   3186 H H    . SER A 1 221 ? 18.64961  9.80836   6.56309  1.000 29.93969  ? 207 SER A H    1 
ATOM   3187 H HA   . SER A 1 221 ? 20.85935  9.62150   5.06193  1.000 33.44399  ? 207 SER A HA   1 
ATOM   3188 H HB2  . SER A 1 221 ? 19.97277  10.93074  3.30435  1.000 32.29659  ? 207 SER A HB2  1 
ATOM   3189 H HB3  . SER A 1 221 ? 19.27199  9.50630   3.37719  1.000 32.29659  ? 207 SER A HB3  1 
ATOM   3190 H HG   . SER A 1 221 ? 17.58971  10.46742  4.34738  1.000 36.70770  ? 207 SER A HG   1 
ATOM   3191 N N    . LYS A 1 222 ? 21.12785  12.26704  5.21864  1.000 29.01889  ? 208 LYS A N    1 
ATOM   3192 C CA   . LYS A 1 222 ? 21.57726  13.53700  5.76401  1.000 34.20508  ? 208 LYS A CA   1 
ATOM   3193 C C    . LYS A 1 222 ? 21.20251  14.66707  4.81681  1.000 34.13925  ? 208 LYS A C    1 
ATOM   3194 O O    . LYS A 1 222 ? 21.09008  14.47461  3.60301  1.000 30.23585  ? 208 LYS A O    1 
ATOM   3195 C CB   . LYS A 1 222 ? 23.09763  13.54260  5.99873  1.000 34.42164  ? 208 LYS A CB   1 
ATOM   3196 C CG   . LYS A 1 222 ? 23.58246  12.52876  7.02901  1.000 34.39625  ? 208 LYS A CG   1 
ATOM   3197 C CD   . LYS A 1 222 ? 23.08637  12.86530  8.42637  1.000 31.08212  ? 208 LYS A CD   1 
ATOM   3198 C CE   . LYS A 1 222 ? 23.81206  12.04494  9.48316  1.000 29.52370  ? 208 LYS A CE   1 
ATOM   3199 N NZ   . LYS A 1 222 ? 23.37684  12.39283  10.86107 1.000 31.06825  ? 208 LYS A NZ   1 
ATOM   3200 H H    . LYS A 1 222 ? 21.40152  12.12275  4.41622  1.000 34.87861  ? 208 LYS A H    1 
ATOM   3201 H HA   . LYS A 1 222 ? 21.13573  13.69535  6.61306  1.000 41.10204  ? 208 LYS A HA   1 
ATOM   3202 H HB2  . LYS A 1 222 ? 23.54045  13.34186  5.15938  1.000 41.36191  ? 208 LYS A HB2  1 
ATOM   3203 H HB3  . LYS A 1 222 ? 23.35894  14.42361  6.30928  1.000 41.36191  ? 208 LYS A HB3  1 
ATOM   3204 H HG2  . LYS A 1 222 ? 23.25108  11.64827  6.79272  1.000 41.33144  ? 208 LYS A HG2  1 
ATOM   3205 H HG3  . LYS A 1 222 ? 24.55234  12.52535  7.04345  1.000 41.33144  ? 208 LYS A HG3  1 
ATOM   3206 H HD2  . LYS A 1 222 ? 23.24493  13.80510  8.60677  1.000 37.35449  ? 208 LYS A HD2  1 
ATOM   3207 H HD3  . LYS A 1 222 ? 22.13789  12.67130  8.48682  1.000 37.35449  ? 208 LYS A HD3  1 
ATOM   3208 H HE2  . LYS A 1 222 ? 23.62864  11.10371  9.33705  1.000 35.48438  ? 208 LYS A HE2  1 
ATOM   3209 H HE3  . LYS A 1 222 ? 24.76533  12.21143  9.41640  1.000 35.48438  ? 208 LYS A HE3  1 
ATOM   3210 H HZ1  . LYS A 1 222 ? 23.82139  11.90022  11.45420 1.000 37.33784  ? 208 LYS A HZ1  1 
ATOM   3211 H HZ2  . LYS A 1 222 ? 23.53660  13.25334  11.02261 1.000 37.33784  ? 208 LYS A HZ2  1 
ATOM   3212 H HZ3  . LYS A 1 222 ? 22.50512  12.23869  10.95300 1.000 37.33784  ? 208 LYS A HZ3  1 
ATOM   3213 N N    . ASP A 1 223 ? 20.99620  15.84876  5.39751  1.000 31.90430  ? 209 ASP A N    1 
ATOM   3214 C CA   . ASP A 1 223 ? 20.75873  17.06840  4.64182  1.000 31.76737  ? 209 ASP A CA   1 
ATOM   3215 C C    . ASP A 1 223 ? 22.07602  17.81033  4.49525  1.000 38.09027  ? 209 ASP A C    1 
ATOM   3216 O O    . ASP A 1 223 ? 22.67665  18.17903  5.51715  1.000 32.37105  ? 209 ASP A O    1 
ATOM   3217 C CB   . ASP A 1 223 ? 19.73219  17.94122  5.35803  1.000 38.77404  ? 209 ASP A CB   1 
ATOM   3218 C CG   . ASP A 1 223 ? 19.44173  19.24035  4.62522  1.000 35.01999  ? 209 ASP A CG   1 
ATOM   3219 O OD1  . ASP A 1 223 ? 20.08109  19.51379  3.58872  1.000 40.09415  ? 209 ASP A OD1  1 
ATOM   3220 O OD2  . ASP A 1 223 ? 18.56094  19.99116  5.09331  1.000 30.29991  ? 209 ASP A OD2  1 
ATOM   3221 H H    . ASP A 1 223 ? 20.98952  15.96920  6.24901  1.000 38.34109  ? 209 ASP A H    1 
ATOM   3222 H HA   . ASP A 1 223 ? 20.41572  16.85734  3.75938  1.000 38.17678  ? 209 ASP A HA   1 
ATOM   3223 H HB2  . ASP A 1 223 ? 18.89975  17.44936  5.43554  1.000 46.58479  ? 209 ASP A HB2  1 
ATOM   3224 H HB3  . ASP A 1 223 ? 20.06896  18.16448  6.23987  1.000 46.58479  ? 209 ASP A HB3  1 
ATOM   3225 N N    . PRO A 1 224 ? 22.57313  18.04689  3.27746  1.000 37.81005  ? 210 PRO A N    1 
ATOM   3226 C CA   . PRO A 1 224 ? 23.88068  18.71153  3.14346  1.000 37.22527  ? 210 PRO A CA   1 
ATOM   3227 C C    . PRO A 1 224 ? 23.90473  20.12768  3.68584  1.000 37.63914  ? 210 PRO A C    1 
ATOM   3228 O O    . PRO A 1 224 ? 24.98984  20.63596  3.99377  1.000 38.53516  ? 210 PRO A O    1 
ATOM   3229 C CB   . PRO A 1 224 ? 24.13674  18.68788  1.62972  1.000 37.98162  ? 210 PRO A CB   1 
ATOM   3230 C CG   . PRO A 1 224 ? 22.78521  18.56095  1.01313  1.000 44.53750  ? 210 PRO A CG   1 
ATOM   3231 C CD   . PRO A 1 224 ? 21.98176  17.72407  1.96712  1.000 37.54042  ? 210 PRO A CD   1 
ATOM   3232 H HA   . PRO A 1 224 ? 24.56308  18.18771  3.59162  1.000 44.72627  ? 210 PRO A HA   1 
ATOM   3233 H HB2  . PRO A 1 224 ? 24.56799  19.51206  1.35469  1.000 45.63389  ? 210 PRO A HB2  1 
ATOM   3234 H HB3  . PRO A 1 224 ? 24.69555  17.92871  1.40101  1.000 45.63389  ? 210 PRO A HB3  1 
ATOM   3235 H HG2  . PRO A 1 224 ? 22.38869  19.43996  0.90821  1.000 53.50094  ? 210 PRO A HG2  1 
ATOM   3236 H HG3  . PRO A 1 224 ? 22.85819  18.12472  0.14984  1.000 53.50094  ? 210 PRO A HG3  1 
ATOM   3237 H HD2  . PRO A 1 224 ? 21.04456  17.97274  1.94015  1.000 45.10444  ? 210 PRO A HD2  1 
ATOM   3238 H HD3  . PRO A 1 224 ? 22.08046  16.78020  1.76644  1.000 45.10444  ? 210 PRO A HD3  1 
ATOM   3239 N N    . ASN A 1 225 ? 22.75184  20.78022  3.81508  1.000 42.65724  ? 211 ASN A N    1 
ATOM   3240 C CA   . ASN A 1 225 ? 22.67842  22.15327  4.29462  1.000 43.30516  ? 211 ASN A CA   1 
ATOM   3241 C C    . ASN A 1 225 ? 22.36697  22.25317  5.78166  1.000 39.28776  ? 211 ASN A C    1 
ATOM   3242 O O    . ASN A 1 225 ? 22.35304  23.36269  6.32353  1.000 39.13148  ? 211 ASN A O    1 
ATOM   3243 C CB   . ASN A 1 225 ? 21.62514  22.92510  3.49638  1.000 41.52614  ? 211 ASN A CB   1 
ATOM   3244 C CG   . ASN A 1 225 ? 21.95197  22.98704  2.01840  1.000 48.20918  ? 211 ASN A CG   1 
ATOM   3245 O OD1  . ASN A 1 225 ? 23.11858  22.93085  1.62902  1.000 46.77696  ? 211 ASN A OD1  1 
ATOM   3246 N ND2  . ASN A 1 225 ? 20.92359  23.10121  1.18638  1.000 53.53447  ? 211 ASN A ND2  1 
ATOM   3247 H H    . ASN A 1 225 ? 21.98471  20.44003  3.62697  1.000 51.24463  ? 211 ASN A H    1 
ATOM   3248 H HA   . ASN A 1 225 ? 23.53899  22.57665  4.14945  1.000 52.02214  ? 211 ASN A HA   1 
ATOM   3249 H HB2  . ASN A 1 225 ? 20.76597  22.48624  3.59701  1.000 49.88731  ? 211 ASN A HB2  1 
ATOM   3250 H HB3  . ASN A 1 225 ? 21.57496  23.83366  3.83238  1.000 49.88731  ? 211 ASN A HB3  1 
ATOM   3251 H HD21 . ASN A 1 225 ? 21.05911  23.14017  0.33802  1.000 64.29730  ? 211 ASN A HD21 1 
ATOM   3252 H HD22 . ASN A 1 225 ? 20.12195  23.13620  1.49583  1.000 64.29730  ? 211 ASN A HD22 1 
ATOM   3253 N N    . GLU A 1 226 ? 22.11803  21.13292  6.45280  1.000 36.45578  ? 212 GLU A N    1 
ATOM   3254 C CA   . GLU A 1 226 ? 21.83893  21.13683  7.88163  1.000 31.54352  ? 212 GLU A CA   1 
ATOM   3255 C C    . GLU A 1 226 ? 23.14696  21.05229  8.65675  1.000 32.00161  ? 212 GLU A C    1 
ATOM   3256 O O    . GLU A 1 226 ? 23.95635  20.14804  8.42894  1.000 39.52026  ? 212 GLU A O    1 
ATOM   3257 C CB   . GLU A 1 226 ? 20.92101  19.97441  8.25666  1.000 29.67492  ? 212 GLU A CB   1 
ATOM   3258 C CG   . GLU A 1 226 ? 20.56344  19.92368  9.73098  1.000 31.89966  ? 212 GLU A CG   1 
ATOM   3259 C CD   . GLU A 1 226 ? 19.94007  21.21637  10.22416 1.000 32.35778  ? 212 GLU A CD   1 
ATOM   3260 O OE1  . GLU A 1 226 ? 18.94666  21.66928  9.61689  1.000 28.25327  ? 212 GLU A OE1  1 
ATOM   3261 O OE2  . GLU A 1 226 ? 20.45223  21.78452  11.21200 1.000 28.40810  ? 212 GLU A OE2  1 
ATOM   3262 H H    . GLU A 1 226 ? 22.10531  20.34989  6.09740  1.000 43.80287  ? 212 GLU A H    1 
ATOM   3263 H HA   . GLU A 1 226 ? 21.39099  21.96272  8.12280  1.000 37.90817  ? 212 GLU A HA   1 
ATOM   3264 H HB2  . GLU A 1 226 ? 20.09488  20.05587  7.75489  1.000 35.66585  ? 212 GLU A HB2  1 
ATOM   3265 H HB3  . GLU A 1 226 ? 21.36520  19.14200  8.03154  1.000 35.66585  ? 212 GLU A HB3  1 
ATOM   3266 H HG2  . GLU A 1 226 ? 19.92616  19.20732  9.87792  1.000 38.33553  ? 212 GLU A HG2  1 
ATOM   3267 H HG3  . GLU A 1 226 ? 21.36884  19.76224  10.24691 1.000 38.33553  ? 212 GLU A HG3  1 
ATOM   3268 N N    . LYS A 1 227 ? 23.34857  21.99552  9.57314  1.000 34.89956  ? 213 LYS A N    1 
ATOM   3269 C CA   . LYS A 1 227 ? 24.58412  22.06167  10.33706 1.000 35.90464  ? 213 LYS A CA   1 
ATOM   3270 C C    . LYS A 1 227 ? 24.46128  21.46349  11.72850 1.000 34.80326  ? 213 LYS A C    1 
ATOM   3271 O O    . LYS A 1 227 ? 25.48645  21.13930  12.33713 1.000 39.17268  ? 213 LYS A O    1 
ATOM   3272 C CB   . LYS A 1 227 ? 25.04973  23.51565  10.44249 1.000 34.16044  ? 213 LYS A CB   1 
ATOM   3273 C CG   . LYS A 1 227 ? 25.35269  24.12991  9.08641  1.000 37.40603  ? 213 LYS A CG   1 
ATOM   3274 C CD   . LYS A 1 227 ? 25.75042  25.58331  9.20205  1.000 36.16957  ? 213 LYS A CD   1 
ATOM   3275 C CE   . LYS A 1 227 ? 26.18649  26.12838  7.85513  1.000 43.43356  ? 213 LYS A CE   1 
ATOM   3276 N NZ   . LYS A 1 227 ? 25.14096  25.93450  6.80540  1.000 42.40697  ? 213 LYS A NZ   1 
ATOM   3277 H H    . LYS A 1 227 ? 22.78033  22.61039  9.76972  1.000 41.93542  ? 213 LYS A H    1 
ATOM   3278 H HA   . LYS A 1 227 ? 25.27404  21.56376  9.87124  1.000 43.14151  ? 213 LYS A HA   1 
ATOM   3279 H HB2  . LYS A 1 227 ? 24.35146  24.04192  10.86243 1.000 41.04847  ? 213 LYS A HB2  1 
ATOM   3280 H HB3  . LYS A 1 227 ? 25.85856  23.55101  10.97676 1.000 41.04847  ? 213 LYS A HB3  1 
ATOM   3281 H HG2  . LYS A 1 227 ? 26.08546  23.64705  8.67315  1.000 44.94317  ? 213 LYS A HG2  1 
ATOM   3282 H HG3  . LYS A 1 227 ? 24.56217  24.07554  8.52693  1.000 44.94317  ? 213 LYS A HG3  1 
ATOM   3283 H HD2  . LYS A 1 227 ? 24.99327  26.10297  9.51443  1.000 43.45943  ? 213 LYS A HD2  1 
ATOM   3284 H HD3  . LYS A 1 227 ? 26.49039  25.66870  9.82338  1.000 43.45943  ? 213 LYS A HD3  1 
ATOM   3285 H HE2  . LYS A 1 227 ? 26.36037  27.07915  7.93701  1.000 52.17621  ? 213 LYS A HE2  1 
ATOM   3286 H HE3  . LYS A 1 227 ? 26.99084  25.66737  7.56982  1.000 52.17621  ? 213 LYS A HE3  1 
ATOM   3287 H HZ1  . LYS A 1 227 ? 24.37346  26.29992  7.06905  1.000 50.94430  ? 213 LYS A HZ1  1 
ATOM   3288 H HZ2  . LYS A 1 227 ? 25.39792  26.31926  6.04512  1.000 50.94430  ? 213 LYS A HZ2  1 
ATOM   3289 H HZ3  . LYS A 1 227 ? 25.01252  25.06582  6.66048  1.000 50.94430  ? 213 LYS A HZ3  1 
ATOM   3290 N N    . ARG A 1 228 ? 23.24700  21.30221  12.23842 1.000 28.93759  ? 214 ARG A N    1 
ATOM   3291 C CA   . ARG A 1 228 ? 23.03609  20.64120  13.51444 1.000 30.44811  ? 214 ARG A CA   1 
ATOM   3292 C C    . ARG A 1 228 ? 22.95173  19.13595  13.30609 1.000 27.85194  ? 214 ARG A C    1 
ATOM   3293 O O    . ARG A 1 228 ? 22.55851  18.65844  12.23820 1.000 27.43148  ? 214 ARG A O    1 
ATOM   3294 C CB   . ARG A 1 228 ? 21.75859  21.14656  14.18595 1.000 29.54262  ? 214 ARG A CB   1 
ATOM   3295 C CG   . ARG A 1 228 ? 21.78603  22.62249  14.53284 1.000 28.35345  ? 214 ARG A CG   1 
ATOM   3296 C CD   . ARG A 1 228 ? 20.53720  23.04226  15.28673 1.000 25.91552  ? 214 ARG A CD   1 
ATOM   3297 N NE   . ARG A 1 228 ? 20.57343  24.45564  15.64449 1.000 27.55380  ? 214 ARG A NE   1 
ATOM   3298 C CZ   . ARG A 1 228 ? 21.19043  24.94744  16.71089 1.000 27.87304  ? 214 ARG A CZ   1 
ATOM   3299 N NH1  . ARG A 1 228 ? 21.84172  24.16578  17.55725 1.000 25.26067  ? 214 ARG A NH1  1 
ATOM   3300 N NH2  . ARG A 1 228 ? 21.15701  26.25828  16.93128 1.000 28.00731  ? 214 ARG A NH2  1 
ATOM   3301 H H    . ARG A 1 228 ? 22.52322  21.57030  11.85913 1.000 34.78105  ? 214 ARG A H    1 
ATOM   3302 H HA   . ARG A 1 228 ? 23.77799  20.83362  14.10896 1.000 36.59368  ? 214 ARG A HA   1 
ATOM   3303 H HB2  . ARG A 1 228 ? 21.01198  20.99864  13.58462 1.000 35.50709  ? 214 ARG A HB2  1 
ATOM   3304 H HB3  . ARG A 1 228 ? 21.62408  20.65233  15.00969 1.000 35.50709  ? 214 ARG A HB3  1 
ATOM   3305 H HG2  . ARG A 1 228 ? 22.55618  22.80625  15.09319 1.000 34.08008  ? 214 ARG A HG2  1 
ATOM   3306 H HG3  . ARG A 1 228 ? 21.83815  23.14324  13.71614 1.000 34.08008  ? 214 ARG A HG3  1 
ATOM   3307 H HD2  . ARG A 1 228 ? 19.75913  22.88963  14.72797 1.000 31.15456  ? 214 ARG A HD2  1 
ATOM   3308 H HD3  . ARG A 1 228 ? 20.46624  22.52340  16.10321 1.000 31.15456  ? 214 ARG A HD3  1 
ATOM   3309 H HE   . ARG A 1 228 ? 20.16607  25.00931  15.12767 1.000 33.12050  ? 214 ARG A HE   1 
ATOM   3310 H HH11 . ARG A 1 228 ? 21.87211  23.31697  17.42233 1.000 30.03311  ? 214 ARG A HH11 1 
ATOM   3311 H HH12 . ARG A 1 228 ? 22.23455  24.50664  18.24216 1.000 30.03311  ? 214 ARG A HH12 1 
ATOM   3312 H HH21 . ARG A 1 228 ? 20.73913  26.77550  16.38588 1.000 33.66471  ? 214 ARG A HH21 1 
ATOM   3313 H HH22 . ARG A 1 228 ? 21.55327  26.58890  17.61923 1.000 33.66471  ? 214 ARG A HH22 1 
ATOM   3314 N N    . ASP A 1 229 ? 23.34357  18.39038  14.33437 1.000 26.97534  ? 215 ASP A N    1 
ATOM   3315 C CA   . ASP A 1 229 ? 23.16517  16.94563  14.32200 1.000 25.45009  ? 215 ASP A CA   1 
ATOM   3316 C C    . ASP A 1 229 ? 21.71304  16.62691  14.00341 1.000 27.93702  ? 215 ASP A C    1 
ATOM   3317 O O    . ASP A 1 229 ? 20.79961  17.11575  14.67491 1.000 27.84092  ? 215 ASP A O    1 
ATOM   3318 C CB   . ASP A 1 229 ? 23.56903  16.36135  15.67555 1.000 28.27984  ? 215 ASP A CB   1 
ATOM   3319 C CG   . ASP A 1 229 ? 23.94784  14.89562  15.59198 1.000 30.62830  ? 215 ASP A CG   1 
ATOM   3320 O OD1  . ASP A 1 229 ? 23.95329  14.34011  14.47323 1.000 30.15255  ? 215 ASP A OD1  1 
ATOM   3321 O OD2  . ASP A 1 229 ? 24.24282  14.29952  16.65031 1.000 30.84146  ? 215 ASP A OD2  1 
ATOM   3322 H H    . ASP A 1 229 ? 23.71375  18.69682  15.04758 1.000 32.42635  ? 215 ASP A H    1 
ATOM   3323 H HA   . ASP A 1 229 ? 23.73493  16.53907  13.65045 1.000 30.59605  ? 215 ASP A HA   1 
ATOM   3324 H HB2  . ASP A 1 229 ? 24.33495  16.85023  16.01506 1.000 33.99174  ? 215 ASP A HB2  1 
ATOM   3325 H HB3  . ASP A 1 229 ? 22.82354  16.44390  16.29062 1.000 33.99174  ? 215 ASP A HB3  1 
ATOM   3326 N N    . HIS A 1 230 ? 21.49716  15.82305  12.96550 1.000 24.61634  ? 216 HIS A N    1 
ATOM   3327 C CA   . HIS A 1 230 ? 20.16774  15.67850  12.39540 1.000 27.14227  ? 216 HIS A CA   1 
ATOM   3328 C C    . HIS A 1 230 ? 20.01024  14.29818  11.77907 1.000 25.77383  ? 216 HIS A C    1 
ATOM   3329 O O    . HIS A 1 230 ? 20.96988  13.53432  11.64817 1.000 25.80721  ? 216 HIS A O    1 
ATOM   3330 C CB   . HIS A 1 230 ? 19.91736  16.74296  11.32833 1.000 27.16403  ? 216 HIS A CB   1 
ATOM   3331 C CG   . HIS A 1 230 ? 20.86407  16.65317  10.17398 1.000 25.40540  ? 216 HIS A CG   1 
ATOM   3332 N ND1  . HIS A 1 230 ? 22.17809  17.05842  10.26000 1.000 32.42340  ? 216 HIS A ND1  1 
ATOM   3333 C CD2  . HIS A 1 230 ? 20.69521  16.18753  8.91411  1.000 29.14593  ? 216 HIS A CD2  1 
ATOM   3334 C CE1  . HIS A 1 230 ? 22.77558  16.85681  9.09939  1.000 35.35002  ? 216 HIS A CE1  1 
ATOM   3335 N NE2  . HIS A 1 230 ? 21.89847  16.32666  8.26654  1.000 28.96916  ? 216 HIS A NE2  1 
ATOM   3336 H H    . HIS A 1 230 ? 22.10417  15.35362  12.57721 1.000 29.59554  ? 216 HIS A H    1 
ATOM   3337 H HA   . HIS A 1 230 ? 19.51974  15.76537  13.11195 1.000 32.62666  ? 216 HIS A HA   1 
ATOM   3338 H HB2  . HIS A 1 230 ? 19.01650  16.63733  10.98454 1.000 32.65278  ? 216 HIS A HB2  1 
ATOM   3339 H HB3  . HIS A 1 230 ? 20.01850  17.62015  11.72985 1.000 32.65278  ? 216 HIS A HB3  1 
ATOM   3340 H HD1  . HIS A 1 230 ? 22.55103  17.39075  10.96005 1.000 38.96402  ? 216 HIS A HD1  1 
ATOM   3341 H HD2  . HIS A 1 230 ? 19.91158  15.83888  8.55456  1.000 35.03106  ? 216 HIS A HD2  1 
ATOM   3342 H HE1  . HIS A 1 230 ? 23.66271  17.05449  8.90233  1.000 42.47596  ? 216 HIS A HE1  1 
ATOM   3343 N N    . MET A 1 231 ? 18.77739  14.00194  11.37322 1.000 27.15028  ? 217 MET A N    1 
ATOM   3344 C CA   . MET A 1 231 ? 18.46236  12.75637  10.68286 1.000 29.57480  ? 217 MET A CA   1 
ATOM   3345 C C    . MET A 1 231 ? 17.32810  13.02575  9.70777  1.000 26.44566  ? 217 MET A C    1 
ATOM   3346 O O    . MET A 1 231 ? 16.23990  13.43441  10.12355 1.000 25.95895  ? 217 MET A O    1 
ATOM   3347 C CB   . MET A 1 231 ? 18.07099  11.65356  11.67389 1.000 28.93327  ? 217 MET A CB   1 
ATOM   3348 C CG   . MET A 1 231 ? 17.47846  10.40878  11.01719 1.000 31.28519  ? 217 MET A CG   1 
ATOM   3349 S SD   . MET A 1 231 ? 17.16219  9.05814   12.17173 1.000 27.33001  ? 217 MET A SD   1 
ATOM   3350 C CE   . MET A 1 231 ? 15.86006  9.76252   13.18449 1.000 28.87899  ? 217 MET A CE   1 
ATOM   3351 H H    . MET A 1 231 ? 18.09646  14.51450  11.48814 1.000 32.63627  ? 217 MET A H    1 
ATOM   3352 H HA   . MET A 1 231 ? 19.24511  12.45611  10.19496 1.000 35.54570  ? 217 MET A HA   1 
ATOM   3353 H HB2  . MET A 1 231 ? 18.86267  11.38035  12.16327 1.000 34.77586  ? 217 MET A HB2  1 
ATOM   3354 H HB3  . MET A 1 231 ? 17.40782  12.00769  12.28683 1.000 34.77586  ? 217 MET A HB3  1 
ATOM   3355 H HG2  . MET A 1 231 ? 16.63469  10.64651  10.60194 1.000 37.59817  ? 217 MET A HG2  1 
ATOM   3356 H HG3  . MET A 1 231 ? 18.09896  10.08465  10.34577 1.000 37.59817  ? 217 MET A HG3  1 
ATOM   3357 H HE1  . MET A 1 231 ? 15.08532  9.93587   12.62715 1.000 34.71073  ? 217 MET A HE1  1 
ATOM   3358 H HE2  . MET A 1 231 ? 15.62925  9.13265   13.88512 1.000 34.71073  ? 217 MET A HE2  1 
ATOM   3359 H HE3  . MET A 1 231 ? 16.17786  10.59109  13.57613 1.000 34.71073  ? 217 MET A HE3  1 
ATOM   3360 N N    . VAL A 1 232 ? 17.58719  12.81936  8.42009  1.000 25.89155  ? 218 VAL A N    1 
ATOM   3361 C CA   . VAL A 1 232 ? 16.53536  12.79463  7.41109  1.000 26.91063  ? 218 VAL A CA   1 
ATOM   3362 C C    . VAL A 1 232 ? 15.97261  11.38150  7.36724  1.000 26.50203  ? 218 VAL A C    1 
ATOM   3363 O O    . VAL A 1 232 ? 16.72118  10.40845  7.20864  1.000 26.54169  ? 218 VAL A O    1 
ATOM   3364 C CB   . VAL A 1 232 ? 17.07001  13.22617  6.03666  1.000 26.78353  ? 218 VAL A CB   1 
ATOM   3365 C CG1  . VAL A 1 232 ? 15.98326  13.08561  4.97783  1.000 29.42879  ? 218 VAL A CG1  1 
ATOM   3366 C CG2  . VAL A 1 232 ? 17.58138  14.65692  6.09521  1.000 30.32474  ? 218 VAL A CG2  1 
ATOM   3367 H H    . VAL A 1 232 ? 18.37572  12.68934  8.10244  1.000 31.12581  ? 218 VAL A H    1 
ATOM   3368 H HA   . VAL A 1 232 ? 15.82766  13.41103  7.65625  1.000 32.34870  ? 218 VAL A HA   1 
ATOM   3369 H HB   . VAL A 1 232 ? 17.80995  12.65029  5.78817  1.000 32.19618  ? 218 VAL A HB   1 
ATOM   3370 H HG11 . VAL A 1 232 ? 15.12713  13.31573  5.37152  1.000 35.37049  ? 218 VAL A HG11 1 
ATOM   3371 H HG12 . VAL A 1 232 ? 16.18051  13.68521  4.24131  1.000 35.37049  ? 218 VAL A HG12 1 
ATOM   3372 H HG13 . VAL A 1 232 ? 15.96645  12.16850  4.66235  1.000 35.37049  ? 218 VAL A HG13 1 
ATOM   3373 H HG21 . VAL A 1 232 ? 17.44096  15.00613  6.98921  1.000 36.44563  ? 218 VAL A HG21 1 
ATOM   3374 H HG22 . VAL A 1 232 ? 18.52777  14.66298  5.88260  1.000 36.44563  ? 218 VAL A HG22 1 
ATOM   3375 H HG23 . VAL A 1 232 ? 17.09403  15.19311  5.45031  1.000 36.44563  ? 218 VAL A HG23 1 
ATOM   3376 N N    . PHE A 1 233 ? 14.65596  11.26495  7.51185  1.000 23.94907  ? 219 PHE A N    1 
ATOM   3377 C CA   . PHE A 1 233 ? 14.01341  9.98734   7.78107  1.000 25.97717  ? 219 PHE A CA   1 
ATOM   3378 C C    . PHE A 1 233 ? 12.88646  9.74137   6.79073  1.000 25.50191  ? 219 PHE A C    1 
ATOM   3379 O O    . PHE A 1 233 ? 11.99251  10.57955  6.63731  1.000 25.94624  ? 219 PHE A O    1 
ATOM   3380 C CB   . PHE A 1 233 ? 13.48115  9.95886   9.21809  1.000 25.52889  ? 219 PHE A CB   1 
ATOM   3381 C CG   . PHE A 1 233 ? 12.88734  8.64592   9.61842  1.000 26.52667  ? 219 PHE A CG   1 
ATOM   3382 C CD1  . PHE A 1 233 ? 13.69861  7.55404   9.87411  1.000 30.35902  ? 219 PHE A CD1  1 
ATOM   3383 C CD2  . PHE A 1 233 ? 11.51830  8.50405   9.74989  1.000 26.95314  ? 219 PHE A CD2  1 
ATOM   3384 C CE1  . PHE A 1 233 ? 13.15390  6.34269   10.24459 1.000 27.42899  ? 219 PHE A CE1  1 
ATOM   3385 C CE2  . PHE A 1 233 ? 10.96791  7.29655   10.12045 1.000 26.30024  ? 219 PHE A CE2  1 
ATOM   3386 C CZ   . PHE A 1 233 ? 11.78750  6.21353   10.36836 1.000 29.32906  ? 219 PHE A CZ   1 
ATOM   3387 H H    . PHE A 1 233 ? 14.10648  11.92424  7.45701  1.000 28.79482  ? 219 PHE A H    1 
ATOM   3388 H HA   . PHE A 1 233 ? 14.65514  9.26992   7.66114  1.000 31.22854  ? 219 PHE A HA   1 
ATOM   3389 H HB2  . PHE A 1 233 ? 14.21338  10.14930  9.82511  1.000 30.69061  ? 219 PHE A HB2  1 
ATOM   3390 H HB3  . PHE A 1 233 ? 12.79130  10.63481  9.30802  1.000 30.69061  ? 219 PHE A HB3  1 
ATOM   3391 H HD1  . PHE A 1 233 ? 14.62141  7.63833   9.79516  1.000 36.48676  ? 219 PHE A HD1  1 
ATOM   3392 H HD2  . PHE A 1 233 ? 10.96278  9.23177   9.58637  1.000 32.39970  ? 219 PHE A HD2  1 
ATOM   3393 H HE1  . PHE A 1 233 ? 13.70763  5.61418   10.41062 1.000 32.97072  ? 219 PHE A HE1  1 
ATOM   3394 H HE2  . PHE A 1 233 ? 10.04557  7.21114   10.20347 1.000 31.61623  ? 219 PHE A HE2  1 
ATOM   3395 H HZ   . PHE A 1 233 ? 11.41784  5.39768   10.61863 1.000 35.25081  ? 219 PHE A HZ   1 
ATOM   3396 N N    . LEU A 1 234 ? 12.93934  8.59159   6.12121  1.000 28.94133  ? 220 LEU A N    1 
ATOM   3397 C CA   . LEU A 1 234 ? 11.87136  8.10774   5.25676  1.000 30.95929  ? 220 LEU A CA   1 
ATOM   3398 C C    . LEU A 1 234 ? 11.46578  6.71445   5.71549  1.000 30.40960  ? 220 LEU A C    1 
ATOM   3399 O O    . LEU A 1 234 ? 12.32349  5.88428   6.03389  1.000 30.57428  ? 220 LEU A O    1 
ATOM   3400 C CB   . LEU A 1 234 ? 12.31508  8.06618   3.79195  1.000 27.79730  ? 220 LEU A CB   1 
ATOM   3401 C CG   . LEU A 1 234 ? 11.34035  7.43663   2.79233  1.000 34.12401  ? 220 LEU A CG   1 
ATOM   3402 C CD1  . LEU A 1 234 ? 10.20302  8.38881   2.46035  1.000 33.89511  ? 220 LEU A CD1  1 
ATOM   3403 C CD2  . LEU A 1 234 ? 12.07875  7.01297   1.52976  1.000 43.52909  ? 220 LEU A CD2  1 
ATOM   3404 H H    . LEU A 1 234 ? 13.61091  8.05542   6.15477  1.000 34.78554  ? 220 LEU A H    1 
ATOM   3405 H HA   . LEU A 1 234 ? 11.10293  8.69667   5.31669  1.000 37.20709  ? 220 LEU A HA   1 
ATOM   3406 H HB2  . LEU A 1 234 ? 12.47067  8.97818   3.50049  1.000 33.41270  ? 220 LEU A HB2  1 
ATOM   3407 H HB3  . LEU A 1 234 ? 13.13937  7.55717   3.74337  1.000 33.41270  ? 220 LEU A HB3  1 
ATOM   3408 H HG   . LEU A 1 234 ? 10.94734  6.64615   3.19429  1.000 41.00475  ? 220 LEU A HG   1 
ATOM   3409 H HD11 . LEU A 1 234 ? 9.56472   7.93185   1.89055  1.000 40.73007  ? 220 LEU A HD11 1 
ATOM   3410 H HD12 . LEU A 1 234 ? 9.77216   8.66553   3.28418  1.000 40.73007  ? 220 LEU A HD12 1 
ATOM   3411 H HD13 . LEU A 1 234 ? 10.56327  9.16253   1.99940  1.000 40.73007  ? 220 LEU A HD13 1 
ATOM   3412 H HD21 . LEU A 1 234 ? 12.75025  6.35300   1.76306  1.000 52.29085  ? 220 LEU A HD21 1 
ATOM   3413 H HD22 . LEU A 1 234 ? 11.44260  6.63102   0.90500  1.000 52.29085  ? 220 LEU A HD22 1 
ATOM   3414 H HD23 . LEU A 1 234 ? 12.50281  7.79130   1.13571  1.000 52.29085  ? 220 LEU A HD23 1 
ATOM   3415 N N    . GLU A 1 235 ? 10.16090  6.45248   5.73874  1.000 28.30506  ? 221 GLU A N    1 
ATOM   3416 C CA   . GLU A 1 235 ? 9.66637   5.18405   6.25228  1.000 31.97199  ? 221 GLU A CA   1 
ATOM   3417 C C    . GLU A 1 235 ? 8.37022   4.80282   5.55479  1.000 31.60178  ? 221 GLU A C    1 
ATOM   3418 O O    . GLU A 1 235 ? 7.53157   5.66107   5.26574  1.000 25.80160  ? 221 GLU A O    1 
ATOM   3419 C CB   . GLU A 1 235 ? 9.44705   5.25591   7.77100  1.000 32.06404  ? 221 GLU A CB   1 
ATOM   3420 C CG   . GLU A 1 235 ? 8.92871   3.96620   8.39714  1.000 33.57874  ? 221 GLU A CG   1 
ATOM   3421 C CD   . GLU A 1 235 ? 8.71044   4.07528   9.90430  1.000 33.21768  ? 221 GLU A CD   1 
ATOM   3422 O OE1  . GLU A 1 235 ? 9.02889   5.12663   10.49135 1.000 35.68584  ? 221 GLU A OE1  1 
ATOM   3423 O OE2  . GLU A 1 235 ? 8.22029   3.10288   10.50936 1.000 44.65717  ? 221 GLU A OE2  1 
ATOM   3424 H H    . GLU A 1 235 ? 9.54898   6.99080   5.46421  1.000 34.02201  ? 221 GLU A H    1 
ATOM   3425 H HA   . GLU A 1 235 ? 10.31440  4.48927   6.05675  1.000 38.42233  ? 221 GLU A HA   1 
ATOM   3426 H HB2  . GLU A 1 235 ? 10.29300  5.46820   8.19549  1.000 38.53278  ? 221 GLU A HB2  1 
ATOM   3427 H HB3  . GLU A 1 235 ? 8.79853   5.95292   7.95673  1.000 38.53278  ? 221 GLU A HB3  1 
ATOM   3428 H HG2  . GLU A 1 235 ? 8.07914   3.73760   7.98863  1.000 40.35043  ? 221 GLU A HG2  1 
ATOM   3429 H HG3  . GLU A 1 235 ? 9.57354   3.25888   8.23970  1.000 40.35043  ? 221 GLU A HG3  1 
ATOM   3430 N N    . PHE A 1 236 ? 8.22828   3.50720   5.27980  1.000 30.95525  ? 222 PHE A N    1 
ATOM   3431 C CA   . PHE A 1 236 ? 6.97620   2.90708   4.83941  1.000 27.55307  ? 222 PHE A CA   1 
ATOM   3432 C C    . PHE A 1 236 ? 6.56584   1.85428   5.85988  1.000 28.39420  ? 222 PHE A C    1 
ATOM   3433 O O    . PHE A 1 236 ? 7.36340   0.97473   6.20218  1.000 29.71649  ? 222 PHE A O    1 
ATOM   3434 C CB   . PHE A 1 236 ? 7.11500   2.27707   3.45206  1.000 30.74785  ? 222 PHE A CB   1 
ATOM   3435 C CG   . PHE A 1 236 ? 7.24700   3.27842   2.33986  1.000 29.47020  ? 222 PHE A CG   1 
ATOM   3436 C CD1  . PHE A 1 236 ? 6.12424   3.76340   1.69243  1.000 29.30969  ? 222 PHE A CD1  1 
ATOM   3437 C CD2  . PHE A 1 236 ? 8.49257   3.72920   1.93784  1.000 34.13718  ? 222 PHE A CD2  1 
ATOM   3438 C CE1  . PHE A 1 236 ? 6.23936   4.68204   0.66488  1.000 38.41844  ? 222 PHE A CE1  1 
ATOM   3439 C CE2  . PHE A 1 236 ? 8.61495   4.64971   0.90988  1.000 38.62697  ? 222 PHE A CE2  1 
ATOM   3440 C CZ   . PHE A 1 236 ? 7.48634   5.12588   0.27346  1.000 36.85094  ? 222 PHE A CZ   1 
ATOM   3441 H H    . PHE A 1 236 ? 8.86874   2.93689   5.34423  1.000 37.20225  ? 222 PHE A H    1 
ATOM   3442 H HA   . PHE A 1 236 ? 6.28464   3.58527   4.78740  1.000 33.11963  ? 222 PHE A HA   1 
ATOM   3443 H HB2  . PHE A 1 236 ? 7.90752   1.71786   3.44186  1.000 36.95336  ? 222 PHE A HB2  1 
ATOM   3444 H HB3  . PHE A 1 236 ? 6.32741   1.73960   3.27390  1.000 36.95336  ? 222 PHE A HB3  1 
ATOM   3445 H HD1  . PHE A 1 236 ? 5.28140   3.46783   1.95159  1.000 35.22757  ? 222 PHE A HD1  1 
ATOM   3446 H HD2  . PHE A 1 236 ? 9.25595   3.41042   2.36273  1.000 41.02056  ? 222 PHE A HD2  1 
ATOM   3447 H HE1  . PHE A 1 236 ? 5.47700   5.00050   0.23793  1.000 46.15807  ? 222 PHE A HE1  1 
ATOM   3448 H HE2  . PHE A 1 236 ? 9.45671   4.94662   0.64876  1.000 46.40830  ? 222 PHE A HE2  1 
ATOM   3449 H HZ   . PHE A 1 236 ? 7.56593   5.74387   -0.41694 1.000 44.27706  ? 222 PHE A HZ   1 
ATOM   3450 N N    . VAL A 1 237 ? 5.33285   1.95206   6.35297  1.000 29.64247  ? 223 VAL A N    1 
ATOM   3451 C CA   A VAL A 1 237 ? 4.80061   1.03212   7.35225  0.461 27.34953  ? 223 VAL A CA   1 
ATOM   3452 C CA   B VAL A 1 237 ? 4.80458   1.03061   7.35067  0.539 29.78543  ? 223 VAL A CA   1 
ATOM   3453 C C    . VAL A 1 237 ? 3.45362   0.52034   6.86645  1.000 29.27366  ? 223 VAL A C    1 
ATOM   3454 O O    . VAL A 1 237 ? 2.56304   1.31505   6.54441  1.000 27.58633  ? 223 VAL A O    1 
ATOM   3455 C CB   A VAL A 1 237 ? 4.64384   1.70262   8.73010  0.461 29.38336  ? 223 VAL A CB   1 
ATOM   3456 C CB   B VAL A 1 237 ? 4.68192   1.69843   8.73506  0.539 31.23060  ? 223 VAL A CB   1 
ATOM   3457 C CG1  A VAL A 1 237 ? 4.13675   0.69580   9.75272  0.461 30.26119  ? 223 VAL A CG1  1 
ATOM   3458 C CG1  B VAL A 1 237 ? 3.97244   3.04392   8.62830  0.539 27.58918  ? 223 VAL A CG1  1 
ATOM   3459 C CG2  A VAL A 1 237 ? 5.95197   2.31190   9.17834  0.461 29.22645  ? 223 VAL A CG2  1 
ATOM   3460 C CG2  B VAL A 1 237 ? 3.96641   0.77447   9.71225  0.539 30.26406  ? 223 VAL A CG2  1 
ATOM   3461 H H    . VAL A 1 237 ? 4.77388   2.56100   6.11558  1.000 35.62690  ? 223 VAL A H    1 
ATOM   3462 H HA   . VAL A 1 237 ? 5.40681   0.28016   7.44151  1.000 35.79846  ? 223 VAL A HA   1 
ATOM   3463 H HB   A VAL A 1 237 ? 3.99204   2.41761   8.66041  0.461 35.31597  ? 223 VAL A HB   1 
ATOM   3464 H HB   B VAL A 1 237 ? 5.57247   1.86532   9.08143  0.539 37.53266  ? 223 VAL A HB   1 
ATOM   3465 H HG11 A VAL A 1 237 ? 4.17038   1.09756   10.63497 0.461 36.36936  ? 223 VAL A HG11 1 
ATOM   3466 H HG11 B VAL A 1 237 ? 4.63044   3.75380   8.69156  0.539 33.16295  ? 223 VAL A HG11 1 
ATOM   3467 H HG12 A VAL A 1 237 ? 3.22294   0.45569   9.53321  0.461 36.36936  ? 223 VAL A HG12 1 
ATOM   3468 H HG12 B VAL A 1 237 ? 3.51442   3.09256   7.77463  0.539 33.16295  ? 223 VAL A HG12 1 
ATOM   3469 H HG13 A VAL A 1 237 ? 4.70131   -0.09255  9.72652  0.461 36.36936  ? 223 VAL A HG13 1 
ATOM   3470 H HG13 B VAL A 1 237 ? 3.33165   3.12137   9.35237  0.539 33.16295  ? 223 VAL A HG13 1 
ATOM   3471 H HG21 A VAL A 1 237 ? 6.64587   2.07155   8.54459  0.461 35.12768  ? 223 VAL A HG21 1 
ATOM   3472 H HG21 B VAL A 1 237 ? 4.00043   1.16558   10.59925 0.539 36.37282  ? 223 VAL A HG21 1 
ATOM   3473 H HG22 A VAL A 1 237 ? 5.85555   3.27647   9.21322  0.461 35.12768  ? 223 VAL A HG22 1 
ATOM   3474 H HG22 B VAL A 1 237 ? 3.04371   0.67131   9.43139  0.539 36.37282  ? 223 VAL A HG22 1 
ATOM   3475 H HG23 A VAL A 1 237 ? 6.17465   1.96970   10.05823 0.461 35.12768  ? 223 VAL A HG23 1 
ATOM   3476 H HG23 B VAL A 1 237 ? 4.41010   -0.08810  9.71383  0.539 36.37282  ? 223 VAL A HG23 1 
ATOM   3477 N N    . THR A 1 238 ? 3.30061   -0.80247  6.82699  1.000 28.22707  ? 224 THR A N    1 
ATOM   3478 C CA   . THR A 1 238 ? 2.08738   -1.43190  6.32958  1.000 28.67817  ? 224 THR A CA   1 
ATOM   3479 C C    . THR A 1 238 ? 1.68211   -2.56358  7.26018  1.000 26.58047  ? 224 THR A C    1 
ATOM   3480 O O    . THR A 1 238 ? 2.53598   -3.27942  7.79027  1.000 25.37748  ? 224 THR A O    1 
ATOM   3481 C CB   . THR A 1 238 ? 2.28581   -1.97569  4.90927  1.000 28.96163  ? 224 THR A CB   1 
ATOM   3482 O OG1  . THR A 1 238 ? 2.96753   -0.99944  4.11349  1.000 38.48390  ? 224 THR A OG1  1 
ATOM   3483 C CG2  . THR A 1 238 ? 0.94980   -2.29169  4.26845  1.000 28.90844  ? 224 THR A CG2  1 
ATOM   3484 H H    . THR A 1 238 ? 3.89807   -1.36317  7.08823  1.000 33.92842  ? 224 THR A H    1 
ATOM   3485 H HA   . THR A 1 238 ? 1.36872   -0.78061  6.31433  1.000 34.46974  ? 224 THR A HA   1 
ATOM   3486 H HB   . THR A 1 238 ? 2.81016   -2.79089  4.94680  1.000 34.80990  ? 224 THR A HB   1 
ATOM   3487 H HG1  . THR A 1 238 ? 3.74014   -0.87027  4.41679  1.000 46.23662  ? 224 THR A HG1  1 
ATOM   3488 H HG21 . THR A 1 238 ? 0.43142   -1.47853  4.16386  1.000 34.74607  ? 224 THR A HG21 1 
ATOM   3489 H HG22 . THR A 1 238 ? 1.08693   -2.69206  3.39563  1.000 34.74607  ? 224 THR A HG22 1 
ATOM   3490 H HG23 . THR A 1 238 ? 0.45342   -2.91208  4.82489  1.000 34.74607  ? 224 THR A HG23 1 
ATOM   3491 N N    . ALA A 1 239 ? 0.37613   -2.72151  7.44916  1.000 23.79039  ? 225 ALA A N    1 
ATOM   3492 C CA   . ALA A 1 239 ? -0.15918  -3.75373  8.32321  1.000 30.59769  ? 225 ALA A CA   1 
ATOM   3493 C C    . ALA A 1 239 ? -0.43291  -5.02818  7.53512  1.000 29.90697  ? 225 ALA A C    1 
ATOM   3494 O O    . ALA A 1 239 ? -0.86941  -4.98045  6.38115  1.000 29.20614  ? 225 ALA A O    1 
ATOM   3495 C CB   . ALA A 1 239 ? -1.44341  -3.26956  8.99879  1.000 25.61782  ? 225 ALA A CB   1 
ATOM   3496 H H    . ALA A 1 239 ? -0.22730  -2.23539  7.07613  1.000 28.60441  ? 225 ALA A H    1 
ATOM   3497 H HA   . ALA A 1 239 ? 0.49020   -3.95970  9.01371  1.000 36.77317  ? 225 ALA A HA   1 
ATOM   3498 H HB1  . ALA A 1 239 ? -1.25624  -2.44957  9.48199  1.000 30.79732  ? 225 ALA A HB1  1 
ATOM   3499 H HB2  . ALA A 1 239 ? -2.11584  -3.10673  8.31891  1.000 30.79732  ? 225 ALA A HB2  1 
ATOM   3500 H HB3  . ALA A 1 239 ? -1.75351  -3.95251  9.61386  1.000 30.79732  ? 225 ALA A HB3  1 
ATOM   3501 N N    . ALA A 1 240 ? -0.16568  -6.16734  8.16616  1.000 29.90046  ? 226 ALA A N    1 
ATOM   3502 C CA   . ALA A 1 240 ? -0.45023  -7.47014  7.57865  1.000 31.49330  ? 226 ALA A CA   1 
ATOM   3503 C C    . ALA A 1 240 ? -0.60994  -8.47819  8.71065  1.000 32.57782  ? 226 ALA A C    1 
ATOM   3504 O O    . ALA A 1 240 ? -0.51569  -8.13530  9.89215  1.000 26.40980  ? 226 ALA A O    1 
ATOM   3505 C CB   . ALA A 1 240 ? 0.65202   -7.89330  6.60447  1.000 29.11769  ? 226 ALA A CB   1 
ATOM   3506 H H    . ALA A 1 240 ? 0.18672   -6.21190  8.94938  1.000 35.93650  ? 226 ALA A H    1 
ATOM   3507 H HA   . ALA A 1 240 ? -1.28642  -7.41944  7.08966  1.000 37.84789  ? 226 ALA A HA   1 
ATOM   3508 H HB1  . ALA A 1 240 ? 1.49766   -7.92450  7.07862  1.000 34.99717  ? 226 ALA A HB1  1 
ATOM   3509 H HB2  . ALA A 1 240 ? 0.43960   -8.77043  6.24891  1.000 34.99717  ? 226 ALA A HB2  1 
ATOM   3510 H HB3  . ALA A 1 240 ? 0.70102   -7.24688  5.88291  1.000 34.99717  ? 226 ALA A HB3  1 
ATOM   3511 N N    . GLY A 1 241 ? -0.85566  -9.73076  8.33863  1.000 26.48404  ? 227 GLY A N    1 
ATOM   3512 C CA   . GLY A 1 241 ? -0.96757  -10.80952 9.29456  1.000 31.88860  ? 227 GLY A CA   1 
ATOM   3513 C C    . GLY A 1 241 ? -2.37158  -11.31063 9.55483  1.000 34.35974  ? 227 GLY A C    1 
ATOM   3514 O O    . GLY A 1 241 ? -2.55776  -12.11523 10.47563 1.000 33.20601  ? 227 GLY A O    1 
ATOM   3515 H H    . GLY A 1 241 ? -0.96232  -9.97851  7.52202  1.000 31.83679  ? 227 GLY A H    1 
ATOM   3516 H HA2  . GLY A 1 241 ? -0.44377  -11.56020 8.97360  1.000 38.32226  ? 227 GLY A HA2  1 
ATOM   3517 H HA3  . GLY A 1 241 ? -0.60253  -10.50884 10.14146 1.000 38.32226  ? 227 GLY A HA3  1 
ATOM   3518 N N    . ILE A 1 242 ? -3.36218  -10.85979 8.78925  1.000 32.65921  ? 228 ILE A N    1 
ATOM   3519 C CA   . ILE A 1 242 ? -4.73794  -11.33629 8.89473  1.000 39.20994  ? 228 ILE A CA   1 
ATOM   3520 C C    . ILE A 1 242 ? -5.14261  -11.87133 7.52783  1.000 39.54188  ? 228 ILE A C    1 
ATOM   3521 O O    . ILE A 1 242 ? -5.19792  -11.11369 6.55152  1.000 37.51336  ? 228 ILE A O    1 
ATOM   3522 C CB   . ILE A 1 242 ? -5.69423  -10.22861 9.36507  1.000 35.36246  ? 228 ILE A CB   1 
ATOM   3523 C CG1  . ILE A 1 242 ? -5.23141  -9.69367  10.72315 1.000 39.34236  ? 228 ILE A CG1  1 
ATOM   3524 C CG2  . ILE A 1 242 ? -7.12752  -10.75499 9.44531  1.000 36.06419  ? 228 ILE A CG2  1 
ATOM   3525 C CD1  . ILE A 1 242 ? -6.14327  -8.65001  11.32939 1.000 37.90533  ? 228 ILE A CD1  1 
ATOM   3526 H H    . ILE A 1 242 ? -3.25784  -10.25903 8.18278  1.000 39.24699  ? 228 ILE A H    1 
ATOM   3527 H HA   . ILE A 1 242 ? -4.78398  -12.06302 9.53554  1.000 47.10787  ? 228 ILE A HA   1 
ATOM   3528 H HB   . ILE A 1 242 ? -5.67833  -9.50339  8.72111  1.000 42.49089  ? 228 ILE A HB   1 
ATOM   3529 H HG12 . ILE A 1 242 ? -5.17993  -10.43530 11.34624 1.000 47.26677  ? 228 ILE A HG12 1 
ATOM   3530 H HG13 . ILE A 1 242 ? -4.35598  -9.29032  10.61445 1.000 47.26677  ? 228 ILE A HG13 1 
ATOM   3531 H HG21 . ILE A 1 242 ? -7.16050  -11.48535 10.08280 1.000 43.33296  ? 228 ILE A HG21 1 
ATOM   3532 H HG22 . ILE A 1 242 ? -7.71195  -10.03686 9.73451  1.000 43.33296  ? 228 ILE A HG22 1 
ATOM   3533 H HG23 . ILE A 1 242 ? -7.39821  -11.06891 8.56834  1.000 43.33296  ? 228 ILE A HG23 1 
ATOM   3534 H HD11 . ILE A 1 242 ? -6.95319  -9.08202  11.64289 1.000 45.54234  ? 228 ILE A HD11 1 
ATOM   3535 H HD12 . ILE A 1 242 ? -5.68659  -8.22462  12.07195 1.000 45.54234  ? 228 ILE A HD12 1 
ATOM   3536 H HD13 . ILE A 1 242 ? -6.36111  -7.98973  10.65302 1.000 45.54234  ? 228 ILE A HD13 1 
ATOM   3537 N N    . THR A 1 243 ? -5.42918  -13.17051 7.46176  1.000 50.38100  ? 229 THR A N    1 
ATOM   3538 C CA   . THR A 1 243 ? -5.66731  -13.83988 6.19093  1.000 62.40345  ? 229 THR A CA   1 
ATOM   3539 C C    . THR A 1 243 ? -7.04457  -13.47017 5.63657  1.000 64.15614  ? 229 THR A C    1 
ATOM   3540 O O    . THR A 1 243 ? -7.81699  -12.72717 6.24703  1.000 64.07918  ? 229 THR A O    1 
ATOM   3541 C CB   . THR A 1 243 ? -5.53036  -15.35493 6.35688  1.000 63.37866  ? 229 THR A CB   1 
ATOM   3542 O OG1  . THR A 1 243 ? -5.69396  -15.99547 5.08476  1.000 57.68461  ? 229 THR A OG1  1 
ATOM   3543 C CG2  . THR A 1 243 ? -6.56732  -15.90611 7.34072  1.000 58.17926  ? 229 THR A CG2  1 
ATOM   3544 H H    . THR A 1 243 ? -5.49149  -13.68850 8.14544  1.000 60.51314  ? 229 THR A H    1 
ATOM   3545 H HA   . THR A 1 243 ? -4.99967  -13.54059 5.55408  1.000 74.94007  ? 229 THR A HA   1 
ATOM   3546 H HB   . THR A 1 243 ? -4.65006  -15.55335 6.71268  1.000 76.11033  ? 229 THR A HB   1 
ATOM   3547 H HG1  . THR A 1 243 ? -5.05381  -15.79663 4.57853  1.000 69.27747  ? 229 THR A HG1  1 
ATOM   3548 H HG21 . THR A 1 243 ? -6.59236  -16.87438 7.28847  1.000 69.87106  ? 229 THR A HG21 1 
ATOM   3549 H HG22 . THR A 1 243 ? -6.33685  -15.64557 8.24620  1.000 69.87106  ? 229 THR A HG22 1 
ATOM   3550 H HG23 . THR A 1 243 ? -7.44642  -15.55647 7.12664  1.000 69.87106  ? 229 THR A HG23 1 
ATOM   3551 N N    . LEU A 1 244 ? -7.34932  -14.00155 4.45432  1.000 74.59128  ? 230 LEU A N    1 
ATOM   3552 C CA   . LEU A 1 244 ? -8.61942  -13.73666 3.78173  1.000 74.20253  ? 230 LEU A CA   1 
ATOM   3553 C C    . LEU A 1 244 ? -8.78144  -12.24807 3.49134  1.000 70.59586  ? 230 LEU A C    1 
ATOM   3554 O O    . LEU A 1 244 ? -8.54523  -11.79478 2.37088  1.000 68.06979  ? 230 LEU A O    1 
ATOM   3555 C CB   . LEU A 1 244 ? -9.79140  -14.23692 4.62828  1.000 73.90476  ? 230 LEU A CB   1 
ATOM   3556 C CG   . LEU A 1 244 ? -9.78298  -15.72831 4.97004  1.000 72.58362  ? 230 LEU A CG   1 
ATOM   3557 C CD1  . LEU A 1 244 ? -10.56593 -15.97901 6.24949  1.000 77.79590  ? 230 LEU A CD1  1 
ATOM   3558 C CD2  . LEU A 1 244 ? -10.35206 -16.55316 3.82357  1.000 69.75239  ? 230 LEU A CD2  1 
ATOM   3559 H H    . LEU A 1 244 ? -6.82964  -14.52678 4.01424  1.000 89.56547  ? 230 LEU A H    1 
ATOM   3560 H HA   . LEU A 1 244 ? -8.63494  -14.21343 2.93713  1.000 89.09897  ? 230 LEU A HA   1 
ATOM   3561 H HB2  . LEU A 1 244 ? -9.78813  -13.74995 5.46718  1.000 88.74165  ? 230 LEU A HB2  1 
ATOM   3562 H HB3  . LEU A 1 244 ? -10.61252 -14.05784 4.14392  1.000 88.74165  ? 230 LEU A HB3  1 
ATOM   3563 H HG   . LEU A 1 244 ? -8.86654  -16.01336 5.11073  1.000 87.15629  ? 230 LEU A HG   1 
ATOM   3564 H HD11 . LEU A 1 244 ? -10.63639 -16.93554 6.39432  1.000 93.41102  ? 230 LEU A HD11 1 
ATOM   3565 H HD12 . LEU A 1 244 ? -10.09833 -15.56559 6.99201  1.000 93.41102  ? 230 LEU A HD12 1 
ATOM   3566 H HD13 . LEU A 1 244 ? -11.45081 -15.59206 6.15918  1.000 93.41102  ? 230 LEU A HD13 1 
ATOM   3567 H HD21 . LEU A 1 244 ? -10.36191 -17.48813 4.08170  1.000 83.75881  ? 230 LEU A HD21 1 
ATOM   3568 H HD22 . LEU A 1 244 ? -11.25492 -16.25230 3.63584  1.000 83.75881  ? 230 LEU A HD22 1 
ATOM   3569 H HD23 . LEU A 1 244 ? -9.79344  -16.43224 3.03985  1.000 83.75881  ? 230 LEU A HD23 1 
ATOM   3570 N N    . LYS B 1 17  ? 18.90983  -32.25932 13.99032 1.000 60.89790  ? 3   LYS B N    1 
ATOM   3571 C CA   . LYS B 1 17  ? 18.54337  -33.51935 14.62678 1.000 58.16809  ? 3   LYS B CA   1 
ATOM   3572 C C    . LYS B 1 17  ? 17.04049  -33.76684 14.54979 1.000 56.69051  ? 3   LYS B C    1 
ATOM   3573 O O    . LYS B 1 17  ? 16.59109  -34.70809 13.89700 1.000 52.75256  ? 3   LYS B O    1 
ATOM   3574 C CB   . LYS B 1 17  ? 18.99628  -33.53218 16.08901 1.000 69.01471  ? 3   LYS B CB   1 
ATOM   3575 C CG   . LYS B 1 17  ? 20.43211  -33.99305 16.30258 1.000 74.73277  ? 3   LYS B CG   1 
ATOM   3576 C CD   . LYS B 1 17  ? 20.59213  -35.47861 16.00414 1.000 76.30056  ? 3   LYS B CD   1 
ATOM   3577 C CE   . LYS B 1 17  ? 21.92085  -36.01624 16.51729 1.000 74.76662  ? 3   LYS B CE   1 
ATOM   3578 N NZ   . LYS B 1 17  ? 23.09145  -35.33419 15.89700 1.000 76.67376  ? 3   LYS B NZ   1 
ATOM   3579 H HA   . LYS B 1 17  ? 18.98996  -34.24316 14.16036 1.000 69.85764  ? 3   LYS B HA   1 
ATOM   3580 H HB2  . LYS B 1 17  ? 18.92192  -32.63221 16.44316 1.000 82.87359  ? 3   LYS B HB2  1 
ATOM   3581 H HB3  . LYS B 1 17  ? 18.41901  -34.13293 16.58576 1.000 82.87359  ? 3   LYS B HB3  1 
ATOM   3582 H HG2  . LYS B 1 17  ? 21.01983  -33.49814 15.71050 1.000 89.73526  ? 3   LYS B HG2  1 
ATOM   3583 H HG3  . LYS B 1 17  ? 20.68507  -33.83870 17.22621 1.000 89.73526  ? 3   LYS B HG3  1 
ATOM   3584 H HD2  . LYS B 1 17  ? 19.87737  -35.97126 16.43693 1.000 91.61661  ? 3   LYS B HD2  1 
ATOM   3585 H HD3  . LYS B 1 17  ? 20.55781  -35.61831 15.04486 1.000 91.61661  ? 3   LYS B HD3  1 
ATOM   3586 H HE2  . LYS B 1 17  ? 21.96814  -35.88146 17.47672 1.000 89.77588  ? 3   LYS B HE2  1 
ATOM   3587 H HE3  . LYS B 1 17  ? 21.98067  -36.96235 16.31184 1.000 89.77588  ? 3   LYS B HE3  1 
ATOM   3588 H HZ1  . LYS B 1 17  ? 23.84711  -35.71378 16.17445 1.000 92.06445  ? 3   LYS B HZ1  1 
ATOM   3589 H HZ2  . LYS B 1 17  ? 23.04546  -35.39658 15.01038 1.000 92.06445  ? 3   LYS B HZ2  1 
ATOM   3590 H HZ3  . LYS B 1 17  ? 23.09919  -34.47419 16.12601 1.000 92.06445  ? 3   LYS B HZ3  1 
ATOM   3591 N N    . GLY B 1 18  ? 16.26518  -32.91823 15.22671 1.000 54.70864  ? 4   GLY B N    1 
ATOM   3592 C CA   . GLY B 1 18  ? 14.82334  -33.10280 15.23774 1.000 45.75434  ? 4   GLY B CA   1 
ATOM   3593 C C    . GLY B 1 18  ? 14.19489  -32.91276 13.87008 1.000 40.70340  ? 4   GLY B C    1 
ATOM   3594 O O    . GLY B 1 18  ? 13.33470  -33.69609 13.45851 1.000 39.02358  ? 4   GLY B O    1 
ATOM   3595 H H    . GLY B 1 18  ? 16.54670  -32.24219 15.67762 1.000 65.70630  ? 4   GLY B H    1 
ATOM   3596 H HA2  . GLY B 1 18  ? 14.61872  -34.00011 15.54410 1.000 54.96115  ? 4   GLY B HA2  1 
ATOM   3597 H HA3  . GLY B 1 18  ? 14.42420  -32.46233 15.84716 1.000 54.96115  ? 4   GLY B HA3  1 
ATOM   3598 N N    . GLU B 1 19  ? 14.61239  -31.87140 13.14645 1.000 39.54880  ? 5   GLU B N    1 
ATOM   3599 C CA   . GLU B 1 19  ? 14.03991  -31.61553 11.82902 1.000 45.86643  ? 5   GLU B CA   1 
ATOM   3600 C C    . GLU B 1 19  ? 14.34922  -32.74732 10.85748 1.000 42.62537  ? 5   GLU B C    1 
ATOM   3601 O O    . GLU B 1 19  ? 13.58423  -32.98255 9.91538  1.000 43.20498  ? 5   GLU B O    1 
ATOM   3602 C CB   . GLU B 1 19  ? 14.55927  -30.28394 11.27976 1.000 43.31941  ? 5   GLU B CB   1 
ATOM   3603 C CG   . GLU B 1 19  ? 15.94027  -30.36008 10.64334 1.000 54.06220  ? 5   GLU B CG   1 
ATOM   3604 C CD   . GLU B 1 19  ? 16.50225  -28.99267 10.29731 1.000 71.96698  ? 5   GLU B CD   1 
ATOM   3605 O OE1  . GLU B 1 19  ? 16.10358  -28.00137 10.94542 1.000 71.65960  ? 5   GLU B OE1  1 
ATOM   3606 O OE2  . GLU B 1 19  ? 17.34097  -28.90888 9.37452  1.000 66.83439  ? 5   GLU B OE2  1 
ATOM   3607 H H    . GLU B 1 19  ? 15.21490  -31.30919 13.39241 1.000 47.51450  ? 5   GLU B H    1 
ATOM   3608 H HA   . GLU B 1 19  ? 13.07602  -31.54781 11.91396 1.000 55.09566  ? 5   GLU B HA   1 
ATOM   3609 H HB2  . GLU B 1 19  ? 13.94146  -29.96698 10.60245 1.000 52.03923  ? 5   GLU B HB2  1 
ATOM   3610 H HB3  . GLU B 1 19  ? 14.60745  -29.64644 12.00927 1.000 52.03923  ? 5   GLU B HB3  1 
ATOM   3611 H HG2  . GLU B 1 19  ? 16.55130  -30.78752 11.26370 1.000 64.93058  ? 5   GLU B HG2  1 
ATOM   3612 H HG3  . GLU B 1 19  ? 15.88317  -30.87710 9.82460  1.000 64.93058  ? 5   GLU B HG3  1 
ATOM   3613 N N    . GLU B 1 20  ? 15.46434  -33.45225 11.06467 1.000 39.52961  ? 6   GLU B N    1 
ATOM   3614 C CA   . GLU B 1 20  ? 15.81115  -34.58404 10.21201 1.000 40.68967  ? 6   GLU B CA   1 
ATOM   3615 C C    . GLU B 1 20  ? 14.73873  -35.66510 10.23031 1.000 43.98343  ? 6   GLU B C    1 
ATOM   3616 O O    . GLU B 1 20  ? 14.64238  -36.44486 9.27638  1.000 38.57015  ? 6   GLU B O    1 
ATOM   3617 C CB   . GLU B 1 20  ? 17.16530  -35.15335 10.65310 1.000 44.04287  ? 6   GLU B CB   1 
ATOM   3618 C CG   . GLU B 1 20  ? 17.40726  -36.62602 10.32351 1.000 64.17733  ? 6   GLU B CG   1 
ATOM   3619 C CD   . GLU B 1 20  ? 17.40974  -36.91441 8.83336  1.000 73.04979  ? 6   GLU B CD   1 
ATOM   3620 O OE1  . GLU B 1 20  ? 17.75174  -36.00594 8.04651  1.000 72.90464  ? 6   GLU B OE1  1 
ATOM   3621 O OE2  . GLU B 1 20  ? 17.06580  -38.05360 8.44990  1.000 72.60061  ? 6   GLU B OE2  1 
ATOM   3622 H H    . GLU B 1 20  ? 16.03309  -33.29454 11.69017 1.000 47.49147  ? 6   GLU B H    1 
ATOM   3623 H HA   . GLU B 1 20  ? 15.89815  -34.28432 9.29359  1.000 48.88354  ? 6   GLU B HA   1 
ATOM   3624 H HB2  . GLU B 1 20  ? 17.86583  -34.64267 10.21793 1.000 52.90739  ? 6   GLU B HB2  1 
ATOM   3625 H HB3  . GLU B 1 20  ? 17.23536  -35.05913 11.61596 1.000 52.90739  ? 6   GLU B HB3  1 
ATOM   3626 H HG2  . GLU B 1 20  ? 18.27022  -36.88987 10.67930 1.000 77.06874  ? 6   GLU B HG2  1 
ATOM   3627 H HG3  . GLU B 1 20  ? 16.70465  -37.15812 10.72860 1.000 77.06874  ? 6   GLU B HG3  1 
ATOM   3628 N N    . LEU B 1 21  ? 13.92852  -35.72755 11.28460 1.000 38.57428  ? 7   LEU B N    1 
ATOM   3629 C CA   . LEU B 1 21  ? 12.88588  -36.73898 11.38175 1.000 41.47159  ? 7   LEU B CA   1 
ATOM   3630 C C    . LEU B 1 21  ? 11.66964  -36.42819 10.51837 1.000 38.05027  ? 7   LEU B C    1 
ATOM   3631 O O    . LEU B 1 21  ? 10.76835  -37.26864 10.42776 1.000 36.67356  ? 7   LEU B O    1 
ATOM   3632 C CB   . LEU B 1 21  ? 12.44951  -36.89043 12.84122 1.000 39.52945  ? 7   LEU B CB   1 
ATOM   3633 C CG   . LEU B 1 21  ? 13.54237  -37.31574 13.82398 1.000 37.15040  ? 7   LEU B CG   1 
ATOM   3634 C CD1  . LEU B 1 21  ? 13.10506  -37.04427 15.25609 1.000 34.50663  ? 7   LEU B CD1  1 
ATOM   3635 C CD2  . LEU B 1 21  ? 13.88493  -38.78501 13.63353 1.000 32.75721  ? 7   LEU B CD2  1 
ATOM   3636 H H    . LEU B 1 21  ? 13.96419  -35.19314 11.95746 1.000 46.34507  ? 7   LEU B H    1 
ATOM   3637 H HA   . LEU B 1 21  ? 13.24763  -37.58788 11.08272 1.000 49.82185  ? 7   LEU B HA   1 
ATOM   3638 H HB2  . LEU B 1 21  ? 12.10614  -36.03560 13.14499 1.000 47.49128  ? 7   LEU B HB2  1 
ATOM   3639 H HB3  . LEU B 1 21  ? 11.75032  -37.56162 12.88025 1.000 47.49128  ? 7   LEU B HB3  1 
ATOM   3640 H HG   . LEU B 1 21  ? 14.34405  -36.79704 13.65316 1.000 44.63641  ? 7   LEU B HG   1 
ATOM   3641 H HD11 . LEU B 1 21  ? 12.28451  -37.53030 15.43323 1.000 41.46389  ? 7   LEU B HD11 1 
ATOM   3642 H HD12 . LEU B 1 21  ? 13.80268  -37.34140 15.86102 1.000 41.46389  ? 7   LEU B HD12 1 
ATOM   3643 H HD13 . LEU B 1 21  ? 12.95573  -36.09211 15.36558 1.000 41.46389  ? 7   LEU B HD13 1 
ATOM   3644 H HD21 . LEU B 1 21  ? 14.27825  -38.90630 12.75519 1.000 39.02896  ? 7   LEU B HD21 1 
ATOM   3645 H HD22 . LEU B 1 21  ? 14.51678  -39.05337 14.31883 1.000 39.02896  ? 7   LEU B HD22 1 
ATOM   3646 H HD23 . LEU B 1 21  ? 13.07316  -39.31075 13.70792 1.000 39.02896  ? 7   LEU B HD23 1 
ATOM   3647 N N    . PHE B 1 22  ? 11.62195  -35.25680 9.87913  1.000 35.46898  ? 8   PHE B N    1 
ATOM   3648 C CA   . PHE B 1 22  ? 10.45201  -34.82895 9.11990  1.000 35.65837  ? 8   PHE B CA   1 
ATOM   3649 C C    . PHE B 1 22  ? 10.76907  -34.59854 7.64574  1.000 36.70478  ? 8   PHE B C    1 
ATOM   3650 O O    . PHE B 1 22  ? 10.04518  -33.86334 6.96757  1.000 33.77407  ? 8   PHE B O    1 
ATOM   3651 C CB   . PHE B 1 22  ? 9.85940   -33.56080 9.73827  1.000 30.31928  ? 8   PHE B CB   1 
ATOM   3652 C CG   . PHE B 1 22  ? 9.32610   -33.75796 11.12978 1.000 31.32599  ? 8   PHE B CG   1 
ATOM   3653 C CD1  . PHE B 1 22  ? 10.15516  -33.62044 12.23015 1.000 31.69136  ? 8   PHE B CD1  1 
ATOM   3654 C CD2  . PHE B 1 22  ? 7.99530   -34.08163 11.33581 1.000 27.86628  ? 8   PHE B CD2  1 
ATOM   3655 C CE1  . PHE B 1 22  ? 9.66688   -33.80136 13.51035 1.000 30.36197  ? 8   PHE B CE1  1 
ATOM   3656 C CE2  . PHE B 1 22  ? 7.50089   -34.26615 12.61270 1.000 30.77017  ? 8   PHE B CE2  1 
ATOM   3657 C CZ   . PHE B 1 22  ? 8.33771   -34.12590 13.70190 1.000 31.74826  ? 8   PHE B CZ   1 
ATOM   3658 H H    . PHE B 1 22  ? 12.26577  -34.68667 9.87228  1.000 42.61872  ? 8   PHE B H    1 
ATOM   3659 H HA   . PHE B 1 22  ? 9.78453   -35.53142 9.16361  1.000 42.84598  ? 8   PHE B HA   1 
ATOM   3660 H HB2  . PHE B 1 22  ? 10.55064  -32.88156 9.77958  1.000 36.43908  ? 8   PHE B HB2  1 
ATOM   3661 H HB3  . PHE B 1 22  ? 9.12672   -33.25505 9.18095  1.000 36.43908  ? 8   PHE B HB3  1 
ATOM   3662 H HD1  . PHE B 1 22  ? 11.05106  -33.40380 12.10634 1.000 38.08558  ? 8   PHE B HD1  1 
ATOM   3663 H HD2  . PHE B 1 22  ? 7.42733   -34.17596 10.60546 1.000 33.49548  ? 8   PHE B HD2  1 
ATOM   3664 H HE1  . PHE B 1 22  ? 10.23252  -33.70473 14.24220 1.000 36.49031  ? 8   PHE B HE1  1 
ATOM   3665 H HE2  . PHE B 1 22  ? 6.60567   -34.48453 12.73836 1.000 36.98015  ? 8   PHE B HE2  1 
ATOM   3666 H HZ   . PHE B 1 22  ? 8.00743   -34.24959 14.56243 1.000 38.15385  ? 8   PHE B HZ   1 
ATOM   3667 N N    . THR B 1 23  ? 11.83019  -35.22326 7.13042  1.000 40.71581  ? 9   THR B N    1 
ATOM   3668 C CA   . THR B 1 23  ? 12.19920  -35.02067 5.73366  1.000 40.73855  ? 9   THR B CA   1 
ATOM   3669 C C    . THR B 1 23  ? 11.24322  -35.73109 4.78420  1.000 40.79062  ? 9   THR B C    1 
ATOM   3670 O O    . THR B 1 23  ? 11.09699  -35.31306 3.62972  1.000 45.59452  ? 9   THR B O    1 
ATOM   3671 C CB   . THR B 1 23  ? 13.62789  -35.50758 5.49123  1.000 41.15647  ? 9   THR B CB   1 
ATOM   3672 O OG1  . THR B 1 23  ? 13.78833  -36.81896 6.04703  1.000 43.02665  ? 9   THR B OG1  1 
ATOM   3673 C CG2  . THR B 1 23  ? 14.63367  -34.55932 6.12524  1.000 46.13429  ? 9   THR B CG2  1 
ATOM   3674 H H    . THR B 1 23  ? 12.34376  -35.76074 7.56281  1.000 48.91491  ? 9   THR B H    1 
ATOM   3675 H HA   . THR B 1 23  ? 12.16287  -34.07023 5.54330  1.000 48.94221  ? 9   THR B HA   1 
ATOM   3676 H HB   . THR B 1 23  ? 13.80175  -35.53819 4.53743  1.000 49.44370  ? 9   THR B HB   1 
ATOM   3677 H HG1  . THR B 1 23  ? 13.21921  -37.34198 5.71817  1.000 51.68792  ? 9   THR B HG1  1 
ATOM   3678 H HG21 . THR B 1 23  ? 14.51496  -33.66428 5.77066  1.000 55.41709  ? 9   THR B HG21 1 
ATOM   3679 H HG22 . THR B 1 23  ? 14.50752  -34.53631 7.08672  1.000 55.41709  ? 9   THR B HG22 1 
ATOM   3680 H HG23 . THR B 1 23  ? 15.53676  -34.85676 5.93326  1.000 55.41709  ? 9   THR B HG23 1 
ATOM   3681 N N    . GLY B 1 24  ? 10.59380  -36.79836 5.24160  1.000 39.02376  ? 10  GLY B N    1 
ATOM   3682 C CA   . GLY B 1 24  ? 9.67745   -37.54328 4.40212  1.000 36.61138  ? 10  GLY B CA   1 
ATOM   3683 C C    . GLY B 1 24  ? 8.28723   -37.62791 4.99380  1.000 36.21251  ? 10  GLY B C    1 
ATOM   3684 O O    . GLY B 1 24  ? 7.94342   -36.86456 5.90113  1.000 41.12729  ? 10  GLY B O    1 
ATOM   3685 H H    . GLY B 1 24  ? 10.67058  -37.10902 6.03984  1.000 46.88445  ? 10  GLY B H    1 
ATOM   3686 H HA2  . GLY B 1 24  ? 9.61460   -37.11223 3.53544  1.000 43.98960  ? 10  GLY B HA2  1 
ATOM   3687 H HA3  . GLY B 1 24  ? 10.01374  -38.44523 4.28260  1.000 43.98960  ? 10  GLY B HA3  1 
ATOM   3688 N N    . VAL B 1 25  ? 7.47587   -38.54502 4.47881  1.000 35.15496  ? 11  VAL B N    1 
ATOM   3689 C CA   . VAL B 1 25  ? 6.13606   -38.76995 5.00814  1.000 32.22046  ? 11  VAL B CA   1 
ATOM   3690 C C    . VAL B 1 25  ? 6.25135   -39.56462 6.30114  1.000 31.27154  ? 11  VAL B C    1 
ATOM   3691 O O    . VAL B 1 25  ? 6.95524   -40.57916 6.36090  1.000 34.42033  ? 11  VAL B O    1 
ATOM   3692 C CB   . VAL B 1 25  ? 5.26158   -39.50093 3.97772  1.000 38.61905  ? 11  VAL B CB   1 
ATOM   3693 C CG1  . VAL B 1 25  ? 3.88565   -39.78789 4.55807  1.000 33.58945  ? 11  VAL B CG1  1 
ATOM   3694 C CG2  . VAL B 1 25  ? 5.15518   -38.67733 2.69421  1.000 37.63573  ? 11  VAL B CG2  1 
ATOM   3695 H H    . VAL B 1 25  ? 7.67944   -39.05457 3.81660  1.000 42.24190  ? 11  VAL B H    1 
ATOM   3696 H HA   . VAL B 1 25  ? 5.71821   -37.91747 5.20708  1.000 38.38486  ? 11  VAL B HA   1 
ATOM   3697 H HB   . VAL B 1 25  ? 5.67302   -40.35065 3.75503  1.000 46.39880  ? 11  VAL B HB   1 
ATOM   3698 H HG11 . VAL B 1 25  ? 3.60918   -39.03433 5.10268  1.000 40.36328  ? 11  VAL B HG11 1 
ATOM   3699 H HG12 . VAL B 1 25  ? 3.25719   -39.91868 3.83086  1.000 40.36328  ? 11  VAL B HG12 1 
ATOM   3700 H HG13 . VAL B 1 25  ? 3.93333   -40.58946 5.10223  1.000 40.36328  ? 11  VAL B HG13 1 
ATOM   3701 H HG21 . VAL B 1 25  ? 5.63242   -37.84151 2.81484  1.000 45.21881  ? 11  VAL B HG21 1 
ATOM   3702 H HG22 . VAL B 1 25  ? 5.54760   -39.17976 1.96314  1.000 45.21881  ? 11  VAL B HG22 1 
ATOM   3703 H HG23 . VAL B 1 25  ? 4.21958   -38.50030 2.50923  1.000 45.21881  ? 11  VAL B HG23 1 
ATOM   3704 N N    . VAL B 1 26  ? 5.56285   -39.10601 7.33980  1.000 33.53977  ? 12  VAL B N    1 
ATOM   3705 C CA   . VAL B 1 26  ? 5.65417   -39.68135 8.67377  1.000 30.46976  ? 12  VAL B CA   1 
ATOM   3706 C C    . VAL B 1 26  ? 4.26699   -40.16065 9.08077  1.000 27.57919  ? 12  VAL B C    1 
ATOM   3707 O O    . VAL B 1 26  ? 3.31557   -39.37872 9.03499  1.000 32.65715  ? 12  VAL B O    1 
ATOM   3708 C CB   . VAL B 1 26  ? 6.20143   -38.66871 9.69668  1.000 33.26872  ? 12  VAL B CB   1 
ATOM   3709 C CG1  . VAL B 1 26  ? 6.23644   -39.27552 11.08415 1.000 29.73865  ? 12  VAL B CG1  1 
ATOM   3710 C CG2  . VAL B 1 26  ? 7.58825   -38.19205 9.27853  1.000 36.92894  ? 12  VAL B CG2  1 
ATOM   3711 H H    . VAL B 1 26  ? 5.01938   -38.44113 7.29328  1.000 40.30367  ? 12  VAL B H    1 
ATOM   3712 H HA   . VAL B 1 26  ? 6.23817   -40.45568 8.65748  1.000 36.61965  ? 12  VAL B HA   1 
ATOM   3713 H HB   . VAL B 1 26  ? 5.61171   -37.89906 9.72443  1.000 39.97841  ? 12  VAL B HB   1 
ATOM   3714 H HG11 . VAL B 1 26  ? 6.84572   -38.76261 11.63787 1.000 35.74232  ? 12  VAL B HG11 1 
ATOM   3715 H HG12 . VAL B 1 26  ? 5.34379   -39.24951 11.46283 1.000 35.74232  ? 12  VAL B HG12 1 
ATOM   3716 H HG13 . VAL B 1 26  ? 6.54171   -40.19396 11.01955 1.000 35.74232  ? 12  VAL B HG13 1 
ATOM   3717 H HG21 . VAL B 1 26  ? 7.88760   -37.50878 9.89856  1.000 44.37067  ? 12  VAL B HG21 1 
ATOM   3718 H HG22 . VAL B 1 26  ? 8.19949   -38.94504 9.29574  1.000 44.37067  ? 12  VAL B HG22 1 
ATOM   3719 H HG23 . VAL B 1 26  ? 7.53928   -37.82619 8.38151  1.000 44.37067  ? 12  VAL B HG23 1 
ATOM   3720 N N    . PRO B 1 27  ? 4.09561   -41.42283 9.47559  1.000 28.40235  ? 13  PRO B N    1 
ATOM   3721 C CA   . PRO B 1 27  ? 2.77350   -41.86411 9.93713  1.000 29.69288  ? 13  PRO B CA   1 
ATOM   3722 C C    . PRO B 1 27  ? 2.40285   -41.19887 11.25295 1.000 30.27268  ? 13  PRO B C    1 
ATOM   3723 O O    . PRO B 1 27  ? 3.25450   -40.95968 12.11279 1.000 27.28630  ? 13  PRO B O    1 
ATOM   3724 C CB   . PRO B 1 27  ? 2.93298   -43.38199 10.09186 1.000 32.98571  ? 13  PRO B CB   1 
ATOM   3725 C CG   . PRO B 1 27  ? 4.39813   -43.60556 10.25263 1.000 34.29385  ? 13  PRO B CG   1 
ATOM   3726 C CD   . PRO B 1 27  ? 5.06900   -42.53047 9.44691  1.000 33.71951  ? 13  PRO B CD   1 
ATOM   3727 H HA   . PRO B 1 27  ? 2.09188   -41.67855 9.27240  1.000 35.68740  ? 13  PRO B HA   1 
ATOM   3728 H HB2  . PRO B 1 27  ? 2.44801   -43.68614 10.87493 1.000 39.63879  ? 13  PRO B HB2  1 
ATOM   3729 H HB3  . PRO B 1 27  ? 2.59879   -43.83089 9.29958  1.000 39.63879  ? 13  PRO B HB3  1 
ATOM   3730 H HG2  . PRO B 1 27  ? 4.63906   -43.53345 11.18947 1.000 41.20856  ? 13  PRO B HG2  1 
ATOM   3731 H HG3  . PRO B 1 27  ? 4.63368   -44.48433 9.91620  1.000 41.20856  ? 13  PRO B HG3  1 
ATOM   3732 H HD2  . PRO B 1 27  ? 5.90653   -42.26403 9.85736  1.000 40.51935  ? 13  PRO B HD2  1 
ATOM   3733 H HD3  . PRO B 1 27  ? 5.22540   -42.82843 8.53715  1.000 40.51935  ? 13  PRO B HD3  1 
ATOM   3734 N N    . ILE B 1 28  ? 1.11671   -40.89053 11.39724 1.000 28.01425  ? 14  ILE B N    1 
ATOM   3735 C CA   . ILE B 1 28  ? 0.59565   -40.19314 12.56476 1.000 24.04054  ? 14  ILE B CA   1 
ATOM   3736 C C    . ILE B 1 28  ? -0.48935  -41.04584 13.20436 1.000 28.72083  ? 14  ILE B C    1 
ATOM   3737 O O    . ILE B 1 28  ? -1.31897  -41.63987 12.50713 1.000 29.10001  ? 14  ILE B O    1 
ATOM   3738 C CB   . ILE B 1 28  ? 0.03615   -38.80211 12.19951 1.000 28.44565  ? 14  ILE B CB   1 
ATOM   3739 C CG1  . ILE B 1 28  ? 1.14753   -37.90022 11.66099 1.000 24.73579  ? 14  ILE B CG1  1 
ATOM   3740 C CG2  . ILE B 1 28  ? -0.62988  -38.16664 13.41427 1.000 25.30245  ? 14  ILE B CG2  1 
ATOM   3741 C CD1  . ILE B 1 28  ? 0.64307   -36.62342 11.02963 1.000 28.48387  ? 14  ILE B CD1  1 
ATOM   3742 H H    . ILE B 1 28  ? 0.51263   -41.08098 10.81551 1.000 33.67304  ? 14  ILE B H    1 
ATOM   3743 H HA   . ILE B 1 28  ? 1.31508   -40.07778 13.20508 1.000 28.90459  ? 14  ILE B HA   1 
ATOM   3744 H HB   . ILE B 1 28  ? -0.62926  -38.91249 11.50241 1.000 34.19072  ? 14  ILE B HB   1 
ATOM   3745 H HG12 . ILE B 1 28  ? 1.73402   -37.65635 12.39411 1.000 29.73888  ? 14  ILE B HG12 1 
ATOM   3746 H HG13 . ILE B 1 28  ? 1.64523   -38.38770 10.98604 1.000 29.73888  ? 14  ILE B HG13 1 
ATOM   3747 H HG21 . ILE B 1 28  ? -0.10976  -38.37678 14.20561 1.000 30.41888  ? 14  ILE B HG21 1 
ATOM   3748 H HG22 . ILE B 1 28  ? -0.66617  -37.20560 13.28787 1.000 30.41888  ? 14  ILE B HG22 1 
ATOM   3749 H HG23 . ILE B 1 28  ? -1.52772  -38.52255 13.50443 1.000 30.41888  ? 14  ILE B HG23 1 
ATOM   3750 H HD11 . ILE B 1 28  ? 1.36854   -36.20508 10.54017 1.000 34.23658  ? 14  ILE B HD11 1 
ATOM   3751 H HD12 . ILE B 1 28  ? -0.08460  -36.83636 10.42461 1.000 34.23658  ? 14  ILE B HD12 1 
ATOM   3752 H HD13 . ILE B 1 28  ? 0.32898   -36.02831 11.72827 1.000 34.23658  ? 14  ILE B HD13 1 
ATOM   3753 N N    . LEU B 1 29  ? -0.47559  -41.10543 14.53307 1.000 25.31856  ? 15  LEU B N    1 
ATOM   3754 C CA   . LEU B 1 29  ? -1.54515  -41.70831 15.31343 1.000 26.65479  ? 15  LEU B CA   1 
ATOM   3755 C C    . LEU B 1 29  ? -1.99461  -40.70387 16.36333 1.000 29.34491  ? 15  LEU B C    1 
ATOM   3756 O O    . LEU B 1 29  ? -1.16506  -40.03733 16.98958 1.000 27.91788  ? 15  LEU B O    1 
ATOM   3757 C CB   . LEU B 1 29  ? -1.09410  -43.01225 15.98529 1.000 29.34845  ? 15  LEU B CB   1 
ATOM   3758 C CG   . LEU B 1 29  ? -0.83396  -44.20815 15.06778 1.000 26.13579  ? 15  LEU B CG   1 
ATOM   3759 C CD1  . LEU B 1 29  ? -0.30455  -45.38016 15.87700 1.000 27.10745  ? 15  LEU B CD1  1 
ATOM   3760 C CD2  . LEU B 1 29  ? -2.09041  -44.60436 14.31222 1.000 26.96974  ? 15  LEU B CD2  1 
ATOM   3761 H H    . LEU B 1 29  ? 0.16302   -40.79326 15.01714 1.000 30.43821  ? 15  LEU B H    1 
ATOM   3762 H HA   . LEU B 1 29  ? -2.29667  -41.92440 14.73949 1.000 32.04169  ? 15  LEU B HA   1 
ATOM   3763 H HB2  . LEU B 1 29  ? -0.26707  -42.83368 16.45968 1.000 35.27407  ? 15  LEU B HB2  1 
ATOM   3764 H HB3  . LEU B 1 29  ? -1.78458  -43.28033 16.61160 1.000 35.27407  ? 15  LEU B HB3  1 
ATOM   3765 H HG   . LEU B 1 29  ? -0.16607  -43.95932 14.40982 1.000 31.41889  ? 15  LEU B HG   1 
ATOM   3766 H HD11 . LEU B 1 29  ? -0.82302  -45.46046 16.69287 1.000 32.58488  ? 15  LEU B HD11 1 
ATOM   3767 H HD12 . LEU B 1 29  ? -0.38823  -46.19071 15.35078 1.000 32.58488  ? 15  LEU B HD12 1 
ATOM   3768 H HD13 . LEU B 1 29  ? 0.62770   -45.22009 16.09192 1.000 32.58488  ? 15  LEU B HD13 1 
ATOM   3769 H HD21 . LEU B 1 29  ? -2.31834  -43.89900 13.68659 1.000 32.41963  ? 15  LEU B HD21 1 
ATOM   3770 H HD22 . LEU B 1 29  ? -1.92309  -45.43067 13.83251 1.000 32.41963  ? 15  LEU B HD22 1 
ATOM   3771 H HD23 . LEU B 1 29  ? -2.81359  -44.73058 14.94624 1.000 32.41963  ? 15  LEU B HD23 1 
ATOM   3772 N N    . VAL B 1 30  ? -3.30710  -40.58718 16.54449 1.000 26.95515  ? 16  VAL B N    1 
ATOM   3773 C CA   . VAL B 1 30  ? -3.88729  -39.63482 17.48220 1.000 27.29404  ? 16  VAL B CA   1 
ATOM   3774 C C    . VAL B 1 30  ? -4.83734  -40.37554 18.41140 1.000 25.36541  ? 16  VAL B C    1 
ATOM   3775 O O    . VAL B 1 30  ? -5.58131  -41.26264 17.97829 1.000 25.74042  ? 16  VAL B O    1 
ATOM   3776 C CB   . VAL B 1 30  ? -4.62671  -38.49358 16.75218 1.000 21.91562  ? 16  VAL B CB   1 
ATOM   3777 C CG1  . VAL B 1 30  ? -5.10831  -37.44904 17.75031 1.000 21.85803  ? 16  VAL B CG1  1 
ATOM   3778 C CG2  . VAL B 1 30  ? -3.72459  -37.86356 15.69931 1.000 21.60079  ? 16  VAL B CG2  1 
ATOM   3779 H H    . VAL B 1 30  ? -3.89204  -41.05906 16.12644 1.000 32.40212  ? 16  VAL B H    1 
ATOM   3780 H HA   . VAL B 1 30  ? -3.17759  -39.24753 18.01814 1.000 32.80879  ? 16  VAL B HA   1 
ATOM   3781 H HB   . VAL B 1 30  ? -5.40430  -38.85762 16.30082 1.000 26.35468  ? 16  VAL B HB   1 
ATOM   3782 H HG11 . VAL B 1 30  ? -4.38255  -37.23342 18.35668 1.000 26.28558  ? 16  VAL B HG11 1 
ATOM   3783 H HG12 . VAL B 1 30  ? -5.38320  -36.65395 17.26745 1.000 26.28558  ? 16  VAL B HG12 1 
ATOM   3784 H HG13 . VAL B 1 30  ? -5.85878  -37.80996 18.24774 1.000 26.28558  ? 16  VAL B HG13 1 
ATOM   3785 H HG21 . VAL B 1 30  ? -2.80546  -37.90226 16.00689 1.000 25.97688  ? 16  VAL B HG21 1 
ATOM   3786 H HG22 . VAL B 1 30  ? -3.81652  -38.35634 14.86888 1.000 25.97688  ? 16  VAL B HG22 1 
ATOM   3787 H HG23 . VAL B 1 30  ? -3.99058  -36.94015 15.56717 1.000 25.97688  ? 16  VAL B HG23 1 
ATOM   3788 N N    . GLU B 1 31  ? -4.80703  -40.00854 19.69102 1.000 25.00715  ? 17  GLU B N    1 
ATOM   3789 C CA   . GLU B 1 31  ? -5.70555  -40.55903 20.69712 1.000 31.43620  ? 17  GLU B CA   1 
ATOM   3790 C C    . GLU B 1 31  ? -6.21697  -39.41431 21.55631 1.000 28.56332  ? 17  GLU B C    1 
ATOM   3791 O O    . GLU B 1 31  ? -5.42675  -38.59022 22.02530 1.000 24.01628  ? 17  GLU B O    1 
ATOM   3792 C CB   . GLU B 1 31  ? -5.00424  -41.60612 21.57309 1.000 26.96370  ? 17  GLU B CB   1 
ATOM   3793 C CG   . GLU B 1 31  ? -4.83234  -42.97425 20.91800 1.000 44.17185  ? 17  GLU B CG   1 
ATOM   3794 C CD   . GLU B 1 31  ? -3.55804  -43.08859 20.10008 1.000 46.26036  ? 17  GLU B CD   1 
ATOM   3795 O OE1  . GLU B 1 31  ? -2.70242  -42.18225 20.19359 1.000 50.43890  ? 17  GLU B OE1  1 
ATOM   3796 O OE2  . GLU B 1 31  ? -3.41170  -44.08878 19.36571 1.000 31.34661  ? 17  GLU B OE2  1 
ATOM   3797 H H    . GLU B 1 31  ? -4.25909  -39.42614 20.00754 1.000 30.06452  ? 17  GLU B H    1 
ATOM   3798 H HA   . GLU B 1 31  ? -6.45760  -40.99166 20.26335 1.000 37.77938  ? 17  GLU B HA   1 
ATOM   3799 N N    . LEU B 1 32  ? -7.53175  -39.36352 21.75951 1.000 32.51949  ? 18  LEU B N    1 
ATOM   3800 C CA   . LEU B 1 32  ? -8.15233  -38.29962 22.53667 1.000 28.77412  ? 18  LEU B CA   1 
ATOM   3801 C C    . LEU B 1 32  ? -9.19622  -38.88451 23.47228 1.000 30.06284  ? 18  LEU B C    1 
ATOM   3802 O O    . LEU B 1 32  ? -10.06644 -39.64394 23.03988 1.000 25.87559  ? 18  LEU B O    1 
ATOM   3803 C CB   . LEU B 1 32  ? -8.79948  -37.25316 21.62037 1.000 28.22268  ? 18  LEU B CB   1 
ATOM   3804 C CG   . LEU B 1 32  ? -9.82385  -36.30392 22.25273 1.000 33.93093  ? 18  LEU B CG   1 
ATOM   3805 C CD1  . LEU B 1 32  ? -9.27959  -35.63398 23.50084 1.000 35.80301  ? 18  LEU B CD1  1 
ATOM   3806 C CD2  . LEU B 1 32  ? -10.26187 -35.25205 21.24124 1.000 37.67695  ? 18  LEU B CD2  1 
ATOM   3807 H H    . LEU B 1 32  ? -8.08981  -39.94160 21.45294 1.000 39.07933  ? 18  LEU B H    1 
ATOM   3808 H HA   . LEU B 1 32  ? -7.47398  -37.86727 23.07871 1.000 34.58489  ? 18  LEU B HA   1 
ATOM   3809 H HB2  . LEU B 1 32  ? -8.09172  -36.70032 21.25385 1.000 33.92315  ? 18  LEU B HB2  1 
ATOM   3810 H HB3  . LEU B 1 32  ? -9.25575  -37.72475 20.90601 1.000 33.92315  ? 18  LEU B HB3  1 
ATOM   3811 H HG   . LEU B 1 32  ? -10.59550 -36.82758 22.51964 1.000 40.77306  ? 18  LEU B HG   1 
ATOM   3812 H HD11 . LEU B 1 32  ? -9.72366  -36.00671 24.27851 1.000 43.01955  ? 18  LEU B HD11 1 
ATOM   3813 H HD12 . LEU B 1 32  ? -8.32485  -35.79634 23.55562 1.000 43.01955  ? 18  LEU B HD12 1 
ATOM   3814 H HD13 . LEU B 1 32  ? -9.45048  -34.68064 23.44760 1.000 43.01955  ? 18  LEU B HD13 1 
ATOM   3815 H HD21 . LEU B 1 32  ? -10.56680 -35.69690 20.43500 1.000 45.26828  ? 18  LEU B HD21 1 
ATOM   3816 H HD22 . LEU B 1 32  ? -10.98338 -34.72801 21.62295 1.000 45.26828  ? 18  LEU B HD22 1 
ATOM   3817 H HD23 . LEU B 1 32  ? -9.50778  -34.67719 21.03682 1.000 45.26828  ? 18  LEU B HD23 1 
ATOM   3818 N N    . ASP B 1 33  ? -9.09987  -38.53106 24.75082 1.000 29.51147  ? 19  ASP B N    1 
ATOM   3819 C CA   A ASP B 1 33  ? -10.09199 -38.89321 25.75775 0.631 30.63138  ? 19  ASP B CA   1 
ATOM   3820 C CA   B ASP B 1 33  ? -10.09071 -38.89365 25.75952 0.369 29.25422  ? 19  ASP B CA   1 
ATOM   3821 C C    . ASP B 1 33  ? -10.71729 -37.60007 26.26353 1.000 29.02674  ? 19  ASP B C    1 
ATOM   3822 O O    . ASP B 1 33  ? -10.04355 -36.79107 26.91147 1.000 28.72534  ? 19  ASP B O    1 
ATOM   3823 C CB   A ASP B 1 33  ? -9.46141  -39.69287 26.89649 0.631 34.90082  ? 19  ASP B CB   1 
ATOM   3824 C CB   B ASP B 1 33  ? -9.44652  -39.68832 26.89533 0.369 34.90522  ? 19  ASP B CB   1 
ATOM   3825 C CG   A ASP B 1 33  ? -9.10993  -41.11324 26.48927 0.631 34.94468  ? 19  ASP B CG   1 
ATOM   3826 C CG   B ASP B 1 33  ? -10.42632 -40.04067 28.00187 0.369 36.26622  ? 19  ASP B CG   1 
ATOM   3827 O OD1  A ASP B 1 33  ? -9.74803  -41.64766 25.55764 0.631 30.58462  ? 19  ASP B OD1  1 
ATOM   3828 O OD1  B ASP B 1 33  ? -11.64059 -39.79373 27.84268 0.369 38.28379  ? 19  ASP B OD1  1 
ATOM   3829 O OD2  A ASP B 1 33  ? -8.19569  -41.69768 27.10705 0.631 42.23106  ? 19  ASP B OD2  1 
ATOM   3830 O OD2  B ASP B 1 33  ? -9.97344  -40.56839 29.03925 0.369 39.53649  ? 19  ASP B OD2  1 
ATOM   3831 H H    . ASP B 1 33  ? -8.44740  -38.06711 25.06488 1.000 35.46971  ? 19  ASP B H    1 
ATOM   3832 H HA   . ASP B 1 33  ? -10.78416 -39.44432 25.36016 1.000 35.16100  ? 19  ASP B HA   1 
ATOM   3833 H HB2  A ASP B 1 33  ? -8.64564  -39.25099 27.17965 0.631 41.93693  ? 19  ASP B HB2  1 
ATOM   3834 H HB2  B ASP B 1 33  ? -9.08884  -40.51604 26.53777 0.369 41.94221  ? 19  ASP B HB2  1 
ATOM   3835 H HB3  A ASP B 1 33  ? -10.08772 -39.73862 27.63578 0.631 41.93693  ? 19  ASP B HB3  1 
ATOM   3836 H HB3  B ASP B 1 33  ? -8.73282  -39.15945 27.28498 0.369 41.94221  ? 19  ASP B HB3  1 
ATOM   3837 N N    . GLY B 1 34  ? -11.99589 -37.39936 25.95379 1.000 27.97146  ? 20  GLY B N    1 
ATOM   3838 C CA   . GLY B 1 34  ? -12.66993 -36.16234 26.29461 1.000 27.18035  ? 20  GLY B CA   1 
ATOM   3839 C C    . GLY B 1 34  ? -13.73972 -36.29286 27.35799 1.000 30.98206  ? 20  GLY B C    1 
ATOM   3840 O O    . GLY B 1 34  ? -14.22720 -37.39149 27.64232 1.000 29.54775  ? 20  GLY B O    1 
ATOM   3841 H H    . GLY B 1 34  ? -12.49268 -37.96970 25.54452 1.000 33.62169  ? 20  GLY B H    1 
ATOM   3842 H HA2  . GLY B 1 34  ? -12.01087 -35.52692 26.61521 1.000 32.67236  ? 20  GLY B HA2  1 
ATOM   3843 H HA3  . GLY B 1 34  ? -13.08948 -35.80623 25.49582 1.000 32.67236  ? 20  GLY B HA3  1 
ATOM   3844 N N    . ASP B 1 35  ? -14.11546 -35.15486 27.94650 1.000 31.03317  ? 21  ASP B N    1 
ATOM   3845 C CA   . ASP B 1 35  ? -15.14368 -35.12257 28.98458 1.000 32.79258  ? 21  ASP B CA   1 
ATOM   3846 C C    . ASP B 1 35  ? -15.68586 -33.69254 29.02851 1.000 33.16884  ? 21  ASP B C    1 
ATOM   3847 O O    . ASP B 1 35  ? -15.02922 -32.79997 29.57041 1.000 30.01750  ? 21  ASP B O    1 
ATOM   3848 C CB   . ASP B 1 35  ? -14.57404 -35.55353 30.32688 1.000 32.72900  ? 21  ASP B CB   1 
ATOM   3849 C CG   . ASP B 1 35  ? -15.57964 -35.44012 31.45564 1.000 30.75718  ? 21  ASP B CG   1 
ATOM   3850 O OD1  . ASP B 1 35  ? -16.77698 -35.22456 31.17553 1.000 35.87176  ? 21  ASP B OD1  1 
ATOM   3851 O OD2  . ASP B 1 35  ? -15.16774 -35.56567 32.62794 1.000 31.49940  ? 21  ASP B OD2  1 
ATOM   3852 H H    . ASP B 1 35  ? -13.78667 -34.38240 27.75995 1.000 37.29575  ? 21  ASP B H    1 
ATOM   3853 H HA   . ASP B 1 35  ? -15.86914 -35.72363 28.75364 1.000 39.40703  ? 21  ASP B HA   1 
ATOM   3854 H HB2  . ASP B 1 35  ? -14.29283 -36.48000 30.26795 1.000 39.33074  ? 21  ASP B HB2  1 
ATOM   3855 H HB3  . ASP B 1 35  ? -13.81517 -34.98964 30.54374 1.000 39.33074  ? 21  ASP B HB3  1 
ATOM   3856 N N    . VAL B 1 36  ? -16.87033 -33.48958 28.45449 1.000 33.08426  ? 22  VAL B N    1 
ATOM   3857 C CA   . VAL B 1 36  ? -17.49327 -32.17165 28.35805 1.000 36.53537  ? 22  VAL B CA   1 
ATOM   3858 C C    . VAL B 1 36  ? -18.80430 -32.21855 29.13096 1.000 31.89450  ? 22  VAL B C    1 
ATOM   3859 O O    . VAL B 1 36  ? -19.74973 -32.90573 28.72302 1.000 30.92074  ? 22  VAL B O    1 
ATOM   3860 C CB   . VAL B 1 36  ? -17.73138 -31.75019 26.90055 1.000 39.07251  ? 22  VAL B CB   1 
ATOM   3861 C CG1  . VAL B 1 36  ? -18.33632 -30.35028 26.83973 1.000 37.66216  ? 22  VAL B CG1  1 
ATOM   3862 C CG2  . VAL B 1 36  ? -16.43429 -31.80765 26.10782 1.000 30.25615  ? 22  VAL B CG2  1 
ATOM   3863 H H    . VAL B 1 36  ? -17.34378 -34.11667 28.10491 1.000 39.75705  ? 22  VAL B H    1 
ATOM   3864 H HA   . VAL B 1 36  ? -16.91437 -31.51731 28.77948 1.000 43.89838  ? 22  VAL B HA   1 
ATOM   3865 H HB   . VAL B 1 36  ? -18.35946 -32.36879 26.49589 1.000 46.94295  ? 22  VAL B HB   1 
ATOM   3866 H HG11 . VAL B 1 36  ? -18.24488 -29.92873 27.70854 1.000 45.25053  ? 22  VAL B HG11 1 
ATOM   3867 H HG12 . VAL B 1 36  ? -17.86511 -29.83149 26.16912 1.000 45.25053  ? 22  VAL B HG12 1 
ATOM   3868 H HG13 . VAL B 1 36  ? -19.27447 -30.42163 26.60378 1.000 45.25053  ? 22  VAL B HG13 1 
ATOM   3869 H HG21 . VAL B 1 36  ? -16.04493 -32.69097 26.20292 1.000 36.36332  ? 22  VAL B HG21 1 
ATOM   3870 H HG22 . VAL B 1 36  ? -16.62682 -31.62983 25.17390 1.000 36.36332  ? 22  VAL B HG22 1 
ATOM   3871 H HG23 . VAL B 1 36  ? -15.82332 -31.13795 26.45294 1.000 36.36332  ? 22  VAL B HG23 1 
ATOM   3872 N N    . ASN B 1 37  ? -18.86964 -31.47584 30.23624 1.000 32.18872  ? 23  ASN B N    1 
ATOM   3873 C CA   . ASN B 1 37  ? -20.05070 -31.46065 31.09943 1.000 35.29865  ? 23  ASN B CA   1 
ATOM   3874 C C    . ASN B 1 37  ? -20.42617 -32.87476 31.53552 1.000 35.87140  ? 23  ASN B C    1 
ATOM   3875 O O    . ASN B 1 37  ? -21.60282 -33.21983 31.66357 1.000 41.88381  ? 23  ASN B O    1 
ATOM   3876 C CB   . ASN B 1 37  ? -21.23084 -30.77593 30.40676 1.000 36.36811  ? 23  ASN B CB   1 
ATOM   3877 C CG   . ASN B 1 37  ? -21.09718 -29.26619 30.37918 1.000 38.17847  ? 23  ASN B CG   1 
ATOM   3878 O OD1  . ASN B 1 37  ? -19.99180 -28.72637 30.42013 1.000 37.99541  ? 23  ASN B OD1  1 
ATOM   3879 N ND2  . ASN B 1 37  ? -22.22971 -28.57494 30.31606 1.000 38.49973  ? 23  ASN B ND2  1 
ATOM   3880 H H    . ASN B 1 37  ? -18.23443 -30.96544 30.51121 1.000 38.68240  ? 23  ASN B H    1 
ATOM   3881 H HA   . ASN B 1 37  ? -19.83722 -30.95182 31.89719 1.000 42.41432  ? 23  ASN B HA   1 
ATOM   3882 H HB2  . ASN B 1 37  ? -21.28493 -31.08929 29.49037 1.000 43.69768  ? 23  ASN B HB2  1 
ATOM   3883 H HB3  . ASN B 1 37  ? -22.04751 -30.99636 30.88150 1.000 43.69768  ? 23  ASN B HB3  1 
ATOM   3884 H HD21 . ASN B 1 37  ? -22.20841 -27.71539 30.29803 1.000 46.25561  ? 23  ASN B HD21 1 
ATOM   3885 H HD22 . ASN B 1 37  ? -22.98424 -28.98695 30.29321 1.000 46.25561  ? 23  ASN B HD22 1 
ATOM   3886 N N    . GLY B 1 38  ? -19.40966 -33.70406 31.76767 1.000 35.60691  ? 24  GLY B N    1 
ATOM   3887 C CA   . GLY B 1 38  ? -19.61213 -35.07009 32.19396 1.000 39.09439  ? 24  GLY B CA   1 
ATOM   3888 C C    . GLY B 1 38  ? -19.81275 -36.06934 31.07529 1.000 36.20494  ? 24  GLY B C    1 
ATOM   3889 O O    . GLY B 1 38  ? -19.80642 -37.27801 31.34028 1.000 31.34660  ? 24  GLY B O    1 
ATOM   3890 H H    . GLY B 1 38  ? -18.58193 -33.48720 31.68140 1.000 42.78423  ? 24  GLY B H    1 
ATOM   3891 H HA2  . GLY B 1 38  ? -18.83820 -35.35246 32.70601 1.000 46.96921  ? 24  GLY B HA2  1 
ATOM   3892 H HA3  . GLY B 1 38  ? -20.39680 -35.10359 32.76323 1.000 46.96921  ? 24  GLY B HA3  1 
ATOM   3893 N N    . HIS B 1 39  ? -19.99379 -35.61039 29.83868 1.000 40.11074  ? 25  HIS B N    1 
ATOM   3894 C CA   . HIS B 1 39  ? -20.16270 -36.50433 28.69736 1.000 32.16837  ? 25  HIS B CA   1 
ATOM   3895 C C    . HIS B 1 39  ? -18.78765 -36.95238 28.22046 1.000 33.13188  ? 25  HIS B C    1 
ATOM   3896 O O    . HIS B 1 39  ? -18.03008 -36.16003 27.65073 1.000 30.80313  ? 25  HIS B O    1 
ATOM   3897 C CB   . HIS B 1 39  ? -20.93044 -35.80680 27.57938 1.000 40.70602  ? 25  HIS B CB   1 
ATOM   3898 C CG   . HIS B 1 39  ? -22.32661 -35.42191 27.95621 1.000 46.39511  ? 25  HIS B CG   1 
ATOM   3899 N ND1  . HIS B 1 39  ? -22.65233 -34.16797 28.42706 1.000 50.19085  ? 25  HIS B ND1  1 
ATOM   3900 C CD2  . HIS B 1 39  ? -23.48152 -36.12838 27.93690 1.000 46.56677  ? 25  HIS B CD2  1 
ATOM   3901 C CE1  . HIS B 1 39  ? -23.94845 -34.11757 28.67821 1.000 53.93032  ? 25  HIS B CE1  1 
ATOM   3902 N NE2  . HIS B 1 39  ? -24.47485 -35.29415 28.38926 1.000 53.34258  ? 25  HIS B NE2  1 
ATOM   3903 H H    . HIS B 1 39  ? -20.02282 -34.77580 29.63324 1.000 48.18883  ? 25  HIS B H    1 
ATOM   3904 H HA   . HIS B 1 39  ? -20.66869 -37.28548 28.97065 1.000 38.65799  ? 25  HIS B HA   1 
ATOM   3905 H HB2  . HIS B 1 39  ? -20.45626 -34.99714 27.33342 1.000 48.90316  ? 25  HIS B HB2  1 
ATOM   3906 H HB3  . HIS B 1 39  ? -20.98356 -36.40464 26.81737 1.000 48.90316  ? 25  HIS B HB3  1 
ATOM   3907 H HD1  . HIS B 1 39  ? -22.09845 -33.51980 28.53972 1.000 60.28496  ? 25  HIS B HD1  1 
ATOM   3908 H HD2  . HIS B 1 39  ? -23.58328 -37.01276 27.66780 1.000 55.93606  ? 25  HIS B HD2  1 
ATOM   3909 H HE1  . HIS B 1 39  ? -24.41142 -33.37935 29.00314 1.000 64.77233  ? 25  HIS B HE1  1 
ATOM   3910 N N    . LYS B 1 40  ? -18.46722 -38.22158 28.44529 1.000 29.64590  ? 26  LYS B N    1 
ATOM   3911 C CA   . LYS B 1 40  ? -17.15279 -38.75511 28.12589 1.000 33.44423  ? 26  LYS B CA   1 
ATOM   3912 C C    . LYS B 1 40  ? -17.16296 -39.39334 26.74423 1.000 31.63929  ? 26  LYS B C    1 
ATOM   3913 O O    . LYS B 1 40  ? -18.14935 -40.01535 26.33967 1.000 28.77911  ? 26  LYS B O    1 
ATOM   3914 C CB   . LYS B 1 40  ? -16.72720 -39.77462 29.18231 1.000 38.67328  ? 26  LYS B CB   1 
ATOM   3915 C CG   . LYS B 1 40  ? -17.00197 -39.30104 30.60102 1.000 40.39482  ? 26  LYS B CG   1 
ATOM   3916 C CD   . LYS B 1 40  ? -16.14939 -40.02293 31.62501 1.000 50.80982  ? 26  LYS B CD   1 
ATOM   3917 C CE   . LYS B 1 40  ? -16.31691 -39.39886 33.00249 1.000 52.14082  ? 26  LYS B CE   1 
ATOM   3918 N NZ   . LYS B 1 40  ? -15.21087 -39.77020 33.92697 1.000 61.87466  ? 26  LYS B NZ   1 
ATOM   3919 H H    . LYS B 1 40  ? -19.00309 -38.80083 28.78722 1.000 35.63102  ? 26  LYS B H    1 
ATOM   3920 H HA   . LYS B 1 40  ? -16.50000 -38.03771 28.11604 1.000 40.18902  ? 26  LYS B HA   1 
ATOM   3921 H HB2  . LYS B 1 40  ? -17.21762 -40.59943 29.04065 1.000 46.46388  ? 26  LYS B HB2  1 
ATOM   3922 H HB3  . LYS B 1 40  ? -15.77447 -39.93662 29.09890 1.000 46.46388  ? 26  LYS B HB3  1 
ATOM   3923 H HG2  . LYS B 1 40  ? -16.80846 -38.35255 30.66277 1.000 48.52973  ? 26  LYS B HG2  1 
ATOM   3924 H HG3  . LYS B 1 40  ? -17.93368 -39.46423 30.81593 1.000 48.52973  ? 26  LYS B HG3  1 
ATOM   3925 H HD2  . LYS B 1 40  ? -16.41934 -40.95335 31.67354 1.000 61.02772  ? 26  LYS B HD2  1 
ATOM   3926 H HD3  . LYS B 1 40  ? -15.21541 -39.96131 31.37051 1.000 61.02772  ? 26  LYS B HD3  1 
ATOM   3927 H HE2  . LYS B 1 40  ? -16.32620 -38.43282 32.91537 1.000 62.62492  ? 26  LYS B HE2  1 
ATOM   3928 H HE3  . LYS B 1 40  ? -17.15117 -39.70493 33.39138 1.000 62.62492  ? 26  LYS B HE3  1 
ATOM   3929 H HZ1  . LYS B 1 40  ? -15.31207 -39.35213 34.70612 1.000 74.30554  ? 26  LYS B HZ1  1 
ATOM   3930 H HZ2  . LYS B 1 40  ? -15.21420 -40.64893 34.06812 1.000 74.30554  ? 26  LYS B HZ2  1 
ATOM   3931 H HZ3  . LYS B 1 40  ? -14.42782 -39.53736 33.57381 1.000 74.30554  ? 26  LYS B HZ3  1 
ATOM   3932 N N    . PHE B 1 41  ? -16.05775 -39.22472 26.02104 1.000 31.02883  ? 27  PHE B N    1 
ATOM   3933 C CA   . PHE B 1 41  ? -15.93341 -39.75392 24.67089 1.000 30.62376  ? 27  PHE B CA   1 
ATOM   3934 C C    . PHE B 1 41  ? -14.46031 -39.95927 24.34990 1.000 30.65000  ? 27  PHE B C    1 
ATOM   3935 O O    . PHE B 1 41  ? -13.57881 -39.37711 24.98739 1.000 26.56999  ? 27  PHE B O    1 
ATOM   3936 C CB   . PHE B 1 41  ? -16.57750 -38.81928 23.64223 1.000 31.50521  ? 27  PHE B CB   1 
ATOM   3937 C CG   . PHE B 1 41  ? -15.99790 -37.43401 23.63622 1.000 35.28260  ? 27  PHE B CG   1 
ATOM   3938 C CD1  . PHE B 1 41  ? -16.47501 -36.46575 24.50370 1.000 30.69730  ? 27  PHE B CD1  1 
ATOM   3939 C CD2  . PHE B 1 41  ? -14.97768 -37.09851 22.76239 1.000 35.72826  ? 27  PHE B CD2  1 
ATOM   3940 C CE1  . PHE B 1 41  ? -15.94494 -35.19035 24.50099 1.000 30.76518  ? 27  PHE B CE1  1 
ATOM   3941 C CE2  . PHE B 1 41  ? -14.44362 -35.82234 22.75504 1.000 34.27302  ? 27  PHE B CE2  1 
ATOM   3942 C CZ   . PHE B 1 41  ? -14.92846 -34.86802 23.62476 1.000 33.17857  ? 27  PHE B CZ   1 
ATOM   3943 H H    . PHE B 1 41  ? -15.36021 -38.80277 26.29490 1.000 37.29054  ? 27  PHE B H    1 
ATOM   3944 H HA   . PHE B 1 41  ? -16.37596 -40.61598 24.62716 1.000 36.80445  ? 27  PHE B HA   1 
ATOM   3945 H HB2  . PHE B 1 41  ? -16.45256 -39.19620 22.75723 1.000 37.86219  ? 27  PHE B HB2  1 
ATOM   3946 H HB3  . PHE B 1 41  ? -17.52411 -38.74316 23.83981 1.000 37.86219  ? 27  PHE B HB3  1 
ATOM   3947 H HD1  . PHE B 1 41  ? -17.16076 -36.67687 25.09537 1.000 36.89270  ? 27  PHE B HD1  1 
ATOM   3948 H HD2  . PHE B 1 41  ? -14.64765 -37.73835 22.17367 1.000 42.92985  ? 27  PHE B HD2  1 
ATOM   3949 H HE1  . PHE B 1 41  ? -16.27280 -34.54905 25.08933 1.000 36.97415  ? 27  PHE B HE1  1 
ATOM   3950 H HE2  . PHE B 1 41  ? -13.75820 -35.60811 22.16410 1.000 41.18357  ? 27  PHE B HE2  1 
ATOM   3951 H HZ   . PHE B 1 41  ? -14.57131 -34.00935 23.62080 1.000 39.87022  ? 27  PHE B HZ   1 
ATOM   3952 N N    . SER B 1 42  ? -14.20733 -40.79509 23.34267 1.000 29.39040  ? 28  SER B N    1 
ATOM   3953 C CA   . SER B 1 42  ? -12.85315 -41.10642 22.90714 1.000 27.97401  ? 28  SER B CA   1 
ATOM   3954 C C    . SER B 1 42  ? -12.78232 -41.07454 21.38844 1.000 29.03526  ? 28  SER B C    1 
ATOM   3955 O O    . SER B 1 42  ? -13.70002 -41.53810 20.70580 1.000 28.71278  ? 28  SER B O    1 
ATOM   3956 C CB   . SER B 1 42  ? -12.40298 -42.48099 23.41550 1.000 29.82327  ? 28  SER B CB   1 
ATOM   3957 O OG   . SER B 1 42  ? -12.39987 -42.52576 24.83223 1.000 38.50762  ? 28  SER B OG   1 
ATOM   3958 H H    . SER B 1 42  ? -14.81642 -41.19975 22.89007 1.000 35.32442  ? 28  SER B H    1 
ATOM   3959 H HA   . SER B 1 42  ? -12.24481 -40.43465 23.25289 1.000 33.62476  ? 28  SER B HA   1 
ATOM   3960 H HB2  . SER B 1 42  ? -13.01403 -43.15586 23.08073 1.000 35.84387  ? 28  SER B HB2  1 
ATOM   3961 H HB3  . SER B 1 42  ? -11.50521 -42.65712 23.09317 1.000 35.84387  ? 28  SER B HB3  1 
ATOM   3962 H HG   . SER B 1 42  ? -11.84527 -41.97277 25.13593 1.000 46.26509  ? 28  SER B HG   1 
ATOM   3963 N N    . VAL B 1 43  ? -11.68134 -40.53471 20.86868 1.000 27.79222  ? 29  VAL B N    1 
ATOM   3964 C CA   . VAL B 1 43  ? -11.44818 -40.41743 19.43436 1.000 29.54282  ? 29  VAL B CA   1 
ATOM   3965 C C    . VAL B 1 43  ? -10.10277 -41.05527 19.11824 1.000 24.53852  ? 29  VAL B C    1 
ATOM   3966 O O    . VAL B 1 43  ? -9.11605  -40.81492 19.82267 1.000 25.58824  ? 29  VAL B O    1 
ATOM   3967 C CB   . VAL B 1 43  ? -11.47567 -38.94688 18.96787 1.000 27.54922  ? 29  VAL B CB   1 
ATOM   3968 C CG1  . VAL B 1 43  ? -11.21014 -38.83758 17.46847 1.000 27.53757  ? 29  VAL B CG1  1 
ATOM   3969 C CG2  . VAL B 1 43  ? -12.80928 -38.30805 19.31335 1.000 26.30426  ? 29  VAL B CG2  1 
ATOM   3970 H H    . VAL B 1 43  ? -11.03667 -40.22036 21.34321 1.000 33.40660  ? 29  VAL B H    1 
ATOM   3971 H HA   . VAL B 1 43  ? -12.13796 -40.90147 18.95394 1.000 35.50732  ? 29  VAL B HA   1 
ATOM   3972 H HB   . VAL B 1 43  ? -10.77081 -38.46703 19.43027 1.000 33.11500  ? 29  VAL B HB   1 
ATOM   3973 H HG11 . VAL B 1 43  ? -10.44569 -38.25810 17.32455 1.000 33.10102  ? 29  VAL B HG11 1 
ATOM   3974 H HG12 . VAL B 1 43  ? -11.02601 -39.72194 17.11507 1.000 33.10102  ? 29  VAL B HG12 1 
ATOM   3975 H HG13 . VAL B 1 43  ? -11.99394 -38.46486 17.03530 1.000 33.10102  ? 29  VAL B HG13 1 
ATOM   3976 H HG21 . VAL B 1 43  ? -12.86095 -37.43657 18.89055 1.000 31.62105  ? 29  VAL B HG21 1 
ATOM   3977 H HG22 . VAL B 1 43  ? -13.52521 -38.87625 18.98854 1.000 31.62105  ? 29  VAL B HG22 1 
ATOM   3978 H HG23 . VAL B 1 43  ? -12.87372 -38.21276 20.27651 1.000 31.62105  ? 29  VAL B HG23 1 
ATOM   3979 N N    . SER B 1 44  ? -10.07146 -41.87634 18.07189 1.000 26.43634  ? 30  SER B N    1 
ATOM   3980 C CA   . SER B 1 44  ? -8.84443  -42.45134 17.53692 1.000 27.89905  ? 30  SER B CA   1 
ATOM   3981 C C    . SER B 1 44  ? -8.62458  -41.90092 16.13482 1.000 28.64942  ? 30  SER B C    1 
ATOM   3982 O O    . SER B 1 44  ? -9.55318  -41.88729 15.31969 1.000 26.69105  ? 30  SER B O    1 
ATOM   3983 C CB   . SER B 1 44  ? -8.91515  -43.98092 17.49385 1.000 27.51917  ? 30  SER B CB   1 
ATOM   3984 O OG   . SER B 1 44  ? -9.03349  -44.53908 18.79233 1.000 29.06367  ? 30  SER B OG   1 
ATOM   3985 H H    . SER B 1 44  ? -10.77406 -42.12249 17.64135 1.000 31.77954  ? 30  SER B H    1 
ATOM   3986 H HA   . SER B 1 44  ? -8.09451  -42.20403 18.10027 1.000 33.53481  ? 30  SER B HA   1 
ATOM   3987 H HB2  . SER B 1 44  ? -9.68836  -44.24287 16.97000 1.000 33.07894  ? 30  SER B HB2  1 
ATOM   3988 H HB3  . SER B 1 44  ? -8.10496  -44.31922 17.08149 1.000 33.07894  ? 30  SER B HB3  1 
ATOM   3989 H HG   . SER B 1 44  ? -8.32426  -44.41376 19.22464 1.000 34.93234  ? 30  SER B HG   1 
ATOM   3990 N N    . GLY B 1 45  ? -7.40499  -41.45825 15.85602 1.000 25.31136  ? 31  GLY B N    1 
ATOM   3991 C CA   . GLY B 1 45  ? -7.08025  -40.89359 14.56218 1.000 24.41099  ? 31  GLY B CA   1 
ATOM   3992 C C    . GLY B 1 45  ? -5.78045  -41.45091 14.02243 1.000 25.37566  ? 31  GLY B C    1 
ATOM   3993 O O    . GLY B 1 45  ? -4.90619  -41.88679 14.77003 1.000 28.30823  ? 31  GLY B O    1 
ATOM   3994 H H    . GLY B 1 45  ? -6.74469  -41.47562 16.40674 1.000 30.42957  ? 31  GLY B H    1 
ATOM   3995 H HA2  . GLY B 1 45  ? -7.78898  -41.09726 13.93201 1.000 29.34913  ? 31  GLY B HA2  1 
ATOM   3996 H HA3  . GLY B 1 45  ? -6.99449  -39.93057 14.64059 1.000 29.34913  ? 31  GLY B HA3  1 
ATOM   3997 N N    . GLU B 1 46  ? -5.66673  -41.42908 12.69635 1.000 27.36922  ? 32  GLU B N    1 
ATOM   3998 C CA   . GLU B 1 46  ? -4.46847  -41.89524 12.01559 1.000 34.38129  ? 32  GLU B CA   1 
ATOM   3999 C C    . GLU B 1 46  ? -4.33332  -41.15380 10.69504 1.000 28.70629  ? 32  GLU B C    1 
ATOM   4000 O O    . GLU B 1 46  ? -5.28009  -40.52828 10.21134 1.000 27.25500  ? 32  GLU B O    1 
ATOM   4001 C CB   . GLU B 1 46  ? -4.50532  -43.40684 11.76870 1.000 32.01005  ? 32  GLU B CB   1 
ATOM   4002 C CG   . GLU B 1 46  ? -5.70391  -43.86408 10.96141 1.000 35.68766  ? 32  GLU B CG   1 
ATOM   4003 C CD   . GLU B 1 46  ? -5.71739  -45.36138 10.73550 1.000 39.36022  ? 32  GLU B CD   1 
ATOM   4004 O OE1  . GLU B 1 46  ? -4.85123  -45.86348 9.98714  1.000 35.27097  ? 32  GLU B OE1  1 
ATOM   4005 O OE2  . GLU B 1 46  ? -6.59392  -46.03679 11.31450 1.000 36.52566  ? 32  GLU B OE2  1 
ATOM   4006 H H    . GLU B 1 46  ? -6.27935  -41.14465 12.16400 1.000 32.89900  ? 32  GLU B H    1 
ATOM   4007 H HA   . GLU B 1 46  ? -3.69420  -41.69538 12.56464 1.000 41.31349  ? 32  GLU B HA   1 
ATOM   4008 H HB2  . GLU B 1 46  ? -3.70577  -43.66310 11.28295 1.000 38.46799  ? 32  GLU B HB2  1 
ATOM   4009 H HB3  . GLU B 1 46  ? -4.53362  -43.86208 12.62477 1.000 38.46799  ? 32  GLU B HB3  1 
ATOM   4010 H HG2  . GLU B 1 46  ? -6.51527  -43.62448 11.43594 1.000 42.88113  ? 32  GLU B HG2  1 
ATOM   4011 H HG3  . GLU B 1 46  ? -5.68606  -43.42953 10.09437 1.000 42.88113  ? 32  GLU B HG3  1 
ATOM   4012 N N    . GLY B 1 47  ? -3.14479  -41.23723 10.11557 1.000 34.00099  ? 33  GLY B N    1 
ATOM   4013 C CA   . GLY B 1 47  ? -2.88691  -40.60752 8.83025  1.000 33.81474  ? 33  GLY B CA   1 
ATOM   4014 C C    . GLY B 1 47  ? -1.39554  -40.40161 8.62789  1.000 32.69752  ? 33  GLY B C    1 
ATOM   4015 O O    . GLY B 1 47  ? -0.57577  -41.14314 9.17075  1.000 30.05411  ? 33  GLY B O    1 
ATOM   4016 H H    . GLY B 1 47  ? -2.46913  -41.65368 10.44670 1.000 40.85713  ? 33  GLY B H    1 
ATOM   4017 H HA2  . GLY B 1 47  ? -3.22529  -41.16891 8.11524  1.000 40.63362  ? 33  GLY B HA2  1 
ATOM   4018 H HA3  . GLY B 1 47  ? -3.33003  -39.74552 8.79158  1.000 40.63362  ? 33  GLY B HA3  1 
ATOM   4019 N N    . GLU B 1 48  ? -1.07427  -39.37342 7.84296  1.000 33.09661  ? 34  GLU B N    1 
ATOM   4020 C CA   . GLU B 1 48  ? 0.30103   -39.07107 7.48006  1.000 34.66125  ? 34  GLU B CA   1 
ATOM   4021 C C    . GLU B 1 48  ? 0.54127   -37.56934 7.54356  1.000 36.13937  ? 34  GLU B C    1 
ATOM   4022 O O    . GLU B 1 48  ? -0.38543  -36.76190 7.43297  1.000 29.17257  ? 34  GLU B O    1 
ATOM   4023 C CB   . GLU B 1 48  ? 0.63722   -39.57101 6.07027  1.000 39.32438  ? 34  GLU B CB   1 
ATOM   4024 C CG   . GLU B 1 48  ? 0.43694   -41.05749 5.85998  1.000 51.07760  ? 34  GLU B CG   1 
ATOM   4025 C CD   . GLU B 1 48  ? -0.94986  -41.40888 5.34529  1.000 49.16152  ? 34  GLU B CD   1 
ATOM   4026 O OE1  . GLU B 1 48  ? -1.93537  -40.76916 5.76801  1.000 46.47900  ? 34  GLU B OE1  1 
ATOM   4027 O OE2  . GLU B 1 48  ? -1.05082  -42.32908 4.50641  1.000 57.57792  ? 34  GLU B OE2  1 
ATOM   4028 H H    . GLU B 1 48  ? -1.64795  -38.82949 7.50440  1.000 39.77188  ? 34  GLU B H    1 
ATOM   4029 H HA   . GLU B 1 48  ? 0.88696   -39.50224 8.12167  1.000 41.64944  ? 34  GLU B HA   1 
ATOM   4030 H HB2  . GLU B 1 48  ? 0.06904   -39.10725 5.43545  1.000 47.24520  ? 34  GLU B HB2  1 
ATOM   4031 H HB3  . GLU B 1 48  ? 1.56912   -39.37333 5.88754  1.000 47.24520  ? 34  GLU B HB3  1 
ATOM   4032 H HG2  . GLU B 1 48  ? 1.08458   -41.37308 5.21047  1.000 61.34907  ? 34  GLU B HG2  1 
ATOM   4033 H HG3  . GLU B 1 48  ? 0.56549   -41.51468 6.70576  1.000 61.34907  ? 34  GLU B HG3  1 
ATOM   4034 N N    . GLY B 1 49  ? 1.80411   -37.20917 7.70256  1.000 31.13645  ? 35  GLY B N    1 
ATOM   4035 C CA   . GLY B 1 49  ? 2.20867   -35.81231 7.69064  1.000 28.97692  ? 35  GLY B CA   1 
ATOM   4036 C C    . GLY B 1 49  ? 3.42028   -35.61454 6.80791  1.000 35.86705  ? 35  GLY B C    1 
ATOM   4037 O O    . GLY B 1 49  ? 4.33514   -36.43767 6.79619  1.000 34.49913  ? 35  GLY B O    1 
ATOM   4038 H H    . GLY B 1 49  ? 2.45388   -37.76008 7.82048  1.000 37.41969  ? 35  GLY B H    1 
ATOM   4039 H HA2  . GLY B 1 49  ? 1.48330   -35.26369 7.35337  1.000 34.82824  ? 35  GLY B HA2  1 
ATOM   4040 H HA3  . GLY B 1 49  ? 2.42815   -35.52678 8.59131  1.000 34.82824  ? 35  GLY B HA3  1 
ATOM   4041 N N    . ASP B 1 50  ? 3.41328   -34.51181 6.05824  1.000 30.74930  ? 36  ASP B N    1 
ATOM   4042 C CA   . ASP B 1 50  ? 4.48630   -34.17495 5.12007  1.000 39.30327  ? 36  ASP B CA   1 
ATOM   4043 C C    . ASP B 1 50  ? 4.89506   -32.73047 5.39665  1.000 37.57844  ? 36  ASP B C    1 
ATOM   4044 O O    . ASP B 1 50  ? 4.36955   -31.79722 4.78412  1.000 35.04047  ? 36  ASP B O    1 
ATOM   4045 C CB   . ASP B 1 50  ? 4.03088   -34.37599 3.67616  1.000 37.66207  ? 36  ASP B CB   1 
ATOM   4046 C CG   . ASP B 1 50  ? 5.18061   -34.33722 2.68728  1.000 43.85470  ? 36  ASP B CG   1 
ATOM   4047 O OD1  . ASP B 1 50  ? 6.34306   -34.19346 3.11961  1.000 45.05784  ? 36  ASP B OD1  1 
ATOM   4048 O OD2  . ASP B 1 50  ? 4.91931   -34.45299 1.47233  1.000 51.71696  ? 36  ASP B OD2  1 
ATOM   4049 H H    . ASP B 1 50  ? 2.78149   -33.92860 6.07603  1.000 36.95510  ? 36  ASP B H    1 
ATOM   4050 H HA   . ASP B 1 50  ? 5.25253   -34.74788 5.27995  1.000 47.21986  ? 36  ASP B HA   1 
ATOM   4051 H HB2  . ASP B 1 50  ? 3.59776   -35.24047 3.59880  1.000 45.25042  ? 36  ASP B HB2  1 
ATOM   4052 H HB3  . ASP B 1 50  ? 3.40826   -33.67066 3.44001  1.000 45.25042  ? 36  ASP B HB3  1 
ATOM   4053 N N    . ALA B 1 51  ? 5.83504   -32.54935 6.32737  1.000 35.45691  ? 37  ALA B N    1 
ATOM   4054 C CA   . ALA B 1 51  ? 6.25074   -31.20610 6.70931  1.000 37.55763  ? 37  ALA B CA   1 
ATOM   4055 C C    . ALA B 1 51  ? 6.95808   -30.47771 5.57636  1.000 35.32810  ? 37  ALA B C    1 
ATOM   4056 O O    . ALA B 1 51  ? 7.02312   -29.24413 5.59671  1.000 36.10877  ? 37  ALA B O    1 
ATOM   4057 C CB   . ALA B 1 51  ? 7.15941   -31.26450 7.93725  1.000 34.91992  ? 37  ALA B CB   1 
ATOM   4058 H H    . ALA B 1 51  ? 6.24068   -33.18184 6.74571  1.000 42.60423  ? 37  ALA B H    1 
ATOM   4059 H HA   . ALA B 1 51  ? 5.46195   -30.69399 6.94688  1.000 45.12510  ? 37  ALA B HA   1 
ATOM   4060 H HB1  . ALA B 1 51  ? 7.97565   -31.73385 7.70407  1.000 41.95984  ? 37  ALA B HB1  1 
ATOM   4061 H HB2  . ALA B 1 51  ? 7.36707   -30.36008 8.21975  1.000 41.95984  ? 37  ALA B HB2  1 
ATOM   4062 H HB3  . ALA B 1 51  ? 6.69865   -31.73577 8.64895  1.000 41.95984  ? 37  ALA B HB3  1 
ATOM   4063 N N    . THR B 1 52  ? 7.49243   -31.20711 4.59468  1.000 34.19399  ? 38  THR B N    1 
ATOM   4064 C CA   . THR B 1 52  ? 8.06758   -30.55026 3.42592  1.000 35.61734  ? 38  THR B CA   1 
ATOM   4065 C C    . THR B 1 52  ? 7.03426   -29.66531 2.74101  1.000 39.80900  ? 38  THR B C    1 
ATOM   4066 O O    . THR B 1 52  ? 7.33645   -28.53306 2.34562  1.000 36.45417  ? 38  THR B O    1 
ATOM   4067 C CB   . THR B 1 52  ? 8.61464   -31.59402 2.45242  1.000 37.83582  ? 38  THR B CB   1 
ATOM   4068 O OG1  . THR B 1 52  ? 9.71014   -32.28913 3.06207  1.000 39.48901  ? 38  THR B OG1  1 
ATOM   4069 C CG2  . THR B 1 52  ? 9.08448   -30.93648 1.16082  1.000 41.79381  ? 38  THR B CG2  1 
ATOM   4070 H H    . THR B 1 52  ? 7.53294   -32.06607 4.58276  1.000 41.08872  ? 38  THR B H    1 
ATOM   4071 H HA   . THR B 1 52  ? 8.80852   -29.99135 3.70791  1.000 42.79675  ? 38  THR B HA   1 
ATOM   4072 H HB   . THR B 1 52  ? 7.91332   -32.22610 2.22990  1.000 45.45892  ? 38  THR B HB   1 
ATOM   4073 H HG1  . THR B 1 52  ? 10.25483  -31.73830 3.38688  1.000 47.44275  ? 38  THR B HG1  1 
ATOM   4074 H HG21 . THR B 1 52  ? 9.50851   -30.08630 1.35654  1.000 50.20851  ? 38  THR B HG21 1 
ATOM   4075 H HG22 . THR B 1 52  ? 9.72324   -31.51037 0.70967  1.000 50.20851  ? 38  THR B HG22 1 
ATOM   4076 H HG23 . THR B 1 52  ? 8.32861   -30.78322 0.57254  1.000 50.20851  ? 38  THR B HG23 1 
ATOM   4077 N N    . TYR B 1 53  ? 5.80695   -30.16042 2.60282  1.000 37.36083  ? 39  TYR B N    1 
ATOM   4078 C CA   . TYR B 1 53  ? 4.70057   -29.38375 2.06477  1.000 40.46759  ? 39  TYR B CA   1 
ATOM   4079 C C    . TYR B 1 53  ? 3.77355   -28.85382 3.14912  1.000 40.67336  ? 39  TYR B C    1 
ATOM   4080 O O    . TYR B 1 53  ? 2.78609   -28.18565 2.82908  1.000 40.06364  ? 39  TYR B O    1 
ATOM   4081 C CB   . TYR B 1 53  ? 3.89642   -30.23261 1.07495  1.000 43.39119  ? 39  TYR B CB   1 
ATOM   4082 C CG   . TYR B 1 53  ? 4.50121   -30.30206 -0.30719 1.000 49.83433  ? 39  TYR B CG   1 
ATOM   4083 C CD1  . TYR B 1 53  ? 5.49762   -31.22159 -0.60914 1.000 47.74336  ? 39  TYR B CD1  1 
ATOM   4084 C CD2  . TYR B 1 53  ? 4.07123   -29.44783 -1.31358 1.000 52.66348  ? 39  TYR B CD2  1 
ATOM   4085 C CE1  . TYR B 1 53  ? 6.05178   -31.28396 -1.87727 1.000 47.36720  ? 39  TYR B CE1  1 
ATOM   4086 C CE2  . TYR B 1 53  ? 4.61533   -29.50334 -2.58019 1.000 46.60109  ? 39  TYR B CE2  1 
ATOM   4087 C CZ   . TYR B 1 53  ? 5.60516   -30.42105 -2.85840 1.000 51.23180  ? 39  TYR B CZ   1 
ATOM   4088 O OH   . TYR B 1 53  ? 6.14405   -30.47133 -4.12527 1.000 55.87205  ? 39  TYR B OH   1 
ATOM   4089 H H    . TYR B 1 53  ? 5.58784   -30.96327 2.81969  1.000 44.88893  ? 39  TYR B H    1 
ATOM   4090 H HA   . TYR B 1 53  ? 5.06092   -28.62334 1.58225  1.000 48.61705  ? 39  TYR B HA   1 
ATOM   4091 H HB2  . TYR B 1 53  ? 3.83838   -31.13825 1.41750  1.000 52.12537  ? 39  TYR B HB2  1 
ATOM   4092 H HB3  . TYR B 1 53  ? 3.00803   -29.85264 0.98956  1.000 52.12537  ? 39  TYR B HB3  1 
ATOM   4093 H HD1  . TYR B 1 53  ? 5.79747   -31.80460 0.05048  1.000 57.34798  ? 39  TYR B HD1  1 
ATOM   4094 H HD2  . TYR B 1 53  ? 3.40389   -28.82651 -1.13049 1.000 63.25212  ? 39  TYR B HD2  1 
ATOM   4095 H HE1  . TYR B 1 53  ? 6.71987   -31.90264 -2.06647 1.000 56.89658  ? 39  TYR B HE1  1 
ATOM   4096 H HE2  . TYR B 1 53  ? 4.31554   -28.92416 -3.24320 1.000 55.97725  ? 39  TYR B HE2  1 
ATOM   4097 H HH   . TYR B 1 53  ? 5.81954   -29.85903 -4.60002 1.000 67.10240  ? 39  TYR B HH   1 
ATOM   4098 N N    . GLY B 1 54  ? 4.06764   -29.12554 4.41626  1.000 37.16683  ? 40  GLY B N    1 
ATOM   4099 C CA   . GLY B 1 54  ? 3.15913   -28.73487 5.48079  1.000 36.39132  ? 40  GLY B CA   1 
ATOM   4100 C C    . GLY B 1 54  ? 1.78510   -29.34239 5.31556  1.000 34.99911  ? 40  GLY B C    1 
ATOM   4101 O O    . GLY B 1 54  ? 0.77866   -28.69691 5.63311  1.000 31.70753  ? 40  GLY B O    1 
ATOM   4102 H H    . GLY B 1 54  ? 4.77876   -29.53028 4.68102  1.000 44.65614  ? 40  GLY B H    1 
ATOM   4103 H HA2  . GLY B 1 54  ? 3.52093   -29.02327 6.33333  1.000 43.72553  ? 40  GLY B HA2  1 
ATOM   4104 H HA3  . GLY B 1 54  ? 3.06823   -27.76915 5.48674  1.000 43.72553  ? 40  GLY B HA3  1 
ATOM   4105 N N    . LYS B 1 55  ? 1.72073   -30.57461 4.82023  1.000 32.98479  ? 41  LYS B N    1 
ATOM   4106 C CA   . LYS B 1 55  ? 0.46602   -31.23018 4.48300  1.000 34.62468  ? 41  LYS B CA   1 
ATOM   4107 C C    . LYS B 1 55  ? 0.14632   -32.30158 5.51430  1.000 33.05883  ? 41  LYS B C    1 
ATOM   4108 O O    . LYS B 1 55  ? 1.01030   -33.11373 5.86367  1.000 29.71755  ? 41  LYS B O    1 
ATOM   4109 C CB   . LYS B 1 55  ? 0.53850   -31.85263 3.08866  1.000 34.06333  ? 41  LYS B CB   1 
ATOM   4110 C CG   . LYS B 1 55  ? -0.76350  -32.47637 2.61390  1.000 36.16675  ? 41  LYS B CG   1 
ATOM   4111 C CD   . LYS B 1 55  ? -0.57286  -33.17284 1.27804  1.000 35.90863  ? 41  LYS B CD   1 
ATOM   4112 C CE   . LYS B 1 55  ? -1.90188  -33.50616 0.62383  1.000 45.47832  ? 41  LYS B CE   1 
ATOM   4113 N NZ   . LYS B 1 55  ? -1.71731  -34.14001 -0.71437 1.000 45.47611  ? 41  LYS B NZ   1 
ATOM   4114 H H    . LYS B 1 55  ? 2.41181   -31.06306 4.66716  1.000 39.63769  ? 41  LYS B H    1 
ATOM   4115 H HA   . LYS B 1 55  ? -0.24978  -30.57572 4.49715  1.000 41.60555  ? 41  LYS B HA   1 
ATOM   4116 H HB2  . LYS B 1 55  ? 0.78207   -31.16141 2.45321  1.000 40.93193  ? 41  LYS B HB2  1 
ATOM   4117 H HB3  . LYS B 1 55  ? 1.21300   -32.54970 3.09536  1.000 40.93193  ? 41  LYS B HB3  1 
ATOM   4118 H HG2  . LYS B 1 55  ? -1.06401  -33.13196 3.26259  1.000 43.45604  ? 41  LYS B HG2  1 
ATOM   4119 H HG3  . LYS B 1 55  ? -1.43427  -31.78389 2.50691  1.000 43.45604  ? 41  LYS B HG3  1 
ATOM   4120 H HD2  . LYS B 1 55  ? -0.07761  -32.59063 0.68082  1.000 43.14629  ? 41  LYS B HD2  1 
ATOM   4121 H HD3  . LYS B 1 55  ? -0.08530  -34.00020 1.41462  1.000 43.14629  ? 41  LYS B HD3  1 
ATOM   4122 H HE2  . LYS B 1 55  ? -2.39009  -34.12552 1.18858  1.000 54.62992  ? 41  LYS B HE2  1 
ATOM   4123 H HE3  . LYS B 1 55  ? -2.41380  -32.69075 0.50572  1.000 54.62992  ? 41  LYS B HE3  1 
ATOM   4124 H HZ1  . LYS B 1 55  ? -2.50168  -34.20919 -1.12920 1.000 54.62727  ? 41  LYS B HZ1  1 
ATOM   4125 H HZ2  . LYS B 1 55  ? -1.36754  -34.95299 -0.62047 1.000 54.62727  ? 41  LYS B HZ2  1 
ATOM   4126 H HZ3  . LYS B 1 55  ? -1.16978  -33.64576 -1.21238 1.000 54.62727  ? 41  LYS B HZ3  1 
ATOM   4127 N N    . LEU B 1 56  ? -1.09782  -32.30553 5.98418  1.000 35.66126  ? 42  LEU B N    1 
ATOM   4128 C CA   . LEU B 1 56  ? -1.59232  -33.29563 6.92913  1.000 31.61112  ? 42  LEU B CA   1 
ATOM   4129 C C    . LEU B 1 56  ? -2.83454  -33.95247 6.34953  1.000 32.16924  ? 42  LEU B C    1 
ATOM   4130 O O    . LEU B 1 56  ? -3.76965  -33.26027 5.93383  1.000 32.43208  ? 42  LEU B O    1 
ATOM   4131 C CB   . LEU B 1 56  ? -1.92032  -32.65685 8.28125  1.000 32.56723  ? 42  LEU B CB   1 
ATOM   4132 C CG   . LEU B 1 56  ? -0.73215  -32.30650 9.17540  1.000 31.11073  ? 42  LEU B CG   1 
ATOM   4133 C CD1  . LEU B 1 56  ? -1.18315  -31.44833 10.34838 1.000 36.84082  ? 42  LEU B CD1  1 
ATOM   4134 C CD2  . LEU B 1 56  ? -0.05078  -33.57347 9.66769  1.000 30.12200  ? 42  LEU B CD2  1 
ATOM   4135 H H    . LEU B 1 56  ? -1.69153  -31.72461 5.76141  1.000 42.84945  ? 42  LEU B H    1 
ATOM   4136 H HA   . LEU B 1 56  ? -0.91544  -33.97590 7.07044  1.000 37.98928  ? 42  LEU B HA   1 
ATOM   4137 H HB2  . LEU B 1 56  ? -2.40457  -31.83301 8.11481  1.000 39.13661  ? 42  LEU B HB2  1 
ATOM   4138 H HB3  . LEU B 1 56  ? -2.47855  -33.27519 8.77819  1.000 39.13661  ? 42  LEU B HB3  1 
ATOM   4139 H HG   . LEU B 1 56  ? -0.08623  -31.79600 8.66249  1.000 37.38881  ? 42  LEU B HG   1 
ATOM   4140 H HD11 . LEU B 1 56  ? -1.82496  -31.94800 10.87688 1.000 44.26492  ? 42  LEU B HD11 1 
ATOM   4141 H HD12 . LEU B 1 56  ? -0.41098  -31.22414 10.89096 1.000 44.26492  ? 42  LEU B HD12 1 
ATOM   4142 H HD13 . LEU B 1 56  ? -1.59430  -30.63857 10.00757 1.000 44.26492  ? 42  LEU B HD13 1 
ATOM   4143 H HD21 . LEU B 1 56  ? 0.48508   -33.94360 8.94882  1.000 36.20234  ? 42  LEU B HD21 1 
ATOM   4144 H HD22 . LEU B 1 56  ? 0.51611   -33.35390 10.42354 1.000 36.20234  ? 42  LEU B HD22 1 
ATOM   4145 H HD23 . LEU B 1 56  ? -0.72897  -34.21237 9.93744  1.000 36.20234  ? 42  LEU B HD23 1 
ATOM   4146 N N    . THR B 1 57  ? -2.83476  -35.28184 6.31107  1.000 32.30345  ? 43  THR B N    1 
ATOM   4147 C CA   . THR B 1 57  ? -4.00020  -36.06725 5.92343  1.000 31.63473  ? 43  THR B CA   1 
ATOM   4148 C C    . THR B 1 57  ? -4.32435  -37.01182 7.07091  1.000 33.87105  ? 43  THR B C    1 
ATOM   4149 O O    . THR B 1 57  ? -3.51658  -37.88527 7.40354  1.000 31.27641  ? 43  THR B O    1 
ATOM   4150 C CB   . THR B 1 57  ? -3.74751  -36.84742 4.63202  1.000 32.69794  ? 43  THR B CB   1 
ATOM   4151 O OG1  . THR B 1 57  ? -2.54210  -37.61168 4.75551  1.000 39.70267  ? 43  THR B OG1  1 
ATOM   4152 C CG2  . THR B 1 57  ? -3.62773  -35.89831 3.44340  1.000 36.88740  ? 43  THR B CG2  1 
ATOM   4153 H H    . THR B 1 57  ? -2.15127  -35.76392 6.51118  1.000 38.82008  ? 43  THR B H    1 
ATOM   4154 H HA   . THR B 1 57  ? -4.75767  -35.48141 5.76875  1.000 38.01761  ? 43  THR B HA   1 
ATOM   4155 H HB   . THR B 1 57  ? -4.49246  -37.44684 4.46879  1.000 39.29346  ? 43  THR B HB   1 
ATOM   4156 H HG1  . THR B 1 57  ? -2.37799  -38.00807 4.03333  1.000 47.69915  ? 43  THR B HG1  1 
ATOM   4157 H HG21 . THR B 1 57  ? -2.79500  -35.40368 3.49642  1.000 44.32082  ? 43  THR B HG21 1 
ATOM   4158 H HG22 . THR B 1 57  ? -3.64276  -36.40147 2.61425  1.000 44.32082  ? 43  THR B HG22 1 
ATOM   4159 H HG23 . THR B 1 57  ? -4.36728  -35.27065 3.44420  1.000 44.32082  ? 43  THR B HG23 1 
ATOM   4160 N N    . LEU B 1 58  ? -5.49468  -36.82919 7.67902  1.000 29.07628  ? 44  LEU B N    1 
ATOM   4161 C CA   . LEU B 1 58  ? -5.87651  -37.58037 8.86464  1.000 30.09974  ? 44  LEU B CA   1 
ATOM   4162 C C    . LEU B 1 58  ? -7.34047  -37.98229 8.77161  1.000 35.81911  ? 44  LEU B C    1 
ATOM   4163 O O    . LEU B 1 58  ? -8.14622  -37.31381 8.11766  1.000 33.01675  ? 44  LEU B O    1 
ATOM   4164 C CB   . LEU B 1 58  ? -5.64529  -36.75977 10.14144 1.000 31.83708  ? 44  LEU B CB   1 
ATOM   4165 C CG   . LEU B 1 58  ? -4.19062  -36.42685 10.47606 1.000 33.09842  ? 44  LEU B CG   1 
ATOM   4166 C CD1  . LEU B 1 58  ? -4.10052  -35.21186 11.38807 1.000 31.56492  ? 44  LEU B CD1  1 
ATOM   4167 C CD2  . LEU B 1 58  ? -3.51071  -37.62353 11.12407 1.000 33.54764  ? 44  LEU B CD2  1 
ATOM   4168 H H    . LEU B 1 58  ? -6.09077  -36.26711 7.41759  1.000 34.94747  ? 44  LEU B H    1 
ATOM   4169 H HA   . LEU B 1 58  ? -5.34756  -38.39193 8.91440  1.000 36.17562  ? 44  LEU B HA   1 
ATOM   4170 H HB2  . LEU B 1 58  ? -6.11763  -35.91766 10.04839 1.000 38.26044  ? 44  LEU B HB2  1 
ATOM   4171 H HB3  . LEU B 1 58  ? -6.00411  -37.26038 10.89080 1.000 38.26044  ? 44  LEU B HB3  1 
ATOM   4172 H HG   . LEU B 1 58  ? -3.72487  -36.21360 9.65235  1.000 39.77404  ? 44  LEU B HG   1 
ATOM   4173 H HD11 . LEU B 1 58  ? -3.57670  -34.52449 10.94757 1.000 37.93385  ? 44  LEU B HD11 1 
ATOM   4174 H HD12 . LEU B 1 58  ? -4.99567  -34.88292 11.56527 1.000 37.93385  ? 44  LEU B HD12 1 
ATOM   4175 H HD13 . LEU B 1 58  ? -3.67309  -35.47180 12.21912 1.000 37.93385  ? 44  LEU B HD13 1 
ATOM   4176 H HD21 . LEU B 1 58  ? -3.97651  -37.84474 11.94566 1.000 40.31311  ? 44  LEU B HD21 1 
ATOM   4177 H HD22 . LEU B 1 58  ? -3.54419  -38.37539 10.51212 1.000 40.31311  ? 44  LEU B HD22 1 
ATOM   4178 H HD23 . LEU B 1 58  ? -2.58800  -37.39572 11.31801 1.000 40.31311  ? 44  LEU B HD23 1 
ATOM   4179 N N    . LYS B 1 59  ? -7.67076  -39.09374 9.42716  1.000 30.19249  ? 45  LYS B N    1 
ATOM   4180 C CA   . LYS B 1 59  ? -9.04839  -39.53112 9.60616  1.000 26.97571  ? 45  LYS B CA   1 
ATOM   4181 C C    . LYS B 1 59  ? -9.25863  -39.85082 11.07757 1.000 29.82880  ? 45  LYS B C    1 
ATOM   4182 O O    . LYS B 1 59  ? -8.42332  -40.51986 11.69315 1.000 26.50041  ? 45  LYS B O    1 
ATOM   4183 C CB   . LYS B 1 59  ? -9.37294  -40.75530 8.74611  1.000 28.31530  ? 45  LYS B CB   1 
ATOM   4184 C CG   . LYS B 1 59  ? -10.73749 -41.36422 9.05023  1.000 32.76984  ? 45  LYS B CG   1 
ATOM   4185 C CD   . LYS B 1 59  ? -11.08355 -42.49159 8.09021  1.000 31.07186  ? 45  LYS B CD   1 
ATOM   4186 C CE   . LYS B 1 59  ? -12.29398 -43.27902 8.57843  1.000 31.14747  ? 45  LYS B CE   1 
ATOM   4187 N NZ   . LYS B 1 59  ? -12.33604 -44.65466 8.00687  1.000 36.81073  ? 45  LYS B NZ   1 
ATOM   4188 H H    . LYS B 1 59  ? -7.09648  -39.62378 9.78612  1.000 36.28693  ? 45  LYS B H    1 
ATOM   4189 H HA   . LYS B 1 59  ? -9.65405  -38.81994 9.34482  1.000 32.42679  ? 45  LYS B HA   1 
ATOM   4190 H HB2  . LYS B 1 59  ? -9.36546  -40.49292 7.81230  1.000 34.03430  ? 45  LYS B HB2  1 
ATOM   4191 H HB3  . LYS B 1 59  ? -8.70090  -41.43657 8.90469  1.000 34.03430  ? 45  LYS B HB3  1 
ATOM   4192 H HG2  . LYS B 1 59  ? -10.73333 -41.72396 9.95105  1.000 39.37975  ? 45  LYS B HG2  1 
ATOM   4193 H HG3  . LYS B 1 59  ? -11.41861 -40.67825 8.97007  1.000 39.37975  ? 45  LYS B HG3  1 
ATOM   4194 H HD2  . LYS B 1 59  ? -11.29110 -42.12045 7.21838  1.000 37.34217  ? 45  LYS B HD2  1 
ATOM   4195 H HD3  . LYS B 1 59  ? -10.33053 -43.09915 8.02142  1.000 37.34217  ? 45  LYS B HD3  1 
ATOM   4196 H HE2  . LYS B 1 59  ? -12.25685 -43.35402 9.54481  1.000 37.09726  ? 45  LYS B HE2  1 
ATOM   4197 H HE3  . LYS B 1 59  ? -13.10384 -42.81610 8.31248  1.000 37.09726  ? 45  LYS B HE3  1 
ATOM   4198 H HZ1  . LYS B 1 59  ? -12.56200 -44.62013 7.14672  1.000 44.22882  ? 45  LYS B HZ1  1 
ATOM   4199 H HZ2  . LYS B 1 59  ? -11.53686 -45.03938 8.08034  1.000 44.22882  ? 45  LYS B HZ2  1 
ATOM   4200 H HZ3  . LYS B 1 59  ? -12.93504 -45.14744 8.44330  1.000 44.22882  ? 45  LYS B HZ3  1 
ATOM   4201 N N    . PHE B 1 60  ? -10.36760 -39.37258 11.63531 1.000 28.78451  ? 46  PHE B N    1 
ATOM   4202 C CA   . PHE B 1 60  ? -10.69820 -39.56822 13.03854 1.000 25.90406  ? 46  PHE B CA   1 
ATOM   4203 C C    . PHE B 1 60  ? -12.03951 -40.27456 13.15097 1.000 29.49195  ? 46  PHE B C    1 
ATOM   4204 O O    . PHE B 1 60  ? -12.94449 -40.03416 12.34743 1.000 31.15578  ? 46  PHE B O    1 
ATOM   4205 C CB   . PHE B 1 60  ? -10.76199 -38.23249 13.78779 1.000 24.91361  ? 46  PHE B CB   1 
ATOM   4206 C CG   . PHE B 1 60  ? -9.50482  -37.42697 13.69372 1.000 30.18600  ? 46  PHE B CG   1 
ATOM   4207 C CD1  . PHE B 1 60  ? -8.48961  -37.60088 14.61551 1.000 26.54852  ? 46  PHE B CD1  1 
ATOM   4208 C CD2  . PHE B 1 60  ? -9.33697  -36.49336 12.68379 1.000 27.36980  ? 46  PHE B CD2  1 
ATOM   4209 C CE1  . PHE B 1 60  ? -7.33112  -36.86310 14.53237 1.000 26.58586  ? 46  PHE B CE1  1 
ATOM   4210 C CE2  . PHE B 1 60  ? -8.17864  -35.75277 12.59683 1.000 25.41542  ? 46  PHE B CE2  1 
ATOM   4211 C CZ   . PHE B 1 60  ? -7.17474  -35.93823 13.52215 1.000 28.67251  ? 46  PHE B CZ   1 
ATOM   4212 H H    . PHE B 1 60  ? -10.95907 -38.91892 11.20641 1.000 34.59735  ? 46  PHE B H    1 
ATOM   4213 H HA   . PHE B 1 60  ? -10.01804 -40.12083 13.45437 1.000 31.14081  ? 46  PHE B HA   1 
ATOM   4214 H HB2  . PHE B 1 60  ? -11.48278 -37.70052 13.41580 1.000 29.95228  ? 46  PHE B HB2  1 
ATOM   4215 H HB3  . PHE B 1 60  ? -10.93053 -38.40936 14.72652 1.000 29.95228  ? 46  PHE B HB3  1 
ATOM   4216 H HD1  . PHE B 1 60  ? -8.59064  -38.22318 15.29920 1.000 31.91417  ? 46  PHE B HD1  1 
ATOM   4217 H HD2  . PHE B 1 60  ? -10.01316 -36.36537 12.05826 1.000 32.89971  ? 46  PHE B HD2  1 
ATOM   4218 H HE1  . PHE B 1 60  ? -6.65394  -36.98833 15.15738 1.000 31.95897  ? 46  PHE B HE1  1 
ATOM   4219 H HE2  . PHE B 1 60  ? -8.07448  -35.12895 11.91499 1.000 30.55444  ? 46  PHE B HE2  1 
ATOM   4220 H HZ   . PHE B 1 60  ? -6.39180  -35.43956 13.46521 1.000 34.46295  ? 46  PHE B HZ   1 
ATOM   4221 N N    . ILE B 1 61  ? -12.16495 -41.14707 14.15068 1.000 25.13512  ? 47  ILE B N    1 
ATOM   4222 C CA   . ILE B 1 61  ? -13.43083 -41.79245 14.46238 1.000 30.68890  ? 47  ILE B CA   1 
ATOM   4223 C C    . ILE B 1 61  ? -13.71673 -41.59849 15.94404 1.000 32.12121  ? 47  ILE B C    1 
ATOM   4224 O O    . ILE B 1 61  ? -12.81827 -41.34585 16.74954 1.000 30.06843  ? 47  ILE B O    1 
ATOM   4225 C CB   . ILE B 1 61  ? -13.44496 -43.30174 14.11857 1.000 28.97243  ? 47  ILE B CB   1 
ATOM   4226 C CG1  . ILE B 1 61  ? -12.46584 -44.07085 15.01470 1.000 32.59332  ? 47  ILE B CG1  1 
ATOM   4227 C CG2  . ILE B 1 61  ? -13.13853 -43.51841 12.64124 1.000 33.23401  ? 47  ILE B CG2  1 
ATOM   4228 C CD1  . ILE B 1 61  ? -12.58303 -45.57949 14.90495 1.000 37.24149  ? 47  ILE B CD1  1 
ATOM   4229 H H    . ILE B 1 61  ? -11.51914 -41.38204 14.66771 1.000 30.21809  ? 47  ILE B H    1 
ATOM   4230 H HA   . ILE B 1 61  ? -14.13067 -41.36414 13.94501 1.000 36.88261  ? 47  ILE B HA   1 
ATOM   4231 H HB   . ILE B 1 61  ? -14.33495 -43.64670 14.29125 1.000 34.82286  ? 47  ILE B HB   1 
ATOM   4232 H HG12 . ILE B 1 61  ? -11.56033 -43.82656 14.76716 1.000 39.16793  ? 47  ILE B HG12 1 
ATOM   4233 H HG13 . ILE B 1 61  ? -12.63404 -43.82839 15.93873 1.000 39.16793  ? 47  ILE B HG13 1 
ATOM   4234 H HG21 . ILE B 1 61  ? -12.44241 -44.18880 12.55812 1.000 39.93675  ? 47  ILE B HG21 1 
ATOM   4235 H HG22 . ILE B 1 61  ? -13.94382 -43.82038 12.19266 1.000 39.93675  ? 47  ILE B HG22 1 
ATOM   4236 H HG23 . ILE B 1 61  ? -12.83888 -42.68074 12.25471 1.000 39.93675  ? 47  ILE B HG23 1 
ATOM   4237 H HD11 . ILE B 1 61  ? -13.43237 -45.85848 15.28136 1.000 44.74573  ? 47  ILE B HD11 1 
ATOM   4238 H HD12 . ILE B 1 61  ? -12.53658 -45.83264 13.96972 1.000 44.74573  ? 47  ILE B HD12 1 
ATOM   4239 H HD13 . ILE B 1 61  ? -11.85332 -45.98942 15.39523 1.000 44.74573  ? 47  ILE B HD13 1 
ATOM   4240 N N    . SER B 1 62  ? -14.99106 -41.72378 16.29367 1.000 32.73882  ? 48  SER B N    1 
ATOM   4241 C CA   . SER B 1 62  ? -15.39813 -41.89760 17.67815 1.000 31.45327  ? 48  SER B CA   1 
ATOM   4242 C C    . SER B 1 62  ? -15.54295 -43.38764 17.95450 1.000 37.33589  ? 48  SER B C    1 
ATOM   4243 O O    . SER B 1 62  ? -16.21245 -44.10205 17.20016 1.000 30.92708  ? 48  SER B O    1 
ATOM   4244 C CB   . SER B 1 62  ? -16.71538 -41.17716 17.95983 1.000 36.78292  ? 48  SER B CB   1 
ATOM   4245 O OG   . SER B 1 62  ? -17.27273 -41.61107 19.18987 1.000 35.34749  ? 48  SER B OG   1 
ATOM   4246 H H    . SER B 1 62  ? -15.64707 -41.71091 15.73772 1.000 39.34253  ? 48  SER B H    1 
ATOM   4247 H HA   . SER B 1 62  ? -14.72787 -41.52174 18.27009 1.000 37.79986  ? 48  SER B HA   1 
ATOM   4248 H HB2  . SER B 1 62  ? -16.54974 -40.22258 18.00712 1.000 44.19545  ? 48  SER B HB2  1 
ATOM   4249 H HB3  . SER B 1 62  ? -17.34067 -41.37031 17.24386 1.000 44.19545  ? 48  SER B HB3  1 
ATOM   4250 H HG   . SER B 1 62  ? -18.01191 -41.23365 19.31936 1.000 42.47293  ? 48  SER B HG   1 
ATOM   4251 N N    . THR B 1 63  ? -14.89642 -43.85780 19.01990 1.000 36.21057  ? 49  THR B N    1 
ATOM   4252 C CA   . THR B 1 63  ? -15.04379 -45.23303 19.47283 1.000 38.04445  ? 49  THR B CA   1 
ATOM   4253 C C    . THR B 1 63  ? -16.06671 -45.35214 20.59590 1.000 35.67401  ? 49  THR B C    1 
ATOM   4254 O O    . THR B 1 63  ? -16.11321 -46.37884 21.28151 1.000 38.87594  ? 49  THR B O    1 
ATOM   4255 C CB   . THR B 1 63  ? -13.69205 -45.79244 19.92006 1.000 33.95714  ? 49  THR B CB   1 
ATOM   4256 O OG1  . THR B 1 63  ? -13.24355 -45.10277 21.09251 1.000 36.29883  ? 49  THR B OG1  1 
ATOM   4257 C CG2  . THR B 1 63  ? -12.65841 -45.62419 18.81441 1.000 31.24223  ? 49  THR B CG2  1 
ATOM   4258 H H    . THR B 1 63  ? -14.35951 -43.38958 19.50166 1.000 43.50863  ? 49  THR B H    1 
ATOM   4259 H HA   . THR B 1 63  ? -15.35093 -45.77473 18.72911 1.000 45.70928  ? 49  THR B HA   1 
ATOM   4260 H HB   . THR B 1 63  ? -13.78459 -46.73723 20.11936 1.000 40.80451  ? 49  THR B HB   1 
ATOM   4261 H HG1  . THR B 1 63  ? -13.02627 -44.31524 20.89710 1.000 43.61454  ? 49  THR B HG1  1 
ATOM   4262 H HG21 . THR B 1 63  ? -12.43992 -44.68553 18.70455 1.000 37.54661  ? 49  THR B HG21 1 
ATOM   4263 H HG22 . THR B 1 63  ? -11.85021 -46.11135 19.03888 1.000 37.54661  ? 49  THR B HG22 1 
ATOM   4264 H HG23 . THR B 1 63  ? -13.00957 -45.96575 17.97719 1.000 37.54661  ? 49  THR B HG23 1 
ATOM   4265 N N    . THR B 1 64  ? -16.90158 -44.32209 20.77923 1.000 33.06928  ? 50  THR B N    1 
ATOM   4266 C CA   . THR B 1 64  ? -17.85293 -44.27879 21.88226 1.000 33.09420  ? 50  THR B CA   1 
ATOM   4267 C C    . THR B 1 64  ? -19.23683 -43.82046 21.43112 1.000 32.67455  ? 50  THR B C    1 
ATOM   4268 O O    . THR B 1 64  ? -20.03690 -43.38397 22.26720 1.000 38.82023  ? 50  THR B O    1 
ATOM   4269 C CB   . THR B 1 64  ? -17.34293 -43.34298 22.98233 1.000 34.92763  ? 50  THR B CB   1 
ATOM   4270 O OG1  . THR B 1 64  ? -17.11351 -42.03994 22.42901 1.000 33.54549  ? 50  THR B OG1  1 
ATOM   4271 C CG2  . THR B 1 64  ? -16.04630 -43.87022 23.56864 1.000 34.76677  ? 50  THR B CG2  1 
ATOM   4272 H H    . THR B 1 64  ? -16.93332 -43.62997 20.26975 1.000 39.73908  ? 50  THR B H    1 
ATOM   4273 H HA   . THR B 1 64  ? -17.94528 -45.17146 22.25039 1.000 39.76898  ? 50  THR B HA   1 
ATOM   4274 H HB   . THR B 1 64  ? -18.00113 -43.28612 23.69257 1.000 41.96910  ? 50  THR B HB   1 
ATOM   4275 H HG1  . THR B 1 64  ? -17.18023 -41.45682 23.02994 1.000 40.31053  ? 50  THR B HG1  1 
ATOM   4276 H HG21 . THR B 1 64  ? -15.84255 -43.40503 24.39507 1.000 41.77607  ? 50  THR B HG21 1 
ATOM   4277 H HG22 . THR B 1 64  ? -16.12728 -44.81905 23.75321 1.000 41.77607  ? 50  THR B HG22 1 
ATOM   4278 H HG23 . THR B 1 64  ? -15.31868 -43.73236 22.94217 1.000 41.77607  ? 50  THR B HG23 1 
ATOM   4279 N N    . GLY B 1 65  ? -19.54032 -43.90534 20.13758 1.000 39.60779  ? 51  GLY B N    1 
ATOM   4280 C CA   . GLY B 1 65  ? -20.80608 -43.42528 19.62289 1.000 36.29570  ? 51  GLY B CA   1 
ATOM   4281 C C    . GLY B 1 65  ? -20.75483 -41.96064 19.23926 1.000 35.91741  ? 51  GLY B C    1 
ATOM   4282 O O    . GLY B 1 65  ? -19.71763 -41.29317 19.29496 1.000 35.76729  ? 51  GLY B O    1 
ATOM   4283 H H    . GLY B 1 65  ? -19.02230 -44.24022 19.53833 1.000 47.58528  ? 51  GLY B H    1 
ATOM   4284 H HA2  . GLY B 1 65  ? -21.04842 -43.93901 18.83659 1.000 43.61078  ? 51  GLY B HA2  1 
ATOM   4285 H HA3  . GLY B 1 65  ? -21.49194 -43.54042 20.29908 1.000 43.61078  ? 51  GLY B HA3  1 
ATOM   4286 N N    . LYS B 1 66  ? -21.91976 -41.45397 18.83737 1.000 35.63534  ? 52  LYS B N    1 
ATOM   4287 C CA   . LYS B 1 66  ? -22.04384 -40.06163 18.42221 1.000 37.36011  ? 52  LYS B CA   1 
ATOM   4288 C C    . LYS B 1 66  ? -21.40411 -39.13775 19.45173 1.000 36.64248  ? 52  LYS B C    1 
ATOM   4289 O O    . LYS B 1 66  ? -21.69826 -39.21785 20.64746 1.000 34.10683  ? 52  LYS B O    1 
ATOM   4290 C CB   . LYS B 1 66  ? -23.52276 -39.71231 18.23156 1.000 45.26201  ? 52  LYS B CB   1 
ATOM   4291 C CG   . LYS B 1 66  ? -23.80550 -38.64869 17.17546 1.000 52.80166  ? 52  LYS B CG   1 
ATOM   4292 C CD   . LYS B 1 66  ? -23.40321 -37.25540 17.63939 1.000 54.35558  ? 52  LYS B CD   1 
ATOM   4293 C CE   . LYS B 1 66  ? -24.04126 -36.17334 16.77423 1.000 53.54060  ? 52  LYS B CE   1 
ATOM   4294 N NZ   . LYS B 1 66  ? -23.68405 -36.30471 15.33180 1.000 58.76374  ? 52  LYS B NZ   1 
ATOM   4295 H H    . LYS B 1 66  ? -22.65493 -41.89832 18.79632 1.000 42.81834  ? 52  LYS B H    1 
ATOM   4296 H HA   . LYS B 1 66  ? -21.58871 -39.93064 17.57569 1.000 44.88807  ? 52  LYS B HA   1 
ATOM   4297 H HB2  . LYS B 1 66  ? -23.99620 -40.51671 17.96757 1.000 54.37035  ? 52  LYS B HB2  1 
ATOM   4298 H HB3  . LYS B 1 66  ? -23.87140 -39.38388 19.07506 1.000 54.37035  ? 52  LYS B HB3  1 
ATOM   4299 H HG2  . LYS B 1 66  ? -23.30309 -38.85605 16.37203 1.000 63.41793  ? 52  LYS B HG2  1 
ATOM   4300 H HG3  . LYS B 1 66  ? -24.75544 -38.63897 16.97947 1.000 63.41793  ? 52  LYS B HG3  1 
ATOM   4301 H HD2  . LYS B 1 66  ? -23.69469 -37.12492 18.55531 1.000 65.28264  ? 52  LYS B HD2  1 
ATOM   4302 H HD3  . LYS B 1 66  ? -22.43933 -37.16318 17.58165 1.000 65.28264  ? 52  LYS B HD3  1 
ATOM   4303 H HE2  . LYS B 1 66  ? -25.00626 -36.23470 16.85108 1.000 64.30466  ? 52  LYS B HE2  1 
ATOM   4304 H HE3  . LYS B 1 66  ? -23.73868 -35.30403 17.08024 1.000 64.30466  ? 52  LYS B HE3  1 
ATOM   4305 H HZ1  . LYS B 1 66  ? -22.81981 -36.50046 15.24884 1.000 70.57243  ? 52  LYS B HZ1  1 
ATOM   4306 H HZ2  . LYS B 1 66  ? -24.16441 -36.95353 14.95712 1.000 70.57243  ? 52  LYS B HZ2  1 
ATOM   4307 H HZ3  . LYS B 1 66  ? -23.84925 -35.54058 14.90648 1.000 70.57243  ? 52  LYS B HZ3  1 
ATOM   4308 N N    . LEU B 1 67  ? -20.50893 -38.27269 18.98168 1.000 36.72590  ? 53  LEU B N    1 
ATOM   4309 C CA   . LEU B 1 67  ? -19.84110 -37.34126 19.87444 1.000 36.38535  ? 53  LEU B CA   1 
ATOM   4310 C C    . LEU B 1 67  ? -20.85650 -36.38329 20.49715 1.000 37.30216  ? 53  LEU B C    1 
ATOM   4311 O O    . LEU B 1 67  ? -21.84416 -36.01046 19.85680 1.000 38.36939  ? 53  LEU B O    1 
ATOM   4312 C CB   . LEU B 1 67  ? -18.78417 -36.53821 19.12152 1.000 35.50504  ? 53  LEU B CB   1 
ATOM   4313 C CG   . LEU B 1 67  ? -17.54282 -37.27318 18.62202 1.000 38.44132  ? 53  LEU B CG   1 
ATOM   4314 C CD1  . LEU B 1 67  ? -16.61010 -36.28266 17.93352 1.000 34.92222  ? 53  LEU B CD1  1 
ATOM   4315 C CD2  . LEU B 1 67  ? -16.83350 -37.98746 19.76110 1.000 36.17391  ? 53  LEU B CD2  1 
ATOM   4316 H H    . LEU B 1 67  ? -20.27447 -38.20756 18.15682 1.000 44.12702  ? 53  LEU B H    1 
ATOM   4317 H HA   . LEU B 1 67  ? -19.40516 -37.83913 20.58366 1.000 43.71837  ? 53  LEU B HA   1 
ATOM   4318 H HB2  . LEU B 1 67  ? -19.21027 -36.15014 18.34130 1.000 42.66198  ? 53  LEU B HB2  1 
ATOM   4319 H HB3  . LEU B 1 67  ? -18.47209 -35.83561 19.71300 1.000 42.66198  ? 53  LEU B HB3  1 
ATOM   4320 H HG   . LEU B 1 67  ? -17.80485 -37.95254 17.98115 1.000 46.18553  ? 53  LEU B HG   1 
ATOM   4321 H HD11 . LEU B 1 67  ? -17.07674 -35.87636 17.18648 1.000 41.96260  ? 53  LEU B HD11 1 
ATOM   4322 H HD12 . LEU B 1 67  ? -16.34841 -35.59989 18.57090 1.000 41.96260  ? 53  LEU B HD12 1 
ATOM   4323 H HD13 . LEU B 1 67  ? -15.82564 -36.75630 17.61542 1.000 41.96260  ? 53  LEU B HD13 1 
ATOM   4324 H HD21 . LEU B 1 67  ? -16.94796 -37.47379 20.57593 1.000 43.46463  ? 53  LEU B HD21 1 
ATOM   4325 H HD22 . LEU B 1 67  ? -17.22014 -38.87042 19.86965 1.000 43.46463  ? 53  LEU B HD22 1 
ATOM   4326 H HD23 . LEU B 1 67  ? -15.89032 -38.06332 19.54765 1.000 43.46463  ? 53  LEU B HD23 1 
ATOM   4327 N N    . PRO B 1 68  ? -20.63560 -35.95966 21.74435 1.000 36.31894  ? 54  PRO B N    1 
ATOM   4328 C CA   . PRO B 1 68  ? -21.48507 -34.92013 22.33667 1.000 37.60830  ? 54  PRO B CA   1 
ATOM   4329 C C    . PRO B 1 68  ? -21.10681 -33.50578 21.92744 1.000 36.41022  ? 54  PRO B C    1 
ATOM   4330 O O    . PRO B 1 68  ? -21.75188 -32.55563 22.38558 1.000 36.60910  ? 54  PRO B O    1 
ATOM   4331 C CB   . PRO B 1 68  ? -21.27081 -35.12990 23.84064 1.000 37.42536  ? 54  PRO B CB   1 
ATOM   4332 C CG   . PRO B 1 68  ? -19.87228 -35.61583 23.93612 1.000 33.95620  ? 54  PRO B CG   1 
ATOM   4333 C CD   . PRO B 1 68  ? -19.62833 -36.45265 22.70214 1.000 36.83869  ? 54  PRO B CD   1 
ATOM   4334 H HA   . PRO B 1 68  ? -22.41771 -35.07767 22.12158 1.000 45.18590  ? 54  PRO B HA   1 
ATOM   4335 H HB2  . PRO B 1 68  ? -21.38454 -34.29154 24.31510 1.000 44.96637  ? 54  PRO B HB2  1 
ATOM   4336 H HB3  . PRO B 1 68  ? -21.89589 -35.79000 24.17894 1.000 44.96637  ? 54  PRO B HB3  1 
ATOM   4337 H HG2  . PRO B 1 68  ? -19.26602 -34.85904 23.96123 1.000 40.80338  ? 54  PRO B HG2  1 
ATOM   4338 H HG3  . PRO B 1 68  ? -19.76803 -36.15118 24.73826 1.000 40.80338  ? 54  PRO B HG3  1 
ATOM   4339 H HD2  . PRO B 1 68  ? -18.73123 -36.31040 22.36174 1.000 44.26237  ? 54  PRO B HD2  1 
ATOM   4340 H HD3  . PRO B 1 68  ? -19.76576 -37.39391 22.89201 1.000 44.26237  ? 54  PRO B HD3  1 
ATOM   4341 N N    . VAL B 1 69  ? -20.08299 -33.34032 21.09247 1.000 37.23742  ? 55  VAL B N    1 
ATOM   4342 C CA   . VAL B 1 69  ? -19.67672 -32.01620 20.61594 1.000 36.76973  ? 55  VAL B CA   1 
ATOM   4343 C C    . VAL B 1 69  ? -19.37436 -32.09060 19.13153 1.000 32.78892  ? 55  VAL B C    1 
ATOM   4344 O O    . VAL B 1 69  ? -19.02139 -33.14950 18.59629 1.000 33.51908  ? 55  VAL B O    1 
ATOM   4345 C CB   . VAL B 1 69  ? -18.43797 -31.49033 21.36926 1.000 36.75804  ? 55  VAL B CB   1 
ATOM   4346 C CG1  . VAL B 1 69  ? -18.75672 -31.29877 22.84257 1.000 36.06455  ? 55  VAL B CG1  1 
ATOM   4347 C CG2  . VAL B 1 69  ? -17.25859 -32.44115 21.19342 1.000 33.40321  ? 55  VAL B CG2  1 
ATOM   4348 H H    . VAL B 1 69  ? -19.60244 -33.98322 20.78368 1.000 44.74084  ? 55  VAL B H    1 
ATOM   4349 H HA   . VAL B 1 69  ? -20.40350 -31.38791 20.74986 1.000 44.17961  ? 55  VAL B HA   1 
ATOM   4350 H HB   . VAL B 1 69  ? -18.18708 -30.62992 20.99825 1.000 44.16559  ? 55  VAL B HB   1 
ATOM   4351 H HG11 . VAL B 1 69  ? -17.98364 -30.91549 23.28569 1.000 43.33340  ? 55  VAL B HG11 1 
ATOM   4352 H HG12 . VAL B 1 69  ? -19.51608 -30.70106 22.92628 1.000 43.33340  ? 55  VAL B HG12 1 
ATOM   4353 H HG13 . VAL B 1 69  ? -18.96916 -32.16034 23.23434 1.000 43.33340  ? 55  VAL B HG13 1 
ATOM   4354 H HG21 . VAL B 1 69  ? -17.55236 -33.21998 20.69539 1.000 40.13980  ? 55  VAL B HG21 1 
ATOM   4355 H HG22 . VAL B 1 69  ? -16.55426 -31.98420 20.70761 1.000 40.13980  ? 55  VAL B HG22 1 
ATOM   4356 H HG23 . VAL B 1 69  ? -16.93651 -32.70993 22.06802 1.000 40.13980  ? 55  VAL B HG23 1 
ATOM   4357 N N    . PRO B 1 70  ? -19.50382 -30.96212 18.43244 1.000 37.99388  ? 56  PRO B N    1 
ATOM   4358 C CA   . PRO B 1 70  ? -19.25214 -30.97229 16.98599 1.000 29.18659  ? 56  PRO B CA   1 
ATOM   4359 C C    . PRO B 1 70  ? -17.78564 -31.22430 16.67702 1.000 30.90346  ? 56  PRO B C    1 
ATOM   4360 O O    . PRO B 1 70  ? -16.89131 -30.73571 17.37180 1.000 29.11422  ? 56  PRO B O    1 
ATOM   4361 C CB   . PRO B 1 70  ? -19.68451 -29.57076 16.53381 1.000 35.05093  ? 56  PRO B CB   1 
ATOM   4362 C CG   . PRO B 1 70  ? -20.50611 -29.02445 17.65551 1.000 36.79806  ? 56  PRO B CG   1 
ATOM   4363 C CD   . PRO B 1 70  ? -19.93951 -29.63448 18.89621 1.000 37.18868  ? 56  PRO B CD   1 
ATOM   4364 H HA   . PRO B 1 70  ? -19.79992 -31.64254 16.54828 1.000 35.07985  ? 56  PRO B HA   1 
ATOM   4365 H HB2  . PRO B 1 70  ? -18.90128 -29.01977 16.37937 1.000 42.11705  ? 56  PRO B HB2  1 
ATOM   4366 H HB3  . PRO B 1 70  ? -20.20984 -29.63588 15.72098 1.000 42.11705  ? 56  PRO B HB3  1 
ATOM   4367 H HG2  . PRO B 1 70  ? -20.42858 -28.05785 17.67967 1.000 44.21361  ? 56  PRO B HG2  1 
ATOM   4368 H HG3  . PRO B 1 70  ? -21.43446 -29.27998 17.53813 1.000 44.21361  ? 56  PRO B HG3  1 
ATOM   4369 H HD2  . PRO B 1 70  ? -19.18796 -29.11744 19.22596 1.000 44.68235  ? 56  PRO B HD2  1 
ATOM   4370 H HD3  . PRO B 1 70  ? -20.61694 -29.71219 19.58611 1.000 44.68235  ? 56  PRO B HD3  1 
ATOM   4371 N N    . TRP B 1 71  ? -17.54637 -31.99465 15.61859 1.000 28.44206  ? 57  TRP B N    1 
ATOM   4372 C CA   . TRP B 1 71  ? -16.17730 -32.25876 15.18761 1.000 31.50143  ? 57  TRP B CA   1 
ATOM   4373 C C    . TRP B 1 71  ? -15.36094 -30.99221 14.95984 1.000 27.21777  ? 57  TRP B C    1 
ATOM   4374 O O    . TRP B 1 71  ? -14.19266 -30.96150 15.38233 1.000 25.65036  ? 57  TRP B O    1 
ATOM   4375 C CB   . TRP B 1 71  ? -16.19063 -33.10367 13.90546 1.000 31.13582  ? 57  TRP B CB   1 
ATOM   4376 C CG   . TRP B 1 71  ? -16.46646 -34.56339 14.12482 1.000 30.74575  ? 57  TRP B CG   1 
ATOM   4377 C CD1  . TRP B 1 71  ? -17.63181 -35.22319 13.87090 1.000 31.49632  ? 57  TRP B CD1  1 
ATOM   4378 C CD2  . TRP B 1 71  ? -15.55282 -35.54394 14.63311 1.000 25.77889  ? 57  TRP B CD2  1 
ATOM   4379 N NE1  . TRP B 1 71  ? -17.50244 -36.55340 14.18867 1.000 28.83320  ? 57  TRP B NE1  1 
ATOM   4380 C CE2  . TRP B 1 71  ? -16.23499 -36.77628 14.65883 1.000 29.99540  ? 57  TRP B CE2  1 
ATOM   4381 C CE3  . TRP B 1 71  ? -14.22504 -35.49892 15.06894 1.000 27.68488  ? 57  TRP B CE3  1 
ATOM   4382 C CZ2  . TRP B 1 71  ? -15.63592 -37.95298 15.10723 1.000 29.44139  ? 57  TRP B CZ2  1 
ATOM   4383 C CZ3  . TRP B 1 71  ? -13.63092 -36.66832 15.51245 1.000 25.76859  ? 57  TRP B CZ3  1 
ATOM   4384 C CH2  . TRP B 1 71  ? -14.33629 -37.87818 15.52865 1.000 28.35002  ? 57  TRP B CH2  1 
ATOM   4385 H H    . TRP B 1 71  ? -18.15169 -32.37208 15.13824 1.000 34.18642  ? 57  TRP B H    1 
ATOM   4386 H HA   . TRP B 1 71  ? -15.74757 -32.77017 15.89095 1.000 37.85766  ? 57  TRP B HA   1 
ATOM   4387 H HB2  . TRP B 1 71  ? -16.88061 -32.76054 13.31632 1.000 37.41892  ? 57  TRP B HB2  1 
ATOM   4388 H HB3  . TRP B 1 71  ? -15.32294 -33.03057 13.47807 1.000 37.41892  ? 57  TRP B HB3  1 
ATOM   4389 H HD1  . TRP B 1 71  ? -18.40310 -34.82968 13.53155 1.000 37.85152  ? 57  TRP B HD1  1 
ATOM   4390 H HE1  . TRP B 1 71  ? -18.11701 -37.14927 14.10595 1.000 34.65579  ? 57  TRP B HE1  1 
ATOM   4391 H HE3  . TRP B 1 71  ? -13.75028 -34.69928 15.06109 1.000 33.27779  ? 57  TRP B HE3  1 
ATOM   4392 H HZ2  . TRP B 1 71  ? -16.10188 -38.75774 15.11938 1.000 35.38560  ? 57  TRP B HZ2  1 
ATOM   4393 H HZ3  . TRP B 1 71  ? -12.74820 -36.65007 15.80465 1.000 30.97825  ? 57  TRP B HZ3  1 
ATOM   4394 H HH2  . TRP B 1 71  ? -13.91189 -38.64786 15.83260 1.000 34.07596  ? 57  TRP B HH2  1 
ATOM   4395 N N    . PRO B 1 72  ? -15.87857 -29.94477 14.31333 1.000 24.68630  ? 58  PRO B N    1 
ATOM   4396 C CA   . PRO B 1 72  ? -15.05091 -28.74869 14.08352 1.000 29.09123  ? 58  PRO B CA   1 
ATOM   4397 C C    . PRO B 1 72  ? -14.40957 -28.18851 15.34349 1.000 28.82062  ? 58  PRO B C    1 
ATOM   4398 O O    . PRO B 1 72  ? -13.34974 -27.55606 15.25499 1.000 30.01485  ? 58  PRO B O    1 
ATOM   4399 C CB   . PRO B 1 72  ? -16.04537 -27.75756 13.46240 1.000 28.55871  ? 58  PRO B CB   1 
ATOM   4400 C CG   . PRO B 1 72  ? -17.05894 -28.62067 12.78875 1.000 30.54979  ? 58  PRO B CG   1 
ATOM   4401 C CD   . PRO B 1 72  ? -17.19709 -29.83796 13.66272 1.000 29.00028  ? 58  PRO B CD   1 
ATOM   4402 H HA   . PRO B 1 72  ? -14.35327 -28.95243 13.44111 1.000 34.96542  ? 58  PRO B HA   1 
ATOM   4403 H HB2  . PRO B 1 72  ? -16.45330 -27.21679 14.15671 1.000 34.32639  ? 58  PRO B HB2  1 
ATOM   4404 H HB3  . PRO B 1 72  ? -15.59096 -27.18787 12.82218 1.000 34.32639  ? 58  PRO B HB3  1 
ATOM   4405 H HG2  . PRO B 1 72  ? -17.90244 -28.14627 12.72273 1.000 36.71569  ? 58  PRO B HG2  1 
ATOM   4406 H HG3  . PRO B 1 72  ? -16.74582 -28.86542 11.90390 1.000 36.71569  ? 58  PRO B HG3  1 
ATOM   4407 H HD2  . PRO B 1 72  ? -17.89734 -29.71124 14.32188 1.000 34.85627  ? 58  PRO B HD2  1 
ATOM   4408 H HD3  . PRO B 1 72  ? -17.38276 -30.62623 13.12881 1.000 34.85627  ? 58  PRO B HD3  1 
ATOM   4409 N N    . THR B 1 73  ? -15.00497 -28.40788 16.51694 1.000 31.16355  ? 59  THR B N    1 
ATOM   4410 C CA   . THR B 1 73  ? -14.44453 -27.87581 17.75297 1.000 32.45512  ? 59  THR B CA   1 
ATOM   4411 C C    . THR B 1 73  ? -13.27203 -28.69576 18.27434 1.000 31.67680  ? 59  THR B C    1 
ATOM   4412 O O    . THR B 1 73  ? -12.57212 -28.23323 19.18214 1.000 30.65231  ? 59  THR B O    1 
ATOM   4413 C CB   . THR B 1 73  ? -15.52513 -27.79446 18.83637 1.000 35.85496  ? 59  THR B CB   1 
ATOM   4414 O OG1  . THR B 1 73  ? -15.94216 -29.11408 19.20859 1.000 31.06292  ? 59  THR B OG1  1 
ATOM   4415 C CG2  . THR B 1 73  ? -16.72546 -27.00818 18.33164 1.000 36.50622  ? 59  THR B CG2  1 
ATOM   4416 H H    . THR B 1 73  ? -15.72969 -28.85923 16.62016 1.000 37.45220  ? 59  THR B H    1 
ATOM   4417 H HA   . THR B 1 73  ? -14.12797 -26.97537 17.58004 1.000 39.00209  ? 59  THR B HA   1 
ATOM   4418 H HB   . THR B 1 73  ? -15.16622 -27.34176 19.61557 1.000 43.08189  ? 59  THR B HB   1 
ATOM   4419 H HG1  . THR B 1 73  ? -16.63334 -29.07350 19.68424 1.000 37.33145  ? 59  THR B HG1  1 
ATOM   4420 H HG21 . THR B 1 73  ? -17.26982 -26.71710 19.07987 1.000 43.86341  ? 59  THR B HG21 1 
ATOM   4421 H HG22 . THR B 1 73  ? -16.42737 -26.22873 17.83717 1.000 43.86341  ? 59  THR B HG22 1 
ATOM   4422 H HG23 . THR B 1 73  ? -17.26456 -27.56425 17.74764 1.000 43.86341  ? 59  THR B HG23 1 
ATOM   4423 N N    . LEU B 1 74  ? -13.04020 -29.88898 17.72559 1.000 29.43320  ? 60  LEU B N    1 
ATOM   4424 C CA   . LEU B 1 74  ? -11.93199 -30.73982 18.13574 1.000 27.84737  ? 60  LEU B CA   1 
ATOM   4425 C C    . LEU B 1 74  ? -10.74620 -30.67714 17.18286 1.000 27.08540  ? 60  LEU B C    1 
ATOM   4426 O O    . LEU B 1 74  ? -9.68417  -31.22126 17.50678 1.000 22.68034  ? 60  LEU B O    1 
ATOM   4427 C CB   . LEU B 1 74  ? -12.40096 -32.19600 18.25201 1.000 26.66172  ? 60  LEU B CB   1 
ATOM   4428 C CG   . LEU B 1 74  ? -13.57468 -32.44694 19.19826 1.000 31.64647  ? 60  LEU B CG   1 
ATOM   4429 C CD1  . LEU B 1 74  ? -13.97627 -33.91361 19.17580 1.000 35.91830  ? 60  LEU B CD1  1 
ATOM   4430 C CD2  . LEU B 1 74  ? -13.22471 -32.01484 20.60807 1.000 32.72617  ? 60  LEU B CD2  1 
ATOM   4431 H H    . LEU B 1 74  ? -13.52267 -30.23145 17.10146 1.000 35.37578  ? 60  LEU B H    1 
ATOM   4432 H HA   . LEU B 1 74  ? -11.62790 -30.44979 19.00999 1.000 33.47279  ? 60  LEU B HA   1 
ATOM   4433 H HB2  . LEU B 1 74  ? -12.67241 -32.49776 17.37101 1.000 32.05000  ? 60  LEU B HB2  1 
ATOM   4434 H HB3  . LEU B 1 74  ? -11.65594 -32.72935 18.57042 1.000 32.05000  ? 60  LEU B HB3  1 
ATOM   4435 H HG   . LEU B 1 74  ? -14.33431 -31.92176 18.90154 1.000 38.03170  ? 60  LEU B HG   1 
ATOM   4436 H HD11 . LEU B 1 74  ? -14.25051 -34.15221 18.27648 1.000 43.15790  ? 60  LEU B HD11 1 
ATOM   4437 H HD12 . LEU B 1 74  ? -13.21620 -34.45330 19.44398 1.000 43.15790  ? 60  LEU B HD12 1 
ATOM   4438 H HD13 . LEU B 1 74  ? -14.71228 -34.04899 19.79293 1.000 43.15790  ? 60  LEU B HD13 1 
ATOM   4439 H HD21 . LEU B 1 74  ? -12.37390 -32.40859 20.85702 1.000 39.32735  ? 60  LEU B HD21 1 
ATOM   4440 H HD22 . LEU B 1 74  ? -13.16204 -31.04725 20.63542 1.000 39.32735  ? 60  LEU B HD22 1 
ATOM   4441 H HD23 . LEU B 1 74  ? -13.91942 -32.31855 21.21308 1.000 39.32735  ? 60  LEU B HD23 1 
ATOM   4442 N N    . VAL B 1 75  ? -10.90232 -30.02600 16.02675 1.000 27.14852  ? 61  VAL B N    1 
ATOM   4443 C CA   . VAL B 1 75  ? -9.84733  -30.00205 15.01321 1.000 22.72001  ? 61  VAL B CA   1 
ATOM   4444 C C    . VAL B 1 75  ? -8.53200  -29.52983 15.62016 1.000 26.35793  ? 61  VAL B C    1 
ATOM   4445 O O    . VAL B 1 75  ? -7.51391  -30.23038 15.57025 1.000 27.67542  ? 61  VAL B O    1 
ATOM   4446 C CB   . VAL B 1 75  ? -10.26353 -29.11301 13.82777 1.000 28.97979  ? 61  VAL B CB   1 
ATOM   4447 C CG1  . VAL B 1 75  ? -9.06526  -28.80648 12.93770 1.000 32.42123  ? 61  VAL B CG1  1 
ATOM   4448 C CG2  . VAL B 1 75  ? -11.37093 -29.78482 13.02497 1.000 26.07430  ? 61  VAL B CG2  1 
ATOM   4449 H H    . VAL B 1 75  ? -11.60997 -29.59032 15.80535 1.000 32.63417  ? 61  VAL B H    1 
ATOM   4450 H HA   . VAL B 1 75  ? -9.71532  -30.90590 14.68683 1.000 27.31995  ? 61  VAL B HA   1 
ATOM   4451 H HB   . VAL B 1 75  ? -10.60343 -28.27196 14.17130 1.000 34.83169  ? 61  VAL B HB   1 
ATOM   4452 H HG11 . VAL B 1 75  ? -8.45608  -29.56107 12.95729 1.000 38.96142  ? 61  VAL B HG11 1 
ATOM   4453 H HG12 . VAL B 1 75  ? -9.37565  -28.65538 12.03121 1.000 38.96142  ? 61  VAL B HG12 1 
ATOM   4454 H HG13 . VAL B 1 75  ? -8.61906  -28.01240 13.27122 1.000 38.96142  ? 61  VAL B HG13 1 
ATOM   4455 H HG21 . VAL B 1 75  ? -11.87733 -30.36784 13.61195 1.000 31.34510  ? 61  VAL B HG21 1 
ATOM   4456 H HG22 . VAL B 1 75  ? -11.95208 -29.10170 12.65550 1.000 31.34510  ? 61  VAL B HG22 1 
ATOM   4457 H HG23 . VAL B 1 75  ? -10.97186 -30.30261 12.30835 1.000 31.34510  ? 61  VAL B HG23 1 
ATOM   4458 N N    . THR B 1 76  ? -8.53450  -28.32511 16.19845 1.000 23.86933  ? 62  THR B N    1 
ATOM   4459 C CA   . THR B 1 76  ? -7.29119  -27.75201 16.70494 1.000 25.30635  ? 62  THR B CA   1 
ATOM   4460 C C    . THR B 1 76  ? -6.65970  -28.63472 17.77106 1.000 23.87995  ? 62  THR B C    1 
ATOM   4461 O O    . THR B 1 76  ? -5.43089  -28.67693 17.89394 1.000 26.23424  ? 62  THR B O    1 
ATOM   4462 C CB   . THR B 1 76  ? -7.53973  -26.35031 17.26528 1.000 25.48490  ? 62  THR B CB   1 
ATOM   4463 O OG1  . THR B 1 76  ? -8.49003  -26.41533 18.33703 1.000 26.85729  ? 62  THR B OG1  1 
ATOM   4464 C CG2  . THR B 1 76  ? -8.06147  -25.42037 16.17268 1.000 28.25760  ? 62  THR B CG2  1 
ATOM   4465 H H    . THR B 1 76  ? -9.22973  -27.83062 16.30674 1.000 28.69913  ? 62  THR B H    1 
ATOM   4466 H HA   . THR B 1 76  ? -6.66731  -27.67380 15.96632 1.000 30.42356  ? 62  THR B HA   1 
ATOM   4467 H HB   . THR B 1 76  ? -6.70615  -25.98602 17.60192 1.000 30.63782  ? 62  THR B HB   1 
ATOM   4468 H HG1  . THR B 1 76  ? -8.16991  -26.85281 18.97869 1.000 32.28468  ? 62  THR B HG1  1 
ATOM   4469 H HG21 . THR B 1 76  ? -7.44657  -25.41209 15.42253 1.000 33.96506  ? 62  THR B HG21 1 
ATOM   4470 H HG22 . THR B 1 76  ? -8.92957  -25.72450 15.86479 1.000 33.96506  ? 62  THR B HG22 1 
ATOM   4471 H HG23 . THR B 1 76  ? -8.14840  -24.51826 16.51844 1.000 33.96506  ? 62  THR B HG23 1 
ATOM   4472 N N    . THR B 1 77  ? -7.47628  -29.34391 18.54884 1.000 25.05945  ? 63  THR B N    1 
ATOM   4473 C CA   . THR B 1 77  ? -6.93532  -30.22699 19.57472 1.000 26.38175  ? 63  THR B CA   1 
ATOM   4474 C C    . THR B 1 77  ? -6.35781  -31.49252 18.95196 1.000 29.55766  ? 63  THR B C    1 
ATOM   4475 O O    . THR B 1 77  ? -5.24976  -31.92097 19.29662 1.000 26.14021  ? 63  THR B O    1 
ATOM   4476 C CB   . THR B 1 77  ? -8.02924  -30.56584 20.58688 1.000 26.64572  ? 63  THR B CB   1 
ATOM   4477 O OG1  . THR B 1 77  ? -8.50348  -29.36046 21.20027 1.000 21.51180  ? 63  THR B OG1  1 
ATOM   4478 C CG2  . THR B 1 77  ? -7.50047  -31.49960 21.65345 1.000 27.58212  ? 63  THR B CG2  1 
ATOM   4479 H H    . THR B 1 77  ? -8.33495  -29.33120 18.50273 1.000 30.12728  ? 63  THR B H    1 
ATOM   4480 H HA   . THR B 1 77  ? -6.21887  -29.77305 20.04541 1.000 31.71404  ? 63  THR B HA   1 
ATOM   4481 H HB   . THR B 1 77  ? -8.76318  -31.00917 20.13335 1.000 32.03081  ? 63  THR B HB   1 
ATOM   4482 H HG1  . THR B 1 77  ? -7.88399  -28.99662 21.63552 1.000 25.87010  ? 63  THR B HG1  1 
ATOM   4483 H HG21 . THR B 1 77  ? -6.65590  -31.16758 21.99603 1.000 33.15448  ? 63  THR B HG21 1 
ATOM   4484 H HG22 . THR B 1 77  ? -8.13464  -31.56080 22.38488 1.000 33.15448  ? 63  THR B HG22 1 
ATOM   4485 H HG23 . THR B 1 77  ? -7.36304  -32.38466 21.28108 1.000 33.15448  ? 63  THR B HG23 1 
ATOM   4486 N N    . LEU B 1 78  ? -7.09047  -32.09700 18.02593 1.000 27.28994  ? 64  LEU B N    1 
ATOM   4487 C CA   . LEU B 1 78  ? -6.63623  -33.30538 17.35690 1.000 26.90210  ? 64  LEU B CA   1 
ATOM   4488 C C    . LEU B 1 78  ? -5.42994  -33.01263 16.46967 1.000 32.77862  ? 64  LEU B C    1 
ATOM   4489 O O    . LEU B 1 78  ? -4.54112  -33.85090 16.31241 1.000 30.20189  ? 64  LEU B O    1 
ATOM   4490 C CB   . LEU B 1 78  ? -7.77186  -33.89964 16.52923 1.000 26.31515  ? 64  LEU B CB   1 
ATOM   4491 C CG   . LEU B 1 78  ? -8.97712  -34.39764 17.32684 1.000 23.90884  ? 64  LEU B CG   1 
ATOM   4492 C CD1  . LEU B 1 78  ? -10.16549 -34.61394 16.41053 1.000 25.89363  ? 64  LEU B CD1  1 
ATOM   4493 C CD2  . LEU B 1 78  ? -8.63203  -35.67971 18.06655 1.000 32.50932  ? 64  LEU B CD2  1 
ATOM   4494 H H    . LEU B 1 78  ? -7.86287  -31.82328 17.76502 1.000 32.80387  ? 64  LEU B H    1 
ATOM   4495 H HA   . LEU B 1 78  ? -6.36661  -33.96205 18.01795 1.000 32.33846  ? 64  LEU B HA   1 
ATOM   4496 H HB2  . LEU B 1 78  ? -8.09141  -33.21813 15.91740 1.000 31.63412  ? 64  LEU B HB2  1 
ATOM   4497 H HB3  . LEU B 1 78  ? -7.42239  -34.65510 16.03118 1.000 31.63412  ? 64  LEU B HB3  1 
ATOM   4498 H HG   . LEU B 1 78  ? -9.22153  -33.72760 17.98427 1.000 28.74654  ? 64  LEU B HG   1 
ATOM   4499 H HD11 . LEU B 1 78  ? -10.43308 -33.76111 16.03372 1.000 31.12829  ? 64  LEU B HD11 1 
ATOM   4500 H HD12 . LEU B 1 78  ? -9.91007  -35.22366 15.70067 1.000 31.12829  ? 64  LEU B HD12 1 
ATOM   4501 H HD13 . LEU B 1 78  ? -10.89593 -34.99221 16.92461 1.000 31.12829  ? 64  LEU B HD13 1 
ATOM   4502 H HD21 . LEU B 1 78  ? -8.10808  -36.25003 17.48250 1.000 39.06713  ? 64  LEU B HD21 1 
ATOM   4503 H HD22 . LEU B 1 78  ? -8.11941  -35.45846 18.85974 1.000 39.06713  ? 64  LEU B HD22 1 
ATOM   4504 H HD23 . LEU B 1 78  ? -9.45351  -36.12983 18.31850 1.000 39.06713  ? 64  LEU B HD23 1 
HETATM 4505 C CD2  . SWG B 1 79  ? -5.32601  -24.74897 13.63268 1.000 33.61304  ? 65  SWG B CD2  1 
HETATM 4506 C CE3  . SWG B 1 79  ? -4.87987  -23.52069 14.14554 1.000 30.10057  ? 65  SWG B CE3  1 
HETATM 4507 C CZ3  . SWG B 1 79  ? -5.41729  -22.33601 13.67972 1.000 35.80660  ? 65  SWG B CZ3  1 
HETATM 4508 C CH2  . SWG B 1 79  ? -6.39250  -22.39160 12.71481 1.000 37.04007  ? 65  SWG B CH2  1 
HETATM 4509 C CZ2  . SWG B 1 79  ? -6.87417  -23.59206 12.17163 1.000 36.50400  ? 65  SWG B CZ2  1 
HETATM 4510 C CE2  . SWG B 1 79  ? -6.31492  -24.76528 12.65675 1.000 34.49151  ? 65  SWG B CE2  1 
HETATM 4511 N NE1  . SWG B 1 79  ? -6.60296  -26.08551 12.29778 1.000 37.83564  ? 65  SWG B NE1  1 
HETATM 4512 C CD1  . SWG B 1 79  ? -5.77959  -26.88397 13.06114 1.000 31.40280  ? 65  SWG B CD1  1 
HETATM 4513 C CG   . SWG B 1 79  ? -4.97885  -26.15434 13.89351 1.000 31.48829  ? 65  SWG B CG   1 
HETATM 4514 C CB2  . SWG B 1 79  ? -3.95187  -26.61458 14.88142 1.000 30.01780  ? 65  SWG B CB2  1 
HETATM 4515 C CA2  . SWG B 1 79  ? -3.79422  -27.94077 15.21120 1.000 31.23343  ? 65  SWG B CA2  1 
HETATM 4516 N N2   . SWG B 1 79  ? -4.35323  -29.01892 14.56040 1.000 29.05190  ? 65  SWG B N2   1 
HETATM 4517 C C2   . SWG B 1 79  ? -3.00763  -28.48090 16.31280 1.000 29.73844  ? 65  SWG B C2   1 
HETATM 4518 O O2   . SWG B 1 79  ? -2.32701  -27.90246 17.17609 1.000 28.14426  ? 65  SWG B O2   1 
HETATM 4519 N N3   . SWG B 1 79  ? -3.15658  -29.81980 16.23775 1.000 27.88468  ? 65  SWG B N3   1 
HETATM 4520 C CA3  . SWG B 1 79  ? -2.54298  -30.73390 17.14389 1.000 25.43790  ? 65  SWG B CA3  1 
HETATM 4521 C C3   . SWG B 1 79  ? -1.13329  -31.15872 17.06494 1.000 23.48144  ? 65  SWG B C3   1 
HETATM 4522 O O3   . SWG B 1 79  ? -0.58792  -31.65349 18.06390 1.000 24.39381  ? 65  SWG B O3   1 
HETATM 4523 C C1   . SWG B 1 79  ? -3.94385  -30.13450 15.20859 1.000 27.04936  ? 65  SWG B C1   1 
HETATM 4524 C CA1  . SWG B 1 79  ? -4.36619  -31.51193 14.77402 1.000 25.25100  ? 65  SWG B CA1  1 
HETATM 4525 N N1   . SWG B 1 79  ? -5.47927  -31.81482 15.69072 1.000 21.41536  ? 65  SWG B N1   1 
HETATM 4526 C CB1  . SWG B 1 79  ? -4.95755  -31.61791 13.35426 1.000 32.81114  ? 65  SWG B CB1  1 
HETATM 4527 O OG1  . SWG B 1 79  ? -3.89289  -31.40966 12.41385 1.000 29.97906  ? 65  SWG B OG1  1 
ATOM   4528 N N    . VAL B 1 80  ? -0.76155  -31.39800 15.70530 1.000 22.53366  ? 66  VAL B N    1 
ATOM   4529 C CA   . VAL B 1 80  ? 0.60340   -31.81015 15.40412 1.000 24.58367  ? 66  VAL B CA   1 
ATOM   4530 C C    . VAL B 1 80  ? 1.29959   -30.73273 14.58012 1.000 24.73219  ? 66  VAL B C    1 
ATOM   4531 O O    . VAL B 1 80  ? 1.59298   -30.92681 13.40056 1.000 24.02834  ? 66  VAL B O    1 
ATOM   4532 C CB   . VAL B 1 80  ? 0.62365   -33.16206 14.67452 1.000 26.58687  ? 66  VAL B CB   1 
ATOM   4533 C CG1  . VAL B 1 80  ? 0.32081   -34.29628 15.64807 1.000 26.33128  ? 66  VAL B CG1  1 
ATOM   4534 C CG2  . VAL B 1 80  ? -0.37155  -33.15955 13.52131 1.000 24.92942  ? 66  VAL B CG2  1 
ATOM   4535 H HA   . VAL B 1 80  ? 1.09302   -31.92035 16.23420 1.000 29.55634  ? 66  VAL B HA   1 
ATOM   4536 H HB   . VAL B 1 80  ? 1.50905   -33.30932 14.30671 1.000 31.96019  ? 66  VAL B HB   1 
ATOM   4537 H HG11 . VAL B 1 80  ? 0.93087   -34.23840 16.39999 1.000 31.65348  ? 66  VAL B HG11 1 
ATOM   4538 H HG12 . VAL B 1 80  ? -0.59455  -34.21095 15.95745 1.000 31.65348  ? 66  VAL B HG12 1 
ATOM   4539 H HG13 . VAL B 1 80  ? 0.43800   -35.14406 15.19153 1.000 31.65348  ? 66  VAL B HG13 1 
ATOM   4540 H HG21 . VAL B 1 80  ? -0.46727  -32.25339 13.18874 1.000 29.97124  ? 66  VAL B HG21 1 
ATOM   4541 H HG22 . VAL B 1 80  ? -0.03954  -33.73728 12.81640 1.000 29.97124  ? 66  VAL B HG22 1 
ATOM   4542 H HG23 . VAL B 1 80  ? -1.22683  -33.48644 13.84156 1.000 29.97124  ? 66  VAL B HG23 1 
ATOM   4543 N N    . GLN B 1 81  ? 1.56415   -29.59262 15.21840 1.000 24.95408  ? 67  GLN B N    1 
ATOM   4544 C CA   . GLN B 1 81  ? 2.18772   -28.45850 14.54783 1.000 29.72552  ? 67  GLN B CA   1 
ATOM   4545 C C    . GLN B 1 81  ? 3.65089   -28.70212 14.20479 1.000 29.01063  ? 67  GLN B C    1 
ATOM   4546 O O    . GLN B 1 81  ? 4.26668   -27.84292 13.56343 1.000 26.71903  ? 67  GLN B O    1 
ATOM   4547 C CB   . GLN B 1 81  ? 2.03992   -27.20927 15.41930 1.000 27.17749  ? 67  GLN B CB   1 
ATOM   4548 C CG   . GLN B 1 81  ? 0.59402   -26.74325 15.53814 1.000 30.92275  ? 67  GLN B CG   1 
ATOM   4549 C CD   . GLN B 1 81  ? 0.41423   -25.61639 16.52866 1.000 27.06053  ? 67  GLN B CD   1 
ATOM   4550 O OE1  . GLN B 1 81  ? 1.21831   -25.44459 17.44348 1.000 35.14633  ? 67  GLN B OE1  1 
ATOM   4551 N NE2  . GLN B 1 81  ? -0.64839  -24.83913 16.35283 1.000 32.76249  ? 67  GLN B NE2  1 
ATOM   4552 H H    . GLN B 1 81  ? 1.38947   -29.45167 16.04860 1.000 30.00083  ? 67  GLN B H    1 
ATOM   4553 H HA   . GLN B 1 81  ? 1.72692   -28.29103 13.71086 1.000 35.72656  ? 67  GLN B HA   1 
ATOM   4554 H HB2  . GLN B 1 81  ? 2.36676   -27.40578 16.31118 1.000 32.66893  ? 67  GLN B HB2  1 
ATOM   4555 H HB3  . GLN B 1 81  ? 2.55709   -26.48801 15.02787 1.000 32.66893  ? 67  GLN B HB3  1 
ATOM   4556 H HG2  . GLN B 1 81  ? 0.29201   -26.42978 14.67128 1.000 37.16324  ? 67  GLN B HG2  1 
ATOM   4557 H HG3  . GLN B 1 81  ? 0.04615   -27.48827 15.83084 1.000 37.16324  ? 67  GLN B HG3  1 
ATOM   4558 H HE21 . GLN B 1 81  ? -1.18937  -24.99119 15.70182 1.000 39.37092  ? 67  GLN B HE21 1 
ATOM   4559 H HE22 . GLN B 1 81  ? -0.79542  -24.18381 16.88999 1.000 39.37092  ? 67  GLN B HE22 1 
ATOM   4560 N N    . CYS B 1 82  ? 4.21685   -29.84600 14.59386 1.000 29.51312  ? 68  CYS B N    1 
ATOM   4561 C CA   . CYS B 1 82  ? 5.55100   -30.21506 14.14016 1.000 24.81743  ? 68  CYS B CA   1 
ATOM   4562 C C    . CYS B 1 82  ? 5.59417   -30.52307 12.64935 1.000 29.39840  ? 68  CYS B C    1 
ATOM   4563 O O    . CYS B 1 82  ? 6.68796   -30.69798 12.10040 1.000 27.89889  ? 68  CYS B O    1 
ATOM   4564 C CB   . CYS B 1 82  ? 6.05244   -31.41766 14.93847 1.000 26.69676  ? 68  CYS B CB   1 
ATOM   4565 S SG   . CYS B 1 82  ? 4.86781   -32.78005 15.05139 1.000 24.84071  ? 68  CYS B SG   1 
ATOM   4566 H H    . CYS B 1 82  ? 3.84850   -30.42029 15.11741 1.000 35.47169  ? 68  CYS B H    1 
ATOM   4567 H HA   . CYS B 1 82  ? 6.15768   -29.47637 14.30500 1.000 29.83685  ? 68  CYS B HA   1 
ATOM   4568 H HB2  . CYS B 1 82  ? 6.85428   -31.75952 14.51294 1.000 32.09205  ? 68  CYS B HB2  1 
ATOM   4569 H HB3  . CYS B 1 82  ? 6.25419   -31.12759 15.84183 1.000 32.09205  ? 68  CYS B HB3  1 
ATOM   4570 H HG   . CYS B 1 82  ? 5.38434   -33.70061 15.62215 1.000 29.86479  ? 68  CYS B HG   1 
ATOM   4571 N N    . PHE B 1 83  ? 4.44286   -30.58619 11.98353 1.000 28.61438  ? 69  PHE B N    1 
ATOM   4572 C CA   . PHE B 1 83  ? 4.38231   -30.82991 10.55047 1.000 30.41365  ? 69  PHE B CA   1 
ATOM   4573 C C    . PHE B 1 83  ? 4.19388   -29.55400 9.74302  1.000 28.16384  ? 69  PHE B C    1 
ATOM   4574 O O    . PHE B 1 83  ? 4.02633   -29.62790 8.52357  1.000 28.77131  ? 69  PHE B O    1 
ATOM   4575 C CB   . PHE B 1 83  ? 3.25778   -31.81589 10.23222 1.000 25.53005  ? 69  PHE B CB   1 
ATOM   4576 C CG   . PHE B 1 83  ? 3.54435   -33.21366 10.68226 1.000 26.50568  ? 69  PHE B CG   1 
ATOM   4577 C CD1  . PHE B 1 83  ? 4.38098   -34.03079 9.94239  1.000 28.98295  ? 69  PHE B CD1  1 
ATOM   4578 C CD2  . PHE B 1 83  ? 2.98715   -33.71096 11.84830 1.000 28.23307  ? 69  PHE B CD2  1 
ATOM   4579 C CE1  . PHE B 1 83  ? 4.65507   -35.31901 10.35385 1.000 29.93089  ? 69  PHE B CE1  1 
ATOM   4580 C CE2  . PHE B 1 83  ? 3.25736   -35.00073 12.26685 1.000 23.88972  ? 69  PHE B CE2  1 
ATOM   4581 C CZ   . PHE B 1 83  ? 4.09099   -35.80561 11.51911 1.000 30.49741  ? 69  PHE B CZ   1 
ATOM   4582 H H    . PHE B 1 83  ? 3.67089   -30.48876 12.34981 1.000 34.39319  ? 69  PHE B H    1 
ATOM   4583 H HA   . PHE B 1 83  ? 5.22112   -31.23154 10.27480 1.000 36.55232  ? 69  PHE B HA   1 
ATOM   4584 H HB2  . PHE B 1 83  ? 2.44782   -31.52078 10.67692 1.000 30.69200  ? 69  PHE B HB2  1 
ATOM   4585 H HB3  . PHE B 1 83  ? 3.12097   -31.83507 9.27211  1.000 30.69200  ? 69  PHE B HB3  1 
ATOM   4586 H HD1  . PHE B 1 83  ? 4.76308   -33.70780 9.15844  1.000 34.83548  ? 69  PHE B HD1  1 
ATOM   4587 H HD2  . PHE B 1 83  ? 2.42479   -33.17130 12.35567 1.000 33.93563  ? 69  PHE B HD2  1 
ATOM   4588 H HE1  . PHE B 1 83  ? 5.21838   -35.85936 9.84828  1.000 35.97301  ? 69  PHE B HE1  1 
ATOM   4589 H HE2  . PHE B 1 83  ? 2.87754   -35.32497 13.05139 1.000 28.72361  ? 69  PHE B HE2  1 
ATOM   4590 H HZ   . PHE B 1 83  ? 4.27348   -36.67388 11.79788 1.000 36.65283  ? 69  PHE B HZ   1 
ATOM   4591 N N    . ALA B 1 84  ? 4.21320   -28.39191 10.38876 1.000 27.33910  ? 70  ALA B N    1 
ATOM   4592 C CA   . ALA B 1 84  ? 4.15553   -27.13796 9.65464  1.000 27.70534  ? 70  ALA B CA   1 
ATOM   4593 C C    . ALA B 1 84  ? 5.35963   -27.01934 8.73056  1.000 31.40737  ? 70  ALA B C    1 
ATOM   4594 O O    . ALA B 1 84  ? 6.46357   -27.46165 9.06050  1.000 34.26472  ? 70  ALA B O    1 
ATOM   4595 C CB   . ALA B 1 84  ? 4.11835   -25.95936 10.62526 1.000 31.55781  ? 70  ALA B CB   1 
ATOM   4596 H H    . ALA B 1 84  ? 4.25886   -28.30489 11.24313 1.000 32.86286  ? 70  ALA B H    1 
ATOM   4597 H HA   . ALA B 1 84  ? 3.34829   -27.11011 9.11753  1.000 33.30235  ? 70  ALA B HA   1 
ATOM   4598 H HB1  . ALA B 1 84  ? 4.92459   -25.96879 11.16451 1.000 37.92531  ? 70  ALA B HB1  1 
ATOM   4599 H HB2  . ALA B 1 84  ? 4.06928   -25.13398 10.11807 1.000 37.92531  ? 70  ALA B HB2  1 
ATOM   4600 H HB3  . ALA B 1 84  ? 3.33812   -26.04419 11.19530 1.000 37.92531  ? 70  ALA B HB3  1 
ATOM   4601 N N    . ARG B 1 85  ? 5.14019   -26.43249 7.55822  1.000 29.94355  ? 71  ARG B N    1 
ATOM   4602 C CA   . ARG B 1 85  ? 6.23281   -26.14037 6.63785  1.000 32.98194  ? 71  ARG B CA   1 
ATOM   4603 C C    . ARG B 1 85  ? 6.92183   -24.86168 7.09885  1.000 29.67423  ? 71  ARG B C    1 
ATOM   4604 O O    . ARG B 1 85  ? 6.33223   -23.77744 7.04870  1.000 32.40730  ? 71  ARG B O    1 
ATOM   4605 C CB   . ARG B 1 85  ? 5.71782   -25.99945 5.20829  1.000 34.91277  ? 71  ARG B CB   1 
ATOM   4606 C CG   . ARG B 1 85  ? 6.80193   -25.62525 4.19922  1.000 41.26186  ? 71  ARG B CG   1 
ATOM   4607 C CD   . ARG B 1 85  ? 6.25542   -25.52471 2.78109  1.000 44.73515  ? 71  ARG B CD   1 
ATOM   4608 N NE   . ARG B 1 85  ? 5.80872   -24.17595 2.45351  1.000 51.31625  ? 71  ARG B NE   1 
ATOM   4609 C CZ   . ARG B 1 85  ? 6.59802   -23.21539 1.98950  1.000 59.41911  ? 71  ARG B CZ   1 
ATOM   4610 N NH1  . ARG B 1 85  ? 7.89266   -23.41469 1.79683  1.000 46.69783  ? 71  ARG B NH1  1 
ATOM   4611 N NH2  . ARG B 1 85  ? 6.07573   -22.02358 1.71366  1.000 63.86783  ? 71  ARG B NH2  1 
ATOM   4612 H H    . ARG B 1 85  ? 4.36513   -26.19326 7.27246  1.000 35.98820  ? 71  ARG B H    1 
ATOM   4613 H HA   . ARG B 1 85  ? 6.87178   -26.86999 6.65427  1.000 39.63427  ? 71  ARG B HA   1 
ATOM   4614 H HB2  . ARG B 1 85  ? 5.33347   -26.84555 4.93028  1.000 41.95127  ? 71  ARG B HB2  1 
ATOM   4615 H HB3  . ARG B 1 85  ? 5.04107   -25.30485 5.18748  1.000 41.95127  ? 71  ARG B HB3  1 
ATOM   4616 H HG2  . ARG B 1 85  ? 7.17813   -24.76417 4.43988  1.000 49.57018  ? 71  ARG B HG2  1 
ATOM   4617 H HG3  . ARG B 1 85  ? 7.49459   -26.30425 4.20875  1.000 49.57018  ? 71  ARG B HG3  1 
ATOM   4618 H HD2  . ARG B 1 85  ? 6.95242   -25.77223 2.15353  1.000 53.73812  ? 71  ARG B HD2  1 
ATOM   4619 H HD3  . ARG B 1 85  ? 5.49811   -26.12382 2.68906  1.000 53.73812  ? 71  ARG B HD3  1 
ATOM   4620 H HE   . ARG B 1 85  ? 4.97697   -23.99026 2.56889  1.000 61.63544  ? 71  ARG B HE   1 
ATOM   4621 H HH11 . ARG B 1 85  ? 8.24070   -24.18106 1.97331  1.000 56.09334  ? 71  ARG B HH11 1 
ATOM   4622 H HH12 . ARG B 1 85  ? 8.38556   -22.77777 1.49519  1.000 56.09334  ? 71  ARG B HH12 1 
ATOM   4623 H HH21 . ARG B 1 85  ? 5.23621   -21.88314 1.83651  1.000 76.69734  ? 71  ARG B HH21 1 
ATOM   4624 H HH22 . ARG B 1 85  ? 6.57755   -21.39347 1.41245  1.000 76.69734  ? 71  ARG B HH22 1 
ATOM   4625 N N    . TYR B 1 86  ? 8.16503   -24.98722 7.56014  1.000 34.38947  ? 72  TYR B N    1 
ATOM   4626 C CA   . TYR B 1 86  ? 8.97780   -23.82957 7.90170  1.000 33.47002  ? 72  TYR B CA   1 
ATOM   4627 C C    . TYR B 1 86  ? 9.93272   -23.54025 6.75725  1.000 34.28455  ? 72  TYR B C    1 
ATOM   4628 O O    . TYR B 1 86  ? 10.76719  -24.40065 6.43560  1.000 37.29794  ? 72  TYR B O    1 
ATOM   4629 C CB   . TYR B 1 86  ? 9.75678   -24.07846 9.18899  1.000 31.98672  ? 72  TYR B CB   1 
ATOM   4630 C CG   . TYR B 1 86  ? 8.97852   -23.76002 10.44664 1.000 29.20642  ? 72  TYR B CG   1 
ATOM   4631 C CD1  . TYR B 1 86  ? 7.95902   -24.59345 10.88595 1.000 29.33297  ? 72  TYR B CD1  1 
ATOM   4632 C CD2  . TYR B 1 86  ? 9.26814   -22.62662 11.19754 1.000 29.84672  ? 72  TYR B CD2  1 
ATOM   4633 C CE1  . TYR B 1 86  ? 7.24589   -24.30564 12.03471 1.000 29.80010  ? 72  TYR B CE1  1 
ATOM   4634 C CE2  . TYR B 1 86  ? 8.56122   -22.33041 12.34559 1.000 28.15871  ? 72  TYR B CE2  1 
ATOM   4635 C CZ   . TYR B 1 86  ? 7.55165   -23.17372 12.76037 1.000 30.85647  ? 72  TYR B CZ   1 
ATOM   4636 O OH   . TYR B 1 86  ? 6.84608   -22.88424 13.90489 1.000 27.82306  ? 72  TYR B OH   1 
ATOM   4637 H H    . TYR B 1 86  ? 8.56124   -25.74037 7.68416  1.000 41.32331  ? 72  TYR B H    1 
ATOM   4638 H HA   . TYR B 1 86  ? 8.40594   -23.05793 8.03752  1.000 40.21996  ? 72  TYR B HA   1 
ATOM   4639 H HB2  . TYR B 1 86  ? 10.00713  -25.01489 9.22540  1.000 38.44001  ? 72  TYR B HB2  1 
ATOM   4640 H HB3  . TYR B 1 86  ? 10.55162  -23.52249 9.18446  1.000 38.44001  ? 72  TYR B HB3  1 
ATOM   4641 H HD1  . TYR B 1 86  ? 7.75223   -25.35843 10.39917 1.000 35.25550  ? 72  TYR B HD1  1 
ATOM   4642 H HD2  . TYR B 1 86  ? 9.95023   -22.05786 10.92157 1.000 35.87201  ? 72  TYR B HD2  1 
ATOM   4643 H HE1  . TYR B 1 86  ? 6.56411   -24.87198 12.31638 1.000 35.81606  ? 72  TYR B HE1  1 
ATOM   4644 H HE2  . TYR B 1 86  ? 8.76440   -21.56700 12.83632 1.000 33.84639  ? 72  TYR B HE2  1 
ATOM   4645 H HH   . TYR B 1 86  ? 7.20208   -22.23779 14.30609 1.000 33.44361  ? 72  TYR B HH   1 
ATOM   4646 N N    . PRO B 1 87  ? 9.85057   -22.38078 6.10509  1.000 39.38077  ? 73  PRO B N    1 
ATOM   4647 C CA   . PRO B 1 87  ? 10.81667  -22.06907 5.04785  1.000 41.58671  ? 73  PRO B CA   1 
ATOM   4648 C C    . PRO B 1 87  ? 12.24577  -22.12265 5.56586  1.000 43.90245  ? 73  PRO B C    1 
ATOM   4649 O O    . PRO B 1 87  ? 12.50399  -22.09149 6.77097  1.000 42.95545  ? 73  PRO B O    1 
ATOM   4650 C CB   . PRO B 1 87  ? 10.42783  -20.65038 4.61620  1.000 43.67781  ? 73  PRO B CB   1 
ATOM   4651 C CG   . PRO B 1 87  ? 8.98371   -20.54132 4.96305  1.000 41.77157  ? 73  PRO B CG   1 
ATOM   4652 C CD   . PRO B 1 87  ? 8.81394   -21.33930 6.22254  1.000 39.34871  ? 73  PRO B CD   1 
ATOM   4653 H HA   . PRO B 1 87  ? 10.71897  -22.67653 4.29795  1.000 49.95999  ? 73  PRO B HA   1 
ATOM   4654 H HB2  . PRO B 1 87  ? 10.95458  -19.99808 5.10399  1.000 52.46931  ? 73  PRO B HB2  1 
ATOM   4655 H HB3  . PRO B 1 87  ? 10.56717  -20.54291 3.66230  1.000 52.46931  ? 73  PRO B HB3  1 
ATOM   4656 H HG2  . PRO B 1 87  ? 8.75006   -19.61136 5.10965  1.000 50.18182  ? 73  PRO B HG2  1 
ATOM   4657 H HG3  . PRO B 1 87  ? 8.44453   -20.90977 4.24582  1.000 50.18182  ? 73  PRO B HG3  1 
ATOM   4658 H HD2  . PRO B 1 87  ? 8.96676   -20.78656 7.00486  1.000 47.27439  ? 73  PRO B HD2  1 
ATOM   4659 H HD3  . PRO B 1 87  ? 7.92948   -21.73544 6.26385  1.000 47.27439  ? 73  PRO B HD3  1 
ATOM   4660 N N    . ASP B 1 88  ? 13.18523  -22.20110 4.62064  1.000 57.37173  ? 74  ASP B N    1 
ATOM   4661 C CA   . ASP B 1 88  ? 14.59456  -22.34188 4.97360  1.000 57.54803  ? 74  ASP B CA   1 
ATOM   4662 C C    . ASP B 1 88  ? 15.04534  -21.24348 5.92963  1.000 52.07224  ? 74  ASP B C    1 
ATOM   4663 O O    . ASP B 1 88  ? 15.70879  -21.51434 6.93668  1.000 49.05433  ? 74  ASP B O    1 
ATOM   4664 C CB   . ASP B 1 88  ? 15.45026  -22.33363 3.70518  1.000 63.04983  ? 74  ASP B CB   1 
ATOM   4665 C CG   . ASP B 1 88  ? 15.37176  -23.64125 2.94041  1.000 80.27797  ? 74  ASP B CG   1 
ATOM   4666 O OD1  . ASP B 1 88  ? 14.75427  -24.59826 3.45570  1.000 71.83009  ? 74  ASP B OD1  1 
ATOM   4667 O OD2  . ASP B 1 88  ? 15.92914  -23.71207 1.82419  1.000 79.93693  ? 74  ASP B OD2  1 
ATOM   4668 H H    . ASP B 1 88  ? 13.03245  -22.17530 3.77471  1.000 68.90201  ? 74  ASP B H    1 
ATOM   4669 H HA   . ASP B 1 88  ? 14.71768  -23.19365 5.42107  1.000 69.11358  ? 74  ASP B HA   1 
ATOM   4670 H HB2  . ASP B 1 88  ? 15.14211  -21.62414 3.11989  1.000 75.71574  ? 74  ASP B HB2  1 
ATOM   4671 H HB3  . ASP B 1 88  ? 16.37694  -22.18335 3.94929  1.000 75.71574  ? 74  ASP B HB3  1 
ATOM   4672 N N    . HIS B 1 89  ? 14.69204  -19.99222 5.63224  1.000 52.72145  ? 75  HIS B N    1 
ATOM   4673 C CA   . HIS B 1 89  ? 15.15825  -18.88063 6.45169  1.000 55.82878  ? 75  HIS B CA   1 
ATOM   4674 C C    . HIS B 1 89  ? 14.49735  -18.83660 7.82319  1.000 51.98096  ? 75  HIS B C    1 
ATOM   4675 O O    . HIS B 1 89  ? 14.91638  -18.03298 8.66293  1.000 53.26540  ? 75  HIS B O    1 
ATOM   4676 C CB   . HIS B 1 89  ? 14.92024  -17.55477 5.72503  1.000 59.62643  ? 75  HIS B CB   1 
ATOM   4677 C CG   . HIS B 1 89  ? 13.49336  -17.10249 5.74060  1.000 63.66543  ? 75  HIS B CG   1 
ATOM   4678 N ND1  . HIS B 1 89  ? 12.53019  -17.64756 4.91906  1.000 67.18692  ? 75  HIS B ND1  1 
ATOM   4679 C CD2  . HIS B 1 89  ? 12.86763  -16.15180 6.47449  1.000 60.13039  ? 75  HIS B CD2  1 
ATOM   4680 C CE1  . HIS B 1 89  ? 11.37195  -17.05474 5.14845  1.000 66.40102  ? 75  HIS B CE1  1 
ATOM   4681 N NE2  . HIS B 1 89  ? 11.54947  -16.14286 6.08748  1.000 63.01085  ? 75  HIS B NE2  1 
ATOM   4682 H H    . HIS B 1 89  ? 14.19080  -19.76663 4.97082  1.000 63.32168  ? 75  HIS B H    1 
ATOM   4683 H HA   . HIS B 1 89  ? 16.11357  -18.98100 6.58659  1.000 67.05047  ? 75  HIS B HA   1 
ATOM   4684 H HB2  . HIS B 1 89  ? 15.45326  -16.86579 6.15175  1.000 71.60766  ? 75  HIS B HB2  1 
ATOM   4685 H HB3  . HIS B 1 89  ? 15.18828  -17.65518 4.79822  1.000 71.60766  ? 75  HIS B HB3  1 
ATOM   4686 H HD2  . HIS B 1 89  ? 13.25728  -15.60699 7.11966  1.000 72.21240  ? 75  HIS B HD2  1 
ATOM   4687 H HE1  . HIS B 1 89  ? 10.56841  -17.24679 4.72145  1.000 79.73716  ? 75  HIS B HE1  1 
ATOM   4688 H HE2  . HIS B 1 89  ? 10.93889  -15.62718 6.40509  1.000 75.66896  ? 75  HIS B HE2  1 
ATOM   4689 N N    . MET B 1 90  ? 13.48893  -19.67218 8.07338  1.000 46.57389  ? 76  MET B N    1 
ATOM   4690 C CA   . MET B 1 90  ? 12.80401  -19.71058 9.35874  1.000 42.91529  ? 76  MET B CA   1 
ATOM   4691 C C    . MET B 1 90  ? 13.07723  -20.99183 10.13673 1.000 43.71658  ? 76  MET B C    1 
ATOM   4692 O O    . MET B 1 90  ? 12.46315  -21.20766 11.18752 1.000 40.43715  ? 76  MET B O    1 
ATOM   4693 C CB   . MET B 1 90  ? 11.29560  -19.55101 9.15842  1.000 42.93408  ? 76  MET B CB   1 
ATOM   4694 C CG   . MET B 1 90  ? 10.87060  -18.18386 8.66431  1.000 42.71667  ? 76  MET B CG   1 
ATOM   4695 S SD   . MET B 1 90  ? 9.07801   -18.02570 8.55094  1.000 41.59112  ? 76  MET B SD   1 
ATOM   4696 C CE   . MET B 1 90  ? 8.59824   -18.28128 10.26027 1.000 33.01814  ? 76  MET B CE   1 
ATOM   4697 H H    . MET B 1 90  ? 13.18008  -20.23560 7.50174  1.000 55.94461  ? 76  MET B H    1 
ATOM   4698 H HA   . MET B 1 90  ? 13.12157  -18.95886 9.88312  1.000 51.55428  ? 76  MET B HA   1 
ATOM   4699 H HB2  . MET B 1 90  ? 10.99966  -20.20405 8.50507  1.000 51.57684  ? 76  MET B HB2  1 
ATOM   4700 H HB3  . MET B 1 90  ? 10.85277  -19.70680 10.00726 1.000 51.57684  ? 76  MET B HB3  1 
ATOM   4701 H HG2  . MET B 1 90  ? 11.19517  -17.50817 9.27994  1.000 51.31594  ? 76  MET B HG2  1 
ATOM   4702 H HG3  . MET B 1 90  ? 11.24349  -18.03476 7.78135  1.000 51.31594  ? 76  MET B HG3  1 
ATOM   4703 H HE1  . MET B 1 90  ? 8.69837   -19.22092 10.47926 1.000 39.34207  ? 76  MET B HE1  1 
ATOM   4704 H HE2  . MET B 1 90  ? 9.16992   -17.74560 10.83221 1.000 39.34207  ? 76  MET B HE2  1 
ATOM   4705 H HE3  . MET B 1 90  ? 7.67302   -18.01233 10.37218 1.000 39.34207  ? 76  MET B HE3  1 
ATOM   4706 N N    . LYS B 1 91  ? 13.98123  -21.84715 9.65226  1.000 47.26865  ? 77  LYS B N    1 
ATOM   4707 C CA   . LYS B 1 91  ? 14.19841  -23.13226 10.30948 1.000 47.50352  ? 77  LYS B CA   1 
ATOM   4708 C C    . LYS B 1 91  ? 14.66179  -22.95926 11.74956 1.000 45.13654  ? 77  LYS B C    1 
ATOM   4709 O O    . LYS B 1 91  ? 14.36883  -23.80648 12.60027 1.000 45.11530  ? 77  LYS B O    1 
ATOM   4710 C CB   . LYS B 1 91  ? 15.21675  -23.96261 9.52822  1.000 50.61088  ? 77  LYS B CB   1 
ATOM   4711 C CG   . LYS B 1 91  ? 14.64315  -25.23918 8.92925  1.000 59.77234  ? 77  LYS B CG   1 
ATOM   4712 C CD   . LYS B 1 91  ? 13.78686  -24.94828 7.70848  1.000 55.52105  ? 77  LYS B CD   1 
ATOM   4713 C CE   . LYS B 1 91  ? 13.14989  -26.21372 7.15577  1.000 60.46286  ? 77  LYS B CE   1 
ATOM   4714 N NZ   . LYS B 1 91  ? 12.57793  -26.00416 5.79322  1.000 58.37798  ? 77  LYS B NZ   1 
ATOM   4715 H H    . LYS B 1 91  ? 14.47081  -21.70884 8.95888  1.000 56.77832  ? 77  LYS B H    1 
ATOM   4716 H HA   . LYS B 1 91  ? 13.35778  -23.61616 10.31867 1.000 57.06017  ? 77  LYS B HA   1 
ATOM   4717 H HB2  . LYS B 1 91  ? 15.56372  -23.42438 8.79965  1.000 60.78900  ? 77  LYS B HB2  1 
ATOM   4718 H HB3  . LYS B 1 91  ? 15.93725  -24.21487 10.12668 1.000 60.78900  ? 77  LYS B HB3  1 
ATOM   4719 H HG2  . LYS B 1 91  ? 15.37010  -25.82194 8.65938  1.000 71.78274  ? 77  LYS B HG2  1 
ATOM   4720 H HG3  . LYS B 1 91  ? 14.08973  -25.68350 9.59046  1.000 71.78274  ? 77  LYS B HG3  1 
ATOM   4721 H HD2  . LYS B 1 91  ? 13.07819  -24.33275 7.95305  1.000 66.68120  ? 77  LYS B HD2  1 
ATOM   4722 H HD3  . LYS B 1 91  ? 14.34034  -24.55795 7.01407  1.000 66.68120  ? 77  LYS B HD3  1 
ATOM   4723 H HE2  . LYS B 1 91  ? 13.82242  -26.91032 7.09789  1.000 72.61137  ? 77  LYS B HE2  1 
ATOM   4724 H HE3  . LYS B 1 91  ? 12.43237  -26.49349 7.74551  1.000 72.61137  ? 77  LYS B HE3  1 
ATOM   4725 H HZ1  . LYS B 1 91  ? 13.22717  -25.80543 5.21782  1.000 70.10952  ? 77  LYS B HZ1  1 
ATOM   4726 H HZ2  . LYS B 1 91  ? 12.16548  -26.74368 5.51918  1.000 70.10952  ? 77  LYS B HZ2  1 
ATOM   4727 H HZ3  . LYS B 1 91  ? 11.99117  -25.33515 5.80899  1.000 70.10952  ? 77  LYS B HZ3  1 
ATOM   4728 N N    . ARG B 1 92  ? 15.38251  -21.87663 12.04461 1.000 41.55852  ? 78  ARG B N    1 
ATOM   4729 C CA   . ARG B 1 92  ? 15.84194  -21.63098 13.40525 1.000 43.85454  ? 78  ARG B CA   1 
ATOM   4730 C C    . ARG B 1 92  ? 14.70128  -21.32033 14.36409 1.000 41.67751  ? 78  ARG B C    1 
ATOM   4731 O O    . ARG B 1 92  ? 14.93354  -21.26651 15.57627 1.000 41.65639  ? 78  ARG B O    1 
ATOM   4732 C CB   . ARG B 1 92  ? 16.85016  -20.48041 13.41280 1.000 56.61982  ? 78  ARG B CB   1 
ATOM   4733 C CG   . ARG B 1 92  ? 18.18371  -20.82857 12.76878 1.000 62.33678  ? 78  ARG B CG   1 
ATOM   4734 C CD   . ARG B 1 92  ? 19.02271  -19.58821 12.49935 1.000 66.96909  ? 78  ARG B CD   1 
ATOM   4735 N NE   . ARG B 1 92  ? 19.05484  -18.68191 13.64204 1.000 74.85015  ? 78  ARG B NE   1 
ATOM   4736 C CZ   . ARG B 1 92  ? 18.28170  -17.61201 13.78294 1.000 76.10829  ? 78  ARG B CZ   1 
ATOM   4737 N NH1  . ARG B 1 92  ? 17.39293  -17.27071 12.86285 1.000 75.43432  ? 78  ARG B NH1  1 
ATOM   4738 N NH2  . ARG B 1 92  ? 18.40551  -16.86305 14.87499 1.000 70.52288  ? 78  ARG B NH2  1 
ATOM   4739 H H    . ARG B 1 92  ? 15.61581  -21.27461 11.47650 1.000 49.92616  ? 78  ARG B H    1 
ATOM   4740 H HA   . ARG B 1 92  ? 16.29191  -22.42661 13.72991 1.000 52.68138  ? 78  ARG B HA   1 
ATOM   4741 H HB2  . ARG B 1 92  ? 16.47242  -19.73185 12.92509 1.000 67.99973  ? 78  ARG B HB2  1 
ATOM   4742 H HB3  . ARG B 1 92  ? 17.02344  -20.22393 14.33209 1.000 67.99973  ? 78  ARG B HB3  1 
ATOM   4743 H HG2  . ARG B 1 92  ? 18.68379  -21.41011 13.36261 1.000 74.86008  ? 78  ARG B HG2  1 
ATOM   4744 H HG3  . ARG B 1 92  ? 18.02363  -21.27622 11.92328 1.000 74.86008  ? 78  ARG B HG3  1 
ATOM   4745 H HD2  . ARG B 1 92  ? 19.93355  -19.85718 12.30206 1.000 80.41885  ? 78  ARG B HD2  1 
ATOM   4746 H HD3  . ARG B 1 92  ? 18.64755  -19.10845 11.74438 1.000 80.41885  ? 78  ARG B HD3  1 
ATOM   4747 H HE   . ARG B 1 92  ? 19.61601  -18.85338 14.27075 1.000 89.87612  ? 78  ARG B HE   1 
ATOM   4748 H HH11 . ARG B 1 92  ? 17.30555  -17.74669 12.15193 1.000 90.57713  ? 78  ARG B HH11 1 
ATOM   4749 H HH12 . ARG B 1 92  ? 16.90302  -16.57303 12.97613 1.000 90.57713  ? 78  ARG B HH12 1 
ATOM   4750 H HH21 . ARG B 1 92  ? 18.98075  -17.07435 15.47837 1.000 84.68340  ? 78  ARG B HH21 1 
ATOM   4751 H HH22 . ARG B 1 92  ? 17.91034  -16.16747 14.97776 1.000 84.68340  ? 78  ARG B HH22 1 
ATOM   4752 N N    . HIS B 1 93  ? 13.48326  -21.12510 13.85856 1.000 40.62637  ? 79  HIS B N    1 
ATOM   4753 C CA   . HIS B 1 93  ? 12.33312  -20.78503 14.68469 1.000 38.69658  ? 79  HIS B CA   1 
ATOM   4754 C C    . HIS B 1 93  ? 11.35089  -21.94229 14.81644 1.000 32.71665  ? 79  HIS B C    1 
ATOM   4755 O O    . HIS B 1 93  ? 10.20838  -21.73456 15.23528 1.000 35.55391  ? 79  HIS B O    1 
ATOM   4756 C CB   . HIS B 1 93  ? 11.62215  -19.55899 14.11205 1.000 36.20481  ? 79  HIS B CB   1 
ATOM   4757 C CG   . HIS B 1 93  ? 12.51468  -18.37174 13.94142 1.000 40.62296  ? 79  HIS B CG   1 
ATOM   4758 N ND1  . HIS B 1 93  ? 13.15500  -17.76536 15.00026 1.000 44.96613  ? 79  HIS B ND1  1 
ATOM   4759 C CD2  . HIS B 1 93  ? 12.87388  -17.67725 12.83628 1.000 44.55199  ? 79  HIS B CD2  1 
ATOM   4760 C CE1  . HIS B 1 93  ? 13.87136  -16.74858 14.55490 1.000 47.76033  ? 79  HIS B CE1  1 
ATOM   4761 N NE2  . HIS B 1 93  ? 13.71796  -16.67338 13.24505 1.000 54.33591  ? 79  HIS B NE2  1 
ATOM   4762 H H    . HIS B 1 93  ? 13.29754  -21.18616 13.02107 1.000 48.80759  ? 79  HIS B H    1 
ATOM   4763 H HA   . HIS B 1 93  ? 12.65060  -20.56675 15.57489 1.000 46.49184  ? 79  HIS B HA   1 
ATOM   4764 H HB2  . HIS B 1 93  ? 11.26134  -19.78607 13.24076 1.000 43.50171  ? 79  HIS B HB2  1 
ATOM   4765 H HB3  . HIS B 1 93  ? 10.90391  -19.30580 14.71283 1.000 43.50171  ? 79  HIS B HB3  1 
ATOM   4766 H HD2  . HIS B 1 93  ? 12.60048  -17.84777 11.96388 1.000 53.51833  ? 79  HIS B HD2  1 
ATOM   4767 H HE1  . HIS B 1 93  ? 14.39451  -16.18225 15.07498 1.000 57.36834  ? 79  HIS B HE1  1 
ATOM   4768 H HE2  . HIS B 1 93  ? 14.08672  -16.09047 12.73141 1.000 65.25903  ? 79  HIS B HE2  1 
ATOM   4769 N N    . ASP B 1 94  ? 11.76866  -23.15733 14.47104 1.000 35.31526  ? 80  ASP B N    1 
ATOM   4770 C CA   . ASP B 1 94  ? 10.88861  -24.32459 14.50810 1.000 30.16344  ? 80  ASP B CA   1 
ATOM   4771 C C    . ASP B 1 94  ? 11.08795  -25.03520 15.84332 1.000 28.66916  ? 80  ASP B C    1 
ATOM   4772 O O    . ASP B 1 94  ? 11.86992  -25.97888 15.95829 1.000 33.22495  ? 80  ASP B O    1 
ATOM   4773 C CB   . ASP B 1 94  ? 11.16623  -25.25480 13.33442 1.000 31.73757  ? 80  ASP B CB   1 
ATOM   4774 C CG   . ASP B 1 94  ? 10.08695  -26.30212 13.15962 1.000 27.78251  ? 80  ASP B CG   1 
ATOM   4775 O OD1  . ASP B 1 94  ? 9.31784   -26.53001 14.11881 1.000 26.37234  ? 80  ASP B OD1  1 
ATOM   4776 O OD2  . ASP B 1 94  ? 10.00612  -26.89527 12.06434 1.000 27.87487  ? 80  ASP B OD2  1 
ATOM   4777 H H    . ASP B 1 94  ? 12.56822  -23.33394 14.20815 1.000 42.43425  ? 80  ASP B H    1 
ATOM   4778 H HA   . ASP B 1 94  ? 9.96837   -24.02232 14.45612 1.000 36.25207  ? 80  ASP B HA   1 
ATOM   4779 H HB2  . ASP B 1 94  ? 11.21328  -24.73157 12.51899 1.000 38.14102  ? 80  ASP B HB2  1 
ATOM   4780 H HB3  . ASP B 1 94  ? 12.00845  -25.71211 13.48422 1.000 38.14102  ? 80  ASP B HB3  1 
ATOM   4781 N N    . PHE B 1 95  ? 10.35971  -24.57501 16.86178 1.000 28.36781  ? 81  PHE B N    1 
ATOM   4782 C CA   . PHE B 1 95  ? 10.41549  -25.22669 18.16532 1.000 28.46888  ? 81  PHE B CA   1 
ATOM   4783 C C    . PHE B 1 95  ? 9.88700   -26.65149 18.08918 1.000 29.89573  ? 81  PHE B C    1 
ATOM   4784 O O    . PHE B 1 95  ? 10.48713  -27.57793 18.64579 1.000 31.13542  ? 81  PHE B O    1 
ATOM   4785 C CB   . PHE B 1 95  ? 9.61036   -24.41881 19.18481 1.000 29.76335  ? 81  PHE B CB   1 
ATOM   4786 C CG   . PHE B 1 95  ? 9.33905   -25.15538 20.47085 1.000 31.16907  ? 81  PHE B CG   1 
ATOM   4787 C CD1  . PHE B 1 95  ? 8.20928   -25.94794 20.60676 1.000 25.59745  ? 81  PHE B CD1  1 
ATOM   4788 C CD2  . PHE B 1 95  ? 10.20788  -25.04803 21.54527 1.000 31.46501  ? 81  PHE B CD2  1 
ATOM   4789 C CE1  . PHE B 1 95  ? 7.95582   -26.62740 21.78620 1.000 33.99317  ? 81  PHE B CE1  1 
ATOM   4790 C CE2  . PHE B 1 95  ? 9.95851   -25.72455 22.73007 1.000 35.31090  ? 81  PHE B CE2  1 
ATOM   4791 C CZ   . PHE B 1 95  ? 8.83080   -26.51505 22.84949 1.000 29.67903  ? 81  PHE B CZ   1 
ATOM   4792 H H    . PHE B 1 95  ? 9.83296   -23.89629 16.82335 1.000 34.09731  ? 81  PHE B H    1 
ATOM   4793 H HA   . PHE B 1 95  ? 11.33890  -25.25970 18.46049 1.000 34.21859  ? 81  PHE B HA   1 
ATOM   4794 H HB2  . PHE B 1 95  ? 10.10474  -23.61362 19.40424 1.000 35.77196  ? 81  PHE B HB2  1 
ATOM   4795 H HB3  . PHE B 1 95  ? 8.75473   -24.18597 18.79163 1.000 35.77196  ? 81  PHE B HB3  1 
ATOM   4796 H HD1  . PHE B 1 95  ? 7.61399   -26.02407 19.89632 1.000 30.77288  ? 81  PHE B HD1  1 
ATOM   4797 H HD2  . PHE B 1 95  ? 10.96708  -24.51606 21.47092 1.000 37.81395  ? 81  PHE B HD2  1 
ATOM   4798 H HE1  . PHE B 1 95  ? 7.19678   -27.15930 21.86266 1.000 40.84775  ? 81  PHE B HE1  1 
ATOM   4799 H HE2  . PHE B 1 95  ? 10.54964  -25.64641 23.44377 1.000 42.42902  ? 81  PHE B HE2  1 
ATOM   4800 H HZ   . PHE B 1 95  ? 8.66165   -26.96974 23.64293 1.000 35.67077  ? 81  PHE B HZ   1 
ATOM   4801 N N    . PHE B 1 96  ? 8.76347   -26.84321 17.39861 1.000 28.83964  ? 82  PHE B N    1 
ATOM   4802 C CA   . PHE B 1 96  ? 8.07552   -28.12805 17.43429 1.000 26.12643  ? 82  PHE B CA   1 
ATOM   4803 C C    . PHE B 1 96  ? 8.99729   -29.26802 17.01839 1.000 28.63250  ? 82  PHE B C    1 
ATOM   4804 O O    . PHE B 1 96  ? 9.02503   -30.32084 17.66717 1.000 26.14268  ? 82  PHE B O    1 
ATOM   4805 C CB   . PHE B 1 96  ? 6.84301   -28.07310 16.53336 1.000 26.85614  ? 82  PHE B CB   1 
ATOM   4806 C CG   . PHE B 1 96  ? 5.94787   -26.89441 16.80025 1.000 26.68071  ? 82  PHE B CG   1 
ATOM   4807 C CD1  . PHE B 1 96  ? 5.02428   -26.92845 17.82842 1.000 25.65655  ? 82  PHE B CD1  1 
ATOM   4808 C CD2  . PHE B 1 96  ? 6.02891   -25.75394 16.01748 1.000 31.73335  ? 82  PHE B CD2  1 
ATOM   4809 C CE1  . PHE B 1 96  ? 4.19964   -25.84869 18.07423 1.000 28.44817  ? 82  PHE B CE1  1 
ATOM   4810 C CE2  . PHE B 1 96  ? 5.20756   -24.66926 16.26018 1.000 31.42644  ? 82  PHE B CE2  1 
ATOM   4811 C CZ   . PHE B 1 96  ? 4.29036   -24.71825 17.28829 1.000 29.14490  ? 82  PHE B CZ   1 
ATOM   4812 H H    . PHE B 1 96  ? 8.38271   -26.24992 16.90604 1.000 34.66351  ? 82  PHE B H    1 
ATOM   4813 H HA   . PHE B 1 96  ? 7.78361   -28.30478 18.34229 1.000 31.40766  ? 82  PHE B HA   1 
ATOM   4814 H HB2  . PHE B 1 96  ? 7.13428   -28.02018 15.60964 1.000 32.28331  ? 82  PHE B HB2  1 
ATOM   4815 H HB3  . PHE B 1 96  ? 6.32034   -28.87860 16.67078 1.000 32.28331  ? 82  PHE B HB3  1 
ATOM   4816 H HD1  . PHE B 1 96  ? 4.95763   -27.68793 18.36101 1.000 30.84380  ? 82  PHE B HD1  1 
ATOM   4817 H HD2  . PHE B 1 96  ? 6.64342   -25.71795 15.32037 1.000 38.13596  ? 82  PHE B HD2  1 
ATOM   4818 H HE1  . PHE B 1 96  ? 3.58302   -25.88333 18.76956 1.000 34.19375  ? 82  PHE B HE1  1 
ATOM   4819 H HE2  . PHE B 1 96  ? 5.27347   -23.90750 15.73077 1.000 37.76766  ? 82  PHE B HE2  1 
ATOM   4820 H HZ   . PHE B 1 96  ? 3.73411   -23.99108 17.45171 1.000 35.02982  ? 82  PHE B HZ   1 
ATOM   4821 N N    . LYS B 1 97  ? 9.76326   -29.07893 15.94230 1.000 29.67573  ? 83  LYS B N    1 
ATOM   4822 C CA   . LYS B 1 97  ? 10.65550  -30.13785 15.48374 1.000 28.15897  ? 83  LYS B CA   1 
ATOM   4823 C C    . LYS B 1 97  ? 11.89962  -30.24882 16.35810 1.000 28.61975  ? 83  LYS B C    1 
ATOM   4824 O O    . LYS B 1 97  ? 12.39543  -31.35669 16.59110 1.000 30.36273  ? 83  LYS B O    1 
ATOM   4825 C CB   . LYS B 1 97  ? 11.05499  -29.89839 14.02751 1.000 33.53406  ? 83  LYS B CB   1 
ATOM   4826 C CG   . LYS B 1 97  ? 9.91332   -30.05089 13.03084 1.000 25.65024  ? 83  LYS B CG   1 
ATOM   4827 C CD   . LYS B 1 97  ? 10.41420  -29.91159 11.60389 1.000 31.01877  ? 83  LYS B CD   1 
ATOM   4828 C CE   . LYS B 1 97  ? 9.26813   -29.86783 10.60395 1.000 30.78337  ? 83  LYS B CE   1 
ATOM   4829 N NZ   . LYS B 1 97  ? 8.31399   -28.76089 10.88950 1.000 31.60957  ? 83  LYS B NZ   1 
ATOM   4830 H H    . LYS B 1 97  ? 9.78329   -28.36015 15.47054 1.000 35.66682  ? 83  LYS B H    1 
ATOM   4831 H HA   . LYS B 1 97  ? 10.17868  -30.98121 15.53166 1.000 33.84670  ? 83  LYS B HA   1 
ATOM   4832 H HB2  . LYS B 1 97  ? 11.39815  -28.99487 13.94514 1.000 40.29681  ? 83  LYS B HB2  1 
ATOM   4833 H HB3  . LYS B 1 97  ? 11.74315  -30.53794 13.78604 1.000 40.29681  ? 83  LYS B HB3  1 
ATOM   4834 H HG2  . LYS B 1 97  ? 9.51190   -30.92824 13.13096 1.000 30.83623  ? 83  LYS B HG2  1 
ATOM   4835 H HG3  . LYS B 1 97  ? 9.24961   -29.36206 13.19178 1.000 30.83623  ? 83  LYS B HG3  1 
ATOM   4836 H HD2  . LYS B 1 97  ? 10.92062  -29.08841 11.52134 1.000 37.27846  ? 83  LYS B HD2  1 
ATOM   4837 H HD3  . LYS B 1 97  ? 10.97753  -30.67084 11.38685 1.000 37.27846  ? 83  LYS B HD3  1 
ATOM   4838 H HE2  . LYS B 1 97  ? 9.62780   -29.73429 9.71304  1.000 36.99598  ? 83  LYS B HE2  1 
ATOM   4839 H HE3  . LYS B 1 97  ? 8.77977   -30.70503 10.64251 1.000 36.99598  ? 83  LYS B HE3  1 
ATOM   4840 H HZ1  . LYS B 1 97  ? 8.75926   -28.00172 11.02174 1.000 37.98742  ? 83  LYS B HZ1  1 
ATOM   4841 H HZ2  . LYS B 1 97  ? 7.75782   -28.65371 10.20299 1.000 37.98742  ? 83  LYS B HZ2  1 
ATOM   4842 H HZ3  . LYS B 1 97  ? 7.83972   -28.94838 11.61890 1.000 37.98742  ? 83  LYS B HZ3  1 
ATOM   4843 N N    . SER B 1 98  ? 12.41509  -29.11850 16.85391 1.000 29.66454  ? 84  SER B N    1 
ATOM   4844 C CA   . SER B 1 98  ? 13.64175  -29.15035 17.64648 1.000 30.11398  ? 84  SER B CA   1 
ATOM   4845 C C    . SER B 1 98  ? 13.48278  -30.00422 18.89764 1.000 31.08829  ? 84  SER B C    1 
ATOM   4846 O O    . SER B 1 98  ? 14.47009  -30.54627 19.40810 1.000 35.93267  ? 84  SER B O    1 
ATOM   4847 C CB   . SER B 1 98  ? 14.06033  -27.72961 18.03409 1.000 36.41650  ? 84  SER B CB   1 
ATOM   4848 O OG   . SER B 1 98  ? 13.16810  -27.16861 18.98333 1.000 32.13237  ? 84  SER B OG   1 
ATOM   4849 H H    . SER B 1 98  ? 12.07809  -28.33461 16.74647 1.000 35.65339  ? 84  SER B H    1 
ATOM   4850 H HA   . SER B 1 98  ? 14.34656  -29.53628 17.10315 1.000 36.19271  ? 84  SER B HA   1 
ATOM   4851 H HB2  . SER B 1 98  ? 14.95016  -27.75885 18.41912 1.000 43.75574  ? 84  SER B HB2  1 
ATOM   4852 H HB3  . SER B 1 98  ? 14.06120  -27.17482 17.23840 1.000 43.75574  ? 84  SER B HB3  1 
ATOM   4853 H HG   . SER B 1 98  ? 12.39029  -27.14416 18.66708 1.000 38.61478  ? 84  SER B HG   1 
ATOM   4854 N N    . ALA B 1 99  ? 12.25683  -30.13452 19.40535 1.000 27.28562  ? 85  ALA B N    1 
ATOM   4855 C CA   . ALA B 1 99  ? 11.99829  -30.91856 20.60585 1.000 35.02419  ? 85  ALA B CA   1 
ATOM   4856 C C    . ALA B 1 99  ? 11.87781  -32.41176 20.33077 1.000 34.77582  ? 85  ALA B C    1 
ATOM   4857 O O    . ALA B 1 99  ? 11.80428  -33.19576 21.28446 1.000 28.80458  ? 85  ALA B O    1 
ATOM   4858 C CB   . ALA B 1 99  ? 10.71685  -30.42589 21.28429 1.000 31.97590  ? 85  ALA B CB   1 
ATOM   4859 H H    . ALA B 1 99  ? 11.55287  -29.77397 19.06765 1.000 32.79869  ? 85  ALA B H    1 
ATOM   4860 H HA   . ALA B 1 99  ? 12.73710  -30.78973 21.22105 1.000 42.08497  ? 85  ALA B HA   1 
ATOM   4861 H HB1  . ALA B 1 99  ? 9.97433   -30.52756 20.66848 1.000 38.42702  ? 85  ALA B HB1  1 
ATOM   4862 H HB2  . ALA B 1 99  ? 10.55915  -30.95381 22.08262 1.000 38.42702  ? 85  ALA B HB2  1 
ATOM   4863 H HB3  . ALA B 1 99  ? 10.82429  -29.49149 21.52150 1.000 38.42702  ? 85  ALA B HB3  1 
ATOM   4864 N N    . MET B 1 100 ? 11.85318  -32.82065 19.06664 1.000 28.95823  ? 86  MET B N    1 
ATOM   4865 C CA   . MET B 1 100 ? 11.70044  -34.22177 18.71982 1.000 32.20009  ? 86  MET B CA   1 
ATOM   4866 C C    . MET B 1 100 ? 13.04228  -34.94113 18.79761 1.000 31.93849  ? 86  MET B C    1 
ATOM   4867 O O    . MET B 1 100 ? 14.10047  -34.31924 18.67543 1.000 32.18117  ? 86  MET B O    1 
ATOM   4868 C CB   . MET B 1 100 ? 11.10849  -34.34617 17.32066 1.000 31.23153  ? 86  MET B CB   1 
ATOM   4869 C CG   . MET B 1 100 ? 9.68114   -33.83344 17.22520 1.000 28.20682  ? 86  MET B CG   1 
ATOM   4870 S SD   . MET B 1 100 ? 8.54766   -34.74987 18.28708 1.000 30.52027  ? 86  MET B SD   1 
ATOM   4871 C CE   . MET B 1 100 ? 7.14284   -33.64193 18.31348 1.000 30.12512  ? 86  MET B CE   1 
ATOM   4872 H H    . MET B 1 100 ? 11.92396  -32.29856 18.38693 1.000 34.80581  ? 86  MET B H    1 
ATOM   4873 H HA   . MET B 1 100 ? 11.08575  -34.64569 19.33897 1.000 38.69605  ? 86  MET B HA   1 
ATOM   4874 H HB2  . MET B 1 100 ? 11.65200  -33.83210 16.70323 1.000 37.53377  ? 86  MET B HB2  1 
ATOM   4875 H HB3  . MET B 1 100 ? 11.10743  -35.28118 17.06246 1.000 37.53377  ? 86  MET B HB3  1 
ATOM   4876 H HG2  . MET B 1 100 ? 9.65996   -32.90192 17.49489 1.000 33.90413  ? 86  MET B HG2  1 
ATOM   4877 H HG3  . MET B 1 100 ? 9.37324   -33.92080 16.30952 1.000 33.90413  ? 86  MET B HG3  1 
ATOM   4878 H HE1  . MET B 1 100 ? 6.62618   -33.76767 17.50221 1.000 36.20609  ? 86  MET B HE1  1 
ATOM   4879 H HE2  . MET B 1 100 ? 6.59583   -33.84395 19.08864 1.000 36.20609  ? 86  MET B HE2  1 
ATOM   4880 H HE3  . MET B 1 100 ? 7.46268   -32.72755 18.36356 1.000 36.20609  ? 86  MET B HE3  1 
ATOM   4881 N N    . PRO B 1 101 ? 13.02806  -36.26830 18.99020 1.000 26.36490  ? 87  PRO B N    1 
ATOM   4882 C CA   . PRO B 1 101 ? 11.86366  -37.16246 19.06291 1.000 30.50950  ? 87  PRO B CA   1 
ATOM   4883 C C    . PRO B 1 101 ? 11.21252  -37.24277 20.44216 1.000 31.72084  ? 87  PRO B C    1 
ATOM   4884 O O    . PRO B 1 101 ? 10.10566  -37.76068 20.56090 1.000 30.83659  ? 87  PRO B O    1 
ATOM   4885 C CB   . PRO B 1 101 ? 12.46182  -38.51208 18.65014 1.000 29.31981  ? 87  PRO B CB   1 
ATOM   4886 C CG   . PRO B 1 101 ? 13.85673  -38.46388 19.20026 1.000 29.06697  ? 87  PRO B CG   1 
ATOM   4887 C CD   . PRO B 1 101 ? 14.29412  -37.01950 19.07612 1.000 29.86859  ? 87  PRO B CD   1 
ATOM   4888 H HA   . PRO B 1 101 ? 11.19697  -36.86501 18.42421 1.000 36.66734  ? 87  PRO B HA   1 
ATOM   4889 H HB2  . PRO B 1 101 ? 11.95321  -39.23867 19.04294 1.000 35.23971  ? 87  PRO B HB2  1 
ATOM   4890 H HB3  . PRO B 1 101 ? 12.46700  -38.59525 17.68373 1.000 35.23971  ? 87  PRO B HB3  1 
ATOM   4891 H HG2  . PRO B 1 101 ? 13.85288  -38.74419 20.12886 1.000 34.93631  ? 87  PRO B HG2  1 
ATOM   4892 H HG3  . PRO B 1 101 ? 14.43435  -39.04472 18.68077 1.000 34.93631  ? 87  PRO B HG3  1 
ATOM   4893 H HD2  . PRO B 1 101 ? 14.80151  -36.74714 19.85668 1.000 35.89825  ? 87  PRO B HD2  1 
ATOM   4894 H HD3  . PRO B 1 101 ? 14.82415  -36.89000 18.27412 1.000 35.89825  ? 87  PRO B HD3  1 
ATOM   4895 N N    . GLU B 1 102 ? 11.85615  -36.74993 21.50342 1.000 29.72226  ? 88  GLU B N    1 
ATOM   4896 C CA   . GLU B 1 102 ? 11.24940  -36.84224 22.82805 1.000 35.99747  ? 88  GLU B CA   1 
ATOM   4897 C C    . GLU B 1 102 ? 9.90305   -36.13275 22.87378 1.000 30.06959  ? 88  GLU B C    1 
ATOM   4898 O O    . GLU B 1 102 ? 9.01288   -36.53797 23.62954 1.000 29.88213  ? 88  GLU B O    1 
ATOM   4899 C CB   . GLU B 1 102 ? 12.18514  -36.26160 23.88857 1.000 37.82616  ? 88  GLU B CB   1 
ATOM   4900 C CG   . GLU B 1 102 ? 13.56422  -36.90093 23.93367 1.000 42.14659  ? 88  GLU B CG   1 
ATOM   4901 C CD   . GLU B 1 102 ? 14.57490  -36.16970 23.06974 1.000 53.67162  ? 88  GLU B CD   1 
ATOM   4902 O OE1  . GLU B 1 102 ? 14.16268  -35.53073 22.07658 1.000 40.55546  ? 88  GLU B OE1  1 
ATOM   4903 O OE2  . GLU B 1 102 ? 15.78105  -36.22620 23.39232 1.000 72.34064  ? 88  GLU B OE2  1 
ATOM   4904 H H    . GLU B 1 102 ? 12.62594  -36.36708 21.48242 1.000 35.72266  ? 88  GLU B H    1 
ATOM   4905 H HA   . GLU B 1 102 ? 11.10963  -37.77911 23.03696 1.000 43.25291  ? 88  GLU B HA   1 
ATOM   4906 H HB2  . GLU B 1 102 ? 12.30661  -35.31620 23.70867 1.000 45.44733  ? 88  GLU B HB2  1 
ATOM   4907 H HB3  . GLU B 1 102 ? 11.77733  -36.38374 24.76016 1.000 45.44733  ? 88  GLU B HB3  1 
ATOM   4908 H HG2  . GLU B 1 102 ? 13.88784  -36.89156 24.84804 1.000 50.63185  ? 88  GLU B HG2  1 
ATOM   4909 H HG3  . GLU B 1 102 ? 13.50038  -37.81440 23.61368 1.000 50.63185  ? 88  GLU B HG3  1 
ATOM   4910 N N    . GLY B 1 103 ? 9.73529   -35.08047 22.08527 1.000 31.14212  ? 89  GLY B N    1 
ATOM   4911 C CA   . GLY B 1 103 ? 8.44286   -34.44967 21.95134 1.000 29.42304  ? 89  GLY B CA   1 
ATOM   4912 C C    . GLY B 1 103 ? 8.23617   -33.28751 22.89677 1.000 26.71374  ? 89  GLY B C    1 
ATOM   4913 O O    . GLY B 1 103 ? 9.13868   -32.81728 23.59699 1.000 26.82019  ? 89  GLY B O    1 
ATOM   4914 H H    . GLY B 1 103 ? 10.35857  -34.71573 21.61828 1.000 37.42648  ? 89  GLY B H    1 
ATOM   4915 H HA2  . GLY B 1 103 ? 8.34396   -34.12058 21.04425 1.000 35.36359  ? 89  GLY B HA2  1 
ATOM   4916 H HA3  . GLY B 1 103 ? 7.75070   -35.10633 22.12628 1.000 35.36359  ? 89  GLY B HA3  1 
ATOM   4917 N N    . TYR B 1 104 ? 6.99342   -32.81538 22.90585 1.000 27.45763  ? 90  TYR B N    1 
ATOM   4918 C CA   . TYR B 1 104 ? 6.61130   -31.67150 23.71390 1.000 28.07186  ? 90  TYR B CA   1 
ATOM   4919 C C    . TYR B 1 104 ? 5.20838   -31.88007 24.25912 1.000 28.91575  ? 90  TYR B C    1 
ATOM   4920 O O    . TYR B 1 104 ? 4.40777   -32.64376 23.71183 1.000 26.85528  ? 90  TYR B O    1 
ATOM   4921 C CB   . TYR B 1 104 ? 6.67233   -30.36428 22.90872 1.000 32.07811  ? 90  TYR B CB   1 
ATOM   4922 C CG   . TYR B 1 104 ? 5.89431   -30.39107 21.60870 1.000 27.42209  ? 90  TYR B CG   1 
ATOM   4923 C CD1  . TYR B 1 104 ? 4.51185   -30.25259 21.59757 1.000 29.61282  ? 90  TYR B CD1  1 
ATOM   4924 C CD2  . TYR B 1 104 ? 6.54514   -30.53988 20.39135 1.000 27.55480  ? 90  TYR B CD2  1 
ATOM   4925 C CE1  . TYR B 1 104 ? 3.79875   -30.27031 20.40924 1.000 29.85251  ? 90  TYR B CE1  1 
ATOM   4926 C CE2  . TYR B 1 104 ? 5.84160   -30.55925 19.19965 1.000 28.40989  ? 90  TYR B CE2  1 
ATOM   4927 C CZ   . TYR B 1 104 ? 4.47006   -30.42347 19.21330 1.000 30.90674  ? 90  TYR B CZ   1 
ATOM   4928 O OH   . TYR B 1 104 ? 3.77174   -30.44023 18.02527 1.000 27.96829  ? 90  TYR B OH   1 
ATOM   4929 H H    . TYR B 1 104 ? 6.34767   -33.14743 22.44504 1.000 33.00509  ? 90  TYR B H    1 
ATOM   4930 H HA   . TYR B 1 104 ? 7.21914   -31.59827 24.46628 1.000 33.74218  ? 90  TYR B HA   1 
ATOM   4931 H HB2  . TYR B 1 104 ? 6.30865   -29.64861 23.45320 1.000 38.54967  ? 90  TYR B HB2  1 
ATOM   4932 H HB3  . TYR B 1 104 ? 7.59919   -30.17787 22.69176 1.000 38.54967  ? 90  TYR B HB3  1 
ATOM   4933 H HD1  . TYR B 1 104 ? 4.05696   -30.14613 22.40171 1.000 35.59132  ? 90  TYR B HD1  1 
ATOM   4934 H HD2  . TYR B 1 104 ? 7.47082   -30.62816 20.37643 1.000 33.12169  ? 90  TYR B HD2  1 
ATOM   4935 H HE1  . TYR B 1 104 ? 2.87323   -30.17952 20.41778 1.000 35.87895  ? 90  TYR B HE1  1 
ATOM   4936 H HE2  . TYR B 1 104 ? 6.29245   -30.66345 18.39294 1.000 34.14781  ? 90  TYR B HE2  1 
ATOM   4937 H HH   . TYR B 1 104 ? 2.95402   -30.31485 18.17089 1.000 33.61789  ? 90  TYR B HH   1 
ATOM   4938 N N    . VAL B 1 105 ? 4.92900   -31.19352 25.35771 1.000 26.55274  ? 91  VAL B N    1 
ATOM   4939 C CA   . VAL B 1 105 ? 3.58465   -31.11465 25.90960 1.000 27.95698  ? 91  VAL B CA   1 
ATOM   4940 C C    . VAL B 1 105 ? 2.89288   -29.90982 25.29278 1.000 29.23275  ? 91  VAL B C    1 
ATOM   4941 O O    . VAL B 1 105 ? 3.45171   -28.80783 25.27177 1.000 29.12306  ? 91  VAL B O    1 
ATOM   4942 C CB   . VAL B 1 105 ? 3.62239   -31.00076 27.44192 1.000 27.23625  ? 91  VAL B CB   1 
ATOM   4943 C CG1  . VAL B 1 105 ? 2.22009   -30.76259 27.99052 1.000 29.18880  ? 91  VAL B CG1  1 
ATOM   4944 C CG2  . VAL B 1 105 ? 4.23997   -32.25046 28.05347 1.000 29.86005  ? 91  VAL B CG2  1 
ATOM   4945 H H    . VAL B 1 105 ? 5.51358   -30.75532 25.81142 1.000 31.91923  ? 91  VAL B H    1 
ATOM   4946 H HA   . VAL B 1 105 ? 3.08964   -31.91625 25.67872 1.000 33.60432  ? 91  VAL B HA   1 
ATOM   4947 H HB   . VAL B 1 105 ? 4.17468   -30.24295 27.69012 1.000 32.73944  ? 91  VAL B HB   1 
ATOM   4948 H HG11 . VAL B 1 105 ? 1.94415   -29.85907 27.77050 1.000 35.08250  ? 91  VAL B HG11 1 
ATOM   4949 H HG12 . VAL B 1 105 ? 1.61099   -31.40161 27.58857 1.000 35.08250  ? 91  VAL B HG12 1 
ATOM   4950 H HG13 . VAL B 1 105 ? 2.23367   -30.87909 28.95340 1.000 35.08250  ? 91  VAL B HG13 1 
ATOM   4951 H HG21 . VAL B 1 105 ? 4.16152   -32.20139 29.01905 1.000 35.88800  ? 91  VAL B HG21 1 
ATOM   4952 H HG22 . VAL B 1 105 ? 3.76781   -33.03045 27.72245 1.000 35.88800  ? 91  VAL B HG22 1 
ATOM   4953 H HG23 . VAL B 1 105 ? 5.17497   -32.29734 27.79953 1.000 35.88800  ? 91  VAL B HG23 1 
ATOM   4954 N N    . GLN B 1 106 ? 1.68255   -30.11653 24.78334 1.000 26.99348  ? 92  GLN B N    1 
ATOM   4955 C CA   . GLN B 1 106 ? 0.86716   -29.04236 24.23263 1.000 26.52309  ? 92  GLN B CA   1 
ATOM   4956 C C    . GLN B 1 106 ? -0.38001  -28.90182 25.09119 1.000 27.32413  ? 92  GLN B C    1 
ATOM   4957 O O    . GLN B 1 106 ? -1.16796  -29.84699 25.20587 1.000 24.22775  ? 92  GLN B O    1 
ATOM   4958 C CB   . GLN B 1 106 ? 0.49712   -29.31345 22.77242 1.000 26.79550  ? 92  GLN B CB   1 
ATOM   4959 C CG   . GLN B 1 106 ? -0.43630  -28.26897 22.17738 1.000 24.10701  ? 92  GLN B CG   1 
ATOM   4960 C CD   . GLN B 1 106 ? -0.25192  -28.10236 20.68260 1.000 26.98878  ? 92  GLN B CD   1 
ATOM   4961 O OE1  . GLN B 1 106 ? 0.86423   -27.91235 20.20280 1.000 30.40677  ? 92  GLN B OE1  1 
ATOM   4962 N NE2  . GLN B 1 106 ? -1.34790  -28.17426 19.93761 1.000 28.34840  ? 92  GLN B NE2  1 
ATOM   4963 H H    . GLN B 1 106 ? 1.30515   -30.88837 24.74546 1.000 32.44811  ? 92  GLN B H    1 
ATOM   4964 H HA   . GLN B 1 106 ? 1.36157   -28.20838 24.26331 1.000 31.88365  ? 92  GLN B HA   1 
ATOM   4965 H HB2  . GLN B 1 106 ? 1.30858   -29.32370 22.24108 1.000 32.21053  ? 92  GLN B HB2  1 
ATOM   4966 H HB3  . GLN B 1 106 ? 0.05341   -30.17424 22.71706 1.000 32.21053  ? 92  GLN B HB3  1 
ATOM   4967 H HG2  . GLN B 1 106 ? -1.35450  -28.53712 22.33837 1.000 28.98435  ? 92  GLN B HG2  1 
ATOM   4968 H HG3  . GLN B 1 106 ? -0.26207  -27.41267 22.59845 1.000 28.98435  ? 92  GLN B HG3  1 
ATOM   4969 H HE21 . GLN B 1 106 ? -2.11193  -28.30930 20.30860 1.000 34.07402  ? 92  GLN B HE21 1 
ATOM   4970 H HE22 . GLN B 1 106 ? -1.29408  -28.08581 19.08387 1.000 34.07402  ? 92  GLN B HE22 1 
ATOM   4971 N N    . GLU B 1 107 ? -0.54635  -27.72968 25.69887 1.000 22.99914  ? 93  GLU B N    1 
ATOM   4972 C CA   . GLU B 1 107 ? -1.68183  -27.42218 26.55548 1.000 26.86467  ? 93  GLU B CA   1 
ATOM   4973 C C    . GLU B 1 107 ? -2.43581  -26.22625 25.99418 1.000 31.48262  ? 93  GLU B C    1 
ATOM   4974 O O    . GLU B 1 107 ? -1.82819  -25.28875 25.46676 1.000 28.58438  ? 93  GLU B O    1 
ATOM   4975 C CB   . GLU B 1 107 ? -1.22769  -27.11761 27.98459 1.000 28.01143  ? 93  GLU B CB   1 
ATOM   4976 C CG   . GLU B 1 107 ? -0.64913  -28.31403 28.72087 1.000 32.51744  ? 93  GLU B CG   1 
ATOM   4977 C CD   . GLU B 1 107 ? -0.00341  -27.93038 30.03743 1.000 44.48096  ? 93  GLU B CD   1 
ATOM   4978 O OE1  . GLU B 1 107 ? 0.66791   -26.87741 30.08676 1.000 46.09366  ? 93  GLU B OE1  1 
ATOM   4979 O OE2  . GLU B 1 107 ? -0.16895  -28.68028 31.02333 1.000 47.64040  ? 93  GLU B OE2  1 
ATOM   4980 H H    . GLU B 1 107 ? 0.00669   -27.07516 25.62573 1.000 27.65491  ? 93  GLU B H    1 
ATOM   4981 H HA   . GLU B 1 107 ? -2.28375  -28.18245 26.57980 1.000 32.29354  ? 93  GLU B HA   1 
ATOM   4982 H HB2  . GLU B 1 107 ? -0.54250  -26.43174 27.95294 1.000 33.66966  ? 93  GLU B HB2  1 
ATOM   4983 H HB3  . GLU B 1 107 ? -1.99124  -26.80061 28.49194 1.000 33.66966  ? 93  GLU B HB3  1 
ATOM   4984 H HG2  . GLU B 1 107 ? -1.36122  -28.94557 28.90794 1.000 39.07686  ? 93  GLU B HG2  1 
ATOM   4985 H HG3  . GLU B 1 107 ? 0.02704   -28.73163 28.16471 1.000 39.07686  ? 93  GLU B HG3  1 
ATOM   4986 N N    . ARG B 1 108 ? -3.76007  -26.25588 26.11755 1.000 29.71865  ? 94  ARG B N    1 
ATOM   4987 C CA   . ARG B 1 108 ? -4.59046  -25.16986 25.62758 1.000 30.83950  ? 94  ARG B CA   1 
ATOM   4988 C C    . ARG B 1 108 ? -5.76664  -24.94456 26.56296 1.000 30.62049  ? 94  ARG B C    1 
ATOM   4989 O O    . ARG B 1 108 ? -6.20392  -25.85016 27.27831 1.000 27.04001  ? 94  ARG B O    1 
ATOM   4990 C CB   . ARG B 1 108 ? -5.13248  -25.44218 24.21466 1.000 30.68139  ? 94  ARG B CB   1 
ATOM   4991 C CG   . ARG B 1 108 ? -4.11333  -25.32598 23.09362 1.000 28.09708  ? 94  ARG B CG   1 
ATOM   4992 C CD   . ARG B 1 108 ? -4.78149  -24.80290 21.82944 1.000 28.12261  ? 94  ARG B CD   1 
ATOM   4993 N NE   . ARG B 1 108 ? -3.92582  -24.90092 20.65307 1.000 27.78288  ? 94  ARG B NE   1 
ATOM   4994 C CZ   . ARG B 1 108 ? -3.91496  -25.92546 19.80994 1.000 26.55781  ? 94  ARG B CZ   1 
ATOM   4995 N NH1  . ARG B 1 108 ? -4.69231  -26.98215 19.99140 1.000 25.66889  ? 94  ARG B NH1  1 
ATOM   4996 N NH2  . ARG B 1 108 ? -3.10389  -25.88835 18.75613 1.000 25.82088  ? 94  ARG B NH2  1 
ATOM   4997 H H    . ARG B 1 108 ? -4.19909  -26.89851 26.48346 1.000 35.71832  ? 94  ARG B H    1 
ATOM   4998 H HA   . ARG B 1 108 ? -4.04951  -24.36494 25.60806 1.000 37.06334  ? 94  ARG B HA   1 
ATOM   4999 H HB2  . ARG B 1 108 ? -5.48616  -26.34511 24.19175 1.000 36.87361  ? 94  ARG B HB2  1 
ATOM   5000 H HB3  . ARG B 1 108 ? -5.83947  -24.80417 24.03028 1.000 36.87361  ? 94  ARG B HB3  1 
ATOM   5001 H HG2  . ARG B 1 108 ? -3.41211  -24.70787 23.35273 1.000 33.77244  ? 94  ARG B HG2  1 
ATOM   5002 H HG3  . ARG B 1 108 ? -3.73367  -26.19862 22.90587 1.000 33.77244  ? 94  ARG B HG3  1 
ATOM   5003 H HD2  . ARG B 1 108 ? -5.58417  -25.32029 21.65939 1.000 33.80307  ? 94  ARG B HD2  1 
ATOM   5004 H HD3  . ARG B 1 108 ? -5.00963  -23.86869 21.95634 1.000 33.80307  ? 94  ARG B HD3  1 
ATOM   5005 H HE   . ARG B 1 108 ? -3.38951  -24.24768 20.49419 1.000 33.39540  ? 94  ARG B HE   1 
ATOM   5006 H HH11 . ARG B 1 108 ? -5.22100  -27.01580 20.66887 1.000 30.85861  ? 94  ARG B HH11 1 
ATOM   5007 H HH12 . ARG B 1 108 ? -4.66844  -27.63472 19.43177 1.000 30.85861  ? 94  ARG B HH12 1 
ATOM   5008 H HH21 . ARG B 1 108 ? -2.59565  -25.20644 18.62849 1.000 31.04100  ? 94  ARG B HH21 1 
ATOM   5009 H HH22 . ARG B 1 108 ? -3.08780  -26.54627 18.20252 1.000 31.04100  ? 94  ARG B HH22 1 
ATOM   5010 N N    . THR B 1 109 ? -6.26152  -23.71247 26.55307 1.000 27.79278  ? 95  THR B N    1 
ATOM   5011 C CA   . THR B 1 109 ? -7.58821  -23.38037 27.05037 1.000 28.95852  ? 95  THR B CA   1 
ATOM   5012 C C    . THR B 1 109 ? -8.31590  -22.69286 25.90436 1.000 29.47518  ? 95  THR B C    1 
ATOM   5013 O O    . THR B 1 109 ? -7.81511  -21.70727 25.35310 1.000 32.95828  ? 95  THR B O    1 
ATOM   5014 C CB   . THR B 1 109 ? -7.52024  -22.48753 28.29047 1.000 38.16264  ? 95  THR B CB   1 
ATOM   5015 O OG1  . THR B 1 109 ? -6.71058  -23.11754 29.29238 1.000 40.00415  ? 95  THR B OG1  1 
ATOM   5016 C CG2  . THR B 1 109 ? -8.91029  -22.25533 28.85699 1.000 40.53950  ? 95  THR B CG2  1 
ATOM   5017 H H    . THR B 1 109 ? -5.83215  -23.03044 26.25293 1.000 33.40728  ? 95  THR B H    1 
ATOM   5018 H HA   . THR B 1 109 ? -8.07212  -24.17943 27.31161 1.000 34.80616  ? 95  THR B HA   1 
ATOM   5019 H HB   . THR B 1 109 ? -7.13572  -21.63058 28.04821 1.000 45.85110  ? 95  THR B HB   1 
ATOM   5020 H HG1  . THR B 1 109 ? -6.92729  -22.83819 30.05435 1.000 48.06092  ? 95  THR B HG1  1 
ATOM   5021 H HG21 . THR B 1 109 ? -9.46151  -21.79470 28.20516 1.000 48.70334  ? 95  THR B HG21 1 
ATOM   5022 H HG22 . THR B 1 109 ? -9.32518  -23.10422 29.07641 1.000 48.70334  ? 95  THR B HG22 1 
ATOM   5023 H HG23 . THR B 1 109 ? -8.85502  -21.71492 29.66060 1.000 48.70334  ? 95  THR B HG23 1 
ATOM   5024 N N    . ILE B 1 110 ? -9.46400  -23.23713 25.51755 1.000 33.02696  ? 96  ILE B N    1 
ATOM   5025 C CA   . ILE B 1 110 ? -10.23353 -22.74216 24.38254 1.000 31.82059  ? 96  ILE B CA   1 
ATOM   5026 C C    . ILE B 1 110 ? -11.53981 -22.18113 24.92306 1.000 34.69303  ? 96  ILE B C    1 
ATOM   5027 O O    . ILE B 1 110 ? -12.41631 -22.93651 25.36020 1.000 29.48001  ? 96  ILE B O    1 
ATOM   5028 C CB   . ILE B 1 110 ? -10.49184 -23.84141 23.34432 1.000 29.25548  ? 96  ILE B CB   1 
ATOM   5029 C CG1  . ILE B 1 110 ? -9.16740  -24.44818 22.87687 1.000 30.58546  ? 96  ILE B CG1  1 
ATOM   5030 C CG2  . ILE B 1 110 ? -11.27297 -23.27466 22.16277 1.000 33.88829  ? 96  ILE B CG2  1 
ATOM   5031 C CD1  . ILE B 1 110 ? -9.31970  -25.74248 22.09036 1.000 33.70369  ? 96  ILE B CD1  1 
ATOM   5032 H H    . ILE B 1 110 ? -9.82682  -23.91220 25.90772 1.000 39.68829  ? 96  ILE B H    1 
ATOM   5033 H HA   . ILE B 1 110 ? -9.74344  -22.02301 23.95413 1.000 38.24064  ? 96  ILE B HA   1 
ATOM   5034 H HB   . ILE B 1 110 ? -11.02088 -24.54229 23.75635 1.000 35.16252  ? 96  ILE B HB   1 
ATOM   5035 H HG12 . ILE B 1 110 ? -8.71692  -23.80722 22.30491 1.000 36.75849  ? 96  ILE B HG12 1 
ATOM   5036 H HG13 . ILE B 1 110 ? -8.62139  -24.63919 23.65551 1.000 36.75849  ? 96  ILE B HG13 1 
ATOM   5037 H HG21 . ILE B 1 110 ? -10.84330 -22.45853 21.86242 1.000 40.72189  ? 96  ILE B HG21 1 
ATOM   5038 H HG22 . ILE B 1 110 ? -11.27958 -23.92812 21.44594 1.000 40.72189  ? 96  ILE B HG22 1 
ATOM   5039 H HG23 . ILE B 1 110 ? -12.18112 -23.08537 22.44620 1.000 40.72189  ? 96  ILE B HG23 1 
ATOM   5040 H HD11 . ILE B 1 110 ? -9.87109  -25.57487 21.31011 1.000 40.50037  ? 96  ILE B HD11 1 
ATOM   5041 H HD12 . ILE B 1 110 ? -8.44184  -26.04994 21.81516 1.000 40.50037  ? 96  ILE B HD12 1 
ATOM   5042 H HD13 . ILE B 1 110 ? -9.74095  -26.40821 22.65627 1.000 40.50037  ? 96  ILE B HD13 1 
ATOM   5043 N N    . PHE B 1 111 ? -11.67741 -20.85815 24.88485 1.000 28.40253  ? 97  PHE B N    1 
ATOM   5044 C CA   . PHE B 1 111 ? -12.86266 -20.18209 25.39883 1.000 31.80013  ? 97  PHE B CA   1 
ATOM   5045 C C    . PHE B 1 111 ? -13.85745 -19.99470 24.25993 1.000 33.59446  ? 97  PHE B C    1 
ATOM   5046 O O    . PHE B 1 111 ? -13.58578 -19.26430 23.30186 1.000 32.90023  ? 97  PHE B O    1 
ATOM   5047 C CB   . PHE B 1 111 ? -12.49196 -18.83875 26.02185 1.000 37.22009  ? 97  PHE B CB   1 
ATOM   5048 C CG   . PHE B 1 111 ? -11.60295 -18.95162 27.22805 1.000 38.00843  ? 97  PHE B CG   1 
ATOM   5049 C CD1  . PHE B 1 111 ? -12.14542 -19.11620 28.49149 1.000 35.31606  ? 97  PHE B CD1  1 
ATOM   5050 C CD2  . PHE B 1 111 ? -10.22540 -18.88501 27.09906 1.000 36.80841  ? 97  PHE B CD2  1 
ATOM   5051 C CE1  . PHE B 1 111 ? -11.33023 -19.21756 29.60294 1.000 44.10854  ? 97  PHE B CE1  1 
ATOM   5052 C CE2  . PHE B 1 111 ? -9.40539  -18.98379 28.20689 1.000 37.05943  ? 97  PHE B CE2  1 
ATOM   5053 C CZ   . PHE B 1 111 ? -9.95832  -19.15072 29.45988 1.000 45.78190  ? 97  PHE B CZ   1 
ATOM   5054 H H    . PHE B 1 111 ? -11.08763 -20.32282 24.56052 1.000 34.13897  ? 97  PHE B H    1 
ATOM   5055 H HA   . PHE B 1 111 ? -13.27310 -20.73655 26.08075 1.000 38.21609  ? 97  PHE B HA   1 
ATOM   5056 H HB2  . PHE B 1 111 ? -12.02454 -18.30661 25.35910 1.000 44.72005  ? 97  PHE B HB2  1 
ATOM   5057 H HB3  . PHE B 1 111 ? -13.30572 -18.38750 26.29581 1.000 44.72005  ? 97  PHE B HB3  1 
ATOM   5058 H HD1  . PHE B 1 111 ? -13.06885 -19.15902 28.59326 1.000 42.43521  ? 97  PHE B HD1  1 
ATOM   5059 H HD2  . PHE B 1 111 ? -9.84782  -18.77244 26.25665 1.000 44.22603  ? 97  PHE B HD2  1 
ATOM   5060 H HE1  . PHE B 1 111 ? -11.70525 -19.33069 30.44642 1.000 52.98619  ? 97  PHE B HE1  1 
ATOM   5061 H HE2  . PHE B 1 111 ? -8.48180  -18.93780 28.10801 1.000 44.52725  ? 97  PHE B HE2  1 
ATOM   5062 H HZ   . PHE B 1 111 ? -9.40820  -19.21808 30.20669 1.000 54.99422  ? 97  PHE B HZ   1 
ATOM   5063 N N    . PHE B 1 112 ? -15.00659 -20.65523 24.36227 1.000 35.40213  ? 98  PHE B N    1 
ATOM   5064 C CA   . PHE B 1 112 ? -16.10510 -20.44693 23.42892 1.000 31.48329  ? 98  PHE B CA   1 
ATOM   5065 C C    . PHE B 1 112 ? -16.94853 -19.28335 23.93552 1.000 34.14645  ? 98  PHE B C    1 
ATOM   5066 O O    . PHE B 1 112 ? -17.48769 -19.33696 25.04684 1.000 36.43562  ? 98  PHE B O    1 
ATOM   5067 C CB   . PHE B 1 112 ? -16.94146 -21.71667 23.28066 1.000 31.11850  ? 98  PHE B CB   1 
ATOM   5068 C CG   . PHE B 1 112 ? -16.20251 -22.85176 22.62568 1.000 32.84587  ? 98  PHE B CG   1 
ATOM   5069 C CD1  . PHE B 1 112 ? -15.47542 -23.75455 23.38430 1.000 30.43028  ? 98  PHE B CD1  1 
ATOM   5070 C CD2  . PHE B 1 112 ? -16.22796 -23.00945 21.24850 1.000 34.70405  ? 98  PHE B CD2  1 
ATOM   5071 C CE1  . PHE B 1 112 ? -14.79060 -24.79892 22.78135 1.000 36.41031  ? 98  PHE B CE1  1 
ATOM   5072 C CE2  . PHE B 1 112 ? -15.54555 -24.04940 20.63910 1.000 30.74571  ? 98  PHE B CE2  1 
ATOM   5073 C CZ   . PHE B 1 112 ? -14.82568 -24.94519 21.40656 1.000 34.12258  ? 98  PHE B CZ   1 
ATOM   5074 H H    . PHE B 1 112 ? -15.17521 -21.23704 24.97273 1.000 42.53849  ? 98  PHE B H    1 
ATOM   5075 H HA   . PHE B 1 112 ? -15.76033 -20.22318 22.55030 1.000 37.83589  ? 98  PHE B HA   1 
ATOM   5076 H HB2  . PHE B 1 112 ? -17.21913 -22.01258 24.16171 1.000 37.39814  ? 98  PHE B HB2  1 
ATOM   5077 H HB3  . PHE B 1 112 ? -17.71970 -21.51656 22.73734 1.000 37.39814  ? 98  PHE B HB3  1 
ATOM   5078 H HD1  . PHE B 1 112 ? -15.44621 -23.65910 24.30893 1.000 36.57228  ? 98  PHE B HD1  1 
ATOM   5079 H HD2  . PHE B 1 112 ? -16.70971 -22.40888 20.72683 1.000 41.70080  ? 98  PHE B HD2  1 
ATOM   5080 H HE1  . PHE B 1 112 ? -14.30810 -25.40051 23.30114 1.000 43.74832  ? 98  PHE B HE1  1 
ATOM   5081 H HE2  . PHE B 1 112 ? -15.57181 -24.14469 19.71437 1.000 36.95079  ? 98  PHE B HE2  1 
ATOM   5082 H HZ   . PHE B 1 112 ? -14.36630 -25.64411 20.99989 1.000 41.00304  ? 98  PHE B HZ   1 
ATOM   5083 N N    . LYS B 1 113 ? -17.04841 -18.23135 23.12763 1.000 34.76788  ? 99  LYS B N    1 
ATOM   5084 C CA   . LYS B 1 113 ? -17.72174 -17.01659 23.56405 1.000 35.45832  ? 99  LYS B CA   1 
ATOM   5085 C C    . LYS B 1 113 ? -19.15498 -17.31842 23.98010 1.000 37.34838  ? 99  LYS B C    1 
ATOM   5086 O O    . LYS B 1 113 ? -19.87955 -18.03910 23.28780 1.000 34.46822  ? 99  LYS B O    1 
ATOM   5087 C CB   . LYS B 1 113 ? -17.70359 -15.97330 22.44817 1.000 35.31516  ? 99  LYS B CB   1 
ATOM   5088 C CG   . LYS B 1 113 ? -18.14706 -14.59157 22.90161 1.000 42.03687  ? 99  LYS B CG   1 
ATOM   5089 C CD   . LYS B 1 113 ? -18.26289 -13.62723 21.73340 1.000 55.87264  ? 99  LYS B CD   1 
ATOM   5090 C CE   . LYS B 1 113 ? -18.78491 -12.27146 22.18725 1.000 57.97953  ? 99  LYS B CE   1 
ATOM   5091 N NZ   . LYS B 1 113 ? -19.00081 -11.34413 21.04370 1.000 84.65571  ? 99  LYS B NZ   1 
ATOM   5092 H H    . LYS B 1 113 ? -16.73621 -18.19695 22.32704 1.000 41.77739  ? 99  LYS B H    1 
ATOM   5093 H HA   . LYS B 1 113 ? -17.25278 -16.65076 24.33031 1.000 42.60592  ? 99  LYS B HA   1 
ATOM   5094 H HB2  . LYS B 1 113 ? -16.79924 -15.89753 22.10568 1.000 42.43413  ? 99  LYS B HB2  1 
ATOM   5095 H HB3  . LYS B 1 113 ? -18.30291 -16.26069 21.74169 1.000 42.43413  ? 99  LYS B HB3  1 
ATOM   5096 H HG2  . LYS B 1 113 ? -19.01558 -14.65771 23.32847 1.000 50.50019  ? 99  LYS B HG2  1 
ATOM   5097 H HG3  . LYS B 1 113 ? -17.49649 -14.23518 23.52663 1.000 50.50019  ? 99  LYS B HG3  1 
ATOM   5098 H HD2  . LYS B 1 113 ? -17.38877 -13.49998 21.33264 1.000 67.10311  ? 99  LYS B HD2  1 
ATOM   5099 H HD3  . LYS B 1 113 ? -18.87929 -13.98839 21.07726 1.000 67.10311  ? 99  LYS B HD3  1 
ATOM   5100 H HE2  . LYS B 1 113 ? -19.63257 -12.39235 22.64306 1.000 69.63137  ? 99  LYS B HE2  1 
ATOM   5101 H HE3  . LYS B 1 113 ? -18.14006 -11.86619 22.78795 1.000 69.63137  ? 99  LYS B HE3  1 
ATOM   5102 H HZ1  . LYS B 1 113 ? -18.23390 -11.20821 20.61303 1.000 101.64279 ? 99  LYS B HZ1  1 
ATOM   5103 H HZ2  . LYS B 1 113 ? -19.59249 -11.69206 20.47717 1.000 101.64279 ? 99  LYS B HZ2  1 
ATOM   5104 H HZ3  . LYS B 1 113 ? -19.30854 -10.56302 21.33913 1.000 101.64279 ? 99  LYS B HZ3  1 
ATOM   5105 N N    . ASP B 1 114 ? -19.55913 -16.76046 25.12133 1.000 41.70491  ? 100 ASP B N    1 
ATOM   5106 C CA   . ASP B 1 114 ? -20.90802 -16.94626 25.65413 1.000 42.09434  ? 100 ASP B CA   1 
ATOM   5107 C C    . ASP B 1 114 ? -21.23602 -18.42721 25.83083 1.000 36.93932  ? 100 ASP B C    1 
ATOM   5108 O O    . ASP B 1 114 ? -22.37680 -18.85525 25.64400 1.000 39.74558  ? 100 ASP B O    1 
ATOM   5109 C CB   . ASP B 1 114 ? -21.94834 -16.26365 24.76189 1.000 42.55201  ? 100 ASP B CB   1 
ATOM   5110 C CG   . ASP B 1 114 ? -21.83709 -14.75179 24.78737 1.000 49.80190  ? 100 ASP B CG   1 
ATOM   5111 O OD1  . ASP B 1 114 ? -21.03993 -14.22516 25.59204 1.000 55.67400  ? 100 ASP B OD1  1 
ATOM   5112 O OD2  . ASP B 1 114 ? -22.54782 -14.08773 24.00342 1.000 52.31231  ? 100 ASP B OD2  1 
ATOM   5113 H H    . ASP B 1 114 ? -19.06138 -16.26114 25.61379 1.000 50.10183  ? 100 ASP B H    1 
ATOM   5114 H HA   . ASP B 1 114 ? -20.94786 -16.53523 26.53184 1.000 50.56915  ? 100 ASP B HA   1 
ATOM   5115 H HB2  . ASP B 1 114 ? -21.82273 -16.55876 23.84645 1.000 51.11835  ? 100 ASP B HB2  1 
ATOM   5116 H HB3  . ASP B 1 114 ? -22.83616 -16.50480 25.06934 1.000 51.11835  ? 100 ASP B HB3  1 
ATOM   5117 N N    . ASP B 1 115 ? -20.23245 -19.21693 26.19890 1.000 43.79354  ? 101 ASP B N    1 
ATOM   5118 C CA   . ASP B 1 115 ? -20.42511 -20.65074 26.38158 1.000 39.78865  ? 101 ASP B CA   1 
ATOM   5119 C C    . ASP B 1 115 ? -19.24260 -21.20055 27.17935 1.000 38.72758  ? 101 ASP B C    1 
ATOM   5120 O O    . ASP B 1 115 ? -18.48381 -20.43635 27.78596 1.000 37.99433  ? 101 ASP B O    1 
ATOM   5121 C CB   . ASP B 1 115 ? -20.59381 -21.34543 25.02010 1.000 37.38265  ? 101 ASP B CB   1 
ATOM   5122 C CG   . ASP B 1 115 ? -21.45748 -22.58682 25.10555 1.000 40.94138  ? 101 ASP B CG   1 
ATOM   5123 O OD1  . ASP B 1 115 ? -21.57835 -23.14994 26.21252 1.000 40.44054  ? 101 ASP B OD1  1 
ATOM   5124 O OD2  . ASP B 1 115 ? -22.01902 -22.99807 24.06892 1.000 45.80384  ? 101 ASP B OD2  1 
ATOM   5125 H H    . ASP B 1 115 ? -19.43016 -18.94597 26.34897 1.000 52.60819  ? 101 ASP B H    1 
ATOM   5126 H HA   . ASP B 1 115 ? -21.23302 -20.78386 26.90165 1.000 47.80232  ? 101 ASP B HA   1 
ATOM   5127 H HB2  . ASP B 1 115 ? -21.01323 -20.72911 24.39951 1.000 44.91512  ? 101 ASP B HB2  1 
ATOM   5128 H HB3  . ASP B 1 115 ? -19.72115 -21.60818 24.68795 1.000 44.91512  ? 101 ASP B HB3  1 
ATOM   5129 N N    . GLY B 1 116 ? -19.08371 -22.52242 27.17287 1.000 42.05967  ? 102 GLY B N    1 
ATOM   5130 C CA   . GLY B 1 116 ? -18.07581 -23.18125 27.97468 1.000 38.68970  ? 102 GLY B CA   1 
ATOM   5131 C C    . GLY B 1 116 ? -16.68357 -23.05378 27.38678 1.000 36.25034  ? 102 GLY B C    1 
ATOM   5132 O O    . GLY B 1 116 ? -16.43297 -22.31264 26.43495 1.000 29.55387  ? 102 GLY B O    1 
ATOM   5133 H H    . GLY B 1 116 ? -19.55903 -23.06266 26.70190 1.000 50.52754  ? 102 GLY B H    1 
ATOM   5134 H HA2  . GLY B 1 116 ? -18.06794 -22.79076 28.86257 1.000 46.48358  ? 102 GLY B HA2  1 
ATOM   5135 H HA3  . GLY B 1 116 ? -18.29047 -24.12448 28.04640 1.000 46.48358  ? 102 GLY B HA3  1 
ATOM   5136 N N    . ASN B 1 117 ? -15.75721 -23.80872 27.97953 1.000 32.16840  ? 103 ASN B N    1 
ATOM   5137 C CA   . ASN B 1 117 ? -14.35513 -23.76352 27.59188 1.000 29.56079  ? 103 ASN B CA   1 
ATOM   5138 C C    . ASN B 1 117 ? -13.73957 -25.15217 27.67322 1.000 31.59476  ? 103 ASN B C    1 
ATOM   5139 O O    . ASN B 1 117 ? -14.06570 -25.93576 28.56989 1.000 29.88721  ? 103 ASN B O    1 
ATOM   5140 C CB   . ASN B 1 117 ? -13.56129 -22.80352 28.48674 1.000 32.64114  ? 103 ASN B CB   1 
ATOM   5141 C CG   . ASN B 1 117 ? -13.53674 -23.24764 29.93834 1.000 38.42577  ? 103 ASN B CG   1 
ATOM   5142 O OD1  . ASN B 1 117 ? -12.71154 -24.07202 30.33426 1.000 32.78356  ? 103 ASN B OD1  1 
ATOM   5143 N ND2  . ASN B 1 117 ? -14.44569 -22.70301 30.73872 1.000 32.94740  ? 103 ASN B ND2  1 
ATOM   5144 H H    . ASN B 1 117 ? -15.92273 -24.36138 28.61732 1.000 38.65802  ? 103 ASN B H    1 
ATOM   5145 H HA   . ASN B 1 117 ? -14.29495 -23.46331 26.67147 1.000 35.52889  ? 103 ASN B HA   1 
ATOM   5146 H HB2  . ASN B 1 117 ? -12.64551 -22.75918 28.17009 1.000 39.22531  ? 103 ASN B HB2  1 
ATOM   5147 H HB3  . ASN B 1 117 ? -13.96868 -21.92407 28.44798 1.000 39.22531  ? 103 ASN B HB3  1 
ATOM   5148 H HD21 . ASN B 1 117 ? -14.47308 -22.92185 31.56995 1.000 39.59282  ? 103 ASN B HD21 1 
ATOM   5149 H HD22 . ASN B 1 117 ? -15.00695 -22.13145 30.42582 1.000 39.59282  ? 103 ASN B HD22 1 
ATOM   5150 N N    . TYR B 1 118 ? -12.84415 -25.44231 26.73059 1.000 29.90934  ? 104 TYR B N    1 
ATOM   5151 C CA   . TYR B 1 118 ? -12.05642 -26.66579 26.74251 1.000 26.55429  ? 104 TYR B CA   1 
ATOM   5152 C C    . TYR B 1 118 ? -10.73469 -26.43572 27.46306 1.000 28.35079  ? 104 TYR B C    1 
ATOM   5153 O O    . TYR B 1 118 ? -10.11006 -25.38101 27.31581 1.000 28.67561  ? 104 TYR B O    1 
ATOM   5154 C CB   . TYR B 1 118 ? -11.74696 -27.14497 25.32088 1.000 26.42273  ? 104 TYR B CB   1 
ATOM   5155 C CG   . TYR B 1 118 ? -12.91411 -27.66031 24.50891 1.000 29.81334  ? 104 TYR B CG   1 
ATOM   5156 C CD1  . TYR B 1 118 ? -14.09912 -28.05551 25.11237 1.000 26.84522  ? 104 TYR B CD1  1 
ATOM   5157 C CD2  . TYR B 1 118 ? -12.81618 -27.76539 23.12704 1.000 26.81568  ? 104 TYR B CD2  1 
ATOM   5158 C CE1  . TYR B 1 118 ? -15.15581 -28.52994 24.36082 1.000 27.71357  ? 104 TYR B CE1  1 
ATOM   5159 C CE2  . TYR B 1 118 ? -13.86369 -28.23701 22.36948 1.000 25.28956  ? 104 TYR B CE2  1 
ATOM   5160 C CZ   . TYR B 1 118 ? -15.02980 -28.61900 22.98728 1.000 27.40692  ? 104 TYR B CZ   1 
ATOM   5161 O OH   . TYR B 1 118 ? -16.06775 -29.09032 22.21990 1.000 25.35164  ? 104 TYR B OH   1 
ATOM   5162 H H    . TYR B 1 118 ? -12.67305 -24.93253 26.05943 1.000 35.94715  ? 104 TYR B H    1 
ATOM   5163 H HA   . TYR B 1 118 ? -12.56695 -27.35071 27.20202 1.000 31.92109  ? 104 TYR B HA   1 
ATOM   5164 H HB2  . TYR B 1 118 ? -11.36616 -26.40061 24.82912 1.000 31.76322  ? 104 TYR B HB2  1 
ATOM   5165 H HB3  . TYR B 1 118 ? -11.10241 -27.86736 25.38092 1.000 31.76322  ? 104 TYR B HB3  1 
ATOM   5166 H HD1  . TYR B 1 118 ? -14.18304 -28.00007 26.03692 1.000 32.27020  ? 104 TYR B HD1  1 
ATOM   5167 H HD2  . TYR B 1 118 ? -12.02687 -27.51192 22.70556 1.000 32.23476  ? 104 TYR B HD2  1 
ATOM   5168 H HE1  . TYR B 1 118 ? -15.94701 -28.78783 24.77602 1.000 33.31223  ? 104 TYR B HE1  1 
ATOM   5169 H HE2  . TYR B 1 118 ? -13.78274 -28.29679 21.44494 1.000 30.40341  ? 104 TYR B HE2  1 
ATOM   5170 H HH   . TYR B 1 118 ? -15.82457 -29.15922 21.41883 1.000 30.47790  ? 104 TYR B HH   1 
ATOM   5171 N N    . LYS B 1 119 ? -10.30235 -27.43864 28.22351 1.000 27.79908  ? 105 LYS B N    1 
ATOM   5172 C CA   . LYS B 1 119 ? -8.94019  -27.51511 28.73918 1.000 33.75251  ? 105 LYS B CA   1 
ATOM   5173 C C    . LYS B 1 119 ? -8.31599  -28.79243 28.19919 1.000 27.69127  ? 105 LYS B C    1 
ATOM   5174 O O    . LYS B 1 119 ? -8.78594  -29.89230 28.50932 1.000 29.30627  ? 105 LYS B O    1 
ATOM   5175 C CB   . LYS B 1 119 ? -8.90221  -27.51455 30.26846 1.000 30.62885  ? 105 LYS B CB   1 
ATOM   5176 C CG   . LYS B 1 119 ? -9.35654  -26.22210 30.92038 1.000 44.99483  ? 105 LYS B CG   1 
ATOM   5177 C CD   . LYS B 1 119 ? -8.81475  -26.11028 32.34330 1.000 53.34963  ? 105 LYS B CD   1 
ATOM   5178 C CE   . LYS B 1 119 ? -9.89553  -25.71949 33.33581 1.000 53.34980  ? 105 LYS B CE   1 
ATOM   5179 N NZ   . LYS B 1 119 ? -10.90801 -26.79873 33.51487 1.000 54.82983  ? 105 LYS B NZ   1 
ATOM   5180 H H    . LYS B 1 119 ? -10.79389 -28.10361 28.45975 1.000 33.41484  ? 105 LYS B H    1 
ATOM   5181 H HA   . LYS B 1 119 ? -8.43545  -26.74531 28.43333 1.000 40.55895  ? 105 LYS B HA   1 
ATOM   5182 H HB2  . LYS B 1 119 ? -9.48235  -28.22224 30.59022 1.000 36.81056  ? 105 LYS B HB2  1 
ATOM   5183 H HB3  . LYS B 1 119 ? -7.98951  -27.67867 30.55296 1.000 36.81056  ? 105 LYS B HB3  1 
ATOM   5184 H HG2  . LYS B 1 119 ? -9.02858  -25.46767 30.40640 1.000 54.04974  ? 105 LYS B HG2  1 
ATOM   5185 H HG3  . LYS B 1 119 ? -10.32560 -26.20181 30.95795 1.000 54.04974  ? 105 LYS B HG3  1 
ATOM   5186 H HD2  . LYS B 1 119 ? -8.45062  -26.96747 32.61449 1.000 64.07550  ? 105 LYS B HD2  1 
ATOM   5187 H HD3  . LYS B 1 119 ? -8.12143  -25.43237 32.36851 1.000 64.07550  ? 105 LYS B HD3  1 
ATOM   5188 H HE2  . LYS B 1 119 ? -9.48773  -25.54105 34.19764 1.000 64.07570  ? 105 LYS B HE2  1 
ATOM   5189 H HE3  . LYS B 1 119 ? -10.35219 -24.92640 33.01429 1.000 64.07570  ? 105 LYS B HE3  1 
ATOM   5190 H HZ1  . LYS B 1 119 ? -10.50133 -27.57449 33.67270 1.000 65.85173  ? 105 LYS B HZ1  1 
ATOM   5191 H HZ2  . LYS B 1 119 ? -11.43975 -26.60629 34.20212 1.000 65.85173  ? 105 LYS B HZ2  1 
ATOM   5192 H HZ3  . LYS B 1 119 ? -11.40322 -26.87659 32.77947 1.000 65.85173  ? 105 LYS B HZ3  1 
ATOM   5193 N N    . THR B 1 120 ? -7.26507  -28.65002 27.39972 1.000 24.79805  ? 106 THR B N    1 
ATOM   5194 C CA   . THR B 1 120 ? -6.63091  -29.78288 26.74723 1.000 31.20587  ? 106 THR B CA   1 
ATOM   5195 C C    . THR B 1 120 ? -5.17410  -29.88652 27.17225 1.000 29.33273  ? 106 THR B C    1 
ATOM   5196 O O    . THR B 1 120 ? -4.50226  -28.87935 27.41260 1.000 27.62793  ? 106 THR B O    1 
ATOM   5197 C CB   . THR B 1 120 ? -6.71105  -29.66647 25.21832 1.000 25.84055  ? 106 THR B CB   1 
ATOM   5198 O OG1  . THR B 1 120 ? -5.84841  -28.61522 24.76831 1.000 27.99841  ? 106 THR B OG1  1 
ATOM   5199 C CG2  . THR B 1 120 ? -8.13360  -29.36597 24.78036 1.000 24.08468  ? 106 THR B CG2  1 
ATOM   5200 H H    . THR B 1 120 ? -6.89744  -27.89395 27.21861 1.000 29.81360  ? 106 THR B H    1 
ATOM   5201 H HA   . THR B 1 120 ? -7.08407  -30.59719 27.01638 1.000 37.50298  ? 106 THR B HA   1 
ATOM   5202 H HB   . THR B 1 120 ? -6.43571  -30.50574 24.81743 1.000 31.06460  ? 106 THR B HB   1 
ATOM   5203 H HG1  . THR B 1 120 ? -5.12991  -28.93818 24.47668 1.000 33.65404  ? 106 THR B HG1  1 
ATOM   5204 H HG21 . THR B 1 120 ? -8.29407  -29.73532 23.89790 1.000 28.95755  ? 106 THR B HG21 1 
ATOM   5205 H HG22 . THR B 1 120 ? -8.76307  -29.75869 25.40521 1.000 28.95755  ? 106 THR B HG22 1 
ATOM   5206 H HG23 . THR B 1 120 ? -8.27608  -28.40695 24.75090 1.000 28.95755  ? 106 THR B HG23 1 
ATOM   5207 N N    . ARG B 1 121 ? -4.69939  -31.12309 27.27266 1.000 27.91882  ? 107 ARG B N    1 
ATOM   5208 C CA   . ARG B 1 121 ? -3.29500  -31.40451 27.52140 1.000 27.70104  ? 107 ARG B CA   1 
ATOM   5209 C C    . ARG B 1 121 ? -2.90421  -32.60102 26.67276 1.000 26.71253  ? 107 ARG B C    1 
ATOM   5210 O O    . ARG B 1 121 ? -3.57933  -33.63396 26.70768 1.000 30.24869  ? 107 ARG B O    1 
ATOM   5211 C CB   . ARG B 1 121 ? -3.03025  -31.68601 29.00083 1.000 23.58703  ? 107 ARG B CB   1 
ATOM   5212 C CG   . ARG B 1 121 ? -1.56527  -31.92576 29.30445 1.000 30.13083  ? 107 ARG B CG   1 
ATOM   5213 C CD   . ARG B 1 121 ? -1.27598  -31.87765 30.79023 1.000 32.23376  ? 107 ARG B CD   1 
ATOM   5214 N NE   . ARG B 1 121 ? 0.15801   -31.87509 31.05205 1.000 35.62861  ? 107 ARG B NE   1 
ATOM   5215 C CZ   . ARG B 1 121 ? 0.92220   -32.95857 31.05270 1.000 33.91300  ? 107 ARG B CZ   1 
ATOM   5216 N NH1  . ARG B 1 121 ? 0.42172   -34.15854 30.80756 1.000 43.08090  ? 107 ARG B NH1  1 
ATOM   5217 N NH2  . ARG B 1 121 ? 2.22220   -32.83476 31.30295 1.000 36.64762  ? 107 ARG B NH2  1 
ATOM   5218 H H    . ARG B 1 121 ? -5.18342  -31.83006 27.19843 1.000 33.55852  ? 107 ARG B H    1 
ATOM   5219 H HA   . ARG B 1 121 ? -2.74995  -30.64306 27.26837 1.000 33.29718  ? 107 ARG B HA   1 
ATOM   5220 H HB2  . ARG B 1 121 ? -3.32356  -30.92351 29.52376 1.000 28.02473  ? 107 ARG B HB2  1 
ATOM   5221 H HB3  . ARG B 1 121 ? -3.52413  -32.47837 29.26379 1.000 28.02473  ? 107 ARG B HB3  1 
ATOM   5222 H HG2  . ARG B 1 121 ? -1.31042  -32.80180 28.97506 1.000 36.21294  ? 107 ARG B HG2  1 
ATOM   5223 H HG3  . ARG B 1 121 ? -1.03325  -31.24050 28.87054 1.000 36.21294  ? 107 ARG B HG3  1 
ATOM   5224 H HD2  . ARG B 1 121 ? -1.65675  -31.06852 31.16602 1.000 38.73646  ? 107 ARG B HD2  1 
ATOM   5225 H HD3  . ARG B 1 121 ? -1.66355  -32.65678 31.21877 1.000 38.73646  ? 107 ARG B HD3  1 
ATOM   5226 H HE   . ARG B 1 121 ? 0.53389   -31.11945 31.21731 1.000 42.81027  ? 107 ARG B HE   1 
ATOM   5227 H HH11 . ARG B 1 121 ? -0.41748  -34.24897 30.64276 1.000 51.75302  ? 107 ARG B HH11 1 
ATOM   5228 H HH12 . ARG B 1 121 ? 0.93562   -34.84809 30.81300 1.000 51.75302  ? 107 ARG B HH12 1 
ATOM   5229 H HH21 . ARG B 1 121 ? 2.55755   -32.05892 31.46173 1.000 44.03309  ? 107 ARG B HH21 1 
ATOM   5230 H HH22 . ARG B 1 121 ? 2.72767   -33.53052 31.30603 1.000 44.03309  ? 107 ARG B HH22 1 
ATOM   5231 N N    . ALA B 1 122 ? -1.82743  -32.45857 25.90713 1.000 23.86272  ? 108 ALA B N    1 
ATOM   5232 C CA   . ALA B 1 122 ? -1.41747  -33.49143 24.97246 1.000 27.56968  ? 108 ALA B CA   1 
ATOM   5233 C C    . ALA B 1 122 ? 0.09312   -33.65008 25.00881 1.000 26.68304  ? 108 ALA B C    1 
ATOM   5234 O O    . ALA B 1 122 ? 0.82843   -32.70177 25.28990 1.000 29.37794  ? 108 ALA B O    1 
ATOM   5235 C CB   . ALA B 1 122 ? -1.87388  -33.16481 23.54344 1.000 27.22951  ? 108 ALA B CB   1 
ATOM   5236 H H    . ALA B 1 122 ? -1.31660  -31.76676 25.91325 1.000 28.69120  ? 108 ALA B H    1 
ATOM   5237 H HA   . ALA B 1 122 ? -1.81038  -34.33781 25.23734 1.000 33.13956  ? 108 ALA B HA   1 
ATOM   5238 H HB1  . ALA B 1 122 ? -2.84029  -33.08229 23.53167 1.000 32.73135  ? 108 ALA B HB1  1 
ATOM   5239 H HB2  . ALA B 1 122 ? -1.46714  -32.32932 23.26521 1.000 32.73135  ? 108 ALA B HB2  1 
ATOM   5240 H HB3  . ALA B 1 122 ? -1.59585  -33.88128 22.95160 1.000 32.73135  ? 108 ALA B HB3  1 
ATOM   5241 N N    . GLU B 1 123 ? 0.54396   -34.86796 24.72753 1.000 27.42396  ? 109 GLU B N    1 
ATOM   5242 C CA   . GLU B 1 123 ? 1.95314   -35.17358 24.52619 1.000 28.48573  ? 109 GLU B CA   1 
ATOM   5243 C C    . GLU B 1 123 ? 2.13341   -35.53858 23.05808 1.000 27.21436  ? 109 GLU B C    1 
ATOM   5244 O O    . GLU B 1 123 ? 1.56560   -36.53112 22.58960 1.000 28.67734  ? 109 GLU B O    1 
ATOM   5245 C CB   . GLU B 1 123 ? 2.41261   -36.31486 25.43413 1.000 28.64498  ? 109 GLU B CB   1 
ATOM   5246 C CG   . GLU B 1 123 ? 2.21929   -36.05730 26.91593 1.000 38.87048  ? 109 GLU B CG   1 
ATOM   5247 C CD   . GLU B 1 123 ? 2.84039   -37.14123 27.77807 1.000 47.44724  ? 109 GLU B CD   1 
ATOM   5248 O OE1  . GLU B 1 123 ? 3.13913   -38.23047 27.24354 1.000 47.80527  ? 109 GLU B OE1  1 
ATOM   5249 O OE2  . GLU B 1 123 ? 3.03558   -36.90198 28.98831 1.000 46.54364  ? 109 GLU B OE2  1 
ATOM   5250 H H    . GLU B 1 123 ? 0.03411   -35.55569 24.64582 1.000 32.96469  ? 109 GLU B H    1 
ATOM   5251 H HA   . GLU B 1 123 ? 2.49887   -34.39951 24.73574 1.000 34.23882  ? 109 GLU B HA   1 
ATOM   5252 H HB2  . GLU B 1 123 ? 1.90859   -37.11198 25.20725 1.000 34.42992  ? 109 GLU B HB2  1 
ATOM   5253 H HB3  . GLU B 1 123 ? 3.35884   -36.46681 25.28431 1.000 34.42992  ? 109 GLU B HB3  1 
ATOM   5254 H HG2  . GLU B 1 123 ? 2.63528   -35.21234 27.14808 1.000 46.70052  ? 109 GLU B HG2  1 
ATOM   5255 H HG3  . GLU B 1 123 ? 1.26970   -36.02427 27.11106 1.000 46.70052  ? 109 GLU B HG3  1 
ATOM   5256 N N    . VAL B 1 124 ? 2.89095   -34.72206 22.33195 1.000 30.51978  ? 110 VAL B N    1 
ATOM   5257 C CA   . VAL B 1 124 ? 3.25498   -34.99888 20.94699 1.000 29.34345  ? 110 VAL B CA   1 
ATOM   5258 C C    . VAL B 1 124 ? 4.69205   -35.49738 20.94281 1.000 31.36468  ? 110 VAL B C    1 
ATOM   5259 O O    . VAL B 1 124 ? 5.61196   -34.75705 21.30837 1.000 30.63121  ? 110 VAL B O    1 
ATOM   5260 C CB   . VAL B 1 124 ? 3.10271   -33.75165 20.06217 1.000 31.98470  ? 110 VAL B CB   1 
ATOM   5261 C CG1  . VAL B 1 124 ? 3.28995   -34.11515 18.58476 1.000 28.63556  ? 110 VAL B CG1  1 
ATOM   5262 C CG2  . VAL B 1 124 ? 1.75427   -33.09216 20.30240 1.000 30.83806  ? 110 VAL B CG2  1 
ATOM   5263 H H    . VAL B 1 124 ? 3.21421   -33.98219 22.62808 1.000 36.67968  ? 110 VAL B H    1 
ATOM   5264 H HA   . VAL B 1 124 ? 2.67840   -35.69329 20.59167 1.000 35.26808  ? 110 VAL B HA   1 
ATOM   5265 H HB   . VAL B 1 124 ? 3.79108   -33.10953 20.29611 1.000 38.43758  ? 110 VAL B HB   1 
ATOM   5266 H HG11 . VAL B 1 124 ? 3.70943   -34.98771 18.52494 1.000 34.41861  ? 110 VAL B HG11 1 
ATOM   5267 H HG12 . VAL B 1 124 ? 2.42208   -34.13499 18.15198 1.000 34.41861  ? 110 VAL B HG12 1 
ATOM   5268 H HG13 . VAL B 1 124 ? 3.85407   -33.44741 18.16429 1.000 34.41861  ? 110 VAL B HG13 1 
ATOM   5269 H HG21 . VAL B 1 124 ? 1.10714   -33.77426 20.54088 1.000 37.06161  ? 110 VAL B HG21 1 
ATOM   5270 H HG22 . VAL B 1 124 ? 1.84060   -32.45098 21.02513 1.000 37.06161  ? 110 VAL B HG22 1 
ATOM   5271 H HG23 . VAL B 1 124 ? 1.47470   -32.64024 19.49092 1.000 37.06161  ? 110 VAL B HG23 1 
ATOM   5272 N N    . LYS B 1 125 ? 4.89157   -36.74514 20.52788 1.000 30.74369  ? 111 LYS B N    1 
ATOM   5273 C CA   . LYS B 1 125 ? 6.21905   -37.34253 20.54432 1.000 28.58907  ? 111 LYS B CA   1 
ATOM   5274 C C    . LYS B 1 125 ? 6.23641   -38.53435 19.59898 1.000 30.15622  ? 111 LYS B C    1 
ATOM   5275 O O    . LYS B 1 125 ? 5.19229   -39.03108 19.17064 1.000 29.44430  ? 111 LYS B O    1 
ATOM   5276 C CB   . LYS B 1 125 ? 6.61824   -37.76712 21.96116 1.000 31.22681  ? 111 LYS B CB   1 
ATOM   5277 C CG   . LYS B 1 125 ? 5.70357   -38.82255 22.57702 1.000 28.81179  ? 111 LYS B CG   1 
ATOM   5278 C CD   . LYS B 1 125 ? 6.14227   -39.16554 23.99332 1.000 34.10083  ? 111 LYS B CD   1 
ATOM   5279 C CE   . LYS B 1 125 ? 5.23076   -40.20047 24.63798 1.000 42.44639  ? 111 LYS B CE   1 
ATOM   5280 N NZ   . LYS B 1 125 ? 3.90259   -39.63682 25.00837 1.000 38.78001  ? 111 LYS B NZ   1 
ATOM   5281 H H    . LYS B 1 125 ? 4.27321   -37.26480 20.23261 1.000 36.94836  ? 111 LYS B H    1 
ATOM   5282 H HA   . LYS B 1 125 ? 6.86132   -36.69137 20.22123 1.000 34.36282  ? 111 LYS B HA   1 
ATOM   5283 H HB2  . LYS B 1 125 ? 7.51551   -38.13462 21.93385 1.000 37.52811  ? 111 LYS B HB2  1 
ATOM   5284 H HB3  . LYS B 1 125 ? 6.59677   -36.98663 22.53672 1.000 37.52811  ? 111 LYS B HB3  1 
ATOM   5285 H HG2  . LYS B 1 125 ? 4.79547   -38.48326 22.61070 1.000 34.63009  ? 111 LYS B HG2  1 
ATOM   5286 H HG3  . LYS B 1 125 ? 5.73616   -39.63064 22.04146 1.000 34.63009  ? 111 LYS B HG3  1 
ATOM   5287 H HD2  . LYS B 1 125 ? 7.04206   -39.52714 23.97021 1.000 40.97694  ? 111 LYS B HD2  1 
ATOM   5288 H HD3  . LYS B 1 125 ? 6.12120   -38.36279 24.53742 1.000 40.97694  ? 111 LYS B HD3  1 
ATOM   5289 H HE2  . LYS B 1 125 ? 5.08531   -40.92834 24.01352 1.000 50.99161  ? 111 LYS B HE2  1 
ATOM   5290 H HE3  . LYS B 1 125 ? 5.65150   -40.53510 25.44538 1.000 50.99161  ? 111 LYS B HE3  1 
ATOM   5291 H HZ1  . LYS B 1 125 ? 4.00919   -38.92671 25.53419 1.000 46.59196  ? 111 LYS B HZ1  1 
ATOM   5292 H HZ2  . LYS B 1 125 ? 3.46158   -39.39012 24.27574 1.000 46.59196  ? 111 LYS B HZ2  1 
ATOM   5293 H HZ3  . LYS B 1 125 ? 3.42278   -40.24808 25.44224 1.000 46.59196  ? 111 LYS B HZ3  1 
ATOM   5294 N N    . PHE B 1 126 ? 7.44652   -38.98645 19.27982 1.000 28.06505  ? 112 PHE B N    1 
ATOM   5295 C CA   . PHE B 1 126 ? 7.62490   -40.16569 18.44695 1.000 34.99043  ? 112 PHE B CA   1 
ATOM   5296 C C    . PHE B 1 126 ? 7.56451   -41.42740 19.29890 1.000 34.72465  ? 112 PHE B C    1 
ATOM   5297 O O    . PHE B 1 126 ? 8.19340   -41.50429 20.35942 1.000 36.45590  ? 112 PHE B O    1 
ATOM   5298 C CB   . PHE B 1 126 ? 8.96286   -40.10749 17.71022 1.000 31.92465  ? 112 PHE B CB   1 
ATOM   5299 C CG   . PHE B 1 126 ? 8.93365   -39.29585 16.44757 1.000 29.08392  ? 112 PHE B CG   1 
ATOM   5300 C CD1  . PHE B 1 126 ? 8.58511   -39.88023 15.24120 1.000 34.08912  ? 112 PHE B CD1  1 
ATOM   5301 C CD2  . PHE B 1 126 ? 9.27279   -37.95489 16.46303 1.000 28.85931  ? 112 PHE B CD2  1 
ATOM   5302 C CE1  . PHE B 1 126 ? 8.56666   -39.13782 14.07465 1.000 29.11388  ? 112 PHE B CE1  1 
ATOM   5303 C CE2  . PHE B 1 126 ? 9.25604   -37.20861 15.30248 1.000 33.44569  ? 112 PHE B CE2  1 
ATOM   5304 C CZ   . PHE B 1 126 ? 8.90354   -37.80114 14.10609 1.000 32.56379  ? 112 PHE B CZ   1 
ATOM   5305 H H    . PHE B 1 126 ? 8.18313   -38.62395 19.53595 1.000 33.73400  ? 112 PHE B H    1 
ATOM   5306 H HA   . PHE B 1 126 ? 6.91131   -40.19721 17.79067 1.000 42.04445  ? 112 PHE B HA   1 
ATOM   5307 H HB2  . PHE B 1 126 ? 9.62454   -39.71216 18.29912 1.000 38.36552  ? 112 PHE B HB2  1 
ATOM   5308 H HB3  . PHE B 1 126 ? 9.22653   -41.01052 17.47373 1.000 38.36552  ? 112 PHE B HB3  1 
ATOM   5309 H HD1  . PHE B 1 126 ? 8.36088   -40.78243 15.21538 1.000 40.96288  ? 112 PHE B HD1  1 
ATOM   5310 H HD2  . PHE B 1 126 ? 9.51500   -37.55147 17.26521 1.000 34.68711  ? 112 PHE B HD2  1 
ATOM   5311 H HE1  . PHE B 1 126 ? 8.32753   -39.53928 13.27057 1.000 34.99259  ? 112 PHE B HE1  1 
ATOM   5312 H HE2  . PHE B 1 126 ? 9.48211   -36.30682 15.32607 1.000 40.19077  ? 112 PHE B HE2  1 
ATOM   5313 H HZ   . PHE B 1 126 ? 8.89336   -37.29958 13.32300 1.000 39.13249  ? 112 PHE B HZ   1 
ATOM   5314 N N    . GLU B 1 127 ? 6.80013   -42.40953 18.83254 1.000 36.54335  ? 113 GLU B N    1 
ATOM   5315 C CA   . GLU B 1 127 ? 6.80489   -43.76804 19.37005 1.000 39.52352  ? 113 GLU B CA   1 
ATOM   5316 C C    . GLU B 1 127 ? 7.23754   -44.66342 18.21239 1.000 40.56063  ? 113 GLU B C    1 
ATOM   5317 O O    . GLU B 1 127 ? 6.42508   -45.01472 17.35093 1.000 32.34316  ? 113 GLU B O    1 
ATOM   5318 C CB   . GLU B 1 127 ? 5.43763   -44.15722 19.92052 1.000 35.73282  ? 113 GLU B CB   1 
ATOM   5319 C CG   . GLU B 1 127 ? 4.96446   -43.26849 21.06208 1.000 46.30489  ? 113 GLU B CG   1 
ATOM   5320 C CD   . GLU B 1 127 ? 3.58110   -43.63794 21.55986 1.000 49.55883  ? 113 GLU B CD   1 
ATOM   5321 O OE1  . GLU B 1 127 ? 3.06383   -44.69793 21.15108 1.000 54.96588  ? 113 GLU B OE1  1 
ATOM   5322 O OE2  . GLU B 1 127 ? 3.01022   -42.86550 22.35886 1.000 48.60268  ? 113 GLU B OE2  1 
ATOM   5323 H H    . GLU B 1 127 ? 6.24900   -42.31005 18.17989 1.000 43.90796  ? 113 GLU B H    1 
ATOM   5324 H HA   . GLU B 1 127 ? 7.43561   -43.84918 20.10251 1.000 47.48417  ? 113 GLU B HA   1 
ATOM   5325 H HB2  . GLU B 1 127 ? 4.78429   -44.09577 19.20619 1.000 42.93533  ? 113 GLU B HB2  1 
ATOM   5326 H HB3  . GLU B 1 127 ? 5.48203   -45.06771 20.25208 1.000 42.93533  ? 113 GLU B HB3  1 
ATOM   5327 H HG2  . GLU B 1 127 ? 5.58260   -43.35244 21.80487 1.000 55.62180  ? 113 GLU B HG2  1 
ATOM   5328 H HG3  . GLU B 1 127 ? 4.93696   -42.34855 20.75570 1.000 55.62180  ? 113 GLU B HG3  1 
ATOM   5329 N N    . GLY B 1 128 ? 8.51840   -45.01079 18.18265 1.000 35.60091  ? 114 GLY B N    1 
ATOM   5330 C CA   . GLY B 1 128 ? 9.06555   -45.68563 17.01694 1.000 44.13593  ? 114 GLY B CA   1 
ATOM   5331 C C    . GLY B 1 128 ? 9.24205   -44.69815 15.88566 1.000 41.14087  ? 114 GLY B C    1 
ATOM   5332 O O    . GLY B 1 128 ? 9.81127   -43.61786 16.06656 1.000 46.10919  ? 114 GLY B O    1 
ATOM   5333 H H    . GLY B 1 128 ? 9.08374   -44.86935 18.81509 1.000 42.77703  ? 114 GLY B H    1 
ATOM   5334 H HA2  . GLY B 1 128 ? 9.92728   -46.07463 17.23373 1.000 53.01905  ? 114 GLY B HA2  1 
ATOM   5335 H HA3  . GLY B 1 128 ? 8.46415   -46.39044 16.72979 1.000 53.01905  ? 114 GLY B HA3  1 
ATOM   5336 N N    . ASP B 1 129 ? 8.74535   -45.06062 14.70637 1.000 36.82008  ? 115 ASP B N    1 
ATOM   5337 C CA   . ASP B 1 129 ? 8.75962   -44.18089 13.54694 1.000 38.36353  ? 115 ASP B CA   1 
ATOM   5338 C C    . ASP B 1 129 ? 7.45804   -43.40511 13.38555 1.000 38.35824  ? 115 ASP B C    1 
ATOM   5339 O O    . ASP B 1 129 ? 7.28238   -42.71287 12.37623 1.000 33.34514  ? 115 ASP B O    1 
ATOM   5340 C CB   . ASP B 1 129 ? 9.03630   -44.99121 12.27755 1.000 43.22084  ? 115 ASP B CB   1 
ATOM   5341 C CG   . ASP B 1 129 ? 10.37852  -45.69457 12.31630 1.000 54.61317  ? 115 ASP B CG   1 
ATOM   5342 O OD1  . ASP B 1 129 ? 11.37307  -45.06380 12.73395 1.000 58.65761  ? 115 ASP B OD1  1 
ATOM   5343 O OD2  . ASP B 1 129 ? 10.43730  -46.88202 11.93386 1.000 72.35163  ? 115 ASP B OD2  1 
ATOM   5344 H H    . ASP B 1 129 ? 8.38784   -45.82741 14.55202 1.000 44.24004  ? 115 ASP B H    1 
ATOM   5345 H HA   . ASP B 1 129 ? 9.47888   -43.53919 13.65550 1.000 46.09218  ? 115 ASP B HA   1 
ATOM   5346 H HB2  . ASP B 1 129 ? 8.34646   -45.66546 12.17560 1.000 51.92094  ? 115 ASP B HB2  1 
ATOM   5347 H HB3  . ASP B 1 129 ? 9.03192   -44.39389 11.51329 1.000 51.92094  ? 115 ASP B HB3  1 
ATOM   5348 N N    . THR B 1 130 ? 6.55130   -43.50036 14.35396 1.000 30.95830  ? 116 THR B N    1 
ATOM   5349 C CA   . THR B 1 130 ? 5.23008   -42.89503 14.26948 1.000 31.43730  ? 116 THR B CA   1 
ATOM   5350 C C    . THR B 1 130 ? 5.17259   -41.66965 15.16990 1.000 27.36386  ? 116 THR B C    1 
ATOM   5351 O O    . THR B 1 130 ? 5.63522   -41.71373 16.31471 1.000 30.65335  ? 116 THR B O    1 
ATOM   5352 C CB   . THR B 1 130 ? 4.14315   -43.89365 14.67634 1.000 26.47975  ? 116 THR B CB   1 
ATOM   5353 O OG1  . THR B 1 130 ? 4.22411   -45.05981 13.84878 1.000 30.51014  ? 116 THR B OG1  1 
ATOM   5354 C CG2  . THR B 1 130 ? 2.76043   -43.26651 14.53801 1.000 29.95438  ? 116 THR B CG2  1 
ATOM   5355 H H    . THR B 1 130 ? 6.68452   -43.92368 15.09061 1.000 37.20590  ? 116 THR B H    1 
ATOM   5356 H HA   . THR B 1 130 ? 5.06428   -42.61307 13.35629 1.000 37.78070  ? 116 THR B HA   1 
ATOM   5357 H HB   . THR B 1 130 ? 4.27048   -44.14905 15.60341 1.000 31.49600  ? 116 THR B HB   1 
ATOM   5358 H HG1  . THR B 1 130 ? 4.95820   -45.44910 13.97193 1.000 36.66810  ? 116 THR B HG1  1 
ATOM   5359 H HG21 . THR B 1 130 ? 2.07563   -43.93405 14.70032 1.000 36.00120  ? 116 THR B HG21 1 
ATOM   5360 H HG22 . THR B 1 130 ? 2.65686   -42.54675 15.17998 1.000 36.00120  ? 116 THR B HG22 1 
ATOM   5361 H HG23 . THR B 1 130 ? 2.64613   -42.90933 13.64345 1.000 36.00120  ? 116 THR B HG23 1 
ATOM   5362 N N    . LEU B 1 131 ? 4.61144   -40.58140 14.64831 1.000 28.01279  ? 117 LEU B N    1 
ATOM   5363 C CA   . LEU B 1 131 ? 4.38321   -39.36686 15.42398 1.000 30.27828  ? 117 LEU B CA   1 
ATOM   5364 C C    . LEU B 1 131 ? 3.02709   -39.48918 16.10838 1.000 30.22723  ? 117 LEU B C    1 
ATOM   5365 O O    . LEU B 1 131 ? 1.99914   -39.63185 15.43743 1.000 26.63403  ? 117 LEU B O    1 
ATOM   5366 C CB   . LEU B 1 131 ? 4.43821   -38.13191 14.52470 1.000 25.73080  ? 117 LEU B CB   1 
ATOM   5367 C CG   . LEU B 1 131 ? 4.47475   -36.74080 15.17286 1.000 30.56010  ? 117 LEU B CG   1 
ATOM   5368 C CD1  . LEU B 1 131 ? 3.10428   -36.31794 15.68138 1.000 28.98468  ? 117 LEU B CD1  1 
ATOM   5369 C CD2  . LEU B 1 131 ? 5.49963   -36.69108 16.29732 1.000 30.28202  ? 117 LEU B CD2  1 
ATOM   5370 H H    . LEU B 1 131 ? 4.34948   -40.52150 13.83137 1.000 33.67129  ? 117 LEU B H    1 
ATOM   5371 H HA   . LEU B 1 131 ? 5.06996   -39.26572 16.10151 1.000 36.38988  ? 117 LEU B HA   1 
ATOM   5372 H HB2  . LEU B 1 131 ? 5.23926   -38.20284 13.98231 1.000 30.93290  ? 117 LEU B HB2  1 
ATOM   5373 H HB3  . LEU B 1 131 ? 3.65118   -38.14981 13.95800 1.000 30.93290  ? 117 LEU B HB3  1 
ATOM   5374 H HG   . LEU B 1 131 ? 4.73973   -36.10322 14.49156 1.000 36.72806  ? 117 LEU B HG   1 
ATOM   5375 H HD11 . LEU B 1 131 ? 2.45407   -36.43464 14.97110 1.000 34.83756  ? 117 LEU B HD11 1 
ATOM   5376 H HD12 . LEU B 1 131 ? 2.86561   -36.87012 16.44232 1.000 34.83756  ? 117 LEU B HD12 1 
ATOM   5377 H HD13 . LEU B 1 131 ? 3.13993   -35.38579 15.94733 1.000 34.83756  ? 117 LEU B HD13 1 
ATOM   5378 H HD21 . LEU B 1 131 ? 6.32353   -37.10207 15.99207 1.000 36.39436  ? 117 LEU B HD21 1 
ATOM   5379 H HD22 . LEU B 1 131 ? 5.66089   -35.76507 16.53691 1.000 36.39436  ? 117 LEU B HD22 1 
ATOM   5380 H HD23 . LEU B 1 131 ? 5.15232   -37.17515 17.06279 1.000 36.39436  ? 117 LEU B HD23 1 
ATOM   5381 N N    . VAL B 1 132 ? 3.02577   -39.43720 17.43733 1.000 30.91556  ? 118 VAL B N    1 
ATOM   5382 C CA   . VAL B 1 132 ? 1.84503   -39.72926 18.24121 1.000 30.42079  ? 118 VAL B CA   1 
ATOM   5383 C C    . VAL B 1 132 ? 1.39828   -38.46687 18.96484 1.000 29.37823  ? 118 VAL B C    1 
ATOM   5384 O O    . VAL B 1 132 ? 2.22681   -37.68159 19.43925 1.000 30.61815  ? 118 VAL B O    1 
ATOM   5385 C CB   . VAL B 1 132 ? 2.13301   -40.86738 19.24019 1.000 33.92399  ? 118 VAL B CB   1 
ATOM   5386 C CG1  . VAL B 1 132 ? 1.07475   -40.91310 20.31637 1.000 40.55391  ? 118 VAL B CG1  1 
ATOM   5387 C CG2  . VAL B 1 132 ? 2.21036   -42.20388 18.51331 1.000 31.39864  ? 118 VAL B CG2  1 
ATOM   5388 H H    . VAL B 1 132 ? 3.71568   -39.22955 17.90691 1.000 37.15461  ? 118 VAL B H    1 
ATOM   5389 H HA   . VAL B 1 132 ? 1.12051   -40.00020 17.65592 1.000 36.56089  ? 118 VAL B HA   1 
ATOM   5390 H HB   . VAL B 1 132 ? 2.98841   -40.69973 19.66573 1.000 40.76472  ? 118 VAL B HB   1 
ATOM   5391 H HG11 . VAL B 1 132 ? 1.10070   -41.78133 20.74811 1.000 48.72063  ? 118 VAL B HG11 1 
ATOM   5392 H HG12 . VAL B 1 132 ? 1.25435   -40.21527 20.96574 1.000 48.72063  ? 118 VAL B HG12 1 
ATOM   5393 H HG13 . VAL B 1 132 ? 0.20523   -40.77138 19.91046 1.000 48.72063  ? 118 VAL B HG13 1 
ATOM   5394 H HG21 . VAL B 1 132 ? 2.35993   -42.90849 19.16296 1.000 37.73431  ? 118 VAL B HG21 1 
ATOM   5395 H HG22 . VAL B 1 132 ? 1.37484   -42.35755 18.04512 1.000 37.73431  ? 118 VAL B HG22 1 
ATOM   5396 H HG23 . VAL B 1 132 ? 2.94440   -42.17680 17.87979 1.000 37.73431  ? 118 VAL B HG23 1 
ATOM   5397 N N    . ASN B 1 133 ? 0.08137   -38.27782 19.04955 1.000 30.53897  ? 119 ASN B N    1 
ATOM   5398 C CA   . ASN B 1 133 ? -0.52811  -37.15915 19.76944 1.000 28.59314  ? 119 ASN B CA   1 
ATOM   5399 C C    . ASN B 1 133 ? -1.58140  -37.74144 20.70971 1.000 27.72099  ? 119 ASN B C    1 
ATOM   5400 O O    . ASN B 1 133 ? -2.66311  -38.13727 20.26545 1.000 25.80849  ? 119 ASN B O    1 
ATOM   5401 C CB   . ASN B 1 133 ? -1.13802  -36.15152 18.79887 1.000 24.69242  ? 119 ASN B CB   1 
ATOM   5402 C CG   . ASN B 1 133 ? -1.68619  -34.92419 19.49665 1.000 26.58536  ? 119 ASN B CG   1 
ATOM   5403 O OD1  . ASN B 1 133 ? -1.29953  -34.60832 20.62174 1.000 26.12310  ? 119 ASN B OD1  1 
ATOM   5404 N ND2  . ASN B 1 133 ? -2.59315  -34.22184 18.82808 1.000 23.99337  ? 119 ASN B ND2  1 
ATOM   5405 H H    . ASN B 1 133 ? -0.49725  -38.80056 18.68688 1.000 36.70270  ? 119 ASN B H    1 
ATOM   5406 H HA   . ASN B 1 133 ? 0.14310   -36.70187 20.29979 1.000 34.36771  ? 119 ASN B HA   1 
ATOM   5407 H HB2  . ASN B 1 133 ? -0.45527  -35.86142 18.17389 1.000 29.68684  ? 119 ASN B HB2  1 
ATOM   5408 H HB3  . ASN B 1 133 ? -1.86749  -36.57533 18.32017 1.000 29.68684  ? 119 ASN B HB3  1 
ATOM   5409 H HD21 . ASN B 1 133 ? -2.93567  -33.51600 19.18030 1.000 28.84799  ? 119 ASN B HD21 1 
ATOM   5410 H HD22 . ASN B 1 133 ? -2.83808  -34.47277 18.04282 1.000 28.84799  ? 119 ASN B HD22 1 
ATOM   5411 N N    . ARG B 1 134 ? -1.26334  -37.80141 22.00249 1.000 27.41089  ? 120 ARG B N    1 
ATOM   5412 C CA   . ARG B 1 134 ? -2.14892  -38.35993 23.02033 1.000 30.25052  ? 120 ARG B CA   1 
ATOM   5413 C C    . ARG B 1 134 ? -2.72740  -37.22276 23.84743 1.000 24.65421  ? 120 ARG B C    1 
ATOM   5414 O O    . ARG B 1 134 ? -1.98015  -36.47518 24.48591 1.000 25.38321  ? 120 ARG B O    1 
ATOM   5415 C CB   . ARG B 1 134 ? -1.40328  -39.34056 23.92239 1.000 28.55994  ? 120 ARG B CB   1 
ATOM   5416 C CG   . ARG B 1 134 ? -0.80282  -40.50817 23.18133 1.000 38.82743  ? 120 ARG B CG   1 
ATOM   5417 C CD   . ARG B 1 134 ? 0.01621   -41.40163 24.09705 1.000 40.78409  ? 120 ARG B CD   1 
ATOM   5418 N NE   . ARG B 1 134 ? 0.46036   -42.60702 23.40686 1.000 40.41669  ? 120 ARG B NE   1 
ATOM   5419 C CZ   . ARG B 1 134 ? -0.29038  -43.68536 23.22571 1.000 43.71899  ? 120 ARG B CZ   1 
ATOM   5420 N NH1  . ARG B 1 134 ? -1.53463  -43.74539 23.67211 1.000 44.13068  ? 120 ARG B NH1  1 
ATOM   5421 N NH2  . ARG B 1 134 ? 0.21873   -44.72842 22.57681 1.000 44.27102  ? 120 ARG B NH2  1 
ATOM   5422 H H    . ARG B 1 134 ? -0.51768  -37.51601 22.32207 1.000 32.94901  ? 120 ARG B H    1 
ATOM   5423 H HA   . ARG B 1 134 ? -2.87614  -38.83201 22.58538 1.000 36.35657  ? 120 ARG B HA   1 
ATOM   5424 H HB2  . ARG B 1 134 ? -0.68171  -38.86885 24.36705 1.000 34.32786  ? 120 ARG B HB2  1 
ATOM   5425 H HB3  . ARG B 1 134 ? -2.02337  -39.69362 24.57945 1.000 34.32786  ? 120 ARG B HB3  1 
ATOM   5426 H HG2  . ARG B 1 134 ? -1.51482  -41.04176 22.79502 1.000 46.64885  ? 120 ARG B HG2  1 
ATOM   5427 H HG3  . ARG B 1 134 ? -0.21954  -40.17630 22.48094 1.000 46.64885  ? 120 ARG B HG3  1 
ATOM   5428 H HD2  . ARG B 1 134 ? 0.79980   -40.91774 24.40155 1.000 48.99685  ? 120 ARG B HD2  1 
ATOM   5429 H HD3  . ARG B 1 134 ? -0.52590  -41.66671 24.85649 1.000 48.99685  ? 120 ARG B HD3  1 
ATOM   5430 H HE   . ARG B 1 134 ? 1.26237   -42.61952 23.09666 1.000 48.55597  ? 120 ARG B HE   1 
ATOM   5431 H HH11 . ARG B 1 134 ? -1.87409  -43.07521 24.09070 1.000 53.01275  ? 120 ARG B HH11 1 
ATOM   5432 H HH12 . ARG B 1 134 ? -2.00381  -44.45460 23.54365 1.000 53.01275  ? 120 ARG B HH12 1 
ATOM   5433 H HH21 . ARG B 1 134 ? 1.02551   -44.69848 22.28047 1.000 53.18117  ? 120 ARG B HH21 1 
ATOM   5434 H HH22 . ARG B 1 134 ? -0.25878  -45.43296 22.45348 1.000 53.18117  ? 120 ARG B HH22 1 
ATOM   5435 N N    . ILE B 1 135 ? -4.05188  -37.12025 23.86628 1.000 25.80418  ? 121 ILE B N    1 
ATOM   5436 C CA   . ILE B 1 135 ? -4.73925  -35.92981 24.34088 1.000 24.19308  ? 121 ILE B CA   1 
ATOM   5437 C C    . ILE B 1 135 ? -5.69937  -36.30031 25.45869 1.000 25.24037  ? 121 ILE B C    1 
ATOM   5438 O O    . ILE B 1 135 ? -6.36086  -37.34271 25.40690 1.000 32.31408  ? 121 ILE B O    1 
ATOM   5439 C CB   . ILE B 1 135 ? -5.51627  -35.23724 23.20389 1.000 28.54046  ? 121 ILE B CB   1 
ATOM   5440 C CG1  . ILE B 1 135 ? -4.63975  -35.03480 21.96808 1.000 29.05152  ? 121 ILE B CG1  1 
ATOM   5441 C CG2  . ILE B 1 135 ? -6.06512  -33.91015 23.68979 1.000 26.69401  ? 121 ILE B CG2  1 
ATOM   5442 C CD1  . ILE B 1 135 ? -5.44542  -34.95292 20.68499 1.000 29.55523  ? 121 ILE B CD1  1 
ATOM   5443 H H    . ILE B 1 135 ? -4.58364  -37.74262 23.60266 1.000 31.02096  ? 121 ILE B H    1 
ATOM   5444 H HA   . ILE B 1 135 ? -4.07459  -35.32101 24.69933 1.000 29.08764  ? 121 ILE B HA   1 
ATOM   5445 H HB   . ILE B 1 135 ? -6.25210  -35.81516 22.94804 1.000 34.30449  ? 121 ILE B HB   1 
ATOM   5446 H HG12 . ILE B 1 135 ? -4.14383  -34.20678 22.06478 1.000 34.91777  ? 121 ILE B HG12 1 
ATOM   5447 H HG13 . ILE B 1 135 ? -4.02603  -35.78192 21.89030 1.000 34.91777  ? 121 ILE B HG13 1 
ATOM   5448 H HG21 . ILE B 1 135 ? -6.24770  -33.34428 22.92340 1.000 32.08875  ? 121 ILE B HG21 1 
ATOM   5449 H HG22 . ILE B 1 135 ? -6.88335  -34.06939 24.18581 1.000 32.08875  ? 121 ILE B HG22 1 
ATOM   5450 H HG23 . ILE B 1 135 ? -5.40728  -33.48748 24.26381 1.000 32.08875  ? 121 ILE B HG23 1 
ATOM   5451 H HD11 . ILE B 1 135 ? -6.27555  -34.48369 20.86274 1.000 35.52222  ? 121 ILE B HD11 1 
ATOM   5452 H HD12 . ILE B 1 135 ? -4.92993  -34.47229 20.01853 1.000 35.52222  ? 121 ILE B HD12 1 
ATOM   5453 H HD13 . ILE B 1 135 ? -5.63384  -35.85167 20.37251 1.000 35.52222  ? 121 ILE B HD13 1 
ATOM   5454 N N    . GLU B 1 136 ? -5.78313  -35.42891 26.45887 1.000 25.21107  ? 122 GLU B N    1 
ATOM   5455 C CA   . GLU B 1 136 ? -6.86613  -35.42398 27.43079 1.000 27.20046  ? 122 GLU B CA   1 
ATOM   5456 C C    . GLU B 1 136 ? -7.55651  -34.07266 27.33733 1.000 25.91701  ? 122 GLU B C    1 
ATOM   5457 O O    . GLU B 1 136 ? -6.88693  -33.03506 27.29641 1.000 26.04662  ? 122 GLU B O    1 
ATOM   5458 C CB   . GLU B 1 136 ? -6.35600  -35.66741 28.85211 1.000 26.40149  ? 122 GLU B CB   1 
ATOM   5459 C CG   . GLU B 1 136 ? -5.83410  -37.07165 29.09396 1.000 46.77343  ? 122 GLU B CG   1 
ATOM   5460 C CD   . GLU B 1 136 ? -5.31457  -37.25914 30.50550 1.000 74.52724  ? 122 GLU B CD   1 
ATOM   5461 O OE1  . GLU B 1 136 ? -5.15769  -36.24528 31.21979 1.000 65.47192  ? 122 GLU B OE1  1 
ATOM   5462 O OE2  . GLU B 1 136 ? -5.06616  -38.41799 30.90167 1.000 88.40297  ? 122 GLU B OE2  1 
ATOM   5463 H H    . GLU B 1 136 ? -5.20271  -34.80981 26.59825 1.000 30.30922  ? 122 GLU B H    1 
ATOM   5464 H HA   . GLU B 1 136 ? -7.50064  -36.13002 27.23128 1.000 32.69650  ? 122 GLU B HA   1 
ATOM   5465 H HB2  . GLU B 1 136 ? -5.63052  -35.04897 29.03130 1.000 31.73773  ? 122 GLU B HB2  1 
ATOM   5466 H HB3  . GLU B 1 136 ? -7.08456  -35.51320 29.47366 1.000 31.73773  ? 122 GLU B HB3  1 
ATOM   5467 H HG2  . GLU B 1 136 ? -6.55310  -37.70675 28.95044 1.000 56.18406  ? 122 GLU B HG2  1 
ATOM   5468 H HG3  . GLU B 1 136 ? -5.10596  -37.25018 28.47845 1.000 56.18406  ? 122 GLU B HG3  1 
ATOM   5469 N N    . LEU B 1 137 ? -8.88597  -34.08533 27.28846 1.000 28.45550  ? 123 LEU B N    1 
ATOM   5470 C CA   . LEU B 1 137 ? -9.67281  -32.87440 27.10514 1.000 30.50912  ? 123 LEU B CA   1 
ATOM   5471 C C    . LEU B 1 137 ? -10.82779 -32.85542 28.09207 1.000 30.11417  ? 123 LEU B C    1 
ATOM   5472 O O    . LEU B 1 137 ? -11.50931 -33.86651 28.28204 1.000 33.57141  ? 123 LEU B O    1 
ATOM   5473 C CB   . LEU B 1 137 ? -10.21138 -32.77811 25.66808 1.000 30.51052  ? 123 LEU B CB   1 
ATOM   5474 C CG   . LEU B 1 137 ? -11.07752 -31.55897 25.32932 1.000 26.16652  ? 123 LEU B CG   1 
ATOM   5475 C CD1  . LEU B 1 137 ? -11.02181 -31.25768 23.83404 1.000 27.72329  ? 123 LEU B CD1  1 
ATOM   5476 C CD2  . LEU B 1 137 ? -12.52291 -31.74883 25.76597 1.000 28.30587  ? 123 LEU B CD2  1 
ATOM   5477 H H    . LEU B 1 137 ? -9.36169  -34.79812 27.36072 1.000 34.20255  ? 123 LEU B H    1 
ATOM   5478 H HA   . LEU B 1 137 ? -9.11766  -32.09831 27.27944 1.000 36.66689  ? 123 LEU B HA   1 
ATOM   5479 H HB2  . LEU B 1 137 ? -9.45171  -32.76168 25.06515 1.000 36.66857  ? 123 LEU B HB2  1 
ATOM   5480 H HB3  . LEU B 1 137 ? -10.75236 -33.56525 25.49876 1.000 36.66857  ? 123 LEU B HB3  1 
ATOM   5481 H HG   . LEU B 1 137 ? -10.72147 -30.79995 25.81718 1.000 31.45576  ? 123 LEU B HG   1 
ATOM   5482 H HD11 . LEU B 1 137 ? -10.09394 -31.18329 23.56124 1.000 33.32388  ? 123 LEU B HD11 1 
ATOM   5483 H HD12 . LEU B 1 137 ? -11.45197 -31.97995 23.35011 1.000 33.32388  ? 123 LEU B HD12 1 
ATOM   5484 H HD13 . LEU B 1 137 ? -11.48493 -30.42279 23.66265 1.000 33.32388  ? 123 LEU B HD13 1 
ATOM   5485 H HD21 . LEU B 1 137 ? -12.65886 -32.67694 26.01300 1.000 34.02298  ? 123 LEU B HD21 1 
ATOM   5486 H HD22 . LEU B 1 137 ? -12.70091 -31.17446 26.52710 1.000 34.02298  ? 123 LEU B HD22 1 
ATOM   5487 H HD23 . LEU B 1 137 ? -13.10878 -31.51329 25.02965 1.000 34.02298  ? 123 LEU B HD23 1 
ATOM   5488 N N    . LYS B 1 138 ? -11.05034 -31.69762 28.71166 1.000 29.77509  ? 124 LYS B N    1 
ATOM   5489 C CA   . LYS B 1 138 ? -12.17531 -31.50253 29.61686 1.000 35.08486  ? 124 LYS B CA   1 
ATOM   5490 C C    . LYS B 1 138 ? -12.88765 -30.21215 29.24722 1.000 30.40032  ? 124 LYS B C    1 
ATOM   5491 O O    . LYS B 1 138 ? -12.27124 -29.14162 29.23265 1.000 31.04872  ? 124 LYS B O    1 
ATOM   5492 C CB   . LYS B 1 138 ? -11.72803 -31.45242 31.08095 1.000 32.41981  ? 124 LYS B CB   1 
ATOM   5493 C CG   . LYS B 1 138 ? -12.90410 -31.39846 32.05315 1.000 38.74509  ? 124 LYS B CG   1 
ATOM   5494 C CD   . LYS B 1 138 ? -12.52267 -30.82661 33.40823 1.000 44.74017  ? 124 LYS B CD   1 
ATOM   5495 C CE   . LYS B 1 138 ? -11.88981 -31.87101 34.30915 1.000 37.88568  ? 124 LYS B CE   1 
ATOM   5496 N NZ   . LYS B 1 138 ? -11.77337 -31.36620 35.70659 1.000 50.36842  ? 124 LYS B NZ   1 
ATOM   5497 H H    . LYS B 1 138 ? -10.55429 -31.00103 28.62055 1.000 35.78605  ? 124 LYS B H    1 
ATOM   5498 H HA   . LYS B 1 138 ? -12.79144 -32.24405 29.50994 1.000 42.15777  ? 124 LYS B HA   1 
ATOM   5499 H HB2  . LYS B 1 138 ? -11.20904 -32.24728 31.28033 1.000 38.95971  ? 124 LYS B HB2  1 
ATOM   5500 H HB3  . LYS B 1 138 ? -11.18674 -30.65945 31.21917 1.000 38.95971  ? 124 LYS B HB3  1 
ATOM   5501 H HG2  . LYS B 1 138 ? -13.60012 -30.83742 31.67673 1.000 46.55004  ? 124 LYS B HG2  1 
ATOM   5502 H HG3  . LYS B 1 138 ? -13.24130 -32.29733 32.19182 1.000 46.55004  ? 124 LYS B HG3  1 
ATOM   5503 H HD2  . LYS B 1 138 ? -11.88360 -30.10772 33.28298 1.000 53.74414  ? 124 LYS B HD2  1 
ATOM   5504 H HD3  . LYS B 1 138 ? -13.31884 -30.48982 33.84822 1.000 53.74414  ? 124 LYS B HD3  1 
ATOM   5505 H HE2  . LYS B 1 138 ? -12.44048 -32.66952 34.31531 1.000 45.51875  ? 124 LYS B HE2  1 
ATOM   5506 H HE3  . LYS B 1 138 ? -11.00108 -32.08340 33.98365 1.000 45.51875  ? 124 LYS B HE3  1 
ATOM   5507 H HZ1  . LYS B 1 138 ? -11.32822 -30.59558 35.71577 1.000 60.49804  ? 124 LYS B HZ1  1 
ATOM   5508 H HZ2  . LYS B 1 138 ? -11.33721 -31.95771 36.20857 1.000 60.49804  ? 124 LYS B HZ2  1 
ATOM   5509 H HZ3  . LYS B 1 138 ? -12.58335 -31.23601 36.05169 1.000 60.49804  ? 124 LYS B HZ3  1 
ATOM   5510 N N    . GLY B 1 139 ? -14.17867 -30.31609 28.95369 1.000 33.66254  ? 125 GLY B N    1 
ATOM   5511 C CA   . GLY B 1 139 ? -15.02996 -29.15468 28.76482 1.000 34.86554  ? 125 GLY B CA   1 
ATOM   5512 C C    . GLY B 1 139 ? -15.90911 -28.95003 29.98604 1.000 34.16889  ? 125 GLY B C    1 
ATOM   5513 O O    . GLY B 1 139 ? -16.36929 -29.91236 30.60137 1.000 35.09469  ? 125 GLY B O    1 
ATOM   5514 H H    . GLY B 1 139 ? -14.59053 -31.06487 28.85733 1.000 40.45099  ? 125 GLY B H    1 
ATOM   5515 H HA2  . GLY B 1 139 ? -14.48485 -28.36331 28.63254 1.000 41.89458  ? 125 GLY B HA2  1 
ATOM   5516 H HA3  . GLY B 1 139 ? -15.59539 -29.28229 27.98706 1.000 41.89458  ? 125 GLY B HA3  1 
ATOM   5517 N N    . ILE B 1 140 ? -16.12956 -27.68473 30.33480 1.000 36.38457  ? 126 ILE B N    1 
ATOM   5518 C CA   . ILE B 1 140 ? -16.94326 -27.33012 31.48881 1.000 37.48521  ? 126 ILE B CA   1 
ATOM   5519 C C    . ILE B 1 140 ? -17.78347 -26.10930 31.14633 1.000 41.59366  ? 126 ILE B C    1 
ATOM   5520 O O    . ILE B 1 140 ? -17.41777 -25.29738 30.29133 1.000 36.67622  ? 126 ILE B O    1 
ATOM   5521 C CB   . ILE B 1 140 ? -16.08055 -27.05423 32.74220 1.000 42.89699  ? 126 ILE B CB   1 
ATOM   5522 C CG1  . ILE B 1 140 ? -15.28304 -25.75693 32.56949 1.000 47.85311  ? 126 ILE B CG1  1 
ATOM   5523 C CG2  . ILE B 1 140 ? -15.14660 -28.22979 33.01464 1.000 38.44521  ? 126 ILE B CG2  1 
ATOM   5524 C CD1  . ILE B 1 140 ? -14.32037 -25.47410 33.70582 1.000 49.85946  ? 126 ILE B CD1  1 
ATOM   5525 H H    . ILE B 1 140 ? -15.81308 -27.00651 29.91117 1.000 43.71743  ? 126 ILE B H    1 
ATOM   5526 H HA   . ILE B 1 140 ? -17.54314 -28.06649 31.68583 1.000 45.03819  ? 126 ILE B HA   1 
ATOM   5527 H HB   . ILE B 1 140 ? -16.67200 -26.94877 33.50376 1.000 51.53232  ? 126 ILE B HB   1 
ATOM   5528 H HG12 . ILE B 1 140 ? -14.76555 -25.81586 31.75119 1.000 57.47967  ? 126 ILE B HG12 1 
ATOM   5529 H HG13 . ILE B 1 140 ? -15.90434 -25.01392 32.51634 1.000 57.47967  ? 126 ILE B HG13 1 
ATOM   5530 H HG21 . ILE B 1 140 ? -15.65812 -29.05336 32.98337 1.000 46.19020  ? 126 ILE B HG21 1 
ATOM   5531 H HG22 . ILE B 1 140 ? -14.45269 -28.24545 32.33703 1.000 46.19020  ? 126 ILE B HG22 1 
ATOM   5532 H HG23 . ILE B 1 140 ? -14.74911 -28.12042 33.89267 1.000 46.19020  ? 126 ILE B HG23 1 
ATOM   5533 H HD11 . ILE B 1 140 ? -14.08788 -24.53243 33.69577 1.000 59.88729  ? 126 ILE B HD11 1 
ATOM   5534 H HD12 . ILE B 1 140 ? -14.74873 -25.70010 34.54626 1.000 59.88729  ? 126 ILE B HD12 1 
ATOM   5535 H HD13 . ILE B 1 140 ? -13.52286 -26.01302 33.58562 1.000 59.88729  ? 126 ILE B HD13 1 
ATOM   5536 N N    . ASP B 1 141 ? -18.92404 -25.98846 31.82504 1.000 44.97875  ? 127 ASP B N    1 
ATOM   5537 C CA   . ASP B 1 141 ? -19.75631 -24.78950 31.77801 1.000 46.87594  ? 127 ASP B CA   1 
ATOM   5538 C C    . ASP B 1 141 ? -20.37511 -24.55981 30.40341 1.000 44.78067  ? 127 ASP B C    1 
ATOM   5539 O O    . ASP B 1 141 ? -20.64090 -23.41813 30.02182 1.000 43.26535  ? 127 ASP B O    1 
ATOM   5540 C CB   . ASP B 1 141 ? -18.95821 -23.55256 32.20392 1.000 47.96792  ? 127 ASP B CB   1 
ATOM   5541 C CG   . ASP B 1 141 ? -18.42342 -23.66503 33.61517 1.000 53.96116  ? 127 ASP B CG   1 
ATOM   5542 O OD1  . ASP B 1 141 ? -19.10417 -24.28604 34.45875 1.000 55.91448  ? 127 ASP B OD1  1 
ATOM   5543 O OD2  . ASP B 1 141 ? -17.32320 -23.13596 33.87967 1.000 56.72782  ? 127 ASP B OD2  1 
ATOM   5544 H H    . ASP B 1 141 ? -19.24398 -26.60451 32.33271 1.000 54.03044  ? 127 ASP B H    1 
ATOM   5545 H HA   . ASP B 1 141 ? -20.48983 -24.91379 32.40043 1.000 56.30706  ? 127 ASP B HA   1 
ATOM   5546 H HB2  . ASP B 1 141 ? -18.20399 -23.44011 31.60441 1.000 57.61745  ? 127 ASP B HB2  1 
ATOM   5547 H HB3  . ASP B 1 141 ? -19.53456 -22.77350 32.16175 1.000 57.61745  ? 127 ASP B HB3  1 
ATOM   5548 N N    . PHE B 1 142 ? -20.61962 -25.62702 29.64978 1.000 43.04006  ? 128 PHE B N    1 
ATOM   5549 C CA   . PHE B 1 142 ? -21.26228 -25.50723 28.34953 1.000 39.89117  ? 128 PHE B CA   1 
ATOM   5550 C C    . PHE B 1 142 ? -22.77614 -25.52076 28.51175 1.000 42.42640  ? 128 PHE B C    1 
ATOM   5551 O O    . PHE B 1 142 ? -23.32138 -26.27487 29.32259 1.000 41.66775  ? 128 PHE B O    1 
ATOM   5552 C CB   . PHE B 1 142 ? -20.82398 -26.63652 27.41650 1.000 38.65466  ? 128 PHE B CB   1 
ATOM   5553 C CG   . PHE B 1 142 ? -19.44237 -26.45534 26.85850 1.000 36.75718  ? 128 PHE B CG   1 
ATOM   5554 C CD1  . PHE B 1 142 ? -19.23780 -25.70896 25.70907 1.000 30.89582  ? 128 PHE B CD1  1 
ATOM   5555 C CD2  . PHE B 1 142 ? -18.34809 -27.02794 27.48311 1.000 35.06699  ? 128 PHE B CD2  1 
ATOM   5556 C CE1  . PHE B 1 142 ? -17.96872 -25.53855 25.19511 1.000 31.48581  ? 128 PHE B CE1  1 
ATOM   5557 C CE2  . PHE B 1 142 ? -17.07664 -26.86062 26.97268 1.000 32.60758  ? 128 PHE B CE2  1 
ATOM   5558 C CZ   . PHE B 1 142 ? -16.88692 -26.11464 25.82829 1.000 30.19928  ? 128 PHE B CZ   1 
ATOM   5559 H H    . PHE B 1 142 ? -20.42129 -26.43382 29.87190 1.000 51.70402  ? 128 PHE B H    1 
ATOM   5560 H HA   . PHE B 1 142 ? -21.00420 -24.66653 27.94022 1.000 47.92535  ? 128 PHE B HA   1 
ATOM   5561 H HB2  . PHE B 1 142 ? -20.83734 -27.47176 27.90953 1.000 46.44153  ? 128 PHE B HB2  1 
ATOM   5562 H HB3  . PHE B 1 142 ? -21.44156 -26.68207 26.66989 1.000 46.44153  ? 128 PHE B HB3  1 
ATOM   5563 H HD1  . PHE B 1 142 ? -19.96415 -25.31844 25.27917 1.000 37.13093  ? 128 PHE B HD1  1 
ATOM   5564 H HD2  . PHE B 1 142 ? -18.47085 -27.53116 28.25551 1.000 42.13633  ? 128 PHE B HD2  1 
ATOM   5565 H HE1  . PHE B 1 142 ? -17.84278 -25.03597 24.42281 1.000 37.83891  ? 128 PHE B HE1  1 
ATOM   5566 H HE2  . PHE B 1 142 ? -16.34851 -27.25057 27.40007 1.000 39.18504  ? 128 PHE B HE2  1 
ATOM   5567 H HZ   . PHE B 1 142 ? -16.03068 -26.00011 25.48385 1.000 36.29508  ? 128 PHE B HZ   1 
ATOM   5568 N N    . LYS B 1 143 ? -23.44917 -24.67088 27.74117 1.000 42.13164  ? 129 LYS B N    1 
ATOM   5569 C CA   . LYS B 1 143 ? -24.90389 -24.62276 27.75145 1.000 48.60730  ? 129 LYS B CA   1 
ATOM   5570 C C    . LYS B 1 143 ? -25.46141 -25.80523 26.96980 1.000 51.60190  ? 129 LYS B C    1 
ATOM   5571 O O    . LYS B 1 143 ? -25.10145 -26.01650 25.80695 1.000 44.47099  ? 129 LYS B O    1 
ATOM   5572 C CB   . LYS B 1 143 ? -25.39743 -23.30823 27.14923 1.000 45.44698  ? 129 LYS B CB   1 
ATOM   5573 C CG   . LYS B 1 143 ? -24.96567 -22.07595 27.92102 1.000 47.75804  ? 129 LYS B CG   1 
ATOM   5574 C CD   . LYS B 1 143 ? -25.19327 -20.80722 27.11357 1.000 47.75989  ? 129 LYS B CD   1 
ATOM   5575 C CE   . LYS B 1 143 ? -24.77059 -19.57167 27.89052 1.000 47.33585  ? 129 LYS B CE   1 
ATOM   5576 N NZ   . LYS B 1 143 ? -24.70931 -18.35947 27.02318 1.000 57.67416  ? 129 LYS B NZ   1 
ATOM   5577 H H    . LYS B 1 143 ? -23.08320 -24.10992 27.20172 1.000 50.61391  ? 129 LYS B H    1 
ATOM   5578 H HA   . LYS B 1 143 ? -25.22610 -24.67525 28.66487 1.000 58.38470  ? 129 LYS B HA   1 
ATOM   5579 H HB2  . LYS B 1 143 ? -25.04868 -23.22901 26.24756 1.000 54.59232  ? 129 LYS B HB2  1 
ATOM   5580 H HB3  . LYS B 1 143 ? -26.36717 -23.31975 27.13004 1.000 54.59232  ? 129 LYS B HB3  1 
ATOM   5581 H HG2  . LYS B 1 143 ? -25.48082 -22.01277 28.74049 1.000 57.36559  ? 129 LYS B HG2  1 
ATOM   5582 H HG3  . LYS B 1 143 ? -24.02016 -22.14075 28.12769 1.000 57.36559  ? 129 LYS B HG3  1 
ATOM   5583 H HD2  . LYS B 1 143 ? -24.67123 -20.84767 26.29703 1.000 57.36781  ? 129 LYS B HD2  1 
ATOM   5584 H HD3  . LYS B 1 143 ? -26.13618 -20.72620 26.90083 1.000 57.36781  ? 129 LYS B HD3  1 
ATOM   5585 H HE2  . LYS B 1 143 ? -25.41203 -19.40515 28.59885 1.000 56.85896  ? 129 LYS B HE2  1 
ATOM   5586 H HE3  . LYS B 1 143 ? -23.88944 -19.71838 28.26863 1.000 56.85896  ? 129 LYS B HE3  1 
ATOM   5587 H HZ1  . LYS B 1 143 ? -24.48406 -17.64862 27.50902 1.000 69.26494  ? 129 LYS B HZ1  1 
ATOM   5588 H HZ2  . LYS B 1 143 ? -24.10337 -18.47458 26.38155 1.000 69.26494  ? 129 LYS B HZ2  1 
ATOM   5589 H HZ3  . LYS B 1 143 ? -25.50301 -18.21317 26.64802 1.000 69.26494  ? 129 LYS B HZ3  1 
ATOM   5590 N N    . GLU B 1 144 ? -26.34063 -26.57869 27.61256 1.000 54.14258  ? 130 GLU B N    1 
ATOM   5591 C CA   . GLU B 1 144 ? -26.92190 -27.73895 26.94586 1.000 59.95012  ? 130 GLU B CA   1 
ATOM   5592 C C    . GLU B 1 144 ? -27.61945 -27.34465 25.65033 1.000 56.59647  ? 130 GLU B C    1 
ATOM   5593 O O    . GLU B 1 144 ? -27.64338 -28.12892 24.69484 1.000 58.93504  ? 130 GLU B O    1 
ATOM   5594 C CB   . GLU B 1 144 ? -27.89725 -28.44886 27.88700 1.000 63.76835  ? 130 GLU B CB   1 
ATOM   5595 C CG   . GLU B 1 144 ? -27.24727 -29.01666 29.14923 1.000 68.89382  ? 130 GLU B CG   1 
ATOM   5596 C CD   . GLU B 1 144 ? -26.30776 -30.18022 28.86349 1.000 72.39387  ? 130 GLU B CD   1 
ATOM   5597 O OE1  . GLU B 1 144 ? -26.36061 -30.73230 27.74323 1.000 70.78744  ? 130 GLU B OE1  1 
ATOM   5598 O OE2  . GLU B 1 144 ? -25.51557 -30.54495 29.76073 1.000 63.68256  ? 130 GLU B OE2  1 
ATOM   5599 H H    . GLU B 1 144 ? -26.61074 -26.45402 28.41946 1.000 65.02703  ? 130 GLU B H    1 
ATOM   5600 H HA   . GLU B 1 144 ? -26.21371 -28.36393 26.72503 1.000 71.99608  ? 130 GLU B HA   1 
ATOM   5601 H HB2  . GLU B 1 144 ? -28.57678 -27.81506 28.16530 1.000 76.57795  ? 130 GLU B HB2  1 
ATOM   5602 H HB3  . GLU B 1 144 ? -28.30753 -29.18685 27.40957 1.000 76.57795  ? 130 GLU B HB3  1 
ATOM   5603 H HG2  . GLU B 1 144 ? -26.73314 -28.31659 29.58107 1.000 82.72852  ? 130 GLU B HG2  1 
ATOM   5604 H HG3  . GLU B 1 144 ? -27.94277 -29.33389 29.74635 1.000 82.72852  ? 130 GLU B HG3  1 
ATOM   5605 N N    . ASP B 1 145 ? -28.17631 -26.13465 25.59252 1.000 52.70393  ? 131 ASP B N    1 
ATOM   5606 C CA   . ASP B 1 145 ? -28.85762 -25.62961 24.40880 1.000 57.82015  ? 131 ASP B CA   1 
ATOM   5607 C C    . ASP B 1 145 ? -27.98861 -24.66979 23.60158 1.000 53.22274  ? 131 ASP B C    1 
ATOM   5608 O O    . ASP B 1 145 ? -28.50966 -23.92710 22.76236 1.000 47.05339  ? 131 ASP B O    1 
ATOM   5609 C CB   . ASP B 1 145 ? -30.16038 -24.93894 24.81285 1.000 60.84941  ? 131 ASP B CB   1 
ATOM   5610 C CG   . ASP B 1 145 ? -29.93250 -23.79593 25.78031 1.000 70.72512  ? 131 ASP B CG   1 
ATOM   5611 O OD1  . ASP B 1 145 ? -28.95607 -23.86672 26.55740 1.000 65.74722  ? 131 ASP B OD1  1 
ATOM   5612 O OD2  . ASP B 1 145 ? -30.72425 -22.82910 25.76385 1.000 71.75015  ? 131 ASP B OD2  1 
ATOM   5613 H H    . ASP B 1 145 ? -28.17036 -25.57551 26.24592 1.000 63.30065  ? 131 ASP B H    1 
ATOM   5614 H HA   . ASP B 1 145 ? -29.07612 -26.38227 23.83726 1.000 69.44012  ? 131 ASP B HA   1 
ATOM   5615 H HB2  . ASP B 1 145 ? -30.58929 -24.58142 24.01968 1.000 73.07523  ? 131 ASP B HB2  1 
ATOM   5616 H HB3  . ASP B 1 145 ? -30.74249 -25.58542 25.24195 1.000 73.07523  ? 131 ASP B HB3  1 
ATOM   5617 N N    . GLY B 1 146 ? -26.68061 -24.66630 23.84060 1.000 46.17940  ? 132 GLY B N    1 
ATOM   5618 C CA   . GLY B 1 146 ? -25.77409 -23.79187 23.13127 1.000 36.17919  ? 132 GLY B CA   1 
ATOM   5619 C C    . GLY B 1 146 ? -25.33602 -24.37576 21.80119 1.000 39.47629  ? 132 GLY B C    1 
ATOM   5620 O O    . GLY B 1 146 ? -25.78961 -25.43347 21.36086 1.000 36.85611  ? 132 GLY B O    1 
ATOM   5621 H H    . GLY B 1 146 ? -26.29432 -25.17170 24.41934 1.000 55.47121  ? 132 GLY B H    1 
ATOM   5622 H HA2  . GLY B 1 146 ? -26.21158 -22.94251 22.96366 1.000 43.27751  ? 132 GLY B HA2  1 
ATOM   5623 H HA3  . GLY B 1 146 ? -24.98449 -23.63882 23.67349 1.000 43.27751  ? 132 GLY B HA3  1 
ATOM   5624 N N    . ASN B 1 147 ? -24.41445 -23.65784 21.15419 1.000 40.20829  ? 133 ASN B N    1 
ATOM   5625 C CA   . ASN B 1 147 ? -23.96074 -24.06213 19.82821 1.000 37.27308  ? 133 ASN B CA   1 
ATOM   5626 C C    . ASN B 1 147 ? -23.15144 -25.35176 19.86935 1.000 37.89187  ? 133 ASN B C    1 
ATOM   5627 O O    . ASN B 1 147 ? -23.15093 -26.11000 18.89294 1.000 36.09196  ? 133 ASN B O    1 
ATOM   5628 C CB   . ASN B 1 147 ? -23.12680 -22.94806 19.19425 1.000 42.94103  ? 133 ASN B CB   1 
ATOM   5629 C CG   . ASN B 1 147 ? -23.96104 -21.74981 18.79064 1.000 40.44925  ? 133 ASN B CG   1 
ATOM   5630 O OD1  . ASN B 1 147 ? -25.14784 -21.87633 18.48595 1.000 37.09396  ? 133 ASN B OD1  1 
ATOM   5631 N ND2  . ASN B 1 147 ? -23.33985 -20.57641 18.77929 1.000 36.79107  ? 133 ASN B ND2  1 
ATOM   5632 H H    . ASN B 1 147 ? -24.04317 -22.94408 21.45799 1.000 48.30589  ? 133 ASN B H    1 
ATOM   5633 H HA   . ASN B 1 147 ? -24.74215 -24.21451 19.27406 1.000 44.78363  ? 133 ASN B HA   1 
ATOM   5634 H HB2  . ASN B 1 147 ? -22.46115 -22.64873 19.83316 1.000 51.58517  ? 133 ASN B HB2  1 
ATOM   5635 H HB3  . ASN B 1 147 ? -22.69172 -23.29245 18.39863 1.000 51.58517  ? 133 ASN B HB3  1 
ATOM   5636 H HD21 . ASN B 1 147 ? -23.76887 -19.86488 18.55734 1.000 44.20522  ? 133 ASN B HD21 1 
ATOM   5637 H HD22 . ASN B 1 147 ? -22.50847 -20.52791 18.99389 1.000 44.20522  ? 133 ASN B HD22 1 
ATOM   5638 N N    . ILE B 1 148 ? -22.45768 -25.61814 20.97448 1.000 37.02887  ? 134 ILE B N    1 
ATOM   5639 C CA   . ILE B 1 148 ? -21.57869 -26.77897 21.06085 1.000 35.98695  ? 134 ILE B CA   1 
ATOM   5640 C C    . ILE B 1 148 ? -22.39634 -28.00952 21.43157 1.000 36.01575  ? 134 ILE B C    1 
ATOM   5641 O O    . ILE B 1 148 ? -22.57749 -28.91565 20.61068 1.000 40.26298  ? 134 ILE B O    1 
ATOM   5642 C CB   . ILE B 1 148 ? -20.43812 -26.54754 22.06899 1.000 36.23211  ? 134 ILE B CB   1 
ATOM   5643 C CG1  . ILE B 1 148 ? -19.45054 -25.50254 21.53934 1.000 37.66265  ? 134 ILE B CG1  1 
ATOM   5644 C CG2  . ILE B 1 148 ? -19.70512 -27.85308 22.35040 1.000 38.15125  ? 134 ILE B CG2  1 
ATOM   5645 C CD1  . ILE B 1 148 ? -19.99695 -24.09610 21.48551 1.000 39.03572  ? 134 ILE B CD1  1 
ATOM   5646 H H    . ILE B 1 148 ? -22.48003 -25.13964 21.68872 1.000 44.49058  ? 134 ILE B H    1 
ATOM   5647 H HA   . ILE B 1 148 ? -21.18230 -26.93225 20.18891 1.000 43.24028  ? 134 ILE B HA   1 
ATOM   5648 H HB   . ILE B 1 148 ? -20.83007 -26.21768 22.89268 1.000 43.53447  ? 134 ILE B HB   1 
ATOM   5649 H HG12 . ILE B 1 148 ? -18.67172 -25.49234 22.11748 1.000 45.25112  ? 134 ILE B HG12 1 
ATOM   5650 H HG13 . ILE B 1 148 ? -19.19151 -25.75089 20.63816 1.000 45.25112  ? 134 ILE B HG13 1 
ATOM   5651 H HG21 . ILE B 1 148 ? -20.22038 -28.37385 22.98618 1.000 45.83745  ? 134 ILE B HG21 1 
ATOM   5652 H HG22 . ILE B 1 148 ? -19.60811 -28.34599 21.52062 1.000 45.83745  ? 134 ILE B HG22 1 
ATOM   5653 H HG23 . ILE B 1 148 ? -18.83104 -27.65130 22.71940 1.000 45.83745  ? 134 ILE B HG23 1 
ATOM   5654 H HD11 . ILE B 1 148 ? -20.53392 -23.99638 20.68388 1.000 46.89881  ? 134 ILE B HD11 1 
ATOM   5655 H HD12 . ILE B 1 148 ? -20.54352 -23.93936 22.27138 1.000 46.89881  ? 134 ILE B HD12 1 
ATOM   5656 H HD13 . ILE B 1 148 ? -19.25627 -23.47002 21.46750 1.000 46.89881  ? 134 ILE B HD13 1 
ATOM   5657 N N    . LEU B 1 149 ? -22.89545 -28.05619 22.66928 1.000 31.40296  ? 135 LEU B N    1 
ATOM   5658 C CA   . LEU B 1 149 ? -23.68088 -29.20873 23.09794 1.000 36.07181  ? 135 LEU B CA   1 
ATOM   5659 C C    . LEU B 1 149 ? -24.95377 -29.37517 22.27839 1.000 36.12543  ? 135 LEU B C    1 
ATOM   5660 O O    . LEU B 1 149 ? -25.53038 -30.46829 22.26662 1.000 35.08429  ? 135 LEU B O    1 
ATOM   5661 C CB   . LEU B 1 149 ? -24.03327 -29.09237 24.58285 1.000 40.10563  ? 135 LEU B CB   1 
ATOM   5662 C CG   . LEU B 1 149 ? -22.89186 -29.33155 25.57629 1.000 42.09930  ? 135 LEU B CG   1 
ATOM   5663 C CD1  . LEU B 1 149 ? -23.39994 -29.25993 27.01005 1.000 39.39474  ? 135 LEU B CD1  1 
ATOM   5664 C CD2  . LEU B 1 149 ? -22.21255 -30.67022 25.32312 1.000 32.71624  ? 135 LEU B CD2  1 
ATOM   5665 H H    . LEU B 1 149 ? -22.79457 -27.44515 23.26599 1.000 37.73949  ? 135 LEU B H    1 
ATOM   5666 H HA   . LEU B 1 149 ? -23.14092 -30.00616 22.98196 1.000 43.34212  ? 135 LEU B HA   1 
ATOM   5667 H HB2  . LEU B 1 149 ? -24.36762 -28.19602 24.74306 1.000 48.18270  ? 135 LEU B HB2  1 
ATOM   5668 H HB3  . LEU B 1 149 ? -24.72403 -29.74425 24.77980 1.000 48.18270  ? 135 LEU B HB3  1 
ATOM   5669 H HG   . LEU B 1 149 ? -22.22970 -28.63370 25.45201 1.000 50.57510  ? 135 LEU B HG   1 
ATOM   5670 H HD11 . LEU B 1 149 ? -22.64306 -29.29732 27.61555 1.000 47.32963  ? 135 LEU B HD11 1 
ATOM   5671 H HD12 . LEU B 1 149 ? -23.88129 -28.42685 27.13327 1.000 47.32963  ? 135 LEU B HD12 1 
ATOM   5672 H HD13 . LEU B 1 149 ? -23.99158 -30.01107 27.17332 1.000 47.32963  ? 135 LEU B HD13 1 
ATOM   5673 H HD21 . LEU B 1 149 ? -22.88217 -31.31817 25.05352 1.000 39.31543  ? 135 LEU B HD21 1 
ATOM   5674 H HD22 . LEU B 1 149 ? -21.55439 -30.56217 24.61881 1.000 39.31543  ? 135 LEU B HD22 1 
ATOM   5675 H HD23 . LEU B 1 149 ? -21.77836 -30.96342 26.13946 1.000 39.31543  ? 135 LEU B HD23 1 
ATOM   5676 N N    . GLY B 1 150 ? -25.40261 -28.32480 21.59682 1.000 36.96701  ? 136 GLY B N    1 
ATOM   5677 C CA   . GLY B 1 150 ? -26.56354 -28.38771 20.73754 1.000 36.18372  ? 136 GLY B CA   1 
ATOM   5678 C C    . GLY B 1 150 ? -26.28232 -28.76406 19.30148 1.000 35.08856  ? 136 GLY B C    1 
ATOM   5679 O O    . GLY B 1 150 ? -27.22343 -28.91160 18.51627 1.000 36.65843  ? 136 GLY B O    1 
ATOM   5680 H H    . GLY B 1 150 ? -25.03680 -27.54686 21.62112 1.000 44.41635  ? 136 GLY B H    1 
ATOM   5681 H HA2  . GLY B 1 150 ? -27.17992 -29.04398 21.09851 1.000 43.47641  ? 136 GLY B HA2  1 
ATOM   5682 H HA3  . GLY B 1 150 ? -26.99365 -27.51829 20.73515 1.000 43.47641  ? 136 GLY B HA3  1 
ATOM   5683 N N    . HIS B 1 151 ? -25.01219 -28.91945 18.92631 1.000 33.21560  ? 137 HIS B N    1 
ATOM   5684 C CA   . HIS B 1 151 ? -24.63266 -29.33653 17.57569 1.000 37.73676  ? 137 HIS B CA   1 
ATOM   5685 C C    . HIS B 1 151 ? -25.20292 -28.38604 16.52416 1.000 35.00215  ? 137 HIS B C    1 
ATOM   5686 O O    . HIS B 1 151 ? -25.82070 -28.80419 15.54285 1.000 34.70782  ? 137 HIS B O    1 
ATOM   5687 C CB   . HIS B 1 151 ? -25.07736 -30.77587 17.30286 1.000 37.46380  ? 137 HIS B CB   1 
ATOM   5688 C CG   . HIS B 1 151 ? -24.40849 -31.79262 18.17400 1.000 41.39327  ? 137 HIS B CG   1 
ATOM   5689 N ND1  . HIS B 1 151 ? -23.21264 -32.38967 17.83721 1.000 43.32390  ? 137 HIS B ND1  1 
ATOM   5690 C CD2  . HIS B 1 151 ? -24.77263 -32.32509 19.36472 1.000 43.77506  ? 137 HIS B CD2  1 
ATOM   5691 C CE1  . HIS B 1 151 ? -22.86583 -33.24159 18.78563 1.000 43.48163  ? 137 HIS B CE1  1 
ATOM   5692 N NE2  . HIS B 1 151 ? -23.79643 -33.22311 19.72293 1.000 42.85225  ? 137 HIS B NE2  1 
ATOM   5693 H H    . HIS B 1 151 ? -24.33965 -28.78686 19.44565 1.000 39.57902  ? 137 HIS B H    1 
ATOM   5694 H HA   . HIS B 1 151 ? -23.66569 -29.30044 17.50811 1.000 45.34005  ? 137 HIS B HA   1 
ATOM   5695 H HB2  . HIS B 1 151 ? -26.03333 -30.84032 17.45405 1.000 45.01250  ? 137 HIS B HB2  1 
ATOM   5696 H HB3  . HIS B 1 151 ? -24.87174 -30.99576 16.38076 1.000 45.01250  ? 137 HIS B HB3  1 
ATOM   5697 H HD1  . HIS B 1 151 ? -22.76257 -32.23223 17.12150 1.000 52.04462  ? 137 HIS B HD1  1 
ATOM   5698 H HD2  . HIS B 1 151 ? -25.53979 -32.12110 19.84923 1.000 52.58601  ? 137 HIS B HD2  1 
ATOM   5699 H HE1  . HIS B 1 151 ? -22.09726 -33.76519 18.79221 1.000 52.23390  ? 137 HIS B HE1  1 
ATOM   5700 N N    . LYS B 1 152 ? -24.98003 -27.09054 16.73338 1.000 36.08034  ? 138 LYS B N    1 
ATOM   5701 C CA   . LYS B 1 152 ? -25.48396 -26.05459 15.84486 1.000 34.24155  ? 138 LYS B CA   1 
ATOM   5702 C C    . LYS B 1 152 ? -24.40860 -25.50320 14.91768 1.000 40.43611  ? 138 LYS B C    1 
ATOM   5703 O O    . LYS B 1 152 ? -24.63851 -24.48567 14.25643 1.000 41.13123  ? 138 LYS B O    1 
ATOM   5704 C CB   . LYS B 1 152 ? -26.09478 -24.91519 16.66420 1.000 36.99143  ? 138 LYS B CB   1 
ATOM   5705 C CG   . LYS B 1 152 ? -27.20751 -25.35298 17.60361 1.000 37.61846  ? 138 LYS B CG   1 
ATOM   5706 C CD   . LYS B 1 152 ? -27.73741 -24.18969 18.43180 1.000 37.74634  ? 138 LYS B CD   1 
ATOM   5707 C CE   . LYS B 1 152 ? -28.93096 -24.61054 19.27917 1.000 39.58817  ? 138 LYS B CE   1 
ATOM   5708 N NZ   . LYS B 1 152 ? -29.44389 -23.50261 20.13380 1.000 46.33017  ? 138 LYS B NZ   1 
ATOM   5709 H H    . LYS B 1 152 ? -24.52954 -26.78342 17.39846 1.000 43.35235  ? 138 LYS B H    1 
ATOM   5710 H HA   . LYS B 1 152 ? -26.18309 -26.43782 15.29238 1.000 40.81016  ? 138 LYS B HA   1 
ATOM   5711 H HB2  . LYS B 1 152 ? -25.39649 -24.51106 17.20270 1.000 44.44565  ? 138 LYS B HB2  1 
ATOM   5712 H HB3  . LYS B 1 152 ? -26.46546 -24.25830 16.05429 1.000 44.44565  ? 138 LYS B HB3  1 
ATOM   5713 H HG2  . LYS B 1 152 ? -27.94192 -25.71500 17.08352 1.000 45.19809  ? 138 LYS B HG2  1 
ATOM   5714 H HG3  . LYS B 1 152 ? -26.86679 -26.02805 18.21113 1.000 45.19809  ? 138 LYS B HG3  1 
ATOM   5715 H HD2  . LYS B 1 152 ? -27.03857 -23.87212 19.02482 1.000 45.01591  ? 138 LYS B HD2  1 
ATOM   5716 H HD3  . LYS B 1 152 ? -28.01996 -23.47532 17.83956 1.000 45.01591  ? 138 LYS B HD3  1 
ATOM   5717 H HE2  . LYS B 1 152 ? -29.64998 -24.89668 18.69432 1.000 47.22611  ? 138 LYS B HE2  1 
ATOM   5718 H HE3  . LYS B 1 152 ? -28.66568 -25.34044 19.86036 1.000 47.22611  ? 138 LYS B HE3  1 
ATOM   5719 H HZ1  . LYS B 1 152 ? -28.80454 -23.22345 20.68643 1.000 55.65214  ? 138 LYS B HZ1  1 
ATOM   5720 H HZ2  . LYS B 1 152 ? -29.70356 -22.82050 19.62448 1.000 55.65214  ? 138 LYS B HZ2  1 
ATOM   5721 H HZ3  . LYS B 1 152 ? -30.13787 -23.78498 20.61417 1.000 55.65214  ? 138 LYS B HZ3  1 
ATOM   5722 N N    . LEU B 1 153 ? -23.24734 -26.14719 14.84948 1.000 37.11082  ? 139 LEU B N    1 
ATOM   5723 C CA   . LEU B 1 153 ? -22.14110 -25.67384 14.03037 1.000 38.25656  ? 139 LEU B CA   1 
ATOM   5724 C C    . LEU B 1 153 ? -22.10845 -26.41565 12.70110 1.000 39.57815  ? 139 LEU B C    1 
ATOM   5725 O O    . LEU B 1 153 ? -22.36457 -27.62198 12.64229 1.000 37.89862  ? 139 LEU B O    1 
ATOM   5726 C CB   . LEU B 1 153 ? -20.80732 -25.85913 14.75430 1.000 28.60403  ? 139 LEU B CB   1 
ATOM   5727 C CG   . LEU B 1 153 ? -20.67777 -25.18376 16.11801 1.000 36.05590  ? 139 LEU B CG   1 
ATOM   5728 C CD1  . LEU B 1 153 ? -19.30318 -25.46485 16.70712 1.000 36.24033  ? 139 LEU B CD1  1 
ATOM   5729 C CD2  . LEU B 1 153 ? -20.92693 -23.68248 16.01603 1.000 38.21070  ? 139 LEU B CD2  1 
ATOM   5730 H H    . LEU B 1 153 ? -23.07509 -26.87330 15.27693 1.000 44.58892  ? 139 LEU B H    1 
ATOM   5731 H HA   . LEU B 1 153 ? -22.26468 -24.72914 13.84829 1.000 45.96381  ? 139 LEU B HA   1 
ATOM   5732 H HB2  . LEU B 1 153 ? -20.66857 -26.80930 14.89153 1.000 34.04513  ? 139 LEU B HB2  1 
ATOM   5733 H HB3  . LEU B 1 153 ? -20.10554 -25.49956 14.18940 1.000 34.04513  ? 139 LEU B HB3  1 
ATOM   5734 H HG   . LEU B 1 153 ? -21.35014 -25.54637 16.71578 1.000 43.32302  ? 139 LEU B HG   1 
ATOM   5735 H HD11 . LEU B 1 153 ? -19.26469 -25.10233 17.60600 1.000 43.54433  ? 139 LEU B HD11 1 
ATOM   5736 H HD12 . LEU B 1 153 ? -19.15987 -26.42392 16.73083 1.000 43.54433  ? 139 LEU B HD12 1 
ATOM   5737 H HD13 . LEU B 1 153 ? -18.62918 -25.04333 16.15130 1.000 43.54433  ? 139 LEU B HD13 1 
ATOM   5738 H HD21 . LEU B 1 153 ? -20.33252 -23.30844 15.34695 1.000 45.90878  ? 139 LEU B HD21 1 
ATOM   5739 H HD22 . LEU B 1 153 ? -21.85020 -23.53231 15.75929 1.000 45.90878  ? 139 LEU B HD22 1 
ATOM   5740 H HD23 . LEU B 1 153 ? -20.75283 -23.27416 16.87851 1.000 45.90878  ? 139 LEU B HD23 1 
ATOM   5741 N N    . GLU B 1 154 ? -21.79022 -25.68524 11.63633 1.000 39.74308  ? 140 GLU B N    1 
ATOM   5742 C CA   . GLU B 1 154 ? -21.64145 -26.29896 10.32639 1.000 41.85523  ? 140 GLU B CA   1 
ATOM   5743 C C    . GLU B 1 154 ? -20.42124 -27.21078 10.30170 1.000 33.85234  ? 140 GLU B C    1 
ATOM   5744 O O    . GLU B 1 154 ? -19.41417 -26.95833 10.96781 1.000 34.54791  ? 140 GLU B O    1 
ATOM   5745 C CB   . GLU B 1 154 ? -21.50129 -25.23007 9.24297  1.000 43.64990  ? 140 GLU B CB   1 
ATOM   5746 C CG   . GLU B 1 154 ? -22.75552 -24.41648 8.99111  1.000 46.99395  ? 140 GLU B CG   1 
ATOM   5747 C CD   . GLU B 1 154 ? -22.57846 -23.42428 7.85807  1.000 53.09828  ? 140 GLU B CD   1 
ATOM   5748 O OE1  . GLU B 1 154 ? -21.45539 -23.33873 7.31631  1.000 50.84593  ? 140 GLU B OE1  1 
ATOM   5749 O OE2  . GLU B 1 154 ? -23.55929 -22.73284 7.50787  1.000 54.69271  ? 140 GLU B OE2  1 
ATOM   5750 H H    . GLU B 1 154 ? -21.65608 -24.83585 11.64784 1.000 47.74763  ? 140 GLU B H    1 
ATOM   5751 H HA   . GLU B 1 154 ? -22.43057 -26.82781 10.13015 1.000 50.28221  ? 140 GLU B HA   1 
ATOM   5752 H HB2  . GLU B 1 154 ? -20.80090 -24.61321 9.50725  1.000 52.43582  ? 140 GLU B HB2  1 
ATOM   5753 H HB3  . GLU B 1 154 ? -21.26293 -25.66530 8.40950  1.000 52.43582  ? 140 GLU B HB3  1 
ATOM   5754 H HG2  . GLU B 1 154 ? -23.48165 -25.01561 8.75727  1.000 56.44868  ? 140 GLU B HG2  1 
ATOM   5755 H HG3  . GLU B 1 154 ? -22.97982 -23.92098 9.79427  1.000 56.44868  ? 140 GLU B HG3  1 
ATOM   5756 N N    . TYR B 1 155 ? -20.51811 -28.28123 9.51665  1.000 40.13914  ? 141 TYR B N    1 
ATOM   5757 C CA   . TYR B 1 155 ? -19.40193 -29.20600 9.32686  1.000 41.80533  ? 141 TYR B CA   1 
ATOM   5758 C C    . TYR B 1 155 ? -18.59373 -28.70455 8.13762  1.000 41.70556  ? 141 TYR B C    1 
ATOM   5759 O O    . TYR B 1 155 ? -18.88236 -29.01736 6.98166  1.000 39.03960  ? 141 TYR B O    1 
ATOM   5760 C CB   . TYR B 1 155 ? -19.90182 -30.62970 9.11704  1.000 31.12668  ? 141 TYR B CB   1 
ATOM   5761 C CG   . TYR B 1 155 ? -18.79543 -31.65862 9.03936  1.000 33.22932  ? 141 TYR B CG   1 
ATOM   5762 C CD1  . TYR B 1 155 ? -18.20686 -32.16403 10.19271 1.000 37.32477  ? 141 TYR B CD1  1 
ATOM   5763 C CD2  . TYR B 1 155 ? -18.34143 -32.12800 7.81451  1.000 36.02537  ? 141 TYR B CD2  1 
ATOM   5764 C CE1  . TYR B 1 155 ? -17.19721 -33.10605 10.12699 1.000 30.23396  ? 141 TYR B CE1  1 
ATOM   5765 C CE2  . TYR B 1 155 ? -17.33171 -33.07065 7.73934  1.000 34.45032  ? 141 TYR B CE2  1 
ATOM   5766 C CZ   . TYR B 1 155 ? -16.76333 -33.55559 8.89818  1.000 32.31517  ? 141 TYR B CZ   1 
ATOM   5767 O OH   . TYR B 1 155 ? -15.75698 -34.49303 8.82512  1.000 30.59001  ? 141 TYR B OH   1 
ATOM   5768 H H    . TYR B 1 155 ? -21.22653 -28.49581 9.07882  1.000 48.22291  ? 141 TYR B H    1 
ATOM   5769 H HA   . TYR B 1 155 ? -18.83705 -29.20320 10.11541 1.000 50.22234  ? 141 TYR B HA   1 
ATOM   5770 H HB2  . TYR B 1 155 ? -20.47844 -30.87033 9.85900  1.000 37.40796  ? 141 TYR B HB2  1 
ATOM   5771 H HB3  . TYR B 1 155 ? -20.39911 -30.66621 8.28501  1.000 37.40796  ? 141 TYR B HB3  1 
ATOM   5772 H HD1  . TYR B 1 155 ? -18.49744 -31.86312 11.02332 1.000 44.84567  ? 141 TYR B HD1  1 
ATOM   5773 H HD2  . TYR B 1 155 ? -18.72262 -31.80317 7.03087  1.000 43.28638  ? 141 TYR B HD2  1 
ATOM   5774 H HE1  . TYR B 1 155 ? -16.81282 -33.43467 10.90747 1.000 36.33669  ? 141 TYR B HE1  1 
ATOM   5775 H HE2  . TYR B 1 155 ? -17.03779 -33.37571 6.91142  1.000 41.39632  ? 141 TYR B HE2  1 
ATOM   5776 H HH   . TYR B 1 155 ? -15.53168 -34.61088 8.02452  1.000 36.76396  ? 141 TYR B HH   1 
ATOM   5777 N N    . ASN B 1 156 ? -17.57189 -27.90427 8.42415  1.000 41.77091  ? 142 ASN B N    1 
ATOM   5778 C CA   . ASN B 1 156 ? -16.72870 -27.36041 7.37199  1.000 48.07479  ? 142 ASN B CA   1 
ATOM   5779 C C    . ASN B 1 156 ? -15.39616 -26.94769 7.97306  1.000 43.62407  ? 142 ASN B C    1 
ATOM   5780 O O    . ASN B 1 156 ? -15.31520 -26.58799 9.15048  1.000 37.93083  ? 142 ASN B O    1 
ATOM   5781 C CB   . ASN B 1 156 ? -17.39167 -26.16250 6.68286  1.000 52.07708  ? 142 ASN B CB   1 
ATOM   5782 C CG   . ASN B 1 156 ? -17.66982 -25.02326 7.64011  1.000 52.50754  ? 142 ASN B CG   1 
ATOM   5783 O OD1  . ASN B 1 156 ? -18.76443 -24.91496 8.19173  1.000 57.89082  ? 142 ASN B OD1  1 
ATOM   5784 N ND2  . ASN B 1 156 ? -16.67556 -24.16762 7.84729  1.000 56.63068  ? 142 ASN B ND2  1 
ATOM   5785 H H    . ASN B 1 156 ? -17.34859 -27.66319 9.21890  1.000 50.18103  ? 142 ASN B H    1 
ATOM   5786 H HA   . ASN B 1 156 ? -16.56529 -28.04608 6.70561  1.000 57.74569  ? 142 ASN B HA   1 
ATOM   5787 H HB2  . ASN B 1 156 ? -16.80364 -25.83271 5.98547  1.000 62.54844  ? 142 ASN B HB2  1 
ATOM   5788 H HB3  . ASN B 1 156 ? -18.23612 -26.44545 6.29847  1.000 62.54844  ? 142 ASN B HB3  1 
ATOM   5789 H HD21 . ASN B 1 156 ? -16.78437 -23.50344 8.38267  1.000 68.01276  ? 142 ASN B HD21 1 
ATOM   5790 H HD22 . ASN B 1 156 ? -15.92289 -24.27769 7.44608  1.000 68.01276  ? 142 ASN B HD22 1 
ATOM   5791 N N    . GLY B 1 157 ? -14.35378 -27.01922 7.15209  1.000 47.85486  ? 143 GLY B N    1 
ATOM   5792 C CA   . GLY B 1 157 ? -13.06418 -26.47379 7.50646  1.000 48.53562  ? 143 GLY B CA   1 
ATOM   5793 C C    . GLY B 1 157 ? -13.05288 -24.96421 7.36528  1.000 50.82927  ? 143 GLY B C    1 
ATOM   5794 O O    . GLY B 1 157 ? -14.07401 -24.31710 7.12727  1.000 46.98561  ? 143 GLY B O    1 
ATOM   5795 H H    . GLY B 1 157 ? -14.37541 -27.38550 6.37429  1.000 57.48177  ? 143 GLY B H    1 
ATOM   5796 H HA2  . GLY B 1 157 ? -12.85504 -26.70189 8.42577  1.000 58.29868  ? 143 GLY B HA2  1 
ATOM   5797 H HA3  . GLY B 1 157 ? -12.38201 -26.84572 6.92577  1.000 58.29868  ? 143 GLY B HA3  1 
ATOM   5798 N N    . TRP B 1 158 ? -11.86341 -24.39701 7.50978  1.000 44.67561  ? 144 TRP B N    1 
ATOM   5799 C CA   . TRP B 1 158 ? -11.71003 -22.94770 7.47877  1.000 48.13315  ? 144 TRP B CA   1 
ATOM   5800 C C    . TRP B 1 158 ? -10.22588 -22.62584 7.35475  1.000 44.62846  ? 144 TRP B C    1 
ATOM   5801 O O    . TRP B 1 158 ? -9.37202  -23.51798 7.34670  1.000 38.84263  ? 144 TRP B O    1 
ATOM   5802 C CB   . TRP B 1 158 ? -12.31942 -22.31355 8.73046  1.000 46.79541  ? 144 TRP B CB   1 
ATOM   5803 C CG   . TRP B 1 158 ? -11.65729 -22.78779 9.97463  1.000 39.48606  ? 144 TRP B CG   1 
ATOM   5804 C CD1  . TRP B 1 158 ? -10.59854 -22.21165 10.59990 1.000 41.25341  ? 144 TRP B CD1  1 
ATOM   5805 C CD2  . TRP B 1 158 ? -11.99169 -23.95311 10.73884 1.000 41.42209  ? 144 TRP B CD2  1 
ATOM   5806 N NE1  . TRP B 1 158 ? -10.25086 -22.93807 11.71136 1.000 47.15822  ? 144 TRP B NE1  1 
ATOM   5807 C CE2  . TRP B 1 158 ? -11.09189 -24.01343 11.81894 1.000 40.72822  ? 144 TRP B CE2  1 
ATOM   5808 C CE3  . TRP B 1 158 ? -12.96555 -24.94889 10.61625 1.000 50.41357  ? 144 TRP B CE3  1 
ATOM   5809 C CZ2  . TRP B 1 158 ? -11.13586 -25.02687 12.77168 1.000 36.04341  ? 144 TRP B CZ2  1 
ATOM   5810 C CZ3  . TRP B 1 158 ? -13.00717 -25.95627 11.56544 1.000 42.57747  ? 144 TRP B CZ3  1 
ATOM   5811 C CH2  . TRP B 1 158 ? -12.09845 -25.98585 12.62824 1.000 33.55358  ? 144 TRP B CH2  1 
ATOM   5812 H H    . TRP B 1 158 ? -11.12943 -24.82955 7.62718  1.000 53.66668  ? 144 TRP B H    1 
ATOM   5813 H HA   . TRP B 1 158 ? -12.15701 -22.59360 6.69409  1.000 57.81572  ? 144 TRP B HA   1 
ATOM   5814 H HB2  . TRP B 1 158 ? -12.21797 -21.35013 8.68115  1.000 56.21043  ? 144 TRP B HB2  1 
ATOM   5815 H HB3  . TRP B 1 158 ? -13.25985 -22.54602 8.77978  1.000 56.21043  ? 144 TRP B HB3  1 
ATOM   5816 H HD1  . TRP B 1 158 ? -10.17054 -21.43637 10.31590 1.000 49.56003  ? 144 TRP B HD1  1 
ATOM   5817 H HE1  . TRP B 1 158 ? -9.60943  -22.74877 12.25204 1.000 56.64581  ? 144 TRP B HE1  1 
ATOM   5818 H HE3  . TRP B 1 158 ? -13.57269 -24.93494 9.91191  1.000 60.55223  ? 144 TRP B HE3  1 
ATOM   5819 H HZ2  . TRP B 1 158 ? -10.53282 -25.05048 13.47927 1.000 43.30804  ? 144 TRP B HZ2  1 
ATOM   5820 H HZ3  . TRP B 1 158 ? -13.65020 -26.62444 11.49504 1.000 51.14890  ? 144 TRP B HZ3  1 
ATOM   5821 H HH2  . TRP B 1 158 ? -12.15062 -26.67404 13.25160 1.000 40.32024  ? 144 TRP B HH2  1 
ATOM   5822 N N    . CYS B 1 159 ? -9.92947  -21.33371 7.25049  1.000 51.95459  ? 145 CYS B N    1 
ATOM   5823 C CA   . CYS B 1 159 ? -8.56747  -20.82004 7.25336  1.000 56.17845  ? 145 CYS B CA   1 
ATOM   5824 C C    . CYS B 1 159 ? -8.42662  -19.82236 8.39372  1.000 48.20653  ? 145 CYS B C    1 
ATOM   5825 O O    . CYS B 1 159 ? -9.28155  -18.94708 8.56537  1.000 51.93069  ? 145 CYS B O    1 
ATOM   5826 C CB   . CYS B 1 159 ? -8.22212  -20.14938 5.92053  1.000 45.36831  ? 145 CYS B CB   1 
ATOM   5827 S SG   . CYS B 1 159 ? -8.23974  -21.23482 4.47627  1.000 53.15171  ? 145 CYS B SG   1 
ATOM   5828 N N    . GLY B 1 160 ? -7.35894  -19.95979 9.17204  1.000 42.08032  ? 146 GLY B N    1 
ATOM   5829 C CA   . GLY B 1 160 ? -7.10049  -19.02531 10.24689 1.000 42.53940  ? 146 GLY B CA   1 
ATOM   5830 C C    . GLY B 1 160 ? -8.08991  -19.14273 11.39901 1.000 39.44852  ? 146 GLY B C    1 
ATOM   5831 O O    . GLY B 1 160 ? -8.93626  -20.03272 11.45590 1.000 38.79547  ? 146 GLY B O    1 
ATOM   5832 N N    . ASP B 1 161 ? -7.95748  -18.21065 12.33873 1.000 41.98630  ? 147 ASP B N    1 
ATOM   5833 C CA   . ASP B 1 161 ? -6.94867  -17.15723 12.32495 1.000 39.74274  ? 147 ASP B CA   1 
ATOM   5834 C C    . ASP B 1 161 ? -5.54323  -17.73518 12.47674 1.000 41.17946  ? 147 ASP B C    1 
ATOM   5835 O O    . ASP B 1 161 ? -5.35607  -18.79019 13.08598 1.000 34.60746  ? 147 ASP B O    1 
ATOM   5836 C CB   . ASP B 1 161 ? -7.22247  -16.13799 13.43551 1.000 42.38238  ? 147 ASP B CB   1 
ATOM   5837 C CG   . ASP B 1 161 ? -8.51966  -15.37593 13.22372 1.000 45.83888  ? 147 ASP B CG   1 
ATOM   5838 O OD1  . ASP B 1 161 ? -9.16155  -15.56936 12.17009 1.000 52.25549  ? 147 ASP B OD1  1 
ATOM   5839 O OD2  . ASP B 1 161 ? -8.89919  -14.58477 14.11247 1.000 40.08669  ? 147 ASP B OD2  1 
ATOM   5840 N N    . ASN B 1 162 ? -4.56409  -17.03987 11.90028 1.000 37.88625  ? 148 ASN B N    1 
ATOM   5841 C CA   . ASN B 1 162 ? -3.17689  -17.47170 11.98994 1.000 33.67273  ? 148 ASN B CA   1 
ATOM   5842 C C    . ASN B 1 162 ? -2.79387  -17.73098 13.44195 1.000 34.07776  ? 148 ASN B C    1 
ATOM   5843 O O    . ASN B 1 162 ? -3.28792  -17.07702 14.36537 1.000 34.04058  ? 148 ASN B O    1 
ATOM   5844 C CB   . ASN B 1 162 ? -2.25644  -16.41116 11.38113 1.000 32.24188  ? 148 ASN B CB   1 
ATOM   5845 C CG   . ASN B 1 162 ? -2.56232  -16.14052 9.91797  1.000 35.78636  ? 148 ASN B CG   1 
ATOM   5846 O OD1  . ASN B 1 162 ? -2.63086  -17.06094 9.10547  1.000 37.32952  ? 148 ASN B OD1  1 
ATOM   5847 N ND2  . ASN B 1 162 ? -2.75572  -14.87070 9.57856  1.000 38.70083  ? 148 ASN B ND2  1 
ATOM   5848 H H    . ASN B 1 162 ? -4.67897  -16.31497 11.45204 1.000 45.51944  ? 148 ASN B H    1 
ATOM   5849 H HA   . ASN B 1 162 ? -3.05920  -18.29670 11.49353 1.000 40.46322  ? 148 ASN B HA   1 
ATOM   5850 H HB2  . ASN B 1 162 ? -2.36499  -15.58003 11.86932 1.000 38.74620  ? 148 ASN B HB2  1 
ATOM   5851 H HB3  . ASN B 1 162 ? -1.33762  -16.71557 11.44450 1.000 38.74620  ? 148 ASN B HB3  1 
ATOM   5852 H HD21 . ASN B 1 162 ? -2.70476  -14.25354 10.17532 1.000 46.49693  ? 148 ASN B HD21 1 
ATOM   5853 H HD22 . ASN B 1 162 ? -2.93187  -14.66587 8.76210  1.000 46.49693  ? 148 ASN B HD22 1 
ATOM   5854 N N    . VAL B 1 163 ? -1.90496  -18.70181 13.63903 1.000 30.86358  ? 149 VAL B N    1 
ATOM   5855 C CA   . VAL B 1 163 ? -1.45905  -19.10284 14.96944 1.000 29.58505  ? 149 VAL B CA   1 
ATOM   5856 C C    . VAL B 1 163 ? -0.23117  -18.26210 15.30461 1.000 29.98021  ? 149 VAL B C    1 
ATOM   5857 O O    . VAL B 1 163 ? 0.87879   -18.56043 14.86695 1.000 29.99580  ? 149 VAL B O    1 
ATOM   5858 C CB   . VAL B 1 163 ? -1.15535  -20.60052 15.03261 1.000 28.28356  ? 149 VAL B CB   1 
ATOM   5859 C CG1  . VAL B 1 163 ? -0.66354  -20.99167 16.41902 1.000 27.04898  ? 149 VAL B CG1  1 
ATOM   5860 C CG2  . VAL B 1 163 ? -2.38881  -21.40879 14.64758 1.000 30.99264  ? 149 VAL B CG2  1 
ATOM   5861 H H    . VAL B 1 163 ? -1.53863  -19.15187 13.00433 1.000 37.09224  ? 149 VAL B H    1 
ATOM   5862 H HA   . VAL B 1 163 ? -2.15387  -18.90191 15.61577 1.000 35.55800  ? 149 VAL B HA   1 
ATOM   5863 H HB   . VAL B 1 163 ? -0.45004  -20.80470 14.39877 1.000 33.99621  ? 149 VAL B HB   1 
ATOM   5864 H HG11 . VAL B 1 163 ? 0.14959   -20.50075 16.61580 1.000 32.51472  ? 149 VAL B HG11 1 
ATOM   5865 H HG12 . VAL B 1 163 ? -1.34808  -20.77253 17.07040 1.000 32.51472  ? 149 VAL B HG12 1 
ATOM   5866 H HG13 . VAL B 1 163 ? -0.48604  -21.94517 16.43377 1.000 32.51472  ? 149 VAL B HG13 1 
ATOM   5867 H HG21 . VAL B 1 163 ? -2.15207  -22.34880 14.61238 1.000 37.24710  ? 149 VAL B HG21 1 
ATOM   5868 H HG22 . VAL B 1 163 ? -3.08003  -21.26646 15.31306 1.000 37.24710  ? 149 VAL B HG22 1 
ATOM   5869 H HG23 . VAL B 1 163 ? -2.70106  -21.11353 13.77797 1.000 37.24710  ? 149 VAL B HG23 1 
ATOM   5870 N N    . TYR B 1 164 ? -0.42951  -17.20799 16.08963 1.000 29.38853  ? 150 TYR B N    1 
ATOM   5871 C CA   . TYR B 1 164 ? 0.66424   -16.31483 16.45051 1.000 27.13372  ? 150 TYR B CA   1 
ATOM   5872 C C    . TYR B 1 164 ? 1.46787   -16.92847 17.58839 1.000 31.51850  ? 150 TYR B C    1 
ATOM   5873 O O    . TYR B 1 164 ? 0.91851   -17.24379 18.64837 1.000 32.54822  ? 150 TYR B O    1 
ATOM   5874 C CB   . TYR B 1 164 ? 0.11990   -14.93968 16.82357 1.000 27.74715  ? 150 TYR B CB   1 
ATOM   5875 C CG   . TYR B 1 164 ? -0.06445  -14.05903 15.60843 1.000 33.57057  ? 150 TYR B CG   1 
ATOM   5876 C CD1  . TYR B 1 164 ? -1.06939  -14.31752 14.68279 1.000 30.82565  ? 150 TYR B CD1  1 
ATOM   5877 C CD2  . TYR B 1 164 ? 0.78200   -12.98655 15.37218 1.000 32.04815  ? 150 TYR B CD2  1 
ATOM   5878 C CE1  . TYR B 1 164 ? -1.23147  -13.52175 13.56240 1.000 30.12055  ? 150 TYR B CE1  1 
ATOM   5879 C CE2  . TYR B 1 164 ? 0.62831   -12.18684 14.25615 1.000 39.01046  ? 150 TYR B CE2  1 
ATOM   5880 C CZ   . TYR B 1 164 ? -0.37789  -12.45940 13.35450 1.000 33.98606  ? 150 TYR B CZ   1 
ATOM   5881 O OH   . TYR B 1 164 ? -0.52943  -11.66124 12.24444 1.000 33.68814  ? 150 TYR B OH   1 
ATOM   5882 H H    . TYR B 1 164 ? -1.18981  -16.98861 16.42639 1.000 35.32218  ? 150 TYR B H    1 
ATOM   5883 H HA   . TYR B 1 164 ? 1.26078   -16.20135 15.69410 1.000 32.61640  ? 150 TYR B HA   1 
ATOM   5884 H HB2  . TYR B 1 164 ? -0.74156  -15.04418 17.25701 1.000 33.01688  ? 150 TYR B HB2  1 
ATOM   5885 H HB3  . TYR B 1 164 ? 0.74284   -14.50209 17.42470 1.000 33.01688  ? 150 TYR B HB3  1 
ATOM   5886 H HD1  . TYR B 1 164 ? -1.64225  -15.03737 14.81900 1.000 37.04672  ? 150 TYR B HD1  1 
ATOM   5887 H HD2  . TYR B 1 164 ? 1.46524   -12.80229 15.97562 1.000 38.51372  ? 150 TYR B HD2  1 
ATOM   5888 H HE1  . TYR B 1 164 ? -1.91133  -13.70231 12.95405 1.000 35.86496  ? 150 TYR B HE1  1 
ATOM   5889 H HE2  . TYR B 1 164 ? 1.20103   -11.46805 14.11395 1.000 46.86849  ? 150 TYR B HE2  1 
ATOM   5890 H HH   . TYR B 1 164 ? -1.20210  -11.90551 11.80461 1.000 40.14607  ? 150 TYR B HH   1 
ATOM   5891 N N    . ILE B 1 165 ? 2.76653   -17.10055 17.36206 1.000 30.39976  ? 151 ILE B N    1 
ATOM   5892 C CA   . ILE B 1 165 ? 3.64521   -17.82946 18.26585 1.000 28.24509  ? 151 ILE B CA   1 
ATOM   5893 C C    . ILE B 1 165 ? 4.64352   -16.85821 18.87530 1.000 32.02594  ? 151 ILE B C    1 
ATOM   5894 O O    . ILE B 1 165 ? 5.20086   -16.00028 18.17933 1.000 28.71431  ? 151 ILE B O    1 
ATOM   5895 C CB   . ILE B 1 165 ? 4.37022   -18.97430 17.53013 1.000 28.05237  ? 151 ILE B CB   1 
ATOM   5896 C CG1  . ILE B 1 165 ? 3.36756   -20.05982 17.13236 1.000 31.83579  ? 151 ILE B CG1  1 
ATOM   5897 C CG2  . ILE B 1 165 ? 5.48895   -19.53953 18.39261 1.000 27.49331  ? 151 ILE B CG2  1 
ATOM   5898 C CD1  . ILE B 1 165 ? 3.93450   -21.10582 16.19530 1.000 28.36758  ? 151 ILE B CD1  1 
ATOM   5899 H H    . ILE B 1 165 ? 3.17271   -16.79371 16.66890 1.000 36.53565  ? 151 ILE B H    1 
ATOM   5900 H HA   . ILE B 1 165 ? 3.11846   -18.20905 18.98651 1.000 33.95005  ? 151 ILE B HA   1 
ATOM   5901 H HB   . ILE B 1 165 ? 4.77134   -18.62222 16.72016 1.000 33.71878  ? 151 ILE B HB   1 
ATOM   5902 H HG12 . ILE B 1 165 ? 3.06621   -20.51423 17.93461 1.000 38.25889  ? 151 ILE B HG12 1 
ATOM   5903 H HG13 . ILE B 1 165 ? 2.61528   -19.64031 16.68628 1.000 38.25889  ? 151 ILE B HG13 1 
ATOM   5904 H HG21 . ILE B 1 165 ? 6.24763   -18.93595 18.36117 1.000 33.04791  ? 151 ILE B HG21 1 
ATOM   5905 H HG22 . ILE B 1 165 ? 5.17171   -19.62482 19.30530 1.000 33.04791  ? 151 ILE B HG22 1 
ATOM   5906 H HG23 . ILE B 1 165 ? 5.74410   -20.40978 18.04843 1.000 33.04791  ? 151 ILE B HG23 1 
ATOM   5907 H HD11 . ILE B 1 165 ? 3.20227   -21.57742 15.76830 1.000 34.09704  ? 151 ILE B HD11 1 
ATOM   5908 H HD12 . ILE B 1 165 ? 4.48065   -20.66639 15.52483 1.000 34.09704  ? 151 ILE B HD12 1 
ATOM   5909 H HD13 . ILE B 1 165 ? 4.47526   -21.72799 16.70656 1.000 34.09704  ? 151 ILE B HD13 1 
ATOM   5910 N N    . THR B 1 166 ? 4.86337   -16.99761 20.17938 1.000 29.53651  ? 152 THR B N    1 
ATOM   5911 C CA   . THR B 1 166 ? 5.83641   -16.20642 20.91473 1.000 31.05009  ? 152 THR B CA   1 
ATOM   5912 C C    . THR B 1 166 ? 6.66466   -17.12819 21.79800 1.000 31.82757  ? 152 THR B C    1 
ATOM   5913 O O    . THR B 1 166 ? 6.20036   -18.19038 22.22255 1.000 31.54753  ? 152 THR B O    1 
ATOM   5914 C CB   . THR B 1 166 ? 5.15803   -15.13732 21.78122 1.000 30.65743  ? 152 THR B CB   1 
ATOM   5915 O OG1  . THR B 1 166 ? 4.18235   -15.75639 22.63088 1.000 36.94308  ? 152 THR B OG1  1 
ATOM   5916 C CG2  . THR B 1 166 ? 4.48367   -14.09105 20.91062 1.000 31.35700  ? 152 THR B CG2  1 
ATOM   5917 H H    . THR B 1 166 ? 4.44574   -17.56375 20.67402 1.000 35.49976  ? 152 THR B H    1 
ATOM   5918 H HA   . THR B 1 166 ? 6.42864   -15.75752 20.29131 1.000 37.31604  ? 152 THR B HA   1 
ATOM   5919 H HB   . THR B 1 166 ? 5.82462   -14.69208 22.32741 1.000 36.50922  ? 152 THR B HB   1 
ATOM   5920 H HG1  . THR B 1 166 ? 3.60259   -16.14722 22.16534 1.000 44.38763  ? 152 THR B HG1  1 
ATOM   5921 H HG21 . THR B 1 166 ? 5.12999   -13.69812 20.30335 1.000 37.34869  ? 152 THR B HG21 1 
ATOM   5922 H HG22 . THR B 1 166 ? 3.77237   -14.49903 20.39244 1.000 37.34869  ? 152 THR B HG22 1 
ATOM   5923 H HG23 . THR B 1 166 ? 4.10679   -13.39047 21.46565 1.000 37.34869  ? 152 THR B HG23 1 
ATOM   5924 N N    . ALA B 1 167 ? 7.89715   -16.71244 22.06925 1.000 30.71497  ? 153 ALA B N    1 
ATOM   5925 C CA   . ALA B 1 167 ? 8.78599   -17.48794 22.91859 1.000 34.01526  ? 153 ALA B CA   1 
ATOM   5926 C C    . ALA B 1 167 ? 8.43088   -17.30119 24.38844 1.000 34.72097  ? 153 ALA B C    1 
ATOM   5927 O O    . ALA B 1 167 ? 7.97727   -16.23451 24.81253 1.000 32.97971  ? 153 ALA B O    1 
ATOM   5928 C CB   . ALA B 1 167 ? 10.24116  -17.08197 22.68695 1.000 34.13843  ? 153 ALA B CB   1 
ATOM   5929 H H    . ALA B 1 167 ? 8.24139   -15.98259 21.77190 1.000 36.57826  ? 153 ALA B H    1 
ATOM   5930 H HA   . ALA B 1 167 ? 8.69320   -18.42848 22.70025 1.000 40.87425  ? 153 ALA B HA   1 
ATOM   5931 H HB1  . ALA B 1 167 ? 10.34169  -16.13845 22.88837 1.000 41.02205  ? 153 ALA B HB1  1 
ATOM   5932 H HB2  . ALA B 1 167 ? 10.81208  -17.60718 23.26927 1.000 41.02205  ? 153 ALA B HB2  1 
ATOM   5933 H HB3  . ALA B 1 167 ? 10.47172  -17.24862 21.75960 1.000 41.02205  ? 153 ALA B HB3  1 
ATOM   5934 N N    . ASP B 1 168 ? 8.64475   -18.36387 25.16982 1.000 42.31526  ? 154 ASP B N    1 
ATOM   5935 C CA   . ASP B 1 168 ? 8.46019   -18.34875 26.62344 1.000 38.51147  ? 154 ASP B CA   1 
ATOM   5936 C C    . ASP B 1 168 ? 9.76172   -18.86936 27.23238 1.000 41.61844  ? 154 ASP B C    1 
ATOM   5937 O O    . ASP B 1 168 ? 9.85643   -20.03211 27.63278 1.000 39.32606  ? 154 ASP B O    1 
ATOM   5938 C CB   . ASP B 1 168 ? 7.25134   -19.18517 27.03680 1.000 34.62237  ? 154 ASP B CB   1 
ATOM   5939 C CG   . ASP B 1 168 ? 6.81577   -18.91718 28.46488 1.000 45.23663  ? 154 ASP B CG   1 
ATOM   5940 O OD1  . ASP B 1 168 ? 7.65518   -18.47206 29.27748 1.000 43.21702  ? 154 ASP B OD1  1 
ATOM   5941 O OD2  . ASP B 1 168 ? 5.62884   -19.15246 28.77367 1.000 50.23113  ? 154 ASP B OD2  1 
ATOM   5942 H H    . ASP B 1 168 ? 8.90494   -19.12712 24.87091 1.000 50.83425  ? 154 ASP B H    1 
ATOM   5943 H HA   . ASP B 1 168 ? 8.30721   -17.44075 26.92845 1.000 46.26970  ? 154 ASP B HA   1 
ATOM   5944 H HB2  . ASP B 1 168 ? 6.50671   -18.97597 26.45144 1.000 41.60278  ? 154 ASP B HB2  1 
ATOM   5945 H HB3  . ASP B 1 168 ? 7.47717   -20.12564 26.96318 1.000 41.60278  ? 154 ASP B HB3  1 
ATOM   5946 N N    . LYS B 1 169 ? 10.77101  -17.99653 27.28864 1.000 41.05290  ? 155 LYS B N    1 
ATOM   5947 C CA   . LYS B 1 169 ? 12.08398  -18.41006 27.77418 1.000 48.81325  ? 155 LYS B CA   1 
ATOM   5948 C C    . LYS B 1 169 ? 12.01018  -18.93982 29.20066 1.000 55.86699  ? 155 LYS B C    1 
ATOM   5949 O O    . LYS B 1 169 ? 12.69218  -19.91337 29.54285 1.000 54.43263  ? 155 LYS B O    1 
ATOM   5950 C CB   . LYS B 1 169 ? 13.06358  -17.24035 27.68672 1.000 52.33686  ? 155 LYS B CB   1 
ATOM   5951 C CG   . LYS B 1 169 ? 13.66440  -17.03863 26.30258 1.000 65.61946  ? 155 LYS B CG   1 
ATOM   5952 C CD   . LYS B 1 169 ? 14.31817  -15.67051 26.17065 1.000 72.54466  ? 155 LYS B CD   1 
ATOM   5953 C CE   . LYS B 1 169 ? 13.28513  -14.58662 25.90180 1.000 70.69005  ? 155 LYS B CE   1 
ATOM   5954 N NZ   . LYS B 1 169 ? 13.82685  -13.22172 26.15239 1.000 78.35037  ? 155 LYS B NZ   1 
ATOM   5955 H H    . LYS B 1 169 ? 10.72078  -17.17058 27.05440 1.000 49.31942  ? 155 LYS B H    1 
ATOM   5956 H HA   . LYS B 1 169 ? 12.41363  -19.12564 27.20834 1.000 58.63184  ? 155 LYS B HA   1 
ATOM   5957 H HB2  . LYS B 1 169 ? 12.59654  -16.42499 27.92748 1.000 62.86017  ? 155 LYS B HB2  1 
ATOM   5958 H HB3  . LYS B 1 169 ? 13.79375  -17.39939 28.30515 1.000 62.86017  ? 155 LYS B HB3  1 
ATOM   5959 H HG2  . LYS B 1 169 ? 14.34054  -17.71587 26.14423 1.000 78.79929  ? 155 LYS B HG2  1 
ATOM   5960 H HG3  . LYS B 1 169 ? 12.96370  -17.10701 25.63531 1.000 78.79929  ? 155 LYS B HG3  1 
ATOM   5961 H HD2  . LYS B 1 169 ? 14.78065  -15.45391 26.99533 1.000 87.10953  ? 155 LYS B HD2  1 
ATOM   5962 H HD3  . LYS B 1 169 ? 14.94634  -15.68387 25.43165 1.000 87.10953  ? 155 LYS B HD3  1 
ATOM   5963 H HE2  . LYS B 1 169 ? 13.00562  -14.63557 24.97423 1.000 84.88400  ? 155 LYS B HE2  1 
ATOM   5964 H HE3  . LYS B 1 169 ? 12.52235  -14.72126 26.48569 1.000 84.88400  ? 155 LYS B HE3  1 
ATOM   5965 H HZ1  . LYS B 1 169 ? 14.01212  -13.12178 27.01714 1.000 94.07638  ? 155 LYS B HZ1  1 
ATOM   5966 H HZ2  . LYS B 1 169 ? 14.57185  -13.09868 25.68129 1.000 94.07638  ? 155 LYS B HZ2  1 
ATOM   5967 H HZ3  . LYS B 1 169 ? 13.22866  -12.60800 25.91235 1.000 94.07638  ? 155 LYS B HZ3  1 
ATOM   5968 N N    . GLN B 1 170 ? 11.19345  -18.31132 30.05008 1.000 58.21507  ? 156 GLN B N    1 
ATOM   5969 C CA   . GLN B 1 170 ? 11.04439  -18.79039 31.42075 1.000 62.95013  ? 156 GLN B CA   1 
ATOM   5970 C C    . GLN B 1 170 ? 10.65408  -20.26270 31.44413 1.000 62.03471  ? 156 GLN B C    1 
ATOM   5971 O O    . GLN B 1 170 ? 11.31173  -21.08468 32.09273 1.000 63.40546  ? 156 GLN B O    1 
ATOM   5972 C CB   . GLN B 1 170 ? 10.00386  -17.95166 32.16521 1.000 67.03319  ? 156 GLN B CB   1 
ATOM   5973 C CG   . GLN B 1 170 ? 10.54236  -16.64814 32.73223 1.000 62.64292  ? 156 GLN B CG   1 
ATOM   5974 C CD   . GLN B 1 170 ? 9.65406   -16.07789 33.82376 1.000 63.51619  ? 156 GLN B CD   1 
ATOM   5975 O OE1  . GLN B 1 170 ? 8.42866   -16.18329 33.76290 1.000 61.50924  ? 156 GLN B OE1  1 
ATOM   5976 N NE2  . GLN B 1 170 ? 10.27185  -15.47948 34.83683 1.000 67.04300  ? 156 GLN B NE2  1 
ATOM   5977 H H    . GLN B 1 170 ? 10.72316  -17.61713 29.85895 1.000 69.91403  ? 156 GLN B H    1 
ATOM   5978 H HA   . GLN B 1 170 ? 11.89370  -18.68984 31.87843 1.000 75.59610  ? 156 GLN B HA   1 
ATOM   5979 H HB2  . GLN B 1 170 ? 9.28654   -17.73090 31.55070 1.000 80.49576  ? 156 GLN B HB2  1 
ATOM   5980 H HB3  . GLN B 1 170 ? 9.65741   -18.47358 32.90580 1.000 80.49576  ? 156 GLN B HB3  1 
ATOM   5981 H HG2  . GLN B 1 170 ? 11.42108  -16.80637 33.11134 1.000 75.22744  ? 156 GLN B HG2  1 
ATOM   5982 H HG3  . GLN B 1 170 ? 10.60163  -15.99289 32.01947 1.000 75.22744  ? 156 GLN B HG3  1 
ATOM   5983 H HE21 . GLN B 1 170 ? 11.13043  -15.43149 34.84897 1.000 80.50754  ? 156 GLN B HE21 1 
ATOM   5984 H HE22 . GLN B 1 170 ? 9.81307   -15.14022 35.48027 1.000 80.50754  ? 156 GLN B HE22 1 
ATOM   5985 N N    . LYS B 1 171 ? 9.58184   -20.61290 30.73710 1.000 54.19525  ? 157 LYS B N    1 
ATOM   5986 C CA   . LYS B 1 171 ? 9.12590   -21.99408 30.66607 1.000 56.37425  ? 157 LYS B CA   1 
ATOM   5987 C C    . LYS B 1 171 ? 9.90973   -22.82616 29.65946 1.000 52.63208  ? 157 LYS B C    1 
ATOM   5988 O O    . LYS B 1 171 ? 9.57702   -23.99953 29.46183 1.000 52.74244  ? 157 LYS B O    1 
ATOM   5989 C CB   . LYS B 1 171 ? 7.63625   -22.03707 30.31247 1.000 58.35387  ? 157 LYS B CB   1 
ATOM   5990 C CG   . LYS B 1 171 ? 6.74728   -21.21391 31.23717 1.000 64.51834  ? 157 LYS B CG   1 
ATOM   5991 C CD   . LYS B 1 171 ? 6.96068   -21.57776 32.70063 1.000 69.49941  ? 157 LYS B CD   1 
ATOM   5992 C CE   . LYS B 1 171 ? 5.89547   -20.95614 33.59365 1.000 71.52829  ? 157 LYS B CE   1 
ATOM   5993 N NZ   . LYS B 1 171 ? 5.90252   -19.46725 33.53877 1.000 89.83397  ? 157 LYS B NZ   1 
ATOM   5994 H H    . LYS B 1 171 ? 9.09868   -20.06232 30.28652 1.000 65.09024  ? 157 LYS B H    1 
ATOM   5995 H HA   . LYS B 1 171 ? 9.23867   -22.39997 31.53981 1.000 67.70504  ? 157 LYS B HA   1 
ATOM   5996 H HB2  . LYS B 1 171 ? 7.52167   -21.69366 29.41256 1.000 70.08059  ? 157 LYS B HB2  1 
ATOM   5997 H HB3  . LYS B 1 171 ? 7.33391   -22.95766 30.35726 1.000 70.08059  ? 157 LYS B HB3  1 
ATOM   5998 H HG2  . LYS B 1 171 ? 6.95384   -20.27278 31.12533 1.000 77.47795  ? 157 LYS B HG2  1 
ATOM   5999 H HG3  . LYS B 1 171 ? 5.81711   -21.37794 31.01631 1.000 77.47795  ? 157 LYS B HG3  1 
ATOM   6000 H HD2  . LYS B 1 171 ? 6.91782   -22.54158 32.80127 1.000 83.45523  ? 157 LYS B HD2  1 
ATOM   6001 H HD3  . LYS B 1 171 ? 7.82770   -21.25230 32.98914 1.000 83.45523  ? 157 LYS B HD3  1 
ATOM   6002 H HE2  . LYS B 1 171 ? 5.02156   -21.26352 33.30608 1.000 85.88988  ? 157 LYS B HE2  1 
ATOM   6003 H HE3  . LYS B 1 171 ? 6.05570   -21.22397 34.51208 1.000 85.88988  ? 157 LYS B HE3  1 
ATOM   6004 H HZ1  . LYS B 1 171 ? 5.27917   -19.13963 34.08302 1.000 107.85670 ? 157 LYS B HZ1  1 
ATOM   6005 H HZ2  . LYS B 1 171 ? 6.69781   -19.15713 33.79064 1.000 107.85670 ? 157 LYS B HZ2  1 
ATOM   6006 H HZ3  . LYS B 1 171 ? 5.73490   -19.19244 32.70903 1.000 107.85670 ? 157 LYS B HZ3  1 
ATOM   6007 N N    . ASN B 1 172 ? 10.93256  -22.25550 29.02314 1.000 49.81885  ? 158 ASN B N    1 
ATOM   6008 C CA   . ASN B 1 172 ? 11.74141  -22.97718 28.04180 1.000 51.43605  ? 158 ASN B CA   1 
ATOM   6009 C C    . ASN B 1 172 ? 10.86453  -23.57707 26.94497 1.000 49.48979  ? 158 ASN B C    1 
ATOM   6010 O O    . ASN B 1 172 ? 11.03989  -24.72620 26.53375 1.000 44.98825  ? 158 ASN B O    1 
ATOM   6011 C CB   . ASN B 1 172 ? 12.57979  -24.06222 28.71926 1.000 55.31314  ? 158 ASN B CB   1 
ATOM   6012 C CG   . ASN B 1 172 ? 13.52596  -24.75499 27.75577 1.000 49.64644  ? 158 ASN B CG   1 
ATOM   6013 O OD1  . ASN B 1 172 ? 14.11934  -24.11859 26.88468 1.000 50.92227  ? 158 ASN B OD1  1 
ATOM   6014 N ND2  . ASN B 1 172 ? 13.65768  -26.06851 27.89779 1.000 52.18020  ? 158 ASN B ND2  1 
ATOM   6015 H H    . ASN B 1 172 ? 11.18091  -21.44109 29.14415 1.000 59.83856  ? 158 ASN B H    1 
ATOM   6016 H HA   . ASN B 1 172 ? 12.34727  -22.34679 27.62173 1.000 61.77920  ? 158 ASN B HA   1 
ATOM   6017 H HB2  . ASN B 1 172 ? 13.11053  -23.65865 29.42377 1.000 66.43171  ? 158 ASN B HB2  1 
ATOM   6018 H HB3  . ASN B 1 172 ? 11.98722  -24.73302 29.09315 1.000 66.43171  ? 158 ASN B HB3  1 
ATOM   6019 H HD21 . ASN B 1 172 ? 14.18219  -26.50697 27.37602 1.000 62.67217  ? 158 ASN B HD21 1 
ATOM   6020 H HD22 . ASN B 1 172 ? 13.21849  -26.48084 28.51154 1.000 62.67217  ? 158 ASN B HD22 1 
ATOM   6021 N N    . GLY B 1 173 ? 9.91446   -22.79508 26.46946 1.000 36.23729  ? 159 GLY B N    1 
ATOM   6022 C CA   . GLY B 1 173 ? 9.00225   -23.24589 25.43709 1.000 32.23193  ? 159 GLY B CA   1 
ATOM   6023 C C    . GLY B 1 173 ? 8.42939   -22.07807 24.67332 1.000 30.56620  ? 159 GLY B C    1 
ATOM   6024 O O    . GLY B 1 173 ? 9.07728   -21.04105 24.51380 1.000 33.22435  ? 159 GLY B O    1 
ATOM   6025 H H    . GLY B 1 173 ? 9.77505   -21.98792 26.73148 1.000 43.54068  ? 159 GLY B H    1 
ATOM   6026 H HA2  . GLY B 1 173 ? 9.47204   -23.82370 24.81553 1.000 38.73425  ? 159 GLY B HA2  1 
ATOM   6027 H HA3  . GLY B 1 173 ? 8.27258   -23.74219 25.83979 1.000 38.73425  ? 159 GLY B HA3  1 
ATOM   6028 N N    . ILE B 1 174 ? 7.19344   -22.24539 24.20207 1.000 31.43762  ? 160 ILE B N    1 
ATOM   6029 C CA   . ILE B 1 174 ? 6.52101   -21.23529 23.40065 1.000 33.45526  ? 160 ILE B CA   1 
ATOM   6030 C C    . ILE B 1 174 ? 5.09199   -21.06226 23.89484 1.000 36.19399  ? 160 ILE B C    1 
ATOM   6031 O O    . ILE B 1 174 ? 4.52438   -21.93007 24.56284 1.000 32.28957  ? 160 ILE B O    1 
ATOM   6032 C CB   . ILE B 1 174 ? 6.52031   -21.58964 21.89653 1.000 33.13867  ? 160 ILE B CB   1 
ATOM   6033 C CG1  . ILE B 1 174 ? 5.83772   -22.93962 21.66019 1.000 33.42431  ? 160 ILE B CG1  1 
ATOM   6034 C CG2  . ILE B 1 174 ? 7.94178   -21.61999 21.35885 1.000 36.29765  ? 160 ILE B CG2  1 
ATOM   6035 C CD1  . ILE B 1 174 ? 5.53257   -23.22668 20.19502 1.000 31.46351  ? 160 ILE B CD1  1 
ATOM   6036 H H    . ILE B 1 174 ? 6.71935   -22.94987 24.33823 1.000 37.78108  ? 160 ILE B H    1 
ATOM   6037 H HA   . ILE B 1 174 ? 6.98171   -20.39022 23.52114 1.000 40.20225  ? 160 ILE B HA   1 
ATOM   6038 H HB   . ILE B 1 174 ? 6.02051   -20.90451 21.42568 1.000 39.82235  ? 160 ILE B HB   1 
ATOM   6039 H HG12 . ILE B 1 174 ? 6.42001   -23.64431 21.98463 1.000 40.16512  ? 160 ILE B HG12 1 
ATOM   6040 H HG13 . ILE B 1 174 ? 4.99795   -22.95344 22.14546 1.000 40.16512  ? 160 ILE B HG13 1 
ATOM   6041 H HG21 . ILE B 1 174 ? 8.41393   -22.36821 21.75652 1.000 43.61312  ? 160 ILE B HG21 1 
ATOM   6042 H HG22 . ILE B 1 174 ? 7.91260   -21.72204 20.39467 1.000 43.61312  ? 160 ILE B HG22 1 
ATOM   6043 H HG23 . ILE B 1 174 ? 8.38476   -20.78865 21.59023 1.000 43.61312  ? 160 ILE B HG23 1 
ATOM   6044 H HD11 . ILE B 1 174 ? 5.11779   -24.10067 20.12419 1.000 37.81215  ? 160 ILE B HD11 1 
ATOM   6045 H HD12 . ILE B 1 174 ? 4.92892   -22.54585 19.85890 1.000 37.81215  ? 160 ILE B HD12 1 
ATOM   6046 H HD13 . ILE B 1 174 ? 6.36126   -23.21200 19.69109 1.000 37.81215  ? 160 ILE B HD13 1 
ATOM   6047 N N    . LYS B 1 175 ? 4.51943   -19.91206 23.55564 1.000 31.49383  ? 161 LYS B N    1 
ATOM   6048 C CA   . LYS B 1 175 ? 3.10543   -19.63443 23.73717 1.000 31.38809  ? 161 LYS B CA   1 
ATOM   6049 C C    . LYS B 1 175 ? 2.49426   -19.29914 22.38404 1.000 32.04192  ? 161 LYS B C    1 
ATOM   6050 O O    . LYS B 1 175 ? 3.18501   -18.86383 21.45832 1.000 32.16517  ? 161 LYS B O    1 
ATOM   6051 C CB   . LYS B 1 175 ? 2.87613   -18.47726 24.71686 1.000 32.60666  ? 161 LYS B CB   1 
ATOM   6052 C CG   . LYS B 1 175 ? 2.97527   -18.86219 26.18266 1.000 38.22610  ? 161 LYS B CG   1 
ATOM   6053 C CD   . LYS B 1 175 ? 2.53029   -17.70820 27.06717 1.000 52.00664  ? 161 LYS B CD   1 
ATOM   6054 C CE   . LYS B 1 175 ? 2.27205   -18.15845 28.49590 1.000 50.86785  ? 161 LYS B CE   1 
ATOM   6055 N NZ   . LYS B 1 175 ? 1.66437   -17.06141 29.29852 1.000 50.67931  ? 161 LYS B NZ   1 
ATOM   6056 H H    . LYS B 1 175 ? 4.94850   -19.25415 23.20542 1.000 37.84854  ? 161 LYS B H    1 
ATOM   6057 H HA   . LYS B 1 175 ? 2.66075   -20.41599 24.10094 1.000 37.72164  ? 161 LYS B HA   1 
ATOM   6058 N N    . ALA B 1 176 ? 1.18659   -19.51199 22.27256 1.000 28.45561  ? 162 ALA B N    1 
ATOM   6059 C CA   . ALA B 1 176 ? 0.48041   -19.21552 21.03706 1.000 27.00472  ? 162 ALA B CA   1 
ATOM   6060 C C    . ALA B 1 176 ? -0.92361  -18.73158 21.36206 1.000 31.23183  ? 162 ALA B C    1 
ATOM   6061 O O    . ALA B 1 176 ? -1.52029  -19.12622 22.36812 1.000 26.46449  ? 162 ALA B O    1 
ATOM   6062 C CB   . ALA B 1 176 ? 0.42657   -20.43355 20.10729 1.000 29.65910  ? 162 ALA B CB   1 
ATOM   6063 H H    . ALA B 1 176 ? 0.68890   -19.82718 22.89911 1.000 34.20268  ? 162 ALA B H    1 
ATOM   6064 H HA   . ALA B 1 176 ? 0.94071   -18.50078 20.56997 1.000 32.46160  ? 162 ALA B HA   1 
ATOM   6065 H HB1  . ALA B 1 176 ? 1.26330   -20.49660 19.62066 1.000 35.64687  ? 162 ALA B HB1  1 
ATOM   6066 H HB2  . ALA B 1 176 ? 0.29325   -21.23253 20.64092 1.000 35.64687  ? 162 ALA B HB2  1 
ATOM   6067 H HB3  . ALA B 1 176 ? -0.31009  -20.32412 19.48580 1.000 35.64687  ? 162 ALA B HB3  1 
ATOM   6068 N N    . ASN B 1 177 ? -1.44139  -17.87583 20.48304 1.000 34.79495  ? 163 ASN B N    1 
ATOM   6069 C CA   . ASN B 1 177 ? -2.72258  -17.20878 20.66924 1.000 32.40360  ? 163 ASN B CA   1 
ATOM   6070 C C    . ASN B 1 177 ? -3.37746  -17.05803 19.30443 1.000 31.05822  ? 163 ASN B C    1 
ATOM   6071 O O    . ASN B 1 177 ? -2.72593  -16.61331 18.35558 1.000 35.11657  ? 163 ASN B O    1 
ATOM   6072 C CB   . ASN B 1 177 ? -2.52854  -15.83603 21.32715 1.000 37.47940  ? 163 ASN B CB   1 
ATOM   6073 C CG   . ASN B 1 177 ? -3.81284  -15.03670 21.40792 1.000 40.53319  ? 163 ASN B CG   1 
ATOM   6074 O OD1  . ASN B 1 177 ? -4.31797  -14.53996 20.39958 1.000 32.35663  ? 163 ASN B OD1  1 
ATOM   6075 N ND2  . ASN B 1 177 ? -4.34064  -14.89360 22.61667 1.000 58.05711  ? 163 ASN B ND2  1 
ATOM   6076 H H    . ASN B 1 177 ? -1.05481  -17.65893 19.74608 1.000 41.80988  ? 163 ASN B H    1 
ATOM   6077 H HA   . ASN B 1 177 ? -3.30284  -17.73989 21.23680 1.000 38.94026  ? 163 ASN B HA   1 
ATOM   6078 H HB2  . ASN B 1 177 ? -2.19690  -15.96242 22.22989 1.000 45.03122  ? 163 ASN B HB2  1 
ATOM   6079 H HB3  . ASN B 1 177 ? -1.88914  -15.32419 20.80744 1.000 45.03122  ? 163 ASN B HB3  1 
ATOM   6080 H HD21 . ASN B 1 177 ? -5.06960  -14.44860 22.71765 1.000 69.72447  ? 163 ASN B HD21 1 
ATOM   6081 H HD22 . ASN B 1 177 ? -3.95382  -15.24583 23.29924 1.000 69.72447  ? 163 ASN B HD22 1 
ATOM   6082 N N    . PHE B 1 178 ? -4.65111  -17.42878 19.20265 1.000 29.57411  ? 164 PHE B N    1 
ATOM   6083 C CA   . PHE B 1 178 ? -5.37337  -17.29299 17.94335 1.000 31.31206  ? 164 PHE B CA   1 
ATOM   6084 C C    . PHE B 1 178 ? -6.84762  -17.57578 18.18174 1.000 30.63456  ? 164 PHE B C    1 
ATOM   6085 O O    . PHE B 1 178 ? -7.22046  -18.28407 19.12109 1.000 33.19416  ? 164 PHE B O    1 
ATOM   6086 C CB   . PHE B 1 178 ? -4.81788  -18.23094 16.86527 1.000 30.63201  ? 164 PHE B CB   1 
ATOM   6087 C CG   . PHE B 1 178 ? -4.84611  -19.68319 17.24767 1.000 28.47393  ? 164 PHE B CG   1 
ATOM   6088 C CD1  . PHE B 1 178 ? -3.82862  -20.23061 18.00804 1.000 28.16001  ? 164 PHE B CD1  1 
ATOM   6089 C CD2  . PHE B 1 178 ? -5.88391  -20.50346 16.83832 1.000 29.23326  ? 164 PHE B CD2  1 
ATOM   6090 C CE1  . PHE B 1 178 ? -3.84627  -21.56622 18.35710 1.000 31.69706  ? 164 PHE B CE1  1 
ATOM   6091 C CE2  . PHE B 1 178 ? -5.90716  -21.84119 17.18687 1.000 28.39745  ? 164 PHE B CE2  1 
ATOM   6092 C CZ   . PHE B 1 178 ? -4.88703  -22.37232 17.94594 1.000 24.48199  ? 164 PHE B CZ   1 
ATOM   6093 H H    . PHE B 1 178 ? -5.11587  -17.76003 19.84597 1.000 35.54487  ? 164 PHE B H    1 
ATOM   6094 H HA   . PHE B 1 178 ? -5.28871  -16.37837 17.63157 1.000 37.63041  ? 164 PHE B HA   1 
ATOM   6095 H HB2  . PHE B 1 178 ? -5.34791  -18.12739 16.05951 1.000 36.81435  ? 164 PHE B HB2  1 
ATOM   6096 H HB3  . PHE B 1 178 ? -3.89504  -17.99000 16.68857 1.000 36.81435  ? 164 PHE B HB3  1 
ATOM   6097 H HD1  . PHE B 1 178 ? -3.12374  -19.69223 18.28767 1.000 33.84795  ? 164 PHE B HD1  1 
ATOM   6098 H HD2  . PHE B 1 178 ? -6.57306  -20.15056 16.32311 1.000 35.13586  ? 164 PHE B HD2  1 
ATOM   6099 H HE1  . PHE B 1 178 ? -3.15654  -21.92226 18.86935 1.000 38.09242  ? 164 PHE B HE1  1 
ATOM   6100 H HE2  . PHE B 1 178 ? -6.61080  -22.38221 16.90922 1.000 34.13287  ? 164 PHE B HE2  1 
ATOM   6101 H HZ   . PHE B 1 178 ? -4.90036  -23.27218 18.18039 1.000 29.43432  ? 164 PHE B HZ   1 
ATOM   6102 N N    . LYS B 1 179 ? -7.67809  -17.01219 17.31080 1.000 31.24531  ? 165 LYS B N    1 
ATOM   6103 C CA   . LYS B 1 179 ? -9.12178  -17.17264 17.36371 1.000 35.41413  ? 165 LYS B CA   1 
ATOM   6104 C C    . LYS B 1 179 ? -9.58703  -18.10754 16.25492 1.000 30.55655  ? 165 LYS B C    1 
ATOM   6105 O O    . LYS B 1 179 ? -9.01518  -18.13492 15.16167 1.000 32.71230  ? 165 LYS B O    1 
ATOM   6106 C CB   . LYS B 1 179 ? -9.82946  -15.82023 17.22249 1.000 38.55633  ? 165 LYS B CB   1 
ATOM   6107 C CG   . LYS B 1 179 ? -9.63299  -14.87844 18.40009 1.000 33.33234  ? 165 LYS B CG   1 
ATOM   6108 C CD   . LYS B 1 179 ? -10.22374 -13.50760 18.10967 1.000 37.21772  ? 165 LYS B CD   1 
ATOM   6109 C CE   . LYS B 1 179 ? -10.26291 -12.63031 19.35349 1.000 31.90176  ? 165 LYS B CE   1 
ATOM   6110 N NZ   . LYS B 1 179 ? -10.66514 -11.23599 19.02252 1.000 38.91626  ? 165 LYS B NZ   1 
ATOM   6111 H H    . LYS B 1 179 ? -7.41730  -16.51573 16.65880 1.000 37.55032  ? 165 LYS B H    1 
ATOM   6112 H HA   . LYS B 1 179 ? -9.37080  -17.56215 18.21645 1.000 42.55290  ? 165 LYS B HA   1 
ATOM   6113 H HB2  . LYS B 1 179 ? -9.48865  -15.37459 16.43118 1.000 46.32354  ? 165 LYS B HB2  1 
ATOM   6114 H HB3  . LYS B 1 179 ? -10.78198 -15.97840 17.12985 1.000 46.32354  ? 165 LYS B HB3  1 
ATOM   6115 H HG2  . LYS B 1 179 ? -10.07533 -15.24329 19.18248 1.000 40.05475  ? 165 LYS B HG2  1 
ATOM   6116 H HG3  . LYS B 1 179 ? -8.68461  -14.77284 18.57421 1.000 40.05475  ? 165 LYS B HG3  1 
ATOM   6117 H HD2  . LYS B 1 179 ? -9.68150  -13.06100 17.44077 1.000 44.71720  ? 165 LYS B HD2  1 
ATOM   6118 H HD3  . LYS B 1 179 ? -11.13150 -13.61305 17.78448 1.000 44.71720  ? 165 LYS B HD3  1 
ATOM   6119 H HE2  . LYS B 1 179 ? -10.90643 -12.99271 19.98234 1.000 38.33805  ? 165 LYS B HE2  1 
ATOM   6120 H HE3  . LYS B 1 179 ? -9.38147  -12.60612 19.75770 1.000 38.33805  ? 165 LYS B HE3  1 
ATOM   6121 H HZ1  . LYS B 1 179 ? -11.47961 -11.23116 18.66376 1.000 46.75545  ? 165 LYS B HZ1  1 
ATOM   6122 H HZ2  . LYS B 1 179 ? -10.67141 -10.73780 19.75999 1.000 46.75545  ? 165 LYS B HZ2  1 
ATOM   6123 H HZ3  . LYS B 1 179 ? -10.09117 -10.88356 18.44075 1.000 46.75545  ? 165 LYS B HZ3  1 
ATOM   6124 N N    . ILE B 1 180 ? -10.63072 -18.87770 16.55275 1.000 30.08361  ? 166 ILE B N    1 
ATOM   6125 C CA   . ILE B 1 180 ? -11.30278 -19.72867 15.57952 1.000 35.69135  ? 166 ILE B CA   1 
ATOM   6126 C C    . ILE B 1 180 ? -12.74972 -19.26989 15.47209 1.000 34.54459  ? 166 ILE B C    1 
ATOM   6127 O O    . ILE B 1 180 ? -13.37721 -18.92913 16.48128 1.000 33.83874  ? 166 ILE B O    1 
ATOM   6128 C CB   . ILE B 1 180 ? -11.23318 -21.21849 15.97283 1.000 40.55235  ? 166 ILE B CB   1 
ATOM   6129 C CG1  . ILE B 1 180 ? -9.77793  -21.67715 16.09266 1.000 36.54560  ? 166 ILE B CG1  1 
ATOM   6130 C CG2  . ILE B 1 180 ? -11.99032 -22.07212 14.96277 1.000 35.47695  ? 166 ILE B CG2  1 
ATOM   6131 C CD1  . ILE B 1 180 ? -8.97437  -21.51978 14.82791 1.000 34.04002  ? 166 ILE B CD1  1 
ATOM   6132 H H    . ILE B 1 180 ? -10.97735 -18.92420 17.33842 1.000 36.15627  ? 166 ILE B H    1 
ATOM   6133 H HA   . ILE B 1 180 ? -10.87551 -19.62750 14.71459 1.000 42.88556  ? 166 ILE B HA   1 
ATOM   6134 H HB   . ILE B 1 180 ? -11.65483 -21.32486 16.83989 1.000 48.71876  ? 166 ILE B HB   1 
ATOM   6135 H HG12 . ILE B 1 180 ? -9.34366  -21.15350 16.78411 1.000 43.91066  ? 166 ILE B HG12 1 
ATOM   6136 H HG13 . ILE B 1 180 ? -9.76773  -22.61696 16.33258 1.000 43.91066  ? 166 ILE B HG13 1 
ATOM   6137 H HG21 . ILE B 1 180 ? -12.94316 -21.95372 15.10051 1.000 42.62828  ? 166 ILE B HG21 1 
ATOM   6138 H HG22 . ILE B 1 180 ? -11.74811 -21.79046 14.06672 1.000 42.62828  ? 166 ILE B HG22 1 
ATOM   6139 H HG23 . ILE B 1 180 ? -11.75040 -23.00290 15.09311 1.000 42.62828  ? 166 ILE B HG23 1 
ATOM   6140 H HD11 . ILE B 1 180 ? -9.46300  -21.91958 14.09150 1.000 40.90397  ? 166 ILE B HD11 1 
ATOM   6141 H HD12 . ILE B 1 180 ? -8.83467  -20.57504 14.65801 1.000 40.90397  ? 166 ILE B HD12 1 
ATOM   6142 H HD13 . ILE B 1 180 ? -8.12016  -21.96575 14.93893 1.000 40.90397  ? 166 ILE B HD13 1 
ATOM   6143 N N    . ARG B 1 181 ? -13.27903 -19.27124 14.25078 1.000 31.83636  ? 167 ARG B N    1 
ATOM   6144 C CA   . ARG B 1 181 ? -14.61368 -18.75249 13.95211 1.000 39.24614  ? 167 ARG B CA   1 
ATOM   6145 C C    . ARG B 1 181 ? -15.43319 -19.85534 13.28758 1.000 34.06193  ? 167 ARG B C    1 
ATOM   6146 O O    . ARG B 1 181 ? -15.43015 -19.99447 12.06255 1.000 41.14348  ? 167 ARG B O    1 
ATOM   6147 C CB   . ARG B 1 181 ? -14.51615 -17.51217 13.06104 1.000 43.50427  ? 167 ARG B CB   1 
ATOM   6148 C CG   . ARG B 1 181 ? -13.69185 -16.39281 13.67106 1.000 40.16650  ? 167 ARG B CG   1 
ATOM   6149 C CD   . ARG B 1 181 ? -13.10283 -15.47966 12.61423 1.000 45.55573  ? 167 ARG B CD   1 
ATOM   6150 N NE   . ARG B 1 181 ? -12.11203 -14.57758 13.18886 1.000 50.60498  ? 167 ARG B NE   1 
ATOM   6151 C CZ   . ARG B 1 181 ? -12.40591 -13.52278 13.93611 1.000 42.04208  ? 167 ARG B CZ   1 
ATOM   6152 N NH1  . ARG B 1 181 ? -13.65821 -13.20604 14.22261 1.000 48.31161  ? 167 ARG B NH1  1 
ATOM   6153 N NH2  . ARG B 1 181 ? -11.41878 -12.77004 14.41200 1.000 44.56745  ? 167 ARG B NH2  1 
ATOM   6154 H H    . ARG B 1 181 ? -12.87183 -19.57678 13.55764 1.000 38.25958  ? 167 ARG B H    1 
ATOM   6155 H HA   . ARG B 1 181 ? -15.05426 -18.51732 14.78367 1.000 47.15131  ? 167 ARG B HA   1 
ATOM   6156 H HB2  . ARG B 1 181 ? -14.10177 -17.76254 12.22050 1.000 52.26107  ? 167 ARG B HB2  1 
ATOM   6157 H HB3  . ARG B 1 181 ? -15.40983 -17.17042 12.90152 1.000 52.26107  ? 167 ARG B HB3  1 
ATOM   6158 H HG2  . ARG B 1 181 ? -14.25751 -15.85922 14.25089 1.000 48.25573  ? 167 ARG B HG2  1 
ATOM   6159 H HG3  . ARG B 1 181 ? -12.96124 -16.77588 14.18132 1.000 48.25573  ? 167 ARG B HG3  1 
ATOM   6160 H HD2  . ARG B 1 181 ? -12.66981 -16.01498 11.93098 1.000 54.72282  ? 167 ARG B HD2  1 
ATOM   6161 H HD3  . ARG B 1 181 ? -13.80999 -14.94614 12.21904 1.000 54.72282  ? 167 ARG B HD3  1 
ATOM   6162 H HE   . ARG B 1 181 ? -11.28216 -14.74052 13.03274 1.000 60.78192  ? 167 ARG B HE   1 
ATOM   6163 H HH11 . ARG B 1 181 ? -14.30338 -13.68885 13.92218 1.000 58.02987  ? 167 ARG B HH11 1 
ATOM   6164 H HH12 . ARG B 1 181 ? -13.82701 -12.51736 14.70926 1.000 58.02987  ? 167 ARG B HH12 1 
ATOM   6165 H HH21 . ARG B 1 181 ? -10.60148 -12.96982 14.23396 1.000 53.53689  ? 167 ARG B HH21 1 
ATOM   6166 H HH22 . ARG B 1 181 ? -11.59755 -12.08334 14.89788 1.000 53.53689  ? 167 ARG B HH22 1 
ATOM   6167 N N    . HIS B 1 182 ? -16.14481 -20.63124 14.10103 1.000 35.18276  ? 168 HIS B N    1 
ATOM   6168 C CA   . HIS B 1 182 ? -16.96852 -21.71816 13.59033 1.000 32.08570  ? 168 HIS B CA   1 
ATOM   6169 C C    . HIS B 1 182 ? -18.28672 -21.17354 13.05561 1.000 31.63232  ? 168 HIS B C    1 
ATOM   6170 O O    . HIS B 1 182 ? -19.01685 -20.48073 13.77006 1.000 35.66767  ? 168 HIS B O    1 
ATOM   6171 C CB   . HIS B 1 182 ? -17.23770 -22.74491 14.68949 1.000 34.10706  ? 168 HIS B CB   1 
ATOM   6172 C CG   . HIS B 1 182 ? -16.00168 -23.39247 15.23015 1.000 30.05472  ? 168 HIS B CG   1 
ATOM   6173 N ND1  . HIS B 1 182 ? -15.18341 -24.19131 14.46109 1.000 33.49989  ? 168 HIS B ND1  1 
ATOM   6174 C CD2  . HIS B 1 182 ? -15.44971 -23.36782 16.46611 1.000 31.22154  ? 168 HIS B CD2  1 
ATOM   6175 C CE1  . HIS B 1 182 ? -14.17685 -24.62526 15.19825 1.000 32.60461  ? 168 HIS B CE1  1 
ATOM   6176 N NE2  . HIS B 1 182 ? -14.31516 -24.14057 16.41895 1.000 32.92793  ? 168 HIS B NE2  1 
ATOM   6177 H H    . HIS B 1 182 ? -16.16655 -20.54694 14.95661 1.000 42.27526  ? 168 HIS B H    1 
ATOM   6178 H HA   . HIS B 1 182 ? -16.49943 -22.15875 12.86456 1.000 38.55878  ? 168 HIS B HA   1 
ATOM   6179 H HB2  . HIS B 1 182 ? -17.68559 -22.30147 15.42682 1.000 40.98442  ? 168 HIS B HB2  1 
ATOM   6180 H HB3  . HIS B 1 182 ? -17.80467 -23.44485 14.32959 1.000 40.98442  ? 168 HIS B HB3  1 
ATOM   6181 H HD2  . HIS B 1 182 ? -15.77736 -22.91286 17.20810 1.000 37.52178  ? 168 HIS B HD2  1 
ATOM   6182 H HE1  . HIS B 1 182 ? -13.48797 -25.17807 14.90716 1.000 39.18147  ? 168 HIS B HE1  1 
ATOM   6183 H HE2  . HIS B 1 182 ? -13.78140 -24.28532 17.07754 1.000 39.56945  ? 168 HIS B HE2  1 
ATOM   6184 N N    . ASN B 1 183 ? -18.59507 -21.49273 11.80216 1.000 31.22216  ? 169 ASN B N    1 
ATOM   6185 C CA   . ASN B 1 183 ? -19.86667 -21.07938 11.22779 1.000 35.89380  ? 169 ASN B CA   1 
ATOM   6186 C C    . ASN B 1 183 ? -21.01945 -21.78582 11.92912 1.000 38.16820  ? 169 ASN B C    1 
ATOM   6187 O O    . ASN B 1 183 ? -20.93732 -22.97340 12.25734 1.000 34.71449  ? 169 ASN B O    1 
ATOM   6188 C CB   . ASN B 1 183 ? -19.90536 -21.38104 9.73010  1.000 38.32638  ? 169 ASN B CB   1 
ATOM   6189 C CG   . ASN B 1 183 ? -19.03014 -20.44283 8.92358  1.000 42.51591  ? 169 ASN B CG   1 
ATOM   6190 O OD1  . ASN B 1 183 ? -18.58074 -19.41164 9.42259  1.000 38.87815  ? 169 ASN B OD1  1 
ATOM   6191 N ND2  . ASN B 1 183 ? -18.79040 -20.79279 7.66554  1.000 42.82602  ? 169 ASN B ND2  1 
ATOM   6192 H H    . ASN B 1 183 ? -18.09034 -21.94266 11.27074 1.000 37.52253  ? 169 ASN B H    1 
ATOM   6193 H HA   . ASN B 1 183 ? -19.97296 -20.12221 11.34367 1.000 43.12850  ? 169 ASN B HA   1 
ATOM   6194 H HB2  . ASN B 1 183 ? -19.59176 -22.28682 9.58137  1.000 46.04760  ? 169 ASN B HB2  1 
ATOM   6195 H HB3  . ASN B 1 183 ? -20.81714 -21.28923 9.41210  1.000 46.04760  ? 169 ASN B HB3  1 
ATOM   6196 H HD21 . ASN B 1 183 ? -18.29926 -20.29350 7.16646  1.000 51.44716  ? 169 ASN B HD21 1 
ATOM   6197 H HD22 . ASN B 1 183 ? -19.12625 -21.51877 7.34971  1.000 51.44716  ? 169 ASN B HD22 1 
ATOM   6198 N N    . ILE B 1 184 ? -22.09648 -21.04398 12.16171 1.000 33.22666  ? 170 ILE B N    1 
ATOM   6199 C CA   . ILE B 1 184 ? -23.31659 -21.57912 12.75314 1.000 35.37657  ? 170 ILE B CA   1 
ATOM   6200 C C    . ILE B 1 184 ? -24.29675 -21.88739 11.63211 1.000 42.11204  ? 170 ILE B C    1 
ATOM   6201 O O    . ILE B 1 184 ? -24.47204 -21.08539 10.70537 1.000 41.04777  ? 170 ILE B O    1 
ATOM   6202 C CB   . ILE B 1 184 ? -23.91947 -20.59149 13.76910 1.000 38.39858  ? 170 ILE B CB   1 
ATOM   6203 C CG1  . ILE B 1 184 ? -22.96451 -20.40215 14.95002 1.000 33.80167  ? 170 ILE B CG1  1 
ATOM   6204 C CG2  . ILE B 1 184 ? -25.27057 -21.08735 14.25397 1.000 42.96255  ? 170 ILE B CG2  1 
ATOM   6205 C CD1  . ILE B 1 184 ? -23.21296 -19.12786 15.74229 1.000 38.57896  ? 170 ILE B CD1  1 
ATOM   6206 H H    . ILE B 1 184 ? -22.14548 -20.20477 11.98025 1.000 39.86673  ? 170 ILE B H    1 
ATOM   6207 H HA   . ILE B 1 184 ? -23.11620 -22.40411 13.22232 1.000 42.50782  ? 170 ILE B HA   1 
ATOM   6208 H HB   . ILE B 1 184 ? -24.04513 -19.73594 13.32961 1.000 46.13424  ? 170 ILE B HB   1 
ATOM   6209 H HG12 . ILE B 1 184 ? -23.06635 -21.15223 15.55658 1.000 40.61794  ? 170 ILE B HG12 1 
ATOM   6210 H HG13 . ILE B 1 184 ? -22.05539 -20.36874 14.61344 1.000 40.61794  ? 170 ILE B HG13 1 
ATOM   6211 H HG21 . ILE B 1 184 ? -25.22574 -22.04721 14.38641 1.000 51.61100  ? 170 ILE B HG21 1 
ATOM   6212 H HG22 . ILE B 1 184 ? -25.48646 -20.64764 15.09119 1.000 51.61100  ? 170 ILE B HG22 1 
ATOM   6213 H HG23 . ILE B 1 184 ? -25.94235 -20.87651 13.58677 1.000 51.61100  ? 170 ILE B HG23 1 
ATOM   6214 H HD11 . ILE B 1 184 ? -23.07474 -18.36309 15.16183 1.000 46.35070  ? 170 ILE B HD11 1 
ATOM   6215 H HD12 . ILE B 1 184 ? -24.12563 -19.13311 16.07078 1.000 46.35070  ? 170 ILE B HD12 1 
ATOM   6216 H HD13 . ILE B 1 184 ? -22.59329 -19.09359 16.48776 1.000 46.35070  ? 170 ILE B HD13 1 
ATOM   6217 N N    . GLU B 1 185 ? -24.93837 -23.05546 11.71642 1.000 46.12320  ? 171 GLU B N    1 
ATOM   6218 C CA   . GLU B 1 185 ? -25.79749 -23.52165 10.63181 1.000 58.83304  ? 171 GLU B CA   1 
ATOM   6219 C C    . GLU B 1 185 ? -26.82516 -22.46556 10.24004 1.000 59.32515  ? 171 GLU B C    1 
ATOM   6220 O O    . GLU B 1 185 ? -26.95215 -22.11246 9.06237  1.000 60.97558  ? 171 GLU B O    1 
ATOM   6221 C CB   . GLU B 1 185 ? -26.48947 -24.82296 11.04347 1.000 57.94161  ? 171 GLU B CB   1 
ATOM   6222 C CG   . GLU B 1 185 ? -25.54030 -25.99814 11.24397 1.000 61.43949  ? 171 GLU B CG   1 
ATOM   6223 C CD   . GLU B 1 185 ? -25.49773 -26.93868 10.04976 1.000 74.05411  ? 171 GLU B CD   1 
ATOM   6224 O OE1  . GLU B 1 185 ? -25.77613 -26.48812 8.91812  1.000 73.87921  ? 171 GLU B OE1  1 
ATOM   6225 O OE2  . GLU B 1 185 ? -25.18954 -28.13421 10.24604 1.000 72.58390  ? 171 GLU B OE2  1 
ATOM   6226 H H    . GLU B 1 185 ? -24.89235 -23.59198 12.38697 1.000 55.40378  ? 171 GLU B H    1 
ATOM   6227 H HA   . GLU B 1 185 ? -25.24734 -23.70156 9.85344  1.000 70.65559  ? 171 GLU B HA   1 
ATOM   6228 H HB2  . GLU B 1 185 ? -26.95561 -24.67484 11.88113 1.000 69.58588  ? 171 GLU B HB2  1 
ATOM   6229 H HB3  . GLU B 1 185 ? -27.12208 -25.07035 10.35101 1.000 69.58588  ? 171 GLU B HB3  1 
ATOM   6230 H HG2  . GLU B 1 185 ? -24.64353 -25.65776 11.38837 1.000 73.78332  ? 171 GLU B HG2  1 
ATOM   6231 H HG3  . GLU B 1 185 ? -25.82973 -26.50870 12.01627 1.000 73.78332  ? 171 GLU B HG3  1 
ATOM   6232 N N    . ASP B 1 186 ? -27.57073 -21.94766 11.21758 1.000 67.03561  ? 172 ASP B N    1 
ATOM   6233 C CA   . ASP B 1 186 ? -28.58040 -20.93645 10.92802 1.000 77.86422  ? 172 ASP B CA   1 
ATOM   6234 C C    . ASP B 1 186 ? -27.97954 -19.59820 10.52072 1.000 70.85598  ? 172 ASP B C    1 
ATOM   6235 O O    . ASP B 1 186 ? -28.71247 -18.73937 10.01832 1.000 69.42291  ? 172 ASP B O    1 
ATOM   6236 C CB   . ASP B 1 186 ? -29.48519 -20.73372 12.14438 1.000 84.95534  ? 172 ASP B CB   1 
ATOM   6237 C CG   . ASP B 1 186 ? -30.28844 -21.97212 12.48579 1.000 93.59679  ? 172 ASP B CG   1 
ATOM   6238 O OD1  . ASP B 1 186 ? -29.98015 -23.05195 11.93902 1.000 91.62298  ? 172 ASP B OD1  1 
ATOM   6239 O OD2  . ASP B 1 186 ? -31.23291 -21.86403 13.29604 1.000 97.38029  ? 172 ASP B OD2  1 
ATOM   6240 H H    . ASP B 1 186 ? -27.51009 -22.16448 12.04758 1.000 80.49867  ? 172 ASP B H    1 
ATOM   6241 H HA   . ASP B 1 186 ? -29.12703 -21.25543 10.19294 1.000 93.49301  ? 172 ASP B HA   1 
ATOM   6242 H HB2  . ASP B 1 186 ? -28.93725 -20.50960 12.91278 1.000 102.00234 ? 172 ASP B HB2  1 
ATOM   6243 H HB3  . ASP B 1 186 ? -30.10775 -20.01323 11.95937 1.000 102.00234 ? 172 ASP B HB3  1 
ATOM   6244 N N    . GLY B 1 187 ? -26.67906 -19.40208 10.71949 1.000 58.79452  ? 173 GLY B N    1 
ATOM   6245 C CA   . GLY B 1 187 ? -26.04747 -18.13085 10.43191 1.000 50.52635  ? 173 GLY B CA   1 
ATOM   6246 C C    . GLY B 1 187 ? -25.34202 -17.57514 11.65022 1.000 48.69782  ? 173 GLY B C    1 
ATOM   6247 O O    . GLY B 1 187 ? -25.74327 -17.85225 12.78464 1.000 51.86211  ? 173 GLY B O    1 
ATOM   6248 H H    . GLY B 1 187 ? -26.13966 -19.99895 11.02347 1.000 70.60936  ? 173 GLY B H    1 
ATOM   6249 H HA2  . GLY B 1 187 ? -25.39633 -18.24522 9.72210  1.000 60.68756  ? 173 GLY B HA2  1 
ATOM   6250 H HA3  . GLY B 1 187 ? -26.71896 -17.49252 10.14463 1.000 60.68756  ? 173 GLY B HA3  1 
ATOM   6251 N N    . GLY B 1 188 ? -24.29697 -16.78520 11.43110 1.000 49.03974  ? 174 GLY B N    1 
ATOM   6252 C CA   . GLY B 1 188 ? -23.45787 -16.29870 12.50863 1.000 46.97539  ? 174 GLY B CA   1 
ATOM   6253 C C    . GLY B 1 188 ? -22.21862 -17.15506 12.67588 1.000 42.63877  ? 174 GLY B C    1 
ATOM   6254 O O    . GLY B 1 188 ? -21.98129 -18.12523 11.94953 1.000 39.57678  ? 174 GLY B O    1 
ATOM   6255 H H    . GLY B 1 188 ? -24.05256 -16.51467 10.65220 1.000 58.90362  ? 174 GLY B H    1 
ATOM   6256 H HA2  . GLY B 1 188 ? -23.18181 -15.38823 12.31958 1.000 56.42641  ? 174 GLY B HA2  1 
ATOM   6257 H HA3  . GLY B 1 188 ? -23.95726 -16.31109 13.34010 1.000 56.42641  ? 174 GLY B HA3  1 
ATOM   6258 N N    . VAL B 1 189 ? -21.41338 -16.77847 13.66516 1.000 39.84088  ? 175 VAL B N    1 
ATOM   6259 C CA   . VAL B 1 189 ? -20.15378 -17.45170 13.95026 1.000 37.00550  ? 175 VAL B CA   1 
ATOM   6260 C C    . VAL B 1 189 ? -20.04492 -17.69043 15.44801 1.000 39.79782  ? 175 VAL B C    1 
ATOM   6261 O O    . VAL B 1 189 ? -20.45059 -16.84583 16.25468 1.000 33.13413  ? 175 VAL B O    1 
ATOM   6262 C CB   . VAL B 1 189 ? -18.94187 -16.63831 13.44881 1.000 37.99446  ? 175 VAL B CB   1 
ATOM   6263 C CG1  . VAL B 1 189 ? -19.00315 -16.47199 11.93813 1.000 45.46633  ? 175 VAL B CG1  1 
ATOM   6264 C CG2  . VAL B 1 189 ? -18.88365 -15.28461 14.14074 1.000 48.55655  ? 175 VAL B CG2  1 
ATOM   6265 H H    . VAL B 1 189 ? -21.58042 -16.12180 14.19477 1.000 47.86500  ? 175 VAL B H    1 
ATOM   6266 H HA   . VAL B 1 189 ? -20.15409 -18.31277 13.50366 1.000 44.46254  ? 175 VAL B HA   1 
ATOM   6267 H HB   . VAL B 1 189 ? -18.12797 -17.11935 13.66574 1.000 45.64929  ? 175 VAL B HB   1 
ATOM   6268 H HG11 . VAL B 1 189 ? -19.53381 -17.19182 11.56244 1.000 54.61554  ? 175 VAL B HG11 1 
ATOM   6269 H HG12 . VAL B 1 189 ? -19.41163 -15.61695 11.73087 1.000 54.61554  ? 175 VAL B HG12 1 
ATOM   6270 H HG13 . VAL B 1 189 ? -18.10219 -16.50360 11.58014 1.000 54.61554  ? 175 VAL B HG13 1 
ATOM   6271 H HG21 . VAL B 1 189 ? -19.78803 -14.97409 14.30371 1.000 58.32380  ? 175 VAL B HG21 1 
ATOM   6272 H HG22 . VAL B 1 189 ? -18.41005 -15.38000 14.98187 1.000 58.32380  ? 175 VAL B HG22 1 
ATOM   6273 H HG23 . VAL B 1 189 ? -18.41660 -14.65678 13.56751 1.000 58.32380  ? 175 VAL B HG23 1 
ATOM   6274 N N    . GLN B 1 190 ? -19.49587 -18.84844 15.81318 1.000 34.04205  ? 176 GLN B N    1 
ATOM   6275 C CA   . GLN B 1 190 ? -19.18857 -19.19071 17.19720 1.000 30.53395  ? 176 GLN B CA   1 
ATOM   6276 C C    . GLN B 1 190 ? -17.69362 -18.97956 17.40631 1.000 31.90390  ? 176 GLN B C    1 
ATOM   6277 O O    . GLN B 1 190 ? -16.87200 -19.71220 16.84566 1.000 32.10266  ? 176 GLN B O    1 
ATOM   6278 C CB   . GLN B 1 190 ? -19.59036 -20.63179 17.50519 1.000 34.43486  ? 176 GLN B CB   1 
ATOM   6279 C CG   . GLN B 1 190 ? -19.14239 -21.13824 18.87294 1.000 36.82662  ? 176 GLN B CG   1 
ATOM   6280 C CD   . GLN B 1 190 ? -19.72114 -20.33143 20.01691 1.000 36.26153  ? 176 GLN B CD   1 
ATOM   6281 O OE1  . GLN B 1 190 ? -20.88093 -20.50539 20.39216 1.000 38.31316  ? 176 GLN B OE1  1 
ATOM   6282 N NE2  . GLN B 1 190 ? -18.91297 -19.44261 20.57943 1.000 32.42260  ? 176 GLN B NE2  1 
ATOM   6283 H H    . GLN B 1 190 ? -19.28635 -19.47055 15.25759 1.000 40.90640  ? 176 GLN B H    1 
ATOM   6284 H HA   . GLN B 1 190 ? -19.67834 -18.60751 17.79795 1.000 36.69669  ? 176 GLN B HA   1 
ATOM   6285 H HB2  . GLN B 1 190 ? -20.55766 -20.69609 17.47198 1.000 41.37777  ? 176 GLN B HB2  1 
ATOM   6286 H HB3  . GLN B 1 190 ? -19.19612 -21.21182 16.83508 1.000 41.37777  ? 176 GLN B HB3  1 
ATOM   6287 H HG2  . GLN B 1 190 ? -19.43091 -22.05823 18.97908 1.000 44.24788  ? 176 GLN B HG2  1 
ATOM   6288 H HG3  . GLN B 1 190 ? -18.17540 -21.08534 18.92811 1.000 44.24788  ? 176 GLN B HG3  1 
ATOM   6289 H HE21 . GLN B 1 190 ? -18.10827 -19.34976 20.29058 1.000 38.96306  ? 176 GLN B HE21 1 
ATOM   6290 H HE22 . GLN B 1 190 ? -19.19371 -18.95922 21.23296 1.000 38.96306  ? 176 GLN B HE22 1 
ATOM   6291 N N    . LEU B 1 191 ? -17.34410 -17.98007 18.20954 1.000 36.25201  ? 177 LEU B N    1 
ATOM   6292 C CA   . LEU B 1 191 ? -15.94680 -17.66027 18.45595 1.000 34.28844  ? 177 LEU B CA   1 
ATOM   6293 C C    . LEU B 1 191 ? -15.35645 -18.61514 19.48413 1.000 28.57442  ? 177 LEU B C    1 
ATOM   6294 O O    . LEU B 1 191 ? -15.99689 -18.94721 20.48513 1.000 31.03387  ? 177 LEU B O    1 
ATOM   6295 C CB   . LEU B 1 191 ? -15.80970 -16.21869 18.94342 1.000 29.60680  ? 177 LEU B CB   1 
ATOM   6296 C CG   . LEU B 1 191 ? -14.37821 -15.69199 19.04431 1.000 45.19728  ? 177 LEU B CG   1 
ATOM   6297 C CD1  . LEU B 1 191 ? -13.84711 -15.32882 17.66119 1.000 43.00369  ? 177 LEU B CD1  1 
ATOM   6298 C CD2  . LEU B 1 191 ? -14.30173 -14.49758 19.99660 1.000 45.57317  ? 177 LEU B CD2  1 
ATOM   6299 H H    . LEU B 1 191 ? -17.90019 -17.47169 18.62416 1.000 43.55835  ? 177 LEU B H    1 
ATOM   6300 H HA   . LEU B 1 191 ? -15.44400 -17.75130 17.63145 1.000 41.20207  ? 177 LEU B HA   1 
ATOM   6301 H HB2  . LEU B 1 191 ? -16.28748 -15.64208 18.32685 1.000 35.56050  ? 177 LEU B HB2  1 
ATOM   6302 H HB3  . LEU B 1 191 ? -16.20360 -16.15758 19.82773 1.000 35.56050  ? 177 LEU B HB3  1 
ATOM   6303 H HG   . LEU B 1 191 ? -13.80958 -16.38842 19.40839 1.000 54.29267  ? 177 LEU B HG   1 
ATOM   6304 H HD11 . LEU B 1 191 ? -12.87880 -15.28374 17.69654 1.000 51.66037  ? 177 LEU B HD11 1 
ATOM   6305 H HD12 . LEU B 1 191 ? -14.12365 -16.00959 17.02795 1.000 51.66037  ? 177 LEU B HD12 1 
ATOM   6306 H HD13 . LEU B 1 191 ? -14.20903 -14.46759 17.40005 1.000 51.66037  ? 177 LEU B HD13 1 
ATOM   6307 H HD21 . LEU B 1 191 ? -14.56792 -14.78392 20.88433 1.000 54.74374  ? 177 LEU B HD21 1 
ATOM   6308 H HD22 . LEU B 1 191 ? -13.39019 -14.16647 20.01531 1.000 54.74374  ? 177 LEU B HD22 1 
ATOM   6309 H HD23 . LEU B 1 191 ? -14.89971 -13.80251 19.68005 1.000 54.74374  ? 177 LEU B HD23 1 
ATOM   6310 N N    . ALA B 1 192 ? -14.12252 -19.05123 19.23022 1.000 32.35233  ? 178 ALA B N    1 
ATOM   6311 C CA   . ALA B 1 192 ? -13.40195 -19.96222 20.12100 1.000 33.79728  ? 178 ALA B CA   1 
ATOM   6312 C C    . ALA B 1 192 ? -11.97989 -19.42465 20.25030 1.000 32.92075  ? 178 ALA B C    1 
ATOM   6313 O O    . ALA B 1 192 ? -11.15772 -19.60163 19.34616 1.000 33.69734  ? 178 ALA B O    1 
ATOM   6314 C CB   . ALA B 1 192 ? -13.41388 -21.39219 19.59144 1.000 34.95943  ? 178 ALA B CB   1 
ATOM   6315 H H    . ALA B 1 192 ? -13.67133 -18.82874 18.53271 1.000 38.87873  ? 178 ALA B H    1 
ATOM   6316 H HA   . ALA B 1 192 ? -13.82126 -19.96442 20.99569 1.000 40.61267  ? 178 ALA B HA   1 
ATOM   6317 H HB1  . ALA B 1 192 ? -12.97551 -21.41226 18.72638 1.000 42.00725  ? 178 ALA B HB1  1 
ATOM   6318 H HB2  . ALA B 1 192 ? -12.94028 -21.96406 20.21560 1.000 42.00725  ? 178 ALA B HB2  1 
ATOM   6319 H HB3  . ALA B 1 192 ? -14.33325 -21.68867 19.50334 1.000 42.00725  ? 178 ALA B HB3  1 
ATOM   6320 N N    . ASP B 1 193 ? -11.69367 -18.77574 21.37469 1.000 38.15135  ? 179 ASP B N    1 
ATOM   6321 C CA   . ASP B 1 193 ? -10.41768 -18.10236 21.58261 1.000 37.72731  ? 179 ASP B CA   1 
ATOM   6322 C C    . ASP B 1 193 ? -9.42311  -19.08602 22.18714 1.000 33.50586  ? 179 ASP B C    1 
ATOM   6323 O O    . ASP B 1 193 ? -9.63834  -19.59221 23.29351 1.000 32.17945  ? 179 ASP B O    1 
ATOM   6324 C CB   . ASP B 1 193 ? -10.60329 -16.88253 22.48416 1.000 41.79597  ? 179 ASP B CB   1 
ATOM   6325 C CG   . ASP B 1 193 ? -11.50673 -15.82169 21.85640 1.000 48.03899  ? 179 ASP B CG   1 
ATOM   6326 O OD1  . ASP B 1 193 ? -11.77132 -15.90522 20.63967 1.000 50.13472  ? 179 ASP B OD1  1 
ATOM   6327 O OD2  . ASP B 1 193 ? -11.96552 -14.91155 22.57324 1.000 51.64368  ? 179 ASP B OD2  1 
ATOM   6328 H H    . ASP B 1 193 ? -12.23159 -18.71062 22.04253 1.000 45.83756  ? 179 ASP B H    1 
ATOM   6329 H HA   . ASP B 1 193 ? -10.06192 -17.80006 20.73234 1.000 45.32871  ? 179 ASP B HA   1 
ATOM   6330 H HB2  . ASP B 1 193 ? -11.00657 -17.16468 23.32002 1.000 50.21110  ? 179 ASP B HB2  1 
ATOM   6331 H HB3  . ASP B 1 193 ? -9.73768  -16.47871 22.65311 1.000 50.21110  ? 179 ASP B HB3  1 
ATOM   6332 N N    . HIS B 1 194 ? -8.33613  -19.34498 21.46371 1.000 30.89856  ? 180 HIS B N    1 
ATOM   6333 C CA   . HIS B 1 194 ? -7.36027  -20.36437 21.82474 1.000 31.35247  ? 180 HIS B CA   1 
ATOM   6334 C C    . HIS B 1 194 ? -6.16843  -19.72091 22.52172 1.000 31.56649  ? 180 HIS B C    1 
ATOM   6335 O O    . HIS B 1 194 ? -5.57602  -18.77285 21.99716 1.000 31.18430  ? 180 HIS B O    1 
ATOM   6336 C CB   . HIS B 1 194 ? -6.87682  -21.11847 20.58137 1.000 31.94284  ? 180 HIS B CB   1 
ATOM   6337 C CG   . HIS B 1 194 ? -7.87211  -22.08811 20.02057 1.000 30.65579  ? 180 HIS B CG   1 
ATOM   6338 N ND1  . HIS B 1 194 ? -9.14271  -21.71750 19.63638 1.000 30.93974  ? 180 HIS B ND1  1 
ATOM   6339 C CD2  . HIS B 1 194 ? -7.77025  -23.41242 19.75341 1.000 30.70676  ? 180 HIS B CD2  1 
ATOM   6340 C CE1  . HIS B 1 194 ? -9.78601  -22.77437 19.17174 1.000 34.02692  ? 180 HIS B CE1  1 
ATOM   6341 N NE2  . HIS B 1 194 ? -8.97481  -23.81529 19.22951 1.000 26.80054  ? 180 HIS B NE2  1 
ATOM   6342 H H    . HIS B 1 194 ? -8.13803  -18.92926 20.73739 1.000 37.13421  ? 180 HIS B H    1 
ATOM   6343 H HA   . HIS B 1 194 ? -7.77390  -20.99380 22.43599 1.000 37.67890  ? 180 HIS B HA   1 
ATOM   6344 H HB2  . HIS B 1 194 ? -6.67334  -20.47232 19.88712 1.000 38.38735  ? 180 HIS B HB2  1 
ATOM   6345 H HB3  . HIS B 1 194 ? -6.07869  -21.61848 20.81348 1.000 38.38735  ? 180 HIS B HB3  1 
ATOM   6346 H HD1  . HIS B 1 194 ? -9.46644  -20.92260 19.69054 1.000 37.18363  ? 180 HIS B HD1  1 
ATOM   6347 H HD2  . HIS B 1 194 ? -7.02425  -23.94867 19.89770 1.000 36.90406  ? 180 HIS B HD2  1 
ATOM   6348 H HE1  . HIS B 1 194 ? -10.66125 -22.78363 18.85745 1.000 40.88825  ? 180 HIS B HE1  1 
ATOM   6349 N N    . TYR B 1 195 ? -5.81568  -20.24408 23.69336 1.000 26.41650  ? 181 TYR B N    1 
ATOM   6350 C CA   . TYR B 1 195 ? -4.58809  -19.88391 24.39374 1.000 28.84040  ? 181 TYR B CA   1 
ATOM   6351 C C    . TYR B 1 195 ? -3.76443  -21.15373 24.55184 1.000 29.56014  ? 181 TYR B C    1 
ATOM   6352 O O    . TYR B 1 195 ? -4.25865  -22.15172 25.08511 1.000 32.78578  ? 181 TYR B O    1 
ATOM   6353 C CB   . TYR B 1 195 ? -4.89071  -19.24218 25.74868 1.000 32.10704  ? 181 TYR B CB   1 
ATOM   6354 C CG   . TYR B 1 195 ? -5.56713  -17.89277 25.63056 1.000 37.72535  ? 181 TYR B CG   1 
ATOM   6355 C CD1  . TYR B 1 195 ? -6.94995  -17.79098 25.56096 1.000 37.54517  ? 181 TYR B CD1  1 
ATOM   6356 C CD2  . TYR B 1 195 ? -4.82165  -16.72166 25.57817 1.000 41.76889  ? 181 TYR B CD2  1 
ATOM   6357 C CE1  . TYR B 1 195 ? -7.57292  -16.56002 25.44763 1.000 44.73770  ? 181 TYR B CE1  1 
ATOM   6358 C CE2  . TYR B 1 195 ? -5.43540  -15.48569 25.46619 1.000 44.01638  ? 181 TYR B CE2  1 
ATOM   6359 C CZ   . TYR B 1 195 ? -6.81007  -15.41089 25.40027 1.000 48.88777  ? 181 TYR B CZ   1 
ATOM   6360 O OH   . TYR B 1 195 ? -7.42073  -14.18264 25.28754 1.000 49.97760  ? 181 TYR B OH   1 
ATOM   6361 H H    . TYR B 1 195 ? -6.28673  -20.82764 24.11426 1.000 31.75574  ? 181 TYR B H    1 
ATOM   6362 H HA   . TYR B 1 195 ? -4.07757  -19.24061 23.87756 1.000 34.66442  ? 181 TYR B HA   1 
ATOM   6363 H HB2  . TYR B 1 195 ? -5.47923  -19.82843 26.24954 1.000 38.58439  ? 181 TYR B HB2  1 
ATOM   6364 H HB3  . TYR B 1 195 ? -4.05800  -19.11769 26.23034 1.000 38.58439  ? 181 TYR B HB3  1 
ATOM   6365 H HD1  . TYR B 1 195 ? -7.46690  -18.56348 25.59100 1.000 45.11014  ? 181 TYR B HD1  1 
ATOM   6366 H HD2  . TYR B 1 195 ? -3.89374  -16.76875 25.61905 1.000 50.17861  ? 181 TYR B HD2  1 
ATOM   6367 H HE1  . TYR B 1 195 ? -8.50040  -16.50765 25.40366 1.000 53.74119  ? 181 TYR B HE1  1 
ATOM   6368 H HE2  . TYR B 1 195 ? -4.92294  -14.71022 25.43562 1.000 52.87560  ? 181 TYR B HE2  1 
ATOM   6369 H HH   . TYR B 1 195 ? -6.84087  -13.57653 25.24277 1.000 60.02907  ? 181 TYR B HH   1 
ATOM   6370 N N    . GLN B 1 196 ? -2.52069  -21.12054 24.07895 1.000 31.47146  ? 182 GLN B N    1 
ATOM   6371 C CA   . GLN B 1 196 ? -1.71775  -22.32233 23.91235 1.000 26.23143  ? 182 GLN B CA   1 
ATOM   6372 C C    . GLN B 1 196 ? -0.35260  -22.14976 24.56067 1.000 29.84666  ? 182 GLN B C    1 
ATOM   6373 O O    . GLN B 1 196 ? 0.18958   -21.04403 24.63043 1.000 32.68114  ? 182 GLN B O    1 
ATOM   6374 C CB   . GLN B 1 196 ? -1.55856  -22.65772 22.41959 1.000 26.78176  ? 182 GLN B CB   1 
ATOM   6375 C CG   . GLN B 1 196 ? -0.56961  -23.76687 22.10609 1.000 28.45190  ? 182 GLN B CG   1 
ATOM   6376 C CD   . GLN B 1 196 ? -0.48384  -24.05961 20.61489 1.000 30.80743  ? 182 GLN B CD   1 
ATOM   6377 O OE1  . GLN B 1 196 ? -1.39209  -23.72816 19.85196 1.000 25.14567  ? 182 GLN B OE1  1 
ATOM   6378 N NE2  . GLN B 1 196 ? 0.61372   -24.67828 20.19467 1.000 24.60137  ? 182 GLN B NE2  1 
ATOM   6379 H H    . GLN B 1 196 ? -2.11546  -20.39920 23.84432 1.000 37.82169  ? 182 GLN B H    1 
ATOM   6380 H HA   . GLN B 1 196 ? -2.14807  -23.06753 24.36002 1.000 31.53366  ? 182 GLN B HA   1 
ATOM   6381 H HB2  . GLN B 1 196 ? -2.42205  -22.93343 22.07424 1.000 32.19406  ? 182 GLN B HB2  1 
ATOM   6382 H HB3  . GLN B 1 196 ? -1.25565  -21.86044 21.95754 1.000 32.19406  ? 182 GLN B HB3  1 
ATOM   6383 H HG2  . GLN B 1 196 ? 0.31186   -23.50295 22.41312 1.000 34.19822  ? 182 GLN B HG2  1 
ATOM   6384 H HG3  . GLN B 1 196 ? -0.84886  -24.57872 22.55755 1.000 34.19822  ? 182 GLN B HG3  1 
ATOM   6385 H HE21 . GLN B 1 196 ? 1.22898   -24.89146 20.75646 1.000 29.57758  ? 182 GLN B HE21 1 
ATOM   6386 H HE22 . GLN B 1 196 ? 0.70915   -24.86569 19.36078 1.000 29.57758  ? 182 GLN B HE22 1 
ATOM   6387 N N    . GLN B 1 197 ? 0.19821   -23.26673 25.03178 1.000 29.44761  ? 183 GLN B N    1 
ATOM   6388 C CA   . GLN B 1 197 ? 1.52011   -23.29015 25.63844 1.000 26.06467  ? 183 GLN B CA   1 
ATOM   6389 C C    . GLN B 1 197 ? 2.15901   -24.63733 25.33366 1.000 32.19849  ? 183 GLN B C    1 
ATOM   6390 O O    . GLN B 1 197 ? 1.49634   -25.67561 25.41274 1.000 29.75245  ? 183 GLN B O    1 
ATOM   6391 C CB   . GLN B 1 197 ? 1.43586   -23.05362 27.15012 1.000 35.87103  ? 183 GLN B CB   1 
ATOM   6392 C CG   . GLN B 1 197 ? 2.70798   -22.50829 27.76998 1.000 41.66171  ? 183 GLN B CG   1 
ATOM   6393 C CD   . GLN B 1 197 ? 2.50817   -22.07075 29.20935 1.000 60.97416  ? 183 GLN B CD   1 
ATOM   6394 O OE1  . GLN B 1 197 ? 1.56911   -22.50479 29.87707 1.000 54.10269  ? 183 GLN B OE1  1 
ATOM   6395 N NE2  . GLN B 1 197 ? 3.38811   -21.20017 29.69196 1.000 67.09227  ? 183 GLN B NE2  1 
ATOM   6396 H H    . GLN B 1 197 ? -0.18353  -24.03705 25.00982 1.000 35.39307  ? 183 GLN B H    1 
ATOM   6397 H HA   . GLN B 1 197 ? 2.08164   -22.59536 25.26049 1.000 31.33354  ? 183 GLN B HA   1 
ATOM   6398 H HB2  . GLN B 1 197 ? 0.72715   -22.41465 27.32431 1.000 43.10117  ? 183 GLN B HB2  1 
ATOM   6399 H HB3  . GLN B 1 197 ? 1.23593   -23.89748 27.58468 1.000 43.10117  ? 183 GLN B HB3  1 
ATOM   6400 H HG2  . GLN B 1 197 ? 3.38906   -23.19884 27.75656 1.000 50.04999  ? 183 GLN B HG2  1 
ATOM   6401 H HG3  . GLN B 1 197 ? 3.00544   -21.73897 27.25953 1.000 50.04999  ? 183 GLN B HG3  1 
ATOM   6402 H HE21 . GLN B 1 197 ? 4.02846   -20.91500 29.19373 1.000 80.56667  ? 183 GLN B HE21 1 
ATOM   6403 H HE22 . GLN B 1 197 ? 3.31736   -20.92182 30.50259 1.000 80.56667  ? 183 GLN B HE22 1 
ATOM   6404 N N    . ASN B 1 198 ? 3.44011   -24.61489 24.97042 1.000 28.31644  ? 184 ASN B N    1 
ATOM   6405 C CA   . ASN B 1 198 ? 4.17323   -25.82553 24.62562 1.000 29.09976  ? 184 ASN B CA   1 
ATOM   6406 C C    . ASN B 1 198 ? 5.49930   -25.85296 25.37184 1.000 32.09803  ? 184 ASN B C    1 
ATOM   6407 O O    . ASN B 1 198 ? 6.20480   -24.84193 25.43896 1.000 31.16432  ? 184 ASN B O    1 
ATOM   6408 C CB   . ASN B 1 198 ? 4.42888   -25.91477 23.11240 1.000 30.41482  ? 184 ASN B CB   1 
ATOM   6409 C CG   . ASN B 1 198 ? 3.14679   -25.90708 22.29630 1.000 28.17546  ? 184 ASN B CG   1 
ATOM   6410 O OD1  . ASN B 1 198 ? 2.37622   -24.94891 22.33592 1.000 29.70144  ? 184 ASN B OD1  1 
ATOM   6411 N ND2  . ASN B 1 198 ? 2.92594   -26.97050 21.53303 1.000 28.58021  ? 184 ASN B ND2  1 
ATOM   6412 H H    . ASN B 1 198 ? 3.91139   -23.89757 24.91616 1.000 34.03567  ? 184 ASN B H    1 
ATOM   6413 H HA   . ASN B 1 198 ? 3.65582   -26.60052 24.89504 1.000 34.97565  ? 184 ASN B HA   1 
ATOM   6414 H HB2  . ASN B 1 198 ? 4.96388   -25.15394 22.83708 1.000 36.55372  ? 184 ASN B HB2  1 
ATOM   6415 H HB3  . ASN B 1 198 ? 4.90154   -26.73970 22.92007 1.000 36.55372  ? 184 ASN B HB3  1 
ATOM   6416 H HD21 . ASN B 1 198 ? 2.21439   -27.01425 21.05202 1.000 34.35219  ? 184 ASN B HD21 1 
ATOM   6417 H HD22 . ASN B 1 198 ? 3.49442   -27.61567 21.51958 1.000 34.35219  ? 184 ASN B HD22 1 
ATOM   6418 N N    . THR B 1 199 ? 5.83660   -27.01774 25.92919 1.000 33.87361  ? 185 THR B N    1 
ATOM   6419 C CA   . THR B 1 199 ? 7.08224   -27.20614 26.65980 1.000 33.40458  ? 185 THR B CA   1 
ATOM   6420 C C    . THR B 1 199 ? 7.67695   -28.55353 26.27089 1.000 37.06696  ? 185 THR B C    1 
ATOM   6421 O O    . THR B 1 199 ? 6.93050   -29.52013 26.05516 1.000 31.11630  ? 185 THR B O    1 
ATOM   6422 C CB   . THR B 1 199 ? 6.87550   -27.15877 28.18076 1.000 33.44562  ? 185 THR B CB   1 
ATOM   6423 O OG1  . THR B 1 199 ? 6.10530   -28.29261 28.59516 1.000 46.04333  ? 185 THR B OG1  1 
ATOM   6424 C CG2  . THR B 1 199 ? 6.15089   -25.88293 28.59082 1.000 39.87962  ? 185 THR B CG2  1 
ATOM   6425 H H    . THR B 1 199 ? 5.34799   -27.72461 25.89462 1.000 40.70428  ? 185 THR B H    1 
ATOM   6426 H HA   . THR B 1 199 ? 7.70352   -26.50198 26.41679 1.000 40.14143  ? 185 THR B HA   1 
ATOM   6427 H HB   . THR B 1 199 ? 7.73956   -27.17182 28.62135 1.000 40.19068  ? 185 THR B HB   1 
ATOM   6428 H HG1  . THR B 1 199 ? 6.04521   -28.30846 29.43286 1.000 55.30793  ? 185 THR B HG1  1 
ATOM   6429 H HG21 . THR B 1 199 ? 5.27363   -25.85234 28.17805 1.000 47.91149  ? 185 THR B HG21 1 
ATOM   6430 H HG22 . THR B 1 199 ? 6.04634   -25.85598 29.55479 1.000 47.91149  ? 185 THR B HG22 1 
ATOM   6431 H HG23 . THR B 1 199 ? 6.65933   -25.10696 28.30751 1.000 47.91149  ? 185 THR B HG23 1 
ATOM   6432 N N    . PRO B 1 200 ? 9.00169   -28.65528 26.17858 1.000 34.51752  ? 186 PRO B N    1 
ATOM   6433 C CA   . PRO B 1 200 ? 9.60840   -29.92359 25.76262 1.000 32.58951  ? 186 PRO B CA   1 
ATOM   6434 C C    . PRO B 1 200 ? 9.49001   -30.99355 26.83628 1.000 31.54940  ? 186 PRO B C    1 
ATOM   6435 O O    . PRO B 1 200 ? 9.53192   -30.71685 28.03714 1.000 30.51755  ? 186 PRO B O    1 
ATOM   6436 C CB   . PRO B 1 200 ? 11.07374  -29.55106 25.50657 1.000 35.92937  ? 186 PRO B CB   1 
ATOM   6437 C CG   . PRO B 1 200 ? 11.31312  -28.35132 26.35297 1.000 38.15395  ? 186 PRO B CG   1 
ATOM   6438 C CD   . PRO B 1 200 ? 10.01123  -27.60297 26.39643 1.000 36.24129  ? 186 PRO B CD   1 
ATOM   6439 H HA   . PRO B 1 200 ? 9.20086   -30.24382 24.94270 1.000 39.16335  ? 186 PRO B HA   1 
ATOM   6440 H HB2  . PRO B 1 200 ? 11.65249  -30.28368 25.76965 1.000 43.17118  ? 186 PRO B HB2  1 
ATOM   6441 H HB3  . PRO B 1 200 ? 11.20407  -29.34609 24.56747 1.000 43.17118  ? 186 PRO B HB3  1 
ATOM   6442 H HG2  . PRO B 1 200 ? 11.57839  -28.62874 27.24379 1.000 45.84068  ? 186 PRO B HG2  1 
ATOM   6443 H HG3  . PRO B 1 200 ? 12.00877  -27.80514 25.95465 1.000 45.84068  ? 186 PRO B HG3  1 
ATOM   6444 H HD2  . PRO B 1 200 ? 9.88620   -27.17923 27.25998 1.000 43.54548  ? 186 PRO B HD2  1 
ATOM   6445 H HD3  . PRO B 1 200 ? 9.97275   -26.93758 25.69169 1.000 43.54548  ? 186 PRO B HD3  1 
ATOM   6446 N N    . ILE B 1 201 ? 9.33643   -32.23728 26.37958 1.000 32.82744  ? 187 ILE B N    1 
ATOM   6447 C CA   . ILE B 1 201 ? 9.26536   -33.36347 27.30268 1.000 31.04000  ? 187 ILE B CA   1 
ATOM   6448 C C    . ILE B 1 201 ? 10.65814  -33.79352 27.74648 1.000 28.98309  ? 187 ILE B C    1 
ATOM   6449 O O    . ILE B 1 201 ? 10.84660  -34.20633 28.89663 1.000 31.88803  ? 187 ILE B O    1 
ATOM   6450 C CB   . ILE B 1 201 ? 8.50412   -34.53314 26.65378 1.000 27.94930  ? 187 ILE B CB   1 
ATOM   6451 C CG1  . ILE B 1 201 ? 7.02020   -34.18167 26.50667 1.000 29.61956  ? 187 ILE B CG1  1 
ATOM   6452 C CG2  . ILE B 1 201 ? 8.69269   -35.80220 27.47067 1.000 27.32329  ? 187 ILE B CG2  1 
ATOM   6453 C CD1  . ILE B 1 201 ? 6.23232   -35.15256 25.64629 1.000 29.30970  ? 187 ILE B CD1  1 
ATOM   6454 H H    . ILE B 1 201 ? 9.27170   -32.45183 25.54928 1.000 39.44886  ? 187 ILE B H    1 
ATOM   6455 H HA   . ILE B 1 201 ? 8.77541   -33.08357 28.09167 1.000 37.30394  ? 187 ILE B HA   1 
ATOM   6456 H HB   . ILE B 1 201 ? 8.86507   -34.68961 25.76714 1.000 33.59510  ? 187 ILE B HB   1 
ATOM   6457 H HG12 . ILE B 1 201 ? 6.61464   -34.17375 27.38778 1.000 35.59942  ? 187 ILE B HG12 1 
ATOM   6458 H HG13 . ILE B 1 201 ? 6.94833   -33.30375 26.10046 1.000 35.59942  ? 187 ILE B HG13 1 
ATOM   6459 H HG21 . ILE B 1 201 ? 9.57243   -36.16763 27.28787 1.000 32.84389  ? 187 ILE B HG21 1 
ATOM   6460 H HG22 . ILE B 1 201 ? 8.61360   -35.58591 28.41293 1.000 32.84389  ? 187 ILE B HG22 1 
ATOM   6461 H HG23 . ILE B 1 201 ? 8.00949   -36.44354 27.22002 1.000 32.84389  ? 187 ILE B HG23 1 
ATOM   6462 H HD11 . ILE B 1 201 ? 6.22227   -36.02097 26.07834 1.000 35.22758  ? 187 ILE B HD11 1 
ATOM   6463 H HD12 . ILE B 1 201 ? 5.32578   -34.82221 25.54656 1.000 35.22758  ? 187 ILE B HD12 1 
ATOM   6464 H HD13 . ILE B 1 201 ? 6.65712   -35.22055 24.77690 1.000 35.22758  ? 187 ILE B HD13 1 
ATOM   6465 N N    . GLY B 1 202 ? 11.64901  -33.70049 26.86244 1.000 30.72451  ? 188 GLY B N    1 
ATOM   6466 C CA   . GLY B 1 202 ? 12.98564  -34.17151 27.14881 1.000 35.11416  ? 188 GLY B CA   1 
ATOM   6467 C C    . GLY B 1 202 ? 13.87784  -33.08340 27.71123 1.000 33.21929  ? 188 GLY B C    1 
ATOM   6468 O O    . GLY B 1 202 ? 13.44004  -31.98243 28.05008 1.000 33.33024  ? 188 GLY B O    1 
ATOM   6469 H H    . GLY B 1 202 ? 11.56280  -33.36079 26.07710 1.000 36.92536  ? 188 GLY B H    1 
ATOM   6470 H HA2  . GLY B 1 202 ? 12.93941  -34.89262 27.79593 1.000 42.19293  ? 188 GLY B HA2  1 
ATOM   6471 H HA3  . GLY B 1 202 ? 13.38948  -34.50521 26.33244 1.000 42.19293  ? 188 GLY B HA3  1 
ATOM   6472 N N    . ASP B 1 203 ? 15.16540  -33.41393 27.81115 1.000 34.85162  ? 189 ASP B N    1 
ATOM   6473 C CA   . ASP B 1 203 ? 16.16459  -32.50087 28.34618 1.000 34.08974  ? 189 ASP B CA   1 
ATOM   6474 C C    . ASP B 1 203 ? 17.00125  -31.82124 27.27119 1.000 37.01785  ? 189 ASP B C    1 
ATOM   6475 O O    . ASP B 1 203 ? 17.69048  -30.84157 27.57608 1.000 37.84661  ? 189 ASP B O    1 
ATOM   6476 C CB   . ASP B 1 203 ? 17.10022  -33.24839 29.30301 1.000 33.90485  ? 189 ASP B CB   1 
ATOM   6477 C CG   . ASP B 1 203 ? 16.36491  -33.84970 30.48116 1.000 38.35707  ? 189 ASP B CG   1 
ATOM   6478 O OD1  . ASP B 1 203 ? 15.34846  -33.26066 30.90596 1.000 36.25540  ? 189 ASP B OD1  1 
ATOM   6479 O OD2  . ASP B 1 203 ? 16.79934  -34.91126 30.97821 1.000 38.08878  ? 189 ASP B OD2  1 
ATOM   6480 H H    . ASP B 1 203 ? 15.48647  -34.17466 27.57073 1.000 41.87788  ? 189 ASP B H    1 
ATOM   6481 H HA   . ASP B 1 203 ? 15.70658  -31.80739 28.84638 1.000 40.96363  ? 189 ASP B HA   1 
ATOM   6482 H HB2  . ASP B 1 203 ? 17.53675  -33.96841 28.82145 1.000 40.40612  ? 189 ASP B HB2  1 
ATOM   6483 H HB3  . ASP B 1 203 ? 17.76319  -32.62912 29.64633 1.000 40.40612  ? 189 ASP B HB3  1 
ATOM   6484 N N    . GLY B 1 204 ? 16.96801  -32.31291 26.03556 1.000 40.73458  ? 190 GLY B N    1 
ATOM   6485 C CA   . GLY B 1 204 ? 17.75188  -31.73650 24.96894 1.000 46.76809  ? 190 GLY B CA   1 
ATOM   6486 C C    . GLY B 1 204 ? 17.37456  -30.29323 24.69926 1.000 44.01138  ? 190 GLY B C    1 
ATOM   6487 O O    . GLY B 1 204 ? 16.25094  -29.86558 24.98102 1.000 43.88657  ? 190 GLY B O    1 
ATOM   6488 H H    . GLY B 1 204 ? 16.49165  -32.98735 25.79509 1.000 48.93743  ? 190 GLY B H    1 
ATOM   6489 H HA2  . GLY B 1 204 ? 18.69185  -31.76867 25.20627 1.000 56.17765  ? 190 GLY B HA2  1 
ATOM   6490 H HA3  . GLY B 1 204 ? 17.61387  -32.24681 24.15565 1.000 56.17765  ? 190 GLY B HA3  1 
ATOM   6491 N N    . PRO B 1 205 ? 18.30100  -29.51017 24.14410 1.000 47.32636  ? 191 PRO B N    1 
ATOM   6492 C CA   . PRO B 1 205 ? 17.98749  -28.10655 23.85600 1.000 41.88750  ? 191 PRO B CA   1 
ATOM   6493 C C    . PRO B 1 205 ? 16.97503  -27.98429 22.72859 1.000 39.97800  ? 191 PRO B C    1 
ATOM   6494 O O    . PRO B 1 205 ? 16.91146  -28.81784 21.82134 1.000 39.34083  ? 191 PRO B O    1 
ATOM   6495 C CB   . PRO B 1 205 ? 19.34190  -27.50432 23.45220 1.000 47.64796  ? 191 PRO B CB   1 
ATOM   6496 C CG   . PRO B 1 205 ? 20.37601  -28.54011 23.79623 1.000 46.74582  ? 191 PRO B CG   1 
ATOM   6497 C CD   . PRO B 1 205 ? 19.67218  -29.85532 23.73207 1.000 44.46320  ? 191 PRO B CD   1 
ATOM   6498 H HA   . PRO B 1 205 ? 17.65617  -27.65801 24.64968 1.000 50.32094  ? 191 PRO B HA   1 
ATOM   6499 H HB2  . PRO B 1 205 ? 19.34525  -27.31880 22.50011 1.000 57.23349  ? 191 PRO B HB2  1 
ATOM   6500 H HB3  . PRO B 1 205 ? 19.49634  -26.68634 23.95014 1.000 57.23349  ? 191 PRO B HB3  1 
ATOM   6501 H HG2  . PRO B 1 205 ? 21.10022  -28.50614 23.15182 1.000 56.15092  ? 191 PRO B HG2  1 
ATOM   6502 H HG3  . PRO B 1 205 ? 20.71838  -28.37680 24.68898 1.000 56.15092  ? 191 PRO B HG3  1 
ATOM   6503 H HD2  . PRO B 1 205 ? 19.68443  -30.21221 22.83019 1.000 53.41177  ? 191 PRO B HD2  1 
ATOM   6504 H HD3  . PRO B 1 205 ? 20.06953  -30.49226 24.34633 1.000 53.41177  ? 191 PRO B HD3  1 
ATOM   6505 N N    . VAL B 1 206 ? 16.18178  -26.91729 22.79170 1.000 40.93006  ? 192 VAL B N    1 
ATOM   6506 C CA   . VAL B 1 206 ? 15.14559  -26.65013 21.80710 1.000 40.77551  ? 192 VAL B CA   1 
ATOM   6507 C C    . VAL B 1 206 ? 15.40456  -25.28275 21.18841 1.000 40.67348  ? 192 VAL B C    1 
ATOM   6508 O O    . VAL B 1 206 ? 16.29960  -24.54548 21.60233 1.000 36.19966  ? 192 VAL B O    1 
ATOM   6509 C CB   . VAL B 1 206 ? 13.72993  -26.71676 22.41302 1.000 38.40513  ? 192 VAL B CB   1 
ATOM   6510 C CG1  . VAL B 1 206 ? 13.43024  -28.12743 22.90659 1.000 40.44846  ? 192 VAL B CG1  1 
ATOM   6511 C CG2  . VAL B 1 206 ? 13.57837  -25.70447 23.54373 1.000 39.81451  ? 192 VAL B CG2  1 
ATOM   6512 H H    . VAL B 1 206 ? 16.22847  -26.32235 23.41095 1.000 49.17202  ? 192 VAL B H    1 
ATOM   6513 H HA   . VAL B 1 206 ? 15.20217  -27.31569 21.10374 1.000 48.98655  ? 192 VAL B HA   1 
ATOM   6514 H HB   . VAL B 1 206 ? 13.08381  -26.49251 21.72517 1.000 46.14210  ? 192 VAL B HB   1 
ATOM   6515 H HG11 . VAL B 1 206 ? 14.21040  -28.68524 22.76130 1.000 48.59410  ? 192 VAL B HG11 1 
ATOM   6516 H HG12 . VAL B 1 206 ? 13.21990  -28.09289 23.85288 1.000 48.59410  ? 192 VAL B HG12 1 
ATOM   6517 H HG13 . VAL B 1 206 ? 12.67416  -28.48096 22.41237 1.000 48.59410  ? 192 VAL B HG13 1 
ATOM   6518 H HG21 . VAL B 1 206 ? 12.68582  -25.77841 23.91626 1.000 47.83335  ? 192 VAL B HG21 1 
ATOM   6519 H HG22 . VAL B 1 206 ? 14.23918  -25.89409 24.22804 1.000 47.83335  ? 192 VAL B HG22 1 
ATOM   6520 H HG23 . VAL B 1 206 ? 13.71597  -24.81211 23.18924 1.000 47.83335  ? 192 VAL B HG23 1 
ATOM   6521 N N    . LEU B 1 207 ? 14.60087  -24.95626 20.17969 1.000 42.83092  ? 193 LEU B N    1 
ATOM   6522 C CA   . LEU B 1 207 ? 14.66833  -23.67184 19.49774 1.000 41.70070  ? 193 LEU B CA   1 
ATOM   6523 C C    . LEU B 1 207 ? 13.55782  -22.77925 20.03458 1.000 37.86535  ? 193 LEU B C    1 
ATOM   6524 O O    . LEU B 1 207 ? 12.37590  -23.11398 19.91051 1.000 39.00171  ? 193 LEU B O    1 
ATOM   6525 C CB   . LEU B 1 207 ? 14.52869  -23.84407 17.98550 1.000 42.10417  ? 193 LEU B CB   1 
ATOM   6526 C CG   . LEU B 1 207 ? 15.65256  -24.58526 17.25700 1.000 42.61280  ? 193 LEU B CG   1 
ATOM   6527 C CD1  . LEU B 1 207 ? 15.26380  -24.84052 15.80666 1.000 37.07527  ? 193 LEU B CD1  1 
ATOM   6528 C CD2  . LEU B 1 207 ? 16.96189  -23.80610 17.32780 1.000 43.68464  ? 193 LEU B CD2  1 
ATOM   6529 H H    . LEU B 1 207 ? 13.99313  -25.47755 19.86583 1.000 51.45305  ? 193 LEU B H    1 
ATOM   6530 H HA   . LEU B 1 207 ? 15.52502  -23.25369 19.67704 1.000 50.09678  ? 193 LEU B HA   1 
ATOM   6531 H HB2  . LEU B 1 207 ? 13.71053  -24.33703 17.81667 1.000 50.58095  ? 193 LEU B HB2  1 
ATOM   6532 H HB3  . LEU B 1 207 ? 14.47126  -22.96039 17.58964 1.000 50.58095  ? 193 LEU B HB3  1 
ATOM   6533 H HG   . LEU B 1 207 ? 15.79474  -25.43981 17.69338 1.000 51.19129  ? 193 LEU B HG   1 
ATOM   6534 H HD11 . LEU B 1 207 ? 14.43872  -25.35015 15.78587 1.000 44.54626  ? 193 LEU B HD11 1 
ATOM   6535 H HD12 . LEU B 1 207 ? 15.13817  -23.98928 15.35887 1.000 44.54626  ? 193 LEU B HD12 1 
ATOM   6536 H HD13 . LEU B 1 207 ? 15.97268  -25.34091 15.37307 1.000 44.54626  ? 193 LEU B HD13 1 
ATOM   6537 H HD21 . LEU B 1 207 ? 16.83544  -22.93783 16.91427 1.000 52.47751  ? 193 LEU B HD21 1 
ATOM   6538 H HD22 . LEU B 1 207 ? 17.21390  -23.69591 18.25799 1.000 52.47751  ? 193 LEU B HD22 1 
ATOM   6539 H HD23 . LEU B 1 207 ? 17.64960  -24.30060 16.85512 1.000 52.47751  ? 193 LEU B HD23 1 
ATOM   6540 N N    . LEU B 1 208 ? 13.93692  -21.65469 20.63809 1.000 38.80517  ? 194 LEU B N    1 
ATOM   6541 C CA   . LEU B 1 208 ? 12.96676  -20.66691 21.08364 1.000 40.02842  ? 194 LEU B CA   1 
ATOM   6542 C C    . LEU B 1 208 ? 12.83796  -19.60717 19.99998 1.000 35.78535  ? 194 LEU B C    1 
ATOM   6543 O O    . LEU B 1 208 ? 13.80271  -18.86700 19.75632 1.000 34.86004  ? 194 LEU B O    1 
ATOM   6544 C CB   . LEU B 1 208 ? 13.40091  -20.03937 22.40630 1.000 34.31736  ? 194 LEU B CB   1 
ATOM   6545 C CG   . LEU B 1 208 ? 13.69530  -21.04606 23.52466 1.000 45.99472  ? 194 LEU B CG   1 
ATOM   6546 C CD1  . LEU B 1 208 ? 13.92091  -20.32879 24.84884 1.000 51.05865  ? 194 LEU B CD1  1 
ATOM   6547 C CD2  . LEU B 1 208 ? 12.57883  -22.07986 23.65395 1.000 36.69282  ? 194 LEU B CD2  1 
ATOM   6548 H H    . LEU B 1 208 ? 14.75439  -21.44254 20.80035 1.000 46.62214  ? 194 LEU B H    1 
ATOM   6549 H HA   . LEU B 1 208 ? 12.10357  -21.08713 21.22227 1.000 48.09005  ? 194 LEU B HA   1 
ATOM   6550 H HB2  . LEU B 1 208 ? 14.20998  -19.52677 22.25289 1.000 41.23678  ? 194 LEU B HB2  1 
ATOM   6551 H HB3  . LEU B 1 208 ? 12.69184  -19.45498 22.71714 1.000 41.23678  ? 194 LEU B HB3  1 
ATOM   6552 H HG   . LEU B 1 208 ? 14.50795  -21.52439 23.29726 1.000 55.24960  ? 194 LEU B HG   1 
ATOM   6553 H HD11 . LEU B 1 208 ? 14.16509  -20.98125 25.52381 1.000 61.32632  ? 194 LEU B HD11 1 
ATOM   6554 H HD12 . LEU B 1 208 ? 14.63568  -19.68216 24.73997 1.000 61.32632  ? 194 LEU B HD12 1 
ATOM   6555 H HD13 . LEU B 1 208 ? 13.10231  -19.87673 25.10660 1.000 61.32632  ? 194 LEU B HD13 1 
ATOM   6556 H HD21 . LEU B 1 208 ? 11.72648  -21.61955 23.70417 1.000 44.08733  ? 194 LEU B HD21 1 
ATOM   6557 H HD22 . LEU B 1 208 ? 12.59547  -22.66139 22.87777 1.000 44.08733  ? 194 LEU B HD22 1 
ATOM   6558 H HD23 . LEU B 1 208 ? 12.72186  -22.60000 24.46010 1.000 44.08733  ? 194 LEU B HD23 1 
ATOM   6559 N N    . PRO B 1 209 ? 11.69797  -19.49428 19.32487 1.000 34.30878  ? 195 PRO B N    1 
ATOM   6560 C CA   . PRO B 1 209 ? 11.62214  -18.66414 18.12278 1.000 31.25078  ? 195 PRO B CA   1 
ATOM   6561 C C    . PRO B 1 209 ? 11.35179  -17.19546 18.41424 1.000 32.91282  ? 195 PRO B C    1 
ATOM   6562 O O    . PRO B 1 209 ? 10.79195  -16.82299 19.44664 1.000 33.87852  ? 195 PRO B O    1 
ATOM   6563 C CB   . PRO B 1 209 ? 10.43455  -19.28136 17.37204 1.000 28.92811  ? 195 PRO B CB   1 
ATOM   6564 C CG   . PRO B 1 209 ? 9.51618   -19.69563 18.47009 1.000 35.90526  ? 195 PRO B CG   1 
ATOM   6565 C CD   . PRO B 1 209 ? 10.40453  -20.14375 19.61426 1.000 29.16605  ? 195 PRO B CD   1 
ATOM   6566 H HA   . PRO B 1 209 ? 12.44029  -18.73888 17.60708 1.000 37.55688  ? 195 PRO B HA   1 
ATOM   6567 H HB2  . PRO B 1 209 ? 10.02032  -18.62105 16.79472 1.000 34.76968  ? 195 PRO B HB2  1 
ATOM   6568 H HB3  . PRO B 1 209 ? 10.72604  -20.04391 16.84815 1.000 34.76968  ? 195 PRO B HB3  1 
ATOM   6569 H HG2  . PRO B 1 209 ? 8.96683   -18.94225 18.73756 1.000 43.14225  ? 195 PRO B HG2  1 
ATOM   6570 H HG3  . PRO B 1 209 ? 8.95361   -20.42537 18.16696 1.000 43.14225  ? 195 PRO B HG3  1 
ATOM   6571 H HD2  . PRO B 1 209 ? 10.04977  -19.84016 20.46448 1.000 35.05520  ? 195 PRO B HD2  1 
ATOM   6572 H HD3  . PRO B 1 209 ? 10.49794  -21.10923 19.61948 1.000 35.05520  ? 195 PRO B HD3  1 
ATOM   6573 N N    . ASP B 1 210 ? 11.76619  -16.36042 17.46484 1.000 30.87865  ? 196 ASP B N    1 
ATOM   6574 C CA   . ASP B 1 210 ? 11.27444  -14.99620 17.41240 1.000 33.46444  ? 196 ASP B CA   1 
ATOM   6575 C C    . ASP B 1 210 ? 9.80190   -15.00270 17.00457 1.000 31.29461  ? 196 ASP B C    1 
ATOM   6576 O O    . ASP B 1 210 ? 9.25717   -16.01716 16.55957 1.000 30.31130  ? 196 ASP B O    1 
ATOM   6577 C CB   . ASP B 1 210 ? 12.08700  -14.15947 16.42347 1.000 34.85340  ? 196 ASP B CB   1 
ATOM   6578 C CG   . ASP B 1 210 ? 13.51407  -13.92250 16.88178 1.000 35.32495  ? 196 ASP B CG   1 
ATOM   6579 O OD1  . ASP B 1 210 ? 13.77696  -13.99192 18.09963 1.000 39.57560  ? 196 ASP B OD1  1 
ATOM   6580 O OD2  . ASP B 1 210 ? 14.37424  -13.65359 16.01628 1.000 41.59432  ? 196 ASP B OD2  1 
ATOM   6581 H H    . ASP B 1 210 ? 12.32785  -16.56182 16.84551 1.000 36.77468  ? 196 ASP B H    1 
ATOM   6582 H HA   . ASP B 1 210 ? 11.36330  -14.58686 18.28730 1.000 40.21326  ? 196 ASP B HA   1 
ATOM   6583 H HB2  . ASP B 1 210 ? 12.11934  -14.62170 15.57129 1.000 41.88002  ? 196 ASP B HB2  1 
ATOM   6584 H HB3  . ASP B 1 210 ? 11.65988  -13.29522 16.31610 1.000 41.88002  ? 196 ASP B HB3  1 
ATOM   6585 N N    . ASN B 1 211 ? 9.15727   -13.84679 17.15130 1.000 32.16532  ? 197 ASN B N    1 
ATOM   6586 C CA   . ASN B 1 211 ? 7.74790   -13.72145 16.80128 1.000 32.06218  ? 197 ASN B CA   1 
ATOM   6587 C C    . ASN B 1 211 ? 7.50337   -14.20103 15.37476 1.000 32.14963  ? 197 ASN B C    1 
ATOM   6588 O O    . ASN B 1 211 ? 8.22693   -13.83061 14.44766 1.000 33.28110  ? 197 ASN B O    1 
ATOM   6589 C CB   . ASN B 1 211 ? 7.29532   -12.26503 16.94829 1.000 33.61324  ? 197 ASN B CB   1 
ATOM   6590 C CG   . ASN B 1 211 ? 7.39591   -11.75391 18.37996 1.000 33.77790  ? 197 ASN B CG   1 
ATOM   6591 O OD1  . ASN B 1 211 ? 7.39604   -12.53100 19.33621 1.000 32.61979  ? 197 ASN B OD1  1 
ATOM   6592 N ND2  . ASN B 1 211 ? 7.47133   -10.43562 18.52976 1.000 35.42834  ? 197 ASN B ND2  1 
ATOM   6593 H H    . ASN B 1 211 ? 9.51336   -13.12345 17.45059 1.000 38.33331  ? 197 ASN B H    1 
ATOM   6594 H HA   . ASN B 1 211 ? 7.22143   -14.26739 17.40599 1.000 38.19491  ? 197 ASN B HA   1 
ATOM   6595 H HB2  . ASN B 1 211 ? 7.85491   -11.70293 16.38989 1.000 40.05619  ? 197 ASN B HB2  1 
ATOM   6596 H HB3  . ASN B 1 211 ? 6.36916   -12.19280 16.66917 1.000 40.05619  ? 197 ASN B HB3  1 
ATOM   6597 H HD21 . ASN B 1 211 ? 7.52971   -10.09497 19.31725 1.000 42.23431  ? 197 ASN B HD21 1 
ATOM   6598 H HD22 . ASN B 1 211 ? 7.46176   -9.92314  17.83920 1.000 42.23431  ? 197 ASN B HD22 1 
ATOM   6599 N N    . HIS B 1 212 ? 6.48192   -15.03356 15.20724 1.000 31.12006  ? 198 HIS B N    1 
ATOM   6600 C CA   . HIS B 1 212 ? 6.05292   -15.50220 13.89458 1.000 31.30188  ? 198 HIS B CA   1 
ATOM   6601 C C    . HIS B 1 212 ? 4.66676   -16.10870 14.06186 1.000 33.27832  ? 198 HIS B C    1 
ATOM   6602 O O    . HIS B 1 212 ? 4.08193   -16.07160 15.14919 1.000 32.33555  ? 198 HIS B O    1 
ATOM   6603 C CB   . HIS B 1 212 ? 7.04342   -16.50458 13.29329 1.000 35.30972  ? 198 HIS B CB   1 
ATOM   6604 C CG   . HIS B 1 212 ? 7.06056   -17.83313 13.98167 1.000 29.51213  ? 198 HIS B CG   1 
ATOM   6605 N ND1  . HIS B 1 212 ? 7.78629   -18.06729 15.12952 1.000 31.55749  ? 198 HIS B ND1  1 
ATOM   6606 C CD2  . HIS B 1 212 ? 6.45138   -19.00299 13.67628 1.000 28.79887  ? 198 HIS B CD2  1 
ATOM   6607 C CE1  . HIS B 1 212 ? 7.61902   -19.32274 15.50504 1.000 32.10768  ? 198 HIS B CE1  1 
ATOM   6608 N NE2  . HIS B 1 212 ? 6.81373   -19.91249 14.63986 1.000 33.10376  ? 198 HIS B NE2  1 
ATOM   6609 H H    . HIS B 1 212 ? 6.01008   -15.34882 15.85345 1.000 37.06437  ? 198 HIS B H    1 
ATOM   6610 H HA   . HIS B 1 212 ? 5.99975   -14.74807 13.28683 1.000 37.52894  ? 198 HIS B HA   1 
ATOM   6611 H HB2  . HIS B 1 212 ? 6.80663   -16.65663 12.36501 1.000 42.42761  ? 198 HIS B HB2  1 
ATOM   6612 H HB3  . HIS B 1 212 ? 7.93683   -16.13122 13.35090 1.000 42.42761  ? 198 HIS B HB3  1 
ATOM   6613 H HD1  . HIS B 1 212 ? 8.27218   -17.48681 15.53763 1.000 37.92493  ? 198 HIS B HD1  1 
ATOM   6614 H HD2  . HIS B 1 212 ? 5.89230   -19.16122 12.95012 1.000 34.61458  ? 198 HIS B HD2  1 
ATOM   6615 H HE1  . HIS B 1 212 ? 8.00290   -19.72319 16.25149 1.000 38.58516  ? 198 HIS B HE1  1 
ATOM   6616 N N    . TYR B 1 213 ? 4.13674   -16.66686 12.97630 1.000 30.39516  ? 199 TYR B N    1 
ATOM   6617 C CA   . TYR B 1 213 ? 2.82510   -17.29055 13.03838 1.000 34.28107  ? 199 TYR B CA   1 
ATOM   6618 C C    . TYR B 1 213 ? 2.74628   -18.42566 12.02900 1.000 33.96108  ? 199 TYR B C    1 
ATOM   6619 O O    . TYR B 1 213 ? 3.59103   -18.56156 11.14011 1.000 35.11535  ? 199 TYR B O    1 
ATOM   6620 C CB   . TYR B 1 213 ? 1.70844   -16.26567 12.79622 1.000 32.29276  ? 199 TYR B CB   1 
ATOM   6621 C CG   . TYR B 1 213 ? 1.67846   -15.67738 11.40262 1.000 32.64399  ? 199 TYR B CG   1 
ATOM   6622 C CD1  . TYR B 1 213 ? 1.10199   -16.37200 10.34639 1.000 33.34941  ? 199 TYR B CD1  1 
ATOM   6623 C CD2  . TYR B 1 213 ? 2.20728   -14.41873 11.14664 1.000 34.34621  ? 199 TYR B CD2  1 
ATOM   6624 C CE1  . TYR B 1 213 ? 1.06312   -15.83774 9.07270  1.000 34.57074  ? 199 TYR B CE1  1 
ATOM   6625 C CE2  . TYR B 1 213 ? 2.17425   -13.87476 9.87434  1.000 37.46897  ? 199 TYR B CE2  1 
ATOM   6626 C CZ   . TYR B 1 213 ? 1.59999   -14.58970 8.84122  1.000 38.11989  ? 199 TYR B CZ   1 
ATOM   6627 O OH   . TYR B 1 213 ? 1.55992   -14.05641 7.57372  1.000 44.00637  ? 199 TYR B OH   1 
ATOM   6628 H H    . TYR B 1 213 ? 4.51441   -16.69517 12.20419 1.000 36.19450  ? 199 TYR B H    1 
ATOM   6629 H HA   . TYR B 1 213 ? 2.70798   -17.67531 13.92107 1.000 41.19323  ? 199 TYR B HA   1 
ATOM   6630 H HB2  . TYR B 1 213 ? 0.85424   -16.69947 12.94810 1.000 38.80725  ? 199 TYR B HB2  1 
ATOM   6631 H HB3  . TYR B 1 213 ? 1.82346   -15.53191 13.42013 1.000 38.80725  ? 199 TYR B HB3  1 
ATOM   6632 H HD1  . TYR B 1 213 ? 0.73520   -17.21276 10.49963 1.000 40.07523  ? 199 TYR B HD1  1 
ATOM   6633 H HD2  . TYR B 1 213 ? 2.58990   -13.93348 11.84165 1.000 40.93576  ? 199 TYR B HD2  1 
ATOM   6634 H HE1  . TYR B 1 213 ? 0.67699   -16.31746 8.37579  1.000 41.20519  ? 199 TYR B HE1  1 
ATOM   6635 H HE2  . TYR B 1 213 ? 2.53648   -13.03297 9.71595  1.000 45.01871  ? 199 TYR B HE2  1 
ATOM   6636 H HH   . TYR B 1 213 ? 1.07448   -14.52992 7.07802  1.000 52.86358  ? 199 TYR B HH   1 
ATOM   6637 N N    . LEU B 1 214 ? 1.71127   -19.24663 12.18744 1.000 30.63072  ? 200 LEU B N    1 
ATOM   6638 C CA   . LEU B 1 214 ? 1.38970   -20.32152 11.25914 1.000 33.43820  ? 200 LEU B CA   1 
ATOM   6639 C C    . LEU B 1 214 ? 0.05467   -20.01879 10.59400 1.000 30.68446  ? 200 LEU B C    1 
ATOM   6640 O O    . LEU B 1 214 ? -0.93169  -19.72863 11.27948 1.000 34.03038  ? 200 LEU B O    1 
ATOM   6641 C CB   . LEU B 1 214 ? 1.30830   -21.67139 11.97503 1.000 29.85909  ? 200 LEU B CB   1 
ATOM   6642 C CG   . LEU B 1 214 ? 2.49853   -22.11589 12.82402 1.000 32.48521  ? 200 LEU B CG   1 
ATOM   6643 C CD1  . LEU B 1 214 ? 2.14672   -23.39434 13.57764 1.000 31.14315  ? 200 LEU B CD1  1 
ATOM   6644 C CD2  . LEU B 1 214 ? 3.73298   -22.32132 11.96589 1.000 28.07096  ? 200 LEU B CD2  1 
ATOM   6645 H H    . LEU B 1 214 ? 1.16344   -19.19707 12.84852 1.000 36.81281  ? 200 LEU B H    1 
ATOM   6646 H HA   . LEU B 1 214 ? 2.08122   -20.37561 10.58107 1.000 40.18178  ? 200 LEU B HA   1 
ATOM   6647 H HB2  . LEU B 1 214 ? 0.54077   -21.64308 12.56747 1.000 35.88685  ? 200 LEU B HB2  1 
ATOM   6648 H HB3  . LEU B 1 214 ? 1.18019   -22.35462 11.29851 1.000 35.88685  ? 200 LEU B HB3  1 
ATOM   6649 H HG   . LEU B 1 214 ? 2.70663   -21.42237 13.46948 1.000 39.03819  ? 200 LEU B HG   1 
ATOM   6650 H HD11 . LEU B 1 214 ? 1.34751   -23.24014 14.10526 1.000 37.42773  ? 200 LEU B HD11 1 
ATOM   6651 H HD12 . LEU B 1 214 ? 1.98806   -24.10512 12.93692 1.000 37.42773  ? 200 LEU B HD12 1 
ATOM   6652 H HD13 . LEU B 1 214 ? 2.88606   -23.63191 14.15888 1.000 37.42773  ? 200 LEU B HD13 1 
ATOM   6653 H HD21 . LEU B 1 214 ? 4.02507   -21.46261 11.62209 1.000 33.74109  ? 200 LEU B HD21 1 
ATOM   6654 H HD22 . LEU B 1 214 ? 4.43319   -22.71564 12.50914 1.000 33.74109  ? 200 LEU B HD22 1 
ATOM   6655 H HD23 . LEU B 1 214 ? 3.51144   -22.91397 11.23065 1.000 33.74109  ? 200 LEU B HD23 1 
ATOM   6656 N N    . SER B 1 215 ? 0.02389   -20.08807 9.26805  1.000 31.82224  ? 201 SER B N    1 
ATOM   6657 C CA   . SER B 1 215 ? -1.21171  -19.96555 8.50719  1.000 32.85956  ? 201 SER B CA   1 
ATOM   6658 C C    . SER B 1 215 ? -1.74216  -21.36484 8.23017  1.000 33.00119  ? 201 SER B C    1 
ATOM   6659 O O    . SER B 1 215 ? -0.99715  -22.23249 7.76344  1.000 33.78050  ? 201 SER B O    1 
ATOM   6660 C CB   . SER B 1 215 ? -0.98271  -19.20833 7.19937  1.000 35.86238  ? 201 SER B CB   1 
ATOM   6661 O OG   . SER B 1 215 ? -0.31290  -20.01915 6.25013  1.000 46.55116  ? 201 SER B OG   1 
ATOM   6662 H H    . SER B 1 215 ? 0.72027   -20.20798 8.77786  1.000 38.24263  ? 201 SER B H    1 
ATOM   6663 H HA   . SER B 1 215 ? -1.87174  -19.47017 9.01696  1.000 39.48741  ? 201 SER B HA   1 
ATOM   6664 H HB2  . SER B 1 215 ? -1.84155  -18.94212 6.83546  1.000 43.09080  ? 201 SER B HB2  1 
ATOM   6665 H HB3  . SER B 1 215 ? -0.44166  -18.42391 7.38062  1.000 43.09080  ? 201 SER B HB3  1 
ATOM   6666 H HG   . SER B 1 215 ? 0.38701   -20.33816 6.58771  1.000 55.91733  ? 201 SER B HG   1 
ATOM   6667 N N    . THR B 1 216 ? -3.01975  -21.58565 8.52863  1.000 37.39536  ? 202 THR B N    1 
ATOM   6668 C CA   . THR B 1 216 ? -3.61229  -22.91351 8.46169  1.000 37.43283  ? 202 THR B CA   1 
ATOM   6669 C C    . THR B 1 216 ? -4.93739  -22.85889 7.71814  1.000 44.66137  ? 202 THR B C    1 
ATOM   6670 O O    . THR B 1 216 ? -5.79858  -22.03129 8.03317  1.000 41.30399  ? 202 THR B O    1 
ATOM   6671 C CB   . THR B 1 216 ? -3.83080  -23.48762 9.86618  1.000 36.64366  ? 202 THR B CB   1 
ATOM   6672 O OG1  . THR B 1 216 ? -2.62077  -23.37402 10.62664 1.000 37.90929  ? 202 THR B OG1  1 
ATOM   6673 C CG2  . THR B 1 216 ? -4.24885  -24.95228 9.78358  1.000 40.13503  ? 202 THR B CG2  1 
ATOM   6674 H H    . THR B 1 216 ? -3.56912  -20.97187 8.77574  1.000 44.93038  ? 202 THR B H    1 
ATOM   6675 H HA   . THR B 1 216 ? -3.01640  -23.49763 7.96710  1.000 44.97533  ? 202 THR B HA   1 
ATOM   6676 H HB   . THR B 1 216 ? -4.53630  -22.99460 10.31352 1.000 44.02834  ? 202 THR B HB   1 
ATOM   6677 H HG1  . THR B 1 216 ? -2.72907  -23.70675 11.39029 1.000 45.54709  ? 202 THR B HG1  1 
ATOM   6678 H HG21 . THR B 1 216 ? -4.18642  -25.36500 10.65918 1.000 48.21798  ? 202 THR B HG21 1 
ATOM   6679 H HG22 . THR B 1 216 ? -5.16390  -25.01887 9.46871  1.000 48.21798  ? 202 THR B HG22 1 
ATOM   6680 H HG23 . THR B 1 216 ? -3.66899  -25.42864 9.16897  1.000 48.21798  ? 202 THR B HG23 1 
ATOM   6681 N N    . CYS B 1 217 ? -5.09390  -23.74128 6.73429  1.000 38.59686  ? 203 CYS B N    1 
ATOM   6682 C CA   . CYS B 1 217 ? -6.37066  -23.98197 6.07380  1.000 44.27534  ? 203 CYS B CA   1 
ATOM   6683 C C    . CYS B 1 217 ? -6.70819  -25.45603 6.23692  1.000 42.55069  ? 203 CYS B C    1 
ATOM   6684 O O    . CYS B 1 217 ? -5.90422  -26.32301 5.87717  1.000 37.39148  ? 203 CYS B O    1 
ATOM   6685 C CB   . CYS B 1 217 ? -6.31915  -23.60247 4.59364  1.000 41.13096  ? 203 CYS B CB   1 
ATOM   6686 S SG   . CYS B 1 217 ? -6.30613  -21.82649 4.26147  1.000 53.70748  ? 203 CYS B SG   1 
ATOM   6687 H H    . CYS B 1 217 ? -4.45485  -24.22607 6.42415  1.000 46.37218  ? 203 CYS B H    1 
ATOM   6688 H HA   . CYS B 1 217 ? -7.06270  -23.44630 6.49216  1.000 53.18635  ? 203 CYS B HA   1 
ATOM   6689 H HB2  . CYS B 1 217 ? -5.51111  -23.97645 4.20879  1.000 49.41310  ? 203 CYS B HB2  1 
ATOM   6690 H HB3  . CYS B 1 217 ? -7.09931  -23.97508 4.15387  1.000 49.41310  ? 203 CYS B HB3  1 
ATOM   6691 N N    . SER B 1 218 ? -7.88320  -25.73830 6.78507  1.000 51.85032  ? 204 SER B N    1 
ATOM   6692 C CA   . SER B 1 218 ? -8.31636  -27.10288 7.03234  1.000 51.34592  ? 204 SER B CA   1 
ATOM   6693 C C    . SER B 1 218 ? -9.50848  -27.43753 6.14638  1.000 50.35307  ? 204 SER B C    1 
ATOM   6694 O O    . SER B 1 218 ? -10.28832 -26.56024 5.76541  1.000 50.22283  ? 204 SER B O    1 
ATOM   6695 C CB   . SER B 1 218 ? -8.68566  -27.30329 8.50377  1.000 52.81808  ? 204 SER B CB   1 
ATOM   6696 O OG   . SER B 1 218 ? -9.94112  -26.71783 8.79351  1.000 62.00039  ? 204 SER B OG   1 
ATOM   6697 H H    . SER B 1 218 ? -8.45596  -25.14375 7.02602  1.000 62.27632  ? 204 SER B H    1 
ATOM   6698 H HA   . SER B 1 218 ? -7.59728  -27.71736 6.81730  1.000 61.67104  ? 204 SER B HA   1 
ATOM   6699 H HB2  . SER B 1 218 ? -8.73004  -28.25396 8.69128  1.000 63.43764  ? 204 SER B HB2  1 
ATOM   6700 H HB3  . SER B 1 218 ? -8.00775  -26.88696 9.05875  1.000 63.43764  ? 204 SER B HB3  1 
ATOM   6701 H HG   . SER B 1 218 ? -10.45276 -27.28965 9.13533  1.000 74.45641  ? 204 SER B HG   1 
ATOM   6702 N N    . LYS B 1 219 ? -9.63808  -28.72033 5.81820  1.000 42.03856  ? 205 LYS B N    1 
ATOM   6703 C CA   . LYS B 1 219 ? -10.71414 -29.21250 4.96767  1.000 40.90006  ? 205 LYS B CA   1 
ATOM   6704 C C    . LYS B 1 219 ? -11.33049 -30.43194 5.63336  1.000 34.07193  ? 205 LYS B C    1 
ATOM   6705 O O    . LYS B 1 219 ? -10.63790 -31.42606 5.87337  1.000 35.22903  ? 205 LYS B O    1 
ATOM   6706 C CB   . LYS B 1 219 ? -10.19257 -29.56175 3.57092  1.000 43.17893  ? 205 LYS B CB   1 
ATOM   6707 C CG   . LYS B 1 219 ? -11.25389 -30.07484 2.60567  1.000 44.95924  ? 205 LYS B CG   1 
ATOM   6708 C CD   . LYS B 1 219 ? -10.62307 -30.90833 1.49581  1.000 51.05356  ? 205 LYS B CD   1 
ATOM   6709 C CE   . LYS B 1 219 ? -11.67088 -31.48894 0.55824  1.000 57.00967  ? 205 LYS B CE   1 
ATOM   6710 N NZ   . LYS B 1 219 ? -12.65866 -32.33995 1.27993  1.000 57.39716  ? 205 LYS B NZ   1 
ATOM   6711 H H    . LYS B 1 219 ? -9.10145  -29.33794 6.08312  1.000 50.50221  ? 205 LYS B H    1 
ATOM   6712 H HA   . LYS B 1 219 ? -11.40005 -28.53284 4.87560  1.000 49.13601  ? 205 LYS B HA   1 
ATOM   6713 H HB2  . LYS B 1 219 ? -9.80231  -28.76468 3.17941  1.000 51.87066  ? 205 LYS B HB2  1 
ATOM   6714 H HB3  . LYS B 1 219 ? -9.51782  -30.25317 3.65782  1.000 51.87066  ? 205 LYS B HB3  1 
ATOM   6715 H HG2  . LYS B 1 219 ? -11.88636 -30.63148 3.08634  1.000 54.00703  ? 205 LYS B HG2  1 
ATOM   6716 H HG3  . LYS B 1 219 ? -11.71420 -29.32280 2.20139  1.000 54.00703  ? 205 LYS B HG3  1 
ATOM   6717 H HD2  . LYS B 1 219 ? -10.02672 -30.34826 0.97466  1.000 61.32021  ? 205 LYS B HD2  1 
ATOM   6718 H HD3  . LYS B 1 219 ? -10.12792 -31.64349 1.88984  1.000 61.32021  ? 205 LYS B HD3  1 
ATOM   6719 H HE2  . LYS B 1 219 ? -12.15215 -30.76391 0.12974  1.000 68.46754  ? 205 LYS B HE2  1 
ATOM   6720 H HE3  . LYS B 1 219 ? -11.23151 -32.03665 -0.11098 1.000 68.46754  ? 205 LYS B HE3  1 
ATOM   6721 H HZ1  . LYS B 1 219 ? -12.99790 -32.94869 0.72635  1.000 68.93253  ? 205 LYS B HZ1  1 
ATOM   6722 H HZ2  . LYS B 1 219 ? -12.26260 -32.75638 1.95952  1.000 68.93253  ? 205 LYS B HZ2  1 
ATOM   6723 H HZ3  . LYS B 1 219 ? -13.32077 -31.83627 1.59618  1.000 68.93253  ? 205 LYS B HZ3  1 
ATOM   6724 N N    . LEU B 1 220 ? -12.62412 -30.35503 5.92974  1.000 40.69392  ? 206 LEU B N    1 
ATOM   6725 C CA   . LEU B 1 220 ? -13.35820 -31.44385 6.55668  1.000 35.98782  ? 206 LEU B CA   1 
ATOM   6726 C C    . LEU B 1 220 ? -14.28635 -32.09672 5.54296  1.000 33.70380  ? 206 LEU B C    1 
ATOM   6727 O O    . LEU B 1 220 ? -14.93114 -31.41075 4.74329  1.000 35.51977  ? 206 LEU B O    1 
ATOM   6728 C CB   . LEU B 1 220 ? -14.17277 -30.94415 7.75176  1.000 37.78942  ? 206 LEU B CB   1 
ATOM   6729 C CG   . LEU B 1 220 ? -13.41250 -30.74556 9.06466  1.000 36.82112  ? 206 LEU B CG   1 
ATOM   6730 C CD1  . LEU B 1 220 ? -12.28019 -29.74622 8.90242  1.000 37.06834  ? 206 LEU B CD1  1 
ATOM   6731 C CD2  . LEU B 1 220 ? -14.36778 -30.30425 10.16426 1.000 36.88881  ? 206 LEU B CD2  1 
ATOM   6732 H H    . LEU B 1 220 ? -13.10921 -29.66262 5.77208  1.000 48.88864  ? 206 LEU B H    1 
ATOM   6733 H HA   . LEU B 1 220 ? -12.73021 -32.11223 6.87259  1.000 43.24132  ? 206 LEU B HA   1 
ATOM   6734 H HB2  . LEU B 1 220 ? -14.55894 -30.08667 7.51408  1.000 45.40324  ? 206 LEU B HB2  1 
ATOM   6735 H HB3  . LEU B 1 220 ? -14.87683 -31.58842 7.92533  1.000 45.40324  ? 206 LEU B HB3  1 
ATOM   6736 H HG   . LEU B 1 220 ? -13.01480 -31.59121 9.32466  1.000 44.24129  ? 206 LEU B HG   1 
ATOM   6737 H HD11 . LEU B 1 220 ? -12.03546 -29.40178 9.77556  1.000 44.53795  ? 206 LEU B HD11 1 
ATOM   6738 H HD12 . LEU B 1 220 ? -11.52008 -30.19311 8.49818  1.000 44.53795  ? 206 LEU B HD12 1 
ATOM   6739 H HD13 . LEU B 1 220 ? -12.57879 -29.02044 8.33234  1.000 44.53795  ? 206 LEU B HD13 1 
ATOM   6740 H HD21 . LEU B 1 220 ? -15.01517 -31.00919 10.32187 1.000 44.32252  ? 206 LEU B HD21 1 
ATOM   6741 H HD22 . LEU B 1 220 ? -13.86075 -30.13382 10.97345 1.000 44.32252  ? 206 LEU B HD22 1 
ATOM   6742 H HD23 . LEU B 1 220 ? -14.82205 -29.49503 9.88196  1.000 44.32252  ? 206 LEU B HD23 1 
ATOM   6743 N N    . SER B 1 221 ? -14.35352 -33.42338 5.58713  1.000 31.45525  ? 207 SER B N    1 
ATOM   6744 C CA   . SER B 1 221 ? -15.20744 -34.19140 4.69246  1.000 35.87814  ? 207 SER B CA   1 
ATOM   6745 C C    . SER B 1 221 ? -15.59445 -35.48340 5.40299  1.000 32.94652  ? 207 SER B C    1 
ATOM   6746 O O    . SER B 1 221 ? -15.30658 -35.66806 6.58946  1.000 32.33444  ? 207 SER B O    1 
ATOM   6747 C CB   . SER B 1 221 ? -14.49992 -34.44523 3.35503  1.000 30.77623  ? 207 SER B CB   1 
ATOM   6748 O OG   . SER B 1 221 ? -13.20558 -34.98445 3.55530  1.000 32.66387  ? 207 SER B OG   1 
ATOM   6749 H H    . SER B 1 221 ? -13.90523 -33.90920 6.13724  1.000 37.80224  ? 207 SER B H    1 
ATOM   6750 H HA   . SER B 1 221 ? -16.01537 -33.68477 4.51509  1.000 43.10971  ? 207 SER B HA   1 
ATOM   6751 H HB2  . SER B 1 221 ? -15.02544 -35.07365 2.83558  1.000 36.98741  ? 207 SER B HB2  1 
ATOM   6752 H HB3  . SER B 1 221 ? -14.42000 -33.60493 2.87711  1.000 36.98741  ? 207 SER B HB3  1 
ATOM   6753 H HG   . SER B 1 221 ? -13.23717 -35.60499 4.12057  1.000 39.25258  ? 207 SER B HG   1 
ATOM   6754 N N    . LYS B 1 222 ? -16.25345 -36.38139 4.67278  1.000 34.09040  ? 208 LYS B N    1 
ATOM   6755 C CA   . LYS B 1 222 ? -16.72618 -37.64131 5.22262  1.000 32.45373  ? 208 LYS B CA   1 
ATOM   6756 C C    . LYS B 1 222 ? -16.28636 -38.80083 4.34038  1.000 30.17000  ? 208 LYS B C    1 
ATOM   6757 O O    . LYS B 1 222 ? -16.05215 -38.64118 3.13891  1.000 33.13532  ? 208 LYS B O    1 
ATOM   6758 C CB   . LYS B 1 222 ? -18.25716 -37.65972 5.35639  1.000 32.65676  ? 208 LYS B CB   1 
ATOM   6759 C CG   . LYS B 1 222 ? -18.82172 -36.65509 6.34495  1.000 32.03010  ? 208 LYS B CG   1 
ATOM   6760 C CD   . LYS B 1 222 ? -18.37608 -36.95433 7.77079  1.000 28.02212  ? 208 LYS B CD   1 
ATOM   6761 C CE   . LYS B 1 222 ? -19.15868 -36.12543 8.77432  1.000 31.84986  ? 208 LYS B CE   1 
ATOM   6762 N NZ   . LYS B 1 222 ? -18.56105 -36.16999 10.13714 1.000 35.37284  ? 208 LYS B NZ   1 
ATOM   6763 H H    . LYS B 1 222 ? -16.44059 -36.27762 3.83983  1.000 40.96442  ? 208 LYS B H    1 
ATOM   6764 H HA   . LYS B 1 222 ? -16.33436 -37.76526 6.10126  1.000 39.00042  ? 208 LYS B HA   1 
ATOM   6765 H HB2  . LYS B 1 222 ? -18.64433 -37.46445 4.48871  1.000 39.24405  ? 208 LYS B HB2  1 
ATOM   6766 H HB3  . LYS B 1 222 ? -18.52987 -38.54302 5.65017  1.000 39.24405  ? 208 LYS B HB3  1 
ATOM   6767 H HG2  . LYS B 1 222 ? -18.51242 -35.76619 6.11024  1.000 38.49206  ? 208 LYS B HG2  1 
ATOM   6768 H HG3  . LYS B 1 222 ? -19.79076 -36.68746 6.31643  1.000 38.49206  ? 208 LYS B HG3  1 
ATOM   6769 H HD2  . LYS B 1 222 ? -18.52576 -37.89274 7.96546  1.000 33.68248  ? 208 LYS B HD2  1 
ATOM   6770 H HD3  . LYS B 1 222 ? -17.43443 -36.74186 7.86591  1.000 33.68248  ? 208 LYS B HD3  1 
ATOM   6771 H HE2  . LYS B 1 222 ? -19.17143 -35.20085 8.48125  1.000 38.27577  ? 208 LYS B HE2  1 
ATOM   6772 H HE3  . LYS B 1 222 ? -20.06442 -36.46788 8.83142  1.000 38.27577  ? 208 LYS B HE3  1 
ATOM   6773 H HZ1  . LYS B 1 222 ? -18.62308 -36.99308 10.46996 1.000 42.50335  ? 208 LYS B HZ1  1 
ATOM   6774 H HZ2  . LYS B 1 222 ? -17.70285 -35.93699 10.10095 1.000 42.50335  ? 208 LYS B HZ2  1 
ATOM   6775 H HZ3  . LYS B 1 222 ? -18.99063 -35.60723 10.67646 1.000 42.50335  ? 208 LYS B HZ3  1 
ATOM   6776 N N    . ASP B 1 223 ? -16.17566 -39.97388 4.96499  1.000 29.67530  ? 209 ASP B N    1 
ATOM   6777 C CA   . ASP B 1 223 ? -15.89878 -41.22143 4.26987  1.000 33.22381  ? 209 ASP B CA   1 
ATOM   6778 C C    . ASP B 1 223 ? -17.20006 -41.98872 4.10227  1.000 33.21451  ? 209 ASP B C    1 
ATOM   6779 O O    . ASP B 1 223 ? -17.82513 -42.34445 5.11393  1.000 31.06576  ? 209 ASP B O    1 
ATOM   6780 C CB   . ASP B 1 223 ? -14.89154 -42.05158 5.05931  1.000 34.23971  ? 209 ASP B CB   1 
ATOM   6781 C CG   . ASP B 1 223 ? -14.51281 -43.34223 4.35784  1.000 35.51937  ? 209 ASP B CG   1 
ATOM   6782 O OD1  . ASP B 1 223 ? -15.07702 -43.63515 3.28404  1.000 43.08000  ? 209 ASP B OD1  1 
ATOM   6783 O OD2  . ASP B 1 223 ? -13.64178 -44.06504 4.88406  1.000 35.86538  ? 209 ASP B OD2  1 
ATOM   6784 H H    . ASP B 1 223 ? -16.25982 -40.07199 5.81522  1.000 35.66630  ? 209 ASP B H    1 
ATOM   6785 H HA   . ASP B 1 223 ? -15.52673 -41.04009 3.39260  1.000 39.92451  ? 209 ASP B HA   1 
ATOM   6786 H HB2  . ASP B 1 223 ? -14.08296 -41.53078 5.18529  1.000 41.14359  ? 209 ASP B HB2  1 
ATOM   6787 H HB3  . ASP B 1 223 ? -15.27635 -42.28021 5.91986  1.000 41.14359  ? 209 ASP B HB3  1 
ATOM   6788 N N    . PRO B 1 224 ? -17.65499 -42.26711 2.87571  1.000 31.71820  ? 210 PRO B N    1 
ATOM   6789 C CA   . PRO B 1 224 ? -18.95230 -42.94591 2.71934  1.000 37.62467  ? 210 PRO B CA   1 
ATOM   6790 C C    . PRO B 1 224 ? -18.95878 -44.37714 3.22324  1.000 38.52020  ? 210 PRO B C    1 
ATOM   6791 O O    . PRO B 1 224 ? -20.04347 -44.93078 3.44169  1.000 40.75667  ? 210 PRO B O    1 
ATOM   6792 C CB   . PRO B 1 224 ? -19.20032 -42.88754 1.20608  1.000 38.07110  ? 210 PRO B CB   1 
ATOM   6793 C CG   . PRO B 1 224 ? -17.83731 -42.80584 0.60854  1.000 38.17763  ? 210 PRO B CG   1 
ATOM   6794 C CD   . PRO B 1 224 ? -17.01917 -41.99101 1.57504  1.000 33.15073  ? 210 PRO B CD   1 
ATOM   6795 H HA   . PRO B 1 224 ? -19.64500 -42.44490 3.17766  1.000 45.20555  ? 210 PRO B HA   1 
ATOM   6796 H HB2  . PRO B 1 224 ? -19.66217 -43.68891 0.91385  1.000 45.74127  ? 210 PRO B HB2  1 
ATOM   6797 H HB3  . PRO B 1 224 ? -19.72585 -42.10265 0.98547  1.000 45.74127  ? 210 PRO B HB3  1 
ATOM   6798 H HG2  . PRO B 1 224 ? -17.46788 -43.69741 0.51090  1.000 45.86909  ? 210 PRO B HG2  1 
ATOM   6799 H HG3  . PRO B 1 224 ? -17.88390 -42.36946 -0.25650 1.000 45.86909  ? 210 PRO B HG3  1 
ATOM   6800 H HD2  . PRO B 1 224 ? -16.09382 -42.28193 1.57461  1.000 39.83681  ? 210 PRO B HD2  1 
ATOM   6801 H HD3  . PRO B 1 224 ? -17.07012 -41.04661 1.35959  1.000 39.83681  ? 210 PRO B HD3  1 
ATOM   6802 N N    . ASN B 1 225 ? -17.79455 -44.99417 3.40939  1.000 34.33612  ? 211 ASN B N    1 
ATOM   6803 C CA   . ASN B 1 225 ? -17.71508 -46.35350 3.92392  1.000 40.72809  ? 211 ASN B CA   1 
ATOM   6804 C C    . ASN B 1 225 ? -17.59183 -46.41242 5.44168  1.000 36.49034  ? 211 ASN B C    1 
ATOM   6805 O O    . ASN B 1 225 ? -17.72154 -47.49942 6.01455  1.000 38.64077  ? 211 ASN B O    1 
ATOM   6806 C CB   . ASN B 1 225 ? -16.52507 -47.08118 3.29118  1.000 40.40262  ? 211 ASN B CB   1 
ATOM   6807 C CG   . ASN B 1 225 ? -16.64410 -47.19066 1.78394  1.000 49.84611  ? 211 ASN B CG   1 
ATOM   6808 O OD1  . ASN B 1 225 ? -17.70726 -47.51735 1.25396  1.000 46.12584  ? 211 ASN B OD1  1 
ATOM   6809 N ND2  . ASN B 1 225 ? -15.55147 -46.90912 1.08360  1.000 56.77433  ? 211 ASN B ND2  1 
ATOM   6810 H H    . ASN B 1 225 ? -17.02872 -44.64032 3.24241  1.000 41.25928  ? 211 ASN B H    1 
ATOM   6811 H HA   . ASN B 1 225 ? -18.52448 -46.82717 3.67614  1.000 48.92964  ? 211 ASN B HA   1 
ATOM   6812 H HB2  . ASN B 1 225 ? -15.71141 -46.59357 3.49389  1.000 48.53908  ? 211 ASN B HB2  1 
ATOM   6813 H HB3  . ASN B 1 225 ? -16.47309 -47.97899 3.65468  1.000 48.53908  ? 211 ASN B HB3  1 
ATOM   6814 H HD21 . ASN B 1 225 ? -15.56699 -46.95634 0.22504  1.000 68.18513  ? 211 ASN B HD21 1 
ATOM   6815 H HD22 . ASN B 1 225 ? -14.82838 -46.67957 1.48863  1.000 68.18513  ? 211 ASN B HD22 1 
ATOM   6816 N N    . GLU B 1 226 ? -17.35089 -45.28303 6.10308  1.000 31.64412  ? 212 GLU B N    1 
ATOM   6817 C CA   . GLU B 1 226 ? -17.18024 -45.24904 7.55038  1.000 31.86306  ? 212 GLU B CA   1 
ATOM   6818 C C    . GLU B 1 226 ? -18.54215 -45.09562 8.21722  1.000 29.54818  ? 212 GLU B C    1 
ATOM   6819 O O    . GLU B 1 226 ? -19.24865 -44.11018 7.97963  1.000 39.01950  ? 212 GLU B O    1 
ATOM   6820 C CB   . GLU B 1 226 ? -16.24850 -44.10735 7.95414  1.000 28.15543  ? 212 GLU B CB   1 
ATOM   6821 C CG   . GLU B 1 226 ? -16.09407 -43.94073 9.45429  1.000 32.08999  ? 212 GLU B CG   1 
ATOM   6822 C CD   . GLU B 1 226 ? -15.67976 -45.22674 10.14066 1.000 26.64967  ? 212 GLU B CD   1 
ATOM   6823 O OE1  . GLU B 1 226 ? -14.61792 -45.77612 9.78683  1.000 23.04015  ? 212 GLU B OE1  1 
ATOM   6824 O OE2  . GLU B 1 226 ? -16.42487 -45.69109 11.02538 1.000 28.82684  ? 212 GLU B OE2  1 
ATOM   6825 H H    . GLU B 1 226 ? -17.28095 -44.51201 5.72860  1.000 38.02889  ? 212 GLU B H    1 
ATOM   6826 H HA   . GLU B 1 226 ? -16.78735 -46.08416 7.84890  1.000 38.29161  ? 212 GLU B HA   1 
ATOM   6827 H HB2  . GLU B 1 226 ? -15.36844 -44.27811 7.58368  1.000 33.84245  ? 212 GLU B HB2  1 
ATOM   6828 H HB3  . GLU B 1 226 ? -16.60229 -43.27673 7.59947  1.000 33.84245  ? 212 GLU B HB3  1 
ATOM   6829 H HG2  . GLU B 1 226 ? -15.41348 -43.27247 9.63076  1.000 38.56393  ? 212 GLU B HG2  1 
ATOM   6830 H HG3  . GLU B 1 226 ? -16.94209 -43.65809 9.83095  1.000 38.56393  ? 212 GLU B HG3  1 
ATOM   6831 N N    . LYS B 1 227 ? -18.90239 -46.06532 9.05670  1.000 31.28219  ? 213 LYS B N    1 
ATOM   6832 C CA   . LYS B 1 227 ? -20.20463 -46.07576 9.70829  1.000 31.92950  ? 213 LYS B CA   1 
ATOM   6833 C C    . LYS B 1 227 ? -20.19534 -45.41770 11.08097 1.000 32.08126  ? 213 LYS B C    1 
ATOM   6834 O O    . LYS B 1 227 ? -21.26773 -45.08704 11.59892 1.000 34.26604  ? 213 LYS B O    1 
ATOM   6835 C CB   . LYS B 1 227 ? -20.70596 -47.51733 9.84268  1.000 38.50134  ? 213 LYS B CB   1 
ATOM   6836 C CG   . LYS B 1 227 ? -20.92423 -48.21665 8.51177  1.000 38.20952  ? 213 LYS B CG   1 
ATOM   6837 C CD   . LYS B 1 227 ? -21.19290 -49.70511 8.69825  1.000 40.92995  ? 213 LYS B CD   1 
ATOM   6838 C CE   . LYS B 1 227 ? -21.65507 -50.34971 7.40447  1.000 37.91589  ? 213 LYS B CE   1 
ATOM   6839 N NZ   . LYS B 1 227 ? -20.60604 -50.29902 6.35545  1.000 47.00694  ? 213 LYS B NZ   1 
ATOM   6840 H H    . LYS B 1 227 ? -18.40356 -46.73395 9.26575  1.000 37.59457  ? 213 LYS B H    1 
ATOM   6841 H HA   . LYS B 1 227 ? -20.83346 -45.58643 9.15509  1.000 38.37134  ? 213 LYS B HA   1 
ATOM   6842 H HB2  . LYS B 1 227 ? -20.05127 -48.02969 10.34244 1.000 46.25755  ? 213 LYS B HB2  1 
ATOM   6843 H HB3  . LYS B 1 227 ? -21.55281 -47.51001 10.31563 1.000 46.25755  ? 213 LYS B HB3  1 
ATOM   6844 H HG2  . LYS B 1 227 ? -21.68924 -47.82288 8.06389  1.000 45.90736  ? 213 LYS B HG2  1 
ATOM   6845 H HG3  . LYS B 1 227 ? -20.13079 -48.11685 7.96277  1.000 45.90736  ? 213 LYS B HG3  1 
ATOM   6846 H HD2  . LYS B 1 227 ? -20.37775 -50.14585 8.98492  1.000 49.17189  ? 213 LYS B HD2  1 
ATOM   6847 H HD3  . LYS B 1 227 ? -21.88730 -49.82579 9.36470  1.000 49.17189  ? 213 LYS B HD3  1 
ATOM   6848 H HE2  . LYS B 1 227 ? -21.87297 -51.28015 7.57095  1.000 45.55501  ? 213 LYS B HE2  1 
ATOM   6849 H HE3  . LYS B 1 227 ? -22.43691 -49.87975 7.07468  1.000 45.55501  ? 213 LYS B HE3  1 
ATOM   6850 H HZ1  . LYS B 1 227 ? -20.79464 -50.87988 5.70805  1.000 56.46427  ? 213 LYS B HZ1  1 
ATOM   6851 H HZ2  . LYS B 1 227 ? -20.56371 -49.48135 6.00656  1.000 56.46427  ? 213 LYS B HZ2  1 
ATOM   6852 H HZ3  . LYS B 1 227 ? -19.81442 -50.50463 6.70640  1.000 56.46427  ? 213 LYS B HZ3  1 
ATOM   6853 N N    . ARG B 1 228 ? -19.02598 -45.22287 11.68047 1.000 31.48283  ? 214 ARG B N    1 
ATOM   6854 C CA   . ARG B 1 228 ? -18.92541 -44.56018 12.97125 1.000 27.77460  ? 214 ARG B CA   1 
ATOM   6855 C C    . ARG B 1 228 ? -18.79816 -43.05492 12.78013 1.000 29.99107  ? 214 ARG B C    1 
ATOM   6856 O O    . ARG B 1 228 ? -18.28843 -42.57918 11.76233 1.000 33.23779  ? 214 ARG B O    1 
ATOM   6857 C CB   . ARG B 1 228 ? -17.72312 -45.08505 13.75948 1.000 26.83982  ? 214 ARG B CB   1 
ATOM   6858 C CG   . ARG B 1 228 ? -17.76101 -46.58164 14.02693 1.000 31.35696  ? 214 ARG B CG   1 
ATOM   6859 C CD   . ARG B 1 228 ? -16.55155 -47.04355 14.83159 1.000 29.54874  ? 214 ARG B CD   1 
ATOM   6860 N NE   . ARG B 1 228 ? -16.60045 -48.47446 15.11284 1.000 26.58181  ? 214 ARG B NE   1 
ATOM   6861 C CZ   . ARG B 1 228 ? -17.23437 -49.01864 16.14326 1.000 26.73812  ? 214 ARG B CZ   1 
ATOM   6862 N NH1  . ARG B 1 228 ? -17.86721 -48.27656 17.03797 1.000 30.95370  ? 214 ARG B NH1  1 
ATOM   6863 N NH2  . ARG B 1 228 ? -17.23640 -50.34147 16.27790 1.000 27.26913  ? 214 ARG B NH2  1 
ATOM   6864 H H    . ARG B 1 228 ? -18.26901 -45.46883 11.35473 1.000 37.83533  ? 214 ARG B H    1 
ATOM   6865 H HA   . ARG B 1 228 ? -19.72562 -44.73966 13.48927 1.000 33.38546  ? 214 ARG B HA   1 
ATOM   6866 H HB2  . ARG B 1 228 ? -16.91562 -44.89601 13.25639 1.000 32.26373  ? 214 ARG B HB2  1 
ATOM   6867 H HB3  . ARG B 1 228 ? -17.69304 -44.63313 14.61725 1.000 32.26373  ? 214 ARG B HB3  1 
ATOM   6868 H HG2  . ARG B 1 228 ? -18.56126 -46.79662 14.53120 1.000 37.68429  ? 214 ARG B HG2  1 
ATOM   6869 H HG3  . ARG B 1 228 ? -17.76340 -47.05794 13.18193 1.000 37.68429  ? 214 ARG B HG3  1 
ATOM   6870 H HD2  . ARG B 1 228 ? -15.74331 -46.86074 14.32737 1.000 35.51443  ? 214 ARG B HD2  1 
ATOM   6871 H HD3  . ARG B 1 228 ? -16.52969 -46.56858 15.67707 1.000 35.51443  ? 214 ARG B HD3  1 
ATOM   6872 H HE   . ARG B 1 228 ? -16.18932 -49.00227 14.57249 1.000 31.95411  ? 214 ARG B HE   1 
ATOM   6873 H HH11 . ARG B 1 228 ? -18.27171 -48.65071 17.69827 1.000 37.20038  ? 214 ARG B HH11 1 
ATOM   6874 H HH12 . ARG B 1 228 ? -17.87393 -47.42022 16.95905 1.000 37.20038  ? 214 ARG B HH12 1 
ATOM   6875 H HH21 . ARG B 1 228 ? -16.83007 -50.83304 15.70097 1.000 32.77890  ? 214 ARG B HH21 1 
ATOM   6876 H HH22 . ARG B 1 228 ? -17.64405 -50.70548 16.94192 1.000 32.77890  ? 214 ARG B HH22 1 
ATOM   6877 N N    . ASP B 1 229 ? -19.28120 -42.30460 13.76704 1.000 34.67885  ? 215 ASP B N    1 
ATOM   6878 C CA   . ASP B 1 229 ? -19.05645 -40.86620 13.78003 1.000 34.77913  ? 215 ASP B CA   1 
ATOM   6879 C C    . ASP B 1 229 ? -17.57106 -40.59618 13.58111 1.000 36.01951  ? 215 ASP B C    1 
ATOM   6880 O O    . ASP B 1 229 ? -16.72807 -41.14363 14.29735 1.000 31.63229  ? 215 ASP B O    1 
ATOM   6881 C CB   . ASP B 1 229 ? -19.54725 -40.27073 15.09947 1.000 32.42921  ? 215 ASP B CB   1 
ATOM   6882 C CG   . ASP B 1 229 ? -19.92530 -38.80462 14.97823 1.000 39.66366  ? 215 ASP B CG   1 
ATOM   6883 O OD1  . ASP B 1 229 ? -19.87038 -38.25527 13.85530 1.000 30.94168  ? 215 ASP B OD1  1 
ATOM   6884 O OD2  . ASP B 1 229 ? -20.28321 -38.20293 16.01294 1.000 39.42299  ? 215 ASP B OD2  1 
ATOM   6885 H H    . ASP B 1 229 ? -19.73706 -42.60243 14.43269 1.000 41.67056  ? 215 ASP B H    1 
ATOM   6886 H HA   . ASP B 1 229 ? -19.55575 -40.43626 13.06816 1.000 41.79090  ? 215 ASP B HA   1 
ATOM   6887 H HB2  . ASP B 1 229 ? -20.33165 -40.75929 15.39431 1.000 38.97099  ? 215 ASP B HB2  1 
ATOM   6888 H HB3  . ASP B 1 229 ? -18.84205 -40.34484 15.76136 1.000 38.97099  ? 215 ASP B HB3  1 
ATOM   6889 N N    . HIS B 1 230 ? -17.25067 -39.76941 12.58918 1.000 28.71992  ? 216 HIS B N    1 
ATOM   6890 C CA   . HIS B 1 230 ? -15.87598 -39.66286 12.12324 1.000 30.70530  ? 216 HIS B CA   1 
ATOM   6891 C C    . HIS B 1 230 ? -15.66015 -38.31402 11.45549 1.000 27.32535  ? 216 HIS B C    1 
ATOM   6892 O O    . HIS B 1 230 ? -16.60053 -37.55167 11.22079 1.000 26.25985  ? 216 HIS B O    1 
ATOM   6893 C CB   . HIS B 1 230 ? -15.55001 -40.78324 11.13731 1.000 28.77494  ? 216 HIS B CB   1 
ATOM   6894 C CG   . HIS B 1 230 ? -16.32865 -40.69077 9.86492  1.000 25.09300  ? 216 HIS B CG   1 
ATOM   6895 N ND1  . HIS B 1 230 ? -17.68102 -40.94753 9.80376  1.000 29.38445  ? 216 HIS B ND1  1 
ATOM   6896 C CD2  . HIS B 1 230 ? -15.95238 -40.35035 8.61022  1.000 30.78460  ? 216 HIS B CD2  1 
ATOM   6897 C CE1  . HIS B 1 230 ? -18.10260 -40.78072 8.56348  1.000 30.34625  ? 216 HIS B CE1  1 
ATOM   6898 N NE2  . HIS B 1 230 ? -17.07402 -40.41592 7.82016  1.000 27.45470  ? 216 HIS B NE2  1 
ATOM   6899 H H    . HIS B 1 230 ? -17.80913 -39.26402 12.17409 1.000 34.51985  ? 216 HIS B H    1 
ATOM   6900 H HA   . HIS B 1 230 ? -15.28881 -39.71576 12.89352 1.000 36.90230  ? 216 HIS B HA   1 
ATOM   6901 H HB2  . HIS B 1 230 ? -14.60698 -40.74100 10.91414 1.000 34.58587  ? 216 HIS B HB2  1 
ATOM   6902 H HB3  . HIS B 1 230 ? -15.75501 -41.63600 11.55164 1.000 34.58587  ? 216 HIS B HB3  1 
ATOM   6903 H HD1  . HIS B 1 230 ? -18.17356 -41.18007 10.46928 1.000 35.31728  ? 216 HIS B HD1  1 
ATOM   6904 H HD2  . HIS B 1 230 ? -15.09555 -40.11609 8.33480  1.000 36.99746  ? 216 HIS B HD2  1 
ATOM   6905 H HE1  . HIS B 1 230 ? -18.97514 -40.89985 8.26451  1.000 36.47145  ? 216 HIS B HE1  1 
ATOM   6906 N N    . MET B 1 231 ? -14.39797 -38.04925 11.12164 1.000 28.81015  ? 217 MET B N    1 
ATOM   6907 C CA   . MET B 1 231 ? -14.01515 -36.83066 10.41780 1.000 30.06692  ? 217 MET B CA   1 
ATOM   6908 C C    . MET B 1 231 ? -12.80751 -37.13481 9.54685  1.000 28.87526  ? 217 MET B C    1 
ATOM   6909 O O    . MET B 1 231 ? -11.77065 -37.57135 10.05447 1.000 25.61871  ? 217 MET B O    1 
ATOM   6910 C CB   . MET B 1 231 ? -13.69180 -35.69977 11.39772 1.000 29.38949  ? 217 MET B CB   1 
ATOM   6911 C CG   . MET B 1 231 ? -13.11656 -34.45126 10.73304 1.000 28.92559  ? 217 MET B CG   1 
ATOM   6912 S SD   . MET B 1 231 ? -12.82972 -33.08726 11.88177 1.000 28.42365  ? 217 MET B SD   1 
ATOM   6913 C CE   . MET B 1 231 ? -11.43387 -33.70696 12.81642 1.000 25.72541  ? 217 MET B CE   1 
ATOM   6914 H H    . MET B 1 231 ? -13.73529 -38.56918 11.29520 1.000 34.62813  ? 217 MET B H    1 
ATOM   6915 H HA   . MET B 1 231 ? -14.75508 -36.54578 9.85901  1.000 36.13625  ? 217 MET B HA   1 
ATOM   6916 H HB2  . MET B 1 231 ? -14.50718 -35.44188 11.85548 1.000 35.32333  ? 217 MET B HB2  1 
ATOM   6917 H HB3  . MET B 1 231 ? -13.03865 -36.02079 12.03900 1.000 35.32333  ? 217 MET B HB3  1 
ATOM   6918 H HG2  . MET B 1 231 ? -12.26670 -34.67800 10.32409 1.000 34.76665  ? 217 MET B HG2  1 
ATOM   6919 H HG3  . MET B 1 231 ? -13.73870 -34.14257 10.05588 1.000 34.76665  ? 217 MET B HG3  1 
ATOM   6920 H HE1  . MET B 1 231 ? -11.66938 -34.56401 13.20488 1.000 30.92643  ? 217 MET B HE1  1 
ATOM   6921 H HE2  . MET B 1 231 ? -10.67582 -33.81111 12.22025 1.000 30.92643  ? 217 MET B HE2  1 
ATOM   6922 H HE3  . MET B 1 231 ? -11.21783 -33.07366 13.51867 1.000 30.92643  ? 217 MET B HE3  1 
ATOM   6923 N N    . VAL B 1 232 ? -12.94540 -36.91557 8.24965  1.000 30.03009  ? 218 VAL B N    1 
ATOM   6924 C CA   . VAL B 1 232 ? -11.81321 -36.92153 7.33250  1.000 31.86589  ? 218 VAL B CA   1 
ATOM   6925 C C    . VAL B 1 232 ? -11.25699 -35.50781 7.28015  1.000 29.46938  ? 218 VAL B C    1 
ATOM   6926 O O    . VAL B 1 232 ? -12.01269 -34.53224 7.20088  1.000 32.67345  ? 218 VAL B O    1 
ATOM   6927 C CB   . VAL B 1 232 ? -12.23301 -37.42120 5.93995  1.000 31.15364  ? 218 VAL B CB   1 
ATOM   6928 C CG1  . VAL B 1 232 ? -11.08391 -37.27349 4.95481  1.000 36.30938  ? 218 VAL B CG1  1 
ATOM   6929 C CG2  . VAL B 1 232 ? -12.69876 -38.86827 6.02082  1.000 31.16220  ? 218 VAL B CG2  1 
ATOM   6930 H H    . VAL B 1 232 ? -13.69908 -36.75752 7.86677  1.000 36.09205  ? 218 VAL B H    1 
ATOM   6931 H HA   . VAL B 1 232 ? -11.12387 -37.52142 7.65785  1.000 38.29501  ? 218 VAL B HA   1 
ATOM   6932 H HB   . VAL B 1 232 ? -12.97281 -36.88378 5.61624  1.000 37.44030  ? 218 VAL B HB   1 
ATOM   6933 H HG11 . VAL B 1 232 ? -11.29465 -37.76795 4.14735  1.000 43.62720  ? 218 VAL B HG11 1 
ATOM   6934 H HG12 . VAL B 1 232 ? -10.96591 -36.33364 4.74586  1.000 43.62720  ? 218 VAL B HG12 1 
ATOM   6935 H HG13 . VAL B 1 232 ? -10.27529 -37.62687 5.35752  1.000 43.62720  ? 218 VAL B HG13 1 
ATOM   6936 H HG21 . VAL B 1 232 ? -12.56034 -39.19458 6.92373  1.000 37.45058  ? 218 VAL B HG21 1 
ATOM   6937 H HG22 . VAL B 1 232 ? -13.64118 -38.90979 5.79493  1.000 37.45058  ? 218 VAL B HG22 1 
ATOM   6938 H HG23 . VAL B 1 232 ? -12.18461 -39.40099 5.39411  1.000 37.45058  ? 218 VAL B HG23 1 
ATOM   6939 N N    . PHE B 1 233 ? -9.93286  -35.39024 7.32550  1.000 27.77698  ? 219 PHE B N    1 
ATOM   6940 C CA   . PHE B 1 233 ? -9.28642  -34.12180 7.63870  1.000 28.46568  ? 219 PHE B CA   1 
ATOM   6941 C C    . PHE B 1 233 ? -8.07309  -33.92913 6.74525  1.000 32.57571  ? 219 PHE B C    1 
ATOM   6942 O O    . PHE B 1 233 ? -7.17646  -34.77794 6.71815  1.000 29.52878  ? 219 PHE B O    1 
ATOM   6943 C CB   . PHE B 1 233 ? -8.89126  -34.09215 9.12018  1.000 34.36998  ? 219 PHE B CB   1 
ATOM   6944 C CG   . PHE B 1 233 ? -8.19797  -32.83490 9.54775  1.000 32.16318  ? 219 PHE B CG   1 
ATOM   6945 C CD1  . PHE B 1 233 ? -8.91566  -31.67522 9.77557  1.000 32.93383  ? 219 PHE B CD1  1 
ATOM   6946 C CD2  . PHE B 1 233 ? -6.82912  -32.82071 9.74726  1.000 35.58278  ? 219 PHE B CD2  1 
ATOM   6947 C CE1  . PHE B 1 233 ? -8.27935  -30.52081 10.17594 1.000 31.08703  ? 219 PHE B CE1  1 
ATOM   6948 C CE2  . PHE B 1 233 ? -6.18838  -31.66961 10.15163 1.000 34.45169  ? 219 PHE B CE2  1 
ATOM   6949 C CZ   . PHE B 1 233 ? -6.91608  -30.51816 10.36832 1.000 32.54055  ? 219 PHE B CZ   1 
ATOM   6950 H H    . PHE B 1 233 ? -9.38460  -36.03604 7.17736  1.000 33.38831  ? 219 PHE B H    1 
ATOM   6951 H HA   . PHE B 1 233 ? -9.89231  -33.38776 7.45167  1.000 34.21475  ? 219 PHE B HA   1 
ATOM   6952 H HB2  . PHE B 1 233 ? -9.69423  -34.18199 9.65690  1.000 41.29991  ? 219 PHE B HB2  1 
ATOM   6953 H HB3  . PHE B 1 233 ? -8.29040  -34.83319 9.29549  1.000 41.29991  ? 219 PHE B HB3  1 
ATOM   6954 H HD1  . PHE B 1 233 ? -9.83810  -31.67452 9.65722  1.000 39.57653  ? 219 PHE B HD1  1 
ATOM   6955 H HD2  . PHE B 1 233 ? -6.33587  -33.59655 9.60695  1.000 42.75528  ? 219 PHE B HD2  1 
ATOM   6956 H HE1  . PHE B 1 233 ? -8.77045  -29.74361 10.31621 1.000 37.36038  ? 219 PHE B HE1  1 
ATOM   6957 H HE2  . PHE B 1 233 ? -5.26703  -31.66918 10.27817 1.000 41.39797  ? 219 PHE B HE2  1 
ATOM   6958 H HZ   . PHE B 1 233 ? -6.48637  -29.74085 10.64407 1.000 39.10459  ? 219 PHE B HZ   1 
ATOM   6959 N N    . LEU B 1 234 ? -8.06108  -32.81989 6.00688  1.000 28.89696  ? 220 LEU B N    1 
ATOM   6960 C CA   . LEU B 1 234 ? -6.91106  -32.37793 5.22827  1.000 30.73089  ? 220 LEU B CA   1 
ATOM   6961 C C    . LEU B 1 234 ? -6.53597  -30.97148 5.67224  1.000 38.42749  ? 220 LEU B C    1 
ATOM   6962 O O    . LEU B 1 234 ? -7.40765  -30.10421 5.79739  1.000 38.65170  ? 220 LEU B O    1 
ATOM   6963 C CB   . LEU B 1 234 ? -7.21314  -32.38940 3.72821  1.000 30.23153  ? 220 LEU B CB   1 
ATOM   6964 C CG   . LEU B 1 234 ? -6.16669  -31.74462 2.81243  1.000 33.06496  ? 220 LEU B CG   1 
ATOM   6965 C CD1  . LEU B 1 234 ? -4.94413  -32.63548 2.65991  1.000 39.45199  ? 220 LEU B CD1  1 
ATOM   6966 C CD2  . LEU B 1 234 ? -6.77577  -31.42736 1.45677  1.000 39.25641  ? 220 LEU B CD2  1 
ATOM   6967 H H    . LEU B 1 234 ? -8.73417  -32.28873 5.94046  1.000 34.73229  ? 220 LEU B H    1 
ATOM   6968 H HA   . LEU B 1 234 ? -6.16149  -32.97243 5.38835  1.000 36.93300  ? 220 LEU B HA   1 
ATOM   6969 H HB2  . LEU B 1 234 ? -7.30600  -33.31336 3.44791  1.000 36.33378  ? 220 LEU B HB2  1 
ATOM   6970 H HB3  . LEU B 1 234 ? -8.04685  -31.91430 3.58641  1.000 36.33378  ? 220 LEU B HB3  1 
ATOM   6971 H HG   . LEU B 1 234 ? -5.87004  -30.91359 3.21528  1.000 39.73390  ? 220 LEU B HG   1 
ATOM   6972 H HD11 . LEU B 1 234 ? -4.63863  -32.90585 3.53995  1.000 47.39833  ? 220 LEU B HD11 1 
ATOM   6973 H HD12 . LEU B 1 234 ? -5.18602  -33.41724 2.13912  1.000 47.39833  ? 220 LEU B HD12 1 
ATOM   6974 H HD13 . LEU B 1 234 ? -4.24591  -32.13847 2.20563  1.000 47.39833  ? 220 LEU B HD13 1 
ATOM   6975 H HD21 . LEU B 1 234 ? -6.10816  -30.99056 0.90504  1.000 47.16363  ? 220 LEU B HD21 1 
ATOM   6976 H HD22 . LEU B 1 234 ? -7.06173  -32.25412 1.03775  1.000 47.16363  ? 220 LEU B HD22 1 
ATOM   6977 H HD23 . LEU B 1 234 ? -7.53712  -30.83960 1.58238  1.000 47.16363  ? 220 LEU B HD23 1 
ATOM   6978 N N    . GLU B 1 235 ? -5.24193  -30.74198 5.88589  1.000 35.66325  ? 221 GLU B N    1 
ATOM   6979 C CA   . GLU B 1 235 ? -4.75770  -29.46934 6.39713  1.000 31.09797  ? 221 GLU B CA   1 
ATOM   6980 C C    . GLU B 1 235 ? -3.44275  -29.10503 5.72868  1.000 35.00808  ? 221 GLU B C    1 
ATOM   6981 O O    . GLU B 1 235 ? -2.59738  -29.96979 5.48136  1.000 30.00681  ? 221 GLU B O    1 
ATOM   6982 C CB   . GLU B 1 235 ? -4.56124  -29.52131 7.92052  1.000 32.97012  ? 221 GLU B CB   1 
ATOM   6983 C CG   . GLU B 1 235 ? -4.08655  -28.21481 8.54264  1.000 32.26827  ? 221 GLU B CG   1 
ATOM   6984 C CD   . GLU B 1 235 ? -3.61917  -28.37182 9.98284  1.000 39.90480  ? 221 GLU B CD   1 
ATOM   6985 O OE1  . GLU B 1 235 ? -4.06024  -29.32014 10.66650 1.000 40.78196  ? 221 GLU B OE1  1 
ATOM   6986 O OE2  . GLU B 1 235 ? -2.80168  -27.54083 10.43205 1.000 48.88887  ? 221 GLU B OE2  1 
ATOM   6987 H H    . GLU B 1 235 ? -4.61975  -31.31734 5.73941  1.000 42.85184  ? 221 GLU B H    1 
ATOM   6988 H HA   . GLU B 1 235 ? -5.40301  -28.77671 6.18561  1.000 37.37350  ? 221 GLU B HA   1 
ATOM   6989 H HB2  . GLU B 1 235 ? -5.40837  -29.75125 8.33330  1.000 39.62009  ? 221 GLU B HB2  1 
ATOM   6990 H HB3  . GLU B 1 235 ? -3.89839  -30.19986 8.12327  1.000 39.62009  ? 221 GLU B HB3  1 
ATOM   6991 H HG2  . GLU B 1 235 ? -3.34258  -27.87139 8.02353  1.000 38.77786  ? 221 GLU B HG2  1 
ATOM   6992 H HG3  . GLU B 1 235 ? -4.81856  -27.57841 8.53447  1.000 38.77786  ? 221 GLU B HG3  1 
ATOM   6993 N N    . PHE B 1 236 ? -3.28194  -27.81619 5.44297  1.000 29.68008  ? 222 PHE B N    1 
ATOM   6994 C CA   . PHE B 1 236 ? -2.02249  -27.24819 4.98127  1.000 32.83281  ? 222 PHE B CA   1 
ATOM   6995 C C    . PHE B 1 236 ? -1.63261  -26.14358 5.95199  1.000 31.15520  ? 222 PHE B C    1 
ATOM   6996 O O    . PHE B 1 236 ? -2.38384  -25.17925 6.13368  1.000 34.30114  ? 222 PHE B O    1 
ATOM   6997 C CB   . PHE B 1 236 ? -2.14445  -26.71319 3.55311  1.000 31.10000  ? 222 PHE B CB   1 
ATOM   6998 C CG   . PHE B 1 236 ? -2.18676  -27.79190 2.50546  1.000 36.51585  ? 222 PHE B CG   1 
ATOM   6999 C CD1  . PHE B 1 236 ? -1.01924  -28.40167 2.07619  1.000 36.17879  ? 222 PHE B CD1  1 
ATOM   7000 C CD2  . PHE B 1 236 ? -3.39057  -28.19630 1.95084  1.000 38.83806  ? 222 PHE B CD2  1 
ATOM   7001 C CE1  . PHE B 1 236 ? -1.04993  -29.39267 1.11352  1.000 39.43994  ? 222 PHE B CE1  1 
ATOM   7002 C CE2  . PHE B 1 236 ? -3.42731  -29.18816 0.98548  1.000 40.74505  ? 222 PHE B CE2  1 
ATOM   7003 C CZ   . PHE B 1 236 ? -2.25491  -29.78714 0.56837  1.000 40.81601  ? 222 PHE B CZ   1 
ATOM   7004 H H    . PHE B 1 236 ? -3.91015  -27.23289 5.51170  1.000 35.67203  ? 222 PHE B H    1 
ATOM   7005 H HA   . PHE B 1 236 ? -1.32776  -27.92512 4.97987  1.000 39.45531  ? 222 PHE B HA   1 
ATOM   7006 H HB2  . PHE B 1 236 ? -2.96333  -26.19821 3.48151  1.000 37.37594  ? 222 PHE B HB2  1 
ATOM   7007 H HB3  . PHE B 1 236 ? -1.37925  -26.14743 3.36526  1.000 37.37594  ? 222 PHE B HB3  1 
ATOM   7008 H HD1  . PHE B 1 236 ? -0.20434  -28.14075 2.44055  1.000 43.47049  ? 222 PHE B HD1  1 
ATOM   7009 H HD2  . PHE B 1 236 ? -4.18268  -27.79700 2.23017  1.000 46.66161  ? 222 PHE B HD2  1 
ATOM   7010 H HE1  . PHE B 1 236 ? -0.25899  -29.79357 0.83317  1.000 47.38386  ? 222 PHE B HE1  1 
ATOM   7011 H HE2  . PHE B 1 236 ? -4.24047  -29.45070 0.61840  1.000 48.95000  ? 222 PHE B HE2  1 
ATOM   7012 H HZ   . PHE B 1 236 ? -2.27733  -30.45492 -0.07852 1.000 49.03516  ? 222 PHE B HZ   1 
ATOM   7013 N N    . VAL B 1 237 ? -0.47381  -26.29489 6.58639  1.000 29.40407  ? 223 VAL B N    1 
ATOM   7014 C CA   . VAL B 1 237 ? -0.01005  -25.37633 7.61837  1.000 30.73417  ? 223 VAL B CA   1 
ATOM   7015 C C    . VAL B 1 237 ? 1.41365   -24.95472 7.28232  1.000 32.70367  ? 223 VAL B C    1 
ATOM   7016 O O    . VAL B 1 237 ? 2.27967   -25.80494 7.04744  1.000 35.57794  ? 223 VAL B O    1 
ATOM   7017 C CB   . VAL B 1 237 ? -0.08378  -26.01642 9.01947  1.000 30.38895  ? 223 VAL B CB   1 
ATOM   7018 C CG1  . VAL B 1 237 ? 0.55157   -27.40260 9.01393  1.000 33.60988  ? 223 VAL B CG1  1 
ATOM   7019 C CG2  . VAL B 1 237 ? 0.57507   -25.11540 10.05396 1.000 33.35863  ? 223 VAL B CG2  1 
ATOM   7020 H H    . VAL B 1 237 ? 0.07427   -26.93921 6.43129  1.000 35.34082  ? 223 VAL B H    1 
ATOM   7021 H HA   . VAL B 1 237 ? -0.56352  -24.57974 7.61963  1.000 36.93695  ? 223 VAL B HA   1 
ATOM   7022 H HB   . VAL B 1 237 ? -1.01574  -26.12117 9.26719  1.000 36.52268  ? 223 VAL B HB   1 
ATOM   7023 H HG11 . VAL B 1 237 ? 1.10651   -27.49248 8.22345  1.000 40.38780  ? 223 VAL B HG11 1 
ATOM   7024 H HG12 . VAL B 1 237 ? 1.09351   -27.50479 9.81190  1.000 40.38780  ? 223 VAL B HG12 1 
ATOM   7025 H HG13 . VAL B 1 237 ? -0.15056  -28.07177 9.00300  1.000 40.38780  ? 223 VAL B HG13 1 
ATOM   7026 H HG21 . VAL B 1 237 ? 0.38282   -24.19017 9.83512  1.000 40.08630  ? 223 VAL B HG21 1 
ATOM   7027 H HG22 . VAL B 1 237 ? 0.21941   -25.32868 10.93083 1.000 40.08630  ? 223 VAL B HG22 1 
ATOM   7028 H HG23 . VAL B 1 237 ? 1.53314   -25.26643 10.03991 1.000 40.08630  ? 223 VAL B HG23 1 
ATOM   7029 N N    . THR B 1 238 ? 1.65096   -23.64388 7.25616  1.000 34.08047  ? 224 THR B N    1 
ATOM   7030 C CA   . THR B 1 238 ? 2.93925   -23.08692 6.87116  1.000 39.24484  ? 224 THR B CA   1 
ATOM   7031 C C    . THR B 1 238 ? 3.31554   -21.96571 7.82877  1.000 36.25369  ? 224 THR B C    1 
ATOM   7032 O O    . THR B 1 238 ? 2.45203   -21.24067 8.32933  1.000 35.99937  ? 224 THR B O    1 
ATOM   7033 C CB   . THR B 1 238 ? 2.91589   -22.53845 5.43640  1.000 35.55332  ? 224 THR B CB   1 
ATOM   7034 O OG1  . THR B 1 238 ? 2.29848   -23.49202 4.56387  1.000 43.52092  ? 224 THR B OG1  1 
ATOM   7035 C CG2  . THR B 1 238 ? 4.32702   -22.25029 4.95219  1.000 40.06626  ? 224 THR B CG2  1 
ATOM   7036 H H    . THR B 1 238 ? 1.06714   -23.04694 7.46210  1.000 40.95251  ? 224 THR B H    1 
ATOM   7037 H HA   . THR B 1 238 ? 3.61345   -23.78200 6.92786  1.000 47.14975  ? 224 THR B HA   1 
ATOM   7038 H HB   . THR B 1 238 ? 2.41063   -21.71068 5.41632  1.000 42.71992  ? 224 THR B HB   1 
ATOM   7039 H HG1  . THR B 1 238 ? 1.46857   -23.50447 4.69309  1.000 52.28105  ? 224 THR B HG1  1 
ATOM   7040 H HG21 . THR B 1 238 ? 4.30958   -21.98126 4.02041  1.000 48.13545  ? 224 THR B HG21 1 
ATOM   7041 H HG22 . THR B 1 238 ? 4.71910   -21.53620 5.47873  1.000 48.13545  ? 224 THR B HG22 1 
ATOM   7042 H HG23 . THR B 1 238 ? 4.87669   -23.04465 5.04027  1.000 48.13545  ? 224 THR B HG23 1 
ATOM   7043 N N    . ALA B 1 239 ? 4.61609   -21.82251 8.06974  1.000 34.66801  ? 225 ALA B N    1 
ATOM   7044 C CA   . ALA B 1 239 ? 5.12753   -20.77311 8.93932  1.000 35.42525  ? 225 ALA B CA   1 
ATOM   7045 C C    . ALA B 1 239 ? 5.41759   -19.51860 8.12628  1.000 32.38476  ? 225 ALA B C    1 
ATOM   7046 O O    . ALA B 1 239 ? 5.86390   -19.59719 6.97832  1.000 36.18820  ? 225 ALA B O    1 
ATOM   7047 C CB   . ALA B 1 239 ? 6.39464   -21.23453 9.66064  1.000 31.96805  ? 225 ALA B CB   1 
ATOM   7048 H H    . ALA B 1 239 ? 5.22738   -22.32741 7.73657  1.000 41.65755  ? 225 ALA B H    1 
ATOM   7049 H HA   . ALA B 1 239 ? 4.46224   -20.55785 9.61160  1.000 42.56624  ? 225 ALA B HA   1 
ATOM   7050 H HB1  . ALA B 1 239 ? 6.69304   -20.52989 10.25674 1.000 38.41760  ? 225 ALA B HB1  1 
ATOM   7051 H HB2  . ALA B 1 239 ? 6.19433   -22.03561 10.16961 1.000 38.41760  ? 225 ALA B HB2  1 
ATOM   7052 H HB3  . ALA B 1 239 ? 7.08150   -21.42394 9.00244  1.000 38.41760  ? 225 ALA B HB3  1 
ATOM   7053 N N    . ALA B 1 240 ? 5.15749   -18.36193 8.72906  1.000 32.65795  ? 226 ALA B N    1 
ATOM   7054 C CA   . ALA B 1 240 ? 5.37871   -17.07766 8.07671  1.000 35.27898  ? 226 ALA B CA   1 
ATOM   7055 C C    . ALA B 1 240 ? 5.45440   -16.00077 9.15224  1.000 35.37895  ? 226 ALA B C    1 
ATOM   7056 O O    . ALA B 1 240 ? 5.40055   -16.28711 10.35098 1.000 33.90130  ? 226 ALA B O    1 
ATOM   7057 C CB   . ALA B 1 240 ? 4.27483   -16.77554 7.05940  1.000 35.90584  ? 226 ALA B CB   1 
ATOM   7058 H H    . ALA B 1 240 ? 4.84743   -18.29475 9.52840  1.000 38.90984  ? 226 ALA B H    1 
ATOM   7059 H HA   . ALA B 1 240 ? 6.22787   -17.10466 7.60863  1.000 42.39071  ? 226 ALA B HA   1 
ATOM   7060 H HB1  . ALA B 1 240 ? 4.26950   -17.47106 6.38329  1.000 42.80731  ? 226 ALA B HB1  1 
ATOM   7061 H HB2  . ALA B 1 240 ? 3.42031   -16.75336 7.51787  1.000 42.80731  ? 226 ALA B HB2  1 
ATOM   7062 H HB3  . ALA B 1 240 ? 4.45171   -15.91529 6.64760  1.000 42.80731  ? 226 ALA B HB3  1 
ATOM   7063 N N    . GLY B 1 241 ? 5.58041   -14.75124 8.71074  1.000 40.11509  ? 227 GLY B N    1 
ATOM   7064 C CA   . GLY B 1 241 ? 5.65543   -13.61991 9.60838  1.000 38.64184  ? 227 GLY B CA   1 
ATOM   7065 C C    . GLY B 1 241 ? 7.04251   -13.05542 9.81744  1.000 43.78260  ? 227 GLY B C    1 
ATOM   7066 O O    . GLY B 1 241 ? 7.19527   -12.12278 10.61598 1.000 48.53098  ? 227 GLY B O    1 
ATOM   7067 H H    . GLY B 1 241 ? 5.62480   -14.53681 7.87908  1.000 48.19404  ? 227 GLY B H    1 
ATOM   7068 H HA2  . GLY B 1 241 ? 5.09793   -12.90839 9.25647  1.000 46.42615  ? 227 GLY B HA2  1 
ATOM   7069 H HA3  . GLY B 1 241 ? 5.31356   -13.88962 10.47514 1.000 46.42615  ? 227 GLY B HA3  1 
ATOM   7070 N N    . ILE B 1 242 ? 8.05405   -13.58791 9.13750  1.000 47.47529  ? 228 ILE B N    1 
ATOM   7071 C CA   . ILE B 1 242 ? 9.41167   -13.06722 9.24891  1.000 52.04558  ? 228 ILE B CA   1 
ATOM   7072 C C    . ILE B 1 242 ? 9.97573   -12.78961 7.86125  1.000 53.58240  ? 228 ILE B C    1 
ATOM   7073 O O    . ILE B 1 242 ? 9.40372   -13.20559 6.85387  1.000 71.44141  ? 228 ILE B O    1 
ATOM   7074 C CB   . ILE B 1 242 ? 10.32345  -14.03659 10.02261 1.000 52.69835  ? 228 ILE B CB   1 
ATOM   7075 C CG1  . ILE B 1 242 ? 9.74510   -14.30228 11.41596 1.000 48.91746  ? 228 ILE B CG1  1 
ATOM   7076 C CG2  . ILE B 1 242 ? 11.73773  -13.46761 10.11465 1.000 54.01478  ? 228 ILE B CG2  1 
ATOM   7077 C CD1  . ILE B 1 242 ? 10.58839  -15.22567 12.27702 1.000 43.84027  ? 228 ILE B CD1  1 
ATOM   7078 H H    . ILE B 1 242 ? 7.97892   -14.25612 8.60135  1.000 57.02629  ? 228 ILE B H    1 
ATOM   7079 H HA   . ILE B 1 242 ? 9.38395   -12.23373 9.74433  1.000 62.51064  ? 228 ILE B HA   1 
ATOM   7080 H HB   . ILE B 1 242 ? 10.36549  -14.87994 9.54524  1.000 63.29395  ? 228 ILE B HB   1 
ATOM   7081 H HG12 . ILE B 1 242 ? 9.66421   -13.45663 11.88417 1.000 58.75689  ? 228 ILE B HG12 1 
ATOM   7082 H HG13 . ILE B 1 242 ? 8.87111   -14.71095 11.31579 1.000 58.75689  ? 228 ILE B HG13 1 
ATOM   7083 H HG21 . ILE B 1 242 ? 12.13165  -13.45575 9.22832  1.000 64.87368  ? 228 ILE B HG21 1 
ATOM   7084 H HG22 . ILE B 1 242 ? 11.69284  -12.56568 10.46878 1.000 64.87368  ? 228 ILE B HG22 1 
ATOM   7085 H HG23 . ILE B 1 242 ? 12.26602  -14.02844 10.70395 1.000 64.87368  ? 228 ILE B HG23 1 
ATOM   7086 H HD11 . ILE B 1 242 ? 10.90428  -15.96389 11.73283 1.000 52.66426  ? 228 ILE B HD11 1 
ATOM   7087 H HD12 . ILE B 1 242 ? 11.34273  -14.72774 12.62905 1.000 52.66426  ? 228 ILE B HD12 1 
ATOM   7088 H HD13 . ILE B 1 242 ? 10.04435  -15.56156 13.00647 1.000 52.66426  ? 228 ILE B HD13 1 
HETATM 7089 C C    . ACY C 2 .   ? -12.61274 -6.19891  2.50137  1.000 58.70544  ? 301 ACY A C    1 
HETATM 7090 O O    . ACY C 2 .   ? -12.91707 -7.16186  3.18834  1.000 59.06576  ? 301 ACY A O    1 
HETATM 7091 O OXT  . ACY C 2 .   ? -13.27764 -5.10182  2.42660  1.000 58.80766  ? 301 ACY A OXT  1 
HETATM 7092 C CH3  . ACY C 2 .   ? -11.36124 -6.20683  1.61234  1.000 52.23564  ? 301 ACY A CH3  1 
HETATM 7093 H H1   . ACY C 2 .   ? -11.08060 -7.11700  1.42865  1.000 62.73871  ? 301 ACY A H1   1 
HETATM 7094 H H2   . ACY C 2 .   ? -10.63031 -5.74332  2.05029  1.000 62.73871  ? 301 ACY A H2   1 
HETATM 7095 H H3   . ACY C 2 .   ? -11.54162 -5.76544  0.76763  1.000 62.73871  ? 301 ACY A H3   1 
HETATM 7096 C C1   . PGE D 3 .   ? 9.68589   6.22572   -3.31845 1.000 69.63796  ? 302 PGE A C1   1 
HETATM 7097 O O1   . PGE D 3 .   ? 8.90931   7.23267   -2.68255 1.000 61.00869  ? 302 PGE A O1   1 
HETATM 7098 C C2   . PGE D 3 .   ? 11.15741  6.55541   -3.16149 1.000 70.84575  ? 302 PGE A C2   1 
HETATM 7099 O O2   . PGE D 3 .   ? 11.62017  6.06017   -1.92012 1.000 66.24107  ? 302 PGE A O2   1 
HETATM 7100 C C3   . PGE D 3 .   ? 12.88474  5.42834   -1.98704 1.000 65.32649  ? 302 PGE A C3   1 
HETATM 7101 C C4   . PGE D 3 .   ? 13.93358  6.43975   -2.41130 1.000 66.59913  ? 302 PGE A C4   1 
HETATM 7102 O O4   . PGE D 3 .   ? 17.62455  3.89495   -3.51894 1.000 65.28573  ? 302 PGE A O4   1 
HETATM 7103 C C6   . PGE D 3 .   ? 17.14317  4.68926   -2.44302 1.000 69.85238  ? 302 PGE A C6   1 
HETATM 7104 C C5   . PGE D 3 .   ? 15.63249  4.78444   -2.53435 1.000 65.23973  ? 302 PGE A C5   1 
HETATM 7105 O O3   . PGE D 3 .   ? 15.20386  6.00610   -1.96349 1.000 70.98175  ? 302 PGE A O3   1 
HETATM 7106 H H1   . PGE D 3 .   ? 9.46343   6.15887   -4.39364 1.000 83.62149  ? 302 PGE A H1   1 
HETATM 7107 H H12  . PGE D 3 .   ? 9.50851   5.23473   -2.87518 1.000 83.62149  ? 302 PGE A H12  1 
HETATM 7108 H HO1  . PGE D 3 .   ? 9.43285   7.60185   -1.96086 1.000 73.26637  ? 302 PGE A HO1  1 
HETATM 7109 H H2   . PGE D 3 .   ? 11.29143  7.64963   -3.22088 1.000 85.07084  ? 302 PGE A H2   1 
HETATM 7110 H H22  . PGE D 3 .   ? 11.72043  6.10447   -3.99724 1.000 85.07084  ? 302 PGE A H22  1 
HETATM 7111 H H3   . PGE D 3 .   ? 12.87161  4.59948   -2.71466 1.000 78.44773  ? 302 PGE A H3   1 
HETATM 7112 H H32  . PGE D 3 .   ? 13.16699  5.00974   -1.00638 1.000 78.44773  ? 302 PGE A H32  1 
HETATM 7113 H H4   . PGE D 3 .   ? 13.68167  7.42499   -1.98159 1.000 79.97490  ? 302 PGE A H4   1 
HETATM 7114 H H42  . PGE D 3 .   ? 13.91808  6.53839   -3.51077 1.000 79.97490  ? 302 PGE A H42  1 
HETATM 7115 H HO4  . PGE D 3 .   ? 18.05941  3.11938   -3.14356 1.000 78.39881  ? 302 PGE A HO4  1 
HETATM 7116 H H6   . PGE D 3 .   ? 17.55825  5.71064   -2.47622 1.000 83.87879  ? 302 PGE A H6   1 
HETATM 7117 H H62  . PGE D 3 .   ? 17.40511  4.24945   -1.46600 1.000 83.87879  ? 302 PGE A H62  1 
HETATM 7118 H H5   . PGE D 3 .   ? 15.18766  3.92398   -2.00676 1.000 78.34362  ? 302 PGE A H5   1 
HETATM 7119 H H52  . PGE D 3 .   ? 15.33357  4.71682   -3.59392 1.000 78.34362  ? 302 PGE A H52  1 
HETATM 7120 C C1   . GOL E 4 .   ? 3.85840   9.72210   -3.21224 1.000 53.09466  ? 303 GOL A C1   1 
HETATM 7121 O O1   . GOL E 4 .   ? 2.62294   9.29502   -2.71719 1.000 48.94096  ? 303 GOL A O1   1 
HETATM 7122 C C2   . GOL E 4 .   ? 4.35804   8.62822   -4.19633 1.000 60.03369  ? 303 GOL A C2   1 
HETATM 7123 O O2   . GOL E 4 .   ? 5.31937   9.11922   -5.07245 1.000 57.22181  ? 303 GOL A O2   1 
HETATM 7124 C C3   . GOL E 4 .   ? 4.90844   7.48216   -3.30551 1.000 54.47619  ? 303 GOL A C3   1 
HETATM 7125 O O3   . GOL E 4 .   ? 4.11886   6.36139   -3.56526 1.000 53.01413  ? 303 GOL A O3   1 
HETATM 7126 H H11  . GOL E 4 .   ? 4.51743   9.84848   -2.51180 1.000 63.76954  ? 303 GOL A H11  1 
HETATM 7127 H H12  . GOL E 4 .   ? 3.80024   10.57062  -3.67863 1.000 63.76954  ? 303 GOL A H12  1 
HETATM 7128 H HO1  . GOL E 4 .   ? 2.29977   9.94571   -2.27348 1.000 58.78509  ? 303 GOL A HO1  1 
HETATM 7129 H H2   . GOL E 4 .   ? 3.62350   8.31112   -4.74479 1.000 72.09637  ? 303 GOL A H2   1 
HETATM 7130 H HO2  . GOL E 4 .   ? 5.60129   8.46980   -5.54306 1.000 68.72211  ? 303 GOL A HO2  1 
HETATM 7131 H H31  . GOL E 4 .   ? 4.88450   7.76441   -2.37779 1.000 65.42736  ? 303 GOL A H31  1 
HETATM 7132 H H32  . GOL E 4 .   ? 5.84745   7.34804   -3.50843 1.000 65.42736  ? 303 GOL A H32  1 
HETATM 7133 H HO3  . GOL E 4 .   ? 4.16089   6.21983   -4.40284 1.000 63.67289  ? 303 GOL A HO3  1 
HETATM 7134 C C1   . PEG F 5 .   ? -0.81921  12.91864  -1.92853 1.000 57.75380  ? 304 PEG A C1   1 
HETATM 7135 O O1   . PEG F 5 .   ? 0.42169   13.37466  -2.43936 1.000 53.46232  ? 304 PEG A O1   1 
HETATM 7136 C C2   . PEG F 5 .   ? -0.99826  11.44911  -2.15929 1.000 56.66601  ? 304 PEG A C2   1 
HETATM 7137 O O2   . PEG F 5 .   ? -1.59593  10.85526  -1.01349 1.000 58.67888  ? 304 PEG A O2   1 
HETATM 7138 C C3   . PEG F 5 .   ? -2.96500  11.19720  -0.84540 1.000 57.34447  ? 304 PEG A C3   1 
HETATM 7139 C C4   . PEG F 5 .   ? -3.79541  9.94991   -0.85529 1.000 53.75179  ? 304 PEG A C4   1 
HETATM 7140 O O4   . PEG F 5 .   ? -3.88097  9.39733   -2.15893 1.000 48.10586  ? 304 PEG A O4   1 
HETATM 7141 H H11  . PEG F 5 .   ? -1.53767  13.39742  -2.37066 1.000 69.36051  ? 304 PEG A H11  1 
HETATM 7142 H H12  . PEG F 5 .   ? -0.85199  13.09475  -0.97521 1.000 69.36051  ? 304 PEG A H12  1 
HETATM 7143 H HO1  . PEG F 5 .   ? 0.69266   12.94740  -3.12245 1.000 64.21072  ? 304 PEG A HO1  1 
HETATM 7144 H H21  . PEG F 5 .   ? -0.13383  11.03986  -2.32103 1.000 68.05515  ? 304 PEG A H21  1 
HETATM 7145 H H22  . PEG F 5 .   ? -1.57053  11.31056  -2.93014 1.000 68.05515  ? 304 PEG A H22  1 
HETATM 7146 H H31  . PEG F 5 .   ? -3.24489  11.77761  -1.57044 1.000 68.86930  ? 304 PEG A H31  1 
HETATM 7147 H H32  . PEG F 5 .   ? -3.08216  11.65681  0.00073  1.000 68.86930  ? 304 PEG A H32  1 
HETATM 7148 H H41  . PEG F 5 .   ? -4.68878  10.16254  -0.54291 1.000 64.55809  ? 304 PEG A H41  1 
HETATM 7149 H H42  . PEG F 5 .   ? -3.39265  9.29738   -0.26125 1.000 64.55809  ? 304 PEG A H42  1 
HETATM 7150 H HO4  . PEG F 5 .   ? -3.35470  9.75600   -2.72177 1.000 57.78298  ? 304 PEG A HO4  1 
HETATM 7151 C C1   . GOL G 4 .   ? -3.01080  -20.72867 29.48041 1.000 63.99042  ? 301 GOL B C1   1 
HETATM 7152 O O1   . GOL G 4 .   ? -4.18665  -19.98824 29.33459 1.000 65.80523  ? 301 GOL B O1   1 
HETATM 7153 C C2   . GOL G 4 .   ? -3.13968  -21.96572 28.55586 1.000 49.14656  ? 301 GOL B C2   1 
HETATM 7154 O O2   . GOL G 4 .   ? -2.22355  -21.93959 27.51593 1.000 42.52172  ? 301 GOL B O2   1 
HETATM 7155 C C3   . GOL G 4 .   ? -2.92531  -23.18319 29.48050 1.000 56.41825  ? 301 GOL B C3   1 
HETATM 7156 O O3   . GOL G 4 .   ? -3.06833  -24.31670 28.68217 1.000 49.92983  ? 301 GOL B O3   1 
HETATM 7157 H H11  . GOL G 4 .   ? -2.86560  -21.02329 30.39311 1.000 76.84445  ? 301 GOL B H11  1 
HETATM 7158 H H12  . GOL G 4 .   ? -2.21917  -20.22484 29.23469 1.000 76.84445  ? 301 GOL B H12  1 
HETATM 7159 H HO1  . GOL G 4 .   ? -4.03131  -19.21725 29.65927 1.000 79.02222  ? 301 GOL B HO1  1 
HETATM 7160 H H2   . GOL G 4 .   ? -4.01762  -21.98706 28.14396 1.000 59.03181  ? 301 GOL B H2   1 
HETATM 7161 H HO2  . GOL G 4 .   ? -1.74419  -22.64025 27.57286 1.000 51.08200  ? 301 GOL B HO2  1 
HETATM 7162 H H31  . GOL G 4 .   ? -3.56303  -23.14187 30.21022 1.000 67.75784  ? 301 GOL B H31  1 
HETATM 7163 H H32  . GOL G 4 .   ? -2.05277  -23.11279 29.89837 1.000 67.75784  ? 301 GOL B H32  1 
HETATM 7164 H HO3  . GOL G 4 .   ? -3.58356  -24.84723 29.10244 1.000 59.97173  ? 301 GOL B HO3  1 
HETATM 7165 C C1   . GOL H 4 .   ? -8.27924  -45.11411 13.76644 1.000 32.91553  ? 302 GOL B C1   1 
HETATM 7166 O O1   . GOL H 4 .   ? -7.32555  -44.15084 14.08439 1.000 28.27312  ? 302 GOL B O1   1 
HETATM 7167 C C2   . GOL H 4 .   ? -9.33312  -44.38553 12.91053 1.000 41.49989  ? 302 GOL B C2   1 
HETATM 7168 O O2   . GOL H 4 .   ? -8.76339  -43.42254 12.09841 1.000 42.76998  ? 302 GOL B O2   1 
HETATM 7169 C C3   . GOL H 4 .   ? -10.05767 -45.48135 12.09615 1.000 37.37701  ? 302 GOL B C3   1 
HETATM 7170 O O3   . GOL H 4 .   ? -10.52224 -44.85838 10.93874 1.000 41.39711  ? 302 GOL B O3   1 
HETATM 7171 H H11  . GOL H 4 .   ? -8.70258  -45.50006 14.54920 1.000 39.55458  ? 302 GOL B H11  1 
HETATM 7172 H H12  . GOL H 4 .   ? -7.91133  -45.86055 13.26807 1.000 39.55458  ? 302 GOL B H12  1 
HETATM 7173 H HO1  . GOL H 4 .   ? -7.70903  -43.59469 14.59328 1.000 33.98368  ? 302 GOL B HO1  1 
HETATM 7174 H H2   . GOL H 4 .   ? -9.96207  -43.92336 13.48648 1.000 49.85580  ? 302 GOL B H2   1 
HETATM 7175 H HO2  . GOL H 4 .   ? -8.65044  -42.72300 12.56733 1.000 51.37991  ? 302 GOL B HO2  1 
HETATM 7176 H H31  . GOL H 4 .   ? -10.76333 -45.86670 12.63878 1.000 44.90835  ? 302 GOL B H31  1 
HETATM 7177 H H32  . GOL H 4 .   ? -9.44062  -46.20956 11.92333 1.000 44.90835  ? 302 GOL B H32  1 
HETATM 7178 H HO3  . GOL H 4 .   ? -10.77749 -45.47588 10.41460 1.000 49.73248  ? 302 GOL B HO3  1 
HETATM 7179 C C1   . GOL I 4 .   ? -13.04635 -50.34780 11.57105 1.000 43.70194  ? 303 GOL B C1   1 
HETATM 7180 O O1   . GOL I 4 .   ? -12.25097 -51.06516 12.45052 1.000 44.01858  ? 303 GOL B O1   1 
HETATM 7181 C C2   . GOL I 4 .   ? -13.99792 -49.47836 12.42923 1.000 45.52821  ? 303 GOL B C2   1 
HETATM 7182 O O2   . GOL I 4 .   ? -14.46393 -50.14737 13.54905 1.000 33.08303  ? 303 GOL B O2   1 
HETATM 7183 C C3   . GOL I 4 .   ? -13.18240 -48.21854 12.80001 1.000 45.76166  ? 303 GOL B C3   1 
HETATM 7184 O O3   . GOL I 4 .   ? -12.90536 -47.53499 11.60044 1.000 50.17663  ? 303 GOL B O3   1 
HETATM 7185 H H11  . GOL I 4 .   ? -13.57103 -50.92050 10.98999 1.000 52.49827  ? 303 GOL B H11  1 
HETATM 7186 H H12  . GOL I 4 .   ? -12.52995 -49.77444 10.98326 1.000 52.49827  ? 303 GOL B H12  1 
HETATM 7187 H HO1  . GOL I 4 .   ? -12.56705 -50.92959 13.22498 1.000 52.87824  ? 303 GOL B HO1  1 
HETATM 7188 H H2   . GOL I 4 .   ? -14.78508 -49.24335 11.91343 1.000 54.68979  ? 303 GOL B H2   1 
HETATM 7189 H HO2  . GOL I 4 .   ? -14.20567 -49.71583 14.23547 1.000 39.75558  ? 303 GOL B HO2  1 
HETATM 7190 H H31  . GOL I 4 .   ? -12.38459 -48.49234 13.27899 1.000 54.96993  ? 303 GOL B H31  1 
HETATM 7191 H H32  . GOL I 4 .   ? -13.69321 -47.69072 13.43355 1.000 54.96993  ? 303 GOL B H32  1 
HETATM 7192 H HO3  . GOL I 4 .   ? -12.84642 -46.70533 11.78995 1.000 60.26790  ? 303 GOL B HO3  1 
HETATM 7193 C C    . ACY J 2 .   ? -11.22152 -15.06347 26.38270 1.000 52.69554  ? 304 ACY B C    1 
HETATM 7194 O O    . ACY J 2 .   ? -10.58218 -15.15880 27.41792 1.000 55.50850  ? 304 ACY B O    1 
HETATM 7195 O OXT  . ACY J 2 .   ? -12.48344 -15.28423 26.27301 1.000 51.98061  ? 304 ACY B OXT  1 
HETATM 7196 C CH3  . ACY J 2 .   ? -10.56370 -14.63379 25.04799 1.000 54.42915  ? 304 ACY B CH3  1 
HETATM 7197 H H1   . ACY J 2 .   ? -10.17729 -15.40080 24.59714 1.000 65.37092  ? 304 ACY B H1   1 
HETATM 7198 H H2   . ACY J 2 .   ? -9.85964  -13.98629 25.20906 1.000 65.37092  ? 304 ACY B H2   1 
HETATM 7199 H H3   . ACY J 2 .   ? -11.22115 -14.23140 24.45913 1.000 65.37092  ? 304 ACY B H3   1 
HETATM 7200 O O    . HOH K 6 .   ? -6.52110  2.08782   9.22464  1.000 32.79780  ? 401 HOH A O    1 
HETATM 7201 O O    . HOH K 6 .   ? 27.700    21.828    12.070   1.000 45.24055  ? 402 HOH A O    1 
HETATM 7202 O O    . HOH K 6 .   ? -3.13586  9.36642   3.17806  1.000 35.39845  ? 403 HOH A O    1 
HETATM 7203 O O    . HOH K 6 .   ? -9.02117  6.46014   27.91818 1.000 51.42837  ? 404 HOH A O    1 
HETATM 7204 O O    . HOH K 6 .   ? -7.74424  17.82997  11.63267 1.000 44.74708  ? 405 HOH A O    1 
HETATM 7205 O O    . HOH K 6 .   ? 7.40387   5.85665   23.70138 1.000 29.35587  ? 406 HOH A O    1 
HETATM 7206 O O    . HOH K 6 .   ? 2.80431   5.46072   17.60794 1.000 26.05029  ? 407 HOH A O    1 
HETATM 7207 O O    . HOH K 6 .   ? 15.42265  2.85175   16.82863 1.000 27.49447  ? 408 HOH A O    1 
HETATM 7208 O O    . HOH K 6 .   ? 10.48414  -10.92077 20.73816 1.000 32.26961  ? 409 HOH A O    1 
HETATM 7209 O O    . HOH K 6 .   ? 18.40400  -7.42909  24.78051 1.000 39.08409  ? 410 HOH A O    1 
HETATM 7210 O O    . HOH K 6 .   ? 13.72438  4.43639   19.64607 1.000 19.91428  ? 411 HOH A O    1 
HETATM 7211 O O    . HOH K 6 .   ? 26.70354  2.06778   25.06962 1.000 29.82166  ? 412 HOH A O    1 
HETATM 7212 O O    . HOH K 6 .   ? 16.32499  21.39066  25.76577 1.000 44.40631  ? 413 HOH A O    1 
HETATM 7213 O O    . HOH K 6 .   ? 24.42700  -2.01537  31.77138 1.000 39.18518  ? 414 HOH A O    1 
HETATM 7214 O O    . HOH K 6 .   ? -0.48240  22.39162  16.03856 1.000 39.40596  ? 415 HOH A O    1 
HETATM 7215 O O    . HOH K 6 .   ? 26.63064  -1.94348  23.30983 1.000 29.98484  ? 416 HOH A O    1 
HETATM 7216 O O    . HOH K 6 .   ? -5.03042  -12.62299 13.55673 1.000 30.88604  ? 417 HOH A O    1 
HETATM 7217 O O    . HOH K 6 .   ? 10.58740  21.52975  19.61373 1.000 35.64274  ? 418 HOH A O    1 
HETATM 7218 O O    . HOH K 6 .   ? 24.93836  17.69876  6.69669  1.000 44.14074  ? 419 HOH A O    1 
HETATM 7219 O O    . HOH K 6 .   ? 14.27096  20.22503  20.48693 1.000 29.25586  ? 420 HOH A O    1 
HETATM 7220 O O    . HOH K 6 .   ? -6.67425  15.49394  9.64176  1.000 33.24688  ? 421 HOH A O    1 
HETATM 7221 O O    . HOH K 6 .   ? 22.37709  11.48381  3.07105  1.000 30.89028  ? 422 HOH A O    1 
HETATM 7222 O O    . HOH K 6 .   ? 22.95348  -4.78046  30.21083 1.000 45.05504  ? 423 HOH A O    1 
HETATM 7223 O O    . HOH K 6 .   ? 15.99270  9.50763   4.29892  1.000 29.95486  ? 424 HOH A O    1 
HETATM 7224 O O    . HOH K 6 .   ? -5.99314  14.66278  23.75306 1.000 38.29705  ? 425 HOH A O    1 
HETATM 7225 O O    . HOH K 6 .   ? 5.09768   8.05517   20.24454 1.000 25.91655  ? 426 HOH A O    1 
HETATM 7226 O O    . HOH K 6 .   ? 2.61102   -2.59570  29.58595 1.000 45.95115  ? 427 HOH A O    1 
HETATM 7227 O O    . HOH K 6 .   ? 28.86910  4.47984   31.11604 1.000 29.68700  ? 428 HOH A O    1 
HETATM 7228 O O    . HOH K 6 .   ? 24.14014  14.82288  11.63528 1.000 29.97264  ? 429 HOH A O    1 
HETATM 7229 O O    . HOH K 6 .   ? -3.74391  -1.79714  15.77658 1.000 30.05109  ? 430 HOH A O    1 
HETATM 7230 O O    . HOH K 6 .   ? 10.23326  4.00461   22.10685 1.000 24.54405  ? 431 HOH A O    1 
HETATM 7231 O O    . HOH K 6 .   ? 2.23250   -7.95540  21.21957 1.000 40.22115  ? 432 HOH A O    1 
HETATM 7232 O O    . HOH K 6 .   ? 2.04675   21.68865  11.21153 1.000 37.55795  ? 433 HOH A O    1 
HETATM 7233 O O    . HOH K 6 .   ? 4.41011   -5.22103  25.37534 1.000 34.88343  ? 434 HOH A O    1 
HETATM 7234 O O    . HOH K 6 .   ? 17.48673  18.81427  26.96267 1.000 40.66110  ? 435 HOH A O    1 
HETATM 7235 O O    . HOH K 6 .   ? 19.32946  4.14041   5.17145  1.000 33.86341  ? 436 HOH A O    1 
HETATM 7236 O O    . HOH K 6 .   ? -6.26047  14.00218  6.34459  1.000 40.54763  ? 437 HOH A O    1 
HETATM 7237 O O    . HOH K 6 .   ? 16.77200  -4.39240  6.68775  1.000 37.28434  ? 438 HOH A O    1 
HETATM 7238 O O    . HOH K 6 .   ? 23.02604  0.68616   12.80382 1.000 28.38345  ? 439 HOH A O    1 
HETATM 7239 O O    . HOH K 6 .   ? -5.01187  -9.41491  19.62826 1.000 29.75503  ? 440 HOH A O    1 
HETATM 7240 O O    . HOH K 6 .   ? 20.48628  0.58676   12.82975 1.000 30.09627  ? 441 HOH A O    1 
HETATM 7241 O O    . HOH K 6 .   ? 22.31035  16.68674  22.47772 1.000 30.53608  ? 442 HOH A O    1 
HETATM 7242 O O    . HOH K 6 .   ? -2.44485  2.97157   11.94466 1.000 25.66509  ? 443 HOH A O    1 
HETATM 7243 O O    . HOH K 6 .   ? -2.17406  10.50161  6.42112  1.000 25.85637  ? 444 HOH A O    1 
HETATM 7244 O O    . HOH K 6 .   ? -8.17077  18.15240  15.65677 1.000 39.84186  ? 445 HOH A O    1 
HETATM 7245 O O    . HOH K 6 .   ? 2.00174   18.72203  4.92524  1.000 37.01877  ? 446 HOH A O    1 
HETATM 7246 O O    . HOH K 6 .   ? 15.84559  3.72366   31.51126 1.000 26.52002  ? 447 HOH A O    1 
HETATM 7247 O O    . HOH K 6 .   ? 16.39606  1.06383   18.83480 1.000 27.82439  ? 448 HOH A O    1 
HETATM 7248 O O    . HOH K 6 .   ? 28.42357  9.29579   24.19938 1.000 39.20172  ? 449 HOH A O    1 
HETATM 7249 O O    . HOH K 6 .   ? 0.49687   -10.41565 17.02251 1.000 33.35486  ? 450 HOH A O    1 
HETATM 7250 O O    . HOH K 6 .   ? 16.09964  -4.88009  12.54125 1.000 38.36619  ? 451 HOH A O    1 
HETATM 7251 O O    . HOH K 6 .   ? 19.40281  9.28428   32.70594 1.000 34.34715  ? 452 HOH A O    1 
HETATM 7252 O O    . HOH K 6 .   ? 9.32380   -4.93877  9.25228  1.000 33.93150  ? 453 HOH A O    1 
HETATM 7253 O O    . HOH K 6 .   ? 8.84488   16.27303  24.83838 1.000 38.36325  ? 454 HOH A O    1 
HETATM 7254 O O    . HOH K 6 .   ? -4.73135  2.69526   6.99514  1.000 31.84891  ? 455 HOH A O    1 
HETATM 7255 O O    . HOH K 6 .   ? 7.27286   6.38682   20.97892 1.000 26.55358  ? 456 HOH A O    1 
HETATM 7256 O O    . HOH K 6 .   ? -5.20206  -10.39829 23.71656 1.000 44.94129  ? 457 HOH A O    1 
HETATM 7257 O O    . HOH K 6 .   ? 12.06876  12.62630  4.70940  1.000 37.43512  ? 458 HOH A O    1 
HETATM 7258 O O    . HOH K 6 .   ? -9.90745  2.02990   10.62584 1.000 37.61959  ? 459 HOH A O    1 
HETATM 7259 O O    . HOH K 6 .   ? 22.34065  5.60699   5.21716  1.000 41.00791  ? 460 HOH A O    1 
HETATM 7260 O O    . HOH K 6 .   ? 9.91566   -9.78210  11.45334 1.000 35.63165  ? 461 HOH A O    1 
HETATM 7261 O O    . HOH K 6 .   ? 24.64142  10.58886  12.62699 1.000 28.76597  ? 462 HOH A O    1 
HETATM 7262 O O    . HOH K 6 .   ? -8.45830  8.39952   22.65300 1.000 39.32215  ? 463 HOH A O    1 
HETATM 7263 O O    . HOH K 6 .   ? 27.73304  4.48793   9.22106  1.000 40.07875  ? 464 HOH A O    1 
HETATM 7264 O O    . HOH K 6 .   ? -3.64349  15.76647  1.23012  1.000 35.48124  ? 465 HOH A O    1 
HETATM 7265 O O    . HOH K 6 .   ? 21.45610  -7.78174  27.99403 1.000 32.22771  ? 466 HOH A O    1 
HETATM 7266 O O    . HOH K 6 .   ? 16.00337  16.61346  28.18436 1.000 40.08746  ? 467 HOH A O    1 
HETATM 7267 O O    . HOH K 6 .   ? -7.91172  -5.46260  1.72644  1.000 38.13792  ? 468 HOH A O    1 
HETATM 7268 O O    . HOH K 6 .   ? 26.63752  -4.76967  7.79616  1.000 50.04221  ? 469 HOH A O    1 
HETATM 7269 O O    . HOH K 6 .   ? -12.08130 9.25961   31.89786 1.000 51.64618  ? 470 HOH A O    1 
HETATM 7270 O O    . HOH K 6 .   ? 14.69987  0.18765   33.21501 1.000 46.54152  ? 471 HOH A O    1 
HETATM 7271 O O    . HOH K 6 .   ? -9.31531  3.03415   12.86671 1.000 36.33228  ? 472 HOH A O    1 
HETATM 7272 O O    . HOH K 6 .   ? 12.03330  -12.01347 13.86958 1.000 35.58054  ? 473 HOH A O    1 
HETATM 7273 O O    . HOH K 6 .   ? -6.68246  -12.14198 17.68080 1.000 30.52015  ? 474 HOH A O    1 
HETATM 7274 O O    . HOH K 6 .   ? 10.18442  7.73644   30.54495 1.000 37.40391  ? 475 HOH A O    1 
HETATM 7275 O O    . HOH K 6 .   ? -5.07496  15.93731  5.12701  1.000 37.86994  ? 476 HOH A O    1 
HETATM 7276 O O    . HOH K 6 .   ? -4.76719  17.10584  9.09416  1.000 33.07045  ? 477 HOH A O    1 
HETATM 7277 O O    . HOH K 6 .   ? 26.11747  12.18126  17.26399 1.000 35.58074  ? 478 HOH A O    1 
HETATM 7278 O O    . HOH K 6 .   ? 11.16155  -9.54390  16.57699 1.000 28.27311  ? 479 HOH A O    1 
HETATM 7279 O O    . HOH K 6 .   ? 27.03764  5.39044   15.82765 1.000 27.31211  ? 480 HOH A O    1 
HETATM 7280 O O    . HOH K 6 .   ? 1.52610   -1.22127  0.87837  1.000 36.79901  ? 481 HOH A O    1 
HETATM 7281 O O    . HOH K 6 .   ? 27.46332  -4.72480  10.32847 1.000 44.91352  ? 482 HOH A O    1 
HETATM 7282 O O    . HOH K 6 .   ? 3.304     2.808     -0.424   1.000 33.39766  ? 483 HOH A O    1 
HETATM 7283 O O    . HOH K 6 .   ? 19.13472  -3.75868  28.29249 1.000 30.18320  ? 484 HOH A O    1 
HETATM 7284 O O    . HOH K 6 .   ? -4.64331  4.08799   5.04902  1.000 35.91427  ? 485 HOH A O    1 
HETATM 7285 O O    . HOH K 6 .   ? 27.78403  19.70555  19.86623 1.000 36.02692  ? 486 HOH A O    1 
HETATM 7286 O O    . HOH K 6 .   ? 22.39934  26.58242  7.66141  1.000 34.33760  ? 487 HOH A O    1 
HETATM 7287 O O    . HOH K 6 .   ? 8.90920   -9.54260  15.73542 1.000 30.49980  ? 488 HOH A O    1 
HETATM 7288 O O    . HOH K 6 .   ? -11.31663 8.09473   20.00392 1.000 41.73623  ? 489 HOH A O    1 
HETATM 7289 O O    . HOH K 6 .   ? 25.60632  16.67321  30.26300 1.000 53.28116  ? 490 HOH A O    1 
HETATM 7290 O O    . HOH K 6 .   ? 7.36458   0.89028   29.69083 1.000 43.63701  ? 491 HOH A O    1 
HETATM 7291 O O    . HOH K 6 .   ? -5.32078  0.79250   1.90279  1.000 39.23653  ? 492 HOH A O    1 
HETATM 7292 O O    . HOH K 6 .   ? -12.14985 12.78302  5.60182  1.000 43.79150  ? 493 HOH A O    1 
HETATM 7293 O O    . HOH K 6 .   ? 23.04252  17.11418  30.73350 1.000 40.35681  ? 494 HOH A O    1 
HETATM 7294 O O    . HOH K 6 .   ? 7.68837   3.80567   29.86583 1.000 36.12547  ? 495 HOH A O    1 
HETATM 7295 O O    . HOH K 6 .   ? 28.71309  11.75723  22.36601 1.000 32.89113  ? 496 HOH A O    1 
HETATM 7296 O O    . HOH K 6 .   ? 35.81996  -0.85198  14.98601 1.000 54.75761  ? 497 HOH A O    1 
HETATM 7297 O O    . HOH K 6 .   ? 26.25966  12.36375  14.41532 1.000 40.38924  ? 498 HOH A O    1 
HETATM 7298 O O    . HOH K 6 .   ? 6.18883   4.55820   12.72602 1.000 32.31380  ? 499 HOH A O    1 
HETATM 7299 O O    . HOH K 6 .   ? 19.64807  -2.56552  30.91708 1.000 33.06186  ? 500 HOH A O    1 
HETATM 7300 O O    . HOH K 6 .   ? -6.53063  -1.37626  0.78733  1.000 39.50527  ? 501 HOH A O    1 
HETATM 7301 O O    . HOH K 6 .   ? 2.64995   11.99745  -0.32349 1.000 47.18245  ? 502 HOH A O    1 
HETATM 7302 O O    . HOH K 6 .   ? 4.70059   11.51558  3.69254  1.000 32.16035  ? 503 HOH A O    1 
HETATM 7303 O O    . HOH K 6 .   ? 21.48926  -3.00670  32.63758 1.000 38.84665  ? 504 HOH A O    1 
HETATM 7304 O O    . HOH K 6 .   ? 28.99047  -5.73108  20.35947 1.000 36.57044  ? 505 HOH A O    1 
HETATM 7305 O O    . HOH K 6 .   ? -13.45648 -0.03767  22.96508 1.000 47.51369  ? 506 HOH A O    1 
HETATM 7306 O O    . HOH K 6 .   ? 6.87569   -1.72672  4.60427  1.000 35.37649  ? 507 HOH A O    1 
HETATM 7307 O O    . HOH K 6 .   ? 15.15661  9.71743   1.24837  1.000 38.68859  ? 508 HOH A O    1 
HETATM 7308 O O    . HOH K 6 .   ? 5.14974   11.80131  28.24600 1.000 40.58706  ? 509 HOH A O    1 
HETATM 7309 O O    . HOH K 6 .   ? 15.97392  -0.61277  4.58105  1.000 40.70313  ? 510 HOH A O    1 
HETATM 7310 O O    . HOH K 6 .   ? 6.16848   0.82710   13.12066 1.000 26.26045  ? 511 HOH A O    1 
HETATM 7311 O O    . HOH K 6 .   ? 3.60720   14.69693  26.55839 1.000 44.50757  ? 512 HOH A O    1 
HETATM 7312 O O    . HOH K 6 .   ? 28.53707  15.85633  29.04369 1.000 45.76480  ? 513 HOH A O    1 
HETATM 7313 O O    . HOH K 6 .   ? -7.96438  18.27542  18.36666 1.000 40.31750  ? 514 HOH A O    1 
HETATM 7314 O O    . HOH K 6 .   ? -5.79939  3.00803   2.98919  1.000 37.44502  ? 515 HOH A O    1 
HETATM 7315 O O    . HOH K 6 .   ? 25.99953  -7.08572  10.24861 1.000 46.64641  ? 516 HOH A O    1 
HETATM 7316 O O    . HOH K 6 .   ? 24.022    7.523     34.889   1.000 34.47123  ? 517 HOH A O    1 
HETATM 7317 O O    . HOH K 6 .   ? 14.83526  -8.22791  27.22622 1.000 37.38780  ? 518 HOH A O    1 
HETATM 7318 O O    . HOH K 6 .   ? 26.27500  16.60655  32.74000 0.50  49.62679  ? 519 HOH A O    1 
HETATM 7319 O O    . HOH K 6 .   ? 6.04289   -1.06221  28.38237 1.000 38.91271  ? 520 HOH A O    1 
HETATM 7320 O O    . HOH K 6 .   ? 14.45359  2.34465   34.78194 1.000 33.22132  ? 521 HOH A O    1 
HETATM 7321 O O    . HOH K 6 .   ? 3.74471   -7.96989  23.91591 1.000 42.56780  ? 522 HOH A O    1 
HETATM 7322 O O    . HOH K 6 .   ? -8.04071  14.35862  24.98085 1.000 43.17269  ? 523 HOH A O    1 
HETATM 7323 O O    . HOH K 6 .   ? 26.61397  -10.11505 20.89165 1.000 40.80401  ? 524 HOH A O    1 
HETATM 7324 O O    . HOH K 6 .   ? 16.08620  1.96253   -0.10165 1.000 45.62390  ? 525 HOH A O    1 
HETATM 7325 O O    . HOH K 6 .   ? 13.78486  2.79286   0.44784  1.000 51.25631  ? 526 HOH A O    1 
HETATM 7326 O O    . HOH K 6 .   ? -9.303    -7.084    35.703   1.000 38.22476  ? 527 HOH A O    1 
HETATM 7327 O O    . HOH K 6 .   ? 3.20105   -10.64765 20.56598 1.000 34.87814  ? 528 HOH A O    1 
HETATM 7328 O O    . HOH K 6 .   ? 14.44643  4.41889   33.81183 1.000 29.41670  ? 529 HOH A O    1 
HETATM 7329 O O    . HOH K 6 .   ? -8.21139  3.99337   7.43753  1.000 41.38309  ? 530 HOH A O    1 
HETATM 7330 O O    . HOH K 6 .   ? 19.22602  21.07217  27.64506 1.000 39.10830  ? 531 HOH A O    1 
HETATM 7331 O O    . HOH K 6 .   ? 2.15339   -11.96487 18.88077 1.000 29.87839  ? 532 HOH A O    1 
HETATM 7332 O O    . HOH K 6 .   ? 8.98667   0.00000   0.00000  0.50  39.77893  ? 533 HOH A O    1 
HETATM 7333 O O    . HOH L 6 .   ? -20.00958 -42.39140 5.70068  1.000 39.69036  ? 401 HOH B O    1 
HETATM 7334 O O    . HOH L 6 .   ? 18.49428  -36.26889 30.09179 1.000 39.87687  ? 402 HOH B O    1 
HETATM 7335 O O    . HOH L 6 .   ? -18.25179 -45.21947 17.51331 1.000 25.59620  ? 403 HOH B O    1 
HETATM 7336 O O    . HOH L 6 .   ? 8.34790   -34.06838 4.45152  1.000 39.05853  ? 404 HOH B O    1 
HETATM 7337 O O    . HOH L 6 .   ? -18.99648 -40.57898 21.87696 1.000 37.76801  ? 405 HOH B O    1 
HETATM 7338 O O    . HOH L 6 .   ? -9.82064  -28.30418 19.42626 1.000 18.99040  ? 406 HOH B O    1 
HETATM 7339 O O    . HOH L 6 .   ? 14.38753  -26.45139 11.95396 1.000 44.19340  ? 407 HOH B O    1 
HETATM 7340 O O    . HOH L 6 .   ? -30.67807 -22.99720 9.51466  1.000 68.81335  ? 408 HOH B O    1 
HETATM 7341 O O    . HOH L 6 .   ? -14.57903 -28.31079 4.99112  1.000 33.40022  ? 409 HOH B O    1 
HETATM 7342 O O    . HOH L 6 .   ? -0.79189  -18.92078 25.58941 1.000 31.18741  ? 410 HOH B O    1 
HETATM 7343 O O    . HOH L 6 .   ? -21.59996 -21.06830 29.89423 1.000 44.74537  ? 411 HOH B O    1 
HETATM 7344 O O    . HOH L 6 .   ? -10.66910 -43.95945 20.65394 1.000 26.09792  ? 412 HOH B O    1 
HETATM 7345 O O    . HOH L 6 .   ? -27.26831 -20.76003 17.62598 1.000 40.86458  ? 413 HOH B O    1 
HETATM 7346 O O    . HOH L 6 .   ? 16.56195  -33.66171 18.78194 1.000 50.08367  ? 414 HOH B O    1 
HETATM 7347 O O    . HOH L 6 .   ? -23.22934 -25.58319 24.09378 1.000 34.82588  ? 415 HOH B O    1 
HETATM 7348 O O    . HOH L 6 .   ? 11.01017  -39.78762 10.96169 1.000 37.93513  ? 416 HOH B O    1 
HETATM 7349 O O    . HOH L 6 .   ? 11.82396  -32.96496 24.38012 1.000 33.67850  ? 417 HOH B O    1 
HETATM 7350 O O    . HOH L 6 .   ? -18.79022 -24.73307 12.15973 1.000 35.03734  ? 418 HOH B O    1 
HETATM 7351 O O    . HOH L 6 .   ? -18.21771 -50.27834 7.38463  1.000 35.37399  ? 419 HOH B O    1 
HETATM 7352 O O    . HOH L 6 .   ? -11.18587 -33.41783 4.04217  1.000 30.81645  ? 420 HOH B O    1 
HETATM 7353 O O    . HOH L 6 .   ? -23.48098 -46.02772 12.61846 1.000 37.14597  ? 421 HOH B O    1 
HETATM 7354 O O    . HOH L 6 .   ? -11.25375 -26.70976 16.58106 1.000 27.48819  ? 422 HOH B O    1 
HETATM 7355 O O    . HOH L 6 .   ? -19.98567 -38.46871 11.24507 1.000 29.18334  ? 423 HOH B O    1 
HETATM 7356 O O    . HOH L 6 .   ? 2.28616   -45.99169 12.33161 1.000 39.10884  ? 424 HOH B O    1 
HETATM 7357 O O    . HOH L 6 .   ? -6.77247  -45.00476 20.07184 1.000 33.50281  ? 425 HOH B O    1 
HETATM 7358 O O    . HOH L 6 .   ? -16.57370 -22.45542 9.85659  1.000 40.14582  ? 426 HOH B O    1 
HETATM 7359 O O    . HOH L 6 .   ? 7.30501   -35.00161 7.66314  1.000 32.49156  ? 427 HOH B O    1 
HETATM 7360 O O    . HOH L 6 .   ? 6.82209   -27.49550 12.67360 1.000 28.68299  ? 428 HOH B O    1 
HETATM 7361 O O    . HOH L 6 .   ? 12.05517  -26.83488 10.38172 1.000 37.93574  ? 429 HOH B O    1 
HETATM 7362 O O    . HOH L 6 .   ? 1.20099   -29.48493 18.07020 1.000 22.26504  ? 430 HOH B O    1 
HETATM 7363 O O    . HOH L 6 .   ? -24.80040 -34.94011 21.50599 1.000 43.13755  ? 431 HOH B O    1 
HETATM 7364 O O    . HOH L 6 .   ? -1.36604  -31.76108 20.61766 1.000 20.63668  ? 432 HOH B O    1 
HETATM 7365 O O    . HOH L 6 .   ? 5.83539   -18.68345 4.46286  1.000 47.48951  ? 433 HOH B O    1 
HETATM 7366 O O    . HOH L 6 .   ? -3.55058  -29.72157 23.95037 1.000 28.44195  ? 434 HOH B O    1 
HETATM 7367 O O    . HOH L 6 .   ? 5.63120   -15.66465 25.98189 1.000 42.75641  ? 435 HOH B O    1 
HETATM 7368 O O    . HOH L 6 .   ? -16.53142 -32.01512 32.26735 1.000 37.15581  ? 436 HOH B O    1 
HETATM 7369 O O    . HOH L 6 .   ? -15.57807 -20.46747 29.74326 1.000 39.24472  ? 437 HOH B O    1 
HETATM 7370 O O    . HOH L 6 .   ? -12.37127 -24.83076 18.18693 1.000 27.82508  ? 438 HOH B O    1 
HETATM 7371 O O    . HOH L 6 .   ? -24.42590 -32.83116 23.03425 1.000 38.59640  ? 439 HOH B O    1 
HETATM 7372 O O    . HOH L 6 .   ? 9.54513   -16.19742 29.56583 1.000 48.55666  ? 440 HOH B O    1 
HETATM 7373 O O    . HOH L 6 .   ? 9.26489   -14.75856 20.35677 1.000 30.15811  ? 441 HOH B O    1 
HETATM 7374 O O    . HOH L 6 .   ? -6.44639  -27.84124 22.14548 1.000 25.83842  ? 442 HOH B O    1 
HETATM 7375 O O    . HOH L 6 .   ? 2.94903   -36.17870 0.70121  1.000 39.47982  ? 443 HOH B O    1 
HETATM 7376 O O    . HOH L 6 .   ? 1.76660   -15.72163 21.33007 1.000 36.35118  ? 444 HOH B O    1 
HETATM 7377 O O    . HOH L 6 .   ? -23.07525 -21.17378 22.29516 1.000 37.02265  ? 445 HOH B O    1 
HETATM 7378 O O    . HOH L 6 .   ? -16.25586 -24.51696 11.91191 1.000 30.14538  ? 446 HOH B O    1 
HETATM 7379 O O    . HOH L 6 .   ? -12.83513 -45.22216 25.38107 1.000 39.14567  ? 447 HOH B O    1 
HETATM 7380 O O    . HOH L 6 .   ? -11.78793 -19.54937 6.18767  1.000 47.40121  ? 448 HOH B O    1 
HETATM 7381 O O    . HOH L 6 .   ? 11.86846  -42.83109 17.77741 1.000 40.65358  ? 449 HOH B O    1 
HETATM 7382 O O    . HOH L 6 .   ? -22.87495 -29.21146 14.88393 1.000 35.51794  ? 450 HOH B O    1 
HETATM 7383 O O    . HOH L 6 .   ? 15.19866  -32.46823 21.30827 1.000 39.96238  ? 451 HOH B O    1 
HETATM 7384 O O    . HOH L 6 .   ? -6.74403  -14.64041 16.14672 1.000 34.51242  ? 452 HOH B O    1 
HETATM 7385 O O    . HOH L 6 .   ? -21.47460 -35.56567 13.75777 1.000 43.81168  ? 453 HOH B O    1 
HETATM 7386 O O    . HOH L 6 .   ? -12.61847 -27.05319 31.09162 1.000 39.44761  ? 454 HOH B O    1 
HETATM 7387 O O    . HOH L 6 .   ? -11.68007 -19.43634 11.82005 1.000 39.22494  ? 455 HOH B O    1 
HETATM 7388 O O    . HOH L 6 .   ? -17.41570 -35.51369 2.23860  1.000 41.98333  ? 456 HOH B O    1 
HETATM 7389 O O    . HOH L 6 .   ? 16.36530  -25.01606 25.40657 1.000 43.07613  ? 457 HOH B O    1 
HETATM 7390 O O    . HOH L 6 .   ? -20.80960 -29.98792 12.83282 1.000 39.03701  ? 458 HOH B O    1 
HETATM 7391 O O    . HOH L 6 .   ? -6.61789  -40.12970 29.24915 1.000 48.20440  ? 459 HOH B O    1 
HETATM 7392 O O    . HOH L 6 .   ? 13.21738  -19.56497 2.93659  1.000 49.54466  ? 460 HOH B O    1 
HETATM 7393 O O    . HOH L 6 .   ? 16.939    -29.477   29.958   1.000 41.62967  ? 461 HOH B O    1 
HETATM 7394 O O    . HOH L 6 .   ? 11.26038  -38.54955 7.93398  1.000 43.31456  ? 462 HOH B O    1 
HETATM 7395 O O    . HOH L 6 .   ? -21.13020 -14.49691 28.43154 1.000 46.62629  ? 463 HOH B O    1 
HETATM 7396 O O    . HOH L 6 .   ? 9.75096   -27.07271 2.87581  1.000 37.05551  ? 464 HOH B O    1 
HETATM 7397 O O    . HOH L 6 .   ? 7.81121   -22.51081 16.61211 1.000 25.93782  ? 465 HOH B O    1 
HETATM 7398 O O    . HOH L 6 .   ? 14.24712  -29.35219 28.87939 1.000 41.62193  ? 466 HOH B O    1 
HETATM 7399 O O    . HOH L 6 .   ? -11.93626 -28.17386 35.82980 1.000 44.24323  ? 467 HOH B O    1 
HETATM 7400 O O    . HOH L 6 .   ? -5.28611  -14.37120 11.08191 1.000 33.66554  ? 468 HOH B O    1 
HETATM 7401 O O    . HOH L 6 .   ? -22.25934 -31.79753 15.17406 1.000 39.31776  ? 469 HOH B O    1 
HETATM 7402 O O    . HOH L 6 .   ? 9.20225   -38.85714 25.34460 1.000 33.46640  ? 470 HOH B O    1 
HETATM 7403 O O    . HOH L 6 .   ? -3.48034  -30.58542 21.21294 1.000 19.35770  ? 471 HOH B O    1 
HETATM 7404 O O    . HOH L 6 .   ? -14.44547 -42.00145 26.86925 1.000 38.32741  ? 472 HOH B O    1 
HETATM 7405 O O    . HOH L 6 .   ? -12.36914 -46.80099 23.32947 1.000 33.98893  ? 473 HOH B O    1 
HETATM 7406 O O    . HOH L 6 .   ? -4.56570  -14.66525 15.47247 1.000 33.68308  ? 474 HOH B O    1 
HETATM 7407 O O    . HOH L 6 .   ? -15.60471 -19.66003 27.44238 1.000 32.89973  ? 475 HOH B O    1 
HETATM 7408 O O    . HOH L 6 .   ? 10.99204  -11.84286 18.32712 1.000 27.39694  ? 476 HOH B O    1 
HETATM 7409 O O    . HOH L 6 .   ? 16.86405  -31.61537 18.02282 1.000 42.66948  ? 477 HOH B O    1 
HETATM 7410 O O    . HOH L 6 .   ? -5.50207  -40.17233 25.14445 1.000 38.76950  ? 478 HOH B O    1 
HETATM 7411 O O    . HOH L 6 .   ? -30.60498 -25.85551 21.91376 1.000 45.53634  ? 479 HOH B O    1 
HETATM 7412 O O    . HOH L 6 .   ? -10.96415 -24.10435 4.23217  1.000 38.99010  ? 480 HOH B O    1 
HETATM 7413 O O    . HOH L 6 .   ? 3.50220   -13.68889 17.34235 1.000 37.11701  ? 481 HOH B O    1 
HETATM 7414 O O    . HOH L 6 .   ? -11.31526 -37.01723 29.62324 1.000 41.52568  ? 482 HOH B O    1 
HETATM 7415 O O    . HOH L 6 .   ? 16.55356  -35.88920 26.76412 1.000 50.51529  ? 483 HOH B O    1 
HETATM 7416 O O    . HOH L 6 .   ? -20.54118 -34.53096 11.73382 1.000 30.73794  ? 484 HOH B O    1 
HETATM 7417 O O    . HOH L 6 .   ? -5.63532  -17.33153 29.52988 1.000 52.89756  ? 485 HOH B O    1 
HETATM 7418 O O    . HOH L 6 .   ? -1.64031  -37.55438 27.32841 1.000 37.82261  ? 486 HOH B O    1 
HETATM 7419 O O    . HOH L 6 .   ? -19.90851 -28.11181 33.81249 1.000 41.22268  ? 487 HOH B O    1 
HETATM 7420 O O    . HOH L 6 .   ? -1.51886  -29.08389 13.30664 1.000 33.85102  ? 488 HOH B O    1 
HETATM 7421 O O    . HOH L 6 .   ? 9.58500   -27.74255 7.47308  1.000 38.64290  ? 489 HOH B O    1 
HETATM 7422 O O    . HOH L 6 .   ? 2.96835   -26.80166 27.98998 1.000 33.69901  ? 490 HOH B O    1 
HETATM 7423 O O    . HOH L 6 .   ? 14.27721  -31.89606 23.65859 1.000 33.12929  ? 491 HOH B O    1 
HETATM 7424 O O    . HOH L 6 .   ? -1.58052  -24.92985 13.36583 1.000 32.41854  ? 492 HOH B O    1 
HETATM 7425 O O    . HOH L 6 .   ? -1.51549  -22.66047 4.48243  1.000 40.49763  ? 493 HOH B O    1 
HETATM 7426 O O    . HOH L 6 .   ? -23.31240 -28.24819 7.73256  1.000 47.35909  ? 494 HOH B O    1 
HETATM 7427 O O    . HOH L 6 .   ? -21.17268 -47.45253 4.98704  1.000 38.77382  ? 495 HOH B O    1 
HETATM 7428 O O    . HOH L 6 .   ? -19.71730 -16.15142 19.33012 1.000 34.15588  ? 496 HOH B O    1 
HETATM 7429 O O    . HOH L 6 .   ? -1.73097  -35.59809 28.44678 1.000 36.62118  ? 497 HOH B O    1 
HETATM 7430 O O    . HOH L 6 .   ? -20.19191 -32.54734 13.87267 1.000 30.79792  ? 498 HOH B O    1 
HETATM 7431 O O    . HOH L 6 .   ? -2.00136  -13.91298 6.58800  1.000 39.58946  ? 499 HOH B O    1 
HETATM 7432 O O    . HOH L 6 .   ? -20.57453 -44.03560 16.21343 1.000 22.31762  ? 500 HOH B O    1 
HETATM 7433 O O    . HOH L 6 .   ? 0.21035   -35.83062 4.16669  1.000 35.27380  ? 501 HOH B O    1 
HETATM 7434 O O    . HOH L 6 .   ? -7.07514  -31.44354 30.88043 1.000 38.04602  ? 502 HOH B O    1 
HETATM 7435 O O    . HOH L 6 .   ? -21.47221 -17.38877 8.67773  1.000 45.83450  ? 503 HOH B O    1 
HETATM 7436 O O    . HOH L 6 .   ? -17.75520 -17.42382 6.79129  1.000 46.43271  ? 504 HOH B O    1 
HETATM 7437 O O    . HOH L 6 .   ? 11.67365  -41.88955 19.90952 1.000 41.30881  ? 505 HOH B O    1 
HETATM 7438 O O    . HOH L 6 .   ? -21.82089 -17.55529 28.98264 1.000 42.62450  ? 506 HOH B O    1 
HETATM 7439 O O    . HOH L 6 .   ? -6.87267  -39.50058 5.39670  1.000 45.82802  ? 507 HOH B O    1 
HETATM 7440 O O    . HOH L 6 .   ? -14.43851 -19.03605 31.61190 1.000 47.10290  ? 508 HOH B O    1 
HETATM 7441 O O    . HOH L 6 .   ? 18.301    -30.730   31.354   1.000 39.21224  ? 509 HOH B O    1 
HETATM 7442 O O    . HOH L 6 .   ? -17.46486 -12.42779 14.00573 1.000 45.43088  ? 510 HOH B O    1 
HETATM 7443 O O    . HOH L 6 .   ? 7.19799   -39.40508 27.15731 1.000 39.46706  ? 511 HOH B O    1 
HETATM 7444 O O    . HOH L 6 .   ? 10.19170  -40.47744 23.94022 1.000 39.95603  ? 512 HOH B O    1 
HETATM 7445 O O    . HOH L 6 .   ? 11.12436  -13.33042 21.77265 1.000 36.88303  ? 513 HOH B O    1 
HETATM 7446 O O    . HOH L 6 .   ? 14.230    -16.909   34.524   1.000 48.74241  ? 514 HOH B O    1 
HETATM 7447 O O    . HOH L 6 .   ? -6.021    -42.659   6.628    1.000 43.49268  ? 515 HOH B O    1 
HETATM 7448 O O    . HOH L 6 .   ? -22.00577 -27.39939 34.84758 1.000 44.01993  ? 516 HOH B O    1 
HETATM 7449 O O    . HOH L 6 .   ? -21.81646 -33.22230 9.95585  1.000 38.28552  ? 517 HOH B O    1 
HETATM 7450 O O    . HOH L 6 .   ? 3.47088   -18.45571 3.29946  1.000 41.58548  ? 518 HOH B O    1 
HETATM 7451 O O    . HOH L 6 .   ? -1.07048  -38.72973 -2.37558 1.000 46.84155  ? 519 HOH B O    1 
HETATM 7452 O O    . HOH L 6 .   ? 1.12486   -38.87793 -4.54580 1.000 41.06234  ? 520 HOH B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LYS A 17  ? 0.44169 0.91648 0.88106 0.07423  0.04597  0.07450  3   LYS A N   
2    C CA  A LYS A 17  ? 0.36474 0.80214 0.80286 0.05048  0.03347  0.08823  3   LYS A CA  
3    C CA  B LYS A 17  ? 0.36838 0.80570 0.80655 0.05053  0.03342  0.08818  3   LYS A CA  
4    C C   . LYS A 17  ? 0.37268 0.76082 0.76299 0.06272  0.04511  0.06188  3   LYS A C   
5    O O   . LYS A 17  ? 0.33426 0.68442 0.70661 0.08224  0.04165  0.03956  3   LYS A O   
6    C CB  A LYS A 17  ? 0.40880 0.81422 0.88323 0.03793  -0.00266 0.09847  3   LYS A CB  
7    C CB  B LYS A 17  ? 0.40747 0.81284 0.88180 0.03836  -0.00264 0.09808  3   LYS A CB  
8    C CG  A LYS A 17  ? 0.40421 0.76263 0.88390 0.01612  -0.02610 0.10877  3   LYS A CG  
9    C CG  B LYS A 17  ? 0.40417 0.75768 0.88011 0.01965  -0.02577 0.10422  3   LYS A CG  
10   C CD  A LYS A 17  ? 0.38846 0.77391 0.87796 -0.00954 -0.02097 0.14094  3   LYS A CD  
11   C CD  B LYS A 17  ? 0.39152 0.76545 0.87933 -0.00767 -0.02470 0.13588  3   LYS A CD  
12   C CE  A LYS A 17  ? 0.42302 0.75425 0.92511 -0.03036 -0.05500 0.15091  3   LYS A CE  
13   C CE  B LYS A 17  ? 0.41877 0.73358 0.91284 -0.02382 -0.05733 0.13847  3   LYS A CE  
14   N NZ  A LYS A 17  ? 0.44794 0.74456 0.99033 -0.04221 -0.10155 0.16039  3   LYS A NZ  
15   N NZ  B LYS A 17  ? 0.38676 0.71327 0.88745 -0.04783 -0.05757 0.17043  3   LYS A NZ  
39   N N   . GLY A 18  ? 0.27611 0.66323 0.64434 0.05080  0.05748  0.06786  4   GLY A N   
40   C CA  . GLY A 18  ? 0.23869 0.58148 0.56218 0.05908  0.06822  0.04578  4   GLY A CA  
41   C C   . GLY A 18  ? 0.28654 0.57929 0.61084 0.05939  0.05254  0.04123  4   GLY A C   
42   O O   . GLY A 18  ? 0.26805 0.52132 0.55482 0.07224  0.06072  0.02226  4   GLY A O   
46   N N   . GLU A 19  ? 0.25062 0.53792 0.61725 0.04561  0.02458  0.05722  5   GLU A N   
47   C CA  . GLU A 19  ? 0.29117 0.51145 0.62978 0.05020  0.00021  0.03827  5   GLU A CA  
48   C C   . GLU A 19  ? 0.26173 0.45618 0.57143 0.07339  0.00014  0.01748  5   GLU A C   
49   O O   . GLU A 19  ? 0.32805 0.47999 0.59237 0.08365  -0.00329 0.00149  5   GLU A O   
50   C CB  . GLU A 19  ? 0.31509 0.52368 0.69775 0.03542  -0.04208 0.05054  5   GLU A CB  
53   N N   . GLU A 20  ? 0.27205 0.49888 0.60889 0.08275  0.00343  0.02083  6   GLU A N   
54   C CA  . GLU A 20  ? 0.29003 0.49051 0.60323 0.10424  -0.00051 0.00406  6   GLU A CA  
55   C C   . GLU A 20  ? 0.31574 0.48576 0.57818 0.11498  0.01787  -0.00931 6   GLU A C   
56   O O   . GLU A 20  ? 0.30599 0.44190 0.54149 0.12687  0.00933  -0.01674 6   GLU A O   
57   C CB  . GLU A 20  ? 0.23706 0.48400 0.59118 0.11525  0.00074  0.00879  6   GLU A CB  
60   N N   . LEU A 21  ? 0.27269 0.45556 0.52460 0.10977  0.03904  -0.00902 7   LEU A N   
61   C CA  . LEU A 21  ? 0.28484 0.43529 0.49698 0.11673  0.04894  -0.01976 7   LEU A CA  
62   C C   . LEU A 21  ? 0.29780 0.40980 0.47451 0.10739  0.04442  -0.01666 7   LEU A C   
63   O O   . LEU A 21  ? 0.33576 0.42080 0.48594 0.10913  0.04652  -0.01712 7   LEU A O   
64   C CB  . LEU A 21  ? 0.21511 0.39320 0.42630 0.11690  0.06856  -0.02330 7   LEU A CB  
65   C CG  . LEU A 21  ? 0.24089 0.46391 0.47469 0.12504  0.07368  -0.02743 7   LEU A CG  
66   C CD1 . LEU A 21  ? 0.28643 0.53172 0.50787 0.11668  0.08832  -0.02731 7   LEU A CD1 
67   C CD2 . LEU A 21  ? 0.30690 0.50770 0.53123 0.14965  0.06572  -0.04310 7   LEU A CD2 
79   N N   . PHE A 22  ? 0.28267 0.39517 0.46133 0.09953  0.03425  -0.01271 8   PHE A N   
80   C CA  . PHE A 22  ? 0.28273 0.37590 0.42662 0.09808  0.03113  -0.01273 8   PHE A CA  
81   C C   . PHE A 22  ? 0.29487 0.37852 0.42336 0.11297  0.01023  -0.01619 8   PHE A C   
82   O O   . PHE A 22  ? 0.31872 0.40140 0.41907 0.11980  0.00415  -0.01929 8   PHE A O   
83   C CB  . PHE A 22  ? 0.32952 0.43043 0.48008 0.08592  0.03091  -0.01237 8   PHE A CB  
84   C CG  . PHE A 22  ? 0.28375 0.39752 0.43761 0.07339  0.05260  -0.00776 8   PHE A CG  
85   C CD1 . PHE A 22  ? 0.28283 0.42786 0.46841 0.06926  0.06129  -0.00225 8   PHE A CD1 
86   C CD2 . PHE A 22  ? 0.28047 0.38425 0.40568 0.06835  0.06373  -0.00788 8   PHE A CD2 
87   C CE1 . PHE A 22  ? 0.22483 0.38929 0.40718 0.06383  0.08020  -0.00025 8   PHE A CE1 
88   C CE2 . PHE A 22  ? 0.31771 0.43163 0.44357 0.05921  0.08014  -0.00632 8   PHE A CE2 
89   C CZ  . PHE A 22  ? 0.22002 0.36350 0.37134 0.05870  0.08810  -0.00416 8   PHE A CZ  
99   N N   . THR A 23  ? 0.37033 0.45284 0.51415 0.12265  -0.00169 -0.01741 9   THR A N   
100  C CA  . THR A 23  ? 0.41985 0.49680 0.54939 0.13989  -0.02548 -0.02316 9   THR A CA  
101  C C   . THR A 23  ? 0.40672 0.48479 0.48835 0.15099  -0.02105 -0.01526 9   THR A C   
102  O O   . THR A 23  ? 0.58694 0.67458 0.64160 0.16959  -0.03632 -0.02285 9   THR A O   
103  C CB  . THR A 23  ? 0.41171 0.48864 0.56751 0.14757  -0.03802 -0.02370 9   THR A CB  
104  O OG1 . THR A 23  ? 0.43730 0.51025 0.59482 0.14638  -0.02219 -0.01646 9   THR A OG1 
105  C CG2 . THR A 23  ? 0.42564 0.51806 0.63428 0.13824  -0.05003 -0.02555 9   THR A CG2 
113  N N   . GLY A 24  ? 0.43581 0.50931 0.50834 0.14176  -0.00415 0.00152  10  GLY A N   
114  C CA  . GLY A 24  ? 0.40796 0.49362 0.44575 0.14557  -0.00078 0.02247  10  GLY A CA  
115  C C   . GLY A 24  ? 0.47940 0.57348 0.50658 0.13006  0.01729  0.03461  10  GLY A C   
116  O O   . GLY A 24  ? 0.48799 0.58250 0.52167 0.12366  0.02499  0.02041  10  GLY A O   
120  N N   . VAL A 25  ? 0.34839 0.45058 0.36371 0.12172  0.02097  0.06511  11  VAL A N   
121  C CA  . VAL A 25  ? 0.35899 0.47087 0.37108 0.10375  0.03433  0.08238  11  VAL A CA  
122  C C   . VAL A 25  ? 0.39618 0.46495 0.43532 0.08574  0.03384  0.07845  11  VAL A C   
123  O O   . VAL A 25  ? 0.43762 0.47657 0.49178 0.08498  0.01964  0.08367  11  VAL A O   
124  C CB  . VAL A 25  ? 0.39233 0.54340 0.38747 0.10019  0.03409  0.12574  11  VAL A CB  
125  C CG1 . VAL A 25  ? 0.41700 0.58163 0.41804 0.07798  0.04484  0.14806  11  VAL A CG1 
126  C CG2 . VAL A 25  ? 0.40370 0.61111 0.36384 0.12931  0.03444  0.12354  11  VAL A CG2 
136  N N   . VAL A 26  ? 0.33761 0.40346 0.38103 0.07574  0.04579  0.06626  12  VAL A N   
137  C CA  . VAL A 26  ? 0.36215 0.39497 0.42460 0.06731  0.04479  0.05309  12  VAL A CA  
138  C C   . VAL A 26  ? 0.33678 0.36531 0.39829 0.04823  0.04557  0.07149  12  VAL A C   
139  O O   . VAL A 26  ? 0.29388 0.35153 0.34334 0.04263  0.05885  0.07707  12  VAL A O   
140  C CB  . VAL A 26  ? 0.32388 0.36355 0.39510 0.07291  0.05633  0.02405  12  VAL A CB  
141  C CG1 . VAL A 26  ? 0.35471 0.37565 0.43793 0.07208  0.05658  0.00941  12  VAL A CG1 
142  C CG2 . VAL A 26  ? 0.33005 0.37840 0.41270 0.08730  0.05100  0.01197  12  VAL A CG2 
152  N N   . PRO A 27  ? 0.30803 0.29910 0.38492 0.03915  0.02662  0.08001  13  PRO A N   
153  C CA  . PRO A 27  ? 0.32071 0.30381 0.40418 0.01816  0.02044  0.09855  13  PRO A CA  
154  C C   . PRO A 27  ? 0.34642 0.32643 0.42594 0.01956  0.03301  0.06865  13  PRO A C   
155  O O   . PRO A 27  ? 0.33256 0.30586 0.41132 0.03612  0.03861  0.03559  13  PRO A O   
156  C CB  . PRO A 27  ? 0.36138 0.29154 0.46781 0.01163  -0.01581 0.11034  13  PRO A CB  
157  C CG  . PRO A 27  ? 0.41501 0.32149 0.52287 0.03733  -0.02234 0.07663  13  PRO A CG  
158  C CD  . PRO A 27  ? 0.38816 0.33860 0.48038 0.04952  0.00317  0.07141  13  PRO A CD  
166  N N   . ILE A 28  ? 0.31949 0.31366 0.39805 0.00220  0.03761  0.08469  14  ILE A N   
167  C CA  . ILE A 28  ? 0.28981 0.28699 0.36187 0.00172  0.04988  0.06183  14  ILE A CA  
168  C C   . ILE A 28  ? 0.33792 0.30678 0.42401 -0.01574 0.02876  0.07223  14  ILE A C   
169  O O   . ILE A 28  ? 0.31048 0.28263 0.41257 -0.03637 0.01409  0.11115  14  ILE A O   
170  C CB  . ILE A 28  ? 0.29857 0.34310 0.35521 0.00105  0.07423  0.06566  14  ILE A CB  
171  C CG1 . ILE A 28  ? 0.33583 0.39903 0.38311 0.01885  0.08382  0.05339  14  ILE A CG1 
172  C CG2 . ILE A 28  ? 0.26540 0.31031 0.31741 -0.00144 0.08376  0.04608  14  ILE A CG2 
173  C CD1 . ILE A 28  ? 0.32840 0.43113 0.36038 0.02488  0.09523  0.05504  14  ILE A CD1 
185  N N   . LEU A 29  ? 0.38445 0.33101 0.46671 -0.00714 0.02458  0.04024  15  LEU A N   
186  C CA  . LEU A 29  ? 0.33905 0.25779 0.43152 -0.02019 0.00218  0.04135  15  LEU A CA  
187  C C   . LEU A 29  ? 0.33555 0.27708 0.40971 -0.01480 0.02370  0.01840  15  LEU A C   
188  O O   . LEU A 29  ? 0.33131 0.28780 0.38978 0.00599  0.04085  -0.00985 15  LEU A O   
189  C CB  . LEU A 29  ? 0.38013 0.23752 0.48401 -0.00674 -0.03882 0.01829  15  LEU A CB  
190  C CG  . LEU A 29  ? 0.42081 0.24162 0.55060 -0.01681 -0.07310 0.04616  15  LEU A CG  
191  C CD1 . LEU A 29  ? 0.49425 0.24927 0.63171 0.00766  -0.11807 0.00988  15  LEU A CD1 
192  C CD2 . LEU A 29  ? 0.43618 0.25922 0.59500 -0.05565 -0.09175 0.10087  15  LEU A CD2 
204  N N   . VAL A 30  ? 0.29358 0.24439 0.37327 -0.03475 0.02209  0.03559  16  VAL A N   
205  C CA  . VAL A 30  ? 0.38646 0.35833 0.45004 -0.03232 0.03967  0.01885  16  VAL A CA  
206  C C   . VAL A 30  ? 0.38489 0.32335 0.45743 -0.04060 0.01058  0.01227  16  VAL A C   
207  O O   . VAL A 30  ? 0.36316 0.28409 0.46271 -0.06347 -0.01541 0.04136  16  VAL A O   
208  C CB  . VAL A 30  ? 0.31477 0.33626 0.37432 -0.04357 0.06542  0.04148  16  VAL A CB  
209  C CG1 . VAL A 30  ? 0.31441 0.35136 0.35997 -0.04161 0.07845  0.02543  16  VAL A CG1 
210  C CG2 . VAL A 30  ? 0.26304 0.30959 0.31379 -0.03136 0.08415  0.04272  16  VAL A CG2 
220  N N   . GLU A 31  ? 0.32356 0.25791 0.37583 -0.02220 0.01210  -0.02270 17  GLU A N   
221  C CA  . GLU A 31  ? 0.39382 0.29835 0.44773 -0.02376 -0.01683 -0.03731 17  GLU A CA  
222  C C   . GLU A 31  ? 0.39314 0.33425 0.42526 -0.02140 0.00818  -0.04672 17  GLU A C   
223  O O   . GLU A 31  ? 0.34718 0.32038 0.35651 -0.00262 0.03464  -0.06294 17  GLU A O   
224  C CB  . GLU A 31  ? 0.46261 0.32285 0.50717 0.00769  -0.05059 -0.07942 17  GLU A CB  
225  C CG  . GLU A 31  ? 0.57327 0.37503 0.64716 0.00225  -0.09607 -0.07131 17  GLU A CG  
226  C CD  . GLU A 31  ? 0.59513 0.40646 0.67252 0.00856  -0.08090 -0.06114 17  GLU A CD  
227  O OE1 . GLU A 31  ? 0.67161 0.52520 0.72596 0.02934  -0.04429 -0.07710 17  GLU A OE1 
228  O OE2 . GLU A 31  ? 0.53253 0.31113 0.63924 -0.00906 -0.10830 -0.03323 17  GLU A OE2 
235  N N   . LEU A 32  ? 0.36060 0.30009 0.40436 -0.04222 -0.00276 -0.03191 18  LEU A N   
236  C CA  . LEU A 32  ? 0.38120 0.35096 0.40707 -0.04197 0.01564  -0.03817 18  LEU A CA  
237  C C   . LEU A 32  ? 0.40770 0.34559 0.43630 -0.04360 -0.01933 -0.05324 18  LEU A C   
238  O O   . LEU A 32  ? 0.36521 0.27993 0.42668 -0.06793 -0.04842 -0.03086 18  LEU A O   
239  C CB  . LEU A 32  ? 0.41323 0.42472 0.45028 -0.06308 0.04004  -0.00478 18  LEU A CB  
240  C CG  . LEU A 32  ? 0.35020 0.38566 0.37747 -0.06723 0.04945  -0.00628 18  LEU A CG  
241  C CD1 . LEU A 32  ? 0.37521 0.42200 0.37156 -0.04633 0.06482  -0.03159 18  LEU A CD1 
242  C CD2 . LEU A 32  ? 0.42292 0.50184 0.46015 -0.07859 0.06978  0.02058  18  LEU A CD2 
254  N N   . ASP A 33  ? 0.48393 0.42618 0.48037 -0.01771 -0.01897 -0.08791 19  ASP A N   
255  C CA  . ASP A 33  ? 0.47007 0.39036 0.46043 -0.01419 -0.04941 -0.10703 19  ASP A CA  
256  C C   . ASP A 33  ? 0.49111 0.45604 0.46689 -0.02220 -0.02071 -0.09659 19  ASP A C   
257  O O   . ASP A 33  ? 0.44271 0.44717 0.39010 -0.00533 0.00948  -0.10425 19  ASP A O   
258  C CB  . ASP A 33  ? 0.62798 0.52815 0.58633 0.02898  -0.07387 -0.15737 19  ASP A CB  
259  C CG  . ASP A 33  ? 0.82142 0.65299 0.80099 0.03647  -0.12818 -0.17484 19  ASP A CG  
260  O OD1 . ASP A 33  ? 0.71817 0.51909 0.74197 0.00104  -0.14733 -0.13952 19  ASP A OD1 
261  O OD2 . ASP A 33  ? 1.05923 0.87150 1.01231 0.07991  -0.15470 -0.22260 19  ASP A OD2 
266  N N   . GLY A 34  ? 0.43087 0.39309 0.43092 -0.04908 -0.03263 -0.07485 20  GLY A N   
267  C CA  . GLY A 34  ? 0.37797 0.38042 0.36982 -0.05767 -0.00836 -0.06228 20  GLY A CA  
268  C C   . GLY A 34  ? 0.41798 0.40928 0.40097 -0.05528 -0.03306 -0.07853 20  GLY A C   
269  O O   . GLY A 34  ? 0.40995 0.35803 0.40680 -0.05654 -0.07625 -0.09172 20  GLY A O   
273  N N   . ASP A 35  ? 0.48044 0.50681 0.44246 -0.05180 -0.01130 -0.07731 21  ASP A N   
274  C CA  . ASP A 35  ? 0.45525 0.47748 0.40570 -0.04882 -0.03203 -0.09101 21  ASP A CA  
275  C C   . ASP A 35  ? 0.44757 0.51112 0.39643 -0.05966 -0.00527 -0.06963 21  ASP A C   
276  O O   . ASP A 35  ? 0.43930 0.53090 0.36090 -0.04668 0.01906  -0.07052 21  ASP A O   
277  C CB  . ASP A 35  ? 0.48332 0.50134 0.38831 -0.01207 -0.04328 -0.13073 21  ASP A CB  
278  C CG  . ASP A 35  ? 0.53280 0.53996 0.42312 -0.00444 -0.07360 -0.15065 21  ASP A CG  
279  O OD1 . ASP A 35  ? 0.59168 0.59509 0.51088 -0.03132 -0.08374 -0.13066 21  ASP A OD1 
280  O OD2 . ASP A 35  ? 0.59359 0.60214 0.44264 0.03186  -0.08832 -0.18729 21  ASP A OD2 
285  N N   . VAL A 36  ? 0.39949 0.47029 0.38186 -0.08310 -0.01303 -0.04755 22  VAL A N   
286  C CA  . VAL A 36  ? 0.35850 0.46609 0.34355 -0.08950 0.00524  -0.03083 22  VAL A CA  
287  C C   . VAL A 36  ? 0.39183 0.49603 0.38038 -0.09480 -0.01960 -0.03631 22  VAL A C   
288  O O   . VAL A 36  ? 0.34497 0.43900 0.36886 -0.11268 -0.04594 -0.02662 22  VAL A O   
289  C CB  . VAL A 36  ? 0.32897 0.46638 0.34834 -0.10415 0.01982  -0.00176 22  VAL A CB  
290  C CG1 . VAL A 36  ? 0.34731 0.52125 0.37099 -0.10399 0.02901  0.00834  22  VAL A CG1 
291  C CG2 . VAL A 36  ? 0.33213 0.47240 0.34333 -0.09550 0.04260  0.00045  22  VAL A CG2 
301  N N   . ASN A 37  ? 0.39287 0.50845 0.34893 -0.08143 -0.01394 -0.04712 23  ASN A N   
302  C CA  . ASN A 37  ? 0.38202 0.49527 0.33491 -0.08270 -0.03779 -0.05507 23  ASN A CA  
303  C C   . ASN A 37  ? 0.45225 0.52472 0.40610 -0.07902 -0.07818 -0.07908 23  ASN A C   
304  O O   . ASN A 37  ? 0.45371 0.51447 0.43249 -0.09208 -0.10981 -0.07801 23  ASN A O   
305  C CB  . ASN A 37  ? 0.33830 0.47836 0.33074 -0.10243 -0.03846 -0.03028 23  ASN A CB  
306  C CG  . ASN A 37  ? 0.35118 0.52243 0.33256 -0.09564 -0.01487 -0.01990 23  ASN A CG  
307  O OD1 . ASN A 37  ? 0.32182 0.49464 0.27967 -0.08461 0.00487  -0.02055 23  ASN A OD1 
308  N ND2 . ASN A 37  ? 0.33762 0.53343 0.34045 -0.10203 -0.02191 -0.00922 23  ASN A ND2 
315  N N   . GLY A 38  ? 0.45438 0.50432 0.38351 -0.05896 -0.08214 -0.10241 24  GLY A N   
316  C CA  . GLY A 38  ? 0.50574 0.50860 0.43177 -0.04639 -0.12864 -0.13406 24  GLY A CA  
317  C C   . GLY A 38  ? 0.55141 0.51630 0.53334 -0.07277 -0.16008 -0.11894 24  GLY A C   
318  O O   . GLY A 38  ? 0.62105 0.53467 0.61135 -0.06622 -0.21187 -0.14343 24  GLY A O   
322  N N   . HIS A 39  ? 0.65398 0.43678 0.41633 -0.19872 -0.16184 0.06929  25  HIS A N   
323  C CA  . HIS A 39  ? 0.71247 0.49168 0.51550 -0.17282 -0.14817 0.05552  25  HIS A CA  
324  C C   . HIS A 39  ? 0.66552 0.46633 0.46812 -0.15358 -0.11512 0.03791  25  HIS A C   
325  O O   . HIS A 39  ? 0.54644 0.36234 0.36528 -0.14775 -0.10365 0.04488  25  HIS A O   
326  C CB  . HIS A 39  ? 0.64797 0.42054 0.51540 -0.16436 -0.16093 0.07086  25  HIS A CB  
327  C CG  . HIS A 39  ? 0.72927 0.48039 0.60903 -0.18020 -0.19684 0.08589  25  HIS A CG  
328  N ND1 . HIS A 39  ? 0.77473 0.50969 0.65960 -0.18202 -0.20919 0.08164  25  HIS A ND1 
329  C CD2 . HIS A 39  ? 0.72151 0.46885 0.61203 -0.18961 -0.22374 0.10499  25  HIS A CD2 
330  C CE1 . HIS A 39  ? 0.81473 0.54505 0.71275 -0.18677 -0.23637 0.09667  25  HIS A CE1 
331  N NE2 . HIS A 39  ? 0.69057 0.42715 0.59238 -0.19053 -0.24677 0.11091  25  HIS A NE2 
339  N N   . LYS A 40  ? 0.66467 0.46464 0.45217 -0.14333 -0.10385 0.01407  26  LYS A N   
340  C CA  . LYS A 40  ? 0.66905 0.48739 0.45511 -0.12576 -0.07815 -0.00595 26  LYS A CA  
341  C C   . LYS A 40  ? 0.53363 0.34550 0.36541 -0.10560 -0.07059 -0.00195 26  LYS A C   
342  O O   . LYS A 40  ? 0.57229 0.36632 0.43088 -0.10481 -0.08294 0.00726  26  LYS A O   
343  C CB  . LYS A 40  ? 0.65288 0.47362 0.40864 -0.12251 -0.07443 -0.03867 26  LYS A CB  
344  C CG  . LYS A 40  ? 0.74143 0.58074 0.44323 -0.14611 -0.07622 -0.04867 26  LYS A CG  
345  C CD  . LYS A 40  ? 0.77011 0.62058 0.44988 -0.13869 -0.06927 -0.09153 26  LYS A CD  
346  C CE  . LYS A 40  ? 0.92645 0.79879 0.54718 -0.16743 -0.07241 -0.10390 26  LYS A CE  
347  N NZ  . LYS A 40  ? 1.01532 0.88011 0.62251 -0.16194 -0.08068 -0.14169 26  LYS A NZ  
361  N N   . PHE A 41  ? 0.51234 0.34190 0.35089 -0.09253 -0.05066 -0.00817 27  PHE A N   
362  C CA  . PHE A 41  ? 0.49746 0.32386 0.36943 -0.07705 -0.04308 -0.00480 27  PHE A CA  
363  C C   . PHE A 41  ? 0.46148 0.30304 0.32722 -0.06292 -0.02595 -0.02177 27  PHE A C   
364  O O   . PHE A 41  ? 0.50650 0.36910 0.34895 -0.06594 -0.01588 -0.03304 27  PHE A O   
365  C CB  . PHE A 41  ? 0.47592 0.31158 0.37983 -0.07920 -0.04109 0.01649  27  PHE A CB  
366  C CG  . PHE A 41  ? 0.44437 0.29953 0.34417 -0.08176 -0.03317 0.02185  27  PHE A CG  
367  C CD1 . PHE A 41  ? 0.49816 0.35174 0.38446 -0.09756 -0.04719 0.03118  27  PHE A CD1 
368  C CD2 . PHE A 41  ? 0.41064 0.28259 0.32011 -0.07076 -0.01607 0.01992  27  PHE A CD2 
369  C CE1 . PHE A 41  ? 0.52328 0.38994 0.40747 -0.10298 -0.04576 0.03953  27  PHE A CE1 
370  C CE2 . PHE A 41  ? 0.39238 0.27952 0.30037 -0.07406 -0.01200 0.02539  27  PHE A CE2 
371  C CZ  . PHE A 41  ? 0.48371 0.36736 0.38012 -0.09048 -0.02759 0.03579  27  PHE A CZ  
381  N N   . SER A 42  ? 0.45299 0.28526 0.34040 -0.05024 -0.02474 -0.02228 28  SER A N   
382  C CA  . SER A 42  ? 0.46908 0.31105 0.35875 -0.03503 -0.01427 -0.03797 28  SER A CA  
383  C C   . SER A 42  ? 0.43706 0.27830 0.34959 -0.03041 -0.01022 -0.02049 28  SER A C   
384  O O   . SER A 42  ? 0.48996 0.31547 0.41689 -0.03627 -0.02008 -0.00493 28  SER A O   
385  C CB  . SER A 42  ? 0.50425 0.32873 0.39431 -0.02360 -0.02638 -0.06460 28  SER A CB  
386  O OG  . SER A 42  ? 0.66585 0.49590 0.53140 -0.02985 -0.02905 -0.08506 28  SER A OG  
392  N N   . VAL A 43  ? 0.41358 0.27516 0.32743 -0.02302 0.00418  -0.02290 29  VAL A N   
393  C CA  . VAL A 43  ? 0.44556 0.31046 0.37489 -0.01999 0.00886  -0.00884 29  VAL A CA  
394  C C   . VAL A 43  ? 0.45535 0.31890 0.38883 -0.00504 0.00828  -0.02326 29  VAL A C   
395  O O   . VAL A 43  ? 0.41022 0.29056 0.33792 0.00310  0.01622  -0.04373 29  VAL A O   
396  C CB  . VAL A 43  ? 0.45828 0.34816 0.39123 -0.02494 0.02302  0.00229  29  VAL A CB  
397  C CG1 . VAL A 43  ? 0.41998 0.31784 0.36491 -0.02301 0.02904  0.01247  29  VAL A CG1 
398  C CG2 . VAL A 43  ? 0.38834 0.27896 0.32778 -0.03719 0.01819  0.01304  29  VAL A CG2 
408  N N   . SER A 44  ? 0.43996 0.28587 0.38477 -0.00389 -0.00296 -0.01220 30  SER A N   
409  C CA  . SER A 44  ? 0.46081 0.30098 0.41577 0.00955  -0.00992 -0.02116 30  SER A CA  
410  C C   . SER A 44  ? 0.48256 0.33435 0.43740 0.00370  -0.00234 -0.00092 30  SER A C   
411  O O   . SER A 44  ? 0.42346 0.27473 0.37493 -0.01206 -0.00241 0.02090  30  SER A O   
412  C CB  . SER A 44  ? 0.48915 0.29073 0.45719 0.01368  -0.03946 -0.02415 30  SER A CB  
413  O OG  . SER A 44  ? 0.50730 0.30055 0.47780 0.02245  -0.04707 -0.05111 30  SER A OG  
419  N N   . GLY A 45  ? 0.41565 0.28276 0.37470 0.01494  0.00490  -0.01040 31  GLY A N   
420  C CA  . GLY A 45  ? 0.42568 0.30479 0.38232 0.01007  0.01135  0.00525  31  GLY A CA  
421  C C   . GLY A 45  ? 0.37349 0.24291 0.34145 0.02194  -0.00234 -0.00027 31  GLY A C   
422  O O   . GLY A 45  ? 0.37139 0.23973 0.35503 0.03862  -0.00826 -0.02406 31  GLY A O   
426  N N   . GLU A 46  ? 0.38314 0.24879 0.34454 0.01202  -0.00838 0.02016  32  GLU A N   
427  C CA  . GLU A 46  ? 0.41506 0.26984 0.38681 0.02076  -0.02528 0.01948  32  GLU A CA  
428  C C   . GLU A 46  ? 0.39816 0.26854 0.35278 0.00731  -0.01754 0.03857  32  GLU A C   
429  O O   . GLU A 46  ? 0.35327 0.24094 0.29084 -0.00951 -0.00224 0.05109  32  GLU A O   
430  C CB  . GLU A 46  ? 0.40777 0.21905 0.39122 0.02027  -0.06250 0.02652  32  GLU A CB  
431  C CG  . GLU A 46  ? 0.44188 0.23384 0.40410 -0.00801 -0.07840 0.06225  32  GLU A CG  
432  C CD  . GLU A 46  ? 0.51878 0.26061 0.49457 -0.01114 -0.12277 0.07271  32  GLU A CD  
433  O OE1 . GLU A 46  ? 0.53746 0.25937 0.53105 -0.00038 -0.13434 0.05656  32  GLU A OE1 
434  O OE2 . GLU A 46  ? 0.62222 0.34241 0.59109 -0.02541 -0.14963 0.09708  32  GLU A OE2 
441  N N   . GLY A 47  ? 0.37780 0.24479 0.34022 0.01533  -0.02921 0.03721  33  GLY A N   
442  C CA  . GLY A 47  ? 0.39562 0.27701 0.33993 0.00307  -0.02446 0.05237  33  GLY A CA  
443  C C   . GLY A 47  ? 0.38142 0.26669 0.34303 0.01968  -0.03157 0.04076  33  GLY A C   
444  O O   . GLY A 47  ? 0.39849 0.26643 0.38775 0.03659  -0.05151 0.02740  33  GLY A O   
448  N N   . GLU A 48  ? 0.36866 0.27920 0.31850 0.01551  -0.01597 0.04266  34  GLU A N   
449  C CA  . GLU A 48  ? 0.41094 0.32765 0.37664 0.02839  -0.02290 0.03406  34  GLU A CA  
450  C C   . GLU A 48  ? 0.42539 0.37614 0.38453 0.02802  0.00289  0.02711  34  GLU A C   
451  O O   . GLU A 48  ? 0.36842 0.33418 0.30844 0.01552  0.01995  0.03196  34  GLU A O   
452  C CB  . GLU A 48  ? 0.49162 0.38311 0.44720 0.01763  -0.05412 0.05479  34  GLU A CB  
453  C CG  . GLU A 48  ? 0.53476 0.42939 0.44780 -0.01236 -0.05168 0.08009  34  GLU A CG  
454  C CD  . GLU A 48  ? 0.70439 0.57335 0.60002 -0.02938 -0.08627 0.10498  34  GLU A CD  
455  O OE1 . GLU A 48  ? 0.74306 0.57512 0.66171 -0.02100 -0.12164 0.10937  34  GLU A OE1 
456  O OE2 . GLU A 48  ? 0.76376 0.64981 0.62392 -0.05178 -0.08054 0.11867  34  GLU A OE2 
463  N N   . GLY A 49  ? 0.38616 0.35005 0.36691 0.04214  0.00328  0.01354  35  GLY A N   
464  C CA  . GLY A 49  ? 0.32551 0.31679 0.30457 0.04158  0.02102  0.00802  35  GLY A CA  
465  C C   . GLY A 49  ? 0.33803 0.33057 0.32388 0.04495  0.00702  0.00960  35  GLY A C   
466  O O   . GLY A 49  ? 0.34315 0.32482 0.35200 0.05585  -0.01251 0.00531  35  GLY A O   
470  N N   . ASP A 50  ? 0.35088 0.35711 0.32072 0.03654  0.01482  0.01300  36  ASP A N   
471  C CA  . ASP A 50  ? 0.33274 0.34025 0.30252 0.03632  0.00117  0.01593  36  ASP A CA  
472  C C   . ASP A 50  ? 0.36450 0.39739 0.34636 0.04022  0.01629  0.00406  36  ASP A C   
473  O O   . ASP A 50  ? 0.33673 0.37934 0.30213 0.03185  0.02595  0.00289  36  ASP A O   
474  C CB  . ASP A 50  ? 0.37134 0.36948 0.30282 0.01702  -0.00848 0.03234  36  ASP A CB  
475  C CG  . ASP A 50  ? 0.43887 0.43282 0.36526 0.01422  -0.02856 0.03816  36  ASP A CG  
476  O OD1 . ASP A 50  ? 0.52175 0.52250 0.47898 0.02903  -0.03296 0.02787  36  ASP A OD1 
477  O OD2 . ASP A 50  ? 0.54012 0.52670 0.43036 -0.00556 -0.04045 0.05363  36  ASP A OD2 
482  N N   . ALA A 51  ? 0.38303 0.42908 0.39699 0.05184  0.01678  -0.00655 37  ALA A N   
483  C CA  . ALA A 51  ? 0.40087 0.47023 0.42756 0.05106  0.02893  -0.01392 37  ALA A CA  
484  C C   . ALA A 51  ? 0.35341 0.42497 0.37445 0.04721  0.02001  -0.01181 37  ALA A C   
485  O O   . ALA A 51  ? 0.38119 0.46297 0.40318 0.04264  0.02663  -0.01534 37  ALA A O   
486  C CB  . ALA A 51  ? 0.39058 0.48238 0.45115 0.05894  0.03290  -0.02553 37  ALA A CB  
492  N N   . THR A 52  ? 0.35124 0.41075 0.36748 0.04820  0.00104  -0.00608 38  THR A N   
493  C CA  . THR A 52  ? 0.34103 0.40175 0.34576 0.04253  -0.00902 -0.00449 38  THR A CA  
494  C C   . THR A 52  ? 0.33633 0.39994 0.31079 0.03166  0.00181  -0.00716 38  THR A C   
495  O O   . THR A 52  ? 0.33014 0.40230 0.30319 0.02915  0.00007  -0.01478 38  THR A O   
496  C CB  . THR A 52  ? 0.42391 0.46591 0.41881 0.04042  -0.03505 0.00649  38  THR A CB  
497  O OG1 . THR A 52  ? 0.46909 0.51261 0.50574 0.05447  -0.04850 0.00207  38  THR A OG1 
498  C CG2 . THR A 52  ? 0.46265 0.50606 0.43637 0.03102  -0.04583 0.00822  38  THR A CG2 
506  N N   . TYR A 53  ? 0.34433 0.40353 0.29902 0.02566  0.01198  -0.00422 39  TYR A N   
507  C CA  . TYR A 53  ? 0.34123 0.41191 0.27623 0.01674  0.02460  -0.01289 39  TYR A CA  
508  C C   . TYR A 53  ? 0.29876 0.37499 0.25079 0.02106  0.04041  -0.02019 39  TYR A C   
509  O O   . TYR A 53  ? 0.32648 0.41401 0.27241 0.01631  0.05009  -0.03082 39  TYR A O   
510  C CB  . TYR A 53  ? 0.38376 0.45207 0.28027 0.00044  0.02243  -0.00327 39  TYR A CB  
511  C CG  . TYR A 53  ? 0.43350 0.49665 0.30402 -0.01049 0.00345  0.00583  39  TYR A CG  
512  C CD1 . TYR A 53  ? 0.37523 0.45750 0.22462 -0.02005 0.00551  -0.00690 39  TYR A CD1 
513  C CD2 . TYR A 53  ? 0.46715 0.50568 0.33634 -0.01137 -0.01991 0.02528  39  TYR A CD2 
514  C CE1 . TYR A 53  ? 0.41842 0.49599 0.23848 -0.03328 -0.01362 0.00265  39  TYR A CE1 
515  C CE2 . TYR A 53  ? 0.51656 0.54627 0.36159 -0.02363 -0.04299 0.03689  39  TYR A CE2 
516  C CZ  . TYR A 53  ? 0.45017 0.49978 0.26684 -0.03612 -0.03898 0.02709  39  TYR A CZ  
517  O OH  . TYR A 53  ? 0.45950 0.50058 0.24650 -0.05150 -0.06349 0.03970  39  TYR A OH  
527  N N   . GLY A 54  ? 0.30693 0.37883 0.28143 0.02881  0.04225  -0.01666 40  GLY A N   
528  C CA  . GLY A 54  ? 0.30839 0.38249 0.29417 0.02932  0.05320  -0.01971 40  GLY A CA  
529  C C   . GLY A 54  ? 0.33708 0.40779 0.30697 0.02406  0.06113  -0.01801 40  GLY A C   
530  O O   . GLY A 54  ? 0.28957 0.36473 0.26816 0.02295  0.06805  -0.02425 40  GLY A O   
534  N N   . LYS A 55  ? 0.33409 0.39590 0.28352 0.01913  0.05681  -0.00825 41  LYS A N   
535  C CA  . LYS A 55  ? 0.32757 0.38931 0.25886 0.00870  0.06277  -0.00378 41  LYS A CA  
536  C C   . LYS A 55  ? 0.36172 0.40610 0.29765 0.01164  0.06108  0.00509  41  LYS A C   
537  O O   . LYS A 55  ? 0.38990 0.41979 0.33322 0.01898  0.05002  0.00982  41  LYS A O   
538  C CB  . LYS A 55  ? 0.43168 0.49449 0.33147 -0.00629 0.05510  0.00551  41  LYS A CB  
539  C CG  . LYS A 55  ? 0.41236 0.48544 0.29059 -0.02413 0.06312  0.01053  41  LYS A CG  
540  C CD  . LYS A 55  ? 0.54517 0.62381 0.38475 -0.04663 0.05421  0.02312  41  LYS A CD  
541  C CE  . LYS A 55  ? 0.70808 0.81251 0.52521 -0.07032 0.06719  0.02464  41  LYS A CE  
542  N NZ  . LYS A 55  ? 0.74991 0.86938 0.52182 -0.09957 0.06059  0.03659  41  LYS A NZ  
556  N N   . LEU A 56  ? 0.35851 0.40611 0.29419 0.00675  0.07054  0.00400  42  LEU A N   
557  C CA  . LEU A 56  ? 0.33573 0.36659 0.27338 0.00770  0.06826  0.01090  42  LEU A CA  
558  C C   . LEU A 56  ? 0.40085 0.43319 0.32167 -0.00800 0.07040  0.01937  42  LEU A C   
559  O O   . LEU A 56  ? 0.34477 0.39975 0.26694 -0.01499 0.08256  0.01122  42  LEU A O   
560  C CB  . LEU A 56  ? 0.35034 0.38376 0.30643 0.01494  0.07582  0.00283  42  LEU A CB  
561  C CG  . LEU A 56  ? 0.35338 0.38900 0.32344 0.02460  0.07408  -0.00250 42  LEU A CG  
562  C CD1 . LEU A 56  ? 0.40985 0.45398 0.39089 0.02269  0.07984  -0.00652 42  LEU A CD1 
563  C CD2 . LEU A 56  ? 0.34310 0.36705 0.31678 0.03142  0.06763  -0.00343 42  LEU A CD2 
575  N N   . THR A 57  ? 0.34993 0.36012 0.25910 -0.01438 0.05645  0.03434  43  THR A N   
576  C CA  . THR A 57  ? 0.36651 0.37539 0.26019 -0.03327 0.05533  0.04708  43  THR A CA  
577  C C   . THR A 57  ? 0.39477 0.37633 0.29961 -0.02691 0.04558  0.05105  43  THR A C   
578  O O   . THR A 57  ? 0.43216 0.38646 0.34242 -0.01859 0.02643  0.05501  43  THR A O   
579  C CB  . THR A 57  ? 0.37205 0.37586 0.23639 -0.05447 0.04060  0.06661  43  THR A CB  
580  O OG1 . THR A 57  ? 0.50382 0.47718 0.37190 -0.04466 0.01660  0.07409  43  THR A OG1 
581  C CG2 . THR A 57  ? 0.35974 0.40011 0.20706 -0.06646 0.05463  0.05897  43  THR A CG2 
589  N N   . LEU A 58  ? 0.37476 0.36431 0.28704 -0.02969 0.05656  0.04687  44  LEU A N   
590  C CA  . LEU A 58  ? 0.37442 0.34103 0.29697 -0.02290 0.04911  0.04622  44  LEU A CA  
591  C C   . LEU A 58  ? 0.40995 0.37983 0.32889 -0.03986 0.05122  0.05526  44  LEU A C   
592  O O   . LEU A 58  ? 0.41219 0.41264 0.33130 -0.05114 0.06600  0.05288  44  LEU A O   
593  C CB  . LEU A 58  ? 0.36851 0.34161 0.30753 -0.00652 0.05921  0.02908  44  LEU A CB  
594  C CG  . LEU A 58  ? 0.35152 0.32558 0.29825 0.00852  0.05764  0.01892  44  LEU A CG  
595  C CD1 . LEU A 58  ? 0.36849 0.35995 0.32456 0.01370  0.07009  0.00795  44  LEU A CD1 
596  C CD2 . LEU A 58  ? 0.42006 0.37219 0.37457 0.01873  0.04252  0.01373  44  LEU A CD2 
608  N N   . LYS A 59  ? 0.38611 0.32676 0.30632 -0.04112 0.03526  0.06255  45  LYS A N   
609  C CA  . LYS A 59  ? 0.41155 0.35174 0.33233 -0.05649 0.03451  0.07120  45  LYS A CA  
610  C C   . LYS A 59  ? 0.43228 0.35237 0.36609 -0.04277 0.02959  0.06022  45  LYS A C   
611  O O   . LYS A 59  ? 0.44746 0.34155 0.38487 -0.02910 0.01531  0.05333  45  LYS A O   
612  C CB  . LYS A 59  ? 0.43157 0.35232 0.33677 -0.07921 0.01381  0.09587  45  LYS A CB  
613  C CG  . LYS A 59  ? 0.46852 0.39475 0.37521 -0.09990 0.01375  0.10698  45  LYS A CG  
614  C CD  . LYS A 59  ? 0.50255 0.40280 0.39334 -0.12599 -0.01304 0.13582  45  LYS A CD  
615  C CE  . LYS A 59  ? 0.50090 0.40762 0.39634 -0.14790 -0.01393 0.14725  45  LYS A CE  
616  N NZ  . LYS A 59  ? 0.59307 0.48092 0.47547 -0.17395 -0.04169 0.17363  45  LYS A NZ  
630  N N   . PHE A 60  ? 0.43909 0.37381 0.38203 -0.04670 0.04006  0.05594  46  PHE A N   
631  C CA  . PHE A 60  ? 0.36594 0.28459 0.31584 -0.03829 0.03521  0.04679  46  PHE A CA  
632  C C   . PHE A 60  ? 0.37082 0.28182 0.32491 -0.05384 0.02714  0.05749  46  PHE A C   
633  O O   . PHE A 60  ? 0.41290 0.34846 0.37229 -0.07012 0.03512  0.06609  46  PHE A O   
634  C CB  . PHE A 60  ? 0.34409 0.28229 0.30241 -0.03023 0.04862  0.03412  46  PHE A CB  
635  C CG  . PHE A 60  ? 0.38513 0.33367 0.34100 -0.01845 0.05615  0.02541  46  PHE A CG  
636  C CD1 . PHE A 60  ? 0.33493 0.27427 0.28577 -0.00715 0.05322  0.01463  46  PHE A CD1 
637  C CD2 . PHE A 60  ? 0.31557 0.28758 0.27627 -0.01964 0.06644  0.02515  46  PHE A CD2 
638  C CE1 . PHE A 60  ? 0.35911 0.31267 0.31046 0.00095  0.06039  0.00740  46  PHE A CE1 
639  C CE2 . PHE A 60  ? 0.24054 0.22037 0.20050 -0.01006 0.07097  0.01834  46  PHE A CE2 
640  C CZ  . PHE A 60  ? 0.32355 0.29427 0.27918 -0.00066 0.06793  0.01130  46  PHE A CZ  
650  N N   . ILE A 61  ? 0.41731 0.29855 0.37107 -0.04950 0.01164  0.05408  47  ILE A N   
651  C CA  A ILE A 61  ? 0.43882 0.30827 0.39796 -0.06375 0.00050  0.06380  47  ILE A CA  
652  C CA  B ILE A 61  ? 0.42247 0.29201 0.38163 -0.06376 0.00055  0.06379  47  ILE A CA  
653  C C   . ILE A 61  ? 0.45511 0.30974 0.41552 -0.05409 -0.00489 0.04924  47  ILE A C   
654  O O   . ILE A 61  ? 0.45646 0.30239 0.40960 -0.03853 -0.00569 0.03228  47  ILE A O   
655  C CB  A ILE A 61  ? 0.46388 0.30207 0.41819 -0.07548 -0.02367 0.08026  47  ILE A CB  
656  C CB  B ILE A 61  ? 0.47554 0.31417 0.42981 -0.07565 -0.02344 0.08041  47  ILE A CB  
657  C CG1 A ILE A 61  ? 0.50079 0.30245 0.45519 -0.05590 -0.04330 0.06565  47  ILE A CG1 
658  C CG1 B ILE A 61  ? 0.50019 0.30185 0.45460 -0.05630 -0.04339 0.06601  47  ILE A CG1 
659  C CG2 A ILE A 61  ? 0.47454 0.32920 0.41947 -0.09241 -0.02048 0.09911  47  ILE A CG2 
660  C CG2 B ILE A 61  ? 0.47754 0.33268 0.42231 -0.09199 -0.02006 0.09881  47  ILE A CG2 
661  C CD1 A ILE A 61  ? 0.54836 0.30850 0.50600 -0.06529 -0.07721 0.08005  47  ILE A CD1 
662  C CD1 B ILE A 61  ? 0.50761 0.27846 0.46811 -0.05382 -0.06308 0.05765  47  ILE A CD1 
683  N N   . SER A 62  ? 0.42991 0.28634 0.39948 -0.06559 -0.00840 0.05488  48  SER A N   
684  C CA  . SER A 62  ? 0.44693 0.28545 0.41347 -0.06178 -0.01857 0.04454  48  SER A CA  
685  C C   . SER A 62  ? 0.43029 0.23207 0.39474 -0.06480 -0.04228 0.04627  48  SER A C   
686  O O   . SER A 62  ? 0.44303 0.23758 0.41543 -0.08064 -0.05263 0.06487  48  SER A O   
687  C CB  . SER A 62  ? 0.44443 0.29970 0.42666 -0.07215 -0.01610 0.04955  48  SER A CB  
688  O OG  . SER A 62  ? 0.47393 0.30708 0.44944 -0.07295 -0.03101 0.04346  48  SER A OG  
694  N N   . THR A 63  ? 0.48936 0.27051 0.44403 -0.05151 -0.05198 0.02563  49  THR A N   
695  C CA  . THR A 63  ? 0.51560 0.25876 0.47334 -0.05046 -0.07870 0.01973  49  THR A CA  
696  C C   . THR A 63  ? 0.53806 0.26979 0.49269 -0.05746 -0.08908 0.01485  49  THR A C   
697  O O   . THR A 63  ? 0.52079 0.22006 0.47765 -0.05514 -0.11274 0.00453  49  THR A O   
698  C CB  . THR A 63  ? 0.51580 0.24688 0.47192 -0.02892 -0.08522 -0.00858 49  THR A CB  
699  O OG1 . THR A 63  ? 0.54670 0.30224 0.48743 -0.01998 -0.06755 -0.03253 49  THR A OG1 
700  C CG2 . THR A 63  ? 0.50347 0.24018 0.46635 -0.02264 -0.08146 -0.00164 49  THR A CG2 
708  N N   . THR A 64  ? 0.44878 0.20402 0.40138 -0.06589 -0.07594 0.02145  50  THR A N   
709  C CA  . THR A 64  ? 0.54943 0.29469 0.49754 -0.07368 -0.08764 0.01804  50  THR A CA  
710  C C   . THR A 64  ? 0.58284 0.34383 0.55242 -0.09022 -0.08665 0.03969  50  THR A C   
711  O O   . THR A 64  ? 0.56827 0.32882 0.53756 -0.09659 -0.09399 0.03911  50  THR A O   
712  C CB  . THR A 64  ? 0.56407 0.32157 0.48699 -0.06788 -0.07904 -0.00100 50  THR A CB  
713  O OG1 . THR A 64  ? 0.52185 0.30958 0.44566 -0.06719 -0.05891 0.00649  50  THR A OG1 
714  C CG2 . THR A 64  ? 0.54233 0.29206 0.44893 -0.05277 -0.08042 -0.03081 50  THR A CG2 
722  N N   . GLY A 65  ? 0.49126 0.26987 0.48069 -0.09854 -0.07852 0.05689  51  GLY A N   
723  C CA  . GLY A 65  ? 0.45163 0.25627 0.46959 -0.11413 -0.07509 0.07113  51  GLY A CA  
724  C C   . GLY A 65  ? 0.40922 0.25392 0.44203 -0.10967 -0.05361 0.06852  51  GLY A C   
725  O O   . GLY A 65  ? 0.45386 0.30497 0.47222 -0.09684 -0.04091 0.06036  51  GLY A O   
729  N N   . LYS A 66  ? 0.43110 0.30475 0.49888 -0.12024 -0.05148 0.07325  52  LYS A N   
730  C CA  . LYS A 66  ? 0.48914 0.40073 0.58277 -0.11433 -0.03658 0.06544  52  LYS A CA  
731  C C   . LYS A 66  ? 0.43494 0.33061 0.51299 -0.10102 -0.04206 0.05694  52  LYS A C   
732  O O   . LYS A 66  ? 0.50774 0.37771 0.57365 -0.10308 -0.06024 0.05735  52  LYS A O   
733  C CB  . LYS A 66  ? 0.42418 0.36809 0.56730 -0.12519 -0.03964 0.06497  52  LYS A CB  
736  N N   . LEU A 67  ? 0.37136 0.28316 0.44689 -0.09074 -0.02773 0.05062  53  LEU A N   
737  C CA  . LEU A 67  ? 0.34125 0.23999 0.39847 -0.08328 -0.03337 0.04659  53  LEU A CA  
738  C C   . LEU A 67  ? 0.38990 0.28882 0.47602 -0.08757 -0.05292 0.04791  53  LEU A C   
739  O O   . LEU A 67  ? 0.37999 0.30322 0.51430 -0.08876 -0.05479 0.04450  53  LEU A O   
740  C CB  . LEU A 67  ? 0.34685 0.26393 0.40211 -0.07321 -0.01659 0.04103  53  LEU A CB  
741  C CG  . LEU A 67  ? 0.37745 0.29060 0.40284 -0.06727 -0.00196 0.03969  53  LEU A CG  
742  C CD1 . LEU A 67  ? 0.40904 0.34041 0.43597 -0.05828 0.01101  0.03435  53  LEU A CD1 
743  C CD2 . LEU A 67  ? 0.41355 0.29817 0.40204 -0.06558 -0.00928 0.03675  53  LEU A CD2 
755  N N   . PRO A 68  ? 0.40883 0.28353 0.46786 -0.09179 -0.06955 0.05197  54  PRO A N   
756  C CA  . PRO A 68  ? 0.42719 0.29634 0.51274 -0.09786 -0.09525 0.05725  54  PRO A CA  
757  C C   . PRO A 68  ? 0.40230 0.28608 0.51704 -0.09076 -0.09738 0.05435  54  PRO A C   
758  O O   . PRO A 68  ? 0.34622 0.22483 0.49665 -0.09367 -0.12386 0.05737  54  PRO A O   
759  C CB  . PRO A 68  ? 0.48435 0.32346 0.51781 -0.11058 -0.11193 0.06513  54  PRO A CB  
760  C CG  . PRO A 68  ? 0.45730 0.29817 0.44480 -0.10582 -0.08935 0.05815  54  PRO A CG  
761  C CD  . PRO A 68  ? 0.44579 0.29999 0.44961 -0.09390 -0.06783 0.05069  54  PRO A CD  
769  N N   . VAL A 69  ? 0.50651 0.40569 0.61103 -0.08133 -0.07459 0.04807  55  VAL A N   
770  C CA  . VAL A 69  ? 0.38268 0.29355 0.51404 -0.07399 -0.07778 0.04349  55  VAL A CA  
771  C C   . VAL A 69  ? 0.42134 0.36614 0.57469 -0.06147 -0.05021 0.02842  55  VAL A C   
772  O O   . VAL A 69  ? 0.37147 0.32395 0.50192 -0.06149 -0.02883 0.02781  55  VAL A O   
773  C CB  . VAL A 69  ? 0.43358 0.32738 0.51983 -0.08044 -0.08184 0.05371  55  VAL A CB  
774  C CG1 . VAL A 69  ? 0.51259 0.37858 0.56577 -0.09942 -0.10713 0.06932  55  VAL A CG1 
775  C CG2 . VAL A 69  ? 0.45676 0.35855 0.50139 -0.07533 -0.05238 0.04908  55  VAL A CG2 
785  N N   . PRO A 70  ? 0.38108 0.34575 0.57872 -0.05204 -0.05321 0.01559  56  PRO A N   
786  C CA  . PRO A 70  ? 0.26007 0.26244 0.47489 -0.04280 -0.02645 -0.00154 56  PRO A CA  
787  C C   . PRO A 70  ? 0.33729 0.33448 0.50500 -0.04011 -0.00792 0.00330  56  PRO A C   
788  O O   . PRO A 70  ? 0.28795 0.26334 0.43130 -0.04075 -0.01713 0.01214  56  PRO A O   
789  C CB  . PRO A 70  ? 0.32485 0.34706 0.60347 -0.03184 -0.04051 -0.02175 56  PRO A CB  
790  C CG  . PRO A 70  ? 0.37265 0.36747 0.67824 -0.03607 -0.07789 -0.01350 56  PRO A CG  
791  C CD  . PRO A 70  ? 0.35151 0.30563 0.59118 -0.05021 -0.08533 0.01400  56  PRO A CD  
799  N N   . TRP A 71  ? 0.26166 0.28143 0.41792 -0.03976 0.01659  -0.00156 57  TRP A N   
800  C CA  . TRP A 71  ? 0.26509 0.28122 0.38315 -0.03631 0.03167  0.00189  57  TRP A CA  
801  C C   . TRP A 71  ? 0.24700 0.26581 0.37438 -0.02739 0.02828  -0.00539 57  TRP A C   
802  O O   . TRP A 71  ? 0.29439 0.29626 0.38853 -0.02677 0.02924  0.00319  57  TRP A O   
803  C CB  . TRP A 71  ? 0.27961 0.32252 0.39161 -0.04048 0.05263  -0.00156 57  TRP A CB  
804  C CG  . TRP A 71  ? 0.29072 0.31935 0.37840 -0.05154 0.05327  0.01262  57  TRP A CG  
805  C CD1 . TRP A 71  ? 0.26225 0.30650 0.36693 -0.06385 0.05404  0.01482  57  TRP A CD1 
806  C CD2 . TRP A 71  ? 0.28746 0.28382 0.33479 -0.05141 0.05024  0.02453  57  TRP A CD2 
807  N NE1 . TRP A 71  ? 0.26985 0.28746 0.34465 -0.07255 0.04884  0.03074  57  TRP A NE1 
808  C CE2 . TRP A 71  ? 0.27641 0.26387 0.31820 -0.06317 0.04563  0.03448  57  TRP A CE2 
809  C CE3 . TRP A 71  ? 0.33040 0.30774 0.35092 -0.04249 0.04990  0.02508  57  TRP A CE3 
810  C CZ2 . TRP A 71  ? 0.33295 0.28784 0.34597 -0.06359 0.03717  0.04299  57  TRP A CZ2 
811  C CZ3 . TRP A 71  ? 0.37575 0.32812 0.37010 -0.04205 0.04511  0.03018  57  TRP A CZ3 
812  C CH2 . TRP A 71  ? 0.38548 0.32420 0.37744 -0.05124 0.03711  0.03815  57  TRP A CH2 
823  N N   . PRO A 72  ? 0.21786 0.25901 0.39220 -0.02034 0.02325  -0.02320 58  PRO A N   
824  C CA  . PRO A 72  ? 0.22646 0.26570 0.41034 -0.01206 0.01642  -0.03011 58  PRO A CA  
825  C C   . PRO A 72  ? 0.28262 0.28581 0.44855 -0.01761 -0.00609 -0.01164 58  PRO A C   
826  O O   . PRO A 72  ? 0.28919 0.28652 0.44377 -0.01614 -0.00817 -0.00883 58  PRO A O   
827  C CB  . PRO A 72  ? 0.21565 0.28255 0.46493 -0.00256 0.00750  -0.05720 58  PRO A CB  
828  C CG  . PRO A 72  ? 0.22583 0.32721 0.49004 -0.00699 0.02503  -0.06796 58  PRO A CG  
829  C CD  . PRO A 72  ? 0.19756 0.27178 0.42299 -0.01909 0.02407  -0.04213 58  PRO A CD  
837  N N   . THR A 73  ? 0.29629 0.27753 0.45724 -0.02735 -0.02381 0.00205  59  THR A N   
838  C CA  . THR A 73  ? 0.29205 0.24387 0.42838 -0.04003 -0.04573 0.02201  59  THR A CA  
839  C C   . THR A 73  ? 0.35476 0.30238 0.43209 -0.04757 -0.02780 0.03318  59  THR A C   
840  O O   . THR A 73  ? 0.38551 0.32188 0.43796 -0.06034 -0.03839 0.04675  59  THR A O   
841  C CB  . THR A 73  ? 0.30974 0.24100 0.45536 -0.05109 -0.07213 0.03294  59  THR A CB  
842  O OG1 . THR A 73  ? 0.30990 0.24051 0.42479 -0.05564 -0.05726 0.03641  59  THR A OG1 
843  C CG2 . THR A 73  ? 0.31961 0.25996 0.53499 -0.04080 -0.09079 0.01660  59  THR A CG2 
851  N N   . LEU A 74  ? 0.33797 0.29633 0.39557 -0.04162 -0.00328 0.02701  60  LEU A N   
852  C CA  . LEU A 74  ? 0.32705 0.28417 0.34081 -0.04388 0.01189  0.03018  60  LEU A CA  
853  C C   . LEU A 74  ? 0.34193 0.31423 0.35269 -0.03382 0.02877  0.02312  60  LEU A C   
854  O O   . LEU A 74  ? 0.33267 0.30729 0.31629 -0.03310 0.03973  0.02230  60  LEU A O   
855  C CB  . LEU A 74  ? 0.33421 0.28576 0.33213 -0.04328 0.01996  0.02809  60  LEU A CB  
856  C CG  . LEU A 74  ? 0.32881 0.26494 0.32857 -0.05301 0.00358  0.03402  60  LEU A CG  
857  C CD1 . LEU A 74  ? 0.40901 0.33868 0.39805 -0.05141 0.01025  0.03093  60  LEU A CD1 
858  C CD2 . LEU A 74  ? 0.37029 0.29461 0.34088 -0.06810 -0.01012 0.04317  60  LEU A CD2 
870  N N   . VAL A 75  ? 0.30618 0.29112 0.34695 -0.02567 0.02987  0.01492  61  VAL A N   
871  C CA  . VAL A 75  ? 0.28698 0.28613 0.32303 -0.01720 0.04470  0.00803  61  VAL A CA  
872  C C   . VAL A 75  ? 0.28798 0.28474 0.30511 -0.02048 0.04365  0.01399  61  VAL A C   
873  O O   . VAL A 75  ? 0.29124 0.29360 0.28859 -0.01666 0.05622  0.01229  61  VAL A O   
874  C CB  . VAL A 75  ? 0.23814 0.25507 0.31004 -0.00972 0.04424  -0.00623 61  VAL A CB  
875  C CG1 . VAL A 75  ? 0.30379 0.33149 0.36940 -0.00355 0.05283  -0.01191 61  VAL A CG1 
876  C CG2 . VAL A 75  ? 0.21879 0.25334 0.30289 -0.00932 0.05492  -0.01490 61  VAL A CG2 
886  N N   . THR A 76  ? 0.28824 0.27763 0.31432 -0.02939 0.02592  0.02161  62  THR A N   
887  C CA  . THR A 76  ? 0.31174 0.30484 0.32098 -0.03801 0.02461  0.02942  62  THR A CA  
888  C C   . THR A 76  ? 0.32541 0.32428 0.29838 -0.04747 0.03516  0.03306  62  THR A C   
889  O O   . THR A 76  ? 0.33625 0.35129 0.29588 -0.04914 0.04575  0.03080  62  THR A O   
890  C CB  . THR A 76  ? 0.31584 0.29597 0.34099 -0.05159 -0.00285 0.04190  62  THR A CB  
891  O OG1 . THR A 76  ? 0.34750 0.31185 0.36532 -0.06592 -0.01961 0.05382  62  THR A OG1 
892  C CG2 . THR A 76  ? 0.33994 0.31719 0.41043 -0.03812 -0.01534 0.02969  62  THR A CG2 
900  N N   . THR A 77  ? 0.34315 0.33264 0.30321 -0.05329 0.03221  0.03506  63  THR A N   
901  C CA  . THR A 77  ? 0.36548 0.36432 0.29314 -0.06096 0.04231  0.03117  63  THR A CA  
902  C C   . THR A 77  ? 0.32709 0.33355 0.25402 -0.04270 0.06023  0.01460  63  THR A C   
903  O O   . THR A 77  ? 0.33419 0.35943 0.24945 -0.04183 0.07131  0.00401  63  THR A O   
904  C CB  . THR A 77  ? 0.39291 0.37699 0.30683 -0.07263 0.03077  0.03662  63  THR A CB  
905  O OG1 . THR A 77  ? 0.40012 0.37398 0.31374 -0.09291 0.00771  0.05523  63  THR A OG1 
906  C CG2 . THR A 77  ? 0.38427 0.38159 0.26548 -0.07891 0.04212  0.02524  63  THR A CG2 
914  N N   . LEU A 78  ? 0.31922 0.31338 0.26128 -0.02983 0.06099  0.01196  64  LEU A N   
915  C CA  . LEU A 78  ? 0.39233 0.38570 0.33438 -0.01607 0.06971  0.00193  64  LEU A CA  
916  C C   . LEU A 78  ? 0.36211 0.36800 0.31245 -0.00734 0.07637  -0.00128 64  LEU A C   
917  O O   . LEU A 78  ? 0.37954 0.38931 0.32889 0.00182  0.08041  -0.01076 64  LEU A O   
918  C CB  . LEU A 78  ? 0.32069 0.29940 0.27240 -0.01291 0.06609  0.00578  64  LEU A CB  
919  C CG  . LEU A 78  ? 0.30355 0.26769 0.24968 -0.02003 0.05793  0.00799  64  LEU A CG  
920  C CD1 . LEU A 78  ? 0.33740 0.29686 0.30098 -0.02197 0.05458  0.01439  64  LEU A CD1 
921  C CD2 . LEU A 78  ? 0.33412 0.28903 0.26624 -0.01542 0.05722  -0.00267 64  LEU A CD2 
956  N N   . VAL A 80  ? 0.31825 0.39254 0.28879 -0.00110 0.09239  -0.01441 66  VAL A N   
957  C CA  . VAL A 80  ? 0.38226 0.47339 0.36535 0.00962  0.09662  -0.02637 66  VAL A CA  
958  C C   . VAL A 80  ? 0.36580 0.46367 0.35935 0.00801  0.09336  -0.01919 66  VAL A C   
959  O O   . VAL A 80  ? 0.30727 0.39596 0.30822 0.01892  0.08893  -0.01959 66  VAL A O   
960  C CB  . VAL A 80  ? 0.34588 0.41805 0.33478 0.02639  0.09149  -0.03338 66  VAL A CB  
961  C CG1 . VAL A 80  ? 0.32973 0.39765 0.31471 0.02960  0.09195  -0.04582 66  VAL A CG1 
962  C CG2 . VAL A 80  ? 0.34960 0.39743 0.33214 0.02640  0.08522  -0.01980 66  VAL A CG2 
971  N N   . GLN A 81  ? 0.43684 0.38805 0.42912 -0.08162 -0.07054 0.05808  67  GLN A N   
972  C CA  . GLN A 81  ? 0.37075 0.34193 0.37697 -0.06862 -0.05639 0.05774  67  GLN A CA  
973  C C   . GLN A 81  ? 0.39732 0.36054 0.38963 -0.06272 -0.03545 0.05332  67  GLN A C   
974  O O   . GLN A 81  ? 0.34105 0.32091 0.34630 -0.05415 -0.02462 0.05216  67  GLN A O   
975  C CB  . GLN A 81  ? 0.37008 0.32547 0.36096 -0.06448 -0.06890 0.05926  67  GLN A CB  
976  C CG  . GLN A 81  ? 0.30856 0.27954 0.32732 -0.06300 -0.09440 0.06186  67  GLN A CG  
977  C CD  . GLN A 81  ? 0.41834 0.35545 0.40821 -0.06249 -0.11742 0.06790  67  GLN A CD  
978  O OE1 . GLN A 81  ? 0.46168 0.36226 0.39803 -0.07230 -0.11523 0.07181  67  GLN A OE1 
979  N NE2 . GLN A 81  ? 0.41991 0.37060 0.44424 -0.05102 -0.14090 0.06821  67  GLN A NE2 
988  N N   . CYS A 82  ? 0.40721 0.34598 0.37746 -0.06520 -0.03258 0.04790  68  CYS A N   
989  C CA  . CYS A 82  ? 0.42777 0.36610 0.39708 -0.05593 -0.01681 0.04151  68  CYS A CA  
990  C C   . CYS A 82  ? 0.35483 0.31537 0.35155 -0.05436 -0.01347 0.04975  68  CYS A C   
991  O O   . CYS A 82  ? 0.32205 0.28639 0.32228 -0.04516 -0.00437 0.04630  68  CYS A O   
992  C CB  . CYS A 82  ? 0.38882 0.29542 0.33474 -0.05366 -0.01963 0.02870  68  CYS A CB  
993  S SG  . CYS A 82  ? 0.45831 0.33625 0.40350 -0.06684 -0.04392 0.03355  68  CYS A SG  
999  N N   . PHE A 83  ? 0.34020 0.32069 0.35584 -0.06455 -0.02071 0.06033  69  PHE A N   
1000 C CA  . PHE A 83  ? 0.36153 0.37062 0.39490 -0.06837 -0.01507 0.06996  69  PHE A CA  
1001 C C   . PHE A 83  ? 0.31587 0.36809 0.36982 -0.06041 -0.00504 0.06566  69  PHE A C   
1002 O O   . PHE A 83  ? 0.27079 0.35699 0.33612 -0.06440 0.00191  0.07055  69  PHE A O   
1003 C CB  . PHE A 83  ? 0.32572 0.34017 0.36745 -0.08975 -0.02565 0.08398  69  PHE A CB  
1004 C CG  . PHE A 83  ? 0.35688 0.32089 0.37889 -0.09780 -0.03987 0.08895  69  PHE A CG  
1005 C CD1 . PHE A 83  ? 0.34806 0.29310 0.36101 -0.09660 -0.04193 0.09736  69  PHE A CD1 
1006 C CD2 . PHE A 83  ? 0.40614 0.33675 0.41737 -0.10481 -0.05583 0.08347  69  PHE A CD2 
1007 C CE1 . PHE A 83  ? 0.42664 0.31636 0.42441 -0.09979 -0.06119 0.09946  69  PHE A CE1 
1008 C CE2 . PHE A 83  ? 0.46456 0.34191 0.45808 -0.10913 -0.07264 0.08261  69  PHE A CE2 
1009 C CZ  . PHE A 83  ? 0.48187 0.33668 0.47078 -0.10533 -0.07610 0.09019  69  PHE A CZ  
1019 N N   . ALA A 84  ? 0.30067 0.34949 0.35603 -0.05018 -0.00606 0.05620  70  ALA A N   
1020 C CA  . ALA A 84  ? 0.30910 0.38655 0.38382 -0.03864 -0.00161 0.04751  70  ALA A CA  
1021 C C   . ALA A 84  ? 0.27482 0.35633 0.34389 -0.03204 0.00959  0.04364  70  ALA A C   
1022 O O   . ALA A 84  ? 0.29239 0.34986 0.34549 -0.03171 0.01255  0.04461  70  ALA A O   
1023 C CB  . ALA A 84  ? 0.31617 0.37232 0.38851 -0.03170 -0.01257 0.04241  70  ALA A CB  
1029 N N   . ARG A 85  ? 0.27370 0.39086 0.35785 -0.02566 0.01507  0.03600  71  ARG A N   
1030 C CA  . ARG A 85  ? 0.25327 0.37598 0.33147 -0.01928 0.02133  0.03002  71  ARG A CA  
1031 C C   . ARG A 85  ? 0.23225 0.33774 0.31563 -0.00969 0.01656  0.01771  71  ARG A C   
1032 O O   . ARG A 85  ? 0.24223 0.35660 0.34152 -0.00021 0.01026  0.00535  71  ARG A O   
1033 C CB  . ARG A 85  ? 0.27205 0.44062 0.35514 -0.01880 0.02886  0.02515  71  ARG A CB  
1034 C CG  . ARG A 85  ? 0.28844 0.46243 0.35997 -0.01289 0.03115  0.01814  71  ARG A CG  
1035 C CD  . ARG A 85  ? 0.34210 0.55648 0.42174 -0.00263 0.03586  -0.00332 71  ARG A CD  
1036 N NE  . ARG A 85  ? 0.31291 0.52138 0.38375 0.00531  0.03181  -0.01602 71  ARG A NE  
1037 C CZ  . ARG A 85  ? 0.25763 0.48614 0.33413 0.01832  0.03068  -0.04203 71  ARG A CZ  
1038 N NH1 . ARG A 85  ? 0.25928 0.51921 0.35407 0.02913  0.03471  -0.06109 71  ARG A NH1 
1039 N NH2 . ARG A 85  ? 0.35190 0.57043 0.41918 0.02223  0.02326  -0.05259 71  ARG A NH2 
1053 N N   . TYR A 86  ? 0.24345 0.32478 0.31614 -0.01284 0.01786  0.02044  72  TYR A N   
1054 C CA  . TYR A 86  ? 0.26554 0.33205 0.34174 -0.01178 0.01371  0.01299  72  TYR A CA  
1055 C C   . TYR A 86  ? 0.29427 0.37916 0.37705 -0.00686 0.01531  0.00286  72  TYR A C   
1056 O O   . TYR A 86  ? 0.33238 0.42512 0.41188 -0.00861 0.02013  0.00666  72  TYR A O   
1057 C CB  . TYR A 86  ? 0.29430 0.33779 0.35742 -0.02295 0.01751  0.02069  72  TYR A CB  
1058 C CG  . TYR A 86  ? 0.30216 0.31937 0.35029 -0.03021 0.01045  0.02900  72  TYR A CG  
1059 C CD1 . TYR A 86  ? 0.29512 0.30994 0.33520 -0.03043 0.00830  0.03430  72  TYR A CD1 
1060 C CD2 . TYR A 86  ? 0.34133 0.33237 0.38021 -0.03997 0.00205  0.03376  72  TYR A CD2 
1061 C CE1 . TYR A 86  ? 0.32095 0.31161 0.34414 -0.03716 -0.00239 0.04155  72  TYR A CE1 
1062 C CE2 . TYR A 86  ? 0.33080 0.29367 0.34813 -0.04812 -0.00900 0.04479  72  TYR A CE2 
1063 C CZ  . TYR A 86  ? 0.35985 0.32446 0.36935 -0.04518 -0.01133 0.04735  72  TYR A CZ  
1064 O OH  . TYR A 86  ? 0.37609 0.31280 0.36129 -0.05328 -0.02629 0.05782  72  TYR A OH  
1074 N N   . PRO A 87  ? 0.27560 0.36632 0.36807 0.00138  0.00789  -0.01256 73  PRO A N   
1075 C CA  . PRO A 87  ? 0.26834 0.37365 0.36242 0.00467  0.00604  -0.02465 73  PRO A CA  
1076 C C   . PRO A 87  ? 0.34232 0.43692 0.44016 -0.00595 0.00561  -0.01959 73  PRO A C   
1077 O O   . PRO A 87  ? 0.32730 0.40258 0.42545 -0.01689 0.00816  -0.00986 73  PRO A O   
1078 C CB  . PRO A 87  ? 0.33047 0.42938 0.43506 0.01564  -0.00628 -0.04633 73  PRO A CB  
1079 C CG  . PRO A 87  ? 0.26152 0.36478 0.37378 0.02431  -0.00693 -0.04753 73  PRO A CG  
1080 C CD  . PRO A 87  ? 0.28616 0.37113 0.39039 0.01146  -0.00262 -0.02355 73  PRO A CD  
1088 N N   . ASP A 88  ? 0.38659 0.49966 0.48719 -0.00404 0.00241  -0.02682 74  ASP A N   
1089 C CA  . ASP A 88  ? 0.38733 0.50449 0.50227 -0.01303 0.00168  -0.02477 74  ASP A CA  
1090 C C   . ASP A 88  ? 0.40071 0.49664 0.52673 -0.02870 -0.00146 -0.02487 74  ASP A C   
1091 O O   . ASP A 88  ? 0.39213 0.49321 0.52706 -0.04211 0.00735  -0.01670 74  ASP A O   
1092 C CB  . ASP A 88  ? 0.34026 0.47911 0.45895 -0.00816 -0.00905 -0.03559 74  ASP A CB  
1093 C CG  . ASP A 88  ? 0.42561 0.58142 0.52969 0.00079  -0.00917 -0.02690 74  ASP A CG  
1094 O OD1 . ASP A 88  ? 0.39253 0.54151 0.49035 0.00200  -0.00117 -0.01294 74  ASP A OD1 
1095 O OD2 . ASP A 88  ? 0.50831 0.67953 0.60352 0.00492  -0.02073 -0.03314 74  ASP A OD2 
1100 N N   . HIS A 89  ? 0.38450 0.45657 0.50937 -0.02817 -0.01492 -0.03459 75  HIS A N   
1101 C CA  . HIS A 89  ? 0.44169 0.48218 0.57303 -0.04764 -0.02488 -0.03039 75  HIS A CA  
1102 C C   . HIS A 89  ? 0.43480 0.44865 0.55147 -0.05874 -0.01995 -0.01130 75  HIS A C   
1103 O O   . HIS A 89  ? 0.42620 0.40928 0.53971 -0.08056 -0.02893 -0.00083 75  HIS A O   
1104 C CB  . HIS A 89  ? 0.43569 0.44736 0.57024 -0.04028 -0.04832 -0.04940 75  HIS A CB  
1105 C CG  . HIS A 89  ? 0.50684 0.49505 0.63395 -0.02208 -0.05653 -0.05535 75  HIS A CG  
1106 N ND1 . HIS A 89  ? 0.56497 0.58394 0.68827 0.00064  -0.04711 -0.06599 75  HIS A ND1 
1107 C CD2 . HIS A 89  ? 0.55313 0.49272 0.67937 -0.02369 -0.07584 -0.05205 75  HIS A CD2 
1108 C CE1 . HIS A 89  ? 0.46834 0.46771 0.59585 0.01438  -0.05794 -0.07263 75  HIS A CE1 
1109 N NE2 . HIS A 89  ? 0.52667 0.47363 0.65557 0.00246  -0.07808 -0.06455 75  HIS A NE2 
1117 N N   . MET A 90  ? 0.36269 0.38497 0.46686 -0.04790 -0.00860 -0.00473 76  MET A N   
1118 C CA  . MET A 90  ? 0.39920 0.39685 0.48416 -0.05754 -0.00686 0.01176  76  MET A CA  
1119 C C   . MET A 90  ? 0.37394 0.39306 0.44830 -0.06252 0.01386  0.02008  76  MET A C   
1120 O O   . MET A 90  ? 0.38203 0.38316 0.43377 -0.07235 0.01625  0.03210  76  MET A O   
1121 C CB  . MET A 90  ? 0.38926 0.37198 0.47062 -0.03940 -0.01870 0.00843  76  MET A CB  
1122 C CG  . MET A 90  ? 0.42305 0.37476 0.51452 -0.03084 -0.04360 -0.00252 76  MET A CG  
1123 S SD  . MET A 90  ? 0.39686 0.35003 0.49760 -0.00504 -0.05546 -0.01161 76  MET A SD  
1124 C CE  . MET A 90  ? 0.39168 0.31438 0.46603 -0.02188 -0.05958 0.01633  76  MET A CE  
1134 N N   . LYS A 91  ? 0.37376 0.42737 0.46200 -0.05438 0.02527  0.01232  77  LYS A N   
1135 C CA  . LYS A 91  ? 0.39669 0.46464 0.47793 -0.05131 0.03991  0.01409  77  LYS A CA  
1136 C C   . LYS A 91  ? 0.37329 0.44592 0.44441 -0.07101 0.05386  0.01868  77  LYS A C   
1137 O O   . LYS A 91  ? 0.39041 0.46750 0.44720 -0.06838 0.06503  0.01688  77  LYS A O   
1138 C CB  . LYS A 91  ? 0.42069 0.51819 0.52225 -0.03672 0.04218  0.00471  77  LYS A CB  
1139 C CG  . LYS A 91  ? 0.42836 0.52318 0.52524 -0.02159 0.03248  0.00525  77  LYS A CG  
1140 C CD  . LYS A 91  ? 0.46346 0.57161 0.56687 -0.00928 0.03069  0.00414  77  LYS A CD  
1141 C CE  . LYS A 91  ? 0.43164 0.53470 0.52004 -0.00319 0.02245  0.01201  77  LYS A CE  
1142 N NZ  . LYS A 91  ? 0.55341 0.67094 0.64081 -0.00236 0.01645  0.00699  77  LYS A NZ  
1156 N N   . ARG A 92  ? 0.31348 0.38568 0.38918 -0.09307 0.05324  0.02392  78  ARG A N   
1157 C CA  . ARG A 92  ? 0.40065 0.48066 0.45861 -0.11984 0.06864  0.03273  78  ARG A CA  
1158 C C   . ARG A 92  ? 0.35101 0.39155 0.36381 -0.12819 0.06369  0.04757  78  ARG A C   
1159 O O   . ARG A 92  ? 0.37604 0.42468 0.36080 -0.14869 0.07885  0.05415  78  ARG A O   
1160 C CB  . ARG A 92  ? 0.41984 0.50030 0.48892 -0.14976 0.06450  0.04167  78  ARG A CB  
1161 C CG  . ARG A 92  ? 0.61774 0.74910 0.73283 -0.15107 0.07184  0.02758  78  ARG A CG  
1162 C CD  . ARG A 92  ? 0.87974 1.01085 1.00338 -0.19045 0.06800  0.03990  78  ARG A CD  
1163 N NE  . ARG A 92  ? 0.92842 0.99006 1.02839 -0.20032 0.03966  0.05504  78  ARG A NE  
1164 C CZ  . ARG A 92  ? 0.92235 0.95679 1.03997 -0.18975 0.01399  0.04628  78  ARG A CZ  
1165 N NH1 . ARG A 92  ? 0.86423 0.93443 1.01775 -0.17394 0.01245  0.02631  78  ARG A NH1 
1166 N NH2 . ARG A 92  ? 0.90545 0.87401 1.00302 -0.19324 -0.01363 0.05563  78  ARG A NH2 
1180 N N   . HIS A 93  ? 0.41090 0.41445 0.41636 -0.11323 0.04247  0.05155  79  HIS A N   
1181 C CA  . HIS A 93  ? 0.47580 0.43869 0.44442 -0.12043 0.02860  0.06666  79  HIS A CA  
1182 C C   . HIS A 93  ? 0.40518 0.36786 0.36508 -0.10078 0.02783  0.06046  79  HIS A C   
1183 O O   . HIS A 93  ? 0.47129 0.40335 0.41079 -0.10050 0.00999  0.06995  79  HIS A O   
1184 C CB  . HIS A 93  ? 0.45667 0.37736 0.43121 -0.11899 -0.00114 0.07445  79  HIS A CB  
1185 C CG  . HIS A 93  ? 0.48926 0.40003 0.47435 -0.13961 -0.00687 0.07988  79  HIS A CG  
1186 N ND1 . HIS A 93  ? 0.48156 0.36445 0.43645 -0.17540 -0.01188 0.10301  79  HIS A ND1 
1187 C CD2 . HIS A 93  ? 0.48093 0.40491 0.50075 -0.13338 -0.01021 0.06629  79  HIS A CD2 
1188 C CE1 . HIS A 93  ? 0.49795 0.37576 0.47318 -0.19182 -0.01874 0.10418  79  HIS A CE1 
1189 N NE2 . HIS A 93  ? 0.54609 0.44848 0.56154 -0.16509 -0.01862 0.08001  79  HIS A NE2 
1197 N N   . ASP A 94  ? 0.29792 0.33635 0.40980 -0.07934 -0.02624 0.03193  80  ASP A N   
1198 C CA  . ASP A 94  ? 0.31618 0.34984 0.41292 -0.06761 -0.02209 0.02763  80  ASP A CA  
1199 C C   . ASP A 94  ? 0.31922 0.36344 0.41422 -0.06329 -0.01090 0.03362  80  ASP A C   
1200 O O   . ASP A 94  ? 0.28518 0.34779 0.38942 -0.05882 -0.00620 0.03457  80  ASP A O   
1201 C CB  . ASP A 94  ? 0.29620 0.33825 0.39481 -0.06210 -0.02638 0.02181  80  ASP A CB  
1202 C CG  . ASP A 94  ? 0.35097 0.38504 0.43437 -0.05176 -0.02430 0.01777  80  ASP A CG  
1203 O OD1 . ASP A 94  ? 0.31655 0.34084 0.38870 -0.04807 -0.01854 0.01885  80  ASP A OD1 
1204 O OD2 . ASP A 94  ? 0.31899 0.35726 0.40161 -0.04830 -0.02911 0.01424  80  ASP A OD2 
1209 N N   . PHE A 95  ? 0.31517 0.34864 0.39870 -0.06448 -0.00686 0.03726  81  PHE A N   
1210 C CA  . PHE A 95  ? 0.35354 0.39751 0.43170 -0.06067 0.00408  0.04111  81  PHE A CA  
1211 C C   . PHE A 95  ? 0.39017 0.43278 0.45875 -0.04821 0.00753  0.03369  81  PHE A C   
1212 O O   . PHE A 95  ? 0.37251 0.42989 0.44435 -0.04245 0.01574  0.03297  81  PHE A O   
1213 C CB  . PHE A 95  ? 0.38606 0.41883 0.45214 -0.06599 0.00592  0.04755  81  PHE A CB  
1214 C CG  . PHE A 95  ? 0.37753 0.41713 0.43057 -0.06076 0.01610  0.04827  81  PHE A CG  
1215 C CD1 . PHE A 95  ? 0.41549 0.47728 0.47354 -0.06439 0.02574  0.05439  81  PHE A CD1 
1216 C CD2 . PHE A 95  ? 0.37245 0.39806 0.40818 -0.05278 0.01608  0.04211  81  PHE A CD2 
1217 C CE1 . PHE A 95  ? 0.43623 0.50603 0.48099 -0.05960 0.03546  0.05282  81  PHE A CE1 
1218 C CE2 . PHE A 95  ? 0.41753 0.44914 0.44051 -0.04852 0.02476  0.04111  81  PHE A CE2 
1219 C CZ  . PHE A 95  ? 0.42640 0.48003 0.45322 -0.05168 0.03460  0.04571  81  PHE A CZ  
1229 N N   . PHE A 96  ? 0.35724 0.38276 0.41517 -0.04406 0.00120  0.02774  82  PHE A N   
1230 C CA  . PHE A 96  ? 0.36919 0.38980 0.41648 -0.03401 0.00344  0.02211  82  PHE A CA  
1231 C C   . PHE A 96  ? 0.39978 0.43488 0.45958 -0.02733 0.00508  0.02007  82  PHE A C   
1232 O O   . PHE A 96  ? 0.37254 0.41213 0.43096 -0.01979 0.01168  0.01759  82  PHE A O   
1233 C CB  . PHE A 96  ? 0.36886 0.37233 0.40536 -0.03258 -0.00441 0.01730  82  PHE A CB  
1234 C CG  . PHE A 96  ? 0.36291 0.35195 0.39073 -0.03769 -0.00734 0.01870  82  PHE A CG  
1235 C CD1 . PHE A 96  ? 0.38699 0.36756 0.40079 -0.03602 -0.00368 0.02018  82  PHE A CD1 
1236 C CD2 . PHE A 96  ? 0.39863 0.38244 0.43328 -0.04397 -0.01455 0.01811  82  PHE A CD2 
1237 C CE1 . PHE A 96  ? 0.42043 0.38798 0.42839 -0.04017 -0.00757 0.02283  82  PHE A CE1 
1238 C CE2 . PHE A 96  ? 0.37521 0.34423 0.40496 -0.04743 -0.01819 0.01920  82  PHE A CE2 
1239 C CZ  . PHE A 96  ? 0.41286 0.37392 0.42986 -0.04534 -0.01491 0.02244  82  PHE A CZ  
1249 N N   . LYS A 97  ? 0.31930 0.36187 0.39213 -0.02979 -0.00155 0.02067  83  LYS A N   
1250 C CA  . LYS A 97  ? 0.38494 0.44165 0.47184 -0.02340 -0.00184 0.02047  83  LYS A CA  
1251 C C   . LYS A 97  ? 0.34704 0.42471 0.44988 -0.02253 0.00643  0.02355  83  LYS A C   
1252 O O   . LYS A 97  ? 0.38922 0.47703 0.50206 -0.01351 0.00988  0.02178  83  LYS A O   
1253 C CB  . LYS A 97  ? 0.33799 0.39944 0.43344 -0.02745 -0.01210 0.02115  83  LYS A CB  
1254 C CG  . LYS A 97  ? 0.32223 0.36851 0.40302 -0.02791 -0.01965 0.01727  83  LYS A CG  
1255 C CD  . LYS A 97  ? 0.31864 0.37428 0.40694 -0.03211 -0.02929 0.01746  83  LYS A CD  
1256 C CE  . LYS A 97  ? 0.29377 0.33879 0.36697 -0.03325 -0.03575 0.01294  83  LYS A CE  
1257 N NZ  . LYS A 97  ? 0.33426 0.36579 0.39707 -0.03805 -0.03565 0.00783  83  LYS A NZ  
1271 N N   . SER A 98  ? 0.33480 0.41996 0.44172 -0.03180 0.00946  0.02832  84  SER A N   
1272 C CA  . SER A 98  ? 0.31599 0.42545 0.43875 -0.03241 0.01802  0.03199  84  SER A CA  
1273 C C   . SER A 98  ? 0.31262 0.42666 0.42847 -0.02391 0.02951  0.02808  84  SER A C   
1274 O O   . SER A 98  ? 0.33263 0.46929 0.46342 -0.01938 0.03730  0.02750  84  SER A O   
1275 C CB  . SER A 98  ? 0.33180 0.44691 0.45853 -0.04613 0.01843  0.03959  84  SER A CB  
1276 O OG  . SER A 98  ? 0.38679 0.48837 0.49547 -0.04993 0.02209  0.04157  84  SER A OG  
1282 N N   . ALA A 99  ? 0.32883 0.42350 0.42308 -0.02154 0.03068  0.02443  85  ALA A N   
1283 C CA  . ALA A 99  ? 0.35474 0.45231 0.43937 -0.01436 0.04082  0.01900  85  ALA A CA  
1284 C C   . ALA A 99  ? 0.38869 0.48105 0.47600 -0.00083 0.04036  0.01018  85  ALA A C   
1285 O O   . ALA A 99  ? 0.34822 0.44182 0.42878 0.00639  0.04820  0.00298  85  ALA A O   
1286 C CB  . ALA A 99  ? 0.32931 0.40913 0.38961 -0.01900 0.04118  0.01978  85  ALA A CB  
1292 N N   . MET A 100 ? 0.37067 0.45734 0.46760 0.00221  0.03088  0.01066  86  MET A N   
1293 C CA  . MET A 100 ? 0.39808 0.47768 0.49949 0.01391  0.02816  0.00487  86  MET A CA  
1294 C C   . MET A 100 ? 0.36906 0.47064 0.49614 0.02223  0.03205  0.00346  86  MET A C   
1295 O O   . MET A 100 ? 0.38139 0.50407 0.52460 0.01752  0.03358  0.00871  86  MET A O   
1296 C CB  . MET A 100 ? 0.37550 0.44029 0.47416 0.01201  0.01540  0.00806  86  MET A CB  
1297 C CG  . MET A 100 ? 0.34464 0.38880 0.42000 0.00595  0.01165  0.00777  86  MET A CG  
1298 S SD  . MET A 100 ? 0.42608 0.45323 0.48253 0.01256  0.01664  0.00006  86  MET A SD  
1299 C CE  . MET A 100 ? 0.39751 0.40846 0.43144 0.00314  0.01294  0.00229  86  MET A CE  
1309 N N   . PRO A 101 ? 0.36080 0.45801 0.49426 0.03490  0.03309  -0.00372 87  PRO A N   
1310 C CA  . PRO A 101 ? 0.36728 0.43964 0.48524 0.04061  0.03012  -0.01000 87  PRO A CA  
1311 C C   . PRO A 101 ? 0.40571 0.47322 0.50505 0.04184  0.04026  -0.01887 87  PRO A C   
1312 O O   . PRO A 101 ? 0.39583 0.44209 0.47859 0.04340  0.03736  -0.02341 87  PRO A O   
1313 C CB  . PRO A 101 ? 0.36692 0.44031 0.50678 0.05360  0.02639  -0.01316 87  PRO A CB  
1314 C CG  . PRO A 101 ? 0.38792 0.49040 0.55085 0.05843  0.03509  -0.01493 87  PRO A CG  
1315 C CD  . PRO A 101 ? 0.35834 0.47628 0.51989 0.04497  0.03596  -0.00577 87  PRO A CD  
1323 N N   . GLU A 102 ? 0.44855 0.53704 0.54964 0.04027  0.05193  -0.02106 88  GLU A N   
1324 C CA  . GLU A 102 ? 0.45139 0.53848 0.53330 0.04086  0.06153  -0.02950 88  GLU A CA  
1325 C C   . GLU A 102 ? 0.43278 0.49889 0.48766 0.03152  0.05680  -0.02568 88  GLU A C   
1326 O O   . GLU A 102 ? 0.40959 0.46387 0.44668 0.03375  0.05916  -0.03338 88  GLU A O   
1327 C CB  . GLU A 102 ? 0.55288 0.66993 0.63942 0.03729  0.07439  -0.02912 88  GLU A CB  
1328 C CG  . GLU A 102 ? 0.57922 0.72203 0.69436 0.04726  0.08078  -0.03403 88  GLU A CG  
1329 C CD  . GLU A 102 ? 0.70444 0.86846 0.83917 0.03971  0.07914  -0.02192 88  GLU A CD  
1330 O OE1 . GLU A 102 ? 0.54601 0.69734 0.68196 0.03308  0.06748  -0.01237 88  GLU A OE1 
1331 O OE2 . GLU A 102 ? 0.79794 0.99285 0.94675 0.03985  0.08960  -0.02247 88  GLU A OE2 
1338 N N   . GLY A 103 ? 0.34735 0.40918 0.39981 0.02137  0.04983  -0.01478 89  GLY A N   
1339 C CA  . GLY A 103 ? 0.38764 0.42965 0.41874 0.01400  0.04396  -0.01127 89  GLY A CA  
1340 C C   . GLY A 103 ? 0.36887 0.41757 0.38748 0.00388  0.04894  -0.00533 89  GLY A C   
1341 O O   . GLY A 103 ? 0.38480 0.45466 0.41096 0.00029  0.05667  -0.00199 89  GLY A O   
1345 N N   . TYR A 104 ? 0.39132 0.42231 0.39142 -0.00120 0.04378  -0.00290 90  TYR A N   
1346 C CA  . TYR A 104 ? 0.41477 0.44779 0.40217 -0.01093 0.04590  0.00450  90  TYR A CA  
1347 C C   . TYR A 104 ? 0.40458 0.42138 0.36962 -0.01097 0.04363  0.00158  90  TYR A C   
1348 O O   . TYR A 104 ? 0.41139 0.41259 0.37190 -0.00564 0.03813  -0.00433 90  TYR A O   
1349 C CB  . TYR A 104 ? 0.38610 0.41506 0.38085 -0.01988 0.03842  0.01466  90  TYR A CB  
1350 C CG  . TYR A 104 ? 0.37024 0.38068 0.36539 -0.01838 0.02756  0.01321  90  TYR A CG  
1351 C CD1 . TYR A 104 ? 0.38445 0.37722 0.36391 -0.01893 0.02229  0.01236  90  TYR A CD1 
1352 C CD2 . TYR A 104 ? 0.42793 0.44143 0.43925 -0.01696 0.02257  0.01293  90  TYR A CD2 
1353 C CE1 . TYR A 104 ? 0.37016 0.35011 0.35026 -0.01783 0.01344  0.01057  90  TYR A CE1 
1354 C CE2 . TYR A 104 ? 0.42213 0.42248 0.43223 -0.01649 0.01331  0.01141  90  TYR A CE2 
1355 C CZ  . TYR A 104 ? 0.41273 0.39699 0.40734 -0.01683 0.00932  0.00991  90  TYR A CZ  
1356 O OH  . TYR A 104 ? 0.37794 0.35307 0.37168 -0.01655 0.00116  0.00791  90  TYR A OH  
1366 N N   . VAL A 105 ? 0.39403 0.41606 0.34550 -0.01797 0.04740  0.00698  91  VAL A N   
1367 C CA  . VAL A 105 ? 0.39790 0.40709 0.32816 -0.01993 0.04430  0.00665  91  VAL A CA  
1368 C C   . VAL A 105 ? 0.43063 0.42683 0.36000 -0.02716 0.03484  0.01725  91  VAL A C   
1369 O O   . VAL A 105 ? 0.43736 0.44007 0.37169 -0.03518 0.03481  0.02782  91  VAL A O   
1370 C CB  . VAL A 105 ? 0.36783 0.39231 0.28263 -0.02350 0.05334  0.00666  91  VAL A CB  
1371 C CG1 . VAL A 105 ? 0.43759 0.44991 0.33077 -0.02736 0.04828  0.00897  91  VAL A CG1 
1372 C CG2 . VAL A 105 ? 0.47523 0.51177 0.39124 -0.01459 0.06285  -0.00752 91  VAL A CG2 
1382 N N   . GLN A 106 ? 0.41238 0.39068 0.33688 -0.02439 0.02661  0.01432  92  GLN A N   
1383 C CA  . GLN A 106 ? 0.37184 0.33754 0.29606 -0.02915 0.01757  0.02163  92  GLN A CA  
1384 C C   . GLN A 106 ? 0.39104 0.35015 0.29680 -0.03129 0.01515  0.02391  92  GLN A C   
1385 O O   . GLN A 106 ? 0.40535 0.35906 0.30062 -0.02683 0.01464  0.01624  92  GLN A O   
1386 C CB  . GLN A 106 ? 0.37785 0.33251 0.31092 -0.02488 0.01023  0.01676  92  GLN A CB  
1387 C CG  . GLN A 106 ? 0.38776 0.33015 0.32094 -0.02770 0.00132  0.02076  92  GLN A CG  
1388 C CD  . GLN A 106 ? 0.41134 0.34907 0.35562 -0.02506 -0.00449 0.01604  92  GLN A CD  
1389 O OE1 . GLN A 106 ? 0.34944 0.29337 0.30651 -0.02577 -0.00397 0.01564  92  GLN A OE1 
1390 N NE2 . GLN A 106 ? 0.44006 0.36926 0.37930 -0.02258 -0.01006 0.01251  92  GLN A NE2 
1399 N N   . GLU A 107 ? 0.41690 0.37654 0.31950 -0.03871 0.01281  0.03527  93  GLU A N   
1400 C CA  . GLU A 107 ? 0.43496 0.38975 0.32145 -0.04176 0.00891  0.04026  93  GLU A CA  
1401 C C   . GLU A 107 ? 0.48881 0.42990 0.38280 -0.04413 -0.00172 0.04824  93  GLU A C   
1402 O O   . GLU A 107 ? 0.42835 0.36704 0.33722 -0.04728 -0.00442 0.05388  93  GLU A O   
1403 C CB  . GLU A 107 ? 0.40264 0.37262 0.27722 -0.04899 0.01521  0.04843  93  GLU A CB  
1404 C CG  . GLU A 107 ? 0.48552 0.47168 0.35288 -0.04591 0.02676  0.03847  93  GLU A CG  
1405 C CD  . GLU A 107 ? 0.60870 0.61363 0.46147 -0.05369 0.03359  0.04565  93  GLU A CD  
1406 O OE1 . GLU A 107 ? 0.65978 0.67407 0.51912 -0.06187 0.03470  0.05884  93  GLU A OE1 
1407 O OE2 . GLU A 107 ? 0.70039 0.71139 0.53473 -0.05247 0.03751  0.03824  93  GLU A OE2 
1414 N N   . ARG A 108 ? 0.47404 0.40641 0.35905 -0.04243 -0.00812 0.04796  94  ARG A N   
1415 C CA  . ARG A 108 ? 0.44909 0.36934 0.34245 -0.04303 -0.01835 0.05433  94  ARG A CA  
1416 C C   . ARG A 108 ? 0.45089 0.36941 0.33068 -0.04533 -0.02364 0.06135  94  ARG A C   
1417 O O   . ARG A 108 ? 0.43289 0.35701 0.29612 -0.04485 -0.02062 0.05698  94  ARG A O   
1418 C CB  . ARG A 108 ? 0.38792 0.29952 0.29164 -0.03605 -0.02294 0.04418  94  ARG A CB  
1419 C CG  . ARG A 108 ? 0.44969 0.36156 0.36916 -0.03466 -0.02131 0.03919  94  ARG A CG  
1420 C CD  . ARG A 108 ? 0.42605 0.32948 0.35683 -0.03034 -0.02856 0.03329  94  ARG A CD  
1421 N NE  . ARG A 108 ? 0.39591 0.30140 0.33929 -0.02924 -0.02752 0.02687  94  ARG A NE  
1422 C CZ  . ARG A 108 ? 0.33029 0.24023 0.27373 -0.02528 -0.02563 0.01798  94  ARG A CZ  
1423 N NH1 . ARG A 108 ? 0.39505 0.30639 0.32775 -0.02212 -0.02442 0.01411  94  ARG A NH1 
1424 N NH2 . ARG A 108 ? 0.35883 0.27198 0.31358 -0.02536 -0.02585 0.01363  94  ARG A NH2 
1438 N N   . THR A 109 ? 0.50465 0.41496 0.39269 -0.04790 -0.03242 0.07216  95  THR A N   
1439 C CA  . THR A 109 ? 0.45228 0.35815 0.33415 -0.04779 -0.04098 0.07832  95  THR A CA  
1440 C C   . THR A 109 ? 0.41948 0.31277 0.32003 -0.04152 -0.04971 0.07485  95  THR A C   
1441 O O   . THR A 109 ? 0.39260 0.27804 0.31013 -0.04197 -0.05304 0.07787  95  THR A O   
1442 C CB  . THR A 109 ? 0.46752 0.37655 0.34313 -0.05657 -0.04457 0.09644  95  THR A CB  
1443 O OG1 . THR A 109 ? 0.50811 0.43284 0.36682 -0.06267 -0.03466 0.09807  95  THR A OG1 
1444 C CG2 . THR A 109 ? 0.53164 0.43822 0.40000 -0.05631 -0.05401 0.10316  95  THR A CG2 
1452 N N   . ILE A 110 ? 0.41407 0.30660 0.31219 -0.03587 -0.05313 0.06740  96  ILE A N   
1453 C CA  . ILE A 110 ? 0.44979 0.33498 0.36506 -0.02896 -0.05995 0.06147  96  ILE A CA  
1454 C C   . ILE A 110 ? 0.46764 0.35059 0.38366 -0.02789 -0.06972 0.06977  96  ILE A C   
1455 O O   . ILE A 110 ? 0.46125 0.35073 0.36470 -0.02768 -0.07053 0.06846  96  ILE A O   
1456 C CB  . ILE A 110 ? 0.42602 0.31572 0.34076 -0.02356 -0.05588 0.04641  96  ILE A CB  
1457 C CG1 . ILE A 110 ? 0.37866 0.27173 0.29188 -0.02484 -0.04697 0.04010  96  ILE A CG1 
1458 C CG2 . ILE A 110 ? 0.46995 0.35621 0.40258 -0.01689 -0.06161 0.03940  96  ILE A CG2 
1459 C CD1 . ILE A 110 ? 0.46889 0.36641 0.38093 -0.02083 -0.04366 0.02793  96  ILE A CD1 
1471 N N   . PHE A 111 ? 0.44118 0.31448 0.37328 -0.02733 -0.07804 0.07849  97  PHE A N   
1472 C CA  . PHE A 111 ? 0.48185 0.35223 0.41919 -0.02541 -0.08900 0.08799  97  PHE A CA  
1473 C C   . PHE A 111 ? 0.48195 0.35061 0.43729 -0.01511 -0.09366 0.07617  97  PHE A C   
1474 O O   . PHE A 111 ? 0.44420 0.30447 0.41903 -0.01030 -0.09564 0.06979  97  PHE A O   
1475 C CB  . PHE A 111 ? 0.52323 0.38305 0.47082 -0.03008 -0.09685 0.10501  97  PHE A CB  
1476 C CG  . PHE A 111 ? 0.58519 0.45100 0.51475 -0.04146 -0.09240 0.11869  97  PHE A CG  
1477 C CD1 . PHE A 111 ? 0.53828 0.40460 0.46746 -0.04663 -0.08427 0.11776  97  PHE A CD1 
1478 C CD2 . PHE A 111 ? 0.55652 0.43012 0.46962 -0.04741 -0.09635 0.13243  97  PHE A CD2 
1479 C CE1 . PHE A 111 ? 0.53766 0.41346 0.45114 -0.05712 -0.07913 0.12983  97  PHE A CE1 
1480 C CE2 . PHE A 111 ? 0.53695 0.41985 0.43218 -0.05839 -0.09138 0.14428  97  PHE A CE2 
1481 C CZ  . PHE A 111 ? 0.52678 0.41140 0.42263 -0.06305 -0.08227 0.14278  97  PHE A CZ  
1491 N N   . PHE A 112 ? 0.43326 0.31139 0.38232 -0.01214 -0.09532 0.07250  98  PHE A N   
1492 C CA  . PHE A 112 ? 0.43826 0.31943 0.40465 -0.00277 -0.09992 0.06283  98  PHE A CA  
1493 C C   . PHE A 112 ? 0.43629 0.31181 0.41838 0.00094  -0.11249 0.07413  98  PHE A C   
1494 O O   . PHE A 112 ? 0.45246 0.33135 0.42416 -0.00344 -0.11802 0.08736  98  PHE A O   
1495 C CB  . PHE A 112 ? 0.42233 0.31778 0.37679 -0.00235 -0.09642 0.05484  98  PHE A CB  
1496 C CG  . PHE A 112 ? 0.44293 0.34267 0.38714 -0.00436 -0.08582 0.04325  98  PHE A CG  
1497 C CD1 . PHE A 112 ? 0.41924 0.31948 0.34277 -0.01148 -0.07927 0.04558  98  PHE A CD1 
1498 C CD2 . PHE A 112 ? 0.42399 0.32843 0.37984 0.00103  -0.08273 0.03000  98  PHE A CD2 
1499 C CE1 . PHE A 112 ? 0.40795 0.31106 0.32489 -0.01244 -0.07080 0.03576  98  PHE A CE1 
1500 C CE2 . PHE A 112 ? 0.42083 0.32945 0.36791 -0.00135 -0.07442 0.02164  98  PHE A CE2 
1501 C CZ  . PHE A 112 ? 0.37582 0.28264 0.30455 -0.00772 -0.06895 0.02498  98  PHE A CZ  
1511 N N   . LYS A 113 ? 0.46799 0.33498 0.47551 0.00906  -0.11757 0.06868  99  LYS A N   
1512 C CA  . LYS A 113 ? 0.47810 0.33617 0.50528 0.01373  -0.13065 0.07962  99  LYS A CA  
1513 C C   . LYS A 113 ? 0.50384 0.37517 0.53105 0.01740  -0.13693 0.08316  99  LYS A C   
1514 O O   . LYS A 113 ? 0.49292 0.37881 0.52019 0.02203  -0.13272 0.07010  99  LYS A O   
1515 C CB  . LYS A 113 ? 0.53456 0.38214 0.59093 0.02385  -0.13425 0.06768  99  LYS A CB  
1516 C CG  . LYS A 113 ? 0.52107 0.35406 0.60230 0.02936  -0.14878 0.07883  99  LYS A CG  
1517 C CD  . LYS A 113 ? 0.70338 0.52087 0.77880 0.01872  -0.15400 0.10017  99  LYS A CD  
1518 C CE  . LYS A 113 ? 0.91503 0.70957 1.02035 0.02343  -0.16524 0.10388  99  LYS A CE  
1519 N NZ  . LYS A 113 ? 0.88720 0.67837 1.01775 0.03474  -0.17876 0.10737  99  LYS A NZ  
1533 N N   . ASP A 114 ? 0.49989 0.36753 0.52721 0.01433  -0.14759 0.10211  100 ASP A N   
1534 C CA  . ASP A 114 ? 0.45022 0.33062 0.47839 0.01675  -0.15580 0.10860  100 ASP A CA  
1535 C C   . ASP A 114 ? 0.46184 0.35980 0.46369 0.01047  -0.14813 0.10337  100 ASP A C   
1536 O O   . ASP A 114 ? 0.46314 0.37519 0.46730 0.01325  -0.15268 0.10245  100 ASP A O   
1537 C CB  . ASP A 114 ? 0.57310 0.45723 0.63269 0.03119  -0.16196 0.09806  100 ASP A CB  
1538 C CG  . ASP A 114 ? 0.61946 0.48389 0.70828 0.03885  -0.17071 0.10078  100 ASP A CG  
1539 O OD1 . ASP A 114 ? 0.62483 0.47450 0.71291 0.03271  -0.17856 0.11969  100 ASP A OD1 
1540 O OD2 . ASP A 114 ? 0.69919 0.56331 0.81191 0.05059  -0.16992 0.08377  100 ASP A OD2 
1545 N N   . ASP A 115 ? 0.48282 0.38015 0.46123 0.00205  -0.13712 0.09978  101 ASP A N   
1546 C CA  . ASP A 115 ? 0.41818 0.32870 0.37335 -0.00349 -0.12985 0.09277  101 ASP A CA  
1547 C C   . ASP A 115 ? 0.46881 0.37595 0.39788 -0.01414 -0.12245 0.09780  101 ASP A C   
1548 O O   . ASP A 115 ? 0.45558 0.35443 0.38306 -0.01858 -0.12483 0.11055  101 ASP A O   
1549 C CB  . ASP A 115 ? 0.40696 0.32400 0.36936 0.00225  -0.12177 0.07359  101 ASP A CB  
1550 C CG  . ASP A 115 ? 0.48094 0.41344 0.43140 -0.00052 -0.12040 0.06810  101 ASP A CG  
1551 O OD1 . ASP A 115 ? 0.45704 0.39220 0.38520 -0.00901 -0.12056 0.07416  101 ASP A OD1 
1552 O OD2 . ASP A 115 ? 0.50284 0.44575 0.46626 0.00519  -0.11927 0.05742  101 ASP A OD2 
1557 N N   . GLY A 116 ? 0.52202 0.43623 0.43186 -0.01833 -0.11362 0.08786  102 GLY A N   
1558 C CA  . GLY A 116 ? 0.50909 0.42309 0.39461 -0.02714 -0.10596 0.08978  102 GLY A CA  
1559 C C   . GLY A 116 ? 0.44425 0.34984 0.33332 -0.02695 -0.09689 0.08522  102 GLY A C   
1560 O O   . GLY A 116 ? 0.43084 0.32852 0.34040 -0.02135 -0.09806 0.08324  102 GLY A O   
1564 N N   . ASN A 117 ? 0.45566 0.36397 0.32496 -0.03309 -0.08782 0.08252  103 ASN A N   
1565 C CA  . ASN A 117 ? 0.49304 0.39644 0.36475 -0.03384 -0.07894 0.07908  103 ASN A CA  
1566 C C   . ASN A 117 ? 0.43820 0.34673 0.29347 -0.03590 -0.06844 0.06755  103 ASN A C   
1567 O O   . ASN A 117 ? 0.47196 0.38703 0.30829 -0.04003 -0.06754 0.06642  103 ASN A O   
1568 C CB  . ASN A 117 ? 0.47352 0.37496 0.34251 -0.04045 -0.08003 0.09448  103 ASN A CB  
1569 C CG  . ASN A 117 ? 0.52537 0.43767 0.36847 -0.04914 -0.07743 0.10116  103 ASN A CG  
1570 O OD1 . ASN A 117 ? 0.50846 0.42701 0.33713 -0.05201 -0.06711 0.09353  103 ASN A OD1 
1571 N ND2 . ASN A 117 ? 0.49422 0.40992 0.33187 -0.05315 -0.08706 0.11507  103 ASN A ND2 
1578 N N   . TYR A 118 ? 0.42555 0.33087 0.28897 -0.03290 -0.06127 0.05871  104 TYR A N   
1579 C CA  . TYR A 118 ? 0.42823 0.33693 0.28024 -0.03397 -0.05156 0.04900  104 TYR A CA  
1580 C C   . TYR A 118 ? 0.43611 0.34785 0.28293 -0.03852 -0.04458 0.05419  104 TYR A C   
1581 O O   . TYR A 118 ? 0.44069 0.34908 0.29956 -0.03962 -0.04579 0.06196  104 TYR A O   
1582 C CB  . TYR A 118 ? 0.40564 0.31154 0.26991 -0.02852 -0.04822 0.03766  104 TYR A CB  
1583 C CG  . TYR A 118 ? 0.39705 0.30381 0.26620 -0.02492 -0.05303 0.03135  104 TYR A CG  
1584 C CD1 . TYR A 118 ? 0.40571 0.31594 0.26513 -0.02685 -0.05817 0.03256  104 TYR A CD1 
1585 C CD2 . TYR A 118 ? 0.40501 0.31154 0.28831 -0.02050 -0.05239 0.02435  104 TYR A CD2 
1586 C CE1 . TYR A 118 ? 0.42933 0.34298 0.29463 -0.02455 -0.06235 0.02757  104 TYR A CE1 
1587 C CE2 . TYR A 118 ? 0.36245 0.27347 0.25025 -0.01823 -0.05600 0.01929  104 TYR A CE2 
1588 C CZ  . TYR A 118 ? 0.42778 0.34248 0.30738 -0.02030 -0.06083 0.02119  104 TYR A CZ  
1589 O OH  . TYR A 118 ? 0.37275 0.29442 0.25825 -0.01895 -0.06422 0.01690  104 TYR A OH  
1599 N N   . LYS A 119 ? 0.41287 0.33159 0.24295 -0.04122 -0.03724 0.04906  105 LYS A N   
1600 C CA  . LYS A 119 ? 0.49231 0.41799 0.31882 -0.04432 -0.02805 0.05020  105 LYS A CA  
1601 C C   . LYS A 119 ? 0.44561 0.37247 0.27102 -0.03986 -0.01985 0.03540  105 LYS A C   
1602 O O   . LYS A 119 ? 0.48486 0.41254 0.29755 -0.03906 -0.01872 0.02657  105 LYS A O   
1603 C CB  . LYS A 119 ? 0.46060 0.39742 0.26783 -0.05195 -0.02642 0.05857  105 LYS A CB  
1604 C CG  . LYS A 119 ? 0.59332 0.52951 0.40452 -0.05763 -0.03424 0.07711  105 LYS A CG  
1605 C CD  . LYS A 119 ? 0.65222 0.60333 0.44473 -0.06701 -0.03080 0.08747  105 LYS A CD  
1606 C CE  . LYS A 119 ? 0.67639 0.62624 0.47795 -0.07369 -0.03711 0.10806  105 LYS A CE  
1607 N NZ  . LYS A 119 ? 0.92663 0.89411 0.70890 -0.08462 -0.03399 0.12065  105 LYS A NZ  
1621 N N   . THR A 120 ? 0.44857 0.37482 0.28844 -0.03711 -0.01524 0.03286  106 THR A N   
1622 C CA  . THR A 120 ? 0.44596 0.37196 0.28968 -0.03191 -0.00945 0.02052  106 THR A CA  
1623 C C   . THR A 120 ? 0.44491 0.38145 0.29059 -0.03251 0.00037  0.01940  106 THR A C   
1624 O O   . THR A 120 ? 0.40155 0.34337 0.25417 -0.03648 0.00185  0.02860  106 THR A O   
1625 C CB  . THR A 120 ? 0.39592 0.31433 0.25679 -0.02747 -0.01354 0.01760  106 THR A CB  
1626 O OG1 . THR A 120 ? 0.36485 0.28406 0.23969 -0.02887 -0.01364 0.02410  106 THR A OG1 
1627 C CG2 . THR A 120 ? 0.35254 0.26445 0.21337 -0.02663 -0.02233 0.01822  106 THR A CG2 
1635 N N   . ARG A 121 ? 0.44643 0.38623 0.28751 -0.02857 0.00670  0.00800  107 ARG A N   
1636 C CA  . ARG A 121 ? 0.46008 0.41106 0.30746 -0.02655 0.01636  0.00397  107 ARG A CA  
1637 C C   . ARG A 121 ? 0.44192 0.38652 0.30091 -0.01886 0.01684  -0.00654 107 ARG A C   
1638 O O   . ARG A 121 ? 0.45190 0.38786 0.30469 -0.01566 0.01423  -0.01500 107 ARG A O   
1639 C CB  . ARG A 121 ? 0.39769 0.36212 0.22846 -0.02855 0.02455  -0.00059 107 ARG A CB  
1640 C CG  . ARG A 121 ? 0.49662 0.47822 0.33522 -0.02751 0.03546  -0.00253 107 ARG A CG  
1641 C CD  . ARG A 121 ? 0.48398 0.48050 0.30630 -0.02744 0.04471  -0.01197 107 ARG A CD  
1642 N NE  . ARG A 121 ? 0.57234 0.59140 0.40043 -0.02910 0.05561  -0.01005 107 ARG A NE  
1643 C CZ  . ARG A 121 ? 0.63658 0.66386 0.48023 -0.02173 0.06303  -0.01921 107 ARG A CZ  
1644 N NH1 . ARG A 121 ? 0.47902 0.49222 0.33416 -0.01218 0.06016  -0.03011 107 ARG A NH1 
1645 N NH2 . ARG A 121 ? 0.68708 0.73855 0.53600 -0.02436 0.07315  -0.01629 107 ARG A NH2 
1659 N N   . ALA A 122 ? 0.36619 0.31498 0.24251 -0.01669 0.01913  -0.00501 108 ALA A N   
1660 C CA  . ALA A 122 ? 0.42114 0.36514 0.31030 -0.01000 0.01830  -0.01215 108 ALA A CA  
1661 C C   . ALA A 122 ? 0.45032 0.40779 0.35256 -0.00667 0.02631  -0.01446 108 ALA A C   
1662 O O   . ALA A 122 ? 0.41770 0.38789 0.32351 -0.01093 0.03096  -0.00794 108 ALA A O   
1663 C CB  . ALA A 122 ? 0.42236 0.35803 0.32216 -0.01054 0.00997  -0.00748 108 ALA A CB  
1669 N N   . GLU A 123 ? 0.37220 0.32715 0.28296 0.00078  0.02730  -0.02314 109 GLU A N   
1670 C CA  . GLU A 123 ? 0.43101 0.39829 0.35915 0.00584  0.03312  -0.02563 109 GLU A CA  
1671 C C   . GLU A 123 ? 0.39089 0.35112 0.33503 0.00889  0.02575  -0.02345 109 GLU A C   
1672 O O   . GLU A 123 ? 0.42467 0.37156 0.36793 0.01225  0.01991  -0.02726 109 GLU A O   
1673 C CB  . GLU A 123 ? 0.40179 0.37380 0.32855 0.01329  0.04058  -0.03840 109 GLU A CB  
1674 C CG  . GLU A 123 ? 0.45298 0.43602 0.36182 0.00977  0.04867  -0.04181 109 GLU A CG  
1675 C CD  . GLU A 123 ? 0.65330 0.64427 0.56240 0.01800  0.05731  -0.05727 109 GLU A CD  
1676 O OE1 . GLU A 123 ? 0.61804 0.61213 0.54689 0.02664  0.05928  -0.06292 109 GLU A OE1 
1677 O OE2 . GLU A 123 ? 0.67548 0.67018 0.56557 0.01610  0.06176  -0.06433 109 GLU A OE2 
1684 N N   . VAL A 124 ? 0.42079 0.39076 0.37902 0.00656  0.02541  -0.01665 110 VAL A N   
1685 C CA  . VAL A 124 ? 0.38633 0.35375 0.35898 0.00800  0.01829  -0.01363 110 VAL A CA  
1686 C C   . VAL A 124 ? 0.42408 0.40589 0.41609 0.01354  0.02270  -0.01513 110 VAL A C   
1687 O O   . VAL A 124 ? 0.38130 0.37875 0.38148 0.01052  0.02772  -0.01140 110 VAL A O   
1688 C CB  . VAL A 124 ? 0.45179 0.41896 0.42551 0.00047  0.01281  -0.00582 110 VAL A CB  
1689 C CG1 . VAL A 124 ? 0.48188 0.44871 0.46761 0.00126  0.00537  -0.00385 110 VAL A CG1 
1690 C CG2 . VAL A 124 ? 0.40902 0.36418 0.36604 -0.00383 0.00908  -0.00464 110 VAL A CG2 
1700 N N   . LYS A 125 ? 0.35644 0.33334 0.35751 0.02141  0.02018  -0.01982 111 LYS A N   
1701 C CA  . LYS A 125 ? 0.43205 0.42241 0.45333 0.02898  0.02436  -0.02263 111 LYS A CA  
1702 C C   . LYS A 125 ? 0.39303 0.37391 0.42690 0.03522  0.01580  -0.02235 111 LYS A C   
1703 O O   . LYS A 125 ? 0.41045 0.37450 0.43519 0.03358  0.00819  -0.02122 111 LYS A O   
1704 C CB  . LYS A 125 ? 0.39176 0.38934 0.41011 0.03498  0.03518  -0.03301 111 LYS A CB  
1705 C CG  . LYS A 125 ? 0.44355 0.42274 0.44949 0.03973  0.03368  -0.04268 111 LYS A CG  
1706 C CD  . LYS A 125 ? 0.53980 0.52784 0.53837 0.04404  0.04491  -0.05468 111 LYS A CD  
1707 C CE  . LYS A 125 ? 0.55835 0.52678 0.54422 0.04794  0.04234  -0.06571 111 LYS A CE  
1708 N NZ  . LYS A 125 ? 0.60613 0.58445 0.58143 0.05124  0.05333  -0.07926 111 LYS A NZ  
1722 N N   . PHE A 126 ? 0.36398 0.35725 0.42015 0.04204  0.01674  -0.02235 112 PHE A N   
1723 C CA  . PHE A 126 ? 0.39821 0.38397 0.46994 0.04877  0.00809  -0.02056 112 PHE A CA  
1724 C C   . PHE A 126 ? 0.44846 0.42458 0.52495 0.05988  0.01122  -0.03203 112 PHE A C   
1725 O O   . PHE A 126 ? 0.41094 0.39977 0.49483 0.06666  0.02132  -0.04104 112 PHE A O   
1726 C CB  . PHE A 126 ? 0.36871 0.37325 0.46464 0.05089  0.00582  -0.01391 112 PHE A CB  
1727 C CG  . PHE A 126 ? 0.39679 0.40423 0.49155 0.04149  -0.00333 -0.00270 112 PHE A CG  
1728 C CD1 . PHE A 126 ? 0.35052 0.36815 0.43830 0.03202  -0.00066 0.00057  112 PHE A CD1 
1729 C CD2 . PHE A 126 ? 0.36791 0.36839 0.46888 0.04172  -0.01502 0.00442  112 PHE A CD2 
1730 C CE1 . PHE A 126 ? 0.36096 0.38138 0.44770 0.02382  -0.00901 0.00809  112 PHE A CE1 
1731 C CE2 . PHE A 126 ? 0.36759 0.37377 0.46582 0.03275  -0.02291 0.01321  112 PHE A CE2 
1732 C CZ  . PHE A 126 ? 0.40694 0.42302 0.49803 0.02424  -0.01966 0.01372  112 PHE A CZ  
1742 N N   A GLU A 127 ? 0.45421 0.40866 0.52660 0.06128  0.00267  -0.03232 113 GLU A N   
1743 N N   B GLU A 127 ? 0.45239 0.40690 0.52500 0.06127  0.00254  -0.03217 113 GLU A N   
1744 C CA  A GLU A 127 ? 0.44384 0.38478 0.52499 0.07212  0.00226  -0.04287 113 GLU A CA  
1745 C CA  B GLU A 127 ? 0.46130 0.40180 0.54207 0.07191  0.00202  -0.04267 113 GLU A CA  
1746 C C   A GLU A 127 ? 0.45101 0.38467 0.55371 0.07653  -0.01002 -0.03400 113 GLU A C   
1747 C C   B GLU A 127 ? 0.45056 0.38407 0.55329 0.07653  -0.01012 -0.03395 113 GLU A C   
1748 O O   A GLU A 127 ? 0.45846 0.37506 0.55544 0.07158  -0.02075 -0.02663 113 GLU A O   
1749 O O   B GLU A 127 ? 0.45876 0.37516 0.55608 0.07172  -0.02090 -0.02660 113 GLU A O   
1750 C CB  A GLU A 127 ? 0.46409 0.38415 0.52316 0.06894  0.00138  -0.05021 113 GLU A CB  
1751 C CB  B GLU A 127 ? 0.46055 0.37988 0.51894 0.06819  0.00059  -0.04922 113 GLU A CB  
1752 C CG  A GLU A 127 ? 0.48523 0.41262 0.52700 0.06842  0.01382  -0.06226 113 GLU A CG  
1753 C CG  B GLU A 127 ? 0.49678 0.42320 0.53241 0.06281  0.01094  -0.05594 113 GLU A CG  
1754 C CD  A GLU A 127 ? 0.45239 0.39061 0.50804 0.08061  0.02366  -0.07677 113 GLU A CD  
1755 C CD  B GLU A 127 ? 0.49463 0.40142 0.50917 0.05898  0.00831  -0.06217 113 GLU A CD  
1756 O OE1 A GLU A 127 ? 0.47110 0.40623 0.55098 0.09109  0.01983  -0.07920 113 GLU A OE1 
1757 O OE1 B GLU A 127 ? 0.51434 0.40149 0.53237 0.05997  -0.00136 -0.06139 113 GLU A OE1 
1758 O OE2 A GLU A 127 ? 0.47932 0.43051 0.52220 0.07978  0.03512  -0.08561 113 GLU A OE2 
1759 O OE2 B GLU A 127 ? 0.49411 0.40572 0.48903 0.05418  0.01519  -0.06678 113 GLU A OE2 
1772 N N   . GLY A 128 ? 0.40323 0.41681 0.60709 0.06004  0.01932  -0.02563 114 GLY A N   
1773 C CA  . GLY A 128 ? 0.32407 0.33341 0.54678 0.06489  0.01110  -0.01388 114 GLY A CA  
1774 C C   . GLY A 128 ? 0.43995 0.45544 0.64912 0.05773  0.00861  0.00213  114 GLY A C   
1775 O O   . GLY A 128 ? 0.45556 0.48770 0.65591 0.05399  0.01292  0.00114  114 GLY A O   
1779 N N   . ASP A 129 ? 0.46070 0.46355 0.66816 0.05534  0.00162  0.01674  115 ASP A N   
1780 C CA  . ASP A 129 ? 0.46218 0.46990 0.65378 0.04829  -0.00093 0.03071  115 ASP A CA  
1781 C C   . ASP A 129 ? 0.40782 0.40619 0.57573 0.03962  0.00144  0.03409  115 ASP A C   
1782 O O   . ASP A 129 ? 0.39360 0.39365 0.54828 0.03424  -0.00099 0.04507  115 ASP A O   
1783 C CB  . ASP A 129 ? 0.46331 0.46801 0.66814 0.05155  -0.01038 0.04597  115 ASP A CB  
1784 C CG  . ASP A 129 ? 0.58724 0.60535 0.81398 0.05935  -0.01391 0.04509  115 ASP A CG  
1785 O OD1 . ASP A 129 ? 0.60226 0.63722 0.82740 0.05892  -0.00901 0.03701  115 ASP A OD1 
1786 O OD2 . ASP A 129 ? 0.67181 0.68412 0.91872 0.06570  -0.02191 0.05322  115 ASP A OD2 
1791 N N   . THR A 130 ? 0.37751 0.36725 0.54025 0.03853  0.00584  0.02416  116 THR A N   
1792 C CA  . THR A 130 ? 0.32107 0.30211 0.46460 0.03124  0.00769  0.02644  116 THR A CA  
1793 C C   . THR A 130 ? 0.36727 0.35597 0.49369 0.02657  0.01430  0.01732  116 THR A C   
1794 O O   . THR A 130 ? 0.38887 0.38325 0.51903 0.02928  0.01858  0.00538  116 THR A O   
1795 C CB  . THR A 130 ? 0.31945 0.28415 0.47076 0.03261  0.00603  0.02356  116 THR A CB  
1796 O OG1 . THR A 130 ? 0.34378 0.30025 0.51234 0.03601  -0.00084 0.03431  116 THR A OG1 
1797 C CG2 . THR A 130 ? 0.38165 0.33958 0.51503 0.02519  0.00781  0.02605  116 THR A CG2 
1805 N N   . LEU A 131 ? 0.36851 0.35796 0.47664 0.01965  0.01498  0.02305  117 LEU A N   
1806 C CA  . LEU A 131 ? 0.29212 0.28551 0.38403 0.01435  0.01982  0.01688  117 LEU A CA  
1807 C C   . LEU A 131 ? 0.30874 0.29059 0.39400 0.01262  0.02103  0.01214  117 LEU A C   
1808 O O   . LEU A 131 ? 0.33115 0.30376 0.41281 0.01047  0.01857  0.01830  117 LEU A O   
1809 C CB  . LEU A 131 ? 0.35102 0.34851 0.42896 0.00844  0.01878  0.02403  117 LEU A CB  
1810 C CG  . LEU A 131 ? 0.31269 0.31392 0.37600 0.00244  0.02224  0.02002  117 LEU A CG  
1811 C CD1 . LEU A 131 ? 0.35571 0.34630 0.40822 -0.00029 0.02349  0.01730  117 LEU A CD1 
1812 C CD2 . LEU A 131 ? 0.31387 0.32719 0.38235 0.00314  0.02644  0.01302  117 LEU A CD2 
1824 N N   . VAL A 132 ? 0.37811 0.36236 0.46173 0.01334  0.02479  0.00121  118 VAL A N   
1825 C CA  . VAL A 132 ? 0.41824 0.39283 0.49746 0.01242  0.02494  -0.00506 118 VAL A CA  
1826 C C   . VAL A 132 ? 0.36854 0.34651 0.42888 0.00634  0.02777  -0.00712 118 VAL A C   
1827 O O   . VAL A 132 ? 0.37202 0.36148 0.42626 0.00431  0.03130  -0.00891 118 VAL A O   
1828 C CB  . VAL A 132 ? 0.41837 0.39262 0.51056 0.01862  0.02586  -0.01738 118 VAL A CB  
1829 C CG1 . VAL A 132 ? 0.47324 0.43700 0.56155 0.01732  0.02450  -0.02434 118 VAL A CG1 
1830 C CG2 . VAL A 132 ? 0.39840 0.36854 0.51218 0.02519  0.02198  -0.01436 118 VAL A CG2 
1840 N N   . ASN A 133 ? 0.38611 0.35450 0.43872 0.00318  0.02578  -0.00601 119 ASN A N   
1841 C CA  . ASN A 133 ? 0.35080 0.32010 0.38701 -0.00214 0.02678  -0.00710 119 ASN A CA  
1842 C C   . ASN A 133 ? 0.37536 0.33855 0.41040 -0.00172 0.02545  -0.01511 119 ASN A C   
1843 O O   . ASN A 133 ? 0.35982 0.31325 0.39796 -0.00234 0.02196  -0.01279 119 ASN A O   
1844 C CB  . ASN A 133 ? 0.31785 0.28264 0.34642 -0.00616 0.02456  0.00203  119 ASN A CB  
1845 C CG  . ASN A 133 ? 0.32371 0.28803 0.33788 -0.01107 0.02430  0.00185  119 ASN A CG  
1846 O OD1 . ASN A 133 ? 0.34063 0.31103 0.34792 -0.01284 0.02637  -0.00243 119 ASN A OD1 
1847 N ND2 . ASN A 133 ? 0.32542 0.28347 0.33549 -0.01317 0.02166  0.00684  119 ASN A ND2 
1854 N N   . ARG A 134 ? 0.40313 0.37373 0.43385 -0.00096 0.02824  -0.02479 120 ARG A N   
1855 C CA  . ARG A 134 ? 0.44524 0.41226 0.47310 -0.00059 0.02658  -0.03456 120 ARG A CA  
1856 C C   . ARG A 134 ? 0.36530 0.33587 0.37421 -0.00646 0.02630  -0.03307 120 ARG A C   
1857 O O   . ARG A 134 ? 0.38776 0.36955 0.38633 -0.00916 0.03006  -0.03204 120 ARG A O   
1858 C CB  . ARG A 134 ? 0.43561 0.41006 0.47035 0.00473  0.02966  -0.04798 120 ARG A CB  
1859 C CG  . ARG A 134 ? 0.58870 0.55814 0.64503 0.01139  0.02858  -0.04949 120 ARG A CG  
1860 C CD  . ARG A 134 ? 0.61212 0.59043 0.67728 0.01791  0.03201  -0.06410 120 ARG A CD  
1861 N NE  . ARG A 134 ? 0.52984 0.50061 0.61848 0.02492  0.02923  -0.06527 120 ARG A NE  
1862 C CZ  . ARG A 134 ? 0.60630 0.56197 0.70874 0.02768  0.02363  -0.06939 120 ARG A CZ  
1863 N NH1 . ARG A 134 ? 0.57130 0.51862 0.66691 0.02410  0.02026  -0.07382 120 ARG A NH1 
1864 N NH2 . ARG A 134 ? 0.64050 0.58915 0.76546 0.03386  0.02052  -0.06834 120 ARG A NH2 
1878 N N   . ILE A 135 ? 0.37731 0.33901 0.38301 -0.00868 0.02145  -0.03219 121 ILE A N   
1879 C CA  . ILE A 135 ? 0.33643 0.29895 0.32675 -0.01400 0.01920  -0.02751 121 ILE A CA  
1880 C C   . ILE A 135 ? 0.37534 0.33735 0.35938 -0.01482 0.01554  -0.03610 121 ILE A C   
1881 O O   . ILE A 135 ? 0.39746 0.35227 0.39193 -0.01245 0.01225  -0.04241 121 ILE A O   
1882 C CB  . ILE A 135 ? 0.33094 0.28480 0.32366 -0.01589 0.01582  -0.01718 121 ILE A CB  
1883 C CG1 . ILE A 135 ? 0.36604 0.32076 0.36421 -0.01501 0.01859  -0.00990 121 ILE A CG1 
1884 C CG2 . ILE A 135 ? 0.35547 0.30958 0.33471 -0.02047 0.01271  -0.01241 121 ILE A CG2 
1885 C CD1 . ILE A 135 ? 0.36094 0.30828 0.36591 -0.01473 0.01622  -0.00315 121 ILE A CD1 
1897 N N   . GLU A 136 ? 0.36528 0.33504 0.33242 -0.01883 0.01537  -0.03548 122 GLU A N   
1898 C CA  . GLU A 136 ? 0.38204 0.35189 0.33938 -0.02109 0.01003  -0.04014 122 GLU A CA  
1899 C C   . GLU A 136 ? 0.37099 0.33742 0.31981 -0.02572 0.00544  -0.02818 122 GLU A C   
1900 O O   . GLU A 136 ? 0.40791 0.37844 0.34886 -0.02882 0.00767  -0.01954 122 GLU A O   
1901 C CB  . GLU A 136 ? 0.44105 0.42503 0.38424 -0.02180 0.01310  -0.04949 122 GLU A CB  
1902 C CG  . GLU A 136 ? 0.62453 0.61297 0.57728 -0.01599 0.01758  -0.06409 122 GLU A CG  
1903 C CD  . GLU A 136 ? 0.75467 0.73394 0.71724 -0.01291 0.01186  -0.07607 122 GLU A CD  
1904 O OE1 . GLU A 136 ? 0.72744 0.70197 0.68452 -0.01611 0.00487  -0.07515 122 GLU A OE1 
1905 O OE2 . GLU A 136 ? 0.80810 0.78465 0.78555 -0.00732 0.01367  -0.08635 122 GLU A OE2 
1912 N N   . LEU A 137 ? 0.33868 0.29754 0.29126 -0.02614 -0.00138 -0.02769 123 LEU A N   
1913 C CA  . LEU A 137 ? 0.40045 0.35559 0.34832 -0.02920 -0.00676 -0.01748 123 LEU A CA  
1914 C C   . LEU A 137 ? 0.35920 0.31625 0.29889 -0.03132 -0.01433 -0.02081 123 LEU A C   
1915 O O   . LEU A 137 ? 0.41786 0.37379 0.36341 -0.02984 -0.01717 -0.03050 123 LEU A O   
1916 C CB  . LEU A 137 ? 0.41687 0.36270 0.38023 -0.02715 -0.00795 -0.01201 123 LEU A CB  
1917 C CG  . LEU A 137 ? 0.32172 0.26351 0.28440 -0.02866 -0.01379 -0.00358 123 LEU A CG  
1918 C CD1 . LEU A 137 ? 0.30295 0.23967 0.27695 -0.02647 -0.01135 0.00198  123 LEU A CD1 
1919 C CD2 . LEU A 137 ? 0.35743 0.29796 0.32414 -0.02889 -0.02127 -0.00671 123 LEU A CD2 
1931 N N   . LYS A 138 ? 0.42183 0.38136 0.34882 -0.03505 -0.01854 -0.01229 124 LYS A N   
1932 C CA  . LYS A 138 ? 0.44051 0.40297 0.35808 -0.03749 -0.02715 -0.01297 124 LYS A CA  
1933 C C   . LYS A 138 ? 0.40326 0.35969 0.32258 -0.03888 -0.03393 -0.00041 124 LYS A C   
1934 O O   . LYS A 138 ? 0.42100 0.37674 0.33440 -0.04113 -0.03268 0.00962  124 LYS A O   
1935 C CB  . LYS A 138 ? 0.47800 0.45349 0.37417 -0.04104 -0.02590 -0.01560 124 LYS A CB  
1936 C CG  . LYS A 138 ? 0.62543 0.60621 0.50904 -0.04380 -0.03538 -0.01712 124 LYS A CG  
1937 C CD  . LYS A 138 ? 0.62413 0.60330 0.51651 -0.04105 -0.03927 -0.03181 124 LYS A CD  
1938 C CE  . LYS A 138 ? 0.70543 0.69606 0.57916 -0.04388 -0.04544 -0.03928 124 LYS A CE  
1939 N NZ  . LYS A 138 ? 0.75201 0.74439 0.61533 -0.04783 -0.05567 -0.02695 124 LYS A NZ  
1953 N N   . GLY A 139 ? 0.42310 0.37525 0.35255 -0.03746 -0.04135 -0.00125 125 GLY A N   
1954 C CA  . GLY A 139 ? 0.40550 0.35257 0.33985 -0.03741 -0.04869 0.00896  125 GLY A CA  
1955 C C   . GLY A 139 ? 0.40118 0.35240 0.32889 -0.03942 -0.05971 0.00954  125 GLY A C   
1956 O O   . GLY A 139 ? 0.39896 0.35403 0.32827 -0.03940 -0.06268 -0.00018 125 GLY A O   
1960 N N   . ILE A 140 ? 0.42823 0.37820 0.34940 -0.04129 -0.06672 0.02116  126 ILE A N   
1961 C CA  . ILE A 140 ? 0.39087 0.34527 0.30473 -0.04338 -0.07876 0.02458  126 ILE A CA  
1962 C C   . ILE A 140 ? 0.44786 0.39477 0.37268 -0.04145 -0.08701 0.03644  126 ILE A C   
1963 O O   . ILE A 140 ? 0.46626 0.40501 0.40019 -0.03929 -0.08303 0.04175  126 ILE A O   
1964 C CB  . ILE A 140 ? 0.45618 0.42056 0.34349 -0.04908 -0.08007 0.02778  126 ILE A CB  
1965 C CG1 . ILE A 140 ? 0.48423 0.44585 0.36308 -0.05228 -0.07732 0.04178  126 ILE A CG1 
1966 C CG2 . ILE A 140 ? 0.48426 0.45718 0.36233 -0.04970 -0.07152 0.01363  126 ILE A CG2 
1967 C CD1 . ILE A 140 ? 0.51033 0.48411 0.36304 -0.05900 -0.07808 0.04775  126 ILE A CD1 
1979 N N   . ASP A 141 ? 0.40296 0.35304 0.32755 -0.04192 -0.09936 0.03976  127 ASP A N   
1980 C CA  . ASP A 141 ? 0.46207 0.40604 0.39687 -0.03973 -0.10960 0.05144  127 ASP A CA  
1981 C C   . ASP A 141 ? 0.46141 0.39846 0.42323 -0.03306 -0.10712 0.04847  127 ASP A C   
1982 O O   . ASP A 141 ? 0.41808 0.34732 0.39036 -0.02991 -0.11081 0.05639  127 ASP A O   
1983 C CB  . ASP A 141 ? 0.47621 0.41497 0.39853 -0.04319 -0.11067 0.06561  127 ASP A CB  
1984 C CG  . ASP A 141 ? 0.49130 0.43989 0.38640 -0.05038 -0.11421 0.07140  127 ASP A CG  
1985 O OD1 . ASP A 141 ? 0.45461 0.41402 0.33950 -0.05200 -0.11586 0.06248  127 ASP A OD1 
1986 O OD2 . ASP A 141 ? 0.51821 0.46433 0.40224 -0.05478 -0.11543 0.08478  127 ASP A OD2 
1991 N N   . PHE A 142 ? 0.43589 0.37626 0.40984 -0.03091 -0.10110 0.03704  128 PHE A N   
1992 C CA  . PHE A 142 ? 0.41599 0.35356 0.41437 -0.02523 -0.09743 0.03412  128 PHE A CA  
1993 C C   . PHE A 142 ? 0.41505 0.35819 0.43110 -0.02260 -0.10745 0.03314  128 PHE A C   
1994 O O   . PHE A 142 ? 0.41311 0.36312 0.42494 -0.02563 -0.11431 0.02964  128 PHE A O   
1995 C CB  . PHE A 142 ? 0.39029 0.32905 0.39354 -0.02501 -0.08501 0.02477  128 PHE A CB  
1996 C CG  . PHE A 142 ? 0.45219 0.38519 0.44827 -0.02494 -0.07478 0.02635  128 PHE A CG  
1997 C CD1 . PHE A 142 ? 0.44140 0.36938 0.44942 -0.02069 -0.07105 0.02879  128 PHE A CD1 
1998 C CD2 . PHE A 142 ? 0.44681 0.38074 0.42489 -0.02893 -0.06918 0.02452  128 PHE A CD2 
1999 C CE1 . PHE A 142 ? 0.40625 0.32946 0.40795 -0.02103 -0.06283 0.02977  128 PHE A CE1 
2000 C CE2 . PHE A 142 ? 0.43439 0.36439 0.40770 -0.02908 -0.06049 0.02622  128 PHE A CE2 
2001 C CZ  . PHE A 142 ? 0.41694 0.34117 0.40185 -0.02544 -0.05779 0.02908  128 PHE A CZ  
2011 N N   . LYS A 143 ? 0.40219 0.34342 0.43886 -0.01677 -0.10842 0.03534  129 LYS A N   
2012 C CA  . LYS A 143 ? 0.40814 0.35576 0.46496 -0.01321 -0.11832 0.03568  129 LYS A CA  
2013 C C   . LYS A 143 ? 0.47179 0.42762 0.54982 -0.01137 -0.11133 0.02710  129 LYS A C   
2014 O O   . LYS A 143 ? 0.39995 0.35458 0.48579 -0.00864 -0.10019 0.02432  129 LYS A O   
2015 C CB  . LYS A 143 ? 0.42952 0.37118 0.49825 -0.00712 -0.12443 0.04311  129 LYS A CB  
2016 C CG  . LYS A 143 ? 0.45008 0.38289 0.50024 -0.00985 -0.13293 0.05443  129 LYS A CG  
2017 C CD  . LYS A 143 ? 0.42681 0.35010 0.49095 -0.00363 -0.13831 0.06119  129 LYS A CD  
2018 C CE  . LYS A 143 ? 0.50319 0.41763 0.55097 -0.00748 -0.14886 0.07510  129 LYS A CE  
2019 N NZ  . LYS A 143 ? 0.56179 0.46295 0.62307 -0.00206 -0.15343 0.08153  129 LYS A NZ  
2033 N N   . GLU A 144 ? 0.42358 0.38860 0.51066 -0.01353 -0.11831 0.02345  130 GLU A N   
2034 C CA  . GLU A 144 ? 0.44317 0.41723 0.55259 -0.01322 -0.11280 0.01698  130 GLU A CA  
2035 C C   . GLU A 144 ? 0.43550 0.41464 0.56911 -0.00611 -0.10964 0.01832  130 GLU A C   
2036 O O   . GLU A 144 ? 0.39439 0.37900 0.54115 -0.00513 -0.09882 0.01471  130 GLU A O   
2037 C CB  . GLU A 144 ? 0.38761 0.37067 0.50461 -0.01718 -0.12347 0.01343  130 GLU A CB  
2038 C CG  . GLU A 144 ? 0.56840 0.56165 0.71097 -0.01847 -0.11912 0.00804  130 GLU A CG  
2039 C CD  . GLU A 144 ? 0.61316 0.60229 0.75087 -0.02252 -0.10695 0.00315  130 GLU A CD  
2040 O OE1 . GLU A 144 ? 0.59816 0.57769 0.71244 -0.02446 -0.10336 0.00196  130 GLU A OE1 
2041 O OE2 . GLU A 144 ? 0.60587 0.60214 0.76422 -0.02386 -0.10114 0.00121  130 GLU A OE2 
2048 N N   . ASP A 145 ? 0.43149 0.40967 0.57165 -0.00092 -0.11917 0.02349  131 ASP A N   
2049 C CA  . ASP A 145 ? 0.47907 0.46214 0.64289 0.00733  -0.11707 0.02315  131 ASP A CA  
2050 C C   . ASP A 145 ? 0.41219 0.38392 0.56798 0.01162  -0.10976 0.02434  131 ASP A C   
2051 O O   . ASP A 145 ? 0.43052 0.40214 0.60198 0.01942  -0.11172 0.02439  131 ASP A O   
2052 C CB  . ASP A 145 ? 0.55723 0.54496 0.73676 0.01184  -0.13247 0.02732  131 ASP A CB  
2053 C CG  . ASP A 145 ? 0.55223 0.52827 0.71101 0.00985  -0.14513 0.03600  131 ASP A CG  
2054 O OD1 . ASP A 145 ? 0.51681 0.48165 0.65001 0.00546  -0.14076 0.03855  131 ASP A OD1 
2055 O OD2 . ASP A 145 ? 0.49348 0.47292 0.66211 0.01241  -0.15965 0.04105  131 ASP A OD2 
2060 N N   . GLY A 146 ? 0.42498 0.38754 0.55822 0.00695  -0.10185 0.02443  132 GLY A N   
2061 C CA  . GLY A 146 ? 0.48914 0.44150 0.61450 0.00976  -0.09499 0.02497  132 GLY A CA  
2062 C C   . GLY A 146 ? 0.40204 0.35953 0.53065 0.01022  -0.07998 0.01872  132 GLY A C   
2063 O O   . GLY A 146 ? 0.41831 0.38715 0.55681 0.00837  -0.07453 0.01513  132 GLY A O   
2067 N N   . ASN A 147 ? 0.44269 0.39160 0.56273 0.01214  -0.07395 0.01825  133 ASN A N   
2068 C CA  . ASN A 147 ? 0.38251 0.33682 0.50469 0.01332  -0.06067 0.01291  133 ASN A CA  
2069 C C   . ASN A 147 ? 0.38702 0.34148 0.49469 0.00634  -0.05309 0.01304  133 ASN A C   
2070 O O   . ASN A 147 ? 0.42650 0.38883 0.53885 0.00619  -0.04317 0.01014  133 ASN A O   
2071 C CB  . ASN A 147 ? 0.39090 0.33602 0.50870 0.01753  -0.05802 0.01132  133 ASN A CB  
2072 C CG  . ASN A 147 ? 0.34644 0.28979 0.48125 0.02563  -0.06547 0.00967  133 ASN A CG  
2073 O OD1 . ASN A 147 ? 0.34173 0.29737 0.49699 0.03065  -0.06636 0.00614  133 ASN A OD1 
2074 N ND2 . ASN A 147 ? 0.40325 0.33143 0.53167 0.02694  -0.07131 0.01239  133 ASN A ND2 
2081 N N   . ILE A 148 ? 0.36278 0.30959 0.45341 0.00081  -0.05753 0.01640  134 ILE A N   
2082 C CA  . ILE A 148 ? 0.38209 0.32816 0.46016 -0.00472 -0.05088 0.01529  134 ILE A CA  
2083 C C   . ILE A 148 ? 0.42925 0.38332 0.51647 -0.00800 -0.05234 0.01299  134 ILE A C   
2084 O O   . ILE A 148 ? 0.41875 0.37931 0.51542 -0.00892 -0.04496 0.01105  134 ILE A O   
2085 C CB  . ILE A 148 ? 0.41730 0.35378 0.47348 -0.00878 -0.05374 0.01844  134 ILE A CB  
2086 C CG1 . ILE A 148 ? 0.45876 0.38726 0.50768 -0.00696 -0.05094 0.02080  134 ILE A CG1 
2087 C CG2 . ILE A 148 ? 0.47707 0.41440 0.52333 -0.01356 -0.04827 0.01559  134 ILE A CG2 
2088 C CD1 . ILE A 148 ? 0.51708 0.43878 0.56802 -0.00442 -0.06042 0.02557  134 ILE A CD1 
2100 N N   . LEU A 149 ? 0.42484 0.37875 0.50963 -0.01030 -0.06249 0.01365  135 LEU A N   
2101 C CA  . LEU A 149 ? 0.36506 0.32596 0.45964 -0.01390 -0.06549 0.01030  135 LEU A CA  
2102 C C   . LEU A 149 ? 0.35685 0.32945 0.47720 -0.01134 -0.06416 0.00966  135 LEU A C   
2103 O O   . LEU A 149 ? 0.39647 0.37566 0.52891 -0.01495 -0.06235 0.00750  135 LEU A O   
2104 C CB  . LEU A 149 ? 0.40164 0.36173 0.48792 -0.01656 -0.07793 0.01052  135 LEU A CB  
2105 C CG  . LEU A 149 ? 0.40125 0.35352 0.46116 -0.01968 -0.07941 0.01147  135 LEU A CG  
2106 C CD1 . LEU A 149 ? 0.40785 0.36298 0.45921 -0.02302 -0.09142 0.01072  135 LEU A CD1 
2107 C CD2 . LEU A 149 ? 0.44746 0.39656 0.49838 -0.02239 -0.06950 0.00690  135 LEU A CD2 
2119 N N   . GLY A 150 ? 0.42246 0.39834 0.55292 -0.00524 -0.06506 0.01131  136 GLY A N   
2120 C CA  . GLY A 150 ? 0.43399 0.42401 0.58953 -0.00192 -0.06233 0.01001  136 GLY A CA  
2121 C C   . GLY A 150 ? 0.37987 0.37649 0.54076 -0.00098 -0.04868 0.00896  136 GLY A C   
2122 O O   . GLY A 150 ? 0.39022 0.40173 0.57156 0.00116  -0.04453 0.00806  136 GLY A O   
2126 N N   . HIS A 151 ? 0.37274 0.36052 0.51592 -0.00262 -0.04160 0.00943  137 HIS A N   
2127 C CA  . HIS A 151 ? 0.39769 0.39174 0.54269 -0.00230 -0.02935 0.00948  137 HIS A CA  
2128 C C   . HIS A 151 ? 0.33872 0.34371 0.49639 0.00484  -0.02506 0.00699  137 HIS A C   
2129 O O   . HIS A 151 ? 0.30485 0.32617 0.47879 0.00530  -0.01858 0.00672  137 HIS A O   
2130 C CB  . HIS A 151 ? 0.38148 0.38381 0.53740 -0.00837 -0.02519 0.01144  137 HIS A CB  
2131 C CG  . HIS A 151 ? 0.42503 0.41607 0.56967 -0.01441 -0.02843 0.01167  137 HIS A CG  
2132 N ND1 . HIS A 151 ? 0.40393 0.38668 0.53401 -0.01624 -0.02263 0.01269  137 HIS A ND1 
2133 C CD2 . HIS A 151 ? 0.43449 0.42206 0.58104 -0.01852 -0.03715 0.00979  137 HIS A CD2 
2134 C CE1 . HIS A 151 ? 0.45778 0.43235 0.58223 -0.02063 -0.02711 0.01089  137 HIS A CE1 
2135 N NE2 . HIS A 151 ? 0.48826 0.46547 0.62160 -0.02224 -0.03588 0.00862  137 HIS A NE2 
2143 N N   . LYS A 152 ? 0.34273 0.33895 0.49336 0.01034  -0.02881 0.00491  138 LYS A N   
2144 C CA  . LYS A 152 ? 0.29846 0.30247 0.46110 0.01850  -0.02627 0.00012  138 LYS A CA  
2145 C C   . LYS A 152 ? 0.35349 0.35232 0.50286 0.02113  -0.01918 -0.00299 138 LYS A C   
2146 O O   . LYS A 152 ? 0.35592 0.35779 0.51243 0.02850  -0.01814 -0.00895 138 LYS A O   
2147 C CB  . LYS A 152 ? 0.28501 0.28275 0.45567 0.02380  -0.03832 -0.00056 138 LYS A CB  
2148 C CG  . LYS A 152 ? 0.36521 0.36915 0.54934 0.02159  -0.04717 0.00220  138 LYS A CG  
2149 C CD  . LYS A 152 ? 0.29777 0.29671 0.49138 0.02771  -0.05980 0.00259  138 LYS A CD  
2150 C CE  . LYS A 152 ? 0.43724 0.44453 0.64504 0.02560  -0.06952 0.00518  138 LYS A CE  
2151 N NZ  . LYS A 152 ? 0.41171 0.41691 0.63294 0.03265  -0.08223 0.00621  138 LYS A NZ  
2165 N N   . LEU A 153 ? 0.38967 0.38126 0.52120 0.01566  -0.01481 0.00001  139 LEU A N   
2166 C CA  . LEU A 153 ? 0.42409 0.41074 0.54224 0.01721  -0.00931 -0.00254 139 LEU A CA  
2167 C C   . LEU A 153 ? 0.40439 0.40676 0.52430 0.01676  0.00231  -0.00340 139 LEU A C   
2168 O O   . LEU A 153 ? 0.32395 0.33374 0.44669 0.01147  0.00632  0.00171  139 LEU A O   
2169 C CB  . LEU A 153 ? 0.35943 0.33068 0.45782 0.01174  -0.01162 0.00162  139 LEU A CB  
2170 C CG  . LEU A 153 ? 0.33904 0.29604 0.43156 0.01062  -0.02233 0.00430  139 LEU A CG  
2171 C CD1 . LEU A 153 ? 0.40589 0.35190 0.47913 0.00531  -0.02207 0.00769  139 LEU A CD1 
2172 C CD2 . LEU A 153 ? 0.40912 0.36040 0.50824 0.01696  -0.02829 0.00118  139 LEU A CD2 
2184 N N   . GLU A 154 ? 0.40521 0.41264 0.52347 0.02209  0.00716  -0.00975 140 GLU A N   
2185 C CA  . GLU A 154 ? 0.44829 0.47153 0.56380 0.02136  0.01813  -0.01005 140 GLU A CA  
2186 C C   . GLU A 154 ? 0.36853 0.38503 0.46806 0.01441  0.02060  -0.00291 140 GLU A C   
2187 O O   . GLU A 154 ? 0.36075 0.36070 0.44787 0.01248  0.01556  -0.00180 140 GLU A O   
2188 C CB  . GLU A 154 ? 0.41528 0.44326 0.52796 0.02839  0.02161  -0.02004 140 GLU A CB  
2189 C CG  . GLU A 154 ? 0.51943 0.55736 0.65065 0.03686  0.02075  -0.02898 140 GLU A CG  
2190 C CD  . GLU A 154 ? 0.60461 0.64849 0.73326 0.04426  0.02486  -0.04124 140 GLU A CD  
2191 O OE1 . GLU A 154 ? 0.51210 0.55227 0.62345 0.04207  0.02779  -0.04218 140 GLU A OE1 
2192 O OE2 . GLU A 154 ? 0.61456 0.66735 0.75935 0.05261  0.02473  -0.05080 140 GLU A OE2 
2199 N N   . TYR A 155 ? 0.35882 0.38913 0.46003 0.01058  0.02832  0.00258  141 TYR A N   
2200 C CA  . TYR A 155 ? 0.32986 0.35545 0.41846 0.00495  0.03079  0.00966  141 TYR A CA  
2201 C C   . TYR A 155 ? 0.37333 0.40516 0.44929 0.00741  0.03622  0.00644  141 TYR A C   
2202 O O   . TYR A 155 ? 0.36272 0.41258 0.43953 0.00728  0.04402  0.00816  141 TYR A O   
2203 C CB  . TYR A 155 ? 0.25309 0.28842 0.35119 -0.00099 0.03475  0.01882  141 TYR A CB  
2204 C CG  . TYR A 155 ? 0.26776 0.29559 0.35592 -0.00617 0.03547  0.02646  141 TYR A CG  
2205 C CD1 . TYR A 155 ? 0.28042 0.29141 0.36596 -0.00911 0.02911  0.02800  141 TYR A CD1 
2206 C CD2 . TYR A 155 ? 0.29310 0.33169 0.37461 -0.00767 0.04222  0.03181  141 TYR A CD2 
2207 C CE1 . TYR A 155 ? 0.30166 0.30605 0.38070 -0.01264 0.02952  0.03379  141 TYR A CE1 
2208 C CE2 . TYR A 155 ? 0.28968 0.32105 0.36419 -0.01169 0.04176  0.03937  141 TYR A CE2 
2209 C CZ  . TYR A 155 ? 0.32144 0.33535 0.39598 -0.01377 0.03542  0.03988  141 TYR A CZ  
2210 O OH  . TYR A 155 ? 0.33973 0.34672 0.40991 -0.01663 0.03474  0.04622  141 TYR A OH  
2220 N N   . ASN A 156 ? 0.43697 0.45492 0.50091 0.00914  0.03180  0.00191  142 ASN A N   
2221 C CA  . ASN A 156 ? 0.55466 0.57712 0.60638 0.01124  0.03516  -0.00255 142 ASN A CA  
2222 C C   . ASN A 156 ? 0.50802 0.51239 0.54807 0.00993  0.02901  -0.00358 142 ASN A C   
2223 O O   . ASN A 156 ? 0.47495 0.46474 0.51708 0.00956  0.02231  -0.00395 142 ASN A O   
2224 C CB  . ASN A 156 ? 0.51629 0.54918 0.57297 0.01843  0.03744  -0.01405 142 ASN A CB  
2225 C CG  . ASN A 156 ? 0.59667 0.61474 0.66010 0.02303  0.02926  -0.02157 142 ASN A CG  
2226 O OD1 . ASN A 156 ? 0.65339 0.65728 0.71962 0.02048  0.02262  -0.01684 142 ASN A OD1 
2227 N ND2 . ASN A 156 ? 0.66925 0.69078 0.73550 0.02994  0.02928  -0.03343 142 ASN A ND2 
2234 N N   . GLY A 157 ? 0.58665 0.59375 0.61456 0.00871  0.03125  -0.00318 143 GLY A N   
2235 C CA  . GLY A 157 ? 0.63907 0.63244 0.65730 0.00741  0.02605  -0.00496 143 GLY A CA  
2236 C C   . GLY A 157 ? 0.61944 0.60656 0.63807 0.01194  0.02189  -0.01596 143 GLY A C   
2237 O O   . GLY A 157 ? 0.65678 0.64948 0.68377 0.01714  0.02276  -0.02323 143 GLY A O   
2241 N N   . TRP A 158 ? 0.49587 0.47126 0.50710 0.00992  0.01697  -0.01735 144 TRP A N   
2242 C CA  . TRP A 158 ? 0.51292 0.47860 0.52589 0.01303  0.01130  -0.02688 144 TRP A CA  
2243 C C   . TRP A 158 ? 0.52342 0.48210 0.52679 0.00909  0.00785  -0.02706 144 TRP A C   
2244 O O   . TRP A 158 ? 0.47960 0.44230 0.47565 0.00488  0.01011  -0.02013 144 TRP A O   
2245 C CB  . TRP A 158 ? 0.50701 0.45869 0.52950 0.01371  0.00485  -0.02557 144 TRP A CB  
2246 C CG  . TRP A 158 ? 0.46896 0.40957 0.48688 0.00742  0.00124  -0.01613 144 TRP A CG  
2247 C CD1 . TRP A 158 ? 0.45492 0.38291 0.46872 0.00367  -0.00441 -0.01468 144 TRP A CD1 
2248 C CD2 . TRP A 158 ? 0.38997 0.33268 0.40737 0.00396  0.00336  -0.00748 144 TRP A CD2 
2249 N NE1 . TRP A 158 ? 0.53785 0.46198 0.54757 -0.00163 -0.00501 -0.00573 144 TRP A NE1 
2250 C CE2 . TRP A 158 ? 0.49790 0.43024 0.50958 -0.00111 -0.00058 -0.00218 144 TRP A CE2 
2251 C CE3 . TRP A 158 ? 0.50721 0.45989 0.52937 0.00435  0.00804  -0.00410 144 TRP A CE3 
2252 C CZ2 . TRP A 158 ? 0.45877 0.39084 0.46832 -0.00476 0.00024  0.00448  144 TRP A CZ2 
2253 C CZ3 . TRP A 158 ? 0.47705 0.42705 0.49834 0.00029  0.00774  0.00285  144 TRP A CZ3 
2254 C CH2 . TRP A 158 ? 0.42584 0.36582 0.44035 -0.00371 0.00398  0.00615  144 TRP A CH2 
2265 N N   . CYS A 159 ? 0.53906 0.48705 0.54459 0.01052  0.00170  -0.03503 145 CYS A N   
2266 C CA  . CYS A 159 ? 0.55400 0.49414 0.55354 0.00606  -0.00300 -0.03566 145 CYS A CA  
2267 C C   . CYS A 159 ? 0.54859 0.46990 0.55472 0.00350  -0.01108 -0.03348 145 CYS A C   
2268 O O   . CYS A 159 ? 0.51444 0.42787 0.53004 0.00777  -0.01512 -0.03839 145 CYS A O   
2269 C CB  . CYS A 159 ? 0.53170 0.47779 0.52737 0.00921  -0.00358 -0.04832 145 CYS A CB  
2270 S SG  . CYS A 159 ? 0.57453 0.54526 0.55881 0.01093  0.00529  -0.04933 145 CYS A SG  
2271 N N   . GLY A 160 ? 0.51572 0.43093 0.51776 -0.00344 -0.01349 -0.02549 146 GLY A N   
2272 C CA  . GLY A 160 ? 0.51898 0.41809 0.52595 -0.00750 -0.02096 -0.02136 146 GLY A CA  
2273 C C   . GLY A 160 ? 0.46168 0.35555 0.47270 -0.00727 -0.02216 -0.01385 146 GLY A C   
2274 O O   . GLY A 160 ? 0.43726 0.33955 0.44819 -0.00438 -0.01729 -0.01206 146 GLY A O   
2275 N N   . ASP A 161 ? 0.51632 0.39618 0.53125 -0.01107 -0.02954 -0.00873 147 ASP A N   
2276 C CA  . ASP A 161 ? 0.45724 0.32646 0.47446 -0.01571 -0.03587 -0.00971 147 ASP A CA  
2277 C C   . ASP A 161 ? 0.48667 0.36257 0.49579 -0.02316 -0.03267 -0.00423 147 ASP A C   
2278 O O   . ASP A 161 ? 0.46713 0.35224 0.46967 -0.02530 -0.02697 0.00250  147 ASP A O   
2279 C CB  . ASP A 161 ? 0.52544 0.37818 0.54989 -0.01883 -0.04487 -0.00244 147 ASP A CB  
2280 C CG  . ASP A 161 ? 0.57518 0.41972 0.61132 -0.01074 -0.05004 -0.00864 147 ASP A CG  
2281 O OD1 . ASP A 161 ? 0.55248 0.40599 0.59097 -0.00276 -0.04550 -0.01923 147 ASP A OD1 
2282 O OD2 . ASP A 161 ? 0.60296 0.43302 0.64671 -0.01241 -0.05876 -0.00230 147 ASP A OD2 
2283 N N   . ASN A 162 ? 0.46742 0.33884 0.47874 -0.02678 -0.03687 -0.00807 148 ASN A N   
2284 C CA  . ASN A 162 ? 0.42789 0.30660 0.43445 -0.03390 -0.03480 -0.00334 148 ASN A CA  
2285 C C   . ASN A 162 ? 0.45877 0.33797 0.46275 -0.04069 -0.03348 0.00994  148 ASN A C   
2286 O O   . ASN A 162 ? 0.43010 0.29869 0.43727 -0.04328 -0.03823 0.01651  148 ASN A O   
2287 C CB  . ASN A 162 ? 0.45705 0.32789 0.46956 -0.03815 -0.04202 -0.00856 148 ASN A CB  
2288 C CG  . ASN A 162 ? 0.46617 0.33978 0.47879 -0.03159 -0.04288 -0.02368 148 ASN A CG  
2289 O OD1 . ASN A 162 ? 0.42440 0.31228 0.42950 -0.02675 -0.03626 -0.02772 148 ASN A OD1 
2290 N ND2 . ASN A 162 ? 0.46035 0.32060 0.48164 -0.03152 -0.05130 -0.03213 148 ASN A ND2 
2297 N N   . VAL A 163 ? 0.37514 0.36087 0.35706 -0.06302 -0.02257 0.00353  149 VAL A N   
2298 C CA  . VAL A 163 ? 0.43262 0.41782 0.41497 -0.06167 -0.01861 0.01347  149 VAL A CA  
2299 C C   . VAL A 163 ? 0.41706 0.40501 0.41339 -0.06684 -0.01896 0.01758  149 VAL A C   
2300 O O   . VAL A 163 ? 0.36241 0.36049 0.36529 -0.06903 -0.02015 0.01805  149 VAL A O   
2301 C CB  . VAL A 163 ? 0.40852 0.40132 0.38379 -0.05809 -0.01707 0.01663  149 VAL A CB  
2302 C CG1 . VAL A 163 ? 0.36909 0.36330 0.34456 -0.05518 -0.01238 0.02379  149 VAL A CG1 
2303 C CG2 . VAL A 163 ? 0.38728 0.37717 0.35221 -0.05472 -0.01771 0.01422  149 VAL A CG2 
2313 N N   . TYR A 164 ? 0.36369 0.34282 0.36659 -0.06929 -0.01873 0.02177  150 TYR A N   
2314 C CA  . TYR A 164 ? 0.36297 0.34441 0.38210 -0.07583 -0.01905 0.02827  150 TYR A CA  
2315 C C   . TYR A 164 ? 0.33282 0.32516 0.35076 -0.07505 -0.01111 0.03905  150 TYR A C   
2316 O O   . TYR A 164 ? 0.33541 0.32500 0.34169 -0.07125 -0.00609 0.04494  150 TYR A O   
2317 C CB  . TYR A 164 ? 0.39553 0.36262 0.42318 -0.07928 -0.02265 0.03107  150 TYR A CB  
2318 C CG  . TYR A 164 ? 0.36826 0.32784 0.40668 -0.08140 -0.03156 0.01869  150 TYR A CG  
2319 C CD1 . TYR A 164 ? 0.43013 0.38662 0.45917 -0.07602 -0.03379 0.00600  150 TYR A CD1 
2320 C CD2 . TYR A 164 ? 0.36350 0.32046 0.42264 -0.08867 -0.03780 0.01886  150 TYR A CD2 
2321 C CE1 . TYR A 164 ? 0.40132 0.35333 0.43876 -0.07654 -0.04111 -0.00791 150 TYR A CE1 
2322 C CE2 . TYR A 164 ? 0.39491 0.34445 0.46377 -0.08944 -0.04723 0.00457  150 TYR A CE2 
2323 C CZ  . TYR A 164 ? 0.40845 0.35611 0.46509 -0.08272 -0.04840 -0.00966 150 TYR A CZ  
2324 O OH  . TYR A 164 ? 0.47486 0.41742 0.53969 -0.08210 -0.05693 -0.02630 150 TYR A OH  
2334 N N   . ILE A 165 ? 0.36729 0.37323 0.39762 -0.07806 -0.01033 0.04056  151 ILE A N   
2335 C CA  . ILE A 165 ? 0.35838 0.37925 0.39064 -0.07603 -0.00207 0.04804  151 ILE A CA  
2336 C C   . ILE A 165 ? 0.37693 0.40540 0.42854 -0.08426 0.00133  0.05856  151 ILE A C   
2337 O O   . ILE A 165 ? 0.34078 0.36752 0.41067 -0.09178 -0.00539 0.05753  151 ILE A O   
2338 C CB  . ILE A 165 ? 0.37425 0.40733 0.40940 -0.07230 -0.00391 0.04235  151 ILE A CB  
2339 C CG1 . ILE A 165 ? 0.35809 0.38333 0.37510 -0.06566 -0.00745 0.03497  151 ILE A CG1 
2340 C CG2 . ILE A 165 ? 0.39657 0.44680 0.43797 -0.06886 0.00466  0.04793  151 ILE A CG2 
2341 C CD1 . ILE A 165 ? 0.37681 0.41143 0.39548 -0.06189 -0.01087 0.03165  151 ILE A CD1 
2353 N N   . THR A 166 ? 0.35028 0.38789 0.39797 -0.08304 0.01156  0.06869  152 THR A N   
2354 C CA  . THR A 166 ? 0.35276 0.40215 0.41840 -0.09134 0.01756  0.08187  152 THR A CA  
2355 C C   . THR A 166 ? 0.35304 0.42608 0.41884 -0.08656 0.02985  0.08574  152 THR A C   
2356 O O   . THR A 166 ? 0.37999 0.45495 0.42636 -0.07637 0.03421  0.08034  152 THR A O   
2357 C CB  . THR A 166 ? 0.40435 0.44144 0.46388 -0.09626 0.01880  0.09388  152 THR A CB  
2358 O OG1 . THR A 166 ? 0.48308 0.51460 0.51481 -0.08761 0.02304  0.09339  152 THR A OG1 
2359 C CG2 . THR A 166 ? 0.37508 0.39057 0.44341 -0.10161 0.00599  0.08983  152 THR A CG2 
2367 N N   . ALA A 167 ? 0.40714 0.49888 0.49731 -0.09379 0.03503  0.09432  153 ALA A N   
2368 C CA  . ALA A 167 ? 0.40129 0.51983 0.49641 -0.08917 0.04803  0.09732  153 ALA A CA  
2369 C C   . ALA A 167 ? 0.41568 0.54080 0.49273 -0.08804 0.06100  0.10869  153 ALA A C   
2370 O O   . ALA A 167 ? 0.46976 0.58469 0.54341 -0.09625 0.06068  0.12120  153 ALA A O   
2371 C CB  . ALA A 167 ? 0.36571 0.50511 0.49665 -0.09787 0.04956  0.10319  153 ALA A CB  
2377 N N   . ASP A 168 ? 0.42425 0.56635 0.48930 -0.07726 0.07150  0.10384  154 ASP A N   
2378 C CA  . ASP A 168 ? 0.48150 0.63489 0.52570 -0.07409 0.08503  0.11221  154 ASP A CA  
2379 C C   . ASP A 168 ? 0.47712 0.66604 0.53651 -0.07020 0.09995  0.11241  154 ASP A C   
2380 O O   . ASP A 168 ? 0.45122 0.64979 0.50246 -0.05674 0.10369  0.09878  154 ASP A O   
2381 C CB  . ASP A 168 ? 0.51599 0.65298 0.52592 -0.06204 0.08178  0.10168  154 ASP A CB  
2382 C CG  . ASP A 168 ? 0.59221 0.73843 0.57589 -0.05873 0.09338  0.10962  154 ASP A CG  
2383 O OD1 . ASP A 168 ? 0.64041 0.80803 0.63130 -0.06586 0.10580  0.12449  154 ASP A OD1 
2384 O OD2 . ASP A 168 ? 0.61863 0.75145 0.57424 -0.04937 0.08969  0.10144  154 ASP A OD2 
2389 N N   . LYS A 169 ? 0.43630 0.64511 0.52070 -0.08200 0.10799  0.12767  155 LYS A N   
2390 C CA  . LYS A 169 ? 0.49902 0.74544 0.60493 -0.07936 0.12269  0.12821  155 LYS A CA  
2391 C C   . LYS A 169 ? 0.50387 0.77092 0.58360 -0.06896 0.13992  0.12750  155 LYS A C   
2392 O O   . LYS A 169 ? 0.52675 0.82120 0.61599 -0.05874 0.15029  0.11763  155 LYS A O   
2393 C CB  . LYS A 169 ? 0.44409 0.70747 0.58474 -0.09625 0.12727  0.14694  155 LYS A CB  
2394 C CG  . LYS A 169 ? 0.55797 0.85197 0.73817 -0.09601 0.13199  0.14290  155 LYS A CG  
2395 C CD  . LYS A 169 ? 0.63121 0.96598 0.81319 -0.08938 0.15465  0.14549  155 LYS A CD  
2396 C CE  . LYS A 169 ? 0.67735 1.03354 0.87025 -0.10483 0.16917  0.17095  155 LYS A CE  
2397 N NZ  . LYS A 169 ? 0.64202 1.00300 0.88128 -0.12150 0.16200  0.18256  155 LYS A NZ  
2400 N N   . GLN A 170 ? 0.57951 0.83438 0.62648 -0.07061 0.14239  0.13681  156 GLN A N   
2401 C CA  . GLN A 170 ? 0.62985 0.90316 0.64628 -0.06004 0.15732  0.13470  156 GLN A CA  
2402 C C   . GLN A 170 ? 0.64076 0.91196 0.64449 -0.04071 0.15414  0.10905  156 GLN A C   
2403 O O   . GLN A 170 ? 0.59393 0.89387 0.59642 -0.02949 0.16774  0.09979  156 GLN A O   
2404 C CB  . GLN A 170 ? 0.71499 0.96838 0.69548 -0.06420 0.15482  0.14718  156 GLN A CB  
2405 C CG  . GLN A 170 ? 0.77494 1.05260 0.74883 -0.07440 0.17132  0.17125  156 GLN A CG  
2406 C CD  . GLN A 170 ? 0.88601 1.14613 0.81768 -0.07447 0.16855  0.18094  156 GLN A CD  
2407 O OE1 . GLN A 170 ? 0.84185 1.10164 0.73915 -0.06034 0.17034  0.16758  156 GLN A OE1 
2408 N NE2 . GLN A 170 ? 0.89903 1.14331 0.83454 -0.09017 0.16234  0.20383  156 GLN A NE2 
2417 N N   . LYS A 171 ? 0.57582 0.81368 0.57143 -0.03655 0.13611  0.09728  157 LYS A N   
2418 C CA  . LYS A 171 ? 0.54568 0.77618 0.53201 -0.01999 0.12963  0.07481  157 LYS A CA  
2419 C C   . LYS A 171 ? 0.49738 0.73483 0.51784 -0.01655 0.12399  0.06408  157 LYS A C   
2420 O O   . LYS A 171 ? 0.46426 0.69371 0.48224 -0.00377 0.11632  0.04681  157 LYS A O   
2421 C CB  . LYS A 171 ? 0.57443 0.76711 0.53704 -0.01817 0.11297  0.06931  157 LYS A CB  
2422 C CG  . LYS A 171 ? 0.63493 0.81592 0.56435 -0.02130 0.11417  0.07961  157 LYS A CG  
2423 C CD  . LYS A 171 ? 0.64068 0.82573 0.53799 -0.00642 0.11812  0.06705  157 LYS A CD  
2424 C CE  . LYS A 171 ? 0.69697 0.91752 0.58517 -0.00378 0.13843  0.07257  157 LYS A CE  
2425 N NZ  . LYS A 171 ? 0.73622 0.96167 0.59187 0.01248  0.14145  0.05657  157 LYS A NZ  
2439 N N   . ASN A 172 ? 0.54815 0.79927 0.60141 -0.02789 0.12595  0.07441  158 ASN A N   
2440 C CA  . ASN A 172 ? 0.49285 0.74818 0.57877 -0.02614 0.11740  0.06590  158 ASN A CA  
2441 C C   . ASN A 172 ? 0.45511 0.67670 0.53204 -0.02317 0.09772  0.05593  158 ASN A C   
2442 O O   . ASN A 172 ? 0.49586 0.71622 0.58434 -0.01434 0.08956  0.04352  158 ASN A O   
2443 C CB  . ASN A 172 ? 0.49815 0.78335 0.59890 -0.01199 0.12730  0.05317  158 ASN A CB  
2444 C CG  . ASN A 172 ? 0.52167 0.81625 0.66167 -0.01171 0.11911  0.04796  158 ASN A CG  
2445 O OD1 . ASN A 172 ? 0.44640 0.74432 0.61106 -0.02501 0.11540  0.05885  158 ASN A OD1 
2446 N ND2 . ASN A 172 ? 0.53314 0.83066 0.68002 0.00360  0.11436  0.03106  158 ASN A ND2 
2453 N N   . GLY A 173 ? 0.37603 0.57087 0.43317 -0.03071 0.08999  0.06222  159 GLY A N   
2454 C CA  . GLY A 173 ? 0.42135 0.58655 0.46765 -0.02876 0.07362  0.05424  159 GLY A CA  
2455 C C   . GLY A 173 ? 0.40214 0.54727 0.44732 -0.04182 0.06533  0.06338  159 GLY A C   
2456 O O   . GLY A 173 ? 0.37438 0.52764 0.43985 -0.05301 0.06688  0.07330  159 GLY A O   
2460 N N   . ILE A 174 ? 0.39430 0.51366 0.41821 -0.04024 0.05604  0.05939  160 ILE A N   
2461 C CA  . ILE A 174 ? 0.40871 0.50789 0.43172 -0.05013 0.04696  0.06423  160 ILE A CA  
2462 C C   . ILE A 174 ? 0.40886 0.48833 0.40475 -0.04758 0.04463  0.06446  160 ILE A C   
2463 O O   . ILE A 174 ? 0.38912 0.46759 0.36648 -0.03791 0.04699  0.05878  160 ILE A O   
2464 C CB  . ILE A 174 ? 0.36670 0.45595 0.39979 -0.05124 0.03414  0.05625  160 ILE A CB  
2465 C CG1 . ILE A 174 ? 0.40117 0.48313 0.42150 -0.04032 0.02903  0.04556  160 ILE A CG1 
2466 C CG2 . ILE A 174 ? 0.36975 0.47661 0.43132 -0.05569 0.03353  0.05738  160 ILE A CG2 
2467 C CD1 . ILE A 174 ? 0.42550 0.48977 0.44109 -0.04227 0.01687  0.04075  160 ILE A CD1 
2479 N N   . LYS A 175 ? 0.37272 0.43613 0.36850 -0.05596 0.03859  0.07004  161 LYS A N   
2480 C CA  . LYS A 175 ? 0.38794 0.43058 0.36367 -0.05414 0.03298  0.06919  161 LYS A CA  
2481 C C   . LYS A 175 ? 0.40732 0.43387 0.39054 -0.05827 0.02178  0.06360  161 LYS A C   
2482 O O   . LYS A 175 ? 0.37391 0.40387 0.37586 -0.06472 0.01855  0.06332  161 LYS A O   
2483 C CB  . LYS A 175 ? 0.39383 0.43365 0.36120 -0.05941 0.03726  0.08278  161 LYS A CB  
2484 C CG  . LYS A 175 ? 0.41625 0.47416 0.37044 -0.05505 0.04970  0.08867  161 LYS A CG  
2485 C CD  . LYS A 175 ? 0.60658 0.66461 0.55499 -0.06315 0.05415  0.10645  161 LYS A CD  
2486 C CE  . LYS A 175 ? 0.73172 0.77744 0.64990 -0.05745 0.05167  0.10795  161 LYS A CE  
2487 N NZ  . LYS A 175 ? 0.72775 0.78840 0.62453 -0.04606 0.06008  0.10070  161 LYS A NZ  
2501 N N   . ALA A 176 ? 0.40150 0.41200 0.37036 -0.05417 0.01575  0.05819  162 ALA A N   
2502 C CA  . ALA A 176 ? 0.41800 0.41583 0.39205 -0.05702 0.00689  0.05192  162 ALA A CA  
2503 C C   . ALA A 176 ? 0.44626 0.42764 0.40910 -0.05556 0.00260  0.05227  162 ALA A C   
2504 O O   . ALA A 176 ? 0.38353 0.36197 0.33087 -0.05020 0.00419  0.05415  162 ALA A O   
2505 C CB  . ALA A 176 ? 0.36232 0.36254 0.33589 -0.05272 0.00306  0.04219  162 ALA A CB  
2511 N N   . ASN A 177 ? 0.44829 0.41945 0.42016 -0.05980 -0.00374 0.04926  163 ASN A N   
2512 C CA  . ASN A 177 ? 0.42985 0.38590 0.39703 -0.05828 -0.00916 0.04831  163 ASN A CA  
2513 C C   . ASN A 177 ? 0.39604 0.34755 0.37085 -0.05832 -0.01479 0.03684  163 ASN A C   
2514 O O   . ASN A 177 ? 0.45608 0.41111 0.44282 -0.06264 -0.01657 0.03248  163 ASN A O   
2515 C CB  . ASN A 177 ? 0.47890 0.42663 0.45243 -0.06375 -0.01096 0.05903  163 ASN A CB  
2516 C CG  . ASN A 177 ? 0.49831 0.42948 0.47241 -0.06193 -0.01894 0.05695  163 ASN A CG  
2517 O OD1 . ASN A 177 ? 0.38027 0.30430 0.36868 -0.06376 -0.02488 0.04966  163 ASN A OD1 
2518 N ND2 . ASN A 177 ? 0.57249 0.49811 0.53160 -0.05753 -0.01985 0.06203  163 ASN A ND2 
2525 N N   . PHE A 178 ? 0.37219 0.31748 0.34031 -0.05343 -0.01761 0.03154  164 PHE A N   
2526 C CA  . PHE A 178 ? 0.39374 0.33800 0.36819 -0.05287 -0.02105 0.02066  164 PHE A CA  
2527 C C   . PHE A 178 ? 0.38012 0.31757 0.35058 -0.04791 -0.02378 0.01818  164 PHE A C   
2528 O O   . PHE A 178 ? 0.42514 0.36008 0.38531 -0.04447 -0.02362 0.02321  164 PHE A O   
2529 C CB  . PHE A 178 ? 0.42092 0.37729 0.39297 -0.05312 -0.01887 0.01509  164 PHE A CB  
2530 C CG  . PHE A 178 ? 0.38153 0.34276 0.34285 -0.04932 -0.01639 0.01822  164 PHE A CG  
2531 C CD1 . PHE A 178 ? 0.37271 0.33955 0.33112 -0.04880 -0.01315 0.02396  164 PHE A CD1 
2532 C CD2 . PHE A 178 ? 0.42830 0.38923 0.38522 -0.04617 -0.01765 0.01491  164 PHE A CD2 
2533 C CE1 . PHE A 178 ? 0.40871 0.37869 0.35958 -0.04406 -0.01235 0.02457  164 PHE A CE1 
2534 C CE2 . PHE A 178 ? 0.39645 0.35947 0.34662 -0.04287 -0.01754 0.01740  164 PHE A CE2 
2535 C CZ  . PHE A 178 ? 0.36272 0.32925 0.30966 -0.04125 -0.01546 0.02133  164 PHE A CZ  
2545 N N   . LYS A 179 ? 0.36356 0.29908 0.34344 -0.04715 -0.02670 0.00922  165 LYS A N   
2546 C CA  . LYS A 179 ? 0.42045 0.35232 0.40225 -0.04266 -0.02939 0.00552  165 LYS A CA  
2547 C C   . LYS A 179 ? 0.32775 0.27186 0.30890 -0.04175 -0.02599 -0.00196 165 LYS A C   
2548 O O   . LYS A 179 ? 0.38284 0.33598 0.36525 -0.04417 -0.02337 -0.00798 165 LYS A O   
2549 C CB  . LYS A 179 ? 0.46423 0.38649 0.46097 -0.04156 -0.03506 0.00075  165 LYS A CB  
2550 C CG  . LYS A 179 ? 0.44331 0.35169 0.44187 -0.04328 -0.04009 0.01127  165 LYS A CG  
2551 C CD  . LYS A 179 ? 0.52637 0.42313 0.54305 -0.04141 -0.04810 0.00641  165 LYS A CD  
2552 C CE  . LYS A 179 ? 0.48822 0.36966 0.50520 -0.04284 -0.05499 0.02030  165 LYS A CE  
2553 N NZ  . LYS A 179 ? 0.60187 0.47095 0.63607 -0.03864 -0.06495 0.01633  165 LYS A NZ  
2567 N N   . ILE A 180 ? 0.40172 0.34654 0.38080 -0.03880 -0.02670 -0.00072 166 ILE A N   
2568 C CA  . ILE A 180 ? 0.43964 0.39649 0.42093 -0.03894 -0.02362 -0.00512 166 ILE A CA  
2569 C C   . ILE A 180 ? 0.43554 0.39241 0.43022 -0.03571 -0.02568 -0.01081 166 ILE A C   
2570 O O   . ILE A 180 ? 0.38914 0.33516 0.38735 -0.03264 -0.03148 -0.00793 166 ILE A O   
2571 C CB  . ILE A 180 ? 0.45921 0.41809 0.43201 -0.03908 -0.02365 0.00168  166 ILE A CB  
2572 C CG1 . ILE A 180 ? 0.42873 0.38866 0.39157 -0.04092 -0.02201 0.00626  166 ILE A CG1 
2573 C CG2 . ILE A 180 ? 0.46949 0.44096 0.44688 -0.04095 -0.02087 0.00020  166 ILE A CG2 
2574 C CD1 . ILE A 180 ? 0.46112 0.43200 0.42337 -0.04481 -0.01857 0.00326  166 ILE A CD1 
2586 N N   . ARG A 181 ? 0.47692 0.44756 0.47901 -0.03611 -0.02102 -0.01899 167 ARG A N   
2587 C CA  . ARG A 181 ? 0.51776 0.49337 0.53653 -0.03249 -0.02124 -0.02656 167 ARG A CA  
2588 C C   . ARG A 181 ? 0.47588 0.46842 0.49714 -0.03454 -0.01577 -0.02503 167 ARG A C   
2589 O O   . ARG A 181 ? 0.50491 0.51438 0.52410 -0.03684 -0.00834 -0.02958 167 ARG A O   
2590 C CB  . ARG A 181 ? 0.52068 0.50011 0.54888 -0.03031 -0.01971 -0.03973 167 ARG A CB  
2591 C CG  . ARG A 181 ? 0.57896 0.54082 0.60787 -0.02998 -0.02623 -0.03940 167 ARG A CG  
2592 C CD  . ARG A 181 ? 0.65346 0.61921 0.68766 -0.02961 -0.02526 -0.05256 167 ARG A CD  
2593 N NE  . ARG A 181 ? 0.65291 0.60325 0.68632 -0.03232 -0.03115 -0.04858 167 ARG A NE  
2594 C CZ  . ARG A 181 ? 0.54877 0.48179 0.59418 -0.03079 -0.03933 -0.04600 167 ARG A CZ  
2595 N NH1 . ARG A 181 ? 0.56745 0.49501 0.62662 -0.02554 -0.04389 -0.04818 167 ARG A NH1 
2596 N NH2 . ARG A 181 ? 0.55798 0.47935 0.60314 -0.03509 -0.04368 -0.03981 167 ARG A NH2 
2610 N N   . HIS A 182 ? 0.44132 0.42957 0.46685 -0.03415 -0.02008 -0.01805 168 HIS A N   
2611 C CA  . HIS A 182 ? 0.42772 0.43049 0.45981 -0.03736 -0.01648 -0.01413 168 HIS A CA  
2612 C C   . HIS A 182 ? 0.44526 0.46283 0.49858 -0.03498 -0.01266 -0.02235 168 HIS A C   
2613 O O   . HIS A 182 ? 0.39717 0.40699 0.46503 -0.03013 -0.01900 -0.02598 168 HIS A O   
2614 C CB  . HIS A 182 ? 0.34325 0.33460 0.37487 -0.03768 -0.02457 -0.00510 168 HIS A CB  
2615 C CG  . HIS A 182 ? 0.37652 0.35585 0.38941 -0.03857 -0.02766 0.00121  168 HIS A CG  
2616 N ND1 . HIS A 182 ? 0.40206 0.38814 0.40541 -0.04296 -0.02369 0.00609  168 HIS A ND1 
2617 C CD2 . HIS A 182 ? 0.41907 0.38181 0.42169 -0.03521 -0.03418 0.00335  168 HIS A CD2 
2618 C CE1 . HIS A 182 ? 0.43149 0.40566 0.42235 -0.04157 -0.02769 0.00968  168 HIS A CE1 
2619 N NE2 . HIS A 182 ? 0.41992 0.38102 0.40917 -0.03694 -0.03308 0.00789  168 HIS A NE2 
2627 N N   . ASN A 183 ? 0.37155 0.41180 0.42681 -0.03812 -0.00237 -0.02510 169 ASN A N   
2628 C CA  . ASN A 183 ? 0.36671 0.42660 0.44346 -0.03571 0.00375  -0.03340 169 ASN A CA  
2629 C C   . ASN A 183 ? 0.41053 0.47113 0.50697 -0.03657 -0.00124 -0.02641 169 ASN A C   
2630 O O   . ASN A 183 ? 0.36807 0.42782 0.46122 -0.04247 -0.00333 -0.01418 169 ASN A O   
2631 C CB  . ASN A 183 ? 0.45061 0.53803 0.52152 -0.04001 0.01708  -0.03519 169 ASN A CB  
2632 C CG  . ASN A 183 ? 0.43536 0.52797 0.49641 -0.03615 0.02194  -0.04986 169 ASN A CG  
2633 O OD1 . ASN A 183 ? 0.45688 0.52976 0.51310 -0.03231 0.01472  -0.05551 169 ASN A OD1 
2634 N ND2 . ASN A 183 ? 0.54545 0.66543 0.60363 -0.03741 0.03395  -0.05605 169 ASN A ND2 
2641 N N   . ILE A 184 ? 0.38741 0.44869 0.50653 -0.03050 -0.00476 -0.03457 170 ILE A N   
2642 C CA  . ILE A 184 ? 0.37719 0.44124 0.51971 -0.03076 -0.01063 -0.02991 170 ILE A CA  
2643 C C   . ILE A 184 ? 0.44545 0.54259 0.60856 -0.03384 0.00203  -0.03176 170 ILE A C   
2644 O O   . ILE A 184 ? 0.42294 0.53883 0.59174 -0.03012 0.01253  -0.04391 170 ILE A O   
2645 C CB  . ILE A 184 ? 0.31461 0.36273 0.47261 -0.02250 -0.02262 -0.03662 170 ILE A CB  
2646 C CG1 . ILE A 184 ? 0.37583 0.39357 0.51092 -0.02103 -0.03424 -0.03126 170 ILE A CG1 
2647 C CG2 . ILE A 184 ? 0.35592 0.41048 0.54215 -0.02238 -0.02920 -0.03367 170 ILE A CG2 
2648 C CD1 . ILE A 184 ? 0.37895 0.37909 0.52378 -0.01362 -0.04662 -0.03543 170 ILE A CD1 
2660 N N   . GLU A 185 ? 0.47624 0.58145 0.65160 -0.04066 0.00094  -0.01995 171 GLU A N   
2661 C CA  . GLU A 185 ? 0.55968 0.69889 0.75192 -0.04662 0.01469  -0.01668 171 GLU A CA  
2662 C C   . GLU A 185 ? 0.59509 0.75767 0.81263 -0.03945 0.02326  -0.03203 171 GLU A C   
2663 O O   . GLU A 185 ? 0.68984 0.87980 0.90490 -0.03975 0.03915  -0.03853 171 GLU A O   
2664 C CB  . GLU A 185 ? 0.57402 0.71480 0.78554 -0.05442 0.00813  -0.00206 171 GLU A CB  
2665 C CG  . GLU A 185 ? 0.71023 0.88697 0.93965 -0.06334 0.02257  0.00628  171 GLU A CG  
2666 C CD  . GLU A 185 ? 0.74876 0.93801 0.95040 -0.07031 0.03500  0.01384  171 GLU A CD  
2667 O OE1 . GLU A 185 ? 0.69603 0.86390 0.87418 -0.07414 0.02752  0.02330  171 GLU A OE1 
2668 O OE2 . GLU A 185 ? 0.73838 0.95975 0.94147 -0.07138 0.05191  0.00968  171 GLU A OE2 
2675 N N   . ASP A 186 ? 0.55977 0.71263 0.80166 -0.03226 0.01241  -0.03876 172 ASP A N   
2676 C CA  . ASP A 186 ? 0.67651 0.85110 0.94888 -0.02413 0.01851  -0.05414 172 ASP A CA  
2677 C C   . ASP A 186 ? 0.63385 0.79231 0.89849 -0.01317 0.01436  -0.07056 172 ASP A C   
2678 O O   . ASP A 186 ? 0.70084 0.85221 0.98937 -0.00427 0.00520  -0.08014 172 ASP A O   
2679 C CB  . ASP A 186 ? 0.86166 1.03750 1.17118 -0.02274 0.00776  -0.05148 172 ASP A CB  
2680 C CG  . ASP A 186 ? 0.99423 1.20513 1.34263 -0.01743 0.01855  -0.06370 172 ASP A CG  
2681 O OD1 . ASP A 186 ? 0.88143 1.11482 1.22574 -0.01363 0.03453  -0.07613 172 ASP A OD1 
2682 O OD2 . ASP A 186 ? 0.98713 1.20428 1.37101 -0.01661 0.01077  -0.06187 172 ASP A OD2 
2687 N N   . GLY A 187 ? 0.47940 0.63120 0.71242 -0.01403 0.01965  -0.07337 173 GLY A N   
2688 C CA  . GLY A 187 ? 0.48683 0.62292 0.71354 -0.00512 0.01525  -0.08820 173 GLY A CA  
2689 C C   . GLY A 187 ? 0.42738 0.52459 0.64057 -0.00393 -0.00230 -0.08125 173 GLY A C   
2690 O O   . GLY A 187 ? 0.49451 0.57764 0.71392 -0.00550 -0.01376 -0.07055 173 GLY A O   
2694 N N   . GLY A 188 ? 0.36625 0.44704 0.56094 -0.00139 -0.00466 -0.08724 174 GLY A N   
2695 C CA  . GLY A 188 ? 0.35121 0.39815 0.53180 -0.00102 -0.01913 -0.07971 174 GLY A CA  
2696 C C   . GLY A 188 ? 0.38450 0.42138 0.53168 -0.00906 -0.01745 -0.06738 174 GLY A C   
2697 O O   . GLY A 188 ? 0.40560 0.45896 0.54055 -0.01524 -0.00716 -0.06303 174 GLY A O   
2701 N N   . VAL A 189 ? 0.39289 0.40287 0.52619 -0.00889 -0.02809 -0.06090 175 VAL A N   
2702 C CA  . VAL A 189 ? 0.40559 0.40483 0.51016 -0.01510 -0.02772 -0.04995 175 VAL A CA  
2703 C C   . VAL A 189 ? 0.40007 0.37703 0.49680 -0.01508 -0.03983 -0.03823 175 VAL A C   
2704 O O   . VAL A 189 ? 0.36608 0.32930 0.47343 -0.01032 -0.05014 -0.03868 175 VAL A O   
2705 C CB  . VAL A 189 ? 0.44303 0.43620 0.53463 -0.01546 -0.02545 -0.05559 175 VAL A CB  
2706 C CG1 . VAL A 189 ? 0.45391 0.47060 0.54516 -0.01611 -0.01333 -0.06701 175 VAL A CG1 
2707 C CG2 . VAL A 189 ? 0.45674 0.43193 0.56118 -0.00982 -0.03538 -0.06119 175 VAL A CG2 
2717 N N   . GLN A 190 ? 0.39250 0.36631 0.47011 -0.02001 -0.03915 -0.02801 176 GLN A N   
2718 C CA  . GLN A 190 ? 0.37419 0.32912 0.43833 -0.01970 -0.04900 -0.01835 176 GLN A CA  
2719 C C   . GLN A 190 ? 0.40430 0.34952 0.44607 -0.02198 -0.04690 -0.01403 176 GLN A C   
2720 O O   . GLN A 190 ? 0.41358 0.36578 0.44308 -0.02604 -0.04008 -0.01176 176 GLN A O   
2721 C CB  . GLN A 190 ? 0.39467 0.35324 0.45698 -0.02239 -0.05088 -0.01215 176 GLN A CB  
2722 C CG  . GLN A 190 ? 0.36595 0.30669 0.41040 -0.02118 -0.06040 -0.00484 176 GLN A CG  
2723 C CD  . GLN A 190 ? 0.42845 0.35491 0.47633 -0.01604 -0.07248 -0.00426 176 GLN A CD  
2724 O OE1 . GLN A 190 ? 0.38977 0.31760 0.45534 -0.01378 -0.08009 -0.00602 176 GLN A OE1 
2725 N NE2 . GLN A 190 ? 0.41266 0.32600 0.44468 -0.01467 -0.07490 -0.00056 176 GLN A NE2 
2734 N N   . LEU A 191 ? 0.39265 0.32254 0.43106 -0.01978 -0.05325 -0.01180 177 LEU A N   
2735 C CA  . LEU A 191 ? 0.36435 0.28678 0.38590 -0.02262 -0.05101 -0.00677 177 LEU A CA  
2736 C C   . LEU A 191 ? 0.38830 0.30562 0.38910 -0.02371 -0.05208 0.00238  177 LEU A C   
2737 O O   . LEU A 191 ? 0.41981 0.33017 0.41676 -0.02092 -0.05946 0.00602  177 LEU A O   
2738 C CB  . LEU A 191 ? 0.44646 0.35443 0.47365 -0.02102 -0.05798 -0.00494 177 LEU A CB  
2739 C CG  . LEU A 191 ? 0.54344 0.44517 0.56009 -0.02516 -0.05565 0.00055  177 LEU A CG  
2740 C CD1 . LEU A 191 ? 0.54517 0.45670 0.56954 -0.02742 -0.04891 -0.00942 177 LEU A CD1 
2741 C CD2 . LEU A 191 ? 0.56294 0.44759 0.58371 -0.02466 -0.06497 0.00803  177 LEU A CD2 
2753 N N   . ALA A 192 ? 0.39993 0.32130 0.38815 -0.02711 -0.04543 0.00480  178 ALA A N   
2754 C CA  . ALA A 192 ? 0.39753 0.31606 0.36753 -0.02706 -0.04518 0.01137  178 ALA A CA  
2755 C C   . ALA A 192 ? 0.44029 0.35774 0.40168 -0.02991 -0.04071 0.01587  178 ALA A C   
2756 O O   . ALA A 192 ? 0.40112 0.32698 0.36415 -0.03321 -0.03472 0.01354  178 ALA A O   
2757 C CB  . ALA A 192 ? 0.42731 0.35519 0.39572 -0.02810 -0.04194 0.00980  178 ALA A CB  
2763 N N   . ASP A 193 ? 0.46570 0.37381 0.41838 -0.02914 -0.04403 0.02323  179 ASP A N   
2764 C CA  . ASP A 193 ? 0.43951 0.34784 0.38677 -0.03290 -0.03963 0.02988  179 ASP A CA  
2765 C C   . ASP A 193 ? 0.41858 0.33442 0.35068 -0.03212 -0.03396 0.03274  179 ASP A C   
2766 O O   . ASP A 193 ? 0.36888 0.28209 0.28664 -0.02802 -0.03613 0.03535  179 ASP A O   
2767 C CB  . ASP A 193 ? 0.47142 0.36806 0.41616 -0.03336 -0.04525 0.03914  179 ASP A CB  
2768 C CG  . ASP A 193 ? 0.45316 0.34094 0.41693 -0.03321 -0.05243 0.03567  179 ASP A CG  
2769 O OD1 . ASP A 193 ? 0.53544 0.42730 0.51450 -0.03496 -0.05017 0.02728  179 ASP A OD1 
2770 O OD2 . ASP A 193 ? 0.64582 0.52279 0.60935 -0.03069 -0.06110 0.04057  179 ASP A OD2 
2775 N N   . HIS A 194 ? 0.37580 0.30127 0.31162 -0.03530 -0.02760 0.03111  180 HIS A N   
2776 C CA  . HIS A 194 ? 0.40436 0.33854 0.33085 -0.03385 -0.02239 0.03236  180 HIS A CA  
2777 C C   . HIS A 194 ? 0.40348 0.34202 0.32680 -0.03694 -0.01695 0.04064  180 HIS A C   
2778 O O   . HIS A 194 ? 0.39697 0.33640 0.33180 -0.04275 -0.01569 0.04322  180 HIS A O   
2779 C CB  . HIS A 194 ? 0.35696 0.30027 0.29102 -0.03543 -0.01991 0.02681  180 HIS A CB  
2780 C CG  . HIS A 194 ? 0.39897 0.34157 0.33495 -0.03311 -0.02365 0.02153  180 HIS A CG  
2781 N ND1 . HIS A 194 ? 0.37897 0.31719 0.32197 -0.03330 -0.02739 0.01835  180 HIS A ND1 
2782 C CD2 . HIS A 194 ? 0.39294 0.33936 0.32764 -0.03107 -0.02452 0.01972  180 HIS A CD2 
2783 C CE1 . HIS A 194 ? 0.39622 0.33713 0.34187 -0.03232 -0.02936 0.01581  180 HIS A CE1 
2784 N NE2 . HIS A 194 ? 0.40952 0.35403 0.35008 -0.03126 -0.02839 0.01712  180 HIS A NE2 
2792 N N   . TYR A 195 ? 0.36451 0.30688 0.27320 -0.03309 -0.01379 0.04430  181 TYR A N   
2793 C CA  . TYR A 195 ? 0.38897 0.34155 0.29462 -0.03565 -0.00585 0.05231  181 TYR A CA  
2794 C C   . TYR A 195 ? 0.42564 0.39102 0.32722 -0.03041 -0.00038 0.04692  181 TYR A C   
2795 O O   . TYR A 195 ? 0.46893 0.43227 0.35878 -0.02296 -0.00295 0.04084  181 TYR A O   
2796 C CB  . TYR A 195 ? 0.41947 0.36816 0.30968 -0.03532 -0.00574 0.06237  181 TYR A CB  
2797 C CG  . TYR A 195 ? 0.41718 0.35167 0.31392 -0.04010 -0.01298 0.06905  181 TYR A CG  
2798 C CD1 . TYR A 195 ? 0.46457 0.38578 0.35942 -0.03636 -0.02266 0.06452  181 TYR A CD1 
2799 C CD2 . TYR A 195 ? 0.46566 0.39985 0.37380 -0.04830 -0.01124 0.07981  181 TYR A CD2 
2800 C CE1 . TYR A 195 ? 0.48901 0.39724 0.39298 -0.03949 -0.03032 0.06959  181 TYR A CE1 
2801 C CE2 . TYR A 195 ? 0.48297 0.40211 0.40006 -0.05200 -0.01973 0.08539  181 TYR A CE2 
2802 C CZ  . TYR A 195 ? 0.52662 0.43292 0.44150 -0.04698 -0.02923 0.07977  181 TYR A CZ  
2803 O OH  . TYR A 195 ? 0.57685 0.46822 0.50367 -0.04944 -0.03867 0.08429  181 TYR A OH  
2813 N N   . GLN A 196 ? 0.41849 0.39651 0.33201 -0.03393 0.00574  0.04841  182 GLN A N   
2814 C CA  . GLN A 196 ? 0.41343 0.40328 0.32993 -0.02887 0.00906  0.04203  182 GLN A CA  
2815 C C   . GLN A 196 ? 0.42114 0.42898 0.34103 -0.02968 0.01934  0.04752  182 GLN A C   
2816 O O   . GLN A 196 ? 0.41221 0.42428 0.33891 -0.03735 0.02350  0.05737  182 GLN A O   
2817 C CB  . GLN A 196 ? 0.37568 0.36557 0.30746 -0.03179 0.00472  0.03701  182 GLN A CB  
2818 C CG  . GLN A 196 ? 0.42186 0.42159 0.35947 -0.02669 0.00523  0.03147  182 GLN A CG  
2819 C CD  . GLN A 196 ? 0.41289 0.41174 0.36188 -0.03018 -0.00060 0.02867  182 GLN A CD  
2820 O OE1 . GLN A 196 ? 0.33928 0.33002 0.28858 -0.03476 -0.00471 0.02838  182 GLN A OE1 
2821 N NE2 . GLN A 196 ? 0.41447 0.42283 0.37269 -0.02757 -0.00114 0.02645  182 GLN A NE2 
2830 N N   . GLN A 197 ? 0.45858 0.47758 0.37627 -0.02162 0.02307  0.04090  183 GLN A N   
2831 C CA  . GLN A 197 ? 0.51868 0.55929 0.44283 -0.02061 0.03401  0.04369  183 GLN A CA  
2832 C C   . GLN A 197 ? 0.47566 0.52474 0.40916 -0.01212 0.03302  0.03264  183 GLN A C   
2833 O O   . GLN A 197 ? 0.47360 0.51451 0.39739 -0.00329 0.02746  0.02310  183 GLN A O   
2834 C CB  . GLN A 197 ? 0.54675 0.59518 0.45061 -0.01698 0.04241  0.04820  183 GLN A CB  
2835 C CG  . GLN A 197 ? 0.65890 0.73322 0.56592 -0.01134 0.05494  0.04615  183 GLN A CG  
2836 C CD  . GLN A 197 ? 0.75951 0.85214 0.68154 -0.02136 0.06563  0.06012  183 GLN A CD  
2837 O OE1 . GLN A 197 ? 0.85895 0.95361 0.77020 -0.02753 0.07102  0.07325  183 GLN A OE1 
2838 N NE2 . GLN A 197 ? 0.70397 0.80996 0.65246 -0.02356 0.06766  0.05845  183 GLN A NE2 
2841 N N   . ASN A 198 ? 0.38621 0.45065 0.34082 -0.01483 0.03673  0.03399  184 ASN A N   
2842 C CA  . ASN A 198 ? 0.39627 0.47018 0.36391 -0.00664 0.03511  0.02465  184 ASN A CA  
2843 C C   . ASN A 198 ? 0.42362 0.52439 0.40270 -0.00358 0.04778  0.02547  184 ASN A C   
2844 O O   . ASN A 198 ? 0.38013 0.49352 0.37036 -0.01253 0.05502  0.03569  184 ASN A O   
2845 C CB  . ASN A 198 ? 0.41131 0.48019 0.39681 -0.01173 0.02549  0.02455  184 ASN A CB  
2846 C CG  . ASN A 198 ? 0.39988 0.44661 0.37527 -0.01431 0.01462  0.02337  184 ASN A CG  
2847 O OD1 . ASN A 198 ? 0.41963 0.45495 0.38207 -0.01846 0.01439  0.02689  184 ASN A OD1 
2848 N ND2 . ASN A 198 ? 0.39818 0.43987 0.38090 -0.01194 0.00544  0.01921  184 ASN A ND2 
2855 N N   . THR A 199 ? 0.39848 0.50867 0.37710 0.00922  0.05016  0.01418  185 THR A N   
2856 C CA  . THR A 199 ? 0.38143 0.52054 0.37196 0.01486  0.06324  0.01184  185 THR A CA  
2857 C C   . THR A 199 ? 0.37779 0.52251 0.38748 0.02635  0.05742  -0.00149 185 THR A C   
2858 O O   . THR A 199 ? 0.37908 0.50584 0.38144 0.03433  0.04625  -0.01147 185 THR A O   
2859 C CB  . THR A 199 ? 0.43120 0.58034 0.39690 0.02164  0.07491  0.00960  185 THR A CB  
2860 O OG1 . THR A 199 ? 0.56035 0.69058 0.50560 0.03191  0.06571  -0.00282 185 THR A OG1 
2861 C CG2 . THR A 199 ? 0.51182 0.65903 0.46248 0.00951  0.08119  0.02606  185 THR A CG2 
2869 N N   . PRO A 200 ? 0.38049 0.54952 0.41725 0.02737  0.06364  -0.00154 186 PRO A N   
2870 C CA  . PRO A 200 ? 0.38843 0.56162 0.44763 0.03831  0.05572  -0.01344 186 PRO A CA  
2871 C C   . PRO A 200 ? 0.38998 0.56915 0.44142 0.05570  0.05915  -0.03023 186 PRO A C   
2872 O O   . PRO A 200 ? 0.41292 0.60746 0.44800 0.06022  0.07335  -0.03297 186 PRO A O   
2873 C CB  . PRO A 200 ? 0.39477 0.59588 0.48622 0.03415  0.06296  -0.00814 186 PRO A CB  
2874 C CG  . PRO A 200 ? 0.37420 0.59354 0.45752 0.02626  0.08033  0.00242  186 PRO A CG  
2875 C CD  . PRO A 200 ? 0.43308 0.62702 0.48480 0.01810  0.07699  0.01012  186 PRO A CD  
2883 N N   . ILE A 201 ? 0.43613 0.61136 0.45064 -0.08052 0.09779  -0.07458 187 ILE A N   
2884 C CA  . ILE A 201 ? 0.46367 0.64273 0.47836 -0.08557 0.11598  -0.09564 187 ILE A CA  
2885 C C   . ILE A 201 ? 0.45557 0.66254 0.50071 -0.08592 0.13553  -0.11770 187 ILE A C   
2886 O O   . ILE A 201 ? 0.56736 0.78683 0.60401 -0.10300 0.15499  -0.13670 187 ILE A O   
2887 C CB  . ILE A 201 ? 0.47813 0.63664 0.50415 -0.06537 0.11164  -0.09735 187 ILE A CB  
2888 C CG1 . ILE A 201 ? 0.44113 0.57563 0.43771 -0.06765 0.09447  -0.07760 187 ILE A CG1 
2889 C CG2 . ILE A 201 ? 0.47608 0.63703 0.50613 -0.06944 0.13132  -0.12145 187 ILE A CG2 
2890 C CD1 . ILE A 201 ? 0.49405 0.60810 0.49921 -0.04960 0.08875  -0.07687 187 ILE A CD1 
2902 N N   . GLY A 202 ? 0.49570 0.71411 0.57761 -0.06823 0.13103  -0.11639 188 GLY A N   
2903 C CA  . GLY A 202 ? 0.53409 0.78144 0.65333 -0.06587 0.14783  -0.13677 188 GLY A CA  
2904 C C   . GLY A 202 ? 0.55119 0.82273 0.66148 -0.08690 0.15357  -0.13605 188 GLY A C   
2905 O O   . GLY A 202 ? 0.51943 0.78310 0.59372 -0.10355 0.14324  -0.11853 188 GLY A O   
2909 N N   . ASP A 203 ? 0.64423 0.94596 0.79084 -0.08615 0.17018  -0.15583 189 ASP A N   
2910 C CA  . ASP A 203 ? 0.67305 1.00235 0.81663 -0.10683 0.17872  -0.15867 189 ASP A CA  
2911 C C   . ASP A 203 ? 0.66721 1.01070 0.84534 -0.09255 0.16698  -0.14938 189 ASP A C   
2912 O O   . ASP A 203 ? 0.69970 1.06939 0.88368 -0.10746 0.17447  -0.15330 189 ASP A O   
2913 C CB  . ASP A 203 ? 0.65586 1.01430 0.81505 -0.12097 0.20872  -0.19005 189 ASP A CB  
2914 C CG  . ASP A 203 ? 0.72626 1.06725 0.84802 -0.13659 0.21890  -0.19988 189 ASP A CG  
2915 O OD1 . ASP A 203 ? 0.78546 1.10588 0.86068 -0.15015 0.20835  -0.18246 189 ASP A OD1 
2916 O OD2 . ASP A 203 ? 0.69577 1.03915 0.83421 -0.13481 0.23345  -0.22290 189 ASP A OD2 
2921 N N   . GLY A 204 ? 0.62892 0.95607 0.82802 -0.06629 0.14862  -0.13701 190 GLY A N   
2922 C CA  . GLY A 204 ? 0.62491 0.96395 0.85467 -0.05366 0.13573  -0.12747 190 GLY A CA  
2923 C C   . GLY A 204 ? 0.64321 0.97345 0.84013 -0.06654 0.12026  -0.10508 190 GLY A C   
2924 O O   . GLY A 204 ? 0.67790 0.98587 0.83110 -0.07914 0.11412  -0.09275 190 GLY A O   
2928 N N   . PRO A 205 ? 0.67723 1.02453 0.89681 -0.06371 0.11288  -0.09946 191 PRO A N   
2929 C CA  . PRO A 205 ? 0.67007 1.00757 0.86090 -0.07577 0.09822  -0.07936 191 PRO A CA  
2930 C C   . PRO A 205 ? 0.61723 0.92054 0.79056 -0.06194 0.07727  -0.06018 191 PRO A C   
2931 O O   . PRO A 205 ? 0.55396 0.85070 0.75068 -0.04062 0.06829  -0.05823 191 PRO A O   
2932 C CB  . PRO A 205 ? 0.56376 0.93040 0.78984 -0.07423 0.09688  -0.08147 191 PRO A CB  
2933 C CG  . PRO A 205 ? 0.60988 0.99084 0.88645 -0.05125 0.10017  -0.09452 191 PRO A CG  
2934 C CD  . PRO A 205 ? 0.69334 1.06980 0.96809 -0.04982 0.11683  -0.11134 191 PRO A CD  
2942 N N   . VAL A 206 ? 0.53085 0.81264 0.66385 -0.07524 0.06934  -0.04612 192 VAL A N   
2943 C CA  . VAL A 206 ? 0.40797 0.65890 0.52398 -0.06485 0.05165  -0.02977 192 VAL A CA  
2944 C C   . VAL A 206 ? 0.41535 0.66127 0.52084 -0.07264 0.03873  -0.01543 192 VAL A C   
2945 O O   . VAL A 206 ? 0.34055 0.60423 0.44687 -0.08791 0.04279  -0.01650 192 VAL A O   
2946 C CB  . VAL A 206 ? 0.43876 0.66625 0.52207 -0.07100 0.05150  -0.02565 192 VAL A CB  
2947 C CG1 . VAL A 206 ? 0.43834 0.66833 0.53143 -0.06320 0.06404  -0.04063 192 VAL A CG1 
2948 C CG2 . VAL A 206 ? 0.43833 0.66668 0.49104 -0.09731 0.05446  -0.02103 192 VAL A CG2 
2958 N N   . LEU A 207 ? 0.37000 0.59126 0.46562 -0.06297 0.02387  -0.00302 193 LEU A N   
2959 C CA  . LEU A 207 ? 0.33572 0.54699 0.42090 -0.06910 0.01149  0.00931  193 LEU A CA  
2960 C C   . LEU A 207 ? 0.33798 0.52695 0.39178 -0.08210 0.00640  0.01941  193 LEU A C   
2961 O O   . LEU A 207 ? 0.35913 0.52767 0.40169 -0.07508 0.00211  0.02328  193 LEU A O   
2962 C CB  . LEU A 207 ? 0.34543 0.54377 0.43952 -0.05251 -0.00072 0.01492  193 LEU A CB  
2963 C CG  . LEU A 207 ? 0.31981 0.53683 0.44490 -0.04016 -0.00183 0.00966  193 LEU A CG  
2964 C CD1 . LEU A 207 ? 0.34497 0.54474 0.46867 -0.02883 -0.01540 0.01752  193 LEU A CD1 
2965 C CD2 . LEU A 207 ? 0.34666 0.58983 0.48725 -0.05070 0.00058  0.00702  193 LEU A CD2 
2977 N N   . LEU A 208 ? 0.36803 0.56095 0.40926 -0.10156 0.00575  0.02441  194 LEU A N   
2978 C CA  . LEU A 208 ? 0.35467 0.52435 0.36943 -0.11441 -0.00345 0.03712  194 LEU A CA  
2979 C C   . LEU A 208 ? 0.36796 0.51946 0.38360 -0.11046 -0.01749 0.04692  194 LEU A C   
2980 O O   . LEU A 208 ? 0.42909 0.59045 0.45152 -0.11685 -0.01895 0.04736  194 LEU A O   
2981 C CB  . LEU A 208 ? 0.35164 0.53193 0.34924 -0.14033 0.00189  0.03883  194 LEU A CB  
2982 C CG  . LEU A 208 ? 0.38353 0.57908 0.37311 -0.14982 0.01695  0.02835  194 LEU A CG  
2983 C CD1 . LEU A 208 ? 0.56111 0.76309 0.52595 -0.18023 0.02013  0.03272  194 LEU A CD1 
2984 C CD2 . LEU A 208 ? 0.47173 0.64869 0.45081 -0.14084 0.01440  0.02988  194 LEU A CD2 
2996 N N   . PRO A 209 ? 0.35774 0.48390 0.36800 -0.10098 -0.02709 0.05345  195 PRO A N   
2997 C CA  . PRO A 209 ? 0.36157 0.47185 0.37676 -0.09482 -0.03739 0.05806  195 PRO A CA  
2998 C C   . PRO A 209 ? 0.36845 0.46038 0.37216 -0.10914 -0.04771 0.06903  195 PRO A C   
2999 O O   . PRO A 209 ? 0.38392 0.46631 0.37361 -0.12084 -0.05157 0.07703  195 PRO A O   
3000 C CB  . PRO A 209 ? 0.34882 0.44278 0.36636 -0.07799 -0.04021 0.05716  195 PRO A CB  
3001 C CG  . PRO A 209 ? 0.38863 0.47822 0.39442 -0.08272 -0.03840 0.05995  195 PRO A CG  
3002 C CD  . PRO A 209 ? 0.40780 0.52026 0.40951 -0.09510 -0.02782 0.05499  195 PRO A CD  
3010 N N   . ASP A 210 ? 0.32268 0.40839 0.33241 -0.10897 -0.05338 0.06982  196 ASP A N   
3011 C CA  . ASP A 210 ? 0.39387 0.45424 0.39798 -0.11668 -0.06501 0.07900  196 ASP A CA  
3012 C C   . ASP A 210 ? 0.37932 0.41662 0.38676 -0.10394 -0.07097 0.08088  196 ASP A C   
3013 O O   . ASP A 210 ? 0.34453 0.38572 0.35708 -0.08955 -0.06582 0.07458  196 ASP A O   
3014 C CB  . ASP A 210 ? 0.38311 0.44122 0.39361 -0.11862 -0.06831 0.07661  196 ASP A CB  
3015 C CG  . ASP A 210 ? 0.39937 0.48228 0.40972 -0.13196 -0.06319 0.07494  196 ASP A CG  
3016 O OD1 . ASP A 210 ? 0.43793 0.53964 0.44366 -0.14050 -0.05596 0.07473  196 ASP A OD1 
3017 O OD2 . ASP A 210 ? 0.45813 0.54283 0.47348 -0.13495 -0.06574 0.07279  196 ASP A OD2 
3022 N N   . ASN A 211 ? 0.37076 0.38380 0.37750 -0.10963 -0.08238 0.08967  197 ASN A N   
3023 C CA  . ASN A 211 ? 0.37948 0.37228 0.39483 -0.09819 -0.08857 0.09127  197 ASN A CA  
3024 C C   . ASN A 211 ? 0.36594 0.35708 0.39374 -0.08143 -0.08321 0.07907  197 ASN A C   
3025 O O   . ASN A 211 ? 0.36059 0.35283 0.39124 -0.08169 -0.08132 0.07294  197 ASN A O   
3026 C CB  . ASN A 211 ? 0.38503 0.35145 0.40422 -0.10641 -0.10317 0.10226  197 ASN A CB  
3027 C CG  . ASN A 211 ? 0.40902 0.37495 0.41153 -0.12702 -0.11057 0.11665  197 ASN A CG  
3028 O OD1 . ASN A 211 ? 0.45624 0.43687 0.44524 -0.13313 -0.10599 0.11905  197 ASN A OD1 
3029 N ND2 . ASN A 211 ? 0.39705 0.34513 0.39887 -0.13960 -0.12189 0.12591  197 ASN A ND2 
3036 N N   . HIS A 212 ? 0.35252 0.34142 0.38571 -0.06899 -0.08085 0.07568  198 HIS A N   
3037 C CA  . HIS A 212 ? 0.38758 0.37466 0.42959 -0.05534 -0.07527 0.06441  198 HIS A CA  
3038 C C   . HIS A 212 ? 0.34828 0.32953 0.39668 -0.04568 -0.07546 0.06431  198 HIS A C   
3039 O O   . HIS A 212 ? 0.35118 0.32822 0.39830 -0.04976 -0.08170 0.07359  198 HIS A O   
3040 C CB  . HIS A 212 ? 0.33239 0.33964 0.36871 -0.05212 -0.06646 0.05719  198 HIS A CB  
3041 C CG  . HIS A 212 ? 0.37511 0.39819 0.40641 -0.04832 -0.06069 0.05752  198 HIS A CG  
3042 N ND1 . HIS A 212 ? 0.38648 0.42263 0.41089 -0.05737 -0.05895 0.06211  198 HIS A ND1 
3043 C CD2 . HIS A 212 ? 0.35036 0.37763 0.38244 -0.03755 -0.05552 0.05269  198 HIS A CD2 
3044 C CE1 . HIS A 212 ? 0.40533 0.45257 0.42812 -0.05133 -0.05239 0.05882  198 HIS A CE1 
3045 N NE2 . HIS A 212 ? 0.34489 0.38605 0.37224 -0.03903 -0.05108 0.05400  198 HIS A NE2 
3053 N N   . TYR A 213 ? 0.34301 0.32447 0.39702 -0.03481 -0.06915 0.05429  199 TYR A N   
3054 C CA  . TYR A 213 ? 0.35871 0.33662 0.41993 -0.02624 -0.06830 0.05300  199 TYR A CA  
3055 C C   . TYR A 213 ? 0.39339 0.38005 0.45054 -0.01809 -0.05869 0.04321  199 TYR A C   
3056 O O   . TYR A 213 ? 0.30789 0.29926 0.35964 -0.01866 -0.05449 0.03710  199 TYR A O   
3057 C CB  . TYR A 213 ? 0.32404 0.28391 0.40559 -0.02294 -0.07431 0.05178  199 TYR A CB  
3058 C CG  . TYR A 213 ? 0.37645 0.32942 0.46696 -0.01941 -0.06861 0.03843  199 TYR A CG  
3059 C CD1 . TYR A 213 ? 0.39313 0.34984 0.48627 -0.01213 -0.05919 0.02661  199 TYR A CD1 
3060 C CD2 . TYR A 213 ? 0.38971 0.33196 0.48403 -0.02552 -0.07213 0.03702  199 TYR A CD2 
3061 C CE1 . TYR A 213 ? 0.39570 0.34681 0.49350 -0.01205 -0.05252 0.01293  199 TYR A CE1 
3062 C CE2 . TYR A 213 ? 0.44112 0.37663 0.54153 -0.02430 -0.06572 0.02289  199 TYR A CE2 
3063 C CZ  . TYR A 213 ? 0.44389 0.38441 0.54535 -0.01805 -0.05547 0.01045  199 TYR A CZ  
3064 O OH  . TYR A 213 ? 0.45092 0.38544 0.55506 -0.01983 -0.04768 -0.00505 199 TYR A OH  
3074 N N   . LEU A 214 ? 0.36015 0.34834 0.41894 -0.01207 -0.05656 0.04291  200 LEU A N   
3075 C CA  . LEU A 214 ? 0.39535 0.38861 0.45012 -0.00552 -0.04873 0.03502  200 LEU A CA  
3076 C C   . LEU A 214 ? 0.35441 0.33885 0.42345 -0.00077 -0.04668 0.02772  200 LEU A C   
3077 O O   . LEU A 214 ? 0.33660 0.31570 0.41919 0.00110  -0.05150 0.03141  200 LEU A O   
3078 C CB  . LEU A 214 ? 0.38740 0.38936 0.43330 -0.00319 -0.04647 0.03864  200 LEU A CB  
3079 C CG  . LEU A 214 ? 0.38862 0.40136 0.42488 -0.00774 -0.04645 0.04364  200 LEU A CG  
3080 C CD1 . LEU A 214 ? 0.38488 0.40363 0.41474 -0.00477 -0.04249 0.04383  200 LEU A CD1 
3081 C CD2 . LEU A 214 ? 0.33958 0.36019 0.37271 -0.00864 -0.04436 0.04047  200 LEU A CD2 
3093 N N   . SER A 215 ? 0.36255 0.34657 0.42927 -0.00007 -0.03973 0.01718  201 SER A N   
3094 C CA  . SER A 215 ? 0.37057 0.34985 0.45022 0.00313  -0.03400 0.00666  201 SER A CA  
3095 C C   . SER A 215 ? 0.36286 0.34907 0.43363 0.00584  -0.02852 0.00526  201 SER A C   
3096 O O   . SER A 215 ? 0.36984 0.36134 0.42197 0.00392  -0.02598 0.00596  201 SER A O   
3097 C CB  . SER A 215 ? 0.32824 0.30318 0.40667 -0.00122 -0.02777 -0.00583 201 SER A CB  
3098 O OG  . SER A 215 ? 0.45186 0.42521 0.54123 0.00022  -0.01894 -0.01895 201 SER A OG  
3104 N N   . THR A 216 ? 0.43081 0.41659 0.51641 0.00988  -0.02800 0.00410  202 THR A N   
3105 C CA  . THR A 216 ? 0.42595 0.41746 0.50373 0.01147  -0.02387 0.00413  202 THR A CA  
3106 C C   . THR A 216 ? 0.41770 0.41007 0.51055 0.01233  -0.01600 -0.00776 202 THR A C   
3107 O O   . THR A 216 ? 0.46772 0.45758 0.58722 0.01549  -0.01760 -0.01163 202 THR A O   
3108 C CB  . THR A 216 ? 0.45365 0.44714 0.53261 0.01347  -0.03100 0.01537  202 THR A CB  
3109 O OG1 . THR A 216 ? 0.50881 0.50351 0.57488 0.01106  -0.03601 0.02404  202 THR A OG1 
3110 C CG2 . THR A 216 ? 0.45631 0.45416 0.52548 0.01424  -0.02658 0.01489  202 THR A CG2 
3118 N N   . CYS A 217 ? 0.39302 0.38917 0.47038 0.00888  -0.00791 -0.01342 203 CYS A N   
3119 C CA  . CYS A 217 ? 0.45085 0.45106 0.53891 0.00739  0.00148  -0.02493 203 CYS A CA  
3120 C C   . CYS A 217 ? 0.44084 0.44469 0.51126 0.00530  0.00319  -0.02037 203 CYS A C   
3121 O O   . CYS A 217 ? 0.37825 0.38006 0.42300 0.00141  0.00271  -0.01590 203 CYS A O   
3122 C CB  . CYS A 217 ? 0.49008 0.48978 0.57347 0.00011  0.01238  -0.04017 203 CYS A CB  
3123 S SG  . CYS A 217 ? 0.54550 0.53973 0.65855 0.00240  0.01439  -0.05217 203 CYS A SG  
3128 N N   . SER A 218 ? 0.44650 0.45515 0.53235 0.00764  0.00402  -0.02101 204 SER A N   
3129 C CA  . SER A 218 ? 0.39756 0.40822 0.46837 0.00526  0.00487  -0.01635 204 SER A CA  
3130 C C   . SER A 218 ? 0.47656 0.49431 0.55492 -0.00008 0.01572  -0.02813 204 SER A C   
3131 O O   . SER A 218 ? 0.45009 0.47362 0.55421 0.00062  0.02186  -0.03991 204 SER A O   
3132 C CB  . SER A 218 ? 0.47179 0.48287 0.54985 0.01009  -0.00456 -0.00518 204 SER A CB  
3133 O OG  . SER A 218 ? 0.59907 0.61529 0.70826 0.01342  -0.00716 -0.00748 204 SER A OG  
3139 N N   . LYS A 219 ? 0.35354 0.37075 0.41060 -0.00595 0.01839  -0.02552 205 LYS A N   
3140 C CA  . LYS A 219 ? 0.34205 0.36683 0.40185 -0.01366 0.02884  -0.03532 205 LYS A CA  
3141 C C   . LYS A 219 ? 0.33617 0.36050 0.38864 -0.01424 0.02470  -0.02662 205 LYS A C   
3142 O O   . LYS A 219 ? 0.33302 0.34764 0.36029 -0.01525 0.01926  -0.01666 205 LYS A O   
3143 C CB  . LYS A 219 ? 0.38255 0.40484 0.41556 -0.02619 0.03776  -0.04222 205 LYS A CB  
3144 C CG  . LYS A 219 ? 0.38602 0.41807 0.42112 -0.03755 0.05135  -0.05518 205 LYS A CG  
3145 C CD  . LYS A 219 ? 0.59766 0.62283 0.59326 -0.05253 0.05393  -0.05190 205 LYS A CD  
3146 C CE  . LYS A 219 ? 0.72050 0.75430 0.70991 -0.06893 0.07028  -0.06917 205 LYS A CE  
3147 N NZ  . LYS A 219 ? 0.84813 0.87337 0.79481 -0.08666 0.07042  -0.06336 205 LYS A NZ  
3161 N N   . LEU A 220 ? 0.31573 0.35052 0.39243 -0.01361 0.02692  -0.03086 206 LEU A N   
3162 C CA  . LEU A 220 ? 0.32706 0.36258 0.39817 -0.01610 0.02371  -0.02420 206 LEU A CA  
3163 C C   . LEU A 220 ? 0.34186 0.38460 0.40753 -0.02778 0.03542  -0.03352 206 LEU A C   
3164 O O   . LEU A 220 ? 0.30199 0.35688 0.38701 -0.03137 0.04618  -0.04761 206 LEU A O   
3165 C CB  . LEU A 220 ? 0.32466 0.36786 0.42588 -0.00924 0.01536  -0.02001 206 LEU A CB  
3166 C CG  . LEU A 220 ? 0.32931 0.36390 0.42500 -0.00270 0.00215  -0.00673 206 LEU A CG  
3167 C CD1 . LEU A 220 ? 0.33883 0.36680 0.43094 0.00214  0.00042  -0.00623 206 LEU A CD1 
3168 C CD2 . LEU A 220 ? 0.30835 0.35073 0.43248 0.00059  -0.00765 -0.00157 206 LEU A CD2 
3180 N N   . SER A 221 ? 0.29047 0.32545 0.33029 -0.03462 0.03395  -0.02655 207 SER A N   
3181 C CA  . SER A 221 ? 0.32931 0.36924 0.35862 -0.04846 0.04400  -0.03319 207 SER A CA  
3182 C C   . SER A 221 ? 0.35919 0.39218 0.37492 -0.05184 0.03818  -0.02362 207 SER A C   
3183 O O   . SER A 221 ? 0.34049 0.36613 0.35631 -0.04361 0.02777  -0.01391 207 SER A O   
3184 C CB  . SER A 221 ? 0.33032 0.36187 0.32865 -0.05960 0.04999  -0.03573 207 SER A CB  
3185 O OG  . SER A 221 ? 0.39204 0.40486 0.36360 -0.05652 0.03923  -0.02225 207 SER A OG  
3191 N N   . LYS A 222 ? 0.35499 0.39007 0.35752 -0.06590 0.04575  -0.02730 208 LYS A N   
3192 C CA  . LYS A 222 ? 0.42747 0.45539 0.41678 -0.07169 0.04157  -0.01986 208 LYS A CA  
3193 C C   . LYS A 222 ? 0.44504 0.45596 0.39613 -0.08508 0.04272  -0.01497 208 LYS A C   
3194 O O   . LYS A 222 ? 0.39982 0.41175 0.33725 -0.09523 0.05005  -0.02022 208 LYS A O   
3195 C CB  . LYS A 222 ? 0.41497 0.46326 0.42963 -0.07778 0.04787  -0.02775 208 LYS A CB  
3196 C CG  . LYS A 222 ? 0.39577 0.45991 0.45122 -0.06535 0.04284  -0.02964 208 LYS A CG  
3197 C CD  . LYS A 222 ? 0.35937 0.41193 0.40967 -0.05712 0.02846  -0.01651 208 LYS A CD  
3198 C CE  . LYS A 222 ? 0.32176 0.39033 0.40968 -0.04990 0.02110  -0.01579 208 LYS A CE  
3199 N NZ  . LYS A 222 ? 0.34810 0.40613 0.42622 -0.04615 0.00781  -0.00353 208 LYS A NZ  
3213 N N   . ASP A 223 ? 0.42829 0.42222 0.36171 -0.08604 0.03463  -0.00463 209 ASP A N   
3214 C CA  . ASP A 223 ? 0.44426 0.41883 0.34393 -0.09900 0.03272  0.00236  209 ASP A CA  
3215 C C   . ASP A 223 ? 0.52321 0.50430 0.41975 -0.11470 0.03930  -0.00116 209 ASP A C   
3216 O O   . ASP A 223 ? 0.44573 0.42986 0.35436 -0.11187 0.03661  -0.00022 209 ASP A O   
3217 C CB  . ASP A 223 ? 0.54555 0.49597 0.43172 -0.09017 0.02024  0.01429  209 ASP A CB  
3218 C CG  . ASP A 223 ? 0.51636 0.44295 0.37128 -0.10214 0.01512  0.02345  209 ASP A CG  
3219 O OD1 . ASP A 223 ? 0.58533 0.51377 0.42430 -0.11981 0.02090  0.02187  209 ASP A OD1 
3220 O OD2 . ASP A 223 ? 0.46616 0.37175 0.31336 -0.09451 0.00511  0.03205  209 ASP A OD2 
3225 N N   . PRO A 224 ? 0.52422 0.50855 0.40383 -0.13325 0.04801  -0.00540 210 PRO A N   
3226 C CA  . PRO A 224 ? 0.51407 0.50783 0.39249 -0.14991 0.05569  -0.00989 210 PRO A CA  
3227 C C   . PRO A 224 ? 0.53364 0.50467 0.39180 -0.15480 0.04625  0.00179  210 PRO A C   
3228 O O   . PRO A 224 ? 0.54027 0.52000 0.40388 -0.16466 0.05033  -0.00124 210 PRO A O   
3229 C CB  . PRO A 224 ? 0.52932 0.52770 0.38611 -0.17112 0.06674  -0.01594 210 PRO A CB  
3230 C CG  . PRO A 224 ? 0.62655 0.60566 0.46001 -0.16790 0.05863  -0.00748 210 PRO A CG  
3231 C CD  . PRO A 224 ? 0.52902 0.50951 0.38783 -0.14255 0.05148  -0.00649 210 PRO A CD  
3239 N N   . ASN A 225 ? 0.61354 0.55609 0.45115 -0.14829 0.03387  0.01420  211 ASN A N   
3240 C CA  . ASN A 225 ? 0.63625 0.55325 0.45590 -0.15215 0.02483  0.02420  211 ASN A CA  
3241 C C   . ASN A 225 ? 0.58142 0.49363 0.41771 -0.13492 0.01811  0.02540  211 ASN A C   
3242 O O   . ASN A 225 ? 0.59020 0.48180 0.41481 -0.13740 0.01203  0.03092  211 ASN A O   
3243 C CB  . ASN A 225 ? 0.63379 0.52052 0.42349 -0.15653 0.01449  0.03686  211 ASN A CB  
3244 C CG  . ASN A 225 ? 0.72622 0.61435 0.49116 -0.17896 0.01959  0.03774  211 ASN A CG  
3245 O OD1 . ASN A 225 ? 0.70230 0.60835 0.46666 -0.19555 0.03150  0.02941  211 ASN A OD1 
3246 N ND2 . ASN A 225 ? 0.80636 0.67684 0.55087 -0.18109 0.01055  0.04760  211 ASN A ND2 
3253 N N   . GLU A 226 ? 0.53130 0.46088 0.39298 -0.11929 0.01914  0.02011  212 GLU A N   
3254 C CA  . GLU A 226 ? 0.46557 0.39275 0.34019 -0.10619 0.01340  0.02088  212 GLU A CA  
3255 C C   . GLU A 226 ? 0.45931 0.40561 0.35100 -0.11184 0.01669  0.01567  212 GLU A C   
3256 O O   . GLU A 226 ? 0.53854 0.51093 0.45213 -0.11354 0.02300  0.00879  212 GLU A O   
3257 C CB  . GLU A 226 ? 0.43355 0.36915 0.32481 -0.08921 0.01131  0.01957  212 GLU A CB  
3258 C CG  . GLU A 226 ? 0.45906 0.39287 0.36011 -0.07848 0.00595  0.02029  212 GLU A CG  
3259 C CD  . GLU A 226 ? 0.47987 0.38683 0.36275 -0.07827 0.00080  0.02457  212 GLU A CD  
3260 O OE1 . GLU A 226 ? 0.43798 0.32653 0.30898 -0.07462 -0.00268 0.02901  212 GLU A OE1 
3261 O OE2 . GLU A 226 ? 0.43113 0.33520 0.31305 -0.08219 -0.00021 0.02318  212 GLU A OE2 
3268 N N   . LYS A 227 ? 0.50298 0.43639 0.38665 -0.11494 0.01207  0.01841  213 LYS A N   
3269 C CA  . LYS A 227 ? 0.50571 0.45568 0.40282 -0.12265 0.01299  0.01511  213 LYS A CA  
3270 C C   . LYS A 227 ? 0.48319 0.44210 0.39708 -0.11253 0.00708  0.01501  213 LYS A C   
3271 O O   . LYS A 227 ? 0.52562 0.50471 0.45806 -0.11720 0.00585  0.01314  213 LYS A O   
3272 C CB  . LYS A 227 ? 0.49752 0.42806 0.37236 -0.13707 0.01167  0.01787  213 LYS A CB  
3273 C CG  . LYS A 227 ? 0.54752 0.47008 0.40366 -0.15173 0.01653  0.01947  213 LYS A CG  
3274 C CD  . LYS A 227 ? 0.54726 0.44670 0.38031 -0.16645 0.01378  0.02349  213 LYS A CD  
3275 C CE  . LYS A 227 ? 0.64773 0.54158 0.46096 -0.18488 0.01826  0.02608  213 LYS A CE  
3276 N NZ  . LYS A 227 ? 0.64394 0.52409 0.44324 -0.18069 0.01629  0.03131  213 LYS A NZ  
3290 N N   . ARG A 228 ? 0.41520 0.36076 0.32354 -0.10027 0.00288  0.01733  214 ARG A N   
3291 C CA  . ARG A 228 ? 0.42736 0.38154 0.34798 -0.09300 -0.00244 0.01767  214 ARG A CA  
3292 C C   . ARG A 228 ? 0.37913 0.35454 0.32457 -0.08326 -0.00262 0.01691  214 ARG A C   
3293 O O   . ARG A 228 ? 0.37242 0.34947 0.32038 -0.07862 0.00188  0.01527  214 ARG A O   
3294 C CB  . ARG A 228 ? 0.42873 0.36071 0.33304 -0.08593 -0.00493 0.01850  214 ARG A CB  
3295 C CG  . ARG A 228 ? 0.42868 0.33698 0.31165 -0.09435 -0.00488 0.01754  214 ARG A CG  
3296 C CD  . ARG A 228 ? 0.40726 0.29672 0.28069 -0.08653 -0.00550 0.01507  214 ARG A CD  
3297 N NE  . ARG A 228 ? 0.44198 0.30695 0.29799 -0.09412 -0.00481 0.01212  214 ARG A NE  
3298 C CZ  . ARG A 228 ? 0.44896 0.31259 0.29750 -0.10475 -0.00518 0.00848  214 ARG A CZ  
3299 N NH1 . ARG A 228 ? 0.40578 0.29167 0.26234 -0.10973 -0.00799 0.00909  214 ARG A NH1 
3300 N NH2 . ARG A 228 ? 0.46440 0.30261 0.29714 -0.11140 -0.00383 0.00461  214 ARG A NH2 
3314 N N   . ASP A 229 ? 0.35706 0.34764 0.32024 -0.08159 -0.00878 0.01850  215 ASP A N   
3315 C CA  . ASP A 229 ? 0.32424 0.33087 0.31188 -0.07163 -0.01128 0.01894  215 ASP A CA  
3316 C C   . ASP A 229 ? 0.36370 0.35740 0.34038 -0.06091 -0.00969 0.01941  215 ASP A C   
3317 O O   . ASP A 229 ? 0.37335 0.35194 0.33253 -0.05884 -0.01177 0.02128  215 ASP A O   
3318 C CB  . ASP A 229 ? 0.35167 0.36950 0.35333 -0.07283 -0.02188 0.02401  215 ASP A CB  
3319 C CG  . ASP A 229 ? 0.36316 0.40108 0.39950 -0.06554 -0.02636 0.02500  215 ASP A CG  
3320 O OD1 . ASP A 229 ? 0.35038 0.39471 0.40057 -0.05977 -0.01902 0.01926  215 ASP A OD1 
3321 O OD2 . ASP A 229 ? 0.35868 0.40496 0.40820 -0.06664 -0.03778 0.03154  215 ASP A OD2 
3326 N N   . HIS A 230 ? 0.31565 0.31615 0.30351 -0.05498 -0.00524 0.01646  216 HIS A N   
3327 C CA  . HIS A 230 ? 0.35584 0.34404 0.33140 -0.04708 -0.00338 0.01687  216 HIS A CA  
3328 C C   . HIS A 230 ? 0.32757 0.32869 0.32303 -0.04003 -0.00165 0.01399  216 HIS A C   
3329 O O   . HIS A 230 ? 0.31399 0.33242 0.33415 -0.04088 -0.00047 0.01026  216 HIS A O   
3330 C CB  . HIS A 230 ? 0.36861 0.34136 0.32213 -0.05234 0.00151  0.01630  216 HIS A CB  
3331 C CG  . HIS A 230 ? 0.34124 0.32453 0.29952 -0.06090 0.00866  0.01151  216 HIS A CG  
3332 N ND1 . HIS A 230 ? 0.42448 0.41800 0.38947 -0.07128 0.01141  0.00880  216 HIS A ND1 
3333 C CD2 . HIS A 230 ? 0.38785 0.37466 0.34490 -0.06242 0.01461  0.00776  216 HIS A CD2 
3334 C CE1 . HIS A 230 ? 0.45688 0.46064 0.42562 -0.07869 0.01996  0.00271  216 HIS A CE1 
3335 N NE2 . HIS A 230 ? 0.37962 0.37893 0.34214 -0.07408 0.02226  0.00172  216 HIS A NE2 
3343 N N   . MET A 231 ? 0.35087 0.34329 0.33742 -0.03310 -0.00146 0.01499  217 MET A N   
3344 C CA  . MET A 231 ? 0.37393 0.37497 0.37480 -0.02743 0.00073  0.01157  217 MET A CA  
3345 C C   . MET A 231 ? 0.34480 0.33363 0.32638 -0.02601 0.00294  0.01216  217 MET A C   
3346 O O   . MET A 231 ? 0.34649 0.32376 0.31608 -0.02123 -0.00136 0.01695  217 MET A O   
3347 C CB  . MET A 231 ? 0.35843 0.36531 0.37559 -0.01973 -0.00626 0.01489  217 MET A CB  
3348 C CG  . MET A 231 ? 0.38302 0.39396 0.41172 -0.01342 -0.00482 0.01186  217 MET A CG  
3349 S SD  . MET A 231 ? 0.32449 0.34080 0.37313 -0.00679 -0.01454 0.01723  217 MET A SD  
3350 C CE  . MET A 231 ? 0.35661 0.36086 0.37980 -0.00637 -0.01886 0.02434  217 MET A CE  
3360 N N   . VAL A 232 ? 0.33740 0.32967 0.31668 -0.03135 0.00955  0.00690  218 VAL A N   
3361 C CA  . VAL A 232 ? 0.35868 0.34207 0.32174 -0.03149 0.00984  0.00813  218 VAL A CA  
3362 C C   . VAL A 232 ? 0.34558 0.33713 0.32425 -0.02394 0.00962  0.00498  218 VAL A C   
3363 O O   . VAL A 232 ? 0.33478 0.33950 0.33419 -0.02398 0.01450  -0.00271 218 VAL A O   
3364 C CB  . VAL A 232 ? 0.36232 0.34499 0.31035 -0.04477 0.01692  0.00409  218 VAL A CB  
3365 C CG1 . VAL A 232 ? 0.40448 0.37880 0.33488 -0.04697 0.01513  0.00658  218 VAL A CG1 
3366 C CG2 . VAL A 232 ? 0.41648 0.38833 0.34739 -0.05343 0.01583  0.00870  218 VAL A CG2 
3376 N N   . PHE A 233 ? 0.31826 0.30209 0.28961 -0.01747 0.00394  0.01033  219 PHE A N   
3377 C CA  . PHE A 233 ? 0.33722 0.32707 0.32273 -0.01014 0.00186  0.00926  219 PHE A CA  
3378 C C   . PHE A 233 ? 0.33692 0.32193 0.31011 -0.01078 0.00097  0.01005  219 PHE A C   
3379 O O   . PHE A 233 ? 0.35092 0.32603 0.30890 -0.01021 -0.00394 0.01656  219 PHE A O   
3380 C CB  . PHE A 233 ? 0.33008 0.31870 0.32120 -0.00288 -0.00480 0.01521  219 PHE A CB  
3381 C CG  . PHE A 233 ? 0.33633 0.33048 0.34108 0.00263  -0.00789 0.01552  219 PHE A CG  
3382 C CD1 . PHE A 233 ? 0.37473 0.37751 0.40126 0.00356  -0.00807 0.01237  219 PHE A CD1 
3383 C CD2 . PHE A 233 ? 0.34510 0.33571 0.34329 0.00663  -0.01131 0.01919  219 PHE A CD2 
3384 C CE1 . PHE A 233 ? 0.33291 0.33779 0.37148 0.00768  -0.01231 0.01383  219 PHE A CE1 
3385 C CE2 . PHE A 233 ? 0.33170 0.32684 0.34075 0.00981  -0.01424 0.01994  219 PHE A CE2 
3386 C CZ  . PHE A 233 ? 0.36192 0.36273 0.38971 0.00999  -0.01510 0.01775  219 PHE A CZ  
3396 N N   . LEU A 234 ? 0.37533 0.36721 0.35710 -0.01220 0.00513  0.00313  220 LEU A N   
3397 C CA  . LEU A 234 ? 0.40512 0.39427 0.37692 -0.01383 0.00366  0.00327  220 LEU A CA  
3398 C C   . LEU A 234 ? 0.39011 0.38487 0.38045 -0.00716 0.00237  0.00058  220 LEU A C   
3399 O O   . LEU A 234 ? 0.38304 0.38444 0.39421 -0.00521 0.00594  -0.00582 220 LEU A O   
3400 C CB  . LEU A 234 ? 0.36923 0.35925 0.32769 -0.02652 0.01126  -0.00431 220 LEU A CB  
3401 C CG  . LEU A 234 ? 0.45393 0.44218 0.40045 -0.03157 0.01009  -0.00557 220 LEU A CG  
3402 C CD1 . LEU A 234 ? 0.46151 0.43958 0.38677 -0.03327 -0.00046 0.00692  220 LEU A CD1 
3403 C CD2 . LEU A 234 ? 0.57410 0.56699 0.51281 -0.04567 0.02154  -0.01832 220 LEU A CD2 
3415 N N   . GLU A 235 ? 0.36619 0.35821 0.35107 -0.00400 -0.00354 0.00578  221 GLU A N   
3416 C CA  . GLU A 235 ? 0.40636 0.40205 0.40638 0.00102  -0.00591 0.00490  221 GLU A CA  
3417 C C   . GLU A 235 ? 0.40549 0.39978 0.39546 -0.00103 -0.00925 0.00663  221 GLU A C   
3418 O O   . GLU A 235 ? 0.33771 0.32885 0.31378 -0.00176 -0.01403 0.01315  221 GLU A O   
3419 C CB  . GLU A 235 ? 0.40414 0.40085 0.41329 0.00800  -0.01163 0.01200  221 GLU A CB  
3420 C CG  . GLU A 235 ? 0.41810 0.41725 0.44049 0.01093  -0.01554 0.01327  221 GLU A CG  
3421 C CD  . GLU A 235 ? 0.41184 0.41229 0.43799 0.01375  -0.02095 0.02066  221 GLU A CD  
3422 O OE1 . GLU A 235 ? 0.44543 0.44510 0.46536 0.01395  -0.02080 0.02324  221 GLU A OE1 
3423 O OE2 . GLU A 235 ? 0.55387 0.55548 0.58741 0.01397  -0.02524 0.02366  221 GLU A OE2 
3430 N N   . PHE A 236 ? 0.39354 0.38981 0.39281 -0.00210 -0.00756 0.00079  222 PHE A N   
3431 C CA  . PHE A 236 ? 0.35245 0.34869 0.34575 -0.00414 -0.01166 0.00253  222 PHE A CA  
3432 C C   . PHE A 236 ? 0.35701 0.35496 0.36687 0.00134  -0.01546 0.00471  222 PHE A C   
3433 O O   . PHE A 236 ? 0.36848 0.36548 0.39513 0.00300  -0.01319 -0.00028 222 PHE A O   
3434 C CB  . PHE A 236 ? 0.39615 0.39119 0.38095 -0.01409 -0.00582 -0.00743 222 PHE A CB  
3435 C CG  . PHE A 236 ? 0.38846 0.38122 0.35006 -0.02383 -0.00413 -0.00723 222 PHE A CG  
3436 C CD1 . PHE A 236 ? 0.39317 0.38401 0.33645 -0.02898 -0.01223 0.00085  222 PHE A CD1 
3437 C CD2 . PHE A 236 ? 0.44848 0.44135 0.40723 -0.02910 0.00447  -0.01429 222 PHE A CD2 
3438 C CE1 . PHE A 236 ? 0.51767 0.50427 0.43778 -0.03993 -0.01343 0.00360  222 PHE A CE1 
3439 C CE2 . PHE A 236 ? 0.51471 0.50430 0.44863 -0.04098 0.00538  -0.01290 222 PHE A CE2 
3440 C CZ  . PHE A 236 ? 0.50053 0.48573 0.41391 -0.04677 -0.00440 -0.00310 222 PHE A CZ  
3450 N N   . VAL A 237 ? 0.37293 0.37360 0.37975 0.00350  -0.02173 0.01236  223 VAL A N   
3451 C CA  A VAL A 237 ? 0.33945 0.34215 0.35756 0.00575  -0.02569 0.01584  223 VAL A CA  
3452 C CA  B VAL A 237 ? 0.37030 0.37298 0.38843 0.00574  -0.02568 0.01582  223 VAL A CA  
3453 C C   . VAL A 237 ? 0.36435 0.37033 0.37759 0.00217  -0.02923 0.01728  223 VAL A C   
3454 O O   . VAL A 237 ? 0.34418 0.35472 0.34925 0.00219  -0.03216 0.02136  223 VAL A O   
3455 C CB  A VAL A 237 ? 0.36336 0.36947 0.38360 0.00995  -0.02837 0.02299  223 VAL A CB  
3456 C CB  B VAL A 237 ? 0.38674 0.39272 0.40716 0.00997  -0.02830 0.02291  223 VAL A CB  
3457 C CG1 A VAL A 237 ? 0.37120 0.37924 0.39935 0.00850  -0.03246 0.02712  223 VAL A CG1 
3458 C CG1 B VAL A 237 ? 0.34278 0.35187 0.35362 0.01221  -0.02882 0.02612  223 VAL A CG1 
3459 C CG2 A VAL A 237 ? 0.36132 0.36468 0.38448 0.01204  -0.02597 0.02225  223 VAL A CG2 
3460 C CG2 B VAL A 237 ? 0.37135 0.38024 0.39830 0.00848  -0.03248 0.02734  223 VAL A CG2 
3477 N N   . THR A 238 ? 0.34954 0.35293 0.37003 -0.00094 -0.02997 0.01430  224 THR A N   
3478 C CA  . THR A 238 ? 0.35571 0.36211 0.37182 -0.00615 -0.03331 0.01489  224 THR A CA  
3479 C C   . THR A 238 ? 0.32597 0.33144 0.35253 -0.00733 -0.03693 0.01803  224 THR A C   
3480 O O   . THR A 238 ? 0.30954 0.30731 0.34738 -0.00603 -0.03694 0.01677  224 THR A O   
3481 C CB  . THR A 238 ? 0.36355 0.36477 0.37209 -0.01343 -0.02972 0.00562  224 THR A CB  
3482 O OG1 . THR A 238 ? 0.48818 0.48839 0.48564 -0.01480 -0.02555 0.00245  224 THR A OG1 
3483 C CG2 . THR A 238 ? 0.36426 0.37029 0.36384 -0.02032 -0.03469 0.00776  224 THR A CG2 
3491 N N   . ALA A 239 ? 0.28875 0.30232 0.31286 -0.01057 -0.04092 0.02275  225 ALA A N   
3492 C CA  . ALA A 239 ? 0.37283 0.38635 0.40339 -0.01463 -0.04462 0.02681  225 ALA A CA  
3493 C C   . ALA A 239 ? 0.36638 0.37240 0.39755 -0.02153 -0.04590 0.02183  225 ALA A C   
3494 O O   . ALA A 239 ? 0.35957 0.36750 0.38263 -0.02540 -0.04503 0.01713  225 ALA A O   
3495 C CB  . ALA A 239 ? 0.30506 0.33374 0.33456 -0.01602 -0.04652 0.03285  225 ALA A CB  
3501 N N   . ALA A 240 ? 0.36662 0.36274 0.40672 -0.02427 -0.04892 0.02330  226 ALA A N   
3502 C CA  . ALA A 240 ? 0.38924 0.37547 0.43189 -0.03124 -0.05052 0.01839  226 ALA A CA  
3503 C C   . ALA A 240 ? 0.40283 0.38157 0.45341 -0.03558 -0.05738 0.02635  226 ALA A C   
3504 O O   . ALA A 240 ? 0.32313 0.30582 0.37450 -0.03464 -0.06052 0.03545  226 ALA A O   
3505 C CB  . ALA A 240 ? 0.36140 0.33465 0.41029 -0.02934 -0.04499 0.00586  226 ALA A CB  
3511 N N   . GLY A 241 ? 0.32832 0.29502 0.38294 -0.04220 -0.06006 0.02297  227 GLY A N   
3512 C CA  . GLY A 241 ? 0.39821 0.35346 0.45995 -0.04813 -0.06832 0.03127  227 GLY A CA  
3513 C C   . GLY A 241 ? 0.43036 0.39270 0.48245 -0.06002 -0.07210 0.03719  227 GLY A C   
3514 O O   . GLY A 241 ? 0.41785 0.37186 0.47197 -0.06760 -0.07958 0.04638  227 GLY A O   
3518 N N   . ILE A 242 ? 0.40695 0.38483 0.44912 -0.06307 -0.06824 0.03318  228 ILE A N   
3519 C CA  . ILE A 242 ? 0.48867 0.47651 0.52463 -0.07483 -0.07134 0.03725  228 ILE A CA  
3520 C C   . ILE A 242 ? 0.49568 0.47937 0.52737 -0.08016 -0.07018 0.02757  228 ILE A C   
3521 O O   . ILE A 242 ? 0.46895 0.46159 0.49480 -0.07673 -0.06629 0.02146  228 ILE A O   
3522 C CB  . ILE A 242 ? 0.43229 0.44718 0.46414 -0.07450 -0.06904 0.04222  228 ILE A CB  
3523 C CG1 . ILE A 242 ? 0.48132 0.49917 0.51434 -0.07139 -0.06858 0.04959  228 ILE A CG1 
3524 C CG2 . ILE A 242 ? 0.43744 0.46589 0.46695 -0.08724 -0.07161 0.04524  228 ILE A CG2 
3525 C CD1 . ILE A 242 ? 0.45487 0.49856 0.48680 -0.07159 -0.06423 0.05186  228 ILE A CD1 
3537 N N   . THR A 243 ? 0.63746 0.60646 0.67033 -0.09023 -0.07429 0.02667  229 THR A N   
3538 C CA  . THR A 243 ? 0.79420 0.75469 0.82215 -0.09717 -0.07271 0.01556  229 THR A CA  
3539 C C   . THR A 243 ? 0.81251 0.79553 0.82960 -0.10587 -0.07412 0.01712  229 THR A C   
3540 O O   . THR A 243 ? 0.80384 0.80933 0.82154 -0.10514 -0.07566 0.02575  229 THR A O   
3541 C CB  . THR A 243 ? 0.81276 0.74802 0.84732 -0.10527 -0.07716 0.01385  229 THR A CB  
3542 O OG1 . THR A 243 ? 0.74575 0.67131 0.77469 -0.11279 -0.07388 0.00023  229 THR A OG1 
3543 C CG2 . THR A 243 ? 0.74615 0.68658 0.77782 -0.11706 -0.08474 0.02674  229 THR A CG2 
3551 N N   . LEU A 244 ? 0.94933 0.92676 0.95804 -0.11479 -0.07358 0.00777  230 LEU A N   
3552 C CA  . LEU A 244 ? 0.94073 0.93862 0.94001 -0.12459 -0.07721 0.00944  230 LEU A CA  
3553 C C   . LEU A 244 ? 0.88830 0.90825 0.88577 -0.11606 -0.07694 0.01317  230 LEU A C   
3554 O O   . LEU A 244 ? 0.85995 0.87961 0.84678 -0.11702 -0.07576 0.00713  230 LEU A O   
3555 C CB  . LEU A 244 ? 0.93145 0.94156 0.93504 -0.13416 -0.08292 0.01911  230 LEU A CB  
3556 C CG  . LEU A 244 ? 0.92211 0.90934 0.92640 -0.14508 -0.08561 0.01814  230 LEU A CG  
3557 C CD1 . LEU A 244 ? 0.98279 0.98127 0.99183 -0.15185 -0.08973 0.03048  230 LEU A CD1 
3558 C CD2 . LEU A 244 ? 0.89195 0.87232 0.88600 -0.15962 -0.08738 0.00940  230 LEU A CD2 
3570 N N   . LYS B 17  ? 0.61301 0.80580 0.89503 -0.04921 0.10739  0.02478  3   LYS B N   
3571 C CA  . LYS B 17  ? 0.57175 0.76724 0.87114 -0.03062 0.09789  0.03228  3   LYS B CA  
3572 C C   . LYS B 17  ? 0.58354 0.73557 0.83487 -0.02640 0.09156  0.02690  3   LYS B C   
3573 O O   . LYS B 17  ? 0.54289 0.67235 0.78912 -0.01404 0.10327  0.02125  3   LYS B O   
3574 C CB  . LYS B 17  ? 0.68511 0.92138 1.01576 -0.03190 0.07394  0.04733  3   LYS B CB  
3575 C CG  . LYS B 17  ? 0.71898 1.00573 1.11479 -0.02564 0.07772  0.05844  3   LYS B CG  
3576 C CD  . LYS B 17  ? 0.72718 1.01261 1.15929 -0.00085 0.09001  0.06457  3   LYS B CD  
3577 C CE  . LYS B 17  ? 0.66527 1.00601 1.16951 0.00890  0.08791  0.08160  3   LYS B CE  
3578 N NZ  . LYS B 17  ? 0.67037 1.04021 1.20267 -0.00171 0.10351  0.07569  3   LYS B NZ  
3591 N N   . GLY B 18  ? 0.57295 0.71437 0.79136 -0.03748 0.07383  0.02724  4   GLY B N   
3592 C CA  . GLY B 18  ? 0.48524 0.59049 0.66273 -0.03373 0.06680  0.02332  4   GLY B CA  
3593 C C   . GLY B 18  ? 0.44540 0.51485 0.58629 -0.03530 0.08256  0.01156  4   GLY B C   
3594 O O   . GLY B 18  ? 0.43767 0.48348 0.56157 -0.02639 0.08527  0.00688  4   GLY B O   
3598 N N   . GLU B 19  ? 0.43605 0.50253 0.56410 -0.04799 0.09277  0.00750  5   GLU B N   
3599 C CA  . GLU B 19  ? 0.53877 0.57537 0.62857 -0.05096 0.10645  -0.00028 5   GLU B CA  
3600 C C   . GLU B 19  ? 0.49530 0.53024 0.59403 -0.04087 0.12607  -0.00828 5   GLU B C   
3601 O O   . GLU B 19  ? 0.52250 0.53257 0.58652 -0.04029 0.13339  -0.01654 5   GLU B O   
3602 C CB  . GLU B 19  ? 0.51035 0.54651 0.58908 -0.06698 0.11488  0.00086  5   GLU B CB  
3603 C CG  . GLU B 19  ? 0.62830 0.68887 0.73695 -0.07023 0.13541  -0.00025 5   GLU B CG  
3604 C CD  . GLU B 19  ? 0.85632 0.91862 0.95948 -0.08834 0.14244  0.00328  5   GLU B CD  
3605 O OE1 . GLU B 19  ? 0.85940 0.91207 0.95126 -0.09817 0.12838  0.00682  5   GLU B OE1 
3606 O OE2 . GLU B 19  ? 0.78531 0.85759 0.89650 -0.09329 0.16374  0.00191  5   GLU B OE2 
3613 N N   . GLU B 20  ? 0.43104 0.49360 0.57730 -0.03323 0.13513  -0.00668 6   GLU B N   
3614 C CA  . GLU B 20  ? 0.44144 0.50161 0.60298 -0.02233 0.15671  -0.01674 6   GLU B CA  
3615 C C   . GLU B 20  ? 0.49624 0.53080 0.64413 -0.01138 0.15230  -0.02289 6   GLU B C   
3616 O O   . GLU B 20  ? 0.43478 0.45468 0.57603 -0.00686 0.17084  -0.03719 6   GLU B O   
3617 C CB  . GLU B 20  ? 0.45047 0.54745 0.67551 -0.01325 0.16459  -0.01061 6   GLU B CB  
3618 C CG  . GLU B 20  ? 0.69545 0.78989 0.95311 0.00458  0.18123  -0.01767 6   GLU B CG  
3619 C CD  . GLU B 20  ? 0.82193 0.89718 1.05645 0.00259  0.20982  -0.03803 6   GLU B CD  
3620 O OE1 . GLU B 20  ? 0.82681 0.90558 1.03765 -0.01109 0.22134  -0.04222 6   GLU B OE1 
3621 O OE2 . GLU B 20  ? 0.82095 0.87743 1.06011 0.01351  0.22145  -0.05016 6   GLU B OE2 
3628 N N   . LEU B 21  ? 0.43109 0.46031 0.57424 -0.00862 0.12950  -0.01388 7   LEU B N   
3629 C CA  . LEU B 21  ? 0.47880 0.48479 0.61214 0.00015  0.12481  -0.01821 7   LEU B CA  
3630 C C   . LEU B 21  ? 0.46370 0.43948 0.54256 -0.00794 0.12428  -0.02956 7   LEU B C   
3631 O O   . LEU B 21  ? 0.45608 0.41242 0.52492 -0.00324 0.12213  -0.03620 7   LEU B O   
3632 C CB  . LEU B 21  ? 0.44687 0.46127 0.59380 0.00470  0.10150  -0.00284 7   LEU B CB  
3633 C CG  . LEU B 21  ? 0.38730 0.43607 0.58817 0.01335  0.09713  0.01258  7   LEU B CG  
3634 C CD1 . LEU B 21  ? 0.34983 0.41179 0.54947 0.01135  0.07192  0.02805  7   LEU B CD1 
3635 C CD2 . LEU B 21  ? 0.31941 0.36509 0.56013 0.03006  0.11099  0.01219  7   LEU B CD2 
3647 N N   . PHE B 22  ? 0.44307 0.41567 0.48891 -0.02033 0.12587  -0.03048 8   PHE B N   
3648 C CA  . PHE B 22  ? 0.47013 0.41915 0.46557 -0.02782 0.12167  -0.03600 8   PHE B CA  
3649 C C   . PHE B 22  ? 0.49384 0.43855 0.46222 -0.03583 0.14145  -0.04610 8   PHE B C   
3650 O O   . PHE B 22  ? 0.47491 0.40739 0.40096 -0.04470 0.13728  -0.04471 8   PHE B O   
3651 C CB  . PHE B 22  ? 0.40993 0.35576 0.38630 -0.03495 0.10311  -0.02406 8   PHE B CB  
3652 C CG  . PHE B 22  ? 0.41636 0.36536 0.40852 -0.02925 0.08404  -0.01648 8   PHE B CG  
3653 C CD1 . PHE B 22  ? 0.40214 0.37391 0.42808 -0.02790 0.07808  -0.00785 8   PHE B CD1 
3654 C CD2 . PHE B 22  ? 0.38449 0.31714 0.35716 -0.02656 0.07208  -0.01773 8   PHE B CD2 
3655 C CE1 . PHE B 22  ? 0.38019 0.35772 0.41571 -0.02428 0.06102  -0.00045 8   PHE B CE1 
3656 C CE2 . PHE B 22  ? 0.41555 0.35264 0.40094 -0.02231 0.05671  -0.01048 8   PHE B CE2 
3657 C CZ  . PHE B 22  ? 0.41081 0.37006 0.42542 -0.02132 0.05142  -0.00176 8   PHE B CZ  
3667 N N   . THR B 23  ? 0.53272 0.48893 0.52536 -0.03262 0.16355  -0.05528 9   THR B N   
3668 C CA  . THR B 23  ? 0.54246 0.49776 0.50766 -0.04155 0.18518  -0.06589 9   THR B CA  
3669 C C   . THR B 23  ? 0.56251 0.49841 0.48893 -0.04419 0.18969  -0.08296 9   THR B C   
3670 O O   . THR B 23  ? 0.63840 0.57139 0.52260 -0.05541 0.19932  -0.08841 9   THR B O   
3671 C CB  . THR B 23  ? 0.52718 0.50282 0.53375 -0.03694 0.21007  -0.07263 9   THR B CB  
3672 O OG1 . THR B 23  ? 0.53670 0.51260 0.58552 -0.02183 0.21323  -0.07948 9   THR B OG1 
3673 C CG2 . THR B 23  ? 0.57216 0.57192 0.60881 -0.04040 0.20728  -0.05651 9   THR B CG2 
3681 N N   . GLY B 24  ? 0.53976 0.46380 0.47916 -0.03558 0.18282  -0.09100 10  GLY B N   
3682 C CA  . GLY B 24  ? 0.52597 0.43270 0.43239 -0.04009 0.18636  -0.10990 10  GLY B CA  
3683 C C   . GLY B 24  ? 0.53020 0.42347 0.42225 -0.03959 0.16107  -0.10435 10  GLY B C   
3684 O O   . GLY B 24  ? 0.58991 0.48633 0.48641 -0.03759 0.14121  -0.08536 10  GLY B O   
3688 N N   . VAL B 25  ? 0.52707 0.40614 0.40252 -0.04264 0.16279  -0.12253 11  VAL B N   
3689 C CA  . VAL B 25  ? 0.49645 0.36468 0.36310 -0.04281 0.14074  -0.11909 11  VAL B CA  
3690 C C   . VAL B 25  ? 0.46911 0.33342 0.38565 -0.02945 0.13608  -0.11240 11  VAL B C   
3691 O O   . VAL B 25  ? 0.49867 0.35888 0.45026 -0.02169 0.15313  -0.12247 11  VAL B O   
3692 C CB  . VAL B 25  ? 0.59231 0.44951 0.42553 -0.05348 0.14434  -0.14224 11  VAL B CB  
3693 C CG1 . VAL B 25  ? 0.53224 0.38116 0.36285 -0.05419 0.12213  -0.13863 11  VAL B CG1 
3694 C CG2 . VAL B 25  ? 0.59473 0.46079 0.37446 -0.06759 0.14712  -0.14507 11  VAL B CG2 
3704 N N   . VAL B 26  ? 0.49581 0.36193 0.41662 -0.02645 0.11397  -0.09445 12  VAL B N   
3705 C CA  . VAL B 26  ? 0.44257 0.30969 0.40545 -0.01515 0.10679  -0.08259 12  VAL B CA  
3706 C C   . VAL B 26  ? 0.41262 0.26763 0.36763 -0.01707 0.09185  -0.08298 12  VAL B C   
3707 O O   . VAL B 26  ? 0.48641 0.34278 0.41164 -0.02361 0.07644  -0.07787 12  VAL B O   
3708 C CB  . VAL B 26  ? 0.46738 0.35243 0.44425 -0.01141 0.09543  -0.06100 12  VAL B CB  
3709 C CG1 . VAL B 26  ? 0.40835 0.29867 0.42291 -0.00143 0.08625  -0.04727 12  VAL B CG1 
3710 C CG2 . VAL B 26  ? 0.50505 0.40469 0.49338 -0.01137 0.11050  -0.06070 12  VAL B CG2 
3720 N N   . PRO B 27  ? 0.41739 0.26055 0.40122 -0.01153 0.09657  -0.08790 13  PRO B N   
3721 C CA  . PRO B 27  ? 0.43839 0.27179 0.41801 -0.01471 0.08277  -0.08662 13  PRO B CA  
3722 C C   . PRO B 27  ? 0.43933 0.28512 0.42578 -0.01040 0.06391  -0.06319 13  PRO B C   
3723 O O   . PRO B 27  ? 0.38935 0.24799 0.39942 -0.00240 0.06287  -0.04786 13  PRO B O   
3724 C CB  . PRO B 27  ? 0.47366 0.28977 0.48988 -0.00909 0.09622  -0.09529 13  PRO B CB  
3725 C CG  . PRO B 27  ? 0.47638 0.29912 0.52751 0.00260  0.11155  -0.09040 13  PRO B CG  
3726 C CD  . PRO B 27  ? 0.47342 0.31019 0.49757 -0.00229 0.11655  -0.09506 13  PRO B CD  
3734 N N   . ILE B 28  ? 0.41807 0.26257 0.38378 -0.01664 0.04921  -0.06149 14  ILE B N   
3735 C CA  . ILE B 28  ? 0.36351 0.21926 0.33066 -0.01424 0.03316  -0.04326 14  ILE B CA  
3736 C C   . ILE B 28  ? 0.42093 0.27008 0.40026 -0.01513 0.02675  -0.04084 14  ILE B C   
3737 O O   . ILE B 28  ? 0.43234 0.27055 0.40278 -0.02238 0.02771  -0.05466 14  ILE B O   
3738 C CB  . ILE B 28  ? 0.42794 0.29080 0.36206 -0.01985 0.02255  -0.04094 14  ILE B CB  
3739 C CG1 . ILE B 28  ? 0.38226 0.25101 0.30657 -0.02008 0.02967  -0.04020 14  ILE B CG1 
3740 C CG2 . ILE B 28  ? 0.38394 0.25590 0.32154 -0.01763 0.00883  -0.02650 14  ILE B CG2 
3741 C CD1 . ILE B 28  ? 0.43978 0.31042 0.33206 -0.02586 0.02238  -0.03771 14  ILE B CD1 
3753 N N   . LEU B 29  ? 0.36840 0.22627 0.36733 -0.00942 0.02035  -0.02333 15  LEU B N   
3754 C CA  . LEU B 29  ? 0.38282 0.23848 0.39146 -0.01105 0.01365  -0.01658 15  LEU B CA  
3755 C C   . LEU B 29  ? 0.41424 0.28724 0.41349 -0.01071 0.00116  -0.00269 15  LEU B C   
3756 O O   . LEU B 29  ? 0.39111 0.27735 0.39229 -0.00673 -0.00078 0.00693  15  LEU B O   
3757 C CB  . LEU B 29  ? 0.40731 0.25556 0.45223 -0.00467 0.02126  -0.00714 15  LEU B CB  
3758 C CG  . LEU B 29  ? 0.36872 0.19424 0.43009 -0.00506 0.03651  -0.02314 15  LEU B CG  
3759 C CD1 . LEU B 29  ? 0.36944 0.18745 0.47308 0.00416  0.04403  -0.00806 15  LEU B CD1 
3760 C CD2 . LEU B 29  ? 0.38886 0.20092 0.43495 -0.01715 0.03540  -0.04128 15  LEU B CD2 
3772 N N   . VAL B 30  ? 0.38650 0.26078 0.37689 -0.01579 -0.00643 -0.00341 16  VAL B N   
3773 C CA  . VAL B 30  ? 0.38863 0.27798 0.37045 -0.01577 -0.01549 0.00597  16  VAL B CA  
3774 C C   . VAL B 30  ? 0.35843 0.25123 0.35411 -0.01772 -0.01767 0.01446  16  VAL B C   
3775 O O   . VAL B 30  ? 0.36386 0.24663 0.36753 -0.02238 -0.01584 0.00849  16  VAL B O   
3776 C CB  . VAL B 30  ? 0.32766 0.21886 0.28618 -0.01899 -0.02165 -0.00193 16  VAL B CB  
3777 C CG1 . VAL B 30  ? 0.32410 0.22830 0.27810 -0.01754 -0.02749 0.00559  16  VAL B CG1 
3778 C CG2 . VAL B 30  ? 0.33037 0.21641 0.27395 -0.01871 -0.01799 -0.00877 16  VAL B CG2 
3788 N N   . GLU B 31  ? 0.34813 0.25624 0.34579 -0.01590 -0.02090 0.02762  17  GLU B N   
3789 C CA  . GLU B 31  ? 0.42386 0.33939 0.43118 -0.01860 -0.02195 0.03797  17  GLU B CA  
3790 C C   . GLU B 31  ? 0.38636 0.31971 0.37921 -0.01972 -0.02635 0.04009  17  GLU B C   
3791 O O   . GLU B 31  ? 0.32871 0.27169 0.31211 -0.01789 -0.02786 0.04195  17  GLU B O   
3792 C CB  . GLU B 31  ? 0.35971 0.27727 0.38752 -0.01548 -0.01849 0.05564  17  GLU B CB  
3793 C CG  . GLU B 31  ? 0.57720 0.47323 0.62790 -0.01458 -0.01097 0.05426  17  GLU B CG  
3794 C CD  . GLU B 31  ? 0.60486 0.49103 0.66180 -0.00851 -0.00559 0.04761  17  GLU B CD  
3795 O OE1 . GLU B 31  ? 0.65702 0.55595 0.70348 -0.00505 -0.00863 0.04857  17  GLU B OE1 
3796 O OE2 . GLU B 31  ? 0.41717 0.28285 0.49100 -0.00805 0.00312  0.04006  17  GLU B OE2 
3799 N N   . LEU B 32  ? 0.43463 0.37298 0.42798 -0.02346 -0.02731 0.03823  18  LEU B N   
3800 C CA  . LEU B 32  ? 0.38542 0.33937 0.36850 -0.02396 -0.02833 0.03734  18  LEU B CA  
3801 C C   . LEU B 32  ? 0.39452 0.36050 0.38723 -0.02835 -0.02529 0.04552  18  LEU B C   
3802 O O   . LEU B 32  ? 0.33863 0.29982 0.34471 -0.03193 -0.02475 0.04457  18  LEU B O   
3803 C CB  . LEU B 32  ? 0.38231 0.33253 0.35749 -0.02222 -0.03145 0.02476  18  LEU B CB  
3804 C CG  . LEU B 32  ? 0.45058 0.41398 0.42465 -0.02150 -0.03017 0.02199  18  LEU B CG  
3805 C CD1 . LEU B 32  ? 0.47397 0.44824 0.43814 -0.02198 -0.02596 0.02365  18  LEU B CD1 
3806 C CD2 . LEU B 32  ? 0.50112 0.45890 0.47153 -0.01723 -0.03402 0.01372  18  LEU B CD2 
3818 N N   . ASP B 33  ? 0.38433 0.36755 0.36942 -0.02980 -0.02280 0.05280  19  ASP B N   
3819 C CA  A ASP B 33  ? 0.39171 0.39056 0.38159 -0.03486 -0.01775 0.06060  19  ASP B CA  
3820 C CA  B ASP B 33  ? 0.37426 0.37313 0.36413 -0.03486 -0.01774 0.06062  19  ASP B CA  
3821 C C   . ASP B 33  ? 0.37062 0.38321 0.34905 -0.03467 -0.01422 0.04952  19  ASP B C   
3822 O O   . ASP B 33  ? 0.36961 0.39025 0.33157 -0.03492 -0.01342 0.04626  19  ASP B O   
3823 C CB  A ASP B 33  ? 0.44229 0.45230 0.43147 -0.03789 -0.01618 0.08034  19  ASP B CB  
3824 C CB  B ASP B 33  ? 0.44240 0.45238 0.43146 -0.03785 -0.01624 0.08033  19  ASP B CB  
3825 C CG  A ASP B 33  ? 0.44131 0.43554 0.45089 -0.03723 -0.01641 0.09333  19  ASP B CG  
3826 C CG  B ASP B 33  ? 0.45313 0.48154 0.44328 -0.04456 -0.00947 0.09048  19  ASP B CG  
3827 O OD1 A ASP B 33  ? 0.38662 0.36457 0.41089 -0.03843 -0.01537 0.08583  19  ASP B OD1 
3828 O OD1 B ASP B 33  ? 0.47532 0.50718 0.47211 -0.04666 -0.00505 0.08145  19  ASP B OD1 
3829 O OD2 A ASP B 33  ? 0.53107 0.52991 0.54361 -0.03580 -0.01754 0.11097  19  ASP B OD2 
3830 O OD2 B ASP B 33  ? 0.49163 0.53376 0.47682 -0.04789 -0.00854 0.10911  19  ASP B OD2 
3837 N N   . GLY B 34  ? 0.35238 0.36821 0.34219 -0.03455 -0.01165 0.04272  20  GLY B N   
3838 C CA  . GLY B 34  ? 0.34010 0.36618 0.32645 -0.03188 -0.00638 0.03115  20  GLY B CA  
3839 C C   . GLY B 34  ? 0.37899 0.42655 0.37163 -0.03650 0.00392  0.03358  20  GLY B C   
3840 O O   . GLY B 34  ? 0.35493 0.40911 0.35864 -0.04235 0.00601  0.04523  20  GLY B O   
3844 N N   . ASP B 35  ? 0.37816 0.43573 0.36523 -0.03435 0.01232  0.02176  21  ASP B N   
3845 C CA  . ASP B 35  ? 0.39119 0.47138 0.38339 -0.03850 0.02555  0.02068  21  ASP B CA  
3846 C C   . ASP B 35  ? 0.39373 0.47571 0.39083 -0.03136 0.03420  0.00228  21  ASP B C   
3847 O O   . ASP B 35  ? 0.36100 0.44048 0.33904 -0.03195 0.03908  -0.00889 21  ASP B O   
3848 C CB  . ASP B 35  ? 0.39285 0.48865 0.36205 -0.04812 0.03118  0.02955  21  ASP B CB  
3849 C CG  . ASP B 35  ? 0.35946 0.48074 0.32843 -0.05391 0.04745  0.02696  21  ASP B CG  
3850 O OD1 . ASP B 35  ? 0.41414 0.54139 0.40744 -0.05004 0.05451  0.02044  21  ASP B OD1 
3851 O OD2 . ASP B 35  ? 0.37133 0.50962 0.31588 -0.06278 0.05327  0.03192  21  ASP B OD2 
3856 N N   . VAL B 36  ? 0.38165 0.46837 0.40703 -0.02496 0.03606  -0.00071 22  VAL B N   
3857 C CA  . VAL B 36  ? 0.42045 0.50734 0.46039 -0.01499 0.04441  -0.01526 22  VAL B CA  
3858 C C   . VAL B 36  ? 0.34598 0.45903 0.40684 -0.01590 0.06017  -0.01820 22  VAL B C   
3859 O O   . VAL B 36  ? 0.32058 0.44679 0.40748 -0.01623 0.05707  -0.00952 22  VAL B O   
3860 C CB  . VAL B 36  ? 0.45066 0.52355 0.51037 -0.00414 0.03168  -0.01369 22  VAL B CB  
3861 C CG1 . VAL B 36  ? 0.42685 0.49810 0.50604 0.00819  0.04094  -0.02514 22  VAL B CG1 
3862 C CG2 . VAL B 36  ? 0.35412 0.40311 0.39236 -0.00475 0.01805  -0.01025 22  VAL B CG2 
3872 N N   . ASN B 37  ? 0.35023 0.47225 0.40054 -0.01748 0.07803  -0.03212 23  ASN B N   
3873 C CA  . ASN B 37  ? 0.37488 0.52378 0.44252 -0.01909 0.09735  -0.03735 23  ASN B CA  
3874 C C   . ASN B 37  ? 0.37573 0.54444 0.44279 -0.03129 0.09709  -0.01996 23  ASN B C   
3875 O O   . ASN B 37  ? 0.43513 0.62547 0.53079 -0.03185 0.10585  -0.01671 23  ASN B O   
3876 C CB  . ASN B 37  ? 0.37174 0.52576 0.48432 -0.00454 0.10107  -0.04238 23  ASN B CB  
3877 C CG  . ASN B 37  ? 0.39814 0.53602 0.51645 0.00747  0.11071  -0.06088 23  ASN B CG  
3878 O OD1 . ASN B 37  ? 0.41263 0.52807 0.50295 0.00559  0.10760  -0.06858 23  ASN B OD1 
3879 N ND2 . ASN B 37  ? 0.38495 0.53434 0.54353 0.01984  0.12333  -0.06783 23  ASN B ND2 
3886 N N   . GLY B 38  ? 0.38458 0.54613 0.42220 -0.04108 0.08748  -0.00739 24  GLY B N   
3887 C CA  . GLY B 38  ? 0.42464 0.59941 0.46135 -0.05265 0.08725  0.01216  24  GLY B CA  
3888 C C   . GLY B 38  ? 0.38398 0.54751 0.44414 -0.05243 0.07170  0.02591  24  GLY B C   
3889 O O   . GLY B 38  ? 0.32123 0.48823 0.38157 -0.06242 0.07049  0.04311  24  GLY B O   
3893 N N   . HIS B 39  ? 0.43143 0.58162 0.51098 -0.04233 0.06027  0.01903  25  HIS B N   
3894 C CA  . HIS B 39  ? 0.32792 0.46836 0.42597 -0.04404 0.04504  0.02790  25  HIS B CA  
3895 C C   . HIS B 39  ? 0.35697 0.47098 0.43091 -0.04513 0.03195  0.03357  25  HIS B C   
3896 O O   . HIS B 39  ? 0.33730 0.43486 0.39822 -0.03720 0.02462  0.02568  25  HIS B O   
3897 C CB  . HIS B 39  ? 0.42611 0.56864 0.55189 -0.03382 0.03726  0.01963  25  HIS B CB  
3898 C CG  . HIS B 39  ? 0.47758 0.64908 0.63615 -0.03107 0.04961  0.01553  25  HIS B CG  
3899 N ND1 . HIS B 39  ? 0.52104 0.70036 0.68562 -0.02038 0.06264  0.00338  25  HIS B ND1 
3900 C CD2 . HIS B 39  ? 0.46112 0.65634 0.65187 -0.03784 0.05231  0.02124  25  HIS B CD2 
3901 C CE1 . HIS B 39  ? 0.54702 0.75481 0.74728 -0.01905 0.07332  0.00232  25  HIS B CE1 
3902 N NE2 . HIS B 39  ? 0.53018 0.74979 0.74680 -0.03010 0.06664  0.01357  25  HIS B NE2 
3910 N N   . LYS B 40  ? 0.31515 0.42481 0.38645 -0.05466 0.03028  0.04805  26  LYS B N   
3911 C CA  . LYS B 40  ? 0.37672 0.46375 0.43027 -0.05497 0.02066  0.05509  26  LYS B CA  
3912 C C   . LYS B 40  ? 0.35483 0.42346 0.42385 -0.05506 0.00862  0.05337  26  LYS B C   
3913 O O   . LYS B 40  ? 0.30841 0.38333 0.40174 -0.06106 0.00816  0.05388  26  LYS B O   
3914 C CB  . LYS B 40  ? 0.44444 0.53608 0.48888 -0.06379 0.02645  0.07412  26  LYS B CB  
3915 C CG  . LYS B 40  ? 0.46302 0.58018 0.49161 -0.06782 0.04000  0.07615  26  LYS B CG  
3916 C CD  . LYS B 40  ? 0.60004 0.72234 0.60816 -0.07459 0.04138  0.09665  26  LYS B CD  
3917 C CE  . LYS B 40  ? 0.61567 0.76607 0.59937 -0.08011 0.05405  0.09511  26  LYS B CE  
3918 N NZ  . LYS B 40  ? 0.74551 0.90429 0.70116 -0.08540 0.05056  0.11304  26  LYS B NZ  
3932 N N   . PHE B 41  ? 0.35889 0.40669 0.41338 -0.04984 -0.00045 0.04985  27  PHE B N   
3933 C CA  . PHE B 41  ? 0.35689 0.38697 0.41971 -0.05059 -0.01055 0.04503  27  PHE B CA  
3934 C C   . PHE B 41  ? 0.37002 0.37864 0.41590 -0.04720 -0.01472 0.04693  27  PHE B C   
3935 O O   . PHE B 41  ? 0.32392 0.33362 0.35200 -0.04276 -0.01296 0.04961  27  PHE B O   
3936 C CB  . PHE B 41  ? 0.36467 0.39931 0.43308 -0.04499 -0.01818 0.03247  27  PHE B CB  
3937 C CG  . PHE B 41  ? 0.41935 0.45088 0.47035 -0.03447 -0.01886 0.02634  27  PHE B CG  
3938 C CD1 . PHE B 41  ? 0.35587 0.40243 0.40805 -0.02981 -0.01016 0.02342  27  PHE B CD1 
3939 C CD2 . PHE B 41  ? 0.43668 0.44932 0.47152 -0.03017 -0.02623 0.02234  27  PHE B CD2 
3940 C CE1 . PHE B 41  ? 0.36338 0.40319 0.40237 -0.02141 -0.00917 0.01608  27  PHE B CE1 
3941 C CE2 . PHE B 41  ? 0.42433 0.43225 0.44563 -0.02211 -0.02585 0.01735  27  PHE B CE2 
3942 C CZ  . PHE B 41  ? 0.40551 0.42550 0.42962 -0.01792 -0.01750 0.01394  27  PHE B CZ  
3952 N N   . SER B 42  ? 0.35762 0.34838 0.41069 -0.05028 -0.01960 0.04391  28  SER B N   
3953 C CA  . SER B 42  ? 0.34976 0.32032 0.39280 -0.04672 -0.02155 0.04447  28  SER B CA  
3954 C C   . SER B 42  ? 0.36856 0.32547 0.40918 -0.04698 -0.02838 0.02983  28  SER B C   
3955 O O   . SER B 42  ? 0.36005 0.31820 0.41270 -0.05424 -0.03146 0.02256  28  SER B O   
3956 C CB  . SER B 42  ? 0.37235 0.33206 0.42874 -0.05087 -0.01584 0.05835  28  SER B CB  
3957 O OG  . SER B 42  ? 0.47780 0.45319 0.53213 -0.05152 -0.01044 0.07517  28  SER B OG  
3963 N N   . VAL B 43  ? 0.36175 0.30819 0.38604 -0.04063 -0.03065 0.02551  29  VAL B N   
3964 C CA  . VAL B 43  ? 0.39064 0.32557 0.40628 -0.04114 -0.03579 0.01248  29  VAL B CA  
3965 C C   . VAL B 43  ? 0.33431 0.25039 0.34766 -0.03912 -0.03094 0.01192  29  VAL B C   
3966 O O   . VAL B 43  ? 0.34856 0.26516 0.35851 -0.03303 -0.02789 0.02083  29  VAL B O   
3967 C CB  . VAL B 43  ? 0.36860 0.31061 0.36754 -0.03491 -0.04171 0.00810  29  VAL B CB  
3968 C CG1 . VAL B 43  ? 0.37590 0.30860 0.36181 -0.03662 -0.04706 -0.00240 29  VAL B CG1 
3969 C CG2 . VAL B 43  ? 0.34338 0.30466 0.35141 -0.03441 -0.04487 0.00947  29  VAL B CG2 
3979 N N   . SER B 44  ? 0.36203 0.26355 0.37888 -0.04484 -0.02976 0.00048  30  SER B N   
3980 C CA  . SER B 44  ? 0.38676 0.26964 0.40364 -0.04239 -0.02292 -0.00428 30  SER B CA  
3981 C C   . SER B 44  ? 0.40461 0.28392 0.40002 -0.04422 -0.02608 -0.02010 30  SER B C   
3982 O O   . SER B 44  ? 0.38052 0.26451 0.36911 -0.05233 -0.03239 -0.03080 30  SER B O   
3983 C CB  . SER B 44  ? 0.38004 0.24514 0.42042 -0.04836 -0.01466 -0.00672 30  SER B CB  
3984 O OG  . SER B 44  ? 0.39207 0.26004 0.45217 -0.04661 -0.01108 0.01230  30  SER B OG  
3990 N N   . GLY B 45  ? 0.36755 0.24161 0.35256 -0.03773 -0.02205 -0.02043 31  GLY B N   
3991 C CA  . GLY B 45  ? 0.36459 0.23623 0.32669 -0.03974 -0.02320 -0.03275 31  GLY B CA  
3992 C C   . GLY B 45  ? 0.38106 0.23798 0.34512 -0.03753 -0.01118 -0.04028 31  GLY B C   
3993 O O   . GLY B 45  ? 0.41330 0.26581 0.39648 -0.03056 -0.00398 -0.03139 31  GLY B O   
3997 N N   . GLU B 46  ? 0.41444 0.26655 0.35891 -0.04368 -0.00891 -0.05626 32  GLU B N   
3998 C CA  . GLU B 46  ? 0.50745 0.34696 0.45192 -0.04234 0.00517  -0.06705 32  GLU B CA  
3999 C C   . GLU B 46  ? 0.44536 0.28955 0.35579 -0.04814 0.00424  -0.07787 32  GLU B C   
4000 O O   . GLU B 46  ? 0.43026 0.28564 0.31967 -0.05423 -0.00820 -0.07785 32  GLU B O   
4001 C CB  . GLU B 46  ? 0.47692 0.29766 0.44165 -0.04737 0.01663  -0.08160 32  GLU B CB  
4002 C CG  . GLU B 46  ? 0.52806 0.34761 0.48029 -0.06232 0.01124  -0.09912 32  GLU B CG  
4003 C CD  . GLU B 46  ? 0.57466 0.37156 0.54929 -0.06910 0.02469  -0.11637 32  GLU B CD  
4004 O OE1 . GLU B 46  ? 0.52796 0.31023 0.50195 -0.06961 0.04031  -0.13334 32  GLU B OE1 
4005 O OE2 . GLU B 46  ? 0.53335 0.32619 0.52827 -0.07421 0.02132  -0.11341 32  GLU B OE2 
4012 N N   . GLY B 47  ? 0.51582 0.35346 0.42261 -0.04600 0.01784  -0.08537 33  GLY B N   
4013 C CA  . GLY B 47  ? 0.52330 0.36559 0.39592 -0.05253 0.02001  -0.09486 33  GLY B CA  
4014 C C   . GLY B 47  ? 0.50874 0.34858 0.38504 -0.04645 0.03552  -0.09503 33  GLY B C   
4015 O O   . GLY B 47  ? 0.46759 0.29958 0.37475 -0.03893 0.04738  -0.09536 33  GLY B O   
4019 N N   . GLU B 48  ? 0.52075 0.36908 0.36769 -0.04969 0.03510  -0.09262 34  GLU B N   
4020 C CA  . GLU B 48  ? 0.54014 0.38939 0.38744 -0.04658 0.05065  -0.09348 34  GLU B CA  
4021 C C   . GLU B 48  ? 0.56056 0.42018 0.39239 -0.04520 0.04323  -0.07549 34  GLU B C   
4022 O O   . GLU B 48  ? 0.47731 0.34185 0.28927 -0.04817 0.02827  -0.06606 34  GLU B O   
4023 C CB  . GLU B 48  ? 0.60840 0.45409 0.43165 -0.05629 0.06609  -0.11580 34  GLU B CB  
4024 C CG  . GLU B 48  ? 0.75711 0.58840 0.59520 -0.05975 0.07695  -0.13869 34  GLU B CG  
4025 C CD  . GLU B 48  ? 0.74056 0.57191 0.55544 -0.07270 0.06423  -0.15030 34  GLU B CD  
4026 O OE1 . GLU B 48  ? 0.70563 0.54677 0.51359 -0.07305 0.04359  -0.13472 34  GLU B OE1 
4027 O OE2 . GLU B 48  ? 0.85322 0.67609 0.65839 -0.08323 0.07560  -0.17644 34  GLU B OE2 
4034 N N   . GLY B 49  ? 0.49182 0.35477 0.33645 -0.04078 0.05466  -0.07075 35  GLY B N   
4035 C CA  . GLY B 49  ? 0.46608 0.33601 0.29890 -0.04150 0.05147  -0.05585 35  GLY B CA  
4036 C C   . GLY B 49  ? 0.55465 0.42838 0.37975 -0.04526 0.06988  -0.06101 35  GLY B C   
4037 O O   . GLY B 49  ? 0.52961 0.40403 0.37717 -0.04181 0.08567  -0.07126 35  GLY B O   
4041 N N   . ASP B 50  ? 0.49879 0.37540 0.29414 -0.05198 0.06881  -0.05242 36  ASP B N   
4042 C CA  . ASP B 50  ? 0.60970 0.49154 0.39211 -0.05792 0.08698  -0.05499 36  ASP B CA  
4043 C C   . ASP B 50  ? 0.58701 0.47131 0.36950 -0.05920 0.08344  -0.03510 36  ASP B C   
4044 O O   . ASP B 50  ? 0.56549 0.44741 0.31848 -0.06479 0.07681  -0.02316 36  ASP B O   
4045 C CB  . ASP B 50  ? 0.60323 0.48594 0.34181 -0.06864 0.09174  -0.06529 36  ASP B CB  
4046 C CG  . ASP B 50  ? 0.68374 0.57311 0.40943 -0.07538 0.11541  -0.07295 36  ASP B CG  
4047 O OD1 . ASP B 50  ? 0.68749 0.58129 0.44321 -0.07093 0.12833  -0.07034 36  ASP B OD1 
4048 O OD2 . ASP B 50  ? 0.79557 0.68866 0.48078 -0.08609 0.12121  -0.08174 36  ASP B OD2 
4053 N N   . ALA B 51  ? 0.54666 0.43627 0.36427 -0.05454 0.08759  -0.03090 37  ALA B N   
4054 C CA  . ALA B 51  ? 0.57141 0.46190 0.39370 -0.05769 0.08479  -0.01524 37  ALA B CA  
4055 C C   . ALA B 51  ? 0.54951 0.44227 0.35052 -0.06734 0.09965  -0.01019 37  ALA B C   
4056 O O   . ALA B 51  ? 0.56290 0.45069 0.35838 -0.07222 0.09688  0.00478  37  ALA B O   
4057 C CB  . ALA B 51  ? 0.52051 0.42152 0.38477 -0.05326 0.08540  -0.01422 37  ALA B CB  
4063 N N   . THR B 52  ? 0.53678 0.43599 0.32644 -0.07080 0.11705  -0.02265 38  THR B N   
4064 C CA  . THR B 52  ? 0.56243 0.46551 0.32536 -0.08149 0.13237  -0.01731 38  THR B CA  
4065 C C   . THR B 52  ? 0.63243 0.52646 0.35368 -0.08729 0.11991  -0.00148 38  THR B C   
4066 O O   . THR B 52  ? 0.59466 0.48631 0.30412 -0.09422 0.12366  0.01600  38  THR B O   
4067 C CB  . THR B 52  ? 0.59119 0.50274 0.34367 -0.08455 0.15375  -0.03727 38  THR B CB  
4068 O OG1 . THR B 52  ? 0.59341 0.51494 0.39205 -0.07754 0.16732  -0.04778 38  THR B OG1 
4069 C CG2 . THR B 52  ? 0.65130 0.56891 0.36776 -0.09741 0.17009  -0.03145 38  THR B CG2 
4077 N N   . TYR B 53  ? 0.60928 0.49913 0.31113 -0.08459 0.10477  -0.00562 39  TYR B N   
4078 C CA  . TYR B 53  ? 0.66111 0.54644 0.33003 -0.08762 0.08899  0.01168  39  TYR B CA  
4079 C C   . TYR B 53  ? 0.66023 0.53557 0.34961 -0.07848 0.06817  0.02308  39  TYR B C   
4080 O O   . TYR B 53  ? 0.65982 0.53180 0.33062 -0.07810 0.05394  0.03918  39  TYR B O   
4081 C CB  . TYR B 53  ? 0.70786 0.60079 0.34002 -0.09302 0.08517  -0.00044 39  TYR B CB  
4082 C CG  . TYR B 53  ? 0.79873 0.70225 0.39250 -0.10569 0.10315  -0.00487 39  TYR B CG  
4083 C CD1 . TYR B 53  ? 0.76822 0.67733 0.36848 -0.10877 0.12667  -0.02865 39  TYR B CD1 
4084 C CD2 . TYR B 53  ? 0.84669 0.75590 0.39838 -0.11433 0.09752  0.01574  39  TYR B CD2 
4085 C CE1 . TYR B 53  ? 0.77205 0.69227 0.33542 -0.12129 0.14592  -0.03499 39  TYR B CE1 
4086 C CE2 . TYR B 53  ? 0.77690 0.69963 0.29410 -0.12588 0.11336  0.01245  39  TYR B CE2 
4087 C CZ  . TYR B 53  ? 0.83100 0.75973 0.35584 -0.12899 0.13727  -0.01414 39  TYR B CZ  
4088 O OH  . TYR B 53  ? 0.89165 0.83674 0.39450 -0.13654 0.15085  -0.01831 39  TYR B OH  
4098 N N   . GLY B 54  ? 0.60398 0.47665 0.33154 -0.07108 0.06651  0.01593  40  GLY B N   
4099 C CA  . GLY B 54  ? 0.59085 0.45589 0.33596 -0.06322 0.04908  0.02283  40  GLY B CA  
4100 C C   . GLY B 54  ? 0.57715 0.44403 0.30863 -0.05986 0.03385  0.01950  40  GLY B C   
4101 O O   . GLY B 54  ? 0.53662 0.39891 0.26921 -0.05527 0.01938  0.03162  40  GLY B O   
4105 N N   . LYS B 55  ? 0.55263 0.42641 0.27423 -0.06248 0.03786  0.00226  41  LYS B N   
4106 C CA  . LYS B 55  ? 0.57699 0.45515 0.28344 -0.06321 0.02452  -0.00353 41  LYS B CA  
4107 C C   . LYS B 55  ? 0.54807 0.42437 0.28364 -0.05705 0.02094  -0.01739 41  LYS B C   
4108 O O   . LYS B 55  ? 0.49982 0.37463 0.25467 -0.05541 0.03362  -0.03021 41  LYS B O   
4109 C CB  . LYS B 55  ? 0.57909 0.46566 0.24950 -0.07410 0.03214  -0.01540 41  LYS B CB  
4110 C CG  . LYS B 55  ? 0.60924 0.50413 0.26080 -0.07861 0.01701  -0.02241 41  LYS B CG  
4111 C CD  . LYS B 55  ? 0.61535 0.51949 0.22952 -0.09214 0.02678  -0.03971 41  LYS B CD  
4112 C CE  . LYS B 55  ? 0.74053 0.65865 0.32879 -0.10037 0.00843  -0.04285 41  LYS B CE  
4113 N NZ  . LYS B 55  ? 0.75084 0.68021 0.29683 -0.11661 0.01800  -0.06223 41  LYS B NZ  
4127 N N   . LEU B 56  ? 0.57882 0.45642 0.31972 -0.05336 0.00429  -0.01297 42  LEU B N   
4128 C CA  . LEU B 56  ? 0.51949 0.39609 0.28550 -0.04893 -0.00012 -0.02309 42  LEU B CA  
4129 C C   . LEU B 56  ? 0.52900 0.41257 0.28071 -0.05444 -0.01143 -0.03039 42  LEU B C   
4130 O O   . LEU B 56  ? 0.53452 0.42617 0.27159 -0.05547 -0.02523 -0.01854 42  LEU B O   
4131 C CB  . LEU B 56  ? 0.52383 0.39810 0.31548 -0.04023 -0.00815 -0.01159 42  LEU B CB  
4132 C CG  . LEU B 56  ? 0.49950 0.37034 0.31223 -0.03648 0.00123  -0.00905 42  LEU B CG  
4133 C CD1 . LEU B 56  ? 0.56714 0.43664 0.39600 -0.03099 -0.00703 0.00073  42  LEU B CD1 
4134 C CD2 . LEU B 56  ? 0.47957 0.35177 0.31316 -0.03469 0.00987  -0.02079 42  LEU B CD2 
4146 N N   . THR B 57  ? 0.52919 0.41022 0.28797 -0.05826 -0.00551 -0.04940 43  THR B N   
4147 C CA  . THR B 57  ? 0.52102 0.40829 0.27267 -0.06568 -0.01558 -0.06009 43  THR B CA  
4148 C C   . THR B 57  ? 0.54004 0.42041 0.32650 -0.06107 -0.01554 -0.06584 43  THR B C   
4149 O O   . THR B 57  ? 0.50486 0.37408 0.30942 -0.05903 -0.00150 -0.07633 43  THR B O   
4150 C CB  . THR B 57  ? 0.54325 0.43186 0.26726 -0.07865 -0.00629 -0.08109 43  THR B CB  
4151 O OG1 . THR B 57  ? 0.63147 0.50673 0.37033 -0.07655 0.01494  -0.09557 43  THR B OG1 
4152 C CG2 . THR B 57  ? 0.60588 0.50609 0.28959 -0.08527 -0.00885 -0.07209 43  THR B CG2 
4160 N N   . LEU B 58  ? 0.47292 0.36090 0.27094 -0.05889 -0.03038 -0.05715 44  LEU B N   
4161 C CA  . LEU B 58  ? 0.47669 0.36027 0.30669 -0.05478 -0.03066 -0.05798 44  LEU B CA  
4162 C C   . LEU B 58  ? 0.54435 0.43914 0.37747 -0.06158 -0.04410 -0.06109 44  LEU B C   
4163 O O   . LEU B 58  ? 0.50932 0.41937 0.32579 -0.06493 -0.05725 -0.05521 44  LEU B O   
4164 C CB  . LEU B 58  ? 0.49242 0.37611 0.34114 -0.04328 -0.03207 -0.04106 44  LEU B CB  
4165 C CG  . LEU B 58  ? 0.50931 0.38565 0.36263 -0.03760 -0.02009 -0.03763 44  LEU B CG  
4166 C CD1 . LEU B 58  ? 0.48649 0.36630 0.34653 -0.03047 -0.02440 -0.02269 44  LEU B CD1 
4167 C CD2 . LEU B 58  ? 0.50934 0.37805 0.38726 -0.03519 -0.00958 -0.04385 44  LEU B CD2 
4179 N N   . LYS B 59  ? 0.46713 0.35567 0.32437 -0.06381 -0.04075 -0.06867 45  LYS B N   
4180 C CA  . LYS B 59  ? 0.41865 0.31853 0.28777 -0.07043 -0.05198 -0.07041 45  LYS B CA  
4181 C C   . LYS B 59  ? 0.44532 0.34158 0.34646 -0.06328 -0.04922 -0.06053 45  LYS B C   
4182 O O   . LYS B 59  ? 0.40323 0.28416 0.31951 -0.05936 -0.03710 -0.06127 45  LYS B O   
4183 C CB  . LYS B 59  ? 0.43858 0.33440 0.30287 -0.08607 -0.04941 -0.09317 45  LYS B CB  
4184 C CG  . LYS B 59  ? 0.48483 0.39190 0.36837 -0.09495 -0.05934 -0.09610 45  LYS B CG  
4185 C CD  . LYS B 59  ? 0.46681 0.37062 0.34315 -0.11383 -0.05756 -0.12187 45  LYS B CD  
4186 C CE  . LYS B 59  ? 0.45622 0.36696 0.36028 -0.12378 -0.06371 -0.12548 45  LYS B CE  
4187 N NZ  . LYS B 59  ? 0.53185 0.42644 0.44035 -0.14145 -0.05437 -0.15303 45  LYS B NZ  
4201 N N   . PHE B 60  ? 0.42300 0.33551 0.33518 -0.06138 -0.06000 -0.05012 46  PHE B N   
4202 C CA  . PHE B 60  ? 0.37738 0.29110 0.31576 -0.05599 -0.05727 -0.04003 46  PHE B CA  
4203 C C   . PHE B 60  ? 0.41289 0.33850 0.36917 -0.06544 -0.06348 -0.04367 46  PHE B C   
4204 O O   . PHE B 60  ? 0.43047 0.37290 0.38041 -0.07209 -0.07525 -0.04766 46  PHE B O   
4205 C CB  . PHE B 60  ? 0.36160 0.28484 0.30016 -0.04453 -0.06058 -0.02496 46  PHE B CB  
4206 C CG  . PHE B 60  ? 0.43683 0.35017 0.35993 -0.03731 -0.05519 -0.02134 46  PHE B CG  
4207 C CD1 . PHE B 60  ? 0.39105 0.29563 0.32204 -0.03233 -0.04582 -0.01733 46  PHE B CD1 
4208 C CD2 . PHE B 60  ? 0.40765 0.32282 0.30946 -0.03641 -0.06000 -0.02019 46  PHE B CD2 
4209 C CE1 . PHE B 60  ? 0.39715 0.29583 0.31716 -0.02751 -0.04123 -0.01471 46  PHE B CE1 
4210 C CE2 . PHE B 60  ? 0.38993 0.29590 0.27984 -0.03148 -0.05377 -0.01658 46  PHE B CE2 
4211 C CZ  . PHE B 60  ? 0.43040 0.32855 0.33047 -0.02749 -0.04432 -0.01507 46  PHE B CZ  
4221 N N   . ILE B 61  ? 0.35198 0.27117 0.33186 -0.06671 -0.05602 -0.04055 47  ILE B N   
4222 C CA  . ILE B 61  ? 0.41110 0.34217 0.41278 -0.07604 -0.05974 -0.04149 47  ILE B CA  
4223 C C   . ILE B 61  ? 0.42064 0.35907 0.44075 -0.06884 -0.05518 -0.02527 47  ILE B C   
4224 O O   . ILE B 61  ? 0.39841 0.32852 0.41553 -0.05950 -0.04800 -0.01581 47  ILE B O   
4225 C CB  . ILE B 61  ? 0.39085 0.30483 0.40514 -0.08961 -0.05273 -0.05560 47  ILE B CB  
4226 C CG1 . ILE B 61  ? 0.43967 0.33020 0.46853 -0.08366 -0.03791 -0.04809 47  ILE B CG1 
4227 C CG2 . ILE B 61  ? 0.45437 0.36187 0.44650 -0.09883 -0.05512 -0.07589 47  ILE B CG2 
4228 C CD1 . ILE B 61  ? 0.49809 0.36815 0.54876 -0.09544 -0.02847 -0.05828 47  ILE B CD1 
4240 N N   . SER B 62  ? 0.41584 0.37322 0.45487 -0.07458 -0.05935 -0.02263 48  SER B N   
4241 C CA  . SER B 62  ? 0.39067 0.35535 0.44906 -0.07249 -0.05201 -0.00970 48  SER B CA  
4242 C C   . SER B 62  ? 0.46282 0.41430 0.54147 -0.08419 -0.04414 -0.01077 48  SER B C   
4243 O O   . SER B 62  ? 0.37808 0.33004 0.46697 -0.09758 -0.04785 -0.02289 48  SER B O   
4244 C CB  . SER B 62  ? 0.44377 0.43800 0.51581 -0.07162 -0.05797 -0.00549 48  SER B CB  
4245 O OG  . SER B 62  ? 0.41587 0.41893 0.50824 -0.07418 -0.04892 0.00424  48  SER B OG  
4251 N N   . THR B 63  ? 0.45035 0.39022 0.53526 -0.08000 -0.03354 0.00239  49  THR B N   
4252 C CA  . THR B 63  ? 0.47040 0.39636 0.57875 -0.08939 -0.02439 0.00743  49  THR B CA  
4253 C C   . THR B 63  ? 0.42767 0.37338 0.55440 -0.09388 -0.02032 0.02139  49  THR B C   
4254 O O   . THR B 63  ? 0.46534 0.40093 0.61085 -0.09995 -0.01095 0.03291  49  THR B O   
4255 C CB  . THR B 63  ? 0.42666 0.32906 0.53449 -0.08180 -0.01539 0.01752  49  THR B CB  
4256 O OG1 . THR B 63  ? 0.45503 0.37068 0.55348 -0.07129 -0.01398 0.03563  49  THR B OG1 
4257 C CG2 . THR B 63  ? 0.40342 0.28898 0.49467 -0.07701 -0.01695 0.00286  49  THR B CG2 
4265 N N   . THR B 64  ? 0.38635 0.36004 0.51009 -0.09086 -0.02587 0.02125  50  THR B N   
4266 C CA  . THR B 64  ? 0.37378 0.37009 0.51356 -0.09388 -0.01961 0.03318  50  THR B CA  
4267 C C   . THR B 64  ? 0.35379 0.37819 0.50951 -0.09912 -0.02662 0.02470  50  THR B C   
4268 O O   . THR B 64  ? 0.41961 0.46857 0.58682 -0.09776 -0.02135 0.03206  50  THR B O   
4269 C CB  . THR B 64  ? 0.39957 0.40586 0.52166 -0.08159 -0.01464 0.04463  50  THR B CB  
4270 O OG1 . THR B 64  ? 0.38613 0.39805 0.49039 -0.07087 -0.02255 0.03496  50  THR B OG1 
4271 C CG2 . THR B 64  ? 0.40788 0.39424 0.51886 -0.07762 -0.00913 0.05699  50  THR B CG2 
4279 N N   . GLY B 65  ? 0.44107 0.46548 0.59836 -0.10532 -0.03818 0.00960  51  GLY B N   
4280 C CA  . GLY B 65  ? 0.38307 0.43901 0.55699 -0.10945 -0.04816 0.00363  51  GLY B CA  
4281 C C   . GLY B 65  ? 0.37865 0.44857 0.53748 -0.09401 -0.05717 0.00311  51  GLY B C   
4282 O O   . GLY B 65  ? 0.39066 0.44422 0.52411 -0.08179 -0.05577 0.00500  51  GLY B O   
4286 N N   . LYS B 66  ? 0.35782 0.45968 0.53647 -0.09487 -0.06656 0.00165  52  LYS B N   
4287 C CA  . LYS B 66  ? 0.37692 0.49345 0.54914 -0.07965 -0.07537 0.00397  52  LYS B CA  
4288 C C   . LYS B 66  ? 0.37532 0.48203 0.53490 -0.06359 -0.06300 0.01130  52  LYS B C   
4289 O O   . LYS B 66  ? 0.33681 0.45086 0.50823 -0.06298 -0.04928 0.01679  52  LYS B O   
4290 C CB  . LYS B 66  ? 0.45168 0.60925 0.65882 -0.08094 -0.08343 0.00639  52  LYS B CB  
4291 C CG  . LYS B 66  ? 0.54202 0.71705 0.74714 -0.07099 -0.10059 0.00841  52  LYS B CG  
4292 C CD  . LYS B 66  ? 0.56639 0.73495 0.76392 -0.04931 -0.09413 0.01638  52  LYS B CD  
4293 C CE  . LYS B 66  ? 0.54354 0.73642 0.75433 -0.03787 -0.10942 0.02406  52  LYS B CE  
4294 N NZ  . LYS B 66  ? 0.61873 0.80897 0.80506 -0.04470 -0.12864 0.02204  52  LYS B NZ  
4308 N N   . LEU B 67  ? 0.39024 0.48092 0.52426 -0.05248 -0.06724 0.01058  53  LEU B N   
4309 C CA  . LEU B 67  ? 0.39366 0.47416 0.51465 -0.03950 -0.05641 0.01441  53  LEU B CA  
4310 C C   . LEU B 67  ? 0.38884 0.49417 0.53430 -0.02980 -0.05072 0.01764  53  LEU B C   
4311 O O   . LEU B 67  ? 0.38709 0.51518 0.55559 -0.02694 -0.06008 0.01929  53  LEU B O   
4312 C CB  . LEU B 67  ? 0.39838 0.45866 0.49199 -0.03098 -0.06249 0.01280  53  LEU B CB  
4313 C CG  . LEU B 67  ? 0.45286 0.48679 0.52094 -0.03715 -0.06376 0.00863  53  LEU B CG  
4314 C CD1 . LEU B 67  ? 0.42116 0.44023 0.46549 -0.02829 -0.06790 0.00825  53  LEU B CD1 
4315 C CD2 . LEU B 67  ? 0.42981 0.45111 0.49353 -0.04029 -0.05118 0.01149  53  LEU B CD2 
4327 N N   . PRO B 68  ? 0.37814 0.48167 0.52015 -0.02466 -0.03508 0.01825  54  PRO B N   
4328 C CA  . PRO B 68  ? 0.38052 0.50375 0.54468 -0.01385 -0.02601 0.01773  54  PRO B CA  
4329 C C   . PRO B 68  ? 0.37126 0.48310 0.52906 0.00139  -0.02817 0.01607  54  PRO B C   
4330 O O   . PRO B 68  ? 0.36281 0.48650 0.54167 0.01226  -0.01884 0.01440  54  PRO B O   
4331 C CB  . PRO B 68  ? 0.38072 0.50477 0.53650 -0.01776 -0.00715 0.01659  54  PRO B CB  
4332 C CG  . PRO B 68  ? 0.35719 0.45460 0.47839 -0.02289 -0.00902 0.01768  54  PRO B CG  
4333 C CD  . PRO B 68  ? 0.39820 0.48447 0.51704 -0.02930 -0.02451 0.01935  54  PRO B CD  
4341 N N   . VAL B 69  ? 0.39826 0.48666 0.52994 0.00237  -0.03824 0.01645  55  VAL B N   
4342 C CA  . VAL B 69  ? 0.39879 0.47360 0.52469 0.01542  -0.04032 0.01724  55  VAL B CA  
4343 C C   . VAL B 69  ? 0.35452 0.42279 0.46852 0.01436  -0.05852 0.02286  55  VAL B C   
4344 O O   . VAL B 69  ? 0.36996 0.43453 0.46908 0.00262  -0.06637 0.02130  55  VAL B O   
4345 C CB  . VAL B 69  ? 0.41591 0.46593 0.51480 0.01669  -0.02891 0.01077  55  VAL B CB  
4346 C CG1 . VAL B 69  ? 0.40158 0.46113 0.50758 0.01656  -0.01056 0.00365  55  VAL B CG1 
4347 C CG2 . VAL B 69  ? 0.38878 0.42226 0.45814 0.00600  -0.03348 0.01049  55  VAL B CG2 
4357 N N   . PRO B 70  ? 0.41902 0.48526 0.53931 0.02631  -0.06444 0.02967  56  PRO B N   
4358 C CA  . PRO B 70  ? 0.31327 0.37710 0.41859 0.02449  -0.08196 0.03709  56  PRO B CA  
4359 C C   . PRO B 70  ? 0.35741 0.39265 0.42412 0.01788  -0.08087 0.03232  56  PRO B C   
4360 O O   . PRO B 70  ? 0.34575 0.36032 0.40014 0.02092  -0.06895 0.02791  56  PRO B O   
4361 C CB  . PRO B 70  ? 0.38060 0.44704 0.50414 0.04086  -0.08531 0.04923  56  PRO B CB  
4362 C CG  . PRO B 70  ? 0.38755 0.46483 0.54578 0.05093  -0.07068 0.04630  56  PRO B CG  
4363 C CD  . PRO B 70  ? 0.40112 0.46762 0.54426 0.04192  -0.05470 0.03177  56  PRO B CD  
4371 N N   . TRP B 71  ? 0.33185 0.36818 0.38064 0.00788  -0.09293 0.03189  57  TRP B N   
4372 C CA  . TRP B 71  ? 0.38989 0.40173 0.40530 0.00217  -0.09100 0.02716  57  TRP B CA  
4373 C C   . TRP B 71  ? 0.34637 0.33919 0.34860 0.01157  -0.08749 0.03339  57  TRP B C   
4374 O O   . TRP B 71  ? 0.33893 0.31127 0.32440 0.00981  -0.07786 0.02782  57  TRP B O   
4375 C CB  . TRP B 71  ? 0.38862 0.40682 0.38758 -0.00944 -0.10379 0.02435  57  TRP B CB  
4376 C CG  . TRP B 71  ? 0.38000 0.40360 0.38460 -0.02282 -0.10291 0.01334  57  TRP B CG  
4377 C CD1 . TRP B 71  ? 0.37512 0.42302 0.39858 -0.03110 -0.11201 0.01133  57  TRP B CD1 
4378 C CD2 . TRP B 71  ? 0.32689 0.33077 0.32182 -0.02974 -0.09203 0.00404  57  TRP B CD2 
4379 N NE1 . TRP B 71  ? 0.34309 0.38393 0.36851 -0.04371 -0.10617 0.00032  57  TRP B NE1 
4380 C CE2 . TRP B 71  ? 0.37250 0.38583 0.38136 -0.04191 -0.09385 -0.00306 57  TRP B CE2 
4381 C CE3 . TRP B 71  ? 0.36400 0.34469 0.34321 -0.02682 -0.08124 0.00225  57  TRP B CE3 
4382 C CZ2 . TRP B 71  ? 0.37122 0.36778 0.37964 -0.04972 -0.08416 -0.01031 57  TRP B CZ2 
4383 C CZ3 . TRP B 71  ? 0.34370 0.31233 0.32306 -0.03374 -0.07323 -0.00404 57  TRP B CZ3 
4384 C CH2 . TRP B 71  ? 0.36941 0.34413 0.36363 -0.04435 -0.07421 -0.00951 57  TRP B CH2 
4395 N N   . PRO B 72  ? 0.30940 0.30811 0.32045 0.02113  -0.09473 0.04607  58  PRO B N   
4396 C CA  . PRO B 72  ? 0.37636 0.35274 0.37623 0.02873  -0.08971 0.05305  58  PRO B CA  
4397 C C   . PRO B 72  ? 0.37789 0.33507 0.38209 0.03251  -0.07260 0.04432  58  PRO B C   
4398 O O   . PRO B 72  ? 0.40552 0.34088 0.39402 0.03247  -0.06650 0.04426  58  PRO B O   
4399 C CB  . PRO B 72  ? 0.35801 0.34751 0.37959 0.04086  -0.09913 0.07085  58  PRO B CB  
4400 C CG  . PRO B 72  ? 0.37047 0.39168 0.39860 0.03466  -0.11543 0.07389  58  PRO B CG  
4401 C CD  . PRO B 72  ? 0.34739 0.37458 0.37991 0.02464  -0.10908 0.05681  58  PRO B CD  
4409 N N   . THR B 73  ? 0.39788 0.36450 0.42170 0.03394  -0.06432 0.03626  59  THR B N   
4410 C CA  . THR B 73  ? 0.41872 0.37132 0.44310 0.03522  -0.04841 0.02598  59  THR B CA  
4411 C C   . THR B 73  ? 0.41954 0.36407 0.41996 0.02390  -0.04398 0.01674  59  THR B C   
4412 O O   . THR B 73  ? 0.41189 0.34612 0.40665 0.02241  -0.03329 0.00869  59  THR B O   
4413 C CB  . THR B 73  ? 0.44732 0.41609 0.49892 0.04003  -0.03946 0.02046  59  THR B CB  
4414 O OG1 . THR B 73  ? 0.38011 0.36770 0.43244 0.03113  -0.04191 0.01727  59  THR B OG1 
4415 C CG2 . THR B 73  ? 0.44118 0.42150 0.52439 0.05333  -0.04360 0.03110  59  THR B CG2 
4423 N N   . LEU B 74  ? 0.39343 0.34321 0.38169 0.01573  -0.05177 0.01742  60  LEU B N   
4424 C CA  . LEU B 74  ? 0.38123 0.32408 0.35277 0.00715  -0.04788 0.01164  60  LEU B CA  
4425 C C   . LEU B 74  ? 0.38355 0.31121 0.33436 0.00424  -0.05033 0.01290  60  LEU B C   
4426 O O   . LEU B 74  ? 0.33301 0.25489 0.27384 -0.00097 -0.04608 0.00904  60  LEU B O   
4427 C CB  . LEU B 74  ? 0.36034 0.31559 0.33709 0.00005  -0.05108 0.01041  60  LEU B CB  
4428 C CG  . LEU B 74  ? 0.41043 0.38369 0.40831 0.00055  -0.04735 0.01008  60  LEU B CG  
4429 C CD1 . LEU B 74  ? 0.45954 0.44153 0.46367 -0.00839 -0.05028 0.01013  60  LEU B CD1 
4430 C CD2 . LEU B 74  ? 0.42449 0.39775 0.42121 0.00133  -0.03532 0.00607  60  LEU B CD2 
4442 N N   . VAL B 75  ? 0.38755 0.31098 0.33299 0.00763  -0.05670 0.01981  61  VAL B N   
4443 C CA  . VAL B 75  ? 0.34258 0.25422 0.26645 0.00361  -0.05777 0.02150  61  VAL B CA  
4444 C C   . VAL B 75  ? 0.39544 0.29315 0.31289 0.00193  -0.04771 0.01744  61  VAL B C   
4445 O O   . VAL B 75  ? 0.41627 0.31117 0.32410 -0.00379 -0.04450 0.01298  61  VAL B O   
4446 C CB  . VAL B 75  ? 0.42394 0.33456 0.34261 0.00805  -0.06531 0.03349  61  VAL B CB  
4447 C CG1 . VAL B 75  ? 0.47983 0.37675 0.37529 0.00379  -0.06243 0.03635  61  VAL B CG1 
4448 C CG2 . VAL B 75  ? 0.38012 0.31019 0.30039 0.00597  -0.07828 0.03684  61  VAL B CG2 
4458 N N   . THR B 76  ? 0.36392 0.25350 0.28951 0.00657  -0.04212 0.01820  62  THR B N   
4459 C CA  . THR B 76  ? 0.38788 0.26578 0.30787 0.00249  -0.03356 0.01321  62  THR B CA  
4460 C C   . THR B 76  ? 0.36675 0.25427 0.28631 -0.00347 -0.03034 0.00499  62  THR B C   
4461 O O   . THR B 76  ? 0.39958 0.28453 0.31267 -0.00892 -0.02687 0.00250  62  THR B O   
4462 C CB  . THR B 76  ? 0.39008 0.25649 0.32175 0.00691  -0.02667 0.01162  62  THR B CB  
4463 O OG1 . THR B 76  ? 0.39914 0.27594 0.34537 0.01033  -0.02381 0.00499  62  THR B OG1 
4464 C CG2 . THR B 76  ? 0.42763 0.28289 0.36313 0.01432  -0.02985 0.02483  62  THR B CG2 
4472 N N   . THR B 77  ? 0.37436 0.27523 0.30256 -0.00268 -0.03156 0.00278  63  THR B N   
4473 C CA  . THR B 77  ? 0.38758 0.29933 0.31548 -0.00796 -0.02942 -0.00032 63  THR B CA  
4474 C C   . THR B 77  ? 0.42858 0.34137 0.35311 -0.01055 -0.03268 0.00304  63  THR B C   
4475 O O   . THR B 77  ? 0.38488 0.30023 0.30809 -0.01387 -0.03055 0.00340  63  THR B O   
4476 C CB  . THR B 77  ? 0.38302 0.30855 0.32085 -0.00705 -0.02793 -0.00172 63  THR B CB  
4477 O OG1 . THR B 77  ? 0.31704 0.24062 0.25969 -0.00435 -0.02163 -0.00803 63  THR B OG1 
4478 C CG2 . THR B 77  ? 0.39118 0.32957 0.32724 -0.01274 -0.02646 -0.00043 63  THR B CG2 
4486 N N   . LEU B 78  ? 0.39994 0.31185 0.32510 -0.00938 -0.03751 0.00477  64  LEU B N   
4487 C CA  . LEU B 78  ? 0.39652 0.30615 0.31949 -0.01258 -0.03824 0.00401  64  LEU B CA  
4488 C C   . LEU B 78  ? 0.47805 0.37804 0.38935 -0.01381 -0.03505 0.00275  64  LEU B C   
4489 O O   . LEU B 78  ? 0.44532 0.34368 0.35853 -0.01563 -0.03097 0.00095  64  LEU B O   
4490 C CB  . LEU B 78  ? 0.38773 0.29998 0.31215 -0.01391 -0.04434 0.00270  64  LEU B CB  
4491 C CG  . LEU B 78  ? 0.34809 0.27219 0.28815 -0.01431 -0.04635 0.00398  64  LEU B CG  
4492 C CD1 . LEU B 78  ? 0.37002 0.30089 0.31293 -0.01633 -0.05449 0.00272  64  LEU B CD1 
4493 C CD2 . LEU B 78  ? 0.45357 0.37852 0.40312 -0.01796 -0.04197 0.00490  64  LEU B CD2 
4528 N N   . VAL B 80  ? 0.35467 0.24525 0.25626 -0.02180 -0.01449 0.00224  66  VAL B N   
4529 C CA  . VAL B 80  ? 0.37675 0.27221 0.28510 -0.02378 -0.00722 0.00129  66  VAL B CA  
4530 C C   . VAL B 80  ? 0.38427 0.27272 0.28273 -0.02839 -0.00112 0.00219  66  VAL B C   
4531 O O   . VAL B 80  ? 0.38055 0.26405 0.26837 -0.02963 0.00493  0.00119  66  VAL B O   
4532 C CB  . VAL B 80  ? 0.40196 0.29579 0.31243 -0.02129 -0.00338 -0.00245 66  VAL B CB  
4533 C CG1 . VAL B 80  ? 0.39050 0.29136 0.31861 -0.01748 -0.00679 -0.00051 66  VAL B CG1 
4534 C CG2 . VAL B 80  ? 0.39120 0.27470 0.28130 -0.02243 -0.00555 -0.00575 66  VAL B CG2 
4543 N N   . GLN B 81  ? 0.38626 0.27410 0.28779 -0.03231 -0.00153 0.00339  67  GLN B N   
4544 C CA  . GLN B 81  ? 0.45186 0.33043 0.34714 -0.03803 0.00500  0.00585  67  GLN B CA  
4545 C C   . GLN B 81  ? 0.43629 0.32523 0.34075 -0.04287 0.01396  0.00496  67  GLN B C   
4546 O O   . GLN B 81  ? 0.41085 0.29339 0.31096 -0.04906 0.02136  0.00776  67  GLN B O   
4547 C CB  . GLN B 81  ? 0.42001 0.29249 0.32012 -0.04211 0.00360  0.00443  67  GLN B CB  
4548 C CG  . GLN B 81  ? 0.47363 0.33365 0.36764 -0.03611 -0.00177 0.00611  67  GLN B CG  
4549 C CD  . GLN B 81  ? 0.42441 0.27743 0.32634 -0.03954 -0.00036 0.00057  67  GLN B CD  
4550 O OE1 . GLN B 81  ? 0.52071 0.38387 0.43082 -0.04737 0.00128  -0.00711 67  GLN B OE1 
4551 N NE2 . GLN B 81  ? 0.50228 0.33927 0.40327 -0.03400 -0.00079 0.00379  67  GLN B NE2 
4560 N N   . CYS B 82  ? 0.43214 0.33712 0.35210 -0.03980 0.01443  0.00265  68  CYS B N   
4561 C CA  . CYS B 82  ? 0.36420 0.28102 0.29773 -0.04191 0.02451  0.00205  68  CYS B CA  
4562 C C   . CYS B 82  ? 0.43080 0.33782 0.34839 -0.04145 0.03497  0.00003  68  CYS B C   
4563 O O   . CYS B 82  ? 0.40584 0.32143 0.33276 -0.04382 0.04688  -0.00157 68  CYS B O   
4564 C CB  . CYS B 82  ? 0.37320 0.30918 0.33198 -0.03610 0.02228  0.00266  68  CYS B CB  
4565 S SG  . CYS B 82  ? 0.35330 0.28131 0.30922 -0.02648 0.01689  0.00172  68  CYS B SG  
4571 N N   . PHE B 83  ? 0.43359 0.32610 0.32753 -0.03937 0.03104  -0.00031 69  PHE B N   
4572 C CA  . PHE B 83  ? 0.46591 0.35183 0.33784 -0.04143 0.03935  -0.00300 69  PHE B CA  
4573 C C   . PHE B 83  ? 0.44861 0.32414 0.29735 -0.04750 0.04054  0.00596  69  PHE B C   
4574 O O   . PHE B 83  ? 0.46566 0.33782 0.28970 -0.05066 0.04555  0.00637  69  PHE B O   
4575 C CB  . PHE B 83  ? 0.40962 0.29054 0.26987 -0.03738 0.03321  -0.00905 69  PHE B CB  
4576 C CG  . PHE B 83  ? 0.41267 0.29937 0.29506 -0.03211 0.03674  -0.01743 69  PHE B CG  
4577 C CD1 . PHE B 83  ? 0.44149 0.33056 0.32917 -0.03224 0.05172  -0.02684 69  PHE B CD1 
4578 C CD2 . PHE B 83  ? 0.42794 0.31720 0.32759 -0.02682 0.02677  -0.01515 69  PHE B CD2 
4579 C CE1 . PHE B 83  ? 0.44413 0.33531 0.35780 -0.02581 0.05649  -0.03315 69  PHE B CE1 
4580 C CE2 . PHE B 83  ? 0.36410 0.25681 0.28679 -0.02144 0.03040  -0.01899 69  PHE B CE2 
4581 C CZ  . PHE B 83  ? 0.44492 0.33722 0.37662 -0.02023 0.04515  -0.02765 69  PHE B CZ  
4591 N N   . ALA B 84  ? 0.43760 0.30773 0.29343 -0.04988 0.03661  0.01330  70  ALA B N   
4592 C CA  . ALA B 84  ? 0.45186 0.30916 0.29165 -0.05529 0.03976  0.02463  70  ALA B CA  
4593 C C   . ALA B 84  ? 0.49869 0.36116 0.33350 -0.06325 0.05561  0.02606  70  ALA B C   
4594 O O   . ALA B 84  ? 0.52336 0.39973 0.37881 -0.06543 0.06413  0.01885  70  ALA B O   
4595 C CB  . ALA B 84  ? 0.49864 0.34672 0.35370 -0.05740 0.03612  0.02853  70  ALA B CB  
4601 N N   . ARG B 85  ? 0.49183 0.34579 0.30011 -0.06753 0.05973  0.03693  71  ARG B N   
4602 C CA  . ARG B 85  ? 0.53145 0.38984 0.33187 -0.07681 0.07664  0.04073  71  ARG B CA  
4603 C C   . ARG B 85  ? 0.48616 0.33657 0.30476 -0.08424 0.08168  0.04965  71  ARG B C   
4604 O O   . ARG B 85  ? 0.52903 0.36110 0.34120 -0.08517 0.07680  0.06335  71  ARG B O   
4605 C CB  . ARG B 85  ? 0.57024 0.42501 0.33127 -0.08025 0.07879  0.05099  71  ARG B CB  
4606 C CG  . ARG B 85  ? 0.65314 0.51311 0.40151 -0.09128 0.09820  0.05687  71  ARG B CG  
4607 C CD  . ARG B 85  ? 0.71200 0.57233 0.41541 -0.09607 0.09927  0.06813  71  ARG B CD  
4608 N NE  . ARG B 85  ? 0.80430 0.64944 0.49605 -0.09864 0.09395  0.09460  71  ARG B NE  
4609 C CZ  . ARG B 85  ? 0.90946 0.74892 0.59927 -0.10825 0.10768  0.11033  71  ARG B CZ  
4610 N NH1 . ARG B 85  ? 0.74156 0.59231 0.44043 -0.11697 0.12768  0.10161  71  ARG B NH1 
4611 N NH2 . ARG B 85  ? 0.97414 0.79632 0.65623 -0.10890 0.10205  0.13659  71  ARG B NH2 
4625 N N   . TYR B 86  ? 0.53245 0.39698 0.37721 -0.08971 0.09157  0.04186  72  TYR B N   
4626 C CA  . TYR B 86  ? 0.51606 0.37622 0.37943 -0.10062 0.09842  0.04767  72  TYR B CA  
4627 C C   . TYR B 86  ? 0.52757 0.39295 0.38213 -0.11100 0.11753  0.05517  72  TYR B C   
4628 O O   . TYR B 86  ? 0.55613 0.44279 0.41823 -0.11148 0.12881  0.04606  72  TYR B O   
4629 C CB  . TYR B 86  ? 0.47912 0.35733 0.37891 -0.10247 0.09543  0.03527  72  TYR B CB  
4630 C CG  . TYR B 86  ? 0.44375 0.31338 0.35258 -0.09871 0.07968  0.03072  72  TYR B CG  
4631 C CD1 . TYR B 86  ? 0.44771 0.31768 0.34913 -0.08645 0.06695  0.02589  72  TYR B CD1 
4632 C CD2 . TYR B 86  ? 0.44921 0.31060 0.37423 -0.10891 0.07926  0.02961  72  TYR B CD2 
4633 C CE1 . TYR B 86  ? 0.45314 0.31743 0.36170 -0.08366 0.05492  0.02123  72  TYR B CE1 
4634 C CE2 . TYR B 86  ? 0.42817 0.28245 0.35929 -0.10655 0.06745  0.02235  72  TYR B CE2 
4635 C CZ  . TYR B 86  ? 0.46446 0.32126 0.38668 -0.09351 0.05566  0.01873  72  TYR B CZ  
4636 O OH  . TYR B 86  ? 0.42601 0.27787 0.35327 -0.09176 0.04611  0.01106  72  TYR B OH  
4646 N N   . PRO B 87  ? 0.60300 0.44997 0.44331 -0.11905 0.12329  0.07237  73  PRO B N   
4647 C CA  . PRO B 87  ? 0.63151 0.48517 0.46342 -0.13087 0.14340  0.08110  73  PRO B CA  
4648 C C   . PRO B 87  ? 0.64121 0.51619 0.51069 -0.14004 0.15556  0.07073  73  PRO B C   
4649 O O   . PRO B 87  ? 0.61645 0.49799 0.51767 -0.13999 0.14695  0.06043  73  PRO B O   
4650 C CB  . PRO B 87  ? 0.67127 0.49734 0.49095 -0.13770 0.14457  0.10420  73  PRO B CB  
4651 C CG  . PRO B 87  ? 0.65703 0.46483 0.46527 -0.12506 0.12499  0.10867  73  PRO B CG  
4652 C CD  . PRO B 87  ? 0.61497 0.43386 0.44624 -0.11664 0.11297  0.08670  73  PRO B CD  
4660 N N   . ASP B 88  ? 0.80842 0.69770 0.67374 -0.14887 0.17601  0.07392  74  ASP B N   
4661 C CA  . ASP B 88  ? 0.78876 0.70469 0.69312 -0.15720 0.18927  0.06485  74  ASP B CA  
4662 C C   . ASP B 88  ? 0.71052 0.62066 0.64732 -0.16905 0.18500  0.06706  74  ASP B C   
4663 O O   . ASP B 88  ? 0.65247 0.58475 0.62662 -0.17054 0.17994  0.05457  74  ASP B O   
4664 C CB  . ASP B 88  ? 0.85812 0.78687 0.75062 -0.16707 0.21487  0.07094  74  ASP B CB  
4665 C CG  . ASP B 88  ? 1.07804 1.02204 0.95011 -0.15737 0.22337  0.05912  74  ASP B CG  
4666 O OD1 . ASP B 88  ? 0.97015 0.91533 0.84374 -0.14319 0.20944  0.04624  74  ASP B OD1 
4667 O OD2 . ASP B 88  ? 1.07617 1.03039 0.93068 -0.16499 0.24542  0.06183  74  ASP B OD2 
4672 N N   . HIS B 89  ? 0.73280 0.61364 0.65673 -0.17824 0.18685  0.08312  75  HIS B N   
4673 C CA  . HIS B 89  ? 0.76496 0.63635 0.71993 -0.19254 0.18625  0.08279  75  HIS B CA  
4674 C C   . HIS B 89  ? 0.71425 0.57778 0.68301 -0.18622 0.16535  0.06951  75  HIS B C   
4675 O O   . HIS B 89  ? 0.72277 0.58258 0.71849 -0.19923 0.16381  0.06294  75  HIS B O   
4676 C CB  . HIS B 89  ? 0.82955 0.66656 0.76942 -0.20326 0.19598  0.10498  75  HIS B CB  
4677 C CG  . HIS B 89  ? 0.90062 0.70218 0.81620 -0.19171 0.18198  0.11579  75  HIS B CG  
4678 N ND1 . HIS B 89  ? 0.95966 0.75676 0.83637 -0.17764 0.17601  0.12629  75  HIS B ND1 
4679 C CD2 . HIS B 89  ? 0.86186 0.63319 0.78963 -0.19190 0.17299  0.11681  75  HIS B CD2 
4680 C CE1 . HIS B 89  ? 0.96237 0.72994 0.83063 -0.16907 0.16325  0.13583  75  HIS B CE1 
4681 N NE2 . HIS B 89  ? 0.91513 0.66461 0.81438 -0.17689 0.16272  0.13007  75  HIS B NE2 
4689 N N   . MET B 90  ? 0.65229 0.51430 0.60301 -0.16845 0.15035  0.06421  76  MET B N   
4690 C CA  . MET B 90  ? 0.60435 0.46137 0.56486 -0.16208 0.13198  0.05195  76  MET B CA  
4691 C C   . MET B 90  ? 0.59819 0.48890 0.57393 -0.15334 0.12227  0.03690  76  MET B C   
4692 O O   . MET B 90  ? 0.55539 0.44612 0.53492 -0.14709 0.10687  0.02771  76  MET B O   
4693 C CB  . MET B 90  ? 0.62410 0.45127 0.55593 -0.14872 0.12156  0.06011  76  MET B CB  
4694 C CG  . MET B 90  ? 0.63612 0.42687 0.56006 -0.15470 0.12761  0.07706  76  MET B CG  
4695 S SD  . MET B 90  ? 0.63940 0.40173 0.53915 -0.13661 0.11331  0.08756  76  MET B SD  
4696 C CE  . MET B 90  ? 0.52230 0.28943 0.44280 -0.13134 0.09845  0.06333  76  MET B CE  
4706 N N   . LYS B 91  ? 0.63015 0.54955 0.61630 -0.15237 0.13210  0.03514  77  LYS B N   
4707 C CA  . LYS B 91  ? 0.61752 0.56639 0.62101 -0.14130 0.12376  0.02460  77  LYS B CA  
4708 C C   . LYS B 91  ? 0.57017 0.53965 0.60516 -0.14795 0.11108  0.01554  77  LYS B C   
4709 O O   . LYS B 91  ? 0.56256 0.54701 0.60460 -0.13769 0.09731  0.00984  77  LYS B O   
4710 C CB  . LYS B 91  ? 0.64342 0.61901 0.66055 -0.13956 0.14019  0.02398  77  LYS B CB  
4711 C CG  . LYS B 91  ? 0.76614 0.74085 0.76409 -0.12290 0.14155  0.02065  77  LYS B CG  
4712 C CD  . LYS B 91  ? 0.73677 0.68346 0.68932 -0.12238 0.14780  0.02816  77  LYS B CD  
4713 C CE  . LYS B 91  ? 0.80643 0.75241 0.73848 -0.10876 0.14784  0.02106  77  LYS B CE  
4714 N NZ  . LYS B 91  ? 0.80043 0.72959 0.68808 -0.11156 0.15640  0.02772  77  LYS B NZ  
4728 N N   . ARG B 92  ? 0.51801 0.48963 0.57140 -0.16653 0.11541  0.01433  78  ARG B N   
4729 C CA  . ARG B 92  ? 0.53065 0.52483 0.61079 -0.17673 0.10266  0.00364  78  ARG B CA  
4730 C C   . ARG B 92  ? 0.51594 0.48896 0.57866 -0.17347 0.08698  -0.00366 78  ARG B C   
4731 O O   . ARG B 92  ? 0.50361 0.49758 0.58156 -0.18088 0.07457  -0.01414 78  ARG B O   
4732 C CB  . ARG B 92  ? 0.68298 0.68203 0.78628 -0.20058 0.11245  0.00172  78  ARG B CB  
4733 C CG  . ARG B 92  ? 0.73452 0.76768 0.86632 -0.20630 0.12697  0.00647  78  ARG B CG  
4734 C CD  . ARG B 92  ? 0.78842 0.81790 0.93820 -0.23097 0.14053  0.00742  78  ARG B CD  
4735 N NE  . ARG B 92  ? 0.88485 0.91180 1.04731 -0.24875 0.12908  -0.00526 78  ARG B NE  
4736 C CZ  . ARG B 92  ? 0.92170 0.90442 1.06565 -0.25621 0.12935  -0.00821 78  ARG B CZ  
4737 N NH1 . ARG B 92  ? 0.93807 0.87678 1.05131 -0.24665 0.13830  0.00441  78  ARG B NH1 
4738 N NH2 . ARG B 92  ? 0.84593 0.82984 1.00378 -0.27393 0.12061  -0.02438 78  ARG B NH2 
4752 N N   . HIS B 93  ? 0.52538 0.46104 0.55719 -0.16302 0.08732  0.00168  79  HIS B N   
4753 C CA  . HIS B 93  ? 0.51279 0.42722 0.53028 -0.15875 0.07554  -0.00510 79  HIS B CA  
4754 C C   . HIS B 93  ? 0.44180 0.35890 0.44239 -0.13877 0.06484  -0.00358 79  HIS B C   
4755 O O   . HIS B 93  ? 0.48958 0.38638 0.47493 -0.13216 0.05755  -0.00631 79  HIS B O   
4756 C CB  . HIS B 93  ? 0.50110 0.37104 0.50349 -0.16202 0.08362  0.00102  79  HIS B CB  
4757 C CG  . HIS B 93  ? 0.55426 0.41505 0.57418 -0.18267 0.09603  0.00073  79  HIS B CG  
4758 N ND1 . HIS B 93  ? 0.59784 0.47030 0.64037 -0.20089 0.09335  -0.01546 79  HIS B ND1 
4759 C CD2 . HIS B 93  ? 0.61102 0.45276 0.62899 -0.18972 0.11156  0.01481  79  HIS B CD2 
4760 C CE1 . HIS B 93  ? 0.63294 0.49211 0.68963 -0.21861 0.10712  -0.01255 79  HIS B CE1 
4761 N NE2 . HIS B 93  ? 0.72742 0.56727 0.76983 -0.21173 0.11882  0.00718  79  HIS B NE2 
4769 N N   . ASP B 94  ? 0.44134 0.43816 0.46232 -0.11480 -0.00707 0.07666  80  ASP B N   
4770 C CA  . ASP B 94  ? 0.38481 0.37956 0.38171 -0.10172 -0.00881 0.06918  80  ASP B CA  
4771 C C   . ASP B 94  ? 0.36409 0.36053 0.36468 -0.10001 -0.02183 0.05839  80  ASP B C   
4772 O O   . ASP B 94  ? 0.41091 0.42659 0.42489 -0.09622 -0.02250 0.05654  80  ASP B O   
4773 C CB  . ASP B 94  ? 0.39874 0.41373 0.39341 -0.09324 0.00322  0.07231  80  ASP B CB  
4774 C CG  . ASP B 94  ? 0.35851 0.36749 0.32961 -0.08095 0.00208  0.06438  80  ASP B CG  
4775 O OD1 . ASP B 94  ? 0.34897 0.34252 0.31054 -0.07888 -0.00787 0.05733  80  ASP B OD1 
4776 O OD2 . ASP B 94  ? 0.35861 0.37911 0.32139 -0.07354 0.01143  0.06462  80  ASP B OD2 
4781 N N   . PHE B 95  ? 0.37104 0.34770 0.35911 -0.10178 -0.03181 0.05186  81  PHE B N   
4782 C CA  . PHE B 95  ? 0.37294 0.35101 0.35774 -0.09894 -0.04387 0.04336  81  PHE B CA  
4783 C C   . PHE B 95  ? 0.39352 0.37573 0.36664 -0.08658 -0.04168 0.04227  81  PHE B C   
4784 O O   . PHE B 95  ? 0.40180 0.39722 0.38399 -0.08254 -0.04690 0.04112  81  PHE B O   
4785 C CB  . PHE B 95  ? 0.40192 0.35806 0.37089 -0.10189 -0.05227 0.03586  81  PHE B CB  
4786 C CG  . PHE B 95  ? 0.42425 0.38045 0.37959 -0.09621 -0.06224 0.02888  81  PHE B CG  
4787 C CD1 . PHE B 95  ? 0.36327 0.31111 0.29821 -0.08625 -0.05908 0.02874  81  PHE B CD1 
4788 C CD2 . PHE B 95  ? 0.42199 0.38799 0.38555 -0.10095 -0.07499 0.02338  81  PHE B CD2 
4789 C CE1 . PHE B 95  ? 0.47357 0.42207 0.39594 -0.08096 -0.06625 0.02570  81  PHE B CE1 
4790 C CE2 . PHE B 95  ? 0.47557 0.44330 0.42278 -0.09469 -0.08391 0.01952  81  PHE B CE2 
4791 C CZ  . PHE B 95  ? 0.41431 0.37282 0.34054 -0.08462 -0.07843 0.02191  81  PHE B CZ  
4801 N N   . PHE B 96  ? 0.38965 0.36072 0.34540 -0.08046 -0.03471 0.04287  82  PHE B N   
4802 C CA  . PHE B 96  ? 0.35845 0.32912 0.30512 -0.07012 -0.03383 0.03997  82  PHE B CA  
4803 C C   . PHE B 96  ? 0.37791 0.36827 0.34172 -0.06488 -0.03065 0.04042  82  PHE B C   
4804 O O   . PHE B 96  ? 0.34429 0.33712 0.31190 -0.05874 -0.03494 0.03888  82  PHE B O   
4805 C CB  . PHE B 96  ? 0.37660 0.33644 0.30737 -0.06563 -0.02734 0.03971  82  PHE B CB  
4806 C CG  . PHE B 96  ? 0.38482 0.32607 0.30286 -0.06940 -0.02917 0.04016  82  PHE B CG  
4807 C CD1 . PHE B 96  ? 0.38008 0.30792 0.28683 -0.06712 -0.03408 0.03566  82  PHE B CD1 
4808 C CD2 . PHE B 96  ? 0.44985 0.38722 0.36866 -0.07449 -0.02483 0.04605  82  PHE B CD2 
4809 C CE1 . PHE B 96  ? 0.42413 0.33522 0.32156 -0.06918 -0.03476 0.03456  82  PHE B CE1 
4810 C CE2 . PHE B 96  ? 0.45491 0.37345 0.36570 -0.07677 -0.02649 0.04656  82  PHE B CE2 
4811 C CZ  . PHE B 96  ? 0.43378 0.33926 0.33434 -0.07376 -0.03152 0.03956  82  PHE B CZ  
4821 N N   . LYS B 97  ? 0.38246 0.38718 0.35790 -0.06653 -0.02214 0.04339  83  LYS B N   
4822 C CA  . LYS B 97  ? 0.35059 0.37515 0.34417 -0.06028 -0.01728 0.04216  83  LYS B CA  
4823 C C   . LYS B 97  ? 0.34334 0.38292 0.36117 -0.06336 -0.02475 0.04432  83  LYS B C   
4824 O O   . LYS B 97  ? 0.35697 0.40733 0.38935 -0.05571 -0.02632 0.04293  83  LYS B O   
4825 C CB  . LYS B 97  ? 0.41340 0.45135 0.40939 -0.05997 -0.00376 0.04448  83  LYS B CB  
4826 C CG  . LYS B 97  ? 0.32447 0.35348 0.29664 -0.05417 0.00232  0.04110  83  LYS B CG  
4827 C CD  . LYS B 97  ? 0.38703 0.43349 0.35805 -0.05223 0.01598  0.04369  83  LYS B CD  
4828 C CE  . LYS B 97  ? 0.39547 0.43485 0.33930 -0.04706 0.01950  0.04113  83  LYS B CE  
4829 N NZ  . LYS B 97  ? 0.41758 0.43727 0.34616 -0.05278 0.01370  0.04809  83  LYS B NZ  
4843 N N   . SER B 98  ? 0.35388 0.39444 0.37880 -0.07429 -0.03040 0.04732  84  SER B N   
4844 C CA  . SER B 98  ? 0.34515 0.40346 0.39559 -0.07813 -0.03960 0.04836  84  SER B CA  
4845 C C   . SER B 98  ? 0.35998 0.41574 0.40549 -0.07151 -0.05251 0.04640  84  SER B C   
4846 O O   . SER B 98  ? 0.40780 0.48220 0.47528 -0.06904 -0.05966 0.04830  84  SER B O   
4847 C CB  . SER B 98  ? 0.42301 0.47926 0.48139 -0.09227 -0.04554 0.04909  84  SER B CB  
4848 O OG  . SER B 98  ? 0.38381 0.41796 0.41911 -0.09508 -0.05547 0.04405  84  SER B OG  
4854 N N   . ALA B 99  ? 0.32800 0.36252 0.34621 -0.06811 -0.05526 0.04421  85  ALA B N   
4855 C CA  . ALA B 99  ? 0.42980 0.46112 0.43984 -0.06166 -0.06548 0.04532  85  ALA B CA  
4856 C C   . ALA B 99  ? 0.42309 0.45718 0.44105 -0.04948 -0.06057 0.04815  85  ALA B C   
4857 O O   . ALA B 99  ? 0.34826 0.38165 0.36454 -0.04317 -0.06807 0.05275  85  ALA B O   
4858 C CB  . ALA B 99  ? 0.40885 0.41768 0.38841 -0.06304 -0.06811 0.04251  85  ALA B CB  
4864 N N   . MET B 100 ? 0.34569 0.38260 0.37199 -0.04574 -0.04824 0.04550  86  MET B N   
4865 C CA  . MET B 100 ? 0.38341 0.42035 0.41970 -0.03439 -0.04322 0.04467  86  MET B CA  
4866 C C   . MET B 100 ? 0.36223 0.42099 0.43030 -0.02868 -0.04522 0.04772  86  MET B C   
4867 O O   . MET B 100 ? 0.35360 0.43102 0.43811 -0.03407 -0.04638 0.04893  86  MET B O   
4868 C CB  . MET B 100 ? 0.37478 0.40703 0.40485 -0.03214 -0.03030 0.03720  86  MET B CB  
4869 C CG  . MET B 100 ? 0.35247 0.36419 0.35507 -0.03535 -0.02932 0.03472  86  MET B CG  
4870 S SD  . MET B 100 ? 0.39066 0.38400 0.38497 -0.02998 -0.03490 0.03701  86  MET B SD  
4871 C CE  . MET B 100 ? 0.40106 0.37668 0.36688 -0.03639 -0.03440 0.03514  86  MET B CE  
4881 N N   . PRO B 101 ? 0.28777 0.34483 0.36914 -0.01755 -0.04536 0.04948  87  PRO B N   
4882 C CA  . PRO B 101 ? 0.35066 0.38687 0.42169 -0.01129 -0.04278 0.04844  87  PRO B CA  
4883 C C   . PRO B 101 ? 0.37557 0.39915 0.43053 -0.01167 -0.05267 0.05820  87  PRO B C   
4884 O O   . PRO B 101 ? 0.37373 0.37947 0.41845 -0.00916 -0.04960 0.05866  87  PRO B O   
4885 C CB  . PRO B 101 ? 0.32310 0.36612 0.42479 0.00064  -0.03826 0.04669  87  PRO B CB  
4886 C CG  . PRO B 101 ? 0.30444 0.37023 0.42975 0.00234  -0.04575 0.05432  87  PRO B CG  
4887 C CD  . PRO B 101 ? 0.31389 0.39166 0.42933 -0.00994 -0.04740 0.05298  87  PRO B CD  
4895 N N   . GLU B 102 ? 0.34769 0.38153 0.40009 -0.01473 -0.06443 0.06579  88  GLU B N   
4896 C CA  . GLU B 102 ? 0.43698 0.46131 0.46946 -0.01380 -0.07290 0.07510  88  GLU B CA  
4897 C C   . GLU B 102 ? 0.37837 0.38364 0.38050 -0.01998 -0.06835 0.07039  88  GLU B C   
4898 O O   . GLU B 102 ? 0.38490 0.37793 0.37255 -0.01701 -0.06837 0.07706  88  GLU B O   
4899 C CB  . GLU B 102 ? 0.45515 0.49639 0.48568 -0.01680 -0.08788 0.08036  88  GLU B CB  
4900 C CG  . GLU B 102 ? 0.49116 0.55509 0.55513 -0.01031 -0.09445 0.08613  88  GLU B CG  
4901 C CD  . GLU B 102 ? 0.62400 0.70616 0.70912 -0.01702 -0.09223 0.07737  88  GLU B CD  
4902 O OE1 . GLU B 102 ? 0.46271 0.53725 0.54096 -0.02363 -0.08100 0.06803  88  GLU B OE1 
4903 O OE2 . GLU B 102 ? 0.84446 0.94999 0.95416 -0.01556 -0.10170 0.08119  88  GLU B OE2 
4910 N N   . GLY B 103 ? 0.39528 0.39861 0.38936 -0.02802 -0.06375 0.06052  89  GLY B N   
4911 C CA  . GLY B 103 ? 0.38721 0.37302 0.35771 -0.03225 -0.05863 0.05581  89  GLY B CA  
4912 C C   . GLY B 103 ? 0.36167 0.34372 0.30960 -0.03903 -0.06572 0.05474  89  GLY B C   
4913 O O   . GLY B 103 ? 0.35879 0.35239 0.30787 -0.04233 -0.07586 0.05549  89  GLY B O   
4917 N N   . TYR B 104 ? 0.38288 0.34894 0.31145 -0.04082 -0.06064 0.05134  90  TYR B N   
4918 C CA  . TYR B 104 ? 0.40025 0.35950 0.30685 -0.04619 -0.06506 0.04724  90  TYR B CA  
4919 C C   . TYR B 104 ? 0.42166 0.36704 0.30996 -0.04239 -0.05951 0.04904  90  TYR B C   
4920 O O   . TYR B 104 ? 0.39550 0.33450 0.29038 -0.03830 -0.05151 0.05146  90  TYR B O   
4921 C CB  . TYR B 104 ? 0.45241 0.40722 0.35920 -0.05441 -0.06294 0.03903  90  TYR B CB  
4922 C CG  . TYR B 104 ? 0.39509 0.34195 0.30487 -0.05333 -0.05246 0.03736  90  TYR B CG  
4923 C CD1 . TYR B 104 ? 0.43213 0.36468 0.32835 -0.05113 -0.04726 0.03562  90  TYR B CD1 
4924 C CD2 . TYR B 104 ? 0.38831 0.34443 0.31421 -0.05398 -0.04794 0.03727  90  TYR B CD2 
4925 C CE1 . TYR B 104 ? 0.43580 0.36375 0.33471 -0.04975 -0.04026 0.03371  90  TYR B CE1 
4926 C CE2 . TYR B 104 ? 0.40126 0.35255 0.32564 -0.05220 -0.03982 0.03514  90  TYR B CE2 
4927 C CZ  . TYR B 104 ? 0.44201 0.37934 0.35297 -0.05019 -0.03722 0.03329  90  TYR B CZ  
4928 O OH  . TYR B 104 ? 0.40601 0.34112 0.31554 -0.04804 -0.03161 0.03085  90  TYR B OH  
4938 N N   . VAL B 105 ? 0.40003 0.34213 0.26672 -0.04384 -0.06377 0.04670  91  VAL B N   
4939 C CA  . VAL B 105 ? 0.42781 0.35830 0.27613 -0.04086 -0.05676 0.04688  91  VAL B CA  
4940 C C   . VAL B 105 ? 0.44949 0.36790 0.29333 -0.04548 -0.05231 0.03633  91  VAL B C   
4941 O O   . VAL B 105 ? 0.44925 0.36649 0.29080 -0.05154 -0.05788 0.02815  91  VAL B O   
4942 C CB  . VAL B 105 ? 0.42529 0.36011 0.24945 -0.03836 -0.06233 0.04900  91  VAL B CB  
4943 C CG1 . VAL B 105 ? 0.45985 0.38423 0.26496 -0.03527 -0.05253 0.04785  91  VAL B CG1 
4944 C CG2 . VAL B 105 ? 0.45297 0.39981 0.28176 -0.03223 -0.06685 0.06351  91  VAL B CG2 
4954 N N   . GLN B 106 ? 0.42341 0.33296 0.26926 -0.04267 -0.04289 0.03700  92  GLN B N   
4955 C CA  . GLN B 106 ? 0.42226 0.32056 0.26494 -0.04487 -0.03867 0.02931  92  GLN B CA  
4956 C C   . GLN B 106 ? 0.43941 0.33088 0.26790 -0.04061 -0.03208 0.02836  92  GLN B C   
4957 O O   . GLN B 106 ? 0.39819 0.29105 0.23131 -0.03617 -0.02542 0.03529  92  GLN B O   
4958 C CB  . GLN B 106 ? 0.42069 0.31791 0.27951 -0.04457 -0.03431 0.03008  92  GLN B CB  
4959 C CG  . GLN B 106 ? 0.39089 0.27770 0.24737 -0.04511 -0.03074 0.02517  92  GLN B CG  
4960 C CD  . GLN B 106 ? 0.42313 0.31200 0.29032 -0.04660 -0.03045 0.02565  92  GLN B CD  
4961 O OE1 . GLN B 106 ? 0.46282 0.35758 0.33492 -0.05060 -0.03337 0.02660  92  GLN B OE1 
4962 N NE2 . GLN B 106 ? 0.43997 0.32620 0.31094 -0.04310 -0.02689 0.02534  92  GLN B NE2 
4971 N N   . GLU B 107 ? 0.39191 0.27626 0.20569 -0.04203 -0.03324 0.01927  93  GLU B N   
4972 C CA  . GLU B 107 ? 0.44754 0.32649 0.24670 -0.03722 -0.02565 0.01591  93  GLU B CA  
4973 C C   . GLU B 107 ? 0.50892 0.37495 0.31233 -0.03756 -0.02215 0.00699  93  GLU B C   
4974 O O   . GLU B 107 ? 0.47281 0.33210 0.28117 -0.04267 -0.02795 0.00108  93  GLU B O   
4975 C CB  . GLU B 107 ? 0.46903 0.35181 0.24347 -0.03633 -0.03003 0.01073  93  GLU B CB  
4976 C CG  . GLU B 107 ? 0.52389 0.42037 0.29125 -0.03362 -0.03310 0.02272  93  GLU B CG  
4977 C CD  . GLU B 107 ? 0.68201 0.58546 0.42260 -0.03296 -0.04132 0.01681  93  GLU B CD  
4978 O OE1 . GLU B 107 ? 0.70470 0.60479 0.44185 -0.03838 -0.05076 0.00267  93  GLU B OE1 
4979 O OE2 . GLU B 107 ? 0.72467 0.63743 0.44802 -0.02713 -0.03865 0.02652  93  GLU B OE2 
4986 N N   . ARG B 108 ? 0.48725 0.35028 0.29164 -0.03193 -0.01229 0.00733  94  ARG B N   
4987 C CA  . ARG B 108 ? 0.50303 0.35462 0.31411 -0.03012 -0.00876 0.00030  94  ARG B CA  
4988 C C   . ARG B 108 ? 0.50360 0.35384 0.30599 -0.02305 0.00185  -0.00420 94  ARG B C   
4989 O O   . ARG B 108 ? 0.45697 0.31691 0.25352 -0.01955 0.00895  0.00229  94  ARG B O   
4990 C CB  . ARG B 108 ? 0.49364 0.34598 0.32613 -0.02968 -0.00802 0.00673  94  ARG B CB  
4991 C CG  . ARG B 108 ? 0.45819 0.31077 0.29860 -0.03543 -0.01605 0.00955  94  ARG B CG  
4992 C CD  . ARG B 108 ? 0.45555 0.30395 0.30903 -0.03360 -0.01576 0.01168  94  ARG B CD  
4993 N NE  . ARG B 108 ? 0.44787 0.30052 0.30723 -0.03779 -0.02091 0.01667  94  ARG B NE  
4994 C CZ  . ARG B 108 ? 0.42626 0.29000 0.29282 -0.03703 -0.02166 0.02095  94  ARG B CZ  
4995 N NH1 . ARG B 108 ? 0.41076 0.28112 0.28342 -0.03346 -0.01867 0.02136  94  ARG B NH1 
4996 N NH2 . ARG B 108 ? 0.41452 0.28303 0.28352 -0.04001 -0.02479 0.02436  94  ARG B NH2 
5010 N N   . THR B 109 ? 0.47154 0.30961 0.27484 -0.02062 0.00387  -0.01462 95  THR B N   
5011 C CA  . THR B 109 ? 0.48643 0.32310 0.29076 -0.01241 0.01567  -0.01911 95  THR B CA  
5012 C C   . THR B 109 ? 0.48794 0.31635 0.31564 -0.01006 0.01558  -0.01851 95  THR B C   
5013 O O   . THR B 109 ? 0.53503 0.35029 0.36695 -0.01299 0.00863  -0.02290 95  THR B O   
5014 C CB  . THR B 109 ? 0.61268 0.44255 0.39478 -0.00926 0.01854  -0.03475 95  THR B CB  
5015 O OG1 . THR B 109 ? 0.64088 0.48072 0.39838 -0.01143 0.01546  -0.03414 95  THR B OG1 
5016 C CG2 . THR B 109 ? 0.64173 0.47339 0.42520 0.00064  0.03354  -0.03922 95  THR B CG2 
5024 N N   . ILE B 110 ? 0.52431 0.36141 0.36915 -0.00512 0.02251  -0.01165 96  ILE B N   
5025 C CA  . ILE B 110 ? 0.50243 0.33633 0.37028 -0.00174 0.02067  -0.00895 96  ILE B CA  
5026 C C   . ILE B 110 ? 0.53584 0.36935 0.41298 0.00783  0.03185  -0.01477 96  ILE B C   
5027 O O   . ILE B 110 ? 0.46274 0.30993 0.34744 0.01147  0.04161  -0.01118 96  ILE B O   
5028 C CB  . ILE B 110 ? 0.45995 0.30708 0.34455 -0.00391 0.01681  0.00196  96  ILE B CB  
5029 C CG1 . ILE B 110 ? 0.47928 0.32794 0.35489 -0.01203 0.00779  0.00625  96  ILE B CG1 
5030 C CG2 . ILE B 110 ? 0.51205 0.35840 0.41714 0.00043  0.01256  0.00464  96  ILE B CG2 
5031 C CD1 . ILE B 110 ? 0.50985 0.37163 0.39911 -0.01405 0.00516  0.01353  96  ILE B CD1 
5043 N N   . PHE B 111 ? 0.46043 0.27829 0.34044 0.01207  0.03131  -0.02328 97  PHE B N   
5044 C CA  . PHE B 111 ? 0.50049 0.31643 0.39133 0.02273  0.04237  -0.03090 97  PHE B CA  
5045 C C   . PHE B 111 ? 0.51157 0.33169 0.43317 0.02844  0.03982  -0.02258 97  PHE B C   
5046 O O   . PHE B 111 ? 0.50380 0.31248 0.43377 0.02803  0.03016  -0.01880 97  PHE B O   
5047 C CB  . PHE B 111 ? 0.57966 0.37466 0.45988 0.02531  0.04299  -0.04668 97  PHE B CB  
5048 C CG  . PHE B 111 ? 0.60059 0.39407 0.44949 0.02085  0.04407  -0.05782 97  PHE B CG  
5049 C CD1 . PHE B 111 ? 0.56902 0.37080 0.40203 0.02747  0.05731  -0.06710 97  PHE B CD1 
5050 C CD2 . PHE B 111 ? 0.59235 0.37846 0.42774 0.01050  0.03177  -0.05865 97  PHE B CD2 
5051 C CE1 . PHE B 111 ? 0.69089 0.49365 0.49138 0.02432  0.05667  -0.07710 97  PHE B CE1 
5052 C CE2 . PHE B 111 ? 0.60439 0.39173 0.41197 0.00679  0.03024  -0.06919 97  PHE B CE2 
5053 C CZ  . PHE B 111 ? 0.71854 0.51419 0.50677 0.01396  0.04188  -0.07850 97  PHE B CZ  
5063 N N   . PHE B 112 ? 0.52256 0.36049 0.46207 0.03371  0.04819  -0.01859 98  PHE B N   
5064 C CA  . PHE B 112 ? 0.45971 0.30535 0.43116 0.04068  0.04553  -0.01257 98  PHE B CA  
5065 C C   . PHE B 112 ? 0.49196 0.32926 0.47619 0.05280  0.05490  -0.02175 98  PHE B C   
5066 O O   . PHE B 112 ? 0.51989 0.36301 0.50149 0.05803  0.07012  -0.02983 98  PHE B O   
5067 C CB  . PHE B 112 ? 0.44040 0.31051 0.43145 0.03961  0.04915  -0.00507 98  PHE B CB  
5068 C CG  . PHE B 112 ? 0.46221 0.33914 0.44664 0.02906  0.03905  0.00253  98  PHE B CG  
5069 C CD1 . PHE B 112 ? 0.43750 0.31635 0.40237 0.02186  0.04364  0.00337  98  PHE B CD1 
5070 C CD2 . PHE B 112 ? 0.47983 0.36175 0.47701 0.02743  0.02485  0.00860  98  PHE B CD2 
5071 C CE1 . PHE B 112 ? 0.51244 0.39637 0.47461 0.01340  0.03492  0.00939  98  PHE B CE1 
5072 C CE2 . PHE B 112 ? 0.42968 0.31775 0.42077 0.01878  0.01648  0.01270  98  PHE B CE2 
5073 C CZ  . PHE B 112 ? 0.47760 0.36577 0.45314 0.01184  0.02185  0.01271  98  PHE B CZ  
5083 N N   . LYS B 113 ? 0.49979 0.32350 0.49774 0.05798  0.04666  -0.01990 99  LYS B N   
5084 C CA  . LYS B 113 ? 0.50807 0.31903 0.52015 0.07020  0.05455  -0.02947 99  LYS B CA  
5085 C C   . LYS B 113 ? 0.51637 0.34823 0.55447 0.08063  0.06761  -0.03088 99  LYS B C   
5086 O O   . LYS B 113 ? 0.46507 0.31829 0.52628 0.08102  0.06356  -0.02003 99  LYS B O   
5087 C CB  . LYS B 113 ? 0.50589 0.30103 0.53490 0.07468  0.04250  -0.02161 99  LYS B CB  
5088 C CG  . LYS B 113 ? 0.59314 0.36746 0.63661 0.08669  0.04942  -0.03242 99  LYS B CG  
5089 C CD  . LYS B 113 ? 0.76583 0.52598 0.83110 0.09250  0.03774  -0.01968 99  LYS B CD  
5090 C CE  . LYS B 113 ? 0.79310 0.53093 0.87893 0.10588  0.04519  -0.03038 99  LYS B CE  
5091 N NZ  . LYS B 113 ? 1.12707 0.85150 1.23796 0.11329  0.03419  -0.01414 99  LYS B NZ  
5105 N N   . ASP B 114 ? 0.57409 0.40102 0.60948 0.08907  0.08352  -0.04552 100 ASP B N   
5106 C CA  . ASP B 114 ? 0.56363 0.41122 0.62454 0.10002  0.09977  -0.04803 100 ASP B CA  
5107 C C   . ASP B 114 ? 0.48820 0.36389 0.55144 0.09275  0.10539  -0.03831 100 ASP B C   
5108 O O   . ASP B 114 ? 0.50471 0.40330 0.60214 0.09786  0.11132  -0.03215 100 ASP B O   
5109 C CB  . ASP B 114 ? 0.55399 0.40504 0.65775 0.11208  0.09470  -0.04202 100 ASP B CB  
5110 C CG  . ASP B 114 ? 0.65377 0.47622 0.76225 0.12216  0.09385  -0.05191 100 ASP B CG  
5111 O OD1 . ASP B 114 ? 0.74476 0.54571 0.82488 0.11974  0.09865  -0.06684 100 ASP B OD1 
5112 O OD2 . ASP B 114 ? 0.67468 0.49604 0.81691 0.13267  0.08756  -0.04487 100 ASP B OD2 
5117 N N   . ASP B 115 ? 0.58650 0.46059 0.61686 0.08071  0.10332  -0.03649 101 ASP B N   
5118 C CA  . ASP B 115 ? 0.52738 0.42401 0.56040 0.07306  0.10837  -0.02598 101 ASP B CA  
5119 C C   . ASP B 115 ? 0.53032 0.42014 0.52100 0.06375  0.10971  -0.02742 101 ASP B C   
5120 O O   . ASP B 115 ? 0.53682 0.40883 0.49796 0.06476  0.10975  -0.03934 101 ASP B O   
5121 C CB  . ASP B 115 ? 0.48492 0.39226 0.54320 0.06683  0.09190  -0.01312 101 ASP B CB  
5122 C CG  . ASP B 115 ? 0.51210 0.44618 0.59730 0.06359  0.09975  -0.00435 101 ASP B CG  
5123 O OD1 . ASP B 115 ? 0.50616 0.44863 0.58176 0.06252  0.11708  -0.00373 101 ASP B OD1 
5124 O OD2 . ASP B 115 ? 0.55884 0.50615 0.67535 0.06198  0.08842  0.00214  101 ASP B OD2 
5129 N N   . GLY B 116 ? 0.56796 0.47193 0.55819 0.05485  0.10977  -0.01563 102 GLY B N   
5130 C CA  . GLY B 116 ? 0.53806 0.43952 0.49245 0.04749  0.11177  -0.01372 102 GLY B CA  
5131 C C   . GLY B 116 ? 0.52016 0.40459 0.45260 0.03894  0.09293  -0.01464 102 GLY B C   
5132 O O   . GLY B 116 ? 0.43684 0.30893 0.37714 0.03886  0.07990  -0.01742 102 GLY B O   
5136 N N   . ASN B 117 ? 0.47712 0.36239 0.38275 0.03199  0.09219  -0.01051 103 ASN B N   
5137 C CA  . ASN B 117 ? 0.45526 0.32765 0.34026 0.02386  0.07619  -0.01138 103 ASN B CA  
5138 C C   . ASN B 117 ? 0.48000 0.36170 0.35876 0.01599  0.07365  0.00123  103 ASN B C   
5139 O O   . ASN B 117 ? 0.45624 0.34967 0.32967 0.01708  0.08595  0.00838  103 ASN B O   
5140 C CB  . ASN B 117 ? 0.50977 0.36831 0.36213 0.02535  0.07561  -0.02568 103 ASN B CB  
5141 C CG  . ASN B 117 ? 0.58898 0.45740 0.41362 0.02806  0.08833  -0.02691 103 ASN B CG  
5142 O OD1 . ASN B 117 ? 0.52215 0.39584 0.32764 0.02237  0.08443  -0.01921 103 ASN B OD1 
5143 N ND2 . ASN B 117 ? 0.51919 0.39137 0.34129 0.03781  0.10403  -0.03592 103 ASN B ND2 
5150 N N   . TYR B 118 ? 0.45986 0.33628 0.34027 0.00872  0.05862  0.00474  104 TYR B N   
5151 C CA  . TYR B 118 ? 0.41731 0.29929 0.29234 0.00188  0.05427  0.01476  104 TYR B CA  
5152 C C   . TYR B 118 ? 0.45318 0.32844 0.29558 -0.00105 0.04851  0.01104  104 TYR B C   
5153 O O   . TYR B 118 ? 0.46499 0.32847 0.29608 -0.00195 0.04070  0.00066  104 TYR B O   
5154 C CB  . TYR B 118 ? 0.40922 0.29120 0.30353 -0.00350 0.04159  0.01864  104 TYR B CB  
5155 C CG  . TYR B 118 ? 0.43760 0.32963 0.36555 -0.00232 0.04305  0.02232  104 TYR B CG  
5156 C CD1 . TYR B 118 ? 0.39046 0.29355 0.33599 0.00124  0.05655  0.02622  104 TYR B CD1 
5157 C CD2 . TYR B 118 ? 0.39457 0.28716 0.33715 -0.00491 0.03064  0.02164  104 TYR B CD2 
5158 C CE1 . TYR B 118 ? 0.38594 0.30018 0.36687 0.00130  0.05615  0.02850  104 TYR B CE1 
5159 C CE2 . TYR B 118 ? 0.36140 0.26511 0.33438 -0.00402 0.02918  0.02285  104 TYR B CE2 
5160 C CZ  . TYR B 118 ? 0.37757 0.29201 0.37176 -0.00139 0.04116  0.02587  104 TYR B CZ  
5161 O OH  . TYR B 118 ? 0.33564 0.26302 0.36459 -0.00145 0.03802  0.02600  104 TYR B OH  
5171 N N   . LYS B 119 ? 0.44760 0.33082 0.27781 -0.00275 0.05160  0.02044  105 LYS B N   
5172 C CA  . LYS B 119 ? 0.53224 0.41338 0.33682 -0.00626 0.04248  0.02002  105 LYS B CA  
5173 C C   . LYS B 119 ? 0.44948 0.33559 0.26707 -0.01125 0.03625  0.03291  105 LYS B C   
5174 O O   . LYS B 119 ? 0.46387 0.35802 0.29161 -0.01035 0.04437  0.04570  105 LYS B O   
5175 C CB  . LYS B 119 ? 0.50082 0.38826 0.27468 -0.00165 0.05073  0.02001  105 LYS B CB  
5176 C CG  . LYS B 119 ? 0.69032 0.57219 0.44709 0.00406  0.05653  0.00305  105 LYS B CG  
5177 C CD  . LYS B 119 ? 0.80735 0.69505 0.52464 0.00725  0.05791  -0.00147 105 LYS B CD  
5178 C CE  . LYS B 119 ? 0.81014 0.70395 0.51296 0.01660  0.07609  -0.00754 105 LYS B CE  
5179 N NZ  . LYS B 119 ? 0.81912 0.72698 0.53718 0.01968  0.09308  0.01180  105 LYS B NZ  
5193 N N   . THR B 120 ? 0.41378 0.29499 0.23344 -0.01631 0.02300  0.02974  106 THR B N   
5194 C CA  . THR B 120 ? 0.48868 0.37388 0.32312 -0.02003 0.01704  0.03882  106 THR B CA  
5195 C C   . THR B 120 ? 0.46992 0.35685 0.28775 -0.02260 0.00728  0.04002  106 THR B C   
5196 O O   . THR B 120 ? 0.45500 0.33800 0.25673 -0.02436 0.00058  0.03039  106 THR B O   
5197 C CB  . THR B 120 ? 0.41460 0.29663 0.27059 -0.02284 0.01088  0.03458  106 THR B CB  
5198 O OG1 . THR B 120 ? 0.44729 0.32290 0.29362 -0.02573 0.00205  0.02647  106 THR B OG1 
5199 C CG2 . THR B 120 ? 0.38682 0.26889 0.25940 -0.01976 0.01750  0.03194  106 THR B CG2 
5207 N N   . ARG B 121 ? 0.44745 0.34042 0.27291 -0.02276 0.00611  0.05184  107 ARG B N   
5208 C CA  . ARG B 121 ? 0.44594 0.34329 0.26328 -0.02441 -0.00424 0.05487  107 ARG B CA  
5209 C C   . ARG B 121 ? 0.42421 0.32363 0.26711 -0.02535 -0.00658 0.06244  107 ARG B C   
5210 O O   . ARG B 121 ? 0.46364 0.36338 0.32229 -0.02335 0.00073  0.07202  107 ARG B O   
5211 C CB  . ARG B 121 ? 0.39951 0.30406 0.19264 -0.02051 -0.00315 0.06322  107 ARG B CB  
5212 C CG  . ARG B 121 ? 0.48229 0.39411 0.26844 -0.02152 -0.01616 0.06634  107 ARG B CG  
5213 C CD  . ARG B 121 ? 0.51638 0.43706 0.27129 -0.01729 -0.01827 0.07120  107 ARG B CD  
5214 N NE  . ARG B 121 ? 0.55828 0.48795 0.30750 -0.01867 -0.03388 0.07098  107 ARG B NE  
5215 C CZ  . ARG B 121 ? 0.52967 0.46702 0.29185 -0.01634 -0.03927 0.08559  107 ARG B CZ  
5216 N NH1 . ARG B 121 ? 0.64016 0.57485 0.42187 -0.01299 -0.03031 0.10128  107 ARG B NH1 
5217 N NH2 . ARG B 121 ? 0.56181 0.50976 0.32087 -0.01737 -0.05434 0.08403  107 ARG B NH2 
5231 N N   . ALA B 122 ? 0.38551 0.28635 0.23482 -0.02845 -0.01589 0.05750  108 ALA B N   
5232 C CA  . ALA B 122 ? 0.42373 0.32655 0.29725 -0.02849 -0.01764 0.06059  108 ALA B CA  
5233 C C   . ALA B 122 ? 0.40983 0.32014 0.28387 -0.02909 -0.02691 0.06220  108 ALA B C   
5234 O O   . ALA B 122 ? 0.44756 0.36095 0.30772 -0.03202 -0.03359 0.05684  108 ALA B O   
5235 C CB  . ALA B 122 ? 0.41612 0.31544 0.30304 -0.03080 -0.01704 0.05061  108 ALA B CB  
5241 N N   . GLU B 123 ? 0.41159 0.32493 0.30547 -0.02626 -0.02736 0.06906  109 GLU B N   
5242 C CA  . GLU B 123 ? 0.41902 0.34125 0.32207 -0.02559 -0.03510 0.07024  109 GLU B CA  
5243 C C   . GLU B 123 ? 0.39575 0.31798 0.32028 -0.02608 -0.03331 0.06188  109 GLU B C   
5244 O O   . GLU B 123 ? 0.40996 0.32723 0.35243 -0.02336 -0.02847 0.06236  109 GLU B O   
5245 C CB  . GLU B 123 ? 0.41739 0.34389 0.32710 -0.01976 -0.03702 0.08550  109 GLU B CB  
5246 C CG  . GLU B 123 ? 0.55457 0.48382 0.43851 -0.01784 -0.03844 0.09528  109 GLU B CG  
5247 C CD  . GLU B 123 ? 0.65927 0.59508 0.54843 -0.01113 -0.04217 0.11335  109 GLU B CD  
5248 O OE1 . GLU B 123 ? 0.65499 0.58877 0.57262 -0.00763 -0.04089 0.11913  109 GLU B OE1 
5249 O OE2 . GLU B 123 ? 0.65355 0.59672 0.51817 -0.00866 -0.04676 0.12154  109 GLU B OE2 
5256 N N   . VAL B 124 ? 0.43624 0.36432 0.35905 -0.02974 -0.03677 0.05373  110 VAL B N   
5257 C CA  . VAL B 124 ? 0.41476 0.34688 0.35328 -0.02936 -0.03457 0.04603  110 VAL B CA  
5258 C C   . VAL B 124 ? 0.43122 0.37579 0.38471 -0.02692 -0.03851 0.04887  110 VAL B C   
5259 O O   . VAL B 124 ? 0.42058 0.37401 0.36926 -0.03035 -0.04407 0.05016  110 VAL B O   
5260 C CB  . VAL B 124 ? 0.45192 0.38376 0.37958 -0.03446 -0.03352 0.03804  110 VAL B CB  
5261 C CG1 . VAL B 124 ? 0.40391 0.34137 0.34274 -0.03272 -0.02978 0.03057  110 VAL B CG1 
5262 C CG2 . VAL B 124 ? 0.44585 0.36648 0.35938 -0.03601 -0.03111 0.03664  110 VAL B CG2 
5272 N N   . LYS B 125 ? 0.41585 0.36143 0.39085 -0.02096 -0.03594 0.04892  111 LYS B N   
5273 C CA  . LYS B 125 ? 0.37809 0.33599 0.37218 -0.01658 -0.03896 0.05206  111 LYS B CA  
5274 C C   . LYS B 125 ? 0.39044 0.34673 0.40863 -0.01016 -0.03332 0.04512  111 LYS B C   
5275 O O   . LYS B 125 ? 0.38441 0.32908 0.40527 -0.00944 -0.02901 0.03945  111 LYS B O   
5276 C CB  . LYS B 125 ? 0.41059 0.37075 0.40514 -0.01320 -0.04586 0.06660  111 LYS B CB  
5277 C CG  . LYS B 125 ? 0.38270 0.32971 0.38231 -0.00841 -0.04266 0.07612  111 LYS B CG  
5278 C CD  . LYS B 125 ? 0.44966 0.40124 0.44478 -0.00423 -0.04949 0.09355  111 LYS B CD  
5279 C CE  . LYS B 125 ? 0.55773 0.49637 0.55867 0.00022  -0.04429 0.10701  111 LYS B CE  
5280 N NZ  . LYS B 125 ? 0.52194 0.45112 0.50040 -0.00480 -0.03849 0.10665  111 LYS B NZ  
5294 N N   . PHE B 126 ? 0.35307 0.32208 0.39119 -0.00536 -0.03367 0.04415  112 PHE B N   
5295 C CA  . PHE B 126 ? 0.43265 0.40064 0.49619 0.00234  -0.02823 0.03557  112 PHE B CA  
5296 C C   . PHE B 126 ? 0.42536 0.38366 0.51036 0.00947  -0.03038 0.04656  112 PHE B C   
5297 O O   . PHE B 126 ? 0.44445 0.40830 0.53241 0.01187  -0.03684 0.06173  112 PHE B O   
5298 C CB  . PHE B 126 ? 0.38246 0.36974 0.46079 0.00572  -0.02558 0.02954  112 PHE B CB  
5299 C CG  . PHE B 126 ? 0.34849 0.34381 0.41275 0.00151  -0.01895 0.01688  112 PHE B CG  
5300 C CD1 . PHE B 126 ? 0.41095 0.40477 0.47951 0.00608  -0.01161 0.00108  112 PHE B CD1 
5301 C CD2 . PHE B 126 ? 0.34827 0.35288 0.39537 -0.00675 -0.02027 0.02093  112 PHE B CD2 
5302 C CE1 . PHE B 126 ? 0.35034 0.35381 0.40205 0.00334  -0.00551 -0.00839 112 PHE B CE1 
5303 C CE2 . PHE B 126 ? 0.40812 0.42000 0.44266 -0.01014 -0.01330 0.01318  112 PHE B CE2 
5304 C CZ  . PHE B 126 ? 0.39669 0.40908 0.43150 -0.00463 -0.00579 -0.00046 112 PHE B CZ  
5314 N N   . GLU B 127 ? 0.44787 0.39192 0.54869 0.01277  -0.02562 0.03932  113 GLU B N   
5315 C CA  . GLU B 127 ? 0.47962 0.41226 0.60984 0.02036  -0.02552 0.04831  113 GLU B CA  
5316 C C   . GLU B 127 ? 0.48334 0.41589 0.64189 0.02760  -0.02029 0.03021  113 GLU B C   
5317 O O   . GLU B 127 ? 0.38112 0.30395 0.54382 0.02627  -0.01622 0.01341  113 GLU B O   
5318 C CB  . GLU B 127 ? 0.43833 0.35219 0.56717 0.01676  -0.02379 0.05553  113 GLU B CB  
5319 C CG  . GLU B 127 ? 0.58187 0.49694 0.68057 0.01085  -0.02697 0.07147  113 GLU B CG  
5320 C CD  . GLU B 127 ? 0.62812 0.52745 0.72744 0.00744  -0.02259 0.07882  113 GLU B CD  
5321 O OE1 . GLU B 127 ? 0.69131 0.57766 0.81948 0.00932  -0.01842 0.07445  113 GLU B OE1 
5322 O OE2 . GLU B 127 ? 0.62439 0.52479 0.69750 0.00277  -0.02283 0.08808  113 GLU B OE2 
5329 N N   . GLY B 128 ? 0.40975 0.35479 0.58813 0.03564  -0.02080 0.03209  114 GLY B N   
5330 C CA  . GLY B 128 ? 0.50861 0.45779 0.71057 0.04339  -0.01425 0.01212  114 GLY B CA  
5331 C C   . GLY B 128 ? 0.47314 0.43861 0.65142 0.03882  -0.00955 -0.00467 114 GLY B C   
5332 O O   . GLY B 128 ? 0.53678 0.51859 0.69657 0.03375  -0.01147 0.00273  114 GLY B O   
5336 N N   . ASP B 129 ? 0.41957 0.38085 0.59857 0.04046  -0.00367 -0.02723 115 ASP B N   
5337 C CA  . ASP B 129 ? 0.44284 0.41908 0.59572 0.03692  0.00139  -0.04212 115 ASP B CA  
5338 C C   . ASP B 129 ? 0.45586 0.42389 0.57769 0.02700  -0.00187 -0.04371 115 ASP B C   
5339 O O   . ASP B 129 ? 0.39665 0.37502 0.49529 0.02452  0.00145  -0.05497 115 ASP B O   
5340 C CB  . ASP B 129 ? 0.49802 0.47878 0.66540 0.04610  0.00939  -0.06762 115 ASP B CB  
5341 C CG  . ASP B 129 ? 0.62772 0.61937 0.82796 0.05745  0.01444  -0.06788 115 ASP B CG  
5342 O OD1 . ASP B 129 ? 0.67282 0.68245 0.87345 0.05686  0.01460  -0.05339 115 ASP B OD1 
5343 O OD2 . ASP B 129 ? 0.84598 0.82832 1.07474 0.06709  0.01784  -0.08334 115 ASP B OD2 
5348 N N   . THR B 130 ? 0.36786 0.31910 0.48932 0.02208  -0.00769 -0.03142 116 THR B N   
5349 C CA  . THR B 130 ? 0.38415 0.32724 0.48308 0.01392  -0.01053 -0.03302 116 THR B CA  
5350 C C   . THR B 130 ? 0.33969 0.28583 0.41418 0.00648  -0.01407 -0.01456 116 THR B C   
5351 O O   . THR B 130 ? 0.37990 0.32474 0.46005 0.00679  -0.01703 0.00220  116 THR B O   
5352 C CB  . THR B 130 ? 0.32125 0.24406 0.44079 0.01342  -0.01262 -0.03387 116 THR B CB  
5353 O OG1 . THR B 130 ? 0.36513 0.28293 0.51118 0.02013  -0.01016 -0.05378 116 THR B OG1 
5354 C CG2 . THR B 130 ? 0.37331 0.29108 0.47374 0.00544  -0.01542 -0.03642 116 THR B CG2 
5362 N N   . LEU B 131 ? 0.35552 0.30585 0.40299 0.00053  -0.01434 -0.01815 117 LEU B N   
5363 C CA  . LEU B 131 ? 0.39179 0.34180 0.41685 -0.00661 -0.01750 -0.00429 117 LEU B CA  
5364 C C   . LEU B 131 ? 0.39691 0.33176 0.41983 -0.00994 -0.01988 0.00048  117 LEU B C   
5365 O O   . LEU B 131 ? 0.35314 0.28338 0.37545 -0.01094 -0.01984 -0.01001 117 LEU B O   
5366 C CB  . LEU B 131 ? 0.33873 0.29900 0.33992 -0.01059 -0.01580 -0.00862 117 LEU B CB  
5367 C CG  . LEU B 131 ? 0.40643 0.36693 0.38779 -0.01777 -0.01840 0.00343  117 LEU B CG  
5368 C CD1 . LEU B 131 ? 0.39503 0.34214 0.36411 -0.02147 -0.02130 0.00645  117 LEU B CD1 
5369 C CD2 . LEU B 131 ? 0.39889 0.36341 0.38828 -0.01854 -0.02154 0.01498  117 LEU B CD2 
5381 N N   . VAL B 132 ? 0.40776 0.33712 0.42976 -0.01134 -0.02195 0.01618  118 VAL B N   
5382 C CA  . VAL B 132 ? 0.40506 0.32179 0.42901 -0.01335 -0.02156 0.02357  118 VAL B CA  
5383 C C   . VAL B 132 ? 0.40072 0.31739 0.39813 -0.01856 -0.02280 0.03143  118 VAL B C   
5384 O O   . VAL B 132 ? 0.41895 0.34232 0.40209 -0.02001 -0.02567 0.03701  118 VAL B O   
5385 C CB  . VAL B 132 ? 0.44464 0.35478 0.48954 -0.00895 -0.02114 0.03687  118 VAL B CB  
5386 C CG1 . VAL B 132 ? 0.53314 0.43392 0.57380 -0.01160 -0.01896 0.05014  118 VAL B CG1 
5387 C CG2 . VAL B 132 ? 0.40391 0.30825 0.48085 -0.00390 -0.01905 0.02691  118 VAL B CG2 
5397 N N   . ASN B 133 ? 0.41903 0.32854 0.41277 -0.02128 -0.02079 0.03053  119 ASN B N   
5398 C CA  . ASN B 133 ? 0.40234 0.31004 0.37404 -0.02484 -0.02041 0.03635  119 ASN B CA  
5399 C C   . ASN B 133 ? 0.39116 0.29124 0.37088 -0.02466 -0.01570 0.04571  119 ASN B C   
5400 O O   . ASN B 133 ? 0.36333 0.25964 0.35763 -0.02571 -0.01308 0.04062  119 ASN B O   
5401 C CB  . ASN B 133 ? 0.35628 0.26572 0.31620 -0.02744 -0.02125 0.02617  119 ASN B CB  
5402 C CG  . ASN B 133 ? 0.38799 0.29418 0.32796 -0.03005 -0.02059 0.03061  119 ASN B CG  
5403 O OD1 . ASN B 133 ? 0.38623 0.29131 0.31502 -0.03052 -0.02062 0.03851  119 ASN B OD1 
5404 N ND2 . ASN B 133 ? 0.35696 0.26221 0.29247 -0.03096 -0.02060 0.02468  119 ASN B ND2 
5411 N N   . ARG B 134 ? 0.39033 0.29003 0.36113 -0.02333 -0.01467 0.05974  120 ARG B N   
5412 C CA  . ARG B 134 ? 0.42633 0.32092 0.40213 -0.02255 -0.00801 0.07262  120 ARG B CA  
5413 C C   . ARG B 134 ? 0.36399 0.26003 0.31273 -0.02396 -0.00515 0.07521  120 ARG B C   
5414 O O   . ARG B 134 ? 0.37966 0.27991 0.30488 -0.02357 -0.00937 0.07703  120 ARG B O   
5415 C CB  . ARG B 134 ? 0.40249 0.29683 0.38582 -0.01824 -0.00815 0.08886  120 ARG B CB  
5416 C CG  . ARG B 134 ? 0.52343 0.41462 0.53721 -0.01540 -0.01019 0.08598  120 ARG B CG  
5417 C CD  . ARG B 134 ? 0.54538 0.43652 0.56771 -0.00967 -0.01139 0.10424  120 ARG B CD  
5418 N NE  . ARG B 134 ? 0.53106 0.41629 0.58831 -0.00593 -0.01184 0.10100  120 ARG B NE  
5419 C CZ  . ARG B 134 ? 0.56660 0.43965 0.65487 -0.00608 -0.00617 0.10307  120 ARG B CZ  
5420 N NH1 . ARG B 134 ? 0.57287 0.44023 0.66366 -0.01025 0.00105  0.11019  120 ARG B NH1 
5421 N NH2 . ARG B 134 ? 0.56498 0.43163 0.68548 -0.00201 -0.00729 0.09699  120 ARG B NH2 
5435 N N   . ILE B 135 ? 0.37753 0.27083 0.33208 -0.02535 0.00187  0.07436  121 ILE B N   
5436 C CA  . ILE B 135 ? 0.36392 0.25829 0.29702 -0.02588 0.00534  0.07163  121 ILE B CA  
5437 C C   . ILE B 135 ? 0.37680 0.27166 0.31056 -0.02422 0.01668  0.08443  121 ILE B C   
5438 O O   . ILE B 135 ? 0.45803 0.35123 0.41853 -0.02490 0.02283  0.09168  121 ILE B O   
5439 C CB  . ILE B 135 ? 0.41687 0.31064 0.35690 -0.02791 0.00378  0.05781  121 ILE B CB  
5440 C CG1 . ILE B 135 ? 0.42263 0.31761 0.36358 -0.02915 -0.00530 0.04732  121 ILE B CG1 
5441 C CG2 . ILE B 135 ? 0.40056 0.29386 0.31983 -0.02718 0.00672  0.05449  121 ILE B CG2 
5442 C CD1 . ILE B 135 ? 0.42385 0.32028 0.37883 -0.03000 -0.00754 0.03643  121 ILE B CD1 
5454 N N   . GLU B 136 ? 0.38502 0.28251 0.29037 -0.02221 0.02009  0.08646  122 GLU B N   
5455 C CA  . GLU B 136 ? 0.41074 0.31120 0.31156 -0.01995 0.03329  0.09515  122 GLU B CA  
5456 C C   . GLU B 136 ? 0.39886 0.29923 0.28664 -0.01934 0.03552  0.08172  122 GLU B C   
5457 O O   . GLU B 136 ? 0.40855 0.30653 0.27457 -0.01938 0.02776  0.07121  122 GLU B O   
5458 C CB  . GLU B 136 ? 0.40757 0.31291 0.28266 -0.01591 0.03676  0.10994  122 GLU B CB  
5459 C CG  . GLU B 136 ? 0.66032 0.56534 0.55152 -0.01487 0.03660  0.12806  122 GLU B CG  
5460 C CD  . GLU B 136 ? 1.01918 0.93129 0.88123 -0.00960 0.03850  0.14481  122 GLU B CD  
5461 O OE1 . GLU B 136 ? 0.91448 0.83219 0.74096 -0.00732 0.03702  0.13795  122 GLU B OE1 
5462 O OE2 . GLU B 136 ? 1.19070 1.10273 1.06548 -0.00730 0.04096  0.16464  122 GLU B OE2 
5469 N N   . LEU B 137 ? 0.42439 0.32728 0.32951 -0.01880 0.04600  0.08217  123 LEU B N   
5470 C CA  . LEU B 137 ? 0.45202 0.35486 0.35234 -0.01686 0.04866  0.07003  123 LEU B CA  
5471 C C   . LEU B 137 ? 0.44440 0.35449 0.34531 -0.01295 0.06564  0.07689  123 LEU B C   
5472 O O   . LEU B 137 ? 0.47838 0.39399 0.40319 -0.01416 0.07529  0.08933  123 LEU B O   
5473 C CB  . LEU B 137 ? 0.44317 0.34488 0.37121 -0.01939 0.04205  0.06052  123 LEU B CB  
5474 C CG  . LEU B 137 ? 0.38782 0.28956 0.31683 -0.01629 0.04335  0.04996  123 LEU B CG  
5475 C CD1 . LEU B 137 ? 0.40374 0.30346 0.34616 -0.01820 0.03082  0.04087  123 LEU B CD1 
5476 C CD2 . LEU B 137 ? 0.40491 0.31551 0.35507 -0.01364 0.05718  0.05432  123 LEU B CD2 
5488 N N   . LYS B 138 ? 0.44813 0.35821 0.32498 -0.00828 0.07016  0.06829  124 LYS B N   
5489 C CA  . LYS B 138 ? 0.51294 0.43155 0.38858 -0.00303 0.08802  0.07183  124 LYS B CA  
5490 C C   . LYS B 138 ? 0.45337 0.36938 0.33233 0.00095  0.08896  0.05577  124 LYS B C   
5491 O O   . LYS B 138 ? 0.47215 0.37901 0.32855 0.00247  0.08073  0.04261  124 LYS B O   
5492 C CB  . LYS B 138 ? 0.49064 0.41383 0.32734 0.00151  0.09577  0.07797  124 LYS B CB  
5493 C CG  . LYS B 138 ? 0.56749 0.50253 0.40211 0.00764  0.11760  0.08380  124 LYS B CG  
5494 C CD  . LYS B 138 ? 0.65788 0.59738 0.44466 0.01439  0.12372  0.08066  124 LYS B CD  
5495 C CE  . LYS B 138 ? 0.57541 0.52232 0.34175 0.01464  0.12627  0.10155  124 LYS B CE  
5496 N NZ  . LYS B 138 ? 0.74642 0.70268 0.46467 0.02270  0.13497  0.09935  124 LYS B NZ  
5510 N N   . GLY B 139 ? 0.48147 0.40554 0.39201 0.00263  0.09867  0.05731  125 GLY B N   
5511 C CA  . GLY B 139 ? 0.49429 0.41843 0.41201 0.00869  0.10248  0.04477  125 GLY B CA  
5512 C C   . GLY B 139 ? 0.48419 0.41926 0.39481 0.01604  0.12391  0.04699  125 GLY B C   
5513 O O   . GLY B 139 ? 0.48879 0.43596 0.40869 0.01513  0.13775  0.06196  125 GLY B O   
5517 N N   . ILE B 140 ? 0.51902 0.44946 0.41397 0.02362  0.12755  0.03217  126 ILE B N   
5518 C CA  . ILE B 140 ? 0.53279 0.47390 0.41757 0.03251  0.14891  0.03019  126 ILE B CA  
5519 C C   . ILE B 140 ? 0.58014 0.51835 0.48188 0.04069  0.15179  0.01465  126 ILE B C   
5520 O O   . ILE B 140 ? 0.52155 0.44492 0.42706 0.04016  0.13607  0.00392  126 ILE B O   
5521 C CB  . ILE B 140 ? 0.61960 0.55782 0.45247 0.03569  0.15225  0.02560  126 ILE B CB  
5522 C CG1 . ILE B 140 ? 0.69620 0.61586 0.50614 0.03718  0.13761  0.00411  126 ILE B CG1 
5523 C CG2 . ILE B 140 ? 0.56764 0.50813 0.38497 0.02858  0.14637  0.04253  126 ILE B CG2 
5524 C CD1 . ILE B 140 ? 0.73898 0.65613 0.49933 0.03887  0.13584  -0.00369 126 ILE B CD1 
5536 N N   . ASP B 141 ? 0.61398 0.56717 0.52784 0.04887  0.17311  0.01501  127 ASP B N   
5537 C CA  . ASP B 141 ? 0.63383 0.58569 0.56155 0.05962  0.17980  -0.00047 127 ASP B CA  
5538 C C   . ASP B 141 ? 0.59224 0.54326 0.56596 0.05887  0.16754  -0.00040 127 ASP B C   
5539 O O   . ASP B 141 ? 0.57351 0.51467 0.55570 0.06636  0.16314  -0.01334 127 ASP B O   
5540 C CB  . ASP B 141 ? 0.66708 0.59902 0.55646 0.06460  0.17341  -0.02100 127 ASP B CB  
5541 C CG  . ASP B 141 ? 0.75780 0.69350 0.59898 0.06715  0.18445  -0.02446 127 ASP B CG  
5542 O OD1 . ASP B 141 ? 0.77654 0.73229 0.61566 0.07120  0.20560  -0.01443 127 ASP B OD1 
5543 O OD2 . ASP B 141 ? 0.80979 0.72994 0.61566 0.06504  0.17183  -0.03661 127 ASP B OD2 
5548 N N   . PHE B 142 ? 0.55660 0.51788 0.56085 0.05044  0.16132  0.01380  128 PHE B N   
5549 C CA  . PHE B 142 ? 0.50135 0.46629 0.54804 0.04997  0.14850  0.01387  128 PHE B CA  
5550 C C   . PHE B 142 ? 0.51152 0.49896 0.60153 0.05709  0.16482  0.01637  128 PHE B C   
5551 O O   . PHE B 142 ? 0.49310 0.49774 0.59235 0.05620  0.18419  0.02590  128 PHE B O   
5552 C CB  . PHE B 142 ? 0.48071 0.44702 0.54097 0.03780  0.13265  0.02404  128 PHE B CB  
5553 C CG  . PHE B 142 ? 0.47381 0.41996 0.50283 0.03208  0.11338  0.02028  128 PHE B CG  
5554 C CD1 . PHE B 142 ? 0.40104 0.33727 0.43559 0.03316  0.09566  0.01400  128 PHE B CD1 
5555 C CD2 . PHE B 142 ? 0.46602 0.40488 0.46149 0.02611  0.11341  0.02462  128 PHE B CD2 
5556 C CE1 . PHE B 142 ? 0.42277 0.34261 0.43094 0.02764  0.08025  0.01189  128 PHE B CE1 
5557 C CE2 . PHE B 142 ? 0.44820 0.37127 0.41947 0.02091  0.09653  0.02123  128 PHE B CE2 
5558 C CZ  . PHE B 142 ? 0.41853 0.33228 0.39663 0.02130  0.08088  0.01474  128 PHE B CZ  
5568 N N   . LYS B 143 ? 0.49809 0.48640 0.61633 0.06454  0.15735  0.00928  129 LYS B N   
5569 C CA  . LYS B 143 ? 0.55619 0.56808 0.72258 0.07198  0.17002  0.01113  129 LYS B CA  
5570 C C   . LYS B 143 ? 0.57322 0.60440 0.78301 0.06205  0.16230  0.02277  129 LYS B C   
5571 O O   . LYS B 143 ? 0.48244 0.50809 0.69917 0.05583  0.13911  0.02303  129 LYS B O   
5572 C CB  . LYS B 143 ? 0.51224 0.51831 0.69623 0.08431  0.16225  0.00068  129 LYS B CB  
5573 C CG  . LYS B 143 ? 0.55996 0.54565 0.70898 0.09470  0.17053  -0.01372 129 LYS B CG  
5574 C CD  . LYS B 143 ? 0.55887 0.53138 0.72441 0.10498  0.15755  -0.02163 129 LYS B CD  
5575 C CE  . LYS B 143 ? 0.57122 0.52062 0.70671 0.11480  0.16573  -0.03829 129 LYS B CE  
5576 N NZ  . LYS B 143 ? 0.70477 0.63400 0.85259 0.12244  0.15005  -0.04334 129 LYS B NZ  
5590 N N   . GLU B 144 ? 0.58772 0.64214 0.82731 0.06043  0.18225  0.03189  130 GLU B N   
5591 C CA  . GLU B 144 ? 0.63939 0.71223 0.92621 0.04980  0.17579  0.04159  130 GLU B CA  
5592 C C   . GLU B 144 ? 0.57978 0.66248 0.90815 0.05279  0.15524  0.03563  130 GLU B C   
5593 O O   . GLU B 144 ? 0.59946 0.68802 0.95178 0.04303  0.13714  0.03769  130 GLU B O   
5594 C CB  . GLU B 144 ? 0.66850 0.76646 0.98795 0.04876  0.20339  0.05302  130 GLU B CB  
5595 C CG  . GLU B 144 ? 0.74904 0.84076 1.02785 0.04538  0.22352  0.06329  130 GLU B CG  
5596 C CD  . GLU B 144 ? 0.80187 0.88110 1.06766 0.03102  0.21095  0.07285  130 GLU B CD  
5597 O OE1 . GLU B 144 ? 0.77090 0.85078 1.06792 0.02244  0.19067  0.07165  130 GLU B OE1 
5598 O OE2 . GLU B 144 ? 0.70860 0.77810 0.93295 0.02911  0.22093  0.08093  130 GLU B OE2 
5605 N N   . ASP B 145 ? 0.52701 0.61162 0.86388 0.06690  0.15686  0.02774  131 ASP B N   
5606 C CA  . ASP B 145 ? 0.57588 0.67079 0.95024 0.07250  0.13698  0.02393  131 ASP B CA  
5607 C C   . ASP B 145 ? 0.53784 0.60716 0.87722 0.07707  0.11523  0.01756  131 ASP B C   
5608 O O   . ASP B 145 ? 0.45041 0.52471 0.81269 0.08600  0.10104  0.01542  131 ASP B O   
5609 C CB  . ASP B 145 ? 0.59298 0.70950 1.00952 0.08654  0.15311  0.02192  131 ASP B CB  
5610 C CG  . ASP B 145 ? 0.73473 0.83474 1.11776 0.10011  0.17124  0.01382  131 ASP B CG  
5611 O OD1 . ASP B 145 ? 0.69540 0.77550 1.02720 0.09619  0.18003  0.01209  131 ASP B OD1 
5612 O OD2 . ASP B 145 ? 0.73664 0.84385 1.14569 0.11508  0.17590  0.00820  131 ASP B OD2 
5617 N N   . GLY B 146 ? 0.47491 0.51820 0.76150 0.07132  0.11250  0.01604  132 GLY B N   
5618 C CA  . GLY B 146 ? 0.36715 0.38604 0.62146 0.07395  0.09424  0.01172  132 GLY B CA  
5619 C C   . GLY B 146 ? 0.40822 0.42797 0.66373 0.06497  0.06885  0.01505  132 GLY B C   
5620 O O   . GLY B 146 ? 0.35910 0.39798 0.64328 0.05705  0.06303  0.01814  132 GLY B O   
5624 N N   . ASN B 147 ? 0.43517 0.43359 0.65897 0.06614  0.05402  0.01364  133 ASN B N   
5625 C CA  . ASN B 147 ? 0.39893 0.39860 0.61867 0.05980  0.03055  0.01623  133 ASN B CA  
5626 C C   . ASN B 147 ? 0.41290 0.41103 0.61578 0.04552  0.02906  0.01671  133 ASN B C   
5627 O O   . ASN B 147 ? 0.38291 0.39157 0.59685 0.03928  0.01328  0.01652  133 ASN B O   
5628 C CB  . ASN B 147 ? 0.48826 0.46559 0.67771 0.06455  0.01848  0.01716  133 ASN B CB  
5629 C CG  . ASN B 147 ? 0.44832 0.42774 0.66084 0.07913  0.01411  0.01923  133 ASN B CG  
5630 O OD1 . ASN B 147 ? 0.38428 0.38739 0.63773 0.08508  0.01114  0.02062  133 ASN B OD1 
5631 N ND2 . ASN B 147 ? 0.41781 0.37247 0.60762 0.08498  0.01318  0.01987  133 ASN B ND2 
5638 N N   . ILE B 148 ? 0.41500 0.40056 0.59137 0.04100  0.04448  0.01673  134 ILE B N   
5639 C CA  . ILE B 148 ? 0.40887 0.39024 0.56824 0.02892  0.04307  0.01874  134 ILE B CA  
5640 C C   . ILE B 148 ? 0.39075 0.39164 0.58605 0.02284  0.05229  0.02252  134 ILE B C   
5641 O O   . ILE B 148 ? 0.43347 0.44488 0.65146 0.01581  0.04008  0.02168  134 ILE B O   
5642 C CB  . ILE B 148 ? 0.43323 0.39434 0.54909 0.02709  0.05330  0.01866  134 ILE B CB  
5643 C CG1 . ILE B 148 ? 0.46852 0.40958 0.55290 0.02942  0.04149  0.01515  134 ILE B CG1 
5644 C CG2 . ILE B 148 ? 0.46121 0.42138 0.56699 0.01626  0.05480  0.02315  134 ILE B CG2 
5645 C CD1 . ILE B 148 ? 0.48588 0.42113 0.57617 0.04090  0.04242  0.01179  134 ILE B CD1 
5657 N N   . LEU B 149 ? 0.32852 0.33466 0.52998 0.02537  0.07438  0.02639  135 LEU B N   
5658 C CA  . LEU B 149 ? 0.36915 0.39381 0.60761 0.01901  0.08616  0.03313  135 LEU B CA  
5659 C C   . LEU B 149 ? 0.34359 0.39211 0.63689 0.01980  0.07782  0.03093  135 LEU B C   
5660 O O   . LEU B 149 ? 0.31263 0.37644 0.64397 0.01138  0.08080  0.03484  135 LEU B O   
5661 C CB  . LEU B 149 ? 0.42095 0.44949 0.65339 0.02343  0.11359  0.03916  135 LEU B CB  
5662 C CG  . LEU B 149 ? 0.46792 0.47956 0.65211 0.02052  0.12324  0.04382  135 LEU B CG  
5663 C CD1 . LEU B 149 ? 0.43242 0.45312 0.61129 0.02597  0.15087  0.05005  135 LEU B CD1 
5664 C CD2 . LEU B 149 ? 0.35019 0.35763 0.53525 0.00824  0.11610  0.05124  135 LEU B CD2 
5676 N N   . GLY B 150 ? 0.35050 0.40282 0.65125 0.02961  0.06676  0.02530  136 GLY B N   
5677 C CA  . GLY B 150 ? 0.31561 0.39244 0.66676 0.03173  0.05484  0.02286  136 GLY B CA  
5678 C C   . GLY B 150 ? 0.30020 0.37951 0.65350 0.02661  0.02675  0.01725  136 GLY B C   
5679 O O   . GLY B 150 ? 0.29868 0.40077 0.69340 0.02758  0.01327  0.01392  136 GLY B O   
5683 N N   . HIS B 151 ? 0.29787 0.35644 0.60773 0.02167  0.01727  0.01542  137 HIS B N   
5684 C CA  . HIS B 151 ? 0.35573 0.41674 0.66136 0.01711  -0.00750 0.00896  137 HIS B CA  
5685 C C   . HIS B 151 ? 0.31439 0.38694 0.62859 0.02755  -0.02591 0.00703  137 HIS B C   
5686 O O   . HIS B 151 ? 0.29464 0.38764 0.63645 0.02616  -0.04435 0.00142  137 HIS B O   
5687 C CB  . HIS B 151 ? 0.33433 0.41087 0.67825 0.00539  -0.01232 0.00426  137 HIS B CB  
5688 C CG  . HIS B 151 ? 0.39151 0.45469 0.72655 -0.00475 0.00295  0.00844  137 HIS B CG  
5689 N ND1 . HIS B 151 ? 0.43190 0.47826 0.73596 -0.01114 -0.00423 0.00520  137 HIS B ND1 
5690 C CD2 . HIS B 151 ? 0.41469 0.47999 0.76858 -0.00872 0.02538  0.01725  137 HIS B CD2 
5691 C CE1 . HIS B 151 ? 0.43636 0.47405 0.74170 -0.01825 0.01180  0.01217  137 HIS B CE1 
5692 N NE2 . HIS B 151 ? 0.41519 0.46405 0.74895 -0.01713 0.03002  0.02041  137 HIS B NE2 
5700 N N   . LYS B 152 ? 0.34043 0.39945 0.63102 0.03835  -0.02168 0.01172  138 LYS B N   
5701 C CA  . LYS B 152 ? 0.31228 0.37887 0.60987 0.05026  -0.03705 0.01385  138 LYS B CA  
5702 C C   . LYS B 152 ? 0.41102 0.46092 0.66445 0.05187  -0.05208 0.01619  138 LYS B C   
5703 O O   . LYS B 152 ? 0.42033 0.47078 0.67169 0.06270  -0.06280 0.02184  138 LYS B O   
5704 C CB  . LYS B 152 ? 0.34442 0.40721 0.65388 0.06277  -0.02160 0.01812  138 LYS B CB  
5705 C CG  . LYS B 152 ? 0.33107 0.41328 0.68499 0.06292  -0.00361 0.01712  138 LYS B CG  
5706 C CD  . LYS B 152 ? 0.33153 0.40909 0.69357 0.07682  0.01347  0.01896  138 LYS B CD  
5707 C CE  . LYS B 152 ? 0.33077 0.43278 0.74061 0.07815  0.03244  0.01877  138 LYS B CE  
5708 N NZ  . LYS B 152 ? 0.41497 0.51328 0.83209 0.09290  0.05145  0.01816  138 LYS B NZ  
5722 N N   . LEU B 153 ? 0.38461 0.42053 0.60490 0.04188  -0.05237 0.01348  139 LEU B N   
5723 C CA  . LEU B 153 ? 0.41785 0.43911 0.59661 0.04246  -0.06331 0.01649  139 LEU B CA  
5724 C C   . LEU B 153 ? 0.42916 0.46744 0.60718 0.03896  -0.08442 0.01091  139 LEU B C   
5725 O O   . LEU B 153 ? 0.39710 0.44809 0.59478 0.03054  -0.08728 0.00147  139 LEU B O   
5726 C CB  . LEU B 153 ? 0.31563 0.31279 0.45840 0.03469  -0.05067 0.01640  139 LEU B CB  
5727 C CG  . LEU B 153 ? 0.41806 0.39790 0.55400 0.03733  -0.03069 0.01892  139 LEU B CG  
5728 C CD1 . LEU B 153 ? 0.43886 0.39895 0.53915 0.02911  -0.02279 0.01818  139 LEU B CD1 
5729 C CD2 . LEU B 153 ? 0.44932 0.41941 0.58310 0.04916  -0.03134 0.02443  139 LEU B CD2 
5741 N N   . GLU B 154 ? 0.43885 0.47710 0.59410 0.04564  -0.09885 0.01670  140 GLU B N   
5742 C CA  . GLU B 154 ? 0.46352 0.51819 0.60860 0.04374  -0.11882 0.01065  140 GLU B CA  
5743 C C   . GLU B 154 ? 0.37518 0.41860 0.49245 0.03294  -0.11477 0.00302  140 GLU B C   
5744 O O   . GLU B 154 ? 0.39966 0.42054 0.49246 0.02954  -0.10076 0.00776  140 GLU B O   
5745 C CB  . GLU B 154 ? 0.49336 0.55016 0.61498 0.05446  -0.13269 0.02235  140 GLU B CB  
5746 C CG  . GLU B 154 ? 0.52049 0.59302 0.67205 0.06703  -0.14205 0.03017  140 GLU B CG  
5747 C CD  . GLU B 154 ? 0.60526 0.68008 0.73215 0.07808  -0.15669 0.04486  140 GLU B CD  
5748 O OE1 . GLU B 154 ? 0.59414 0.65780 0.67997 0.07522  -0.15716 0.04930  140 GLU B OE1 
5749 O OE2 . GLU B 154 ? 0.61314 0.70195 0.76299 0.09007  -0.16719 0.05341  140 GLU B OE2 
5756 N N   . TYR B 155 ? 0.44726 0.50736 0.57048 0.02792  -0.12803 -0.01018 141 TYR B N   
5757 C CA  . TYR B 155 ? 0.47889 0.53060 0.57893 0.01934  -0.12601 -0.01930 141 TYR B CA  
5758 C C   . TYR B 155 ? 0.49093 0.54424 0.54945 0.02447  -0.13660 -0.01575 141 TYR B C   
5759 O O   . TYR B 155 ? 0.45193 0.52545 0.50595 0.02737  -0.15443 -0.02408 141 TYR B O   
5760 C CB  . TYR B 155 ? 0.32863 0.39516 0.45888 0.01143  -0.13364 -0.03732 141 TYR B CB  
5761 C CG  . TYR B 155 ? 0.36458 0.42040 0.47759 0.00333  -0.12977 -0.04769 141 TYR B CG  
5762 C CD1 . TYR B 155 ? 0.42154 0.45819 0.53845 -0.00376 -0.11155 -0.04461 141 TYR B CD1 
5763 C CD2 . TYR B 155 ? 0.40336 0.46945 0.49599 0.00392  -0.14430 -0.06058 141 TYR B CD2 
5764 C CE1 . TYR B 155 ? 0.33891 0.36602 0.44382 -0.00981 -0.10841 -0.05302 141 TYR B CE1 
5765 C CE2 . TYR B 155 ? 0.39085 0.44730 0.47081 -0.00213 -0.13983 -0.07125 141 TYR B CE2 
5766 C CZ  . TYR B 155 ? 0.36771 0.40423 0.45589 -0.00887 -0.12210 -0.06689 141 TYR B CZ  
5767 O OH  . TYR B 155 ? 0.35204 0.37919 0.43105 -0.01359 -0.11807 -0.07644 141 TYR B OH  
5777 N N   . ASN B 156 ? 0.50866 0.54180 0.53664 0.02555  -0.12539 -0.00318 142 ASN B N   
5778 C CA  . ASN B 156 ? 0.60113 0.63494 0.59055 0.02984  -0.13156 0.00392  142 ASN B CA  
5779 C C   . ASN B 156 ? 0.56095 0.57077 0.52580 0.02545  -0.11542 0.01250  142 ASN B C   
5780 O O   . ASN B 156 ? 0.49143 0.48373 0.46604 0.02284  -0.10216 0.01722  142 ASN B O   
5781 C CB  . ASN B 156 ? 0.65013 0.69251 0.63605 0.04144  -0.14219 0.01878  142 ASN B CB  
5782 C CG  . ASN B 156 ? 0.65745 0.68133 0.65626 0.04543  -0.13068 0.03305  142 ASN B CG  
5783 O OD1 . ASN B 156 ? 0.71275 0.74194 0.74490 0.04870  -0.13073 0.03164  142 ASN B OD1 
5784 N ND2 . ASN B 156 ? 0.72482 0.72736 0.69953 0.04512  -0.12028 0.04568  142 ASN B ND2 
5791 N N   . GLY B 157 ? 0.62453 0.63585 0.55788 0.02479  -0.11679 0.01347  143 GLY B N   
5792 C CA  . GLY B 157 ? 0.64683 0.63941 0.55789 0.02126  -0.10375 0.02358  143 GLY B CA  
5793 C C   . GLY B 157 ? 0.68240 0.66507 0.58381 0.02742  -0.10232 0.04381  143 GLY B C   
5794 O O   . GLY B 157 ? 0.62780 0.61612 0.54132 0.03538  -0.11029 0.05091  143 GLY B O   
5798 N N   . TRP B 158 ? 0.61570 0.58333 0.49844 0.02368  -0.09216 0.05354  144 TRP B N   
5799 C CA  . TRP B 158 ? 0.66605 0.61922 0.54357 0.02765  -0.08880 0.07305  144 TRP B CA  
5800 C C   . TRP B 158 ? 0.63196 0.57510 0.48862 0.02134  -0.07902 0.08121  144 TRP B C   
5801 O O   . TRP B 158 ? 0.56005 0.50846 0.40734 0.01503  -0.07484 0.07137  144 TRP B O   
5802 C CB  . TRP B 158 ? 0.64722 0.58201 0.54878 0.02821  -0.08247 0.07339  144 TRP B CB  
5803 C CG  . TRP B 158 ? 0.55790 0.47914 0.46325 0.01894  -0.07079 0.06298  144 TRP B CG  
5804 C CD1 . TRP B 158 ? 0.58929 0.49166 0.48649 0.01290  -0.06111 0.06722  144 TRP B CD1 
5805 C CD2 . TRP B 158 ? 0.57609 0.50284 0.49492 0.01467  -0.06836 0.04764  144 TRP B CD2 
5806 N NE1 . TRP B 158 ? 0.66428 0.56154 0.56599 0.00609  -0.05398 0.05533  144 TRP B NE1 
5807 C CE2 . TRP B 158 ? 0.57391 0.48512 0.48846 0.00727  -0.05736 0.04468  144 TRP B CE2 
5808 C CE3 . TRP B 158 ? 0.67853 0.62216 0.61480 0.01603  -0.07474 0.03687  144 TRP B CE3 
5809 C CZ2 . TRP B 158 ? 0.51120 0.42307 0.43522 0.00240  -0.05194 0.03396  144 TRP B CZ2 
5810 C CZ3 . TRP B 158 ? 0.57529 0.51778 0.52468 0.00997  -0.06807 0.02606  144 TRP B CZ3 
5811 C CH2 . TRP B 158 ? 0.46886 0.39549 0.41054 0.00382  -0.05648 0.02594  144 TRP B CH2 
5822 N N   . CYS B 159 ? 0.73068 0.65939 0.58397 0.02321  -0.07520 0.09972  145 CYS B N   
5823 C CA  . CYS B 159 ? 0.79202 0.70907 0.63343 0.01611  -0.06493 0.10966  145 CYS B CA  
5824 C C   . CYS B 159 ? 0.69450 0.58405 0.55308 0.01229  -0.05746 0.11323  145 CYS B C   
5825 O O   . CYS B 159 ? 0.74073 0.61942 0.61298 0.01900  -0.06018 0.12035  145 CYS B O   
5826 C CB  . CYS B 159 ? 0.65887 0.58450 0.48042 0.02093  -0.06655 0.13069  145 CYS B CB  
5827 S SG  . CYS B 159 ? 0.75527 0.71528 0.54897 0.02629  -0.07490 0.12498  145 CYS B SG  
5828 N N   . GLY B 160 ? 0.62024 0.49944 0.47918 0.00221  -0.04885 0.10697  146 GLY B N   
5829 C CA  . GLY B 160 ? 0.62980 0.48386 0.50265 -0.00229 -0.04284 0.10719  146 GLY B CA  
5830 C C   . GLY B 160 ? 0.58824 0.43431 0.47631 0.00087  -0.04324 0.09312  146 GLY B C   
5831 O O   . GLY B 160 ? 0.57422 0.43439 0.46544 0.00503  -0.04721 0.08362  146 GLY B O   
5832 N N   . ASP B 161 ? 0.62436 0.44769 0.52324 -0.00145 -0.03830 0.09127  147 ASP B N   
5833 C CA  . ASP B 161 ? 0.60134 0.40658 0.50212 -0.00800 -0.03414 0.10082  147 ASP B CA  
5834 C C   . ASP B 161 ? 0.62067 0.43205 0.51191 -0.01959 -0.03055 0.09683  147 ASP B C   
5835 O O   . ASP B 161 ? 0.53578 0.35734 0.42180 -0.02267 -0.03027 0.08303  147 ASP B O   
5836 C CB  . ASP B 161 ? 0.63807 0.41738 0.55489 -0.00770 -0.03082 0.09342  147 ASP B CB  
5837 C CG  . ASP B 161 ? 0.67972 0.45100 0.61096 0.00481  -0.03326 0.09958  147 ASP B CG  
5838 O OD1 . ASP B 161 ? 0.75682 0.54326 0.68540 0.01276  -0.03901 0.11183  147 ASP B OD1 
5839 O OD2 . ASP B 161 ? 0.60886 0.35977 0.55449 0.00741  -0.02992 0.09124  147 ASP B OD2 
5840 N N   . ASN B 162 ? 0.58060 0.38658 0.47232 -0.02561 -0.02741 0.11066  148 ASN B N   
5841 C CA  . ASN B 162 ? 0.52605 0.33951 0.41385 -0.03648 -0.02352 0.10846  148 ASN B CA  
5842 C C   . ASN B 162 ? 0.53198 0.33751 0.42531 -0.04302 -0.02345 0.08953  148 ASN B C   
5843 O O   . ASN B 162 ? 0.53473 0.32184 0.43682 -0.04193 -0.02410 0.08104  148 ASN B O   
5844 C CB  . ASN B 162 ? 0.50829 0.31267 0.40409 -0.04312 -0.01863 0.12661  148 ASN B CB  
5845 C CG  . ASN B 162 ? 0.55312 0.36742 0.43918 -0.03600 -0.01791 0.14876  148 ASN B CG  
5846 O OD1 . ASN B 162 ? 0.57077 0.40886 0.43872 -0.03144 -0.01901 0.14975  148 ASN B OD1 
5847 N ND2 . ASN B 162 ? 0.59224 0.38813 0.49009 -0.03444 -0.01640 0.16646  148 ASN B ND2 
5854 N N   . VAL B 163 ? 0.48818 0.30886 0.37564 -0.04882 -0.02270 0.08276  149 VAL B N   
5855 C CA  . VAL B 163 ? 0.47227 0.29028 0.36154 -0.05420 -0.02398 0.06680  149 VAL B CA  
5856 C C   . VAL B 163 ? 0.47641 0.28498 0.37772 -0.06544 -0.02317 0.06813  149 VAL B C   
5857 O O   . VAL B 163 ? 0.47130 0.29290 0.37551 -0.07200 -0.02119 0.07361  149 VAL B O   
5858 C CB  . VAL B 163 ? 0.45175 0.29054 0.33236 -0.05363 -0.02458 0.06013  149 VAL B CB  
5859 C CG1 . VAL B 163 ? 0.43649 0.27363 0.31762 -0.05824 -0.02663 0.04706  149 VAL B CG1 
5860 C CG2 . VAL B 163 ? 0.48538 0.33286 0.35934 -0.04398 -0.02599 0.05803  149 VAL B CG2 
5870 N N   . TYR B 164 ? 0.47305 0.25955 0.38403 -0.06771 -0.02461 0.06177  150 TYR B N   
5871 C CA  . TYR B 164 ? 0.44283 0.21813 0.36999 -0.07945 -0.02538 0.06062  150 TYR B CA  
5872 C C   . TYR B 164 ? 0.49632 0.28047 0.42077 -0.08584 -0.03032 0.04439  150 TYR B C   
5873 O O   . TYR B 164 ? 0.51391 0.29510 0.42767 -0.08158 -0.03344 0.02940  150 TYR B O   
5874 C CB  . TYR B 164 ? 0.45573 0.20219 0.39635 -0.07893 -0.02575 0.05775  150 TYR B CB  
5875 C CG  . TYR B 164 ? 0.52888 0.26561 0.48104 -0.07734 -0.02127 0.07981  150 TYR B CG  
5876 C CD1 . TYR B 164 ? 0.49538 0.23896 0.43690 -0.06556 -0.01955 0.09277  150 TYR B CD1 
5877 C CD2 . TYR B 164 ? 0.50693 0.22901 0.48174 -0.08779 -0.01926 0.08891  150 TYR B CD2 
5878 C CE1 . TYR B 164 ? 0.48621 0.22290 0.43533 -0.06289 -0.01627 0.11548  150 TYR B CE1 
5879 C CE2 . TYR B 164 ? 0.59461 0.30782 0.57978 -0.08597 -0.01415 0.11294  150 TYR B CE2 
5880 C CZ  . TYR B 164 ? 0.53338 0.25438 0.50355 -0.07284 -0.01282 0.12686  150 TYR B CZ  
5881 O OH  . TYR B 164 ? 0.52948 0.24328 0.50724 -0.06986 -0.00855 0.15305  150 TYR B OH  
5891 N N   . ILE B 165 ? 0.47455 0.27153 0.40897 -0.09543 -0.03069 0.04862  151 ILE B N   
5892 C CA  . ILE B 165 ? 0.44290 0.25421 0.37608 -0.10052 -0.03655 0.03678  151 ILE B CA  
5893 C C   . ILE B 165 ? 0.48692 0.28923 0.44069 -0.11331 -0.04201 0.02954  151 ILE B C   
5894 O O   . ILE B 165 ? 0.44007 0.23608 0.41486 -0.12134 -0.03841 0.04052  151 ILE B O   
5895 C CB  . ILE B 165 ? 0.43206 0.26988 0.36393 -0.10012 -0.03340 0.04573  151 ILE B CB  
5896 C CG1 . ILE B 165 ? 0.48356 0.32977 0.39628 -0.08807 -0.03048 0.04727  151 ILE B CG1 
5897 C CG2 . ILE B 165 ? 0.41787 0.27063 0.35613 -0.10630 -0.04020 0.03661  151 ILE B CG2 
5898 C CD1 . ILE B 165 ? 0.43229 0.30149 0.34406 -0.08601 -0.02610 0.05490  151 ILE B CD1 
5910 N N   . THR B 166 ? 0.45718 0.25972 0.40535 -0.11534 -0.05093 0.01134  152 THR B N   
5911 C CA  . THR B 166 ? 0.47187 0.26926 0.43863 -0.12768 -0.05955 -0.00049 152 THR B CA  
5912 C C   . THR B 166 ? 0.47620 0.29644 0.43666 -0.12968 -0.06911 -0.01011 152 THR B C   
5913 O O   . THR B 166 ? 0.47665 0.30798 0.41403 -0.12010 -0.06958 -0.01204 152 THR B O   
5914 C CB  . THR B 166 ? 0.47653 0.24673 0.44159 -0.12732 -0.06350 -0.01785 152 THR B CB  
5915 O OG1 . THR B 166 ? 0.56570 0.33664 0.50133 -0.11560 -0.06425 -0.02921 152 THR B OG1 
5916 C CG2 . THR B 166 ? 0.48888 0.23490 0.46764 -0.12595 -0.05519 -0.00674 152 THR B CG2 
5924 N N   . ALA B 167 ? 0.45179 0.27949 0.43574 -0.14225 -0.07706 -0.01494 153 ALA B N   
5925 C CA  . ALA B 167 ? 0.48644 0.33760 0.46838 -0.14435 -0.08852 -0.02336 153 ALA B CA  
5926 C C   . ALA B 167 ? 0.50483 0.34865 0.46577 -0.14191 -0.10030 -0.04560 153 ALA B C   
5927 O O   . ALA B 167 ? 0.49038 0.31096 0.45173 -0.14462 -0.10234 -0.05937 153 ALA B O   
5928 C CB  . ALA B 167 ? 0.47118 0.33616 0.48977 -0.15897 -0.09391 -0.02115 153 ALA B CB  
5934 N N   . ASP B 168 ? 0.60052 0.46471 0.54255 -0.13588 -0.10763 -0.04879 154 ASP B N   
5935 C CA  . ASP B 168 ? 0.56049 0.42488 0.47789 -0.13269 -0.11948 -0.06810 154 ASP B CA  
5936 C C   . ASP B 168 ? 0.58766 0.47958 0.51407 -0.13794 -0.13505 -0.07113 154 ASP B C   
5937 O O   . ASP B 168 ? 0.55767 0.46896 0.46758 -0.12950 -0.13784 -0.06420 154 ASP B O   
5938 C CB  . ASP B 168 ? 0.52372 0.38643 0.40534 -0.11768 -0.11196 -0.06530 154 ASP B CB  
5939 C CG  . ASP B 168 ? 0.66938 0.52769 0.52172 -0.11330 -0.11974 -0.08533 154 ASP B CG  
5940 O OD1 . ASP B 168 ? 0.64073 0.50595 0.49537 -0.12051 -0.13514 -0.10118 154 ASP B OD1 
5941 O OD2 . ASP B 168 ? 0.74388 0.59354 0.57113 -0.10251 -0.11035 -0.08581 154 ASP B OD2 
5946 N N   . LYS B 169 ? 0.56989 0.46365 0.52628 -0.15205 -0.14553 -0.08066 155 LYS B N   
5947 C CA  . LYS B 169 ? 0.65311 0.57585 0.62572 -0.15808 -0.16164 -0.08321 155 LYS B CA  
5948 C C   . LYS B 169 ? 0.74972 0.68517 0.68780 -0.15022 -0.17661 -0.09625 155 LYS B C   
5949 O O   . LYS B 169 ? 0.72285 0.68558 0.65977 -0.14613 -0.18546 -0.08865 155 LYS B O   
5950 C CB  . LYS B 169 ? 0.68492 0.60545 0.69820 -0.17595 -0.17117 -0.09437 155 LYS B CB  
5951 C CG  . LYS B 169 ? 0.83837 0.76202 0.89285 -0.18475 -0.15856 -0.07506 155 LYS B CG  
5952 C CD  . LYS B 169 ? 0.91637 0.82817 1.01182 -0.20297 -0.16374 -0.08495 155 LYS B CD  
5953 C CE  . LYS B 169 ? 0.90767 0.78048 0.99775 -0.20362 -0.15371 -0.08979 155 LYS B CE  
5954 N NZ  . LYS B 169 ? 0.99746 0.85787 1.12164 -0.21720 -0.15837 -0.10541 155 LYS B NZ  
5968 N N   . GLN B 170 ? 0.79519 0.71207 0.70465 -0.14704 -0.17919 -0.11526 156 GLN B N   
5969 C CA  . GLN B 170 ? 0.86385 0.79368 0.73429 -0.13829 -0.19156 -0.12683 156 GLN B CA  
5970 C C   . GLN B 170 ? 0.85497 0.80017 0.70190 -0.12389 -0.18384 -0.10516 156 GLN B C   
5971 O O   . GLN B 170 ? 0.86652 0.83748 0.70512 -0.11977 -0.19639 -0.10028 156 GLN B O   
5972 C CB  . GLN B 170 ? 0.93362 0.83932 0.77401 -0.13431 -0.18905 -0.14874 156 GLN B CB  
5973 C CG  . GLN B 170 ? 0.87434 0.77410 0.73171 -0.14502 -0.20132 -0.17687 156 GLN B CG  
5974 C CD  . GLN B 170 ? 0.90019 0.79012 0.72301 -0.13629 -0.19819 -0.20023 156 GLN B CD  
5975 O OE1 . GLN B 170 ? 0.89004 0.76062 0.68641 -0.12628 -0.18467 -0.19758 156 GLN B OE1 
5976 N NE2 . GLN B 170 ? 0.94029 0.84481 0.76223 -0.14120 -0.20975 -0.22293 156 GLN B NE2 
5985 N N   . LYS B 171 ? 0.76365 0.69328 0.60225 -0.11606 -0.16392 -0.09162 157 LYS B N   
5986 C CA  . LYS B 171 ? 0.79319 0.73363 0.61514 -0.10352 -0.15510 -0.07150 157 LYS B CA  
5987 C C   . LYS B 171 ? 0.73033 0.68633 0.58311 -0.10493 -0.15223 -0.05206 157 LYS B C   
5988 O O   . LYS B 171 ? 0.73186 0.69476 0.57735 -0.09512 -0.14445 -0.03569 157 LYS B O   
5989 C CB  . LYS B 171 ? 0.83122 0.75034 0.63563 -0.09518 -0.13599 -0.06687 157 LYS B CB  
5990 C CG  . LYS B 171 ? 0.92419 0.82742 0.69979 -0.09191 -0.13503 -0.08623 157 LYS B CG  
5991 C CD  . LYS B 171 ? 0.99295 0.91313 0.73458 -0.08618 -0.14737 -0.09473 157 LYS B CD  
5992 C CE  . LYS B 171 ? 1.03458 0.94095 0.74222 -0.07957 -0.14160 -0.11235 157 LYS B CE  
5993 N NZ  . LYS B 171 ? 1.26931 1.15455 0.98943 -0.08819 -0.14521 -0.13712 157 LYS B NZ  
6007 N N   . ASN B 172 ? 0.68080 0.64252 0.56958 -0.11677 -0.15734 -0.05385 158 ASN B N   
6008 C CA  . ASN B 172 ? 0.68535 0.66401 0.60498 -0.11783 -0.15304 -0.03706 158 ASN B CA  
6009 C C   . ASN B 172 ? 0.66536 0.63275 0.58228 -0.11037 -0.13306 -0.02216 158 ASN B C   
6010 O O   . ASN B 172 ? 0.60217 0.58258 0.52460 -0.10305 -0.12821 -0.00847 158 ASN B O   
6011 C CB  . ASN B 172 ? 0.72478 0.73193 0.64494 -0.11183 -0.16585 -0.03018 158 ASN B CB  
6012 C CG  . ASN B 172 ? 0.63450 0.66089 0.59095 -0.11248 -0.16178 -0.01563 158 ASN B CG  
6013 O OD1 . ASN B 172 ? 0.63966 0.66739 0.62776 -0.12271 -0.15747 -0.01575 158 ASN B OD1 
6014 N ND2 . ASN B 172 ? 0.66278 0.70386 0.61597 -0.10101 -0.16176 -0.00240 158 ASN B ND2 
6021 N N   . GLY B 173 ? 0.50788 0.45114 0.41782 -0.11181 -0.12236 -0.02581 159 GLY B N   
6022 C CA  . GLY B 173 ? 0.46176 0.39481 0.36809 -0.10507 -0.10564 -0.01391 159 GLY B CA  
6023 C C   . GLY B 173 ? 0.44582 0.35683 0.35873 -0.11049 -0.09704 -0.01640 159 GLY B C   
6024 O O   . GLY B 173 ? 0.47411 0.38082 0.40744 -0.12155 -0.10112 -0.02178 159 GLY B O   
6028 N N   . ILE B 174 ? 0.46638 0.36347 0.36463 -0.10263 -0.08545 -0.01160 160 ILE B N   
6029 C CA  . ILE B 174 ? 0.49689 0.37362 0.40064 -0.10501 -0.07698 -0.01060 160 ILE B CA  
6030 C C   . ILE B 174 ? 0.54503 0.40453 0.42565 -0.09654 -0.07238 -0.01684 160 ILE B C   
6031 O O   . ILE B 174 ? 0.50021 0.36534 0.36131 -0.08819 -0.07177 -0.01748 160 ILE B O   
6032 C CB  . ILE B 174 ? 0.48710 0.36889 0.40313 -0.10361 -0.06604 0.00515  160 ILE B CB  
6033 C CG1 . ILE B 174 ? 0.49261 0.38284 0.39453 -0.09239 -0.06047 0.01152  160 ILE B CG1 
6034 C CG2 . ILE B 174 ? 0.51263 0.41220 0.45432 -0.11208 -0.06773 0.01133  160 ILE B CG2 
6035 C CD1 . ILE B 174 ? 0.46515 0.35787 0.37245 -0.08914 -0.05018 0.02278  160 ILE B CD1 
6047 N N   . LYS B 175 ? 0.49070 0.32934 0.37658 -0.09858 -0.06832 -0.02022 161 LYS B N   
6048 C CA  . LYS B 175 ? 0.49970 0.32208 0.37082 -0.08985 -0.06156 -0.02408 161 LYS B CA  
6049 C C   . LYS B 175 ? 0.50723 0.32069 0.38953 -0.08759 -0.05252 -0.01102 161 LYS B C   
6050 O O   . LYS B 175 ? 0.50263 0.31643 0.40306 -0.09444 -0.05152 -0.00172 161 LYS B O   
6051 C CB  . LYS B 175 ? 0.52268 0.32677 0.38945 -0.09195 -0.06596 -0.04268 161 LYS B CB  
6052 C CG  . LYS B 175 ? 0.59871 0.41133 0.44238 -0.08924 -0.07318 -0.05723 161 LYS B CG  
6053 C CD  . LYS B 175 ? 0.78219 0.57544 0.61839 -0.08896 -0.07533 -0.07843 161 LYS B CD  
6054 C CE  . LYS B 175 ? 0.77522 0.57794 0.57958 -0.08229 -0.07878 -0.09176 161 LYS B CE  
6055 N NZ  . LYS B 175 ? 0.78246 0.56611 0.57702 -0.07953 -0.07807 -0.11446 161 LYS B NZ  
6058 N N   . ALA B 176 ? 0.46730 0.27486 0.33902 -0.07763 -0.04587 -0.00937 162 ALA B N   
6059 C CA  . ALA B 176 ? 0.44835 0.24951 0.32819 -0.07369 -0.03933 0.00272  162 ALA B CA  
6060 C C   . ALA B 176 ? 0.50854 0.29503 0.38310 -0.06470 -0.03496 -0.00280 162 ALA B C   
6061 O O   . ALA B 176 ? 0.45208 0.24027 0.31318 -0.05929 -0.03376 -0.01262 162 ALA B O   
6062 C CB  . ALA B 176 ? 0.47653 0.29637 0.35401 -0.06978 -0.03617 0.01474  162 ALA B CB  
6068 N N   . ASN B 177 ? 0.55409 0.32762 0.44034 -0.06248 -0.03187 0.00520  163 ASN B N   
6069 C CA  . ASN B 177 ? 0.52824 0.28659 0.41636 -0.05348 -0.02791 0.00105  163 ASN B CA  
6070 C C   . ASN B 177 ? 0.50813 0.26692 0.40503 -0.04790 -0.02537 0.01795  163 ASN B C   
6071 O O   . ASN B 177 ? 0.55718 0.31407 0.46301 -0.05303 -0.02616 0.03075  163 ASN B O   
6072 C CB  . ASN B 177 ? 0.59736 0.33165 0.49503 -0.05704 -0.02950 -0.01119 163 ASN B CB  
6073 C CG  . ASN B 177 ? 0.63950 0.35649 0.54409 -0.04656 -0.02456 -0.01487 163 ASN B CG  
6074 O OD1 . ASN B 177 ? 0.53385 0.24372 0.45183 -0.04219 -0.02266 -0.00074 163 ASN B OD1 
6075 N ND2 . ASN B 177 ? 0.86640 0.57777 0.76173 -0.04155 -0.02226 -0.03356 163 ASN B ND2 
6082 N N   . PHE B 178 ? 0.48853 0.25185 0.38331 -0.03739 -0.02240 0.01876  164 PHE B N   
6083 C CA  . PHE B 178 ? 0.50708 0.27345 0.40919 -0.03075 -0.02237 0.03371  164 PHE B CA  
6084 C C   . PHE B 178 ? 0.49624 0.26676 0.40098 -0.01942 -0.01984 0.02973  164 PHE B C   
6085 O O   . PHE B 178 ? 0.52843 0.30618 0.42661 -0.01768 -0.01675 0.01882  164 PHE B O   
6086 C CB  . PHE B 178 ? 0.49392 0.28063 0.38933 -0.03370 -0.02450 0.04516  164 PHE B CB  
6087 C CG  . PHE B 178 ? 0.46361 0.26902 0.34925 -0.03356 -0.02452 0.03817  164 PHE B CG  
6088 C CD1 . PHE B 178 ? 0.46023 0.27027 0.33946 -0.04088 -0.02499 0.03115  164 PHE B CD1 
6089 C CD2 . PHE B 178 ? 0.46876 0.28726 0.35471 -0.02617 -0.02483 0.03923  164 PHE B CD2 
6090 C CE1 . PHE B 178 ? 0.50207 0.32737 0.37491 -0.04004 -0.02474 0.02721  164 PHE B CE1 
6091 C CE2 . PHE B 178 ? 0.45478 0.28785 0.33634 -0.02671 -0.02434 0.03366  164 PHE B CE2 
6092 C CZ  . PHE B 178 ? 0.40666 0.24211 0.28144 -0.03326 -0.02379 0.02863  164 PHE B CZ  
6102 N N   . LYS B 179 ? 0.50129 0.26871 0.41717 -0.01153 -0.02101 0.04035  165 LYS B N   
6103 C CA  . LYS B 179 ? 0.54904 0.32264 0.47390 -0.00022 -0.01957 0.03857  165 LYS B CA  
6104 C C   . LYS B 179 ? 0.48030 0.27669 0.40402 0.00304  -0.02472 0.04832  165 LYS B C   
6105 O O   . LYS B 179 ? 0.50767 0.30982 0.42542 0.00038  -0.02938 0.06030  165 LYS B O   
6106 C CB  . LYS B 179 ? 0.58932 0.34390 0.53174 0.00829  -0.01880 0.04255  165 LYS B CB  
6107 C CG  . LYS B 179 ? 0.52959 0.26050 0.47638 0.00728  -0.01349 0.02776  165 LYS B CG  
6108 C CD  . LYS B 179 ? 0.57893 0.28802 0.54716 0.01583  -0.01301 0.03310  165 LYS B CD  
6109 C CE  . LYS B 179 ? 0.51720 0.20319 0.49173 0.01724  -0.00708 0.01319  165 LYS B CE  
6110 N NZ  . LYS B 179 ? 0.60637 0.26659 0.60568 0.02475  -0.00681 0.01867  165 LYS B NZ  
6124 N N   . ILE B 180 ? 0.46752 0.27789 0.39762 0.00868  -0.02347 0.04231  166 ILE B N   
6125 C CA  . ILE B 180 ? 0.52989 0.36195 0.46427 0.01251  -0.02978 0.04771  166 ILE B CA  
6126 C C   . ILE B 180 ? 0.50731 0.34264 0.46259 0.02403  -0.03091 0.04935  166 ILE B C   
6127 O O   . ILE B 180 ? 0.49714 0.32527 0.46332 0.02832  -0.02327 0.04117  166 ILE B O   
6128 C CB  . ILE B 180 ? 0.58743 0.43567 0.51770 0.00749  -0.02819 0.03925  166 ILE B CB  
6129 C CG1 . ILE B 180 ? 0.54326 0.38940 0.45590 -0.00249 -0.02746 0.03810  166 ILE B CG1 
6130 C CG2 . ILE B 180 ? 0.51321 0.38286 0.45190 0.01099  -0.03597 0.04142  166 ILE B CG2 
6131 C CD1 . ILE B 180 ? 0.51341 0.36332 0.41664 -0.00503 -0.03326 0.04791  166 ILE B CD1 
6143 N N   . ARG B 181 ? 0.46688 0.31521 0.42755 0.02979  -0.04051 0.05955  167 ARG B N   
6144 C CA  . ARG B 181 ? 0.55132 0.40536 0.53450 0.04186  -0.04451 0.06394  167 ARG B CA  
6145 C C   . ARG B 181 ? 0.47323 0.35562 0.46535 0.04396  -0.05328 0.06181  167 ARG B C   
6146 O O   . ARG B 181 ? 0.56080 0.45644 0.54602 0.04612  -0.06491 0.07008  167 ARG B O   
6147 C CB  . ARG B 181 ? 0.60893 0.45143 0.59261 0.04831  -0.05036 0.08064  167 ARG B CB  
6148 C CG  . ARG B 181 ? 0.57776 0.39025 0.55813 0.04492  -0.04243 0.08192  167 ARG B CG  
6149 C CD  . ARG B 181 ? 0.65141 0.45362 0.62588 0.04582  -0.04749 0.10184  167 ARG B CD  
6150 N NE  . ARG B 181 ? 0.72517 0.49937 0.69821 0.03870  -0.04016 0.10138  167 ARG B NE  
6151 C CZ  . ARG B 181 ? 0.61888 0.36876 0.60977 0.04313  -0.03480 0.09666  167 ARG B CZ  
6152 N NH1 . ARG B 181 ? 0.69124 0.44148 0.70290 0.05574  -0.03436 0.09304  167 ARG B NH1 
6153 N NH2 . ARG B 181 ? 0.65926 0.38450 0.64959 0.03480  -0.02979 0.09410  167 ARG B NH2 
6167 N N   . HIS B 182 ? 0.47881 0.37118 0.48680 0.04324  -0.04758 0.05052  168 HIS B N   
6168 C CA  . HIS B 182 ? 0.42574 0.34414 0.44923 0.04359  -0.05549 0.04628  168 HIS B CA  
6169 C C   . HIS B 182 ? 0.40663 0.33827 0.45698 0.05559  -0.06386 0.05164  168 HIS B C   
6170 O O   . HIS B 182 ? 0.45300 0.37860 0.52360 0.06297  -0.05610 0.05128  168 HIS B O   
6171 C CB  . HIS B 182 ? 0.44575 0.36955 0.48061 0.03762  -0.04477 0.03502  168 HIS B CB  
6172 C CG  . HIS B 182 ? 0.40566 0.31942 0.41687 0.02701  -0.03816 0.03079  168 HIS B CG  
6173 N ND1 . HIS B 182 ? 0.45247 0.37216 0.44822 0.02040  -0.04554 0.03000  168 HIS B ND1 
6174 C CD2 . HIS B 182 ? 0.42851 0.32842 0.42934 0.02281  -0.02542 0.02680  168 HIS B CD2 
6175 C CE1 . HIS B 182 ? 0.44972 0.35931 0.42979 0.01276  -0.03764 0.02688  168 HIS B CE1 
6176 N NE2 . HIS B 182 ? 0.45712 0.35516 0.43883 0.01388  -0.02628 0.02530  168 HIS B NE2 
6184 N N   . ASN B 183 ? 0.39478 0.34604 0.44548 0.05836  -0.08003 0.05576  169 ASN B N   
6185 C CA  . ASN B 183 ? 0.43911 0.40778 0.51691 0.07009  -0.09117 0.06106  169 ASN B CA  
6186 C C   . ASN B 183 ? 0.44982 0.43571 0.56469 0.07020  -0.08688 0.05010  169 ASN B C   
6187 O O   . ASN B 183 ? 0.40203 0.39650 0.52046 0.06040  -0.08360 0.03921  169 ASN B O   
6188 C CB  . ASN B 183 ? 0.46687 0.45644 0.53292 0.07258  -0.11122 0.06607  169 ASN B CB  
6189 C CG  . ASN B 183 ? 0.53470 0.51097 0.56974 0.07609  -0.11508 0.08262  169 ASN B CG  
6190 O OD1 . ASN B 183 ? 0.49849 0.44952 0.52919 0.07800  -0.10481 0.09156  169 ASN B OD1 
6191 N ND2 . ASN B 183 ? 0.53981 0.53350 0.55388 0.07691  -0.12956 0.08651  169 ASN B ND2 
6198 N N   . ILE B 184 ? 0.37534 0.36624 0.52088 0.08160  -0.08597 0.05406  170 ILE B N   
6199 C CA  . ILE B 184 ? 0.38204 0.39307 0.56904 0.08333  -0.08128 0.04602  170 ILE B CA  
6200 C C   . ILE B 184 ? 0.44835 0.49095 0.66077 0.08887  -0.10268 0.04740  170 ILE B C   
6201 O O   . ILE B 184 ? 0.43488 0.48125 0.64350 0.09932  -0.11728 0.05876  170 ILE B O   
6202 C CB  . ILE B 184 ? 0.41699 0.41666 0.62532 0.09337  -0.06539 0.04742  170 ILE B CB  
6203 C CG1 . ILE B 184 ? 0.37705 0.34846 0.55880 0.08697  -0.04549 0.04225  170 ILE B CG1 
6204 C CG2 . ILE B 184 ? 0.45045 0.47590 0.70603 0.09662  -0.06028 0.04130  170 ILE B CG2 
6205 C CD1 . ILE B 184 ? 0.44133 0.39341 0.63109 0.09795  -0.03239 0.04275  170 ILE B CD1 
6217 N N   . GLU B 185 ? 0.48232 0.54816 0.72199 0.08176  -0.10522 0.03635  171 GLU B N   
6218 C CA  . GLU B 185 ? 0.62443 0.72268 0.88828 0.08446  -0.12819 0.03353  171 GLU B CA  
6219 C C   . GLU B 185 ? 0.61689 0.72868 0.90852 0.10108  -0.13809 0.04418  171 GLU B C   
6220 O O   . GLU B 185 ? 0.63642 0.76120 0.91918 0.10878  -0.15977 0.05157  171 GLU B O   
6221 C CB  . GLU B 185 ? 0.59355 0.71262 0.89535 0.07411  -0.12560 0.01974  171 GLU B CB  
6222 C CG  . GLU B 185 ? 0.64897 0.75733 0.92812 0.05852  -0.11984 0.00972  171 GLU B CG  
6223 C CD  . GLU B 185 ? 0.80314 0.93074 1.07984 0.05262  -0.14255 -0.00134 171 GLU B CD  
6224 O OE1 . GLU B 185 ? 0.79784 0.94118 1.06805 0.06112  -0.16387 0.00136  171 GLU B OE1 
6225 O OE2 . GLU B 185 ? 0.78321 0.91025 1.06440 0.04005  -0.13926 -0.01299 171 GLU B OE2 
6232 N N   . ASP B 186 ? 0.70396 0.81398 1.02911 0.10790  -0.12212 0.04558  172 ASP B N   
6233 C CA  . ASP B 186 ? 0.82616 0.94869 1.18364 0.12519  -0.12994 0.05552  172 ASP B CA  
6234 C C   . ASP B 186 ? 0.75575 0.85306 1.08340 0.13658  -0.13280 0.07139  172 ASP B C   
6235 O O   . ASP B 186 ? 0.72686 0.83389 1.07701 0.15220  -0.14397 0.08295  172 ASP B O   
6236 C CB  . ASP B 186 ? 0.90003 1.02656 1.30133 0.13015  -0.10871 0.05143  172 ASP B CB  
6237 C CG  . ASP B 186 ? 0.98610 1.14199 1.42816 0.12026  -0.10601 0.03967  172 ASP B CG  
6238 O OD1 . ASP B 186 ? 0.96081 1.12708 1.39337 0.10739  -0.11812 0.03215  172 ASP B OD1 
6239 O OD2 . ASP B 186 ? 1.01516 1.18383 1.50101 0.12543  -0.09102 0.03779  172 ASP B OD2 
6244 N N   . GLY B 187 ? 0.62885 0.69476 0.91031 0.12924  -0.12329 0.07323  173 GLY B N   
6245 C CA  . GLY B 187 ? 0.54126 0.58015 0.79836 0.13792  -0.12324 0.08861  173 GLY B CA  
6246 C C   . GLY B 187 ? 0.53435 0.53790 0.77804 0.13460  -0.09900 0.08433  173 GLY B C   
6247 O O   . GLY B 187 ? 0.56789 0.57140 0.83123 0.13249  -0.08173 0.07219  173 GLY B O   
6251 N N   . GLY B 188 ? 0.55926 0.53398 0.77005 0.13407  -0.09747 0.09417  174 GLY B N   
6252 C CA  . GLY B 188 ? 0.54995 0.49107 0.74383 0.12877  -0.07759 0.08798  174 GLY B CA  
6253 C C   . GLY B 188 ? 0.51041 0.44371 0.66596 0.11147  -0.07322 0.08057  174 GLY B C   
6254 O O   . GLY B 188 ? 0.47004 0.42185 0.61185 0.10385  -0.08427 0.07967  174 GLY B O   
6258 N N   . VAL B 189 ? 0.48957 0.39530 0.62890 0.10583  -0.05729 0.07387  175 VAL B N   
6259 C CA  . VAL B 189 ? 0.46837 0.36436 0.57332 0.09052  -0.05227 0.06759  175 VAL B CA  
6260 C C   . VAL B 189 ? 0.50717 0.39315 0.61182 0.08563  -0.03366 0.05215  175 VAL B C   
6261 O O   . VAL B 189 ? 0.42274 0.29499 0.54122 0.09356  -0.02276 0.04736  175 VAL B O   
6262 C CB  . VAL B 189 ? 0.49811 0.36978 0.57573 0.08718  -0.05500 0.07862  175 VAL B CB  
6263 C CG1 . VAL B 189 ? 0.59035 0.47470 0.66246 0.09224  -0.07230 0.09620  175 VAL B CG1 
6264 C CG2 . VAL B 189 ? 0.63865 0.48057 0.72571 0.09377  -0.04520 0.07902  175 VAL B CG2 
6274 N N   . GLN B 190 ? 0.43730 0.33060 0.52555 0.07344  -0.03002 0.04439  176 GLN B N   
6275 C CA  . GLN B 190 ? 0.39854 0.28356 0.47804 0.06765  -0.01349 0.03235  176 GLN B CA  
6276 C C   . GLN B 190 ? 0.43468 0.29771 0.47981 0.05810  -0.01222 0.03140  176 GLN B C   
6277 O O   . GLN B 190 ? 0.44166 0.30945 0.46864 0.04888  -0.01922 0.03437  176 GLN B O   
6278 C CB  . GLN B 190 ? 0.43748 0.34518 0.52571 0.06096  -0.01017 0.02707  176 GLN B CB  
6279 C CG  . GLN B 190 ? 0.47488 0.37604 0.54833 0.05432  0.00607  0.01847  176 GLN B CG  
6280 C CD  . GLN B 190 ? 0.46762 0.36077 0.54938 0.06309  0.02197  0.01147  176 GLN B CD  
6281 O OE1 . GLN B 190 ? 0.47871 0.38823 0.58878 0.06962  0.03037  0.00970  176 GLN B OE1 
6282 N NE2 . GLN B 190 ? 0.43479 0.30360 0.49352 0.06325  0.02648  0.00619  176 GLN B NE2 
6291 N N   . LEU B 191 ? 0.49963 0.33951 0.53827 0.06047  -0.00351 0.02586  177 LEU B N   
6292 C CA  . LEU B 191 ? 0.49067 0.31013 0.50201 0.05118  -0.00322 0.02385  177 LEU B CA  
6293 C C   . LEU B 191 ? 0.42325 0.24697 0.41547 0.04194  0.00471  0.01383  177 LEU B C   
6294 O O   . LEU B 191 ? 0.45037 0.28099 0.44779 0.04508  0.01589  0.00538  177 LEU B O   
6295 C CB  . LEU B 191 ? 0.43921 0.23156 0.45416 0.05665  0.00165  0.01926  177 LEU B CB  
6296 C CG  . LEU B 191 ? 0.65098 0.42133 0.64498 0.04662  -0.00042 0.01809  177 LEU B CG  
6297 C CD1 . LEU B 191 ? 0.62447 0.39141 0.61806 0.04431  -0.01173 0.03619  177 LEU B CD1 
6298 C CD2 . LEU B 191 ? 0.66311 0.40731 0.66115 0.05044  0.00723  0.00489  177 LEU B CD2 
6310 N N   . ALA B 192 ? 0.47927 0.30009 0.44988 0.03119  -0.00055 0.01625  178 ALA B N   
6311 C CA  . ALA B 192 ? 0.50254 0.32718 0.45443 0.02265  0.00461  0.00947  178 ALA B CA  
6312 C C   . ALA B 192 ? 0.50376 0.31134 0.43574 0.01457  0.00125  0.00773  178 ALA B C   
6313 O O   . ALA B 192 ? 0.51519 0.32412 0.44103 0.00848  -0.00676 0.01582  178 ALA B O   
6314 C CB  . ALA B 192 ? 0.50997 0.35510 0.46323 0.01765  0.00044  0.01447  178 ALA B CB  
6320 N N   . ASP B 193 ? 0.57782 0.37110 0.50066 0.01454  0.00749  -0.00383 179 ASP B N   
6321 C CA  . ASP B 193 ? 0.58246 0.35888 0.49213 0.00668  0.00343  -0.00798 179 ASP B CA  
6322 C C   . ASP B 193 ? 0.53251 0.31849 0.42207 -0.00233 0.00241  -0.01093 179 ASP B C   
6323 O O   . ASP B 193 ? 0.51724 0.30965 0.39579 -0.00085 0.00903  -0.01888 179 ASP B O   
6324 C CB  . ASP B 193 ? 0.64025 0.39623 0.55158 0.01126  0.00869  -0.02217 179 ASP B CB  
6325 C CG  . ASP B 193 ? 0.71545 0.45913 0.65068 0.02117  0.00921  -0.01793 179 ASP B CG  
6326 O OD1 . ASP B 193 ? 0.73593 0.48589 0.68308 0.02297  0.00314  -0.00207 179 ASP B OD1 
6327 O OD2 . ASP B 193 ? 0.76393 0.49238 0.70592 0.02812  0.01541  -0.03062 179 ASP B OD2 
6332 N N   . HIS B 194 ? 0.50024 0.28827 0.38550 -0.01080 -0.00524 -0.00336 180 HIS B N   
6333 C CA  . HIS B 194 ? 0.50692 0.30626 0.37807 -0.01837 -0.00758 -0.00342 180 HIS B CA  
6334 C C   . HIS B 194 ? 0.51675 0.30510 0.37754 -0.02580 -0.01133 -0.01198 180 HIS B C   
6335 O O   . HIS B 194 ? 0.51364 0.28917 0.38205 -0.03024 -0.01556 -0.01044 180 HIS B O   
6336 C CB  . HIS B 194 ? 0.50907 0.32042 0.38419 -0.02227 -0.01309 0.00852  180 HIS B CB  
6337 C CG  . HIS B 194 ? 0.48489 0.31123 0.36867 -0.01702 -0.01176 0.01364  180 HIS B CG  
6338 N ND1 . HIS B 194 ? 0.48379 0.31047 0.38130 -0.00900 -0.01010 0.01533  180 HIS B ND1 
6339 C CD2 . HIS B 194 ? 0.48031 0.32189 0.36452 -0.01890 -0.01278 0.01658  180 HIS B CD2 
6340 C CE1 . HIS B 194 ? 0.51467 0.35748 0.42072 -0.00708 -0.01089 0.01834  180 HIS B CE1 
6341 N NE2 . HIS B 194 ? 0.42312 0.27378 0.32140 -0.01317 -0.01221 0.01867  180 HIS B NE2 
6349 N N   . TYR B 195 ? 0.45487 0.24928 0.29956 -0.02733 -0.01023 -0.02009 181 TYR B N   
6350 C CA  . TYR B 195 ? 0.49056 0.28070 0.32455 -0.03506 -0.01668 -0.02885 181 TYR B CA  
6351 C C   . TYR B 195 ? 0.49655 0.30483 0.32177 -0.03935 -0.02048 -0.02231 181 TYR B C   
6352 O O   . TYR B 195 ? 0.53636 0.35634 0.35301 -0.03476 -0.01569 -0.01937 181 TYR B O   
6353 C CB  . TYR B 195 ? 0.53947 0.32112 0.35933 -0.03140 -0.01364 -0.04640 181 TYR B CB  
6354 C CG  . TYR B 195 ? 0.61351 0.37423 0.44565 -0.02692 -0.01029 -0.05522 181 TYR B CG  
6355 C CD1 . TYR B 195 ? 0.60917 0.36862 0.44876 -0.01612 -0.00062 -0.05437 181 TYR B CD1 
6356 C CD2 . TYR B 195 ? 0.66806 0.41022 0.50874 -0.03344 -0.01679 -0.06397 181 TYR B CD2 
6357 C CE1 . TYR B 195 ? 0.70192 0.44193 0.55598 -0.01045 0.00245  -0.06181 181 TYR B CE1 
6358 C CE2 . TYR B 195 ? 0.69888 0.41908 0.55446 -0.02874 -0.01355 -0.07144 181 TYR B CE2 
6359 C CZ  . TYR B 195 ? 0.75893 0.47799 0.62059 -0.01651 -0.00396 -0.07019 181 TYR B CZ  
6360 O OH  . TYR B 195 ? 0.77417 0.47110 0.65365 -0.01034 -0.00077 -0.07708 181 TYR B OH  
6370 N N   . GLN B 196 ? 0.51814 0.32896 0.34868 -0.04782 -0.02823 -0.01886 182 GLN B N   
6371 C CA  . GLN B 196 ? 0.44639 0.27450 0.27578 -0.05082 -0.03168 -0.01053 182 GLN B CA  
6372 C C   . GLN B 196 ? 0.49214 0.32447 0.31742 -0.05846 -0.04086 -0.01632 182 GLN B C   
6373 O O   . GLN B 196 ? 0.52970 0.35137 0.36067 -0.06463 -0.04567 -0.02427 182 GLN B O   
6374 C CB  . GLN B 196 ? 0.44665 0.27989 0.29104 -0.05225 -0.03118 0.00140  182 GLN B CB  
6375 C CG  . GLN B 196 ? 0.46131 0.31096 0.30878 -0.05533 -0.03442 0.00804  182 GLN B CG  
6376 C CD  . GLN B 196 ? 0.48539 0.34094 0.34421 -0.05539 -0.03259 0.01702  182 GLN B CD  
6377 O OE1 . GLN B 196 ? 0.41443 0.26479 0.27620 -0.05147 -0.02932 0.01996  182 GLN B OE1 
6378 N NE2 . GLN B 196 ? 0.40059 0.26875 0.26541 -0.05899 -0.03488 0.02105  182 GLN B NE2 
6387 N N   . GLN B 197 ? 0.48404 0.33229 0.30254 -0.05801 -0.04392 -0.01190 183 GLN B N   
6388 C CA  . GLN B 197 ? 0.43873 0.29622 0.25538 -0.06419 -0.05442 -0.01569 183 GLN B CA  
6389 C C   . GLN B 197 ? 0.50837 0.38360 0.33143 -0.06311 -0.05598 -0.00357 183 GLN B C   
6390 O O   . GLN B 197 ? 0.47730 0.35738 0.29577 -0.05632 -0.05014 0.00395  183 GLN B O   
6391 C CB  . GLN B 197 ? 0.57058 0.42822 0.36414 -0.06189 -0.05859 -0.02768 183 GLN B CB  
6392 C CG  . GLN B 197 ? 0.64225 0.50500 0.43570 -0.06983 -0.07242 -0.03801 183 GLN B CG  
6393 C CD  . GLN B 197 ? 0.89614 0.75760 0.66300 -0.06698 -0.07704 -0.05396 183 GLN B CD  
6394 O OE1 . GLN B 197 ? 0.81589 0.67853 0.56123 -0.05796 -0.06908 -0.05305 183 GLN B OE1 
6395 N NE2 . GLN B 197 ? 0.97342 0.83353 0.74225 -0.07480 -0.08963 -0.06937 183 GLN B NE2 
6404 N N   . ASN B 198 ? 0.45126 0.33595 0.28869 -0.06980 -0.06320 -0.00178 184 ASN B N   
6405 C CA  . ASN B 198 ? 0.45203 0.35366 0.29997 -0.06817 -0.06463 0.00842  184 ASN B CA  
6406 C C   . ASN B 198 ? 0.48401 0.39992 0.33565 -0.07265 -0.07702 0.00588  184 ASN B C   
6407 O O   . ASN B 198 ? 0.46990 0.38452 0.32968 -0.08112 -0.08386 -0.00212 184 ASN B O   
6408 C CB  . ASN B 198 ? 0.46140 0.36531 0.32891 -0.07027 -0.05892 0.01503  184 ASN B CB  
6409 C CG  . ASN B 198 ? 0.43772 0.33070 0.30212 -0.06550 -0.04932 0.01742  184 ASN B CG  
6410 O OD1 . ASN B 198 ? 0.46384 0.34251 0.32217 -0.06585 -0.04699 0.01287  184 ASN B OD1 
6411 N ND2 . ASN B 198 ? 0.43831 0.33850 0.30910 -0.06069 -0.04455 0.02356  184 ASN B ND2 
6418 N N   . THR B 199 ? 0.50287 0.43269 0.35148 -0.06698 -0.08054 0.01330  185 THR B N   
6419 C CA  . THR B 199 ? 0.48962 0.43683 0.34277 -0.06922 -0.09395 0.01301  185 THR B CA  
6420 C C   . THR B 199 ? 0.52533 0.48763 0.39542 -0.06366 -0.09326 0.02605  185 THR B C   
6421 O O   . THR B 199 ? 0.45225 0.41033 0.31969 -0.05611 -0.08452 0.03439  185 THR B O   
6422 C CB  . THR B 199 ? 0.49869 0.44835 0.32374 -0.06561 -0.10217 0.00814  185 THR B CB  
6423 O OG1 . THR B 199 ? 0.66267 0.61300 0.47377 -0.05547 -0.09518 0.02001  185 THR B OG1 
6424 C CG2 . THR B 199 ? 0.59161 0.52448 0.39915 -0.06910 -0.10089 -0.00738 185 THR B CG2 
6432 N N   . PRO B 200 ? 0.48017 0.46013 0.37122 -0.06710 -0.10218 0.02744  186 PRO B N   
6433 C CA  . PRO B 200 ? 0.44433 0.43841 0.35551 -0.06056 -0.10074 0.03878  186 PRO B CA  
6434 C C   . PRO B 200 ? 0.43325 0.43333 0.33215 -0.05087 -0.10609 0.04867  186 PRO B C   
6435 O O   . PRO B 200 ? 0.42575 0.42988 0.30390 -0.05038 -0.11645 0.04694  186 PRO B O   
6436 C CB  . PRO B 200 ? 0.47107 0.48447 0.40961 -0.06729 -0.10940 0.03661  186 PRO B CB  
6437 C CG  . PRO B 200 ? 0.50306 0.51569 0.43093 -0.07605 -0.12146 0.02524  186 PRO B CG  
6438 C CD  . PRO B 200 ? 0.49552 0.48361 0.39788 -0.07740 -0.11357 0.01797  186 PRO B CD  
6446 N N   . ILE B 201 ? 0.39147 0.41543 0.44039 -0.04171 -0.01529 0.03355  187 ILE B N   
6447 C CA  . ILE B 201 ? 0.36922 0.38932 0.42084 -0.04644 -0.02943 0.04060  187 ILE B CA  
6448 C C   . ILE B 201 ? 0.32902 0.35812 0.41409 -0.05259 -0.04778 0.05336  187 ILE B C   
6449 O O   . ILE B 201 ? 0.37159 0.39095 0.44906 -0.06545 -0.06669 0.06390  187 ILE B O   
6450 C CB  . ILE B 201 ? 0.32490 0.34978 0.38727 -0.03333 -0.02233 0.03524  187 ILE B CB  
6451 C CG1 . ILE B 201 ? 0.36072 0.37521 0.38948 -0.03037 -0.00880 0.02498  187 ILE B CG1 
6452 C CG2 . ILE B 201 ? 0.31379 0.33587 0.38849 -0.03811 -0.04034 0.04510  187 ILE B CG2 
6453 C CD1 . ILE B 201 ? 0.35204 0.37154 0.39005 -0.01732 -0.00010 0.01889  187 ILE B CD1 
6465 N N   . GLY B 202 ? 0.33214 0.38014 0.45511 -0.04522 -0.04322 0.05293  188 GLY B N   
6466 C CA  . GLY B 202 ? 0.36884 0.42995 0.53539 -0.04834 -0.05953 0.06359  188 GLY B CA  
6467 C C   . GLY B 202 ? 0.34656 0.40663 0.50899 -0.06280 -0.06941 0.07193  188 GLY B C   
6468 O O   . GLY B 202 ? 0.36665 0.41175 0.48800 -0.07192 -0.06561 0.06967  188 GLY B O   
6472 N N   . ASP B 203 ? 0.34613 0.42242 0.55566 -0.06475 -0.08308 0.08126  189 ASP B N   
6473 C CA  . ASP B 203 ? 0.33464 0.41251 0.54811 -0.07939 -0.09571 0.09131  189 ASP B CA  
6474 C C   . ASP B 203 ? 0.35380 0.45525 0.59746 -0.07468 -0.08054 0.08611  189 ASP B C   
6475 O O   . ASP B 203 ? 0.36571 0.46715 0.60514 -0.08743 -0.08727 0.09281  189 ASP B O   
6476 C CB  . ASP B 203 ? 0.32013 0.40021 0.56789 -0.08837 -0.12554 0.10818  189 ASP B CB  
6477 C CG  . ASP B 203 ? 0.39702 0.45161 0.60876 -0.09936 -0.14385 0.11645  189 ASP B CG  
6478 O OD1 . ASP B 203 ? 0.39698 0.43060 0.54997 -0.10724 -0.13604 0.11083  189 ASP B OD1 
6479 O OD2 . ASP B 203 ? 0.38272 0.43827 0.62621 -0.10092 -0.16614 0.12828  189 ASP B OD2 
6484 N N   . GLY B 204 ? 0.38507 0.50600 0.65666 -0.05899 -0.06032 0.07430  190 GLY B N   
6485 C CA  . GLY B 204 ? 0.44469 0.58964 0.74264 -0.05728 -0.04376 0.06851  190 GLY B CA  
6486 C C   . GLY B 204 ? 0.42936 0.56176 0.68111 -0.06634 -0.03383 0.06648  190 GLY B C   
6487 O O   . GLY B 204 ? 0.45270 0.55997 0.65483 -0.06746 -0.03201 0.06347  190 GLY B O   
6491 N N   . PRO B 205 ? 0.45956 0.60933 0.72929 -0.07334 -0.02756 0.06783  191 PRO B N   
6492 C CA  . PRO B 205 ? 0.40951 0.54502 0.63700 -0.08302 -0.02072 0.06730  191 PRO B CA  
6493 C C   . PRO B 205 ? 0.39604 0.52623 0.59671 -0.07441 0.00058  0.05517  191 PRO B C   
6494 O O   . PRO B 205 ? 0.37504 0.52235 0.59739 -0.06376 0.01551  0.04616  191 PRO B O   
6495 C CB  . PRO B 205 ? 0.46298 0.62315 0.72427 -0.09338 -0.01937 0.07264  191 PRO B CB  
6496 C CG  . PRO B 205 ? 0.42251 0.60825 0.74537 -0.08969 -0.02940 0.07718  191 PRO B CG  
6497 C CD  . PRO B 205 ? 0.39116 0.57504 0.72319 -0.07335 -0.02618 0.06948  191 PRO B CD  
6505 N N   . VAL B 206 ? 0.43209 0.53701 0.58606 -0.07981 0.00080  0.05475  192 VAL B N   
6506 C CA  . VAL B 206 ? 0.44270 0.53790 0.56869 -0.07367 0.01597  0.04596  192 VAL B CA  
6507 C C   . VAL B 206 ? 0.44925 0.53906 0.55710 -0.08569 0.01930  0.04915  192 VAL B C   
6508 O O   . VAL B 206 ? 0.38981 0.48171 0.50391 -0.09822 0.01021  0.05736  192 VAL B O   
6509 C CB  . VAL B 206 ? 0.43371 0.50145 0.52406 -0.06699 0.01213  0.04154  192 VAL B CB  
6510 C CG1 . VAL B 206 ? 0.45259 0.52559 0.55868 -0.05690 0.00917  0.03931  192 VAL B CG1 
6511 C CG2 . VAL B 206 ? 0.46917 0.51230 0.53130 -0.07748 -0.00174 0.04600  192 VAL B CG2 
6521 N N   . LEU B 207 ? 0.48703 0.56849 0.57186 -0.08307 0.03050  0.04378  193 LEU B N   
6522 C CA  . LEU B 207 ? 0.48324 0.55471 0.54649 -0.09516 0.03161  0.04793  193 LEU B CA  
6523 C C   . LEU B 207 ? 0.45870 0.49437 0.48564 -0.09405 0.02141  0.04754  193 LEU B C   
6524 O O   . LEU B 207 ? 0.48219 0.50520 0.49449 -0.08299 0.02449  0.04079  193 LEU B O   
6525 C CB  . LEU B 207 ? 0.48528 0.56888 0.54560 -0.09621 0.04823  0.04364  193 LEU B CB  
6526 C CG  . LEU B 207 ? 0.46739 0.58806 0.56364 -0.09944 0.06331  0.04028  193 LEU B CG  
6527 C CD1 . LEU B 207 ? 0.39940 0.52679 0.48250 -0.10128 0.08093  0.03326  193 LEU B CD1 
6528 C CD2 . LEU B 207 ? 0.47025 0.60620 0.58336 -0.11595 0.06058  0.04872  193 LEU B CD2 
6540 N N   . LEU B 208 ? 0.47978 0.49959 0.49504 -0.10548 0.00947  0.05373  194 LEU B N   
6541 C CA  . LEU B 208 ? 0.51694 0.50218 0.50178 -0.10515 0.00082  0.05112  194 LEU B CA  
6542 C C   . LEU B 208 ? 0.47210 0.44558 0.44200 -0.11337 0.00067  0.05568  194 LEU B C   
6543 O O   . LEU B 208 ? 0.45829 0.43578 0.43044 -0.12847 -0.00345 0.06448  194 LEU B O   
6544 C CB  . LEU B 208 ? 0.45205 0.42216 0.42970 -0.11388 -0.01299 0.05364  194 LEU B CB  
6545 C CG  . LEU B 208 ? 0.59229 0.57293 0.58237 -0.11116 -0.01693 0.05288  194 LEU B CG  
6546 C CD1 . LEU B 208 ? 0.66953 0.62860 0.64187 -0.12246 -0.03131 0.05427  194 LEU B CD1 
6547 C CD2 . LEU B 208 ? 0.47571 0.45588 0.46258 -0.09586 -0.00958 0.04359  194 LEU B CD2 
6559 N N   . PRO B 209 ? 0.46321 0.42198 0.41840 -0.10578 0.00321  0.05153  195 PRO B N   
6560 C CA  . PRO B 209 ? 0.43197 0.38167 0.37375 -0.11573 0.00160  0.05851  195 PRO B CA  
6561 C C   . PRO B 209 ? 0.47005 0.38578 0.39471 -0.12304 -0.01424 0.06249  195 PRO B C   
6562 O O   . PRO B 209 ? 0.49090 0.38538 0.41095 -0.11607 -0.02159 0.05539  195 PRO B O   
6563 C CB  . PRO B 209 ? 0.40560 0.35241 0.34112 -0.10377 0.00790  0.05288  195 PRO B CB  
6564 C CG  . PRO B 209 ? 0.49676 0.43295 0.43452 -0.08784 0.00608  0.04248  195 PRO B CG  
6565 C CD  . PRO B 209 ? 0.40245 0.35245 0.35327 -0.08921 0.00634  0.04138  195 PRO B CD  
6573 N N   . ASP B 210 ? 0.44943 0.35968 0.36414 -0.13870 -0.01908 0.07336  196 ASP B N   
6574 C CA  . ASP B 210 ? 0.49979 0.37341 0.39830 -0.14455 -0.03595 0.07798  196 ASP B CA  
6575 C C   . ASP B 210 ? 0.48103 0.33436 0.37366 -0.13101 -0.03961 0.07265  196 ASP B C   
6576 O O   . ASP B 210 ? 0.46207 0.33097 0.35865 -0.12093 -0.02886 0.06792  196 ASP B O   
6577 C CB  . ASP B 210 ? 0.52129 0.39402 0.40896 -0.16749 -0.04177 0.09334  196 ASP B CB  
6578 C CG  . ASP B 210 ? 0.51869 0.40848 0.41502 -0.18238 -0.04118 0.09941  196 ASP B CG  
6579 O OD1 . ASP B 210 ? 0.56986 0.45851 0.47532 -0.17662 -0.04396 0.09355  196 ASP B OD1 
6580 O OD2 . ASP B 210 ? 0.59421 0.49871 0.48747 -0.20178 -0.03832 0.11045  196 ASP B OD2 
6585 N N   . ASN B 211 ? 0.50616 0.32384 0.39213 -0.13092 -0.05606 0.07333  197 ASN B N   
6586 C CA  . ASN B 211 ? 0.51126 0.30830 0.39865 -0.11797 -0.06266 0.06873  197 ASN B CA  
6587 C C   . ASN B 211 ? 0.51162 0.31918 0.39074 -0.12363 -0.06029 0.07841  197 ASN B C   
6588 O O   . ASN B 211 ? 0.52966 0.34013 0.39474 -0.14342 -0.06364 0.09244  197 ASN B O   
6589 C CB  . ASN B 211 ? 0.54501 0.30137 0.43077 -0.12058 -0.08355 0.07076  197 ASN B CB  
6590 C CG  . ASN B 211 ? 0.55023 0.29194 0.44123 -0.11515 -0.08508 0.05768  197 ASN B CG  
6591 O OD1 . ASN B 211 ? 0.52853 0.28647 0.42441 -0.10573 -0.07168 0.04511  197 ASN B OD1 
6592 N ND2 . ASN B 211 ? 0.58318 0.29186 0.47108 -0.12277 -0.10247 0.06070  197 ASN B ND2 
6599 N N   . HIS B 212 ? 0.49448 0.30774 0.38020 -0.10824 -0.05417 0.07067  198 HIS B N   
6600 C CA  . HIS B 212 ? 0.49837 0.31710 0.37385 -0.11308 -0.05360 0.07836  198 HIS B CA  
6601 C C   . HIS B 212 ? 0.52048 0.33536 0.40858 -0.09277 -0.05290 0.06806  198 HIS B C   
6602 O O   . HIS B 212 ? 0.50534 0.31361 0.40965 -0.07681 -0.05213 0.05516  198 HIS B O   
6603 C CB  . HIS B 212 ? 0.53987 0.39359 0.40815 -0.12321 -0.03465 0.08041  198 HIS B CB  
6604 C CG  . HIS B 212 ? 0.45223 0.33274 0.33636 -0.10713 -0.01653 0.06669  198 HIS B CG  
6605 N ND1 . HIS B 212 ? 0.46926 0.36274 0.36704 -0.10250 -0.00990 0.06010  198 HIS B ND1 
6606 C CD2 . HIS B 212 ? 0.43721 0.33210 0.32492 -0.09626 -0.00586 0.05965  198 HIS B CD2 
6607 C CE1 . HIS B 212 ? 0.46540 0.37945 0.37510 -0.08952 0.00313  0.05037  198 HIS B CE1 
6608 N NE2 . HIS B 212 ? 0.47937 0.39478 0.38364 -0.08502 0.00645  0.04935  198 HIS B NE2 
6616 N N   . TYR B 213 ? 0.48535 0.30474 0.36479 -0.09522 -0.05269 0.07338  199 TYR B N   
6617 C CA  . TYR B 213 ? 0.53080 0.34857 0.42316 -0.07761 -0.05275 0.06514  199 TYR B CA  
6618 C C   . TYR B 213 ? 0.52462 0.36171 0.40404 -0.08192 -0.04238 0.06761  199 TYR B C   
6619 O O   . TYR B 213 ? 0.54262 0.39000 0.40161 -0.10001 -0.03697 0.07596  199 TYR B O   
6620 C CB  . TYR B 213 ? 0.51343 0.29812 0.41542 -0.07382 -0.07619 0.07001  199 TYR B CB  
6621 C CG  . TYR B 213 ? 0.53049 0.29760 0.41223 -0.09331 -0.09453 0.08954  199 TYR B CG  
6622 C CD1 . TYR B 213 ? 0.54185 0.31369 0.41159 -0.09779 -0.09601 0.09583  199 TYR B CD1 
6623 C CD2 . TYR B 213 ? 0.56314 0.30672 0.43514 -0.10942 -0.11199 0.10251  199 TYR B CD2 
6624 C CE1 . TYR B 213 ? 0.57129 0.32509 0.41715 -0.11930 -0.11429 0.11486  199 TYR B CE1 
6625 C CE2 . TYR B 213 ? 0.61615 0.34167 0.46583 -0.13071 -0.13083 0.12238  199 TYR B CE2 
6626 C CZ  . TYR B 213 ? 0.62743 0.35812 0.46284 -0.13627 -0.13194 0.12866  199 TYR B CZ  
6627 O OH  . TYR B 213 ? 0.71770 0.42867 0.52568 -0.16099 -0.15202 0.14953  199 TYR B OH  
6637 N N   . LEU B 214 ? 0.47669 0.31893 0.36821 -0.06603 -0.03861 0.05896  200 LEU B N   
6638 C CA  . LEU B 214 ? 0.51161 0.36710 0.39179 -0.06831 -0.03131 0.05990  200 LEU B CA  
6639 C C   . LEU B 214 ? 0.48312 0.31743 0.36532 -0.06604 -0.05024 0.06653  200 LEU B C   
6640 O O   . LEU B 214 ? 0.52074 0.34442 0.42783 -0.04996 -0.05838 0.06028  200 LEU B O   
6641 C CB  . LEU B 214 ? 0.45371 0.33373 0.34707 -0.05287 -0.01243 0.04547  200 LEU B CB  
6642 C CG  . LEU B 214 ? 0.47782 0.37906 0.37741 -0.05174 0.00358  0.03840  200 LEU B CG  
6643 C CD1 . LEU B 214 ? 0.45016 0.36882 0.36432 -0.03606 0.01603  0.02618  200 LEU B CD1 
6644 C CD2 . LEU B 214 ? 0.42185 0.33855 0.30617 -0.06896 0.01341  0.04377  200 LEU B CD2 
6656 N N   . SER B 215 ? 0.50779 0.33653 0.36478 -0.08329 -0.05721 0.07871  201 SER B N   
6657 C CA  . SER B 215 ? 0.52722 0.33723 0.38406 -0.08387 -0.07697 0.08727  201 SER B CA  
6658 C C   . SER B 215 ? 0.52382 0.35176 0.37832 -0.07687 -0.06421 0.07932  201 SER B C   
6659 O O   . SER B 215 ? 0.53454 0.38105 0.36792 -0.08601 -0.04621 0.07578  201 SER B O   
6660 C CB  . SER B 215 ? 0.58266 0.37220 0.40775 -0.11080 -0.09545 0.10732  201 SER B CB  
6661 O OG  . SER B 215 ? 0.72421 0.52981 0.51472 -0.12918 -0.08011 0.10877  201 SER B OG  
6667 N N   . THR B 216 ? 0.57304 0.39595 0.45186 -0.06072 -0.07301 0.07543  202 THR B N   
6668 C CA  . THR B 216 ? 0.56719 0.40660 0.44848 -0.05187 -0.06172 0.06693  202 THR B CA  
6669 C C   . THR B 216 ? 0.66236 0.48575 0.54882 -0.05262 -0.08344 0.07621  202 THR B C   
6670 O O   . THR B 216 ? 0.61552 0.42318 0.53066 -0.04348 -0.10200 0.07933  202 THR B O   
6671 C CB  . THR B 216 ? 0.54151 0.39830 0.45248 -0.02956 -0.04614 0.04979  202 THR B CB  
6672 O OG1 . THR B 216 ? 0.55457 0.42252 0.46330 -0.02989 -0.03122 0.04359  202 THR B OG1 
6673 C CG2 . THR B 216 ? 0.58020 0.45475 0.49000 -0.02310 -0.03340 0.04186  202 THR B CG2 
6681 N N   . CYS B 217 ? 0.59285 0.41999 0.45366 -0.06376 -0.08148 0.07985  203 CYS B N   
6682 C CA  . CYS B 217 ? 0.66696 0.48293 0.53237 -0.06427 -0.10035 0.08754  203 CYS B CA  
6683 C C   . CYS B 217 ? 0.63787 0.47430 0.50456 -0.05478 -0.08280 0.07501  203 CYS B C   
6684 O O   . CYS B 217 ? 0.57736 0.42662 0.41673 -0.06314 -0.06382 0.06893  203 CYS B O   
6685 C CB  . CYS B 217 ? 0.64727 0.44236 0.47316 -0.09207 -0.11950 0.10656  203 CYS B CB  
6686 S SG  . CYS B 217 ? 0.81656 0.57948 0.64460 -0.10493 -0.15126 0.12680  203 CYS B SG  
6691 N N   . SER B 218 ? 0.74315 0.58299 0.64393 -0.03765 -0.08877 0.07034  204 SER B N   
6692 C CA  . SER B 218 ? 0.72930 0.58704 0.63457 -0.02842 -0.07464 0.05946  204 SER B CA  
6693 C C   . SER B 218 ? 0.72045 0.56803 0.62471 -0.03409 -0.09425 0.06914  204 SER B C   
6694 O O   . SER B 218 ? 0.71959 0.54960 0.63905 -0.03675 -0.11991 0.08176  204 SER B O   
6695 C CB  . SER B 218 ? 0.72950 0.60354 0.67380 -0.00589 -0.06241 0.04489  204 SER B CB  
6696 O OG  . SER B 218 ? 0.83547 0.70303 0.81723 0.00459  -0.07911 0.04686  204 SER B OG  
6702 N N   . LYS B 219 ? 0.61726 0.47482 0.50519 -0.03630 -0.08368 0.06350  205 LYS B N   
6703 C CA  . LYS B 219 ? 0.60752 0.45638 0.49011 -0.04348 -0.10097 0.07198  205 LYS B CA  
6704 C C   . LYS B 219 ? 0.50812 0.37561 0.41085 -0.02857 -0.08829 0.05954  205 LYS B C   
6705 O O   . LYS B 219 ? 0.52356 0.40404 0.41094 -0.02687 -0.06627 0.04772  205 LYS B O   
6706 C CB  . LYS B 219 ? 0.65869 0.49493 0.48699 -0.06942 -0.10316 0.07951  205 LYS B CB  
6707 C CG  . LYS B 219 ? 0.68971 0.51363 0.50491 -0.08098 -0.12300 0.08950  205 LYS B CG  
6708 C CD  . LYS B 219 ? 0.78738 0.60616 0.54626 -0.10368 -0.11252 0.08713  205 LYS B CD  
6709 C CE  . LYS B 219 ? 0.87316 0.67821 0.61474 -0.11694 -0.13232 0.09639  205 LYS B CE  
6710 N NZ  . LYS B 219 ? 0.86064 0.67963 0.64056 -0.09655 -0.13129 0.08896  205 LYS B NZ  
6724 N N   . LEU B 220 ? 0.57918 0.44816 0.51885 -0.01836 -0.10285 0.06235  206 LEU B N   
6725 C CA  . LEU B 220 ? 0.50664 0.39317 0.46757 -0.00629 -0.09343 0.05250  206 LEU B CA  
6726 C C   . LEU B 220 ? 0.48425 0.36235 0.43399 -0.01719 -0.11078 0.06201  206 LEU B C   
6727 O O   . LEU B 220 ? 0.51187 0.37330 0.46443 -0.02656 -0.13708 0.07722  206 LEU B O   
6728 C CB  . LEU B 220 ? 0.50726 0.40655 0.52202 0.01281  -0.09332 0.04581  206 LEU B CB  
6729 C CG  . LEU B 220 ? 0.48670 0.39964 0.51270 0.02496  -0.07076 0.03155  206 LEU B CG  
6730 C CD1 . LEU B 220 ? 0.50030 0.40088 0.50725 0.01883  -0.07049 0.03512  206 LEU B CD1 
6731 C CD2 . LEU B 220 ? 0.46660 0.39186 0.54315 0.04082  -0.06962 0.02292  206 LEU B CD2 
6743 N N   . SER B 221 ? 0.45658 0.34450 0.39408 -0.01679 -0.09807 0.05382  207 SER B N   
6744 C CA  . SER B 221 ? 0.51956 0.39974 0.44390 -0.02763 -0.11273 0.06104  207 SER B CA  
6745 C C   . SER B 221 ? 0.47204 0.36989 0.40989 -0.01734 -0.09815 0.04930  207 SER B C   
6746 O O   . SER B 221 ? 0.45130 0.36652 0.41075 -0.00272 -0.07978 0.03766  207 SER B O   
6747 C CB  . SER B 221 ? 0.48061 0.34177 0.34698 -0.05077 -0.11505 0.06618  207 SER B CB  
6748 O OG  . SER B 221 ? 0.51061 0.37882 0.35164 -0.05066 -0.08803 0.05218  207 SER B OG  
6754 N N   . LYS B 222 ? 0.49363 0.38530 0.41635 -0.02709 -0.10790 0.05331  208 LYS B N   
6755 C CA  . LYS B 222 ? 0.46474 0.36987 0.39849 -0.02023 -0.09826 0.04465  208 LYS B CA  
6756 C C   . LYS B 222 ? 0.45530 0.34819 0.34284 -0.03401 -0.09316 0.04055  208 LYS B C   
6757 O O   . LYS B 222 ? 0.51210 0.38561 0.36128 -0.05186 -0.10287 0.04706  208 LYS B O   
6758 C CB  . LYS B 222 ? 0.45163 0.36417 0.42500 -0.01660 -0.11684 0.05252  208 LYS B CB  
6759 C CG  . LYS B 222 ? 0.42036 0.34868 0.44795 -0.00100 -0.11836 0.05179  208 LYS B CG  
6760 C CD  . LYS B 222 ? 0.35704 0.30622 0.40145 0.01348  -0.09201 0.03618  208 LYS B CD  
6761 C CE  . LYS B 222 ? 0.38137 0.34813 0.48065 0.02721  -0.09154 0.03226  208 LYS B CE  
6762 N NZ  . LYS B 222 ? 0.41799 0.40079 0.52523 0.03758  -0.06651 0.01771  208 LYS B NZ  
6776 N N   . ASP B 223 ? 0.44444 0.34772 0.33537 -0.02677 -0.07789 0.02911  209 ASP B N   
6777 C CA  . ASP B 223 ? 0.50484 0.39705 0.36046 -0.03697 -0.07273 0.02237  209 ASP B CA  
6778 C C   . ASP B 223 ? 0.50150 0.39286 0.36764 -0.04062 -0.08827 0.02823  209 ASP B C   
6779 O O   . ASP B 223 ? 0.45667 0.36528 0.35841 -0.02884 -0.08579 0.02660  209 ASP B O   
6780 C CB  . ASP B 223 ? 0.51452 0.41611 0.37033 -0.02677 -0.04872 0.00675  209 ASP B CB  
6781 C CG  . ASP B 223 ? 0.54559 0.43451 0.36948 -0.03551 -0.04198 -0.00328 209 ASP B CG  
6782 O OD1 . ASP B 223 ? 0.65547 0.52823 0.45314 -0.05063 -0.05491 0.00128  209 ASP B OD1 
6783 O OD2 . ASP B 223 ? 0.54758 0.44155 0.37359 -0.02771 -0.02463 -0.01605 209 ASP B OD2 
6788 N N   . PRO B 224 ? 0.49920 0.37135 0.33459 -0.05848 -0.10453 0.03530  210 PRO B N   
6789 C CA  . PRO B 224 ? 0.56981 0.44160 0.41816 -0.06286 -0.12201 0.04264  210 PRO B CA  
6790 C C   . PRO B 224 ? 0.57960 0.45610 0.42789 -0.05818 -0.10976 0.03120  210 PRO B C   
6791 O O   . PRO B 224 ? 0.59885 0.48152 0.46819 -0.05840 -0.12128 0.03665  210 PRO B O   
6792 C CB  . PRO B 224 ? 0.59862 0.44430 0.40361 -0.08660 -0.14180 0.05240  210 PRO B CB  
6793 C CG  . PRO B 224 ? 0.61969 0.45233 0.37856 -0.09537 -0.12469 0.04211  210 PRO B CG  
6794 C CD  . PRO B 224 ? 0.54159 0.39139 0.32660 -0.07810 -0.10785 0.03706  210 PRO B CD  
6802 N N   . ASN B 225 ? 0.53423 0.40793 0.36245 -0.05445 -0.08820 0.01609  211 ASN B N   
6803 C CA  . ASN B 225 ? 0.61385 0.48922 0.44442 -0.04954 -0.07844 0.00562  211 ASN B CA  
6804 C C   . ASN B 225 ? 0.53972 0.43774 0.40901 -0.03212 -0.06644 0.00226  211 ASN B C   
6805 O O   . ASN B 225 ? 0.56365 0.46413 0.44040 -0.02892 -0.06268 -0.00260 211 ASN B O   
6806 C CB  . ASN B 225 ? 0.62777 0.48672 0.42063 -0.05492 -0.06285 -0.01018 211 ASN B CB  
6807 C CG  . ASN B 225 ? 0.77079 0.60555 0.51759 -0.07606 -0.07222 -0.00965 211 ASN B CG  
6808 O OD1 . ASN B 225 ? 0.72941 0.55446 0.46870 -0.08730 -0.09143 -0.00046 211 ASN B OD1 
6809 N ND2 . ASN B 225 ? 0.87241 0.69772 0.58704 -0.08355 -0.05868 -0.01945 211 ASN B ND2 
6816 N N   . GLU B 226 ? 0.46605 0.37863 0.35765 -0.02270 -0.06138 0.00499  212 GLU B N   
6817 C CA  . GLU B 226 ? 0.45178 0.38445 0.37442 -0.00911 -0.04933 0.00123  212 GLU B CA  
6818 C C   . GLU B 226 ? 0.40464 0.35462 0.36344 -0.00663 -0.05866 0.00903  212 GLU B C   
6819 O O   . GLU B 226 ? 0.51679 0.47181 0.49397 -0.00676 -0.06960 0.01699  212 GLU B O   
6820 C CB  . GLU B 226 ? 0.40108 0.34005 0.32864 -0.00152 -0.03858 -0.00125 212 GLU B CB  
6821 C CG  . GLU B 226 ? 0.43505 0.39324 0.39097 0.00993  -0.02722 -0.00472 212 GLU B CG  
6822 C CD  . GLU B 226 ? 0.36667 0.32583 0.32007 0.01177  -0.01889 -0.01127 212 GLU B CD  
6823 O OE1 . GLU B 226 ? 0.33117 0.27918 0.26507 0.01148  -0.01178 -0.01848 212 GLU B OE1 
6824 O OE2 . GLU B 226 ? 0.38387 0.35497 0.35645 0.01265  -0.01992 -0.00927 212 GLU B OE2 
6831 N N   . LYS B 227 ? 0.41929 0.37871 0.39058 -0.00505 -0.05460 0.00659  213 LYS B N   
6832 C CA  . LYS B 227 ? 0.40962 0.38834 0.41521 -0.00503 -0.06060 0.01221  213 LYS B CA  
6833 C C   . LYS B 227 ? 0.39399 0.39571 0.42924 0.00406  -0.04715 0.00824  213 LYS B C   
6834 O O   . LYS B 227 ? 0.40384 0.42519 0.47293 0.00482  -0.04922 0.01063  213 LYS B O   
6835 C CB  . LYS B 227 ? 0.49548 0.47157 0.49583 -0.01224 -0.06460 0.01282  213 LYS B CB  
6836 C CG  . LYS B 227 ? 0.50891 0.46193 0.48095 -0.02313 -0.07898 0.01589  213 LYS B CG  
6837 C CD  . LYS B 227 ? 0.54844 0.49459 0.51212 -0.02957 -0.08175 0.01459  213 LYS B CD  
6838 C CE  . LYS B 227 ? 0.52616 0.45018 0.46428 -0.04220 -0.09784 0.01781  213 LYS B CE  
6839 N NZ  . LYS B 227 ? 0.66243 0.56204 0.56157 -0.04490 -0.09410 0.00985  213 LYS B NZ  
6853 N N   . ARG B 228 ? 0.39048 0.39084 0.41488 0.00992  -0.03317 0.00143  214 ARG B N   
6854 C CA  . ARG B 228 ? 0.33011 0.34912 0.37608 0.01625  -0.02031 -0.00311 214 ARG B CA  
6855 C C   . ARG B 228 ? 0.35320 0.37438 0.41195 0.02296  -0.02010 -0.00351 214 ARG B C   
6856 O O   . ARG B 228 ? 0.40538 0.41069 0.44681 0.02252  -0.02681 -0.00059 214 ARG B O   
6857 C CB  . ARG B 228 ? 0.32530 0.34043 0.35407 0.01774  -0.00842 -0.00855 214 ARG B CB  
6858 C CG  . ARG B 228 ? 0.38783 0.39771 0.40589 0.01120  -0.01074 -0.00752 214 ARG B CG  
6859 C CD  . ARG B 228 ? 0.37041 0.37539 0.37692 0.01279  -0.00263 -0.01120 214 ARG B CD  
6860 N NE  . ARG B 228 ? 0.33782 0.33514 0.33703 0.00626  -0.00794 -0.00900 214 ARG B NE  
6861 C CZ  . ARG B 228 ? 0.33347 0.34174 0.34072 -0.00157 -0.00804 -0.00522 214 ARG B CZ  
6862 N NH1 . ARG B 228 ? 0.37449 0.40402 0.39759 -0.00390 -0.00014 -0.00552 214 ARG B NH1 
6863 N NH2 . ARG B 228 ? 0.34667 0.34376 0.34567 -0.00842 -0.01592 -0.00179 214 ARG B NH2 
6877 N N   . ASP B 229 ? 0.39626 0.43648 0.48490 0.02776  -0.01224 -0.00775 215 ASP B N   
6878 C CA  . ASP B 229 ? 0.39262 0.43345 0.49538 0.03513  -0.01087 -0.01001 215 ASP B CA  
6879 C C   . ASP B 229 ? 0.42375 0.44895 0.49587 0.03675  -0.00555 -0.01149 215 ASP B C   
6880 O O   . ASP B 229 ? 0.37312 0.39881 0.42995 0.03627  0.00547  -0.01595 215 ASP B O   
6881 C CB  . ASP B 229 ? 0.34505 0.40783 0.47928 0.03948  0.00251  -0.01912 215 ASP B CB  
6882 C CG  . ASP B 229 ? 0.42541 0.49108 0.59055 0.04757  -0.00107 -0.02152 215 ASP B CG  
6883 O OD1 . ASP B 229 ? 0.32109 0.37126 0.48330 0.04863  -0.01686 -0.01326 215 ASP B OD1 
6884 O OD2 . ASP B 229 ? 0.40789 0.49020 0.59980 0.05169  0.01158  -0.03205 215 ASP B OD2 
6889 N N   . HIS B 230 ? 0.33864 0.34997 0.40262 0.03717  -0.01479 -0.00673 216 HIS B N   
6890 C CA  . HIS B 230 ? 0.37920 0.37581 0.41165 0.03568  -0.01069 -0.00725 216 HIS B CA  
6891 C C   . HIS B 230 ? 0.33954 0.32624 0.37246 0.03612  -0.01882 -0.00254 216 HIS B C   
6892 O O   . HIS B 230 ? 0.31742 0.30540 0.37494 0.03774  -0.03087 0.00230  216 HIS B O   
6893 C CB  . HIS B 230 ? 0.36940 0.35233 0.37159 0.02792  -0.01476 -0.00518 216 HIS B CB  
6894 C CG  . HIS B 230 ? 0.32878 0.30026 0.32437 0.02021  -0.03213 0.00342  216 HIS B CG  
6895 N ND1 . HIS B 230 ? 0.37365 0.35177 0.39106 0.01853  -0.04389 0.00866  216 HIS B ND1 
6896 C CD2 . HIS B 230 ? 0.41571 0.36949 0.38447 0.01155  -0.04075 0.00851  216 HIS B CD2 
6897 C CE1 . HIS B 230 ? 0.39492 0.35847 0.39963 0.00960  -0.06113 0.01763  216 HIS B CE1 
6898 N NE2 . HIS B 230 ? 0.37428 0.32206 0.34681 0.00427  -0.05942 0.01774  216 HIS B NE2 
6906 N N   . MET B 231 ? 0.37026 0.34680 0.37759 0.03388  -0.01327 -0.00348 217 MET B N   
6907 C CA  . MET B 231 ? 0.39251 0.35702 0.39287 0.03096  -0.02124 0.00233  217 MET B CA  
6908 C C   . MET B 231 ? 0.39410 0.34663 0.35640 0.02215  -0.01647 0.00231  217 MET B C   
6909 O O   . MET B 231 ? 0.35401 0.31157 0.30782 0.02470  -0.00162 -0.00522 217 MET B O   
6910 C CB  . MET B 231 ? 0.37514 0.34583 0.39569 0.03915  -0.01477 -0.00191 217 MET B CB  
6911 C CG  . MET B 231 ? 0.37727 0.33354 0.38823 0.03514  -0.02297 0.00452  217 MET B CG  
6912 S SD  . MET B 231 ? 0.36121 0.32147 0.39729 0.04457  -0.01721 -0.00138 217 MET B SD  
6913 C CE  . MET B 231 ? 0.33041 0.29953 0.34751 0.04544  0.00411  -0.01049 217 MET B CE  
6923 N N   . VAL B 232 ? 0.42105 0.35831 0.36164 0.01058  -0.02912 0.01042  218 VAL B N   
6924 C CA  . VAL B 232 ? 0.46024 0.38651 0.36401 -0.00076 -0.02354 0.00970  218 VAL B CA  
6925 C C   . VAL B 232 ? 0.43170 0.35273 0.33527 -0.00292 -0.02697 0.01532  218 VAL B C   
6926 O O   . VAL B 232 ? 0.46869 0.38365 0.38910 -0.00245 -0.04351 0.02467  218 VAL B O   
6927 C CB  . VAL B 232 ? 0.46667 0.37732 0.33971 -0.01657 -0.03495 0.01526  218 VAL B CB  
6928 C CG1 . VAL B 232 ? 0.54876 0.44891 0.38192 -0.03139 -0.02728 0.01328  218 VAL B CG1 
6929 C CG2 . VAL B 232 ? 0.46582 0.37999 0.33821 -0.01459 -0.03106 0.00857  218 VAL B CG2 
6939 N N   . PHE B 233 ? 0.41480 0.33801 0.30258 -0.00533 -0.01236 0.00969  219 PHE B N   
6940 C CA  . PHE B 233 ? 0.42226 0.34408 0.31522 -0.00480 -0.01243 0.01308  219 PHE B CA  
6941 C C   . PHE B 233 ? 0.48748 0.40344 0.34681 -0.01953 -0.00489 0.01322  219 PHE B C   
6942 O O   . PHE B 233 ? 0.44962 0.37404 0.29830 -0.02028 0.01250  0.00281  219 PHE B O   
6943 C CB  . PHE B 233 ? 0.48316 0.42019 0.40255 0.01013  0.00034  0.00445  219 PHE B CB  
6944 C CG  . PHE B 233 ? 0.45405 0.38911 0.37889 0.01084  0.00080  0.00658  219 PHE B CG  
6945 C CD1 . PHE B 233 ? 0.45986 0.38734 0.40414 0.01436  -0.01298 0.01256  219 PHE B CD1 
6946 C CD2 . PHE B 233 ? 0.49896 0.43980 0.41323 0.00834  0.01449  0.00198  219 PHE B CD2 
6947 C CE1 . PHE B 233 ? 0.43646 0.35950 0.38521 0.01464  -0.01340 0.01392  219 PHE B CE1 
6948 C CE2 . PHE B 233 ? 0.48404 0.42240 0.40257 0.00779  0.01393  0.00451  219 PHE B CE2 
6949 C CZ  . PHE B 233 ? 0.45812 0.38632 0.39196 0.01069  -0.00010 0.01043  219 PHE B CZ  
6959 N N   . LEU B 234 ? 0.45056 0.35213 0.29526 -0.03203 -0.01843 0.02491  220 LEU B N   
6960 C CA  . LEU B 234 ? 0.48587 0.38265 0.29912 -0.04872 -0.01169 0.02658  220 LEU B CA  
6961 C C   . LEU B 234 ? 0.58088 0.47333 0.40586 -0.04785 -0.01875 0.03420  220 LEU B C   
6962 O O   . LEU B 234 ? 0.58189 0.46277 0.42393 -0.04462 -0.03876 0.04434  220 LEU B O   
6963 C CB  . LEU B 234 ? 0.49870 0.37781 0.27215 -0.07181 -0.02350 0.03566  220 LEU B CB  
6964 C CG  . LEU B 234 ? 0.54931 0.42137 0.28563 -0.09453 -0.01912 0.03995  220 LEU B CG  
6965 C CD1 . LEU B 234 ? 0.62973 0.51790 0.35137 -0.09805 0.01006  0.02264  220 LEU B CD1 
6966 C CD2 . LEU B 234 ? 0.64816 0.49707 0.34634 -0.11945 -0.03987 0.05468  220 LEU B CD2 
6978 N N   . GLU B 235 ? 0.54510 0.44640 0.36354 -0.05098 -0.00316 0.02902  221 GLU B N   
6979 C CA  . GLU B 235 ? 0.48498 0.38257 0.31403 -0.05032 -0.00822 0.03493  221 GLU B CA  
6980 C C   . GLU B 235 ? 0.54320 0.44247 0.34448 -0.06862 0.00193  0.03628  221 GLU B C   
6981 O O   . GLU B 235 ? 0.47865 0.39251 0.26896 -0.07255 0.02217  0.02542  221 GLU B O   
6982 C CB  . GLU B 235 ? 0.49252 0.40439 0.35580 -0.02998 0.00154  0.02531  221 GLU B CB  
6983 C CG  . GLU B 235 ? 0.48174 0.38818 0.35612 -0.02891 -0.00362 0.02968  221 GLU B CG  
6984 C CD  . GLU B 235 ? 0.56560 0.48656 0.46404 -0.01403 0.00899  0.01915  221 GLU B CD  
6985 O OE1 . GLU B 235 ? 0.56812 0.50017 0.48124 -0.00197 0.01626  0.01054  221 GLU B OE1 
6986 O OE2 . GLU B 235 ? 0.67898 0.59905 0.57952 -0.01643 0.01039  0.02044  221 GLU B OE2 
6993 N N   . PHE B 236 ? 0.48348 0.36797 0.27626 -0.08004 -0.01234 0.04917  222 PHE B N   
6994 C CA  . PHE B 236 ? 0.53007 0.41693 0.30050 -0.09805 -0.00389 0.05202  222 PHE B CA  
6995 C C   . PHE B 236 ? 0.50191 0.38653 0.29532 -0.09001 -0.00944 0.05561  222 PHE B C   
6996 O O   . PHE B 236 ? 0.54431 0.40980 0.34917 -0.08694 -0.03119 0.06587  222 PHE B O   
6997 C CB  . PHE B 236 ? 0.52848 0.39573 0.25745 -0.12630 -0.01802 0.06664  222 PHE B CB  
6998 C CG  . PHE B 236 ? 0.60670 0.47730 0.30343 -0.14024 -0.00718 0.06045  222 PHE B CG  
6999 C CD1 . PHE B 236 ? 0.60265 0.49137 0.28061 -0.15174 0.01965  0.04770  222 PHE B CD1 
7000 C CD2 . PHE B 236 ? 0.64417 0.50008 0.33142 -0.14223 -0.02349 0.06619  222 PHE B CD2 
7001 C CE1 . PHE B 236 ? 0.65330 0.54392 0.30132 -0.16495 0.03156  0.03886  222 PHE B CE1 
7002 C CE2 . PHE B 236 ? 0.67912 0.53569 0.33332 -0.15660 -0.01369 0.05951  222 PHE B CE2 
7003 C CZ  . PHE B 236 ? 0.68138 0.55460 0.31484 -0.16793 0.01467  0.04484  222 PHE B CZ  
7013 N N   . VAL B 237 ? 0.47033 0.37379 0.27310 -0.08639 0.00930  0.04659  223 VAL B N   
7014 C CA  . VAL B 237 ? 0.48049 0.38322 0.30405 -0.07887 0.00614  0.04790  223 VAL B CA  
7015 C C   . VAL B 237 ? 0.50725 0.41932 0.31602 -0.09610 0.01693  0.05001  223 VAL B C   
7016 O O   . VAL B 237 ? 0.53760 0.47130 0.34291 -0.09999 0.03777  0.04039  223 VAL B O   
7017 C CB  . VAL B 237 ? 0.46043 0.37805 0.31616 -0.05569 0.01621  0.03498  223 VAL B CB  
7018 C CG1 . VAL B 237 ? 0.49283 0.43383 0.35036 -0.05233 0.03745  0.02284  223 VAL B CG1 
7019 C CG2 . VAL B 237 ? 0.49308 0.41028 0.36411 -0.05182 0.01500  0.03521  223 VAL B CG2 
7029 N N   . THR B 238 ? 0.53193 0.42798 0.33500 -0.10653 0.00259  0.06205  224 THR B N   
7030 C CA  . THR B 238 ? 0.60015 0.50329 0.38768 -0.12633 0.01007  0.06674  224 THR B CA  
7031 C C   . THR B 238 ? 0.55945 0.45383 0.36420 -0.12191 0.00013  0.07145  224 THR B C   
7032 O O   . THR B 238 ? 0.55932 0.43191 0.37659 -0.11182 -0.01881 0.07596  224 THR B O   
7033 C CB  . THR B 238 ? 0.57197 0.45925 0.31964 -0.15508 -0.00012 0.08105  224 THR B CB  
7034 O OG1 . THR B 238 ? 0.67888 0.56721 0.40750 -0.15937 0.00425  0.07742  224 THR B OG1 
7035 C CG2 . THR B 238 ? 0.62991 0.53244 0.35999 -0.17793 0.01482  0.08245  224 THR B CG2 
7043 N N   . ALA B 239 ? 0.53276 0.44444 0.34002 -0.12997 0.01320  0.06942  225 ALA B N   
7044 C CA  . ALA B 239 ? 0.54073 0.44450 0.36076 -0.12910 0.00450  0.07393  225 ALA B CA  
7045 C C   . ALA B 239 ? 0.51732 0.40082 0.31234 -0.15385 -0.01118 0.09101  225 ALA B C   
7046 O O   . ALA B 239 ? 0.57282 0.46185 0.34032 -0.17661 -0.00545 0.09712  225 ALA B O   
7047 C CB  . ALA B 239 ? 0.48127 0.41370 0.31967 -0.12623 0.02345  0.06494  225 ALA B CB  
7053 N N   . ALA B 240 ? 0.52613 0.38502 0.32970 -0.15071 -0.03096 0.09812  226 ALA B N   
7054 C CA  . ALA B 240 ? 0.57443 0.40886 0.35716 -0.17345 -0.05055 0.11593  226 ALA B CA  
7055 C C   . ALA B 240 ? 0.57555 0.39105 0.37764 -0.16499 -0.06468 0.11686  226 ALA B C   
7056 O O   . ALA B 240 ? 0.54577 0.36929 0.37303 -0.14422 -0.05702 0.10333  226 ALA B O   
7057 C CB  . ALA B 240 ? 0.59759 0.40498 0.36169 -0.18192 -0.07210 0.12855  226 ALA B CB  
7063 N N   . GLY B 241 ? 0.64935 0.43767 0.43717 -0.18317 -0.08619 0.13307  227 GLY B N   
7064 C CA  . GLY B 241 ? 0.63321 0.39844 0.43656 -0.17799 -0.10182 0.13438  227 GLY B CA  
7065 C C   . GLY B 241 ? 0.69817 0.47183 0.49354 -0.19582 -0.09703 0.13986  227 GLY B C   
7066 O O   . GLY B 241 ? 0.76113 0.51516 0.56766 -0.19271 -0.10945 0.14010  227 GLY B O   
7070 N N   . ILE B 242 ? 0.74095 0.54365 0.51924 -0.21467 -0.07884 0.14300  228 ILE B N   
7071 C CA  . ILE B 242 ? 0.79644 0.61118 0.56988 -0.23396 -0.07364 0.14906  228 ILE B CA  
7072 C C   . ILE B 242 ? 0.82615 0.64422 0.56551 -0.26810 -0.07363 0.16493  228 ILE B C   
7073 O O   . ILE B 242 ? 1.06014 0.87591 0.77840 -0.27611 -0.07351 0.16878  228 ILE B O   
7074 C CB  . ILE B 242 ? 0.78381 0.63889 0.57960 -0.22323 -0.04709 0.13397  228 ILE B CB  
7075 C CG1 . ILE B 242 ? 0.72869 0.57824 0.55171 -0.19358 -0.04830 0.11956  228 ILE B CG1 
7076 C CG2 . ILE B 242 ? 0.79594 0.66523 0.59114 -0.24418 -0.04312 0.14124  228 ILE B CG2 
7077 C CD1 . ILE B 242 ? 0.64529 0.52957 0.49088 -0.18357 -0.02784 0.10723  228 ILE B CD1 
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